data_8ZXX
# 
_entry.id   8ZXX 
# 
_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   8ZXX         pdb_00008zxx 10.2210/pdb8zxx/pdb 
WWPDB D_1300048733 ?            ?                   
# 
_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       2025-05-21 
_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                        8ZXX 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tanakan@pharm.kitasato-u.ac.jp 
_pdbx_contact_author.name_first         Nobutada 
_pdbx_contact_author.name_last          Tanaka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5365-4698 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanaka, N.'   1 0000-0001-5365-4698 
'Takada, S.'   2 0009-0006-7357-244X 
'Sakamoto, Y.' 3 0000-0003-1067-954X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Med.Chem.Lett.' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1948-5875 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                136 
_citation.page_last                 143 
_citation.title                     'Expanding the Chemical Space of Reverse Fosmidomycin Analogs.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acsmedchemlett.4c00501 
_citation.pdbx_database_id_PubMed   39811140 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Knak, T.'                 1  0000-0002-9185-5156 
primary 'Takada, S.'               2  0009-0006-7357-244X 
primary 'Illarionov, B.'           3  ?                   
primary 'Krisilia, V.'             4  0009-0000-3256-8627 
primary 'Pessanha de Carvalho, L.' 5  ?                   
primary 'Lungerich, B.'            6  ?                   
primary 'Sakamoto, Y.'             7  ?                   
primary 'Hofmann, S.'              8  0000-0003-0588-6974 
primary 'Bacher, A.'               9  ?                   
primary 'Kalscheuer, R.'           10 0000-0002-3378-2067 
primary 'Held, J.'                 11 0000-0002-7970-1429 
primary 'Fischer, M.'              12 0000-0001-7243-4199 
primary 'Tanaka, N.'               13 0000-0001-5365-4698 
primary 'Kurz, T.'                 14 0000-0002-9474-4224 
# 
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 '1-deoxy-D-xylulose 5-phosphate reductoisomerase, apicoplastic'                                             
47133.336 1   1.1.1.267 ? ? ? 
2 non-polymer syn 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                                                 
745.421   1   ?         ? ? ? 
3 non-polymer syn 'MANGANESE (II) ION'                                                                                        
54.938    1   ?         ? ? ? 
4 non-polymer syn '[(~{S})-(4-hexoxyphenyl)-[2-[methyl(oxidanyl)amino]-2-oxidanylidene-ethyl]sulfanyl-methyl]phosphonic acid' 
391.420   1   ?         ? ? ? 
5 non-polymer syn GLYCEROL                                                                                                    
92.094    1   ?         ? ? ? 
6 water       nat water                                                                                                       
18.015    360 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '1-deoxyxylulose-5-phosphate reductoisomerase,DOXP reductoisomerase,DXP reductoisomerase' 
# 
_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       
;KKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDY
KPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEH
SAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGL
EVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKP
SLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWA
KDKATDIYNKHNSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;KKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDY
KPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEH
SAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGL
EVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKP
SLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWA
KDKATDIYNKHNSS
;
_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 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE'                                                 NDP   
3 'MANGANESE (II) ION'                                                                                        MN    
4 '[(~{S})-(4-hexoxyphenyl)-[2-[methyl(oxidanyl)amino]-2-oxidanylidene-ethyl]sulfanyl-methyl]phosphonic acid' A1L2H 
5 GLYCEROL                                                                                                    GOL   
6 water                                                                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   LYS n 
1 2   LYS n 
1 3   PRO n 
1 4   ILE n 
1 5   ASN n 
1 6   VAL n 
1 7   ALA n 
1 8   ILE n 
1 9   PHE n 
1 10  GLY n 
1 11  SER n 
1 12  THR n 
1 13  GLY n 
1 14  SER n 
1 15  ILE n 
1 16  GLY n 
1 17  THR n 
1 18  ASN n 
1 19  ALA n 
1 20  LEU n 
1 21  ASN n 
1 22  ILE n 
1 23  ILE n 
1 24  ARG n 
1 25  GLU n 
1 26  CYS n 
1 27  ASN n 
1 28  LYS n 
1 29  ILE n 
1 30  GLU n 
1 31  ASN n 
1 32  VAL n 
1 33  PHE n 
1 34  ASN n 
1 35  VAL n 
1 36  LYS n 
1 37  ALA n 
1 38  LEU n 
1 39  TYR n 
1 40  VAL n 
1 41  ASN n 
1 42  LYS n 
1 43  SER n 
1 44  VAL n 
1 45  ASN n 
1 46  GLU n 
1 47  LEU n 
1 48  TYR n 
1 49  GLU n 
1 50  GLN n 
1 51  ALA n 
1 52  ARG n 
1 53  GLU n 
1 54  PHE n 
1 55  LEU n 
1 56  PRO n 
1 57  GLU n 
1 58  TYR n 
1 59  LEU n 
1 60  CYS n 
1 61  ILE n 
1 62  HIS n 
1 63  ASP n 
1 64  LYS n 
1 65  SER n 
1 66  VAL n 
1 67  TYR n 
1 68  GLU n 
1 69  GLU n 
1 70  LEU n 
1 71  LYS n 
1 72  GLU n 
1 73  LEU n 
1 74  VAL n 
1 75  LYS n 
1 76  ASN n 
1 77  ILE n 
1 78  LYS n 
1 79  ASP n 
1 80  TYR n 
1 81  LYS n 
1 82  PRO n 
1 83  ILE n 
1 84  ILE n 
1 85  LEU n 
1 86  CYS n 
1 87  GLY n 
1 88  ASP n 
1 89  GLU n 
1 90  GLY n 
1 91  MET n 
1 92  LYS n 
1 93  GLU n 
1 94  ILE n 
1 95  CYS n 
1 96  SER n 
1 97  SER n 
1 98  ASN n 
1 99  SER n 
1 100 ILE n 
1 101 ASP n 
1 102 LYS n 
1 103 ILE n 
1 104 VAL n 
1 105 ILE n 
1 106 GLY n 
1 107 ILE n 
1 108 ASP n 
1 109 SER n 
1 110 PHE n 
1 111 GLN n 
1 112 GLY n 
1 113 LEU n 
1 114 TYR n 
1 115 SER n 
1 116 THR n 
1 117 MET n 
1 118 TYR n 
1 119 ALA n 
1 120 ILE n 
1 121 MET n 
1 122 ASN n 
1 123 ASN n 
1 124 LYS n 
1 125 ILE n 
1 126 VAL n 
1 127 ALA n 
1 128 LEU n 
1 129 ALA n 
1 130 ASN n 
1 131 LYS n 
1 132 GLU n 
1 133 SER n 
1 134 ILE n 
1 135 VAL n 
1 136 SER n 
1 137 ALA n 
1 138 GLY n 
1 139 PHE n 
1 140 PHE n 
1 141 LEU n 
1 142 LYS n 
1 143 LYS n 
1 144 LEU n 
1 145 LEU n 
1 146 ASN n 
1 147 ILE n 
1 148 HIS n 
1 149 LYS n 
1 150 ASN n 
1 151 ALA n 
1 152 LYS n 
1 153 ILE n 
1 154 ILE n 
1 155 PRO n 
1 156 VAL n 
1 157 ASP n 
1 158 SER n 
1 159 GLU n 
1 160 HIS n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 PHE n 
1 165 GLN n 
1 166 CYS n 
1 167 LEU n 
1 168 ASP n 
1 169 ASN n 
1 170 ASN n 
1 171 LYS n 
1 172 VAL n 
1 173 LEU n 
1 174 LYS n 
1 175 THR n 
1 176 LYS n 
1 177 CYS n 
1 178 LEU n 
1 179 GLN n 
1 180 ASP n 
1 181 ASN n 
1 182 PHE n 
1 183 SER n 
1 184 LYS n 
1 185 ILE n 
1 186 ASN n 
1 187 ASN n 
1 188 ILE n 
1 189 ASN n 
1 190 LYS n 
1 191 ILE n 
1 192 PHE n 
1 193 LEU n 
1 194 CYS n 
1 195 SER n 
1 196 SER n 
1 197 GLY n 
1 198 GLY n 
1 199 PRO n 
1 200 PHE n 
1 201 GLN n 
1 202 ASN n 
1 203 LEU n 
1 204 THR n 
1 205 MET n 
1 206 ASP n 
1 207 GLU n 
1 208 LEU n 
1 209 LYS n 
1 210 ASN n 
1 211 VAL n 
1 212 THR n 
1 213 SER n 
1 214 GLU n 
1 215 ASN n 
1 216 ALA n 
1 217 LEU n 
1 218 LYS n 
1 219 HIS n 
1 220 PRO n 
1 221 LYS n 
1 222 TRP n 
1 223 LYS n 
1 224 MET n 
1 225 GLY n 
1 226 LYS n 
1 227 LYS n 
1 228 ILE n 
1 229 THR n 
1 230 ILE n 
1 231 ASP n 
1 232 SER n 
1 233 ALA n 
1 234 THR n 
1 235 MET n 
1 236 MET n 
1 237 ASN n 
1 238 LYS n 
1 239 GLY n 
1 240 LEU n 
1 241 GLU n 
1 242 VAL n 
1 243 ILE n 
1 244 GLU n 
1 245 THR n 
1 246 HIS n 
1 247 PHE n 
1 248 LEU n 
1 249 PHE n 
1 250 ASP n 
1 251 VAL n 
1 252 ASP n 
1 253 TYR n 
1 254 ASN n 
1 255 ASP n 
1 256 ILE n 
1 257 GLU n 
1 258 VAL n 
1 259 ILE n 
1 260 VAL n 
1 261 HIS n 
1 262 LYS n 
1 263 GLU n 
1 264 CYS n 
1 265 ILE n 
1 266 ILE n 
1 267 HIS n 
1 268 SER n 
1 269 CYS n 
1 270 VAL n 
1 271 GLU n 
1 272 PHE n 
1 273 ILE n 
1 274 ASP n 
1 275 LYS n 
1 276 SER n 
1 277 VAL n 
1 278 ILE n 
1 279 SER n 
1 280 GLN n 
1 281 MET n 
1 282 TYR n 
1 283 TYR n 
1 284 PRO n 
1 285 ASP n 
1 286 MET n 
1 287 GLN n 
1 288 ILE n 
1 289 PRO n 
1 290 ILE n 
1 291 LEU n 
1 292 TYR n 
1 293 SER n 
1 294 LEU n 
1 295 THR n 
1 296 TRP n 
1 297 PRO n 
1 298 ASP n 
1 299 ARG n 
1 300 ILE n 
1 301 LYS n 
1 302 THR n 
1 303 ASN n 
1 304 LEU n 
1 305 LYS n 
1 306 PRO n 
1 307 LEU n 
1 308 ASP n 
1 309 LEU n 
1 310 ALA n 
1 311 GLN n 
1 312 VAL n 
1 313 SER n 
1 314 THR n 
1 315 LEU n 
1 316 THR n 
1 317 PHE n 
1 318 HIS n 
1 319 LYS n 
1 320 PRO n 
1 321 SER n 
1 322 LEU n 
1 323 GLU n 
1 324 HIS n 
1 325 PHE n 
1 326 PRO n 
1 327 CYS n 
1 328 ILE n 
1 329 LYS n 
1 330 LEU n 
1 331 ALA n 
1 332 TYR n 
1 333 GLN n 
1 334 ALA n 
1 335 GLY n 
1 336 ILE n 
1 337 LYS n 
1 338 GLY n 
1 339 ASN n 
1 340 PHE n 
1 341 TYR n 
1 342 PRO n 
1 343 THR n 
1 344 VAL n 
1 345 LEU n 
1 346 ASN n 
1 347 ALA n 
1 348 SER n 
1 349 ASN n 
1 350 GLU n 
1 351 ILE n 
1 352 ALA n 
1 353 ASN n 
1 354 ASN n 
1 355 LEU n 
1 356 PHE n 
1 357 LEU n 
1 358 ASN n 
1 359 ASN n 
1 360 LYS n 
1 361 ILE n 
1 362 LYS n 
1 363 TYR n 
1 364 PHE n 
1 365 ASP n 
1 366 ILE n 
1 367 SER n 
1 368 SER n 
1 369 ILE n 
1 370 ILE n 
1 371 SER n 
1 372 GLN n 
1 373 VAL n 
1 374 LEU n 
1 375 GLU n 
1 376 SER n 
1 377 PHE n 
1 378 ASN n 
1 379 SER n 
1 380 GLN n 
1 381 LYS n 
1 382 VAL n 
1 383 SER n 
1 384 GLU n 
1 385 ASN n 
1 386 SER n 
1 387 GLU n 
1 388 ASP n 
1 389 LEU n 
1 390 MET n 
1 391 LYS n 
1 392 GLN n 
1 393 ILE n 
1 394 LEU n 
1 395 GLN n 
1 396 ILE n 
1 397 HIS n 
1 398 SER n 
1 399 TRP n 
1 400 ALA n 
1 401 LYS n 
1 402 ASP n 
1 403 LYS n 
1 404 ALA n 
1 405 THR n 
1 406 ASP n 
1 407 ILE n 
1 408 TYR n 
1 409 ASN n 
1 410 LYS n 
1 411 HIS n 
1 412 ASN n 
1 413 SER n 
1 414 SER 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                   414 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 DXR 
_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      'Plasmodium falciparum HB3' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     137071 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1L2H non-polymer         . 
'[(~{S})-(4-hexoxyphenyl)-[2-[methyl(oxidanyl)amino]-2-oxidanylidene-ethyl]sulfanyl-methyl]phosphonic acid' ? 'C16 H26 N O6 P S'  
391.420 
ALA   'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'        89.093  
ARG   'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'    175.209 
ASN   'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'       132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'        133.103 
CYS   'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'        75.067  
GOL   non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS   'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ?                               'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'     149.211 
MN    non-polymer         . 'MANGANESE (II) ION' ?                               'Mn 2'              54.938  
NDP   non-polymer         . 'NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE' ?                               
'C21 H30 N7 O17 P3' 745.421 
PHE   'L-peptide linking' y PHENYLALANINE ?                               'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                               'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                               'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                               'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                               'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                               'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                               'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   LYS 1   75  ?   ?   ?   A . n 
A 1 2   LYS 2   76  76  LYS LYS A . n 
A 1 3   PRO 3   77  77  PRO PRO A . n 
A 1 4   ILE 4   78  78  ILE ILE A . n 
A 1 5   ASN 5   79  79  ASN ASN A . n 
A 1 6   VAL 6   80  80  VAL VAL A . n 
A 1 7   ALA 7   81  81  ALA ALA A . n 
A 1 8   ILE 8   82  82  ILE ILE A . n 
A 1 9   PHE 9   83  83  PHE PHE A . n 
A 1 10  GLY 10  84  84  GLY GLY A . n 
A 1 11  SER 11  85  85  SER SER A . n 
A 1 12  THR 12  86  86  THR THR A . n 
A 1 13  GLY 13  87  87  GLY GLY A . n 
A 1 14  SER 14  88  88  SER SER A . n 
A 1 15  ILE 15  89  89  ILE ILE A . n 
A 1 16  GLY 16  90  90  GLY GLY A . n 
A 1 17  THR 17  91  91  THR THR A . n 
A 1 18  ASN 18  92  92  ASN ASN A . n 
A 1 19  ALA 19  93  93  ALA ALA A . n 
A 1 20  LEU 20  94  94  LEU LEU A . n 
A 1 21  ASN 21  95  95  ASN ASN A . n 
A 1 22  ILE 22  96  96  ILE ILE A . n 
A 1 23  ILE 23  97  97  ILE ILE A . n 
A 1 24  ARG 24  98  98  ARG ARG A . n 
A 1 25  GLU 25  99  99  GLU GLU A . n 
A 1 26  CYS 26  100 100 CYS CYS A . n 
A 1 27  ASN 27  101 101 ASN ASN A . n 
A 1 28  LYS 28  102 102 LYS LYS A . n 
A 1 29  ILE 29  103 103 ILE ILE A . n 
A 1 30  GLU 30  104 104 GLU GLU A . n 
A 1 31  ASN 31  105 105 ASN ASN A . n 
A 1 32  VAL 32  106 106 VAL VAL A . n 
A 1 33  PHE 33  107 107 PHE PHE A . n 
A 1 34  ASN 34  108 108 ASN ASN A . n 
A 1 35  VAL 35  109 109 VAL VAL A . n 
A 1 36  LYS 36  110 110 LYS LYS A . n 
A 1 37  ALA 37  111 111 ALA ALA A . n 
A 1 38  LEU 38  112 112 LEU LEU A . n 
A 1 39  TYR 39  113 113 TYR TYR A . n 
A 1 40  VAL 40  114 114 VAL VAL A . n 
A 1 41  ASN 41  115 115 ASN ASN A . n 
A 1 42  LYS 42  116 116 LYS LYS A . n 
A 1 43  SER 43  117 117 SER SER A . n 
A 1 44  VAL 44  118 118 VAL VAL A . n 
A 1 45  ASN 45  119 119 ASN ASN A . n 
A 1 46  GLU 46  120 120 GLU GLU A . n 
A 1 47  LEU 47  121 121 LEU LEU A . n 
A 1 48  TYR 48  122 122 TYR TYR A . n 
A 1 49  GLU 49  123 123 GLU GLU A . n 
A 1 50  GLN 50  124 124 GLN GLN A . n 
A 1 51  ALA 51  125 125 ALA ALA A . n 
A 1 52  ARG 52  126 126 ARG ARG A . n 
A 1 53  GLU 53  127 127 GLU GLU A . n 
A 1 54  PHE 54  128 128 PHE PHE A . n 
A 1 55  LEU 55  129 129 LEU LEU A . n 
A 1 56  PRO 56  130 130 PRO PRO A . n 
A 1 57  GLU 57  131 131 GLU GLU A . n 
A 1 58  TYR 58  132 132 TYR TYR A . n 
A 1 59  LEU 59  133 133 LEU LEU A . n 
A 1 60  CYS 60  134 134 CYS CYS A . n 
A 1 61  ILE 61  135 135 ILE ILE A . n 
A 1 62  HIS 62  136 136 HIS HIS A . n 
A 1 63  ASP 63  137 137 ASP ASP A . n 
A 1 64  LYS 64  138 138 LYS LYS A . n 
A 1 65  SER 65  139 139 SER SER A . n 
A 1 66  VAL 66  140 140 VAL VAL A . n 
A 1 67  TYR 67  141 141 TYR TYR A . n 
A 1 68  GLU 68  142 142 GLU GLU A . n 
A 1 69  GLU 69  143 143 GLU GLU A . n 
A 1 70  LEU 70  144 144 LEU LEU A . n 
A 1 71  LYS 71  145 145 LYS LYS A . n 
A 1 72  GLU 72  146 146 GLU GLU A . n 
A 1 73  LEU 73  147 147 LEU LEU A . n 
A 1 74  VAL 74  148 148 VAL VAL A . n 
A 1 75  LYS 75  149 149 LYS LYS A . n 
A 1 76  ASN 76  150 150 ASN ASN A . n 
A 1 77  ILE 77  151 151 ILE ILE A . n 
A 1 78  LYS 78  152 152 LYS LYS A . n 
A 1 79  ASP 79  153 153 ASP ASP A . n 
A 1 80  TYR 80  154 154 TYR TYR A . n 
A 1 81  LYS 81  155 155 LYS LYS A . n 
A 1 82  PRO 82  156 156 PRO PRO A . n 
A 1 83  ILE 83  157 157 ILE ILE A . n 
A 1 84  ILE 84  158 158 ILE ILE A . n 
A 1 85  LEU 85  159 159 LEU LEU A . n 
A 1 86  CYS 86  160 160 CYS CYS A . n 
A 1 87  GLY 87  161 161 GLY GLY A . n 
A 1 88  ASP 88  162 162 ASP ASP A . n 
A 1 89  GLU 89  163 163 GLU GLU A . n 
A 1 90  GLY 90  164 164 GLY GLY A . n 
A 1 91  MET 91  165 165 MET MET A . n 
A 1 92  LYS 92  166 166 LYS LYS A . n 
A 1 93  GLU 93  167 167 GLU GLU A . n 
A 1 94  ILE 94  168 168 ILE ILE A . n 
A 1 95  CYS 95  169 169 CYS CYS A . n 
A 1 96  SER 96  170 170 SER SER A . n 
A 1 97  SER 97  171 171 SER SER A . n 
A 1 98  ASN 98  172 172 ASN ASN A . n 
A 1 99  SER 99  173 173 SER SER A . n 
A 1 100 ILE 100 174 174 ILE ILE A . n 
A 1 101 ASP 101 175 175 ASP ASP A . n 
A 1 102 LYS 102 176 176 LYS LYS A . n 
A 1 103 ILE 103 177 177 ILE ILE A . n 
A 1 104 VAL 104 178 178 VAL VAL A . n 
A 1 105 ILE 105 179 179 ILE ILE A . n 
A 1 106 GLY 106 180 180 GLY GLY A . n 
A 1 107 ILE 107 181 181 ILE ILE A . n 
A 1 108 ASP 108 182 182 ASP ASP A . n 
A 1 109 SER 109 183 183 SER SER A . n 
A 1 110 PHE 110 184 184 PHE PHE A . n 
A 1 111 GLN 111 185 185 GLN GLN A . n 
A 1 112 GLY 112 186 186 GLY GLY A . n 
A 1 113 LEU 113 187 187 LEU LEU A . n 
A 1 114 TYR 114 188 188 TYR TYR A . n 
A 1 115 SER 115 189 189 SER SER A . n 
A 1 116 THR 116 190 190 THR THR A . n 
A 1 117 MET 117 191 191 MET MET A . n 
A 1 118 TYR 118 192 192 TYR TYR A . n 
A 1 119 ALA 119 193 193 ALA ALA A . n 
A 1 120 ILE 120 194 194 ILE ILE A . n 
A 1 121 MET 121 195 195 MET MET A . n 
A 1 122 ASN 122 196 196 ASN ASN A . n 
A 1 123 ASN 123 197 197 ASN ASN A . n 
A 1 124 LYS 124 198 198 LYS LYS A . n 
A 1 125 ILE 125 199 199 ILE ILE A . n 
A 1 126 VAL 126 200 200 VAL VAL A . n 
A 1 127 ALA 127 201 201 ALA ALA A . n 
A 1 128 LEU 128 202 202 LEU LEU A . n 
A 1 129 ALA 129 203 203 ALA ALA A . n 
A 1 130 ASN 130 204 204 ASN ASN A . n 
A 1 131 LYS 131 205 205 LYS LYS A . n 
A 1 132 GLU 132 206 206 GLU GLU A . n 
A 1 133 SER 133 207 207 SER SER A . n 
A 1 134 ILE 134 208 208 ILE ILE A . n 
A 1 135 VAL 135 209 209 VAL VAL A . n 
A 1 136 SER 136 210 210 SER SER A . n 
A 1 137 ALA 137 211 211 ALA ALA A . n 
A 1 138 GLY 138 212 212 GLY GLY A . n 
A 1 139 PHE 139 213 213 PHE PHE A . n 
A 1 140 PHE 140 214 214 PHE PHE A . n 
A 1 141 LEU 141 215 215 LEU LEU A . n 
A 1 142 LYS 142 216 216 LYS LYS A . n 
A 1 143 LYS 143 217 217 LYS LYS A . n 
A 1 144 LEU 144 218 218 LEU LEU A . n 
A 1 145 LEU 145 219 219 LEU LEU A . n 
A 1 146 ASN 146 220 220 ASN ASN A . n 
A 1 147 ILE 147 221 221 ILE ILE A . n 
A 1 148 HIS 148 222 222 HIS HIS A . n 
A 1 149 LYS 149 223 223 LYS LYS A . n 
A 1 150 ASN 150 224 224 ASN ASN A . n 
A 1 151 ALA 151 225 225 ALA ALA A . n 
A 1 152 LYS 152 226 226 LYS LYS A . n 
A 1 153 ILE 153 227 227 ILE ILE A . n 
A 1 154 ILE 154 228 228 ILE ILE A . n 
A 1 155 PRO 155 229 229 PRO PRO A . n 
A 1 156 VAL 156 230 230 VAL VAL A . n 
A 1 157 ASP 157 231 231 ASP ASP A . n 
A 1 158 SER 158 232 232 SER SER A . n 
A 1 159 GLU 159 233 233 GLU GLU A . n 
A 1 160 HIS 160 234 234 HIS HIS A . n 
A 1 161 SER 161 235 235 SER SER A . n 
A 1 162 ALA 162 236 236 ALA ALA A . n 
A 1 163 ILE 163 237 237 ILE ILE A . n 
A 1 164 PHE 164 238 238 PHE PHE A . n 
A 1 165 GLN 165 239 239 GLN GLN A . n 
A 1 166 CYS 166 240 240 CYS CYS A . n 
A 1 167 LEU 167 241 241 LEU LEU A . n 
A 1 168 ASP 168 242 242 ASP ASP A . n 
A 1 169 ASN 169 243 243 ASN ASN A . n 
A 1 170 ASN 170 244 244 ASN ASN A . n 
A 1 171 LYS 171 245 245 LYS LYS A . n 
A 1 172 VAL 172 246 246 VAL VAL A . n 
A 1 173 LEU 173 247 247 LEU LEU A . n 
A 1 174 LYS 174 248 248 LYS LYS A . n 
A 1 175 THR 175 249 249 THR THR A . n 
A 1 176 LYS 176 250 250 LYS LYS A . n 
A 1 177 CYS 177 251 251 CYS CYS A . n 
A 1 178 LEU 178 252 252 LEU LEU A . n 
A 1 179 GLN 179 253 253 GLN GLN A . n 
A 1 180 ASP 180 254 254 ASP ASP A . n 
A 1 181 ASN 181 255 255 ASN ASN A . n 
A 1 182 PHE 182 256 256 PHE PHE A . n 
A 1 183 SER 183 257 257 SER SER A . n 
A 1 184 LYS 184 258 258 LYS LYS A . n 
A 1 185 ILE 185 259 259 ILE ILE A . n 
A 1 186 ASN 186 260 260 ASN ASN A . n 
A 1 187 ASN 187 261 261 ASN ASN A . n 
A 1 188 ILE 188 262 262 ILE ILE A . n 
A 1 189 ASN 189 263 263 ASN ASN A . n 
A 1 190 LYS 190 264 264 LYS LYS A . n 
A 1 191 ILE 191 265 265 ILE ILE A . n 
A 1 192 PHE 192 266 266 PHE PHE A . n 
A 1 193 LEU 193 267 267 LEU LEU A . n 
A 1 194 CYS 194 268 268 CYS CYS A . n 
A 1 195 SER 195 269 269 SER SER A . n 
A 1 196 SER 196 270 270 SER SER A . n 
A 1 197 GLY 197 271 271 GLY GLY A . n 
A 1 198 GLY 198 272 272 GLY GLY A . n 
A 1 199 PRO 199 273 273 PRO PRO A . n 
A 1 200 PHE 200 274 274 PHE PHE A . n 
A 1 201 GLN 201 275 275 GLN GLN A . n 
A 1 202 ASN 202 276 276 ASN ASN A . n 
A 1 203 LEU 203 277 277 LEU LEU A . n 
A 1 204 THR 204 278 278 THR THR A . n 
A 1 205 MET 205 279 279 MET MET A . n 
A 1 206 ASP 206 280 280 ASP ASP A . n 
A 1 207 GLU 207 281 281 GLU GLU A . n 
A 1 208 LEU 208 282 282 LEU LEU A . n 
A 1 209 LYS 209 283 283 LYS LYS A . n 
A 1 210 ASN 210 284 284 ASN ASN A . n 
A 1 211 VAL 211 285 285 VAL VAL A . n 
A 1 212 THR 212 286 286 THR THR A . n 
A 1 213 SER 213 287 287 SER SER A . n 
A 1 214 GLU 214 288 288 GLU GLU A . n 
A 1 215 ASN 215 289 289 ASN ASN A . n 
A 1 216 ALA 216 290 290 ALA ALA A . n 
A 1 217 LEU 217 291 291 LEU LEU A . n 
A 1 218 LYS 218 292 292 LYS LYS A . n 
A 1 219 HIS 219 293 293 HIS HIS A . n 
A 1 220 PRO 220 294 294 PRO PRO A . n 
A 1 221 LYS 221 295 295 LYS LYS A . n 
A 1 222 TRP 222 296 296 TRP TRP A . n 
A 1 223 LYS 223 297 297 LYS LYS A . n 
A 1 224 MET 224 298 298 MET MET A . n 
A 1 225 GLY 225 299 299 GLY GLY A . n 
A 1 226 LYS 226 300 300 LYS LYS A . n 
A 1 227 LYS 227 301 301 LYS LYS A . n 
A 1 228 ILE 228 302 302 ILE ILE A . n 
A 1 229 THR 229 303 303 THR THR A . n 
A 1 230 ILE 230 304 304 ILE ILE A . n 
A 1 231 ASP 231 305 305 ASP ASP A . n 
A 1 232 SER 232 306 306 SER SER A . n 
A 1 233 ALA 233 307 307 ALA ALA A . n 
A 1 234 THR 234 308 308 THR THR A . n 
A 1 235 MET 235 309 309 MET MET A . n 
A 1 236 MET 236 310 310 MET MET A . n 
A 1 237 ASN 237 311 311 ASN ASN A . n 
A 1 238 LYS 238 312 312 LYS LYS A . n 
A 1 239 GLY 239 313 313 GLY GLY A . n 
A 1 240 LEU 240 314 314 LEU LEU A . n 
A 1 241 GLU 241 315 315 GLU GLU A . n 
A 1 242 VAL 242 316 316 VAL VAL A . n 
A 1 243 ILE 243 317 317 ILE ILE A . n 
A 1 244 GLU 244 318 318 GLU GLU A . n 
A 1 245 THR 245 319 319 THR THR A . n 
A 1 246 HIS 246 320 320 HIS HIS A . n 
A 1 247 PHE 247 321 321 PHE PHE A . n 
A 1 248 LEU 248 322 322 LEU LEU A . n 
A 1 249 PHE 249 323 323 PHE PHE A . n 
A 1 250 ASP 250 324 324 ASP ASP A . n 
A 1 251 VAL 251 325 325 VAL VAL A . n 
A 1 252 ASP 252 326 326 ASP ASP A . n 
A 1 253 TYR 253 327 327 TYR TYR A . n 
A 1 254 ASN 254 328 328 ASN ASN A . n 
A 1 255 ASP 255 329 329 ASP ASP A . n 
A 1 256 ILE 256 330 330 ILE ILE A . n 
A 1 257 GLU 257 331 331 GLU GLU A . n 
A 1 258 VAL 258 332 332 VAL VAL A . n 
A 1 259 ILE 259 333 333 ILE ILE A . n 
A 1 260 VAL 260 334 334 VAL VAL A . n 
A 1 261 HIS 261 335 335 HIS HIS A . n 
A 1 262 LYS 262 336 336 LYS LYS A . n 
A 1 263 GLU 263 337 337 GLU GLU A . n 
A 1 264 CYS 264 338 338 CYS CYS A . n 
A 1 265 ILE 265 339 339 ILE ILE A . n 
A 1 266 ILE 266 340 340 ILE ILE A . n 
A 1 267 HIS 267 341 341 HIS HIS A . n 
A 1 268 SER 268 342 342 SER SER A . n 
A 1 269 CYS 269 343 343 CYS CYS A . n 
A 1 270 VAL 270 344 344 VAL VAL A . n 
A 1 271 GLU 271 345 345 GLU GLU A . n 
A 1 272 PHE 272 346 346 PHE PHE A . n 
A 1 273 ILE 273 347 347 ILE ILE A . n 
A 1 274 ASP 274 348 348 ASP ASP A . n 
A 1 275 LYS 275 349 349 LYS LYS A . n 
A 1 276 SER 276 350 350 SER SER A . n 
A 1 277 VAL 277 351 351 VAL VAL A . n 
A 1 278 ILE 278 352 352 ILE ILE A . n 
A 1 279 SER 279 353 353 SER SER A . n 
A 1 280 GLN 280 354 354 GLN GLN A . n 
A 1 281 MET 281 355 355 MET MET A . n 
A 1 282 TYR 282 356 356 TYR TYR A . n 
A 1 283 TYR 283 357 357 TYR TYR A . n 
A 1 284 PRO 284 358 358 PRO PRO A . n 
A 1 285 ASP 285 359 359 ASP ASP A . n 
A 1 286 MET 286 360 360 MET MET A . n 
A 1 287 GLN 287 361 361 GLN GLN A . n 
A 1 288 ILE 288 362 362 ILE ILE A . n 
A 1 289 PRO 289 363 363 PRO PRO A . n 
A 1 290 ILE 290 364 364 ILE ILE A . n 
A 1 291 LEU 291 365 365 LEU LEU A . n 
A 1 292 TYR 292 366 366 TYR TYR A . n 
A 1 293 SER 293 367 367 SER SER A . n 
A 1 294 LEU 294 368 368 LEU LEU A . n 
A 1 295 THR 295 369 369 THR THR A . n 
A 1 296 TRP 296 370 370 TRP TRP A . n 
A 1 297 PRO 297 371 371 PRO PRO A . n 
A 1 298 ASP 298 372 372 ASP ASP A . n 
A 1 299 ARG 299 373 373 ARG ARG A . n 
A 1 300 ILE 300 374 374 ILE ILE A . n 
A 1 301 LYS 301 375 375 LYS LYS A . n 
A 1 302 THR 302 376 376 THR THR A . n 
A 1 303 ASN 303 377 377 ASN ASN A . n 
A 1 304 LEU 304 378 378 LEU LEU A . n 
A 1 305 LYS 305 379 379 LYS LYS A . n 
A 1 306 PRO 306 380 380 PRO PRO A . n 
A 1 307 LEU 307 381 381 LEU LEU A . n 
A 1 308 ASP 308 382 382 ASP ASP A . n 
A 1 309 LEU 309 383 383 LEU LEU A . n 
A 1 310 ALA 310 384 384 ALA ALA A . n 
A 1 311 GLN 311 385 385 GLN GLN A . n 
A 1 312 VAL 312 386 386 VAL VAL A . n 
A 1 313 SER 313 387 387 SER SER A . n 
A 1 314 THR 314 388 388 THR THR A . n 
A 1 315 LEU 315 389 389 LEU LEU A . n 
A 1 316 THR 316 390 390 THR THR A . n 
A 1 317 PHE 317 391 391 PHE PHE A . n 
A 1 318 HIS 318 392 392 HIS HIS A . n 
A 1 319 LYS 319 393 393 LYS LYS A . n 
A 1 320 PRO 320 394 394 PRO PRO A . n 
A 1 321 SER 321 395 395 SER SER A . n 
A 1 322 LEU 322 396 396 LEU LEU A . n 
A 1 323 GLU 323 397 397 GLU GLU A . n 
A 1 324 HIS 324 398 398 HIS HIS A . n 
A 1 325 PHE 325 399 399 PHE PHE A . n 
A 1 326 PRO 326 400 400 PRO PRO A . n 
A 1 327 CYS 327 401 401 CYS CYS A . n 
A 1 328 ILE 328 402 402 ILE ILE A . n 
A 1 329 LYS 329 403 403 LYS LYS A . n 
A 1 330 LEU 330 404 404 LEU LEU A . n 
A 1 331 ALA 331 405 405 ALA ALA A . n 
A 1 332 TYR 332 406 406 TYR TYR A . n 
A 1 333 GLN 333 407 407 GLN GLN A . n 
A 1 334 ALA 334 408 408 ALA ALA A . n 
A 1 335 GLY 335 409 409 GLY GLY A . n 
A 1 336 ILE 336 410 410 ILE ILE A . n 
A 1 337 LYS 337 411 411 LYS LYS A . n 
A 1 338 GLY 338 412 412 GLY GLY A . n 
A 1 339 ASN 339 413 413 ASN ASN A . n 
A 1 340 PHE 340 414 414 PHE PHE A . n 
A 1 341 TYR 341 415 415 TYR TYR A . n 
A 1 342 PRO 342 416 416 PRO PRO A . n 
A 1 343 THR 343 417 417 THR THR A . n 
A 1 344 VAL 344 418 418 VAL VAL A . n 
A 1 345 LEU 345 419 419 LEU LEU A . n 
A 1 346 ASN 346 420 420 ASN ASN A . n 
A 1 347 ALA 347 421 421 ALA ALA A . n 
A 1 348 SER 348 422 422 SER SER A . n 
A 1 349 ASN 349 423 423 ASN ASN A . n 
A 1 350 GLU 350 424 424 GLU GLU A . n 
A 1 351 ILE 351 425 425 ILE ILE A . n 
A 1 352 ALA 352 426 426 ALA ALA A . n 
A 1 353 ASN 353 427 427 ASN ASN A . n 
A 1 354 ASN 354 428 428 ASN ASN A . n 
A 1 355 LEU 355 429 429 LEU LEU A . n 
A 1 356 PHE 356 430 430 PHE PHE A . n 
A 1 357 LEU 357 431 431 LEU LEU A . n 
A 1 358 ASN 358 432 432 ASN ASN A . n 
A 1 359 ASN 359 433 433 ASN ASN A . n 
A 1 360 LYS 360 434 434 LYS LYS A . n 
A 1 361 ILE 361 435 435 ILE ILE A . n 
A 1 362 LYS 362 436 436 LYS LYS A . n 
A 1 363 TYR 363 437 437 TYR TYR A . n 
A 1 364 PHE 364 438 438 PHE PHE A . n 
A 1 365 ASP 365 439 439 ASP ASP A . n 
A 1 366 ILE 366 440 440 ILE ILE A . n 
A 1 367 SER 367 441 441 SER SER A . n 
A 1 368 SER 368 442 442 SER SER A . n 
A 1 369 ILE 369 443 443 ILE ILE A . n 
A 1 370 ILE 370 444 444 ILE ILE A . n 
A 1 371 SER 371 445 445 SER SER A . n 
A 1 372 GLN 372 446 446 GLN GLN A . n 
A 1 373 VAL 373 447 447 VAL VAL A . n 
A 1 374 LEU 374 448 448 LEU LEU A . n 
A 1 375 GLU 375 449 449 GLU GLU A . n 
A 1 376 SER 376 450 450 SER SER A . n 
A 1 377 PHE 377 451 451 PHE PHE A . n 
A 1 378 ASN 378 452 452 ASN ASN A . n 
A 1 379 SER 379 453 453 SER SER A . n 
A 1 380 GLN 380 454 454 GLN GLN A . n 
A 1 381 LYS 381 455 455 LYS LYS A . n 
A 1 382 VAL 382 456 456 VAL VAL A . n 
A 1 383 SER 383 457 457 SER SER A . n 
A 1 384 GLU 384 458 458 GLU GLU A . n 
A 1 385 ASN 385 459 459 ASN ASN A . n 
A 1 386 SER 386 460 460 SER SER A . n 
A 1 387 GLU 387 461 461 GLU GLU A . n 
A 1 388 ASP 388 462 462 ASP ASP A . n 
A 1 389 LEU 389 463 463 LEU LEU A . n 
A 1 390 MET 390 464 464 MET MET A . n 
A 1 391 LYS 391 465 465 LYS LYS A . n 
A 1 392 GLN 392 466 466 GLN GLN A . n 
A 1 393 ILE 393 467 467 ILE ILE A . n 
A 1 394 LEU 394 468 468 LEU LEU A . n 
A 1 395 GLN 395 469 469 GLN GLN A . n 
A 1 396 ILE 396 470 470 ILE ILE A . n 
A 1 397 HIS 397 471 471 HIS HIS A . n 
A 1 398 SER 398 472 472 SER SER A . n 
A 1 399 TRP 399 473 473 TRP TRP A . n 
A 1 400 ALA 400 474 474 ALA ALA A . n 
A 1 401 LYS 401 475 475 LYS LYS A . n 
A 1 402 ASP 402 476 476 ASP ASP A . n 
A 1 403 LYS 403 477 477 LYS LYS A . n 
A 1 404 ALA 404 478 478 ALA ALA A . n 
A 1 405 THR 405 479 479 THR THR A . n 
A 1 406 ASP 406 480 480 ASP ASP A . n 
A 1 407 ILE 407 481 481 ILE ILE A . n 
A 1 408 TYR 408 482 482 TYR TYR A . n 
A 1 409 ASN 409 483 483 ASN ASN A . n 
A 1 410 LYS 410 484 484 LYS LYS A . n 
A 1 411 HIS 411 485 485 HIS HIS A . n 
A 1 412 ASN 412 486 486 ASN ASN A . n 
A 1 413 SER 413 487 ?   ?   ?   A . n 
A 1 414 SER 414 488 ?   ?   ?   A . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 A1L2H ? ? A1L2H ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MN    ? ? MN    ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NDP   ? ? NDP   ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NDP   1   501 501 NDP   NDP A . 
C 3 MN    1   502 502 MN    MN  A . 
D 4 A1L2H 1   503 1   A1L2H LIG A . 
E 5 GOL   1   504 601 GOL   GOL A . 
F 6 HOH   1   601 502 HOH   HOH A . 
F 6 HOH   2   602 266 HOH   HOH A . 
F 6 HOH   3   603 268 HOH   HOH A . 
F 6 HOH   4   604 219 HOH   HOH A . 
F 6 HOH   5   605 177 HOH   HOH A . 
F 6 HOH   6   606 169 HOH   HOH A . 
F 6 HOH   7   607 393 HOH   HOH A . 
F 6 HOH   8   608 341 HOH   HOH A . 
F 6 HOH   9   609 306 HOH   HOH A . 
F 6 HOH   10  610 391 HOH   HOH A . 
F 6 HOH   11  611 151 HOH   HOH A . 
F 6 HOH   12  612 76  HOH   HOH A . 
F 6 HOH   13  613 47  HOH   HOH A . 
F 6 HOH   14  614 356 HOH   HOH A . 
F 6 HOH   15  615 218 HOH   HOH A . 
F 6 HOH   16  616 313 HOH   HOH A . 
F 6 HOH   17  617 278 HOH   HOH A . 
F 6 HOH   18  618 89  HOH   HOH A . 
F 6 HOH   19  619 183 HOH   HOH A . 
F 6 HOH   20  620 106 HOH   HOH A . 
F 6 HOH   21  621 59  HOH   HOH A . 
F 6 HOH   22  622 117 HOH   HOH A . 
F 6 HOH   23  623 244 HOH   HOH A . 
F 6 HOH   24  624 299 HOH   HOH A . 
F 6 HOH   25  625 186 HOH   HOH A . 
F 6 HOH   26  626 152 HOH   HOH A . 
F 6 HOH   27  627 224 HOH   HOH A . 
F 6 HOH   28  628 118 HOH   HOH A . 
F 6 HOH   29  629 12  HOH   HOH A . 
F 6 HOH   30  630 161 HOH   HOH A . 
F 6 HOH   31  631 87  HOH   HOH A . 
F 6 HOH   32  632 162 HOH   HOH A . 
F 6 HOH   33  633 134 HOH   HOH A . 
F 6 HOH   34  634 48  HOH   HOH A . 
F 6 HOH   35  635 129 HOH   HOH A . 
F 6 HOH   36  636 88  HOH   HOH A . 
F 6 HOH   37  637 40  HOH   HOH A . 
F 6 HOH   38  638 115 HOH   HOH A . 
F 6 HOH   39  639 324 HOH   HOH A . 
F 6 HOH   40  640 9   HOH   HOH A . 
F 6 HOH   41  641 208 HOH   HOH A . 
F 6 HOH   42  642 209 HOH   HOH A . 
F 6 HOH   43  643 52  HOH   HOH A . 
F 6 HOH   44  644 121 HOH   HOH A . 
F 6 HOH   45  645 6   HOH   HOH A . 
F 6 HOH   46  646 254 HOH   HOH A . 
F 6 HOH   47  647 398 HOH   HOH A . 
F 6 HOH   48  648 35  HOH   HOH A . 
F 6 HOH   49  649 138 HOH   HOH A . 
F 6 HOH   50  650 263 HOH   HOH A . 
F 6 HOH   51  651 17  HOH   HOH A . 
F 6 HOH   52  652 69  HOH   HOH A . 
F 6 HOH   53  653 171 HOH   HOH A . 
F 6 HOH   54  654 1   HOH   HOH A . 
F 6 HOH   55  655 158 HOH   HOH A . 
F 6 HOH   56  656 175 HOH   HOH A . 
F 6 HOH   57  657 137 HOH   HOH A . 
F 6 HOH   58  658 428 HOH   HOH A . 
F 6 HOH   59  659 39  HOH   HOH A . 
F 6 HOH   60  660 29  HOH   HOH A . 
F 6 HOH   61  661 363 HOH   HOH A . 
F 6 HOH   62  662 82  HOH   HOH A . 
F 6 HOH   63  663 44  HOH   HOH A . 
F 6 HOH   64  664 122 HOH   HOH A . 
F 6 HOH   65  665 16  HOH   HOH A . 
F 6 HOH   66  666 429 HOH   HOH A . 
F 6 HOH   67  667 75  HOH   HOH A . 
F 6 HOH   68  668 378 HOH   HOH A . 
F 6 HOH   69  669 23  HOH   HOH A . 
F 6 HOH   70  670 179 HOH   HOH A . 
F 6 HOH   71  671 109 HOH   HOH A . 
F 6 HOH   72  672 5   HOH   HOH A . 
F 6 HOH   73  673 316 HOH   HOH A . 
F 6 HOH   74  674 68  HOH   HOH A . 
F 6 HOH   75  675 33  HOH   HOH A . 
F 6 HOH   76  676 36  HOH   HOH A . 
F 6 HOH   77  677 18  HOH   HOH A . 
F 6 HOH   78  678 104 HOH   HOH A . 
F 6 HOH   79  679 189 HOH   HOH A . 
F 6 HOH   80  680 301 HOH   HOH A . 
F 6 HOH   81  681 32  HOH   HOH A . 
F 6 HOH   82  682 41  HOH   HOH A . 
F 6 HOH   83  683 62  HOH   HOH A . 
F 6 HOH   84  684 190 HOH   HOH A . 
F 6 HOH   85  685 77  HOH   HOH A . 
F 6 HOH   86  686 72  HOH   HOH A . 
F 6 HOH   87  687 329 HOH   HOH A . 
F 6 HOH   88  688 148 HOH   HOH A . 
F 6 HOH   89  689 130 HOH   HOH A . 
F 6 HOH   90  690 24  HOH   HOH A . 
F 6 HOH   91  691 103 HOH   HOH A . 
F 6 HOH   92  692 310 HOH   HOH A . 
F 6 HOH   93  693 114 HOH   HOH A . 
F 6 HOH   94  694 21  HOH   HOH A . 
F 6 HOH   95  695 332 HOH   HOH A . 
F 6 HOH   96  696 101 HOH   HOH A . 
F 6 HOH   97  697 95  HOH   HOH A . 
F 6 HOH   98  698 285 HOH   HOH A . 
F 6 HOH   99  699 53  HOH   HOH A . 
F 6 HOH   100 700 74  HOH   HOH A . 
F 6 HOH   101 701 333 HOH   HOH A . 
F 6 HOH   102 702 149 HOH   HOH A . 
F 6 HOH   103 703 61  HOH   HOH A . 
F 6 HOH   104 704 64  HOH   HOH A . 
F 6 HOH   105 705 102 HOH   HOH A . 
F 6 HOH   106 706 178 HOH   HOH A . 
F 6 HOH   107 707 108 HOH   HOH A . 
F 6 HOH   108 708 28  HOH   HOH A . 
F 6 HOH   109 709 66  HOH   HOH A . 
F 6 HOH   110 710 67  HOH   HOH A . 
F 6 HOH   111 711 43  HOH   HOH A . 
F 6 HOH   112 712 99  HOH   HOH A . 
F 6 HOH   113 713 195 HOH   HOH A . 
F 6 HOH   114 714 355 HOH   HOH A . 
F 6 HOH   115 715 168 HOH   HOH A . 
F 6 HOH   116 716 131 HOH   HOH A . 
F 6 HOH   117 717 54  HOH   HOH A . 
F 6 HOH   118 718 427 HOH   HOH A . 
F 6 HOH   119 719 426 HOH   HOH A . 
F 6 HOH   120 720 19  HOH   HOH A . 
F 6 HOH   121 721 163 HOH   HOH A . 
F 6 HOH   122 722 146 HOH   HOH A . 
F 6 HOH   123 723 90  HOH   HOH A . 
F 6 HOH   124 724 73  HOH   HOH A . 
F 6 HOH   125 725 153 HOH   HOH A . 
F 6 HOH   126 726 55  HOH   HOH A . 
F 6 HOH   127 727 172 HOH   HOH A . 
F 6 HOH   128 728 311 HOH   HOH A . 
F 6 HOH   129 729 223 HOH   HOH A . 
F 6 HOH   130 730 34  HOH   HOH A . 
F 6 HOH   131 731 376 HOH   HOH A . 
F 6 HOH   132 732 120 HOH   HOH A . 
F 6 HOH   133 733 111 HOH   HOH A . 
F 6 HOH   134 734 432 HOH   HOH A . 
F 6 HOH   135 735 22  HOH   HOH A . 
F 6 HOH   136 736 110 HOH   HOH A . 
F 6 HOH   137 737 25  HOH   HOH A . 
F 6 HOH   138 738 280 HOH   HOH A . 
F 6 HOH   139 739 200 HOH   HOH A . 
F 6 HOH   140 740 8   HOH   HOH A . 
F 6 HOH   141 741 94  HOH   HOH A . 
F 6 HOH   142 742 79  HOH   HOH A . 
F 6 HOH   143 743 165 HOH   HOH A . 
F 6 HOH   144 744 227 HOH   HOH A . 
F 6 HOH   145 745 119 HOH   HOH A . 
F 6 HOH   146 746 37  HOH   HOH A . 
F 6 HOH   147 747 139 HOH   HOH A . 
F 6 HOH   148 748 71  HOH   HOH A . 
F 6 HOH   149 749 4   HOH   HOH A . 
F 6 HOH   150 750 86  HOH   HOH A . 
F 6 HOH   151 751 145 HOH   HOH A . 
F 6 HOH   152 752 2   HOH   HOH A . 
F 6 HOH   153 753 7   HOH   HOH A . 
F 6 HOH   154 754 167 HOH   HOH A . 
F 6 HOH   155 755 319 HOH   HOH A . 
F 6 HOH   156 756 65  HOH   HOH A . 
F 6 HOH   157 757 107 HOH   HOH A . 
F 6 HOH   158 758 98  HOH   HOH A . 
F 6 HOH   159 759 27  HOH   HOH A . 
F 6 HOH   160 760 3   HOH   HOH A . 
F 6 HOH   161 761 180 HOH   HOH A . 
F 6 HOH   162 762 136 HOH   HOH A . 
F 6 HOH   163 763 173 HOH   HOH A . 
F 6 HOH   164 764 80  HOH   HOH A . 
F 6 HOH   165 765 38  HOH   HOH A . 
F 6 HOH   166 766 191 HOH   HOH A . 
F 6 HOH   167 767 501 HOH   HOH A . 
F 6 HOH   168 768 105 HOH   HOH A . 
F 6 HOH   169 769 133 HOH   HOH A . 
F 6 HOH   170 770 303 HOH   HOH A . 
F 6 HOH   171 771 123 HOH   HOH A . 
F 6 HOH   172 772 196 HOH   HOH A . 
F 6 HOH   173 773 112 HOH   HOH A . 
F 6 HOH   174 774 81  HOH   HOH A . 
F 6 HOH   175 775 10  HOH   HOH A . 
F 6 HOH   176 776 194 HOH   HOH A . 
F 6 HOH   177 777 60  HOH   HOH A . 
F 6 HOH   178 778 277 HOH   HOH A . 
F 6 HOH   179 779 279 HOH   HOH A . 
F 6 HOH   180 780 404 HOH   HOH A . 
F 6 HOH   181 781 49  HOH   HOH A . 
F 6 HOH   182 782 113 HOH   HOH A . 
F 6 HOH   183 783 14  HOH   HOH A . 
F 6 HOH   184 784 182 HOH   HOH A . 
F 6 HOH   185 785 46  HOH   HOH A . 
F 6 HOH   186 786 15  HOH   HOH A . 
F 6 HOH   187 787 116 HOH   HOH A . 
F 6 HOH   188 788 83  HOH   HOH A . 
F 6 HOH   189 789 202 HOH   HOH A . 
F 6 HOH   190 790 132 HOH   HOH A . 
F 6 HOH   191 791 395 HOH   HOH A . 
F 6 HOH   192 792 269 HOH   HOH A . 
F 6 HOH   193 793 185 HOH   HOH A . 
F 6 HOH   194 794 97  HOH   HOH A . 
F 6 HOH   195 795 294 HOH   HOH A . 
F 6 HOH   196 796 126 HOH   HOH A . 
F 6 HOH   197 797 300 HOH   HOH A . 
F 6 HOH   198 798 156 HOH   HOH A . 
F 6 HOH   199 799 217 HOH   HOH A . 
F 6 HOH   200 800 11  HOH   HOH A . 
F 6 HOH   201 801 31  HOH   HOH A . 
F 6 HOH   202 802 210 HOH   HOH A . 
F 6 HOH   203 803 174 HOH   HOH A . 
F 6 HOH   204 804 141 HOH   HOH A . 
F 6 HOH   205 805 222 HOH   HOH A . 
F 6 HOH   206 806 205 HOH   HOH A . 
F 6 HOH   207 807 215 HOH   HOH A . 
F 6 HOH   208 808 78  HOH   HOH A . 
F 6 HOH   209 809 286 HOH   HOH A . 
F 6 HOH   210 810 13  HOH   HOH A . 
F 6 HOH   211 811 85  HOH   HOH A . 
F 6 HOH   212 812 365 HOH   HOH A . 
F 6 HOH   213 813 193 HOH   HOH A . 
F 6 HOH   214 814 203 HOH   HOH A . 
F 6 HOH   215 815 390 HOH   HOH A . 
F 6 HOH   216 816 124 HOH   HOH A . 
F 6 HOH   217 817 144 HOH   HOH A . 
F 6 HOH   218 818 199 HOH   HOH A . 
F 6 HOH   219 819 50  HOH   HOH A . 
F 6 HOH   220 820 143 HOH   HOH A . 
F 6 HOH   221 821 30  HOH   HOH A . 
F 6 HOH   222 822 305 HOH   HOH A . 
F 6 HOH   223 823 296 HOH   HOH A . 
F 6 HOH   224 824 20  HOH   HOH A . 
F 6 HOH   225 825 425 HOH   HOH A . 
F 6 HOH   226 826 84  HOH   HOH A . 
F 6 HOH   227 827 56  HOH   HOH A . 
F 6 HOH   228 828 142 HOH   HOH A . 
F 6 HOH   229 829 251 HOH   HOH A . 
F 6 HOH   230 830 431 HOH   HOH A . 
F 6 HOH   231 831 92  HOH   HOH A . 
F 6 HOH   232 832 298 HOH   HOH A . 
F 6 HOH   233 833 297 HOH   HOH A . 
F 6 HOH   234 834 283 HOH   HOH A . 
F 6 HOH   235 835 265 HOH   HOH A . 
F 6 HOH   236 836 204 HOH   HOH A . 
F 6 HOH   237 837 360 HOH   HOH A . 
F 6 HOH   238 838 213 HOH   HOH A . 
F 6 HOH   239 839 230 HOH   HOH A . 
F 6 HOH   240 840 309 HOH   HOH A . 
F 6 HOH   241 841 45  HOH   HOH A . 
F 6 HOH   242 842 128 HOH   HOH A . 
F 6 HOH   243 843 284 HOH   HOH A . 
F 6 HOH   244 844 26  HOH   HOH A . 
F 6 HOH   245 845 160 HOH   HOH A . 
F 6 HOH   246 846 220 HOH   HOH A . 
F 6 HOH   247 847 140 HOH   HOH A . 
F 6 HOH   248 848 135 HOH   HOH A . 
F 6 HOH   249 849 176 HOH   HOH A . 
F 6 HOH   250 850 155 HOH   HOH A . 
F 6 HOH   251 851 289 HOH   HOH A . 
F 6 HOH   252 852 93  HOH   HOH A . 
F 6 HOH   253 853 63  HOH   HOH A . 
F 6 HOH   254 854 225 HOH   HOH A . 
F 6 HOH   255 855 58  HOH   HOH A . 
F 6 HOH   256 856 125 HOH   HOH A . 
F 6 HOH   257 857 346 HOH   HOH A . 
F 6 HOH   258 858 127 HOH   HOH A . 
F 6 HOH   259 859 70  HOH   HOH A . 
F 6 HOH   260 860 420 HOH   HOH A . 
F 6 HOH   261 861 91  HOH   HOH A . 
F 6 HOH   262 862 164 HOH   HOH A . 
F 6 HOH   263 863 100 HOH   HOH A . 
F 6 HOH   264 864 51  HOH   HOH A . 
F 6 HOH   265 865 273 HOH   HOH A . 
F 6 HOH   266 866 207 HOH   HOH A . 
F 6 HOH   267 867 96  HOH   HOH A . 
F 6 HOH   268 868 157 HOH   HOH A . 
F 6 HOH   269 869 221 HOH   HOH A . 
F 6 HOH   270 870 170 HOH   HOH A . 
F 6 HOH   271 871 187 HOH   HOH A . 
F 6 HOH   272 872 147 HOH   HOH A . 
F 6 HOH   273 873 216 HOH   HOH A . 
F 6 HOH   274 874 338 HOH   HOH A . 
F 6 HOH   275 875 351 HOH   HOH A . 
F 6 HOH   276 876 154 HOH   HOH A . 
F 6 HOH   277 877 379 HOH   HOH A . 
F 6 HOH   278 878 293 HOH   HOH A . 
F 6 HOH   279 879 415 HOH   HOH A . 
F 6 HOH   280 880 417 HOH   HOH A . 
F 6 HOH   281 881 226 HOH   HOH A . 
F 6 HOH   282 882 201 HOH   HOH A . 
F 6 HOH   283 883 259 HOH   HOH A . 
F 6 HOH   284 884 322 HOH   HOH A . 
F 6 HOH   285 885 377 HOH   HOH A . 
F 6 HOH   286 886 150 HOH   HOH A . 
F 6 HOH   287 887 290 HOH   HOH A . 
F 6 HOH   288 888 206 HOH   HOH A . 
F 6 HOH   289 889 231 HOH   HOH A . 
F 6 HOH   290 890 361 HOH   HOH A . 
F 6 HOH   291 891 233 HOH   HOH A . 
F 6 HOH   292 892 308 HOH   HOH A . 
F 6 HOH   293 893 397 HOH   HOH A . 
F 6 HOH   294 894 327 HOH   HOH A . 
F 6 HOH   295 895 406 HOH   HOH A . 
F 6 HOH   296 896 248 HOH   HOH A . 
F 6 HOH   297 897 249 HOH   HOH A . 
F 6 HOH   298 898 229 HOH   HOH A . 
F 6 HOH   299 899 257 HOH   HOH A . 
F 6 HOH   300 900 243 HOH   HOH A . 
F 6 HOH   301 901 339 HOH   HOH A . 
F 6 HOH   302 902 315 HOH   HOH A . 
F 6 HOH   303 903 245 HOH   HOH A . 
F 6 HOH   304 904 250 HOH   HOH A . 
F 6 HOH   305 905 276 HOH   HOH A . 
F 6 HOH   306 906 302 HOH   HOH A . 
F 6 HOH   307 907 381 HOH   HOH A . 
F 6 HOH   308 908 331 HOH   HOH A . 
F 6 HOH   309 909 307 HOH   HOH A . 
F 6 HOH   310 910 374 HOH   HOH A . 
F 6 HOH   311 911 382 HOH   HOH A . 
F 6 HOH   312 912 238 HOH   HOH A . 
F 6 HOH   313 913 350 HOH   HOH A . 
F 6 HOH   314 914 239 HOH   HOH A . 
F 6 HOH   315 915 405 HOH   HOH A . 
F 6 HOH   316 916 258 HOH   HOH A . 
F 6 HOH   317 917 242 HOH   HOH A . 
F 6 HOH   318 918 275 HOH   HOH A . 
F 6 HOH   319 919 345 HOH   HOH A . 
F 6 HOH   320 920 264 HOH   HOH A . 
F 6 HOH   321 921 237 HOH   HOH A . 
F 6 HOH   322 922 380 HOH   HOH A . 
F 6 HOH   323 923 320 HOH   HOH A . 
F 6 HOH   324 924 261 HOH   HOH A . 
F 6 HOH   325 925 357 HOH   HOH A . 
F 6 HOH   326 926 236 HOH   HOH A . 
F 6 HOH   327 927 367 HOH   HOH A . 
F 6 HOH   328 928 255 HOH   HOH A . 
F 6 HOH   329 929 399 HOH   HOH A . 
F 6 HOH   330 930 271 HOH   HOH A . 
F 6 HOH   331 931 252 HOH   HOH A . 
F 6 HOH   332 932 422 HOH   HOH A . 
F 6 HOH   333 933 241 HOH   HOH A . 
F 6 HOH   334 934 262 HOH   HOH A . 
F 6 HOH   335 935 433 HOH   HOH A . 
F 6 HOH   336 936 424 HOH   HOH A . 
F 6 HOH   337 937 385 HOH   HOH A . 
F 6 HOH   338 938 323 HOH   HOH A . 
F 6 HOH   339 939 358 HOH   HOH A . 
F 6 HOH   340 940 232 HOH   HOH A . 
F 6 HOH   341 941 334 HOH   HOH A . 
F 6 HOH   342 942 235 HOH   HOH A . 
F 6 HOH   343 943 330 HOH   HOH A . 
F 6 HOH   344 944 343 HOH   HOH A . 
F 6 HOH   345 945 419 HOH   HOH A . 
F 6 HOH   346 946 253 HOH   HOH A . 
F 6 HOH   347 947 246 HOH   HOH A . 
F 6 HOH   348 948 292 HOH   HOH A . 
F 6 HOH   349 949 373 HOH   HOH A . 
F 6 HOH   350 950 274 HOH   HOH A . 
F 6 HOH   351 951 234 HOH   HOH A . 
F 6 HOH   352 952 314 HOH   HOH A . 
F 6 HOH   353 953 288 HOH   HOH A . 
F 6 HOH   354 954 240 HOH   HOH A . 
F 6 HOH   355 955 272 HOH   HOH A . 
F 6 HOH   356 956 389 HOH   HOH A . 
F 6 HOH   357 957 383 HOH   HOH A . 
F 6 HOH   358 958 291 HOH   HOH A . 
F 6 HOH   359 959 348 HOH   HOH A . 
F 6 HOH   360 960 353 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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 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                     8ZXX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     92.616 
_cell.length_a_esd                 ? 
_cell.length_b                     92.616 
_cell.length_b_esd                 ? 
_cell.length_c                     105.043 
_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                         8ZXX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZXX 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.76 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.46 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '0.08 M MES-NaOH pH 6.0, 16%(w/v) PEG6000, and 0.16 M NaCl' 
_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         2023-07-28 
_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   0.90000 
_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                        'SPRING-8 BEAMLINE BL44XU' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.90000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL44XU 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          14.49 
_reflns.entry_id                                       8ZXX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.23 
_reflns.d_resolution_low                               42.37 
_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                                     150636 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.4 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.136 
_reflns.pdbx_Rpim_I_all                                0.066 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.984 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.118 
_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                                    1.23 
_reflns_shell.d_res_low                                     1.25 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             7387 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               4.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.097 
_reflns_shell.pdbx_Rpim_I_all                               0.543 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.538 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.950 
_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]                            -0.10 
_refine.aniso_B[1][2]                            -0.05 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.10 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.32 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.026 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.972 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 8ZXX 
_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                            1.23 
_refine.ls_d_res_low                             42.37 
_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                     142829 
_refine.ls_number_reflns_R_free                  7600 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.76 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16747 
_refine.ls_R_factor_R_free                       0.17804 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16691 
_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                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.036 
_refine.pdbx_overall_ESU_R_Free                  0.036 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_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                             1.184 
_refine.overall_SU_ML                            0.027 
_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                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.23 
_refine_hist.d_res_low                        42.37 
_refine_hist.number_atoms_solvent             360 
_refine_hist.number_atoms_total               3726 
_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        3286 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         80 
_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' ? 0.013  0.012  3431 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3303 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.924  1.819  4641 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.623  1.776  7647 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 5.932  5.000  410  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.947  5.000  8    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.582 10.000 641  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.099  0.200  529  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  3826 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  721  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.580  1.599  1643 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.580  1.598  1643 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.377  2.871  2052 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.380  2.874  2053 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.907  1.981  1788 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.906  1.981  1789 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.462  3.471  2590 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.593  18.28  3996 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.470  15.87  3900 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.230 
_refine_ls_shell.d_res_low                        1.262 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             570 
_refine_ls_shell.number_reflns_R_work             10435 
_refine_ls_shell.percent_reflns_obs               99.59 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.291 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.280 
# 
_struct.entry_id                     8ZXX 
_struct.title                        'PfDXR - Mn2+ - NADPH - TAKK442 quaternary complex' 
_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        8ZXX 
_struct_keywords.text            'malaria, ISOMERASE' 
_struct_keywords.pdbx_keywords   ISOMERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DXR_PLAFX 
_struct_ref.pdbx_db_accession          O96693 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;KKPINVAIFGSTGSIGTNALNIIRECNKIENVFNVKALYVNKSVNELYEQAREFLPEYLCIHDKSVYEELKELVKNIKDY
KPIILCGDEGMKEICSSNSIDKIVIGIDSFQGLYSTMYAIMNNKIVALANKESIVSAGFFLKKLLNIHKNAKIIPVDSEH
SAIFQCLDNNKVLKTKCLQDNFSKINNINKIFLCSSGGPFQNLTMDELKNVTSENALKHPKWKMGKKITIDSATMMNKGL
EVIETHFLFDVDYNDIEVIVHKECIIHSCVEFIDKSVISQMYYPDMQIPILYSLTWPDRIKTNLKPLDLAQVSTLTFHKP
SLEHFPCIKLAYQAGIKGNFYPTVLNASNEIANNLFLNNKIKYFDISSIISQVLESFNSQKVSENSEDLMKQILQIHSWA
KDKATDIYNKHNSS
;
_struct_ref.pdbx_align_begin           75 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8ZXX 
_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                 414 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O96693 
_struct_ref_seq.db_align_beg                  75 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  488 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       75 
_struct_ref_seq.pdbx_auth_seq_align_end       488 
# 
_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)' 6870  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  31610 ? 
# 
_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   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'       1_555 x,y,z 1.0 0.0 0.0 0.0 0.0 1.0  0.0 0.0 0.0 0.0 1.0  0.0           
2 'point symmetry operation' ?     ?     1.0 0.0 0.0 0.0 0.0 -1.0 0.0 0.0 0.0 0.0 -1.0 70.0406666667 
# 
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 GLY A 13  ? GLU A 30  ? GLY A 87  GLU A 104 1 ? 18 
HELX_P HELX_P2  AA2 SER A 43  ? LEU A 55  ? SER A 117 LEU A 129 1 ? 13 
HELX_P HELX_P3  AA3 ASP A 63  ? SER A 65  ? ASP A 137 SER A 139 5 ? 3  
HELX_P HELX_P4  AA4 VAL A 66  ? LYS A 75  ? VAL A 140 LYS A 149 1 ? 10 
HELX_P HELX_P5  AA5 GLY A 87  ? SER A 96  ? GLY A 161 SER A 170 1 ? 10 
HELX_P HELX_P6  AA6 SER A 109 ? GLN A 111 ? SER A 183 GLN A 185 5 ? 3  
HELX_P HELX_P7  AA7 GLY A 112 ? ASN A 122 ? GLY A 186 ASN A 196 1 ? 11 
HELX_P HELX_P8  AA8 LYS A 131 ? HIS A 148 ? LYS A 205 HIS A 222 1 ? 18 
HELX_P HELX_P9  AA9 ASP A 157 ? CYS A 166 ? ASP A 231 CYS A 240 1 ? 10 
HELX_P HELX_P10 AB1 ASP A 168 ? LEU A 173 ? ASP A 242 LEU A 247 1 ? 6  
HELX_P HELX_P11 AB2 ASN A 181 ? ASN A 186 ? ASN A 255 ASN A 260 1 ? 6  
HELX_P HELX_P12 AB3 THR A 204 ? ASN A 210 ? THR A 278 ASN A 284 1 ? 7  
HELX_P HELX_P13 AB4 THR A 212 ? LYS A 218 ? THR A 286 LYS A 292 1 ? 7  
HELX_P HELX_P14 AB5 GLY A 225 ? MET A 235 ? GLY A 299 MET A 309 1 ? 11 
HELX_P HELX_P15 AB6 MET A 235 ? ASP A 250 ? MET A 309 ASP A 324 1 ? 16 
HELX_P HELX_P16 AB7 ASP A 252 ? ASN A 254 ? ASP A 326 ASN A 328 5 ? 3  
HELX_P HELX_P17 AB8 MET A 286 ? TRP A 296 ? MET A 360 TRP A 370 1 ? 11 
HELX_P HELX_P18 AB9 ASP A 308 ? SER A 313 ? ASP A 382 SER A 387 1 ? 6  
HELX_P HELX_P19 AC1 PHE A 325 ? GLY A 338 ? PHE A 399 GLY A 412 1 ? 14 
HELX_P HELX_P20 AC2 PHE A 340 ? ASN A 358 ? PHE A 414 ASN A 432 1 ? 19 
HELX_P HELX_P21 AC3 LYS A 362 ? PHE A 377 ? LYS A 436 PHE A 451 1 ? 16 
HELX_P HELX_P22 AC4 ASN A 385 ? ASN A 412 ? ASN A 459 ASN A 486 1 ? 28 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A ASP 157 OD1 ? ? ? 1_555 C MN    . MN ? ? A ASP 231 A MN    502 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc2 metalc ? ? A GLU 159 OE1 ? ? ? 1_555 C MN    . MN ? ? A GLU 233 A MN    502 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
metalc3 metalc ? ? A GLU 241 OE2 ? ? ? 1_555 C MN    . MN ? ? A GLU 315 A MN    502 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc4 metalc ? ? C MN  .   MN  ? ? ? 1_555 D A1L2H . O6 ? ? A MN  502 A A1L2H 503 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc5 metalc ? ? C MN  .   MN  ? ? ? 1_555 D A1L2H . O5 ? ? A MN  502 A A1L2H 503 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP   157 ? A ASP   231 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 OE1 ? A GLU   159 ? A GLU   233 ? 1_555 99.6  ? 
2  OD1 ? A ASP   157 ? A ASP   231 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 OE2 ? A GLU   241 ? A GLU   315 ? 1_555 98.3  ? 
3  OE1 ? A GLU   159 ? A GLU   233 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 OE2 ? A GLU   241 ? A GLU   315 ? 1_555 95.5  ? 
4  OD1 ? A ASP   157 ? A ASP   231 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O6  ? D A1L2H .   ? A A1L2H 503 ? 1_555 108.3 ? 
5  OE1 ? A GLU   159 ? A GLU   233 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O6  ? D A1L2H .   ? A A1L2H 503 ? 1_555 151.4 ? 
6  OE2 ? A GLU   241 ? A GLU   315 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O6  ? D A1L2H .   ? A A1L2H 503 ? 1_555 86.7  ? 
7  OD1 ? A ASP   157 ? A ASP   231 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O5  ? D A1L2H .   ? A A1L2H 503 ? 1_555 90.9  ? 
8  OE1 ? A GLU   159 ? A GLU   233 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O5  ? D A1L2H .   ? A A1L2H 503 ? 1_555 96.6  ? 
9  OE2 ? A GLU   241 ? A GLU   315 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O5  ? D A1L2H .   ? A A1L2H 503 ? 1_555 163.5 ? 
10 O6  ? D A1L2H .   ? A A1L2H 503 ? 1_555 MN ? C MN . ? A MN 502 ? 1_555 O5  ? D A1L2H .   ? A A1L2H 503 ? 1_555 77.3  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TRP 
_struct_mon_prot_cis.label_seq_id           296 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TRP 
_struct_mon_prot_cis.auth_seq_id            370 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    297 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     371 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       6.04 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 83  ? CYS A 86  ? ILE A 157 CYS A 160 
AA1 2 TYR A 58  ? ILE A 61  ? TYR A 132 ILE A 135 
AA1 3 PHE A 33  ? VAL A 40  ? PHE A 107 VAL A 114 
AA1 4 ILE A 4   ? PHE A 9   ? ILE A 78  PHE A 83  
AA1 5 LYS A 102 ? ILE A 105 ? LYS A 176 ILE A 179 
AA1 6 ILE A 125 ? LEU A 128 ? ILE A 199 LEU A 202 
AA1 7 LYS A 152 ? PRO A 155 ? LYS A 226 PRO A 229 
AA2 1 ILE A 256 ? VAL A 260 ? ILE A 330 VAL A 334 
AA2 2 ILE A 188 ? SER A 195 ? ILE A 262 SER A 269 
AA2 3 ILE A 266 ? PHE A 272 ? ILE A 340 PHE A 346 
AA2 4 VAL A 277 ? MET A 281 ? VAL A 351 MET A 355 
# 
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 O LEU A 85  ? O LEU A 159 N LEU A 59  ? N LEU A 133 
AA1 2 3 O CYS A 60  ? O CYS A 134 N LEU A 38  ? N LEU A 112 
AA1 3 4 O LYS A 36  ? O LYS A 110 N VAL A 6   ? N VAL A 80  
AA1 4 5 N PHE A 9   ? N PHE A 83  O VAL A 104 ? O VAL A 178 
AA1 5 6 N ILE A 105 ? N ILE A 179 O ALA A 127 ? O ALA A 201 
AA1 6 7 N VAL A 126 ? N VAL A 200 O LYS A 152 ? O LYS A 226 
AA2 1 2 O GLU A 257 ? O GLU A 331 N LEU A 193 ? N LEU A 267 
AA2 2 3 N ASN A 189 ? N ASN A 263 O GLU A 271 ? O GLU A 345 
AA2 3 4 N VAL A 270 ? N VAL A 344 O ILE A 278 ? O ILE A 352 
# 
_pdbx_entry_details.entry_id                   8ZXX 
_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 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CE1 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_1             341 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            NE2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            HIS 
_pdbx_validate_rmsd_bond.auth_seq_id_2             341 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.208 
_pdbx_validate_rmsd_bond.bond_target_value         1.317 
_pdbx_validate_rmsd_bond.bond_deviation            -0.109 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A CYS 100 ? ? CA A CYS 100 ? ? C   A CYS 100 ? ? 121.09 111.50 9.59   1.20 N 
2 1 CG A MET 355 ? ? SD A MET 355 ? ? CE  A MET 355 ? ? 84.51  100.20 -15.69 1.60 N 
3 1 CB A ASP 359 ? ? CA A ASP 359 ? ? C   A ASP 359 ? ? 123.42 110.40 13.02  2.00 N 
4 1 CB A HIS 471 ? ? CG A HIS 471 ? ? CD2 A HIS 471 ? ? 141.39 131.40 9.99   1.20 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 GLU A 104 ? ? -172.30 142.48  
2 1 SER A 183 ? ? 69.54   -176.72 
3 1 ALA A 211 ? ? -142.48 28.20   
4 1 THR A 249 ? ? -146.13 -148.15 
5 1 SER A 342 ? ? 168.62  171.36  
6 1 LYS A 349 ? ? 85.32   0.97    
7 1 SER A 387 ? ? 74.65   -52.12  
8 1 ASN A 413 ? ? 55.18   -133.43 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         32.1688 
_pdbx_refine_tls.origin_y         7.3344 
_pdbx_refine_tls.origin_z         14.0211 
_pdbx_refine_tls.T[1][1]          0.0350 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0230 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0071 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0241 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0094 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0079 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.1431 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0997 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0164 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.2662 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.0523 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.1120 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0439 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.0170 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0181 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0642 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0615 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0261 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0004 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0083 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0176 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     76 
_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    A 
_pdbx_refine_tls_group.end_auth_seq_id     486 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
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 LYS 75  ? A LYS 1   
2 1 Y 1 A SER 487 ? A SER 413 
3 1 Y 1 A SER 488 ? A SER 414 
# 
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 
A1L2H N1   N  N N 1   
A1L2H C4   C  Y N 2   
A1L2H C5   C  Y N 3   
A1L2H C6   C  Y N 4   
A1L2H C7   C  N N 5   
A1L2H C8   C  N N 6   
A1L2H C10  C  N N 7   
A1L2H C13  C  N S 8   
A1L2H C15  C  N N 9   
A1L2H O6   O  N N 10  
A1L2H C16  C  N N 11  
A1L2H O5   O  N N 12  
A1L2H C14  C  N N 13  
A1L2H S1   S  N N 14  
A1L2H P1   P  N N 15  
A1L2H O4   O  N N 16  
A1L2H O3   O  N N 17  
A1L2H O2   O  N N 18  
A1L2H C1   C  Y N 19  
A1L2H C3   C  Y N 20  
A1L2H C2   C  Y N 21  
A1L2H O1   O  N N 22  
A1L2H C9   C  N N 23  
A1L2H C11  C  N N 24  
A1L2H C12  C  N N 25  
A1L2H H1   H  N N 26  
A1L2H H2   H  N N 27  
A1L2H H3   H  N N 28  
A1L2H H4   H  N N 29  
A1L2H H5   H  N N 30  
A1L2H H6   H  N N 31  
A1L2H H7   H  N N 32  
A1L2H H8   H  N N 33  
A1L2H H9   H  N N 34  
A1L2H H10  H  N N 35  
A1L2H H11  H  N N 36  
A1L2H H12  H  N N 37  
A1L2H H13  H  N N 38  
A1L2H H14  H  N N 39  
A1L2H H15  H  N N 40  
A1L2H H16  H  N N 41  
A1L2H H17  H  N N 42  
A1L2H H18  H  N N 43  
A1L2H H19  H  N N 44  
A1L2H H20  H  N N 45  
A1L2H H21  H  N N 46  
A1L2H H22  H  N N 47  
A1L2H H23  H  N N 48  
A1L2H H24  H  N N 49  
A1L2H H25  H  N N 50  
A1L2H H26  H  N N 51  
ALA   N    N  N N 52  
ALA   CA   C  N S 53  
ALA   C    C  N N 54  
ALA   O    O  N N 55  
ALA   CB   C  N N 56  
ALA   OXT  O  N N 57  
ALA   H    H  N N 58  
ALA   H2   H  N N 59  
ALA   HA   H  N N 60  
ALA   HB1  H  N N 61  
ALA   HB2  H  N N 62  
ALA   HB3  H  N N 63  
ALA   HXT  H  N N 64  
ARG   N    N  N N 65  
ARG   CA   C  N S 66  
ARG   C    C  N N 67  
ARG   O    O  N N 68  
ARG   CB   C  N N 69  
ARG   CG   C  N N 70  
ARG   CD   C  N N 71  
ARG   NE   N  N N 72  
ARG   CZ   C  N N 73  
ARG   NH1  N  N N 74  
ARG   NH2  N  N N 75  
ARG   OXT  O  N N 76  
ARG   H    H  N N 77  
ARG   H2   H  N N 78  
ARG   HA   H  N N 79  
ARG   HB2  H  N N 80  
ARG   HB3  H  N N 81  
ARG   HG2  H  N N 82  
ARG   HG3  H  N N 83  
ARG   HD2  H  N N 84  
ARG   HD3  H  N N 85  
ARG   HE   H  N N 86  
ARG   HH11 H  N N 87  
ARG   HH12 H  N N 88  
ARG   HH21 H  N N 89  
ARG   HH22 H  N N 90  
ARG   HXT  H  N N 91  
ASN   N    N  N N 92  
ASN   CA   C  N S 93  
ASN   C    C  N N 94  
ASN   O    O  N N 95  
ASN   CB   C  N N 96  
ASN   CG   C  N N 97  
ASN   OD1  O  N N 98  
ASN   ND2  N  N N 99  
ASN   OXT  O  N N 100 
ASN   H    H  N N 101 
ASN   H2   H  N N 102 
ASN   HA   H  N N 103 
ASN   HB2  H  N N 104 
ASN   HB3  H  N N 105 
ASN   HD21 H  N N 106 
ASN   HD22 H  N N 107 
ASN   HXT  H  N N 108 
ASP   N    N  N N 109 
ASP   CA   C  N S 110 
ASP   C    C  N N 111 
ASP   O    O  N N 112 
ASP   CB   C  N N 113 
ASP   CG   C  N N 114 
ASP   OD1  O  N N 115 
ASP   OD2  O  N N 116 
ASP   OXT  O  N N 117 
ASP   H    H  N N 118 
ASP   H2   H  N N 119 
ASP   HA   H  N N 120 
ASP   HB2  H  N N 121 
ASP   HB3  H  N N 122 
ASP   HD2  H  N N 123 
ASP   HXT  H  N N 124 
CYS   N    N  N N 125 
CYS   CA   C  N R 126 
CYS   C    C  N N 127 
CYS   O    O  N N 128 
CYS   CB   C  N N 129 
CYS   SG   S  N N 130 
CYS   OXT  O  N N 131 
CYS   H    H  N N 132 
CYS   H2   H  N N 133 
CYS   HA   H  N N 134 
CYS   HB2  H  N N 135 
CYS   HB3  H  N N 136 
CYS   HG   H  N N 137 
CYS   HXT  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
GOL   C1   C  N N 188 
GOL   O1   O  N N 189 
GOL   C2   C  N N 190 
GOL   O2   O  N N 191 
GOL   C3   C  N N 192 
GOL   O3   O  N N 193 
GOL   H11  H  N N 194 
GOL   H12  H  N N 195 
GOL   HO1  H  N N 196 
GOL   H2   H  N N 197 
GOL   HO2  H  N N 198 
GOL   H31  H  N N 199 
GOL   H32  H  N N 200 
GOL   HO3  H  N N 201 
HIS   N    N  N N 202 
HIS   CA   C  N S 203 
HIS   C    C  N N 204 
HIS   O    O  N N 205 
HIS   CB   C  N N 206 
HIS   CG   C  Y N 207 
HIS   ND1  N  Y N 208 
HIS   CD2  C  Y N 209 
HIS   CE1  C  Y N 210 
HIS   NE2  N  Y N 211 
HIS   OXT  O  N N 212 
HIS   H    H  N N 213 
HIS   H2   H  N N 214 
HIS   HA   H  N N 215 
HIS   HB2  H  N N 216 
HIS   HB3  H  N N 217 
HIS   HD1  H  N N 218 
HIS   HD2  H  N N 219 
HIS   HE1  H  N N 220 
HIS   HE2  H  N N 221 
HIS   HXT  H  N N 222 
HOH   O    O  N N 223 
HOH   H1   H  N N 224 
HOH   H2   H  N N 225 
ILE   N    N  N N 226 
ILE   CA   C  N S 227 
ILE   C    C  N N 228 
ILE   O    O  N N 229 
ILE   CB   C  N S 230 
ILE   CG1  C  N N 231 
ILE   CG2  C  N N 232 
ILE   CD1  C  N N 233 
ILE   OXT  O  N N 234 
ILE   H    H  N N 235 
ILE   H2   H  N N 236 
ILE   HA   H  N N 237 
ILE   HB   H  N N 238 
ILE   HG12 H  N N 239 
ILE   HG13 H  N N 240 
ILE   HG21 H  N N 241 
ILE   HG22 H  N N 242 
ILE   HG23 H  N N 243 
ILE   HD11 H  N N 244 
ILE   HD12 H  N N 245 
ILE   HD13 H  N N 246 
ILE   HXT  H  N N 247 
LEU   N    N  N N 248 
LEU   CA   C  N S 249 
LEU   C    C  N N 250 
LEU   O    O  N N 251 
LEU   CB   C  N N 252 
LEU   CG   C  N N 253 
LEU   CD1  C  N N 254 
LEU   CD2  C  N N 255 
LEU   OXT  O  N N 256 
LEU   H    H  N N 257 
LEU   H2   H  N N 258 
LEU   HA   H  N N 259 
LEU   HB2  H  N N 260 
LEU   HB3  H  N N 261 
LEU   HG   H  N N 262 
LEU   HD11 H  N N 263 
LEU   HD12 H  N N 264 
LEU   HD13 H  N N 265 
LEU   HD21 H  N N 266 
LEU   HD22 H  N N 267 
LEU   HD23 H  N N 268 
LEU   HXT  H  N N 269 
LYS   N    N  N N 270 
LYS   CA   C  N S 271 
LYS   C    C  N N 272 
LYS   O    O  N N 273 
LYS   CB   C  N N 274 
LYS   CG   C  N N 275 
LYS   CD   C  N N 276 
LYS   CE   C  N N 277 
LYS   NZ   N  N N 278 
LYS   OXT  O  N N 279 
LYS   H    H  N N 280 
LYS   H2   H  N N 281 
LYS   HA   H  N N 282 
LYS   HB2  H  N N 283 
LYS   HB3  H  N N 284 
LYS   HG2  H  N N 285 
LYS   HG3  H  N N 286 
LYS   HD2  H  N N 287 
LYS   HD3  H  N N 288 
LYS   HE2  H  N N 289 
LYS   HE3  H  N N 290 
LYS   HZ1  H  N N 291 
LYS   HZ2  H  N N 292 
LYS   HZ3  H  N N 293 
LYS   HXT  H  N N 294 
MET   N    N  N N 295 
MET   CA   C  N S 296 
MET   C    C  N N 297 
MET   O    O  N N 298 
MET   CB   C  N N 299 
MET   CG   C  N N 300 
MET   SD   S  N N 301 
MET   CE   C  N N 302 
MET   OXT  O  N N 303 
MET   H    H  N N 304 
MET   H2   H  N N 305 
MET   HA   H  N N 306 
MET   HB2  H  N N 307 
MET   HB3  H  N N 308 
MET   HG2  H  N N 309 
MET   HG3  H  N N 310 
MET   HE1  H  N N 311 
MET   HE2  H  N N 312 
MET   HE3  H  N N 313 
MET   HXT  H  N N 314 
MN    MN   MN N N 315 
NDP   PA   P  N S 316 
NDP   O1A  O  N N 317 
NDP   O2A  O  N N 318 
NDP   O5B  O  N N 319 
NDP   C5B  C  N N 320 
NDP   C4B  C  N R 321 
NDP   O4B  O  N N 322 
NDP   C3B  C  N R 323 
NDP   O3B  O  N N 324 
NDP   C2B  C  N R 325 
NDP   O2B  O  N N 326 
NDP   C1B  C  N R 327 
NDP   N9A  N  Y N 328 
NDP   C8A  C  Y N 329 
NDP   N7A  N  Y N 330 
NDP   C5A  C  Y N 331 
NDP   C6A  C  Y N 332 
NDP   N6A  N  N N 333 
NDP   N1A  N  Y N 334 
NDP   C2A  C  Y N 335 
NDP   N3A  N  Y N 336 
NDP   C4A  C  Y N 337 
NDP   O3   O  N N 338 
NDP   PN   P  N S 339 
NDP   O1N  O  N N 340 
NDP   O2N  O  N N 341 
NDP   O5D  O  N N 342 
NDP   C5D  C  N N 343 
NDP   C4D  C  N R 344 
NDP   O4D  O  N N 345 
NDP   C3D  C  N S 346 
NDP   O3D  O  N N 347 
NDP   C2D  C  N R 348 
NDP   O2D  O  N N 349 
NDP   C1D  C  N R 350 
NDP   N1N  N  N N 351 
NDP   C2N  C  N N 352 
NDP   C3N  C  N N 353 
NDP   C7N  C  N N 354 
NDP   O7N  O  N N 355 
NDP   N7N  N  N N 356 
NDP   C4N  C  N N 357 
NDP   C5N  C  N N 358 
NDP   C6N  C  N N 359 
NDP   P2B  P  N N 360 
NDP   O1X  O  N N 361 
NDP   O2X  O  N N 362 
NDP   O3X  O  N N 363 
NDP   HOA2 H  N N 364 
NDP   H51A H  N N 365 
NDP   H52A H  N N 366 
NDP   H4B  H  N N 367 
NDP   H3B  H  N N 368 
NDP   HO3A H  N N 369 
NDP   H2B  H  N N 370 
NDP   H1B  H  N N 371 
NDP   H8A  H  N N 372 
NDP   H61A H  N N 373 
NDP   H62A H  N N 374 
NDP   H2A  H  N N 375 
NDP   H21N H  N N 376 
NDP   H51N H  N N 377 
NDP   H52N H  N N 378 
NDP   H4D  H  N N 379 
NDP   H3D  H  N N 380 
NDP   HO3N H  N N 381 
NDP   H2D  H  N N 382 
NDP   HO2N H  N N 383 
NDP   H1D  H  N N 384 
NDP   H2N  H  N N 385 
NDP   H71N H  N N 386 
NDP   H72N H  N N 387 
NDP   H41N H  N N 388 
NDP   H42N H  N N 389 
NDP   H5N  H  N N 390 
NDP   H6N  H  N N 391 
NDP   HOP2 H  N N 392 
NDP   HOP3 H  N N 393 
PHE   N    N  N N 394 
PHE   CA   C  N S 395 
PHE   C    C  N N 396 
PHE   O    O  N N 397 
PHE   CB   C  N N 398 
PHE   CG   C  Y N 399 
PHE   CD1  C  Y N 400 
PHE   CD2  C  Y N 401 
PHE   CE1  C  Y N 402 
PHE   CE2  C  Y N 403 
PHE   CZ   C  Y N 404 
PHE   OXT  O  N N 405 
PHE   H    H  N N 406 
PHE   H2   H  N N 407 
PHE   HA   H  N N 408 
PHE   HB2  H  N N 409 
PHE   HB3  H  N N 410 
PHE   HD1  H  N N 411 
PHE   HD2  H  N N 412 
PHE   HE1  H  N N 413 
PHE   HE2  H  N N 414 
PHE   HZ   H  N N 415 
PHE   HXT  H  N N 416 
PRO   N    N  N N 417 
PRO   CA   C  N S 418 
PRO   C    C  N N 419 
PRO   O    O  N N 420 
PRO   CB   C  N N 421 
PRO   CG   C  N N 422 
PRO   CD   C  N N 423 
PRO   OXT  O  N N 424 
PRO   H    H  N N 425 
PRO   HA   H  N N 426 
PRO   HB2  H  N N 427 
PRO   HB3  H  N N 428 
PRO   HG2  H  N N 429 
PRO   HG3  H  N N 430 
PRO   HD2  H  N N 431 
PRO   HD3  H  N N 432 
PRO   HXT  H  N N 433 
SER   N    N  N N 434 
SER   CA   C  N S 435 
SER   C    C  N N 436 
SER   O    O  N N 437 
SER   CB   C  N N 438 
SER   OG   O  N N 439 
SER   OXT  O  N N 440 
SER   H    H  N N 441 
SER   H2   H  N N 442 
SER   HA   H  N N 443 
SER   HB2  H  N N 444 
SER   HB3  H  N N 445 
SER   HG   H  N N 446 
SER   HXT  H  N N 447 
THR   N    N  N N 448 
THR   CA   C  N S 449 
THR   C    C  N N 450 
THR   O    O  N N 451 
THR   CB   C  N R 452 
THR   OG1  O  N N 453 
THR   CG2  C  N N 454 
THR   OXT  O  N N 455 
THR   H    H  N N 456 
THR   H2   H  N N 457 
THR   HA   H  N N 458 
THR   HB   H  N N 459 
THR   HG1  H  N N 460 
THR   HG21 H  N N 461 
THR   HG22 H  N N 462 
THR   HG23 H  N N 463 
THR   HXT  H  N N 464 
TRP   N    N  N N 465 
TRP   CA   C  N S 466 
TRP   C    C  N N 467 
TRP   O    O  N N 468 
TRP   CB   C  N N 469 
TRP   CG   C  Y N 470 
TRP   CD1  C  Y N 471 
TRP   CD2  C  Y N 472 
TRP   NE1  N  Y N 473 
TRP   CE2  C  Y N 474 
TRP   CE3  C  Y N 475 
TRP   CZ2  C  Y N 476 
TRP   CZ3  C  Y N 477 
TRP   CH2  C  Y N 478 
TRP   OXT  O  N N 479 
TRP   H    H  N N 480 
TRP   H2   H  N N 481 
TRP   HA   H  N N 482 
TRP   HB2  H  N N 483 
TRP   HB3  H  N N 484 
TRP   HD1  H  N N 485 
TRP   HE1  H  N N 486 
TRP   HE3  H  N N 487 
TRP   HZ2  H  N N 488 
TRP   HZ3  H  N N 489 
TRP   HH2  H  N N 490 
TRP   HXT  H  N N 491 
TYR   N    N  N N 492 
TYR   CA   C  N S 493 
TYR   C    C  N N 494 
TYR   O    O  N N 495 
TYR   CB   C  N N 496 
TYR   CG   C  Y N 497 
TYR   CD1  C  Y N 498 
TYR   CD2  C  Y N 499 
TYR   CE1  C  Y N 500 
TYR   CE2  C  Y N 501 
TYR   CZ   C  Y N 502 
TYR   OH   O  N N 503 
TYR   OXT  O  N N 504 
TYR   H    H  N N 505 
TYR   H2   H  N N 506 
TYR   HA   H  N N 507 
TYR   HB2  H  N N 508 
TYR   HB3  H  N N 509 
TYR   HD1  H  N N 510 
TYR   HD2  H  N N 511 
TYR   HE1  H  N N 512 
TYR   HE2  H  N N 513 
TYR   HH   H  N N 514 
TYR   HXT  H  N N 515 
VAL   N    N  N N 516 
VAL   CA   C  N S 517 
VAL   C    C  N N 518 
VAL   O    O  N N 519 
VAL   CB   C  N N 520 
VAL   CG1  C  N N 521 
VAL   CG2  C  N N 522 
VAL   OXT  O  N N 523 
VAL   H    H  N N 524 
VAL   H2   H  N N 525 
VAL   HA   H  N N 526 
VAL   HB   H  N N 527 
VAL   HG11 H  N N 528 
VAL   HG12 H  N N 529 
VAL   HG13 H  N N 530 
VAL   HG21 H  N N 531 
VAL   HG22 H  N N 532 
VAL   HG23 H  N N 533 
VAL   HXT  H  N N 534 
# 
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 
A1L2H C14 S1   sing N N 1   
A1L2H C14 C15  sing N N 2   
A1L2H S1  C13  sing N N 3   
A1L2H C15 O6   doub N N 4   
A1L2H C15 N1   sing N N 5   
A1L2H C6  C5   doub Y N 6   
A1L2H C6  C1   sing Y N 7   
A1L2H C16 N1   sing N N 8   
A1L2H N1  O5   sing N N 9   
A1L2H C5  C4   sing Y N 10  
A1L2H C13 C1   sing N N 11  
A1L2H C13 P1   sing N N 12  
A1L2H O4  P1   doub N N 13  
A1L2H C7  C8   sing N N 14  
A1L2H C7  O1   sing N N 15  
A1L2H O2  P1   sing N N 16  
A1L2H C1  C2   doub Y N 17  
A1L2H P1  O3   sing N N 18  
A1L2H C8  C9   sing N N 19  
A1L2H C4  O1   sing N N 20  
A1L2H C4  C3   doub Y N 21  
A1L2H C2  C3   sing Y N 22  
A1L2H C9  C10  sing N N 23  
A1L2H C10 C11  sing N N 24  
A1L2H C12 C11  sing N N 25  
A1L2H C5  H1   sing N N 26  
A1L2H C6  H2   sing N N 27  
A1L2H C7  H3   sing N N 28  
A1L2H C7  H4   sing N N 29  
A1L2H C8  H5   sing N N 30  
A1L2H C8  H6   sing N N 31  
A1L2H C10 H7   sing N N 32  
A1L2H C10 H8   sing N N 33  
A1L2H C13 H9   sing N N 34  
A1L2H C16 H10  sing N N 35  
A1L2H C16 H11  sing N N 36  
A1L2H C16 H12  sing N N 37  
A1L2H O5  H13  sing N N 38  
A1L2H C14 H14  sing N N 39  
A1L2H C14 H15  sing N N 40  
A1L2H O3  H16  sing N N 41  
A1L2H O2  H17  sing N N 42  
A1L2H C3  H18  sing N N 43  
A1L2H C2  H19  sing N N 44  
A1L2H C9  H20  sing N N 45  
A1L2H C9  H21  sing N N 46  
A1L2H C11 H22  sing N N 47  
A1L2H C11 H23  sing N N 48  
A1L2H C12 H24  sing N N 49  
A1L2H C12 H25  sing N N 50  
A1L2H C12 H26  sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
GOL   C1  O1   sing N N 180 
GOL   C1  C2   sing N N 181 
GOL   C1  H11  sing N N 182 
GOL   C1  H12  sing N N 183 
GOL   O1  HO1  sing N N 184 
GOL   C2  O2   sing N N 185 
GOL   C2  C3   sing N N 186 
GOL   C2  H2   sing N N 187 
GOL   O2  HO2  sing N N 188 
GOL   C3  O3   sing N N 189 
GOL   C3  H31  sing N N 190 
GOL   C3  H32  sing N N 191 
GOL   O3  HO3  sing N N 192 
HIS   N   CA   sing N N 193 
HIS   N   H    sing N N 194 
HIS   N   H2   sing N N 195 
HIS   CA  C    sing N N 196 
HIS   CA  CB   sing N N 197 
HIS   CA  HA   sing N N 198 
HIS   C   O    doub N N 199 
HIS   C   OXT  sing N N 200 
HIS   CB  CG   sing N N 201 
HIS   CB  HB2  sing N N 202 
HIS   CB  HB3  sing N N 203 
HIS   CG  ND1  sing Y N 204 
HIS   CG  CD2  doub Y N 205 
HIS   ND1 CE1  doub Y N 206 
HIS   ND1 HD1  sing N N 207 
HIS   CD2 NE2  sing Y N 208 
HIS   CD2 HD2  sing N N 209 
HIS   CE1 NE2  sing Y N 210 
HIS   CE1 HE1  sing N N 211 
HIS   NE2 HE2  sing N N 212 
HIS   OXT HXT  sing N N 213 
HOH   O   H1   sing N N 214 
HOH   O   H2   sing N N 215 
ILE   N   CA   sing N N 216 
ILE   N   H    sing N N 217 
ILE   N   H2   sing N N 218 
ILE   CA  C    sing N N 219 
ILE   CA  CB   sing N N 220 
ILE   CA  HA   sing N N 221 
ILE   C   O    doub N N 222 
ILE   C   OXT  sing N N 223 
ILE   CB  CG1  sing N N 224 
ILE   CB  CG2  sing N N 225 
ILE   CB  HB   sing N N 226 
ILE   CG1 CD1  sing N N 227 
ILE   CG1 HG12 sing N N 228 
ILE   CG1 HG13 sing N N 229 
ILE   CG2 HG21 sing N N 230 
ILE   CG2 HG22 sing N N 231 
ILE   CG2 HG23 sing N N 232 
ILE   CD1 HD11 sing N N 233 
ILE   CD1 HD12 sing N N 234 
ILE   CD1 HD13 sing N N 235 
ILE   OXT HXT  sing N N 236 
LEU   N   CA   sing N N 237 
LEU   N   H    sing N N 238 
LEU   N   H2   sing N N 239 
LEU   CA  C    sing N N 240 
LEU   CA  CB   sing N N 241 
LEU   CA  HA   sing N N 242 
LEU   C   O    doub N N 243 
LEU   C   OXT  sing N N 244 
LEU   CB  CG   sing N N 245 
LEU   CB  HB2  sing N N 246 
LEU   CB  HB3  sing N N 247 
LEU   CG  CD1  sing N N 248 
LEU   CG  CD2  sing N N 249 
LEU   CG  HG   sing N N 250 
LEU   CD1 HD11 sing N N 251 
LEU   CD1 HD12 sing N N 252 
LEU   CD1 HD13 sing N N 253 
LEU   CD2 HD21 sing N N 254 
LEU   CD2 HD22 sing N N 255 
LEU   CD2 HD23 sing N N 256 
LEU   OXT HXT  sing N N 257 
LYS   N   CA   sing N N 258 
LYS   N   H    sing N N 259 
LYS   N   H2   sing N N 260 
LYS   CA  C    sing N N 261 
LYS   CA  CB   sing N N 262 
LYS   CA  HA   sing N N 263 
LYS   C   O    doub N N 264 
LYS   C   OXT  sing N N 265 
LYS   CB  CG   sing N N 266 
LYS   CB  HB2  sing N N 267 
LYS   CB  HB3  sing N N 268 
LYS   CG  CD   sing N N 269 
LYS   CG  HG2  sing N N 270 
LYS   CG  HG3  sing N N 271 
LYS   CD  CE   sing N N 272 
LYS   CD  HD2  sing N N 273 
LYS   CD  HD3  sing N N 274 
LYS   CE  NZ   sing N N 275 
LYS   CE  HE2  sing N N 276 
LYS   CE  HE3  sing N N 277 
LYS   NZ  HZ1  sing N N 278 
LYS   NZ  HZ2  sing N N 279 
LYS   NZ  HZ3  sing N N 280 
LYS   OXT HXT  sing N N 281 
MET   N   CA   sing N N 282 
MET   N   H    sing N N 283 
MET   N   H2   sing N N 284 
MET   CA  C    sing N N 285 
MET   CA  CB   sing N N 286 
MET   CA  HA   sing N N 287 
MET   C   O    doub N N 288 
MET   C   OXT  sing N N 289 
MET   CB  CG   sing N N 290 
MET   CB  HB2  sing N N 291 
MET   CB  HB3  sing N N 292 
MET   CG  SD   sing N N 293 
MET   CG  HG2  sing N N 294 
MET   CG  HG3  sing N N 295 
MET   SD  CE   sing N N 296 
MET   CE  HE1  sing N N 297 
MET   CE  HE2  sing N N 298 
MET   CE  HE3  sing N N 299 
MET   OXT HXT  sing N N 300 
NDP   PA  O1A  doub N N 301 
NDP   PA  O2A  sing N N 302 
NDP   PA  O5B  sing N N 303 
NDP   PA  O3   sing N N 304 
NDP   O2A HOA2 sing N N 305 
NDP   O5B C5B  sing N N 306 
NDP   C5B C4B  sing N N 307 
NDP   C5B H51A sing N N 308 
NDP   C5B H52A sing N N 309 
NDP   C4B O4B  sing N N 310 
NDP   C4B C3B  sing N N 311 
NDP   C4B H4B  sing N N 312 
NDP   O4B C1B  sing N N 313 
NDP   C3B O3B  sing N N 314 
NDP   C3B C2B  sing N N 315 
NDP   C3B H3B  sing N N 316 
NDP   O3B HO3A sing N N 317 
NDP   C2B O2B  sing N N 318 
NDP   C2B C1B  sing N N 319 
NDP   C2B H2B  sing N N 320 
NDP   O2B P2B  sing N N 321 
NDP   C1B N9A  sing N N 322 
NDP   C1B H1B  sing N N 323 
NDP   N9A C8A  sing Y N 324 
NDP   N9A C4A  sing Y N 325 
NDP   C8A N7A  doub Y N 326 
NDP   C8A H8A  sing N N 327 
NDP   N7A C5A  sing Y N 328 
NDP   C5A C6A  sing Y N 329 
NDP   C5A C4A  doub Y N 330 
NDP   C6A N6A  sing N N 331 
NDP   C6A N1A  doub Y N 332 
NDP   N6A H61A sing N N 333 
NDP   N6A H62A sing N N 334 
NDP   N1A C2A  sing Y N 335 
NDP   C2A N3A  doub Y N 336 
NDP   C2A H2A  sing N N 337 
NDP   N3A C4A  sing Y N 338 
NDP   O3  PN   sing N N 339 
NDP   PN  O1N  doub N N 340 
NDP   PN  O2N  sing N N 341 
NDP   PN  O5D  sing N N 342 
NDP   O2N H21N sing N N 343 
NDP   O5D C5D  sing N N 344 
NDP   C5D C4D  sing N N 345 
NDP   C5D H51N sing N N 346 
NDP   C5D H52N sing N N 347 
NDP   C4D O4D  sing N N 348 
NDP   C4D C3D  sing N N 349 
NDP   C4D H4D  sing N N 350 
NDP   O4D C1D  sing N N 351 
NDP   C3D O3D  sing N N 352 
NDP   C3D C2D  sing N N 353 
NDP   C3D H3D  sing N N 354 
NDP   O3D HO3N sing N N 355 
NDP   C2D O2D  sing N N 356 
NDP   C2D C1D  sing N N 357 
NDP   C2D H2D  sing N N 358 
NDP   O2D HO2N sing N N 359 
NDP   C1D N1N  sing N N 360 
NDP   C1D H1D  sing N N 361 
NDP   N1N C2N  sing N N 362 
NDP   N1N C6N  sing N N 363 
NDP   C2N C3N  doub N N 364 
NDP   C2N H2N  sing N N 365 
NDP   C3N C7N  sing N N 366 
NDP   C3N C4N  sing N N 367 
NDP   C7N O7N  doub N N 368 
NDP   C7N N7N  sing N N 369 
NDP   N7N H71N sing N N 370 
NDP   N7N H72N sing N N 371 
NDP   C4N C5N  sing N N 372 
NDP   C4N H41N sing N N 373 
NDP   C4N H42N sing N N 374 
NDP   C5N C6N  doub N N 375 
NDP   C5N H5N  sing N N 376 
NDP   C6N H6N  sing N N 377 
NDP   P2B O1X  doub N N 378 
NDP   P2B O2X  sing N N 379 
NDP   P2B O3X  sing N N 380 
NDP   O2X HOP2 sing N N 381 
NDP   O3X HOP3 sing N N 382 
PHE   N   CA   sing N N 383 
PHE   N   H    sing N N 384 
PHE   N   H2   sing N N 385 
PHE   CA  C    sing N N 386 
PHE   CA  CB   sing N N 387 
PHE   CA  HA   sing N N 388 
PHE   C   O    doub N N 389 
PHE   C   OXT  sing N N 390 
PHE   CB  CG   sing N N 391 
PHE   CB  HB2  sing N N 392 
PHE   CB  HB3  sing N N 393 
PHE   CG  CD1  doub Y N 394 
PHE   CG  CD2  sing Y N 395 
PHE   CD1 CE1  sing Y N 396 
PHE   CD1 HD1  sing N N 397 
PHE   CD2 CE2  doub Y N 398 
PHE   CD2 HD2  sing N N 399 
PHE   CE1 CZ   doub Y N 400 
PHE   CE1 HE1  sing N N 401 
PHE   CE2 CZ   sing Y N 402 
PHE   CE2 HE2  sing N N 403 
PHE   CZ  HZ   sing N N 404 
PHE   OXT HXT  sing N N 405 
PRO   N   CA   sing N N 406 
PRO   N   CD   sing N N 407 
PRO   N   H    sing N N 408 
PRO   CA  C    sing N N 409 
PRO   CA  CB   sing N N 410 
PRO   CA  HA   sing N N 411 
PRO   C   O    doub N N 412 
PRO   C   OXT  sing N N 413 
PRO   CB  CG   sing N N 414 
PRO   CB  HB2  sing N N 415 
PRO   CB  HB3  sing N N 416 
PRO   CG  CD   sing N N 417 
PRO   CG  HG2  sing N N 418 
PRO   CG  HG3  sing N N 419 
PRO   CD  HD2  sing N N 420 
PRO   CD  HD3  sing N N 421 
PRO   OXT HXT  sing N N 422 
SER   N   CA   sing N N 423 
SER   N   H    sing N N 424 
SER   N   H2   sing N N 425 
SER   CA  C    sing N N 426 
SER   CA  CB   sing N N 427 
SER   CA  HA   sing N N 428 
SER   C   O    doub N N 429 
SER   C   OXT  sing N N 430 
SER   CB  OG   sing N N 431 
SER   CB  HB2  sing N N 432 
SER   CB  HB3  sing N N 433 
SER   OG  HG   sing N N 434 
SER   OXT HXT  sing N N 435 
THR   N   CA   sing N N 436 
THR   N   H    sing N N 437 
THR   N   H2   sing N N 438 
THR   CA  C    sing N N 439 
THR   CA  CB   sing N N 440 
THR   CA  HA   sing N N 441 
THR   C   O    doub N N 442 
THR   C   OXT  sing N N 443 
THR   CB  OG1  sing N N 444 
THR   CB  CG2  sing N N 445 
THR   CB  HB   sing N N 446 
THR   OG1 HG1  sing N N 447 
THR   CG2 HG21 sing N N 448 
THR   CG2 HG22 sing N N 449 
THR   CG2 HG23 sing N N 450 
THR   OXT HXT  sing N N 451 
TRP   N   CA   sing N N 452 
TRP   N   H    sing N N 453 
TRP   N   H2   sing N N 454 
TRP   CA  C    sing N N 455 
TRP   CA  CB   sing N N 456 
TRP   CA  HA   sing N N 457 
TRP   C   O    doub N N 458 
TRP   C   OXT  sing N N 459 
TRP   CB  CG   sing N N 460 
TRP   CB  HB2  sing N N 461 
TRP   CB  HB3  sing N N 462 
TRP   CG  CD1  doub Y N 463 
TRP   CG  CD2  sing Y N 464 
TRP   CD1 NE1  sing Y N 465 
TRP   CD1 HD1  sing N N 466 
TRP   CD2 CE2  doub Y N 467 
TRP   CD2 CE3  sing Y N 468 
TRP   NE1 CE2  sing Y N 469 
TRP   NE1 HE1  sing N N 470 
TRP   CE2 CZ2  sing Y N 471 
TRP   CE3 CZ3  doub Y N 472 
TRP   CE3 HE3  sing N N 473 
TRP   CZ2 CH2  doub Y N 474 
TRP   CZ2 HZ2  sing N N 475 
TRP   CZ3 CH2  sing Y N 476 
TRP   CZ3 HZ3  sing N N 477 
TRP   CH2 HH2  sing N N 478 
TRP   OXT HXT  sing N N 479 
TYR   N   CA   sing N N 480 
TYR   N   H    sing N N 481 
TYR   N   H2   sing N N 482 
TYR   CA  C    sing N N 483 
TYR   CA  CB   sing N N 484 
TYR   CA  HA   sing N N 485 
TYR   C   O    doub N N 486 
TYR   C   OXT  sing N N 487 
TYR   CB  CG   sing N N 488 
TYR   CB  HB2  sing N N 489 
TYR   CB  HB3  sing N N 490 
TYR   CG  CD1  doub Y N 491 
TYR   CG  CD2  sing Y N 492 
TYR   CD1 CE1  sing Y N 493 
TYR   CD1 HD1  sing N N 494 
TYR   CD2 CE2  doub Y N 495 
TYR   CD2 HD2  sing N N 496 
TYR   CE1 CZ   doub Y N 497 
TYR   CE1 HE1  sing N N 498 
TYR   CE2 CZ   sing Y N 499 
TYR   CE2 HE2  sing N N 500 
TYR   CZ  OH   sing N N 501 
TYR   OH  HH   sing N N 502 
TYR   OXT HXT  sing N N 503 
VAL   N   CA   sing N N 504 
VAL   N   H    sing N N 505 
VAL   N   H2   sing N N 506 
VAL   CA  C    sing N N 507 
VAL   CA  CB   sing N N 508 
VAL   CA  HA   sing N N 509 
VAL   C   O    doub N N 510 
VAL   C   OXT  sing N N 511 
VAL   CB  CG1  sing N N 512 
VAL   CB  CG2  sing N N 513 
VAL   CB  HB   sing N N 514 
VAL   CG1 HG11 sing N N 515 
VAL   CG1 HG12 sing N N 516 
VAL   CG1 HG13 sing N N 517 
VAL   CG2 HG21 sing N N 518 
VAL   CG2 HG22 sing N N 519 
VAL   CG2 HG23 sing N N 520 
VAL   OXT HXT  sing N N 521 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8JNW 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZXX 
_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]   0.010797 
_atom_sites.fract_transf_matrix[1][2]   0.006234 
_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]   0.012468 
_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]   0.009520 
_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  
MN 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LYS   A 1 2   ? 13.038 -14.165 17.686  1.00 71.82 ? 76  LYS   A N   1 
ATOM   2    C  CA  . LYS   A 1 2   ? 12.953 -12.690 17.517  1.00 66.00 ? 76  LYS   A CA  1 
ATOM   3    C  C   . LYS   A 1 2   ? 14.296 -12.198 16.981  1.00 56.54 ? 76  LYS   A C   1 
ATOM   4    O  O   . LYS   A 1 2   ? 15.099 -11.662 17.737  1.00 59.56 ? 76  LYS   A O   1 
ATOM   5    C  CB  . LYS   A 1 2   ? 12.524 -12.112 18.874  1.00 70.37 ? 76  LYS   A CB  1 
ATOM   6    C  CG  . LYS   A 1 2   ? 11.979 -10.686 18.881  1.00 73.95 ? 76  LYS   A CG  1 
ATOM   7    C  CD  . LYS   A 1 2   ? 13.011 -9.584  18.681  1.00 76.25 ? 76  LYS   A CD  1 
ATOM   8    C  CE  . LYS   A 1 2   ? 14.062 -9.564  19.749  1.00 76.80 ? 76  LYS   A CE  1 
ATOM   9    N  NZ  . LYS   A 1 2   ? 15.178 -8.687  19.391  1.00 74.38 ? 76  LYS   A NZ  1 
ATOM   10   N  N   . PRO   A 1 3   ? 14.613 -12.407 15.679  1.00 48.64 ? 77  PRO   A N   1 
ATOM   11   C  CA  . PRO   A 1 3   ? 15.904 -12.000 15.128  1.00 43.17 ? 77  PRO   A CA  1 
ATOM   12   C  C   . PRO   A 1 3   ? 15.937 -10.480 15.018  1.00 37.06 ? 77  PRO   A C   1 
ATOM   13   O  O   . PRO   A 1 3   ? 14.898 -9.839  14.871  1.00 40.45 ? 77  PRO   A O   1 
ATOM   14   C  CB  . PRO   A 1 3   ? 16.020 -12.676 13.752  1.00 46.82 ? 77  PRO   A CB  1 
ATOM   15   C  CG  . PRO   A 1 3   ? 14.773 -13.549 13.627  1.00 47.69 ? 77  PRO   A CG  1 
ATOM   16   C  CD  . PRO   A 1 3   ? 13.760 -13.028 14.655  1.00 51.66 ? 77  PRO   A CD  1 
ATOM   17   N  N   . ILE   A 1 4   ? 17.145 -9.916  15.093  1.00 28.85 ? 78  ILE   A N   1 
ATOM   18   C  CA  . ILE   A 1 4   ? 17.342 -8.485  14.948  1.00 26.45 ? 78  ILE   A CA  1 
ATOM   19   C  C   . ILE   A 1 4   ? 17.696 -8.182  13.500  1.00 23.80 ? 78  ILE   A C   1 
ATOM   20   O  O   . ILE   A 1 4   ? 18.671 -8.715  12.979  1.00 23.41 ? 78  ILE   A O   1 
ATOM   21   C  CB  . ILE   A 1 4   ? 18.450 -8.034  15.906  1.00 31.49 ? 78  ILE   A CB  1 
ATOM   22   C  CG1 . ILE   A 1 4   ? 18.026 -8.269  17.365  1.00 32.84 ? 78  ILE   A CG1 1 
ATOM   23   C  CG2 . ILE   A 1 4   ? 18.829 -6.567  15.661  1.00 32.81 ? 78  ILE   A CG2 1 
ATOM   24   C  CD1 . ILE   A 1 4   ? 19.183 -8.325  18.346  1.00 35.52 ? 78  ILE   A CD1 1 
ATOM   25   N  N   . ASN   A 1 5   ? 16.882 -7.332  12.867  1.00 23.13 ? 79  ASN   A N   1 
ATOM   26   C  CA  . ASN   A 1 5   ? 16.988 -7.030  11.457  1.00 22.98 ? 79  ASN   A CA  1 
ATOM   27   C  C   . ASN   A 1 5   ? 17.918 -5.825  11.302  1.00 21.73 ? 79  ASN   A C   1 
ATOM   28   O  O   . ASN   A 1 5   ? 17.530 -4.726  11.730  1.00 21.61 ? 79  ASN   A O   1 
ATOM   29   C  CB  . ASN   A 1 5   ? 15.592 -6.780  10.882  1.00 25.44 ? 79  ASN   A CB  1 
ATOM   30   C  CG  . ASN   A 1 5   ? 14.753 -8.040  10.881  1.00 31.15 ? 79  ASN   A CG  1 
ATOM   31   O  OD1 . ASN   A 1 5   ? 15.284 -9.151  10.841  1.00 30.72 ? 79  ASN   A OD1 1 
ATOM   32   N  ND2 . ASN   A 1 5   ? 13.439 -7.873  10.926  1.00 36.04 ? 79  ASN   A ND2 1 
ATOM   33   N  N   . VAL   A 1 6   ? 19.070 -6.023  10.659  1.00 20.35 ? 80  VAL   A N   1 
ATOM   34   C  CA  . VAL   A 1 6   ? 20.096 -4.992  10.629  1.00 19.87 ? 80  VAL   A CA  1 
ATOM   35   C  C   . VAL   A 1 6   ? 20.532 -4.671  9.206   1.00 20.54 ? 80  VAL   A C   1 
ATOM   36   O  O   . VAL   A 1 6   ? 20.584 -5.557  8.330   1.00 22.93 ? 80  VAL   A O   1 
ATOM   37   C  CB  . VAL   A 1 6   ? 21.285 -5.440  11.499  1.00 24.01 ? 80  VAL   A CB  1 
ATOM   38   C  CG1 . VAL   A 1 6   ? 21.978 -6.685  10.965  1.00 27.35 ? 80  VAL   A CG1 1 
ATOM   39   C  CG2 . VAL   A 1 6   ? 22.345 -4.367  11.692  1.00 25.79 ? 80  VAL   A CG2 1 
ATOM   40   N  N   . ALA   A 1 7   ? 20.762 -3.386  8.945   1.00 17.47 ? 81  ALA   A N   1 
ATOM   41   C  CA  . ALA   A 1 7   ? 21.391 -2.900  7.743   1.00 17.82 ? 81  ALA   A CA  1 
ATOM   42   C  C   . ALA   A 1 7   ? 22.823 -2.487  8.073   1.00 17.33 ? 81  ALA   A C   1 
ATOM   43   O  O   . ALA   A 1 7   ? 23.063 -1.892  9.151   1.00 17.91 ? 81  ALA   A O   1 
ATOM   44   C  CB  . ALA   A 1 7   ? 20.628 -1.726  7.188   1.00 18.01 ? 81  ALA   A CB  1 
ATOM   45   N  N   . ILE   A 1 8   ? 23.747 -2.752  7.168   1.00 17.33 ? 82  ILE   A N   1 
ATOM   46   C  CA  . ILE   A 1 8   ? 25.128 -2.291  7.318   1.00 17.17 ? 82  ILE   A CA  1 
ATOM   47   C  C   . ILE   A 1 8   ? 25.456 -1.296  6.219   1.00 16.48 ? 82  ILE   A C   1 
ATOM   48   O  O   . ILE   A 1 8   ? 25.496 -1.629  5.010   1.00 18.02 ? 82  ILE   A O   1 
ATOM   49   C  CB  . ILE   A 1 8   ? 26.114 -3.456  7.235   1.00 18.95 ? 82  ILE   A CB  1 
ATOM   50   C  CG1 . ILE   A 1 8   ? 25.713 -4.648  8.093   1.00 20.39 ? 82  ILE   A CG1 1 
ATOM   51   C  CG2 . ILE   A 1 8   ? 27.543 -2.967  7.521   1.00 18.42 ? 82  ILE   A CG2 1 
ATOM   52   C  CD1 . ILE   A 1 8   ? 25.674 -4.376  9.559   1.00 20.41 ? 82  ILE   A CD1 1 
ATOM   53   N  N   . PHE   A 1 9   ? 25.615 -0.040  6.617   1.00 16.21 ? 83  PHE   A N   1 
ATOM   54   C  CA  . PHE   A 1 9   ? 25.990 1.038   5.723   1.00 15.96 ? 83  PHE   A CA  1 
ATOM   55   C  C   . PHE   A 1 9   ? 27.498 1.237   5.762   1.00 17.00 ? 83  PHE   A C   1 
ATOM   56   O  O   . PHE   A 1 9   ? 28.058 1.438   6.839   1.00 17.45 ? 83  PHE   A O   1 
ATOM   57   C  CB  . PHE   A 1 9   ? 25.251 2.312   6.082   1.00 15.85 ? 83  PHE   A CB  1 
ATOM   58   C  CG  . PHE   A 1 9   ? 23.770 2.372   5.733   1.00 16.52 ? 83  PHE   A CG  1 
ATOM   59   C  CD1 . PHE   A 1 9   ? 23.093 1.252   5.192   1.00 18.01 ? 83  PHE   A CD1 1 
ATOM   60   C  CD2 . PHE   A 1 9   ? 23.053 3.548   5.885   1.00 17.81 ? 83  PHE   A CD2 1 
ATOM   61   C  CE1 . PHE   A 1 9   ? 21.736 1.339   4.869   1.00 18.79 ? 83  PHE   A CE1 1 
ATOM   62   C  CE2 . PHE   A 1 9   ? 21.698 3.606   5.584   1.00 18.51 ? 83  PHE   A CE2 1 
ATOM   63   C  CZ  . PHE   A 1 9   ? 21.057 2.493   5.093   1.00 19.84 ? 83  PHE   A CZ  1 
ATOM   64   N  N   . GLY   A 1 10  ? 28.155 1.181   4.616   1.00 16.56 ? 84  GLY   A N   1 
ATOM   65   C  CA  . GLY   A 1 10  ? 29.594 1.143   4.535   1.00 16.93 ? 84  GLY   A CA  1 
ATOM   66   C  C   . GLY   A 1 10  ? 30.117 -0.248  4.846   1.00 16.32 ? 84  GLY   A C   1 
ATOM   67   O  O   . GLY   A 1 10  ? 31.039 -0.455  5.623   1.00 17.96 ? 84  GLY   A O   1 
ATOM   68   N  N   . SER   A 1 11  ? 29.550 -1.256  4.150   1.00 17.28 ? 85  SER   A N   1 
ATOM   69   C  CA  . SER   A 1 11  ? 29.741 -2.646  4.547   1.00 18.16 ? 85  SER   A CA  1 
ATOM   70   C  C   . SER   A 1 11  ? 31.112 -3.192  4.154   1.00 16.81 ? 85  SER   A C   1 
ATOM   71   O  O   . SER   A 1 11  ? 31.541 -4.163  4.770   1.00 17.84 ? 85  SER   A O   1 
ATOM   72   C  CB  . SER   A 1 11  ? 28.622 -3.536  4.035   1.00 18.57 ? 85  SER   A CB  1 
ATOM   73   O  OG  . SER   A 1 11  ? 28.684 -3.600  2.623   1.00 20.44 ? 85  SER   A OG  1 
ATOM   74   N  N   . THR   A 1 12  ? 31.787 -2.553  3.200   1.00 17.73 ? 86  THR   A N   1 
ATOM   75   C  CA  . THR   A 1 12  ? 33.075 -3.022  2.703   1.00 19.02 ? 86  THR   A CA  1 
ATOM   76   C  C   . THR   A 1 12  ? 34.258 -2.410  3.439   1.00 18.57 ? 86  THR   A C   1 
ATOM   77   O  O   . THR   A 1 12  ? 35.386 -2.833  3.225   1.00 21.18 ? 86  THR   A O   1 
ATOM   78   C  CB  . THR   A 1 12  ? 33.169 -2.728  1.212   1.00 19.97 ? 86  THR   A CB  1 
ATOM   79   O  OG1 . THR   A 1 12  ? 32.707 -1.416  0.968   1.00 19.75 ? 86  THR   A OG1 1 
ATOM   80   C  CG2 . THR   A 1 12  ? 32.356 -3.746  0.417   1.00 20.60 ? 86  THR   A CG2 1 
ATOM   81   N  N   . GLY   A 1 13  ? 34.027 -1.422  4.329   1.00 16.95 ? 87  GLY   A N   1 
ATOM   82   C  CA  . GLY   A 1 13  ? 35.110 -0.777  5.059   1.00 18.01 ? 87  GLY   A CA  1 
ATOM   83   C  C   . GLY   A 1 13  ? 35.445 -1.525  6.342   1.00 16.84 ? 87  GLY   A C   1 
ATOM   84   O  O   . GLY   A 1 13  ? 35.017 -2.653  6.592   1.00 17.71 ? 87  GLY   A O   1 
ATOM   85   N  N   . SER   A 1 14  ? 36.256 -0.885  7.184   1.00 16.75 ? 88  SER   A N   1 
ATOM   86   C  CA  . SER   A 1 14  ? 36.755 -1.486  8.396   1.00 15.70 ? 88  SER   A CA  1 
ATOM   87   C  C   . SER   A 1 14  ? 35.593 -1.783  9.328   1.00 15.95 ? 88  SER   A C   1 
ATOM   88   O  O   . SER   A 1 14  ? 35.465 -2.890  9.854   1.00 16.63 ? 88  SER   A O   1 
ATOM   89   C  CB  . SER   A 1 14  ? 37.811 -0.588  9.023   1.00 15.97 ? 88  SER   A CB  1 
ATOM   90   O  OG  . SER   A 1 14  ? 38.201 -1.044  10.314  1.00 15.64 ? 88  SER   A OG  1 
ATOM   91   N  N   . ILE   A 1 15  ? 34.783 -0.780  9.691   1.00 15.19 ? 89  ILE   A N   1 
ATOM   92   C  CA  . ILE   A 1 15  ? 33.634 -0.997  10.549  1.00 15.59 ? 89  ILE   A CA  1 
ATOM   93   C  C   . ILE   A 1 15  ? 32.691 -2.042  9.939   1.00 15.91 ? 89  ILE   A C   1 
ATOM   94   O  O   . ILE   A 1 15  ? 32.237 -2.951  10.628  1.00 15.60 ? 89  ILE   A O   1 
ATOM   95   C  CB  . ILE   A 1 15  ? 32.898 0.336   10.822  1.00 15.16 ? 89  ILE   A CB  1 
ATOM   96   C  CG1 . ILE   A 1 15  ? 33.719 1.220   11.776  1.00 15.11 ? 89  ILE   A CG1 1 
ATOM   97   C  CG2 . ILE   A 1 15  ? 31.498 0.083   11.376  1.00 15.27 ? 89  ILE   A CG2 1 
ATOM   98   C  CD1 . ILE   A 1 15  ? 33.740 0.751   13.215  1.00 16.09 ? 89  ILE   A CD1 1 
ATOM   99   N  N   . GLY   A 1 16  ? 32.400 -1.891  8.661   1.00 15.87 ? 90  GLY   A N   1 
ATOM   100  C  CA  . GLY   A 1 16  ? 31.403 -2.763  8.028   1.00 16.32 ? 90  GLY   A CA  1 
ATOM   101  C  C   . GLY   A 1 16  ? 31.835 -4.227  8.028   1.00 18.68 ? 90  GLY   A C   1 
ATOM   102  O  O   . GLY   A 1 16  ? 31.048 -5.099  8.384   1.00 19.09 ? 90  GLY   A O   1 
ATOM   103  N  N   . THR   A 1 17  ? 33.105 -4.452  7.748   1.00 18.38 ? 91  THR   A N   1 
ATOM   104  C  CA  . THR   A 1 17  ? 33.575 -5.833  7.719   1.00 20.10 ? 91  THR   A CA  1 
ATOM   105  C  C   . THR   A 1 17  ? 33.641 -6.361  9.144   1.00 19.77 ? 91  THR   A C   1 
ATOM   106  O  O   . THR   A 1 17  ? 33.308 -7.526  9.427   1.00 20.86 ? 91  THR   A O   1 
ATOM   107  C  CB  . THR   A 1 17  ? 34.868 -5.938  6.907   1.00 23.10 ? 91  THR   A CB  1 
ATOM   108  O  OG1 . THR   A 1 17  ? 35.886 -5.206  7.555   1.00 26.81 ? 91  THR   A OG1 1 
ATOM   109  C  CG2 . THR   A 1 17  ? 34.781 -5.425  5.492   1.00 23.72 ? 91  THR   A CG2 1 
ATOM   110  N  N   . ASN   A 1 18  ? 34.075 -5.584  10.130  1.00 18.98 ? 92  ASN   A N   1 
ATOM   111  C  CA  . ASN   A 1 18  ? 34.035 -6.025  11.508  1.00 19.12 ? 92  ASN   A CA  1 
ATOM   112  C  C   . ASN   A 1 18  ? 32.624 -6.325  12.015  1.00 19.67 ? 92  ASN   A C   1 
ATOM   113  O  O   . ASN   A 1 18  ? 32.419 -7.200  12.882  1.00 21.61 ? 92  ASN   A O   1 
ATOM   114  C  CB  . ASN   A 1 18  ? 34.672 -4.995  12.432  1.00 21.48 ? 92  ASN   A CB  1 
ATOM   115  C  CG  . ASN   A 1 18  ? 36.048 -5.379  12.883  1.00 32.05 ? 92  ASN   A CG  1 
ATOM   116  O  OD1 . ASN   A 1 18  ? 36.260 -6.542  13.253  1.00 37.21 ? 92  ASN   A OD1 1 
ATOM   117  N  ND2 . ASN   A 1 18  ? 36.982 -4.442  12.797  1.00 38.30 ? 92  ASN   A ND2 1 
ATOM   118  N  N   . ALA   A 1 19  ? 31.627 -5.546  11.567  1.00 16.73 ? 93  ALA   A N   1 
ATOM   119  C  CA  . ALA   A 1 19  ? 30.248 -5.805  11.950  1.00 17.04 ? 93  ALA   A CA  1 
ATOM   120  C  C   . ALA   A 1 19  ? 29.776 -7.144  11.383  1.00 19.01 ? 93  ALA   A C   1 
ATOM   121  O  O   . ALA   A 1 19  ? 29.155 -7.915  12.112  1.00 19.62 ? 93  ALA   A O   1 
ATOM   122  C  CB  . ALA   A 1 19  ? 29.366 -4.660  11.453  1.00 16.15 ? 93  ALA   A CB  1 
ATOM   123  N  N   . LEU   A 1 20  ? 30.060 -7.363  10.112  1.00 18.83 ? 94  LEU   A N   1 
ATOM   124  C  CA  . LEU   A 1 20  ? 29.679 -8.646  9.512   1.00 20.34 ? 94  LEU   A CA  1 
ATOM   125  C  C   . LEU   A 1 20  ? 30.419 -9.784  10.236  1.00 22.59 ? 94  LEU   A C   1 
ATOM   126  O  O   . LEU   A 1 20  ? 29.831 -10.862 10.468  1.00 24.21 ? 94  LEU   A O   1 
ATOM   127  C  CB  . LEU   A 1 20  ? 29.917 -8.599  8.008   1.00 20.07 ? 94  LEU   A CB  1 
ATOM   128  C  CG  . LEU   A 1 20  ? 28.984 -7.691  7.200   1.00 21.25 ? 94  LEU   A CG  1 
ATOM   129  C  CD1 . LEU   A 1 20  ? 29.380 -7.440  5.747   1.00 23.64 ? 94  LEU   A CD1 1 
ATOM   130  C  CD2 . LEU   A 1 20  ? 27.532 -8.233  7.248   1.00 22.41 ? 94  LEU   A CD2 1 
ATOM   131  N  N   . ASN   A 1 21  ? 31.673 -9.593  10.661  1.00 22.81 ? 95  ASN   A N   1 
ATOM   132  C  CA  . ASN   A 1 21  ? 32.372 -10.670 11.383  1.00 23.23 ? 95  ASN   A CA  1 
ATOM   133  C  C   . ASN   A 1 21  ? 31.717 -11.005 12.735  1.00 24.30 ? 95  ASN   A C   1 
ATOM   134  O  O   . ASN   A 1 21  ? 31.539 -12.201 13.044  1.00 24.75 ? 95  ASN   A O   1 
ATOM   135  C  CB  . ASN   A 1 21  ? 33.833 -10.310 11.640  1.00 26.09 ? 95  ASN   A CB  1 
ATOM   136  C  CG  . ASN   A 1 21  ? 34.701 -10.232 10.403  1.00 31.77 ? 95  ASN   A CG  1 
ATOM   137  O  OD1 . ASN   A 1 21  ? 34.353 -10.704 9.312   1.00 37.80 ? 95  ASN   A OD1 1 
ATOM   138  N  ND2 . ASN   A 1 21  ? 35.858 -9.589  10.554  1.00 37.87 ? 95  ASN   A ND2 1 
ATOM   139  N  N   . ILE   A 1 22  ? 31.374 -10.040 13.606  1.00 21.80 ? 96  ILE   A N   1 
ATOM   140  C  CA  . ILE   A 1 22  ? 30.801 -10.380 14.897  1.00 21.50 ? 96  ILE   A CA  1 
ATOM   141  C  C   . ILE   A 1 22  ? 29.392 -10.945 14.728  1.00 24.80 ? 96  ILE   A C   1 
ATOM   142  O  O   . ILE   A 1 22  ? 28.981 -11.787 15.526  1.00 24.30 ? 96  ILE   A O   1 
ATOM   143  C  CB  . ILE   A 1 22  ? 30.873 -9.234  15.948  1.00 22.18 ? 96  ILE   A CB  1 
ATOM   144  C  CG1 . ILE   A 1 22  ? 30.515 -9.711  17.384  1.00 22.72 ? 96  ILE   A CG1 1 
ATOM   145  C  CG2 . ILE   A 1 22  ? 30.017 -8.012  15.602  1.00 23.27 ? 96  ILE   A CG2 1 
ATOM   146  C  CD1 . ILE   A 1 22  ? 31.407 -10.825 17.946  1.00 21.49 ? 96  ILE   A CD1 1 
ATOM   147  N  N   . ILE   A 1 23  ? 28.663 -10.466 13.723  1.00 22.87 ? 97  ILE   A N   1 
ATOM   148  C  CA  . ILE   A 1 23  ? 27.353 -11.005 13.369  1.00 24.66 ? 97  ILE   A CA  1 
ATOM   149  C  C   . ILE   A 1 23  ? 27.499 -12.482 13.008  1.00 24.82 ? 97  ILE   A C   1 
ATOM   150  O  O   . ILE   A 1 23  ? 26.772 -13.295 13.606  1.00 25.77 ? 97  ILE   A O   1 
ATOM   151  C  CB  . ILE   A 1 23  ? 26.669 -10.171 12.262  1.00 24.57 ? 97  ILE   A CB  1 
ATOM   152  C  CG1 . ILE   A 1 23  ? 26.184 -8.833  12.843  1.00 23.88 ? 97  ILE   A CG1 1 
ATOM   153  C  CG2 . ILE   A 1 23  ? 25.517 -10.920 11.581  1.00 26.66 ? 97  ILE   A CG2 1 
ATOM   154  C  CD1 . ILE   A 1 23  ? 25.793 -7.789  11.795  1.00 25.58 ? 97  ILE   A CD1 1 
ATOM   155  N  N   . ARG   A 1 24  ? 28.413 -12.788 12.073  1.00 25.65 ? 98  ARG   A N   1 
ATOM   156  C  CA  . ARG   A 1 24  ? 28.647 -14.156 11.619  1.00 26.23 ? 98  ARG   A CA  1 
ATOM   157  C  C   . ARG   A 1 24  ? 28.921 -15.034 12.836  1.00 28.70 ? 98  ARG   A C   1 
ATOM   158  O  O   . ARG   A 1 24  ? 28.288 -16.095 13.011  1.00 30.53 ? 98  ARG   A O   1 
ATOM   159  C  CB  . ARG   A 1 24  ? 29.775 -14.136 10.578  1.00 27.48 ? 98  ARG   A CB  1 
ATOM   160  C  CG  . ARG   A 1 24  ? 30.037 -15.481 9.900   1.00 31.27 ? 98  ARG   A CG  1 
ATOM   161  C  CD  . ARG   A 1 24  ? 31.348 -15.485 9.140   1.00 32.10 ? 98  ARG   A CD  1 
ATOM   162  N  NE  . ARG   A 1 24  ? 31.411 -14.575 7.997   1.00 38.30 ? 98  ARG   A NE  1 
ATOM   163  C  CZ  . ARG   A 1 24  ? 32.220 -13.524 7.874   1.00 36.25 ? 98  ARG   A CZ  1 
ATOM   164  N  NH1 . ARG   A 1 24  ? 33.025 -13.148 8.853   1.00 34.55 ? 98  ARG   A NH1 1 
ATOM   165  N  NH2 . ARG   A 1 24  ? 32.193 -12.843 6.756   1.00 38.94 ? 98  ARG   A NH2 1 
ATOM   166  N  N   . GLU   A 1 25  ? 29.857 -14.612 13.688  1.00 27.27 ? 99  GLU   A N   1 
ATOM   167  C  CA  . GLU   A 1 25  ? 30.262 -15.396 14.844  1.00 28.39 ? 99  GLU   A CA  1 
ATOM   168  C  C   . GLU   A 1 25  ? 29.146 -15.542 15.877  1.00 32.79 ? 99  GLU   A C   1 
ATOM   169  O  O   . GLU   A 1 25  ? 29.017 -16.581 16.547  1.00 31.81 ? 99  GLU   A O   1 
ATOM   170  C  CB  . GLU   A 1 25  ? 31.504 -14.792 15.508  1.00 30.94 ? 99  GLU   A CB  1 
ATOM   171  C  CG  . GLU   A 1 25  ? 32.769 -14.977 14.675  1.00 33.32 ? 99  GLU   A CG  1 
ATOM   172  C  CD  . GLU   A 1 25  ? 33.037 -16.433 14.304  1.00 36.56 ? 99  GLU   A CD  1 
ATOM   173  O  OE1 . GLU   A 1 25  ? 32.915 -17.319 15.179  1.00 39.55 ? 99  GLU   A OE1 1 
ATOM   174  O  OE2 . GLU   A 1 25  ? 33.305 -16.693 13.117  1.00 43.48 ? 99  GLU   A OE2 1 
ATOM   175  N  N   . CYS   A 1 26  ? 28.361 -14.478 16.044  1.00 32.01 ? 100 CYS   A N   1 
ATOM   176  C  CA  . CYS   A 1 26  ? 27.294 -14.443 17.031  1.00 33.15 ? 100 CYS   A CA  1 
ATOM   177  C  C   . CYS   A 1 26  ? 26.224 -15.448 16.588  1.00 35.09 ? 100 CYS   A C   1 
ATOM   178  O  O   . CYS   A 1 26  ? 25.731 -16.232 17.412  1.00 37.32 ? 100 CYS   A O   1 
ATOM   179  C  CB  . CYS   A 1 26  ? 26.927 -12.968 17.346  1.00 28.47 ? 100 CYS   A CB  1 
ATOM   180  S  SG  . CYS   A 1 26  ? 27.779 -12.303 18.783  1.00 32.73 ? 100 CYS   A SG  1 
ATOM   181  N  N   . ASN   A 1 27  ? 25.959 -15.524 15.275  1.00 31.75 ? 101 ASN   A N   1 
ATOM   182  C  CA  . ASN   A 1 27  ? 24.910 -16.373 14.725  1.00 35.65 ? 101 ASN   A CA  1 
ATOM   183  C  C   . ASN   A 1 27  ? 25.243 -17.857 14.949  1.00 38.83 ? 101 ASN   A C   1 
ATOM   184  O  O   . ASN   A 1 27  ? 24.338 -18.660 15.152  1.00 40.70 ? 101 ASN   A O   1 
ATOM   185  C  CB  . ASN   A 1 27  ? 24.598 -16.037 13.261  1.00 31.07 ? 101 ASN   A CB  1 
ATOM   186  C  CG  . ASN   A 1 27  ? 23.611 -14.895 13.073  1.00 31.31 ? 101 ASN   A CG  1 
ATOM   187  O  OD1 . ASN   A 1 27  ? 23.410 -14.388 11.971  1.00 32.59 ? 101 ASN   A OD1 1 
ATOM   188  N  ND2 . ASN   A 1 27  ? 22.938 -14.501 14.119  1.00 29.37 ? 101 ASN   A ND2 1 
ATOM   189  N  N   . LYS   A 1 28  ? 26.524 -18.239 14.919  1.00 38.75 ? 102 LYS   A N   1 
ATOM   190  C  CA  . LYS   A 1 28  ? 26.894 -19.631 15.175  1.00 36.82 ? 102 LYS   A CA  1 
ATOM   191  C  C   . LYS   A 1 28  ? 26.484 -20.085 16.579  1.00 37.71 ? 102 LYS   A C   1 
ATOM   192  O  O   . LYS   A 1 28  ? 26.191 -21.266 16.794  1.00 42.59 ? 102 LYS   A O   1 
ATOM   193  C  CB  . LYS   A 1 28  ? 28.402 -19.815 14.994  1.00 35.59 ? 102 LYS   A CB  1 
ATOM   194  C  CG  . LYS   A 1 28  ? 28.880 -19.706 13.571  1.00 37.19 ? 102 LYS   A CG  1 
ATOM   195  C  CD  . LYS   A 1 28  ? 30.388 -19.538 13.475  1.00 42.69 ? 102 LYS   A CD  1 
ATOM   196  C  CE  . LYS   A 1 28  ? 30.830 -19.347 12.067  1.00 47.77 ? 102 LYS   A CE  1 
ATOM   197  N  NZ  . LYS   A 1 28  ? 32.281 -19.162 11.995  1.00 53.95 ? 102 LYS   A NZ  1 
ATOM   198  N  N   . ILE   A 1 29  ? 26.520 -19.181 17.565  1.00 39.17 ? 103 ILE   A N   1 
ATOM   199  C  CA  . ILE   A 1 29  ? 26.124 -19.527 18.926  1.00 38.00 ? 103 ILE   A CA  1 
ATOM   200  C  C   . ILE   A 1 29  ? 24.607 -19.649 19.004  1.00 40.61 ? 103 ILE   A C   1 
ATOM   201  O  O   . ILE   A 1 29  ? 24.107 -20.533 19.692  1.00 39.69 ? 103 ILE   A O   1 
ATOM   202  C  CB  . ILE   A 1 29  ? 26.667 -18.510 19.949  1.00 36.03 ? 103 ILE   A CB  1 
ATOM   203  C  CG1 . ILE   A 1 29  ? 28.189 -18.495 19.908  1.00 34.11 ? 103 ILE   A CG1 1 
ATOM   204  C  CG2 . ILE   A 1 29  ? 26.137 -18.785 21.366  1.00 34.82 ? 103 ILE   A CG2 1 
ATOM   205  C  CD1 . ILE   A 1 29  ? 28.826 -17.449 20.810  1.00 32.41 ? 103 ILE   A CD1 1 
ATOM   206  N  N   . GLU   A 1 30  ? 23.890 -18.729 18.348  1.00 42.37 ? 104 GLU   A N   1 
ATOM   207  C  CA  . GLU   A 1 30  ? 22.456 -18.863 18.097  1.00 51.67 ? 104 GLU   A CA  1 
ATOM   208  C  C   . GLU   A 1 30  ? 22.028 -17.728 17.165  1.00 50.66 ? 104 GLU   A C   1 
ATOM   209  O  O   . GLU   A 1 30  ? 22.522 -16.607 17.317  1.00 43.14 ? 104 GLU   A O   1 
ATOM   210  C  CB  . GLU   A 1 30  ? 21.594 -18.879 19.366  1.00 60.27 ? 104 GLU   A CB  1 
ATOM   211  C  CG  . GLU   A 1 30  ? 21.272 -17.500 19.932  1.00 65.93 ? 104 GLU   A CG  1 
ATOM   212  C  CD  . GLU   A 1 30  ? 20.531 -17.505 21.254  1.00 71.81 ? 104 GLU   A CD  1 
ATOM   213  O  OE1 . GLU   A 1 30  ? 21.085 -18.029 22.242  1.00 78.17 ? 104 GLU   A OE1 1 
ATOM   214  O  OE2 . GLU   A 1 30  ? 19.399 -16.975 21.293  1.00 75.90 ? 104 GLU   A OE2 1 
ATOM   215  N  N   . ASN   A 1 31  ? 21.103 -18.022 16.232  1.00 48.48 ? 105 ASN   A N   1 
ATOM   216  C  CA  . ASN   A 1 31  ? 20.802 -17.153 15.098  1.00 53.08 ? 105 ASN   A CA  1 
ATOM   217  C  C   . ASN   A 1 31  ? 19.976 -15.922 15.490  1.00 49.62 ? 105 ASN   A C   1 
ATOM   218  O  O   . ASN   A 1 31  ? 18.753 -15.920 15.364  1.00 52.06 ? 105 ASN   A O   1 
ATOM   219  C  CB  . ASN   A 1 31  ? 20.014 -17.876 14.011  1.00 54.96 ? 105 ASN   A CB  1 
ATOM   220  C  CG  . ASN   A 1 31  ? 19.622 -16.937 12.888  1.00 63.04 ? 105 ASN   A CG  1 
ATOM   221  O  OD1 . ASN   A 1 31  ? 18.437 -16.620 12.712  1.00 62.15 ? 105 ASN   A OD1 1 
ATOM   222  N  ND2 . ASN   A 1 31  ? 20.599 -16.455 12.133  1.00 64.71 ? 105 ASN   A ND2 1 
ATOM   223  N  N   . VAL   A 1 32  ? 20.649 -14.837 15.888  1.00 40.10 ? 106 VAL   A N   1 
ATOM   224  C  CA  . VAL   A 1 32  ? 19.963 -13.665 16.411  1.00 39.02 ? 106 VAL   A CA  1 
ATOM   225  C  C   . VAL   A 1 32  ? 19.938 -12.504 15.411  1.00 31.19 ? 106 VAL   A C   1 
ATOM   226  O  O   . VAL   A 1 32  ? 19.129 -11.618 15.604  1.00 32.82 ? 106 VAL   A O   1 
ATOM   227  C  CB  . VAL   A 1 32  ? 20.522 -13.169 17.766  1.00 46.16 ? 106 VAL   A CB  1 
ATOM   228  C  CG1 . VAL   A 1 32  ? 20.512 -14.256 18.843  1.00 50.33 ? 106 VAL   A CG1 1 
ATOM   229  C  CG2 . VAL   A 1 32  ? 21.908 -12.563 17.616  1.00 41.77 ? 106 VAL   A CG2 1 
ATOM   230  N  N   . PHE   A 1 33  ? 20.750 -12.481 14.349  1.00 27.41 ? 107 PHE   A N   1 
ATOM   231  C  CA  . PHE   A 1 33  ? 20.742 -11.335 13.432  1.00 27.28 ? 107 PHE   A CA  1 
ATOM   232  C  C   . PHE   A 1 33  ? 20.343 -11.734 12.011  1.00 28.45 ? 107 PHE   A C   1 
ATOM   233  O  O   . PHE   A 1 33  ? 20.807 -12.762 11.529  1.00 31.08 ? 107 PHE   A O   1 
ATOM   234  C  CB  . PHE   A 1 33  ? 22.128 -10.675 13.348  1.00 27.10 ? 107 PHE   A CB  1 
ATOM   235  C  CG  . PHE   A 1 33  ? 22.657 -10.186 14.681  1.00 27.14 ? 107 PHE   A CG  1 
ATOM   236  C  CD1 . PHE   A 1 33  ? 22.143 -9.036  15.259  1.00 27.61 ? 107 PHE   A CD1 1 
ATOM   237  C  CD2 . PHE   A 1 33  ? 23.682 -10.865 15.344  1.00 28.08 ? 107 PHE   A CD2 1 
ATOM   238  C  CE1 . PHE   A 1 33  ? 22.635 -8.582  16.467  1.00 29.41 ? 107 PHE   A CE1 1 
ATOM   239  C  CE2 . PHE   A 1 33  ? 24.151 -10.405 16.567  1.00 29.83 ? 107 PHE   A CE2 1 
ATOM   240  C  CZ  . PHE   A 1 33  ? 23.613 -9.276  17.132  1.00 28.50 ? 107 PHE   A CZ  1 
ATOM   241  N  N   . ASN   A 1 34  ? 19.492 -10.923 11.352  1.00 25.51 ? 108 ASN   A N   1 
ATOM   242  C  CA  . ASN   A 1 34  ? 19.244 -10.990 9.927   1.00 26.12 ? 108 ASN   A CA  1 
ATOM   243  C  C   . ASN   A 1 34  ? 19.849 -9.766  9.244   1.00 26.68 ? 108 ASN   A C   1 
ATOM   244  O  O   . ASN   A 1 34  ? 19.415 -8.632  9.504   1.00 24.39 ? 108 ASN   A O   1 
ATOM   245  C  CB  . ASN   A 1 34  ? 17.753 -10.973 9.589   1.00 30.13 ? 108 ASN   A CB  1 
ATOM   246  C  CG  . ASN   A 1 34  ? 16.984 -12.196 10.029  1.00 37.96 ? 108 ASN   A CG  1 
ATOM   247  O  OD1 . ASN   A 1 34  ? 15.842 -12.085 10.493  1.00 46.54 ? 108 ASN   A OD1 1 
ATOM   248  N  ND2 . ASN   A 1 34  ? 17.554 -13.370 9.846   1.00 39.06 ? 108 ASN   A ND2 1 
ATOM   249  N  N   . VAL   A 1 35  ? 20.842 -10.000 8.386   1.00 25.88 ? 109 VAL   A N   1 
ATOM   250  C  CA  . VAL   A 1 35  ? 21.467 -8.962  7.588   1.00 26.54 ? 109 VAL   A CA  1 
ATOM   251  C  C   . VAL   A 1 35  ? 20.544 -8.639  6.414   1.00 24.55 ? 109 VAL   A C   1 
ATOM   252  O  O   . VAL   A 1 35  ? 20.467 -9.392  5.423   1.00 27.06 ? 109 VAL   A O   1 
ATOM   253  C  CB  . VAL   A 1 35  ? 22.878 -9.375  7.128   1.00 25.74 ? 109 VAL   A CB  1 
ATOM   254  C  CG1 . VAL   A 1 35  ? 23.497 -8.287  6.261   1.00 27.26 ? 109 VAL   A CG1 1 
ATOM   255  C  CG2 . VAL   A 1 35  ? 23.782 -9.745  8.311   1.00 28.61 ? 109 VAL   A CG2 1 
ATOM   256  N  N   . LYS   A 1 36  ? 19.799 -7.537  6.547   1.00 24.49 ? 110 LYS   A N   1 
ATOM   257  C  CA  . LYS   A 1 36  ? 18.729 -7.176  5.637   1.00 23.81 ? 110 LYS   A CA  1 
ATOM   258  C  C   . LYS   A 1 36  ? 19.174 -6.268  4.485   1.00 24.09 ? 110 LYS   A C   1 
ATOM   259  O  O   . LYS   A 1 36  ? 18.509 -6.175  3.449   1.00 23.87 ? 110 LYS   A O   1 
ATOM   260  C  CB  . LYS   A 1 36  ? 17.573 -6.420  6.285   1.00 28.60 ? 110 LYS   A CB  1 
ATOM   261  C  CG  . LYS   A 1 36  ? 16.967 -7.102  7.482   1.00 33.87 ? 110 LYS   A CG  1 
ATOM   262  C  CD  . LYS   A 1 36  ? 16.260 -8.409  7.177   1.00 38.70 ? 110 LYS   A CD  1 
ATOM   263  C  CE  . LYS   A 1 36  ? 15.062 -8.166  6.344   1.00 43.76 ? 110 LYS   A CE  1 
ATOM   264  N  NZ  . LYS   A 1 36  ? 14.375 -9.451  6.180   1.00 46.39 ? 110 LYS   A NZ  1 
ATOM   265  N  N   . ALA   A 1 37  ? 20.294 -5.547  4.661   1.00 20.78 ? 111 ALA   A N   1 
ATOM   266  C  CA  . ALA   A 1 37  ? 20.720 -4.600  3.644   1.00 20.16 ? 111 ALA   A CA  1 
ATOM   267  C  C   . ALA   A 1 37  ? 22.217 -4.322  3.769   1.00 20.45 ? 111 ALA   A C   1 
ATOM   268  O  O   . ALA   A 1 37  ? 22.728 -4.279  4.892   1.00 20.47 ? 111 ALA   A O   1 
ATOM   269  C  CB  . ALA   A 1 37  ? 19.963 -3.286  3.758   1.00 20.80 ? 111 ALA   A CB  1 
ATOM   270  N  N   . LEU   A 1 38  ? 22.863 -4.082  2.628   1.00 20.30 ? 112 LEU   A N   1 
ATOM   271  C  CA  . LEU   A 1 38  ? 24.271 -3.730  2.524   1.00 19.95 ? 112 LEU   A CA  1 
ATOM   272  C  C   . LEU   A 1 38  ? 24.373 -2.554  1.573   1.00 21.96 ? 112 LEU   A C   1 
ATOM   273  O  O   . LEU   A 1 38  ? 23.742 -2.591  0.495   1.00 21.60 ? 112 LEU   A O   1 
ATOM   274  C  CB  . LEU   A 1 38  ? 25.113 -4.897  2.010   1.00 21.26 ? 112 LEU   A CB  1 
ATOM   275  C  CG  . LEU   A 1 38  ? 25.112 -6.165  2.850   1.00 20.67 ? 112 LEU   A CG  1 
ATOM   276  C  CD1 . LEU   A 1 38  ? 25.926 -7.247  2.110   1.00 23.78 ? 112 LEU   A CD1 1 
ATOM   277  C  CD2 . LEU   A 1 38  ? 25.687 -5.921  4.232   1.00 20.91 ? 112 LEU   A CD2 1 
ATOM   278  N  N   . TYR   A 1 39  ? 25.165 -1.524  1.916   1.00 20.24 ? 113 TYR   A N   1 
ATOM   279  C  CA  . TYR   A 1 39  ? 25.319 -0.315  1.138   1.00 19.52 ? 113 TYR   A CA  1 
ATOM   280  C  C   . TYR   A 1 39  ? 26.784 0.085   1.142   1.00 19.92 ? 113 TYR   A C   1 
ATOM   281  O  O   . TYR   A 1 39  ? 27.436 0.057   2.218   1.00 19.39 ? 113 TYR   A O   1 
ATOM   282  C  CB  . TYR   A 1 39  ? 24.438 0.757   1.777   1.00 20.47 ? 113 TYR   A CB  1 
ATOM   283  C  CG  . TYR   A 1 39  ? 24.451 2.185   1.253   1.00 20.56 ? 113 TYR   A CG  1 
ATOM   284  C  CD1 . TYR   A 1 39  ? 24.667 2.503   -0.100  1.00 21.37 ? 113 TYR   A CD1 1 
ATOM   285  C  CD2 . TYR   A 1 39  ? 24.117 3.232   2.099   1.00 20.35 ? 113 TYR   A CD2 1 
ATOM   286  C  CE1 . TYR   A 1 39  ? 24.573 3.809   -0.553  1.00 21.04 ? 113 TYR   A CE1 1 
ATOM   287  C  CE2 . TYR   A 1 39  ? 24.075 4.542   1.666   1.00 21.24 ? 113 TYR   A CE2 1 
ATOM   288  C  CZ  . TYR   A 1 39  ? 24.283 4.828   0.327   1.00 21.94 ? 113 TYR   A CZ  1 
ATOM   289  O  OH  . TYR   A 1 39  ? 24.176 6.124   -0.106  1.00 23.21 ? 113 TYR   A OH  1 
ATOM   290  N  N   . VAL   A 1 40  ? 27.310 0.387   -0.048  1.00 20.55 ? 114 VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 40  ? 28.688 0.809   -0.235  1.00 20.29 ? 114 VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 40  ? 28.710 1.960   -1.235  1.00 20.21 ? 114 VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 40  ? 27.688 2.342   -1.806  1.00 20.75 ? 114 VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 40  ? 29.578 -0.372  -0.679  1.00 20.10 ? 114 VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 40  ? 29.327 -1.630  0.145   1.00 22.05 ? 114 VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 40  ? 29.449 -0.672  -2.187  1.00 22.49 ? 114 VAL   A CG2 1 
ATOM   297  N  N   . ASN   A 1 41  ? 29.895 2.565   -1.411  1.00 21.93 ? 115 ASN   A N   1 
ATOM   298  C  CA  . ASN   A 1 41  ? 30.069 3.649   -2.369  1.00 22.38 ? 115 ASN   A CA  1 
ATOM   299  C  C   . ASN   A 1 41  ? 30.349 3.105   -3.780  1.00 22.78 ? 115 ASN   A C   1 
ATOM   300  O  O   . ASN   A 1 41  ? 29.556 3.339   -4.691  1.00 25.12 ? 115 ASN   A O   1 
ATOM   301  C  CB  . ASN   A 1 41  ? 31.171 4.602   -1.935  1.00 22.49 ? 115 ASN   A CB  1 
ATOM   302  C  CG  . ASN   A 1 41  ? 31.254 5.837   -2.796  1.00 25.97 ? 115 ASN   A CG  1 
ATOM   303  O  OD1 . ASN   A 1 41  ? 30.317 6.172   -3.533  1.00 28.12 ? 115 ASN   A OD1 1 
ATOM   304  N  ND2 . ASN   A 1 41  ? 32.358 6.546   -2.703  1.00 28.49 ? 115 ASN   A ND2 1 
ATOM   305  N  N   . LYS   A 1 42  ? 31.483 2.457   -3.940  1.00 21.63 ? 116 LYS   A N   1 
ATOM   306  C  CA  . LYS   A 1 42  ? 31.908 2.007   -5.262  1.00 25.37 ? 116 LYS   A CA  1 
ATOM   307  C  C   . LYS   A 1 42  ? 32.557 0.629   -5.263  1.00 25.56 ? 116 LYS   A C   1 
ATOM   308  O  O   . LYS   A 1 42  ? 32.949 0.164   -6.349  1.00 25.47 ? 116 LYS   A O   1 
ATOM   309  C  CB  . LYS   A 1 42  ? 32.735 3.128   -5.894  1.00 30.80 ? 116 LYS   A CB  1 
ATOM   310  C  CG  . LYS   A 1 42  ? 34.104 3.457   -5.338  1.00 37.40 ? 116 LYS   A CG  1 
ATOM   311  C  CD  . LYS   A 1 42  ? 34.516 4.819   -5.897  1.00 45.74 ? 116 LYS   A CD  1 
ATOM   312  C  CE  . LYS   A 1 42  ? 35.997 4.979   -6.026  1.00 53.95 ? 116 LYS   A CE  1 
ATOM   313  N  NZ  . LYS   A 1 42  ? 36.657 4.652   -4.758  1.00 58.30 ? 116 LYS   A NZ  1 
ATOM   314  N  N   . SER   A 1 43  ? 32.680 -0.082  -4.144  1.00 24.20 ? 117 SER   A N   1 
ATOM   315  C  CA  . SER   A 1 43  ? 33.363 -1.356  -4.062  1.00 23.60 ? 117 SER   A CA  1 
ATOM   316  C  C   . SER   A 1 43  ? 32.422 -2.479  -4.515  1.00 23.58 ? 117 SER   A C   1 
ATOM   317  O  O   . SER   A 1 43  ? 31.999 -3.335  -3.743  1.00 23.02 ? 117 SER   A O   1 
ATOM   318  C  CB  . SER   A 1 43  ? 33.872 -1.607  -2.639  1.00 24.05 ? 117 SER   A CB  1 
ATOM   319  O  OG  . SER   A 1 43  ? 34.976 -0.773  -2.321  1.00 24.29 ? 117 SER   A OG  1 
ATOM   320  N  N   . VAL   A 1 44  ? 32.182 -2.508  -5.835  1.00 25.47 ? 118 VAL   A N   1 
ATOM   321  C  CA  . VAL   A 1 44  ? 31.120 -3.299  -6.445  1.00 27.41 ? 118 VAL   A CA  1 
ATOM   322  C  C   . VAL   A 1 44  ? 31.466 -4.786  -6.375  1.00 25.45 ? 118 VAL   A C   1 
ATOM   323  O  O   . VAL   A 1 44  ? 30.621 -5.592  -6.003  1.00 25.56 ? 118 VAL   A O   1 
ATOM   324  C  CB  . VAL   A 1 44  ? 30.795 -2.857  -7.892  1.00 29.81 ? 118 VAL   A CB  1 
ATOM   325  C  CG1 . VAL   A 1 44  ? 32.000 -2.914  -8.834  1.00 30.97 ? 118 VAL   A CG1 1 
ATOM   326  C  CG2 . VAL   A 1 44  ? 29.661 -3.703  -8.460  1.00 29.76 ? 118 VAL   A CG2 1 
ATOM   327  N  N   . ASN   A 1 45  ? 32.741 -5.180  -6.601  1.00 25.99 ? 119 ASN   A N   1 
ATOM   328  C  CA  . ASN   A 1 45  ? 33.137 -6.579  -6.546  1.00 28.79 ? 119 ASN   A CA  1 
ATOM   329  C  C   . ASN   A 1 45  ? 33.019 -7.116  -5.129  1.00 28.15 ? 119 ASN   A C   1 
ATOM   330  O  O   . ASN   A 1 45  ? 32.567 -8.228  -4.887  1.00 27.52 ? 119 ASN   A O   1 
ATOM   331  C  CB  . ASN   A 1 45  ? 34.525 -6.799  -7.152  1.00 30.27 ? 119 ASN   A CB  1 
ATOM   332  C  CG  . ASN   A 1 45  ? 34.533 -6.470  -8.627  1.00 33.80 ? 119 ASN   A CG  1 
ATOM   333  O  OD1 . ASN   A 1 45  ? 35.052 -5.429  -9.048  1.00 36.79 ? 119 ASN   A OD1 1 
ATOM   334  N  ND2 . ASN   A 1 45  ? 33.859 -7.281  -9.425  1.00 36.57 ? 119 ASN   A ND2 1 
ATOM   335  N  N   . GLU   A 1 46  ? 33.430 -6.297  -4.139  1.00 25.57 ? 120 GLU   A N   1 
ATOM   336  C  CA  . GLU   A 1 46  ? 33.424 -6.720  -2.754  1.00 25.31 ? 120 GLU   A CA  1 
ATOM   337  C  C   . GLU   A 1 46  ? 31.987 -6.824  -2.227  1.00 22.53 ? 120 GLU   A C   1 
ATOM   338  O  O   . GLU   A 1 46  ? 31.693 -7.717  -1.438  1.00 24.29 ? 120 GLU   A O   1 
ATOM   339  C  CB  . GLU   A 1 46  ? 34.305 -5.801  -1.899  1.00 26.30 ? 120 GLU   A CB  1 
ATOM   340  C  CG  . GLU   A 1 46  ? 35.745 -5.712  -2.402  1.00 26.35 ? 120 GLU   A CG  1 
ATOM   341  C  CD  . GLU   A 1 46  ? 36.090 -4.797  -3.582  1.00 26.15 ? 120 GLU   A CD  1 
ATOM   342  O  OE1 . GLU   A 1 46  ? 35.338 -4.140  -4.308  1.00 28.07 ? 120 GLU   A OE1 1 
ATOM   343  O  OE2 . GLU   A 1 46  ? 37.340 -4.788  -3.777  1.00 37.65 ? 120 GLU   A OE2 1 
ATOM   344  N  N   . LEU   A 1 47  ? 31.133 -5.876  -2.618  1.00 23.65 ? 121 LEU   A N   1 
ATOM   345  C  CA  . LEU   A 1 47  ? 29.726 -5.938  -2.230  1.00 24.40 ? 121 LEU   A CA  1 
ATOM   346  C  C   . LEU   A 1 47  ? 29.060 -7.188  -2.828  1.00 25.11 ? 121 LEU   A C   1 
ATOM   347  O  O   . LEU   A 1 47  ? 28.329 -7.887  -2.135  1.00 25.33 ? 121 LEU   A O   1 
ATOM   348  C  CB  . LEU   A 1 47  ? 28.948 -4.715  -2.674  1.00 24.03 ? 121 LEU   A CB  1 
ATOM   349  C  CG  . LEU   A 1 47  ? 27.446 -4.777  -2.415  1.00 23.28 ? 121 LEU   A CG  1 
ATOM   350  C  CD1 . LEU   A 1 47  ? 27.139 -4.950  -0.928  1.00 22.89 ? 121 LEU   A CD1 1 
ATOM   351  C  CD2 . LEU   A 1 47  ? 26.811 -3.568  -2.990  1.00 23.48 ? 121 LEU   A CD2 1 
ATOM   352  N  N   . TYR   A 1 48  ? 29.401 -7.514  -4.074  1.00 28.70 ? 122 TYR   A N   1 
ATOM   353  C  CA  . TYR   A 1 48  ? 28.908 -8.742  -4.702  1.00 29.38 ? 122 TYR   A CA  1 
ATOM   354  C  C   . TYR   A 1 48  ? 29.280 -9.964  -3.876  1.00 25.13 ? 122 TYR   A C   1 
ATOM   355  O  O   . TYR   A 1 48  ? 28.449 -10.820 -3.562  1.00 26.88 ? 122 TYR   A O   1 
ATOM   356  C  CB  . TYR   A 1 48  ? 29.461 -8.874  -6.123  1.00 28.96 ? 122 TYR   A CB  1 
ATOM   357  C  CG  . TYR   A 1 48  ? 29.475 -10.298 -6.673  1.00 32.44 ? 122 TYR   A CG  1 
ATOM   358  C  CD1 . TYR   A 1 48  ? 28.283 -10.963 -6.936  1.00 35.09 ? 122 TYR   A CD1 1 
ATOM   359  C  CD2 . TYR   A 1 48  ? 30.669 -10.971 -6.903  1.00 35.57 ? 122 TYR   A CD2 1 
ATOM   360  C  CE1 . TYR   A 1 48  ? 28.277 -12.248 -7.466  1.00 37.00 ? 122 TYR   A CE1 1 
ATOM   361  C  CE2 . TYR   A 1 48  ? 30.677 -12.266 -7.412  1.00 38.50 ? 122 TYR   A CE2 1 
ATOM   362  C  CZ  . TYR   A 1 48  ? 29.475 -12.902 -7.674  1.00 41.25 ? 122 TYR   A CZ  1 
ATOM   363  O  OH  . TYR   A 1 48  ? 29.425 -14.171 -8.172  1.00 45.85 ? 122 TYR   A OH  1 
ATOM   364  N  N   . GLU   A 1 49  ? 30.549 -10.071 -3.478  1.00 24.24 ? 123 GLU   A N   1 
ATOM   365  C  CA  . GLU   A 1 49  ? 30.969 -11.185 -2.658  1.00 26.46 ? 123 GLU   A CA  1 
ATOM   366  C  C   . GLU   A 1 49  ? 30.194 -11.244 -1.335  1.00 27.20 ? 123 GLU   A C   1 
ATOM   367  O  O   . GLU   A 1 49  ? 29.882 -12.312 -0.815  1.00 28.23 ? 123 GLU   A O   1 
ATOM   368  C  CB  . GLU   A 1 49  ? 32.486 -11.220 -2.461  1.00 29.15 ? 123 GLU   A CB  1 
ATOM   369  C  CG  . GLU   A 1 49  ? 33.280 -11.370 -3.760  1.00 32.53 ? 123 GLU   A CG  1 
ATOM   370  C  CD  . GLU   A 1 49  ? 33.165 -12.720 -4.462  1.00 35.38 ? 123 GLU   A CD  1 
ATOM   371  O  OE1 . GLU   A 1 49  ? 32.615 -13.674 -3.858  1.00 38.37 ? 123 GLU   A OE1 1 
ATOM   372  O  OE2 . GLU   A 1 49  ? 33.654 -12.817 -5.615  1.00 40.81 ? 123 GLU   A OE2 1 
ATOM   373  N  N   . GLN   A 1 50  ? 29.966 -10.076 -0.688  1.00 25.00 ? 124 GLN   A N   1 
ATOM   374  C  CA  . GLN   A 1 50  ? 29.199 -10.051 0.547   1.00 23.99 ? 124 GLN   A CA  1 
ATOM   375  C  C   . GLN   A 1 50  ? 27.747 -10.479 0.302   1.00 23.80 ? 124 GLN   A C   1 
ATOM   376  O  O   . GLN   A 1 50  ? 27.195 -11.176 1.144   1.00 24.59 ? 124 GLN   A O   1 
ATOM   377  C  CB  . GLN   A 1 50  ? 29.252 -8.639  1.155   1.00 24.18 ? 124 GLN   A CB  1 
ATOM   378  C  CG  . GLN   A 1 50  ? 30.606 -8.262  1.735   1.00 23.37 ? 124 GLN   A CG  1 
ATOM   379  C  CD  . GLN   A 1 50  ? 30.598 -6.861  2.327   1.00 22.32 ? 124 GLN   A CD  1 
ATOM   380  O  OE1 . GLN   A 1 50  ? 29.744 -6.048  1.998   1.00 22.19 ? 124 GLN   A OE1 1 
ATOM   381  N  NE2 . GLN   A 1 50  ? 31.545 -6.625  3.210   1.00 22.73 ? 124 GLN   A NE2 1 
ATOM   382  N  N   . ALA   A 1 51  ? 27.193 -10.072 -0.831  1.00 23.43 ? 125 ALA   A N   1 
ATOM   383  C  CA  . ALA   A 1 51  ? 25.833 -10.429 -1.238  1.00 26.63 ? 125 ALA   A CA  1 
ATOM   384  C  C   . ALA   A 1 51  ? 25.720 -11.951 -1.361  1.00 29.36 ? 125 ALA   A C   1 
ATOM   385  O  O   . ALA   A 1 51  ? 24.761 -12.551 -0.870  1.00 27.57 ? 125 ALA   A O   1 
ATOM   386  C  CB  . ALA   A 1 51  ? 25.488 -9.746  -2.525  1.00 28.18 ? 125 ALA   A CB  1 
ATOM   387  N  N   . ARG   A 1 52  ? 26.745 -12.588 -1.938  1.00 29.41 ? 126 ARG   A N   1 
ATOM   388  C  CA  . ARG   A 1 52  ? 26.676 -14.039 -2.097  1.00 30.65 ? 126 ARG   A CA  1 
ATOM   389  C  C   . ARG   A 1 52  ? 26.668 -14.722 -0.739  1.00 30.56 ? 126 ARG   A C   1 
ATOM   390  O  O   . ARG   A 1 52  ? 26.022 -15.749 -0.564  1.00 31.96 ? 126 ARG   A O   1 
ATOM   391  C  CB  . ARG   A 1 52  ? 27.822 -14.533 -2.995  1.00 33.66 ? 126 ARG   A CB  1 
ATOM   392  C  CG  . ARG   A 1 52  ? 27.880 -16.052 -3.099  1.00 36.13 ? 126 ARG   A CG  1 
ATOM   393  C  CD  . ARG   A 1 52  ? 29.010 -16.549 -4.017  1.00 38.12 ? 126 ARG   A CD  1 
ATOM   394  N  NE  . ARG   A 1 52  ? 28.711 -16.185 -5.401  1.00 36.28 ? 126 ARG   A NE  1 
ATOM   395  C  CZ  . ARG   A 1 52  ? 27.845 -16.852 -6.197  1.00 34.85 ? 126 ARG   A CZ  1 
ATOM   396  N  NH1 . ARG   A 1 52  ? 27.237 -17.949 -5.767  1.00 35.41 ? 126 ARG   A NH1 1 
ATOM   397  N  NH2 . ARG   A 1 52  ? 27.592 -16.399 -7.388  1.00 32.09 ? 126 ARG   A NH2 1 
ATOM   398  N  N   . GLU   A 1 53  ? 27.414 -14.190 0.246   1.00 26.01 ? 127 GLU   A N   1 
ATOM   399  C  CA  . GLU   A 1 53  ? 27.455 -14.827 1.552   1.00 26.41 ? 127 GLU   A CA  1 
ATOM   400  C  C   . GLU   A 1 53  ? 26.178 -14.560 2.361   1.00 30.56 ? 127 GLU   A C   1 
ATOM   401  O  O   . GLU   A 1 53  ? 25.620 -15.461 2.970   1.00 30.37 ? 127 GLU   A O   1 
ATOM   402  C  CB  . GLU   A 1 53  ? 28.670 -14.390 2.374   1.00 28.42 ? 127 GLU   A CB  1 
ATOM   403  C  CG  . GLU   A 1 53  ? 28.695 -14.982 3.779   1.00 29.48 ? 127 GLU   A CG  1 
ATOM   404  C  CD  . GLU   A 1 53  ? 29.943 -14.799 4.617   1.00 32.39 ? 127 GLU   A CD  1 
ATOM   405  O  OE1 . GLU   A 1 53  ? 30.848 -14.065 4.163   1.00 34.87 ? 127 GLU   A OE1 1 
ATOM   406  O  OE2 . GLU   A 1 53  ? 29.997 -15.365 5.733   1.00 35.46 ? 127 GLU   A OE2 1 
ATOM   407  N  N   . PHE   A 1 54  ? 25.773 -13.280 2.476   1.00 28.78 ? 128 PHE   A N   1 
ATOM   408  C  CA  . PHE   A 1 54  ? 24.743 -12.894 3.432   1.00 27.02 ? 128 PHE   A CA  1 
ATOM   409  C  C   . PHE   A 1 54  ? 23.341 -12.881 2.821   1.00 27.69 ? 128 PHE   A C   1 
ATOM   410  O  O   . PHE   A 1 54  ? 22.367 -12.921 3.578   1.00 30.46 ? 128 PHE   A O   1 
ATOM   411  C  CB  . PHE   A 1 54  ? 25.159 -11.528 4.019   1.00 24.34 ? 128 PHE   A CB  1 
ATOM   412  C  CG  . PHE   A 1 54  ? 26.289 -11.684 5.022   1.00 23.59 ? 128 PHE   A CG  1 
ATOM   413  C  CD1 . PHE   A 1 54  ? 26.072 -12.155 6.315   1.00 23.95 ? 128 PHE   A CD1 1 
ATOM   414  C  CD2 . PHE   A 1 54  ? 27.600 -11.414 4.649   1.00 23.54 ? 128 PHE   A CD2 1 
ATOM   415  C  CE1 . PHE   A 1 54  ? 27.117 -12.286 7.221   1.00 25.80 ? 128 PHE   A CE1 1 
ATOM   416  C  CE2 . PHE   A 1 54  ? 28.638 -11.611 5.549   1.00 22.80 ? 128 PHE   A CE2 1 
ATOM   417  C  CZ  . PHE   A 1 54  ? 28.404 -12.056 6.810   1.00 24.57 ? 128 PHE   A CZ  1 
ATOM   418  N  N   . LEU   A 1 55  ? 23.246 -12.776 1.484   1.00 28.33 ? 129 LEU   A N   1 
ATOM   419  C  CA  . LEU   A 1 55  ? 21.983 -12.784 0.759   1.00 28.97 ? 129 LEU   A CA  1 
ATOM   420  C  C   . LEU   A 1 55  ? 20.987 -11.802 1.372   1.00 29.06 ? 129 LEU   A C   1 
ATOM   421  O  O   . LEU   A 1 55  ? 19.818 -12.118 1.582   1.00 27.60 ? 129 LEU   A O   1 
ATOM   422  C  CB  . LEU   A 1 55  ? 21.418 -14.205 0.689   1.00 31.86 ? 129 LEU   A CB  1 
ATOM   423  C  CG  . LEU   A 1 55  ? 22.312 -15.233 -0.029  1.00 31.10 ? 129 LEU   A CG  1 
ATOM   424  C  CD1 . LEU   A 1 55  ? 21.864 -16.669 0.202   1.00 34.58 ? 129 LEU   A CD1 1 
ATOM   425  C  CD2 . LEU   A 1 55  ? 22.399 -14.935 -1.512  1.00 30.61 ? 129 LEU   A CD2 1 
ATOM   426  N  N   . PRO   A 1 56  ? 21.374 -10.524 1.574   1.00 26.00 ? 130 PRO   A N   1 
ATOM   427  C  CA  . PRO   A 1 56  ? 20.418 -9.541  2.086   1.00 25.15 ? 130 PRO   A CA  1 
ATOM   428  C  C   . PRO   A 1 56  ? 19.260 -9.280  1.127   1.00 27.48 ? 130 PRO   A C   1 
ATOM   429  O  O   . PRO   A 1 56  ? 19.430 -9.303  -0.090  1.00 27.60 ? 130 PRO   A O   1 
ATOM   430  C  CB  . PRO   A 1 56  ? 21.284 -8.280  2.259   1.00 24.40 ? 130 PRO   A CB  1 
ATOM   431  C  CG  . PRO   A 1 56  ? 22.349 -8.432  1.194   1.00 25.51 ? 130 PRO   A CG  1 
ATOM   432  C  CD  . PRO   A 1 56  ? 22.670 -9.933  1.186   1.00 25.43 ? 130 PRO   A CD  1 
ATOM   433  N  N   . GLU   A 1 57  ? 18.116 -8.860  1.684   1.00 26.44 ? 131 GLU   A N   1 
ATOM   434  C  CA  . GLU   A 1 57  ? 16.981 -8.423  0.906   1.00 26.38 ? 131 GLU   A CA  1 
ATOM   435  C  C   . GLU   A 1 57  ? 17.335 -7.228  0.024   1.00 28.60 ? 131 GLU   A C   1 
ATOM   436  O  O   . GLU   A 1 57  ? 16.798 -7.092  -1.067  1.00 29.47 ? 131 GLU   A O   1 
ATOM   437  C  CB  . GLU   A 1 57  ? 15.815 -8.124  1.849   1.00 32.67 ? 131 GLU   A CB  1 
ATOM   438  C  CG  . GLU   A 1 57  ? 14.592 -7.519  1.173   1.00 39.27 ? 131 GLU   A CG  1 
ATOM   439  C  CD  . GLU   A 1 57  ? 13.401 -7.288  2.103   1.00 47.90 ? 131 GLU   A CD  1 
ATOM   440  O  OE1 . GLU   A 1 57  ? 13.555 -7.232  3.351   1.00 52.45 ? 131 GLU   A OE1 1 
ATOM   441  O  OE2 . GLU   A 1 57  ? 12.289 -7.183  1.545   1.00 53.90 ? 131 GLU   A OE2 1 
ATOM   442  N  N   . TYR   A 1 58  ? 18.167 -6.292  0.532   1.00 24.72 ? 132 TYR   A N   1 
ATOM   443  C  CA  . TYR   A 1 58  ? 18.489 -5.076  -0.194  1.00 22.33 ? 132 TYR   A CA  1 
ATOM   444  C  C   . TYR   A 1 58  ? 19.995 -4.962  -0.421  1.00 21.78 ? 132 TYR   A C   1 
ATOM   445  O  O   . TYR   A 1 58  ? 20.801 -5.280  0.461   1.00 22.56 ? 132 TYR   A O   1 
ATOM   446  C  CB  . TYR   A 1 58  ? 18.151 -3.810  0.595   1.00 22.84 ? 132 TYR   A CB  1 
ATOM   447  C  CG  . TYR   A 1 58  ? 16.680 -3.540  0.835   1.00 25.46 ? 132 TYR   A CG  1 
ATOM   448  C  CD1 . TYR   A 1 58  ? 16.028 -4.106  1.914   1.00 27.54 ? 132 TYR   A CD1 1 
ATOM   449  C  CD2 . TYR   A 1 58  ? 15.948 -2.788  -0.067  1.00 27.41 ? 132 TYR   A CD2 1 
ATOM   450  C  CE1 . TYR   A 1 58  ? 14.680 -3.859  2.135   1.00 28.64 ? 132 TYR   A CE1 1 
ATOM   451  C  CE2 . TYR   A 1 58  ? 14.606 -2.519  0.147   1.00 27.83 ? 132 TYR   A CE2 1 
ATOM   452  C  CZ  . TYR   A 1 58  ? 13.979 -3.069  1.246   1.00 28.37 ? 132 TYR   A CZ  1 
ATOM   453  O  OH  . TYR   A 1 58  ? 12.648 -2.811  1.433   1.00 36.32 ? 132 TYR   A OH  1 
ATOM   454  N  N   . LEU   A 1 59  ? 20.342 -4.421  -1.596  1.00 23.63 ? 133 LEU   A N   1 
ATOM   455  C  CA  . LEU   A 1 59  ? 21.707 -4.048  -1.931  1.00 22.53 ? 133 LEU   A CA  1 
ATOM   456  C  C   . LEU   A 1 59  ? 21.676 -2.637  -2.460  1.00 23.56 ? 133 LEU   A C   1 
ATOM   457  O  O   . LEU   A 1 59  ? 20.765 -2.270  -3.188  1.00 24.67 ? 133 LEU   A O   1 
ATOM   458  C  CB  . LEU   A 1 59  ? 22.316 -4.930  -3.014  1.00 24.30 ? 133 LEU   A CB  1 
ATOM   459  C  CG  . LEU   A 1 59  ? 22.507 -6.373  -2.621  1.00 21.63 ? 133 LEU   A CG  1 
ATOM   460  C  CD1 . LEU   A 1 59  ? 22.870 -7.199  -3.881  1.00 25.51 ? 133 LEU   A CD1 1 
ATOM   461  C  CD2 . LEU   A 1 59  ? 23.564 -6.608  -1.570  1.00 24.15 ? 133 LEU   A CD2 1 
ATOM   462  N  N   . CYS   A 1 60  ? 22.634 -1.783  -2.072  1.00 23.19 ? 134 CYS   A N   1 
ATOM   463  C  CA  . CYS   A 1 60  ? 22.672 -0.443  -2.604  1.00 22.64 ? 134 CYS   A CA  1 
ATOM   464  C  C   . CYS   A 1 60  ? 24.115 -0.021  -2.852  1.00 22.78 ? 134 CYS   A C   1 
ATOM   465  O  O   . CYS   A 1 60  ? 25.006 -0.358  -2.050  1.00 22.65 ? 134 CYS   A O   1 
ATOM   466  C  CB  . CYS   A 1 60  ? 21.907 0.521   -1.701  1.00 24.39 ? 134 CYS   A CB  1 
ATOM   467  S  SG  . CYS   A 1 60  ? 21.687 2.182   -2.377  1.00 25.42 ? 134 CYS   A SG  1 
ATOM   468  N  N   . ILE   A 1 61  ? 24.340 0.649   -3.992  1.00 23.05 ? 135 ILE   A N   1 
ATOM   469  C  CA  . ILE   A 1 61  ? 25.652 1.187   -4.301  1.00 23.09 ? 135 ILE   A CA  1 
ATOM   470  C  C   . ILE   A 1 61  ? 25.529 2.657   -4.630  1.00 23.63 ? 135 ILE   A C   1 
ATOM   471  O  O   . ILE   A 1 61  ? 24.652 3.051   -5.403  1.00 24.71 ? 135 ILE   A O   1 
ATOM   472  C  CB  . ILE   A 1 61  ? 26.344 0.370   -5.411  1.00 23.52 ? 135 ILE   A CB  1 
ATOM   473  C  CG1 . ILE   A 1 61  ? 27.848 0.670   -5.495  1.00 24.28 ? 135 ILE   A CG1 1 
ATOM   474  C  CG2 . ILE   A 1 61  ? 25.648 0.562   -6.765  1.00 26.53 ? 135 ILE   A CG2 1 
ATOM   475  C  CD1 . ILE   A 1 61  ? 28.672 -0.445  -6.079  1.00 25.40 ? 135 ILE   A CD1 1 
ATOM   476  N  N   . HIS   A 1 62  ? 26.355 3.525   -4.023  1.00 23.32 ? 136 HIS   A N   1 
ATOM   477  C  CA  . HIS   A 1 62  ? 26.141 4.954   -4.120  1.00 23.01 ? 136 HIS   A CA  1 
ATOM   478  C  C   . HIS   A 1 62  ? 26.472 5.451   -5.533  1.00 25.14 ? 136 HIS   A C   1 
ATOM   479  O  O   . HIS   A 1 62  ? 25.748 6.321   -6.035  1.00 28.51 ? 136 HIS   A O   1 
ATOM   480  C  CB  . HIS   A 1 62  ? 26.962 5.728   -3.082  1.00 22.44 ? 136 HIS   A CB  1 
ATOM   481  C  CG  . HIS   A 1 62  ? 26.511 7.112   -2.934  1.00 22.32 ? 136 HIS   A CG  1 
ATOM   482  N  ND1 . HIS   A 1 62  ? 25.352 7.362   -2.253  1.00 22.10 ? 136 HIS   A ND1 1 
ATOM   483  C  CD2 . HIS   A 1 62  ? 26.958 8.310   -3.362  1.00 24.49 ? 136 HIS   A CD2 1 
ATOM   484  C  CE1 . HIS   A 1 62  ? 25.110 8.660   -2.258  1.00 25.13 ? 136 HIS   A CE1 1 
ATOM   485  N  NE2 . HIS   A 1 62  ? 26.085 9.264   -2.906  1.00 26.36 ? 136 HIS   A NE2 1 
ATOM   486  N  N   . ASP   A 1 63  ? 27.592 4.962   -6.082  1.00 26.17 ? 137 ASP   A N   1 
ATOM   487  C  CA  . ASP   A 1 63  ? 28.109 5.462   -7.354  1.00 29.13 ? 137 ASP   A CA  1 
ATOM   488  C  C   . ASP   A 1 63  ? 27.310 4.885   -8.535  1.00 30.23 ? 137 ASP   A C   1 
ATOM   489  O  O   . ASP   A 1 63  ? 27.338 3.679   -8.793  1.00 28.37 ? 137 ASP   A O   1 
ATOM   490  C  CB  . ASP   A 1 63  ? 29.598 5.186   -7.422  1.00 31.10 ? 137 ASP   A CB  1 
ATOM   491  C  CG  . ASP   A 1 63  ? 30.341 5.677   -8.655  1.00 38.69 ? 137 ASP   A CG  1 
ATOM   492  O  OD1 . ASP   A 1 63  ? 29.673 6.167   -9.598  1.00 37.11 ? 137 ASP   A OD1 1 
ATOM   493  O  OD2 . ASP   A 1 63  ? 31.579 5.536   -8.662  1.00 40.93 ? 137 ASP   A OD2 1 
ATOM   494  N  N   . LYS   A 1 64  ? 26.609 5.782   -9.231  1.00 31.74 ? 138 LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 64  ? 25.753 5.411   -10.357 1.00 38.25 ? 138 LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 64  ? 26.543 4.672   -11.433 1.00 37.71 ? 138 LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 64  ? 26.001 3.796   -12.105 1.00 34.89 ? 138 LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 64  ? 25.141 6.649   -11.024 1.00 42.53 ? 138 LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 64  ? 23.992 7.324   -10.287 1.00 54.49 ? 138 LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 64  ? 22.597 6.814   -10.639 1.00 60.65 ? 138 LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 64  ? 21.512 7.583   -9.940  1.00 63.26 ? 138 LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 64  ? 21.693 7.668   -8.486  1.00 64.07 ? 138 LYS   A NZ  1 
ATOM   503  N  N   . SER   A 1 65  ? 27.835 4.997   -11.569 1.00 35.94 ? 139 SER   A N   1 
ATOM   504  C  CA  . SER   A 1 65  ? 28.646 4.451   -12.647 1.00 36.41 ? 139 SER   A CA  1 
ATOM   505  C  C   . SER   A 1 65  ? 28.951 2.968   -12.454 1.00 35.02 ? 139 SER   A C   1 
ATOM   506  O  O   . SER   A 1 65  ? 29.524 2.359   -13.363 1.00 39.30 ? 139 SER   A O   1 
ATOM   507  C  CB  . SER   A 1 65  ? 29.934 5.238   -12.850 1.00 38.83 ? 139 SER   A CB  1 
ATOM   508  O  OG  . SER   A 1 65  ? 30.821 5.112   -11.744 1.00 40.17 ? 139 SER   A OG  1 
ATOM   509  N  N   . VAL   A 1 66  ? 28.628 2.378   -11.281 1.00 30.61 ? 140 VAL   A N   1 
ATOM   510  C  CA  . VAL   A 1 66  ? 28.826 0.947   -11.105 1.00 29.49 ? 140 VAL   A CA  1 
ATOM   511  C  C   . VAL   A 1 66  ? 27.533 0.197   -10.763 1.00 24.79 ? 140 VAL   A C   1 
ATOM   512  O  O   . VAL   A 1 66  ? 27.604 -0.987  -10.472 1.00 28.63 ? 140 VAL   A O   1 
ATOM   513  C  CB  . VAL   A 1 66  ? 29.958 0.616   -10.110 1.00 34.47 ? 140 VAL   A CB  1 
ATOM   514  C  CG1 . VAL   A 1 66  ? 31.327 0.961   -10.690 1.00 37.76 ? 140 VAL   A CG1 1 
ATOM   515  C  CG2 . VAL   A 1 66  ? 29.752 1.279   -8.754  1.00 34.08 ? 140 VAL   A CG2 1 
ATOM   516  N  N   . TYR   A 1 67  ? 26.380 0.843   -10.866 1.00 27.48 ? 141 TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 67  ? 25.105 0.219   -10.536 1.00 30.13 ? 141 TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 67  ? 24.724 -0.919  -11.491 1.00 30.70 ? 141 TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 67  ? 24.341 -2.011  -11.055 1.00 29.57 ? 141 TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 67  ? 24.098 1.362   -10.579 1.00 30.26 ? 141 TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 67  ? 22.661 0.986   -10.257 1.00 31.53 ? 141 TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 67  ? 22.346 0.087   -9.236  1.00 31.37 ? 141 TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 67  ? 21.613 1.522   -10.994 1.00 35.18 ? 141 TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 67  ? 21.039 -0.227  -8.926  1.00 32.10 ? 141 TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 67  ? 20.297 1.204   -10.701 1.00 38.01 ? 141 TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 67  ? 20.014 0.316   -9.678  1.00 37.76 ? 141 TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 67  ? 18.734 -0.015  -9.353  1.00 40.84 ? 141 TYR   A OH  1 
ATOM   528  N  N   . GLU   A 1 68  ? 24.809 -0.646  -12.809 1.00 36.58 ? 142 GLU   A N   1 
ATOM   529  C  CA  . GLU   A 1 68  ? 24.604 -1.684  -13.811 1.00 36.92 ? 142 GLU   A CA  1 
ATOM   530  C  C   . GLU   A 1 68  ? 25.545 -2.864  -13.596 1.00 34.54 ? 142 GLU   A C   1 
ATOM   531  O  O   . GLU   A 1 68  ? 25.087 -4.008  -13.560 1.00 35.64 ? 142 GLU   A O   1 
ATOM   532  C  CB  . GLU   A 1 68  ? 24.759 -1.155  -15.241 1.00 39.30 ? 142 GLU   A CB  1 
ATOM   533  C  CG  . GLU   A 1 68  ? 23.697 -0.125  -15.615 1.00 38.38 ? 142 GLU   A CG  1 
ATOM   534  C  CD  . GLU   A 1 68  ? 22.245 -0.530  -15.393 1.00 41.86 ? 142 GLU   A CD  1 
ATOM   535  O  OE1 . GLU   A 1 68  ? 21.929 -1.716  -15.617 1.00 44.16 ? 142 GLU   A OE1 1 
ATOM   536  O  OE2 . GLU   A 1 68  ? 21.420 0.348   -15.027 1.00 49.50 ? 142 GLU   A OE2 1 
ATOM   537  N  N   . GLU   A 1 69  ? 26.851 -2.594  -13.404 1.00 32.09 ? 143 GLU   A N   1 
ATOM   538  C  CA  . GLU   A 1 69  ? 27.801 -3.646  -13.095 1.00 34.78 ? 143 GLU   A CA  1 
ATOM   539  C  C   . GLU   A 1 69  ? 27.318 -4.478  -11.907 1.00 32.66 ? 143 GLU   A C   1 
ATOM   540  O  O   . GLU   A 1 69  ? 27.443 -5.697  -11.894 1.00 31.96 ? 143 GLU   A O   1 
ATOM   541  C  CB  . GLU   A 1 69  ? 29.196 -3.056  -12.865 1.00 33.80 ? 143 GLU   A CB  1 
ATOM   542  C  CG  . GLU   A 1 69  ? 30.287 -4.091  -12.635 1.00 34.09 ? 143 GLU   A CG  1 
ATOM   543  C  CD  . GLU   A 1 69  ? 31.694 -3.516  -12.576 1.00 34.56 ? 143 GLU   A CD  1 
ATOM   544  O  OE1 . GLU   A 1 69  ? 31.862 -2.275  -12.646 1.00 42.80 ? 143 GLU   A OE1 1 
ATOM   545  O  OE2 . GLU   A 1 69  ? 32.644 -4.312  -12.480 1.00 43.31 ? 143 GLU   A OE2 1 
ATOM   546  N  N   . LEU   A 1 70  ? 26.848 -3.817  -10.833 1.00 31.73 ? 144 LEU   A N   1 
ATOM   547  C  CA  . LEU   A 1 70  ? 26.421 -4.577  -9.663  1.00 31.47 ? 144 LEU   A CA  1 
ATOM   548  C  C   . LEU   A 1 70  ? 25.303 -5.572  -10.013 1.00 28.67 ? 144 LEU   A C   1 
ATOM   549  O  O   . LEU   A 1 70  ? 25.337 -6.730  -9.582  1.00 28.66 ? 144 LEU   A O   1 
ATOM   550  C  CB  . LEU   A 1 70  ? 25.987 -3.619  -8.544  1.00 29.77 ? 144 LEU   A CB  1 
ATOM   551  C  CG  . LEU   A 1 70  ? 25.432 -4.281  -7.275  1.00 29.08 ? 144 LEU   A CG  1 
ATOM   552  C  CD1 . LEU   A 1 70  ? 26.440 -5.134  -6.602  1.00 29.32 ? 144 LEU   A CD1 1 
ATOM   553  C  CD2 . LEU   A 1 70  ? 24.905 -3.198  -6.329  1.00 27.98 ? 144 LEU   A CD2 1 
ATOM   554  N  N   . LYS   A 1 71  ? 24.269 -5.067  -10.694 1.00 31.97 ? 145 LYS   A N   1 
ATOM   555  C  CA  . LYS   A 1 71  ? 23.151 -5.896  -11.133 1.00 34.58 ? 145 LYS   A CA  1 
ATOM   556  C  C   . LYS   A 1 71  ? 23.652 -7.090  -11.954 1.00 33.88 ? 145 LYS   A C   1 
ATOM   557  O  O   . LYS   A 1 71  ? 23.247 -8.228  -11.717 1.00 32.86 ? 145 LYS   A O   1 
ATOM   558  C  CB  . LYS   A 1 71  ? 22.169 -5.042  -11.933 1.00 35.79 ? 145 LYS   A CB  1 
ATOM   559  C  CG  . LYS   A 1 71  ? 21.246 -4.207  -11.067 1.00 40.30 ? 145 LYS   A CG  1 
ATOM   560  C  CD  . LYS   A 1 71  ? 20.146 -3.505  -11.843 1.00 45.21 ? 145 LYS   A CD  1 
ATOM   561  C  CE  . LYS   A 1 71  ? 20.642 -2.275  -12.527 1.00 50.50 ? 145 LYS   A CE  1 
ATOM   562  N  NZ  . LYS   A 1 71  ? 19.638 -1.659  -13.406 1.00 54.16 ? 145 LYS   A NZ  1 
ATOM   563  N  N   . GLU   A 1 72  ? 24.613 -6.835  -12.838 1.00 33.54 ? 146 GLU   A N   1 
ATOM   564  C  CA  . GLU   A 1 72  ? 25.083 -7.887  -13.733 1.00 37.06 ? 146 GLU   A CA  1 
ATOM   565  C  C   . GLU   A 1 72  ? 25.777 -8.959  -12.903 1.00 38.85 ? 146 GLU   A C   1 
ATOM   566  O  O   . GLU   A 1 72  ? 25.528 -10.143 -13.070 1.00 36.60 ? 146 GLU   A O   1 
ATOM   567  C  CB  . GLU   A 1 72  ? 25.916 -7.281  -14.865 1.00 40.97 ? 146 GLU   A CB  1 
ATOM   568  C  CG  . GLU   A 1 72  ? 25.099 -6.390  -15.802 1.00 44.72 ? 146 GLU   A CG  1 
ATOM   569  C  CD  . GLU   A 1 72  ? 24.110 -7.101  -16.726 1.00 52.06 ? 146 GLU   A CD  1 
ATOM   570  O  OE1 . GLU   A 1 72  ? 24.135 -8.353  -16.821 1.00 52.40 ? 146 GLU   A OE1 1 
ATOM   571  O  OE2 . GLU   A 1 72  ? 23.301 -6.385  -17.362 1.00 58.02 ? 146 GLU   A OE2 1 
ATOM   572  N  N   . LEU   A 1 73  ? 26.585 -8.548  -11.915 1.00 32.71 ? 147 LEU   A N   1 
ATOM   573  C  CA  . LEU   A 1 73  ? 27.266 -9.507  -11.068 1.00 30.84 ? 147 LEU   A CA  1 
ATOM   574  C  C   . LEU   A 1 73  ? 26.282 -10.362 -10.265 1.00 35.64 ? 147 LEU   A C   1 
ATOM   575  O  O   . LEU   A 1 73  ? 26.505 -11.560 -10.058 1.00 33.28 ? 147 LEU   A O   1 
ATOM   576  C  CB  . LEU   A 1 73  ? 28.212 -8.751  -10.130 1.00 32.47 ? 147 LEU   A CB  1 
ATOM   577  C  CG  . LEU   A 1 73  ? 29.574 -8.357  -10.701 1.00 36.39 ? 147 LEU   A CG  1 
ATOM   578  C  CD1 . LEU   A 1 73  ? 30.347 -7.499  -9.715  1.00 37.92 ? 147 LEU   A CD1 1 
ATOM   579  C  CD2 . LEU   A 1 73  ? 30.350 -9.627  -11.054 1.00 38.13 ? 147 LEU   A CD2 1 
ATOM   580  N  N   . VAL   A 1 74  ? 25.259 -9.711  -9.680  1.00 33.07 ? 148 VAL   A N   1 
ATOM   581  C  CA  . VAL   A 1 74  ? 24.390 -10.382 -8.724  1.00 33.39 ? 148 VAL   A CA  1 
ATOM   582  C  C   . VAL   A 1 74  ? 23.494 -11.386 -9.458  1.00 35.28 ? 148 VAL   A C   1 
ATOM   583  O  O   . VAL   A 1 74  ? 23.065 -12.365 -8.859  1.00 32.53 ? 148 VAL   A O   1 
ATOM   584  C  CB  . VAL   A 1 74  ? 23.599 -9.336  -7.895  1.00 33.35 ? 148 VAL   A CB  1 
ATOM   585  C  CG1 . VAL   A 1 74  ? 22.501 -9.971  -7.044  1.00 35.12 ? 148 VAL   A CG1 1 
ATOM   586  C  CG2 . VAL   A 1 74  ? 24.527 -8.526  -7.004  1.00 35.27 ? 148 VAL   A CG2 1 
ATOM   587  N  N   . LYS   A 1 75  ? 23.297 -11.181 -10.765 1.00 37.38 ? 149 LYS   A N   1 
ATOM   588  C  CA  . LYS   A 1 75  ? 22.646 -12.171 -11.620 1.00 41.94 ? 149 LYS   A CA  1 
ATOM   589  C  C   . LYS   A 1 75  ? 23.282 -13.556 -11.489 1.00 40.96 ? 149 LYS   A C   1 
ATOM   590  O  O   . LYS   A 1 75  ? 22.599 -14.559 -11.721 1.00 40.14 ? 149 LYS   A O   1 
ATOM   591  C  CB  . LYS   A 1 75  ? 22.683 -11.780 -13.101 1.00 45.76 ? 149 LYS   A CB  1 
ATOM   592  C  CG  . LYS   A 1 75  ? 21.898 -10.539 -13.469 1.00 50.48 ? 149 LYS   A CG  1 
ATOM   593  C  CD  . LYS   A 1 75  ? 21.558 -10.443 -14.952 1.00 55.75 ? 149 LYS   A CD  1 
ATOM   594  C  CE  . LYS   A 1 75  ? 21.248 -9.046  -15.385 1.00 57.50 ? 149 LYS   A CE  1 
ATOM   595  N  NZ  . LYS   A 1 75  ? 20.261 -8.394  -14.521 1.00 59.67 ? 149 LYS   A NZ  1 
ATOM   596  N  N   . ASN   A 1 76  ? 24.584 -13.616 -11.157 1.00 36.57 ? 150 ASN   A N   1 
ATOM   597  C  CA  . ASN   A 1 76  ? 25.316 -14.874 -11.065 1.00 35.90 ? 150 ASN   A CA  1 
ATOM   598  C  C   . ASN   A 1 76  ? 25.044 -15.629 -9.775  1.00 34.03 ? 150 ASN   A C   1 
ATOM   599  O  O   . ASN   A 1 76  ? 25.635 -16.678 -9.558  1.00 33.91 ? 150 ASN   A O   1 
ATOM   600  C  CB  . ASN   A 1 76  ? 26.832 -14.710 -11.124 1.00 39.96 ? 150 ASN   A CB  1 
ATOM   601  C  CG  . ASN   A 1 76  ? 27.295 -14.193 -12.459 1.00 43.72 ? 150 ASN   A CG  1 
ATOM   602  O  OD1 . ASN   A 1 76  ? 27.750 -13.054 -12.581 1.00 48.67 ? 150 ASN   A OD1 1 
ATOM   603  N  ND2 . ASN   A 1 76  ? 27.165 -15.009 -13.483 1.00 45.97 ? 150 ASN   A ND2 1 
ATOM   604  N  N   . ILE   A 1 77  ? 24.279 -15.023 -8.843  1.00 33.59 ? 151 ILE   A N   1 
ATOM   605  C  CA  . ILE   A 1 77  ? 23.928 -15.714 -7.618  1.00 32.27 ? 151 ILE   A CA  1 
ATOM   606  C  C   . ILE   A 1 77  ? 22.563 -16.353 -7.818  1.00 36.88 ? 151 ILE   A C   1 
ATOM   607  O  O   . ILE   A 1 77  ? 21.568 -15.653 -7.929  1.00 34.93 ? 151 ILE   A O   1 
ATOM   608  C  CB  . ILE   A 1 77  ? 23.888 -14.749 -6.410  1.00 29.32 ? 151 ILE   A CB  1 
ATOM   609  C  CG1 . ILE   A 1 77  ? 25.233 -14.009 -6.185  1.00 30.84 ? 151 ILE   A CG1 1 
ATOM   610  C  CG2 . ILE   A 1 77  ? 23.486 -15.541 -5.170  1.00 29.23 ? 151 ILE   A CG2 1 
ATOM   611  C  CD1 . ILE   A 1 77  ? 25.119 -12.790 -5.270  1.00 29.79 ? 151 ILE   A CD1 1 
ATOM   612  N  N   . LYS   A 1 78  ? 22.514 -17.687 -7.880  1.00 40.75 ? 152 LYS   A N   1 
ATOM   613  C  CA  . LYS   A 1 78  ? 21.263 -18.370 -8.182  1.00 43.78 ? 152 LYS   A CA  1 
ATOM   614  C  C   . LYS   A 1 78  ? 20.289 -18.292 -7.000  1.00 44.59 ? 152 LYS   A C   1 
ATOM   615  O  O   . LYS   A 1 78  ? 20.705 -18.277 -5.838  1.00 46.20 ? 152 LYS   A O   1 
ATOM   616  C  CB  . LYS   A 1 78  ? 21.607 -19.810 -8.595  1.00 45.99 ? 152 LYS   A CB  1 
ATOM   617  C  CG  . LYS   A 1 78  ? 22.330 -19.928 -9.939  1.00 49.14 ? 152 LYS   A CG  1 
ATOM   618  C  CD  . LYS   A 1 78  ? 21.654 -19.184 -11.093 1.00 52.08 ? 152 LYS   A CD  1 
ATOM   619  C  CE  . LYS   A 1 78  ? 22.402 -19.232 -12.403 1.00 51.43 ? 152 LYS   A CE  1 
ATOM   620  N  NZ  . LYS   A 1 78  ? 23.650 -18.453 -12.382 1.00 45.59 ? 152 LYS   A NZ  1 
ATOM   621  N  N   . ASP   A 1 79  ? 18.982 -18.242 -7.324  1.00 43.80 ? 153 ASP   A N   1 
ATOM   622  C  CA  . ASP   A 1 79  ? 17.901 -18.378 -6.352  1.00 43.88 ? 153 ASP   A CA  1 
ATOM   623  C  C   . ASP   A 1 79  ? 17.876 -17.162 -5.427  1.00 42.16 ? 153 ASP   A C   1 
ATOM   624  O  O   . ASP   A 1 79  ? 17.445 -17.260 -4.279  1.00 43.98 ? 153 ASP   A O   1 
ATOM   625  C  CB  . ASP   A 1 79  ? 18.006 -19.662 -5.544  1.00 45.71 ? 153 ASP   A CB  1 
ATOM   626  C  CG  . ASP   A 1 79  ? 17.743 -20.943 -6.324  1.00 51.41 ? 153 ASP   A CG  1 
ATOM   627  O  OD1 . ASP   A 1 79  ? 17.098 -20.857 -7.390  1.00 53.61 ? 153 ASP   A OD1 1 
ATOM   628  O  OD2 . ASP   A 1 79  ? 18.203 -22.008 -5.858  1.00 58.12 ? 153 ASP   A OD2 1 
ATOM   629  N  N   . TYR   A 1 80  ? 18.331 -16.024 -5.961  1.00 39.48 ? 154 TYR   A N   1 
ATOM   630  C  CA  . TYR   A 1 80  ? 18.501 -14.814 -5.171  1.00 34.99 ? 154 TYR   A CA  1 
ATOM   631  C  C   . TYR   A 1 80  ? 17.990 -13.642 -5.977  1.00 34.20 ? 154 TYR   A C   1 
ATOM   632  O  O   . TYR   A 1 80  ? 18.527 -13.339 -7.042  1.00 36.08 ? 154 TYR   A O   1 
ATOM   633  C  CB  . TYR   A 1 80  ? 19.983 -14.659 -4.816  1.00 33.75 ? 154 TYR   A CB  1 
ATOM   634  C  CG  . TYR   A 1 80  ? 20.341 -13.432 -3.975  1.00 34.37 ? 154 TYR   A CG  1 
ATOM   635  C  CD1 . TYR   A 1 80  ? 19.630 -13.103 -2.823  1.00 32.25 ? 154 TYR   A CD1 1 
ATOM   636  C  CD2 . TYR   A 1 80  ? 21.400 -12.603 -4.352  1.00 34.46 ? 154 TYR   A CD2 1 
ATOM   637  C  CE1 . TYR   A 1 80  ? 20.010 -12.014 -2.042  1.00 29.72 ? 154 TYR   A CE1 1 
ATOM   638  C  CE2 . TYR   A 1 80  ? 21.761 -11.493 -3.599  1.00 31.37 ? 154 TYR   A CE2 1 
ATOM   639  C  CZ  . TYR   A 1 80  ? 21.046 -11.196 -2.457  1.00 31.56 ? 154 TYR   A CZ  1 
ATOM   640  O  OH  . TYR   A 1 80  ? 21.403 -10.075 -1.728  1.00 28.09 ? 154 TYR   A OH  1 
ATOM   641  N  N   . LYS   A 1 81  ? 16.944 -12.976 -5.465  1.00 33.98 ? 155 LYS   A N   1 
ATOM   642  C  CA  . LYS   A 1 81  ? 16.335 -11.860 -6.164  1.00 35.86 ? 155 LYS   A CA  1 
ATOM   643  C  C   . LYS   A 1 81  ? 16.201 -10.667 -5.225  1.00 35.60 ? 155 LYS   A C   1 
ATOM   644  O  O   . LYS   A 1 81  ? 15.103 -10.240 -4.849  1.00 36.10 ? 155 LYS   A O   1 
ATOM   645  C  CB  . LYS   A 1 81  ? 14.986 -12.252 -6.775  1.00 41.24 ? 155 LYS   A CB  1 
ATOM   646  C  CG  . LYS   A 1 81  ? 15.061 -13.318 -7.873  1.00 45.41 ? 155 LYS   A CG  1 
ATOM   647  C  CD  . LYS   A 1 81  ? 15.785 -12.855 -9.138  1.00 49.06 ? 155 LYS   A CD  1 
ATOM   648  C  CE  . LYS   A 1 81  ? 15.802 -13.877 -10.235 1.00 51.20 ? 155 LYS   A CE  1 
ATOM   649  N  NZ  . LYS   A 1 81  ? 16.534 -15.093 -9.854  1.00 53.49 ? 155 LYS   A NZ  1 
ATOM   650  N  N   . PRO   A 1 82  ? 17.339 -10.050 -4.863  1.00 30.98 ? 156 PRO   A N   1 
ATOM   651  C  CA  . PRO   A 1 82  ? 17.286 -8.870  -3.993  1.00 30.34 ? 156 PRO   A CA  1 
ATOM   652  C  C   . PRO   A 1 82  ? 16.763 -7.639  -4.714  1.00 29.67 ? 156 PRO   A C   1 
ATOM   653  O  O   . PRO   A 1 82  ? 16.700 -7.571  -5.939  1.00 32.29 ? 156 PRO   A O   1 
ATOM   654  C  CB  . PRO   A 1 82  ? 18.757 -8.724  -3.570  1.00 30.23 ? 156 PRO   A CB  1 
ATOM   655  C  CG  . PRO   A 1 82  ? 19.539 -9.242  -4.764  1.00 30.35 ? 156 PRO   A CG  1 
ATOM   656  C  CD  . PRO   A 1 82  ? 18.719 -10.483 -5.166  1.00 31.03 ? 156 PRO   A CD  1 
ATOM   657  N  N   . ILE   A 1 83  ? 16.399 -6.634  -3.916  1.00 27.72 ? 157 ILE   A N   1 
ATOM   658  C  CA  . ILE   A 1 83  ? 16.143 -5.298  -4.390  1.00 28.03 ? 157 ILE   A CA  1 
ATOM   659  C  C   . ILE   A 1 83  ? 17.487 -4.580  -4.497  1.00 30.52 ? 157 ILE   A C   1 
ATOM   660  O  O   . ILE   A 1 83  ? 18.181 -4.395  -3.479  1.00 28.47 ? 157 ILE   A O   1 
ATOM   661  C  CB  . ILE   A 1 83  ? 15.153 -4.627  -3.417  1.00 31.05 ? 157 ILE   A CB  1 
ATOM   662  C  CG1 . ILE   A 1 83  ? 13.844 -5.457  -3.274  1.00 31.62 ? 157 ILE   A CG1 1 
ATOM   663  C  CG2 . ILE   A 1 83  ? 14.857 -3.180  -3.797  1.00 30.37 ? 157 ILE   A CG2 1 
ATOM   664  C  CD1 . ILE   A 1 83  ? 12.919 -4.975  -2.165  1.00 32.28 ? 157 ILE   A CD1 1 
ATOM   665  N  N   . ILE   A 1 84  ? 17.822 -4.084  -5.686  1.00 30.14 ? 158 ILE   A N   1 
ATOM   666  C  CA  . ILE   A 1 84  ? 19.133 -3.523  -5.977  1.00 28.16 ? 158 ILE   A CA  1 
ATOM   667  C  C   . ILE   A 1 84  ? 18.975 -2.058  -6.341  1.00 31.32 ? 158 ILE   A C   1 
ATOM   668  O  O   . ILE   A 1 84  ? 18.357 -1.708  -7.347  1.00 29.82 ? 158 ILE   A O   1 
ATOM   669  C  CB  . ILE   A 1 84  ? 19.871 -4.328  -7.074  1.00 28.78 ? 158 ILE   A CB  1 
ATOM   670  C  CG1 . ILE   A 1 84  ? 19.853 -5.809  -6.785  1.00 28.03 ? 158 ILE   A CG1 1 
ATOM   671  C  CG2 . ILE   A 1 84  ? 21.305 -3.827  -7.278  1.00 28.76 ? 158 ILE   A CG2 1 
ATOM   672  C  CD1 . ILE   A 1 84  ? 20.581 -6.651  -7.830  1.00 30.17 ? 158 ILE   A CD1 1 
ATOM   673  N  N   . LEU   A 1 85  ? 19.515 -1.188  -5.468  1.00 27.64 ? 159 LEU   A N   1 
ATOM   674  C  CA  . LEU   A 1 85  ? 19.256 0.235   -5.532  1.00 26.71 ? 159 LEU   A CA  1 
ATOM   675  C  C   . LEU   A 1 85  ? 20.556 1.024   -5.701  1.00 23.29 ? 159 LEU   A C   1 
ATOM   676  O  O   . LEU   A 1 85  ? 21.644 0.458   -5.598  1.00 25.16 ? 159 LEU   A O   1 
ATOM   677  C  CB  . LEU   A 1 85  ? 18.528 0.631   -4.243  1.00 27.12 ? 159 LEU   A CB  1 
ATOM   678  C  CG  . LEU   A 1 85  ? 17.288 -0.204  -3.894  1.00 27.73 ? 159 LEU   A CG  1 
ATOM   679  C  CD1 . LEU   A 1 85  ? 16.788 0.101   -2.486  1.00 29.29 ? 159 LEU   A CD1 1 
ATOM   680  C  CD2 . LEU   A 1 85  ? 16.195 0.028   -4.965  1.00 29.80 ? 159 LEU   A CD2 1 
ATOM   681  N  N   . CYS   A 1 86  ? 20.404 2.323   -5.930  1.00 25.76 ? 160 CYS   A N   1 
ATOM   682  C  CA  . CYS   A 1 86  ? 21.543 3.199   -6.142  1.00 27.90 ? 160 CYS   A CA  1 
ATOM   683  C  C   . CYS   A 1 86  ? 21.346 4.570   -5.499  1.00 26.38 ? 160 CYS   A C   1 
ATOM   684  O  O   . CYS   A 1 86  ? 20.240 5.105   -5.402  1.00 26.70 ? 160 CYS   A O   1 
ATOM   685  C  CB  . CYS   A 1 86  ? 21.874 3.218   -7.637  1.00 30.32 ? 160 CYS   A CB  1 
ATOM   686  S  SG  . CYS   A 1 86  ? 23.054 4.498   -8.118  1.00 34.79 ? 160 CYS   A SG  1 
ATOM   687  N  N   . GLY   A 1 87  ? 22.455 5.097   -4.934  1.00 25.44 ? 161 GLY   A N   1 
ATOM   688  C  CA  . GLY   A 1 87  ? 22.575 6.489   -4.530  1.00 25.86 ? 161 GLY   A CA  1 
ATOM   689  C  C   . GLY   A 1 87  ? 21.719 6.861   -3.316  1.00 23.78 ? 161 GLY   A C   1 
ATOM   690  O  O   . GLY   A 1 87  ? 21.228 6.002   -2.578  1.00 23.70 ? 161 GLY   A O   1 
ATOM   691  N  N   . ASP   A 1 88  ? 21.510 8.173   -3.174  1.00 24.42 ? 162 ASP   A N   1 
ATOM   692  C  CA  . ASP   A 1 88  ? 20.694 8.759   -2.124  1.00 26.11 ? 162 ASP   A CA  1 
ATOM   693  C  C   . ASP   A 1 88  ? 19.294 8.138   -2.104  1.00 26.67 ? 162 ASP   A C   1 
ATOM   694  O  O   . ASP   A 1 88  ? 18.763 7.843   -1.043  1.00 26.15 ? 162 ASP   A O   1 
ATOM   695  C  CB  . ASP   A 1 88  ? 20.670 10.273  -2.235  1.00 30.50 ? 162 ASP   A CB  1 
ATOM   696  C  CG  . ASP   A 1 88  ? 21.956 11.019  -1.925  1.00 35.89 ? 162 ASP   A CG  1 
ATOM   697  O  OD1 . ASP   A 1 88  ? 22.819 10.447  -1.221  1.00 37.60 ? 162 ASP   A OD1 1 
ATOM   698  O  OD2 . ASP   A 1 88  ? 22.096 12.173  -2.379  1.00 40.78 ? 162 ASP   A OD2 1 
ATOM   699  N  N   . GLU   A 1 89  ? 18.642 7.973   -3.278  1.00 27.64 ? 163 GLU   A N   1 
ATOM   700  C  CA  . GLU   A 1 89  ? 17.276 7.459   -3.280  1.00 26.11 ? 163 GLU   A CA  1 
ATOM   701  C  C   . GLU   A 1 89  ? 17.234 6.029   -2.753  1.00 24.25 ? 163 GLU   A C   1 
ATOM   702  O  O   . GLU   A 1 89  ? 16.296 5.627   -2.046  1.00 25.57 ? 163 GLU   A O   1 
ATOM   703  C  CB  . GLU   A 1 89  ? 16.632 7.596   -4.674  1.00 29.01 ? 163 GLU   A CB  1 
ATOM   704  C  CG  . GLU   A 1 89  ? 16.278 9.039   -5.013  1.00 37.04 ? 163 GLU   A CG  1 
ATOM   705  C  CD  . GLU   A 1 89  ? 15.445 9.754   -3.955  1.00 45.22 ? 163 GLU   A CD  1 
ATOM   706  O  OE1 . GLU   A 1 89  ? 14.388 9.224   -3.532  1.00 51.71 ? 163 GLU   A OE1 1 
ATOM   707  O  OE2 . GLU   A 1 89  ? 15.861 10.856  -3.535  1.00 53.01 ? 163 GLU   A OE2 1 
ATOM   708  N  N   . GLY   A 1 90  ? 18.249 5.224   -3.104  1.00 23.63 ? 164 GLY   A N   1 
ATOM   709  C  CA  . GLY   A 1 90  ? 18.353 3.865   -2.611  1.00 24.22 ? 164 GLY   A CA  1 
ATOM   710  C  C   . GLY   A 1 90  ? 18.520 3.805   -1.082  1.00 23.31 ? 164 GLY   A C   1 
ATOM   711  O  O   . GLY   A 1 90  ? 17.909 2.987   -0.396  1.00 24.04 ? 164 GLY   A O   1 
ATOM   712  N  N   . MET   A 1 91  ? 19.383 4.673   -0.558  1.00 22.20 ? 165 MET   A N   1 
ATOM   713  C  CA  . MET   A 1 91  ? 19.627 4.752   0.882   1.00 21.80 ? 165 MET   A CA  1 
ATOM   714  C  C   . MET   A 1 91  ? 18.315 5.101   1.591   1.00 22.19 ? 165 MET   A C   1 
ATOM   715  O  O   . MET   A 1 91  ? 17.965 4.486   2.598   1.00 22.38 ? 165 MET   A O   1 
ATOM   716  C  CB  . MET   A 1 91  ? 20.687 5.835   1.086   1.00 21.61 ? 165 MET   A CB  1 
ATOM   717  C  CG  . MET   A 1 91  ? 21.048 6.099   2.563   1.00 22.52 ? 165 MET   A CG  1 
ATOM   718  S  SD  . MET   A 1 91  ? 19.868 7.155   3.417   1.00 24.33 ? 165 MET   A SD  1 
ATOM   719  C  CE  . MET   A 1 91  ? 20.261 8.752   2.707   1.00 26.69 ? 165 MET   A CE  1 
ATOM   720  N  N   . LYS   A 1 92  ? 17.566 6.072   1.041   1.00 21.87 ? 166 LYS   A N   1 
ATOM   721  C  CA  . LYS   A 1 92  ? 16.312 6.493   1.649   1.00 24.31 ? 166 LYS   A CA  1 
ATOM   722  C  C   . LYS   A 1 92  ? 15.282 5.364   1.661   1.00 25.16 ? 166 LYS   A C   1 
ATOM   723  O  O   . LYS   A 1 92  ? 14.534 5.199   2.619   1.00 24.22 ? 166 LYS   A O   1 
ATOM   724  C  CB  . LYS   A 1 92  ? 15.740 7.754   1.001   1.00 25.94 ? 166 LYS   A CB  1 
ATOM   725  C  CG  . LYS   A 1 92  ? 16.617 8.955   1.198   1.00 29.86 ? 166 LYS   A CG  1 
ATOM   726  C  CD  . LYS   A 1 92  ? 16.096 10.200  0.481   1.00 33.28 ? 166 LYS   A CD  1 
ATOM   727  C  CE  . LYS   A 1 92  ? 17.144 11.259  0.516   1.00 39.01 ? 166 LYS   A CE  1 
ATOM   728  N  NZ  . LYS   A 1 92  ? 16.679 12.522  -0.049  1.00 42.61 ? 166 LYS   A NZ  1 
ATOM   729  N  N   . GLU   A 1 93  ? 15.240 4.566   0.584   1.00 25.11 ? 167 GLU   A N   1 
ATOM   730  C  CA  . GLU   A 1 93  ? 14.316 3.456   0.507   1.00 24.99 ? 167 GLU   A CA  1 
ATOM   731  C  C   . GLU   A 1 93  ? 14.632 2.397   1.559   1.00 25.19 ? 167 GLU   A C   1 
ATOM   732  O  O   . GLU   A 1 93  ? 13.737 1.864   2.209   1.00 25.89 ? 167 GLU   A O   1 
ATOM   733  C  CB  . GLU   A 1 93  ? 14.347 2.904   -0.924  1.00 28.16 ? 167 GLU   A CB  1 
ATOM   734  C  CG  . GLU   A 1 93  ? 13.541 1.619   -1.101  1.00 28.09 ? 167 GLU   A CG  1 
ATOM   735  C  CD  . GLU   A 1 93  ? 13.295 1.152   -2.539  1.00 33.42 ? 167 GLU   A CD  1 
ATOM   736  O  OE1 . GLU   A 1 93  ? 13.549 1.940   -3.484  1.00 33.26 ? 167 GLU   A OE1 1 
ATOM   737  O  OE2 . GLU   A 1 93  ? 12.869 -0.017  -2.671  1.00 35.63 ? 167 GLU   A OE2 1 
ATOM   738  N  N   . ILE   A 1 94  ? 15.923 2.073   1.755   1.00 25.06 ? 168 ILE   A N   1 
ATOM   739  C  CA  . ILE   A 1 94  ? 16.308 1.136   2.794   1.00 24.17 ? 168 ILE   A CA  1 
ATOM   740  C  C   . ILE   A 1 94  ? 15.922 1.685   4.174   1.00 22.76 ? 168 ILE   A C   1 
ATOM   741  O  O   . ILE   A 1 94  ? 15.357 0.967   4.983   1.00 23.23 ? 168 ILE   A O   1 
ATOM   742  C  CB  . ILE   A 1 94  ? 17.809 0.789   2.677   1.00 22.89 ? 168 ILE   A CB  1 
ATOM   743  C  CG1 . ILE   A 1 94  ? 18.068 0.037   1.362   1.00 24.77 ? 168 ILE   A CG1 1 
ATOM   744  C  CG2 . ILE   A 1 94  ? 18.289 0.012   3.894   1.00 23.18 ? 168 ILE   A CG2 1 
ATOM   745  C  CD1 . ILE   A 1 94  ? 19.526 -0.043  0.950   1.00 25.97 ? 168 ILE   A CD1 1 
ATOM   746  N  N   . CYS   A 1 95  ? 16.218 2.956   4.435   1.00 22.36 ? 169 CYS   A N   1 
ATOM   747  C  CA  . CYS   A 1 95  ? 15.923 3.501   5.758   1.00 22.14 ? 169 CYS   A CA  1 
ATOM   748  C  C   . CYS   A 1 95  ? 14.426 3.502   6.076   1.00 24.38 ? 169 CYS   A C   1 
ATOM   749  O  O   . CYS   A 1 95  ? 14.036 3.430   7.245   1.00 24.66 ? 169 CYS   A O   1 
ATOM   750  C  CB  . CYS   A 1 95  ? 16.402 4.938   5.917   1.00 22.31 ? 169 CYS   A CB  1 
ATOM   751  S  SG  . CYS   A 1 95  ? 18.201 5.128   5.992   1.00 21.68 ? 169 CYS   A SG  1 
ATOM   752  N  N   . SER   A 1 96  ? 13.568 3.587   5.046   1.00 24.93 ? 170 SER   A N   1 
ATOM   753  C  CA  . SER   A 1 96  ? 12.135 3.597   5.296   1.00 27.91 ? 170 SER   A CA  1 
ATOM   754  C  C   . SER   A 1 96  ? 11.522 2.196   5.291   1.00 28.62 ? 170 SER   A C   1 
ATOM   755  O  O   . SER   A 1 96  ? 10.320 2.042   5.500   1.00 29.62 ? 170 SER   A O   1 
ATOM   756  C  CB  . SER   A 1 96  ? 11.435 4.511   4.323   1.00 30.69 ? 170 SER   A CB  1 
ATOM   757  O  OG  . SER   A 1 96  ? 11.466 3.943   3.040   1.00 34.93 ? 170 SER   A OG  1 
ATOM   758  N  N   . SER   A 1 97  ? 12.324 1.151   5.111   1.00 26.13 ? 171 SER   A N   1 
ATOM   759  C  CA  . SER   A 1 97  ? 11.778 -0.196  5.151   1.00 26.61 ? 171 SER   A CA  1 
ATOM   760  C  C   . SER   A 1 97  ? 11.360 -0.618  6.566   1.00 27.58 ? 171 SER   A C   1 
ATOM   761  O  O   . SER   A 1 97  ? 12.146 -0.577  7.514   1.00 26.51 ? 171 SER   A O   1 
ATOM   762  C  CB  . SER   A 1 97  ? 12.765 -1.194  4.588   1.00 28.83 ? 171 SER   A CB  1 
ATOM   763  O  OG  . SER   A 1 97  ? 12.271 -2.520  4.713   1.00 30.02 ? 171 SER   A OG  1 
ATOM   764  N  N   . ASN   A 1 98  ? 10.136 -1.139  6.723   1.00 28.67 ? 172 ASN   A N   1 
ATOM   765  C  CA  . ASN   A 1 98  ? 9.663  -1.640  7.999   1.00 28.68 ? 172 ASN   A CA  1 
ATOM   766  C  C   . ASN   A 1 98  ? 10.336 -2.960  8.370   1.00 29.12 ? 172 ASN   A C   1 
ATOM   767  O  O   . ASN   A 1 98  ? 10.157 -3.444  9.483   1.00 33.54 ? 172 ASN   A O   1 
ATOM   768  C  CB  . ASN   A 1 98  ? 8.146  -1.778  7.965   1.00 36.07 ? 172 ASN   A CB  1 
ATOM   769  C  CG  . ASN   A 1 98  ? 7.512  -0.421  7.846   1.00 42.72 ? 172 ASN   A CG  1 
ATOM   770  O  OD1 . ASN   A 1 98  ? 6.774  -0.158  6.887   1.00 57.68 ? 172 ASN   A OD1 1 
ATOM   771  N  ND2 . ASN   A 1 98  ? 7.817  0.462   8.788   1.00 45.59 ? 172 ASN   A ND2 1 
ATOM   772  N  N   . SER   A 1 99  ? 11.116 -3.537  7.459   1.00 27.75 ? 173 SER   A N   1 
ATOM   773  C  CA  . SER   A 1 99  ? 11.807 -4.778  7.748   1.00 29.93 ? 173 SER   A CA  1 
ATOM   774  C  C   . SER   A 1 99  ? 13.171 -4.542  8.421   1.00 26.16 ? 173 SER   A C   1 
ATOM   775  O  O   . SER   A 1 99  ? 13.867 -5.523  8.685   1.00 29.38 ? 173 SER   A O   1 
ATOM   776  C  CB  . SER   A 1 99  ? 12.014 -5.583  6.500   1.00 34.39 ? 173 SER   A CB  1 
ATOM   777  O  OG  . SER   A 1 99  ? 12.926 -4.922  5.630   1.00 39.80 ? 173 SER   A OG  1 
ATOM   778  N  N   . ILE   A 1 100 ? 13.579 -3.270  8.587   1.00 23.25 ? 174 ILE   A N   1 
ATOM   779  C  CA  . ILE   A 1 100 ? 14.877 -2.944  9.177   1.00 22.97 ? 174 ILE   A CA  1 
ATOM   780  C  C   . ILE   A 1 100 ? 14.652 -2.246  10.509  1.00 21.74 ? 174 ILE   A C   1 
ATOM   781  O  O   . ILE   A 1 100 ? 13.915 -1.266  10.569  1.00 23.33 ? 174 ILE   A O   1 
ATOM   782  C  CB  . ILE   A 1 100 ? 15.648 -2.067  8.194   1.00 24.24 ? 174 ILE   A CB  1 
ATOM   783  C  CG1 . ILE   A 1 100 ? 15.996 -2.905  6.993   1.00 30.01 ? 174 ILE   A CG1 1 
ATOM   784  C  CG2 . ILE   A 1 100 ? 16.889 -1.431  8.857   1.00 26.65 ? 174 ILE   A CG2 1 
ATOM   785  C  CD1 . ILE   A 1 100 ? 16.606 -2.126  5.868   1.00 30.09 ? 174 ILE   A CD1 1 
ATOM   786  N  N   . ASP   A 1 101 ? 15.316 -2.758  11.542  1.00 21.86 ? 175 ASP   A N   1 
ATOM   787  C  CA  . ASP   A 1 101 ? 15.184 -2.280  12.918  1.00 22.25 ? 175 ASP   A CA  1 
ATOM   788  C  C   . ASP   A 1 101 ? 16.387 -1.399  13.336  1.00 20.29 ? 175 ASP   A C   1 
ATOM   789  O  O   . ASP   A 1 101 ? 16.203 -0.399  14.020  1.00 19.45 ? 175 ASP   A O   1 
ATOM   790  C  CB  . ASP   A 1 101 ? 15.141 -3.482  13.850  1.00 26.51 ? 175 ASP   A CB  1 
ATOM   791  C  CG  . ASP   A 1 101 ? 14.016 -4.491  13.615  1.00 33.29 ? 175 ASP   A CG  1 
ATOM   792  O  OD1 . ASP   A 1 101 ? 12.911 -4.001  13.352  1.00 35.36 ? 175 ASP   A OD1 1 
ATOM   793  O  OD2 . ASP   A 1 101 ? 14.274 -5.732  13.737  1.00 35.35 ? 175 ASP   A OD2 1 
ATOM   794  N  N   . LYS   A 1 102 ? 17.602 -1.793  12.907  1.00 17.98 ? 176 LYS   A N   1 
ATOM   795  C  CA  . LYS   A 1 102 ? 18.858 -1.175  13.349  1.00 18.15 ? 176 LYS   A CA  1 
ATOM   796  C  C   . LYS   A 1 102 ? 19.766 -0.978  12.156  1.00 17.82 ? 176 LYS   A C   1 
ATOM   797  O  O   . LYS   A 1 102 ? 19.810 -1.820  11.244  1.00 20.11 ? 176 LYS   A O   1 
ATOM   798  C  CB  . LYS   A 1 102 ? 19.532 -2.028  14.423  1.00 18.44 ? 176 LYS   A CB  1 
ATOM   799  C  CG  . LYS   A 1 102 ? 18.573 -2.480  15.502  1.00 20.03 ? 176 LYS   A CG  1 
ATOM   800  C  CD  . LYS   A 1 102 ? 19.249 -2.983  16.772  1.00 20.16 ? 176 LYS   A CD  1 
ATOM   801  C  CE  . LYS   A 1 102 ? 18.223 -3.387  17.785  1.00 21.44 ? 176 LYS   A CE  1 
ATOM   802  N  NZ  . LYS   A 1 102 ? 18.789 -3.887  19.053  1.00 22.54 ? 176 LYS   A NZ  1 
ATOM   803  N  N   . ILE   A 1 103 ? 20.453 0.156   12.125  1.00 15.85 ? 177 ILE   A N   1 
ATOM   804  C  CA  . ILE   A 1 103 ? 21.331 0.478   11.024  1.00 16.64 ? 177 ILE   A CA  1 
ATOM   805  C  C   . ILE   A 1 103 ? 22.701 0.805   11.592  1.00 15.14 ? 177 ILE   A C   1 
ATOM   806  O  O   . ILE   A 1 103 ? 22.844 1.753   12.371  1.00 15.83 ? 177 ILE   A O   1 
ATOM   807  C  CB  . ILE   A 1 103 ? 20.775 1.633   10.184  1.00 15.72 ? 177 ILE   A CB  1 
ATOM   808  C  CG1 . ILE   A 1 103 ? 19.342 1.329   9.716   1.00 17.65 ? 177 ILE   A CG1 1 
ATOM   809  C  CG2 . ILE   A 1 103 ? 21.692 1.931   9.019   1.00 17.24 ? 177 ILE   A CG2 1 
ATOM   810  C  CD1 . ILE   A 1 103 ? 18.693 2.412   8.862   1.00 20.51 ? 177 ILE   A CD1 1 
ATOM   811  N  N   . VAL   A 1 104 ? 23.709 0.074   11.160  1.00 15.43 ? 178 VAL   A N   1 
ATOM   812  C  CA  . VAL   A 1 104 ? 25.092 0.367   11.475  1.00 15.10 ? 178 VAL   A CA  1 
ATOM   813  C  C   . VAL   A 1 104 ? 25.625 1.362   10.450  1.00 14.97 ? 178 VAL   A C   1 
ATOM   814  O  O   . VAL   A 1 104 ? 25.656 1.065   9.243   1.00 16.69 ? 178 VAL   A O   1 
ATOM   815  C  CB  . VAL   A 1 104 ? 25.962 -0.901  11.468  1.00 15.85 ? 178 VAL   A CB  1 
ATOM   816  C  CG1 . VAL   A 1 104 ? 27.419 -0.536  11.757  1.00 16.70 ? 178 VAL   A CG1 1 
ATOM   817  C  CG2 . VAL   A 1 104 ? 25.483 -1.964  12.454  1.00 17.70 ? 178 VAL   A CG2 1 
ATOM   818  N  N   . ILE   A 1 105 ? 26.055 2.522   10.923  1.00 14.55 ? 179 ILE   A N   1 
ATOM   819  C  CA  . ILE   A 1 105 ? 26.605 3.568   10.081  1.00 15.56 ? 179 ILE   A CA  1 
ATOM   820  C  C   . ILE   A 1 105 ? 28.120 3.507   10.165  1.00 14.40 ? 179 ILE   A C   1 
ATOM   821  O  O   . ILE   A 1 105 ? 28.727 4.017   11.122  1.00 15.23 ? 179 ILE   A O   1 
ATOM   822  C  CB  . ILE   A 1 105 ? 26.101 4.980   10.429  1.00 17.34 ? 179 ILE   A CB  1 
ATOM   823  C  CG1 . ILE   A 1 105 ? 24.635 5.101   10.612  1.00 22.35 ? 179 ILE   A CG1 1 
ATOM   824  C  CG2 . ILE   A 1 105 ? 26.667 5.973   9.401   1.00 17.83 ? 179 ILE   A CG2 1 
ATOM   825  C  CD1 . ILE   A 1 105 ? 23.851 5.056   9.329   1.00 22.37 ? 179 ILE   A CD1 1 
ATOM   826  N  N   . GLY   A 1 106 ? 28.710 2.856   9.164   1.00 14.57 ? 180 GLY   A N   1 
ATOM   827  C  CA  . GLY   A 1 106 ? 30.134 2.729   8.975   1.00 13.99 ? 180 GLY   A CA  1 
ATOM   828  C  C   . GLY   A 1 106 ? 30.667 3.426   7.731   1.00 15.13 ? 180 GLY   A C   1 
ATOM   829  O  O   . GLY   A 1 106 ? 31.699 3.040   7.189   1.00 15.76 ? 180 GLY   A O   1 
ATOM   830  N  N   . ILE   A 1 107 ? 29.963 4.480   7.329   1.00 15.08 ? 181 ILE   A N   1 
ATOM   831  C  CA  . ILE   A 1 107 ? 30.382 5.368   6.263   1.00 14.95 ? 181 ILE   A CA  1 
ATOM   832  C  C   . ILE   A 1 107 ? 31.308 6.403   6.884   1.00 14.84 ? 181 ILE   A C   1 
ATOM   833  O  O   . ILE   A 1 107 ? 31.006 6.880   7.967   1.00 16.36 ? 181 ILE   A O   1 
ATOM   834  C  CB  . ILE   A 1 107 ? 29.151 5.979   5.580   1.00 16.36 ? 181 ILE   A CB  1 
ATOM   835  C  CG1 . ILE   A 1 107 ? 28.332 4.858   4.927   1.00 16.38 ? 181 ILE   A CG1 1 
ATOM   836  C  CG2 . ILE   A 1 107 ? 29.552 7.083   4.589   1.00 17.49 ? 181 ILE   A CG2 1 
ATOM   837  C  CD1 . ILE   A 1 107 ? 27.025 5.361   4.360   1.00 17.72 ? 181 ILE   A CD1 1 
ATOM   838  N  N   . ASP   A 1 108 ? 32.405 6.767   6.222   1.00 16.03 ? 182 ASP   A N   1 
ATOM   839  C  CA  . ASP   A 1 108 ? 33.352 7.732   6.745   1.00 17.10 ? 182 ASP   A CA  1 
ATOM   840  C  C   . ASP   A 1 108 ? 32.948 9.166   6.446   1.00 16.90 ? 182 ASP   A C   1 
ATOM   841  O  O   . ASP   A 1 108 ? 32.190 9.414   5.519   1.00 17.46 ? 182 ASP   A O   1 
ATOM   842  C  CB  . ASP   A 1 108 ? 34.738 7.447   6.170   1.00 17.83 ? 182 ASP   A CB  1 
ATOM   843  C  CG  . ASP   A 1 108 ? 34.847 7.655   4.678   1.00 22.33 ? 182 ASP   A CG  1 
ATOM   844  O  OD1 . ASP   A 1 108 ? 34.199 6.895   3.966   1.00 21.25 ? 182 ASP   A OD1 1 
ATOM   845  O  OD2 . ASP   A 1 108 ? 35.403 8.726   4.255   1.00 24.68 ? 182 ASP   A OD2 1 
ATOM   846  N  N   . SER   A 1 109 ? 33.550 10.086  7.189   1.00 16.70 ? 183 SER   A N   1 
ATOM   847  C  CA  . SER   A 1 109 ? 33.583 11.508  6.865   1.00 17.61 ? 183 SER   A CA  1 
ATOM   848  C  C   . SER   A 1 109 ? 32.201 12.148  7.017   1.00 15.91 ? 183 SER   A C   1 
ATOM   849  O  O   . SER   A 1 109 ? 31.223 11.571  7.473   1.00 15.56 ? 183 SER   A O   1 
ATOM   850  C  CB  . SER   A 1 109 ? 34.211 11.768  5.531   1.00 18.60 ? 183 SER   A CB  1 
ATOM   851  O  OG  . SER   A 1 109 ? 35.508 11.190  5.471   1.00 20.88 ? 183 SER   A OG  1 
ATOM   852  N  N   . PHE   A 1 110 ? 32.125 13.446  6.671   1.00 17.57 ? 184 PHE   A N   1 
ATOM   853  C  CA  . PHE   A 1 110 ? 30.889 14.204  6.733   1.00 17.05 ? 184 PHE   A CA  1 
ATOM   854  C  C   . PHE   A 1 110 ? 29.767 13.510  5.954   1.00 16.79 ? 184 PHE   A C   1 
ATOM   855  O  O   . PHE   A 1 110 ? 28.599 13.573  6.345   1.00 17.45 ? 184 PHE   A O   1 
ATOM   856  C  CB  . PHE   A 1 110 ? 31.158 15.624  6.215   1.00 19.60 ? 184 PHE   A CB  1 
ATOM   857  C  CG  . PHE   A 1 110 ? 29.926 16.520  6.172   1.00 18.97 ? 184 PHE   A CG  1 
ATOM   858  C  CD1 . PHE   A 1 110 ? 29.523 17.208  7.277   1.00 18.99 ? 184 PHE   A CD1 1 
ATOM   859  C  CD2 . PHE   A 1 110 ? 29.139 16.593  5.026   1.00 21.04 ? 184 PHE   A CD2 1 
ATOM   860  C  CE1 . PHE   A 1 110 ? 28.419 18.043  7.242   1.00 19.59 ? 184 PHE   A CE1 1 
ATOM   861  C  CE2 . PHE   A 1 110 ? 28.020 17.417  5.001   1.00 21.19 ? 184 PHE   A CE2 1 
ATOM   862  C  CZ  . PHE   A 1 110 ? 27.696 18.156  6.085   1.00 20.74 ? 184 PHE   A CZ  1 
ATOM   863  N  N   . GLN   A 1 111 ? 30.123 12.812  4.882   1.00 17.53 ? 185 GLN   A N   1 
ATOM   864  C  CA  . GLN   A 1 111 ? 29.180 12.052  4.079   1.00 18.19 ? 185 GLN   A CA  1 
ATOM   865  C  C   . GLN   A 1 111 ? 28.291 11.144  4.908   1.00 18.36 ? 185 GLN   A C   1 
ATOM   866  O  O   . GLN   A 1 111 ? 27.129 10.940  4.562   1.00 19.79 ? 185 GLN   A O   1 
ATOM   867  C  CB  . GLN   A 1 111 ? 29.877 11.209  3.002   1.00 21.34 ? 185 GLN   A CB  1 
ATOM   868  C  CG  . GLN   A 1 111 ? 28.926 10.378  2.138   1.00 21.76 ? 185 GLN   A CG  1 
ATOM   869  C  CD  . GLN   A 1 111 ? 27.999 11.218  1.286   1.00 22.71 ? 185 GLN   A CD  1 
ATOM   870  O  OE1 . GLN   A 1 111 ? 28.296 12.375  1.012   1.00 26.72 ? 185 GLN   A OE1 1 
ATOM   871  N  NE2 . GLN   A 1 111 ? 26.828 10.671  0.985   1.00 23.45 ? 185 GLN   A NE2 1 
ATOM   872  N  N   . GLY   A 1 112 ? 28.794 10.608  6.037   1.00 16.97 ? 186 GLY   A N   1 
ATOM   873  C  CA  . GLY   A 1 112 ? 27.970 9.727   6.841   1.00 16.57 ? 186 GLY   A CA  1 
ATOM   874  C  C   . GLY   A 1 112 ? 26.788 10.421  7.510   1.00 15.66 ? 186 GLY   A C   1 
ATOM   875  O  O   . GLY   A 1 112 ? 25.855 9.744   7.940   1.00 16.92 ? 186 GLY   A O   1 
ATOM   876  N  N   . LEU   A 1 113 ? 26.789 11.760  7.552   1.00 15.71 ? 187 LEU   A N   1 
ATOM   877  C  CA  . LEU   A 1 113 ? 25.669 12.492  8.129   1.00 16.35 ? 187 LEU   A CA  1 
ATOM   878  C  C   . LEU   A 1 113 ? 24.345 12.215  7.403   1.00 16.43 ? 187 LEU   A C   1 
ATOM   879  O  O   . LEU   A 1 113 ? 23.286 12.143  8.005   1.00 16.80 ? 187 LEU   A O   1 
ATOM   880  C  CB  . LEU   A 1 113 ? 25.996 13.979  8.130   1.00 17.20 ? 187 LEU   A CB  1 
ATOM   881  C  CG  . LEU   A 1 113 ? 24.866 14.903  8.597   1.00 17.56 ? 187 LEU   A CG  1 
ATOM   882  C  CD1 . LEU   A 1 113 ? 24.459 14.632  10.017  1.00 16.32 ? 187 LEU   A CD1 1 
ATOM   883  C  CD2 . LEU   A 1 113 ? 25.386 16.327  8.454   1.00 19.13 ? 187 LEU   A CD2 1 
ATOM   884  N  N   . TYR   A 1 114 ? 24.406 12.058  6.069   1.00 16.85 ? 188 TYR   A N   1 
ATOM   885  C  CA  . TYR   A 1 114 ? 23.162 11.952  5.304   1.00 18.76 ? 188 TYR   A CA  1 
ATOM   886  C  C   . TYR   A 1 114 ? 22.334 10.727  5.688   1.00 18.40 ? 188 TYR   A C   1 
ATOM   887  O  O   . TYR   A 1 114 ? 21.155 10.822  5.982   1.00 18.92 ? 188 TYR   A O   1 
ATOM   888  C  CB  . TYR   A 1 114 ? 23.510 11.945  3.815   1.00 21.66 ? 188 TYR   A CB  1 
ATOM   889  C  CG  . TYR   A 1 114 ? 24.104 13.243  3.326   1.00 27.78 ? 188 TYR   A CG  1 
ATOM   890  C  CD1 . TYR   A 1 114 ? 23.318 14.392  3.201   1.00 37.47 ? 188 TYR   A CD1 1 
ATOM   891  C  CD2 . TYR   A 1 114 ? 25.426 13.307  2.913   1.00 34.52 ? 188 TYR   A CD2 1 
ATOM   892  C  CE1 . TYR   A 1 114 ? 23.867 15.584  2.739   1.00 40.90 ? 188 TYR   A CE1 1 
ATOM   893  C  CE2 . TYR   A 1 114 ? 25.981 14.482  2.433   1.00 33.34 ? 188 TYR   A CE2 1 
ATOM   894  C  CZ  . TYR   A 1 114 ? 25.201 15.621  2.366   1.00 40.19 ? 188 TYR   A CZ  1 
ATOM   895  O  OH  . TYR   A 1 114 ? 25.813 16.738  1.891   1.00 49.35 ? 188 TYR   A OH  1 
ATOM   896  N  N   . SER   A 1 115 ? 22.952 9.557   5.680   1.00 17.36 ? 189 SER   A N   1 
ATOM   897  C  CA  . SER   A 1 115 ? 22.264 8.345   6.103   1.00 18.38 ? 189 SER   A CA  1 
ATOM   898  C  C   . SER   A 1 115 ? 21.906 8.382   7.594   1.00 17.48 ? 189 SER   A C   1 
ATOM   899  O  O   . SER   A 1 115 ? 20.877 7.861   8.002   1.00 18.85 ? 189 SER   A O   1 
ATOM   900  C  CB  . SER   A 1 115 ? 23.062 7.118   5.748   1.00 19.20 ? 189 SER   A CB  1 
ATOM   901  O  OG  . SER   A 1 115 ? 24.329 7.042   6.421   1.00 18.86 ? 189 SER   A OG  1 
ATOM   902  N  N   . THR   A 1 116 ? 22.763 8.987   8.435   1.00 16.72 ? 190 THR   A N   1 
ATOM   903  C  CA  . THR   A 1 116 ? 22.460 9.126   9.855   1.00 15.75 ? 190 THR   A CA  1 
ATOM   904  C  C   . THR   A 1 116 ? 21.119 9.851   10.031  1.00 16.48 ? 190 THR   A C   1 
ATOM   905  O  O   . THR   A 1 116 ? 20.248 9.460   10.823  1.00 16.15 ? 190 THR   A O   1 
ATOM   906  C  CB  . THR   A 1 116 ? 23.611 9.837   10.579  1.00 15.73 ? 190 THR   A CB  1 
ATOM   907  O  OG1 . THR   A 1 116 ? 24.792 9.059   10.446  1.00 16.16 ? 190 THR   A OG1 1 
ATOM   908  C  CG2 . THR   A 1 116 ? 23.306 10.012  12.058  1.00 15.80 ? 190 THR   A CG2 1 
ATOM   909  N  N   . MET   A 1 117 ? 20.999 11.006  9.341   1.00 16.83 ? 191 MET   A N   1 
ATOM   910  C  CA  . MET   A 1 117 ? 19.807 11.813  9.414   1.00 18.29 ? 191 MET   A CA  1 
ATOM   911  C  C   . MET   A 1 117 ? 18.597 11.011  8.957   1.00 18.11 ? 191 MET   A C   1 
ATOM   912  O  O   . MET   A 1 117 ? 17.567 11.050  9.618   1.00 18.44 ? 191 MET   A O   1 
ATOM   913  C  CB  . MET   A 1 117 ? 20.025 13.096  8.593   1.00 21.68 ? 191 MET   A CB  1 
ATOM   914  C  CG  . MET   A 1 117 ? 18.803 13.996  8.344   1.00 26.27 ? 191 MET   A CG  1 
ATOM   915  S  SD  . MET   A 1 117 ? 19.150 15.320  7.151   1.00 31.23 ? 191 MET   A SD  1 
ATOM   916  C  CE  . MET   A 1 117 ? 20.945 15.181  7.173   1.00 27.41 ? 191 MET   A CE  1 
ATOM   917  N  N   . TYR   A 1 118 ? 18.697 10.316  7.826   1.00 19.49 ? 192 TYR   A N   1 
ATOM   918  C  CA  . TYR   A 1 118 ? 17.530 9.620   7.302   1.00 19.96 ? 192 TYR   A CA  1 
ATOM   919  C  C   . TYR   A 1 118 ? 17.185 8.418   8.164   1.00 19.97 ? 192 TYR   A C   1 
ATOM   920  O  O   . TYR   A 1 118 ? 16.022 8.078   8.320   1.00 21.25 ? 192 TYR   A O   1 
ATOM   921  C  CB  . TYR   A 1 118 ? 17.692 9.229   5.830   1.00 22.62 ? 192 TYR   A CB  1 
ATOM   922  C  CG  . TYR   A 1 118 ? 17.235 10.373  4.941   1.00 28.27 ? 192 TYR   A CG  1 
ATOM   923  C  CD1 . TYR   A 1 118 ? 15.889 10.510  4.658   1.00 29.60 ? 192 TYR   A CD1 1 
ATOM   924  C  CD2 . TYR   A 1 118 ? 18.091 11.385  4.523   1.00 30.89 ? 192 TYR   A CD2 1 
ATOM   925  C  CE1 . TYR   A 1 118 ? 15.410 11.562  3.891   1.00 34.74 ? 192 TYR   A CE1 1 
ATOM   926  C  CE2 . TYR   A 1 118 ? 17.624 12.463  3.781   1.00 37.94 ? 192 TYR   A CE2 1 
ATOM   927  C  CZ  . TYR   A 1 118 ? 16.280 12.545  3.456   1.00 40.06 ? 192 TYR   A CZ  1 
ATOM   928  O  OH  . TYR   A 1 118 ? 15.807 13.598  2.709   1.00 43.11 ? 192 TYR   A OH  1 
ATOM   929  N  N   . ALA   A 1 119 ? 18.173 7.805   8.821   1.00 19.08 ? 193 ALA   A N   1 
ATOM   930  C  CA  . ALA   A 1 119 ? 17.862 6.701   9.709   1.00 19.64 ? 193 ALA   A CA  1 
ATOM   931  C  C   . ALA   A 1 119 ? 17.069 7.224   10.911  1.00 18.81 ? 193 ALA   A C   1 
ATOM   932  O  O   . ALA   A 1 119 ? 16.132 6.596   11.383  1.00 20.62 ? 193 ALA   A O   1 
ATOM   933  C  CB  . ALA   A 1 119 ? 19.140 6.003   10.101  1.00 18.80 ? 193 ALA   A CB  1 
ATOM   934  N  N   . ILE   A 1 120 ? 17.462 8.379   11.463  1.00 17.39 ? 194 ILE   A N   1 
ATOM   935  C  CA  . ILE   A 1 120 ? 16.719 8.990   12.557  1.00 17.57 ? 194 ILE   A CA  1 
ATOM   936  C  C   . ILE   A 1 120 ? 15.295 9.403   12.141  1.00 18.04 ? 194 ILE   A C   1 
ATOM   937  O  O   . ILE   A 1 120 ? 14.339 9.179   12.866  1.00 19.11 ? 194 ILE   A O   1 
ATOM   938  C  CB  . ILE   A 1 120 ? 17.517 10.200  13.077  1.00 17.46 ? 194 ILE   A CB  1 
ATOM   939  C  CG1 . ILE   A 1 120 ? 18.846 9.720   13.738  1.00 16.39 ? 194 ILE   A CG1 1 
ATOM   940  C  CG2 . ILE   A 1 120 ? 16.674 10.997  14.049  1.00 17.46 ? 194 ILE   A CG2 1 
ATOM   941  C  CD1 . ILE   A 1 120 ? 19.789 10.835  14.110  1.00 17.48 ? 194 ILE   A CD1 1 
ATOM   942  N  N   . MET   A 1 121 ? 15.186 9.991   10.956  1.00 19.39 ? 195 MET   A N   1 
ATOM   943  C  CA  . MET   A 1 121 ? 13.881 10.422  10.428  1.00 20.31 ? 195 MET   A CA  1 
ATOM   944  C  C   . MET   A 1 121 ? 12.931 9.243   10.275  1.00 21.14 ? 195 MET   A C   1 
ATOM   945  O  O   . MET   A 1 121 ? 11.722 9.477   10.275  1.00 24.32 ? 195 MET   A O   1 
ATOM   946  C  CB  . MET   A 1 121 ? 14.095 11.120  9.085   1.00 21.24 ? 195 MET   A CB  1 
ATOM   947  C  CG  . MET   A 1 121 ? 14.722 12.484  9.212   1.00 24.06 ? 195 MET   A CG  1 
ATOM   948  S  SD  . MET   A 1 121 ? 15.243 13.114  7.597   1.00 30.12 ? 195 MET   A SD  1 
ATOM   949  C  CE  . MET   A 1 121 ? 13.636 13.227  6.789   1.00 31.16 ? 195 MET   A CE  1 
ATOM   950  N  N   . ASN   A 1 122 ? 13.447 8.027   10.108  1.00 20.92 ? 196 ASN   A N   1 
ATOM   951  C  CA  . ASN   A 1 122 ? 12.659 6.813   10.020  1.00 20.60 ? 196 ASN   A CA  1 
ATOM   952  C  C   . ASN   A 1 122 ? 12.557 6.073   11.342  1.00 21.71 ? 196 ASN   A C   1 
ATOM   953  O  O   . ASN   A 1 122 ? 12.184 4.905   11.349  1.00 22.43 ? 196 ASN   A O   1 
ATOM   954  C  CB  . ASN   A 1 122 ? 13.190 5.933   8.904   1.00 22.49 ? 196 ASN   A CB  1 
ATOM   955  C  CG  . ASN   A 1 122 ? 12.788 6.488   7.563   1.00 23.96 ? 196 ASN   A CG  1 
ATOM   956  O  OD1 . ASN   A 1 122 ? 11.633 6.293   7.144   1.00 25.15 ? 196 ASN   A OD1 1 
ATOM   957  N  ND2 . ASN   A 1 122 ? 13.664 7.217   6.897   1.00 22.74 ? 196 ASN   A ND2 1 
ATOM   958  N  N   . ASN   A 1 123 ? 12.963 6.724   12.454  1.00 21.41 ? 197 ASN   A N   1 
ATOM   959  C  CA  . ASN   A 1 123 ? 12.694 6.212   13.786  1.00 20.38 ? 197 ASN   A CA  1 
ATOM   960  C  C   . ASN   A 1 123 ? 13.442 4.907   14.030  1.00 20.91 ? 197 ASN   A C   1 
ATOM   961  O  O   . ASN   A 1 123 ? 12.994 4.072   14.821  1.00 23.22 ? 197 ASN   A O   1 
ATOM   962  C  CB  . ASN   A 1 123 ? 11.187 6.135   14.053  1.00 23.22 ? 197 ASN   A CB  1 
ATOM   963  C  CG  . ASN   A 1 123 ? 10.513 7.445   13.735  1.00 26.53 ? 197 ASN   A CG  1 
ATOM   964  O  OD1 . ASN   A 1 123 ? 10.909 8.482   14.260  1.00 28.46 ? 197 ASN   A OD1 1 
ATOM   965  N  ND2 . ASN   A 1 123 ? 9.579  7.437   12.796  1.00 30.89 ? 197 ASN   A ND2 1 
ATOM   966  N  N   . LYS   A 1 124 ? 14.668 4.787   13.471  1.00 19.22 ? 198 LYS   A N   1 
ATOM   967  C  CA  . LYS   A 1 124 ? 15.455 3.589   13.642  1.00 19.10 ? 198 LYS   A CA  1 
ATOM   968  C  C   . LYS   A 1 124 ? 16.445 3.698   14.794  1.00 17.82 ? 198 LYS   A C   1 
ATOM   969  O  O   . LYS   A 1 124 ? 16.657 4.791   15.334  1.00 19.06 ? 198 LYS   A O   1 
ATOM   970  C  CB  . LYS   A 1 124 ? 16.238 3.230   12.384  1.00 20.73 ? 198 LYS   A CB  1 
ATOM   971  C  CG  . LYS   A 1 124 ? 15.351 3.132   11.131  1.00 22.20 ? 198 LYS   A CG  1 
ATOM   972  C  CD  . LYS   A 1 124 ? 14.285 2.042   11.243  1.00 23.00 ? 198 LYS   A CD  1 
ATOM   973  C  CE  . LYS   A 1 124 ? 13.540 1.874   9.942   1.00 26.30 ? 198 LYS   A CE  1 
ATOM   974  N  NZ  . LYS   A 1 124 ? 12.478 0.883   10.113  1.00 27.24 ? 198 LYS   A NZ  1 
ATOM   975  N  N   . ILE   A 1 125 ? 16.932 2.539   15.231  1.00 18.13 ? 199 ILE   A N   1 
ATOM   976  C  CA  . ILE   A 1 125 ? 18.106 2.471   16.099  1.00 17.40 ? 199 ILE   A CA  1 
ATOM   977  C  C   . ILE   A 1 125 ? 19.334 2.605   15.215  1.00 16.76 ? 199 ILE   A C   1 
ATOM   978  O  O   . ILE   A 1 125 ? 19.519 1.831   14.279  1.00 17.17 ? 199 ILE   A O   1 
ATOM   979  C  CB  . ILE   A 1 125 ? 18.137 1.188   16.939  1.00 20.27 ? 199 ILE   A CB  1 
ATOM   980  C  CG1 . ILE   A 1 125 ? 16.896 1.136   17.832  1.00 25.00 ? 199 ILE   A CG1 1 
ATOM   981  C  CG2 . ILE   A 1 125 ? 19.438 1.080   17.731  1.00 21.74 ? 199 ILE   A CG2 1 
ATOM   982  C  CD1 . ILE   A 1 125 ? 16.782 -0.076  18.720  1.00 29.60 ? 199 ILE   A CD1 1 
ATOM   983  N  N   . VAL   A 1 126 ? 20.147 3.633   15.481  1.00 15.45 ? 200 VAL   A N   1 
ATOM   984  C  CA  . VAL   A 1 126 ? 21.294 3.980   14.652  1.00 16.03 ? 200 VAL   A CA  1 
ATOM   985  C  C   . VAL   A 1 126 ? 22.555 3.658   15.461  1.00 15.09 ? 200 VAL   A C   1 
ATOM   986  O  O   . VAL   A 1 126 ? 22.864 4.339   16.456  1.00 15.14 ? 200 VAL   A O   1 
ATOM   987  C  CB  . VAL   A 1 126 ? 21.217 5.466   14.255  1.00 16.09 ? 200 VAL   A CB  1 
ATOM   988  C  CG1 . VAL   A 1 126 ? 22.311 5.813   13.274  1.00 17.45 ? 200 VAL   A CG1 1 
ATOM   989  C  CG2 . VAL   A 1 126 ? 19.832 5.828   13.683  1.00 19.02 ? 200 VAL   A CG2 1 
ATOM   990  N  N   . ALA   A 1 127 ? 23.206 2.584   15.052  1.00 14.01 ? 201 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 127 ? 24.456 2.124   15.660  1.00 13.76 ? 201 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 127 ? 25.561 2.884   14.938  1.00 12.54 ? 201 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 127 ? 26.007 2.541   13.831  1.00 14.23 ? 201 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 127 ? 24.558 0.628   15.527  1.00 13.76 ? 201 ALA   A CB  1 
ATOM   995  N  N   . LEU   A 1 128 ? 25.923 4.020   15.530  1.00 12.66 ? 202 LEU   A N   1 
ATOM   996  C  CA  . LEU   A 1 128 ? 26.641 5.070   14.847  1.00 13.48 ? 202 LEU   A CA  1 
ATOM   997  C  C   . LEU   A 1 128 ? 28.127 4.997   15.146  1.00 13.28 ? 202 LEU   A C   1 
ATOM   998  O  O   . LEU   A 1 128 ? 28.534 5.337   16.248  1.00 13.37 ? 202 LEU   A O   1 
ATOM   999  C  CB  . LEU   A 1 128 ? 26.091 6.422   15.241  1.00 14.22 ? 202 LEU   A CB  1 
ATOM   1000 C  CG  . LEU   A 1 128 ? 26.643 7.652   14.520  1.00 14.91 ? 202 LEU   A CG  1 
ATOM   1001 C  CD1 . LEU   A 1 128 ? 26.538 7.533   13.018  1.00 16.08 ? 202 LEU   A CD1 1 
ATOM   1002 C  CD2 . LEU   A 1 128 ? 25.888 8.889   14.989  1.00 16.84 ? 202 LEU   A CD2 1 
ATOM   1003 N  N   . ALA   A 1 129 ? 28.930 4.598   14.183  1.00 12.88 ? 203 ALA   A N   1 
ATOM   1004 C  CA  . ALA   A 1 129 ? 30.379 4.651   14.292  1.00 12.74 ? 203 ALA   A CA  1 
ATOM   1005 C  C   . ALA   A 1 129 ? 30.916 5.981   13.809  1.00 14.00 ? 203 ALA   A C   1 
ATOM   1006 O  O   . ALA   A 1 129 ? 31.926 6.477   14.269  1.00 13.63 ? 203 ALA   A O   1 
ATOM   1007 C  CB  . ALA   A 1 129 ? 31.044 3.528   13.529  1.00 14.25 ? 203 ALA   A CB  1 
ATOM   1008 N  N   . ASN   A 1 130 ? 30.252 6.548   12.787  1.00 14.74 ? 204 ASN   A N   1 
ATOM   1009 C  CA  . ASN   A 1 130 ? 30.683 7.797   12.173  1.00 14.83 ? 204 ASN   A CA  1 
ATOM   1010 C  C   . ASN   A 1 130 ? 30.590 8.915   13.182  1.00 15.55 ? 204 ASN   A C   1 
ATOM   1011 O  O   . ASN   A 1 130 ? 29.533 9.204   13.697  1.00 18.62 ? 204 ASN   A O   1 
ATOM   1012 C  CB  . ASN   A 1 130 ? 29.816 8.066   10.944  1.00 14.66 ? 204 ASN   A CB  1 
ATOM   1013 C  CG  . ASN   A 1 130 ? 30.119 9.399   10.324  1.00 14.96 ? 204 ASN   A CG  1 
ATOM   1014 O  OD1 . ASN   A 1 130 ? 29.705 10.444  10.859  1.00 18.17 ? 204 ASN   A OD1 1 
ATOM   1015 N  ND2 . ASN   A 1 130 ? 30.885 9.417   9.279   1.00 15.76 ? 204 ASN   A ND2 1 
ATOM   1016 N  N   . LYS   A 1 131 ? 31.683 9.566   13.475  1.00 13.72 ? 205 LYS   A N   1 
ATOM   1017 C  CA  . LYS   A 1 131 ? 31.729 10.637  14.453  1.00 13.90 ? 205 LYS   A CA  1 
ATOM   1018 C  C   . LYS   A 1 131 ? 31.680 12.008  13.773  1.00 13.10 ? 205 LYS   A C   1 
ATOM   1019 O  O   . LYS   A 1 131 ? 31.277 12.962  14.433  1.00 13.55 ? 205 LYS   A O   1 
ATOM   1020 C  CB  . LYS   A 1 131 ? 32.988 10.581  15.318  1.00 13.29 ? 205 LYS   A CB  1 
ATOM   1021 C  CG  . LYS   A 1 131 ? 34.298 10.777  14.652  1.00 13.48 ? 205 LYS   A CG  1 
ATOM   1022 C  CD  . LYS   A 1 131 ? 35.499 10.220  15.446  1.00 13.14 ? 205 LYS   A CD  1 
ATOM   1023 C  CE  . LYS   A 1 131 ? 35.600 8.752   15.277  1.00 13.15 ? 205 LYS   A CE  1 
ATOM   1024 N  NZ  . LYS   A 1 131 ? 36.610 8.095   16.140  1.00 12.93 ? 205 LYS   A NZ  1 
ATOM   1025 N  N   . GLU   A 1 132 ? 32.072 12.109  12.517  1.00 13.16 ? 206 GLU   A N   1 
ATOM   1026 C  CA  . GLU   A 1 132 ? 32.085 13.392  11.829  1.00 14.09 ? 206 GLU   A CA  1 
ATOM   1027 C  C   . GLU   A 1 132 ? 30.671 13.969  11.747  1.00 13.97 ? 206 GLU   A C   1 
ATOM   1028 O  O   . GLU   A 1 132 ? 30.476 15.192  11.829  1.00 14.55 ? 206 GLU   A O   1 
ATOM   1029 C  CB  . GLU   A 1 132 ? 32.676 13.271  10.434  1.00 13.87 ? 206 GLU   A CB  1 
ATOM   1030 C  CG  . GLU   A 1 132 ? 34.166 12.907  10.381  1.00 15.44 ? 206 GLU   A CG  1 
ATOM   1031 C  CD  . GLU   A 1 132 ? 34.575 11.450  10.405  1.00 15.20 ? 206 GLU   A CD  1 
ATOM   1032 O  OE1 . GLU   A 1 132 ? 33.754 10.587  10.756  1.00 16.73 ? 206 GLU   A OE1 1 
ATOM   1033 O  OE2 . GLU   A 1 132 ? 35.734 11.234  10.016  1.00 17.08 ? 206 GLU   A OE2 1 
ATOM   1034 N  N   . SER   A 1 133 ? 29.673 13.110  11.642  1.00 13.57 ? 207 SER   A N   1 
ATOM   1035 C  CA  . SER   A 1 133 ? 28.282 13.547  11.658  1.00 14.08 ? 207 SER   A CA  1 
ATOM   1036 C  C   . SER   A 1 133 ? 27.953 14.299  12.936  1.00 13.84 ? 207 SER   A C   1 
ATOM   1037 O  O   . SER   A 1 133 ? 27.280 15.358  12.922  1.00 14.52 ? 207 SER   A O   1 
ATOM   1038 C  CB  . SER   A 1 133 ? 27.361 12.386  11.469  1.00 15.53 ? 207 SER   A CB  1 
ATOM   1039 O  OG  . SER   A 1 133 ? 27.569 11.395  12.481  1.00 17.00 ? 207 SER   A OG  1 
ATOM   1040 N  N   . ILE   A 1 134 ? 28.298 13.723  14.105  1.00 13.61 ? 208 ILE   A N   1 
ATOM   1041 C  CA  . ILE   A 1 134 ? 27.997 14.315  15.386  1.00 13.28 ? 208 ILE   A CA  1 
ATOM   1042 C  C   . ILE   A 1 134 ? 28.792 15.596  15.563  1.00 13.47 ? 208 ILE   A C   1 
ATOM   1043 O  O   . ILE   A 1 134 ? 28.255 16.593  16.034  1.00 14.18 ? 208 ILE   A O   1 
ATOM   1044 C  CB  . ILE   A 1 134 ? 28.329 13.287  16.490  1.00 14.52 ? 208 ILE   A CB  1 
ATOM   1045 C  CG1 . ILE   A 1 134 ? 27.525 11.986  16.308  1.00 17.17 ? 208 ILE   A CG1 1 
ATOM   1046 C  CG2 . ILE   A 1 134 ? 28.120 13.944  17.865  1.00 14.44 ? 208 ILE   A CG2 1 
ATOM   1047 C  CD1 . ILE   A 1 134 ? 28.026 10.823  17.163  1.00 19.53 ? 208 ILE   A CD1 1 
ATOM   1048 N  N   . VAL   A 1 135 ? 30.071 15.618  15.196  1.00 12.78 ? 209 VAL   A N   1 
ATOM   1049 C  CA  . VAL   A 1 135 ? 30.869 16.830  15.337  1.00 12.59 ? 209 VAL   A CA  1 
ATOM   1050 C  C   . VAL   A 1 135 ? 30.293 17.959  14.501  1.00 13.91 ? 209 VAL   A C   1 
ATOM   1051 O  O   . VAL   A 1 135 ? 30.242 19.096  14.978  1.00 14.81 ? 209 VAL   A O   1 
ATOM   1052 C  CB  . VAL   A 1 135 ? 32.332 16.539  14.984  1.00 12.66 ? 209 VAL   A CB  1 
ATOM   1053 C  CG1 . VAL   A 1 135 ? 33.175 17.804  14.915  1.00 13.03 ? 209 VAL   A CG1 1 
ATOM   1054 C  CG2 . VAL   A 1 135 ? 32.955 15.539  15.961  1.00 13.45 ? 209 VAL   A CG2 1 
ATOM   1055 N  N   . SER   A 1 136 ? 29.935 17.664  13.272  1.00 13.14 ? 210 SER   A N   1 
ATOM   1056 C  CA  . SER   A 1 136 ? 29.545 18.689  12.294  1.00 14.40 ? 210 SER   A CA  1 
ATOM   1057 C  C   . SER   A 1 136 ? 28.131 19.149  12.526  1.00 14.69 ? 210 SER   A C   1 
ATOM   1058 O  O   . SER   A 1 136 ? 27.779 20.269  12.083  1.00 15.89 ? 210 SER   A O   1 
ATOM   1059 C  CB  . SER   A 1 136 ? 29.693 18.152  10.951  1.00 15.43 ? 210 SER   A CB  1 
ATOM   1060 O  OG  . SER   A 1 136 ? 31.037 17.842  10.631  1.00 22.42 ? 210 SER   A OG  1 
ATOM   1061 N  N   . ALA   A 1 137 ? 27.267 18.332  13.104  1.00 13.97 ? 211 ALA   A N   1 
ATOM   1062 C  CA  . ALA   A 1 137 ? 25.839 18.583  13.076  1.00 14.64 ? 211 ALA   A CA  1 
ATOM   1063 C  C   . ALA   A 1 137 ? 25.166 18.198  14.378  1.00 14.67 ? 211 ALA   A C   1 
ATOM   1064 O  O   . ALA   A 1 137 ? 23.986 17.879  14.416  1.00 15.50 ? 211 ALA   A O   1 
ATOM   1065 C  CB  . ALA   A 1 137 ? 25.200 17.899  11.923  1.00 15.07 ? 211 ALA   A CB  1 
ATOM   1066 N  N   . GLY   A 1 138 ? 25.883 18.250  15.491  1.00 16.62 ? 212 GLY   A N   1 
ATOM   1067 C  CA  . GLY   A 1 138 ? 25.360 17.791  16.769  1.00 16.45 ? 212 GLY   A CA  1 
ATOM   1068 C  C   . GLY   A 1 138 ? 24.044 18.444  17.174  1.00 16.97 ? 212 GLY   A C   1 
ATOM   1069 O  O   . GLY   A 1 138 ? 23.150 17.722  17.608  1.00 17.34 ? 212 GLY   A O   1 
ATOM   1070 N  N   . PHE   A 1 139 ? 23.987 19.771  17.110  1.00 18.13 ? 213 PHE   A N   1 
ATOM   1071 C  CA  . PHE   A 1 139 ? 22.780 20.473  17.530  1.00 19.24 ? 213 PHE   A CA  1 
ATOM   1072 C  C   . PHE   A 1 139 ? 21.609 20.119  16.606  1.00 17.93 ? 213 PHE   A C   1 
ATOM   1073 O  O   . PHE   A 1 139 ? 20.493 19.880  17.077  1.00 18.60 ? 213 PHE   A O   1 
ATOM   1074 C  CB  . PHE   A 1 139 ? 22.985 21.991  17.634  1.00 20.83 ? 213 PHE   A CB  1 
ATOM   1075 C  CG  . PHE   A 1 139 ? 21.712 22.793  17.901  1.00 24.11 ? 213 PHE   A CG  1 
ATOM   1076 C  CD1 . PHE   A 1 139 ? 21.180 22.914  19.187  1.00 26.60 ? 213 PHE   A CD1 1 
ATOM   1077 C  CD2 . PHE   A 1 139 ? 21.046 23.398  16.834  1.00 27.06 ? 213 PHE   A CD2 1 
ATOM   1078 C  CE1 . PHE   A 1 139 ? 20.018 23.680  19.401  1.00 26.93 ? 213 PHE   A CE1 1 
ATOM   1079 C  CE2 . PHE   A 1 139 ? 19.892 24.154  17.040  1.00 27.72 ? 213 PHE   A CE2 1 
ATOM   1080 C  CZ  . PHE   A 1 139 ? 19.366 24.266  18.307  1.00 26.68 ? 213 PHE   A CZ  1 
ATOM   1081 N  N   . PHE   A 1 140 ? 21.842 20.032  15.316  1.00 17.44 ? 214 PHE   A N   1 
ATOM   1082 C  CA  . PHE   A 1 140 ? 20.869 19.555  14.356  1.00 17.04 ? 214 PHE   A CA  1 
ATOM   1083 C  C   . PHE   A 1 140 ? 20.351 18.162  14.712  1.00 17.76 ? 214 PHE   A C   1 
ATOM   1084 O  O   . PHE   A 1 140 ? 19.147 17.886  14.655  1.00 17.66 ? 214 PHE   A O   1 
ATOM   1085 C  CB  . PHE   A 1 140 ? 21.489 19.631  12.956  1.00 18.38 ? 214 PHE   A CB  1 
ATOM   1086 C  CG  . PHE   A 1 140 ? 20.653 18.986  11.881  1.00 20.68 ? 214 PHE   A CG  1 
ATOM   1087 C  CD1 . PHE   A 1 140 ? 19.642 19.685  11.234  1.00 25.64 ? 214 PHE   A CD1 1 
ATOM   1088 C  CD2 . PHE   A 1 140 ? 20.844 17.648  11.550  1.00 25.14 ? 214 PHE   A CD2 1 
ATOM   1089 C  CE1 . PHE   A 1 140 ? 18.872 19.068  10.244  1.00 25.74 ? 214 PHE   A CE1 1 
ATOM   1090 C  CE2 . PHE   A 1 140 ? 20.070 17.030  10.585  1.00 26.53 ? 214 PHE   A CE2 1 
ATOM   1091 C  CZ  . PHE   A 1 140 ? 19.085 17.748  9.927   1.00 26.14 ? 214 PHE   A CZ  1 
ATOM   1092 N  N   . LEU   A 1 141 ? 21.264 17.220  14.962  1.00 17.71 ? 215 LEU   A N   1 
ATOM   1093 C  CA  . LEU   A 1 141 ? 20.850 15.867  15.284  1.00 16.30 ? 215 LEU   A CA  1 
ATOM   1094 C  C   . LEU   A 1 141 ? 20.031 15.827  16.561  1.00 15.92 ? 215 LEU   A C   1 
ATOM   1095 O  O   . LEU   A 1 141 ? 19.068 15.042  16.698  1.00 16.56 ? 215 LEU   A O   1 
ATOM   1096 C  CB  . LEU   A 1 141 ? 22.077 14.959  15.419  1.00 15.82 ? 215 LEU   A CB  1 
ATOM   1097 C  CG  . LEU   A 1 141 ? 22.788 14.692  14.097  1.00 17.10 ? 215 LEU   A CG  1 
ATOM   1098 C  CD1 . LEU   A 1 141 ? 24.073 13.940  14.367  1.00 18.76 ? 215 LEU   A CD1 1 
ATOM   1099 C  CD2 . LEU   A 1 141 ? 21.962 13.967  13.077  1.00 18.01 ? 215 LEU   A CD2 1 
ATOM   1100 N  N   . LYS   A 1 142 ? 20.393 16.633  17.538  1.00 16.07 ? 216 LYS   A N   1 
ATOM   1101 C  CA  . LYS   A 1 142 ? 19.631 16.722  18.774  1.00 16.60 ? 216 LYS   A CA  1 
ATOM   1102 C  C   . LYS   A 1 142 ? 18.177 17.159  18.502  1.00 19.02 ? 216 LYS   A C   1 
ATOM   1103 O  O   . LYS   A 1 142 ? 17.228 16.547  19.025  1.00 18.74 ? 216 LYS   A O   1 
ATOM   1104 C  CB  . LYS   A 1 142 ? 20.291 17.674  19.768  1.00 18.21 ? 216 LYS   A CB  1 
ATOM   1105 C  CG  . LYS   A 1 142 ? 19.597 17.769  21.125  1.00 19.71 ? 216 LYS   A CG  1 
ATOM   1106 C  CD  . LYS   A 1 142 ? 20.189 18.822  22.047  1.00 25.10 ? 216 LYS   A CD  1 
ATOM   1107 C  CE  . LYS   A 1 142 ? 19.693 20.194  21.670  1.00 28.87 ? 216 LYS   A CE  1 
ATOM   1108 N  NZ  . LYS   A 1 142 ? 20.298 21.149  22.590  1.00 32.65 ? 216 LYS   A NZ  1 
ATOM   1109 N  N   . LYS   A 1 143 ? 18.029 18.166  17.643  1.00 17.81 ? 217 LYS   A N   1 
ATOM   1110 C  CA  . LYS   A 1 143 ? 16.690 18.638  17.289  1.00 20.35 ? 217 LYS   A CA  1 
ATOM   1111 C  C   . LYS   A 1 143 ? 15.905 17.533  16.594  1.00 19.40 ? 217 LYS   A C   1 
ATOM   1112 O  O   . LYS   A 1 143 ? 14.709 17.330  16.872  1.00 20.13 ? 217 LYS   A O   1 
ATOM   1113 C  CB  . LYS   A 1 143 ? 16.856 19.911  16.449  1.00 23.94 ? 217 LYS   A CB  1 
ATOM   1114 C  CG  . LYS   A 1 143 ? 17.359 21.127  17.253  1.00 30.31 ? 217 LYS   A CG  1 
ATOM   1115 C  CD  . LYS   A 1 143 ? 16.491 21.702  18.370  1.00 35.46 ? 217 LYS   A CD  1 
ATOM   1116 C  CE  . LYS   A 1 143 ? 15.405 22.548  17.787  1.00 40.94 ? 217 LYS   A CE  1 
ATOM   1117 N  NZ  . LYS   A 1 143 ? 14.660 23.185  18.875  1.00 44.66 ? 217 LYS   A NZ  1 
ATOM   1118 N  N   . LEU   A 1 144 ? 16.537 16.820  15.677  1.00 18.65 ? 218 LEU   A N   1 
ATOM   1119 C  CA  . LEU   A 1 144 ? 15.913 15.735  14.957  1.00 19.58 ? 218 LEU   A CA  1 
ATOM   1120 C  C   . LEU   A 1 144 ? 15.478 14.639  15.932  1.00 18.62 ? 218 LEU   A C   1 
ATOM   1121 O  O   . LEU   A 1 144 ? 14.403 14.050  15.811  1.00 19.40 ? 218 LEU   A O   1 
ATOM   1122 C  CB  . LEU   A 1 144 ? 16.862 15.126  13.932  1.00 23.60 ? 218 LEU   A CB  1 
ATOM   1123 C  CG  . LEU   A 1 144 ? 16.794 15.446  12.452  1.00 29.25 ? 218 LEU   A CG  1 
ATOM   1124 C  CD1 . LEU   A 1 144 ? 17.549 14.262  11.831  1.00 26.55 ? 218 LEU   A CD1 1 
ATOM   1125 C  CD2 . LEU   A 1 144 ? 15.422 15.581  11.877  1.00 25.29 ? 218 LEU   A CD2 1 
ATOM   1126 N  N   . LEU   A 1 145 ? 16.377 14.252  16.863  1.00 18.19 ? 219 LEU   A N   1 
ATOM   1127 C  CA  . LEU   A 1 145 ? 16.071 13.242  17.865  1.00 17.94 ? 219 LEU   A CA  1 
ATOM   1128 C  C   . LEU   A 1 145 ? 14.958 13.684  18.818  1.00 18.01 ? 219 LEU   A C   1 
ATOM   1129 O  O   . LEU   A 1 145 ? 14.240 12.830  19.354  1.00 17.88 ? 219 LEU   A O   1 
ATOM   1130 C  CB  . LEU   A 1 145 ? 17.349 12.838  18.628  1.00 16.22 ? 219 LEU   A CB  1 
ATOM   1131 C  CG  . LEU   A 1 145 ? 18.336 11.974  17.835  1.00 15.96 ? 219 LEU   A CG  1 
ATOM   1132 C  CD1 . LEU   A 1 145 ? 19.734 12.102  18.488  1.00 17.23 ? 219 LEU   A CD1 1 
ATOM   1133 C  CD2 . LEU   A 1 145 ? 17.849 10.517  17.811  1.00 17.28 ? 219 LEU   A CD2 1 
ATOM   1134 N  N   . ASN   A 1 146 ? 14.843 14.990  19.065  1.00 18.40 ? 220 ASN   A N   1 
ATOM   1135 C  CA  . ASN   A 1 146 ? 13.728 15.461  19.868  1.00 19.75 ? 220 ASN   A CA  1 
ATOM   1136 C  C   . ASN   A 1 146 ? 12.391 15.177  19.175  1.00 20.76 ? 220 ASN   A C   1 
ATOM   1137 O  O   . ASN   A 1 146 ? 11.428 14.905  19.904  1.00 25.92 ? 220 ASN   A O   1 
ATOM   1138 C  CB  . ASN   A 1 146 ? 13.846 16.949  20.135  1.00 20.79 ? 220 ASN   A CB  1 
ATOM   1139 C  CG  . ASN   A 1 146 ? 14.925 17.363  21.107  1.00 22.01 ? 220 ASN   A CG  1 
ATOM   1140 O  OD1 . ASN   A 1 146 ? 15.504 16.553  21.829  1.00 22.20 ? 220 ASN   A OD1 1 
ATOM   1141 N  ND2 . ASN   A 1 146 ? 15.235 18.643  21.122  1.00 23.48 ? 220 ASN   A ND2 1 
ATOM   1142 N  N   . ILE   A 1 147 ? 12.322 15.299  17.851  1.00 20.10 ? 221 ILE   A N   1 
ATOM   1143 C  CA  . ILE   A 1 147 ? 11.107 15.111  17.061  1.00 22.16 ? 221 ILE   A CA  1 
ATOM   1144 C  C   . ILE   A 1 147 ? 10.821 13.621  16.913  1.00 22.99 ? 221 ILE   A C   1 
ATOM   1145 O  O   . ILE   A 1 147 ? 9.663  13.205  17.039  1.00 25.02 ? 221 ILE   A O   1 
ATOM   1146 C  CB  . ILE   A 1 147 ? 11.259 15.805  15.695  1.00 26.28 ? 221 ILE   A CB  1 
ATOM   1147 C  CG1 . ILE   A 1 147 ? 11.305 17.332  15.872  1.00 31.91 ? 221 ILE   A CG1 1 
ATOM   1148 C  CG2 . ILE   A 1 147 ? 10.203 15.360  14.665  1.00 28.12 ? 221 ILE   A CG2 1 
ATOM   1149 C  CD1 . ILE   A 1 147 ? 11.674 18.056  14.590  1.00 36.26 ? 221 ILE   A CD1 1 
ATOM   1150 N  N   . HIS   A 1 148 ? 11.855 12.810  16.617  1.00 20.36 ? 222 HIS   A N   1 
ATOM   1151 C  CA  . HIS   A 1 148 ? 11.697 11.397  16.290  1.00 20.79 ? 222 HIS   A CA  1 
ATOM   1152 C  C   . HIS   A 1 148 ? 11.907 10.585  17.564  1.00 23.83 ? 222 HIS   A C   1 
ATOM   1153 O  O   . HIS   A 1 148 ? 13.015 10.130  17.880  1.00 21.30 ? 222 HIS   A O   1 
ATOM   1154 C  CB  . HIS   A 1 148 ? 12.631 11.016  15.143  1.00 20.95 ? 222 HIS   A CB  1 
ATOM   1155 C  CG  . HIS   A 1 148 ? 12.286 11.746  13.888  1.00 20.44 ? 222 HIS   A CG  1 
ATOM   1156 N  ND1 . HIS   A 1 148 ? 11.276 11.285  13.062  1.00 24.79 ? 222 HIS   A ND1 1 
ATOM   1157 C  CD2 . HIS   A 1 148 ? 12.709 12.910  13.351  1.00 21.21 ? 222 HIS   A CD2 1 
ATOM   1158 C  CE1 . HIS   A 1 148 ? 11.122 12.156  12.063  1.00 23.06 ? 222 HIS   A CE1 1 
ATOM   1159 N  NE2 . HIS   A 1 148 ? 11.984 13.128  12.184  1.00 23.57 ? 222 HIS   A NE2 1 
ATOM   1160 N  N   . LYS   A 1 149 ? 10.834 10.439  18.331  1.00 22.99 ? 223 LYS   A N   1 
ATOM   1161 C  CA  . LYS   A 1 149 ? 10.892 9.944   19.696  1.00 25.23 ? 223 LYS   A CA  1 
ATOM   1162 C  C   . LYS   A 1 149 ? 11.531 8.560   19.755  1.00 22.61 ? 223 LYS   A C   1 
ATOM   1163 O  O   . LYS   A 1 149 ? 12.329 8.298   20.672  1.00 22.80 ? 223 LYS   A O   1 
ATOM   1164 C  CB  . LYS   A 1 149 ? 9.489  9.834   20.309  1.00 30.16 ? 223 LYS   A CB  1 
ATOM   1165 C  CG  . LYS   A 1 149 ? 8.688  11.108  20.430  1.00 38.72 ? 223 LYS   A CG  1 
ATOM   1166 C  CD  . LYS   A 1 149 ? 9.356  12.280  21.132  1.00 44.65 ? 223 LYS   A CD  1 
ATOM   1167 C  CE  . LYS   A 1 149 ? 8.286  13.255  21.550  1.00 48.85 ? 223 LYS   A CE  1 
ATOM   1168 N  NZ  . LYS   A 1 149 ? 8.821  14.616  21.653  1.00 52.01 ? 223 LYS   A NZ  1 
ATOM   1169 N  N   . ASN   A 1 150 ? 11.235 7.682   18.793  1.00 22.81 ? 224 ASN   A N   1 
ATOM   1170 C  CA  . ASN   A 1 150 ? 11.681 6.298   18.875  1.00 23.41 ? 224 ASN   A CA  1 
ATOM   1171 C  C   . ASN   A 1 150 ? 13.046 6.106   18.206  1.00 21.59 ? 224 ASN   A C   1 
ATOM   1172 O  O   . ASN   A 1 150 ? 13.612 5.020   18.273  1.00 23.64 ? 224 ASN   A O   1 
ATOM   1173 C  CB  . ASN   A 1 150 ? 10.670 5.318   18.282  1.00 27.24 ? 224 ASN   A CB  1 
ATOM   1174 C  CG  . ASN   A 1 150 ? 9.367  5.330   19.047  1.00 31.11 ? 224 ASN   A CG  1 
ATOM   1175 O  OD1 . ASN   A 1 150 ? 8.292  5.287   18.436  1.00 38.88 ? 224 ASN   A OD1 1 
ATOM   1176 N  ND2 . ASN   A 1 150 ? 9.426  5.389   20.359  1.00 32.24 ? 224 ASN   A ND2 1 
ATOM   1177 N  N   . ALA   A 1 151 ? 13.560 7.127   17.523  1.00 20.33 ? 225 ALA   A N   1 
ATOM   1178 C  CA  . ALA   A 1 151 ? 14.924 7.059   17.023  1.00 18.96 ? 225 ALA   A CA  1 
ATOM   1179 C  C   . ALA   A 1 151 ? 15.908 7.143   18.179  1.00 17.48 ? 225 ALA   A C   1 
ATOM   1180 O  O   . ALA   A 1 151 ? 15.686 7.875   19.143  1.00 17.18 ? 225 ALA   A O   1 
ATOM   1181 C  CB  . ALA   A 1 151 ? 15.215 8.173   16.063  1.00 19.01 ? 225 ALA   A CB  1 
ATOM   1182 N  N   . LYS   A 1 152 ? 16.995 6.394   18.056  1.00 16.25 ? 226 LYS   A N   1 
ATOM   1183 C  CA  . LYS   A 1 152 ? 18.055 6.442   19.063  1.00 16.91 ? 226 LYS   A CA  1 
ATOM   1184 C  C   . LYS   A 1 152 ? 19.387 6.298   18.378  1.00 18.30 ? 226 LYS   A C   1 
ATOM   1185 O  O   . LYS   A 1 152 ? 19.524 5.439   17.522  1.00 19.51 ? 226 LYS   A O   1 
ATOM   1186 C  CB  . LYS   A 1 152 ? 17.915 5.301   20.082  1.00 18.63 ? 226 LYS   A CB  1 
ATOM   1187 C  CG  . LYS   A 1 152 ? 16.684 5.326   20.979  1.00 23.22 ? 226 LYS   A CG  1 
ATOM   1188 C  CD  . LYS   A 1 152 ? 16.631 4.055   21.830  1.00 27.85 ? 226 LYS   A CD  1 
ATOM   1189 C  CE  . LYS   A 1 152 ? 15.651 4.176   22.934  1.00 34.55 ? 226 LYS   A CE  1 
ATOM   1190 N  NZ  . LYS   A 1 152 ? 14.315 4.157   22.352  1.00 39.98 ? 226 LYS   A NZ  1 
ATOM   1191 N  N   . ILE   A 1 153 ? 20.366 7.103   18.802  1.00 15.43 ? 227 ILE   A N   1 
ATOM   1192 C  CA  . ILE   A 1 153 ? 21.763 6.831   18.499  1.00 15.37 ? 227 ILE   A CA  1 
ATOM   1193 C  C   . ILE   A 1 153 ? 22.350 5.982   19.613  1.00 15.32 ? 227 ILE   A C   1 
ATOM   1194 O  O   . ILE   A 1 153 ? 22.310 6.373   20.788  1.00 16.21 ? 227 ILE   A O   1 
ATOM   1195 C  CB  . ILE   A 1 153 ? 22.546 8.137   18.326  1.00 15.62 ? 227 ILE   A CB  1 
ATOM   1196 C  CG1 . ILE   A 1 153 ? 22.102 8.859   17.092  1.00 17.49 ? 227 ILE   A CG1 1 
ATOM   1197 C  CG2 . ILE   A 1 153 ? 24.050 7.840   18.330  1.00 16.10 ? 227 ILE   A CG2 1 
ATOM   1198 C  CD1 . ILE   A 1 153 ? 22.668 10.270  16.918  1.00 19.48 ? 227 ILE   A CD1 1 
ATOM   1199 N  N   . ILE   A 1 154 ? 22.932 4.850   19.247  1.00 14.35 ? 228 ILE   A N   1 
ATOM   1200 C  CA  . ILE   A 1 154 ? 23.678 4.019   20.172  1.00 14.79 ? 228 ILE   A CA  1 
ATOM   1201 C  C   . ILE   A 1 154 ? 25.122 4.073   19.695  1.00 13.66 ? 228 ILE   A C   1 
ATOM   1202 O  O   . ILE   A 1 154 ? 25.427 3.701   18.552  1.00 14.49 ? 228 ILE   A O   1 
ATOM   1203 C  CB  . ILE   A 1 154 ? 23.175 2.569   20.237  1.00 16.52 ? 228 ILE   A CB  1 
ATOM   1204 C  CG1 . ILE   A 1 154 ? 21.647 2.447   20.448  1.00 18.27 ? 228 ILE   A CG1 1 
ATOM   1205 C  CG2 . ILE   A 1 154 ? 23.936 1.796   21.292  1.00 16.64 ? 228 ILE   A CG2 1 
ATOM   1206 C  CD1 . ILE   A 1 154 ? 21.163 2.981   21.761  1.00 18.57 ? 228 ILE   A CD1 1 
ATOM   1207 N  N   . PRO   A 1 155 ? 26.056 4.635   20.521  1.00 13.54 ? 229 PRO   A N   1 
ATOM   1208 C  CA  . PRO   A 1 155 ? 27.402 4.878   20.015  1.00 13.46 ? 229 PRO   A CA  1 
ATOM   1209 C  C   . PRO   A 1 155 ? 28.197 3.614   19.769  1.00 13.15 ? 229 PRO   A C   1 
ATOM   1210 O  O   . PRO   A 1 155 ? 28.195 2.700   20.620  1.00 14.53 ? 229 PRO   A O   1 
ATOM   1211 C  CB  . PRO   A 1 155 ? 28.059 5.711   21.084  1.00 14.90 ? 229 PRO   A CB  1 
ATOM   1212 C  CG  . PRO   A 1 155 ? 27.257 5.438   22.265  1.00 18.36 ? 229 PRO   A CG  1 
ATOM   1213 C  CD  . PRO   A 1 155 ? 25.839 5.090   21.892  1.00 14.15 ? 229 PRO   A CD  1 
ATOM   1214 N  N   . VAL   A 1 156 ? 28.891 3.573   18.639  1.00 12.23 ? 230 VAL   A N   1 
ATOM   1215 C  CA  . VAL   A 1 156 ? 29.803 2.503   18.283  1.00 12.22 ? 230 VAL   A CA  1 
ATOM   1216 C  C   . VAL   A 1 156 ? 31.267 2.897   18.417  1.00 12.40 ? 230 VAL   A C   1 
ATOM   1217 O  O   . VAL   A 1 156 ? 32.131 2.041   18.664  1.00 13.37 ? 230 VAL   A O   1 
ATOM   1218 C  CB  . VAL   A 1 156 ? 29.510 1.984   16.861  1.00 12.70 ? 230 VAL   A CB  1 
ATOM   1219 C  CG1 . VAL   A 1 156 ? 30.531 0.981   16.344  1.00 13.72 ? 230 VAL   A CG1 1 
ATOM   1220 C  CG2 . VAL   A 1 156 ? 28.122 1.367   16.768  1.00 14.52 ? 230 VAL   A CG2 1 
ATOM   1221 N  N   . ASP   A 1 157 ? 31.611 4.180   18.270  1.00 11.36 ? 231 ASP   A N   1 
ATOM   1222 C  CA  . ASP   A 1 157 ? 32.982 4.604   18.486  1.00 11.68 ? 231 ASP   A CA  1 
ATOM   1223 C  C   . ASP   A 1 157 ? 33.414 4.058   19.839  1.00 11.79 ? 231 ASP   A C   1 
ATOM   1224 O  O   . ASP   A 1 157 ? 32.663 4.106   20.811  1.00 12.35 ? 231 ASP   A O   1 
ATOM   1225 C  CB  . ASP   A 1 157 ? 33.026 6.123   18.416  1.00 11.56 ? 231 ASP   A CB  1 
ATOM   1226 C  CG  . ASP   A 1 157 ? 34.388 6.745   18.247  1.00 11.52 ? 231 ASP   A CG  1 
ATOM   1227 O  OD1 . ASP   A 1 157 ? 35.338 5.971   18.214  1.00 12.20 ? 231 ASP   A OD1 1 
ATOM   1228 O  OD2 . ASP   A 1 157 ? 34.487 7.999   18.104  1.00 11.90 ? 231 ASP   A OD2 1 
ATOM   1229 N  N   . SER   A 1 158 ? 34.633 3.469   19.924  1.00 11.39 ? 232 SER   A N   1 
ATOM   1230 C  CA  . SER   A 1 158 ? 34.928 2.564   21.041  1.00 11.75 ? 232 SER   A CA  1 
ATOM   1231 C  C   . SER   A 1 158 ? 34.862 3.226   22.410  1.00 10.74 ? 232 SER   A C   1 
ATOM   1232 O  O   . SER   A 1 158 ? 34.405 2.636   23.387  1.00 11.45 ? 232 SER   A O   1 
ATOM   1233 C  CB  . SER   A 1 158 ? 36.247 1.872   20.884  1.00 11.94 ? 232 SER   A CB  1 
ATOM   1234 O  OG  . SER   A 1 158 ? 37.358 2.721   21.036  1.00 12.94 ? 232 SER   A OG  1 
ATOM   1235 N  N   . GLU   A 1 159 ? 35.338 4.460   22.500  1.00 10.11 ? 233 GLU   A N   1 
ATOM   1236 C  CA  . GLU   A 1 159 ? 35.372 5.193   23.766  1.00 10.26 ? 233 GLU   A CA  1 
ATOM   1237 C  C   . GLU   A 1 159 ? 33.983 5.561   24.201  1.00 10.73 ? 233 GLU   A C   1 
ATOM   1238 O  O   . GLU   A 1 159 ? 33.666 5.549   25.390  1.00 11.07 ? 233 GLU   A O   1 
ATOM   1239 C  CB  . GLU   A 1 159 ? 36.233 6.445   23.558  1.00 10.81 ? 233 GLU   A CB  1 
ATOM   1240 C  CG  . GLU   A 1 159 ? 37.656 6.147   23.123  1.00 11.94 ? 233 GLU   A CG  1 
ATOM   1241 C  CD  . GLU   A 1 159 ? 37.853 6.013   21.640  1.00 11.62 ? 233 GLU   A CD  1 
ATOM   1242 O  OE1 . GLU   A 1 159 ? 36.849 6.091   20.883  1.00 12.08 ? 233 GLU   A OE1 1 
ATOM   1243 O  OE2 . GLU   A 1 159 ? 39.010 5.821   21.222  1.00 13.01 ? 233 GLU   A OE2 1 
ATOM   1244 N  N   . HIS   A 1 160 ? 33.125 5.924   23.227  1.00 10.67 ? 234 HIS   A N   1 
ATOM   1245 C  CA  . HIS   A 1 160 ? 31.755 6.315   23.503  1.00 11.26 ? 234 HIS   A CA  1 
ATOM   1246 C  C   . HIS   A 1 160 ? 30.844 5.120   23.808  1.00 10.54 ? 234 HIS   A C   1 
ATOM   1247 O  O   . HIS   A 1 160 ? 29.977 5.228   24.679  1.00 11.11 ? 234 HIS   A O   1 
ATOM   1248 C  CB  . HIS   A 1 160 ? 31.238 7.195   22.346  1.00 11.48 ? 234 HIS   A CB  1 
ATOM   1249 C  CG  . HIS   A 1 160 ? 32.223 8.257   22.041  1.00 11.12 ? 234 HIS   A CG  1 
ATOM   1250 N  ND1 . HIS   A 1 160 ? 33.364 7.926   21.324  1.00 12.15 ? 234 HIS   A ND1 1 
ATOM   1251 C  CD2 . HIS   A 1 160 ? 32.358 9.547   22.405  1.00 12.04 ? 234 HIS   A CD2 1 
ATOM   1252 C  CE1 . HIS   A 1 160 ? 34.161 8.989   21.315  1.00 12.30 ? 234 HIS   A CE1 1 
ATOM   1253 N  NE2 . HIS   A 1 160 ? 33.549 10.003  21.910  1.00 12.34 ? 234 HIS   A NE2 1 
ATOM   1254 N  N   . SER   A 1 161 ? 31.147 3.987   23.179  1.00 11.12 ? 235 SER   A N   1 
ATOM   1255 C  CA  . SER   A 1 161 ? 30.550 2.728   23.589  1.00 10.86 ? 235 SER   A CA  1 
ATOM   1256 C  C   . SER   A 1 161 ? 30.931 2.402   25.023  1.00 11.42 ? 235 SER   A C   1 
ATOM   1257 O  O   . SER   A 1 161 ? 30.091 2.031   25.831  1.00 11.73 ? 235 SER   A O   1 
ATOM   1258 C  CB  . SER   A 1 161 ? 31.011 1.622   22.688  1.00 11.80 ? 235 SER   A CB  1 
ATOM   1259 O  OG  . SER   A 1 161 ? 30.460 0.376   23.123  1.00 12.33 ? 235 SER   A OG  1 
ATOM   1260 N  N   . ALA   A 1 162 ? 32.217 2.580   25.373  1.00 10.62 ? 236 ALA   A N   1 
ATOM   1261 C  CA  . ALA   A 1 162 ? 32.666 2.335   26.732  1.00 11.34 ? 236 ALA   A CA  1 
ATOM   1262 C  C   . ALA   A 1 162 ? 31.900 3.192   27.726  1.00 10.63 ? 236 ALA   A C   1 
ATOM   1263 O  O   . ALA   A 1 162 ? 31.355 2.700   28.713  1.00 10.62 ? 236 ALA   A O   1 
ATOM   1264 C  CB  . ALA   A 1 162 ? 34.166 2.591   26.827  1.00 11.73 ? 236 ALA   A CB  1 
ATOM   1265 N  N   . ILE   A 1 163 ? 31.852 4.511   27.464  1.00 11.01 ? 237 ILE   A N   1 
ATOM   1266 C  CA  . ILE   A 1 163 ? 31.122 5.423   28.328  1.00 11.27 ? 237 ILE   A CA  1 
ATOM   1267 C  C   . ILE   A 1 163 ? 29.697 4.938   28.507  1.00 11.27 ? 237 ILE   A C   1 
ATOM   1268 O  O   . ILE   A 1 163 ? 29.167 4.866   29.598  1.00 11.99 ? 237 ILE   A O   1 
ATOM   1269 C  CB  . ILE   A 1 163 ? 31.188 6.854   27.792  1.00 11.76 ? 237 ILE   A CB  1 
ATOM   1270 C  CG1 . ILE   A 1 163 ? 32.597 7.399   27.902  1.00 12.56 ? 237 ILE   A CG1 1 
ATOM   1271 C  CG2 . ILE   A 1 163 ? 30.157 7.763   28.436  1.00 12.81 ? 237 ILE   A CG2 1 
ATOM   1272 C  CD1 . ILE   A 1 163 ? 32.914 8.547   26.937  1.00 13.60 ? 237 ILE   A CD1 1 
ATOM   1273 N  N   . PHE   A 1 164 ? 29.033 4.644   27.378  1.00 11.49 ? 238 PHE   A N   1 
ATOM   1274 C  CA  . PHE   A 1 164 ? 27.638 4.222   27.416  1.00 11.88 ? 238 PHE   A CA  1 
ATOM   1275 C  C   . PHE   A 1 164 ? 27.467 2.951   28.244  1.00 12.19 ? 238 PHE   A C   1 
ATOM   1276 O  O   . PHE   A 1 164 ? 26.499 2.842   28.982  1.00 13.30 ? 238 PHE   A O   1 
ATOM   1277 C  CB  . PHE   A 1 164 ? 27.161 4.060   25.973  1.00 12.79 ? 238 PHE   A CB  1 
ATOM   1278 C  CG  . PHE   A 1 164 ? 25.660 3.900   25.792  1.00 13.82 ? 238 PHE   A CG  1 
ATOM   1279 C  CD1 . PHE   A 1 164 ? 24.841 4.922   26.171  1.00 14.97 ? 238 PHE   A CD1 1 
ATOM   1280 C  CD2 . PHE   A 1 164 ? 25.127 2.781   25.228  1.00 16.01 ? 238 PHE   A CD2 1 
ATOM   1281 C  CE1 . PHE   A 1 164 ? 23.455 4.802   26.031  1.00 17.08 ? 238 PHE   A CE1 1 
ATOM   1282 C  CE2 . PHE   A 1 164 ? 23.739 2.685   25.066  1.00 17.12 ? 238 PHE   A CE2 1 
ATOM   1283 C  CZ  . PHE   A 1 164 ? 22.954 3.701   25.442  1.00 17.07 ? 238 PHE   A CZ  1 
ATOM   1284 N  N   . GLN   A 1 165 ? 28.393 1.993   28.080  1.00 12.77 ? 239 GLN   A N   1 
ATOM   1285 C  CA  . GLN   A 1 165 ? 28.365 0.757   28.852  1.00 12.38 ? 239 GLN   A CA  1 
ATOM   1286 C  C   . GLN   A 1 165 ? 28.545 1.007   30.334  1.00 13.39 ? 239 GLN   A C   1 
ATOM   1287 O  O   . GLN   A 1 165 ? 28.151 0.138   31.139  1.00 17.68 ? 239 GLN   A O   1 
ATOM   1288 C  CB  . GLN   A 1 165 ? 29.428 -0.222  28.342  1.00 11.90 ? 239 GLN   A CB  1 
ATOM   1289 C  CG  . GLN   A 1 165 ? 29.111 -0.812  26.969  1.00 11.36 ? 239 GLN   A CG  1 
ATOM   1290 C  CD  . GLN   A 1 165 ? 30.171 -1.779  26.544  1.00 12.47 ? 239 GLN   A CD  1 
ATOM   1291 O  OE1 . GLN   A 1 165 ? 30.376 -2.802  27.217  1.00 12.92 ? 239 GLN   A OE1 1 
ATOM   1292 N  NE2 . GLN   A 1 165 ? 30.921 -1.492  25.494  1.00 12.76 ? 239 GLN   A NE2 1 
ATOM   1293 N  N   . CYS   A 1 166 ? 29.217 2.078   30.719  1.00 12.53 ? 240 CYS   A N   1 
ATOM   1294 C  CA  . CYS   A 1 166 ? 29.456 2.402   32.129  1.00 14.06 ? 240 CYS   A CA  1 
ATOM   1295 C  C   . CYS   A 1 166 ? 28.239 3.011   32.822  1.00 14.75 ? 240 CYS   A C   1 
ATOM   1296 O  O   . CYS   A 1 166 ? 28.277 3.295   34.033  1.00 16.43 ? 240 CYS   A O   1 
ATOM   1297 C  CB  . CYS   A 1 166 ? 30.618 3.363   32.275  1.00 13.82 ? 240 CYS   A CB  1 
ATOM   1298 S  SG  . CYS   A 1 166 ? 32.213 2.658   31.837  1.00 17.63 ? 240 CYS   A SG  1 
ATOM   1299 N  N   . LEU   A 1 167 ? 27.170 3.274   32.088  1.00 15.51 ? 241 LEU   A N   1 
ATOM   1300 C  CA  . LEU   A 1 167 ? 25.995 3.951   32.604  1.00 15.90 ? 241 LEU   A CA  1 
ATOM   1301 C  C   . LEU   A 1 167 ? 25.009 2.916   33.094  1.00 17.89 ? 241 LEU   A C   1 
ATOM   1302 O  O   . LEU   A 1 167 ? 25.016 1.758   32.674  1.00 23.34 ? 241 LEU   A O   1 
ATOM   1303 C  CB  . LEU   A 1 167 ? 25.383 4.864   31.551  1.00 15.57 ? 241 LEU   A CB  1 
ATOM   1304 C  CG  . LEU   A 1 167 ? 26.317 5.916   30.978  1.00 14.96 ? 241 LEU   A CG  1 
ATOM   1305 C  CD1 . LEU   A 1 167 ? 25.575 6.762   29.909  1.00 15.67 ? 241 LEU   A CD1 1 
ATOM   1306 C  CD2 . LEU   A 1 167 ? 26.953 6.803   32.026  1.00 16.11 ? 241 LEU   A CD2 1 
ATOM   1307 N  N   . ASP   A 1 168 ? 24.148 3.345   33.979  1.00 17.69 ? 242 ASP   A N   1 
ATOM   1308 C  CA  . ASP   A 1 168 ? 23.129 2.500   34.528  1.00 19.83 ? 242 ASP   A CA  1 
ATOM   1309 C  C   . ASP   A 1 168 ? 21.914 2.621   33.627  1.00 19.01 ? 242 ASP   A C   1 
ATOM   1310 O  O   . ASP   A 1 168 ? 21.337 3.711   33.481  1.00 18.05 ? 242 ASP   A O   1 
ATOM   1311 C  CB  . ASP   A 1 168 ? 22.860 3.023   35.920  1.00 21.97 ? 242 ASP   A CB  1 
ATOM   1312 C  CG  . ASP   A 1 168 ? 21.771 2.316   36.686  1.00 28.31 ? 242 ASP   A CG  1 
ATOM   1313 O  OD1 . ASP   A 1 168 ? 21.261 1.334   36.111  1.00 26.16 ? 242 ASP   A OD1 1 
ATOM   1314 O  OD2 . ASP   A 1 168 ? 21.432 2.820   37.800  1.00 32.30 ? 242 ASP   A OD2 1 
ATOM   1315 N  N   . ASN   A 1 169 ? 21.523 1.496   33.016  1.00 18.53 ? 243 ASN   A N   1 
ATOM   1316 C  CA  . ASN   A 1 169 ? 20.432 1.523   32.053  1.00 18.74 ? 243 ASN   A CA  1 
ATOM   1317 C  C   . ASN   A 1 169 ? 19.110 1.914   32.702  1.00 21.49 ? 243 ASN   A C   1 
ATOM   1318 O  O   . ASN   A 1 169 ? 18.222 2.396   32.017  1.00 21.92 ? 243 ASN   A O   1 
ATOM   1319 C  CB  . ASN   A 1 169 ? 20.319 0.271   31.191  1.00 20.33 ? 243 ASN   A CB  1 
ATOM   1320 C  CG  . ASN   A 1 169 ? 21.470 0.092   30.212  1.00 20.59 ? 243 ASN   A CG  1 
ATOM   1321 O  OD1 . ASN   A 1 169 ? 21.961 -1.020  29.970  1.00 26.50 ? 243 ASN   A OD1 1 
ATOM   1322 N  ND2 . ASN   A 1 169 ? 21.792 1.143   29.499  1.00 22.21 ? 243 ASN   A ND2 1 
ATOM   1323 N  N   . ASN   A 1 170 ? 18.988 1.726   34.021  1.00 22.21 ? 244 ASN   A N   1 
ATOM   1324 C  CA  . ASN   A 1 170 ? 17.830 2.186   34.756  1.00 23.79 ? 244 ASN   A CA  1 
ATOM   1325 C  C   . ASN   A 1 170 ? 17.653 3.695   34.538  1.00 24.45 ? 244 ASN   A C   1 
ATOM   1326 O  O   . ASN   A 1 170 ? 16.549 4.213   34.519  1.00 26.15 ? 244 ASN   A O   1 
ATOM   1327 C  CB  . ASN   A 1 170 ? 18.020 1.807   36.226  1.00 26.29 ? 244 ASN   A CB  1 
ATOM   1328 C  CG  . ASN   A 1 170 ? 16.790 2.020   37.073  1.00 33.30 ? 244 ASN   A CG  1 
ATOM   1329 O  OD1 . ASN   A 1 170 ? 15.683 1.668   36.655  1.00 32.30 ? 244 ASN   A OD1 1 
ATOM   1330 N  ND2 . ASN   A 1 170 ? 16.970 2.572   38.262  1.00 33.34 ? 244 ASN   A ND2 1 
ATOM   1331 N  N   . LYS   A 1 171 ? 18.763 4.443   34.460  1.00 21.62 ? 245 LYS   A N   1 
ATOM   1332 C  CA  . LYS   A 1 171 ? 18.734 5.881   34.192  1.00 19.76 ? 245 LYS   A CA  1 
ATOM   1333 C  C   . LYS   A 1 171 ? 18.742 6.197   32.698  1.00 18.83 ? 245 LYS   A C   1 
ATOM   1334 O  O   . LYS   A 1 171 ? 18.005 7.064   32.232  1.00 19.46 ? 245 LYS   A O   1 
ATOM   1335 C  CB  . LYS   A 1 171 ? 19.919 6.595   34.853  1.00 21.25 ? 245 LYS   A CB  1 
ATOM   1336 C  CG  . LYS   A 1 171 ? 19.944 6.422   36.347  1.00 25.87 ? 245 LYS   A CG  1 
ATOM   1337 C  CD  . LYS   A 1 171 ? 18.833 7.105   37.111  1.00 32.69 ? 245 LYS   A CD  1 
ATOM   1338 C  CE  . LYS   A 1 171 ? 18.942 6.972   38.604  1.00 39.29 ? 245 LYS   A CE  1 
ATOM   1339 N  NZ  . LYS   A 1 171 ? 20.330 6.822   39.039  1.00 42.64 ? 245 LYS   A NZ  1 
ATOM   1340 N  N   . VAL   A 1 172 ? 19.528 5.471   31.904  1.00 17.68 ? 246 VAL   A N   1 
ATOM   1341 C  CA  . VAL   A 1 172 ? 19.593 5.709   30.466  1.00 17.89 ? 246 VAL   A CA  1 
ATOM   1342 C  C   . VAL   A 1 172 ? 18.198 5.645   29.860  1.00 19.33 ? 246 VAL   A C   1 
ATOM   1343 O  O   . VAL   A 1 172 ? 17.848 6.479   29.016  1.00 18.79 ? 246 VAL   A O   1 
ATOM   1344 C  CB  . VAL   A 1 172 ? 20.534 4.743   29.728  1.00 17.08 ? 246 VAL   A CB  1 
ATOM   1345 C  CG1 . VAL   A 1 172 ? 20.464 4.908   28.230  1.00 16.64 ? 246 VAL   A CG1 1 
ATOM   1346 C  CG2 . VAL   A 1 172 ? 21.970 4.909   30.191  1.00 16.62 ? 246 VAL   A CG2 1 
ATOM   1347 N  N   . LEU   A 1 173 ? 17.406 4.655   30.311  1.00 20.45 ? 247 LEU   A N   1 
ATOM   1348 C  CA  . LEU   A 1 173 ? 16.119 4.394   29.682  1.00 20.92 ? 247 LEU   A CA  1 
ATOM   1349 C  C   . LEU   A 1 173 ? 15.134 5.537   29.926  1.00 21.87 ? 247 LEU   A C   1 
ATOM   1350 O  O   . LEU   A 1 173 ? 14.101 5.558   29.243  1.00 24.49 ? 247 LEU   A O   1 
ATOM   1351 C  CB  . LEU   A 1 173 ? 15.583 3.031   30.123  1.00 23.21 ? 247 LEU   A CB  1 
ATOM   1352 C  CG  . LEU   A 1 173 ? 16.295 1.829   29.498  1.00 25.64 ? 247 LEU   A CG  1 
ATOM   1353 C  CD1 . LEU   A 1 173 ? 15.909 0.571   30.219  1.00 27.26 ? 247 LEU   A CD1 1 
ATOM   1354 C  CD2 . LEU   A 1 173 ? 15.980 1.649   28.026  1.00 26.39 ? 247 LEU   A CD2 1 
ATOM   1355 N  N   . LYS   A 1 174 ? 15.422 6.479   30.817  1.00 20.73 ? 248 LYS   A N   1 
ATOM   1356 C  CA  . LYS   A 1 174 ? 14.595 7.647   31.050  1.00 21.64 ? 248 LYS   A CA  1 
ATOM   1357 C  C   . LYS   A 1 174 ? 14.892 8.726   30.012  1.00 22.15 ? 248 LYS   A C   1 
ATOM   1358 O  O   . LYS   A 1 174 ? 14.161 9.712   29.936  1.00 24.56 ? 248 LYS   A O   1 
ATOM   1359 C  CB  . LYS   A 1 174 ? 14.831 8.246   32.434  1.00 22.99 ? 248 LYS   A CB  1 
ATOM   1360 C  CG  . LYS   A 1 174 ? 14.547 7.295   33.592  1.00 26.12 ? 248 LYS   A CG  1 
ATOM   1361 C  CD  . LYS   A 1 174 ? 14.987 7.847   34.951  1.00 33.96 ? 248 LYS   A CD  1 
ATOM   1362 C  CE  . LYS   A 1 174 ? 14.360 7.228   36.171  1.00 42.77 ? 248 LYS   A CE  1 
ATOM   1363 N  NZ  . LYS   A 1 174 ? 14.000 5.813   36.030  1.00 48.32 ? 248 LYS   A NZ  1 
ATOM   1364 N  N   . THR   A 1 175 ? 15.942 8.561   29.194  1.00 19.30 ? 249 THR   A N   1 
ATOM   1365 C  CA  . THR   A 1 175 ? 16.345 9.545   28.207  1.00 19.62 ? 249 THR   A CA  1 
ATOM   1366 C  C   . THR   A 1 175 ? 16.903 8.780   27.001  1.00 17.73 ? 249 THR   A C   1 
ATOM   1367 O  O   . THR   A 1 175 ? 16.469 7.686   26.722  1.00 18.32 ? 249 THR   A O   1 
ATOM   1368 C  CB  . THR   A 1 175 ? 17.273 10.571  28.867  1.00 21.46 ? 249 THR   A CB  1 
ATOM   1369 O  OG1 . THR   A 1 175 ? 17.657 11.587  27.944  1.00 23.82 ? 249 THR   A OG1 1 
ATOM   1370 C  CG2 . THR   A 1 175 ? 18.530 9.977   29.466  1.00 20.34 ? 249 THR   A CG2 1 
ATOM   1371 N  N   . LYS   A 1 176 ? 17.875 9.360   26.299  1.00 16.07 ? 250 LYS   A N   1 
ATOM   1372 C  CA  . LYS   A 1 176 ? 18.595 8.714   25.209  1.00 16.12 ? 250 LYS   A CA  1 
ATOM   1373 C  C   . LYS   A 1 176 ? 19.772 9.618   24.861  1.00 13.91 ? 250 LYS   A C   1 
ATOM   1374 O  O   . LYS   A 1 176 ? 19.820 10.775  25.273  1.00 14.65 ? 250 LYS   A O   1 
ATOM   1375 C  CB  . LYS   A 1 176 ? 17.712 8.410   23.985  1.00 15.37 ? 250 LYS   A CB  1 
ATOM   1376 C  CG  . LYS   A 1 176 ? 17.129 9.610   23.277  1.00 16.68 ? 250 LYS   A CG  1 
ATOM   1377 C  CD  . LYS   A 1 176 ? 16.138 9.302   22.151  1.00 16.39 ? 250 LYS   A CD  1 
ATOM   1378 C  CE  . LYS   A 1 176 ? 15.700 10.504  21.416  1.00 17.05 ? 250 LYS   A CE  1 
ATOM   1379 N  NZ  . LYS   A 1 176 ? 14.676 10.168  20.399  1.00 17.73 ? 250 LYS   A NZ  1 
ATOM   1380 N  N   . CYS   A 1 177 ? 20.750 9.067   24.132  1.00 13.83 ? 251 CYS   A N   1 
ATOM   1381 C  CA  . CYS   A 1 177 ? 21.917 9.863   23.807  1.00 14.57 ? 251 CYS   A CA  1 
ATOM   1382 C  C   . CYS   A 1 177 ? 21.583 11.076  22.960  1.00 14.91 ? 251 CYS   A C   1 
ATOM   1383 O  O   . CYS   A 1 177 ? 20.608 11.083  22.209  1.00 14.89 ? 251 CYS   A O   1 
ATOM   1384 C  CB  . CYS   A 1 177 ? 22.955 9.019   23.072  1.00 15.00 ? 251 CYS   A CB  1 
ATOM   1385 S  SG  . CYS   A 1 177 ? 23.712 7.695   24.063  1.00 16.46 ? 251 CYS   A SG  1 
ATOM   1386 N  N   . LEU   A 1 178 ? 22.421 12.091  23.071  1.00 15.27 ? 252 LEU   A N   1 
ATOM   1387 C  CA  . LEU   A 1 178 ? 22.378 13.271  22.240  1.00 16.10 ? 252 LEU   A CA  1 
ATOM   1388 C  C   . LEU   A 1 178 ? 21.089 14.028  22.590  1.00 16.16 ? 252 LEU   A C   1 
ATOM   1389 O  O   . LEU   A 1 178 ? 20.333 14.387  21.681  1.00 18.48 ? 252 LEU   A O   1 
ATOM   1390 C  CB  . LEU   A 1 178 ? 22.582 12.953  20.754  1.00 17.03 ? 252 LEU   A CB  1 
ATOM   1391 C  CG  . LEU   A 1 178 ? 23.621 13.849  20.067  1.00 18.69 ? 252 LEU   A CG  1 
ATOM   1392 C  CD1 . LEU   A 1 178 ? 23.903 13.437  18.655  1.00 20.47 ? 252 LEU   A CD1 1 
ATOM   1393 C  CD2 . LEU   A 1 178 ? 23.218 15.340  20.126  1.00 19.43 ? 252 LEU   A CD2 1 
ATOM   1394 N  N   . GLN   A 1 179 ? 20.860 14.250  23.880  1.00 16.04 ? 253 GLN   A N   1 
ATOM   1395 C  CA  . GLN   A 1 179 ? 19.701 14.916  24.455  1.00 16.96 ? 253 GLN   A CA  1 
ATOM   1396 C  C   . GLN   A 1 179 ? 20.131 15.839  25.579  1.00 18.14 ? 253 GLN   A C   1 
ATOM   1397 O  O   . GLN   A 1 179 ? 21.044 15.542  26.349  1.00 17.51 ? 253 GLN   A O   1 
ATOM   1398 C  CB  . GLN   A 1 179 ? 18.709 13.908  25.030  1.00 17.44 ? 253 GLN   A CB  1 
ATOM   1399 C  CG  . GLN   A 1 179 ? 18.110 13.020  23.952  1.00 18.66 ? 253 GLN   A CG  1 
ATOM   1400 C  CD  . GLN   A 1 179 ? 17.114 13.742  23.073  1.00 19.23 ? 253 GLN   A CD  1 
ATOM   1401 O  OE1 . GLN   A 1 179 ? 17.400 14.296  21.996  1.00 22.14 ? 253 GLN   A OE1 1 
ATOM   1402 N  NE2 . GLN   A 1 179 ? 15.920 13.767  23.590  1.00 19.04 ? 253 GLN   A NE2 1 
ATOM   1403 N  N   . ASP   A 1 180 ? 19.472 16.991  25.688  1.00 17.20 ? 254 ASP   A N   1 
ATOM   1404 C  CA  . ASP   A 1 180 ? 19.640 17.874  26.817  1.00 18.08 ? 254 ASP   A CA  1 
ATOM   1405 C  C   . ASP   A 1 180 ? 19.337 17.122  28.106  1.00 16.53 ? 254 ASP   A C   1 
ATOM   1406 O  O   . ASP   A 1 180 ? 18.488 16.262  28.177  1.00 18.69 ? 254 ASP   A O   1 
ATOM   1407 C  CB  . ASP   A 1 180 ? 18.704 19.064  26.698  1.00 20.42 ? 254 ASP   A CB  1 
ATOM   1408 C  CG  . ASP   A 1 180 ? 19.043 20.075  25.626  1.00 25.59 ? 254 ASP   A CG  1 
ATOM   1409 O  OD1 . ASP   A 1 180 ? 20.195 20.119  25.185  1.00 29.93 ? 254 ASP   A OD1 1 
ATOM   1410 O  OD2 . ASP   A 1 180 ? 18.104 20.828  25.267  1.00 35.02 ? 254 ASP   A OD2 1 
ATOM   1411 N  N   . ASN   A 1 181 ? 20.143 17.444  29.115  1.00 18.79 ? 255 ASN   A N   1 
ATOM   1412 C  CA  . ASN   A 1 181 ? 19.978 16.965  30.482  1.00 22.14 ? 255 ASN   A CA  1 
ATOM   1413 C  C   . ASN   A 1 181 ? 20.498 15.532  30.668  1.00 18.24 ? 255 ASN   A C   1 
ATOM   1414 O  O   . ASN   A 1 181 ? 20.310 14.981  31.746  1.00 18.23 ? 255 ASN   A O   1 
ATOM   1415 C  CB  . ASN   A 1 181 ? 18.545 17.083  30.996  1.00 24.12 ? 255 ASN   A CB  1 
ATOM   1416 C  CG  . ASN   A 1 181 ? 18.101 18.533  31.056  1.00 32.02 ? 255 ASN   A CG  1 
ATOM   1417 O  OD1 . ASN   A 1 181 ? 18.874 19.398  31.481  1.00 38.94 ? 255 ASN   A OD1 1 
ATOM   1418 N  ND2 . ASN   A 1 181 ? 16.912 18.818  30.554  1.00 35.19 ? 255 ASN   A ND2 1 
ATOM   1419 N  N   . PHE   A 1 182 ? 21.069 14.910  29.650  1.00 16.59 ? 256 PHE   A N   1 
ATOM   1420 C  CA  . PHE   A 1 182 ? 21.520 13.523  29.758  1.00 15.95 ? 256 PHE   A CA  1 
ATOM   1421 C  C   . PHE   A 1 182 ? 22.472 13.306  30.921  1.00 15.58 ? 256 PHE   A C   1 
ATOM   1422 O  O   . PHE   A 1 182 ? 22.328 12.316  31.639  1.00 14.95 ? 256 PHE   A O   1 
ATOM   1423 C  CB  . PHE   A 1 182 ? 22.161 13.112  28.433  1.00 15.48 ? 256 PHE   A CB  1 
ATOM   1424 C  CG  . PHE   A 1 182 ? 22.579 11.664  28.386  1.00 14.53 ? 256 PHE   A CG  1 
ATOM   1425 C  CD1 . PHE   A 1 182 ? 23.831 11.249  28.862  1.00 13.70 ? 256 PHE   A CD1 1 
ATOM   1426 C  CD2 . PHE   A 1 182 ? 21.737 10.724  27.839  1.00 14.77 ? 256 PHE   A CD2 1 
ATOM   1427 C  CE1 . PHE   A 1 182 ? 24.186 9.914   28.808  1.00 13.69 ? 256 PHE   A CE1 1 
ATOM   1428 C  CE2 . PHE   A 1 182 ? 22.103 9.403   27.748  1.00 14.19 ? 256 PHE   A CE2 1 
ATOM   1429 C  CZ  . PHE   A 1 182 ? 23.334 9.005   28.253  1.00 14.91 ? 256 PHE   A CZ  1 
ATOM   1430 N  N   . SER   A 1 183 ? 23.406 14.217  31.131  1.00 14.66 ? 257 SER   A N   1 
ATOM   1431 C  CA  . SER   A 1 183 ? 24.365 14.046  32.207  1.00 15.01 ? 257 SER   A CA  1 
ATOM   1432 C  C   . SER   A 1 183 ? 23.715 14.169  33.580  1.00 16.09 ? 257 SER   A C   1 
ATOM   1433 O  O   . SER   A 1 183 ? 24.087 13.480  34.532  1.00 15.58 ? 257 SER   A O   1 
ATOM   1434 C  CB  . SER   A 1 183 ? 25.531 14.956  32.061  1.00 15.78 ? 257 SER   A CB  1 
ATOM   1435 O  OG  . SER   A 1 183 ? 25.120 16.303  32.035  1.00 21.77 ? 257 SER   A OG  1 
ATOM   1436 N  N   . LYS   A 1 184 ? 22.724 15.051  33.726  1.00 16.63 ? 258 LYS   A N   1 
ATOM   1437 C  CA  . LYS   A 1 184 ? 22.027 15.222  34.980  1.00 17.24 ? 258 LYS   A CA  1 
ATOM   1438 C  C   . LYS   A 1 184 ? 21.261 13.956  35.329  1.00 16.34 ? 258 LYS   A C   1 
ATOM   1439 O  O   . LYS   A 1 184 ? 21.351 13.460  36.463  1.00 16.89 ? 258 LYS   A O   1 
ATOM   1440 C  CB  . LYS   A 1 184 ? 21.054 16.418  34.926  1.00 21.05 ? 258 LYS   A CB  1 
ATOM   1441 C  CG  . LYS   A 1 184 ? 20.226 16.572  36.177  1.00 29.83 ? 258 LYS   A CG  1 
ATOM   1442 C  CD  . LYS   A 1 184 ? 19.471 17.897  36.116  1.00 36.09 ? 258 LYS   A CD  1 
ATOM   1443 C  CE  . LYS   A 1 184 ? 19.075 18.382  37.481  1.00 42.76 ? 258 LYS   A CE  1 
ATOM   1444 N  NZ  . LYS   A 1 184 ? 18.408 17.321  38.236  1.00 50.07 ? 258 LYS   A NZ  1 
ATOM   1445 N  N   . ILE   A 1 185 ? 20.526 13.402  34.362  1.00 15.43 ? 259 ILE   A N   1 
ATOM   1446 C  CA  . ILE   A 1 185 ? 19.720 12.226  34.573  1.00 16.29 ? 259 ILE   A CA  1 
ATOM   1447 C  C   . ILE   A 1 185 ? 20.610 11.051  34.988  1.00 16.05 ? 259 ILE   A C   1 
ATOM   1448 O  O   . ILE   A 1 185 ? 20.254 10.191  35.771  1.00 17.14 ? 259 ILE   A O   1 
ATOM   1449 C  CB  . ILE   A 1 185 ? 18.876 11.924  33.332  1.00 18.61 ? 259 ILE   A CB  1 
ATOM   1450 C  CG1 . ILE   A 1 185 ? 17.841 13.076  33.096  1.00 21.34 ? 259 ILE   A CG1 1 
ATOM   1451 C  CG2 . ILE   A 1 185 ? 18.210 10.554  33.397  1.00 21.17 ? 259 ILE   A CG2 1 
ATOM   1452 C  CD1 . ILE   A 1 185 ? 17.173 13.065  31.751  1.00 26.47 ? 259 ILE   A CD1 1 
ATOM   1453 N  N   . ASN   A 1 186 ? 21.809 10.976  34.368  1.00 14.88 ? 260 ASN   A N   1 
ATOM   1454 C  CA  . ASN   A 1 186 ? 22.722 9.856   34.557  1.00 15.08 ? 260 ASN   A CA  1 
ATOM   1455 C  C   . ASN   A 1 186 ? 23.720 10.150  35.678  1.00 14.27 ? 260 ASN   A C   1 
ATOM   1456 O  O   . ASN   A 1 186 ? 24.594 9.299   35.926  1.00 15.26 ? 260 ASN   A O   1 
ATOM   1457 C  CB  . ASN   A 1 186 ? 23.403 9.483   33.241  1.00 14.36 ? 260 ASN   A CB  1 
ATOM   1458 C  CG  . ASN   A 1 186 ? 22.463 8.710   32.361  1.00 14.97 ? 260 ASN   A CG  1 
ATOM   1459 O  OD1 . ASN   A 1 186 ? 22.271 7.499   32.566  1.00 16.93 ? 260 ASN   A OD1 1 
ATOM   1460 N  ND2 . ASN   A 1 186 ? 21.862 9.413   31.424  1.00 15.22 ? 260 ASN   A ND2 1 
ATOM   1461 N  N   . ASN   A 1 187 ? 23.670 11.288  36.332  1.00 14.26 ? 261 ASN   A N   1 
ATOM   1462 C  CA  . ASN   A 1 187 ? 24.564 11.602  37.440  1.00 14.47 ? 261 ASN   A CA  1 
ATOM   1463 C  C   . ASN   A 1 187 ? 26.028 11.620  36.992  1.00 12.91 ? 261 ASN   A C   1 
ATOM   1464 O  O   . ASN   A 1 187 ? 26.923 11.327  37.796  1.00 12.86 ? 261 ASN   A O   1 
ATOM   1465 C  CB  . ASN   A 1 187 ? 24.387 10.652  38.623  1.00 16.27 ? 261 ASN   A CB  1 
ATOM   1466 C  CG  . ASN   A 1 187 ? 23.020 10.764  39.282  1.00 20.44 ? 261 ASN   A CG  1 
ATOM   1467 O  OD1 . ASN   A 1 187 ? 22.455 11.851  39.370  1.00 22.63 ? 261 ASN   A OD1 1 
ATOM   1468 N  ND2 . ASN   A 1 187 ? 22.489 9.619   39.627  1.00 25.79 ? 261 ASN   A ND2 1 
ATOM   1469 N  N   . ILE   A 1 188 ? 26.284 12.025  35.758  1.00 12.49 ? 262 ILE   A N   1 
ATOM   1470 C  CA  . ILE   A 1 188 ? 27.638 12.105  35.218  1.00 12.85 ? 262 ILE   A CA  1 
ATOM   1471 C  C   . ILE   A 1 188 ? 28.288 13.382  35.635  1.00 12.76 ? 262 ILE   A C   1 
ATOM   1472 O  O   . ILE   A 1 188 ? 27.709 14.474  35.410  1.00 14.15 ? 262 ILE   A O   1 
ATOM   1473 C  CB  . ILE   A 1 188 ? 27.613 11.989  33.699  1.00 13.16 ? 262 ILE   A CB  1 
ATOM   1474 C  CG1 . ILE   A 1 188 ? 27.053 10.675  33.210  1.00 14.02 ? 262 ILE   A CG1 1 
ATOM   1475 C  CG2 . ILE   A 1 188 ? 29.030 12.188  33.130  1.00 13.88 ? 262 ILE   A CG2 1 
ATOM   1476 C  CD1 . ILE   A 1 188 ? 26.786 10.606  31.729  1.00 14.20 ? 262 ILE   A CD1 1 
ATOM   1477 N  N   . ASN   A 1 189 ? 29.497 13.329  36.181  1.00 12.07 ? 263 ASN   A N   1 
ATOM   1478 C  CA  . ASN   A 1 189 ? 30.260 14.515  36.523  1.00 12.06 ? 263 ASN   A CA  1 
ATOM   1479 C  C   . ASN   A 1 189 ? 31.353 14.839  35.536  1.00 12.55 ? 263 ASN   A C   1 
ATOM   1480 O  O   . ASN   A 1 189 ? 31.603 16.008  35.221  1.00 14.56 ? 263 ASN   A O   1 
ATOM   1481 C  CB  . ASN   A 1 189 ? 30.853 14.365  37.912  1.00 13.65 ? 263 ASN   A CB  1 
ATOM   1482 C  CG  . ASN   A 1 189 ? 31.328 15.687  38.428  1.00 17.39 ? 263 ASN   A CG  1 
ATOM   1483 O  OD1 . ASN   A 1 189 ? 30.555 16.683  38.465  1.00 20.97 ? 263 ASN   A OD1 1 
ATOM   1484 N  ND2 . ASN   A 1 189 ? 32.586 15.754  38.804  1.00 18.49 ? 263 ASN   A ND2 1 
ATOM   1485 N  N   . LYS   A 1 190 ? 32.084 13.833  35.037  1.00 11.45 ? 264 LYS   A N   1 
ATOM   1486 C  CA  . LYS   A 1 190 ? 33.286 14.048  34.242  1.00 11.49 ? 264 LYS   A CA  1 
ATOM   1487 C  C   . LYS   A 1 190 ? 33.596 12.774  33.467  1.00 10.61 ? 264 LYS   A C   1 
ATOM   1488 O  O   . LYS   A 1 190 ? 33.193 11.688  33.875  1.00 11.63 ? 264 LYS   A O   1 
ATOM   1489 C  CB  . LYS   A 1 190 ? 34.425 14.441  35.180  1.00 13.54 ? 264 LYS   A CB  1 
ATOM   1490 C  CG  . LYS   A 1 190 ? 35.800 14.596  34.621  1.00 14.56 ? 264 LYS   A CG  1 
ATOM   1491 C  CD  . LYS   A 1 190 ? 36.606 13.298  34.727  1.00 15.50 ? 264 LYS   A CD  1 
ATOM   1492 C  CE  . LYS   A 1 190 ? 37.961 13.429  34.143  1.00 16.92 ? 264 LYS   A CE  1 
ATOM   1493 N  NZ  . LYS   A 1 190 ? 38.789 14.344  34.923  1.00 19.75 ? 264 LYS   A NZ  1 
ATOM   1494 N  N   . ILE   A 1 191 ? 34.265 12.923  32.335  1.00 10.83 ? 265 ILE   A N   1 
ATOM   1495 C  CA  . ILE   A 1 191 ? 34.669 11.812  31.467  1.00 10.38 ? 265 ILE   A CA  1 
ATOM   1496 C  C   . ILE   A 1 191 ? 36.172 11.793  31.329  1.00 10.63 ? 265 ILE   A C   1 
ATOM   1497 O  O   . ILE   A 1 191 ? 36.784 12.822  31.037  1.00 11.05 ? 265 ILE   A O   1 
ATOM   1498 C  CB  . ILE   A 1 191 ? 34.042 11.981  30.084  1.00 11.61 ? 265 ILE   A CB  1 
ATOM   1499 C  CG1 . ILE   A 1 191 ? 32.517 11.978  30.147  1.00 13.31 ? 265 ILE   A CG1 1 
ATOM   1500 C  CG2 . ILE   A 1 191 ? 34.552 10.928  29.089  1.00 11.58 ? 265 ILE   A CG2 1 
ATOM   1501 C  CD1 . ILE   A 1 191 ? 31.928 10.681  30.561  1.00 13.60 ? 265 ILE   A CD1 1 
ATOM   1502 N  N   . PHE   A 1 192 ? 36.755 10.595  31.470  1.00 10.62 ? 266 PHE   A N   1 
ATOM   1503 C  CA  . PHE   A 1 192 ? 38.104 10.311  31.036  1.00 11.09 ? 266 PHE   A CA  1 
ATOM   1504 C  C   . PHE   A 1 192 ? 38.016 9.652   29.668  1.00 10.88 ? 266 PHE   A C   1 
ATOM   1505 O  O   . PHE   A 1 192 ? 37.545 8.522   29.542  1.00 11.41 ? 266 PHE   A O   1 
ATOM   1506 C  CB  . PHE   A 1 192 ? 38.851 9.355   31.968  1.00 12.20 ? 266 PHE   A CB  1 
ATOM   1507 C  CG  . PHE   A 1 192 ? 39.235 9.948   33.313  1.00 16.08 ? 266 PHE   A CG  1 
ATOM   1508 C  CD1 . PHE   A 1 192 ? 40.398 10.723  33.394  1.00 17.77 ? 266 PHE   A CD1 1 
ATOM   1509 C  CD2 . PHE   A 1 192 ? 38.471 9.754   34.436  1.00 17.15 ? 266 PHE   A CD2 1 
ATOM   1510 C  CE1 . PHE   A 1 192 ? 40.800 11.257  34.603  1.00 20.84 ? 266 PHE   A CE1 1 
ATOM   1511 C  CE2 . PHE   A 1 192 ? 38.928 10.248  35.692  1.00 18.35 ? 266 PHE   A CE2 1 
ATOM   1512 C  CZ  . PHE   A 1 192 ? 40.062 11.010  35.718  1.00 19.04 ? 266 PHE   A CZ  1 
ATOM   1513 N  N   . LEU   A 1 193 ? 38.490 10.365  28.649  1.00 10.09 ? 267 LEU   A N   1 
ATOM   1514 C  CA  . LEU   A 1 193 ? 38.449 9.909   27.271  1.00 10.63 ? 267 LEU   A CA  1 
ATOM   1515 C  C   . LEU   A 1 193 ? 39.825 9.348   26.949  1.00 10.44 ? 267 LEU   A C   1 
ATOM   1516 O  O   . LEU   A 1 193 ? 40.796 10.103  26.768  1.00 11.18 ? 267 LEU   A O   1 
ATOM   1517 C  CB  . LEU   A 1 193 ? 38.047 11.118  26.391  1.00 12.11 ? 267 LEU   A CB  1 
ATOM   1518 C  CG  . LEU   A 1 193 ? 37.885 10.794  24.916  1.00 12.95 ? 267 LEU   A CG  1 
ATOM   1519 C  CD1 . LEU   A 1 193 ? 36.708 9.878   24.711  1.00 14.90 ? 267 LEU   A CD1 1 
ATOM   1520 C  CD2 . LEU   A 1 193 ? 37.681 12.089  24.157  1.00 13.71 ? 267 LEU   A CD2 1 
ATOM   1521 N  N   . CYS   A 1 194 ? 39.920 8.030   26.902  1.00 10.21 ? 268 CYS   A N   1 
ATOM   1522 C  CA  . CYS   A 1 194 ? 41.184 7.384   26.669  1.00 11.41 ? 268 CYS   A CA  1 
ATOM   1523 C  C   . CYS   A 1 194 ? 41.574 7.421   25.203  1.00 11.90 ? 268 CYS   A C   1 
ATOM   1524 O  O   . CYS   A 1 194 ? 40.718 7.524   24.307  1.00 12.85 ? 268 CYS   A O   1 
ATOM   1525 C  CB  . CYS   A 1 194 ? 41.113 5.927   27.117  1.00 12.07 ? 268 CYS   A CB  1 
ATOM   1526 S  SG  . CYS   A 1 194 ? 41.015 5.784   28.907  1.00 14.53 ? 268 CYS   A SG  1 
ATOM   1527 N  N   . SER   A 1 195 ? 42.895 7.430   24.972  1.00 11.51 ? 269 SER   A N   1 
ATOM   1528 C  CA  . SER   A 1 195 ? 43.469 7.400   23.629  1.00 11.60 ? 269 SER   A CA  1 
ATOM   1529 C  C   . SER   A 1 195 ? 44.635 6.438   23.549  1.00 12.04 ? 269 SER   A C   1 
ATOM   1530 O  O   . SER   A 1 195 ? 45.427 6.323   24.471  1.00 11.73 ? 269 SER   A O   1 
ATOM   1531 C  CB  . SER   A 1 195 ? 43.998 8.749   23.294  1.00 12.16 ? 269 SER   A CB  1 
ATOM   1532 O  OG  . SER   A 1 195 ? 44.589 8.750   21.963  1.00 14.04 ? 269 SER   A OG  1 
ATOM   1533 N  N   . SER   A 1 196 ? 44.781 5.811   22.394  1.00 11.38 ? 270 SER   A N   1 
ATOM   1534 C  CA  . SER   A 1 196 ? 45.948 5.008   22.118  1.00 11.22 ? 270 SER   A CA  1 
ATOM   1535 C  C   . SER   A 1 196 ? 47.213 5.838   22.058  1.00 11.82 ? 270 SER   A C   1 
ATOM   1536 O  O   . SER   A 1 196 ? 48.302 5.294   22.223  1.00 12.12 ? 270 SER   A O   1 
ATOM   1537 C  CB  . SER   A 1 196 ? 45.833 4.234   20.820  1.00 11.97 ? 270 SER   A CB  1 
ATOM   1538 O  OG  . SER   A 1 196 ? 46.169 5.040   19.673  1.00 12.14 ? 270 SER   A OG  1 
ATOM   1539 N  N   . GLY   A 1 197 ? 47.080 7.119   21.716  1.00 11.66 ? 271 GLY   A N   1 
ATOM   1540 C  CA  . GLY   A 1 197 ? 48.165 8.031   21.449  1.00 11.86 ? 271 GLY   A CA  1 
ATOM   1541 C  C   . GLY   A 1 197 ? 48.717 7.992   20.035  1.00 12.02 ? 271 GLY   A C   1 
ATOM   1542 O  O   . GLY   A 1 197 ? 49.469 8.903   19.674  1.00 12.88 ? 271 GLY   A O   1 
ATOM   1543 N  N   . GLY   A 1 198 ? 48.402 6.946   19.294  1.00 12.33 ? 272 GLY   A N   1 
ATOM   1544 C  CA  . GLY   A 1 198 ? 48.822 6.879   17.899  1.00 13.37 ? 272 GLY   A CA  1 
ATOM   1545 C  C   . GLY   A 1 198 ? 50.284 6.527   17.735  1.00 14.11 ? 272 GLY   A C   1 
ATOM   1546 O  O   . GLY   A 1 198 ? 51.043 6.447   18.675  1.00 15.58 ? 272 GLY   A O   1 
ATOM   1547 N  N   . PRO   A 1 199 ? 50.729 6.384   16.464  1.00 15.66 ? 273 PRO   A N   1 
ATOM   1548 C  CA  . PRO   A 1 199 ? 52.093 5.892   16.196  1.00 16.77 ? 273 PRO   A CA  1 
ATOM   1549 C  C   . PRO   A 1 199 ? 53.171 6.927   16.454  1.00 18.14 ? 273 PRO   A C   1 
ATOM   1550 O  O   . PRO   A 1 199 ? 54.347 6.575   16.504  1.00 20.08 ? 273 PRO   A O   1 
ATOM   1551 C  CB  . PRO   A 1 199 ? 52.023 5.530   14.700  1.00 18.83 ? 273 PRO   A CB  1 
ATOM   1552 C  CG  . PRO   A 1 199 ? 50.941 6.392   14.160  1.00 19.20 ? 273 PRO   A CG  1 
ATOM   1553 C  CD  . PRO   A 1 199 ? 49.860 6.370   15.294  1.00 16.58 ? 273 PRO   A CD  1 
ATOM   1554 N  N   . PHE   A 1 200 ? 52.789 8.208   16.619  1.00 16.27 ? 274 PHE   A N   1 
ATOM   1555 C  CA  . PHE   A 1 200 ? 53.757 9.266   16.777  1.00 17.12 ? 274 PHE   A CA  1 
ATOM   1556 C  C   . PHE   A 1 200 ? 53.955 9.708   18.216  1.00 15.83 ? 274 PHE   A C   1 
ATOM   1557 O  O   . PHE   A 1 200 ? 54.602 10.689  18.527  1.00 17.35 ? 274 PHE   A O   1 
ATOM   1558 C  CB  . PHE   A 1 200 ? 53.407 10.474  15.908  1.00 17.06 ? 274 PHE   A CB  1 
ATOM   1559 C  CG  . PHE   A 1 200 ? 53.276 10.200  14.420  1.00 18.27 ? 274 PHE   A CG  1 
ATOM   1560 C  CD1 . PHE   A 1 200 ? 53.887 9.089   13.827  1.00 20.29 ? 274 PHE   A CD1 1 
ATOM   1561 C  CD2 . PHE   A 1 200 ? 52.525 11.025  13.615  1.00 17.99 ? 274 PHE   A CD2 1 
ATOM   1562 C  CE1 . PHE   A 1 200 ? 53.741 8.881   12.458  1.00 21.78 ? 274 PHE   A CE1 1 
ATOM   1563 C  CE2 . PHE   A 1 200 ? 52.428 10.815  12.250  1.00 20.62 ? 274 PHE   A CE2 1 
ATOM   1564 C  CZ  . PHE   A 1 200 ? 52.986 9.702   11.708  1.00 22.05 ? 274 PHE   A CZ  1 
ATOM   1565 N  N   . GLN   A 1 201 ? 53.310 8.982   19.162  1.00 16.47 ? 275 GLN   A N   1 
ATOM   1566 C  CA  . GLN   A 1 201 ? 53.199 9.439   20.526  1.00 17.32 ? 275 GLN   A CA  1 
ATOM   1567 C  C   . GLN   A 1 201 ? 54.531 9.690   21.203  1.00 17.02 ? 275 GLN   A C   1 
ATOM   1568 O  O   . GLN   A 1 201 ? 54.568 10.548  22.080  1.00 19.76 ? 275 GLN   A O   1 
ATOM   1569 C  CB  . GLN   A 1 201 ? 52.367 8.428   21.336  1.00 15.90 ? 275 GLN   A CB  1 
ATOM   1570 C  CG  . GLN   A 1 201 ? 51.986 8.941   22.712  1.00 15.28 ? 275 GLN   A CG  1 
ATOM   1571 C  CD  . GLN   A 1 201 ? 51.128 10.174  22.763  1.00 15.06 ? 275 GLN   A CD  1 
ATOM   1572 O  OE1 . GLN   A 1 201 ? 50.286 10.537  21.897  1.00 15.50 ? 275 GLN   A OE1 1 
ATOM   1573 N  NE2 . GLN   A 1 201 ? 51.312 10.838  23.870  1.00 13.75 ? 275 GLN   A NE2 1 
ATOM   1574 N  N   . ASN   A 1 202 ? 55.598 8.965   20.833  1.00 18.55 ? 276 ASN   A N   1 
ATOM   1575 C  CA  . ASN   A 1 202 ? 56.881 9.079   21.508  1.00 20.18 ? 276 ASN   A CA  1 
ATOM   1576 C  C   . ASN   A 1 202 ? 57.934 9.852   20.707  1.00 22.82 ? 276 ASN   A C   1 
ATOM   1577 O  O   . ASN   A 1 202 ? 59.118 9.867   21.080  1.00 23.17 ? 276 ASN   A O   1 
ATOM   1578 C  CB  . ASN   A 1 202 ? 57.452 7.710   21.868  1.00 24.31 ? 276 ASN   A CB  1 
ATOM   1579 C  CG  . ASN   A 1 202 ? 56.516 6.925   22.753  1.00 28.18 ? 276 ASN   A CG  1 
ATOM   1580 O  OD1 . ASN   A 1 202 ? 55.797 7.490   23.585  1.00 29.97 ? 276 ASN   A OD1 1 
ATOM   1581 N  ND2 . ASN   A 1 202 ? 56.493 5.618   22.552  1.00 37.15 ? 276 ASN   A ND2 1 
ATOM   1582 N  N   . LEU   A 1 203 ? 57.518 10.518  19.636  1.00 19.74 ? 277 LEU   A N   1 
ATOM   1583 C  CA  . LEU   A 1 203 ? 58.466 11.216  18.765  1.00 20.80 ? 277 LEU   A CA  1 
ATOM   1584 C  C   . LEU   A 1 203 ? 58.765 12.585  19.354  1.00 22.34 ? 277 LEU   A C   1 
ATOM   1585 O  O   . LEU   A 1 203 ? 57.941 13.234  19.964  1.00 22.61 ? 277 LEU   A O   1 
ATOM   1586 C  CB  . LEU   A 1 203 ? 57.928 11.315  17.350  1.00 20.44 ? 277 LEU   A CB  1 
ATOM   1587 C  CG  . LEU   A 1 203 ? 57.688 10.014  16.593  1.00 21.03 ? 277 LEU   A CG  1 
ATOM   1588 C  CD1 . LEU   A 1 203 ? 57.225 10.297  15.213  1.00 20.69 ? 277 LEU   A CD1 1 
ATOM   1589 C  CD2 . LEU   A 1 203 ? 58.914 9.088   16.599  1.00 22.40 ? 277 LEU   A CD2 1 
ATOM   1590 N  N   . THR   A 1 204 ? 59.959 13.112  19.054  1.00 23.79 ? 278 THR   A N   1 
ATOM   1591 C  CA  . THR   A 1 204 ? 60.332 14.476  19.395  1.00 23.08 ? 278 THR   A CA  1 
ATOM   1592 C  C   . THR   A 1 204 ? 59.702 15.449  18.395  1.00 20.24 ? 278 THR   A C   1 
ATOM   1593 O  O   . THR   A 1 204 ? 59.244 15.054  17.324  1.00 20.03 ? 278 THR   A O   1 
ATOM   1594 C  CB  . THR   A 1 204 ? 61.858 14.618  19.387  1.00 24.71 ? 278 THR   A CB  1 
ATOM   1595 O  OG1 . THR   A 1 204 ? 62.254 14.467  18.022  1.00 25.57 ? 278 THR   A OG1 1 
ATOM   1596 C  CG2 . THR   A 1 204 ? 62.551 13.584  20.257  1.00 25.27 ? 278 THR   A CG2 1 
ATOM   1597 N  N   . MET   A 1 205 ? 59.713 16.728  18.756  1.00 20.75 ? 279 MET   A N   1 
ATOM   1598 C  CA  . MET   A 1 205 ? 59.311 17.789  17.849  1.00 22.21 ? 279 MET   A CA  1 
ATOM   1599 C  C   . MET   A 1 205 ? 60.085 17.725  16.529  1.00 22.55 ? 279 MET   A C   1 
ATOM   1600 O  O   . MET   A 1 205 ? 59.487 17.846  15.465  1.00 22.68 ? 279 MET   A O   1 
ATOM   1601 C  CB  . MET   A 1 205 ? 59.438 19.175  18.479  1.00 23.45 ? 279 MET   A CB  1 
ATOM   1602 C  CG  . MET   A 1 205 ? 58.449 19.446  19.600  1.00 23.82 ? 279 MET   A CG  1 
ATOM   1603 S  SD  . MET   A 1 205 ? 56.702 19.457  19.124  1.00 22.27 ? 279 MET   A SD  1 
ATOM   1604 C  CE  . MET   A 1 205 ? 56.645 21.014  18.230  1.00 22.84 ? 279 MET   A CE  1 
ATOM   1605 N  N   . ASP   A 1 206 ? 61.403 17.516  16.594  1.00 23.46 ? 280 ASP   A N   1 
ATOM   1606 C  CA  . ASP   A 1 206 ? 62.218 17.422  15.391  1.00 24.06 ? 280 ASP   A CA  1 
ATOM   1607 C  C   . ASP   A 1 206 ? 61.801 16.245  14.519  1.00 22.92 ? 280 ASP   A C   1 
ATOM   1608 O  O   . ASP   A 1 206 ? 61.720 16.347  13.290  1.00 24.24 ? 280 ASP   A O   1 
ATOM   1609 C  CB  . ASP   A 1 206 ? 63.696 17.323  15.736  1.00 28.44 ? 280 ASP   A CB  1 
ATOM   1610 C  CG  . ASP   A 1 206 ? 64.341 18.596  16.269  1.00 32.40 ? 280 ASP   A CG  1 
ATOM   1611 O  OD1 . ASP   A 1 206 ? 63.727 19.642  16.118  1.00 33.24 ? 280 ASP   A OD1 1 
ATOM   1612 O  OD2 . ASP   A 1 206 ? 65.446 18.504  16.867  1.00 35.73 ? 280 ASP   A OD2 1 
ATOM   1613 N  N   . GLU   A 1 207 ? 61.466 15.110  15.160  1.00 21.04 ? 281 GLU   A N   1 
ATOM   1614 C  CA  . GLU   A 1 207 ? 61.000 13.970  14.397  1.00 20.88 ? 281 GLU   A CA  1 
ATOM   1615 C  C   . GLU   A 1 207 ? 59.628 14.219  13.782  1.00 20.25 ? 281 GLU   A C   1 
ATOM   1616 O  O   . GLU   A 1 207 ? 59.370 13.831  12.652  1.00 21.76 ? 281 GLU   A O   1 
ATOM   1617 C  CB  . GLU   A 1 207 ? 60.973 12.754  15.323  1.00 22.34 ? 281 GLU   A CB  1 
ATOM   1618 C  CG  . GLU   A 1 207 ? 62.377 12.247  15.636  1.00 24.66 ? 281 GLU   A CG  1 
ATOM   1619 C  CD  . GLU   A 1 207 ? 62.371 11.069  16.593  1.00 26.30 ? 281 GLU   A CD  1 
ATOM   1620 O  OE1 . GLU   A 1 207 ? 61.689 11.121  17.638  1.00 25.26 ? 281 GLU   A OE1 1 
ATOM   1621 O  OE2 . GLU   A 1 207 ? 63.054 10.055  16.298  1.00 30.91 ? 281 GLU   A OE2 1 
ATOM   1622 N  N   . LEU   A 1 208 ? 58.692 14.815  14.560  1.00 20.66 ? 282 LEU   A N   1 
ATOM   1623 C  CA  . LEU   A 1 208 ? 57.349 15.110  14.047  1.00 21.16 ? 282 LEU   A CA  1 
ATOM   1624 C  C   . LEU   A 1 208 ? 57.365 15.995  12.825  1.00 22.29 ? 282 LEU   A C   1 
ATOM   1625 O  O   . LEU   A 1 208 ? 56.545 15.881  11.907  1.00 23.46 ? 282 LEU   A O   1 
ATOM   1626 C  CB  . LEU   A 1 208 ? 56.459 15.767  15.080  1.00 21.02 ? 282 LEU   A CB  1 
ATOM   1627 C  CG  . LEU   A 1 208 ? 55.962 14.853  16.191  1.00 20.17 ? 282 LEU   A CG  1 
ATOM   1628 C  CD1 . LEU   A 1 208 ? 55.354 15.632  17.297  1.00 19.99 ? 282 LEU   A CD1 1 
ATOM   1629 C  CD2 . LEU   A 1 208 ? 54.943 13.844  15.659  1.00 19.12 ? 282 LEU   A CD2 1 
ATOM   1630 N  N   . LYS   A 1 209 ? 58.320 16.920  12.771  1.00 22.98 ? 283 LYS   A N   1 
ATOM   1631 C  CA  . LYS   A 1 209 ? 58.338 17.847  11.651  1.00 23.38 ? 283 LYS   A CA  1 
ATOM   1632 C  C   . LYS   A 1 209 ? 58.306 17.071  10.337  1.00 23.41 ? 283 LYS   A C   1 
ATOM   1633 O  O   . LYS   A 1 209 ? 57.678 17.515  9.370   1.00 24.25 ? 283 LYS   A O   1 
ATOM   1634 C  CB  . LYS   A 1 209 ? 59.555 18.772  11.756  1.00 26.46 ? 283 LYS   A CB  1 
ATOM   1635 C  CG  . LYS   A 1 209 ? 59.652 19.856  10.672  1.00 34.63 ? 283 LYS   A CG  1 
ATOM   1636 C  CD  . LYS   A 1 209 ? 60.951 20.664  10.749  1.00 37.04 ? 283 LYS   A CD  1 
ATOM   1637 C  CE  . LYS   A 1 209 ? 61.284 21.187  12.133  1.00 42.73 ? 283 LYS   A CE  1 
ATOM   1638 N  NZ  . LYS   A 1 209 ? 62.419 22.124  12.142  1.00 47.48 ? 283 LYS   A NZ  1 
ATOM   1639 N  N   . ASN   A 1 210 ? 58.996 15.909  10.299  1.00 22.92 ? 284 ASN   A N   1 
ATOM   1640 C  CA  . ASN   A 1 210 ? 59.270 15.202  9.056   1.00 22.71 ? 284 ASN   A CA  1 
ATOM   1641 C  C   . ASN   A 1 210 ? 58.570 13.851  8.903   1.00 23.39 ? 284 ASN   A C   1 
ATOM   1642 O  O   . ASN   A 1 210 ? 58.791 13.128  7.935   1.00 24.07 ? 284 ASN   A O   1 
ATOM   1643 C  CB  . ASN   A 1 210 ? 60.780 15.047  8.917   1.00 27.71 ? 284 ASN   A CB  1 
ATOM   1644 C  CG  . ASN   A 1 210 ? 61.398 16.403  8.682   1.00 30.72 ? 284 ASN   A CG  1 
ATOM   1645 O  OD1 . ASN   A 1 210 ? 62.173 16.879  9.520   1.00 38.17 ? 284 ASN   A OD1 1 
ATOM   1646 N  ND2 . ASN   A 1 210 ? 60.929 17.069  7.645   1.00 30.61 ? 284 ASN   A ND2 1 
ATOM   1647 N  N   . VAL   A 1 211 ? 57.618 13.526  9.799   1.00 20.41 ? 285 VAL   A N   1 
ATOM   1648 C  CA  . VAL   A 1 211 ? 56.859 12.292  9.656   1.00 20.47 ? 285 VAL   A CA  1 
ATOM   1649 C  C   . VAL   A 1 211 ? 56.038 12.290  8.367   1.00 20.15 ? 285 VAL   A C   1 
ATOM   1650 O  O   . VAL   A 1 211 ? 55.532 13.318  7.928   1.00 20.75 ? 285 VAL   A O   1 
ATOM   1651 C  CB  . VAL   A 1 211 ? 55.957 11.934  10.863  1.00 20.56 ? 285 VAL   A CB  1 
ATOM   1652 C  CG1 . VAL   A 1 211 ? 56.744 11.582  12.108  1.00 22.96 ? 285 VAL   A CG1 1 
ATOM   1653 C  CG2 . VAL   A 1 211 ? 54.902 13.009  11.159  1.00 19.71 ? 285 VAL   A CG2 1 
ATOM   1654 N  N   . THR   A 1 212 ? 55.744 11.094  7.865   1.00 21.93 ? 286 THR   A N   1 
ATOM   1655 C  CA  . THR   A 1 212 ? 54.996 10.894  6.643   1.00 22.98 ? 286 THR   A CA  1 
ATOM   1656 C  C   . THR   A 1 212 ? 53.730 10.099  6.908   1.00 20.30 ? 286 THR   A C   1 
ATOM   1657 O  O   . THR   A 1 212 ? 53.622 9.409   7.928   1.00 20.72 ? 286 THR   A O   1 
ATOM   1658 C  CB  . THR   A 1 212 ? 55.831 10.177  5.583   1.00 26.18 ? 286 THR   A CB  1 
ATOM   1659 O  OG1 . THR   A 1 212 ? 55.955 8.844   6.060   1.00 29.11 ? 286 THR   A OG1 1 
ATOM   1660 C  CG2 . THR   A 1 212 ? 57.192 10.823  5.407   1.00 29.23 ? 286 THR   A CG2 1 
ATOM   1661 N  N   . SER   A 1 213 ? 52.840 10.099  5.927   1.00 19.74 ? 287 SER   A N   1 
ATOM   1662 C  CA  . SER   A 1 213 ? 51.633 9.318   6.022   1.00 20.06 ? 287 SER   A CA  1 
ATOM   1663 C  C   . SER   A 1 213 ? 51.945 7.828   5.990   1.00 20.66 ? 287 SER   A C   1 
ATOM   1664 O  O   . SER   A 1 213 ? 51.258 7.078   6.643   1.00 20.48 ? 287 SER   A O   1 
ATOM   1665 C  CB  . SER   A 1 213 ? 50.601 9.681   5.021   1.00 22.07 ? 287 SER   A CB  1 
ATOM   1666 O  OG  . SER   A 1 213 ? 51.090 9.415   3.712   1.00 21.91 ? 287 SER   A OG  1 
ATOM   1667 N  N   . GLU   A 1 214 ? 53.000 7.401   5.278   1.00 22.11 ? 288 GLU   A N   1 
ATOM   1668 C  CA  . GLU   A 1 214 ? 53.380 5.998   5.315   1.00 23.37 ? 288 GLU   A CA  1 
ATOM   1669 C  C   . GLU   A 1 214 ? 53.676 5.577   6.753   1.00 23.43 ? 288 GLU   A C   1 
ATOM   1670 O  O   . GLU   A 1 214 ? 53.249 4.500   7.172   1.00 22.55 ? 288 GLU   A O   1 
ATOM   1671 C  CB  . GLU   A 1 214 ? 54.581 5.765   4.390   1.00 26.35 ? 288 GLU   A CB  1 
ATOM   1672 C  CG  . GLU   A 1 214 ? 55.100 4.337   4.413   1.00 33.52 ? 288 GLU   A CG  1 
ATOM   1673 C  CD  . GLU   A 1 214 ? 56.331 4.104   3.555   1.00 39.55 ? 288 GLU   A CD  1 
ATOM   1674 O  OE1 . GLU   A 1 214 ? 56.804 5.023   2.855   1.00 42.35 ? 288 GLU   A OE1 1 
ATOM   1675 O  OE2 . GLU   A 1 214 ? 56.818 2.959   3.618   1.00 50.05 ? 288 GLU   A OE2 1 
ATOM   1676 N  N   . ASN   A 1 215 ? 54.369 6.443   7.497   1.00 21.74 ? 289 ASN   A N   1 
ATOM   1677 C  CA  . ASN   A 1 215 ? 54.681 6.166   8.886   1.00 22.47 ? 289 ASN   A CA  1 
ATOM   1678 C  C   . ASN   A 1 215 ? 53.391 6.041   9.717   1.00 22.37 ? 289 ASN   A C   1 
ATOM   1679 O  O   . ASN   A 1 215 ? 53.319 5.227   10.647  1.00 24.18 ? 289 ASN   A O   1 
ATOM   1680 C  CB  . ASN   A 1 215 ? 55.514 7.268   9.545   1.00 25.49 ? 289 ASN   A CB  1 
ATOM   1681 C  CG  . ASN   A 1 215 ? 56.849 7.583   8.897   1.00 28.26 ? 289 ASN   A CG  1 
ATOM   1682 O  OD1 . ASN   A 1 215 ? 57.534 6.676   8.376   1.00 31.14 ? 289 ASN   A OD1 1 
ATOM   1683 N  ND2 . ASN   A 1 215 ? 57.329 8.813   9.057   1.00 24.33 ? 289 ASN   A ND2 1 
ATOM   1684 N  N   . ALA   A 1 216 ? 52.389 6.861   9.418   1.00 20.59 ? 290 ALA   A N   1 
ATOM   1685 C  CA  . ALA   A 1 216 ? 51.131 6.869   10.172  1.00 21.27 ? 290 ALA   A CA  1 
ATOM   1686 C  C   . ALA   A 1 216 ? 50.312 5.608   9.880   1.00 21.78 ? 290 ALA   A C   1 
ATOM   1687 O  O   . ALA   A 1 216 ? 49.580 5.139   10.766  1.00 23.16 ? 290 ALA   A O   1 
ATOM   1688 C  CB  . ALA   A 1 216 ? 50.349 8.131   9.866   1.00 21.74 ? 290 ALA   A CB  1 
ATOM   1689 N  N   . LEU   A 1 217 ? 50.398 5.025   8.673   1.00 22.96 ? 291 LEU   A N   1 
ATOM   1690 C  CA  . LEU   A 1 217 ? 49.507 3.964   8.243   1.00 24.59 ? 291 LEU   A CA  1 
ATOM   1691 C  C   . LEU   A 1 217 ? 50.051 2.573   8.547   1.00 27.84 ? 291 LEU   A C   1 
ATOM   1692 O  O   . LEU   A 1 217 ? 49.278 1.618   8.513   1.00 28.02 ? 291 LEU   A O   1 
ATOM   1693 C  CB  . LEU   A 1 217 ? 49.249 4.066   6.740   1.00 24.94 ? 291 LEU   A CB  1 
ATOM   1694 C  CG  . LEU   A 1 217 ? 48.458 5.292   6.265   1.00 26.49 ? 291 LEU   A CG  1 
ATOM   1695 C  CD1 . LEU   A 1 217 ? 48.400 5.310   4.760   1.00 31.03 ? 291 LEU   A CD1 1 
ATOM   1696 C  CD2 . LEU   A 1 217 ? 47.056 5.339   6.805   1.00 26.84 ? 291 LEU   A CD2 1 
ATOM   1697 N  N   . LYS   A 1 218 ? 51.358 2.429   8.755   1.00 30.65 ? 292 LYS   A N   1 
ATOM   1698 C  CA  . LYS   A 1 218 ? 51.952 1.091   8.753   1.00 35.12 ? 292 LYS   A CA  1 
ATOM   1699 C  C   . LYS   A 1 218 ? 51.573 0.298   10.015  1.00 39.82 ? 292 LYS   A C   1 
ATOM   1700 O  O   . LYS   A 1 218 ? 51.405 0.873   11.095  1.00 36.25 ? 292 LYS   A O   1 
ATOM   1701 C  CB  . LYS   A 1 218 ? 53.463 1.281   8.582   1.00 42.54 ? 292 LYS   A CB  1 
ATOM   1702 C  CG  . LYS   A 1 218 ? 54.145 1.766   9.858   1.00 48.32 ? 292 LYS   A CG  1 
ATOM   1703 C  CD  . LYS   A 1 218 ? 55.618 2.142   9.733   1.00 55.60 ? 292 LYS   A CD  1 
ATOM   1704 C  CE  . LYS   A 1 218 ? 56.173 2.605   11.055  1.00 60.59 ? 292 LYS   A CE  1 
ATOM   1705 N  NZ  . LYS   A 1 218 ? 57.227 3.611   10.891  1.00 60.46 ? 292 LYS   A NZ  1 
ATOM   1706 N  N   . HIS   A 1 219 ? 51.390 -1.027  9.839   1.00 39.20 ? 293 HIS   A N   1 
ATOM   1707 C  CA  . HIS   A 1 219 ? 51.299 -2.029  10.907  1.00 46.10 ? 293 HIS   A CA  1 
ATOM   1708 C  C   . HIS   A 1 219 ? 50.200 -1.715  11.925  1.00 42.86 ? 293 HIS   A C   1 
ATOM   1709 O  O   . HIS   A 1 219 ? 50.443 -1.661  13.135  1.00 45.94 ? 293 HIS   A O   1 
ATOM   1710 C  CB  . HIS   A 1 219 ? 52.666 -2.263  11.570  1.00 52.71 ? 293 HIS   A CB  1 
ATOM   1711 C  CG  . HIS   A 1 219 ? 53.729 -2.653  10.588  1.00 61.70 ? 293 HIS   A CG  1 
ATOM   1712 N  ND1 . HIS   A 1 219 ? 55.033 -2.201  10.657  1.00 67.12 ? 293 HIS   A ND1 1 
ATOM   1713 C  CD2 . HIS   A 1 219 ? 53.663 -3.418  9.485   1.00 65.03 ? 293 HIS   A CD2 1 
ATOM   1714 C  CE1 . HIS   A 1 219 ? 55.726 -2.697  9.637   1.00 63.64 ? 293 HIS   A CE1 1 
ATOM   1715 N  NE2 . HIS   A 1 219 ? 54.914 -3.437  8.914   1.00 66.87 ? 293 HIS   A NE2 1 
ATOM   1716 N  N   . PRO   A 1 220 ? 48.938 -1.553  11.473  1.00 41.14 ? 294 PRO   A N   1 
ATOM   1717 C  CA  . PRO   A 1 220 ? 47.810 -1.325  12.394  1.00 40.43 ? 294 PRO   A CA  1 
ATOM   1718 C  C   . PRO   A 1 220 ? 47.424 -2.562  13.210  1.00 40.23 ? 294 PRO   A C   1 
ATOM   1719 O  O   . PRO   A 1 220 ? 47.589 -3.691  12.740  1.00 36.98 ? 294 PRO   A O   1 
ATOM   1720 C  CB  . PRO   A 1 220 ? 46.684 -0.919  11.431  1.00 38.87 ? 294 PRO   A CB  1 
ATOM   1721 C  CG  . PRO   A 1 220 ? 47.027 -1.663  10.140  1.00 39.61 ? 294 PRO   A CG  1 
ATOM   1722 C  CD  . PRO   A 1 220 ? 48.540 -1.565  10.051  1.00 39.82 ? 294 PRO   A CD  1 
ATOM   1723 N  N   . LYS   A 1 221 ? 46.870 -2.349  14.413  1.00 35.27 ? 295 LYS   A N   1 
ATOM   1724 C  CA  . LYS   A 1 221 ? 46.379 -3.462  15.223  1.00 32.09 ? 295 LYS   A CA  1 
ATOM   1725 C  C   . LYS   A 1 221 ? 45.283 -4.210  14.459  1.00 34.21 ? 295 LYS   A C   1 
ATOM   1726 O  O   . LYS   A 1 221 ? 45.332 -5.441  14.333  1.00 39.91 ? 295 LYS   A O   1 
ATOM   1727 C  CB  . LYS   A 1 221 ? 45.850 -2.959  16.569  1.00 32.30 ? 295 LYS   A CB  1 
ATOM   1728 C  CG  . LYS   A 1 221 ? 45.411 -4.060  17.536  1.00 34.13 ? 295 LYS   A CG  1 
ATOM   1729 C  CD  . LYS   A 1 221 ? 46.545 -4.902  18.129  1.00 35.26 ? 295 LYS   A CD  1 
ATOM   1730 C  CE  . LYS   A 1 221 ? 46.014 -6.023  18.987  1.00 38.96 ? 295 LYS   A CE  1 
ATOM   1731 N  NZ  . LYS   A 1 221 ? 45.369 -7.058  18.165  1.00 40.14 ? 295 LYS   A NZ  1 
ATOM   1732 N  N   . TRP   A 1 222 ? 44.252 -3.470  14.019  1.00 32.37 ? 296 TRP   A N   1 
ATOM   1733 C  CA  . TRP   A 1 222 ? 43.363 -3.915  12.958  1.00 32.07 ? 296 TRP   A CA  1 
ATOM   1734 C  C   . TRP   A 1 222 ? 43.355 -2.796  11.930  1.00 31.94 ? 296 TRP   A C   1 
ATOM   1735 O  O   . TRP   A 1 222 ? 43.503 -1.636  12.302  1.00 34.49 ? 296 TRP   A O   1 
ATOM   1736 C  CB  . TRP   A 1 222 ? 41.946 -4.254  13.463  1.00 29.32 ? 296 TRP   A CB  1 
ATOM   1737 C  CG  . TRP   A 1 222 ? 41.150 -3.075  13.977  1.00 27.24 ? 296 TRP   A CG  1 
ATOM   1738 C  CD1 . TRP   A 1 222 ? 40.175 -2.386  13.313  1.00 26.34 ? 296 TRP   A CD1 1 
ATOM   1739 C  CD2 . TRP   A 1 222 ? 41.216 -2.500  15.307  1.00 28.31 ? 296 TRP   A CD2 1 
ATOM   1740 N  NE1 . TRP   A 1 222 ? 39.650 -1.387  14.104  1.00 25.11 ? 296 TRP   A NE1 1 
ATOM   1741 C  CE2 . TRP   A 1 222 ? 40.279 -1.434  15.320  1.00 27.37 ? 296 TRP   A CE2 1 
ATOM   1742 C  CE3 . TRP   A 1 222 ? 41.976 -2.762  16.469  1.00 27.64 ? 296 TRP   A CE3 1 
ATOM   1743 C  CZ2 . TRP   A 1 222 ? 40.082 -0.646  16.450  1.00 29.46 ? 296 TRP   A CZ2 1 
ATOM   1744 C  CZ3 . TRP   A 1 222 ? 41.750 -1.983  17.585  1.00 30.28 ? 296 TRP   A CZ3 1 
ATOM   1745 C  CH2 . TRP   A 1 222 ? 40.787 -0.977  17.588  1.00 28.84 ? 296 TRP   A CH2 1 
ATOM   1746 N  N   . LYS   A 1 223 ? 43.216 -3.146  10.649  1.00 31.02 ? 297 LYS   A N   1 
ATOM   1747 C  CA  . LYS   A 1 223 ? 43.243 -2.145  9.595   1.00 31.68 ? 297 LYS   A CA  1 
ATOM   1748 C  C   . LYS   A 1 223 ? 41.999 -1.278  9.729   1.00 28.63 ? 297 LYS   A C   1 
ATOM   1749 O  O   . LYS   A 1 223 ? 40.859 -1.770  9.698   1.00 28.39 ? 297 LYS   A O   1 
ATOM   1750 C  CB  . LYS   A 1 223 ? 43.306 -2.721  8.180   1.00 34.39 ? 297 LYS   A CB  1 
ATOM   1751 C  CG  . LYS   A 1 223 ? 43.494 -1.628  7.104   1.00 39.83 ? 297 LYS   A CG  1 
ATOM   1752 C  CD  . LYS   A 1 223 ? 43.448 -2.131  5.662   1.00 48.48 ? 297 LYS   A CD  1 
ATOM   1753 C  CE  . LYS   A 1 223 ? 42.147 -2.799  5.311   1.00 53.88 ? 297 LYS   A CE  1 
ATOM   1754 N  NZ  . LYS   A 1 223 ? 41.978 -3.044  3.872   1.00 57.12 ? 297 LYS   A NZ  1 
ATOM   1755 N  N   . MET   A 1 224 ? 42.240 0.017   9.970   1.00 20.52 ? 298 MET   A N   1 
ATOM   1756 C  CA  . MET   A 1 224 ? 41.138 0.959   9.971   1.00 18.17 ? 298 MET   A CA  1 
ATOM   1757 C  C   . MET   A 1 224 ? 41.219 1.724   8.687   1.00 17.20 ? 298 MET   A C   1 
ATOM   1758 O  O   . MET   A 1 224 ? 42.237 1.679   7.996   1.00 18.94 ? 298 MET   A O   1 
ATOM   1759 C  CB  . MET   A 1 224 ? 41.274 1.947   11.121  1.00 16.15 ? 298 MET   A CB  1 
ATOM   1760 C  CG  . MET   A 1 224 ? 41.293 1.292   12.425  1.00 17.21 ? 298 MET   A CG  1 
ATOM   1761 S  SD  . MET   A 1 224 ? 41.148 2.387   13.840  1.00 19.45 ? 298 MET   A SD  1 
ATOM   1762 C  CE  . MET   A 1 224 ? 42.596 3.353   13.633  1.00 18.52 ? 298 MET   A CE  1 
ATOM   1763 N  N   . GLY   A 1 225 ? 40.166 2.425   8.369   1.00 16.77 ? 299 GLY   A N   1 
ATOM   1764 C  CA  . GLY   A 1 225 ? 40.197 3.262   7.205   1.00 16.71 ? 299 GLY   A CA  1 
ATOM   1765 C  C   . GLY   A 1 225 ? 41.289 4.315   7.254   1.00 15.85 ? 299 GLY   A C   1 
ATOM   1766 O  O   . GLY   A 1 225 ? 41.829 4.669   8.326   1.00 15.67 ? 299 GLY   A O   1 
ATOM   1767 N  N   . LYS   A 1 226 ? 41.689 4.790   6.094   1.00 16.30 ? 300 LYS   A N   1 
ATOM   1768 C  CA  . LYS   A 1 226 ? 42.805 5.706   5.996   1.00 16.06 ? 300 LYS   A CA  1 
ATOM   1769 C  C   . LYS   A 1 226 ? 42.524 7.018   6.740   1.00 15.11 ? 300 LYS   A C   1 
ATOM   1770 O  O   . LYS   A 1 226 ? 43.449 7.543   7.352   1.00 16.24 ? 300 LYS   A O   1 
ATOM   1771 C  CB  . LYS   A 1 226 ? 43.151 5.983   4.537   1.00 18.60 ? 300 LYS   A CB  1 
ATOM   1772 C  CG  . LYS   A 1 226 ? 43.709 4.769   3.834   1.00 21.79 ? 300 LYS   A CG  1 
ATOM   1773 C  CD  . LYS   A 1 226 ? 43.998 5.087   2.376   1.00 26.32 ? 300 LYS   A CD  1 
ATOM   1774 C  CE  . LYS   A 1 226 ? 44.399 3.912   1.540   1.00 32.41 ? 300 LYS   A CE  1 
ATOM   1775 N  NZ  . LYS   A 1 226 ? 45.681 3.456   2.056   1.00 35.36 ? 300 LYS   A NZ  1 
ATOM   1776 N  N   . LYS   A 1 227 ? 41.291 7.518   6.693   1.00 14.68 ? 301 LYS   A N   1 
ATOM   1777 C  CA  . LYS   A 1 227 ? 41.022 8.824   7.287   1.00 14.96 ? 301 LYS   A CA  1 
ATOM   1778 C  C   . LYS   A 1 227 ? 41.215 8.803   8.806   1.00 13.20 ? 301 LYS   A C   1 
ATOM   1779 O  O   . LYS   A 1 227 ? 41.968 9.579   9.372   1.00 13.63 ? 301 LYS   A O   1 
ATOM   1780 C  CB  . LYS   A 1 227 ? 39.647 9.252   6.814   1.00 16.15 ? 301 LYS   A CB  1 
ATOM   1781 C  CG  . LYS   A 1 227 ? 39.337 10.740  6.963   1.00 18.33 ? 301 LYS   A CG  1 
ATOM   1782 C  CD  . LYS   A 1 227 ? 39.010 11.146  8.382   1.00 17.68 ? 301 LYS   A CD  1 
ATOM   1783 C  CE  . LYS   A 1 227 ? 38.462 12.579  8.399   1.00 16.70 ? 301 LYS   A CE  1 
ATOM   1784 N  NZ  . LYS   A 1 227 ? 37.988 12.921  9.740   1.00 15.20 ? 301 LYS   A NZ  1 
ATOM   1785 N  N   . ILE   A 1 228 ? 40.563 7.815   9.460   1.00 12.80 ? 302 ILE   A N   1 
ATOM   1786 C  CA  . ILE   A 1 228 ? 40.679 7.719   10.910  1.00 12.65 ? 302 ILE   A CA  1 
ATOM   1787 C  C   . ILE   A 1 228 ? 42.108 7.410   11.282  1.00 13.37 ? 302 ILE   A C   1 
ATOM   1788 O  O   . ILE   A 1 228 ? 42.598 7.877   12.337  1.00 13.76 ? 302 ILE   A O   1 
ATOM   1789 C  CB  . ILE   A 1 228 ? 39.667 6.749   11.542  1.00 12.82 ? 302 ILE   A CB  1 
ATOM   1790 C  CG1 . ILE   A 1 228 ? 39.679 6.843   13.072  1.00 15.48 ? 302 ILE   A CG1 1 
ATOM   1791 C  CG2 . ILE   A 1 228 ? 39.875 5.305   11.116  1.00 14.19 ? 302 ILE   A CG2 1 
ATOM   1792 C  CD1 . ILE   A 1 228 ? 38.453 6.227   13.711  1.00 16.46 ? 302 ILE   A CD1 1 
ATOM   1793 N  N   . THR   A 1 229 ? 42.816 6.599   10.477  1.00 13.21 ? 303 THR   A N   1 
ATOM   1794 C  CA  . THR   A 1 229 ? 44.178 6.276   10.825  1.00 13.68 ? 303 THR   A CA  1 
ATOM   1795 C  C   . THR   A 1 229 ? 45.051 7.529   10.889  1.00 13.27 ? 303 THR   A C   1 
ATOM   1796 O  O   . THR   A 1 229 ? 45.871 7.705   11.781  1.00 13.53 ? 303 THR   A O   1 
ATOM   1797 C  CB  . THR   A 1 229 ? 44.748 5.253   9.845   1.00 16.14 ? 303 THR   A CB  1 
ATOM   1798 O  OG1 . THR   A 1 229 ? 43.913 4.091   9.896   1.00 17.13 ? 303 THR   A OG1 1 
ATOM   1799 C  CG2 . THR   A 1 229 ? 46.135 4.831   10.242  1.00 17.29 ? 303 THR   A CG2 1 
ATOM   1800 N  N   . ILE   A 1 230 ? 44.914 8.426   9.903   1.00 13.29 ? 304 ILE   A N   1 
ATOM   1801 C  CA  . ILE   A 1 230 ? 45.654 9.683   9.962   1.00 13.15 ? 304 ILE   A CA  1 
ATOM   1802 C  C   . ILE   A 1 230 ? 45.217 10.542  11.160  1.00 12.90 ? 304 ILE   A C   1 
ATOM   1803 O  O   . ILE   A 1 230 ? 46.075 11.132  11.828  1.00 13.25 ? 304 ILE   A O   1 
ATOM   1804 C  CB  . ILE   A 1 230 ? 45.541 10.450  8.623   1.00 14.59 ? 304 ILE   A CB  1 
ATOM   1805 C  CG1 . ILE   A 1 230 ? 46.145 9.707   7.407   1.00 16.33 ? 304 ILE   A CG1 1 
ATOM   1806 C  CG2 . ILE   A 1 230 ? 46.120 11.864  8.718   1.00 14.54 ? 304 ILE   A CG2 1 
ATOM   1807 C  CD1 . ILE   A 1 230 ? 47.593 9.379   7.548   1.00 18.40 ? 304 ILE   A CD1 1 
ATOM   1808 N  N   . ASP   A 1 231 ? 43.926 10.596  11.424  1.00 12.29 ? 305 ASP   A N   1 
ATOM   1809 C  CA  . ASP   A 1 231 ? 43.466 11.363  12.589  1.00 12.28 ? 305 ASP   A CA  1 
ATOM   1810 C  C   . ASP   A 1 231 ? 43.988 10.793  13.912  1.00 11.49 ? 305 ASP   A C   1 
ATOM   1811 O  O   . ASP   A 1 231 ? 44.221 11.559  14.852  1.00 12.01 ? 305 ASP   A O   1 
ATOM   1812 C  CB  . ASP   A 1 231 ? 41.959 11.444  12.595  1.00 12.72 ? 305 ASP   A CB  1 
ATOM   1813 C  CG  . ASP   A 1 231 ? 41.271 12.411  11.632  1.00 13.69 ? 305 ASP   A CG  1 
ATOM   1814 O  OD1 . ASP   A 1 231 ? 41.988 13.260  11.057  1.00 13.90 ? 305 ASP   A OD1 1 
ATOM   1815 O  OD2 . ASP   A 1 231 ? 40.049 12.256  11.513  1.00 15.73 ? 305 ASP   A OD2 1 
ATOM   1816 N  N   . SER   A 1 232 ? 44.190 9.487   14.015  1.00 11.47 ? 306 SER   A N   1 
ATOM   1817 C  CA  . SER   A 1 232 ? 44.805 8.921   15.201  1.00 11.64 ? 306 SER   A CA  1 
ATOM   1818 C  C   . SER   A 1 232 ? 46.247 9.407   15.323  1.00 11.63 ? 306 SER   A C   1 
ATOM   1819 O  O   . SER   A 1 232 ? 46.715 9.709   16.414  1.00 12.14 ? 306 SER   A O   1 
ATOM   1820 C  CB  . SER   A 1 232 ? 44.723 7.406   15.109  1.00 11.82 ? 306 SER   A CB  1 
ATOM   1821 O  OG  . SER   A 1 232 ? 45.453 6.758   16.147  1.00 13.05 ? 306 SER   A OG  1 
ATOM   1822 N  N   . ALA   A 1 233 ? 46.973 9.478   14.207  1.00 13.18 ? 307 ALA   A N   1 
ATOM   1823 C  CA  . ALA   A 1 233 ? 48.358 9.910   14.263  1.00 13.44 ? 307 ALA   A CA  1 
ATOM   1824 C  C   . ALA   A 1 233 ? 48.512 11.350  14.719  1.00 13.22 ? 307 ALA   A C   1 
ATOM   1825 O  O   . ALA   A 1 233 ? 49.459 11.671  15.403  1.00 13.28 ? 307 ALA   A O   1 
ATOM   1826 C  CB  . ALA   A 1 233 ? 48.993 9.689   12.925  1.00 14.36 ? 307 ALA   A CB  1 
ATOM   1827 N  N   . THR   A 1 234 ? 47.583 12.252  14.300  1.00 12.93 ? 308 THR   A N   1 
ATOM   1828 C  CA  . THR   A 1 234 ? 47.648 13.651  14.676  1.00 13.12 ? 308 THR   A CA  1 
ATOM   1829 C  C   . THR   A 1 234 ? 46.973 13.941  16.014  1.00 12.05 ? 308 THR   A C   1 
ATOM   1830 O  O   . THR   A 1 234 ? 47.052 15.049  16.533  1.00 12.78 ? 308 THR   A O   1 
ATOM   1831 C  CB  . THR   A 1 234 ? 47.021 14.543  13.606  1.00 13.78 ? 308 THR   A CB  1 
ATOM   1832 O  OG1 . THR   A 1 234 ? 45.643 14.226  13.591  1.00 13.57 ? 308 THR   A OG1 1 
ATOM   1833 C  CG2 . THR   A 1 234 ? 47.632 14.363  12.219  1.00 15.15 ? 308 THR   A CG2 1 
ATOM   1834 N  N   . MET   A 1 235 ? 46.249 12.949  16.528  1.00 12.15 ? 309 MET   A N   1 
ATOM   1835 C  CA  . MET   A 1 235 ? 45.349 13.076  17.671  1.00 11.81 ? 309 MET   A CA  1 
ATOM   1836 C  C   . MET   A 1 235 ? 44.173 13.998  17.368  1.00 11.34 ? 309 MET   A C   1 
ATOM   1837 O  O   . MET   A 1 235 ? 43.368 14.283  18.277  1.00 12.33 ? 309 MET   A O   1 
ATOM   1838 C  CB  . MET   A 1 235 ? 46.017 13.379  19.013  1.00 11.71 ? 309 MET   A CB  1 
ATOM   1839 C  CG  . MET   A 1 235 ? 46.992 12.323  19.462  1.00 12.92 ? 309 MET   A CG  1 
ATOM   1840 S  SD  . MET   A 1 235 ? 47.468 12.460  21.184  1.00 13.85 ? 309 MET   A SD  1 
ATOM   1841 C  CE  . MET   A 1 235 ? 45.963 11.850  21.953  1.00 14.41 ? 309 MET   A CE  1 
ATOM   1842 N  N   . MET   A 1 236 ? 43.966 14.404  16.111  1.00 11.33 ? 310 MET   A N   1 
ATOM   1843 C  CA  . MET   A 1 236 ? 42.707 15.037  15.794  1.00 11.27 ? 310 MET   A CA  1 
ATOM   1844 C  C   . MET   A 1 236 ? 41.556 14.092  16.020  1.00 11.38 ? 310 MET   A C   1 
ATOM   1845 O  O   . MET   A 1 236 ? 40.442 14.532  16.329  1.00 12.06 ? 310 MET   A O   1 
ATOM   1846 C  CB  . MET   A 1 236 ? 42.676 15.539  14.370  1.00 12.36 ? 310 MET   A CB  1 
ATOM   1847 C  CG  . MET   A 1 236 ? 41.376 16.361  14.094  1.00 14.66 ? 310 MET   A CG  1 
ATOM   1848 S  SD  . MET   A 1 236 ? 40.920 17.688  15.329  1.00 15.84 ? 310 MET   A SD  1 
ATOM   1849 C  CE  . MET   A 1 236 ? 41.700 19.070  14.497  1.00 17.41 ? 310 MET   A CE  1 
ATOM   1850 N  N   . ASN   A 1 237 ? 41.779 12.779  15.891  1.00 10.90 ? 311 ASN   A N   1 
ATOM   1851 C  CA  . ASN   A 1 237 ? 40.700 11.874  16.218  1.00 11.49 ? 311 ASN   A CA  1 
ATOM   1852 C  C   . ASN   A 1 237 ? 40.189 12.124  17.624  1.00 10.84 ? 311 ASN   A C   1 
ATOM   1853 O  O   . ASN   A 1 237 ? 38.973 12.176  17.841  1.00 11.12 ? 311 ASN   A O   1 
ATOM   1854 C  CB  . ASN   A 1 237 ? 41.129 10.416  16.046  1.00 11.15 ? 311 ASN   A CB  1 
ATOM   1855 C  CG  . ASN   A 1 237 ? 39.950 9.521   16.299  1.00 12.44 ? 311 ASN   A CG  1 
ATOM   1856 O  OD1 . ASN   A 1 237 ? 38.919 9.585   15.607  1.00 13.28 ? 311 ASN   A OD1 1 
ATOM   1857 N  ND2 . ASN   A 1 237 ? 40.034 8.674   17.315  1.00 12.97 ? 311 ASN   A ND2 1 
ATOM   1858 N  N   . LYS   A 1 238 ? 41.099 12.242  18.585  1.00 11.08 ? 312 LYS   A N   1 
ATOM   1859 C  CA  . LYS   A 1 238 ? 40.670 12.451  19.939  1.00 11.05 ? 312 LYS   A CA  1 
ATOM   1860 C  C   . LYS   A 1 238 ? 39.985 13.818  20.087  1.00 11.26 ? 312 LYS   A C   1 
ATOM   1861 O  O   . LYS   A 1 238 ? 39.033 13.923  20.834  1.00 11.46 ? 312 LYS   A O   1 
ATOM   1862 C  CB  . LYS   A 1 238 ? 41.859 12.330  20.900  1.00 11.25 ? 312 LYS   A CB  1 
ATOM   1863 C  CG  . LYS   A 1 238 ? 41.407 11.836  22.235  1.00 12.91 ? 312 LYS   A CG  1 
ATOM   1864 C  CD  . LYS   A 1 238 ? 40.638 10.511  22.273  1.00 11.64 ? 312 LYS   A CD  1 
ATOM   1865 C  CE  . LYS   A 1 238 ? 41.216 9.491   21.345  1.00 12.39 ? 312 LYS   A CE  1 
ATOM   1866 N  NZ  . LYS   A 1 238 ? 40.617 8.158   21.525  1.00 11.43 ? 312 LYS   A NZ  1 
ATOM   1867 N  N   . GLY   A 1 239 ? 40.481 14.856  19.369  1.00 11.45 ? 313 GLY   A N   1 
ATOM   1868 C  CA  . GLY   A 1 239 ? 39.764 16.139  19.376  1.00 11.55 ? 313 GLY   A CA  1 
ATOM   1869 C  C   . GLY   A 1 239 ? 38.330 15.994  18.901  1.00 10.89 ? 313 GLY   A C   1 
ATOM   1870 O  O   . GLY   A 1 239 ? 37.410 16.509  19.550  1.00 11.55 ? 313 GLY   A O   1 
ATOM   1871 N  N   . LEU   A 1 240 ? 38.118 15.312  17.791  1.00 10.64 ? 314 LEU   A N   1 
ATOM   1872 C  CA  . LEU   A 1 240 ? 36.781 15.014  17.313  1.00 10.89 ? 314 LEU   A CA  1 
ATOM   1873 C  C   . LEU   A 1 240 ? 35.974 14.281  18.369  1.00 10.56 ? 314 LEU   A C   1 
ATOM   1874 O  O   . LEU   A 1 240 ? 34.793 14.584  18.576  1.00 10.63 ? 314 LEU   A O   1 
ATOM   1875 C  CB  . LEU   A 1 240 ? 36.804 14.255  16.000  1.00 11.71 ? 314 LEU   A CB  1 
ATOM   1876 C  CG  . LEU   A 1 240 ? 37.463 14.989  14.818  1.00 12.78 ? 314 LEU   A CG  1 
ATOM   1877 C  CD1 . LEU   A 1 240 ? 37.547 14.077  13.637  1.00 15.86 ? 314 LEU   A CD1 1 
ATOM   1878 C  CD2 . LEU   A 1 240 ? 36.752 16.259  14.441  1.00 15.20 ? 314 LEU   A CD2 1 
ATOM   1879 N  N   . GLU   A 1 241 ? 36.610 13.293  19.031  1.00 9.89  ? 315 GLU   A N   1 
ATOM   1880 C  CA  . GLU   A 1 241 ? 35.922 12.508  20.035  1.00 10.23 ? 315 GLU   A CA  1 
ATOM   1881 C  C   . GLU   A 1 241 ? 35.580 13.298  21.304  1.00 9.91  ? 315 GLU   A C   1 
ATOM   1882 O  O   . GLU   A 1 241 ? 34.617 12.949  21.959  1.00 10.79 ? 315 GLU   A O   1 
ATOM   1883 C  CB  . GLU   A 1 241 ? 36.775 11.290  20.386  1.00 10.20 ? 315 GLU   A CB  1 
ATOM   1884 C  CG  . GLU   A 1 241 ? 36.836 10.279  19.256  1.00 11.44 ? 315 GLU   A CG  1 
ATOM   1885 C  CD  . GLU   A 1 241 ? 37.567 9.005   19.625  1.00 10.96 ? 315 GLU   A CD  1 
ATOM   1886 O  OE1 . GLU   A 1 241 ? 38.119 8.943   20.753  1.00 11.85 ? 315 GLU   A OE1 1 
ATOM   1887 O  OE2 . GLU   A 1 241 ? 37.521 8.076   18.808  1.00 11.34 ? 315 GLU   A OE2 1 
ATOM   1888 N  N   . VAL   A 1 242 ? 36.293 14.381  21.606  1.00 10.01 ? 316 VAL   A N   1 
ATOM   1889 C  CA  . VAL   A 1 242 ? 35.926 15.277  22.708  1.00 10.22 ? 316 VAL   A CA  1 
ATOM   1890 C  C   . VAL   A 1 242 ? 34.585 15.939  22.387  1.00 9.75  ? 316 VAL   A C   1 
ATOM   1891 O  O   . VAL   A 1 242 ? 33.661 15.957  23.185  1.00 10.28 ? 316 VAL   A O   1 
ATOM   1892 C  CB  . VAL   A 1 242 ? 37.031 16.303  22.949  1.00 11.09 ? 316 VAL   A CB  1 
ATOM   1893 C  CG1 . VAL   A 1 242 ? 36.546 17.451  23.832  1.00 11.44 ? 316 VAL   A CG1 1 
ATOM   1894 C  CG2 . VAL   A 1 242 ? 38.266 15.676  23.560  1.00 10.83 ? 316 VAL   A CG2 1 
ATOM   1895 N  N   . ILE   A 1 243 ? 34.452 16.457  21.151  1.00 10.39 ? 317 ILE   A N   1 
ATOM   1896 C  CA  . ILE   A 1 243 ? 33.211 17.086  20.724  1.00 9.85  ? 317 ILE   A CA  1 
ATOM   1897 C  C   . ILE   A 1 243 ? 32.093 16.058  20.671  1.00 10.22 ? 317 ILE   A C   1 
ATOM   1898 O  O   . ILE   A 1 243 ? 30.955 16.304  21.083  1.00 10.86 ? 317 ILE   A O   1 
ATOM   1899 C  CB  . ILE   A 1 243 ? 33.430 17.824  19.394  1.00 10.49 ? 317 ILE   A CB  1 
ATOM   1900 C  CG1 . ILE   A 1 243 ? 34.423 18.972  19.586  1.00 11.66 ? 317 ILE   A CG1 1 
ATOM   1901 C  CG2 . ILE   A 1 243 ? 32.108 18.349  18.838  1.00 10.93 ? 317 ILE   A CG2 1 
ATOM   1902 C  CD1 . ILE   A 1 243 ? 34.929 19.595  18.275  1.00 11.94 ? 317 ILE   A CD1 1 
ATOM   1903 N  N   . GLU   A 1 244 ? 32.398 14.854  20.152  1.00 10.36 ? 318 GLU   A N   1 
ATOM   1904 C  CA  . GLU   A 1 244 ? 31.423 13.783  20.126  1.00 10.72 ? 318 GLU   A CA  1 
ATOM   1905 C  C   . GLU   A 1 244 ? 30.890 13.491  21.532  1.00 10.51 ? 318 GLU   A C   1 
ATOM   1906 O  O   . GLU   A 1 244 ? 29.699 13.238  21.740  1.00 11.56 ? 318 GLU   A O   1 
ATOM   1907 C  CB  . GLU   A 1 244 ? 32.071 12.550  19.477  1.00 11.03 ? 318 GLU   A CB  1 
ATOM   1908 C  CG  . GLU   A 1 244 ? 31.132 11.374  19.302  1.00 12.02 ? 318 GLU   A CG  1 
ATOM   1909 C  CD  . GLU   A 1 244 ? 31.788 10.098  18.801  1.00 12.25 ? 318 GLU   A CD  1 
ATOM   1910 O  OE1 . GLU   A 1 244 ? 33.047 10.079  18.732  1.00 12.42 ? 318 GLU   A OE1 1 
ATOM   1911 O  OE2 . GLU   A 1 244 ? 31.051 9.149   18.476  1.00 13.92 ? 318 GLU   A OE2 1 
ATOM   1912 N  N   . THR   A 1 245 ? 31.792 13.426  22.525  1.00 10.65 ? 319 THR   A N   1 
ATOM   1913 C  CA  . THR   A 1 245 ? 31.432 13.172  23.916  1.00 10.17 ? 319 THR   A CA  1 
ATOM   1914 C  C   . THR   A 1 245 ? 30.467 14.258  24.399  1.00 11.35 ? 319 THR   A C   1 
ATOM   1915 O  O   . THR   A 1 245 ? 29.477 13.987  25.074  1.00 11.65 ? 319 THR   A O   1 
ATOM   1916 C  CB  . THR   A 1 245 ? 32.692 13.147  24.779  1.00 10.71 ? 319 THR   A CB  1 
ATOM   1917 O  OG1 . THR   A 1 245 ? 33.543 12.076  24.370  1.00 11.91 ? 319 THR   A OG1 1 
ATOM   1918 C  CG2 . THR   A 1 245 ? 32.387 12.971  26.256  1.00 10.95 ? 319 THR   A CG2 1 
ATOM   1919 N  N   . HIS   A 1 246 ? 30.832 15.531  24.165  1.00 10.82 ? 320 HIS   A N   1 
ATOM   1920 C  CA  . HIS   A 1 246 ? 30.014 16.656  24.568  1.00 11.41 ? 320 HIS   A CA  1 
ATOM   1921 C  C   . HIS   A 1 246 ? 28.575 16.469  24.081  1.00 11.40 ? 320 HIS   A C   1 
ATOM   1922 O  O   . HIS   A 1 246 ? 27.642 16.654  24.853  1.00 12.69 ? 320 HIS   A O   1 
ATOM   1923 C  CB  . HIS   A 1 246 ? 30.612 17.945  24.044  1.00 11.77 ? 320 HIS   A CB  1 
ATOM   1924 C  CG  . HIS   A 1 246 ? 29.689 19.122  24.148  1.00 12.29 ? 320 HIS   A CG  1 
ATOM   1925 N  ND1 . HIS   A 1 246 ? 29.366 19.662  25.361  1.00 13.47 ? 320 HIS   A ND1 1 
ATOM   1926 C  CD2 . HIS   A 1 246 ? 29.027 19.819  23.197  1.00 14.26 ? 320 HIS   A CD2 1 
ATOM   1927 C  CE1 . HIS   A 1 246 ? 28.502 20.680  25.121  1.00 14.92 ? 320 HIS   A CE1 1 
ATOM   1928 N  NE2 . HIS   A 1 246 ? 28.280 20.790  23.839  1.00 15.92 ? 320 HIS   A NE2 1 
ATOM   1929 N  N   . PHE   A 1 247 ? 28.420 16.194  22.786  1.00 11.28 ? 321 PHE   A N   1 
ATOM   1930 C  CA  . PHE   A 1 247 ? 27.094 16.099  22.213  1.00 12.41 ? 321 PHE   A CA  1 
ATOM   1931 C  C   . PHE   A 1 247 ? 26.373 14.837  22.648  1.00 12.53 ? 321 PHE   A C   1 
ATOM   1932 O  O   . PHE   A 1 247 ? 25.195 14.870  23.032  1.00 13.78 ? 321 PHE   A O   1 
ATOM   1933 C  CB  . PHE   A 1 247 ? 27.122 16.161  20.693  1.00 13.06 ? 321 PHE   A CB  1 
ATOM   1934 C  CG  . PHE   A 1 247 ? 27.297 17.585  20.201  1.00 14.27 ? 321 PHE   A CG  1 
ATOM   1935 C  CD1 . PHE   A 1 247 ? 26.342 18.554  20.436  1.00 17.87 ? 321 PHE   A CD1 1 
ATOM   1936 C  CD2 . PHE   A 1 247 ? 28.405 17.933  19.487  1.00 16.67 ? 321 PHE   A CD2 1 
ATOM   1937 C  CE1 . PHE   A 1 247 ? 26.532 19.866  19.986  1.00 18.51 ? 321 PHE   A CE1 1 
ATOM   1938 C  CE2 . PHE   A 1 247 ? 28.599 19.252  19.042  1.00 18.78 ? 321 PHE   A CE2 1 
ATOM   1939 C  CZ  . PHE   A 1 247 ? 27.655 20.211  19.315  1.00 19.93 ? 321 PHE   A CZ  1 
ATOM   1940 N  N   . LEU   A 1 248 ? 27.020 13.663  22.593  1.00 11.94 ? 322 LEU   A N   1 
ATOM   1941 C  CA  . LEU   A 1 248 ? 26.322 12.427  22.957  1.00 11.95 ? 322 LEU   A CA  1 
ATOM   1942 C  C   . LEU   A 1 248 ? 25.828 12.448  24.401  1.00 12.95 ? 322 LEU   A C   1 
ATOM   1943 O  O   . LEU   A 1 248 ? 24.776 11.899  24.710  1.00 14.17 ? 322 LEU   A O   1 
ATOM   1944 C  CB  . LEU   A 1 248 ? 27.215 11.198  22.746  1.00 13.03 ? 322 LEU   A CB  1 
ATOM   1945 C  CG  . LEU   A 1 248 ? 27.452 10.813  21.298  1.00 12.26 ? 322 LEU   A CG  1 
ATOM   1946 C  CD1 . LEU   A 1 248 ? 28.499 9.676   21.257  1.00 12.60 ? 322 LEU   A CD1 1 
ATOM   1947 C  CD2 . LEU   A 1 248 ? 26.171 10.272  20.674  1.00 14.75 ? 322 LEU   A CD2 1 
ATOM   1948 N  N   . PHE   A 1 249 ? 26.653 12.925  25.330  1.00 12.42 ? 323 PHE   A N   1 
ATOM   1949 C  CA  . PHE   A 1 249 ? 26.455 12.715  26.750  1.00 12.68 ? 323 PHE   A CA  1 
ATOM   1950 C  C   . PHE   A 1 249 ? 26.168 13.988  27.514  1.00 13.99 ? 323 PHE   A C   1 
ATOM   1951 O  O   . PHE   A 1 249 ? 26.039 13.945  28.742  1.00 15.02 ? 323 PHE   A O   1 
ATOM   1952 C  CB  . PHE   A 1 249 ? 27.655 11.949  27.308  1.00 13.47 ? 323 PHE   A CB  1 
ATOM   1953 C  CG  . PHE   A 1 249 ? 27.912 10.643  26.592  1.00 12.78 ? 323 PHE   A CG  1 
ATOM   1954 C  CD1 . PHE   A 1 249 ? 26.950 9.655   26.473  1.00 13.32 ? 323 PHE   A CD1 1 
ATOM   1955 C  CD2 . PHE   A 1 249 ? 29.132 10.429  26.008  1.00 13.09 ? 323 PHE   A CD2 1 
ATOM   1956 C  CE1 . PHE   A 1 249 ? 27.240 8.505   25.786  1.00 13.74 ? 323 PHE   A CE1 1 
ATOM   1957 C  CE2 . PHE   A 1 249 ? 29.413 9.280   25.318  1.00 12.46 ? 323 PHE   A CE2 1 
ATOM   1958 C  CZ  . PHE   A 1 249 ? 28.476 8.295   25.217  1.00 12.80 ? 323 PHE   A CZ  1 
ATOM   1959 N  N   . ASP   A 1 250 ? 26.106 15.134  26.837  1.00 13.89 ? 324 ASP   A N   1 
ATOM   1960 C  CA  . ASP   A 1 250 ? 25.792 16.399  27.478  1.00 14.40 ? 324 ASP   A CA  1 
ATOM   1961 C  C   . ASP   A 1 250 ? 26.771 16.747  28.586  1.00 13.78 ? 324 ASP   A C   1 
ATOM   1962 O  O   . ASP   A 1 250 ? 26.391 17.167  29.689  1.00 15.40 ? 324 ASP   A O   1 
ATOM   1963 C  CB  . ASP   A 1 250 ? 24.361 16.253  28.002  1.00 18.82 ? 324 ASP   A CB  1 
ATOM   1964 C  CG  . ASP   A 1 250 ? 23.774 17.354  28.836  1.00 26.92 ? 324 ASP   A CG  1 
ATOM   1965 O  OD1 . ASP   A 1 250 ? 23.857 18.477  28.327  1.00 26.24 ? 324 ASP   A OD1 1 
ATOM   1966 O  OD2 . ASP   A 1 250 ? 23.186 17.013  29.931  1.00 26.40 ? 324 ASP   A OD2 1 
ATOM   1967 N  N   . VAL   A 1 251 ? 28.055 16.622  28.276  1.00 12.55 ? 325 VAL   A N   1 
ATOM   1968 C  CA  . VAL   A 1 251 ? 29.140 16.876  29.210  1.00 13.03 ? 325 VAL   A CA  1 
ATOM   1969 C  C   . VAL   A 1 251 ? 29.859 18.143  28.780  1.00 11.84 ? 325 VAL   A C   1 
ATOM   1970 O  O   . VAL   A 1 251 ? 30.216 18.267  27.612  1.00 12.84 ? 325 VAL   A O   1 
ATOM   1971 C  CB  . VAL   A 1 251 ? 30.098 15.669  29.335  1.00 13.63 ? 325 VAL   A CB  1 
ATOM   1972 C  CG1 . VAL   A 1 251 ? 31.227 15.948  30.287  1.00 14.25 ? 325 VAL   A CG1 1 
ATOM   1973 C  CG2 . VAL   A 1 251 ? 29.376 14.404  29.803  1.00 17.31 ? 325 VAL   A CG2 1 
ATOM   1974 N  N   . ASP   A 1 252 ? 30.093 19.043  29.708  1.00 12.34 ? 326 ASP   A N   1 
ATOM   1975 C  CA  . ASP   A 1 252 ? 30.831 20.265  29.427  1.00 13.19 ? 326 ASP   A CA  1 
ATOM   1976 C  C   . ASP   A 1 252 ? 32.254 19.960  29.024  1.00 12.85 ? 326 ASP   A C   1 
ATOM   1977 O  O   . ASP   A 1 252 ? 32.871 19.020  29.537  1.00 12.09 ? 326 ASP   A O   1 
ATOM   1978 C  CB  . ASP   A 1 252 ? 30.844 21.175  30.660  1.00 14.62 ? 326 ASP   A CB  1 
ATOM   1979 C  CG  . ASP   A 1 252 ? 29.510 21.783  31.051  1.00 18.61 ? 326 ASP   A CG  1 
ATOM   1980 O  OD1 . ASP   A 1 252 ? 28.510 21.620  30.362  1.00 21.13 ? 326 ASP   A OD1 1 
ATOM   1981 O  OD2 . ASP   A 1 252 ? 29.538 22.379  32.140  1.00 22.54 ? 326 ASP   A OD2 1 
ATOM   1982 N  N   . TYR   A 1 253 ? 32.864 20.787  28.168  1.00 12.43 ? 327 TYR   A N   1 
ATOM   1983 C  CA  . TYR   A 1 253 ? 34.216 20.556  27.727  1.00 11.99 ? 327 TYR   A CA  1 
ATOM   1984 C  C   . TYR   A 1 253 ? 35.206 20.585  28.879  1.00 12.77 ? 327 TYR   A C   1 
ATOM   1985 O  O   . TYR   A 1 253 ? 36.189 19.863  28.869  1.00 12.46 ? 327 TYR   A O   1 
ATOM   1986 C  CB  . TYR   A 1 253 ? 34.589 21.633  26.673  1.00 11.83 ? 327 TYR   A CB  1 
ATOM   1987 C  CG  . TYR   A 1 253 ? 33.915 21.353  25.355  1.00 11.53 ? 327 TYR   A CG  1 
ATOM   1988 C  CD1 . TYR   A 1 253 ? 34.409 20.381  24.494  1.00 11.60 ? 327 TYR   A CD1 1 
ATOM   1989 C  CD2 . TYR   A 1 253 ? 32.746 21.999  24.989  1.00 11.90 ? 327 TYR   A CD2 1 
ATOM   1990 C  CE1 . TYR   A 1 253 ? 33.745 20.064  23.323  1.00 11.81 ? 327 TYR   A CE1 1 
ATOM   1991 C  CE2 . TYR   A 1 253 ? 32.076 21.685  23.822  1.00 12.41 ? 327 TYR   A CE2 1 
ATOM   1992 C  CZ  . TYR   A 1 253 ? 32.575 20.713  22.977  1.00 11.26 ? 327 TYR   A CZ  1 
ATOM   1993 O  OH  . TYR   A 1 253 ? 31.976 20.368  21.798  1.00 12.56 ? 327 TYR   A OH  1 
ATOM   1994 N  N   . ASN   A 1 254 ? 34.966 21.389  29.904  1.00 12.81 ? 328 ASN   A N   1 
ATOM   1995 C  CA  . ASN   A 1 254 ? 35.854 21.407  31.059  1.00 14.10 ? 328 ASN   A CA  1 
ATOM   1996 C  C   . ASN   A 1 254 ? 35.827 20.104  31.849  1.00 13.15 ? 328 ASN   A C   1 
ATOM   1997 O  O   . ASN   A 1 254 ? 36.719 19.908  32.664  1.00 15.05 ? 328 ASN   A O   1 
ATOM   1998 C  CB  . ASN   A 1 254 ? 35.469 22.555  31.987  1.00 16.79 ? 328 ASN   A CB  1 
ATOM   1999 C  CG  . ASN   A 1 254 ? 35.861 23.907  31.429  1.00 22.50 ? 328 ASN   A CG  1 
ATOM   2000 O  OD1 . ASN   A 1 254 ? 36.614 24.028  30.444  1.00 25.95 ? 328 ASN   A OD1 1 
ATOM   2001 N  ND2 . ASN   A 1 254 ? 35.380 24.932  32.120  1.00 29.05 ? 328 ASN   A ND2 1 
ATOM   2002 N  N   . ASP   A 1 255 ? 34.843 19.282  31.613  1.00 12.09 ? 329 ASP   A N   1 
ATOM   2003 C  CA  . ASP   A 1 255 ? 34.653 18.006  32.295  1.00 12.24 ? 329 ASP   A CA  1 
ATOM   2004 C  C   . ASP   A 1 255 ? 35.000 16.831  31.386  1.00 11.64 ? 329 ASP   A C   1 
ATOM   2005 O  O   . ASP   A 1 255 ? 34.587 15.713  31.693  1.00 11.62 ? 329 ASP   A O   1 
ATOM   2006 C  CB  . ASP   A 1 255 ? 33.253 17.910  32.855  1.00 12.98 ? 329 ASP   A CB  1 
ATOM   2007 C  CG  . ASP   A 1 255 ? 32.915 19.012  33.849  1.00 15.54 ? 329 ASP   A CG  1 
ATOM   2008 O  OD1 . ASP   A 1 255 ? 33.817 19.378  34.605  1.00 18.57 ? 329 ASP   A OD1 1 
ATOM   2009 O  OD2 . ASP   A 1 255 ? 31.745 19.430  33.900  1.00 16.67 ? 329 ASP   A OD2 1 
ATOM   2010 N  N   . ILE   A 1 256 ? 35.735 17.051  30.301  1.00 10.74 ? 330 ILE   A N   1 
ATOM   2011 C  CA  . ILE   A 1 256 ? 36.211 15.970  29.439  1.00 10.53 ? 330 ILE   A CA  1 
ATOM   2012 C  C   . ILE   A 1 256 ? 37.709 16.030  29.425  1.00 11.09 ? 330 ILE   A C   1 
ATOM   2013 O  O   . ILE   A 1 256 ? 38.272 17.058  29.047  1.00 11.43 ? 330 ILE   A O   1 
ATOM   2014 C  CB  . ILE   A 1 256 ? 35.672 16.091  28.011  1.00 10.45 ? 330 ILE   A CB  1 
ATOM   2015 C  CG1 . ILE   A 1 256 ? 34.158 16.153  28.009  1.00 11.23 ? 330 ILE   A CG1 1 
ATOM   2016 C  CG2 . ILE   A 1 256 ? 36.214 14.921  27.146  1.00 11.16 ? 330 ILE   A CG2 1 
ATOM   2017 C  CD1 . ILE   A 1 256 ? 33.548 16.579  26.688  1.00 11.87 ? 330 ILE   A CD1 1 
ATOM   2018 N  N   . GLU   A 1 257 ? 38.390 14.970  29.884  1.00 10.70 ? 331 GLU   A N   1 
ATOM   2019 C  CA  . GLU   A 1 257 ? 39.842 14.945  29.993  1.00 11.15 ? 331 GLU   A CA  1 
ATOM   2020 C  C   . GLU   A 1 257 ? 40.399 13.858  29.085  1.00 11.97 ? 331 GLU   A C   1 
ATOM   2021 O  O   . GLU   A 1 257 ? 39.997 12.686  29.252  1.00 13.29 ? 331 GLU   A O   1 
ATOM   2022 C  CB  . GLU   A 1 257 ? 40.229 14.657  31.447  1.00 12.46 ? 331 GLU   A CB  1 
ATOM   2023 C  CG  . GLU   A 1 257 ? 41.740 14.653  31.643  1.00 15.61 ? 331 GLU   A CG  1 
ATOM   2024 C  CD  . GLU   A 1 257 ? 42.239 14.466  33.051  1.00 18.64 ? 331 GLU   A CD  1 
ATOM   2025 O  OE1 . GLU   A 1 257 ? 41.487 14.475  33.996  1.00 19.82 ? 331 GLU   A OE1 1 
ATOM   2026 O  OE2 . GLU   A 1 257 ? 43.488 14.316  33.169  1.00 24.77 ? 331 GLU   A OE2 1 
ATOM   2027 N  N   . VAL   A 1 258 ? 41.306 14.214  28.185  1.00 11.39 ? 332 VAL   A N   1 
ATOM   2028 C  CA  . VAL   A 1 258 ? 41.952 13.215  27.334  1.00 11.30 ? 332 VAL   A CA  1 
ATOM   2029 C  C   . VAL   A 1 258 ? 43.125 12.599  28.101  1.00 11.63 ? 332 VAL   A C   1 
ATOM   2030 O  O   . VAL   A 1 258 ? 43.967 13.325  28.660  1.00 13.36 ? 332 VAL   A O   1 
ATOM   2031 C  CB  . VAL   A 1 258 ? 42.464 13.861  26.042  1.00 11.83 ? 332 VAL   A CB  1 
ATOM   2032 C  CG1 . VAL   A 1 258 ? 43.272 12.873  25.213  1.00 13.52 ? 332 VAL   A CG1 1 
ATOM   2033 C  CG2 . VAL   A 1 258 ? 41.287 14.393  25.252  1.00 12.44 ? 332 VAL   A CG2 1 
ATOM   2034 N  N   . ILE   A 1 259 ? 43.193 11.274  28.082  1.00 10.47 ? 333 ILE   A N   1 
ATOM   2035 C  CA  . ILE   A 1 259 ? 44.298 10.562  28.714  1.00 11.34 ? 333 ILE   A CA  1 
ATOM   2036 C  C   . ILE   A 1 259 ? 44.868 9.556   27.730  1.00 11.12 ? 333 ILE   A C   1 
ATOM   2037 O  O   . ILE   A 1 259 ? 44.108 8.791   27.162  1.00 11.91 ? 333 ILE   A O   1 
ATOM   2038 C  CB  . ILE   A 1 259 ? 43.840 9.930   30.023  1.00 14.19 ? 333 ILE   A CB  1 
ATOM   2039 C  CG1 . ILE   A 1 259 ? 45.016 9.453   30.871  1.00 17.01 ? 333 ILE   A CG1 1 
ATOM   2040 C  CG2 . ILE   A 1 259 ? 42.785 8.935   29.889  1.00 16.26 ? 333 ILE   A CG2 1 
ATOM   2041 C  CD1 . ILE   A 1 259 ? 45.706 10.636  31.563  1.00 20.51 ? 333 ILE   A CD1 1 
ATOM   2042 N  N   . VAL   A 1 260 ? 46.176 9.550   27.565  1.00 10.28 ? 334 VAL   A N   1 
ATOM   2043 C  CA  . VAL   A 1 260 ? 46.855 8.585   26.716  1.00 9.70  ? 334 VAL   A CA  1 
ATOM   2044 C  C   . VAL   A 1 260 ? 47.082 7.305   27.531  1.00 10.32 ? 334 VAL   A C   1 
ATOM   2045 O  O   . VAL   A 1 260 ? 47.732 7.318   28.572  1.00 10.54 ? 334 VAL   A O   1 
ATOM   2046 C  CB  . VAL   A 1 260 ? 48.179 9.088   26.165  1.00 11.07 ? 334 VAL   A CB  1 
ATOM   2047 C  CG1 . VAL   A 1 260 ? 48.851 8.035   25.302  1.00 11.69 ? 334 VAL   A CG1 1 
ATOM   2048 C  CG2 . VAL   A 1 260 ? 47.931 10.329  25.324  1.00 12.91 ? 334 VAL   A CG2 1 
ATOM   2049 N  N   . HIS   A 1 261 ? 46.485 6.237   27.056  1.00 10.09 ? 335 HIS   A N   1 
ATOM   2050 C  CA  . HIS   A 1 261 ? 46.497 4.902   27.674  1.00 9.99  ? 335 HIS   A CA  1 
ATOM   2051 C  C   . HIS   A 1 261 ? 46.969 3.936   26.590  1.00 10.60 ? 335 HIS   A C   1 
ATOM   2052 O  O   . HIS   A 1 261 ? 46.177 3.394   25.835  1.00 11.03 ? 335 HIS   A O   1 
ATOM   2053 C  CB  . HIS   A 1 261 ? 45.110 4.561   28.212  1.00 10.44 ? 335 HIS   A CB  1 
ATOM   2054 C  CG  . HIS   A 1 261 ? 44.987 3.149   28.687  1.00 10.46 ? 335 HIS   A CG  1 
ATOM   2055 N  ND1 . HIS   A 1 261 ? 45.945 2.561   29.491  1.00 11.23 ? 335 HIS   A ND1 1 
ATOM   2056 C  CD2 . HIS   A 1 261 ? 44.088 2.197   28.432  1.00 10.41 ? 335 HIS   A CD2 1 
ATOM   2057 C  CE1 . HIS   A 1 261 ? 45.580 1.276   29.661  1.00 11.19 ? 335 HIS   A CE1 1 
ATOM   2058 N  NE2 . HIS   A 1 261 ? 44.458 1.033   29.058  1.00 11.24 ? 335 HIS   A NE2 1 
ATOM   2059 N  N   . LYS   A 1 262 ? 48.277 3.745   26.513  1.00 10.78 ? 336 LYS   A N   1 
ATOM   2060 C  CA  . LYS   A 1 262 ? 48.839 3.125   25.312  1.00 11.72 ? 336 LYS   A CA  1 
ATOM   2061 C  C   . LYS   A 1 262 ? 48.478 1.649   25.160  1.00 11.35 ? 336 LYS   A C   1 
ATOM   2062 O  O   . LYS   A 1 262 ? 48.486 1.113   24.042  1.00 12.79 ? 336 LYS   A O   1 
ATOM   2063 C  CB  . LYS   A 1 262 ? 50.351 3.289   25.281  1.00 14.02 ? 336 LYS   A CB  1 
ATOM   2064 C  CG  . LYS   A 1 262 ? 51.076 2.560   26.313  1.00 15.97 ? 336 LYS   A CG  1 
ATOM   2065 C  CD  . LYS   A 1 262 ? 52.595 2.844   26.269  1.00 20.07 ? 336 LYS   A CD  1 
ATOM   2066 C  CE  . LYS   A 1 262 ? 53.340 1.796   27.010  1.00 25.77 ? 336 LYS   A CE  1 
ATOM   2067 N  NZ  . LYS   A 1 262 ? 53.196 2.057   28.410  1.00 30.51 ? 336 LYS   A NZ  1 
ATOM   2068 N  N   . GLU   A 1 263 ? 48.127 0.977   26.259  1.00 10.87 ? 337 GLU   A N   1 
ATOM   2069 C  CA  . GLU   A 1 263 ? 47.779 -0.441  26.184  1.00 11.05 ? 337 GLU   A CA  1 
ATOM   2070 C  C   . GLU   A 1 263 ? 46.392 -0.650  25.623  1.00 10.64 ? 337 GLU   A C   1 
ATOM   2071 O  O   . GLU   A 1 263 ? 46.044 -1.754  25.193  1.00 11.67 ? 337 GLU   A O   1 
ATOM   2072 C  CB  . GLU   A 1 263 ? 47.911 -1.162  27.520  1.00 12.18 ? 337 GLU   A CB  1 
ATOM   2073 C  CG  . GLU   A 1 263 ? 49.293 -1.022  28.149  1.00 12.72 ? 337 GLU   A CG  1 
ATOM   2074 C  CD  . GLU   A 1 263 ? 49.604 0.275   28.883  1.00 14.42 ? 337 GLU   A CD  1 
ATOM   2075 O  OE1 . GLU   A 1 263 ? 48.690 1.045   29.137  1.00 13.43 ? 337 GLU   A OE1 1 
ATOM   2076 O  OE2 . GLU   A 1 263 ? 50.784 0.426   29.284  1.00 17.88 ? 337 GLU   A OE2 1 
ATOM   2077 N  N   . CYS   A 1 264 ? 45.535 0.376   25.632  1.00 10.90 ? 338 CYS   A N   1 
ATOM   2078 C  CA  . CYS   A 1 264 ? 44.204 0.287   25.044  1.00 11.75 ? 338 CYS   A CA  1 
ATOM   2079 C  C   . CYS   A 1 264 ? 43.363 -0.838  25.622  1.00 11.20 ? 338 CYS   A C   1 
ATOM   2080 O  O   . CYS   A 1 264 ? 42.632 -1.503  24.878  1.00 11.70 ? 338 CYS   A O   1 
ATOM   2081 C  CB  . CYS   A 1 264 ? 44.272 0.181   23.531  1.00 11.97 ? 338 CYS   A CB  1 
ATOM   2082 S  SG  . CYS   A 1 264 ? 45.064 1.569   22.707  1.00 16.04 ? 338 CYS   A SG  1 
ATOM   2083 N  N   . ILE   A 1 265 ? 43.440 -0.983  26.951  1.00 10.58 ? 339 ILE   A N   1 
ATOM   2084 C  CA  . ILE   A 1 265 ? 42.607 -1.931  27.671  1.00 10.97 ? 339 ILE   A CA  1 
ATOM   2085 C  C   . ILE   A 1 265 ? 41.418 -1.226  28.323  1.00 10.92 ? 339 ILE   A C   1 
ATOM   2086 O  O   . ILE   A 1 265 ? 40.273 -1.624  28.139  1.00 11.45 ? 339 ILE   A O   1 
ATOM   2087 C  CB  . ILE   A 1 265 ? 43.433 -2.703  28.707  1.00 10.84 ? 339 ILE   A CB  1 
ATOM   2088 C  CG1 . ILE   A 1 265 ? 44.557 -3.517  28.059  1.00 11.79 ? 339 ILE   A CG1 1 
ATOM   2089 C  CG2 . ILE   A 1 265 ? 42.559 -3.617  29.567  1.00 11.70 ? 339 ILE   A CG2 1 
ATOM   2090 C  CD1 . ILE   A 1 265 ? 44.129 -4.597  27.094  1.00 12.33 ? 339 ILE   A CD1 1 
ATOM   2091 N  N   . ILE   A 1 266 ? 41.659 -0.168  29.082  1.00 10.39 ? 340 ILE   A N   1 
ATOM   2092 C  CA  . ILE   A 1 266 ? 40.571 0.690   29.555  1.00 11.61 ? 340 ILE   A CA  1 
ATOM   2093 C  C   . ILE   A 1 266 ? 40.126 1.563   28.399  1.00 10.89 ? 340 ILE   A C   1 
ATOM   2094 O  O   . ILE   A 1 266 ? 40.947 2.317   27.852  1.00 13.39 ? 340 ILE   A O   1 
ATOM   2095 C  CB  . ILE   A 1 266 ? 41.012 1.507   30.763  1.00 11.58 ? 340 ILE   A CB  1 
ATOM   2096 C  CG1 . ILE   A 1 266 ? 41.323 0.598   31.929  1.00 14.66 ? 340 ILE   A CG1 1 
ATOM   2097 C  CG2 . ILE   A 1 266 ? 39.947 2.531   31.162  1.00 13.67 ? 340 ILE   A CG2 1 
ATOM   2098 C  CD1 . ILE   A 1 266 ? 41.818 1.289   33.174  1.00 19.06 ? 340 ILE   A CD1 1 
ATOM   2099 N  N   . HIS   A 1 267 ? 38.883 1.486   27.987  1.00 10.78 ? 341 HIS   A N   1 
ATOM   2100 C  CA  . HIS   A 1 267 ? 38.461 2.162   26.776  1.00 10.77 ? 341 HIS   A CA  1 
ATOM   2101 C  C   . HIS   A 1 267 ? 37.926 3.546   27.011  1.00 10.94 ? 341 HIS   A C   1 
ATOM   2102 O  O   . HIS   A 1 267 ? 37.898 4.298   26.022  1.00 12.39 ? 341 HIS   A O   1 
ATOM   2103 C  CB  . HIS   A 1 267 ? 37.493 1.261   25.989  1.00 12.02 ? 341 HIS   A CB  1 
ATOM   2104 C  CG  . HIS   A 1 267 ? 38.192 0.030   25.505  1.00 13.44 ? 341 HIS   A CG  1 
ATOM   2105 N  ND1 . HIS   A 1 267 ? 39.507 -0.045  25.079  1.00 22.19 ? 341 HIS   A ND1 1 
ATOM   2106 C  CD2 . HIS   A 1 267 ? 37.874 -1.218  25.619  1.00 15.76 ? 341 HIS   A CD2 1 
ATOM   2107 C  CE1 . HIS   A 1 267 ? 39.817 -1.321  24.773  1.00 15.15 ? 341 HIS   A CE1 1 
ATOM   2108 N  NE2 . HIS   A 1 267 ? 38.866 -1.996  25.087  1.00 16.68 ? 341 HIS   A NE2 1 
ATOM   2109 N  N   . SER   A 1 268 ? 37.522 3.872   28.222  1.00 10.71 ? 342 SER   A N   1 
ATOM   2110 C  CA  . SER   A 1 268 ? 37.192 5.209   28.731  1.00 10.82 ? 342 SER   A CA  1 
ATOM   2111 C  C   . SER   A 1 268 ? 36.514 5.006   30.081  1.00 10.81 ? 342 SER   A C   1 
ATOM   2112 O  O   . SER   A 1 268 ? 36.182 3.852   30.457  1.00 11.54 ? 342 SER   A O   1 
ATOM   2113 C  CB  . SER   A 1 268 ? 36.422 6.123   27.782  1.00 10.62 ? 342 SER   A CB  1 
ATOM   2114 O  OG  . SER   A 1 268 ? 37.258 6.682   26.769  1.00 11.41 ? 342 SER   A OG  1 
ATOM   2115 N  N   . CYS   A 1 269 ? 36.290 6.092   30.799  1.00 10.28 ? 343 CYS   A N   1 
ATOM   2116 C  CA  . CYS   A 1 269 ? 35.811 6.050   32.179  1.00 11.22 ? 343 CYS   A CA  1 
ATOM   2117 C  C   . CYS   A 1 269 ? 34.836 7.175   32.420  1.00 10.89 ? 343 CYS   A C   1 
ATOM   2118 O  O   . CYS   A 1 269 ? 35.023 8.291   31.892  1.00 12.31 ? 343 CYS   A O   1 
ATOM   2119 C  CB  . CYS   A 1 269 ? 36.935 6.174   33.202  1.00 12.97 ? 343 CYS   A CB  1 
ATOM   2120 S  SG  . CYS   A 1 269 ? 38.477 5.320   32.831  1.00 14.16 ? 343 CYS   A SG  1 
ATOM   2121 N  N   . VAL   A 1 270 ? 33.887 6.915   33.307  1.00 10.89 ? 344 VAL   A N   1 
ATOM   2122 C  CA  . VAL   A 1 270 ? 32.878 7.885   33.714  1.00 10.61 ? 344 VAL   A CA  1 
ATOM   2123 C  C   . VAL   A 1 270 ? 33.006 8.145   35.199  1.00 10.24 ? 344 VAL   A C   1 
ATOM   2124 O  O   . VAL   A 1 270 ? 32.891 7.195   35.996  1.00 10.87 ? 344 VAL   A O   1 
ATOM   2125 C  CB  . VAL   A 1 270 ? 31.464 7.401   33.398  1.00 11.30 ? 344 VAL   A CB  1 
ATOM   2126 C  CG1 . VAL   A 1 270 ? 30.444 8.469   33.787  1.00 12.50 ? 344 VAL   A CG1 1 
ATOM   2127 C  CG2 . VAL   A 1 270 ? 31.312 7.097   31.913  1.00 13.16 ? 344 VAL   A CG2 1 
ATOM   2128 N  N   . GLU   A 1 271 ? 33.196 9.407   35.600  1.00 10.20 ? 345 GLU   A N   1 
ATOM   2129 C  CA  . GLU   A 1 271 ? 33.138 9.810   36.988  1.00 10.40 ? 345 GLU   A CA  1 
ATOM   2130 C  C   . GLU   A 1 271 ? 31.736 10.293  37.285  1.00 10.55 ? 345 GLU   A C   1 
ATOM   2131 O  O   . GLU   A 1 271 ? 31.256 11.207  36.604  1.00 11.21 ? 345 GLU   A O   1 
ATOM   2132 C  CB  . GLU   A 1 271 ? 34.130 10.930  37.270  1.00 11.01 ? 345 GLU   A CB  1 
ATOM   2133 C  CG  . GLU   A 1 271 ? 34.117 11.386  38.718  1.00 12.52 ? 345 GLU   A CG  1 
ATOM   2134 C  CD  . GLU   A 1 271 ? 34.992 12.596  38.843  1.00 16.23 ? 345 GLU   A CD  1 
ATOM   2135 O  OE1 . GLU   A 1 271 ? 36.220 12.320  38.996  1.00 21.43 ? 345 GLU   A OE1 1 
ATOM   2136 O  OE2 . GLU   A 1 271 ? 34.547 13.733  38.574  1.00 17.50 ? 345 GLU   A OE2 1 
ATOM   2137 N  N   . PHE   A 1 272 ? 31.073 9.685   38.258  1.00 10.74 ? 346 PHE   A N   1 
ATOM   2138 C  CA  . PHE   A 1 272 ? 29.750 10.118  38.683  1.00 11.18 ? 346 PHE   A CA  1 
ATOM   2139 C  C   . PHE   A 1 272 ? 29.884 11.192  39.737  1.00 11.62 ? 346 PHE   A C   1 
ATOM   2140 O  O   . PHE   A 1 272 ? 30.946 11.516  40.254  1.00 12.12 ? 346 PHE   A O   1 
ATOM   2141 C  CB  . PHE   A 1 272 ? 28.938 8.891   39.137  1.00 11.92 ? 346 PHE   A CB  1 
ATOM   2142 C  CG  . PHE   A 1 272 ? 28.699 7.967   37.977  1.00 12.08 ? 346 PHE   A CG  1 
ATOM   2143 C  CD1 . PHE   A 1 272 ? 27.640 8.173   37.103  1.00 12.67 ? 346 PHE   A CD1 1 
ATOM   2144 C  CD2 . PHE   A 1 272 ? 29.571 6.910   37.724  1.00 12.89 ? 346 PHE   A CD2 1 
ATOM   2145 C  CE1 . PHE   A 1 272 ? 27.447 7.340   36.007  1.00 12.82 ? 346 PHE   A CE1 1 
ATOM   2146 C  CE2 . PHE   A 1 272 ? 29.368 6.111   36.618  1.00 13.43 ? 346 PHE   A CE2 1 
ATOM   2147 C  CZ  . PHE   A 1 272 ? 28.332 6.320   35.772  1.00 13.34 ? 346 PHE   A CZ  1 
ATOM   2148 N  N   . ILE   A 1 273 ? 28.720 11.797  40.108  1.00 12.62 ? 347 ILE   A N   1 
ATOM   2149 C  CA  . ILE   A 1 273 ? 28.733 12.950  41.007  1.00 12.82 ? 347 ILE   A CA  1 
ATOM   2150 C  C   . ILE   A 1 273 ? 29.205 12.672  42.419  1.00 12.93 ? 347 ILE   A C   1 
ATOM   2151 O  O   . ILE   A 1 273 ? 29.591 13.601  43.126  1.00 12.96 ? 347 ILE   A O   1 
ATOM   2152 C  CB  . ILE   A 1 273 ? 27.338 13.616  41.031  1.00 14.45 ? 347 ILE   A CB  1 
ATOM   2153 C  CG1 . ILE   A 1 273 ? 26.253 12.676  41.562  1.00 14.48 ? 347 ILE   A CG1 1 
ATOM   2154 C  CG2 . ILE   A 1 273 ? 27.000 14.228  39.683  1.00 14.57 ? 347 ILE   A CG2 1 
ATOM   2155 C  CD1 . ILE   A 1 273 ? 24.875 13.337  41.726  1.00 16.07 ? 347 ILE   A CD1 1 
ATOM   2156 N  N   . ASP   A 1 274 ? 29.236 11.394  42.813  1.00 12.14 ? 348 ASP   A N   1 
ATOM   2157 C  CA  . ASP   A 1 274 ? 29.790 11.000  44.094  1.00 12.37 ? 348 ASP   A CA  1 
ATOM   2158 C  C   . ASP   A 1 274 ? 31.317 10.806  44.074  1.00 11.69 ? 348 ASP   A C   1 
ATOM   2159 O  O   . ASP   A 1 274 ? 31.924 10.564  45.149  1.00 13.40 ? 348 ASP   A O   1 
ATOM   2160 C  CB  . ASP   A 1 274 ? 29.148 9.741   44.640  1.00 13.45 ? 348 ASP   A CB  1 
ATOM   2161 C  CG  . ASP   A 1 274 ? 29.132 8.549   43.708  1.00 15.58 ? 348 ASP   A CG  1 
ATOM   2162 O  OD1 . ASP   A 1 274 ? 29.689 8.621   42.592  1.00 14.72 ? 348 ASP   A OD1 1 
ATOM   2163 O  OD2 . ASP   A 1 274 ? 28.507 7.502   44.126  1.00 18.01 ? 348 ASP   A OD2 1 
ATOM   2164 N  N   . LYS   A 1 275 ? 31.896 10.912  42.864  1.00 11.35 ? 349 LYS   A N   1 
ATOM   2165 C  CA  . LYS   A 1 275 ? 33.323 10.737  42.537  1.00 11.85 ? 349 LYS   A CA  1 
ATOM   2166 C  C   . LYS   A 1 275 ? 33.690 9.282   42.294  1.00 11.78 ? 349 LYS   A C   1 
ATOM   2167 O  O   . LYS   A 1 275 ? 34.850 9.009   41.973  1.00 11.67 ? 349 LYS   A O   1 
ATOM   2168 C  CB  . LYS   A 1 275 ? 34.303 11.425  43.473  1.00 13.37 ? 349 LYS   A CB  1 
ATOM   2169 C  CG  . LYS   A 1 275 ? 33.929 12.893  43.777  1.00 17.13 ? 349 LYS   A CG  1 
ATOM   2170 C  CD  . LYS   A 1 275 ? 33.762 13.772  42.540  1.00 16.59 ? 349 LYS   A CD  1 
ATOM   2171 C  CE  . LYS   A 1 275 ? 33.324 15.148  42.987  1.00 24.06 ? 349 LYS   A CE  1 
ATOM   2172 N  NZ  . LYS   A 1 275 ? 34.351 15.805  43.748  1.00 28.05 ? 349 LYS   A NZ  1 
ATOM   2173 N  N   . SER   A 1 276 ? 32.755 8.348   42.370  1.00 11.20 ? 350 SER   A N   1 
ATOM   2174 C  CA  . SER   A 1 276 ? 33.020 6.989   41.928  1.00 11.45 ? 350 SER   A CA  1 
ATOM   2175 C  C   . SER   A 1 276 ? 33.245 7.005   40.429  1.00 10.80 ? 350 SER   A C   1 
ATOM   2176 O  O   . SER   A 1 276 ? 32.530 7.673   39.689  1.00 11.40 ? 350 SER   A O   1 
ATOM   2177 C  CB  . SER   A 1 276 ? 31.916 6.098   42.341  1.00 10.86 ? 350 SER   A CB  1 
ATOM   2178 O  OG  . SER   A 1 276 ? 32.343 4.727   42.158  1.00 12.71 ? 350 SER   A OG  1 
ATOM   2179 N  N   . VAL   A 1 277 ? 34.205 6.205   39.965  1.00 10.57 ? 351 VAL   A N   1 
ATOM   2180 C  CA  . VAL   A 1 277 ? 34.490 6.069   38.541  1.00 9.98  ? 351 VAL   A CA  1 
ATOM   2181 C  C   . VAL   A 1 277 ? 34.183 4.650   38.070  1.00 10.60 ? 351 VAL   A C   1 
ATOM   2182 O  O   . VAL   A 1 277 ? 34.560 3.685   38.742  1.00 11.61 ? 351 VAL   A O   1 
ATOM   2183 C  CB  . VAL   A 1 277 ? 35.939 6.458   38.267  1.00 10.32 ? 351 VAL   A CB  1 
ATOM   2184 C  CG1 . VAL   A 1 277 ? 36.301 6.292   36.767  1.00 11.29 ? 351 VAL   A CG1 1 
ATOM   2185 C  CG2 . VAL   A 1 277 ? 36.209 7.913   38.679  1.00 10.72 ? 351 VAL   A CG2 1 
ATOM   2186 N  N   . ILE   A 1 278 ? 33.530 4.531   36.935  1.00 10.04 ? 352 ILE   A N   1 
ATOM   2187 C  CA  . ILE   A 1 278 ? 33.245 3.245   36.310  1.00 10.35 ? 352 ILE   A CA  1 
ATOM   2188 C  C   . ILE   A 1 278 ? 33.928 3.235   34.963  1.00 10.62 ? 352 ILE   A C   1 
ATOM   2189 O  O   . ILE   A 1 278 ? 33.942 4.273   34.272  1.00 11.33 ? 352 ILE   A O   1 
ATOM   2190 C  CB  . ILE   A 1 278 ? 31.731 3.007   36.181  1.00 10.76 ? 352 ILE   A CB  1 
ATOM   2191 C  CG1 . ILE   A 1 278 ? 31.030 3.086   37.512  1.00 11.74 ? 352 ILE   A CG1 1 
ATOM   2192 C  CG2 . ILE   A 1 278 ? 31.469 1.659   35.495  1.00 11.33 ? 352 ILE   A CG2 1 
ATOM   2193 C  CD1 . ILE   A 1 278 ? 31.363 1.987   38.501  1.00 13.27 ? 352 ILE   A CD1 1 
ATOM   2194 N  N   . SER   A 1 279 ? 34.572 2.138   34.584  1.00 10.41 ? 353 SER   A N   1 
ATOM   2195 C  CA  . SER   A 1 279 ? 35.270 2.039   33.317  1.00 11.09 ? 353 SER   A CA  1 
ATOM   2196 C  C   . SER   A 1 279 ? 34.891 0.749   32.617  1.00 10.53 ? 353 SER   A C   1 
ATOM   2197 O  O   . SER   A 1 279 ? 34.481 -0.224  33.244  1.00 11.10 ? 353 SER   A O   1 
ATOM   2198 C  CB  . SER   A 1 279 ? 36.761 2.104   33.485  1.00 13.55 ? 353 SER   A CB  1 
ATOM   2199 O  OG  . SER   A 1 279 ? 37.317 0.939   34.038  1.00 19.65 ? 353 SER   A OG  1 
ATOM   2200 N  N   . GLN   A 1 280 ? 35.020 0.733   31.293  1.00 10.38 ? 354 GLN   A N   1 
ATOM   2201 C  CA  . GLN   A 1 280 ? 34.894 -0.479  30.493  1.00 10.86 ? 354 GLN   A CA  1 
ATOM   2202 C  C   . GLN   A 1 280 ? 36.239 -0.890  29.945  1.00 10.73 ? 354 GLN   A C   1 
ATOM   2203 O  O   . GLN   A 1 280 ? 37.035 -0.036  29.552  1.00 11.32 ? 354 GLN   A O   1 
ATOM   2204 C  CB  . GLN   A 1 280 ? 33.837 -0.281  29.394  1.00 11.71 ? 354 GLN   A CB  1 
ATOM   2205 C  CG  . GLN   A 1 280 ? 33.526 -1.555  28.585  1.00 12.12 ? 354 GLN   A CG  1 
ATOM   2206 C  CD  . GLN   A 1 280 ? 34.345 -1.700  27.349  1.00 14.71 ? 354 GLN   A CD  1 
ATOM   2207 O  OE1 . GLN   A 1 280 ? 34.823 -0.666  26.817  1.00 16.40 ? 354 GLN   A OE1 1 
ATOM   2208 N  NE2 . GLN   A 1 280 ? 34.420 -2.904  26.832  1.00 14.95 ? 354 GLN   A NE2 1 
ATOM   2209 N  N   . MET   A 1 281 ? 36.492 -2.188  29.962  1.00 10.22 ? 355 MET   A N   1 
ATOM   2210 C  CA  . MET   A 1 281 ? 37.789 -2.764  29.634  1.00 11.83 ? 355 MET   A CA  1 
ATOM   2211 C  C   . MET   A 1 281 ? 37.605 -3.981  28.752  1.00 11.55 ? 355 MET   A C   1 
ATOM   2212 O  O   . MET   A 1 281 ? 36.721 -4.819  28.971  1.00 12.03 ? 355 MET   A O   1 
ATOM   2213 C  CB  . MET   A 1 281 ? 38.489 -3.272  30.922  1.00 14.66 ? 355 MET   A CB  1 
ATOM   2214 C  CG  . MET   A 1 281 ? 38.593 -2.179  32.015  1.00 17.00 ? 355 MET   A CG  1 
ATOM   2215 S  SD  . MET   A 1 281 ? 39.029 -2.794  33.655  1.00 24.06 ? 355 MET   A SD  1 
ATOM   2216 C  CE  . MET   A 1 281 ? 40.584 -3.136  32.929  1.00 18.14 ? 355 MET   A CE  1 
ATOM   2217 N  N   . TYR   A 1 282 ? 38.540 -4.126  27.808  1.00 11.55 ? 356 TYR   A N   1 
ATOM   2218 C  CA  . TYR   A 1 282 ? 38.666 -5.329  26.963  1.00 12.37 ? 356 TYR   A CA  1 
ATOM   2219 C  C   . TYR   A 1 282 ? 39.941 -5.152  26.156  1.00 13.19 ? 356 TYR   A C   1 
ATOM   2220 O  O   . TYR   A 1 282 ? 40.545 -4.078  26.154  1.00 14.10 ? 356 TYR   A O   1 
ATOM   2221 C  CB  . TYR   A 1 282 ? 37.443 -5.550  26.061  1.00 12.28 ? 356 TYR   A CB  1 
ATOM   2222 C  CG  . TYR   A 1 282 ? 37.489 -6.900  25.382  1.00 11.96 ? 356 TYR   A CG  1 
ATOM   2223 C  CD1 . TYR   A 1 282 ? 37.503 -8.062  26.118  1.00 12.74 ? 356 TYR   A CD1 1 
ATOM   2224 C  CD2 . TYR   A 1 282 ? 37.607 -6.996  24.015  1.00 12.63 ? 356 TYR   A CD2 1 
ATOM   2225 C  CE1 . TYR   A 1 282 ? 37.656 -9.296  25.508  1.00 12.93 ? 356 TYR   A CE1 1 
ATOM   2226 C  CE2 . TYR   A 1 282 ? 37.819 -8.217  23.389  1.00 13.76 ? 356 TYR   A CE2 1 
ATOM   2227 C  CZ  . TYR   A 1 282 ? 37.828 -9.354  24.142  1.00 13.00 ? 356 TYR   A CZ  1 
ATOM   2228 O  OH  . TYR   A 1 282 ? 38.056 -10.569 23.526  1.00 14.09 ? 356 TYR   A OH  1 
ATOM   2229 N  N   . TYR   A 1 283 ? 40.408 -6.180  25.444  1.00 12.16 ? 357 TYR   A N   1 
ATOM   2230 C  CA  . TYR   A 1 283 ? 41.472 -5.987  24.481  1.00 13.47 ? 357 TYR   A CA  1 
ATOM   2231 C  C   . TYR   A 1 283 ? 41.017 -4.939  23.477  1.00 14.82 ? 357 TYR   A C   1 
ATOM   2232 O  O   . TYR   A 1 283 ? 39.843 -4.681  23.290  1.00 15.63 ? 357 TYR   A O   1 
ATOM   2233 C  CB  . TYR   A 1 283 ? 41.783 -7.329  23.792  1.00 13.31 ? 357 TYR   A CB  1 
ATOM   2234 C  CG  . TYR   A 1 283 ? 42.253 -8.394  24.755  1.00 12.07 ? 357 TYR   A CG  1 
ATOM   2235 C  CD1 . TYR   A 1 283 ? 43.396 -8.228  25.501  1.00 13.19 ? 357 TYR   A CD1 1 
ATOM   2236 C  CD2 . TYR   A 1 283 ? 41.528 -9.553  24.940  1.00 12.70 ? 357 TYR   A CD2 1 
ATOM   2237 C  CE1 . TYR   A 1 283 ? 43.805 -9.174  26.412  1.00 12.62 ? 357 TYR   A CE1 1 
ATOM   2238 C  CE2 . TYR   A 1 283 ? 41.919 -10.504 25.834  1.00 13.47 ? 357 TYR   A CE2 1 
ATOM   2239 C  CZ  . TYR   A 1 283 ? 43.067 -10.337 26.567  1.00 12.97 ? 357 TYR   A CZ  1 
ATOM   2240 O  OH  . TYR   A 1 283 ? 43.436 -11.255 27.520  1.00 15.09 ? 357 TYR   A OH  1 
ATOM   2241 N  N   . PRO   A 1 284 ? 41.986 -4.323  22.756  1.00 15.69 ? 358 PRO   A N   1 
ATOM   2242 C  CA  . PRO   A 1 284 ? 41.634 -3.356  21.730  1.00 16.95 ? 358 PRO   A CA  1 
ATOM   2243 C  C   . PRO   A 1 284 ? 40.873 -4.096  20.641  1.00 20.56 ? 358 PRO   A C   1 
ATOM   2244 O  O   . PRO   A 1 284 ? 41.328 -5.139  20.206  1.00 24.13 ? 358 PRO   A O   1 
ATOM   2245 C  CB  . PRO   A 1 284 ? 42.986 -2.778  21.312  1.00 19.39 ? 358 PRO   A CB  1 
ATOM   2246 C  CG  . PRO   A 1 284 ? 44.001 -3.486  21.990  1.00 18.56 ? 358 PRO   A CG  1 
ATOM   2247 C  CD  . PRO   A 1 284 ? 43.411 -4.432  22.993  1.00 16.53 ? 358 PRO   A CD  1 
ATOM   2248 N  N   . ASP   A 1 285 ? 39.630 -3.746  20.331  1.00 19.59 ? 359 ASP   A N   1 
ATOM   2249 C  CA  . ASP   A 1 285 ? 38.769 -4.547  19.455  1.00 24.09 ? 359 ASP   A CA  1 
ATOM   2250 C  C   . ASP   A 1 285 ? 37.624 -3.553  19.212  1.00 22.51 ? 359 ASP   A C   1 
ATOM   2251 O  O   . ASP   A 1 285 ? 37.424 -2.559  19.955  1.00 23.61 ? 359 ASP   A O   1 
ATOM   2252 C  CB  . ASP   A 1 285 ? 38.543 -6.030  19.887  1.00 31.03 ? 359 ASP   A CB  1 
ATOM   2253 C  CG  . ASP   A 1 285 ? 37.967 -7.166  19.003  1.00 34.99 ? 359 ASP   A CG  1 
ATOM   2254 O  OD1 . ASP   A 1 285 ? 38.219 -8.380  19.297  1.00 32.86 ? 359 ASP   A OD1 1 
ATOM   2255 O  OD2 . ASP   A 1 285 ? 37.191 -6.947  18.037  1.00 28.82 ? 359 ASP   A OD2 1 
ATOM   2256 N  N   . MET   A 1 286 ? 37.005 -3.769  18.061  1.00 16.82 ? 360 MET   A N   1 
ATOM   2257 C  CA  . MET   A 1 286 ? 35.732 -3.120  17.776  1.00 15.29 ? 360 MET   A CA  1 
ATOM   2258 C  C   . MET   A 1 286 ? 34.543 -4.074  17.781  1.00 14.61 ? 360 MET   A C   1 
ATOM   2259 O  O   . MET   A 1 286 ? 33.421 -3.646  17.623  1.00 15.18 ? 360 MET   A O   1 
ATOM   2260 C  CB  . MET   A 1 286 ? 35.790 -2.388  16.429  1.00 15.54 ? 360 MET   A CB  1 
ATOM   2261 C  CG  . MET   A 1 286 ? 36.588 -1.099  16.500  1.00 17.40 ? 360 MET   A CG  1 
ATOM   2262 S  SD  . MET   A 1 286 ? 35.825 0.092   17.627  1.00 16.36 ? 360 MET   A SD  1 
ATOM   2263 C  CE  . MET   A 1 286 ? 34.278 0.380   16.772  1.00 18.39 ? 360 MET   A CE  1 
ATOM   2264 N  N   . GLN   A 1 287 ? 34.786 -5.361  18.036  1.00 15.60 ? 361 GLN   A N   1 
ATOM   2265 C  CA  . GLN   A 1 287 ? 33.670 -6.292  18.021  1.00 15.43 ? 361 GLN   A CA  1 
ATOM   2266 C  C   . GLN   A 1 287 ? 32.706 -6.064  19.177  1.00 14.21 ? 361 GLN   A C   1 
ATOM   2267 O  O   . GLN   A 1 287 ? 31.506 -6.117  18.978  1.00 14.38 ? 361 GLN   A O   1 
ATOM   2268 C  CB  . GLN   A 1 287 ? 34.121 -7.743  17.990  1.00 18.75 ? 361 GLN   A CB  1 
ATOM   2269 C  CG  . GLN   A 1 287 ? 34.823 -8.101  16.681  1.00 24.03 ? 361 GLN   A CG  1 
ATOM   2270 C  CD  . GLN   A 1 287 ? 35.259 -9.550  16.708  1.00 25.47 ? 361 GLN   A CD  1 
ATOM   2271 O  OE1 . GLN   A 1 287 ? 36.241 -9.939  17.367  1.00 32.15 ? 361 GLN   A OE1 1 
ATOM   2272 N  NE2 . GLN   A 1 287 ? 34.407 -10.362 16.128  1.00 28.35 ? 361 GLN   A NE2 1 
ATOM   2273 N  N   . ILE   A 1 288 ? 33.204 -5.763  20.390  1.00 13.14 ? 362 ILE   A N   1 
ATOM   2274 C  CA  . ILE   A 1 288 ? 32.287 -5.494  21.489  1.00 13.34 ? 362 ILE   A CA  1 
ATOM   2275 C  C   . ILE   A 1 288 ? 31.501 -4.209  21.270  1.00 11.87 ? 362 ILE   A C   1 
ATOM   2276 O  O   . ILE   A 1 288 ? 30.289 -4.247  21.472  1.00 13.95 ? 362 ILE   A O   1 
ATOM   2277 C  CB  . ILE   A 1 288 ? 32.948 -5.548  22.873  1.00 14.95 ? 362 ILE   A CB  1 
ATOM   2278 C  CG1 . ILE   A 1 288 ? 33.403 -6.998  23.169  1.00 17.06 ? 362 ILE   A CG1 1 
ATOM   2279 C  CG2 . ILE   A 1 288 ? 31.970 -5.018  23.949  1.00 17.37 ? 362 ILE   A CG2 1 
ATOM   2280 C  CD1 . ILE   A 1 288 ? 34.121 -7.233  24.491  1.00 18.25 ? 362 ILE   A CD1 1 
ATOM   2281 N  N   . PRO   A 1 289 ? 32.127 -3.078  20.913  1.00 12.33 ? 363 PRO   A N   1 
ATOM   2282 C  CA  . PRO   A 1 289 ? 31.311 -1.895  20.628  1.00 13.02 ? 363 PRO   A CA  1 
ATOM   2283 C  C   . PRO   A 1 289 ? 30.208 -2.121  19.593  1.00 13.21 ? 363 PRO   A C   1 
ATOM   2284 O  O   . PRO   A 1 289 ? 29.091 -1.645  19.757  1.00 13.58 ? 363 PRO   A O   1 
ATOM   2285 C  CB  . PRO   A 1 289 ? 32.370 -0.896  20.176  1.00 14.81 ? 363 PRO   A CB  1 
ATOM   2286 C  CG  . PRO   A 1 289 ? 33.626 -1.299  20.852  1.00 14.18 ? 363 PRO   A CG  1 
ATOM   2287 C  CD  . PRO   A 1 289 ? 33.541 -2.787  20.920  1.00 12.18 ? 363 PRO   A CD  1 
ATOM   2288 N  N   . ILE   A 1 290 ? 30.581 -2.781  18.511  1.00 13.07 ? 364 ILE   A N   1 
ATOM   2289 C  CA  . ILE   A 1 290 ? 29.571 -3.048  17.484  1.00 13.71 ? 364 ILE   A CA  1 
ATOM   2290 C  C   . ILE   A 1 290 ? 28.458 -3.959  18.016  1.00 14.81 ? 364 ILE   A C   1 
ATOM   2291 O  O   . ILE   A 1 290 ? 27.266 -3.674  17.887  1.00 15.30 ? 364 ILE   A O   1 
ATOM   2292 C  CB  . ILE   A 1 290 ? 30.214 -3.595  16.209  1.00 14.47 ? 364 ILE   A CB  1 
ATOM   2293 C  CG1 . ILE   A 1 290 ? 31.129 -2.593  15.565  1.00 14.02 ? 364 ILE   A CG1 1 
ATOM   2294 C  CG2 . ILE   A 1 290 ? 29.134 -4.092  15.239  1.00 16.88 ? 364 ILE   A CG2 1 
ATOM   2295 C  CD1 . ILE   A 1 290 ? 32.045 -3.182  14.541  1.00 15.83 ? 364 ILE   A CD1 1 
ATOM   2296 N  N   . LEU   A 1 291 ? 28.845 -5.048  18.679  1.00 14.38 ? 365 LEU   A N   1 
ATOM   2297 C  CA  . LEU   A 1 291 ? 27.842 -5.976  19.162  1.00 15.59 ? 365 LEU   A CA  1 
ATOM   2298 C  C   . LEU   A 1 291 ? 26.934 -5.327  20.177  1.00 15.36 ? 365 LEU   A C   1 
ATOM   2299 O  O   . LEU   A 1 291 ? 25.704 -5.465  20.143  1.00 16.20 ? 365 LEU   A O   1 
ATOM   2300 C  CB  . LEU   A 1 291 ? 28.506 -7.211  19.758  1.00 17.66 ? 365 LEU   A CB  1 
ATOM   2301 C  CG  . LEU   A 1 291 ? 27.516 -8.246  20.313  1.00 18.56 ? 365 LEU   A CG  1 
ATOM   2302 C  CD1 . LEU   A 1 291 ? 26.588 -8.731  19.246  1.00 19.63 ? 365 LEU   A CD1 1 
ATOM   2303 C  CD2 . LEU   A 1 291 ? 28.299 -9.388  20.969  1.00 20.01 ? 365 LEU   A CD2 1 
ATOM   2304 N  N   . TYR   A 1 292 ? 27.500 -4.597  21.133  1.00 14.16 ? 366 TYR   A N   1 
ATOM   2305 C  CA  . TYR   A 1 292 ? 26.695 -3.963  22.160  1.00 15.10 ? 366 TYR   A CA  1 
ATOM   2306 C  C   . TYR   A 1 292 ? 25.685 -2.976  21.570  1.00 15.14 ? 366 TYR   A C   1 
ATOM   2307 O  O   . TYR   A 1 292 ? 24.573 -2.852  22.065  1.00 15.86 ? 366 TYR   A O   1 
ATOM   2308 C  CB  . TYR   A 1 292 ? 27.540 -3.241  23.210  1.00 15.37 ? 366 TYR   A CB  1 
ATOM   2309 C  CG  . TYR   A 1 292 ? 26.769 -2.775  24.433  1.00 14.96 ? 366 TYR   A CG  1 
ATOM   2310 C  CD1 . TYR   A 1 292 ? 26.283 -3.668  25.366  1.00 16.87 ? 366 TYR   A CD1 1 
ATOM   2311 C  CD2 . TYR   A 1 292 ? 26.488 -1.443  24.658  1.00 16.50 ? 366 TYR   A CD2 1 
ATOM   2312 C  CE1 . TYR   A 1 292 ? 25.578 -3.254  26.487  1.00 17.85 ? 366 TYR   A CE1 1 
ATOM   2313 C  CE2 . TYR   A 1 292 ? 25.791 -1.019  25.774  1.00 15.47 ? 366 TYR   A CE2 1 
ATOM   2314 C  CZ  . TYR   A 1 292 ? 25.333 -1.914  26.699  1.00 16.74 ? 366 TYR   A CZ  1 
ATOM   2315 O  OH  . TYR   A 1 292 ? 24.645 -1.520  27.832  1.00 18.78 ? 366 TYR   A OH  1 
ATOM   2316 N  N   . SER   A 1 293 ? 26.091 -2.262  20.512  1.00 14.85 ? 367 SER   A N   1 
ATOM   2317 C  CA  . SER   A 1 293 ? 25.149 -1.336  19.895  1.00 15.08 ? 367 SER   A CA  1 
ATOM   2318 C  C   . SER   A 1 293 ? 23.924 -2.063  19.349  1.00 16.03 ? 367 SER   A C   1 
ATOM   2319 O  O   . SER   A 1 293 ? 22.853 -1.464  19.271  1.00 17.05 ? 367 SER   A O   1 
ATOM   2320 C  CB  . SER   A 1 293 ? 25.809 -0.546  18.785  1.00 15.67 ? 367 SER   A CB  1 
ATOM   2321 O  OG  . SER   A 1 293 ? 26.074 -1.240  17.602  1.00 15.30 ? 367 SER   A OG  1 
ATOM   2322 N  N   . LEU   A 1 294 ? 24.105 -3.304  18.912  1.00 15.87 ? 368 LEU   A N   1 
ATOM   2323 C  CA  . LEU   A 1 294 ? 22.999 -4.091  18.363  1.00 16.76 ? 368 LEU   A CA  1 
ATOM   2324 C  C   . LEU   A 1 294 ? 22.242 -4.899  19.418  1.00 18.27 ? 368 LEU   A C   1 
ATOM   2325 O  O   . LEU   A 1 294 ? 21.130 -5.385  19.115  1.00 19.69 ? 368 LEU   A O   1 
ATOM   2326 C  CB  . LEU   A 1 294 ? 23.593 -4.988  17.295  1.00 17.65 ? 368 LEU   A CB  1 
ATOM   2327 C  CG  . LEU   A 1 294 ? 24.185 -4.243  16.100  1.00 19.26 ? 368 LEU   A CG  1 
ATOM   2328 C  CD1 . LEU   A 1 294 ? 24.858 -5.175  15.133  1.00 20.91 ? 368 LEU   A CD1 1 
ATOM   2329 C  CD2 . LEU   A 1 294 ? 23.158 -3.359  15.406  1.00 20.57 ? 368 LEU   A CD2 1 
ATOM   2330 N  N   . THR   A 1 295 ? 22.788 -5.111  20.614  1.00 17.53 ? 369 THR   A N   1 
ATOM   2331 C  CA  . THR   A 1 295 ? 22.086 -5.897  21.637  1.00 17.81 ? 369 THR   A CA  1 
ATOM   2332 C  C   . THR   A 1 295 ? 21.497 -5.017  22.731  1.00 18.09 ? 369 THR   A C   1 
ATOM   2333 O  O   . THR   A 1 295 ? 20.576 -5.424  23.444  1.00 17.86 ? 369 THR   A O   1 
ATOM   2334 C  CB  . THR   A 1 295 ? 22.978 -6.957  22.288  1.00 19.71 ? 369 THR   A CB  1 
ATOM   2335 O  OG1 . THR   A 1 295 ? 24.078 -6.396  22.989  1.00 18.27 ? 369 THR   A OG1 1 
ATOM   2336 C  CG2 . THR   A 1 295 ? 23.443 -7.950  21.257  1.00 21.71 ? 369 THR   A CG2 1 
ATOM   2337 N  N   . TRP   A 1 296 ? 22.027 -3.806  22.929  1.00 16.47 ? 370 TRP   A N   1 
ATOM   2338 C  CA  . TRP   A 1 296 ? 21.573 -2.918  23.986  1.00 16.16 ? 370 TRP   A CA  1 
ATOM   2339 C  C   . TRP   A 1 296 ? 20.048 -2.876  23.961  1.00 18.00 ? 370 TRP   A C   1 
ATOM   2340 O  O   . TRP   A 1 296 ? 19.510 -2.715  22.876  1.00 19.04 ? 370 TRP   A O   1 
ATOM   2341 C  CB  . TRP   A 1 296 ? 22.161 -1.505  23.746  1.00 16.33 ? 370 TRP   A CB  1 
ATOM   2342 C  CG  . TRP   A 1 296 ? 21.615 -0.524  24.737  1.00 15.88 ? 370 TRP   A CG  1 
ATOM   2343 C  CD1 . TRP   A 1 296 ? 22.118 -0.209  25.967  1.00 17.15 ? 370 TRP   A CD1 1 
ATOM   2344 C  CD2 . TRP   A 1 296 ? 20.386 0.230   24.607  1.00 16.78 ? 370 TRP   A CD2 1 
ATOM   2345 N  NE1 . TRP   A 1 296 ? 21.271 0.643   26.611  1.00 18.39 ? 370 TRP   A NE1 1 
ATOM   2346 C  CE2 . TRP   A 1 296 ? 20.215 0.943   25.802  1.00 17.65 ? 370 TRP   A CE2 1 
ATOM   2347 C  CE3 . TRP   A 1 296 ? 19.446 0.358   23.584  1.00 18.30 ? 370 TRP   A CE3 1 
ATOM   2348 C  CZ2 . TRP   A 1 296 ? 19.111 1.774   26.025  1.00 18.68 ? 370 TRP   A CZ2 1 
ATOM   2349 C  CZ3 . TRP   A 1 296 ? 18.332 1.154   23.825  1.00 18.89 ? 370 TRP   A CZ3 1 
ATOM   2350 C  CH2 . TRP   A 1 296 ? 18.181 1.823   25.014  1.00 19.10 ? 370 TRP   A CH2 1 
ATOM   2351 N  N   . PRO   A 1 297 ? 19.358 -2.920  25.105  1.00 17.43 ? 371 PRO   A N   1 
ATOM   2352 C  CA  . PRO   A 1 297 ? 19.891 -2.886  26.465  1.00 18.27 ? 371 PRO   A CA  1 
ATOM   2353 C  C   . PRO   A 1 297 ? 20.340 -4.202  27.083  1.00 18.90 ? 371 PRO   A C   1 
ATOM   2354 O  O   . PRO   A 1 297 ? 20.612 -4.247  28.272  1.00 22.02 ? 371 PRO   A O   1 
ATOM   2355 C  CB  . PRO   A 1 297 ? 18.725 -2.265  27.230  1.00 21.66 ? 371 PRO   A CB  1 
ATOM   2356 C  CG  . PRO   A 1 297 ? 17.548 -2.836  26.551  1.00 22.26 ? 371 PRO   A CG  1 
ATOM   2357 C  CD  . PRO   A 1 297 ? 17.883 -2.799  25.106  1.00 19.09 ? 371 PRO   A CD  1 
ATOM   2358 N  N   . ASP   A 1 298 ? 20.442 -5.234  26.277  1.00 18.13 ? 372 ASP   A N   1 
ATOM   2359 C  CA  . ASP   A 1 298 ? 20.898 -6.522  26.755  1.00 18.38 ? 372 ASP   A CA  1 
ATOM   2360 C  C   . ASP   A 1 298 ? 22.341 -6.776  26.333  1.00 18.00 ? 372 ASP   A C   1 
ATOM   2361 O  O   . ASP   A 1 298 ? 22.887 -6.072  25.489  1.00 17.90 ? 372 ASP   A O   1 
ATOM   2362 C  CB  . ASP   A 1 298 ? 19.955 -7.596  26.226  1.00 21.32 ? 372 ASP   A CB  1 
ATOM   2363 C  CG  . ASP   A 1 298 ? 18.536 -7.460  26.751  1.00 28.68 ? 372 ASP   A CG  1 
ATOM   2364 O  OD1 . ASP   A 1 298 ? 18.358 -7.072  27.945  1.00 31.86 ? 372 ASP   A OD1 1 
ATOM   2365 O  OD2 . ASP   A 1 298 ? 17.640 -7.743  25.957  1.00 38.67 ? 372 ASP   A OD2 1 
ATOM   2366 N  N   . ARG   A 1 299 ? 22.874 -7.894  26.813  1.00 15.91 ? 373 ARG   A N   1 
ATOM   2367 C  CA  . ARG   A 1 299 ? 24.108 -8.482  26.347  1.00 15.81 ? 373 ARG   A CA  1 
ATOM   2368 C  C   . ARG   A 1 299 ? 23.867 -9.941  25.993  1.00 16.85 ? 373 ARG   A C   1 
ATOM   2369 O  O   . ARG   A 1 299 ? 22.964 -10.547 26.584  1.00 18.93 ? 373 ARG   A O   1 
ATOM   2370 C  CB  . ARG   A 1 299 ? 25.214 -8.437  27.411  1.00 15.36 ? 373 ARG   A CB  1 
ATOM   2371 C  CG  . ARG   A 1 299 ? 25.659 -7.031  27.784  1.00 15.05 ? 373 ARG   A CG  1 
ATOM   2372 C  CD  . ARG   A 1 299 ? 26.732 -7.058  28.871  1.00 14.99 ? 373 ARG   A CD  1 
ATOM   2373 N  NE  . ARG   A 1 299 ? 27.159 -5.730  29.286  1.00 14.80 ? 373 ARG   A NE  1 
ATOM   2374 C  CZ  . ARG   A 1 299 ? 28.024 -4.958  28.657  1.00 14.83 ? 373 ARG   A CZ  1 
ATOM   2375 N  NH1 . ARG   A 1 299 ? 28.552 -5.291  27.510  1.00 14.66 ? 373 ARG   A NH1 1 
ATOM   2376 N  NH2 . ARG   A 1 299 ? 28.325 -3.777  29.152  1.00 15.72 ? 373 ARG   A NH2 1 
ATOM   2377 N  N   . ILE   A 1 300 ? 24.605 -10.450 25.024  1.00 15.10 ? 374 ILE   A N   1 
ATOM   2378 C  CA  . ILE   A 1 300 ? 24.470 -11.844 24.635  1.00 16.25 ? 374 ILE   A CA  1 
ATOM   2379 C  C   . ILE   A 1 300 ? 25.807 -12.551 24.801  1.00 15.05 ? 374 ILE   A C   1 
ATOM   2380 O  O   . ILE   A 1 300 ? 26.885 -11.920 24.761  1.00 15.67 ? 374 ILE   A O   1 
ATOM   2381 C  CB  . ILE   A 1 300 ? 23.936 -11.997 23.179  1.00 17.31 ? 374 ILE   A CB  1 
ATOM   2382 C  CG1 . ILE   A 1 300 ? 24.955 -11.571 22.130  1.00 18.00 ? 374 ILE   A CG1 1 
ATOM   2383 C  CG2 . ILE   A 1 300 ? 22.596 -11.247 23.027  1.00 18.58 ? 374 ILE   A CG2 1 
ATOM   2384 C  CD1 . ILE   A 1 300 ? 24.510 -11.807 20.681  1.00 20.29 ? 374 ILE   A CD1 1 
ATOM   2385 N  N   . LYS   A 1 301 ? 25.757 -13.876 24.853  1.00 15.59 ? 375 LYS   A N   1 
ATOM   2386 C  CA  . LYS   A 1 301 ? 26.943 -14.685 24.970  1.00 15.97 ? 375 LYS   A CA  1 
ATOM   2387 C  C   . LYS   A 1 301 ? 27.813 -14.601 23.734  1.00 17.86 ? 375 LYS   A C   1 
ATOM   2388 O  O   . LYS   A 1 301 ? 27.316 -14.631 22.592  1.00 19.08 ? 375 LYS   A O   1 
ATOM   2389 C  CB  . LYS   A 1 301 ? 26.558 -16.148 25.219  1.00 18.80 ? 375 LYS   A CB  1 
ATOM   2390 C  CG  . LYS   A 1 301 ? 27.753 -17.090 25.447  1.00 23.09 ? 375 LYS   A CG  1 
ATOM   2391 C  CD  . LYS   A 1 301 ? 27.370 -18.513 25.807  1.00 30.16 ? 375 LYS   A CD  1 
ATOM   2392 C  CE  . LYS   A 1 301 ? 28.612 -19.366 25.929  1.00 37.17 ? 375 LYS   A CE  1 
ATOM   2393 N  NZ  . LYS   A 1 301 ? 28.292 -20.796 25.977  1.00 44.11 ? 375 LYS   A NZ  1 
ATOM   2394 N  N   . THR   A 1 302 ? 29.126 -14.460 23.926  1.00 15.77 ? 376 THR   A N   1 
ATOM   2395 C  CA  . THR   A 1 302 ? 30.081 -14.618 22.835  1.00 15.78 ? 376 THR   A CA  1 
ATOM   2396 C  C   . THR   A 1 302 ? 31.175 -15.611 23.264  1.00 15.48 ? 376 THR   A C   1 
ATOM   2397 O  O   . THR   A 1 302 ? 31.282 -15.979 24.419  1.00 18.01 ? 376 THR   A O   1 
ATOM   2398 C  CB  . THR   A 1 302 ? 30.758 -13.306 22.440  1.00 15.72 ? 376 THR   A CB  1 
ATOM   2399 O  OG1 . THR   A 1 302 ? 31.740 -12.977 23.443  1.00 15.12 ? 376 THR   A OG1 1 
ATOM   2400 C  CG2 . THR   A 1 302 ? 29.812 -12.146 22.218  1.00 15.69 ? 376 THR   A CG2 1 
ATOM   2401 N  N   . ASN   A 1 303 ? 32.028 -15.960 22.310  1.00 16.96 ? 377 ASN   A N   1 
ATOM   2402 C  CA  . ASN   A 1 303 ? 33.189 -16.782 22.603  1.00 18.26 ? 377 ASN   A CA  1 
ATOM   2403 C  C   . ASN   A 1 303 ? 34.467 -15.990 22.368  1.00 17.87 ? 377 ASN   A C   1 
ATOM   2404 O  O   . ASN   A 1 303 ? 35.524 -16.547 22.035  1.00 18.09 ? 377 ASN   A O   1 
ATOM   2405 C  CB  . ASN   A 1 303 ? 33.133 -18.110 21.851  1.00 22.73 ? 377 ASN   A CB  1 
ATOM   2406 C  CG  . ASN   A 1 303 ? 32.075 -19.031 22.435  1.00 27.45 ? 377 ASN   A CG  1 
ATOM   2407 O  OD1 . ASN   A 1 303 ? 31.259 -19.590 21.692  1.00 41.67 ? 377 ASN   A OD1 1 
ATOM   2408 N  ND2 . ASN   A 1 303 ? 32.057 -19.243 23.740  1.00 30.36 ? 377 ASN   A ND2 1 
ATOM   2409 N  N   . LEU   A 1 304 ? 34.406 -14.662 22.580  1.00 14.94 ? 378 LEU   A N   1 
ATOM   2410 C  CA  . LEU   A 1 304 ? 35.587 -13.838 22.467  1.00 14.76 ? 378 LEU   A CA  1 
ATOM   2411 C  C   . LEU   A 1 304 ? 36.636 -14.253 23.500  1.00 13.59 ? 378 LEU   A C   1 
ATOM   2412 O  O   . LEU   A 1 304 ? 36.324 -14.747 24.566  1.00 14.74 ? 378 LEU   A O   1 
ATOM   2413 C  CB  . LEU   A 1 304 ? 35.192 -12.371 22.623  1.00 15.82 ? 378 LEU   A CB  1 
ATOM   2414 C  CG  . LEU   A 1 304 ? 34.464 -11.724 21.440  1.00 19.44 ? 378 LEU   A CG  1 
ATOM   2415 C  CD1 . LEU   A 1 304 ? 34.100 -10.290 21.815  1.00 19.44 ? 378 LEU   A CD1 1 
ATOM   2416 C  CD2 . LEU   A 1 304 ? 35.233 -11.718 20.171  1.00 23.45 ? 378 LEU   A CD2 1 
ATOM   2417 N  N   . LYS   A 1 305 ? 37.878 -14.000 23.138  1.00 13.69 ? 379 LYS   A N   1 
ATOM   2418 C  CA  . LYS   A 1 305 ? 39.026 -14.244 24.008  1.00 13.86 ? 379 LYS   A CA  1 
ATOM   2419 C  C   . LYS   A 1 305 ? 38.838 -13.502 25.333  1.00 13.93 ? 379 LYS   A C   1 
ATOM   2420 O  O   . LYS   A 1 305 ? 38.665 -12.295 25.321  1.00 13.66 ? 379 LYS   A O   1 
ATOM   2421 C  CB  . LYS   A 1 305 ? 40.288 -13.749 23.292  1.00 14.54 ? 379 LYS   A CB  1 
ATOM   2422 C  CG  . LYS   A 1 305 ? 41.618 -14.044 23.944  1.00 14.42 ? 379 LYS   A CG  1 
ATOM   2423 C  CD  . LYS   A 1 305 ? 42.782 -13.331 23.280  1.00 14.24 ? 379 LYS   A CD  1 
ATOM   2424 C  CE  . LYS   A 1 305 ? 42.921 -13.750 21.843  1.00 15.37 ? 379 LYS   A CE  1 
ATOM   2425 N  NZ  . LYS   A 1 305 ? 44.049 -13.050 21.211  1.00 16.92 ? 379 LYS   A NZ  1 
ATOM   2426 N  N   . PRO   A 1 306 ? 38.928 -14.151 26.492  1.00 13.04 ? 380 PRO   A N   1 
ATOM   2427 C  CA  . PRO   A 1 306 ? 38.680 -13.435 27.763  1.00 13.28 ? 380 PRO   A CA  1 
ATOM   2428 C  C   . PRO   A 1 306 ? 39.848 -12.526 28.084  1.00 13.19 ? 380 PRO   A C   1 
ATOM   2429 O  O   . PRO   A 1 306 ? 41.026 -12.880 27.977  1.00 13.44 ? 380 PRO   A O   1 
ATOM   2430 C  CB  . PRO   A 1 306 ? 38.540 -14.469 28.818  1.00 16.33 ? 380 PRO   A CB  1 
ATOM   2431 C  CG  . PRO   A 1 306 ? 38.800 -15.766 28.159  1.00 19.28 ? 380 PRO   A CG  1 
ATOM   2432 C  CD  . PRO   A 1 306 ? 39.056 -15.608 26.671  1.00 15.88 ? 380 PRO   A CD  1 
ATOM   2433 N  N   . LEU   A 1 307 ? 39.518 -11.350 28.642  1.00 11.98 ? 381 LEU   A N   1 
ATOM   2434 C  CA  . LEU   A 1 307 ? 40.516 -10.467 29.220  1.00 11.82 ? 381 LEU   A CA  1 
ATOM   2435 C  C   . LEU   A 1 307 ? 41.243 -11.165 30.361  1.00 11.53 ? 381 LEU   A C   1 
ATOM   2436 O  O   . LEU   A 1 307 ? 40.641 -11.812 31.207  1.00 13.90 ? 381 LEU   A O   1 
ATOM   2437 C  CB  . LEU   A 1 307 ? 39.840 -9.181  29.726  1.00 12.25 ? 381 LEU   A CB  1 
ATOM   2438 C  CG  . LEU   A 1 307 ? 40.804 -8.106  30.252  1.00 12.57 ? 381 LEU   A CG  1 
ATOM   2439 C  CD1 . LEU   A 1 307 ? 41.759 -7.608  29.153  1.00 13.02 ? 381 LEU   A CD1 1 
ATOM   2440 C  CD2 . LEU   A 1 307 ? 39.992 -6.942  30.835  1.00 13.80 ? 381 LEU   A CD2 1 
ATOM   2441 N  N   . ASP   A 1 308 ? 42.567 -11.007 30.422  1.00 11.37 ? 382 ASP   A N   1 
ATOM   2442 C  CA  . ASP   A 1 308 ? 43.406 -11.644 31.434  1.00 12.26 ? 382 ASP   A CA  1 
ATOM   2443 C  C   . ASP   A 1 308 ? 44.306 -10.586 31.995  1.00 11.88 ? 382 ASP   A C   1 
ATOM   2444 O  O   . ASP   A 1 308 ? 45.209 -10.125 31.365  1.00 12.79 ? 382 ASP   A O   1 
ATOM   2445 C  CB  . ASP   A 1 308 ? 44.199 -12.755 30.760  1.00 12.77 ? 382 ASP   A CB  1 
ATOM   2446 C  CG  . ASP   A 1 308 ? 45.166 -13.519 31.618  1.00 14.89 ? 382 ASP   A CG  1 
ATOM   2447 O  OD1 . ASP   A 1 308 ? 45.538 -13.044 32.683  1.00 14.50 ? 382 ASP   A OD1 1 
ATOM   2448 O  OD2 . ASP   A 1 308 ? 45.591 -14.619 31.146  1.00 16.84 ? 382 ASP   A OD2 1 
ATOM   2449 N  N   . LEU   A 1 309 ? 43.970 -10.109 33.230  1.00 11.79 ? 383 LEU   A N   1 
ATOM   2450 C  CA  . LEU   A 1 309 ? 44.687 -8.967  33.798  1.00 12.72 ? 383 LEU   A CA  1 
ATOM   2451 C  C   . LEU   A 1 309 ? 46.125 -9.280  34.200  1.00 11.72 ? 383 LEU   A C   1 
ATOM   2452 O  O   . LEU   A 1 309 ? 46.985 -8.418  34.023  1.00 13.12 ? 383 LEU   A O   1 
ATOM   2453 C  CB  . LEU   A 1 309 ? 43.956 -8.436  35.026  1.00 14.01 ? 383 LEU   A CB  1 
ATOM   2454 C  CG  . LEU   A 1 309 ? 42.630 -7.771  34.705  1.00 15.72 ? 383 LEU   A CG  1 
ATOM   2455 C  CD1 . LEU   A 1 309 ? 41.970 -7.342  36.031  1.00 16.59 ? 383 LEU   A CD1 1 
ATOM   2456 C  CD2 . LEU   A 1 309 ? 42.737 -6.633  33.790  1.00 17.34 ? 383 LEU   A CD2 1 
ATOM   2457 N  N   . ALA   A 1 310 ? 46.394 -10.489 34.659  1.00 12.57 ? 384 ALA   A N   1 
ATOM   2458 C  CA  . ALA   A 1 310 ? 47.782 -10.836 34.946  1.00 13.75 ? 384 ALA   A CA  1 
ATOM   2459 C  C   . ALA   A 1 310 ? 48.610 -10.843 33.663  1.00 13.34 ? 384 ALA   A C   1 
ATOM   2460 O  O   . ALA   A 1 310 ? 49.798 -10.500 33.662  1.00 14.77 ? 384 ALA   A O   1 
ATOM   2461 C  CB  . ALA   A 1 310 ? 47.848 -12.185 35.637  1.00 15.22 ? 384 ALA   A CB  1 
ATOM   2462 N  N   . GLN   A 1 311 ? 48.003 -11.238 32.539  1.00 12.91 ? 385 GLN   A N   1 
ATOM   2463 C  CA  . GLN   A 1 311 ? 48.669 -11.231 31.241  1.00 13.10 ? 385 GLN   A CA  1 
ATOM   2464 C  C   . GLN   A 1 311 ? 49.002 -9.811  30.821  1.00 13.40 ? 385 GLN   A C   1 
ATOM   2465 O  O   . GLN   A 1 311 ? 50.085 -9.516  30.327  1.00 14.46 ? 385 GLN   A O   1 
ATOM   2466 C  CB  . GLN   A 1 311 ? 47.773 -11.945 30.243  1.00 13.26 ? 385 GLN   A CB  1 
ATOM   2467 C  CG  . GLN   A 1 311 ? 48.359 -12.057 28.838  1.00 14.72 ? 385 GLN   A CG  1 
ATOM   2468 C  CD  . GLN   A 1 311 ? 47.315 -12.492 27.848  1.00 14.41 ? 385 GLN   A CD  1 
ATOM   2469 O  OE1 . GLN   A 1 311 ? 46.514 -13.397 28.059  1.00 16.48 ? 385 GLN   A OE1 1 
ATOM   2470 N  NE2 . GLN   A 1 311 ? 47.354 -11.854 26.715  1.00 15.15 ? 385 GLN   A NE2 1 
ATOM   2471 N  N   . VAL   A 1 312 ? 48.016 -8.907  30.986  1.00 13.27 ? 386 VAL   A N   1 
ATOM   2472 C  CA  . VAL   A 1 312 ? 48.213 -7.507  30.673  1.00 14.23 ? 386 VAL   A CA  1 
ATOM   2473 C  C   . VAL   A 1 312 ? 49.340 -6.891  31.505  1.00 13.64 ? 386 VAL   A C   1 
ATOM   2474 O  O   . VAL   A 1 312 ? 50.185 -6.146  31.027  1.00 14.48 ? 386 VAL   A O   1 
ATOM   2475 C  CB  . VAL   A 1 312 ? 46.852 -6.812  30.925  1.00 16.24 ? 386 VAL   A CB  1 
ATOM   2476 C  CG1 . VAL   A 1 312 ? 46.985 -5.314  30.896  1.00 18.18 ? 386 VAL   A CG1 1 
ATOM   2477 C  CG2 . VAL   A 1 312 ? 45.807 -7.209  29.891  1.00 16.07 ? 386 VAL   A CG2 1 
ATOM   2478 N  N   . SER   A 1 313 ? 49.273 -7.177  32.815  1.00 12.43 ? 387 SER   A N   1 
ATOM   2479 C  CA  . SER   A 1 313 ? 50.276 -6.843  33.814  1.00 12.63 ? 387 SER   A CA  1 
ATOM   2480 C  C   . SER   A 1 313 ? 50.317 -5.364  34.224  1.00 12.47 ? 387 SER   A C   1 
ATOM   2481 O  O   . SER   A 1 313 ? 50.321 -5.067  35.432  1.00 13.61 ? 387 SER   A O   1 
ATOM   2482 C  CB  . SER   A 1 313 ? 51.668 -7.342  33.344  1.00 14.30 ? 387 SER   A CB  1 
ATOM   2483 O  OG  . SER   A 1 313 ? 52.638 -7.079  34.340  1.00 16.88 ? 387 SER   A OG  1 
ATOM   2484 N  N   . THR   A 1 314 ? 50.408 -4.452  33.260  1.00 13.40 ? 388 THR   A N   1 
ATOM   2485 C  CA  . THR   A 1 314 ? 50.577 -3.020  33.532  1.00 14.12 ? 388 THR   A CA  1 
ATOM   2486 C  C   . THR   A 1 314 ? 49.668 -2.212  32.623  1.00 13.86 ? 388 THR   A C   1 
ATOM   2487 O  O   . THR   A 1 314 ? 49.544 -2.497  31.408  1.00 15.41 ? 388 THR   A O   1 
ATOM   2488 C  CB  . THR   A 1 314 ? 52.019 -2.523  33.375  1.00 18.18 ? 388 THR   A CB  1 
ATOM   2489 O  OG1 . THR   A 1 314 ? 52.852 -3.131  34.372  1.00 23.64 ? 388 THR   A OG1 1 
ATOM   2490 C  CG2 . THR   A 1 314 ? 52.189 -1.062  33.750  1.00 24.35 ? 388 THR   A CG2 1 
ATOM   2491 N  N   . LEU   A 1 315 ? 49.005 -1.216  33.206  1.00 12.85 ? 389 LEU   A N   1 
ATOM   2492 C  CA  . LEU   A 1 315 ? 48.217 -0.229  32.495  1.00 12.98 ? 389 LEU   A CA  1 
ATOM   2493 C  C   . LEU   A 1 315 ? 48.815 1.129   32.798  1.00 13.23 ? 389 LEU   A C   1 
ATOM   2494 O  O   . LEU   A 1 315 ? 49.101 1.416   33.976  1.00 14.60 ? 389 LEU   A O   1 
ATOM   2495 C  CB  . LEU   A 1 315 ? 46.770 -0.246  32.923  1.00 13.43 ? 389 LEU   A CB  1 
ATOM   2496 C  CG  . LEU   A 1 315 ? 46.026 -1.552  32.746  1.00 14.88 ? 389 LEU   A CG  1 
ATOM   2497 C  CD1 . LEU   A 1 315 ? 44.644 -1.490  33.398  1.00 18.27 ? 389 LEU   A CD1 1 
ATOM   2498 C  CD2 . LEU   A 1 315 ? 45.971 -1.991  31.331  1.00 17.47 ? 389 LEU   A CD2 1 
ATOM   2499 N  N   . THR   A 1 316 ? 48.992 1.980   31.802  1.00 11.94 ? 390 THR   A N   1 
ATOM   2500 C  CA  . THR   A 1 316 ? 49.631 3.274   31.996  1.00 12.00 ? 390 THR   A CA  1 
ATOM   2501 C  C   . THR   A 1 316 ? 48.763 4.411   31.502  1.00 11.34 ? 390 THR   A C   1 
ATOM   2502 O  O   . THR   A 1 316 ? 47.987 4.254   30.570  1.00 11.65 ? 390 THR   A O   1 
ATOM   2503 C  CB  . THR   A 1 316 ? 50.979 3.333   31.300  1.00 13.40 ? 390 THR   A CB  1 
ATOM   2504 O  OG1 . THR   A 1 316 ? 50.913 3.203   29.901  1.00 15.78 ? 390 THR   A OG1 1 
ATOM   2505 C  CG2 . THR   A 1 316 ? 51.898 2.229   31.711  1.00 16.39 ? 390 THR   A CG2 1 
ATOM   2506 N  N   . PHE   A 1 317 ? 48.953 5.589   32.090  1.00 11.21 ? 391 PHE   A N   1 
ATOM   2507 C  CA  . PHE   A 1 317 ? 48.151 6.768   31.777  1.00 11.50 ? 391 PHE   A CA  1 
ATOM   2508 C  C   . PHE   A 1 317 ? 49.063 7.977   31.799  1.00 12.14 ? 391 PHE   A C   1 
ATOM   2509 O  O   . PHE   A 1 317 ? 49.767 8.197   32.808  1.00 13.15 ? 391 PHE   A O   1 
ATOM   2510 C  CB  . PHE   A 1 317 ? 47.051 6.960   32.832  1.00 12.86 ? 391 PHE   A CB  1 
ATOM   2511 C  CG  . PHE   A 1 317 ? 46.215 5.705   32.935  1.00 14.76 ? 391 PHE   A CG  1 
ATOM   2512 C  CD1 . PHE   A 1 317 ? 45.148 5.472   32.109  1.00 15.23 ? 391 PHE   A CD1 1 
ATOM   2513 C  CD2 . PHE   A 1 317 ? 46.610 4.681   33.801  1.00 17.22 ? 391 PHE   A CD2 1 
ATOM   2514 C  CE1 . PHE   A 1 317 ? 44.412 4.258   32.221  1.00 16.80 ? 391 PHE   A CE1 1 
ATOM   2515 C  CE2 . PHE   A 1 317 ? 45.960 3.450   33.814  1.00 21.23 ? 391 PHE   A CE2 1 
ATOM   2516 C  CZ  . PHE   A 1 317 ? 44.847 3.290   33.069  1.00 19.82 ? 391 PHE   A CZ  1 
ATOM   2517 N  N   . HIS   A 1 318 ? 48.977 8.823   30.770  1.00 11.60 ? 392 HIS   A N   1 
ATOM   2518 C  CA  . HIS   A 1 318 ? 49.678 10.099  30.788  1.00 12.21 ? 392 HIS   A CA  1 
ATOM   2519 C  C   . HIS   A 1 318 ? 48.897 11.135  30.024  1.00 12.38 ? 392 HIS   A C   1 
ATOM   2520 O  O   . HIS   A 1 318 ? 48.125 10.818  29.137  1.00 13.48 ? 392 HIS   A O   1 
ATOM   2521 C  CB  . HIS   A 1 318 ? 51.108 10.011  30.278  1.00 14.82 ? 392 HIS   A CB  1 
ATOM   2522 C  CG  . HIS   A 1 318 ? 51.292 9.709   28.882  1.00 17.23 ? 392 HIS   A CG  1 
ATOM   2523 N  ND1 . HIS   A 1 318 ? 51.531 8.447   28.393  1.00 19.30 ? 392 HIS   A ND1 1 
ATOM   2524 C  CD2 . HIS   A 1 318 ? 51.383 10.548  27.805  1.00 16.42 ? 392 HIS   A CD2 1 
ATOM   2525 C  CE1 . HIS   A 1 318 ? 51.755 8.546   27.057  1.00 19.31 ? 392 HIS   A CE1 1 
ATOM   2526 N  NE2 . HIS   A 1 318 ? 51.681 9.801   26.674  1.00 18.06 ? 392 HIS   A NE2 1 
ATOM   2527 N  N   . LYS   A 1 319 ? 49.161 12.396  30.293  1.00 13.78 ? 393 LYS   A N   1 
ATOM   2528 C  CA  . LYS   A 1 319 ? 48.515 13.450  29.536  1.00 14.78 ? 393 LYS   A CA  1 
ATOM   2529 C  C   . LYS   A 1 319 ? 49.192 13.627  28.190  1.00 14.64 ? 393 LYS   A C   1 
ATOM   2530 O  O   . LYS   A 1 319 ? 50.398 13.515  28.092  1.00 15.75 ? 393 LYS   A O   1 
ATOM   2531 C  CB  . LYS   A 1 319 ? 48.456 14.773  30.291  1.00 20.56 ? 393 LYS   A CB  1 
ATOM   2532 C  CG  . LYS   A 1 319 ? 47.367 14.625  31.383  1.00 25.79 ? 393 LYS   A CG  1 
ATOM   2533 C  CD  . LYS   A 1 319 ? 45.875 14.344  31.068  1.00 26.35 ? 393 LYS   A CD  1 
ATOM   2534 C  CE  . LYS   A 1 319 ? 45.003 15.506  30.688  1.00 33.25 ? 393 LYS   A CE  1 
ATOM   2535 N  NZ  . LYS   A 1 319 ? 44.856 15.862  29.264  1.00 29.90 ? 393 LYS   A NZ  1 
ATOM   2536 N  N   . PRO   A 1 320 ? 48.454 13.913  27.117  1.00 14.14 ? 394 PRO   A N   1 
ATOM   2537 C  CA  . PRO   A 1 320 ? 49.092 14.220  25.839  1.00 14.34 ? 394 PRO   A CA  1 
ATOM   2538 C  C   . PRO   A 1 320 ? 49.728 15.614  25.860  1.00 14.67 ? 394 PRO   A C   1 
ATOM   2539 O  O   . PRO   A 1 320 ? 49.199 16.528  26.497  1.00 16.59 ? 394 PRO   A O   1 
ATOM   2540 C  CB  . PRO   A 1 320 ? 47.931 14.168  24.841  1.00 16.56 ? 394 PRO   A CB  1 
ATOM   2541 C  CG  . PRO   A 1 320 ? 46.783 14.534  25.592  1.00 16.39 ? 394 PRO   A CG  1 
ATOM   2542 C  CD  . PRO   A 1 320 ? 47.003 14.031  27.037  1.00 17.12 ? 394 PRO   A CD  1 
ATOM   2543 N  N   . SER   A 1 321 ? 50.828 15.729  25.136  1.00 15.01 ? 395 SER   A N   1 
ATOM   2544 C  CA  . SER   A 1 321 ? 51.484 17.016  24.925  1.00 16.03 ? 395 SER   A CA  1 
ATOM   2545 C  C   . SER   A 1 321 ? 50.752 17.804  23.836  1.00 15.19 ? 395 SER   A C   1 
ATOM   2546 O  O   . SER   A 1 321 ? 50.717 17.399  22.680  1.00 15.45 ? 395 SER   A O   1 
ATOM   2547 C  CB  . SER   A 1 321 ? 52.892 16.811  24.514  1.00 18.76 ? 395 SER   A CB  1 
ATOM   2548 O  OG  . SER   A 1 321 ? 53.418 18.069  24.048  1.00 22.47 ? 395 SER   A OG  1 
ATOM   2549 N  N   . LEU   A 1 322 ? 50.213 18.979  24.159  1.00 16.27 ? 396 LEU   A N   1 
ATOM   2550 C  CA  . LEU   A 1 322 ? 49.515 19.832  23.213  1.00 17.37 ? 396 LEU   A CA  1 
ATOM   2551 C  C   . LEU   A 1 322 ? 50.493 20.494  22.248  1.00 16.51 ? 396 LEU   A C   1 
ATOM   2552 O  O   . LEU   A 1 322 ? 50.067 20.850  21.140  1.00 18.46 ? 396 LEU   A O   1 
ATOM   2553 C  CB  . LEU   A 1 322 ? 48.697 20.894  23.927  1.00 18.62 ? 396 LEU   A CB  1 
ATOM   2554 C  CG  . LEU   A 1 322 ? 47.601 20.338  24.840  1.00 22.49 ? 396 LEU   A CG  1 
ATOM   2555 C  CD1 . LEU   A 1 322 ? 46.808 21.438  25.493  1.00 24.97 ? 396 LEU   A CD1 1 
ATOM   2556 C  CD2 . LEU   A 1 322 ? 46.644 19.421  24.105  1.00 22.37 ? 396 LEU   A CD2 1 
ATOM   2557 N  N   . GLU   A 1 323 ? 51.774 20.567  22.596  1.00 15.75 ? 397 GLU   A N   1 
ATOM   2558 C  CA  . GLU   A 1 323 ? 52.781 21.069  21.664  1.00 18.46 ? 397 GLU   A CA  1 
ATOM   2559 C  C   . GLU   A 1 323 ? 52.986 20.076  20.536  1.00 16.19 ? 397 GLU   A C   1 
ATOM   2560 O  O   . GLU   A 1 323 ? 53.156 20.434  19.366  1.00 17.38 ? 397 GLU   A O   1 
ATOM   2561 C  CB  . GLU   A 1 323 ? 54.083 21.357  22.418  1.00 20.49 ? 397 GLU   A CB  1 
ATOM   2562 C  CG  . GLU   A 1 323 ? 55.195 21.934  21.556  1.00 25.78 ? 397 GLU   A CG  1 
ATOM   2563 C  CD  . GLU   A 1 323 ? 56.551 21.978  22.238  1.00 31.50 ? 397 GLU   A CD  1 
ATOM   2564 O  OE1 . GLU   A 1 323 ? 56.853 21.165  23.153  1.00 37.35 ? 397 GLU   A OE1 1 
ATOM   2565 O  OE2 . GLU   A 1 323 ? 57.332 22.815  21.750  1.00 36.61 ? 397 GLU   A OE2 1 
ATOM   2566 N  N   . HIS   A 1 324 ? 53.050 18.780  20.878  1.00 14.44 ? 398 HIS   A N   1 
ATOM   2567 C  CA  . HIS   A 1 324 ? 53.222 17.726  19.901  1.00 14.95 ? 398 HIS   A CA  1 
ATOM   2568 C  C   . HIS   A 1 324 ? 51.945 17.429  19.104  1.00 13.90 ? 398 HIS   A C   1 
ATOM   2569 O  O   . HIS   A 1 324 ? 52.016 16.981  17.974  1.00 15.02 ? 398 HIS   A O   1 
ATOM   2570 C  CB  . HIS   A 1 324 ? 53.757 16.461  20.585  1.00 15.83 ? 398 HIS   A CB  1 
ATOM   2571 C  CG  . HIS   A 1 324 ? 55.138 16.625  21.131  1.00 17.88 ? 398 HIS   A CG  1 
ATOM   2572 N  ND1 . HIS   A 1 324 ? 55.410 17.422  22.212  1.00 21.24 ? 398 HIS   A ND1 1 
ATOM   2573 C  CD2 . HIS   A 1 324 ? 56.304 16.065  20.785  1.00 25.29 ? 398 HIS   A CD2 1 
ATOM   2574 C  CE1 . HIS   A 1 324 ? 56.708 17.319  22.519  1.00 22.58 ? 398 HIS   A CE1 1 
ATOM   2575 N  NE2 . HIS   A 1 324 ? 57.262 16.555  21.649  1.00 24.29 ? 398 HIS   A NE2 1 
ATOM   2576 N  N   . PHE   A 1 325 ? 50.803 17.619  19.749  1.00 13.46 ? 399 PHE   A N   1 
ATOM   2577 C  CA  . PHE   A 1 325 ? 49.491 17.262  19.211  1.00 13.44 ? 399 PHE   A CA  1 
ATOM   2578 C  C   . PHE   A 1 325 ? 48.552 18.474  19.271  1.00 13.96 ? 399 PHE   A C   1 
ATOM   2579 O  O   . PHE   A 1 325 ? 47.519 18.467  19.945  1.00 13.29 ? 399 PHE   A O   1 
ATOM   2580 C  CB  . PHE   A 1 325 ? 48.893 16.065  19.940  1.00 12.54 ? 399 PHE   A CB  1 
ATOM   2581 C  CG  . PHE   A 1 325 ? 49.813 14.865  19.755  1.00 12.86 ? 399 PHE   A CG  1 
ATOM   2582 C  CD1 . PHE   A 1 325 ? 49.846 14.223  18.547  1.00 13.46 ? 399 PHE   A CD1 1 
ATOM   2583 C  CD2 . PHE   A 1 325 ? 50.655 14.430  20.768  1.00 13.43 ? 399 PHE   A CD2 1 
ATOM   2584 C  CE1 . PHE   A 1 325 ? 50.762 13.193  18.313  1.00 14.20 ? 399 PHE   A CE1 1 
ATOM   2585 C  CE2 . PHE   A 1 325 ? 51.525 13.384  20.526  1.00 14.01 ? 399 PHE   A CE2 1 
ATOM   2586 C  CZ  . PHE   A 1 325 ? 51.599 12.787  19.310  1.00 14.40 ? 399 PHE   A CZ  1 
ATOM   2587 N  N   . PRO   A 1 326 ? 48.888 19.562  18.533  1.00 14.18 ? 400 PRO   A N   1 
ATOM   2588 C  CA  . PRO   A 1 326 ? 48.102 20.790  18.572  1.00 14.75 ? 400 PRO   A CA  1 
ATOM   2589 C  C   . PRO   A 1 326 ? 46.679 20.648  18.088  1.00 13.58 ? 400 PRO   A C   1 
ATOM   2590 O  O   . PRO   A 1 326 ? 45.827 21.460  18.435  1.00 13.70 ? 400 PRO   A O   1 
ATOM   2591 C  CB  . PRO   A 1 326 ? 48.930 21.765  17.712  1.00 15.49 ? 400 PRO   A CB  1 
ATOM   2592 C  CG  . PRO   A 1 326 ? 49.703 20.873  16.779  1.00 15.96 ? 400 PRO   A CG  1 
ATOM   2593 C  CD  . PRO   A 1 326 ? 50.068 19.688  17.681  1.00 14.25 ? 400 PRO   A CD  1 
ATOM   2594 N  N   . CYS   A 1 327 ? 46.365 19.599  17.347  1.00 12.70 ? 401 CYS   A N   1 
ATOM   2595 C  CA  . CYS   A 1 327 ? 44.997 19.403  16.912  1.00 12.53 ? 401 CYS   A CA  1 
ATOM   2596 C  C   . CYS   A 1 327 ? 44.055 19.271  18.095  1.00 12.68 ? 401 CYS   A C   1 
ATOM   2597 O  O   . CYS   A 1 327 ? 42.869 19.607  17.999  1.00 12.56 ? 401 CYS   A O   1 
ATOM   2598 C  CB  . CYS   A 1 327 ? 44.862 18.214  15.978  1.00 13.08 ? 401 CYS   A CB  1 
ATOM   2599 S  SG  . CYS   A 1 327 ? 45.457 18.512  14.283  1.00 14.81 ? 401 CYS   A SG  1 
ATOM   2600 N  N   . ILE   A 1 328 ? 44.516 18.666  19.223  1.00 12.61 ? 402 ILE   A N   1 
ATOM   2601 C  CA  . ILE   A 1 328 ? 43.624 18.495  20.351  1.00 12.98 ? 402 ILE   A CA  1 
ATOM   2602 C  C   . ILE   A 1 328 ? 43.100 19.843  20.846  1.00 12.09 ? 402 ILE   A C   1 
ATOM   2603 O  O   . ILE   A 1 328 ? 41.919 20.019  21.138  1.00 12.26 ? 402 ILE   A O   1 
ATOM   2604 C  CB  . ILE   A 1 328 ? 44.320 17.737  21.510  1.00 13.25 ? 402 ILE   A CB  1 
ATOM   2605 C  CG1 . ILE   A 1 328 ? 44.798 16.376  21.103  1.00 13.69 ? 402 ILE   A CG1 1 
ATOM   2606 C  CG2 . ILE   A 1 328 ? 43.408 17.660  22.730  1.00 14.14 ? 402 ILE   A CG2 1 
ATOM   2607 C  CD1 . ILE   A 1 328 ? 45.719 15.711  22.128  1.00 14.81 ? 402 ILE   A CD1 1 
ATOM   2608 N  N   . LYS   A 1 329 ? 44.015 20.792  20.999  1.00 12.83 ? 403 LYS   A N   1 
ATOM   2609 C  CA  . LYS   A 1 329 ? 43.652 22.102  21.506  1.00 13.86 ? 403 LYS   A CA  1 
ATOM   2610 C  C   . LYS   A 1 329 ? 42.698 22.823  20.541  1.00 13.24 ? 403 LYS   A C   1 
ATOM   2611 O  O   . LYS   A 1 329 ? 41.744 23.462  20.985  1.00 12.90 ? 403 LYS   A O   1 
ATOM   2612 C  CB  . LYS   A 1 329 ? 44.911 22.941  21.686  1.00 16.42 ? 403 LYS   A CB  1 
ATOM   2613 C  CG  . LYS   A 1 329 ? 44.643 24.332  22.202  1.00 21.38 ? 403 LYS   A CG  1 
ATOM   2614 C  CD  . LYS   A 1 329 ? 43.994 24.465  23.563  1.00 26.54 ? 403 LYS   A CD  1 
ATOM   2615 C  CE  . LYS   A 1 329 ? 44.134 25.906  24.037  1.00 29.60 ? 403 LYS   A CE  1 
ATOM   2616 N  NZ  . LYS   A 1 329 ? 43.234 26.082  25.176  1.00 33.76 ? 403 LYS   A NZ  1 
ATOM   2617 N  N   . LEU   A 1 330 ? 42.938 22.682  19.226  1.00 12.20 ? 404 LEU   A N   1 
ATOM   2618 C  CA  . LEU   A 1 330 ? 42.047 23.298  18.252  1.00 11.96 ? 404 LEU   A CA  1 
ATOM   2619 C  C   . LEU   A 1 330 ? 40.645 22.758  18.411  1.00 11.15 ? 404 LEU   A C   1 
ATOM   2620 O  O   . LEU   A 1 330 ? 39.654 23.486  18.293  1.00 12.53 ? 404 LEU   A O   1 
ATOM   2621 C  CB  . LEU   A 1 330 ? 42.548 23.067  16.845  1.00 12.80 ? 404 LEU   A CB  1 
ATOM   2622 C  CG  . LEU   A 1 330 ? 43.900 23.711  16.517  1.00 13.29 ? 404 LEU   A CG  1 
ATOM   2623 C  CD1 . LEU   A 1 330 ? 44.343 23.311  15.138  1.00 14.74 ? 404 LEU   A CD1 1 
ATOM   2624 C  CD2 . LEU   A 1 330 ? 43.817 25.248  16.597  1.00 15.18 ? 404 LEU   A CD2 1 
ATOM   2625 N  N   . ALA   A 1 331 ? 40.493 21.453  18.645  1.00 11.56 ? 405 ALA   A N   1 
ATOM   2626 C  CA  . ALA   A 1 331 ? 39.179 20.839  18.815  1.00 11.11 ? 405 ALA   A CA  1 
ATOM   2627 C  C   . ALA   A 1 331 ? 38.484 21.367  20.059  1.00 10.93 ? 405 ALA   A C   1 
ATOM   2628 O  O   . ALA   A 1 331 ? 37.302 21.676  20.036  1.00 11.50 ? 405 ALA   A O   1 
ATOM   2629 C  CB  . ALA   A 1 331 ? 39.300 19.328  18.865  1.00 11.56 ? 405 ALA   A CB  1 
ATOM   2630 N  N   . TYR   A 1 332 ? 39.179 21.453  21.199  1.00 11.61 ? 406 TYR   A N   1 
ATOM   2631 C  CA  . TYR   A 1 332 ? 38.576 22.041  22.383  1.00 11.56 ? 406 TYR   A CA  1 
ATOM   2632 C  C   . TYR   A 1 332 ? 38.153 23.488  22.108  1.00 12.06 ? 406 TYR   A C   1 
ATOM   2633 O  O   . TYR   A 1 332 ? 37.070 23.893  22.507  1.00 12.74 ? 406 TYR   A O   1 
ATOM   2634 C  CB  . TYR   A 1 332 ? 39.481 22.026  23.620  1.00 11.06 ? 406 TYR   A CB  1 
ATOM   2635 C  CG  . TYR   A 1 332 ? 39.493 20.724  24.409  1.00 11.46 ? 406 TYR   A CG  1 
ATOM   2636 C  CD1 . TYR   A 1 332 ? 40.367 19.695  24.129  1.00 11.78 ? 406 TYR   A CD1 1 
ATOM   2637 C  CD2 . TYR   A 1 332 ? 38.634 20.577  25.464  1.00 11.49 ? 406 TYR   A CD2 1 
ATOM   2638 C  CE1 . TYR   A 1 332 ? 40.386 18.556  24.924  1.00 11.87 ? 406 TYR   A CE1 1 
ATOM   2639 C  CE2 . TYR   A 1 332 ? 38.609 19.422  26.245  1.00 11.52 ? 406 TYR   A CE2 1 
ATOM   2640 C  CZ  . TYR   A 1 332 ? 39.502 18.433  25.968  1.00 11.76 ? 406 TYR   A CZ  1 
ATOM   2641 O  OH  . TYR   A 1 332 ? 39.592 17.264  26.731  1.00 12.45 ? 406 TYR   A OH  1 
ATOM   2642 N  N   . GLN   A 1 333 ? 39.020 24.260  21.455  1.00 11.67 ? 407 GLN   A N   1 
ATOM   2643 C  CA  . GLN   A 1 333 ? 38.671 25.660  21.216  1.00 12.90 ? 407 GLN   A CA  1 
ATOM   2644 C  C   . GLN   A 1 333 ? 37.426 25.777  20.365  1.00 12.96 ? 407 GLN   A C   1 
ATOM   2645 O  O   . GLN   A 1 333 ? 36.539 26.585  20.664  1.00 13.07 ? 407 GLN   A O   1 
ATOM   2646 C  CB  . GLN   A 1 333 ? 39.842 26.370  20.571  1.00 14.08 ? 407 GLN   A CB  1 
ATOM   2647 C  CG  . GLN   A 1 333 ? 40.983 26.612  21.539  1.00 14.72 ? 407 GLN   A CG  1 
ATOM   2648 C  CD  . GLN   A 1 333 ? 42.212 27.184  20.876  1.00 18.59 ? 407 GLN   A CD  1 
ATOM   2649 O  OE1 . GLN   A 1 333 ? 42.549 26.893  19.740  1.00 19.88 ? 407 GLN   A OE1 1 
ATOM   2650 N  NE2 . GLN   A 1 333 ? 42.850 28.100  21.588  1.00 24.84 ? 407 GLN   A NE2 1 
ATOM   2651 N  N   . ALA   A 1 334 ? 37.345 24.982  19.313  1.00 11.37 ? 408 ALA   A N   1 
ATOM   2652 C  CA  . ALA   A 1 334 ? 36.177 24.967  18.448  1.00 11.61 ? 408 ALA   A CA  1 
ATOM   2653 C  C   . ALA   A 1 334 ? 34.911 24.538  19.175  1.00 11.96 ? 408 ALA   A C   1 
ATOM   2654 O  O   . ALA   A 1 334 ? 33.836 25.125  19.045  1.00 12.32 ? 408 ALA   A O   1 
ATOM   2655 C  CB  . ALA   A 1 334 ? 36.420 24.120  17.224  1.00 12.15 ? 408 ALA   A CB  1 
ATOM   2656 N  N   . GLY   A 1 335 ? 35.028 23.470  19.991  1.00 12.13 ? 409 GLY   A N   1 
ATOM   2657 C  CA  . GLY   A 1 335 ? 33.877 22.991  20.732  1.00 11.80 ? 409 GLY   A CA  1 
ATOM   2658 C  C   . GLY   A 1 335 ? 33.379 24.028  21.715  1.00 11.54 ? 409 GLY   A C   1 
ATOM   2659 O  O   . GLY   A 1 335 ? 32.189 24.242  21.823  1.00 12.58 ? 409 GLY   A O   1 
ATOM   2660 N  N   . ILE   A 1 336 ? 34.280 24.677  22.415  1.00 12.24 ? 410 ILE   A N   1 
ATOM   2661 C  CA  . ILE   A 1 336 ? 33.920 25.680  23.408  1.00 13.25 ? 410 ILE   A CA  1 
ATOM   2662 C  C   . ILE   A 1 336 ? 33.258 26.861  22.727  1.00 13.79 ? 410 ILE   A C   1 
ATOM   2663 O  O   . ILE   A 1 336 ? 32.322 27.428  23.292  1.00 15.61 ? 410 ILE   A O   1 
ATOM   2664 C  CB  . ILE   A 1 336 ? 35.139 26.052  24.262  1.00 13.46 ? 410 ILE   A CB  1 
ATOM   2665 C  CG1 . ILE   A 1 336 ? 35.490 24.884  25.186  1.00 14.19 ? 410 ILE   A CG1 1 
ATOM   2666 C  CG2 . ILE   A 1 336 ? 34.903 27.341  25.074  1.00 15.09 ? 410 ILE   A CG2 1 
ATOM   2667 C  CD1 . ILE   A 1 336 ? 36.857 24.964  25.825  1.00 15.32 ? 410 ILE   A CD1 1 
ATOM   2668 N  N   . LYS   A 1 337 ? 33.772 27.286  21.578  1.00 13.13 ? 411 LYS   A N   1 
ATOM   2669 C  CA  . LYS   A 1 337 ? 33.128 28.392  20.863  1.00 14.32 ? 411 LYS   A CA  1 
ATOM   2670 C  C   . LYS   A 1 337 ? 31.754 27.996  20.395  1.00 15.45 ? 411 LYS   A C   1 
ATOM   2671 O  O   . LYS   A 1 337 ? 30.859 28.871  20.285  1.00 17.86 ? 411 LYS   A O   1 
ATOM   2672 C  CB  . LYS   A 1 337 ? 33.998 28.769  19.681  1.00 17.06 ? 411 LYS   A CB  1 
ATOM   2673 C  CG  . LYS   A 1 337 ? 35.167 29.558  20.031  1.00 21.47 ? 411 LYS   A CG  1 
ATOM   2674 C  CD  . LYS   A 1 337 ? 35.732 30.218  18.771  1.00 29.61 ? 411 LYS   A CD  1 
ATOM   2675 C  CE  . LYS   A 1 337 ? 37.024 30.947  18.970  1.00 36.45 ? 411 LYS   A CE  1 
ATOM   2676 N  NZ  . LYS   A 1 337 ? 36.968 31.811  20.143  1.00 44.73 ? 411 LYS   A NZ  1 
ATOM   2677 N  N   . GLY   A 1 338 ? 31.527 26.747  20.051  1.00 14.22 ? 412 GLY   A N   1 
ATOM   2678 C  CA  . GLY   A 1 338 ? 30.233 26.280  19.641  1.00 13.45 ? 412 GLY   A CA  1 
ATOM   2679 C  C   . GLY   A 1 338 ? 29.854 26.860  18.290  1.00 13.68 ? 412 GLY   A C   1 
ATOM   2680 O  O   . GLY   A 1 338 ? 30.659 26.992  17.383  1.00 13.12 ? 412 GLY   A O   1 
ATOM   2681 N  N   . ASN   A 1 339 ? 28.553 27.130  18.120  1.00 14.87 ? 413 ASN   A N   1 
ATOM   2682 C  CA  . ASN   A 1 339 ? 28.023 27.618  16.856  1.00 14.37 ? 413 ASN   A CA  1 
ATOM   2683 C  C   . ASN   A 1 339 ? 28.431 26.631  15.792  1.00 13.87 ? 413 ASN   A C   1 
ATOM   2684 O  O   . ASN   A 1 339 ? 28.314 25.423  15.995  1.00 15.93 ? 413 ASN   A O   1 
ATOM   2685 C  CB  . ASN   A 1 339 ? 28.458 29.071  16.639  1.00 13.66 ? 413 ASN   A CB  1 
ATOM   2686 C  CG  . ASN   A 1 339 ? 27.754 29.786  15.502  1.00 13.62 ? 413 ASN   A CG  1 
ATOM   2687 O  OD1 . ASN   A 1 339 ? 28.292 29.940  14.420  1.00 13.56 ? 413 ASN   A OD1 1 
ATOM   2688 N  ND2 . ASN   A 1 339 ? 26.510 30.193  15.745  1.00 17.02 ? 413 ASN   A ND2 1 
ATOM   2689 N  N   . PHE   A 1 340 ? 28.943 27.068  14.658  1.00 12.75 ? 414 PHE   A N   1 
ATOM   2690 C  CA  . PHE   A 1 340 ? 29.351 26.178  13.599  1.00 12.52 ? 414 PHE   A CA  1 
ATOM   2691 C  C   . PHE   A 1 340 ? 30.865 25.942  13.592  1.00 12.43 ? 414 PHE   A C   1 
ATOM   2692 O  O   . PHE   A 1 340 ? 31.387 25.370  12.648  1.00 12.56 ? 414 PHE   A O   1 
ATOM   2693 C  CB  . PHE   A 1 340 ? 28.918 26.706  12.220  1.00 14.54 ? 414 PHE   A CB  1 
ATOM   2694 C  CG  . PHE   A 1 340 ? 27.407 26.769  12.095  1.00 15.89 ? 414 PHE   A CG  1 
ATOM   2695 C  CD1 . PHE   A 1 340 ? 26.669 25.618  11.782  1.00 18.46 ? 414 PHE   A CD1 1 
ATOM   2696 C  CD2 . PHE   A 1 340 ? 26.704 27.957  12.331  1.00 16.49 ? 414 PHE   A CD2 1 
ATOM   2697 C  CE1 . PHE   A 1 340 ? 25.265 25.644  11.728  1.00 22.14 ? 414 PHE   A CE1 1 
ATOM   2698 C  CE2 . PHE   A 1 340 ? 25.314 27.979  12.256  1.00 18.46 ? 414 PHE   A CE2 1 
ATOM   2699 C  CZ  . PHE   A 1 340 ? 24.603 26.848  11.925  1.00 21.13 ? 414 PHE   A CZ  1 
ATOM   2700 N  N   . TYR   A 1 341 ? 31.576 26.359  14.637  1.00 11.15 ? 415 TYR   A N   1 
ATOM   2701 C  CA  . TYR   A 1 341 ? 33.007 26.099  14.689  1.00 11.17 ? 415 TYR   A CA  1 
ATOM   2702 C  C   . TYR   A 1 341 ? 33.347 24.601  14.599  1.00 11.59 ? 415 TYR   A C   1 
ATOM   2703 O  O   . TYR   A 1 341 ? 34.295 24.262  13.900  1.00 11.68 ? 415 TYR   A O   1 
ATOM   2704 C  CB  . TYR   A 1 341 ? 33.681 26.783  15.873  1.00 11.67 ? 415 TYR   A CB  1 
ATOM   2705 C  CG  . TYR   A 1 341 ? 33.865 28.287  15.717  1.00 11.94 ? 415 TYR   A CG  1 
ATOM   2706 C  CD1 . TYR   A 1 341 ? 35.041 28.770  15.177  1.00 12.38 ? 415 TYR   A CD1 1 
ATOM   2707 C  CD2 . TYR   A 1 341 ? 32.914 29.194  16.133  1.00 12.50 ? 415 TYR   A CD2 1 
ATOM   2708 C  CE1 . TYR   A 1 341 ? 35.299 30.119  15.054  1.00 14.03 ? 415 TYR   A CE1 1 
ATOM   2709 C  CE2 . TYR   A 1 341 ? 33.138 30.563  15.998  1.00 13.56 ? 415 TYR   A CE2 1 
ATOM   2710 C  CZ  . TYR   A 1 341 ? 34.362 30.990  15.528  1.00 14.26 ? 415 TYR   A CZ  1 
ATOM   2711 O  OH  . TYR   A 1 341 ? 34.644 32.370  15.480  1.00 16.52 ? 415 TYR   A OH  1 
ATOM   2712 N  N   . PRO   A 1 342 ? 32.592 23.691  15.242  1.00 11.50 ? 416 PRO   A N   1 
ATOM   2713 C  CA  . PRO   A 1 342 ? 32.878 22.273  15.043  1.00 11.73 ? 416 PRO   A CA  1 
ATOM   2714 C  C   . PRO   A 1 342 ? 32.722 21.819  13.603  1.00 12.30 ? 416 PRO   A C   1 
ATOM   2715 O  O   . PRO   A 1 342 ? 33.501 20.995  13.125  1.00 12.24 ? 416 PRO   A O   1 
ATOM   2716 C  CB  . PRO   A 1 342 ? 31.941 21.599  16.034  1.00 11.92 ? 416 PRO   A CB  1 
ATOM   2717 C  CG  . PRO   A 1 342 ? 31.780 22.570  17.158  1.00 11.88 ? 416 PRO   A CG  1 
ATOM   2718 C  CD  . PRO   A 1 342 ? 31.657 23.903  16.377  1.00 12.48 ? 416 PRO   A CD  1 
ATOM   2719 N  N   . THR   A 1 343 ? 31.711 22.360  12.886  1.00 11.79 ? 417 THR   A N   1 
ATOM   2720 C  CA  . THR   A 1 343 ? 31.575 22.068  11.457  1.00 12.16 ? 417 THR   A CA  1 
ATOM   2721 C  C   . THR   A 1 343 ? 32.836 22.457  10.692  1.00 11.73 ? 417 THR   A C   1 
ATOM   2722 O  O   . THR   A 1 343 ? 33.338 21.719  9.841   1.00 13.01 ? 417 THR   A O   1 
ATOM   2723 C  CB  . THR   A 1 343 ? 30.347 22.815  10.900  1.00 12.93 ? 417 THR   A CB  1 
ATOM   2724 O  OG1 . THR   A 1 343 ? 29.197 22.522  11.705  1.00 14.33 ? 417 THR   A OG1 1 
ATOM   2725 C  CG2 . THR   A 1 343 ? 30.067 22.504  9.457   1.00 15.03 ? 417 THR   A CG2 1 
ATOM   2726 N  N   . VAL   A 1 344 ? 33.339 23.671  10.987  1.00 11.72 ? 418 VAL   A N   1 
ATOM   2727 C  CA  . VAL   A 1 344 ? 34.519 24.187  10.350  1.00 11.47 ? 418 VAL   A CA  1 
ATOM   2728 C  C   . VAL   A 1 344 ? 35.762 23.353  10.651  1.00 11.65 ? 418 VAL   A C   1 
ATOM   2729 O  O   . VAL   A 1 344 ? 36.595 23.083  9.789   1.00 12.54 ? 418 VAL   A O   1 
ATOM   2730 C  CB  . VAL   A 1 344 ? 34.691 25.676  10.707  1.00 12.08 ? 418 VAL   A CB  1 
ATOM   2731 C  CG1 . VAL   A 1 344 ? 36.004 26.248  10.183  1.00 12.89 ? 418 VAL   A CG1 1 
ATOM   2732 C  CG2 . VAL   A 1 344 ? 33.504 26.491  10.203  1.00 12.75 ? 418 VAL   A CG2 1 
ATOM   2733 N  N   . LEU   A 1 345 ? 35.890 22.989  11.944  1.00 11.47 ? 419 LEU   A N   1 
ATOM   2734 C  CA  . LEU   A 1 345 ? 36.969 22.111  12.390  1.00 11.25 ? 419 LEU   A CA  1 
ATOM   2735 C  C   . LEU   A 1 345 ? 36.959 20.802  11.593  1.00 10.90 ? 419 LEU   A C   1 
ATOM   2736 O  O   . LEU   A 1 345 ? 37.989 20.386  11.056  1.00 12.00 ? 419 LEU   A O   1 
ATOM   2737 C  CB  . LEU   A 1 345 ? 36.793 21.823  13.879  1.00 11.75 ? 419 LEU   A CB  1 
ATOM   2738 C  CG  . LEU   A 1 345 ? 37.845 20.860  14.482  1.00 11.89 ? 419 LEU   A CG  1 
ATOM   2739 C  CD1 . LEU   A 1 345 ? 39.062 21.583  14.918  1.00 12.64 ? 419 LEU   A CD1 1 
ATOM   2740 C  CD2 . LEU   A 1 345 ? 37.226 20.104  15.669  1.00 12.86 ? 419 LEU   A CD2 1 
ATOM   2741 N  N   . ASN   A 1 346 ? 35.801 20.174  11.508  1.00 11.33 ? 420 ASN   A N   1 
ATOM   2742 C  CA  . ASN   A 1 346 ? 35.725 18.882  10.834  1.00 11.86 ? 420 ASN   A CA  1 
ATOM   2743 C  C   . ASN   A 1 346 ? 36.111 19.036  9.370   1.00 12.33 ? 420 ASN   A C   1 
ATOM   2744 O  O   . ASN   A 1 346 ? 36.854 18.213  8.833   1.00 12.81 ? 420 ASN   A O   1 
ATOM   2745 C  CB  . ASN   A 1 346 ? 34.323 18.322  10.973  1.00 12.58 ? 420 ASN   A CB  1 
ATOM   2746 C  CG  . ASN   A 1 346 ? 34.245 16.981  10.315  1.00 14.18 ? 420 ASN   A CG  1 
ATOM   2747 O  OD1 . ASN   A 1 346 ? 33.779 16.845  9.158   1.00 16.94 ? 420 ASN   A OD1 1 
ATOM   2748 N  ND2 . ASN   A 1 346 ? 34.832 16.005  10.951  1.00 13.09 ? 420 ASN   A ND2 1 
ATOM   2749 N  N   . ALA   A 1 347 ? 35.546 20.046  8.712   1.00 12.15 ? 421 ALA   A N   1 
ATOM   2750 C  CA  . ALA   A 1 347 ? 35.735 20.219  7.274   1.00 12.76 ? 421 ALA   A CA  1 
ATOM   2751 C  C   . ALA   A 1 347 ? 37.169 20.533  6.917   1.00 12.78 ? 421 ALA   A C   1 
ATOM   2752 O  O   . ALA   A 1 347 ? 37.772 19.963  5.993   1.00 13.05 ? 421 ALA   A O   1 
ATOM   2753 C  CB  . ALA   A 1 347 ? 34.825 21.359  6.822   1.00 14.00 ? 421 ALA   A CB  1 
ATOM   2754 N  N   . SER   A 1 348 ? 37.775 21.485  7.655   1.00 12.72 ? 422 SER   A N   1 
ATOM   2755 C  CA  . SER   A 1 348 ? 39.151 21.843  7.398   1.00 13.00 ? 422 SER   A CA  1 
ATOM   2756 C  C   . SER   A 1 348 ? 40.045 20.632  7.621   1.00 13.48 ? 422 SER   A C   1 
ATOM   2757 O  O   . SER   A 1 348 ? 41.028 20.425  6.902   1.00 13.72 ? 422 SER   A O   1 
ATOM   2758 C  CB  . SER   A 1 348 ? 39.599 23.084  8.131   1.00 13.21 ? 422 SER   A CB  1 
ATOM   2759 O  OG  . SER   A 1 348 ? 39.457 22.950  9.548   1.00 13.71 ? 422 SER   A OG  1 
ATOM   2760 N  N   . ASN   A 1 349 ? 39.752 19.846  8.693   1.00 12.60 ? 423 ASN   A N   1 
ATOM   2761 C  CA  . ASN   A 1 349 ? 40.555 18.646  8.945   1.00 12.59 ? 423 ASN   A CA  1 
ATOM   2762 C  C   . ASN   A 1 349 ? 40.370 17.653  7.802   1.00 12.70 ? 423 ASN   A C   1 
ATOM   2763 O  O   . ASN   A 1 349 ? 41.318 16.955  7.453   1.00 13.30 ? 423 ASN   A O   1 
ATOM   2764 C  CB  . ASN   A 1 349 ? 40.217 18.046  10.309  1.00 12.71 ? 423 ASN   A CB  1 
ATOM   2765 C  CG  . ASN   A 1 349 ? 41.048 16.816  10.554  1.00 12.15 ? 423 ASN   A CG  1 
ATOM   2766 O  OD1 . ASN   A 1 349 ? 42.274 16.932  10.647  1.00 13.42 ? 423 ASN   A OD1 1 
ATOM   2767 N  ND2 . ASN   A 1 349 ? 40.354 15.688  10.658  1.00 13.16 ? 423 ASN   A ND2 1 
ATOM   2768 N  N   . GLU   A 1 350 ? 39.169 17.478  7.268   1.00 12.79 ? 424 GLU   A N   1 
ATOM   2769 C  CA  . GLU   A 1 350 ? 39.036 16.552  6.145   1.00 13.50 ? 424 GLU   A CA  1 
ATOM   2770 C  C   . GLU   A 1 350 ? 40.016 16.877  5.025   1.00 14.39 ? 424 GLU   A C   1 
ATOM   2771 O  O   . GLU   A 1 350 ? 40.667 15.994  4.482   1.00 14.56 ? 424 GLU   A O   1 
ATOM   2772 C  CB  . GLU   A 1 350 ? 37.614 16.461  5.616   1.00 14.55 ? 424 GLU   A CB  1 
ATOM   2773 C  CG  . GLU   A 1 350 ? 36.643 15.794  6.582   1.00 16.27 ? 424 GLU   A CG  1 
ATOM   2774 C  CD  . GLU   A 1 350 ? 35.258 15.514  6.067   1.00 18.67 ? 424 GLU   A CD  1 
ATOM   2775 O  OE1 . GLU   A 1 350 ? 34.969 15.817  4.870   1.00 20.75 ? 424 GLU   A OE1 1 
ATOM   2776 O  OE2 . GLU   A 1 350 ? 34.436 14.988  6.868   1.00 19.49 ? 424 GLU   A OE2 1 
ATOM   2777 N  N   . ILE   A 1 351 ? 40.140 18.165  4.684   1.00 13.82 ? 425 ILE   A N   1 
ATOM   2778 C  CA  . ILE   A 1 351 ? 41.102 18.567  3.657   1.00 14.13 ? 425 ILE   A CA  1 
ATOM   2779 C  C   . ILE   A 1 351 ? 42.535 18.372  4.118   1.00 14.35 ? 425 ILE   A C   1 
ATOM   2780 O  O   . ILE   A 1 351 ? 43.338 17.795  3.360   1.00 15.51 ? 425 ILE   A O   1 
ATOM   2781 C  CB  . ILE   A 1 351 ? 40.869 20.038  3.253   1.00 15.28 ? 425 ILE   A CB  1 
ATOM   2782 C  CG1 . ILE   A 1 351 ? 39.530 20.233  2.555   1.00 15.85 ? 425 ILE   A CG1 1 
ATOM   2783 C  CG2 . ILE   A 1 351 ? 42.024 20.565  2.400   1.00 15.49 ? 425 ILE   A CG2 1 
ATOM   2784 C  CD1 . ILE   A 1 351 ? 39.399 19.495  1.211   1.00 18.34 ? 425 ILE   A CD1 1 
ATOM   2785 N  N   . ALA   A 1 352 ? 42.896 18.851  5.310   1.00 13.70 ? 426 ALA   A N   1 
ATOM   2786 C  CA  . ALA   A 1 352 ? 44.271 18.757  5.745   1.00 14.34 ? 426 ALA   A CA  1 
ATOM   2787 C  C   . ALA   A 1 352 ? 44.743 17.296  5.895   1.00 14.14 ? 426 ALA   A C   1 
ATOM   2788 O  O   . ALA   A 1 352 ? 45.866 16.944  5.555   1.00 15.19 ? 426 ALA   A O   1 
ATOM   2789 C  CB  . ALA   A 1 352 ? 44.462 19.531  7.016   1.00 15.81 ? 426 ALA   A CB  1 
ATOM   2790 N  N   . ASN   A 1 353 ? 43.879 16.451  6.466   1.00 13.77 ? 427 ASN   A N   1 
ATOM   2791 C  CA  . ASN   A 1 353 ? 44.152 15.014  6.588   1.00 14.40 ? 427 ASN   A CA  1 
ATOM   2792 C  C   . ASN   A 1 353 ? 44.477 14.436  5.200   1.00 14.41 ? 427 ASN   A C   1 
ATOM   2793 O  O   . ASN   A 1 353 ? 45.517 13.771  5.029   1.00 15.00 ? 427 ASN   A O   1 
ATOM   2794 C  CB  . ASN   A 1 353 ? 42.938 14.383  7.238   1.00 14.06 ? 427 ASN   A CB  1 
ATOM   2795 C  CG  . ASN   A 1 353 ? 42.937 12.876  7.291   1.00 14.50 ? 427 ASN   A CG  1 
ATOM   2796 O  OD1 . ASN   A 1 353 ? 43.258 12.170  6.325   1.00 16.16 ? 427 ASN   A OD1 1 
ATOM   2797 N  ND2 . ASN   A 1 353 ? 42.507 12.333  8.415   1.00 14.48 ? 427 ASN   A ND2 1 
ATOM   2798 N  N   . ASN   A 1 354 ? 43.614 14.707  4.217   1.00 15.27 ? 428 ASN   A N   1 
ATOM   2799 C  CA  . ASN   A 1 354 ? 43.806 14.162  2.872   1.00 17.27 ? 428 ASN   A CA  1 
ATOM   2800 C  C   . ASN   A 1 354 ? 45.082 14.698  2.215   1.00 16.53 ? 428 ASN   A C   1 
ATOM   2801 O  O   . ASN   A 1 354 ? 45.786 13.934  1.524   1.00 17.28 ? 428 ASN   A O   1 
ATOM   2802 C  CB  . ASN   A 1 354 ? 42.562 14.329  2.020   1.00 17.64 ? 428 ASN   A CB  1 
ATOM   2803 C  CG  . ASN   A 1 354 ? 42.558 13.344  0.881   1.00 22.47 ? 428 ASN   A CG  1 
ATOM   2804 O  OD1 . ASN   A 1 354 ? 42.860 13.733  -0.244  1.00 23.33 ? 428 ASN   A OD1 1 
ATOM   2805 N  ND2 . ASN   A 1 354 ? 42.295 12.088  1.167   1.00 21.54 ? 428 ASN   A ND2 1 
ATOM   2806 N  N   . LEU   A 1 355 ? 45.427 15.958  2.453   1.00 16.00 ? 429 LEU   A N   1 
ATOM   2807 C  CA  . LEU   A 1 355 ? 46.650 16.519  1.906   1.00 16.29 ? 429 LEU   A CA  1 
ATOM   2808 C  C   . LEU   A 1 355 ? 47.843 15.781  2.488   1.00 16.56 ? 429 LEU   A C   1 
ATOM   2809 O  O   . LEU   A 1 355 ? 48.777 15.421  1.782   1.00 17.76 ? 429 LEU   A O   1 
ATOM   2810 C  CB  . LEU   A 1 355 ? 46.767 18.016  2.164   1.00 16.92 ? 429 LEU   A CB  1 
ATOM   2811 C  CG  . LEU   A 1 355 ? 45.826 18.898  1.358   1.00 17.09 ? 429 LEU   A CG  1 
ATOM   2812 C  CD1 . LEU   A 1 355 ? 45.835 20.296  1.931   1.00 17.19 ? 429 LEU   A CD1 1 
ATOM   2813 C  CD2 . LEU   A 1 355 ? 46.112 18.905  -0.189  1.00 18.69 ? 429 LEU   A CD2 1 
ATOM   2814 N  N   . PHE   A 1 356 ? 47.872 15.545  3.806   1.00 15.68 ? 430 PHE   A N   1 
ATOM   2815 C  CA  . PHE   A 1 356 ? 48.985 14.856  4.426   1.00 15.31 ? 430 PHE   A CA  1 
ATOM   2816 C  C   . PHE   A 1 356 ? 49.018 13.399  3.956   1.00 16.27 ? 430 PHE   A C   1 
ATOM   2817 O  O   . PHE   A 1 356 ? 50.095 12.846  3.655   1.00 17.18 ? 430 PHE   A O   1 
ATOM   2818 C  CB  . PHE   A 1 356 ? 48.806 14.898  5.947   1.00 15.39 ? 430 PHE   A CB  1 
ATOM   2819 C  CG  . PHE   A 1 356 ? 49.909 14.148  6.665   1.00 16.28 ? 430 PHE   A CG  1 
ATOM   2820 C  CD1 . PHE   A 1 356 ? 51.177 14.696  6.751   1.00 16.15 ? 430 PHE   A CD1 1 
ATOM   2821 C  CD2 . PHE   A 1 356 ? 49.654 12.960  7.345   1.00 15.82 ? 430 PHE   A CD2 1 
ATOM   2822 C  CE1 . PHE   A 1 356 ? 52.192 14.036  7.416   1.00 17.55 ? 430 PHE   A CE1 1 
ATOM   2823 C  CE2 . PHE   A 1 356 ? 50.652 12.332  8.055   1.00 16.29 ? 430 PHE   A CE2 1 
ATOM   2824 C  CZ  . PHE   A 1 356 ? 51.915 12.870  8.089   1.00 16.61 ? 430 PHE   A CZ  1 
ATOM   2825 N  N   . LEU   A 1 357 ? 47.861 12.742  3.864   1.00 16.15 ? 431 LEU   A N   1 
ATOM   2826 C  CA  . LEU   A 1 357 ? 47.780 11.368  3.385   1.00 16.58 ? 431 LEU   A CA  1 
ATOM   2827 C  C   . LEU   A 1 357 ? 48.482 11.250  2.027   1.00 17.88 ? 431 LEU   A C   1 
ATOM   2828 O  O   . LEU   A 1 357 ? 49.242 10.274  1.815   1.00 19.66 ? 431 LEU   A O   1 
ATOM   2829 C  CB  . LEU   A 1 357 ? 46.314 10.975  3.272   1.00 16.60 ? 431 LEU   A CB  1 
ATOM   2830 C  CG  . LEU   A 1 357 ? 46.038 9.572   2.725   1.00 19.43 ? 431 LEU   A CG  1 
ATOM   2831 C  CD1 . LEU   A 1 357 ? 46.615 8.474   3.600   1.00 21.38 ? 431 LEU   A CD1 1 
ATOM   2832 C  CD2 . LEU   A 1 357 ? 44.549 9.339   2.545   1.00 21.69 ? 431 LEU   A CD2 1 
ATOM   2833 N  N   . ASN   A 1 358 ? 48.249 12.216  1.160   1.00 18.21 ? 432 ASN   A N   1 
ATOM   2834 C  CA  . ASN   A 1 358 ? 48.768 12.225  -0.219  1.00 19.26 ? 432 ASN   A CA  1 
ATOM   2835 C  C   . ASN   A 1 358 ? 50.102 12.971  -0.308  1.00 20.74 ? 432 ASN   A C   1 
ATOM   2836 O  O   . ASN   A 1 358 ? 50.527 13.292  -1.444  1.00 21.48 ? 432 ASN   A O   1 
ATOM   2837 C  CB  . ASN   A 1 358 ? 47.712 12.801  -1.140  1.00 20.71 ? 432 ASN   A CB  1 
ATOM   2838 C  CG  . ASN   A 1 358 ? 46.555 11.862  -1.308  1.00 24.17 ? 432 ASN   A CG  1 
ATOM   2839 O  OD1 . ASN   A 1 358 ? 45.455 12.051  -0.780  1.00 26.93 ? 432 ASN   A OD1 1 
ATOM   2840 N  ND2 . ASN   A 1 358 ? 46.817 10.748  -1.958  1.00 24.33 ? 432 ASN   A ND2 1 
ATOM   2841 N  N   . ASN   A 1 359 ? 50.839 13.170  0.800   1.00 19.32 ? 433 ASN   A N   1 
ATOM   2842 C  CA  . ASN   A 1 359 ? 52.217 13.655  0.809   1.00 20.46 ? 433 ASN   A CA  1 
ATOM   2843 C  C   . ASN   A 1 359 ? 52.331 15.062  0.224   1.00 21.60 ? 433 ASN   A C   1 
ATOM   2844 O  O   . ASN   A 1 359 ? 53.360 15.416  -0.351  1.00 24.07 ? 433 ASN   A O   1 
ATOM   2845 C  CB  . ASN   A 1 359 ? 53.172 12.710  0.056   1.00 22.35 ? 433 ASN   A CB  1 
ATOM   2846 C  CG  . ASN   A 1 359 ? 53.021 11.280  0.509   1.00 27.44 ? 433 ASN   A CG  1 
ATOM   2847 O  OD1 . ASN   A 1 359 ? 52.696 10.388  -0.289  1.00 36.11 ? 433 ASN   A OD1 1 
ATOM   2848 N  ND2 . ASN   A 1 359 ? 53.205 11.054  1.791   1.00 23.54 ? 433 ASN   A ND2 1 
ATOM   2849 N  N   . LYS   A 1 360 ? 51.319 15.902  0.436   1.00 19.26 ? 434 LYS   A N   1 
ATOM   2850 C  CA  . LYS   A 1 360 ? 51.339 17.250  -0.102  1.00 20.05 ? 434 LYS   A CA  1 
ATOM   2851 C  C   . LYS   A 1 360 ? 51.769 18.296  0.904   1.00 19.84 ? 434 LYS   A C   1 
ATOM   2852 O  O   . LYS   A 1 360 ? 52.062 19.436  0.526   1.00 21.68 ? 434 LYS   A O   1 
ATOM   2853 C  CB  . LYS   A 1 360 ? 49.968 17.635  -0.655  1.00 20.74 ? 434 LYS   A CB  1 
ATOM   2854 C  CG  . LYS   A 1 360 ? 49.343 16.722  -1.704  1.00 24.22 ? 434 LYS   A CG  1 
ATOM   2855 C  CD  . LYS   A 1 360 ? 50.203 16.548  -2.945  1.00 28.13 ? 434 LYS   A CD  1 
ATOM   2856 C  CE  . LYS   A 1 360 ? 49.496 15.705  -3.935  1.00 32.69 ? 434 LYS   A CE  1 
ATOM   2857 N  NZ  . LYS   A 1 360 ? 50.451 15.389  -5.007  1.00 38.04 ? 434 LYS   A NZ  1 
ATOM   2858 N  N   . ILE   A 1 361 ? 51.545 17.996  2.202   1.00 18.01 ? 435 ILE   A N   1 
ATOM   2859 C  CA  . ILE   A 1 361 ? 51.893 18.900  3.286   1.00 17.18 ? 435 ILE   A CA  1 
ATOM   2860 C  C   . ILE   A 1 361 ? 52.562 18.091  4.399   1.00 17.43 ? 435 ILE   A C   1 
ATOM   2861 O  O   . ILE   A 1 361 ? 52.540 16.863  4.372   1.00 18.52 ? 435 ILE   A O   1 
ATOM   2862 C  CB  . ILE   A 1 361 ? 50.656 19.636  3.850   1.00 17.77 ? 435 ILE   A CB  1 
ATOM   2863 C  CG1 . ILE   A 1 361 ? 49.694 18.682  4.598   1.00 18.01 ? 435 ILE   A CG1 1 
ATOM   2864 C  CG2 . ILE   A 1 361 ? 49.968 20.473  2.762   1.00 18.61 ? 435 ILE   A CG2 1 
ATOM   2865 C  CD1 . ILE   A 1 361 ? 48.498 19.379  5.241   1.00 16.77 ? 435 ILE   A CD1 1 
ATOM   2866 N  N   . LYS   A 1 362 ? 53.203 18.816  5.309   1.00 17.68 ? 436 LYS   A N   1 
ATOM   2867 C  CA  . LYS   A 1 362 ? 53.840 18.217  6.461   1.00 18.33 ? 436 LYS   A CA  1 
ATOM   2868 C  C   . LYS   A 1 362 ? 52.924 18.194  7.684   1.00 17.62 ? 436 LYS   A C   1 
ATOM   2869 O  O   . LYS   A 1 362 ? 51.882 18.839  7.739   1.00 16.80 ? 436 LYS   A O   1 
ATOM   2870 C  CB  . LYS   A 1 362 ? 55.063 19.061  6.807   1.00 21.52 ? 436 LYS   A CB  1 
ATOM   2871 C  CG  . LYS   A 1 362 ? 56.071 19.081  5.657   1.00 25.59 ? 436 LYS   A CG  1 
ATOM   2872 C  CD  . LYS   A 1 362 ? 57.352 19.799  6.073   1.00 32.81 ? 436 LYS   A CD  1 
ATOM   2873 C  CE  . LYS   A 1 362 ? 58.406 19.728  5.000   1.00 40.84 ? 436 LYS   A CE  1 
ATOM   2874 N  NZ  . LYS   A 1 362 ? 59.238 20.930  5.134   1.00 46.97 ? 436 LYS   A NZ  1 
ATOM   2875 N  N   . TYR   A 1 363 ? 53.352 17.440  8.689   1.00 16.94 ? 437 TYR   A N   1 
ATOM   2876 C  CA  . TYR   A 1 363 ? 52.571 17.189  9.910   1.00 16.54 ? 437 TYR   A CA  1 
ATOM   2877 C  C   . TYR   A 1 363 ? 52.040 18.493  10.524  1.00 16.52 ? 437 TYR   A C   1 
ATOM   2878 O  O   . TYR   A 1 363 ? 50.834 18.600  10.830  1.00 16.49 ? 437 TYR   A O   1 
ATOM   2879 C  CB  . TYR   A 1 363 ? 53.456 16.399  10.868  1.00 16.78 ? 437 TYR   A CB  1 
ATOM   2880 C  CG  . TYR   A 1 363 ? 52.794 16.135  12.218  1.00 15.34 ? 437 TYR   A CG  1 
ATOM   2881 C  CD1 . TYR   A 1 363 ? 51.920 15.074  12.393  1.00 15.94 ? 437 TYR   A CD1 1 
ATOM   2882 C  CD2 . TYR   A 1 363 ? 53.015 16.979  13.294  1.00 15.21 ? 437 TYR   A CD2 1 
ATOM   2883 C  CE1 . TYR   A 1 363 ? 51.314 14.827  13.616  1.00 15.57 ? 437 TYR   A CE1 1 
ATOM   2884 C  CE2 . TYR   A 1 363 ? 52.395 16.753  14.518  1.00 14.93 ? 437 TYR   A CE2 1 
ATOM   2885 C  CZ  . TYR   A 1 363 ? 51.533 15.683  14.678  1.00 15.19 ? 437 TYR   A CZ  1 
ATOM   2886 O  OH  . TYR   A 1 363 ? 50.891 15.437  15.869  1.00 16.61 ? 437 TYR   A OH  1 
ATOM   2887 N  N   . PHE   A 1 364 ? 52.909 19.460  10.804  1.00 16.84 ? 438 PHE   A N   1 
ATOM   2888 C  CA  . PHE   A 1 364 ? 52.481 20.671  11.487  1.00 16.73 ? 438 PHE   A CA  1 
ATOM   2889 C  C   . PHE   A 1 364 ? 51.692 21.606  10.567  1.00 16.46 ? 438 PHE   A C   1 
ATOM   2890 O  O   . PHE   A 1 364 ? 50.999 22.510  11.051  1.00 17.89 ? 438 PHE   A O   1 
ATOM   2891 C  CB  . PHE   A 1 364 ? 53.615 21.439  12.157  1.00 17.46 ? 438 PHE   A CB  1 
ATOM   2892 C  CG  . PHE   A 1 364 ? 54.093 20.718  13.405  1.00 17.84 ? 438 PHE   A CG  1 
ATOM   2893 C  CD1 . PHE   A 1 364 ? 53.304 20.650  14.548  1.00 18.03 ? 438 PHE   A CD1 1 
ATOM   2894 C  CD2 . PHE   A 1 364 ? 55.360 20.143  13.438  1.00 18.45 ? 438 PHE   A CD2 1 
ATOM   2895 C  CE1 . PHE   A 1 364 ? 53.730 19.973  15.674  1.00 19.05 ? 438 PHE   A CE1 1 
ATOM   2896 C  CE2 . PHE   A 1 364 ? 55.789 19.444  14.556  1.00 19.44 ? 438 PHE   A CE2 1 
ATOM   2897 C  CZ  . PHE   A 1 364 ? 54.994 19.387  15.673  1.00 19.75 ? 438 PHE   A CZ  1 
ATOM   2898 N  N   . ASP   A 1 365 ? 51.694 21.346  9.249   1.00 15.99 ? 439 ASP   A N   1 
ATOM   2899 C  CA  . ASP   A 1 365 ? 50.842 22.092  8.351   1.00 15.88 ? 439 ASP   A CA  1 
ATOM   2900 C  C   . ASP   A 1 365 ? 49.381 21.709  8.536   1.00 16.12 ? 439 ASP   A C   1 
ATOM   2901 O  O   . ASP   A 1 365 ? 48.495 22.492  8.208   1.00 16.25 ? 439 ASP   A O   1 
ATOM   2902 C  CB  . ASP   A 1 365 ? 51.233 21.893  6.894   1.00 16.69 ? 439 ASP   A CB  1 
ATOM   2903 C  CG  . ASP   A 1 365 ? 52.639 22.320  6.505   1.00 19.81 ? 439 ASP   A CG  1 
ATOM   2904 O  OD1 . ASP   A 1 365 ? 53.111 23.290  7.099   1.00 24.01 ? 439 ASP   A OD1 1 
ATOM   2905 O  OD2 . ASP   A 1 365 ? 53.166 21.674  5.579   1.00 20.41 ? 439 ASP   A OD2 1 
ATOM   2906 N  N   . ILE   A 1 366 ? 49.117 20.497  9.066   1.00 14.82 ? 440 ILE   A N   1 
ATOM   2907 C  CA  . ILE   A 1 366 ? 47.751 20.064  9.270   1.00 14.26 ? 440 ILE   A CA  1 
ATOM   2908 C  C   . ILE   A 1 366 ? 47.059 21.015  10.240  1.00 14.54 ? 440 ILE   A C   1 
ATOM   2909 O  O   . ILE   A 1 366 ? 46.018 21.609  9.952   1.00 14.94 ? 440 ILE   A O   1 
ATOM   2910 C  CB  . ILE   A 1 366 ? 47.722 18.612  9.748   1.00 14.72 ? 440 ILE   A CB  1 
ATOM   2911 C  CG1 . ILE   A 1 366 ? 48.341 17.666  8.726   1.00 14.96 ? 440 ILE   A CG1 1 
ATOM   2912 C  CG2 . ILE   A 1 366 ? 46.305 18.209  10.154  1.00 15.32 ? 440 ILE   A CG2 1 
ATOM   2913 C  CD1 . ILE   A 1 366 ? 48.536 16.276  9.333   1.00 14.86 ? 440 ILE   A CD1 1 
ATOM   2914 N  N   . SER   A 1 367 ? 47.644 21.148  11.427  1.00 13.78 ? 441 SER   A N   1 
ATOM   2915 C  CA  . SER   A 1 367 ? 47.142 22.038  12.452  1.00 14.87 ? 441 SER   A CA  1 
ATOM   2916 C  C   . SER   A 1 367 ? 47.191 23.496  12.018  1.00 14.34 ? 441 SER   A C   1 
ATOM   2917 O  O   . SER   A 1 367 ? 46.307 24.258  12.339  1.00 14.73 ? 441 SER   A O   1 
ATOM   2918 C  CB  . SER   A 1 367 ? 47.820 21.796  13.789  1.00 15.82 ? 441 SER   A CB  1 
ATOM   2919 O  OG  . SER   A 1 367 ? 49.219 21.581  13.579  1.00 16.92 ? 441 SER   A OG  1 
ATOM   2920 N  N   . SER   A 1 368 ? 48.209 23.895  11.256  1.00 14.56 ? 442 SER   A N   1 
ATOM   2921 C  CA  . SER   A 1 368 ? 48.285 25.276  10.784  1.00 16.08 ? 442 SER   A CA  1 
ATOM   2922 C  C   . SER   A 1 368 ? 47.098 25.613  9.886   1.00 15.60 ? 442 SER   A C   1 
ATOM   2923 O  O   . SER   A 1 368 ? 46.472 26.672  10.040  1.00 15.85 ? 442 SER   A O   1 
ATOM   2924 C  CB  . SER   A 1 368 ? 49.590 25.531  10.065  1.00 17.89 ? 442 SER   A CB  1 
ATOM   2925 O  OG  . SER   A 1 368 ? 49.561 26.862  9.522   1.00 19.77 ? 442 SER   A OG  1 
ATOM   2926 N  N   . ILE   A 1 369 ? 46.783 24.741  8.940   1.00 14.93 ? 443 ILE   A N   1 
ATOM   2927 C  CA  . ILE   A 1 369 ? 45.655 24.962  8.047   1.00 15.00 ? 443 ILE   A CA  1 
ATOM   2928 C  C   . ILE   A 1 369 ? 44.354 25.032  8.829   1.00 13.62 ? 443 ILE   A C   1 
ATOM   2929 O  O   . ILE   A 1 369 ? 43.538 25.969  8.671   1.00 14.55 ? 443 ILE   A O   1 
ATOM   2930 C  CB  . ILE   A 1 369 ? 45.564 23.907  6.954   1.00 15.38 ? 443 ILE   A CB  1 
ATOM   2931 C  CG1 . ILE   A 1 369 ? 46.705 24.095  5.964   1.00 16.87 ? 443 ILE   A CG1 1 
ATOM   2932 C  CG2 . ILE   A 1 369 ? 44.205 23.906  6.253   1.00 16.37 ? 443 ILE   A CG2 1 
ATOM   2933 C  CD1 . ILE   A 1 369 ? 46.891 22.937  4.992   1.00 19.87 ? 443 ILE   A CD1 1 
ATOM   2934 N  N   . ILE   A 1 370 ? 44.131 24.066  9.721   1.00 13.77 ? 444 ILE   A N   1 
ATOM   2935 C  CA  . ILE   A 1 370 ? 42.899 24.027  10.499  1.00 13.34 ? 444 ILE   A CA  1 
ATOM   2936 C  C   . ILE   A 1 370 ? 42.759 25.279  11.349  1.00 13.04 ? 444 ILE   A C   1 
ATOM   2937 O  O   . ILE   A 1 370 ? 41.697 25.920  11.352  1.00 12.96 ? 444 ILE   A O   1 
ATOM   2938 C  CB  . ILE   A 1 370 ? 42.848 22.760  11.381  1.00 12.85 ? 444 ILE   A CB  1 
ATOM   2939 C  CG1 . ILE   A 1 370 ? 42.785 21.506  10.525  1.00 13.63 ? 444 ILE   A CG1 1 
ATOM   2940 C  CG2 . ILE   A 1 370 ? 41.649 22.827  12.326  1.00 13.47 ? 444 ILE   A CG2 1 
ATOM   2941 C  CD1 . ILE   A 1 370 ? 43.142 20.223  11.264  1.00 13.63 ? 444 ILE   A CD1 1 
ATOM   2942 N  N   . SER   A 1 371 ? 43.830 25.677  12.016  1.00 13.12 ? 445 SER   A N   1 
ATOM   2943 C  CA  . SER   A 1 371 ? 43.822 26.884  12.824  1.00 13.50 ? 445 SER   A CA  1 
ATOM   2944 C  C   . SER   A 1 371 ? 43.465 28.132  12.021  1.00 13.66 ? 445 SER   A C   1 
ATOM   2945 O  O   . SER   A 1 371 ? 42.623 28.925  12.443  1.00 13.89 ? 445 SER   A O   1 
ATOM   2946 C  CB  . SER   A 1 371 ? 45.137 27.059  13.488  1.00 14.52 ? 445 SER   A CB  1 
ATOM   2947 O  OG  . SER   A 1 371 ? 45.181 28.225  14.290  1.00 17.63 ? 445 SER   A OG  1 
ATOM   2948 N  N   . GLN   A 1 372 ? 44.036 28.228  10.828  1.00 13.04 ? 446 GLN   A N   1 
ATOM   2949 C  CA  . GLN   A 1 372 ? 43.772 29.410  10.021  1.00 14.68 ? 446 GLN   A CA  1 
ATOM   2950 C  C   . GLN   A 1 372 ? 42.320 29.417  9.565   1.00 14.12 ? 446 GLN   A C   1 
ATOM   2951 O  O   . GLN   A 1 372 ? 41.705 30.505  9.505   1.00 15.23 ? 446 GLN   A O   1 
ATOM   2952 C  CB  . GLN   A 1 372 ? 44.727 29.432  8.843   1.00 15.84 ? 446 GLN   A CB  1 
ATOM   2953 C  CG  . GLN   A 1 372 ? 46.160 29.792  9.195   1.00 17.32 ? 446 GLN   A CG  1 
ATOM   2954 C  CD  . GLN   A 1 372 ? 47.032 29.774  7.965   1.00 21.01 ? 446 GLN   A CD  1 
ATOM   2955 O  OE1 . GLN   A 1 372 ? 46.797 30.545  7.021   1.00 22.79 ? 446 GLN   A OE1 1 
ATOM   2956 N  NE2 . GLN   A 1 372 ? 47.928 28.812  7.849   1.00 20.87 ? 446 GLN   A NE2 1 
ATOM   2957 N  N   . VAL   A 1 373 ? 41.727 28.287  9.227   1.00 13.86 ? 447 VAL   A N   1 
ATOM   2958 C  CA  . VAL   A 1 373 ? 40.355 28.263  8.799   1.00 13.01 ? 447 VAL   A CA  1 
ATOM   2959 C  C   . VAL   A 1 373 ? 39.466 28.675  9.962   1.00 13.30 ? 447 VAL   A C   1 
ATOM   2960 O  O   . VAL   A 1 373 ? 38.528 29.473  9.814   1.00 12.92 ? 447 VAL   A O   1 
ATOM   2961 C  CB  . VAL   A 1 373 ? 39.937 26.938  8.169   1.00 13.76 ? 447 VAL   A CB  1 
ATOM   2962 C  CG1 . VAL   A 1 373 ? 38.501 26.987  7.746   1.00 13.84 ? 447 VAL   A CG1 1 
ATOM   2963 C  CG2 . VAL   A 1 373 ? 40.831 26.577  6.998   1.00 14.54 ? 447 VAL   A CG2 1 
ATOM   2964 N  N   . LEU   A 1 374 ? 39.698 28.093  11.151  1.00 12.90 ? 448 LEU   A N   1 
ATOM   2965 C  CA  . LEU   A 1 374 ? 38.926 28.471  12.337  1.00 12.64 ? 448 LEU   A CA  1 
ATOM   2966 C  C   . LEU   A 1 374 ? 39.012 29.965  12.626  1.00 12.55 ? 448 LEU   A C   1 
ATOM   2967 O  O   . LEU   A 1 374 ? 37.969 30.596  12.935  1.00 13.16 ? 448 LEU   A O   1 
ATOM   2968 C  CB  . LEU   A 1 374 ? 39.390 27.689  13.571  1.00 12.25 ? 448 LEU   A CB  1 
ATOM   2969 C  CG  . LEU   A 1 374 ? 39.056 26.202  13.538  1.00 13.61 ? 448 LEU   A CG  1 
ATOM   2970 C  CD1 . LEU   A 1 374 ? 39.868 25.460  14.597  1.00 15.15 ? 448 LEU   A CD1 1 
ATOM   2971 C  CD2 . LEU   A 1 374 ? 37.589 25.949  13.776  1.00 13.21 ? 448 LEU   A CD2 1 
ATOM   2972 N  N   . GLU   A 1 375 ? 40.215 30.550  12.532  1.00 13.23 ? 449 GLU   A N   1 
ATOM   2973 C  CA  . GLU   A 1 375 ? 40.341 31.976  12.817  1.00 13.66 ? 449 GLU   A CA  1 
ATOM   2974 C  C   . GLU   A 1 375 ? 39.591 32.836  11.791  1.00 14.14 ? 449 GLU   A C   1 
ATOM   2975 O  O   . GLU   A 1 375 ? 39.194 33.946  12.145  1.00 15.84 ? 449 GLU   A O   1 
ATOM   2976 C  CB  . GLU   A 1 375 ? 41.819 32.351  12.844  1.00 15.71 ? 449 GLU   A CB  1 
ATOM   2977 C  CG  . GLU   A 1 375 ? 42.581 31.790  14.048  1.00 19.28 ? 449 GLU   A CG  1 
ATOM   2978 C  CD  . GLU   A 1 375 ? 41.943 32.116  15.377  1.00 24.45 ? 449 GLU   A CD  1 
ATOM   2979 O  OE1 . GLU   A 1 375 ? 41.744 33.316  15.675  1.00 27.96 ? 449 GLU   A OE1 1 
ATOM   2980 O  OE2 . GLU   A 1 375 ? 41.496 31.156  16.047  1.00 30.79 ? 449 GLU   A OE2 1 
ATOM   2981 N  N   . SER   A 1 376 ? 39.407 32.326  10.576  1.00 13.54 ? 450 SER   A N   1 
ATOM   2982 C  CA  . SER   A 1 376 ? 38.772 33.088  9.502   1.00 13.16 ? 450 SER   A CA  1 
ATOM   2983 C  C   . SER   A 1 376 ? 37.260 33.060  9.639   1.00 13.64 ? 450 SER   A C   1 
ATOM   2984 O  O   . SER   A 1 376 ? 36.583 33.908  9.042   1.00 14.37 ? 450 SER   A O   1 
ATOM   2985 C  CB  . SER   A 1 376 ? 39.205 32.573  8.168   1.00 15.15 ? 450 SER   A CB  1 
ATOM   2986 O  OG  . SER   A 1 376 ? 38.525 31.404  7.812   1.00 16.94 ? 450 SER   A OG  1 
ATOM   2987 N  N   . PHE   A 1 377 ? 36.649 32.103  10.362  1.00 13.16 ? 451 PHE   A N   1 
ATOM   2988 C  CA  . PHE   A 1 377 ? 35.215 31.903  10.435  1.00 12.97 ? 451 PHE   A CA  1 
ATOM   2989 C  C   . PHE   A 1 377 ? 34.608 32.854  11.458  1.00 13.21 ? 451 PHE   A C   1 
ATOM   2990 O  O   . PHE   A 1 377 ? 35.191 33.117  12.524  1.00 13.86 ? 451 PHE   A O   1 
ATOM   2991 C  CB  . PHE   A 1 377 ? 34.922 30.460  10.873  1.00 13.35 ? 451 PHE   A CB  1 
ATOM   2992 C  CG  . PHE   A 1 377 ? 33.434 30.194  10.939  1.00 13.08 ? 451 PHE   A CG  1 
ATOM   2993 C  CD1 . PHE   A 1 377 ? 32.663 30.177  9.783   1.00 13.79 ? 451 PHE   A CD1 1 
ATOM   2994 C  CD2 . PHE   A 1 377 ? 32.826 30.009  12.166  1.00 13.90 ? 451 PHE   A CD2 1 
ATOM   2995 C  CE1 . PHE   A 1 377 ? 31.304 30.008  9.879   1.00 14.59 ? 451 PHE   A CE1 1 
ATOM   2996 C  CE2 . PHE   A 1 377 ? 31.460 29.813  12.246  1.00 14.59 ? 451 PHE   A CE2 1 
ATOM   2997 C  CZ  . PHE   A 1 377 ? 30.707 29.795  11.082  1.00 15.30 ? 451 PHE   A CZ  1 
ATOM   2998 N  N   . ASN   A 1 378 ? 33.412 33.363  11.163  1.00 13.39 ? 452 ASN   A N   1 
ATOM   2999 C  CA  . ASN   A 1 378 ? 32.642 34.192  12.048  1.00 12.93 ? 452 ASN   A CA  1 
ATOM   3000 C  C   . ASN   A 1 378 ? 31.304 33.518  12.335  1.00 12.76 ? 452 ASN   A C   1 
ATOM   3001 O  O   . ASN   A 1 378 ? 30.630 33.046  11.433  1.00 14.06 ? 452 ASN   A O   1 
ATOM   3002 C  CB  . ASN   A 1 378 ? 32.384 35.594  11.446  1.00 13.33 ? 452 ASN   A CB  1 
ATOM   3003 C  CG  . ASN   A 1 378 ? 32.102 36.628  12.516  1.00 14.81 ? 452 ASN   A CG  1 
ATOM   3004 O  OD1 . ASN   A 1 378 ? 30.980 37.130  12.658  1.00 16.63 ? 452 ASN   A OD1 1 
ATOM   3005 N  ND2 . ASN   A 1 378 ? 33.096 36.945  13.275  1.00 13.98 ? 452 ASN   A ND2 1 
ATOM   3006 N  N   . SER   A 1 379 ? 30.930 33.519  13.600  1.00 12.91 ? 453 SER   A N   1 
ATOM   3007 C  CA  . SER   A 1 379 ? 29.677 32.885  14.009  1.00 13.78 ? 453 SER   A CA  1 
ATOM   3008 C  C   . SER   A 1 379 ? 28.501 33.372  13.164  1.00 14.66 ? 453 SER   A C   1 
ATOM   3009 O  O   . SER   A 1 379 ? 28.414 34.581  12.911  1.00 15.74 ? 453 SER   A O   1 
ATOM   3010 C  CB  . SER   A 1 379 ? 29.367 33.136  15.460  1.00 16.54 ? 453 SER   A CB  1 
ATOM   3011 O  OG  . SER   A 1 379 ? 30.366 32.534  16.261  1.00 21.89 ? 453 SER   A OG  1 
ATOM   3012 N  N   . GLN   A 1 380 ? 27.549 32.495  12.863  1.00 14.76 ? 454 GLN   A N   1 
ATOM   3013 C  CA  . GLN   A 1 380 ? 26.319 32.856  12.154  1.00 14.58 ? 454 GLN   A CA  1 
ATOM   3014 C  C   . GLN   A 1 380 ? 25.128 32.586  13.033  1.00 16.38 ? 454 GLN   A C   1 
ATOM   3015 O  O   . GLN   A 1 380 ? 25.139 31.670  13.852  1.00 19.04 ? 454 GLN   A O   1 
ATOM   3016 C  CB  . GLN   A 1 380 ? 26.203 32.061  10.871  1.00 16.37 ? 454 GLN   A CB  1 
ATOM   3017 C  CG  . GLN   A 1 380 ? 27.255 32.376  9.831   1.00 17.61 ? 454 GLN   A CG  1 
ATOM   3018 C  CD  . GLN   A 1 380 ? 27.059 31.702  8.500   1.00 19.31 ? 454 GLN   A CD  1 
ATOM   3019 O  OE1 . GLN   A 1 380 ? 25.993 31.107  8.264   1.00 22.78 ? 454 GLN   A OE1 1 
ATOM   3020 N  NE2 . GLN   A 1 380 ? 28.075 31.797  7.650   1.00 20.70 ? 454 GLN   A NE2 1 
ATOM   3021 N  N   . LYS   A 1 381 ? 24.019 33.295  12.800  1.00 18.21 ? 455 LYS   A N   1 
ATOM   3022 C  CA  . LYS   A 1 381 ? 22.811 32.915  13.501  1.00 21.60 ? 455 LYS   A CA  1 
ATOM   3023 C  C   . LYS   A 1 381 ? 22.364 31.536  13.029  1.00 17.96 ? 455 LYS   A C   1 
ATOM   3024 O  O   . LYS   A 1 381 ? 22.402 31.215  11.872  1.00 18.99 ? 455 LYS   A O   1 
ATOM   3025 C  CB  . LYS   A 1 381 ? 21.679 33.910  13.234  1.00 27.78 ? 455 LYS   A CB  1 
ATOM   3026 C  CG  . LYS   A 1 381 ? 20.645 33.959  14.350  1.00 34.64 ? 455 LYS   A CG  1 
ATOM   3027 C  CD  . LYS   A 1 381 ? 19.871 35.276  14.435  1.00 38.53 ? 455 LYS   A CD  1 
ATOM   3028 C  CE  . LYS   A 1 381 ? 19.188 35.601  13.139  1.00 45.35 ? 455 LYS   A CE  1 
ATOM   3029 N  NZ  . LYS   A 1 381 ? 18.041 36.491  13.350  1.00 47.52 ? 455 LYS   A NZ  1 
ATOM   3030 N  N   . VAL   A 1 382 ? 21.952 30.724  13.990  1.00 21.21 ? 456 VAL   A N   1 
ATOM   3031 C  CA  . VAL   A 1 382 ? 21.588 29.352  13.707  1.00 22.65 ? 456 VAL   A CA  1 
ATOM   3032 C  C   . VAL   A 1 382 ? 20.153 29.299  13.181  1.00 22.33 ? 456 VAL   A C   1 
ATOM   3033 O  O   . VAL   A 1 382 ? 19.241 29.780  13.854  1.00 25.83 ? 456 VAL   A O   1 
ATOM   3034 C  CB  . VAL   A 1 382 ? 21.723 28.494  14.971  1.00 23.85 ? 456 VAL   A CB  1 
ATOM   3035 C  CG1 . VAL   A 1 382 ? 21.290 27.065  14.684  1.00 24.14 ? 456 VAL   A CG1 1 
ATOM   3036 C  CG2 . VAL   A 1 382 ? 23.139 28.548  15.548  1.00 23.53 ? 456 VAL   A CG2 1 
ATOM   3037 N  N   . SER   A 1 383 ? 19.980 28.784  11.966  1.00 20.98 ? 457 SER   A N   1 
ATOM   3038 C  CA  . SER   A 1 383 ? 18.671 28.615  11.339  1.00 23.70 ? 457 SER   A CA  1 
ATOM   3039 C  C   . SER   A 1 383 ? 17.733 27.874  12.278  1.00 27.43 ? 457 SER   A C   1 
ATOM   3040 O  O   . SER   A 1 383 ? 18.101 26.893  12.941  1.00 27.22 ? 457 SER   A O   1 
ATOM   3041 C  CB  . SER   A 1 383 ? 18.745 27.886  10.042  1.00 24.42 ? 457 SER   A CB  1 
ATOM   3042 O  OG  . SER   A 1 383 ? 19.515 28.509  9.028   1.00 28.49 ? 457 SER   A OG  1 
ATOM   3043 N  N   . GLU   A 1 384 ? 16.470 28.303  12.241  1.00 29.16 ? 458 GLU   A N   1 
ATOM   3044 C  CA  . GLU   A 1 384 ? 15.501 27.868  13.232  1.00 31.03 ? 458 GLU   A CA  1 
ATOM   3045 C  C   . GLU   A 1 384 ? 14.690 26.679  12.718  1.00 29.69 ? 458 GLU   A C   1 
ATOM   3046 O  O   . GLU   A 1 384 ? 14.075 25.955  13.488  1.00 40.55 ? 458 GLU   A O   1 
ATOM   3047 C  CB  . GLU   A 1 384 ? 14.592 29.070  13.507  1.00 35.32 ? 458 GLU   A CB  1 
ATOM   3048 C  CG  . GLU   A 1 384 ? 15.329 30.204  14.226  1.00 40.92 ? 458 GLU   A CG  1 
ATOM   3049 C  CD  . GLU   A 1 384 ? 14.609 31.535  14.410  1.00 46.05 ? 458 GLU   A CD  1 
ATOM   3050 O  OE1 . GLU   A 1 384 ? 13.392 31.630  14.149  1.00 46.55 ? 458 GLU   A OE1 1 
ATOM   3051 O  OE2 . GLU   A 1 384 ? 15.294 32.502  14.820  1.00 51.08 ? 458 GLU   A OE2 1 
ATOM   3052 N  N   . ASN   A 1 385 ? 14.734 26.497  11.421  1.00 26.15 ? 459 ASN   A N   1 
ATOM   3053 C  CA  . ASN   A 1 385 ? 14.055 25.463  10.669  1.00 30.59 ? 459 ASN   A CA  1 
ATOM   3054 C  C   . ASN   A 1 385 ? 15.060 24.358  10.340  1.00 29.91 ? 459 ASN   A C   1 
ATOM   3055 O  O   . ASN   A 1 385 ? 16.171 24.646  9.894   1.00 28.20 ? 459 ASN   A O   1 
ATOM   3056 C  CB  . ASN   A 1 385 ? 13.446 26.179  9.469   1.00 33.41 ? 459 ASN   A CB  1 
ATOM   3057 C  CG  . ASN   A 1 385 ? 13.008 25.292  8.348   1.00 38.81 ? 459 ASN   A CG  1 
ATOM   3058 O  OD1 . ASN   A 1 385 ? 13.822 24.857  7.531   1.00 36.55 ? 459 ASN   A OD1 1 
ATOM   3059 N  ND2 . ASN   A 1 385 ? 11.697 25.144  8.204   1.00 46.31 ? 459 ASN   A ND2 1 
ATOM   3060 N  N   . SER   A 1 386 ? 14.663 23.095  10.527  1.00 28.36 ? 460 SER   A N   1 
ATOM   3061 C  CA  . SER   A 1 386 ? 15.567 21.968  10.304  1.00 28.61 ? 460 SER   A CA  1 
ATOM   3062 C  C   . SER   A 1 386 ? 16.134 21.956  8.885   1.00 29.33 ? 460 SER   A C   1 
ATOM   3063 O  O   . SER   A 1 386 ? 17.319 21.711  8.667   1.00 27.37 ? 460 SER   A O   1 
ATOM   3064 C  CB  . SER   A 1 386 ? 14.890 20.649  10.676  1.00 28.33 ? 460 SER   A CB  1 
ATOM   3065 O  OG  . SER   A 1 386 ? 15.813 19.567  10.595  1.00 30.66 ? 460 SER   A OG  1 
ATOM   3066 N  N   . GLU   A 1 387 ? 15.307 22.173  7.865   1.00 28.50 ? 461 GLU   A N   1 
ATOM   3067 C  CA  . GLU   A 1 387 ? 15.761 22.144  6.491   1.00 27.68 ? 461 GLU   A CA  1 
ATOM   3068 C  C   . GLU   A 1 387 ? 16.799 23.242  6.208   1.00 26.26 ? 461 GLU   A C   1 
ATOM   3069 O  O   . GLU   A 1 387 ? 17.779 23.019  5.507   1.00 27.43 ? 461 GLU   A O   1 
ATOM   3070 C  CB  . GLU   A 1 387 ? 14.539 22.217  5.573   1.00 35.90 ? 461 GLU   A CB  1 
ATOM   3071 C  CG  . GLU   A 1 387 ? 14.899 22.302  4.094   1.00 41.06 ? 461 GLU   A CG  1 
ATOM   3072 C  CD  . GLU   A 1 387 ? 13.721 22.206  3.130   1.00 50.87 ? 461 GLU   A CD  1 
ATOM   3073 O  OE1 . GLU   A 1 387 ? 12.940 21.234  3.236   1.00 57.76 ? 461 GLU   A OE1 1 
ATOM   3074 O  OE2 . GLU   A 1 387 ? 13.591 23.093  2.258   1.00 55.12 ? 461 GLU   A OE2 1 
ATOM   3075 N  N   . ASP   A 1 388 ? 16.531 24.465  6.670   1.00 25.39 ? 462 ASP   A N   1 
ATOM   3076 C  CA  . ASP   A 1 388 ? 17.473 25.562  6.482   1.00 24.79 ? 462 ASP   A CA  1 
ATOM   3077 C  C   . ASP   A 1 388 ? 18.773 25.299  7.258   1.00 20.93 ? 462 ASP   A C   1 
ATOM   3078 O  O   . ASP   A 1 388 ? 19.832 25.735  6.791   1.00 22.42 ? 462 ASP   A O   1 
ATOM   3079 C  CB  . ASP   A 1 388 ? 16.842 26.901  6.846   1.00 26.13 ? 462 ASP   A CB  1 
ATOM   3080 C  CG  . ASP   A 1 388 ? 15.809 27.401  5.840   1.00 31.27 ? 462 ASP   A CG  1 
ATOM   3081 O  OD1 . ASP   A 1 388 ? 15.795 26.904  4.709   1.00 32.98 ? 462 ASP   A OD1 1 
ATOM   3082 O  OD2 . ASP   A 1 388 ? 14.987 28.227  6.244   1.00 36.33 ? 462 ASP   A OD2 1 
ATOM   3083 N  N   . LEU   A 1 389 ? 18.619 24.724  8.437   1.00 22.58 ? 463 LEU   A N   1 
ATOM   3084 C  CA  . LEU   A 1 389 ? 19.791 24.410  9.262   1.00 20.87 ? 463 LEU   A CA  1 
ATOM   3085 C  C   . LEU   A 1 389 ? 20.719 23.398  8.594   1.00 20.71 ? 463 LEU   A C   1 
ATOM   3086 O  O   . LEU   A 1 389 ? 21.925 23.619  8.514   1.00 19.60 ? 463 LEU   A O   1 
ATOM   3087 C  CB  . LEU   A 1 389 ? 19.372 23.950  10.643  1.00 19.52 ? 463 LEU   A CB  1 
ATOM   3088 C  CG  . LEU   A 1 389 ? 20.524 23.565  11.581  1.00 19.69 ? 463 LEU   A CG  1 
ATOM   3089 C  CD1 . LEU   A 1 389 ? 21.522 24.706  11.728  1.00 19.71 ? 463 LEU   A CD1 1 
ATOM   3090 C  CD2 . LEU   A 1 389 ? 20.001 23.123  12.914  1.00 19.67 ? 463 LEU   A CD2 1 
ATOM   3091 N  N   . MET   A 1 390 ? 20.166 22.379  7.956   1.00 20.91 ? 464 MET   A N   1 
ATOM   3092 C  CA  . MET   A 1 390 ? 20.985 21.477  7.160   1.00 21.02 ? 464 MET   A CA  1 
ATOM   3093 C  C   . MET   A 1 390 ? 21.666 22.197  6.003   1.00 20.29 ? 464 MET   A C   1 
ATOM   3094 O  O   . MET   A 1 390 ? 22.834 21.990  5.685   1.00 20.08 ? 464 MET   A O   1 
ATOM   3095 C  CB  . MET   A 1 390 ? 20.184 20.281  6.640   1.00 23.35 ? 464 MET   A CB  1 
ATOM   3096 C  CG  . MET   A 1 390 ? 21.033 19.180  6.016   1.00 26.55 ? 464 MET   A CG  1 
ATOM   3097 S  SD  . MET   A 1 390 ? 22.530 18.644  6.878   1.00 28.64 ? 464 MET   A SD  1 
ATOM   3098 C  CE  . MET   A 1 390 ? 21.981 18.148  8.509   1.00 31.64 ? 464 MET   A CE  1 
ATOM   3099 N  N   . LYS   A 1 391 ? 20.936 23.091  5.271   1.00 21.53 ? 465 LYS   A N   1 
ATOM   3100 C  CA  . LYS   A 1 391 ? 21.581 23.818  4.193   1.00 19.62 ? 465 LYS   A CA  1 
ATOM   3101 C  C   . LYS   A 1 391 ? 22.758 24.692  4.666   1.00 17.48 ? 465 LYS   A C   1 
ATOM   3102 O  O   . LYS   A 1 391 ? 23.744 24.823  3.975   1.00 18.72 ? 465 LYS   A O   1 
ATOM   3103 C  CB  . LYS   A 1 391 ? 20.570 24.723  3.462   1.00 24.28 ? 465 LYS   A CB  1 
ATOM   3104 C  CG  . LYS   A 1 391 ? 19.607 23.988  2.575   1.00 30.63 ? 465 LYS   A CG  1 
ATOM   3105 C  CD  . LYS   A 1 391 ? 18.739 24.951  1.763   1.00 37.34 ? 465 LYS   A CD  1 
ATOM   3106 C  CE  . LYS   A 1 391 ? 17.648 24.214  1.067   1.00 43.31 ? 465 LYS   A CE  1 
ATOM   3107 N  NZ  . LYS   A 1 391 ? 16.768 25.156  0.370   1.00 46.16 ? 465 LYS   A NZ  1 
ATOM   3108 N  N   . GLN   A 1 392 ? 22.562 25.291  5.833   1.00 18.48 ? 466 GLN   A N   1 
ATOM   3109 C  CA  . GLN   A 1 392 ? 23.567 26.149  6.436   1.00 18.43 ? 466 GLN   A CA  1 
ATOM   3110 C  C   . GLN   A 1 392 ? 24.803 25.329  6.853   1.00 17.30 ? 466 GLN   A C   1 
ATOM   3111 O  O   . GLN   A 1 392 ? 25.930 25.714  6.541   1.00 15.74 ? 466 GLN   A O   1 
ATOM   3112 C  CB  . GLN   A 1 392 ? 22.945 26.802  7.654   1.00 18.87 ? 466 GLN   A CB  1 
ATOM   3113 C  CG  . GLN   A 1 392 ? 23.849 27.768  8.393   1.00 20.14 ? 466 GLN   A CG  1 
ATOM   3114 C  CD  . GLN   A 1 392 ? 23.077 28.575  9.405   1.00 21.24 ? 466 GLN   A CD  1 
ATOM   3115 O  OE1 . GLN   A 1 392 ? 22.099 28.124  10.016  1.00 20.48 ? 466 GLN   A OE1 1 
ATOM   3116 N  NE2 . GLN   A 1 392 ? 23.638 29.719  9.772   1.00 19.99 ? 466 GLN   A NE2 1 
ATOM   3117 N  N   . ILE   A 1 393 ? 24.594 24.134  7.430   1.00 17.33 ? 467 ILE   A N   1 
ATOM   3118 C  CA  . ILE   A 1 393 ? 25.706 23.216  7.746   1.00 16.29 ? 467 ILE   A CA  1 
ATOM   3119 C  C   . ILE   A 1 393 ? 26.474 22.841  6.494   1.00 16.29 ? 467 ILE   A C   1 
ATOM   3120 O  O   . ILE   A 1 393 ? 27.696 22.913  6.447   1.00 16.52 ? 467 ILE   A O   1 
ATOM   3121 C  CB  . ILE   A 1 393 ? 25.169 21.987  8.496   1.00 16.25 ? 467 ILE   A CB  1 
ATOM   3122 C  CG1 . ILE   A 1 393 ? 24.694 22.387  9.867   1.00 17.26 ? 467 ILE   A CG1 1 
ATOM   3123 C  CG2 . ILE   A 1 393 ? 26.238 20.895  8.616   1.00 17.07 ? 467 ILE   A CG2 1 
ATOM   3124 C  CD1 . ILE   A 1 393 ? 23.846 21.353  10.573  1.00 17.73 ? 467 ILE   A CD1 1 
ATOM   3125 N  N   . LEU   A 1 394 ? 25.745 22.456  5.422   1.00 17.56 ? 468 LEU   A N   1 
ATOM   3126 C  CA  . LEU   A 1 394 ? 26.384 22.080  4.182   1.00 18.48 ? 468 LEU   A CA  1 
ATOM   3127 C  C   . LEU   A 1 394 ? 27.216 23.225  3.582   1.00 16.54 ? 468 LEU   A C   1 
ATOM   3128 O  O   . LEU   A 1 394 ? 28.306 23.055  3.101   1.00 17.15 ? 468 LEU   A O   1 
ATOM   3129 C  CB  . LEU   A 1 394 ? 25.304 21.610  3.197   1.00 20.72 ? 468 LEU   A CB  1 
ATOM   3130 C  CG  . LEU   A 1 394 ? 24.550 20.315  3.500   1.00 28.37 ? 468 LEU   A CG  1 
ATOM   3131 C  CD1 . LEU   A 1 394 ? 23.306 20.090  2.644   1.00 30.20 ? 468 LEU   A CD1 1 
ATOM   3132 C  CD2 . LEU   A 1 394 ? 25.502 19.204  3.232   1.00 31.40 ? 468 LEU   A CD2 1 
ATOM   3133 N  N   . GLN   A 1 395 ? 26.626 24.443  3.583   1.00 17.38 ? 469 GLN   A N   1 
ATOM   3134 C  CA  . GLN   A 1 395 ? 27.321 25.580  3.018   1.00 18.12 ? 469 GLN   A CA  1 
ATOM   3135 C  C   . GLN   A 1 395 ? 28.612 25.902  3.784   1.00 14.74 ? 469 GLN   A C   1 
ATOM   3136 O  O   . GLN   A 1 395 ? 29.642 26.165  3.194   1.00 15.42 ? 469 GLN   A O   1 
ATOM   3137 C  CB  . GLN   A 1 395 ? 26.391 26.805  2.978   1.00 19.92 ? 469 GLN   A CB  1 
ATOM   3138 C  CG  . GLN   A 1 395 ? 27.076 28.077  2.459   1.00 20.75 ? 469 GLN   A CG  1 
ATOM   3139 C  CD  . GLN   A 1 395 ? 27.699 28.918  3.543   1.00 19.75 ? 469 GLN   A CD  1 
ATOM   3140 O  OE1 . GLN   A 1 395 ? 27.106 29.143  4.581   1.00 23.38 ? 469 GLN   A OE1 1 
ATOM   3141 N  NE2 . GLN   A 1 395 ? 28.891 29.462  3.307   1.00 20.98 ? 469 GLN   A NE2 1 
ATOM   3142 N  N   . ILE   A 1 396 ? 28.516 25.900  5.124   1.00 15.76 ? 470 ILE   A N   1 
ATOM   3143 C  CA  . ILE   A 1 396 ? 29.680 26.176  5.964   1.00 15.55 ? 470 ILE   A CA  1 
ATOM   3144 C  C   . ILE   A 1 396 ? 30.752 25.084  5.815   1.00 13.92 ? 470 ILE   A C   1 
ATOM   3145 O  O   . ILE   A 1 396 ? 31.923 25.386  5.679   1.00 14.23 ? 470 ILE   A O   1 
ATOM   3146 C  CB  . ILE   A 1 396 ? 29.264 26.435  7.413   1.00 15.00 ? 470 ILE   A CB  1 
ATOM   3147 C  CG1 . ILE   A 1 396 ? 28.435 27.719  7.500   1.00 15.37 ? 470 ILE   A CG1 1 
ATOM   3148 C  CG2 . ILE   A 1 396 ? 30.473 26.492  8.342   1.00 15.11 ? 470 ILE   A CG2 1 
ATOM   3149 C  CD1 . ILE   A 1 396 ? 27.747 27.895  8.825   1.00 17.04 ? 470 ILE   A CD1 1 
ATOM   3150 N  N   . HIS   A 1 397 ? 30.314 23.818  5.767   1.00 14.59 ? 471 HIS   A N   1 
ATOM   3151 C  CA  . HIS   A 1 397 ? 31.254 22.704  5.585   1.00 15.05 ? 471 HIS   A CA  1 
ATOM   3152 C  C   . HIS   A 1 397 ? 31.996 22.872  4.270   1.00 15.11 ? 471 HIS   A C   1 
ATOM   3153 O  O   . HIS   A 1 397 ? 33.190 22.755  4.193   1.00 14.66 ? 471 HIS   A O   1 
ATOM   3154 C  CB  . HIS   A 1 397 ? 30.467 21.400  5.614   1.00 16.76 ? 471 HIS   A CB  1 
ATOM   3155 C  CG  . HIS   A 1 397 ? 31.131 20.215  4.968   1.00 22.38 ? 471 HIS   A CG  1 
ATOM   3156 N  ND1 . HIS   A 1 397 ? 32.017 19.556  5.770   1.00 19.07 ? 471 HIS   A ND1 1 
ATOM   3157 C  CD2 . HIS   A 1 397 ? 31.161 19.532  3.819   1.00 24.44 ? 471 HIS   A CD2 1 
ATOM   3158 C  CE1 . HIS   A 1 397 ? 32.510 18.501  5.243   1.00 20.85 ? 471 HIS   A CE1 1 
ATOM   3159 N  NE2 . HIS   A 1 397 ? 32.036 18.463  3.985   1.00 23.19 ? 471 HIS   A NE2 1 
ATOM   3160 N  N   . SER   A 1 398 ? 31.234 23.175  3.187   1.00 16.05 ? 472 SER   A N   1 
ATOM   3161 C  CA  . SER   A 1 398 ? 31.847 23.342  1.878   1.00 16.99 ? 472 SER   A CA  1 
ATOM   3162 C  C   . SER   A 1 398 ? 32.799 24.534  1.799   1.00 15.39 ? 472 SER   A C   1 
ATOM   3163 O  O   . SER   A 1 398 ? 33.863 24.446  1.218   1.00 15.90 ? 472 SER   A O   1 
ATOM   3164 C  CB  . SER   A 1 398 ? 30.781 23.463  0.856   1.00 20.92 ? 472 SER   A CB  1 
ATOM   3165 O  OG  . SER   A 1 398 ? 30.092 22.234  0.792   1.00 28.49 ? 472 SER   A OG  1 
ATOM   3166 N  N   . TRP   A 1 399 ? 32.368 25.673  2.389   1.00 14.71 ? 473 TRP   A N   1 
ATOM   3167 C  CA  . TRP   A 1 399 ? 33.227 26.836  2.454   1.00 15.92 ? 473 TRP   A CA  1 
ATOM   3168 C  C   . TRP   A 1 399 ? 34.542 26.494  3.152   1.00 14.84 ? 473 TRP   A C   1 
ATOM   3169 O  O   . TRP   A 1 399 ? 35.613 26.917  2.767   1.00 15.11 ? 473 TRP   A O   1 
ATOM   3170 C  CB  . TRP   A 1 399 ? 32.518 28.027  3.150   1.00 15.92 ? 473 TRP   A CB  1 
ATOM   3171 C  CG  . TRP   A 1 399 ? 33.495 29.066  3.611   1.00 16.79 ? 473 TRP   A CG  1 
ATOM   3172 C  CD1 . TRP   A 1 399 ? 34.105 29.993  2.808   1.00 16.07 ? 473 TRP   A CD1 1 
ATOM   3173 C  CD2 . TRP   A 1 399 ? 34.149 29.157  4.893   1.00 15.41 ? 473 TRP   A CD2 1 
ATOM   3174 N  NE1 . TRP   A 1 399 ? 35.080 30.638  3.499   1.00 15.78 ? 473 TRP   A NE1 1 
ATOM   3175 C  CE2 . TRP   A 1 399 ? 35.152 30.128  4.776   1.00 15.04 ? 473 TRP   A CE2 1 
ATOM   3176 C  CE3 . TRP   A 1 399 ? 34.024 28.472  6.104   1.00 14.74 ? 473 TRP   A CE3 1 
ATOM   3177 C  CZ2 . TRP   A 1 399 ? 35.983 30.474  5.818   1.00 15.58 ? 473 TRP   A CZ2 1 
ATOM   3178 C  CZ3 . TRP   A 1 399 ? 34.849 28.807  7.135   1.00 15.54 ? 473 TRP   A CZ3 1 
ATOM   3179 C  CH2 . TRP   A 1 399 ? 35.833 29.781  6.992   1.00 15.71 ? 473 TRP   A CH2 1 
ATOM   3180 N  N   . ALA   A 1 400 ? 34.436 25.793  4.320   1.00 14.34 ? 474 ALA   A N   1 
ATOM   3181 C  CA  . ALA   A 1 400 ? 35.617 25.533  5.133   1.00 14.47 ? 474 ALA   A CA  1 
ATOM   3182 C  C   . ALA   A 1 400 ? 36.574 24.590  4.388   1.00 13.41 ? 474 ALA   A C   1 
ATOM   3183 O  O   . ALA   A 1 400 ? 37.767 24.781  4.474   1.00 14.62 ? 474 ALA   A O   1 
ATOM   3184 C  CB  . ALA   A 1 400 ? 35.205 24.944  6.470   1.00 14.13 ? 474 ALA   A CB  1 
ATOM   3185 N  N   . LYS   A 1 401 ? 36.046 23.616  3.618   1.00 14.43 ? 475 LYS   A N   1 
ATOM   3186 C  CA  . LYS   A 1 401 ? 36.896 22.783  2.784   1.00 16.13 ? 475 LYS   A CA  1 
ATOM   3187 C  C   . LYS   A 1 401 ? 37.601 23.628  1.728   1.00 15.41 ? 475 LYS   A C   1 
ATOM   3188 O  O   . LYS   A 1 401 ? 38.775 23.498  1.455   1.00 17.25 ? 475 LYS   A O   1 
ATOM   3189 C  CB  . LYS   A 1 401 ? 36.105 21.634  2.143   1.00 17.77 ? 475 LYS   A CB  1 
ATOM   3190 C  CG  . LYS   A 1 401 ? 35.602 20.596  3.132   1.00 18.67 ? 475 LYS   A CG  1 
ATOM   3191 C  CD  . LYS   A 1 401 ? 35.215 19.250  2.522   1.00 22.76 ? 475 LYS   A CD  1 
ATOM   3192 C  CE  . LYS   A 1 401 ? 34.126 19.266  1.518   1.00 30.51 ? 475 LYS   A CE  1 
ATOM   3193 N  NZ  . LYS   A 1 401 ? 34.036 17.970  0.806   1.00 36.72 ? 475 LYS   A NZ  1 
ATOM   3194 N  N   . ASP   A 1 402 ? 36.824 24.542  1.103   1.00 16.36 ? 476 ASP   A N   1 
ATOM   3195 C  CA  . ASP   A 1 402 ? 37.384 25.385  0.061   1.00 18.12 ? 476 ASP   A CA  1 
ATOM   3196 C  C   . ASP   A 1 402 ? 38.437 26.313  0.625   1.00 16.19 ? 476 ASP   A C   1 
ATOM   3197 O  O   . ASP   A 1 402 ? 39.473 26.577  0.043   1.00 19.57 ? 476 ASP   A O   1 
ATOM   3198 C  CB  . ASP   A 1 402 ? 36.319 26.257  -0.598  1.00 19.89 ? 476 ASP   A CB  1 
ATOM   3199 C  CG  . ASP   A 1 402 ? 35.346 25.569  -1.532  1.00 23.10 ? 476 ASP   A CG  1 
ATOM   3200 O  OD1 . ASP   A 1 402 ? 35.608 24.430  -1.909  1.00 25.98 ? 476 ASP   A OD1 1 
ATOM   3201 O  OD2 . ASP   A 1 402 ? 34.273 26.191  -1.788  1.00 26.78 ? 476 ASP   A OD2 1 
ATOM   3202 N  N   . LYS   A 1 403 ? 38.203 26.824  1.862   1.00 16.22 ? 477 LYS   A N   1 
ATOM   3203 C  CA  . LYS   A 1 403 ? 39.131 27.735  2.508   1.00 16.29 ? 477 LYS   A CA  1 
ATOM   3204 C  C   . LYS   A 1 403 ? 40.439 27.007  2.818   1.00 17.01 ? 477 LYS   A C   1 
ATOM   3205 O  O   . LYS   A 1 403 ? 41.540 27.519  2.634   1.00 17.99 ? 477 LYS   A O   1 
ATOM   3206 C  CB  . LYS   A 1 403 ? 38.519 28.308  3.804   1.00 16.78 ? 477 LYS   A CB  1 
ATOM   3207 C  CG  . LYS   A 1 403 ? 39.352 29.336  4.522   1.00 17.28 ? 477 LYS   A CG  1 
ATOM   3208 C  CD  . LYS   A 1 403 ? 39.471 30.737  3.878   1.00 23.55 ? 477 LYS   A CD  1 
ATOM   3209 C  CE  . LYS   A 1 403 ? 40.601 31.494  4.580   1.00 25.40 ? 477 LYS   A CE  1 
ATOM   3210 N  NZ  . LYS   A 1 403 ? 40.802 32.893  4.119   1.00 28.42 ? 477 LYS   A NZ  1 
ATOM   3211 N  N   . ALA   A 1 404 ? 40.335 25.767  3.361   1.00 16.30 ? 478 ALA   A N   1 
ATOM   3212 C  CA  . ALA   A 1 404 ? 41.528 24.960  3.601   1.00 15.90 ? 478 ALA   A CA  1 
ATOM   3213 C  C   . ALA   A 1 404 ? 42.343 24.738  2.333   1.00 15.89 ? 478 ALA   A C   1 
ATOM   3214 O  O   . ALA   A 1 404 ? 43.551 24.868  2.367   1.00 17.53 ? 478 ALA   A O   1 
ATOM   3215 C  CB  . ALA   A 1 404 ? 41.134 23.649  4.263   1.00 14.85 ? 478 ALA   A CB  1 
ATOM   3216 N  N   . THR   A 1 405 ? 41.649 24.345  1.269   1.00 16.99 ? 479 THR   A N   1 
ATOM   3217 C  CA  . THR   A 1 405 ? 42.331 24.134  -0.012  1.00 18.54 ? 479 THR   A CA  1 
ATOM   3218 C  C   . THR   A 1 405 ? 42.970 25.430  -0.518  1.00 19.92 ? 479 THR   A C   1 
ATOM   3219 O  O   . THR   A 1 405 ? 44.089 25.401  -1.027  1.00 21.22 ? 479 THR   A O   1 
ATOM   3220 C  CB  . THR   A 1 405 ? 41.323 23.532  -0.983  1.00 19.68 ? 479 THR   A CB  1 
ATOM   3221 O  OG1 . THR   A 1 405 ? 40.901 22.254  -0.515  1.00 20.90 ? 479 THR   A OG1 1 
ATOM   3222 C  CG2 . THR   A 1 405 ? 41.903 23.331  -2.381  1.00 21.54 ? 479 THR   A CG2 1 
ATOM   3223 N  N   . ASP   A 1 406 ? 42.292 26.558  -0.319  1.00 19.60 ? 480 ASP   A N   1 
ATOM   3224 C  CA  . ASP   A 1 406 ? 42.821 27.828  -0.774  1.00 23.43 ? 480 ASP   A CA  1 
ATOM   3225 C  C   . ASP   A 1 406 ? 44.100 28.177  -0.028  1.00 22.30 ? 480 ASP   A C   1 
ATOM   3226 O  O   . ASP   A 1 406 ? 45.055 28.657  -0.618  1.00 25.29 ? 480 ASP   A O   1 
ATOM   3227 C  CB  . ASP   A 1 406 ? 41.771 28.902  -0.635  1.00 26.83 ? 480 ASP   A CB  1 
ATOM   3228 C  CG  . ASP   A 1 406 ? 41.990 30.153  -1.451  1.00 35.61 ? 480 ASP   A CG  1 
ATOM   3229 O  OD1 . ASP   A 1 406 ? 42.356 30.029  -2.641  1.00 38.04 ? 480 ASP   A OD1 1 
ATOM   3230 O  OD2 . ASP   A 1 406 ? 41.714 31.216  -0.889  1.00 40.91 ? 480 ASP   A OD2 1 
ATOM   3231 N  N   . ILE   A 1 407 ? 44.161 27.918  1.292   1.00 21.60 ? 481 ILE   A N   1 
ATOM   3232 C  CA  . ILE   A 1 407 ? 45.340 28.181  2.100   1.00 21.21 ? 481 ILE   A CA  1 
ATOM   3233 C  C   . ILE   A 1 407 ? 46.499 27.312  1.610   1.00 22.32 ? 481 ILE   A C   1 
ATOM   3234 O  O   . ILE   A 1 407 ? 47.649 27.767  1.471   1.00 24.65 ? 481 ILE   A O   1 
ATOM   3235 C  CB  . ILE   A 1 407 ? 45.064 27.951  3.608   1.00 21.83 ? 481 ILE   A CB  1 
ATOM   3236 C  CG1 . ILE   A 1 407 ? 44.133 29.058  4.149   1.00 20.94 ? 481 ILE   A CG1 1 
ATOM   3237 C  CG2 . ILE   A 1 407 ? 46.344 27.882  4.439   1.00 21.64 ? 481 ILE   A CG2 1 
ATOM   3238 C  CD1 . ILE   A 1 407 ? 43.396 28.631  5.401   1.00 22.24 ? 481 ILE   A CD1 1 
ATOM   3239 N  N   . TYR   A 1 408 ? 46.210 26.035  1.357   1.00 21.17 ? 482 TYR   A N   1 
ATOM   3240 C  CA  . TYR   A 1 408 ? 47.191 25.129  0.778   1.00 20.92 ? 482 TYR   A CA  1 
ATOM   3241 C  C   . TYR   A 1 408 ? 47.718 25.701  -0.550  1.00 23.56 ? 482 TYR   A C   1 
ATOM   3242 O  O   . TYR   A 1 408 ? 48.940 25.690  -0.709  1.00 26.75 ? 482 TYR   A O   1 
ATOM   3243 C  CB  . TYR   A 1 408 ? 46.607 23.715  0.626   1.00 20.55 ? 482 TYR   A CB  1 
ATOM   3244 C  CG  . TYR   A 1 408 ? 47.445 22.832  -0.275  1.00 21.05 ? 482 TYR   A CG  1 
ATOM   3245 C  CD1 . TYR   A 1 408 ? 48.686 22.370  0.139   1.00 21.07 ? 482 TYR   A CD1 1 
ATOM   3246 C  CD2 . TYR   A 1 408 ? 47.016 22.537  -1.559  1.00 22.29 ? 482 TYR   A CD2 1 
ATOM   3247 C  CE1 . TYR   A 1 408 ? 49.476 21.608  -0.712  1.00 21.56 ? 482 TYR   A CE1 1 
ATOM   3248 C  CE2 . TYR   A 1 408 ? 47.777 21.755  -2.414  1.00 23.21 ? 482 TYR   A CE2 1 
ATOM   3249 C  CZ  . TYR   A 1 408 ? 48.997 21.278  -1.970  1.00 22.69 ? 482 TYR   A CZ  1 
ATOM   3250 O  OH  . TYR   A 1 408 ? 49.794 20.519  -2.792  1.00 24.07 ? 482 TYR   A OH  1 
ATOM   3251 N  N   . ASN   A 1 409 ? 46.795 26.031  -1.466  1.00 23.71 ? 483 ASN   A N   1 
ATOM   3252 C  CA  . ASN   A 1 409 ? 47.124 26.526  -2.815  1.00 25.40 ? 483 ASN   A CA  1 
ATOM   3253 C  C   . ASN   A 1 409 ? 48.005 27.765  -2.734  1.00 30.40 ? 483 ASN   A C   1 
ATOM   3254 O  O   . ASN   A 1 409 ? 48.876 27.923  -3.605  1.00 31.61 ? 483 ASN   A O   1 
ATOM   3255 C  CB  . ASN   A 1 409 ? 45.874 26.790  -3.641  1.00 27.79 ? 483 ASN   A CB  1 
ATOM   3256 C  CG  . ASN   A 1 409 ? 45.244 25.519  -4.139  1.00 25.09 ? 483 ASN   A CG  1 
ATOM   3257 O  OD1 . ASN   A 1 409 ? 45.913 24.495  -4.236  1.00 30.17 ? 483 ASN   A OD1 1 
ATOM   3258 N  ND2 . ASN   A 1 409 ? 43.977 25.579  -4.521  1.00 31.67 ? 483 ASN   A ND2 1 
ATOM   3259 N  N   . LYS   A 1 410 ? 47.799 28.609  -1.717  1.00 35.83 ? 484 LYS   A N   1 
ATOM   3260 C  CA  . LYS   A 1 410 ? 48.477 29.890  -1.589  1.00 42.88 ? 484 LYS   A CA  1 
ATOM   3261 C  C   . LYS   A 1 410 ? 49.916 29.712  -1.114  1.00 52.63 ? 484 LYS   A C   1 
ATOM   3262 O  O   . LYS   A 1 410 ? 50.804 30.400  -1.613  1.00 59.45 ? 484 LYS   A O   1 
ATOM   3263 C  CB  . LYS   A 1 410 ? 47.691 30.853  -0.686  1.00 43.89 ? 484 LYS   A CB  1 
ATOM   3264 C  CG  . LYS   A 1 410 ? 48.471 32.084  -0.214  1.00 50.65 ? 484 LYS   A CG  1 
ATOM   3265 C  CD  . LYS   A 1 410 ? 47.639 33.358  -0.106  1.00 57.04 ? 484 LYS   A CD  1 
ATOM   3266 C  CE  . LYS   A 1 410 ? 48.458 34.608  -0.259  1.00 59.52 ? 484 LYS   A CE  1 
ATOM   3267 N  NZ  . LYS   A 1 410 ? 47.612 35.757  -0.604  1.00 63.40 ? 484 LYS   A NZ  1 
ATOM   3268 N  N   . HIS   A 1 411 ? 50.159 28.813  -0.154  1.00 55.91 ? 485 HIS   A N   1 
ATOM   3269 C  CA  . HIS   A 1 411 ? 51.501 28.623  0.378   1.00 61.54 ? 485 HIS   A CA  1 
ATOM   3270 C  C   . HIS   A 1 411 ? 52.378 27.896  -0.642  1.00 65.40 ? 485 HIS   A C   1 
ATOM   3271 O  O   . HIS   A 1 411 ? 53.599 27.946  -0.533  1.00 74.43 ? 485 HIS   A O   1 
ATOM   3272 C  CB  . HIS   A 1 411 ? 51.469 27.903  1.731   1.00 69.07 ? 485 HIS   A CB  1 
ATOM   3273 C  CG  . HIS   A 1 411 ? 52.699 28.102  2.568   1.00 79.20 ? 485 HIS   A CG  1 
ATOM   3274 N  ND1 . HIS   A 1 411 ? 52.935 29.259  3.285   1.00 82.83 ? 485 HIS   A ND1 1 
ATOM   3275 C  CD2 . HIS   A 1 411 ? 53.754 27.303  2.805   1.00 80.55 ? 485 HIS   A CD2 1 
ATOM   3276 C  CE1 . HIS   A 1 411 ? 54.094 29.154  3.924   1.00 80.26 ? 485 HIS   A CE1 1 
ATOM   3277 N  NE2 . HIS   A 1 411 ? 54.606 27.973  3.649   1.00 80.16 ? 485 HIS   A NE2 1 
ATOM   3278 N  N   . ASN   A 1 412 ? 51.749 27.218  -1.614  1.00 63.89 ? 486 ASN   A N   1 
ATOM   3279 C  CA  . ASN   A 1 412 ? 52.433 26.677  -2.782  1.00 67.26 ? 486 ASN   A CA  1 
ATOM   3280 C  C   . ASN   A 1 412 ? 52.732 27.752  -3.842  1.00 73.14 ? 486 ASN   A C   1 
ATOM   3281 O  O   . ASN   A 1 412 ? 52.095 28.828  -3.797  1.00 74.29 ? 486 ASN   A O   1 
ATOM   3282 C  CB  . ASN   A 1 412 ? 51.605 25.596  -3.460  1.00 63.36 ? 486 ASN   A CB  1 
ATOM   3283 C  CG  . ASN   A 1 412 ? 51.823 24.251  -2.829  1.00 59.21 ? 486 ASN   A CG  1 
ATOM   3284 O  OD1 . ASN   A 1 412 ? 52.202 24.166  -1.658  1.00 62.95 ? 486 ASN   A OD1 1 
ATOM   3285 N  ND2 . ASN   A 1 412 ? 51.617 23.198  -3.600  1.00 61.49 ? 486 ASN   A ND2 1 
HETATM 3286 P  PA  . NDP   B 2 .   ? 36.616 2.841   5.682   1.00 15.12 ? 501 NDP   A PA  1 
HETATM 3287 O  O1A . NDP   B 2 .   ? 37.321 3.787   4.840   1.00 16.02 ? 501 NDP   A O1A 1 
HETATM 3288 O  O2A . NDP   B 2 .   ? 37.289 1.557   6.048   1.00 15.82 ? 501 NDP   A O2A 1 
HETATM 3289 O  O5B . NDP   B 2 .   ? 35.233 2.483   5.143   1.00 15.88 ? 501 NDP   A O5B 1 
HETATM 3290 C  C5B . NDP   B 2 .   ? 34.251 3.445   4.651   1.00 15.83 ? 501 NDP   A C5B 1 
HETATM 3291 C  C4B . NDP   B 2 .   ? 33.046 2.715   4.144   1.00 16.09 ? 501 NDP   A C4B 1 
HETATM 3292 O  O4B . NDP   B 2 .   ? 32.048 3.707   3.776   1.00 16.67 ? 501 NDP   A O4B 1 
HETATM 3293 C  C3B . NDP   B 2 .   ? 33.276 1.868   2.873   1.00 16.57 ? 501 NDP   A C3B 1 
HETATM 3294 O  O3B . NDP   B 2 .   ? 32.428 0.745   2.932   1.00 17.57 ? 501 NDP   A O3B 1 
HETATM 3295 C  C2B . NDP   B 2 .   ? 32.887 2.881   1.806   1.00 17.49 ? 501 NDP   A C2B 1 
HETATM 3296 O  O2B . NDP   B 2 .   ? 32.467 2.200   0.600   1.00 18.93 ? 501 NDP   A O2B 1 
HETATM 3297 C  C1B . NDP   B 2 .   ? 31.643 3.462   2.427   1.00 17.82 ? 501 NDP   A C1B 1 
HETATM 3298 N  N9A . NDP   B 2 .   ? 31.155 4.700   1.849   1.00 17.48 ? 501 NDP   A N9A 1 
HETATM 3299 C  C8A . NDP   B 2 .   ? 31.855 5.844   1.577   1.00 18.36 ? 501 NDP   A C8A 1 
HETATM 3300 N  N7A . NDP   B 2 .   ? 31.084 6.773   1.025   1.00 17.39 ? 501 NDP   A N7A 1 
HETATM 3301 C  C5A . NDP   B 2 .   ? 29.830 6.188   0.961   1.00 16.09 ? 501 NDP   A C5A 1 
HETATM 3302 C  C6A . NDP   B 2 .   ? 28.594 6.598   0.406   1.00 18.70 ? 501 NDP   A C6A 1 
HETATM 3303 N  N6A . NDP   B 2 .   ? 28.395 7.797   -0.124  1.00 22.94 ? 501 NDP   A N6A 1 
HETATM 3304 N  N1A . NDP   B 2 .   ? 27.543 5.773   0.526   1.00 19.05 ? 501 NDP   A N1A 1 
HETATM 3305 C  C2A . NDP   B 2 .   ? 27.713 4.554   1.044   1.00 19.01 ? 501 NDP   A C2A 1 
HETATM 3306 N  N3A . NDP   B 2 .   ? 28.838 4.015   1.522   1.00 17.72 ? 501 NDP   A N3A 1 
HETATM 3307 C  C4A . NDP   B 2 .   ? 29.851 4.885   1.440   1.00 16.74 ? 501 NDP   A C4A 1 
HETATM 3308 O  O3  . NDP   B 2 .   ? 36.285 3.682   7.060   1.00 14.01 ? 501 NDP   A O3  1 
HETATM 3309 P  PN  . NDP   B 2 .   ? 36.171 3.096   8.561   1.00 14.07 ? 501 NDP   A PN  1 
HETATM 3310 O  O1N . NDP   B 2 .   ? 35.370 1.901   8.566   1.00 14.78 ? 501 NDP   A O1N 1 
HETATM 3311 O  O2N . NDP   B 2 .   ? 37.493 3.084   9.139   1.00 14.98 ? 501 NDP   A O2N 1 
HETATM 3312 O  O5D . NDP   B 2 .   ? 35.378 4.316   9.246   1.00 13.75 ? 501 NDP   A O5D 1 
HETATM 3313 C  C5D . NDP   B 2 .   ? 33.994 4.483   9.106   1.00 13.73 ? 501 NDP   A C5D 1 
HETATM 3314 C  C4D . NDP   B 2 .   ? 33.544 5.463   10.153  1.00 13.69 ? 501 NDP   A C4D 1 
HETATM 3315 O  O4D . NDP   B 2 .   ? 33.649 4.775   11.448  1.00 13.35 ? 501 NDP   A O4D 1 
HETATM 3316 C  C3D . NDP   B 2 .   ? 34.363 6.733   10.242  1.00 13.38 ? 501 NDP   A C3D 1 
HETATM 3317 O  O3D . NDP   B 2 .   ? 33.435 7.801   10.433  1.00 14.32 ? 501 NDP   A O3D 1 
HETATM 3318 C  C2D . NDP   B 2 .   ? 35.252 6.481   11.445  1.00 13.16 ? 501 NDP   A C2D 1 
HETATM 3319 O  O2D . NDP   B 2 .   ? 35.580 7.662   12.161  1.00 15.28 ? 501 NDP   A O2D 1 
HETATM 3320 C  C1D . NDP   B 2 .   ? 34.380 5.593   12.314  1.00 13.57 ? 501 NDP   A C1D 1 
HETATM 3321 N  N1N . NDP   B 2 .   ? 35.165 4.703   13.216  1.00 13.79 ? 501 NDP   A N1N 1 
HETATM 3322 C  C2N . NDP   B 2 .   ? 35.956 3.698   12.702  1.00 13.31 ? 501 NDP   A C2N 1 
HETATM 3323 C  C3N . NDP   B 2 .   ? 36.707 2.854   13.505  1.00 13.94 ? 501 NDP   A C3N 1 
HETATM 3324 C  C7N . NDP   B 2 .   ? 37.364 1.688   12.957  1.00 14.59 ? 501 NDP   A C7N 1 
HETATM 3325 O  O7N . NDP   B 2 .   ? 37.709 0.762   13.734  1.00 15.86 ? 501 NDP   A O7N 1 
HETATM 3326 N  N7N . NDP   B 2 .   ? 37.649 1.578   11.678  1.00 14.27 ? 501 NDP   A N7N 1 
HETATM 3327 C  C4N . NDP   B 2 .   ? 36.781 3.118   14.970  1.00 14.46 ? 501 NDP   A C4N 1 
HETATM 3328 C  C5N . NDP   B 2 .   ? 35.805 4.079   15.425  1.00 14.67 ? 501 NDP   A C5N 1 
HETATM 3329 C  C6N . NDP   B 2 .   ? 35.131 4.899   14.595  1.00 14.17 ? 501 NDP   A C6N 1 
HETATM 3330 P  P2B . NDP   B 2 .   ? 33.572 1.761   -0.554  1.00 19.29 ? 501 NDP   A P2B 1 
HETATM 3331 O  O1X . NDP   B 2 .   ? 34.213 0.530   -0.029  1.00 20.40 ? 501 NDP   A O1X 1 
HETATM 3332 O  O2X . NDP   B 2 .   ? 34.498 2.825   -0.762  1.00 19.85 ? 501 NDP   A O2X 1 
HETATM 3333 O  O3X . NDP   B 2 .   ? 32.622 1.450   -1.752  1.00 20.32 ? 501 NDP   A O3X 1 
HETATM 3334 MN MN  . MN    C 3 .   ? 37.253 6.074   18.966  1.00 10.16 ? 502 MN    A MN  1 
HETATM 3335 N  N1  . A1L2H D 4 .   ? 38.530 3.754   17.972  1.00 12.05 ? 503 A1L2H A N1  1 
HETATM 3336 C  C4  . A1L2H D 4 .   ? 43.425 1.576   19.101  1.00 15.41 ? 503 A1L2H A C4  1 
HETATM 3337 C  C5  . A1L2H D 4 .   ? 44.031 2.325   18.097  1.00 15.42 ? 503 A1L2H A C5  1 
HETATM 3338 C  C6  . A1L2H D 4 .   ? 43.512 3.632   17.888  1.00 13.90 ? 503 A1L2H A C6  1 
HETATM 3339 C  C7  . A1L2H D 4 .   ? 44.785 -0.346  18.579  1.00 22.37 ? 503 A1L2H A C7  1 
HETATM 3340 C  C8  . A1L2H D 4 .   ? 46.062 0.025   19.113  1.00 23.51 ? 503 A1L2H A C8  1 
HETATM 3341 C  C10 . A1L2H D 4 .   ? 47.731 -1.052  20.615  1.00 30.53 ? 503 A1L2H A C10 1 
HETATM 3342 C  C13 . A1L2H D 4 .   ? 41.896 5.530   18.355  1.00 11.56 ? 503 A1L2H A C13 1 
HETATM 3343 C  C15 . A1L2H D 4 .   ? 39.072 4.734   17.290  1.00 11.56 ? 503 A1L2H A C15 1 
HETATM 3344 O  O6  . A1L2H D 4 .   ? 38.564 5.893   17.412  1.00 11.60 ? 503 A1L2H A O6  1 
HETATM 3345 C  C16 . A1L2H D 4 .   ? 38.914 2.327   17.964  1.00 12.78 ? 503 A1L2H A C16 1 
HETATM 3346 O  O5  . A1L2H D 4 .   ? 37.468 4.032   18.789  1.00 12.20 ? 503 A1L2H A O5  1 
HETATM 3347 C  C14 . A1L2H D 4 .   ? 40.271 4.550   16.411  1.00 13.88 ? 503 A1L2H A C14 1 
HETATM 3348 S  S1  . A1L2H D 4 .   ? 41.546 5.802   16.630  1.00 13.23 ? 503 A1L2H A S1  1 
HETATM 3349 P  P1  . A1L2H D 4 .   ? 42.989 6.858   19.044  1.00 12.19 ? 503 A1L2H A P1  1 
HETATM 3350 O  O4  . A1L2H D 4 .   ? 42.418 8.165   18.514  1.00 13.12 ? 503 A1L2H A O4  1 
HETATM 3351 O  O3  . A1L2H D 4 .   ? 42.871 6.757   20.567  1.00 12.46 ? 503 A1L2H A O3  1 
HETATM 3352 O  O2  . A1L2H D 4 .   ? 44.403 6.641   18.587  1.00 11.87 ? 503 A1L2H A O2  1 
HETATM 3353 C  C1  . A1L2H D 4 .   ? 42.475 4.132   18.662  1.00 13.15 ? 503 A1L2H A C1  1 
HETATM 3354 C  C3  . A1L2H D 4 .   ? 42.406 2.027   19.836  1.00 14.96 ? 503 A1L2H A C3  1 
HETATM 3355 C  C2  . A1L2H D 4 .   ? 41.913 3.315   19.627  1.00 14.71 ? 503 A1L2H A C2  1 
HETATM 3356 O  O1  . A1L2H D 4 .   ? 43.840 0.266   19.401  1.00 19.18 ? 503 A1L2H A O1  1 
HETATM 3357 C  C9  . A1L2H D 4 .   ? 46.301 -1.080  20.152  1.00 26.29 ? 503 A1L2H A C9  1 
HETATM 3358 C  C11 . A1L2H D 4 .   ? 47.901 -1.904  21.886  1.00 26.96 ? 503 A1L2H A C11 1 
HETATM 3359 C  C12 . A1L2H D 4 .   ? 48.033 -3.394  21.596  1.00 26.55 ? 503 A1L2H A C12 1 
HETATM 3360 C  C1  . GOL   E 5 .   ? 42.522 3.904   24.108  0.60 16.00 ? 504 GOL   A C1  1 
HETATM 3361 O  O1  . GOL   E 5 .   ? 43.262 3.866   25.308  0.60 13.83 ? 504 GOL   A O1  1 
HETATM 3362 C  C2  . GOL   E 5 .   ? 41.173 3.254   24.276  0.60 17.89 ? 504 GOL   A C2  1 
HETATM 3363 O  O2  . GOL   E 5 .   ? 41.374 1.976   24.874  0.60 15.20 ? 504 GOL   A O2  1 
HETATM 3364 C  C3  . GOL   E 5 .   ? 40.413 3.132   22.974  0.60 20.21 ? 504 GOL   A C3  1 
HETATM 3365 O  O3  . GOL   E 5 .   ? 39.119 2.586   23.188  0.60 20.81 ? 504 GOL   A O3  1 
HETATM 3366 O  O   . HOH   F 6 .   ? 39.554 1.718   22.217  0.40 21.24 ? 601 HOH   A O   1 
HETATM 3367 O  O   . HOH   F 6 .   ? 19.616 3.444   39.163  1.00 37.44 ? 602 HOH   A O   1 
HETATM 3368 O  O   . HOH   F 6 .   ? 60.239 16.600  5.402   1.00 40.47 ? 603 HOH   A O   1 
HETATM 3369 O  O   . HOH   F 6 .   ? 44.959 22.287  -4.792  1.00 34.10 ? 604 HOH   A O   1 
HETATM 3370 O  O   . HOH   F 6 .   ? 25.191 30.133  5.804   1.00 32.88 ? 605 HOH   A O   1 
HETATM 3371 O  O   . HOH   F 6 .   ? 31.860 26.012  -1.248  1.00 35.62 ? 606 HOH   A O   1 
HETATM 3372 O  O   . HOH   F 6 .   ? 24.617 8.375   -6.873  1.00 44.59 ? 607 HOH   A O   1 
HETATM 3373 O  O   . HOH   F 6 .   ? 22.831 7.038   39.185  1.00 36.96 ? 608 HOH   A O   1 
HETATM 3374 O  O   . HOH   F 6 .   ? 16.587 20.362  23.273  1.00 39.86 ? 609 HOH   A O   1 
HETATM 3375 O  O   . HOH   F 6 .   ? 28.323 16.525  1.407   1.00 56.03 ? 610 HOH   A O   1 
HETATM 3376 O  O   . HOH   F 6 .   ? 27.227 -2.257  31.168  1.00 27.65 ? 611 HOH   A O   1 
HETATM 3377 O  O   . HOH   F 6 .   ? 38.381 13.186  37.913  1.00 20.48 ? 612 HOH   A O   1 
HETATM 3378 O  O   . HOH   F 6 .   ? 37.306 9.284   11.164  1.00 18.00 ? 613 HOH   A O   1 
HETATM 3379 O  O   . HOH   F 6 .   ? 52.128 3.028   12.299  1.00 40.93 ? 614 HOH   A O   1 
HETATM 3380 O  O   . HOH   F 6 .   ? 11.553 -1.139  -0.765  1.00 40.43 ? 615 HOH   A O   1 
HETATM 3381 O  O   . HOH   F 6 .   ? 21.273 -12.464 26.888  1.00 39.82 ? 616 HOH   A O   1 
HETATM 3382 O  O   . HOH   F 6 .   ? 36.526 0.327   -4.080  1.00 40.90 ? 617 HOH   A O   1 
HETATM 3383 O  O   . HOH   F 6 .   ? 50.594 23.732  14.024  1.00 26.14 ? 618 HOH   A O   1 
HETATM 3384 O  O   . HOH   F 6 .   ? 18.135 13.791  29.224  1.00 29.40 ? 619 HOH   A O   1 
HETATM 3385 O  O   . HOH   F 6 .   ? 52.607 -1.344  29.841  1.00 24.58 ? 620 HOH   A O   1 
HETATM 3386 O  O   . HOH   F 6 .   ? 50.098 -4.336  29.144  1.00 20.86 ? 621 HOH   A O   1 
HETATM 3387 O  O   . HOH   F 6 .   ? 22.771 14.315  38.533  1.00 30.08 ? 622 HOH   A O   1 
HETATM 3388 O  O   . HOH   F 6 .   ? 31.209 22.104  34.148  1.00 32.19 ? 623 HOH   A O   1 
HETATM 3389 O  O   . HOH   F 6 .   ? 33.738 -18.569 25.646  1.00 41.26 ? 624 HOH   A O   1 
HETATM 3390 O  O   . HOH   F 6 .   ? 21.587 19.753  28.728  1.00 31.03 ? 625 HOH   A O   1 
HETATM 3391 O  O   . HOH   F 6 .   ? 40.355 35.677  13.757  1.00 32.72 ? 626 HOH   A O   1 
HETATM 3392 O  O   . HOH   F 6 .   ? 33.944 21.761  35.732  1.00 40.49 ? 627 HOH   A O   1 
HETATM 3393 O  O   . HOH   F 6 .   ? 23.038 -4.884  29.102  1.00 27.84 ? 628 HOH   A O   1 
HETATM 3394 O  O   . HOH   F 6 .   ? 43.586 10.535  18.640  1.00 16.62 ? 629 HOH   A O   1 
HETATM 3395 O  O   . HOH   F 6 .   ? 32.063 -15.552 19.696  1.00 30.75 ? 630 HOH   A O   1 
HETATM 3396 O  O   . HOH   F 6 .   ? 37.327 12.792  4.408   1.00 27.00 ? 631 HOH   A O   1 
HETATM 3397 O  O   . HOH   F 6 .   ? 35.263 -3.375  -6.847  1.00 35.03 ? 632 HOH   A O   1 
HETATM 3398 O  O   . HOH   F 6 .   ? 23.893 -0.645  32.746  1.00 30.25 ? 633 HOH   A O   1 
HETATM 3399 O  O   . HOH   F 6 .   ? 43.255 -6.959  20.350  1.00 19.59 ? 634 HOH   A O   1 
HETATM 3400 O  O   . HOH   F 6 .   ? 60.607 11.816  11.438  1.00 28.49 ? 635 HOH   A O   1 
HETATM 3401 O  O   . HOH   F 6 .   ? 42.642 28.767  15.822  1.00 26.92 ? 636 HOH   A O   1 
HETATM 3402 O  O   . HOH   F 6 .   ? 32.878 34.358  15.500  1.00 20.08 ? 637 HOH   A O   1 
HETATM 3403 O  O   . HOH   F 6 .   ? 24.862 12.040  -0.618  1.00 29.85 ? 638 HOH   A O   1 
HETATM 3404 O  O   . HOH   F 6 .   ? 61.699 9.414   19.681  1.00 39.31 ? 639 HOH   A O   1 
HETATM 3405 O  O   . HOH   F 6 .   ? 29.677 18.502  32.501  1.00 16.75 ? 640 HOH   A O   1 
HETATM 3406 O  O   . HOH   F 6 .   ? 31.165 -14.598 -1.293  1.00 35.54 ? 641 HOH   A O   1 
HETATM 3407 O  O   . HOH   F 6 .   ? 13.871 0.174   15.179  1.00 31.52 ? 642 HOH   A O   1 
HETATM 3408 O  O   . HOH   F 6 .   ? 28.567 6.932   46.733  1.00 26.57 ? 643 HOH   A O   1 
HETATM 3409 O  O   . HOH   F 6 .   ? 54.117 8.780   2.870   1.00 26.29 ? 644 HOH   A O   1 
HETATM 3410 O  O   . HOH   F 6 .   ? 28.201 0.131   21.704  1.00 13.64 ? 645 HOH   A O   1 
HETATM 3411 O  O   . HOH   F 6 .   ? 18.365 10.108  37.670  1.00 40.42 ? 646 HOH   A O   1 
HETATM 3412 O  O   . HOH   F 6 .   ? 52.110 27.275  8.798   1.00 46.25 ? 647 HOH   A O   1 
HETATM 3413 O  O   . HOH   F 6 .   ? 55.785 15.981  8.121   1.00 20.91 ? 648 HOH   A O   1 
HETATM 3414 O  O   . HOH   F 6 .   ? 34.478 9.940   2.048   1.00 32.13 ? 649 HOH   A O   1 
HETATM 3415 O  O   . HOH   F 6 .   ? 15.621 36.860  12.243  1.00 35.27 ? 650 HOH   A O   1 
HETATM 3416 O  O   . HOH   F 6 .   ? 37.133 32.989  14.677  1.00 16.53 ? 651 HOH   A O   1 
HETATM 3417 O  O   . HOH   F 6 .   ? 34.488 5.510   -0.910  1.00 24.54 ? 652 HOH   A O   1 
HETATM 3418 O  O   . HOH   F 6 .   ? 46.628 1.333   8.148   1.00 28.03 ? 653 HOH   A O   1 
HETATM 3419 O  O   . HOH   F 6 .   ? 36.827 10.710  41.067  1.00 12.90 ? 654 HOH   A O   1 
HETATM 3420 O  O   . HOH   F 6 .   ? 27.180 -17.523 11.014  1.00 32.82 ? 655 HOH   A O   1 
HETATM 3421 O  O   . HOH   F 6 .   ? 17.854 20.878  3.869   1.00 37.03 ? 656 HOH   A O   1 
HETATM 3422 O  O   . HOH   F 6 .   ? 52.377 20.041  -2.181  1.00 30.16 ? 657 HOH   A O   1 
HETATM 3423 O  O   . HOH   F 6 .   ? 36.007 9.072   8.423   1.00 26.89 ? 658 HOH   A O   1 
HETATM 3424 O  O   . HOH   F 6 .   ? 30.226 33.275  8.772   1.00 18.63 ? 659 HOH   A O   1 
HETATM 3425 O  O   . HOH   F 6 .   ? 44.263 12.447  34.964  1.00 15.94 ? 660 HOH   A O   1 
HETATM 3426 O  O   . HOH   F 6 .   ? 37.559 -4.932  9.666   1.00 43.28 ? 661 HOH   A O   1 
HETATM 3427 O  O   . HOH   F 6 .   ? 28.973 22.994  14.362  1.00 20.98 ? 662 HOH   A O   1 
HETATM 3428 O  O   . HOH   F 6 .   ? 26.762 3.070   36.271  1.00 19.18 ? 663 HOH   A O   1 
HETATM 3429 O  O   . HOH   F 6 .   ? 24.364 1.068   28.593  1.00 24.62 ? 664 HOH   A O   1 
HETATM 3430 O  O   . HOH   F 6 .   ? 30.410 22.378  20.861  1.00 15.59 ? 665 HOH   A O   1 
HETATM 3431 O  O   . HOH   F 6 .   ? 46.898 20.648  21.439  1.00 35.83 ? 666 HOH   A O   1 
HETATM 3432 O  O   . HOH   F 6 .   ? 52.768 12.352  4.137   1.00 23.72 ? 667 HOH   A O   1 
HETATM 3433 O  O   . HOH   F 6 .   ? 11.564 9.678   30.736  1.00 50.97 ? 668 HOH   A O   1 
HETATM 3434 O  O   . HOH   F 6 .   ? 47.517 -4.029  24.986  1.00 16.43 ? 669 HOH   A O   1 
HETATM 3435 O  O   . HOH   F 6 .   ? 30.163 8.227   -5.308  1.00 36.66 ? 670 HOH   A O   1 
HETATM 3436 O  O   . HOH   F 6 .   ? 46.015 30.413  12.906  1.00 24.65 ? 671 HOH   A O   1 
HETATM 3437 O  O   . HOH   F 6 .   ? 37.411 15.698  10.141  1.00 14.63 ? 672 HOH   A O   1 
HETATM 3438 O  O   . HOH   F 6 .   ? 15.749 -13.474 -3.071  1.00 46.51 ? 673 HOH   A O   1 
HETATM 3439 O  O   . HOH   F 6 .   ? 50.855 5.422   21.287  1.00 22.67 ? 674 HOH   A O   1 
HETATM 3440 O  O   . HOH   F 6 .   ? 25.563 8.713   4.500   1.00 19.13 ? 675 HOH   A O   1 
HETATM 3441 O  O   . HOH   F 6 .   ? 28.570 36.536  11.021  1.00 17.75 ? 676 HOH   A O   1 
HETATM 3442 O  O   . HOH   F 6 .   ? 20.381 6.624   22.695  1.00 16.30 ? 677 HOH   A O   1 
HETATM 3443 O  O   . HOH   F 6 .   ? 42.738 14.736  36.402  1.00 27.92 ? 678 HOH   A O   1 
HETATM 3444 O  O   . HOH   F 6 .   ? 9.550  8.244   16.727  1.00 34.02 ? 679 HOH   A O   1 
HETATM 3445 O  O   . HOH   F 6 .   ? 31.999 9.309   0.617   1.00 37.59 ? 680 HOH   A O   1 
HETATM 3446 O  O   . HOH   F 6 .   ? 38.532 10.636  13.099  1.00 18.15 ? 681 HOH   A O   1 
HETATM 3447 O  O   . HOH   F 6 .   ? 52.204 13.397  24.188  1.00 20.07 ? 682 HOH   A O   1 
HETATM 3448 O  O   . HOH   F 6 .   ? 24.170 6.856   37.074  1.00 23.05 ? 683 HOH   A O   1 
HETATM 3449 O  O   . HOH   F 6 .   ? 24.923 -18.978 12.501  1.00 48.86 ? 684 HOH   A O   1 
HETATM 3450 O  O   . HOH   F 6 .   ? 46.637 4.506   15.146  1.00 23.84 ? 685 HOH   A O   1 
HETATM 3451 O  O   . HOH   F 6 .   ? 33.660 39.315  14.517  1.00 30.59 ? 686 HOH   A O   1 
HETATM 3452 O  O   . HOH   F 6 .   ? 34.523 1.029   -8.412  1.00 36.92 ? 687 HOH   A O   1 
HETATM 3453 O  O   . HOH   F 6 .   ? 36.001 -4.785  1.410   1.00 33.03 ? 688 HOH   A O   1 
HETATM 3454 O  O   . HOH   F 6 .   ? 51.316 10.057  34.085  1.00 26.13 ? 689 HOH   A O   1 
HETATM 3455 O  O   . HOH   F 6 .   ? 41.822 11.548  4.078   1.00 18.00 ? 690 HOH   A O   1 
HETATM 3456 O  O   . HOH   F 6 .   ? 36.221 15.895  38.426  1.00 30.63 ? 691 HOH   A O   1 
HETATM 3457 O  O   . HOH   F 6 .   ? 23.862 16.514  24.770  1.00 29.36 ? 692 HOH   A O   1 
HETATM 3458 O  O   . HOH   F 6 .   ? 43.714 -16.191 29.913  1.00 23.85 ? 693 HOH   A O   1 
HETATM 3459 O  O   . HOH   F 6 .   ? 42.635 -15.064 27.579  1.00 16.57 ? 694 HOH   A O   1 
HETATM 3460 O  O   . HOH   F 6 .   ? 49.020 29.729  2.810   1.00 44.16 ? 695 HOH   A O   1 
HETATM 3461 O  O   . HOH   F 6 .   ? 39.321 -0.135  5.319   1.00 25.60 ? 696 HOH   A O   1 
HETATM 3462 O  O   . HOH   F 6 .   ? 52.989 22.981  18.360  1.00 25.17 ? 697 HOH   A O   1 
HETATM 3463 O  O   . HOH   F 6 .   ? 13.074 1.292   -6.110  1.00 45.11 ? 698 HOH   A O   1 
HETATM 3464 O  O   . HOH   F 6 .   ? 43.246 32.777  9.421   1.00 19.45 ? 699 HOH   A O   1 
HETATM 3465 O  O   . HOH   F 6 .   ? 45.013 32.630  7.165   1.00 26.82 ? 700 HOH   A O   1 
HETATM 3466 O  O   . HOH   F 6 .   ? 13.898 3.593   34.144  1.00 43.09 ? 701 HOH   A O   1 
HETATM 3467 O  O   . HOH   F 6 .   ? 28.290 20.811  15.875  1.00 28.12 ? 702 HOH   A O   1 
HETATM 3468 O  O   . HOH   F 6 .   ? 25.695 15.952  36.557  1.00 25.53 ? 703 HOH   A O   1 
HETATM 3469 O  O   . HOH   F 6 .   ? 23.808 24.586  1.237   1.00 25.14 ? 704 HOH   A O   1 
HETATM 3470 O  O   . HOH   F 6 .   ? 36.533 1.140   1.315   1.00 29.14 ? 705 HOH   A O   1 
HETATM 3471 O  O   . HOH   F 6 .   ? 9.843  4.817   8.621   1.00 32.47 ? 706 HOH   A O   1 
HETATM 3472 O  O   . HOH   F 6 .   ? 44.304 15.989  -0.879  1.00 29.48 ? 707 HOH   A O   1 
HETATM 3473 O  O   . HOH   F 6 .   ? 32.071 19.445  8.646   1.00 20.15 ? 708 HOH   A O   1 
HETATM 3474 O  O   . HOH   F 6 .   ? 36.530 -1.727  12.652  1.00 22.62 ? 709 HOH   A O   1 
HETATM 3475 O  O   . HOH   F 6 .   ? 39.155 -10.498 20.998  1.00 23.92 ? 710 HOH   A O   1 
HETATM 3476 O  O   . HOH   F 6 .   ? 55.186 13.148  20.054  1.00 20.94 ? 711 HOH   A O   1 
HETATM 3477 O  O   . HOH   F 6 .   ? 35.334 6.136   1.569   1.00 24.93 ? 712 HOH   A O   1 
HETATM 3478 O  O   . HOH   F 6 .   ? 25.831 -19.266 -10.898 1.00 37.85 ? 713 HOH   A O   1 
HETATM 3479 O  O   . HOH   F 6 .   ? 26.966 -19.154 -3.297  1.00 42.85 ? 714 HOH   A O   1 
HETATM 3480 O  O   . HOH   F 6 .   ? 13.471 15.046  23.707  1.00 34.14 ? 715 HOH   A O   1 
HETATM 3481 O  O   . HOH   F 6 .   ? 20.108 28.097  5.376   1.00 29.89 ? 716 HOH   A O   1 
HETATM 3482 O  O   . HOH   F 6 .   ? 36.729 3.936   2.140   1.00 25.11 ? 717 HOH   A O   1 
HETATM 3483 O  O   . HOH   F 6 .   ? 23.145 8.540   0.770   1.00 33.06 ? 718 HOH   A O   1 
HETATM 3484 O  O   . HOH   F 6 .   ? 37.291 -3.753  22.451  1.00 32.73 ? 719 HOH   A O   1 
HETATM 3485 O  O   . HOH   F 6 .   ? 38.392 6.196   5.692   1.00 17.77 ? 720 HOH   A O   1 
HETATM 3486 O  O   . HOH   F 6 .   ? 38.470 21.616  -1.681  1.00 35.56 ? 721 HOH   A O   1 
HETATM 3487 O  O   . HOH   F 6 .   ? 20.596 8.909   41.522  1.00 29.45 ? 722 HOH   A O   1 
HETATM 3488 O  O   . HOH   F 6 .   ? 44.770 1.466   10.135  1.00 24.77 ? 723 HOH   A O   1 
HETATM 3489 O  O   . HOH   F 6 .   ? 38.068 8.204   3.698   1.00 22.94 ? 724 HOH   A O   1 
HETATM 3490 O  O   . HOH   F 6 .   ? 54.178 14.636  4.155   1.00 28.19 ? 725 HOH   A O   1 
HETATM 3491 O  O   . HOH   F 6 .   ? 20.299 -1.869  20.280  1.00 19.61 ? 726 HOH   A O   1 
HETATM 3492 O  O   . HOH   F 6 .   ? 24.946 -15.726 21.643  1.00 33.06 ? 727 HOH   A O   1 
HETATM 3493 O  O   . HOH   F 6 .   ? 17.164 -8.916  -8.325  1.00 37.78 ? 728 HOH   A O   1 
HETATM 3494 O  O   . HOH   F 6 .   ? 13.706 6.629   -2.120  1.00 36.78 ? 729 HOH   A O   1 
HETATM 3495 O  O   . HOH   F 6 .   ? 39.935 13.354  4.949   1.00 18.78 ? 730 HOH   A O   1 
HETATM 3496 O  O   . HOH   F 6 .   ? 31.266 -11.566 3.016   1.00 46.39 ? 731 HOH   A O   1 
HETATM 3497 O  O   . HOH   F 6 .   ? 27.906 17.424  38.053  1.00 27.55 ? 732 HOH   A O   1 
HETATM 3498 O  O   . HOH   F 6 .   ? 26.341 22.299  22.535  1.00 29.29 ? 733 HOH   A O   1 
HETATM 3499 O  O   . HOH   F 6 .   ? 35.787 -5.382  21.353  1.00 25.23 ? 734 HOH   A O   1 
HETATM 3500 O  O   . HOH   F 6 .   ? 48.978 2.617   21.752  1.00 16.45 ? 735 HOH   A O   1 
HETATM 3501 O  O   . HOH   F 6 .   ? 27.462 20.475  28.051  1.00 26.20 ? 736 HOH   A O   1 
HETATM 3502 O  O   . HOH   F 6 .   ? 19.581 8.816   20.961  1.00 15.44 ? 737 HOH   A O   1 
HETATM 3503 O  O   . HOH   F 6 .   ? 34.063 22.346  -0.897  1.00 37.15 ? 738 HOH   A O   1 
HETATM 3504 O  O   . HOH   F 6 .   ? 10.195 2.100   8.283   1.00 34.88 ? 739 HOH   A O   1 
HETATM 3505 O  O   . HOH   F 6 .   ? 48.172 17.567  16.121  1.00 15.06 ? 740 HOH   A O   1 
HETATM 3506 O  O   . HOH   F 6 .   ? 41.016 27.712  17.560  1.00 25.46 ? 741 HOH   A O   1 
HETATM 3507 O  O   . HOH   F 6 .   ? 36.140 18.260  35.676  1.00 28.39 ? 742 HOH   A O   1 
HETATM 3508 O  O   . HOH   F 6 .   ? 46.449 27.880  16.755  1.00 35.36 ? 743 HOH   A O   1 
HETATM 3509 O  O   . HOH   F 6 .   ? 10.612 2.640   14.531  1.00 47.04 ? 744 HOH   A O   1 
HETATM 3510 O  O   . HOH   F 6 .   ? 15.314 12.472  25.991  1.00 28.51 ? 745 HOH   A O   1 
HETATM 3511 O  O   . HOH   F 6 .   ? 23.876 6.177   34.435  1.00 19.03 ? 746 HOH   A O   1 
HETATM 3512 O  O   . HOH   F 6 .   ? 12.017 15.340  10.472  1.00 34.71 ? 747 HOH   A O   1 
HETATM 3513 O  O   . HOH   F 6 .   ? 46.695 -15.288 33.890  1.00 24.39 ? 748 HOH   A O   1 
HETATM 3514 O  O   . HOH   F 6 .   ? 29.760 6.652   18.393  1.00 14.52 ? 749 HOH   A O   1 
HETATM 3515 O  O   . HOH   F 6 .   ? 46.830 17.415  27.695  1.00 23.86 ? 750 HOH   A O   1 
HETATM 3516 O  O   . HOH   F 6 .   ? 18.537 -7.082  22.480  1.00 30.85 ? 751 HOH   A O   1 
HETATM 3517 O  O   . HOH   F 6 .   ? 45.960 8.957   19.005  1.00 13.62 ? 752 HOH   A O   1 
HETATM 3518 O  O   . HOH   F 6 .   ? 44.231 14.933  11.274  1.00 14.90 ? 753 HOH   A O   1 
HETATM 3519 O  O   . HOH   F 6 .   ? 13.151 19.563  17.547  1.00 31.22 ? 754 HOH   A O   1 
HETATM 3520 O  O   . HOH   F 6 .   ? 17.018 -5.494  20.520  1.00 36.86 ? 755 HOH   A O   1 
HETATM 3521 O  O   . HOH   F 6 .   ? 56.031 7.127   18.682  1.00 23.01 ? 756 HOH   A O   1 
HETATM 3522 O  O   . HOH   F 6 .   ? 30.266 15.985  41.801  1.00 26.27 ? 757 HOH   A O   1 
HETATM 3523 O  O   . HOH   F 6 .   ? 47.811 6.036   12.947  1.00 21.56 ? 758 HOH   A O   1 
HETATM 3524 O  O   . HOH   F 6 .   ? 34.575 -0.118  24.068  1.00 17.63 ? 759 HOH   A O   1 
HETATM 3525 O  O   . HOH   F 6 .   ? 50.437 9.665   17.139  1.00 13.91 ? 760 HOH   A O   1 
HETATM 3526 O  O   . HOH   F 6 .   ? 31.160 27.129  25.846  1.00 31.43 ? 761 HOH   A O   1 
HETATM 3527 O  O   . HOH   F 6 .   ? 42.821 20.250  -1.037  1.00 27.38 ? 762 HOH   A O   1 
HETATM 3528 O  O   . HOH   F 6 .   ? 17.061 24.751  14.463  1.00 39.03 ? 763 HOH   A O   1 
HETATM 3529 O  O   . HOH   F 6 .   ? 33.875 28.843  -0.874  1.00 24.27 ? 764 HOH   A O   1 
HETATM 3530 O  O   . HOH   F 6 .   ? 37.347 28.629  22.452  1.00 18.95 ? 765 HOH   A O   1 
HETATM 3531 O  O   . HOH   F 6 .   ? 65.029 14.073  17.599  1.00 33.49 ? 766 HOH   A O   1 
HETATM 3532 O  O   . HOH   F 6 .   ? 41.243 4.779   22.625  0.40 16.40 ? 767 HOH   A O   1 
HETATM 3533 O  O   . HOH   F 6 .   ? 43.538 -13.477 18.451  1.00 28.05 ? 768 HOH   A O   1 
HETATM 3534 O  O   . HOH   F 6 .   ? 44.567 2.691   6.721   1.00 28.69 ? 769 HOH   A O   1 
HETATM 3535 O  O   . HOH   F 6 .   ? 26.852 -0.371  33.619  1.00 38.15 ? 770 HOH   A O   1 
HETATM 3536 O  O   . HOH   F 6 .   ? 11.813 32.581  16.322  1.00 29.28 ? 771 HOH   A O   1 
HETATM 3537 O  O   . HOH   F 6 .   ? 37.932 -2.969  4.498   1.00 35.86 ? 772 HOH   A O   1 
HETATM 3538 O  O   . HOH   F 6 .   ? 33.906 -8.878  -0.067  1.00 27.80 ? 773 HOH   A O   1 
HETATM 3539 O  O   . HOH   F 6 .   ? 47.574 3.540   17.696  1.00 24.00 ? 774 HOH   A O   1 
HETATM 3540 O  O   . HOH   F 6 .   ? 33.216 0.568   7.253   1.00 16.93 ? 775 HOH   A O   1 
HETATM 3541 O  O   . HOH   F 6 .   ? 13.862 7.596   4.075   1.00 34.49 ? 776 HOH   A O   1 
HETATM 3542 O  O   . HOH   F 6 .   ? 17.300 5.037   26.056  1.00 21.79 ? 777 HOH   A O   1 
HETATM 3543 O  O   . HOH   F 6 .   ? 58.016 7.275   4.852   1.00 36.25 ? 778 HOH   A O   1 
HETATM 3544 O  O   . HOH   F 6 .   ? 8.381  -0.998  4.468   1.00 42.18 ? 779 HOH   A O   1 
HETATM 3545 O  O   . HOH   F 6 .   ? 28.918 32.386  18.725  1.00 36.42 ? 780 HOH   A O   1 
HETATM 3546 O  O   . HOH   F 6 .   ? 17.071 17.335  24.095  1.00 22.64 ? 781 HOH   A O   1 
HETATM 3547 O  O   . HOH   F 6 .   ? 29.850 25.027  23.281  1.00 26.22 ? 782 HOH   A O   1 
HETATM 3548 O  O   . HOH   F 6 .   ? 26.127 -8.271  23.710  1.00 19.22 ? 783 HOH   A O   1 
HETATM 3549 O  O   . HOH   F 6 .   ? 21.722 31.736  16.668  1.00 35.34 ? 784 HOH   A O   1 
HETATM 3550 O  O   . HOH   F 6 .   ? 55.769 19.542  10.075  1.00 21.71 ? 785 HOH   A O   1 
HETATM 3551 O  O   . HOH   F 6 .   ? 42.190 16.949  28.127  1.00 17.37 ? 786 HOH   A O   1 
HETATM 3552 O  O   . HOH   F 6 .   ? 29.376 17.829  35.263  1.00 26.70 ? 787 HOH   A O   1 
HETATM 3553 O  O   . HOH   F 6 .   ? 38.038 22.562  28.416  1.00 26.18 ? 788 HOH   A O   1 
HETATM 3554 O  O   . HOH   F 6 .   ? 10.636 2.547   11.928  1.00 38.78 ? 789 HOH   A O   1 
HETATM 3555 O  O   . HOH   F 6 .   ? 45.393 26.522  19.427  1.00 28.38 ? 790 HOH   A O   1 
HETATM 3556 O  O   . HOH   F 6 .   ? 15.638 18.218  8.050   1.00 44.79 ? 791 HOH   A O   1 
HETATM 3557 O  O   . HOH   F 6 .   ? 48.829 2.503   11.676  1.00 34.48 ? 792 HOH   A O   1 
HETATM 3558 O  O   . HOH   F 6 .   ? 39.314 26.353  -2.832  1.00 31.70 ? 793 HOH   A O   1 
HETATM 3559 O  O   . HOH   F 6 .   ? 17.129 19.409  13.161  1.00 27.26 ? 794 HOH   A O   1 
HETATM 3560 O  O   . HOH   F 6 .   ? 21.311 -12.801 7.854   1.00 37.23 ? 795 HOH   A O   1 
HETATM 3561 O  O   . HOH   F 6 .   ? 40.424 25.478  24.873  1.00 24.87 ? 796 HOH   A O   1 
HETATM 3562 O  O   . HOH   F 6 .   ? 20.516 31.984  9.821   1.00 34.48 ? 797 HOH   A O   1 
HETATM 3563 O  O   . HOH   F 6 .   ? 28.106 0.043   -14.366 1.00 34.52 ? 798 HOH   A O   1 
HETATM 3564 O  O   . HOH   F 6 .   ? 13.563 20.571  19.751  1.00 34.52 ? 799 HOH   A O   1 
HETATM 3565 O  O   . HOH   F 6 .   ? 49.949 5.395   28.213  1.00 13.40 ? 800 HOH   A O   1 
HETATM 3566 O  O   . HOH   F 6 .   ? 51.013 12.793  32.489  1.00 18.58 ? 801 HOH   A O   1 
HETATM 3567 O  O   . HOH   F 6 .   ? 12.090 22.483  11.720  1.00 40.13 ? 802 HOH   A O   1 
HETATM 3568 O  O   . HOH   F 6 .   ? 22.775 9.797   -5.223  1.00 36.53 ? 803 HOH   A O   1 
HETATM 3569 O  O   . HOH   F 6 .   ? 16.002 16.497  26.685  1.00 32.00 ? 804 HOH   A O   1 
HETATM 3570 O  O   . HOH   F 6 .   ? 32.852 14.228  3.660   1.00 30.92 ? 805 HOH   A O   1 
HETATM 3571 O  O   . HOH   F 6 .   ? 38.980 33.764  16.475  1.00 35.50 ? 806 HOH   A O   1 
HETATM 3572 O  O   . HOH   F 6 .   ? 26.873 23.950  18.056  1.00 33.69 ? 807 HOH   A O   1 
HETATM 3573 O  O   . HOH   F 6 .   ? 38.968 20.044  29.745  1.00 24.04 ? 808 HOH   A O   1 
HETATM 3574 O  O   . HOH   F 6 .   ? 35.209 -11.906 13.781  1.00 46.73 ? 809 HOH   A O   1 
HETATM 3575 O  O   . HOH   F 6 .   ? 49.427 18.666  13.710  1.00 19.56 ? 810 HOH   A O   1 
HETATM 3576 O  O   . HOH   F 6 .   ? 46.805 24.161  18.993  1.00 22.71 ? 811 HOH   A O   1 
HETATM 3577 O  O   . HOH   F 6 .   ? 9.013  5.276   10.902  1.00 44.58 ? 812 HOH   A O   1 
HETATM 3578 O  O   . HOH   F 6 .   ? 38.764 -4.829  15.972  1.00 41.74 ? 813 HOH   A O   1 
HETATM 3579 O  O   . HOH   F 6 .   ? 52.934 22.188  1.025   1.00 33.44 ? 814 HOH   A O   1 
HETATM 3580 O  O   . HOH   F 6 .   ? 52.566 15.481  28.243  1.00 42.62 ? 815 HOH   A O   1 
HETATM 3581 O  O   . HOH   F 6 .   ? 26.722 26.891  20.404  1.00 29.59 ? 816 HOH   A O   1 
HETATM 3582 O  O   . HOH   F 6 .   ? 62.939 17.911  19.067  1.00 30.50 ? 817 HOH   A O   1 
HETATM 3583 O  O   . HOH   F 6 .   ? 13.419 2.203   17.048  1.00 34.50 ? 818 HOH   A O   1 
HETATM 3584 O  O   . HOH   F 6 .   ? 23.099 -15.091 25.163  1.00 23.08 ? 819 HOH   A O   1 
HETATM 3585 O  O   . HOH   F 6 .   ? 60.394 17.066  21.599  1.00 31.29 ? 820 HOH   A O   1 
HETATM 3586 O  O   . HOH   F 6 .   ? 33.195 23.737  29.763  1.00 21.41 ? 821 HOH   A O   1 
HETATM 3587 O  O   . HOH   F 6 .   ? 51.327 6.812   2.355   1.00 37.92 ? 822 HOH   A O   1 
HETATM 3588 O  O   . HOH   F 6 .   ? 33.356 18.219  40.221  1.00 41.37 ? 823 HOH   A O   1 
HETATM 3589 O  O   . HOH   F 6 .   ? 24.058 35.067  10.447  1.00 17.85 ? 824 HOH   A O   1 
HETATM 3590 O  O   . HOH   F 6 .   ? 36.960 -1.306  22.582  1.00 27.75 ? 825 HOH   A O   1 
HETATM 3591 O  O   . HOH   F 6 .   ? 26.159 21.655  16.462  1.00 23.42 ? 826 HOH   A O   1 
HETATM 3592 O  O   . HOH   F 6 .   ? 40.112 3.676   3.863   1.00 21.94 ? 827 HOH   A O   1 
HETATM 3593 O  O   . HOH   F 6 .   ? 48.676 23.458  21.021  1.00 28.98 ? 828 HOH   A O   1 
HETATM 3594 O  O   . HOH   F 6 .   ? 25.240 -19.058 -7.846  1.00 34.92 ? 829 HOH   A O   1 
HETATM 3595 O  O   . HOH   F 6 .   ? 50.949 -0.487  24.470  1.00 28.03 ? 830 HOH   A O   1 
HETATM 3596 O  O   . HOH   F 6 .   ? 50.533 20.045  26.911  1.00 27.17 ? 831 HOH   A O   1 
HETATM 3597 O  O   . HOH   F 6 .   ? 26.558 8.709   -8.717  1.00 41.99 ? 832 HOH   A O   1 
HETATM 3598 O  O   . HOH   F 6 .   ? 15.521 3.852   -4.625  1.00 36.84 ? 833 HOH   A O   1 
HETATM 3599 O  O   . HOH   F 6 .   ? 52.872 -5.793  37.015  1.00 33.29 ? 834 HOH   A O   1 
HETATM 3600 O  O   . HOH   F 6 .   ? 16.062 -4.893  -7.954  1.00 36.15 ? 835 HOH   A O   1 
HETATM 3601 O  O   . HOH   F 6 .   ? 53.328 6.469   24.913  1.00 35.27 ? 836 HOH   A O   1 
HETATM 3602 O  O   . HOH   F 6 .   ? 31.382 -17.825 17.880  1.00 41.68 ? 837 HOH   A O   1 
HETATM 3603 O  O   . HOH   F 6 .   ? 24.686 17.669  34.655  1.00 30.69 ? 838 HOH   A O   1 
HETATM 3604 O  O   . HOH   F 6 .   ? 49.864 28.214  5.655   1.00 40.55 ? 839 HOH   A O   1 
HETATM 3605 O  O   . HOH   F 6 .   ? 24.487 -2.786  30.535  1.00 35.16 ? 840 HOH   A O   1 
HETATM 3606 O  O   . HOH   F 6 .   ? 25.882 -4.980  31.883  1.00 20.01 ? 841 HOH   A O   1 
HETATM 3607 O  O   . HOH   F 6 .   ? 42.996 10.156  -1.020  1.00 29.93 ? 842 HOH   A O   1 
HETATM 3608 O  O   . HOH   F 6 .   ? 59.151 20.809  15.108  1.00 36.63 ? 843 HOH   A O   1 
HETATM 3609 O  O   . HOH   F 6 .   ? 31.218 23.280  27.845  1.00 19.04 ? 844 HOH   A O   1 
HETATM 3610 O  O   . HOH   F 6 .   ? 38.074 17.085  33.912  1.00 32.11 ? 845 HOH   A O   1 
HETATM 3611 O  O   . HOH   F 6 .   ? 8.264  10.138  12.635  1.00 44.19 ? 846 HOH   A O   1 
HETATM 3612 O  O   . HOH   F 6 .   ? 52.513 24.872  12.142  1.00 30.94 ? 847 HOH   A O   1 
HETATM 3613 O  O   . HOH   F 6 .   ? 12.774 10.657  22.703  1.00 30.49 ? 848 HOH   A O   1 
HETATM 3614 O  O   . HOH   F 6 .   ? 17.596 3.354   -6.414  1.00 33.66 ? 849 HOH   A O   1 
HETATM 3615 O  O   . HOH   F 6 .   ? 30.106 27.136  0.360   1.00 29.36 ? 850 HOH   A O   1 
HETATM 3616 O  O   . HOH   F 6 .   ? 41.479 29.090  24.106  1.00 39.95 ? 851 HOH   A O   1 
HETATM 3617 O  O   . HOH   F 6 .   ? 35.483 -2.990  23.992  1.00 27.01 ? 852 HOH   A O   1 
HETATM 3618 O  O   . HOH   F 6 .   ? 25.533 8.052   1.810   1.00 25.12 ? 853 HOH   A O   1 
HETATM 3619 O  O   . HOH   F 6 .   ? 32.731 -9.163  4.381   1.00 37.91 ? 854 HOH   A O   1 
HETATM 3620 O  O   . HOH   F 6 .   ? 24.028 33.414  8.072   1.00 22.24 ? 855 HOH   A O   1 
HETATM 3621 O  O   . HOH   F 6 .   ? 42.591 17.645  0.418   1.00 25.03 ? 856 HOH   A O   1 
HETATM 3622 O  O   . HOH   F 6 .   ? 52.878 20.810  25.419  1.00 38.51 ? 857 HOH   A O   1 
HETATM 3623 O  O   . HOH   F 6 .   ? 25.489 29.707  18.570  1.00 31.06 ? 858 HOH   A O   1 
HETATM 3624 O  O   . HOH   F 6 .   ? 54.450 13.519  22.743  1.00 26.52 ? 859 HOH   A O   1 
HETATM 3625 O  O   . HOH   F 6 .   ? 35.166 26.074  28.709  1.00 43.56 ? 860 HOH   A O   1 
HETATM 3626 O  O   . HOH   F 6 .   ? 38.576 -13.114 20.303  1.00 21.35 ? 861 HOH   A O   1 
HETATM 3627 O  O   . HOH   F 6 .   ? 37.463 -12.709 17.787  1.00 35.78 ? 862 HOH   A O   1 
HETATM 3628 O  O   . HOH   F 6 .   ? 38.526 30.399  16.134  1.00 29.34 ? 863 HOH   A O   1 
HETATM 3629 O  O   . HOH   F 6 .   ? 38.023 6.436   8.416   1.00 21.26 ? 864 HOH   A O   1 
HETATM 3630 O  O   . HOH   F 6 .   ? 17.290 -10.189 4.349   1.00 41.96 ? 865 HOH   A O   1 
HETATM 3631 O  O   . HOH   F 6 .   ? 39.303 -0.497  21.295  1.00 35.86 ? 866 HOH   A O   1 
HETATM 3632 O  O   . HOH   F 6 .   ? 41.149 -14.855 31.617  1.00 26.47 ? 867 HOH   A O   1 
HETATM 3633 O  O   . HOH   F 6 .   ? 7.933  10.322  17.190  1.00 36.37 ? 868 HOH   A O   1 
HETATM 3634 O  O   . HOH   F 6 .   ? 19.870 8.742   -6.045  1.00 40.17 ? 869 HOH   A O   1 
HETATM 3635 O  O   . HOH   F 6 .   ? 30.475 9.863   -1.215  1.00 34.03 ? 870 HOH   A O   1 
HETATM 3636 O  O   . HOH   F 6 .   ? 36.426 14.336  2.462   1.00 32.85 ? 871 HOH   A O   1 
HETATM 3637 O  O   . HOH   F 6 .   ? 24.337 21.791  14.326  1.00 29.05 ? 872 HOH   A O   1 
HETATM 3638 O  O   . HOH   F 6 .   ? 39.617 29.770  18.302  1.00 47.42 ? 873 HOH   A O   1 
HETATM 3639 O  O   . HOH   F 6 .   ? 48.310 28.857  11.784  1.00 43.28 ? 874 HOH   A O   1 
HETATM 3640 O  O   . HOH   F 6 .   ? 39.509 18.269  32.141  1.00 46.86 ? 875 HOH   A O   1 
HETATM 3641 O  O   . HOH   F 6 .   ? 23.417 21.102  21.527  1.00 28.59 ? 876 HOH   A O   1 
HETATM 3642 O  O   . HOH   F 6 .   ? 15.057 3.480   40.815  1.00 45.78 ? 877 HOH   A O   1 
HETATM 3643 O  O   . HOH   F 6 .   ? 48.509 25.406  14.601  1.00 36.40 ? 878 HOH   A O   1 
HETATM 3644 O  O   . HOH   F 6 .   ? 25.266 19.072  24.633  1.00 33.98 ? 879 HOH   A O   1 
HETATM 3645 O  O   . HOH   F 6 .   ? 35.836 -8.941  -4.263  1.00 43.31 ? 880 HOH   A O   1 
HETATM 3646 O  O   . HOH   F 6 .   ? 12.881 17.847  11.046  1.00 36.84 ? 881 HOH   A O   1 
HETATM 3647 O  O   . HOH   F 6 .   ? 44.245 17.748  26.462  1.00 27.59 ? 882 HOH   A O   1 
HETATM 3648 O  O   . HOH   F 6 .   ? 39.566 29.939  21.414  1.00 34.54 ? 883 HOH   A O   1 
HETATM 3649 O  O   . HOH   F 6 .   ? 55.101 -1.437  36.397  1.00 45.58 ? 884 HOH   A O   1 
HETATM 3650 O  O   . HOH   F 6 .   ? 45.014 -10.455 17.158  1.00 48.25 ? 885 HOH   A O   1 
HETATM 3651 O  O   . HOH   F 6 .   ? 38.082 27.731  17.164  1.00 24.40 ? 886 HOH   A O   1 
HETATM 3652 O  O   . HOH   F 6 .   ? 42.867 22.583  25.787  1.00 51.92 ? 887 HOH   A O   1 
HETATM 3653 O  O   . HOH   F 6 .   ? 38.873 16.259  37.944  1.00 31.42 ? 888 HOH   A O   1 
HETATM 3654 O  O   . HOH   F 6 .   ? 56.721 15.634  5.459   1.00 33.73 ? 889 HOH   A O   1 
HETATM 3655 O  O   . HOH   F 6 .   ? 40.441 16.412  -0.238  1.00 43.09 ? 890 HOH   A O   1 
HETATM 3656 O  O   . HOH   F 6 .   ? 35.847 30.743  23.407  1.00 26.67 ? 891 HOH   A O   1 
HETATM 3657 O  O   . HOH   F 6 .   ? 24.868 25.358  17.207  1.00 45.16 ? 892 HOH   A O   1 
HETATM 3658 O  O   . HOH   F 6 .   ? 11.992 6.143   -0.020  1.00 45.96 ? 893 HOH   A O   1 
HETATM 3659 O  O   . HOH   F 6 .   ? 38.476 16.010  1.502   1.00 38.08 ? 894 HOH   A O   1 
HETATM 3660 O  O   . HOH   F 6 .   ? 20.739 12.376  1.162   1.00 47.03 ? 895 HOH   A O   1 
HETATM 3661 O  O   . HOH   F 6 .   ? 26.485 23.992  -0.096  1.00 37.77 ? 896 HOH   A O   1 
HETATM 3662 O  O   . HOH   F 6 .   ? 53.851 -5.062  31.351  1.00 36.56 ? 897 HOH   A O   1 
HETATM 3663 O  O   . HOH   F 6 .   ? 29.465 23.875  25.679  1.00 31.23 ? 898 HOH   A O   1 
HETATM 3664 O  O   . HOH   F 6 .   ? 33.078 -11.324 1.106   1.00 41.86 ? 899 HOH   A O   1 
HETATM 3665 O  O   . HOH   F 6 .   ? 40.839 35.376  7.010   1.00 30.51 ? 900 HOH   A O   1 
HETATM 3666 O  O   . HOH   F 6 .   ? 46.084 13.753  -4.260  1.00 41.17 ? 901 HOH   A O   1 
HETATM 3667 O  O   . HOH   F 6 .   ? 12.189 17.461  23.602  1.00 47.90 ? 902 HOH   A O   1 
HETATM 3668 O  O   . HOH   F 6 .   ? 40.599 9.222   3.185   1.00 32.98 ? 903 HOH   A O   1 
HETATM 3669 O  O   . HOH   F 6 .   ? 16.281 22.052  13.920  1.00 32.15 ? 904 HOH   A O   1 
HETATM 3670 O  O   . HOH   F 6 .   ? 13.876 10.211  25.228  1.00 31.53 ? 905 HOH   A O   1 
HETATM 3671 O  O   . HOH   F 6 .   ? 60.864 6.944   19.137  1.00 37.70 ? 906 HOH   A O   1 
HETATM 3672 O  O   . HOH   F 6 .   ? 36.155 20.566  -1.236  1.00 51.63 ? 907 HOH   A O   1 
HETATM 3673 O  O   . HOH   F 6 .   ? 33.388 33.139  19.196  1.00 51.81 ? 908 HOH   A O   1 
HETATM 3674 O  O   . HOH   F 6 .   ? 54.760 -0.164  31.280  1.00 41.22 ? 909 HOH   A O   1 
HETATM 3675 O  O   . HOH   F 6 .   ? 60.673 9.682   13.139  1.00 48.10 ? 910 HOH   A O   1 
HETATM 3676 O  O   . HOH   F 6 .   ? 36.891 27.589  28.641  1.00 44.62 ? 911 HOH   A O   1 
HETATM 3677 O  O   . HOH   F 6 .   ? 41.892 35.220  9.302   1.00 26.40 ? 912 HOH   A O   1 
HETATM 3678 O  O   . HOH   F 6 .   ? 56.120 -8.362  35.905  1.00 48.22 ? 913 HOH   A O   1 
HETATM 3679 O  O   . HOH   F 6 .   ? 41.799 36.979  11.399  1.00 32.00 ? 914 HOH   A O   1 
HETATM 3680 O  O   . HOH   F 6 .   ? 50.312 25.901  5.625   1.00 48.24 ? 915 HOH   A O   1 
HETATM 3681 O  O   . HOH   F 6 .   ? 30.937 27.297  -3.872  1.00 37.85 ? 916 HOH   A O   1 
HETATM 3682 O  O   . HOH   F 6 .   ? 34.305 12.715  1.830   1.00 29.63 ? 917 HOH   A O   1 
HETATM 3683 O  O   . HOH   F 6 .   ? 34.194 -14.764 18.233  1.00 38.98 ? 918 HOH   A O   1 
HETATM 3684 O  O   . HOH   F 6 .   ? 44.957 34.690  13.372  1.00 43.52 ? 919 HOH   A O   1 
HETATM 3685 O  O   . HOH   F 6 .   ? 45.875 15.721  -2.753  1.00 39.56 ? 920 HOH   A O   1 
HETATM 3686 O  O   . HOH   F 6 .   ? 29.214 35.753  8.552   1.00 21.96 ? 921 HOH   A O   1 
HETATM 3687 O  O   . HOH   F 6 .   ? 26.828 23.353  26.860  1.00 51.64 ? 922 HOH   A O   1 
HETATM 3688 O  O   . HOH   F 6 .   ? 37.294 28.436  -3.698  1.00 47.15 ? 923 HOH   A O   1 
HETATM 3689 O  O   . HOH   F 6 .   ? 21.449 32.537  7.501   1.00 34.68 ? 924 HOH   A O   1 
HETATM 3690 O  O   . HOH   F 6 .   ? 19.261 -10.000 -9.556  1.00 44.46 ? 925 HOH   A O   1 
HETATM 3691 O  O   . HOH   F 6 .   ? 48.061 -5.169  27.450  1.00 22.30 ? 926 HOH   A O   1 
HETATM 3692 O  O   . HOH   F 6 .   ? 29.782 22.536  36.426  1.00 44.12 ? 927 HOH   A O   1 
HETATM 3693 O  O   . HOH   F 6 .   ? 27.901 23.636  20.642  1.00 29.64 ? 928 HOH   A O   1 
HETATM 3694 O  O   . HOH   F 6 .   ? 35.853 5.288   -9.221  1.00 49.72 ? 929 HOH   A O   1 
HETATM 3695 O  O   . HOH   F 6 .   ? 40.985 1.153   3.624   1.00 34.21 ? 930 HOH   A O   1 
HETATM 3696 O  O   . HOH   F 6 .   ? 42.195 -11.060 17.845  1.00 35.17 ? 931 HOH   A O   1 
HETATM 3697 O  O   . HOH   F 6 .   ? 49.535 27.389  13.820  1.00 48.51 ? 932 HOH   A O   1 
HETATM 3698 O  O   . HOH   F 6 .   ? 39.975 24.018  27.200  1.00 33.40 ? 933 HOH   A O   1 
HETATM 3699 O  O   . HOH   F 6 .   ? 40.236 -15.368 19.731  1.00 33.13 ? 934 HOH   A O   1 
HETATM 3700 O  O   . HOH   F 6 .   ? 50.230 24.529  3.875   1.00 41.29 ? 935 HOH   A O   1 
HETATM 3701 O  O   . HOH   F 6 .   ? 41.857 -15.308 18.055  1.00 45.86 ? 936 HOH   A O   1 
HETATM 3702 O  O   . HOH   F 6 .   ? 24.085 24.531  14.887  1.00 38.92 ? 937 HOH   A O   1 
HETATM 3703 O  O   . HOH   F 6 .   ? 27.911 26.323  -0.918  1.00 38.89 ? 938 HOH   A O   1 
HETATM 3704 O  O   . HOH   F 6 .   ? 51.493 3.922   2.886   1.00 39.40 ? 939 HOH   A O   1 
HETATM 3705 O  O   . HOH   F 6 .   ? 19.394 4.771   24.391  1.00 18.38 ? 940 HOH   A O   1 
HETATM 3706 O  O   . HOH   F 6 .   ? 40.071 5.272   1.564   1.00 43.13 ? 941 HOH   A O   1 
HETATM 3707 O  O   . HOH   F 6 .   ? 45.110 32.717  11.512  1.00 25.85 ? 942 HOH   A O   1 
HETATM 3708 O  O   . HOH   F 6 .   ? 35.807 -9.593  -1.737  1.00 38.11 ? 943 HOH   A O   1 
HETATM 3709 O  O   . HOH   F 6 .   ? 41.584 7.617   1.388   1.00 37.34 ? 944 HOH   A O   1 
HETATM 3710 O  O   . HOH   F 6 .   ? 22.748 18.767  38.300  1.00 43.00 ? 945 HOH   A O   1 
HETATM 3711 O  O   . HOH   F 6 .   ? 56.860 22.027  9.543   1.00 36.50 ? 946 HOH   A O   1 
HETATM 3712 O  O   . HOH   F 6 .   ? 24.193 16.394  38.588  1.00 30.03 ? 947 HOH   A O   1 
HETATM 3713 O  O   . HOH   F 6 .   ? 51.985 24.079  16.294  1.00 39.08 ? 948 HOH   A O   1 
HETATM 3714 O  O   . HOH   F 6 .   ? 23.081 -16.668 27.378  1.00 36.93 ? 949 HOH   A O   1 
HETATM 3715 O  O   . HOH   F 6 .   ? 47.906 25.370  16.895  1.00 38.93 ? 950 HOH   A O   1 
HETATM 3716 O  O   . HOH   F 6 .   ? 38.943 27.886  24.608  1.00 25.07 ? 951 HOH   A O   1 
HETATM 3717 O  O   . HOH   F 6 .   ? 42.963 20.518  27.110  1.00 49.79 ? 952 HOH   A O   1 
HETATM 3718 O  O   . HOH   F 6 .   ? 38.832 0.075   1.001   1.00 43.92 ? 953 HOH   A O   1 
HETATM 3719 O  O   . HOH   F 6 .   ? 44.138 20.117  -3.325  1.00 31.40 ? 954 HOH   A O   1 
HETATM 3720 O  O   . HOH   F 6 .   ? 22.165 22.657  -0.122  1.00 36.98 ? 955 HOH   A O   1 
HETATM 3721 O  O   . HOH   F 6 .   ? 55.423 23.584  16.025  1.00 54.59 ? 956 HOH   A O   1 
HETATM 3722 O  O   . HOH   F 6 .   ? 59.407 12.158  2.885   1.00 52.05 ? 957 HOH   A O   1 
HETATM 3723 O  O   . HOH   F 6 .   ? 43.220 7.290   -0.567  1.00 36.60 ? 958 HOH   A O   1 
HETATM 3724 O  O   . HOH   F 6 .   ? 25.164 -17.275 28.866  1.00 33.76 ? 959 HOH   A O   1 
HETATM 3725 O  O   . HOH   F 6 .   ? 51.842 32.766  -8.003  1.00 38.86 ? 960 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   . LYS A 2   ? 0.8855 0.8846 0.9585 0.0012  -0.0328 -0.0317 76  LYS A N   
2    C CA  . LYS A 2   ? 0.8123 0.8131 0.8819 0.0025  -0.0327 -0.0317 76  LYS A CA  
3    C C   . LYS A 2   ? 0.6965 0.6949 0.7569 0.0043  -0.0323 -0.0314 76  LYS A C   
4    O O   . LYS A 2   ? 0.7355 0.7347 0.7925 0.0042  -0.0293 -0.0294 76  LYS A O   
5    C CB  . LYS A 2   ? 0.8651 0.8697 0.9386 0.0011  -0.0294 -0.0295 76  LYS A CB  
6    C CG  . LYS A 2   ? 0.9098 0.9169 0.9829 0.0019  -0.0293 -0.0296 76  LYS A CG  
7    C CD  . LYS A 2   ? 0.9420 0.9482 1.0067 0.0035  -0.0282 -0.0290 76  LYS A CD  
8    C CE  . LYS A 2   ? 0.9500 0.9563 1.0115 0.0028  -0.0246 -0.0265 76  LYS A CE  
9    N NZ  . LYS A 2   ? 0.9225 0.9274 0.9761 0.0044  -0.0240 -0.0261 76  LYS A NZ  
10   N N   . PRO A 3   ? 0.5989 0.5940 0.6549 0.0061  -0.0352 -0.0334 77  PRO A N   
11   C CA  . PRO A 3   ? 0.5333 0.5260 0.5808 0.0080  -0.0347 -0.0331 77  PRO A CA  
12   C C   . PRO A 3   ? 0.4566 0.4509 0.5006 0.0092  -0.0341 -0.0327 77  PRO A C   
13   O O   . PRO A 3   ? 0.4979 0.4941 0.5450 0.0093  -0.0355 -0.0337 77  PRO A O   
14   C CB  . PRO A 3   ? 0.5818 0.5706 0.6262 0.0096  -0.0381 -0.0355 77  PRO A CB  
15   C CG  . PRO A 3   ? 0.5903 0.5794 0.6422 0.0083  -0.0407 -0.0373 77  PRO A CG  
16   C CD  . PRO A 3   ? 0.6367 0.6302 0.6956 0.0065  -0.0393 -0.0362 77  PRO A CD  
17   N N   . ILE A 4   ? 0.3550 0.3484 0.3925 0.0102  -0.0321 -0.0313 78  ILE A N   
18   C CA  . ILE A 4   ? 0.3256 0.3200 0.3592 0.0114  -0.0314 -0.0309 78  ILE A CA  
19   C C   . ILE A 4   ? 0.2950 0.2864 0.3227 0.0140  -0.0338 -0.0325 78  ILE A C   
20   O O   . ILE A 4   ? 0.2926 0.2811 0.3156 0.0150  -0.0338 -0.0324 78  ILE A O   
21   C CB  . ILE A 4   ? 0.3901 0.3854 0.4207 0.0109  -0.0278 -0.0283 78  ILE A CB  
22   C CG1 . ILE A 4   ? 0.4045 0.4027 0.4406 0.0085  -0.0254 -0.0267 78  ILE A CG1 
23   C CG2 . ILE A 4   ? 0.4083 0.4041 0.4341 0.0123  -0.0271 -0.0278 78  ILE A CG2 
24   C CD1 . ILE A 4   ? 0.4391 0.4377 0.4727 0.0077  -0.0222 -0.0242 78  ILE A CD1 
25   N N   . ASN A 5   ? 0.2863 0.2784 0.3141 0.0151  -0.0359 -0.0339 79  ASN A N   
26   C CA  . ASN A 5   ? 0.2871 0.2764 0.3096 0.0177  -0.0385 -0.0356 79  ASN A CA  
27   C C   . ASN A 5   ? 0.2734 0.2624 0.2896 0.0192  -0.0366 -0.0342 79  ASN A C   
28   O O   . ASN A 5   ? 0.2708 0.2622 0.2880 0.0190  -0.0357 -0.0336 79  ASN A O   
29   C CB  . ASN A 5   ? 0.3166 0.3069 0.3429 0.0181  -0.0418 -0.0377 79  ASN A CB  
30   C CG  . ASN A 5   ? 0.3869 0.3771 0.4194 0.0167  -0.0440 -0.0392 79  ASN A CG  
31   O OD1 . ASN A 5   ? 0.3824 0.3704 0.4144 0.0163  -0.0440 -0.0393 79  ASN A OD1 
32   N ND2 . ASN A 5   ? 0.4461 0.4385 0.4847 0.0160  -0.0459 -0.0404 79  ASN A ND2 
33   N N   . VAL A 6   ? 0.2590 0.2450 0.2689 0.0208  -0.0362 -0.0339 80  VAL A N   
34   C CA  . VAL A 6   ? 0.2550 0.2406 0.2593 0.0219  -0.0340 -0.0323 80  VAL A CA  
35   C C   . VAL A 6   ? 0.2668 0.2491 0.2644 0.0249  -0.0356 -0.0333 80  VAL A C   
36   O O   . VAL A 6   ? 0.2987 0.2780 0.2944 0.0261  -0.0376 -0.0348 80  VAL A O   
37   C CB  . VAL A 6   ? 0.3076 0.2934 0.3111 0.0207  -0.0308 -0.0300 80  VAL A CB  
38   C CG1 . VAL A 6   ? 0.3516 0.3343 0.3529 0.0213  -0.0314 -0.0304 80  VAL A CG1 
39   C CG2 . VAL A 6   ? 0.3316 0.3177 0.3306 0.0214  -0.0283 -0.0281 80  VAL A CG2 
40   N N   . ALA A 7   ? 0.2290 0.2116 0.2231 0.0263  -0.0348 -0.0326 81  ALA A N   
41   C CA  . ALA A 7   ? 0.2367 0.2163 0.2239 0.0292  -0.0353 -0.0328 81  ALA A CA  
42   C C   . ALA A 7   ? 0.2319 0.2111 0.2152 0.0293  -0.0320 -0.0304 81  ALA A C   
43   O O   . ALA A 7   ? 0.2376 0.2195 0.2232 0.0276  -0.0296 -0.0286 81  ALA A O   
44   C CB  . ALA A 7   ? 0.2393 0.2195 0.2255 0.0306  -0.0368 -0.0337 81  ALA A CB  
45   N N   . ILE A 8   ? 0.2349 0.2109 0.2125 0.0315  -0.0318 -0.0302 82  ILE A N   
46   C CA  . ILE A 8   ? 0.2343 0.2098 0.2082 0.0320  -0.0288 -0.0279 82  ILE A CA  
47   C C   . ILE A 8   ? 0.2282 0.2016 0.1961 0.0348  -0.0289 -0.0278 82  ILE A C   
48   O O   . ILE A 8   ? 0.2503 0.2204 0.2138 0.0374  -0.0306 -0.0290 82  ILE A O   
49   C CB  . ILE A 8   ? 0.2581 0.2316 0.2303 0.0321  -0.0279 -0.0273 82  ILE A CB  
50   C CG1 . ILE A 8   ? 0.2741 0.2488 0.2517 0.0297  -0.0282 -0.0277 82  ILE A CG1 
51   C CG2 . ILE A 8   ? 0.2522 0.2258 0.2216 0.0323  -0.0246 -0.0246 82  ILE A CG2 
52   C CD1 . ILE A 8   ? 0.2715 0.2499 0.2540 0.0268  -0.0262 -0.0261 82  ILE A CD1 
53   N N   . PHE A 9   ? 0.2242 0.1994 0.1920 0.0346  -0.0272 -0.0264 83  PHE A N   
54   C CA  . PHE A 9   ? 0.2233 0.1969 0.1860 0.0371  -0.0268 -0.0258 83  PHE A CA  
55   C C   . PHE A 9   ? 0.2379 0.2105 0.1972 0.0376  -0.0237 -0.0234 83  PHE A C   
56   O O   . PHE A 9   ? 0.2419 0.2169 0.2040 0.0354  -0.0215 -0.0217 83  PHE A O   
57   C CB  . PHE A 9   ? 0.2206 0.1964 0.1852 0.0366  -0.0268 -0.0257 83  PHE A CB  
58   C CG  . PHE A 9   ? 0.2282 0.2045 0.1950 0.0369  -0.0299 -0.0281 83  PHE A CG  
59   C CD1 . PHE A 9   ? 0.2472 0.2222 0.2149 0.0374  -0.0328 -0.0302 83  PHE A CD1 
60   C CD2 . PHE A 9   ? 0.2435 0.2216 0.2116 0.0370  -0.0301 -0.0281 83  PHE A CD2 
61   C CE1 . PHE A 9   ? 0.2559 0.2316 0.2262 0.0376  -0.0359 -0.0323 83  PHE A CE1 
62   C CE2 . PHE A 9   ? 0.2512 0.2300 0.2218 0.0373  -0.0330 -0.0301 83  PHE A CE2 
63   C CZ  . PHE A 9   ? 0.2680 0.2457 0.2398 0.0376  -0.0359 -0.0322 83  PHE A CZ  
64   N N   . GLY A 10  ? 0.2353 0.2047 0.1890 0.0404  -0.0236 -0.0233 84  GLY A N   
65   C CA  . GLY A 10  ? 0.2414 0.2096 0.1921 0.0411  -0.0209 -0.0210 84  GLY A CA  
66   C C   . GLY A 10  ? 0.2334 0.2011 0.1854 0.0402  -0.0206 -0.0210 84  GLY A C   
67   O O   . GLY A 10  ? 0.2532 0.2223 0.2068 0.0387  -0.0183 -0.0191 84  GLY A O   
68   N N   . SER A 11  ? 0.2467 0.2121 0.1975 0.0413  -0.0231 -0.0231 85  SER A N   
69   C CA  . SER A 11  ? 0.2573 0.2223 0.2103 0.0400  -0.0233 -0.0235 85  SER A CA  
70   C C   . SER A 11  ? 0.2422 0.2050 0.1915 0.0415  -0.0212 -0.0220 85  SER A C   
71   O O   . SER A 11  ? 0.2543 0.2175 0.2059 0.0401  -0.0204 -0.0214 85  SER A O   
72   C CB  . SER A 11  ? 0.2628 0.2262 0.2165 0.0404  -0.0267 -0.0265 85  SER A CB  
73   O OG  . SER A 11  ? 0.2899 0.2493 0.2374 0.0438  -0.0282 -0.0277 85  SER A OG  
74   N N   . THR A 12  ? 0.2564 0.2169 0.2001 0.0443  -0.0201 -0.0211 86  THR A N   
75   C CA  . THR A 12  ? 0.2748 0.2329 0.2147 0.0461  -0.0180 -0.0195 86  THR A CA  
76   C C   . THR A 12  ? 0.2679 0.2283 0.2092 0.0450  -0.0145 -0.0164 86  THR A C   
77   O O   . THR A 12  ? 0.3020 0.2612 0.2413 0.0460  -0.0125 -0.0148 86  THR A O   
78   C CB  . THR A 12  ? 0.2906 0.2446 0.2234 0.0500  -0.0186 -0.0202 86  THR A CB  
79   O OG1 . THR A 12  ? 0.2879 0.2428 0.2198 0.0506  -0.0188 -0.0201 86  THR A OG1 
80   C CG2 . THR A 12  ? 0.3004 0.2512 0.2311 0.0514  -0.0218 -0.0232 86  THR A CG2 
81   N N   . GLY A 13  ? 0.2450 0.2089 0.1899 0.0428  -0.0138 -0.0155 87  GLY A N   
82   C CA  . GLY A 13  ? 0.2572 0.2233 0.2037 0.0416  -0.0109 -0.0127 87  GLY A CA  
83   C C   . GLY A 13  ? 0.2399 0.2086 0.1913 0.0386  -0.0101 -0.0118 87  GLY A C   
84   O O   . GLY A 13  ? 0.2504 0.2188 0.2036 0.0378  -0.0114 -0.0131 87  GLY A O   
85   N N   . SER A 14  ? 0.2372 0.2084 0.1908 0.0371  -0.0079 -0.0095 88  SER A N   
86   C CA  . SER A 14  ? 0.2217 0.1954 0.1794 0.0345  -0.0069 -0.0083 88  SER A CA  
87   C C   . SER A 14  ? 0.2227 0.1984 0.1846 0.0320  -0.0086 -0.0099 88  SER A C   
88   O O   . SER A 14  ? 0.2304 0.2065 0.1947 0.0308  -0.0090 -0.0103 88  SER A O   
89   C CB  . SER A 14  ? 0.2240 0.1998 0.1829 0.0335  -0.0045 -0.0057 88  SER A CB  
90   O OG  . SER A 14  ? 0.2175 0.1960 0.1805 0.0309  -0.0038 -0.0045 88  SER A OG  
91   N N   . ILE A 15  ? 0.2121 0.1895 0.1754 0.0311  -0.0093 -0.0105 89  ILE A N   
92   C CA  . ILE A 15  ? 0.2152 0.1946 0.1826 0.0289  -0.0107 -0.0119 89  ILE A CA  
93   C C   . ILE A 15  ? 0.2198 0.1974 0.1872 0.0296  -0.0131 -0.0143 89  ILE A C   
94   O O   . ILE A 15  ? 0.2144 0.1929 0.1852 0.0279  -0.0137 -0.0149 89  ILE A O   
95   C CB  . ILE A 15  ? 0.2088 0.1898 0.1771 0.0283  -0.0110 -0.0123 89  ILE A CB  
96   C CG1 . ILE A 15  ? 0.2071 0.1903 0.1767 0.0267  -0.0089 -0.0102 89  ILE A CG1 
97   C CG2 . ILE A 15  ? 0.2085 0.1910 0.1805 0.0267  -0.0128 -0.0142 89  ILE A CG2 
98   C CD1 . ILE A 15  ? 0.2172 0.2030 0.1909 0.0239  -0.0083 -0.0095 89  ILE A CD1 
99   N N   . GLY A 16  ? 0.2215 0.1963 0.1850 0.0322  -0.0144 -0.0156 90  GLY A N   
100  C CA  . GLY A 16  ? 0.2279 0.2008 0.1913 0.0330  -0.0171 -0.0181 90  GLY A CA  
101  C C   . GLY A 16  ? 0.2581 0.2296 0.2218 0.0329  -0.0171 -0.0183 90  GLY A C   
102  O O   . GLY A 16  ? 0.2622 0.2339 0.2292 0.0316  -0.0186 -0.0197 90  GLY A O   
103  N N   . THR A 17  ? 0.2557 0.2258 0.2165 0.0341  -0.0151 -0.0165 91  THR A N   
104  C CA  . THR A 17  ? 0.2781 0.2466 0.2390 0.0342  -0.0150 -0.0166 91  THR A CA  
105  C C   . THR A 17  ? 0.2711 0.2426 0.2373 0.0311  -0.0141 -0.0155 91  THR A C   
106  O O   . THR A 17  ? 0.2843 0.2552 0.2528 0.0302  -0.0149 -0.0164 91  THR A O   
107  C CB  . THR A 17  ? 0.3185 0.2845 0.2746 0.0367  -0.0132 -0.0151 91  THR A CB  
108  O OG1 . THR A 17  ? 0.3643 0.3326 0.3213 0.0359  -0.0105 -0.0124 91  THR A OG1 
109  C CG2 . THR A 17  ? 0.3293 0.2921 0.2797 0.0400  -0.0140 -0.0160 91  THR A CG2 
110  N N   . ASN A 18  ? 0.2593 0.2339 0.2277 0.0294  -0.0123 -0.0136 92  ASN A N   
111  C CA  . ASN A 18  ? 0.2586 0.2359 0.2317 0.0266  -0.0116 -0.0127 92  ASN A CA  
112  C C   . ASN A 18  ? 0.2639 0.2424 0.2410 0.0249  -0.0134 -0.0146 92  ASN A C   
113  O O   . ASN A 18  ? 0.2868 0.2664 0.2675 0.0230  -0.0133 -0.0144 92  ASN A O   
114  C CB  . ASN A 18  ? 0.2871 0.2674 0.2615 0.0252  -0.0096 -0.0106 92  ASN A CB  
115  C CG  . ASN A 18  ? 0.4209 0.4016 0.3952 0.0249  -0.0075 -0.0082 92  ASN A CG  
116  O OD1 . ASN A 18  ? 0.4858 0.4663 0.4616 0.0243  -0.0074 -0.0079 92  ASN A OD1 
117  N ND2 . ASN A 18  ? 0.5004 0.4818 0.4730 0.0255  -0.0060 -0.0064 92  ASN A ND2 
118  N N   . ALA A 19  ? 0.2267 0.2053 0.2035 0.0254  -0.0150 -0.0162 93  ALA A N   
119  C CA  . ALA A 19  ? 0.2289 0.2087 0.2098 0.0240  -0.0168 -0.0180 93  ALA A CA  
120  C C   . ALA A 19  ? 0.2545 0.2318 0.2359 0.0245  -0.0187 -0.0197 93  ALA A C   
121  O O   . ALA A 19  ? 0.2604 0.2388 0.2462 0.0226  -0.0192 -0.0202 93  ALA A O   
122  C CB  . ALA A 19  ? 0.2178 0.1979 0.1979 0.0248  -0.0182 -0.0192 93  ALA A CB  
123  N N   . LEU A 20  ? 0.2549 0.2289 0.2317 0.0270  -0.0197 -0.0207 94  LEU A N   
124  C CA  . LEU A 20  ? 0.2749 0.2461 0.2518 0.0277  -0.0217 -0.0226 94  LEU A CA  
125  C C   . LEU A 20  ? 0.3027 0.2739 0.2814 0.0265  -0.0201 -0.0212 94  LEU A C   
126  O O   . LEU A 20  ? 0.3224 0.2930 0.3043 0.0254  -0.0213 -0.0223 94  LEU A O   
127  C CB  . LEU A 20  ? 0.2747 0.2421 0.2456 0.0309  -0.0229 -0.0238 94  LEU A CB  
128  C CG  . LEU A 20  ? 0.2904 0.2572 0.2595 0.0323  -0.0251 -0.0256 94  LEU A CG  
129  C CD1 . LEU A 20  ? 0.3242 0.2873 0.2865 0.0358  -0.0259 -0.0263 94  LEU A CD1 
130  C CD2 . LEU A 20  ? 0.3035 0.2708 0.2770 0.0311  -0.0281 -0.0281 94  LEU A CD2 
131  N N   . ASN A 21  ? 0.3057 0.2777 0.2830 0.0265  -0.0174 -0.0187 95  ASN A N   
132  C CA  . ASN A 21  ? 0.3104 0.2825 0.2896 0.0253  -0.0160 -0.0173 95  ASN A CA  
133  C C   . ASN A 21  ? 0.3209 0.2960 0.3061 0.0223  -0.0158 -0.0169 95  ASN A C   
134  O O   . ASN A 21  ? 0.3260 0.3004 0.3137 0.0215  -0.0161 -0.0172 95  ASN A O   
135  C CB  . ASN A 21  ? 0.3471 0.3200 0.3242 0.0258  -0.0133 -0.0146 95  ASN A CB  
136  C CG  . ASN A 21  ? 0.4219 0.3916 0.3934 0.0288  -0.0128 -0.0144 95  ASN A CG  
137  O OD1 . ASN A 21  ? 0.5003 0.4667 0.4689 0.0308  -0.0145 -0.0163 95  ASN A OD1 
138  N ND2 . ASN A 21  ? 0.4992 0.4701 0.4692 0.0293  -0.0106 -0.0120 95  ASN A ND2 
139  N N   . ILE A 22  ? 0.2874 0.2659 0.2750 0.0207  -0.0150 -0.0161 96  ILE A N   
140  C CA  . ILE A 22  ? 0.2810 0.2620 0.2737 0.0181  -0.0145 -0.0156 96  ILE A CA  
141  C C   . ILE A 22  ? 0.3218 0.3024 0.3179 0.0174  -0.0168 -0.0179 96  ILE A C   
142  O O   . ILE A 22  ? 0.3138 0.2952 0.3141 0.0157  -0.0166 -0.0177 96  ILE A O   
143  C CB  . ILE A 22  ? 0.2880 0.2725 0.2820 0.0166  -0.0130 -0.0141 96  ILE A CB  
144  C CG1 . ILE A 22  ? 0.2926 0.2795 0.2912 0.0141  -0.0120 -0.0131 96  ILE A CG1 
145  C CG2 . ILE A 22  ? 0.3016 0.2870 0.2952 0.0170  -0.0141 -0.0153 96  ILE A CG2 
146  C CD1 . ILE A 22  ? 0.2769 0.2634 0.2761 0.0135  -0.0106 -0.0114 96  ILE A CD1 
147  N N   . ILE A 23  ? 0.2982 0.2776 0.2929 0.0188  -0.0189 -0.0200 97  ILE A N   
148  C CA  . ILE A 23  ? 0.3201 0.2988 0.3178 0.0184  -0.0215 -0.0224 97  ILE A CA  
149  C C   . ILE A 23  ? 0.3230 0.2988 0.3212 0.0187  -0.0223 -0.0231 97  ILE A C   
150  O O   . ILE A 23  ? 0.3331 0.3096 0.3362 0.0169  -0.0228 -0.0236 97  ILE A O   
151  C CB  . ILE A 23  ? 0.3201 0.2978 0.3155 0.0202  -0.0238 -0.0243 97  ILE A CB  
152  C CG1 . ILE A 23  ? 0.3098 0.2907 0.3066 0.0194  -0.0231 -0.0238 97  ILE A CG1 
153  C CG2 . ILE A 23  ? 0.3464 0.3224 0.3440 0.0204  -0.0269 -0.0271 97  ILE A CG2 
154  C CD1 . ILE A 23  ? 0.3327 0.3127 0.3261 0.0214  -0.0247 -0.0251 97  ILE A CD1 
155  N N   . ARG A 24  ? 0.3363 0.3089 0.3293 0.0209  -0.0223 -0.0232 98  ARG A N   
156  C CA  . ARG A 24  ? 0.3448 0.3142 0.3374 0.0215  -0.0231 -0.0241 98  ARG A CA  
157  C C   . ARG A 24  ? 0.3742 0.3451 0.3710 0.0193  -0.0213 -0.0223 98  ARG A C   
158  O O   . ARG A 24  ? 0.3964 0.3664 0.3969 0.0182  -0.0223 -0.0234 98  ARG A O   
159  C CB  . ARG A 24  ? 0.3639 0.3301 0.3498 0.0243  -0.0226 -0.0238 98  ARG A CB  
160  C CG  . ARG A 24  ? 0.4138 0.3759 0.3981 0.0255  -0.0235 -0.0249 98  ARG A CG  
161  C CD  . ARG A 24  ? 0.4272 0.3868 0.4054 0.0281  -0.0221 -0.0239 98  ARG A CD  
162  N NE  . ARG A 24  ? 0.5081 0.4659 0.4809 0.0307  -0.0229 -0.0248 98  ARG A NE  
163  C CZ  . ARG A 24  ? 0.4829 0.4419 0.4525 0.0318  -0.0210 -0.0230 98  ARG A CZ  
164  N NH1 . ARG A 24  ? 0.4598 0.4218 0.4311 0.0305  -0.0183 -0.0203 98  ARG A NH1 
165  N NH2 . ARG A 24  ? 0.5193 0.4762 0.4839 0.0343  -0.0220 -0.0240 98  ARG A NH2 
166  N N   . GLU A 25  ? 0.3555 0.3286 0.3518 0.0187  -0.0185 -0.0197 99  GLU A N   
167  C CA  . GLU A 25  ? 0.3682 0.3427 0.3678 0.0168  -0.0166 -0.0178 99  GLU A CA  
168  C C   . GLU A 25  ? 0.4210 0.3981 0.4267 0.0143  -0.0168 -0.0179 99  GLU A C   
169  O O   . GLU A 25  ? 0.4074 0.3844 0.4166 0.0129  -0.0163 -0.0174 99  GLU A O   
170  C CB  . GLU A 25  ? 0.4005 0.3769 0.3981 0.0168  -0.0140 -0.0150 99  GLU A CB  
171  C CG  . GLU A 25  ? 0.4331 0.4069 0.4258 0.0191  -0.0132 -0.0143 99  GLU A CG  
172  C CD  . GLU A 25  ? 0.4753 0.4460 0.4678 0.0197  -0.0135 -0.0147 99  GLU A CD  
173  O OE1 . GLU A 25  ? 0.5116 0.4829 0.5079 0.0181  -0.0129 -0.0140 99  GLU A OE1 
174  O OE2 . GLU A 25  ? 0.5653 0.5326 0.5539 0.0220  -0.0145 -0.0160 99  GLU A OE2 
175  N N   . CYS A 26  ? 0.4099 0.3893 0.4168 0.0138  -0.0174 -0.0185 100 CYS A N   
176  C CA  . CYS A 26  ? 0.4217 0.4037 0.4341 0.0115  -0.0173 -0.0185 100 CYS A CA  
177  C C   . CYS A 26  ? 0.4455 0.4259 0.4618 0.0111  -0.0195 -0.0206 100 CYS A C   
178  O O   . CYS A 26  ? 0.4718 0.4531 0.4930 0.0093  -0.0190 -0.0201 100 CYS A O   
179  C CB  . CYS A 26  ? 0.3616 0.3464 0.3737 0.0113  -0.0169 -0.0182 100 CYS A CB  
180  S SG  . CYS A 26  ? 0.4145 0.4025 0.4265 0.0099  -0.0137 -0.0152 100 CYS A SG  
181  N N   . ASN A 27  ? 0.4050 0.3826 0.4187 0.0129  -0.0221 -0.0229 101 ASN A N   
182  C CA  . ASN A 27  ? 0.4538 0.4296 0.4708 0.0126  -0.0247 -0.0253 101 ASN A CA  
183  C C   . ASN A 27  ? 0.4942 0.4679 0.5131 0.0120  -0.0243 -0.0250 101 ASN A C   
184  O O   . ASN A 27  ? 0.5163 0.4898 0.5403 0.0106  -0.0255 -0.0260 101 ASN A O   
185  C CB  . ASN A 27  ? 0.3980 0.3712 0.4113 0.0148  -0.0277 -0.0279 101 ASN A CB  
186  C CG  . ASN A 27  ? 0.3999 0.3753 0.4144 0.0149  -0.0291 -0.0290 101 ASN A CG  
187  O OD1 . ASN A 27  ? 0.4179 0.3916 0.4288 0.0168  -0.0312 -0.0308 101 ASN A OD1 
188  N ND2 . ASN A 27  ? 0.3725 0.3515 0.3919 0.0129  -0.0280 -0.0281 101 ASN A ND2 
189  N N   . LYS A 28  ? 0.4951 0.4672 0.5100 0.0130  -0.0226 -0.0235 102 LYS A N   
190  C CA  . LYS A 28  ? 0.4708 0.4408 0.4872 0.0124  -0.0220 -0.0230 102 LYS A CA  
191  C C   . LYS A 28  ? 0.4792 0.4519 0.5017 0.0098  -0.0202 -0.0213 102 LYS A C   
192  O O   . LYS A 28  ? 0.5402 0.5114 0.5663 0.0088  -0.0205 -0.0215 102 LYS A O   
193  C CB  . LYS A 28  ? 0.4575 0.4259 0.4688 0.0140  -0.0201 -0.0213 102 LYS A CB  
194  C CG  . LYS A 28  ? 0.4810 0.4458 0.4862 0.0168  -0.0216 -0.0229 102 LYS A CG  
195  C CD  . LYS A 28  ? 0.5525 0.5166 0.5527 0.0184  -0.0193 -0.0208 102 LYS A CD  
196  C CE  . LYS A 28  ? 0.6200 0.5807 0.6142 0.0213  -0.0205 -0.0222 102 LYS A CE  
197  N NZ  . LYS A 28  ? 0.6998 0.6601 0.6897 0.0228  -0.0181 -0.0200 102 LYS A NZ  
198  N N   . ILE A 29  ? 0.4961 0.4725 0.5196 0.0087  -0.0183 -0.0194 103 ILE A N   
199  C CA  . ILE A 29  ? 0.4786 0.4576 0.5074 0.0064  -0.0165 -0.0177 103 ILE A CA  
200  C C   . ILE A 29  ? 0.5093 0.4894 0.5440 0.0050  -0.0181 -0.0193 103 ILE A C   
201  O O   . ILE A 29  ? 0.4959 0.4762 0.5357 0.0034  -0.0175 -0.0188 103 ILE A O   
202  C CB  . ILE A 29  ? 0.4530 0.4354 0.4805 0.0059  -0.0140 -0.0153 103 ILE A CB  
203  C CG1 . ILE A 29  ? 0.4307 0.4122 0.4531 0.0071  -0.0125 -0.0136 103 ILE A CG1 
204  C CG2 . ILE A 29  ? 0.4351 0.4201 0.4677 0.0036  -0.0121 -0.0136 103 ILE A CG2 
205  C CD1 . ILE A 29  ? 0.4087 0.3932 0.4294 0.0067  -0.0104 -0.0114 103 ILE A CD1 
206  N N   . GLU A 30  ? 0.5316 0.5123 0.5658 0.0056  -0.0200 -0.0211 104 GLU A N   
207  C CA  . GLU A 30  ? 0.6475 0.6287 0.6871 0.0047  -0.0223 -0.0232 104 GLU A CA  
208  C C   . GLU A 30  ? 0.6354 0.6169 0.6723 0.0062  -0.0244 -0.0250 104 GLU A C   
209  O O   . GLU A 30  ? 0.5408 0.5240 0.5741 0.0069  -0.0232 -0.0240 104 GLU A O   
210  C CB  . GLU A 30  ? 0.7530 0.7376 0.7991 0.0024  -0.0206 -0.0218 104 GLU A CB  
211  C CG  . GLU A 30  ? 0.8236 0.8118 0.8696 0.0022  -0.0195 -0.0210 104 GLU A CG  
212  C CD  . GLU A 30  ? 0.8950 0.8863 0.9468 0.0001  -0.0174 -0.0194 104 GLU A CD  
213  O OE1 . GLU A 30  ? 0.9753 0.9671 1.0276 -0.0007 -0.0149 -0.0172 104 GLU A OE1 
214  O OE2 . GLU A 30  ? 0.9449 0.9382 1.0005 -0.0004 -0.0183 -0.0203 104 GLU A OE2 
215  N N   . ASN A 31  ? 0.6076 0.5876 0.6465 0.0066  -0.0276 -0.0277 105 ASN A N   
216  C CA  . ASN A 31  ? 0.6674 0.6466 0.7028 0.0084  -0.0302 -0.0298 105 ASN A CA  
217  C C   . ASN A 31  ? 0.6215 0.6044 0.6592 0.0078  -0.0300 -0.0296 105 ASN A C   
218  O O   . ASN A 31  ? 0.6504 0.6344 0.6931 0.0071  -0.0320 -0.0311 105 ASN A O   
219  C CB  . ASN A 31  ? 0.6915 0.6679 0.7285 0.0090  -0.0340 -0.0328 105 ASN A CB  
220  C CG  . ASN A 31  ? 0.7953 0.7710 0.8287 0.0109  -0.0367 -0.0349 105 ASN A CG  
221  O OD1 . ASN A 31  ? 0.7821 0.7594 0.8197 0.0104  -0.0388 -0.0364 105 ASN A OD1 
222  N ND2 . ASN A 31  ? 0.8197 0.7933 0.8456 0.0132  -0.0365 -0.0349 105 ASN A ND2 
223  N N   . VAL A 32  ? 0.5016 0.4862 0.5356 0.0084  -0.0279 -0.0280 106 VAL A N   
224  C CA  . VAL A 32  ? 0.4861 0.4742 0.5221 0.0078  -0.0273 -0.0275 106 VAL A CA  
225  C C   . VAL A 32  ? 0.3886 0.3762 0.4200 0.0098  -0.0289 -0.0288 106 VAL A C   
226  O O   . VAL A 32  ? 0.4078 0.3978 0.4414 0.0095  -0.0292 -0.0291 106 VAL A O   
227  C CB  . VAL A 32  ? 0.5756 0.5664 0.6117 0.0066  -0.0236 -0.0247 106 VAL A CB  
228  C CG1 . VAL A 32  ? 0.6268 0.6182 0.6673 0.0046  -0.0218 -0.0232 106 VAL A CG1 
229  C CG2 . VAL A 32  ? 0.5226 0.5124 0.5518 0.0079  -0.0221 -0.0234 106 VAL A CG2 
230  N N   . PHE A 33  ? 0.3438 0.3283 0.3690 0.0120  -0.0299 -0.0296 107 PHE A N   
231  C CA  . PHE A 33  ? 0.3439 0.3279 0.3645 0.0140  -0.0312 -0.0305 107 PHE A CA  
232  C C   . PHE A 33  ? 0.3605 0.3412 0.3790 0.0159  -0.0348 -0.0333 107 PHE A C   
233  O O   . PHE A 33  ? 0.3954 0.3731 0.4122 0.0164  -0.0356 -0.0339 107 PHE A O   
234  C CB  . PHE A 33  ? 0.3441 0.3273 0.3582 0.0154  -0.0290 -0.0288 107 PHE A CB  
235  C CG  . PHE A 33  ? 0.3433 0.3295 0.3585 0.0138  -0.0257 -0.0262 107 PHE A CG  
236  C CD1 . PHE A 33  ? 0.3477 0.3368 0.3643 0.0131  -0.0249 -0.0256 107 PHE A CD1 
237  C CD2 . PHE A 33  ? 0.3556 0.3414 0.3700 0.0131  -0.0235 -0.0243 107 PHE A CD2 
238  C CE1 . PHE A 33  ? 0.3696 0.3610 0.3868 0.0118  -0.0220 -0.0234 107 PHE A CE1 
239  C CE2 . PHE A 33  ? 0.3766 0.3650 0.3918 0.0117  -0.0207 -0.0220 107 PHE A CE2 
240  C CZ  . PHE A 33  ? 0.3584 0.3495 0.3749 0.0110  -0.0200 -0.0216 107 PHE A CZ  
241  N N   . ASN A 34  ? 0.3232 0.3045 0.3416 0.0169  -0.0371 -0.0349 108 ASN A N   
242  C CA  . ASN A 34  ? 0.3331 0.3113 0.3479 0.0192  -0.0405 -0.0373 108 ASN A CA  
243  C C   . ASN A 34  ? 0.3427 0.3201 0.3506 0.0215  -0.0400 -0.0369 108 ASN A C   
244  O O   . ASN A 34  ? 0.3126 0.2926 0.3214 0.0215  -0.0395 -0.0365 108 ASN A O   
245  C CB  . ASN A 34  ? 0.3818 0.3610 0.4017 0.0188  -0.0438 -0.0396 108 ASN A CB  
246  C CG  . ASN A 34  ? 0.4785 0.4582 0.5056 0.0166  -0.0449 -0.0404 108 ASN A CG  
247  O OD1 . ASN A 34  ? 0.5840 0.5665 0.6178 0.0151  -0.0458 -0.0409 108 ASN A OD1 
248  N ND2 . ASN A 34  ? 0.4938 0.4704 0.5197 0.0166  -0.0451 -0.0407 108 ASN A ND2 
249  N N   . VAL A 35  ? 0.3360 0.3099 0.3374 0.0237  -0.0400 -0.0371 109 VAL A N   
250  C CA  . VAL A 35  ? 0.3471 0.3196 0.3416 0.0262  -0.0397 -0.0367 109 VAL A CA  
251  C C   . VAL A 35  ? 0.3229 0.2938 0.3158 0.0282  -0.0434 -0.0393 109 VAL A C   
252  O O   . VAL A 35  ? 0.3568 0.3242 0.3471 0.0297  -0.0460 -0.0413 109 VAL A O   
253  C CB  . VAL A 35  ? 0.3401 0.3094 0.3284 0.0279  -0.0380 -0.0357 109 VAL A CB  
254  C CG1 . VAL A 35  ? 0.3621 0.3300 0.3436 0.0306  -0.0375 -0.0352 109 VAL A CG1 
255  C CG2 . VAL A 35  ? 0.3752 0.3462 0.3655 0.0259  -0.0345 -0.0331 109 VAL A CG2 
256  N N   . LYS A 36  ? 0.3207 0.2943 0.3154 0.0281  -0.0438 -0.0394 110 LYS A N   
257  C CA  . LYS A 36  ? 0.3123 0.2853 0.3070 0.0295  -0.0475 -0.0417 110 LYS A CA  
258  C C   . LYS A 36  ? 0.3192 0.2897 0.3061 0.0328  -0.0481 -0.0420 110 LYS A C   
259  O O   . LYS A 36  ? 0.3178 0.2865 0.3027 0.0347  -0.0514 -0.0441 110 LYS A O   
260  C CB  . LYS A 36  ? 0.3695 0.3466 0.3703 0.0280  -0.0479 -0.0417 110 LYS A CB  
261  C CG  . LYS A 36  ? 0.4325 0.4127 0.4416 0.0248  -0.0471 -0.0413 110 LYS A CG  
262  C CD  . LYS A 36  ? 0.4927 0.4715 0.5059 0.0240  -0.0501 -0.0434 110 LYS A CD  
263  C CE  . LYS A 36  ? 0.5563 0.5350 0.5712 0.0250  -0.0541 -0.0459 110 LYS A CE  
264  N NZ  . LYS A 36  ? 0.5883 0.5660 0.6081 0.0239  -0.0569 -0.0478 110 LYS A NZ  
265  N N   . ALA A 37  ? 0.2788 0.2492 0.2613 0.0335  -0.0448 -0.0397 111 ALA A N   
266  C CA  . ALA A 37  ? 0.2740 0.2424 0.2495 0.0365  -0.0449 -0.0396 111 ALA A CA  
267  C C   . ALA A 37  ? 0.2797 0.2470 0.2503 0.0372  -0.0413 -0.0371 111 ALA A C   
268  O O   . ALA A 37  ? 0.2780 0.2478 0.2517 0.0351  -0.0384 -0.0351 111 ALA A O   
269  C CB  . ALA A 37  ? 0.2808 0.2518 0.2578 0.0367  -0.0452 -0.0395 111 ALA A CB  
270  N N   . LEU A 38  ? 0.2814 0.2451 0.2447 0.0403  -0.0415 -0.0373 112 LEU A N   
271  C CA  . LEU A 38  ? 0.2791 0.2415 0.2373 0.0415  -0.0382 -0.0349 112 LEU A CA  
272  C C   . LEU A 38  ? 0.3068 0.2678 0.2594 0.0444  -0.0383 -0.0347 112 LEU A C   
273  O O   . LEU A 38  ? 0.3042 0.2627 0.2536 0.0467  -0.0413 -0.0368 112 LEU A O   
274  C CB  . LEU A 38  ? 0.2980 0.2569 0.2527 0.0427  -0.0380 -0.0352 112 LEU A CB  
275  C CG  . LEU A 38  ? 0.2886 0.2484 0.2483 0.0402  -0.0378 -0.0353 112 LEU A CG  
276  C CD1 . LEU A 38  ? 0.3310 0.2864 0.2860 0.0420  -0.0378 -0.0357 112 LEU A CD1 
277  C CD2 . LEU A 38  ? 0.2890 0.2524 0.2529 0.0374  -0.0344 -0.0327 112 LEU A CD2 
278  N N   . TYR A 39  ? 0.2851 0.2474 0.2362 0.0445  -0.0352 -0.0323 113 TYR A N   
279  C CA  . TYR A 39  ? 0.2780 0.2391 0.2242 0.0470  -0.0348 -0.0317 113 TYR A CA  
280  C C   . TYR A 39  ? 0.2846 0.2449 0.2271 0.0478  -0.0311 -0.0289 113 TYR A C   
281  O O   . TYR A 39  ? 0.2760 0.2387 0.2219 0.0454  -0.0285 -0.0271 113 TYR A O   
282  C CB  . TYR A 39  ? 0.2875 0.2521 0.2380 0.0455  -0.0350 -0.0316 113 TYR A CB  
283  C CG  . TYR A 39  ? 0.2900 0.2543 0.2368 0.0475  -0.0343 -0.0307 113 TYR A CG  
284  C CD1 . TYR A 39  ? 0.3038 0.2644 0.2437 0.0511  -0.0352 -0.0311 113 TYR A CD1 
285  C CD2 . TYR A 39  ? 0.2849 0.2525 0.2355 0.0458  -0.0331 -0.0297 113 TYR A CD2 
286  C CE1 . TYR A 39  ? 0.3007 0.2611 0.2377 0.0529  -0.0347 -0.0303 113 TYR A CE1 
287  C CE2 . TYR A 39  ? 0.2973 0.2646 0.2450 0.0475  -0.0325 -0.0289 113 TYR A CE2 
288  C CZ  . TYR A 39  ? 0.3095 0.2732 0.2506 0.0510  -0.0333 -0.0292 113 TYR A CZ  
289  O OH  . TYR A 39  ? 0.3267 0.2901 0.2651 0.0527  -0.0328 -0.0284 113 TYR A OH  
290  N N   . VAL A 40  ? 0.2961 0.2528 0.2317 0.0512  -0.0309 -0.0287 114 VAL A N   
291  C CA  . VAL A 40  ? 0.2944 0.2500 0.2261 0.0524  -0.0274 -0.0261 114 VAL A CA  
292  C C   . VAL A 40  ? 0.2960 0.2496 0.2222 0.0555  -0.0272 -0.0257 114 VAL A C   
293  O O   . VAL A 40  ? 0.3034 0.2564 0.2285 0.0567  -0.0299 -0.0274 114 VAL A O   
294  C CB  . VAL A 40  ? 0.2942 0.2468 0.2227 0.0536  -0.0267 -0.0260 114 VAL A CB  
295  C CG1 . VAL A 40  ? 0.3167 0.2707 0.2504 0.0510  -0.0276 -0.0270 114 VAL A CG1 
296  C CG2 . VAL A 40  ? 0.3284 0.2762 0.2498 0.0576  -0.0287 -0.0276 114 VAL A CG2 
297  N N   . ASN A 41  ? 0.3190 0.2719 0.2422 0.0566  -0.0239 -0.0231 115 ASN A N   
298  C CA  . ASN A 41  ? 0.3273 0.2781 0.2450 0.0597  -0.0232 -0.0222 115 ASN A CA  
299  C C   . ASN A 41  ? 0.3365 0.2824 0.2467 0.0636  -0.0240 -0.0230 115 ASN A C   
300  O O   . ASN A 41  ? 0.3680 0.3118 0.2746 0.0660  -0.0266 -0.0248 115 ASN A O   
301  C CB  . ASN A 41  ? 0.3280 0.2802 0.2462 0.0591  -0.0193 -0.0190 115 ASN A CB  
302  C CG  . ASN A 41  ? 0.3742 0.3246 0.2877 0.0619  -0.0184 -0.0180 115 ASN A CG  
303  O OD1 . ASN A 41  ? 0.4028 0.3517 0.3136 0.0638  -0.0209 -0.0197 115 ASN A OD1 
304  N ND2 . ASN A 41  ? 0.4063 0.3569 0.3190 0.0621  -0.0149 -0.0151 115 ASN A ND2 
305  N N   . LYS A 42  ? 0.3232 0.2674 0.2312 0.0644  -0.0218 -0.0217 116 LYS A N   
306  C CA  . LYS A 42  ? 0.3747 0.3140 0.2750 0.0684  -0.0219 -0.0221 116 LYS A CA  
307  C C   . LYS A 42  ? 0.3778 0.3155 0.2776 0.0684  -0.0215 -0.0223 116 LYS A C   
308  O O   . LYS A 42  ? 0.3804 0.3137 0.2735 0.0717  -0.0215 -0.0227 116 LYS A O   
309  C CB  . LYS A 42  ? 0.4455 0.3834 0.3412 0.0709  -0.0189 -0.0194 116 LYS A CB  
310  C CG  . LYS A 42  ? 0.5279 0.4674 0.4254 0.0699  -0.0145 -0.0160 116 LYS A CG  
311  C CD  . LYS A 42  ? 0.6350 0.5736 0.5291 0.0720  -0.0122 -0.0138 116 LYS A CD  
312  C CE  . LYS A 42  ? 0.7397 0.6777 0.6324 0.0730  -0.0080 -0.0106 116 LYS A CE  
313  N NZ  . LYS A 42  ? 0.7913 0.7330 0.6906 0.0693  -0.0062 -0.0092 116 LYS A NZ  
314  N N   . SER A 43  ? 0.3577 0.2982 0.2636 0.0650  -0.0211 -0.0222 117 SER A N   
315  C CA  . SER A 43  ? 0.3506 0.2897 0.2562 0.0648  -0.0204 -0.0221 117 SER A CA  
316  C C   . SER A 43  ? 0.3515 0.2881 0.2561 0.0654  -0.0243 -0.0256 117 SER A C   
317  O O   . SER A 43  ? 0.3421 0.2804 0.2518 0.0627  -0.0257 -0.0268 117 SER A O   
318  C CB  . SER A 43  ? 0.3526 0.2958 0.2652 0.0610  -0.0184 -0.0205 117 SER A CB  
319  O OG  . SER A 43  ? 0.3550 0.2998 0.2680 0.0608  -0.0146 -0.0172 117 SER A OG  
320  N N   . VAL A 44  ? 0.3793 0.3115 0.2768 0.0691  -0.0260 -0.0271 118 VAL A N   
321  C CA  . VAL A 44  ? 0.4052 0.3348 0.3011 0.0700  -0.0304 -0.0306 118 VAL A CA  
322  C C   . VAL A 44  ? 0.3810 0.3086 0.2771 0.0697  -0.0307 -0.0316 118 VAL A C   
323  O O   . VAL A 44  ? 0.3810 0.3091 0.2810 0.0677  -0.0337 -0.0340 118 VAL A O   
324  C CB  . VAL A 44  ? 0.4398 0.3651 0.3274 0.0744  -0.0321 -0.0319 118 VAL A CB  
325  C CG1 . VAL A 44  ? 0.4586 0.3796 0.3384 0.0781  -0.0292 -0.0302 118 VAL A CG1 
326  C CG2 . VAL A 44  ? 0.4404 0.3631 0.3269 0.0750  -0.0371 -0.0358 118 VAL A CG2 
327  N N   . ASN A 45  ? 0.3897 0.3152 0.2824 0.0712  -0.0275 -0.0297 119 ASN A N   
328  C CA  . ASN A 45  ? 0.4259 0.3492 0.3185 0.0710  -0.0276 -0.0305 119 ASN A CA  
329  C C   . ASN A 45  ? 0.4135 0.3411 0.3148 0.0666  -0.0273 -0.0300 119 ASN A C   
330  O O   . ASN A 45  ? 0.4050 0.3319 0.3088 0.0652  -0.0294 -0.0320 119 ASN A O   
331  C CB  . ASN A 45  ? 0.4476 0.3679 0.3346 0.0739  -0.0240 -0.0283 119 ASN A CB  
332  C CG  . ASN A 45  ? 0.4970 0.4123 0.3747 0.0786  -0.0247 -0.0291 119 ASN A CG  
333  O OD1 . ASN A 45  ? 0.5360 0.4512 0.4104 0.0806  -0.0223 -0.0270 119 ASN A OD1 
334  N ND2 . ASN A 45  ? 0.5349 0.4459 0.4084 0.0805  -0.0283 -0.0324 119 ASN A ND2 
335  N N   . GLU A 46  ? 0.3777 0.3100 0.2839 0.0642  -0.0246 -0.0274 120 GLU A N   
336  C CA  . GLU A 46  ? 0.3704 0.3067 0.2843 0.0601  -0.0239 -0.0266 120 GLU A CA  
337  C C   . GLU A 46  ? 0.3327 0.2713 0.2519 0.0576  -0.0274 -0.0291 120 GLU A C   
338  O O   . GLU A 46  ? 0.3529 0.2928 0.2772 0.0550  -0.0282 -0.0298 120 GLU A O   
339  C CB  . GLU A 46  ? 0.3807 0.3209 0.2976 0.0585  -0.0202 -0.0232 120 GLU A CB  
340  C CG  . GLU A 46  ? 0.3834 0.3217 0.2959 0.0609  -0.0166 -0.0206 120 GLU A CG  
341  C CD  . GLU A 46  ? 0.3841 0.3197 0.2897 0.0647  -0.0156 -0.0199 120 GLU A CD  
342  O OE1 . GLU A 46  ? 0.4099 0.3441 0.3122 0.0664  -0.0175 -0.0213 120 GLU A OE1 
343  O OE2 . GLU A 46  ? 0.5307 0.4654 0.4341 0.0661  -0.0123 -0.0173 120 GLU A OE2 
344  N N   . LEU A 47  ? 0.3470 0.2861 0.2653 0.0583  -0.0292 -0.0301 121 LEU A N   
345  C CA  . LEU A 47  ? 0.3542 0.2952 0.2774 0.0562  -0.0327 -0.0325 121 LEU A CA  
346  C C   . LEU A 47  ? 0.3648 0.3024 0.2869 0.0569  -0.0362 -0.0356 121 LEU A C   
347  O O   . LEU A 47  ? 0.3649 0.3044 0.2930 0.0543  -0.0379 -0.0370 121 LEU A O   
348  C CB  . LEU A 47  ? 0.3497 0.2915 0.2715 0.0573  -0.0341 -0.0331 121 LEU A CB  
349  C CG  . LEU A 47  ? 0.3380 0.2816 0.2647 0.0555  -0.0379 -0.0357 121 LEU A CG  
350  C CD1 . LEU A 47  ? 0.3286 0.2770 0.2638 0.0513  -0.0370 -0.0349 121 LEU A CD1 
351  C CD2 . LEU A 47  ? 0.3412 0.2851 0.2656 0.0572  -0.0391 -0.0361 121 LEU A CD2 
352  N N   . TYR A 48  ? 0.4143 0.3470 0.3289 0.0606  -0.0370 -0.0366 122 TYR A N   
353  C CA  . TYR A 48  ? 0.4248 0.3536 0.3376 0.0615  -0.0402 -0.0396 122 TYR A CA  
354  C C   . TYR A 48  ? 0.3693 0.2987 0.2866 0.0591  -0.0393 -0.0393 122 TYR A C   
355  O O   . TYR A 48  ? 0.3899 0.3195 0.3117 0.0572  -0.0420 -0.0415 122 TYR A O   
356  C CB  . TYR A 48  ? 0.4247 0.3478 0.3278 0.0661  -0.0404 -0.0403 122 TYR A CB  
357  C CG  . TYR A 48  ? 0.4712 0.3897 0.3717 0.0672  -0.0424 -0.0426 122 TYR A CG  
358  C CD1 . TYR A 48  ? 0.5045 0.4217 0.4068 0.0666  -0.0470 -0.0461 122 TYR A CD1 
359  C CD2 . TYR A 48  ? 0.5130 0.4287 0.4096 0.0688  -0.0396 -0.0412 122 TYR A CD2 
360  C CE1 . TYR A 48  ? 0.5312 0.4438 0.4308 0.0677  -0.0490 -0.0484 122 TYR A CE1 
361  C CE2 . TYR A 48  ? 0.5525 0.4637 0.4464 0.0700  -0.0414 -0.0434 122 TYR A CE2 
362  C CZ  . TYR A 48  ? 0.5873 0.4970 0.4828 0.0693  -0.0461 -0.0470 122 TYR A CZ  
363  O OH  . TYR A 48  ? 0.6479 0.5530 0.5410 0.0703  -0.0482 -0.0494 122 TYR A OH  
364  N N   . GLU A 49  ? 0.3581 0.2879 0.2748 0.0590  -0.0353 -0.0365 123 GLU A N   
365  C CA  . GLU A 49  ? 0.3845 0.3151 0.3055 0.0568  -0.0341 -0.0360 123 GLU A CA  
366  C C   . GLU A 49  ? 0.3893 0.3247 0.3192 0.0526  -0.0347 -0.0359 123 GLU A C   
367  O O   . GLU A 49  ? 0.4009 0.3363 0.3351 0.0506  -0.0358 -0.0369 123 GLU A O   
368  C CB  . GLU A 49  ? 0.4193 0.3497 0.3382 0.0576  -0.0297 -0.0328 123 GLU A CB  
369  C CG  . GLU A 49  ? 0.4669 0.3921 0.3770 0.0620  -0.0289 -0.0328 123 GLU A CG  
370  C CD  . GLU A 49  ? 0.5057 0.4259 0.4125 0.0636  -0.0310 -0.0353 123 GLU A CD  
371  O OE1 . GLU A 49  ? 0.5417 0.4624 0.4535 0.0611  -0.0327 -0.0367 123 GLU A OE1 
372  O OE2 . GLU A 49  ? 0.5787 0.4942 0.4776 0.0674  -0.0307 -0.0357 123 GLU A OE2 
373  N N   . GLN A 50  ? 0.3590 0.2986 0.2921 0.0510  -0.0337 -0.0345 124 GLN A N   
374  C CA  . GLN A 50  ? 0.3420 0.2861 0.2832 0.0472  -0.0341 -0.0344 124 GLN A CA  
375  C C   . GLN A 50  ? 0.3388 0.2824 0.2829 0.0465  -0.0384 -0.0377 124 GLN A C   
376  O O   . GLN A 50  ? 0.3461 0.2916 0.2965 0.0437  -0.0392 -0.0382 124 GLN A O   
377  C CB  . GLN A 50  ? 0.3425 0.2907 0.2856 0.0462  -0.0322 -0.0324 124 GLN A CB  
378  C CG  . GLN A 50  ? 0.3318 0.2816 0.2744 0.0458  -0.0281 -0.0291 124 GLN A CG  
379  C CD  . GLN A 50  ? 0.3167 0.2702 0.2612 0.0447  -0.0265 -0.0273 124 GLN A CD  
380  O OE1 . GLN A 50  ? 0.3149 0.2689 0.2591 0.0452  -0.0282 -0.0285 124 GLN A OE1 
381  N NE2 . GLN A 50  ? 0.3204 0.2763 0.2668 0.0433  -0.0233 -0.0246 124 GLN A NE2 
382  N N   . ALA A 51  ? 0.3365 0.2776 0.2760 0.0491  -0.0411 -0.0397 125 ALA A N   
383  C CA  . ALA A 51  ? 0.3766 0.3169 0.3182 0.0489  -0.0455 -0.0429 125 ALA A CA  
384  C C   . ALA A 51  ? 0.4119 0.3492 0.3545 0.0484  -0.0473 -0.0448 125 ALA A C   
385  O O   . ALA A 51  ? 0.3866 0.3254 0.3355 0.0460  -0.0496 -0.0463 125 ALA A O   
386  C CB  . ALA A 51  ? 0.3994 0.3368 0.3345 0.0523  -0.0478 -0.0444 125 ALA A CB  
387  N N   . ARG A 52  ? 0.4157 0.3491 0.3527 0.0506  -0.0459 -0.0444 126 ARG A N   
388  C CA  . ARG A 52  ? 0.4323 0.3624 0.3698 0.0503  -0.0476 -0.0462 126 ARG A CA  
389  C C   . ARG A 52  ? 0.4274 0.3608 0.3729 0.0466  -0.0460 -0.0450 126 ARG A C   
390  O O   . ARG A 52  ? 0.4440 0.3765 0.3935 0.0450  -0.0483 -0.0468 126 ARG A O   
391  C CB  . ARG A 52  ? 0.4748 0.3999 0.4043 0.0537  -0.0461 -0.0459 126 ARG A CB  
392  C CG  . ARG A 52  ? 0.5071 0.4285 0.4369 0.0534  -0.0474 -0.0475 126 ARG A CG  
393  C CD  . ARG A 52  ? 0.5368 0.4530 0.4584 0.0570  -0.0458 -0.0473 126 ARG A CD  
394  N NE  . ARG A 52  ? 0.5175 0.4294 0.4313 0.0607  -0.0484 -0.0494 126 ARG A NE  
395  C CZ  . ARG A 52  ? 0.5014 0.4094 0.4133 0.0617  -0.0529 -0.0531 126 ARG A CZ  
396  N NH1 . ARG A 52  ? 0.5067 0.4144 0.4241 0.0594  -0.0551 -0.0549 126 ARG A NH1 
397  N NH2 . ARG A 52  ? 0.4699 0.3745 0.3747 0.0651  -0.0551 -0.0548 126 ARG A NH2 
398  N N   . GLU A 53  ? 0.3676 0.3048 0.3156 0.0450  -0.0421 -0.0417 127 GLU A N   
399  C CA  . GLU A 53  ? 0.3693 0.3096 0.3244 0.0416  -0.0405 -0.0404 127 GLU A CA  
400  C C   . GLU A 53  ? 0.4180 0.3623 0.3808 0.0386  -0.0422 -0.0412 127 GLU A C   
401  O O   . GLU A 53  ? 0.4135 0.3585 0.3819 0.0363  -0.0432 -0.0419 127 GLU A O   
402  C CB  . GLU A 53  ? 0.3939 0.3368 0.3491 0.0409  -0.0361 -0.0368 127 GLU A CB  
403  C CG  . GLU A 53  ? 0.4039 0.3501 0.3662 0.0375  -0.0344 -0.0353 127 GLU A CG  
404  C CD  . GLU A 53  ? 0.4399 0.3883 0.4024 0.0367  -0.0303 -0.0319 127 GLU A CD  
405  O OE1 . GLU A 53  ? 0.4731 0.4209 0.4306 0.0388  -0.0284 -0.0304 127 GLU A OE1 
406  O OE2 . GLU A 53  ? 0.4762 0.4268 0.4440 0.0341  -0.0290 -0.0306 127 GLU A OE2 
407  N N   . PHE A 54  ? 0.3943 0.3416 0.3575 0.0385  -0.0421 -0.0406 128 PHE A N   
408  C CA  . PHE A 54  ? 0.3680 0.3198 0.3386 0.0356  -0.0427 -0.0406 128 PHE A CA  
409  C C   . PHE A 54  ? 0.3760 0.3273 0.3487 0.0357  -0.0470 -0.0436 128 PHE A C   
410  O O   . PHE A 54  ? 0.4077 0.3622 0.3874 0.0332  -0.0479 -0.0440 128 PHE A O   
411  C CB  . PHE A 54  ? 0.3329 0.2883 0.3033 0.0352  -0.0398 -0.0380 128 PHE A CB  
412  C CG  . PHE A 54  ? 0.3225 0.2797 0.2940 0.0338  -0.0359 -0.0351 128 PHE A CG  
413  C CD1 . PHE A 54  ? 0.3238 0.2841 0.3019 0.0306  -0.0347 -0.0340 128 PHE A CD1 
414  C CD2 . PHE A 54  ? 0.3244 0.2799 0.2901 0.0357  -0.0334 -0.0333 128 PHE A CD2 
415  C CE1 . PHE A 54  ? 0.3465 0.3083 0.3252 0.0295  -0.0313 -0.0313 128 PHE A CE1 
416  C CE2 . PHE A 54  ? 0.3141 0.2712 0.2810 0.0345  -0.0301 -0.0306 128 PHE A CE2 
417  C CZ  . PHE A 54  ? 0.3333 0.2934 0.3065 0.0314  -0.0292 -0.0297 128 PHE A CZ  
418  N N   . LEU A 55  ? 0.3874 0.3349 0.3538 0.0388  -0.0495 -0.0456 129 LEU A N   
419  C CA  . LEU A 55  ? 0.3956 0.3421 0.3631 0.0394  -0.0540 -0.0487 129 LEU A CA  
420  C C   . LEU A 55  ? 0.3932 0.3445 0.3663 0.0377  -0.0545 -0.0484 129 LEU A C   
421  O O   . LEU A 55  ? 0.3722 0.3250 0.3514 0.0360  -0.0572 -0.0501 129 LEU A O   
422  C CB  . LEU A 55  ? 0.4316 0.3759 0.4027 0.0383  -0.0568 -0.0510 129 LEU A CB  
423  C CG  . LEU A 55  ? 0.4258 0.3647 0.3909 0.0403  -0.0567 -0.0517 129 LEU A CG  
424  C CD1 . LEU A 55  ? 0.4688 0.4062 0.4388 0.0385  -0.0586 -0.0534 129 LEU A CD1 
425  C CD2 . LEU A 55  ? 0.4240 0.3585 0.3805 0.0442  -0.0591 -0.0536 129 LEU A CD2 
426  N N   . PRO A 56  ? 0.3544 0.3079 0.3254 0.0383  -0.0521 -0.0464 130 PRO A N   
427  C CA  . PRO A 56  ? 0.3406 0.2984 0.3165 0.0369  -0.0526 -0.0462 130 PRO A CA  
428  C C   . PRO A 56  ? 0.3706 0.3273 0.3460 0.0384  -0.0570 -0.0490 130 PRO A C   
429  O O   . PRO A 56  ? 0.3757 0.3285 0.3444 0.0414  -0.0591 -0.0505 130 PRO A O   
430  C CB  . PRO A 56  ? 0.3321 0.2911 0.3038 0.0379  -0.0492 -0.0436 130 PRO A CB  
431  C CG  . PRO A 56  ? 0.3505 0.3050 0.3136 0.0411  -0.0487 -0.0435 130 PRO A CG  
432  C CD  . PRO A 56  ? 0.3502 0.3020 0.3139 0.0405  -0.0492 -0.0444 130 PRO A CD  
433  N N   . GLU A 57  ? 0.3539 0.3145 0.3361 0.0365  -0.0583 -0.0494 131 GLU A N   
434  C CA  . GLU A 57  ? 0.3530 0.3135 0.3356 0.0378  -0.0623 -0.0517 131 GLU A CA  
435  C C   . GLU A 57  ? 0.3841 0.3432 0.3592 0.0410  -0.0621 -0.0514 131 GLU A C   
436  O O   . GLU A 57  ? 0.3971 0.3538 0.3688 0.0433  -0.0657 -0.0535 131 GLU A O   
437  C CB  . GLU A 57  ? 0.4280 0.3934 0.4199 0.0350  -0.0627 -0.0516 131 GLU A CB  
438  C CG  . GLU A 57  ? 0.5108 0.4771 0.5041 0.0362  -0.0666 -0.0537 131 GLU A CG  
439  C CD  . GLU A 57  ? 0.6152 0.5864 0.6182 0.0335  -0.0669 -0.0535 131 GLU A CD  
440  O OE1 . GLU A 57  ? 0.6702 0.6447 0.6780 0.0309  -0.0635 -0.0514 131 GLU A OE1 
441  O OE2 . GLU A 57  ? 0.6902 0.6619 0.6958 0.0340  -0.0708 -0.0556 131 GLU A OE2 
442  N N   . TYR A 58  ? 0.3352 0.2959 0.3081 0.0410  -0.0581 -0.0486 132 TYR A N   
443  C CA  . TYR A 58  ? 0.3073 0.2671 0.2739 0.0438  -0.0576 -0.0479 132 TYR A CA  
444  C C   . TYR A 58  ? 0.3035 0.2607 0.2631 0.0454  -0.0542 -0.0459 132 TYR A C   
445  O O   . TYR A 58  ? 0.3124 0.2708 0.2738 0.0436  -0.0509 -0.0439 132 TYR A O   
446  C CB  . TYR A 58  ? 0.3112 0.2753 0.2813 0.0426  -0.0556 -0.0462 132 TYR A CB  
447  C CG  . TYR A 58  ? 0.3411 0.3082 0.3178 0.0414  -0.0584 -0.0476 132 TYR A CG  
448  C CD1 . TYR A 58  ? 0.3635 0.3339 0.3487 0.0381  -0.0582 -0.0476 132 TYR A CD1 
449  C CD2 . TYR A 58  ? 0.3669 0.3334 0.3412 0.0436  -0.0612 -0.0490 132 TYR A CD2 
450  C CE1 . TYR A 58  ? 0.3743 0.3478 0.3660 0.0370  -0.0606 -0.0488 132 TYR A CE1 
451  C CE2 . TYR A 58  ? 0.3691 0.3386 0.3498 0.0426  -0.0637 -0.0502 132 TYR A CE2 
452  C CZ  . TYR A 58  ? 0.3717 0.3448 0.3612 0.0393  -0.0634 -0.0501 132 TYR A CZ  
453  O OH  . TYR A 58  ? 0.4693 0.4454 0.4653 0.0383  -0.0657 -0.0513 132 TYR A OH  
454  N N   . LEU A 59  ? 0.3307 0.2846 0.2825 0.0489  -0.0549 -0.0462 133 LEU A N   
455  C CA  . LEU A 59  ? 0.3198 0.2714 0.2648 0.0509  -0.0515 -0.0441 133 LEU A CA  
456  C C   . LEU A 59  ? 0.3341 0.2859 0.2751 0.0531  -0.0510 -0.0432 133 LEU A C   
457  O O   . LEU A 59  ? 0.3488 0.2999 0.2886 0.0547  -0.0543 -0.0451 133 LEU A O   
458  C CB  . LEU A 59  ? 0.3462 0.2926 0.2844 0.0536  -0.0526 -0.0453 133 LEU A CB  
459  C CG  . LEU A 59  ? 0.3117 0.2571 0.2527 0.0519  -0.0529 -0.0460 133 LEU A CG  
460  C CD1 . LEU A 59  ? 0.3653 0.3050 0.2990 0.0551  -0.0548 -0.0479 133 LEU A CD1 
461  C CD2 . LEU A 59  ? 0.3422 0.2896 0.2856 0.0498  -0.0486 -0.0433 133 LEU A CD2 
462  N N   . CYS A 60  ? 0.3297 0.2826 0.2689 0.0531  -0.0471 -0.0404 134 CYS A N   
463  C CA  . CYS A 60  ? 0.3241 0.2768 0.2593 0.0552  -0.0464 -0.0394 134 CYS A CA  
464  C C   . CYS A 60  ? 0.3283 0.2791 0.2578 0.0569  -0.0426 -0.0368 134 CYS A C   
465  O O   . CYS A 60  ? 0.3255 0.2776 0.2572 0.0550  -0.0396 -0.0350 134 CYS A O   
466  C CB  . CYS A 60  ? 0.3428 0.3000 0.2840 0.0530  -0.0460 -0.0388 134 CYS A CB  
467  S SG  . CYS A 60  ? 0.3573 0.3143 0.2943 0.0557  -0.0458 -0.0380 134 CYS A SG  
468  N N   . ILE A 61  ? 0.3351 0.2829 0.2576 0.0604  -0.0428 -0.0367 135 ILE A N   
469  C CA  . ILE A 61  ? 0.3379 0.2840 0.2551 0.0622  -0.0390 -0.0341 135 ILE A CA  
470  C C   . ILE A 61  ? 0.3455 0.2920 0.2604 0.0638  -0.0382 -0.0328 135 ILE A C   
471  O O   . ILE A 61  ? 0.3603 0.3056 0.2728 0.0658  -0.0410 -0.0345 135 ILE A O   
472  C CB  . ILE A 61  ? 0.3475 0.2886 0.2575 0.0654  -0.0393 -0.0346 135 ILE A CB  
473  C CG1 . ILE A 61  ? 0.3588 0.2986 0.2649 0.0666  -0.0348 -0.0316 135 ILE A CG1 
474  C CG2 . ILE A 61  ? 0.3889 0.3263 0.2926 0.0691  -0.0426 -0.0368 135 ILE A CG2 
475  C CD1 . ILE A 61  ? 0.3757 0.3117 0.2773 0.0683  -0.0342 -0.0318 135 ILE A CD1 
476  N N   . HIS A 62  ? 0.3405 0.2889 0.2564 0.0628  -0.0344 -0.0300 136 HIS A N   
477  C CA  . HIS A 62  ? 0.3365 0.2859 0.2516 0.0636  -0.0335 -0.0288 136 HIS A CA  
478  C C   . HIS A 62  ? 0.3677 0.3129 0.2744 0.0680  -0.0335 -0.0285 136 HIS A C   
479  O O   . HIS A 62  ? 0.4111 0.3560 0.3161 0.0696  -0.0350 -0.0291 136 HIS A O   
480  C CB  . HIS A 62  ? 0.3272 0.2795 0.2457 0.0613  -0.0295 -0.0260 136 HIS A CB  
481  C CG  . HIS A 62  ? 0.3248 0.2788 0.2443 0.0613  -0.0291 -0.0252 136 HIS A CG  
482  N ND1 . HIS A 62  ? 0.3192 0.2763 0.2442 0.0593  -0.0310 -0.0265 136 HIS A ND1 
483  C CD2 . HIS A 62  ? 0.3537 0.3067 0.2698 0.0631  -0.0271 -0.0233 136 HIS A CD2 
484  C CE1 . HIS A 62  ? 0.3574 0.3152 0.2821 0.0598  -0.0302 -0.0256 136 HIS A CE1 
485  N NE2 . HIS A 62  ? 0.3755 0.3309 0.2949 0.0621  -0.0278 -0.0236 136 HIS A NE2 
486  N N   . ASP A 63  ? 0.3835 0.3256 0.2852 0.0699  -0.0314 -0.0274 137 ASP A N   
487  C CA  . ASP A 63  ? 0.4250 0.3630 0.3185 0.0741  -0.0305 -0.0265 137 ASP A CA  
488  C C   . ASP A 63  ? 0.4421 0.3763 0.3302 0.0772  -0.0346 -0.0294 137 ASP A C   
489  O O   . ASP A 63  ? 0.4196 0.3518 0.3064 0.0775  -0.0362 -0.0310 137 ASP A O   
490  C CB  . ASP A 63  ? 0.4514 0.3878 0.3422 0.0748  -0.0266 -0.0240 137 ASP A CB  
491  C CG  . ASP A 63  ? 0.5518 0.4840 0.4342 0.0792  -0.0247 -0.0224 137 ASP A CG  
492  O OD1 . ASP A 63  ? 0.5341 0.4639 0.4117 0.0821  -0.0268 -0.0235 137 ASP A OD1 
493  O OD2 . ASP A 63  ? 0.5809 0.5123 0.4619 0.0797  -0.0211 -0.0201 137 ASP A OD2 
494  N N   . LYS A 64  ? 0.4625 0.3958 0.3475 0.0795  -0.0362 -0.0299 138 LYS A N   
495  C CA  . LYS A 64  ? 0.5478 0.4776 0.4276 0.0825  -0.0405 -0.0327 138 LYS A CA  
496  C C   . LYS A 64  ? 0.5455 0.4702 0.4171 0.0860  -0.0400 -0.0329 138 LYS A C   
497  O O   . LYS A 64  ? 0.5117 0.4336 0.3803 0.0876  -0.0436 -0.0356 138 LYS A O   
498  C CB  . LYS A 64  ? 0.6033 0.5326 0.4799 0.0850  -0.0415 -0.0325 138 LYS A CB  
499  C CG  . LYS A 64  ? 0.7512 0.6847 0.6346 0.0826  -0.0434 -0.0333 138 LYS A CG  
500  C CD  . LYS A 64  ? 0.8287 0.7622 0.7134 0.0828  -0.0488 -0.0368 138 LYS A CD  
501  C CE  . LYS A 64  ? 0.8581 0.7959 0.7496 0.0807  -0.0502 -0.0373 138 LYS A CE  
502  N NZ  . LYS A 64  ? 0.8640 0.8064 0.7637 0.0763  -0.0477 -0.0359 138 LYS A NZ  
503  N N   . SER A 65  ? 0.5246 0.4479 0.3928 0.0873  -0.0355 -0.0299 139 SER A N   
504  C CA  . SER A 65  ? 0.5351 0.4533 0.3949 0.0911  -0.0345 -0.0296 139 SER A CA  
505  C C   . SER A 65  ? 0.5175 0.4346 0.3783 0.0900  -0.0352 -0.0310 139 SER A C   
506  O O   . SER A 65  ? 0.5757 0.4882 0.4293 0.0932  -0.0348 -0.0313 139 SER A O   
507  C CB  . SER A 65  ? 0.5671 0.4844 0.4236 0.0927  -0.0293 -0.0258 139 SER A CB  
508  O OG  . SER A 65  ? 0.5809 0.5015 0.4435 0.0893  -0.0259 -0.0236 139 SER A OG  
509  N N   . VAL A 66  ? 0.4576 0.3786 0.3267 0.0857  -0.0360 -0.0318 140 VAL A N   
510  C CA  . VAL A 66  ? 0.4434 0.3632 0.3135 0.0846  -0.0370 -0.0333 140 VAL A CA  
511  C C   . VAL A 66  ? 0.3818 0.3030 0.2568 0.0824  -0.0417 -0.0368 140 VAL A C   
512  O O   . VAL A 66  ? 0.4299 0.3506 0.3070 0.0810  -0.0426 -0.0380 140 VAL A O   
513  C CB  . VAL A 66  ? 0.5043 0.4265 0.3788 0.0820  -0.0328 -0.0307 140 VAL A CB  
514  C CG1 . VAL A 66  ? 0.5487 0.4684 0.4174 0.0848  -0.0285 -0.0278 140 VAL A CG1 
515  C CG2 . VAL A 66  ? 0.4945 0.4225 0.3778 0.0777  -0.0316 -0.0294 140 VAL A CG2 
516  N N   . TYR A 67  ? 0.4148 0.3375 0.2915 0.0823  -0.0448 -0.0382 141 TYR A N   
517  C CA  . TYR A 67  ? 0.4460 0.3704 0.3281 0.0802  -0.0493 -0.0414 141 TYR A CA  
518  C C   . TYR A 67  ? 0.4564 0.3761 0.3337 0.0824  -0.0532 -0.0445 141 TYR A C   
519  O O   . TYR A 67  ? 0.4405 0.3607 0.3222 0.0801  -0.0553 -0.0465 141 TYR A O   
520  C CB  . TYR A 67  ? 0.4464 0.3730 0.3302 0.0803  -0.0512 -0.0417 141 TYR A CB  
521  C CG  . TYR A 67  ? 0.4597 0.3886 0.3497 0.0782  -0.0558 -0.0447 141 TYR A CG  
522  C CD1 . TYR A 67  ? 0.4540 0.3859 0.3519 0.0743  -0.0565 -0.0455 141 TYR A CD1 
523  C CD2 . TYR A 67  ? 0.5068 0.4350 0.3947 0.0802  -0.0595 -0.0465 141 TYR A CD2 
524  C CE1 . TYR A 67  ? 0.4605 0.3947 0.3645 0.0724  -0.0604 -0.0480 141 TYR A CE1 
525  C CE2 . TYR A 67  ? 0.5398 0.4704 0.4339 0.0783  -0.0638 -0.0490 141 TYR A CE2 
526  C CZ  . TYR A 67  ? 0.5329 0.4665 0.4351 0.0744  -0.0642 -0.0498 141 TYR A CZ  
527  O OH  . TYR A 67  ? 0.5689 0.5050 0.4778 0.0724  -0.0681 -0.0521 141 TYR A OH  
528  N N   . GLU A 68  ? 0.5356 0.4506 0.4036 0.0869  -0.0543 -0.0452 142 GLU A N   
529  C CA  . GLU A 68  ? 0.5436 0.4534 0.4057 0.0896  -0.0577 -0.0481 142 GLU A CA  
530  C C   . GLU A 68  ? 0.5143 0.4221 0.3758 0.0889  -0.0556 -0.0478 142 GLU A C   
531  O O   . GLU A 68  ? 0.5279 0.4346 0.3914 0.0879  -0.0587 -0.0504 142 GLU A O   
532  C CB  . GLU A 68  ? 0.5791 0.4838 0.4303 0.0948  -0.0583 -0.0482 142 GLU A CB  
533  C CG  . GLU A 68  ? 0.5671 0.4730 0.4181 0.0959  -0.0612 -0.0491 142 GLU A CG  
534  C CD  . GLU A 68  ? 0.6085 0.5165 0.4654 0.0939  -0.0668 -0.0525 142 GLU A CD  
535  O OE1 . GLU A 68  ? 0.6384 0.5440 0.4952 0.0936  -0.0700 -0.0553 142 GLU A OE1 
536  O OE2 . GLU A 68  ? 0.7024 0.6142 0.5641 0.0926  -0.0679 -0.0523 142 GLU A OE2 
537  N N   . GLU A 69  ? 0.4839 0.3917 0.3434 0.0894  -0.0505 -0.0444 143 GLU A N   
538  C CA  . GLU A 69  ? 0.5184 0.4249 0.3781 0.0887  -0.0481 -0.0438 143 GLU A CA  
539  C C   . GLU A 69  ? 0.4870 0.3973 0.3564 0.0840  -0.0494 -0.0449 143 GLU A C   
540  O O   . GLU A 69  ? 0.4788 0.3870 0.3483 0.0835  -0.0504 -0.0464 143 GLU A O   
541  C CB  . GLU A 69  ? 0.5062 0.4134 0.3644 0.0892  -0.0423 -0.0397 143 GLU A CB  
542  C CG  . GLU A 69  ? 0.5105 0.4162 0.3683 0.0889  -0.0395 -0.0386 143 GLU A CG  
543  C CD  . GLU A 69  ? 0.5171 0.4231 0.3728 0.0900  -0.0339 -0.0346 143 GLU A CD  
544  O OE1 . GLU A 69  ? 0.6213 0.5288 0.4762 0.0908  -0.0319 -0.0325 143 GLU A OE1 
545  O OE2 . GLU A 69  ? 0.6286 0.5332 0.4835 0.0903  -0.0315 -0.0336 143 GLU A OE2 
546  N N   . LEU A 70  ? 0.4706 0.3865 0.3481 0.0804  -0.0489 -0.0438 144 LEU A N   
547  C CA  . LEU A 70  ? 0.4632 0.3827 0.3497 0.0760  -0.0497 -0.0446 144 LEU A CA  
548  C C   . LEU A 70  ? 0.4279 0.3456 0.3156 0.0757  -0.0550 -0.0485 144 LEU A C   
549  O O   . LEU A 70  ? 0.4267 0.3441 0.3178 0.0739  -0.0556 -0.0496 144 LEU A O   
550  C CB  . LEU A 70  ? 0.4371 0.3626 0.3314 0.0727  -0.0486 -0.0430 144 LEU A CB  
551  C CG  . LEU A 70  ? 0.4238 0.3534 0.3277 0.0681  -0.0493 -0.0437 144 LEU A CG  
552  C CD1 . LEU A 70  ? 0.4261 0.3559 0.3319 0.0665  -0.0463 -0.0421 144 LEU A CD1 
553  C CD2 . LEU A 70  ? 0.4059 0.3409 0.3162 0.0655  -0.0484 -0.0423 144 LEU A CD2 
554  N N   . LYS A 71  ? 0.4705 0.3875 0.3565 0.0773  -0.0588 -0.0506 145 LYS A N   
555  C CA  . LYS A 71  ? 0.5039 0.4191 0.3908 0.0773  -0.0642 -0.0544 145 LYS A CA  
556  C C   . LYS A 71  ? 0.4991 0.4084 0.3796 0.0797  -0.0653 -0.0561 145 LYS A C   
557  O O   . LYS A 71  ? 0.4852 0.3938 0.3693 0.0779  -0.0677 -0.0583 145 LYS A O   
558  C CB  . LYS A 71  ? 0.5203 0.4350 0.4044 0.0795  -0.0677 -0.0560 145 LYS A CB  
559  C CG  . LYS A 71  ? 0.5727 0.4932 0.4651 0.0766  -0.0683 -0.0555 145 LYS A CG  
560  C CD  . LYS A 71  ? 0.6357 0.5559 0.5262 0.0786  -0.0725 -0.0574 145 LYS A CD  
561  C CE  . LYS A 71  ? 0.7055 0.6243 0.5888 0.0820  -0.0703 -0.0554 145 LYS A CE  
562  N NZ  . LYS A 71  ? 0.7533 0.6709 0.6334 0.0846  -0.0744 -0.0573 145 LYS A NZ  
563  N N   . GLU A 72  ? 0.4992 0.4044 0.3704 0.0835  -0.0629 -0.0549 146 GLU A N   
564  C CA  . GLU A 72  ? 0.5483 0.4474 0.4122 0.0864  -0.0639 -0.0566 146 GLU A CA  
565  C C   . GLU A 72  ? 0.5693 0.4690 0.4377 0.0838  -0.0615 -0.0558 146 GLU A C   
566  O O   . GLU A 72  ? 0.5417 0.4386 0.4102 0.0835  -0.0641 -0.0583 146 GLU A O   
567  C CB  . GLU A 72  ? 0.6030 0.4976 0.4560 0.0913  -0.0618 -0.0552 146 GLU A CB  
568  C CG  . GLU A 72  ? 0.6526 0.5458 0.5006 0.0942  -0.0650 -0.0566 146 GLU A CG  
569  C CD  . GLU A 72  ? 0.7482 0.6371 0.5924 0.0961  -0.0711 -0.0609 146 GLU A CD  
570  O OE1 . GLU A 72  ? 0.7536 0.6396 0.5975 0.0958  -0.0728 -0.0631 146 GLU A OE1 
571  O OE2 . GLU A 72  ? 0.8248 0.7134 0.6663 0.0980  -0.0742 -0.0622 146 GLU A OE2 
572  N N   . LEU A 73  ? 0.4887 0.3925 0.3615 0.0815  -0.0568 -0.0523 147 LEU A N   
573  C CA  . LEU A 73  ? 0.4632 0.3679 0.3404 0.0790  -0.0544 -0.0513 147 LEU A CA  
574  C C   . LEU A 73  ? 0.5203 0.4274 0.4062 0.0751  -0.0576 -0.0535 147 LEU A C   
575  O O   . LEU A 73  ? 0.4906 0.3960 0.3779 0.0741  -0.0578 -0.0544 147 LEU A O   
576  C CB  . LEU A 73  ? 0.4813 0.3903 0.3620 0.0772  -0.0491 -0.0472 147 LEU A CB  
577  C CG  . LEU A 73  ? 0.5342 0.4407 0.4077 0.0804  -0.0448 -0.0444 147 LEU A CG  
578  C CD1 . LEU A 73  ? 0.5503 0.4617 0.4284 0.0783  -0.0402 -0.0405 147 LEU A CD1 
579  C CD2 . LEU A 73  ? 0.5588 0.4610 0.4286 0.0819  -0.0439 -0.0449 147 LEU A CD2 
580  N N   . VAL A 74  ? 0.4841 0.3958 0.3766 0.0726  -0.0594 -0.0539 148 VAL A N   
581  C CA  . VAL A 74  ? 0.4838 0.3989 0.3858 0.0685  -0.0615 -0.0552 148 VAL A CA  
582  C C   . VAL A 74  ? 0.5094 0.4206 0.4103 0.0693  -0.0667 -0.0593 148 VAL A C   
583  O O   . VAL A 74  ? 0.4723 0.3843 0.3795 0.0665  -0.0682 -0.0606 148 VAL A O   
584  C CB  . VAL A 74  ? 0.4790 0.4000 0.3881 0.0659  -0.0615 -0.0543 148 VAL A CB  
585  C CG1 . VAL A 74  ? 0.4971 0.4213 0.4158 0.0620  -0.0642 -0.0559 148 VAL A CG1 
586  C CG2 . VAL A 74  ? 0.5015 0.4262 0.4125 0.0645  -0.0563 -0.0504 148 VAL A CG2 
587  N N   . LYS A 75  ? 0.5403 0.4469 0.4329 0.0732  -0.0694 -0.0612 149 LYS A N   
588  C CA  . LYS A 75  ? 0.6006 0.5024 0.4903 0.0747  -0.0744 -0.0651 149 LYS A CA  
589  C C   . LYS A 75  ? 0.5893 0.4880 0.4788 0.0741  -0.0735 -0.0657 149 LYS A C   
590  O O   . LYS A 75  ? 0.5792 0.4754 0.4703 0.0735  -0.0776 -0.0689 149 LYS A O   
591  C CB  . LYS A 75  ? 0.6544 0.5509 0.5332 0.0797  -0.0765 -0.0666 149 LYS A CB  
592  C CG  . LYS A 75  ? 0.7137 0.6123 0.5918 0.0808  -0.0784 -0.0668 149 LYS A CG  
593  C CD  . LYS A 75  ? 0.7856 0.6785 0.6538 0.0854  -0.0823 -0.0694 149 LYS A CD  
594  C CE  . LYS A 75  ? 0.8084 0.7028 0.6736 0.0875  -0.0824 -0.0684 149 LYS A CE  
595  N NZ  . LYS A 75  ? 0.8306 0.7312 0.7054 0.0840  -0.0835 -0.0681 149 LYS A NZ  
596  N N   . ASN A 76  ? 0.5345 0.4330 0.4218 0.0745  -0.0685 -0.0627 150 ASN A N   
597  C CA  . ASN A 76  ? 0.5275 0.4227 0.4138 0.0744  -0.0672 -0.0629 150 ASN A CA  
598  C C   . ASN A 76  ? 0.4990 0.3981 0.3957 0.0697  -0.0667 -0.0625 150 ASN A C   
599  O O   . ASN A 76  ? 0.4981 0.3950 0.3950 0.0692  -0.0654 -0.0624 150 ASN A O   
600  C CB  . ASN A 76  ? 0.5811 0.4750 0.4620 0.0764  -0.0618 -0.0596 150 ASN A CB  
601  C CG  . ASN A 76  ? 0.6342 0.5232 0.5038 0.0815  -0.0616 -0.0598 150 ASN A CG  
602  O OD1 . ASN A 76  ? 0.6972 0.5879 0.5641 0.0829  -0.0588 -0.0573 150 ASN A OD1 
603  N ND2 . ASN A 76  ? 0.6670 0.5498 0.5299 0.0843  -0.0645 -0.0627 150 ASN A ND2 
604  N N   . ILE A 77  ? 0.4886 0.3936 0.3938 0.0663  -0.0670 -0.0618 151 ILE A N   
605  C CA  . ILE A 77  ? 0.4674 0.3761 0.3825 0.0619  -0.0667 -0.0615 151 ILE A CA  
606  C C   . ILE A 77  ? 0.5246 0.4325 0.4441 0.0606  -0.0722 -0.0652 151 ILE A C   
607  O O   . ILE A 77  ? 0.4982 0.4085 0.4202 0.0602  -0.0749 -0.0663 151 ILE A O   
608  C CB  . ILE A 77  ? 0.4254 0.3410 0.3475 0.0589  -0.0637 -0.0584 151 ILE A CB  
609  C CG1 . ILE A 77  ? 0.4456 0.3622 0.3638 0.0601  -0.0584 -0.0547 151 ILE A CG1 
610  C CG2 . ILE A 77  ? 0.4199 0.3388 0.3518 0.0546  -0.0634 -0.0582 151 ILE A CG2 
611  C CD1 . ILE A 77  ? 0.4287 0.3513 0.3518 0.0580  -0.0560 -0.0521 151 ILE A CD1 
612  N N   . LYS A 78  ? 0.5743 0.4790 0.4950 0.0600  -0.0738 -0.0671 152 LYS A N   
613  C CA  . LYS A 78  ? 0.6118 0.5151 0.5363 0.0589  -0.0793 -0.0708 152 LYS A CA  
614  C C   . LYS A 78  ? 0.6160 0.5255 0.5524 0.0544  -0.0799 -0.0704 152 LYS A C   
615  O O   . LYS A 78  ? 0.6332 0.5467 0.5752 0.0517  -0.0760 -0.0675 152 LYS A O   
616  C CB  . LYS A 78  ? 0.6427 0.5403 0.5645 0.0596  -0.0805 -0.0728 152 LYS A CB  
617  C CG  . LYS A 78  ? 0.6888 0.5796 0.5985 0.0645  -0.0810 -0.0741 152 LYS A CG  
618  C CD  . LYS A 78  ? 0.7288 0.6175 0.6324 0.0676  -0.0850 -0.0764 152 LYS A CD  
619  C CE  . LYS A 78  ? 0.7270 0.6090 0.6180 0.0726  -0.0851 -0.0773 152 LYS A CE  
620  N NZ  . LYS A 78  ? 0.6547 0.5373 0.5402 0.0746  -0.0795 -0.0736 152 LYS A NZ  
621  N N   . ASP A 79  ? 0.6046 0.5146 0.5447 0.0538  -0.0848 -0.0732 153 ASP A N   
622  C CA  . ASP A 79  ? 0.6001 0.5152 0.5517 0.0497  -0.0861 -0.0734 153 ASP A CA  
623  C C   . ASP A 79  ? 0.5748 0.4962 0.5307 0.0481  -0.0827 -0.0702 153 ASP A C   
624  O O   . ASP A 79  ? 0.5933 0.5194 0.5584 0.0445  -0.0814 -0.0689 153 ASP A O   
625  C CB  . ASP A 79  ? 0.6212 0.5361 0.5792 0.0467  -0.0852 -0.0733 153 ASP A CB  
626  C CG  . ASP A 79  ? 0.6960 0.6050 0.6521 0.0475  -0.0892 -0.0768 153 ASP A CG  
627  O OD1 . ASP A 79  ? 0.7262 0.6322 0.6785 0.0497  -0.0939 -0.0799 153 ASP A OD1 
628  O OD2 . ASP A 79  ? 0.7808 0.6883 0.7392 0.0461  -0.0877 -0.0764 153 ASP A OD2 
629  N N   . TYR A 80  ? 0.5432 0.4646 0.4922 0.0508  -0.0814 -0.0690 154 TYR A N   
630  C CA  . TYR A 80  ? 0.4837 0.4104 0.4352 0.0498  -0.0778 -0.0659 154 TYR A CA  
631  C C   . TYR A 80  ? 0.4750 0.4019 0.4223 0.0522  -0.0799 -0.0667 154 TYR A C   
632  O O   . TYR A 80  ? 0.5034 0.4261 0.4413 0.0560  -0.0803 -0.0672 154 TYR A O   
633  C CB  . TYR A 80  ? 0.4696 0.3959 0.4166 0.0505  -0.0724 -0.0627 154 TYR A CB  
634  C CG  . TYR A 80  ? 0.4751 0.4064 0.4241 0.0494  -0.0684 -0.0593 154 TYR A CG  
635  C CD1 . TYR A 80  ? 0.4434 0.3803 0.4016 0.0459  -0.0677 -0.0583 154 TYR A CD1 
636  C CD2 . TYR A 80  ? 0.4791 0.4094 0.4208 0.0519  -0.0652 -0.0572 154 TYR A CD2 
637  C CE1 . TYR A 80  ? 0.4094 0.3505 0.3690 0.0450  -0.0640 -0.0553 154 TYR A CE1 
638  C CE2 . TYR A 80  ? 0.4380 0.3726 0.3814 0.0509  -0.0617 -0.0542 154 TYR A CE2 
639  C CZ  . TYR A 80  ? 0.4357 0.3756 0.3879 0.0475  -0.0612 -0.0534 154 TYR A CZ  
640  O OH  . TYR A 80  ? 0.3900 0.3338 0.3435 0.0466  -0.0578 -0.0506 154 TYR A OH  
641  N N   . LYS A 81  ? 0.4683 0.3999 0.4227 0.0503  -0.0812 -0.0667 155 LYS A N   
642  C CA  . LYS A 81  ? 0.4929 0.4252 0.4444 0.0525  -0.0835 -0.0674 155 LYS A CA  
643  C C   . LYS A 81  ? 0.4861 0.4242 0.4422 0.0507  -0.0804 -0.0647 155 LYS A C   
644  O O   . LYS A 81  ? 0.4889 0.4308 0.4518 0.0491  -0.0822 -0.0652 155 LYS A O   
645  C CB  . LYS A 81  ? 0.5602 0.4917 0.5149 0.0525  -0.0895 -0.0711 155 LYS A CB  
646  C CG  . LYS A 81  ? 0.6171 0.5422 0.5659 0.0547  -0.0933 -0.0742 155 LYS A CG  
647  C CD  . LYS A 81  ? 0.6692 0.5892 0.6055 0.0594  -0.0934 -0.0746 155 LYS A CD  
648  C CE  . LYS A 81  ? 0.7006 0.6140 0.6308 0.0618  -0.0973 -0.0779 155 LYS A CE  
649  N NZ  . LYS A 81  ? 0.7301 0.6412 0.6609 0.0605  -0.0953 -0.0777 155 LYS A NZ  
650  N N   . PRO A 82  ? 0.4287 0.3674 0.3810 0.0513  -0.0755 -0.0616 156 PRO A N   
651  C CA  . PRO A 82  ? 0.4176 0.3613 0.3736 0.0498  -0.0725 -0.0590 156 PRO A CA  
652  C C   . PRO A 82  ? 0.4101 0.3543 0.3628 0.0522  -0.0742 -0.0594 156 PRO A C   
653  O O   . PRO A 82  ? 0.4470 0.3872 0.3927 0.0555  -0.0769 -0.0612 156 PRO A O   
654  C CB  . PRO A 82  ? 0.4177 0.3610 0.3698 0.0500  -0.0673 -0.0559 156 PRO A CB  
655  C CG  . PRO A 82  ? 0.4243 0.3617 0.3671 0.0535  -0.0680 -0.0570 156 PRO A CG  
656  C CD  . PRO A 82  ? 0.4329 0.3678 0.3781 0.0530  -0.0726 -0.0604 156 PRO A CD  
657  N N   . ILE A 83  ? 0.3822 0.3311 0.3397 0.0506  -0.0724 -0.0576 157 ILE A N   
658  C CA  . ILE A 83  ? 0.3870 0.3367 0.3411 0.0527  -0.0726 -0.0571 157 ILE A CA  
659  C C   . ILE A 83  ? 0.4213 0.3696 0.3684 0.0545  -0.0682 -0.0544 157 ILE A C   
660  O O   . ILE A 83  ? 0.3937 0.3445 0.3435 0.0524  -0.0641 -0.0518 157 ILE A O   
661  C CB  . ILE A 83  ? 0.4204 0.3757 0.3834 0.0500  -0.0725 -0.0564 157 ILE A CB  
662  C CG1 . ILE A 83  ? 0.4245 0.3814 0.3953 0.0480  -0.0766 -0.0590 157 ILE A CG1 
663  C CG2 . ILE A 83  ? 0.4123 0.3689 0.3726 0.0520  -0.0724 -0.0557 157 ILE A CG2 
664  C CD1 . ILE A 83  ? 0.4278 0.3904 0.4082 0.0450  -0.0760 -0.0581 157 ILE A CD1 
665  N N   . ILE A 84  ? 0.4207 0.3653 0.3592 0.0583  -0.0690 -0.0547 158 ILE A N   
666  C CA  . ILE A 84  ? 0.3987 0.3412 0.3298 0.0604  -0.0651 -0.0523 158 ILE A CA  
667  C C   . ILE A 84  ? 0.4394 0.3829 0.3676 0.0623  -0.0645 -0.0512 158 ILE A C   
668  O O   . ILE A 84  ? 0.4224 0.3638 0.3466 0.0650  -0.0678 -0.0529 158 ILE A O   
669  C CB  . ILE A 84  ? 0.4113 0.3480 0.3340 0.0635  -0.0659 -0.0534 158 ILE A CB  
670  C CG1 . ILE A 84  ? 0.4012 0.3366 0.3271 0.0616  -0.0671 -0.0550 158 ILE A CG1 
671  C CG2 . ILE A 84  ? 0.4138 0.3487 0.3299 0.0654  -0.0613 -0.0505 158 ILE A CG2 
672  C CD1 . ILE A 84  ? 0.4330 0.3625 0.3507 0.0647  -0.0678 -0.0561 158 ILE A CD1 
673  N N   . LEU A 85  ? 0.3910 0.3377 0.3214 0.0608  -0.0604 -0.0483 159 LEU A N   
674  C CA  . LEU A 85  ? 0.3788 0.3273 0.3084 0.0618  -0.0595 -0.0470 159 LEU A CA  
675  C C   . LEU A 85  ? 0.3380 0.2850 0.2616 0.0635  -0.0552 -0.0441 159 LEU A C   
676  O O   . LEU A 85  ? 0.3630 0.3084 0.2843 0.0634  -0.0527 -0.0429 159 LEU A O   
677  C CB  . LEU A 85  ? 0.3791 0.3330 0.3180 0.0582  -0.0589 -0.0464 159 LEU A CB  
678  C CG  . LEU A 85  ? 0.3838 0.3397 0.3300 0.0560  -0.0625 -0.0488 159 LEU A CG  
679  C CD1 . LEU A 85  ? 0.3988 0.3600 0.3540 0.0523  -0.0608 -0.0477 159 LEU A CD1 
680  C CD2 . LEU A 85  ? 0.4111 0.3656 0.3554 0.0584  -0.0673 -0.0514 159 LEU A CD2 
681  N N   . CYS A 86  ? 0.3697 0.3175 0.2915 0.0649  -0.0545 -0.0430 160 CYS A N   
682  C CA  . CYS A 86  ? 0.3990 0.3456 0.3155 0.0666  -0.0505 -0.0402 160 CYS A CA  
683  C C   . CYS A 86  ? 0.3775 0.3274 0.2971 0.0655  -0.0485 -0.0384 160 CYS A C   
684  O O   . CYS A 86  ? 0.3798 0.3318 0.3027 0.0651  -0.0507 -0.0394 160 CYS A O   
685  C CB  . CYS A 86  ? 0.4346 0.3759 0.3415 0.0711  -0.0517 -0.0408 160 CYS A CB  
686  S SG  . CYS A 86  ? 0.4941 0.4335 0.3941 0.0739  -0.0473 -0.0375 160 CYS A SG  
687  N N   . GLY A 87  ? 0.3655 0.3163 0.2848 0.0646  -0.0441 -0.0355 161 GLY A N   
688  C CA  . GLY A 87  ? 0.3697 0.3226 0.2899 0.0643  -0.0416 -0.0334 161 GLY A CA  
689  C C   . GLY A 87  ? 0.3391 0.2967 0.2675 0.0609  -0.0418 -0.0336 161 GLY A C   
690  O O   . GLY A 87  ? 0.3355 0.2952 0.2696 0.0583  -0.0431 -0.0348 161 GLY A O   
691  N N   . ASP A 88  ? 0.3467 0.3056 0.2754 0.0613  -0.0407 -0.0324 162 ASP A N   
692  C CA  . ASP A 88  ? 0.3645 0.3275 0.3001 0.0586  -0.0406 -0.0323 162 ASP A CA  
693  C C   . ASP A 88  ? 0.3695 0.3341 0.3097 0.0579  -0.0447 -0.0351 162 ASP A C   
694  O O   . ASP A 88  ? 0.3594 0.3274 0.3065 0.0548  -0.0447 -0.0354 162 ASP A O   
695  C CB  . ASP A 88  ? 0.4205 0.3838 0.3544 0.0599  -0.0391 -0.0308 162 ASP A CB  
696  C CG  . ASP A 88  ? 0.4897 0.4525 0.4214 0.0596  -0.0348 -0.0280 162 ASP A CG  
697  O OD1 . ASP A 88  ? 0.5106 0.4741 0.4439 0.0576  -0.0326 -0.0269 162 ASP A OD1 
698  O OD2 . ASP A 88  ? 0.5531 0.5148 0.4815 0.0615  -0.0336 -0.0267 162 ASP A OD2 
699  N N   . GLU A 89  ? 0.3838 0.3460 0.3203 0.0607  -0.0482 -0.0370 163 GLU A N   
700  C CA  . GLU A 89  ? 0.3623 0.3261 0.3036 0.0600  -0.0523 -0.0396 163 GLU A CA  
701  C C   . GLU A 89  ? 0.3370 0.3016 0.2826 0.0576  -0.0533 -0.0408 163 GLU A C   
702  O O   . GLU A 89  ? 0.3503 0.3180 0.3031 0.0551  -0.0548 -0.0419 163 GLU A O   
703  C CB  . GLU A 89  ? 0.4016 0.3626 0.3378 0.0637  -0.0562 -0.0414 163 GLU A CB  
704  C CG  . GLU A 89  ? 0.5039 0.4652 0.4381 0.0656  -0.0558 -0.0404 163 GLU A CG  
705  C CD  . GLU A 89  ? 0.6034 0.5694 0.5452 0.0632  -0.0552 -0.0400 163 GLU A CD  
706  O OE1 . GLU A 89  ? 0.6826 0.6512 0.6309 0.0614  -0.0578 -0.0417 163 GLU A OE1 
707  O OE2 . GLU A 89  ? 0.7019 0.6687 0.6433 0.0630  -0.0520 -0.0379 163 GLU A OE2 
708  N N   . GLY A 90  ? 0.3316 0.2933 0.2728 0.0582  -0.0523 -0.0405 164 GLY A N   
709  C CA  . GLY A 90  ? 0.3378 0.2997 0.2825 0.0560  -0.0528 -0.0414 164 GLY A CA  
710  C C   . GLY A 90  ? 0.3226 0.2886 0.2744 0.0521  -0.0498 -0.0399 164 GLY A C   
711  O O   . GLY A 90  ? 0.3291 0.2972 0.2871 0.0496  -0.0510 -0.0410 164 GLY A O   
712  N N   . MET A 91  ? 0.3087 0.2755 0.2592 0.0517  -0.0460 -0.0373 165 MET A N   
713  C CA  . MET A 91  ? 0.3005 0.2709 0.2568 0.0482  -0.0431 -0.0358 165 MET A CA  
714  C C   . MET A 91  ? 0.3019 0.2760 0.2651 0.0464  -0.0445 -0.0366 165 MET A C   
715  O O   . MET A 91  ? 0.3013 0.2781 0.2707 0.0435  -0.0442 -0.0368 165 MET A O   
716  C CB  . MET A 91  ? 0.2993 0.2695 0.2523 0.0487  -0.0394 -0.0331 165 MET A CB  
717  C CG  . MET A 91  ? 0.3080 0.2816 0.2660 0.0454  -0.0362 -0.0313 165 MET A CG  
718  S SD  . MET A 91  ? 0.3278 0.3052 0.2915 0.0438  -0.0364 -0.0314 165 MET A SD  
719  C CE  . MET A 91  ? 0.3600 0.3358 0.3182 0.0465  -0.0350 -0.0300 165 MET A CE  
720  N N   . LYS A 92  ? 0.2982 0.2724 0.2604 0.0482  -0.0460 -0.0372 166 LYS A N   
721  C CA  . LYS A 92  ? 0.3257 0.3035 0.2944 0.0468  -0.0472 -0.0379 166 LYS A CA  
722  C C   . LYS A 92  ? 0.3343 0.3132 0.3083 0.0456  -0.0506 -0.0402 166 LYS A C   
723  O O   . LYS A 92  ? 0.3190 0.3012 0.3000 0.0431  -0.0506 -0.0404 166 LYS A O   
724  C CB  . LYS A 92  ? 0.3472 0.3248 0.3136 0.0491  -0.0482 -0.0380 166 LYS A CB  
725  C CG  . LYS A 92  ? 0.3982 0.3753 0.3610 0.0497  -0.0447 -0.0356 166 LYS A CG  
726  C CD  . LYS A 92  ? 0.4426 0.4191 0.4026 0.0523  -0.0456 -0.0356 166 LYS A CD  
727  C CE  . LYS A 92  ? 0.5170 0.4923 0.4726 0.0531  -0.0420 -0.0332 166 LYS A CE  
728  N NZ  . LYS A 92  ? 0.5636 0.5383 0.5169 0.0554  -0.0424 -0.0329 166 LYS A NZ  
729  N N   . GLU A 93  ? 0.3360 0.3117 0.3064 0.0475  -0.0537 -0.0420 167 GLU A N   
730  C CA  . GLU A 93  ? 0.3326 0.3089 0.3077 0.0465  -0.0571 -0.0443 167 GLU A CA  
731  C C   . GLU A 93  ? 0.3330 0.3108 0.3130 0.0433  -0.0555 -0.0438 167 GLU A C   
732  O O   . GLU A 93  ? 0.3386 0.3191 0.3260 0.0411  -0.0566 -0.0447 167 GLU A O   
733  C CB  . GLU A 93  ? 0.3762 0.3483 0.3453 0.0495  -0.0606 -0.0463 167 GLU A CB  
734  C CG  . GLU A 93  ? 0.3739 0.3458 0.3473 0.0485  -0.0644 -0.0489 167 GLU A CG  
735  C CD  . GLU A 93  ? 0.4446 0.4124 0.4125 0.0516  -0.0687 -0.0514 167 GLU A CD  
736  O OE1 . GLU A 93  ? 0.4458 0.4111 0.4066 0.0548  -0.0691 -0.0512 167 GLU A OE1 
737  O OE2 . GLU A 93  ? 0.4719 0.4390 0.4426 0.0507  -0.0715 -0.0534 167 GLU A OE2 
738  N N   . ILE A 94  ? 0.3333 0.3093 0.3095 0.0431  -0.0526 -0.0423 168 ILE A N   
739  C CA  . ILE A 94  ? 0.3201 0.2975 0.3006 0.0402  -0.0507 -0.0416 168 ILE A CA  
740  C C   . ILE A 94  ? 0.2986 0.2804 0.2856 0.0374  -0.0483 -0.0401 168 ILE A C   
741  O O   . ILE A 94  ? 0.3017 0.2858 0.2952 0.0349  -0.0485 -0.0405 168 ILE A O   
742  C CB  . ILE A 94  ? 0.3067 0.2813 0.2815 0.0408  -0.0480 -0.0401 168 ILE A CB  
743  C CG1 . ILE A 94  ? 0.3339 0.3042 0.3030 0.0434  -0.0506 -0.0418 168 ILE A CG1 
744  C CG2 . ILE A 94  ? 0.3083 0.2848 0.2875 0.0377  -0.0455 -0.0389 168 ILE A CG2 
745  C CD1 . ILE A 94  ? 0.3524 0.3195 0.3145 0.0450  -0.0481 -0.0403 168 ILE A CD1 
746  N N   . CYS A 95  ? 0.2938 0.2766 0.2789 0.0379  -0.0460 -0.0385 169 CYS A N   
747  C CA  . CYS A 95  ? 0.2880 0.2745 0.2785 0.0354  -0.0435 -0.0371 169 CYS A CA  
748  C C   . CYS A 95  ? 0.3130 0.3025 0.3105 0.0344  -0.0456 -0.0385 169 CYS A C   
749  O O   . CYS A 95  ? 0.3136 0.3062 0.3170 0.0319  -0.0440 -0.0377 169 CYS A O   
750  C CB  . CYS A 95  ? 0.2911 0.2779 0.2784 0.0362  -0.0410 -0.0354 169 CYS A CB  
751  S SG  . CYS A 95  ? 0.2860 0.2706 0.2671 0.0366  -0.0374 -0.0331 169 CYS A SG  
752  N N   . SER A 96  ? 0.3204 0.3091 0.3174 0.0363  -0.0493 -0.0404 170 SER A N   
753  C CA  . SER A 96  ? 0.3548 0.3465 0.3589 0.0355  -0.0514 -0.0416 170 SER A CA  
754  C C   . SER A 96  ? 0.3620 0.3539 0.3712 0.0341  -0.0540 -0.0433 170 SER A C   
755  O O   . SER A 96  ? 0.3716 0.3661 0.3875 0.0331  -0.0560 -0.0444 170 SER A O   
756  C CB  . SER A 96  ? 0.3910 0.3821 0.3929 0.0381  -0.0540 -0.0426 170 SER A CB  
757  O OG  . SER A 96  ? 0.4472 0.4351 0.4448 0.0403  -0.0574 -0.0445 170 SER A OG  
758  N N   . SER A 97  ? 0.3322 0.3216 0.3388 0.0338  -0.0539 -0.0435 171 SER A N   
759  C CA  . SER A 97  ? 0.3366 0.3261 0.3482 0.0323  -0.0562 -0.0451 171 SER A CA  
760  C C   . SER A 97  ? 0.3450 0.3382 0.3647 0.0290  -0.0541 -0.0440 171 SER A C   
761  O O   . SER A 97  ? 0.3312 0.3251 0.3506 0.0275  -0.0504 -0.0420 171 SER A O   
762  C CB  . SER A 97  ? 0.3677 0.3533 0.3742 0.0330  -0.0565 -0.0456 171 SER A CB  
763  O OG  . SER A 97  ? 0.3811 0.3666 0.3926 0.0314  -0.0585 -0.0470 171 SER A OG  
764  N N   . ASN A 98  ? 0.3555 0.3508 0.3827 0.0277  -0.0565 -0.0454 172 ASN A N   
765  C CA  . ASN A 98  ? 0.3519 0.3506 0.3871 0.0247  -0.0546 -0.0444 172 ASN A CA  
766  C C   . ASN A 98  ? 0.3578 0.3549 0.3935 0.0231  -0.0536 -0.0442 172 ASN A C   
767  O O   . ASN A 98  ? 0.4111 0.4105 0.4525 0.0206  -0.0515 -0.0430 172 ASN A O   
768  C CB  . ASN A 98  ? 0.4419 0.4433 0.4852 0.0240  -0.0574 -0.0459 172 ASN A CB  
769  C CG  . ASN A 98  ? 0.5253 0.5288 0.5688 0.0254  -0.0576 -0.0456 172 ASN A CG  
770  O OD1 . ASN A 98  ? 0.7150 0.7181 0.7585 0.0271  -0.0612 -0.0474 172 ASN A OD1 
771  N ND2 . ASN A 98  ? 0.5611 0.5665 0.6043 0.0247  -0.0537 -0.0435 172 ASN A ND2 
772  N N   . SER A 99  ? 0.3438 0.3369 0.3735 0.0246  -0.0550 -0.0451 173 SER A N   
773  C CA  . SER A 99  ? 0.3720 0.3633 0.4016 0.0233  -0.0541 -0.0449 173 SER A CA  
774  C C   . SER A 99  ? 0.3260 0.3169 0.3511 0.0229  -0.0499 -0.0424 173 SER A C   
775  O O   . SER A 99  ? 0.3674 0.3567 0.3919 0.0220  -0.0488 -0.0419 173 SER A O   
776  C CB  . SER A 99  ? 0.4313 0.4185 0.4567 0.0250  -0.0575 -0.0471 173 SER A CB  
777  O OG  . SER A 99  ? 0.5039 0.4881 0.5203 0.0278  -0.0573 -0.0469 173 SER A OG  
778  N N   . ILE A 100 ? 0.2900 0.2817 0.3114 0.0239  -0.0477 -0.0410 174 ILE A N   
779  C CA  . ILE A 100 ? 0.2881 0.2794 0.3052 0.0236  -0.0439 -0.0387 174 ILE A CA  
780  C C   . ILE A 100 ? 0.2699 0.2649 0.2910 0.0217  -0.0409 -0.0368 174 ILE A C   
781  O O   . ILE A 100 ? 0.2889 0.2858 0.3116 0.0221  -0.0411 -0.0369 174 ILE A O   
782  C CB  . ILE A 100 ? 0.3077 0.2964 0.3167 0.0264  -0.0440 -0.0386 174 ILE A CB  
783  C CG1 . ILE A 100 ? 0.3836 0.3683 0.3881 0.0282  -0.0466 -0.0402 174 ILE A CG1 
784  C CG2 . ILE A 100 ? 0.3394 0.3283 0.3446 0.0261  -0.0400 -0.0360 174 ILE A CG2 
785  C CD1 . ILE A 100 ? 0.3883 0.3701 0.3848 0.0313  -0.0470 -0.0403 174 ILE A CD1 
786  N N   . ASP A 101 ? 0.2708 0.2665 0.2931 0.0198  -0.0380 -0.0351 175 ASP A N   
787  C CA  . ASP A 101 ? 0.2734 0.2723 0.2994 0.0179  -0.0350 -0.0333 175 ASP A CA  
788  C C   . ASP A 101 ? 0.2506 0.2491 0.2711 0.0182  -0.0319 -0.0313 175 ASP A C   
789  O O   . ASP A 101 ? 0.2391 0.2396 0.2603 0.0178  -0.0301 -0.0303 175 ASP A O   
790  C CB  . ASP A 101 ? 0.3255 0.3254 0.3564 0.0155  -0.0338 -0.0326 175 ASP A CB  
791  C CG  . ASP A 101 ? 0.4091 0.4094 0.4463 0.0147  -0.0364 -0.0343 175 ASP A CG  
792  O OD1 . ASP A 101 ? 0.4336 0.4355 0.4742 0.0150  -0.0382 -0.0354 175 ASP A OD1 
793  O OD2 . ASP A 101 ? 0.4351 0.4341 0.4738 0.0137  -0.0366 -0.0344 175 ASP A OD2 
794  N N   . LYS A 102 ? 0.2240 0.2198 0.2393 0.0190  -0.0314 -0.0308 176 LYS A N   
795  C CA  . LYS A 102 ? 0.2278 0.2233 0.2386 0.0191  -0.0285 -0.0288 176 LYS A CA  
796  C C   . LYS A 102 ? 0.2268 0.2191 0.2309 0.0214  -0.0292 -0.0290 176 LYS A C   
797  O O   . LYS A 102 ? 0.2572 0.2471 0.2598 0.0226  -0.0313 -0.0303 176 LYS A O   
798  C CB  . LYS A 102 ? 0.2306 0.2267 0.2431 0.0170  -0.0262 -0.0272 176 LYS A CB  
799  C CG  . LYS A 102 ? 0.2476 0.2464 0.2669 0.0148  -0.0257 -0.0271 176 LYS A CG  
800  C CD  . LYS A 102 ? 0.2485 0.2483 0.2690 0.0129  -0.0228 -0.0251 176 LYS A CD  
801  C CE  . LYS A 102 ? 0.2616 0.2641 0.2887 0.0110  -0.0222 -0.0249 176 LYS A CE  
802  N NZ  . LYS A 102 ? 0.2748 0.2783 0.3031 0.0092  -0.0195 -0.0230 176 LYS A NZ  
803  N N   . ILE A 103 ? 0.2033 0.1954 0.2033 0.0223  -0.0276 -0.0278 177 ILE A N   
804  C CA  . ILE A 103 ? 0.2164 0.2056 0.2101 0.0247  -0.0279 -0.0277 177 ILE A CA  
805  C C   . ILE A 103 ? 0.1984 0.1875 0.1892 0.0242  -0.0248 -0.0254 177 ILE A C   
806  O O   . ILE A 103 ? 0.2064 0.1972 0.1977 0.0233  -0.0230 -0.0242 177 ILE A O   
807  C CB  . ILE A 103 ? 0.2057 0.1944 0.1970 0.0267  -0.0292 -0.0285 177 ILE A CB  
808  C CG1 . ILE A 103 ? 0.2288 0.2180 0.2237 0.0271  -0.0324 -0.0308 177 ILE A CG1 
809  C CG2 . ILE A 103 ? 0.2283 0.2138 0.2128 0.0293  -0.0293 -0.0283 177 ILE A CG2 
810  C CD1 . ILE A 103 ? 0.2658 0.2547 0.2587 0.0292  -0.0341 -0.0317 177 ILE A CD1 
811  N N   . VAL A 104 ? 0.2038 0.1907 0.1915 0.0249  -0.0244 -0.0249 178 VAL A N   
812  C CA  . VAL A 104 ? 0.2008 0.1874 0.1855 0.0248  -0.0218 -0.0228 178 VAL A CA  
813  C C   . VAL A 104 ? 0.2016 0.1862 0.1809 0.0273  -0.0217 -0.0225 178 VAL A C   
814  O O   . VAL A 104 ? 0.2255 0.2073 0.2012 0.0296  -0.0233 -0.0235 178 VAL A O   
815  C CB  . VAL A 104 ? 0.2110 0.1961 0.1949 0.0246  -0.0213 -0.0222 178 VAL A CB  
816  C CG1 . VAL A 104 ? 0.2228 0.2077 0.2038 0.0247  -0.0187 -0.0199 178 VAL A CG1 
817  C CG2 . VAL A 104 ? 0.2321 0.2189 0.2212 0.0223  -0.0213 -0.0224 178 VAL A CG2 
818  N N   . ILE A 105 ? 0.1962 0.1819 0.1747 0.0269  -0.0198 -0.0210 179 ILE A N   
819  C CA  . ILE A 105 ? 0.2111 0.1951 0.1849 0.0291  -0.0193 -0.0203 179 ILE A CA  
820  C C   . ILE A 105 ? 0.1975 0.1807 0.1688 0.0292  -0.0170 -0.0183 179 ILE A C   
821  O O   . ILE A 105 ? 0.2071 0.1920 0.1796 0.0275  -0.0149 -0.0166 179 ILE A O   
822  C CB  . ILE A 105 ? 0.2329 0.2184 0.2074 0.0288  -0.0188 -0.0201 179 ILE A CB  
823  C CG1 . ILE A 105 ? 0.2946 0.2817 0.2727 0.0283  -0.0206 -0.0218 179 ILE A CG1 
824  C CG2 . ILE A 105 ? 0.2415 0.2248 0.2110 0.0313  -0.0183 -0.0194 179 ILE A CG2 
825  C CD1 . ILE A 105 ? 0.2962 0.2814 0.2723 0.0307  -0.0233 -0.0237 179 ILE A CD1 
826  N N   . GLY A 106 ? 0.2018 0.1823 0.1694 0.0311  -0.0173 -0.0184 180 GLY A N   
827  C CA  . GLY A 106 ? 0.1958 0.1751 0.1606 0.0318  -0.0153 -0.0165 180 GLY A CA  
828  C C   . GLY A 106 ? 0.2128 0.1895 0.1723 0.0347  -0.0149 -0.0160 180 GLY A C   
829  O O   . GLY A 106 ? 0.2225 0.1973 0.1790 0.0361  -0.0137 -0.0148 180 GLY A O   
830  N N   . ILE A 107 ? 0.2126 0.1892 0.1711 0.0357  -0.0157 -0.0166 181 ILE A N   
831  C CA  . ILE A 107 ? 0.2134 0.1876 0.1670 0.0384  -0.0151 -0.0159 181 ILE A CA  
832  C C   . ILE A 107 ? 0.2113 0.1869 0.1654 0.0374  -0.0124 -0.0136 181 ILE A C   
833  O O   . ILE A 107 ? 0.2286 0.2067 0.1864 0.0350  -0.0119 -0.0133 181 ILE A O   
834  C CB  . ILE A 107 ? 0.2318 0.2053 0.1843 0.0399  -0.0173 -0.0178 181 ILE A CB  
835  C CG1 . ILE A 107 ? 0.2327 0.2048 0.1847 0.0409  -0.0202 -0.0201 181 ILE A CG1 
836  C CG2 . ILE A 107 ? 0.2484 0.2198 0.1961 0.0426  -0.0164 -0.0168 181 ILE A CG2 
837  C CD1 . ILE A 107 ? 0.2497 0.2216 0.2016 0.0421  -0.0228 -0.0221 181 ILE A CD1 
838  N N   . ASP A 108 ? 0.2282 0.2020 0.1788 0.0391  -0.0105 -0.0118 182 ASP A N   
839  C CA  . ASP A 108 ? 0.2412 0.2161 0.1925 0.0382  -0.0080 -0.0095 182 ASP A CA  
840  C C   . ASP A 108 ? 0.2392 0.2137 0.1892 0.0390  -0.0078 -0.0094 182 ASP A C   
841  O O   . ASP A 108 ? 0.2477 0.2205 0.1949 0.0412  -0.0093 -0.0106 182 ASP A O   
842  C CB  . ASP A 108 ? 0.2519 0.2251 0.2004 0.0396  -0.0060 -0.0075 182 ASP A CB  
843  C CG  . ASP A 108 ? 0.3118 0.2816 0.2548 0.0432  -0.0060 -0.0075 182 ASP A CG  
844  O OD1 . ASP A 108 ? 0.2995 0.2675 0.2403 0.0448  -0.0080 -0.0094 182 ASP A OD1 
845  O OD2 . ASP A 108 ? 0.3426 0.3115 0.2836 0.0444  -0.0043 -0.0059 182 ASP A OD2 
846  N N   . SER A 109 ? 0.2355 0.2114 0.1873 0.0375  -0.0060 -0.0077 183 SER A N   
847  C CA  . SER A 109 ? 0.2477 0.2230 0.1982 0.0384  -0.0050 -0.0068 183 SER A CA  
848  C C   . SER A 109 ? 0.2256 0.2016 0.1770 0.0382  -0.0068 -0.0086 183 SER A C   
849  O O   . SER A 109 ? 0.2200 0.1973 0.1738 0.0371  -0.0086 -0.0104 183 SER A O   
850  C CB  . SER A 109 ? 0.2629 0.2352 0.2086 0.0416  -0.0040 -0.0057 183 SER A CB  
851  O OG  . SER A 109 ? 0.2921 0.2640 0.2373 0.0416  -0.0022 -0.0039 183 SER A OG  
852  N N   . PHE A 110 ? 0.2475 0.2225 0.1974 0.0393  -0.0061 -0.0080 184 PHE A N   
853  C CA  . PHE A 110 ? 0.2405 0.2160 0.1912 0.0394  -0.0075 -0.0094 184 PHE A CA  
854  C C   . PHE A 110 ? 0.2380 0.2127 0.1873 0.0412  -0.0102 -0.0117 184 PHE A C   
855  O O   . PHE A 110 ? 0.2450 0.2211 0.1967 0.0404  -0.0118 -0.0133 184 PHE A O   
856  C CB  . PHE A 110 ? 0.2740 0.2480 0.2224 0.0409  -0.0061 -0.0081 184 PHE A CB  
857  C CG  . PHE A 110 ? 0.2659 0.2401 0.2146 0.0414  -0.0074 -0.0094 184 PHE A CG  
858  C CD1 . PHE A 110 ? 0.2644 0.2406 0.2166 0.0392  -0.0070 -0.0096 184 PHE A CD1 
859  C CD2 . PHE A 110 ? 0.2939 0.2662 0.2394 0.0443  -0.0090 -0.0106 184 PHE A CD2 
860  C CE1 . PHE A 110 ? 0.2718 0.2481 0.2244 0.0398  -0.0080 -0.0107 184 PHE A CE1 
861  C CE2 . PHE A 110 ? 0.2954 0.2680 0.2415 0.0448  -0.0102 -0.0117 184 PHE A CE2 
862  C CZ  . PHE A 110 ? 0.2878 0.2624 0.2375 0.0426  -0.0096 -0.0116 184 PHE A CZ  
863  N N   . GLN A 111 ? 0.2493 0.2217 0.1949 0.0435  -0.0106 -0.0117 185 GLN A N   
864  C CA  . GLN A 111 ? 0.2587 0.2299 0.2026 0.0452  -0.0134 -0.0139 185 GLN A CA  
865  C C   . GLN A 111 ? 0.2584 0.2320 0.2069 0.0430  -0.0153 -0.0157 185 GLN A C   
866  O O   . GLN A 111 ? 0.2765 0.2501 0.2254 0.0437  -0.0178 -0.0177 185 GLN A O   
867  C CB  . GLN A 111 ? 0.3010 0.2693 0.2404 0.0476  -0.0133 -0.0137 185 GLN A CB  
868  C CG  . GLN A 111 ? 0.3075 0.2743 0.2449 0.0495  -0.0165 -0.0161 185 GLN A CG  
869  C CD  . GLN A 111 ? 0.3209 0.2863 0.2556 0.0519  -0.0182 -0.0171 185 GLN A CD  
870  O OE1 . GLN A 111 ? 0.3726 0.3372 0.3053 0.0530  -0.0166 -0.0157 185 GLN A OE1 
871  N NE2 . GLN A 111 ? 0.3300 0.2955 0.2654 0.0524  -0.0214 -0.0196 185 GLN A NE2 
872  N N   . GLY A 112 ? 0.2390 0.2147 0.1911 0.0402  -0.0141 -0.0150 186 GLY A N   
873  C CA  . GLY A 112 ? 0.2318 0.2096 0.1881 0.0381  -0.0156 -0.0166 186 GLY A CA  
874  C C   . GLY A 112 ? 0.2183 0.1982 0.1782 0.0368  -0.0165 -0.0176 186 GLY A C   
875  O O   . GLY A 112 ? 0.2326 0.2142 0.1960 0.0357  -0.0181 -0.0191 186 GLY A O   
876  N N   . LEU A 113 ? 0.2193 0.1993 0.1784 0.0372  -0.0154 -0.0168 187 LEU A N   
877  C CA  . LEU A 113 ? 0.2257 0.2075 0.1878 0.0364  -0.0161 -0.0177 187 LEU A CA  
878  C C   . LEU A 113 ? 0.2267 0.2082 0.1891 0.0379  -0.0190 -0.0198 187 LEU A C   
879  O O   . LEU A 113 ? 0.2293 0.2130 0.1958 0.0367  -0.0201 -0.0210 187 LEU A O   
880  C CB  . LEU A 113 ? 0.2372 0.2184 0.1977 0.0369  -0.0144 -0.0164 187 LEU A CB  
881  C CG  . LEU A 113 ? 0.2405 0.2231 0.2034 0.0365  -0.0150 -0.0172 187 LEU A CG  
882  C CD1 . LEU A 113 ? 0.2223 0.2078 0.1901 0.0335  -0.0146 -0.0176 187 LEU A CD1 
883  C CD2 . LEU A 113 ? 0.2615 0.2429 0.2222 0.0372  -0.0132 -0.0158 187 LEU A CD2 
884  N N   . TYR A 114 ? 0.2344 0.2133 0.1924 0.0407  -0.0203 -0.0203 188 TYR A N   
885  C CA  . TYR A 114 ? 0.2587 0.2372 0.2167 0.0424  -0.0233 -0.0223 188 TYR A CA  
886  C C   . TYR A 114 ? 0.2522 0.2324 0.2144 0.0410  -0.0255 -0.0241 188 TYR A C   
887  O O   . TYR A 114 ? 0.2568 0.2389 0.2228 0.0404  -0.0271 -0.0254 188 TYR A O   
888  C CB  . TYR A 114 ? 0.2986 0.2737 0.2505 0.0458  -0.0242 -0.0224 188 TYR A CB  
889  C CG  . TYR A 114 ? 0.3780 0.3513 0.3259 0.0476  -0.0223 -0.0207 188 TYR A CG  
890  C CD1 . TYR A 114 ? 0.5006 0.4743 0.4487 0.0485  -0.0228 -0.0209 188 TYR A CD1 
891  C CD2 . TYR A 114 ? 0.4654 0.4366 0.4094 0.0486  -0.0201 -0.0189 188 TYR A CD2 
892  C CE1 . TYR A 114 ? 0.5457 0.5177 0.4903 0.0502  -0.0210 -0.0193 188 TYR A CE1 
893  C CE2 . TYR A 114 ? 0.4522 0.4218 0.3928 0.0502  -0.0183 -0.0172 188 TYR A CE2 
894  C CZ  . TYR A 114 ? 0.5387 0.5086 0.4796 0.0510  -0.0187 -0.0174 188 TYR A CZ  
895  O OH  . TYR A 114 ? 0.6564 0.6245 0.5941 0.0526  -0.0167 -0.0156 188 TYR A OH  
896  N N   . SER A 115 ? 0.2394 0.2189 0.2012 0.0404  -0.0254 -0.0242 189 SER A N   
897  C CA  . SER A 115 ? 0.2504 0.2314 0.2165 0.0388  -0.0272 -0.0257 189 SER A CA  
898  C C   . SER A 115 ? 0.2359 0.2203 0.2079 0.0356  -0.0259 -0.0252 189 SER A C   
899  O O   . SER A 115 ? 0.2510 0.2373 0.2276 0.0345  -0.0275 -0.0266 189 SER A O   
900  C CB  . SER A 115 ? 0.2621 0.2411 0.2261 0.0390  -0.0273 -0.0257 189 SER A CB  
901  O OG  . SER A 115 ? 0.2578 0.2371 0.2214 0.0377  -0.0243 -0.0236 189 SER A OG  
902  N N   . THR A 116 ? 0.2260 0.2112 0.1979 0.0343  -0.0231 -0.0233 190 THR A N   
903  C CA  . THR A 116 ? 0.2112 0.1993 0.1879 0.0315  -0.0217 -0.0229 190 THR A CA  
904  C C   . THR A 116 ? 0.2188 0.2086 0.1985 0.0315  -0.0228 -0.0240 190 THR A C   
905  O O   . THR A 116 ? 0.2122 0.2044 0.1969 0.0299  -0.0233 -0.0247 190 THR A O   
906  C CB  . THR A 116 ? 0.2113 0.1996 0.1867 0.0304  -0.0188 -0.0208 190 THR A CB  
907  O OG1 . THR A 116 ? 0.2178 0.2049 0.1912 0.0303  -0.0178 -0.0198 190 THR A OG1 
908  C CG2 . THR A 116 ? 0.2098 0.2008 0.1895 0.0277  -0.0174 -0.0204 190 THR A CG2 
909  N N   . MET A 117 ? 0.2246 0.2132 0.2014 0.0335  -0.0230 -0.0238 191 MET A N   
910  C CA  . MET A 117 ? 0.2419 0.2319 0.2210 0.0339  -0.0239 -0.0247 191 MET A CA  
911  C C   . MET A 117 ? 0.2383 0.2291 0.2205 0.0344  -0.0270 -0.0267 191 MET A C   
912  O O   . MET A 117 ? 0.2400 0.2333 0.2270 0.0332  -0.0275 -0.0274 191 MET A O   
913  C CB  . MET A 117 ? 0.2869 0.2750 0.2617 0.0363  -0.0236 -0.0241 191 MET A CB  
914  C CG  . MET A 117 ? 0.3443 0.3331 0.3204 0.0375  -0.0249 -0.0250 191 MET A CG  
915  S SD  . MET A 117 ? 0.4101 0.3960 0.3803 0.0407  -0.0247 -0.0243 191 MET A SD  
916  C CE  . MET A 117 ? 0.3637 0.3476 0.3298 0.0403  -0.0220 -0.0223 191 MET A CE  
917  N N   . TYR A 118 ? 0.2575 0.2461 0.2367 0.0362  -0.0291 -0.0277 192 TYR A N   
918  C CA  . TYR A 118 ? 0.2623 0.2515 0.2443 0.0368  -0.0324 -0.0298 192 TYR A CA  
919  C C   . TYR A 118 ? 0.2599 0.2512 0.2474 0.0343  -0.0326 -0.0303 192 TYR A C   
920  O O   . TYR A 118 ? 0.2740 0.2671 0.2663 0.0336  -0.0345 -0.0317 192 TYR A O   
921  C CB  . TYR A 118 ? 0.2988 0.2847 0.2757 0.0396  -0.0348 -0.0308 192 TYR A CB  
922  C CG  . TYR A 118 ? 0.3717 0.3566 0.3456 0.0423  -0.0359 -0.0311 192 TYR A CG  
923  C CD1 . TYR A 118 ? 0.3871 0.3733 0.3641 0.0429  -0.0386 -0.0327 192 TYR A CD1 
924  C CD2 . TYR A 118 ? 0.4074 0.3903 0.3759 0.0439  -0.0339 -0.0296 192 TYR A CD2 
925  C CE1 . TYR A 118 ? 0.4533 0.4387 0.4278 0.0454  -0.0397 -0.0329 192 TYR A CE1 
926  C CE2 . TYR A 118 ? 0.4979 0.4798 0.4638 0.0463  -0.0348 -0.0297 192 TYR A CE2 
927  C CZ  . TYR A 118 ? 0.5234 0.5065 0.4921 0.0471  -0.0377 -0.0314 192 TYR A CZ  
928  O OH  . TYR A 118 ? 0.5632 0.5454 0.5294 0.0496  -0.0386 -0.0314 192 TYR A OH  
929  N N   . ALA A 119 ? 0.2489 0.2399 0.2360 0.0326  -0.0306 -0.0292 193 ALA A N   
930  C CA  . ALA A 119 ? 0.2537 0.2466 0.2460 0.0302  -0.0305 -0.0295 193 ALA A CA  
931  C C   . ALA A 119 ? 0.2402 0.2364 0.2378 0.0283  -0.0292 -0.0291 193 ALA A C   
932  O O   . ALA A 119 ? 0.2606 0.2589 0.2637 0.0270  -0.0302 -0.0299 193 ALA A O   
933  C CB  . ALA A 119 ? 0.2439 0.2359 0.2342 0.0291  -0.0286 -0.0282 193 ALA A CB  
934  N N   . ILE A 120 ? 0.2226 0.2193 0.2187 0.0281  -0.0269 -0.0277 194 ILE A N   
935  C CA  . ILE A 120 ? 0.2226 0.2220 0.2230 0.0266  -0.0256 -0.0273 194 ILE A CA  
936  C C   . ILE A 120 ? 0.2270 0.2278 0.2306 0.0277  -0.0277 -0.0287 194 ILE A C   
937  O O   . ILE A 120 ? 0.2378 0.2411 0.2470 0.0263  -0.0277 -0.0291 194 ILE A O   
938  C CB  . ILE A 120 ? 0.2224 0.2214 0.2196 0.0265  -0.0229 -0.0257 194 ILE A CB  
939  C CG1 . ILE A 120 ? 0.2096 0.2080 0.2050 0.0250  -0.0207 -0.0243 194 ILE A CG1 
940  C CG2 . ILE A 120 ? 0.2203 0.2216 0.2212 0.0255  -0.0217 -0.0256 194 ILE A CG2 
941  C CD1 . ILE A 120 ? 0.2248 0.2224 0.2168 0.0249  -0.0184 -0.0227 194 ILE A CD1 
942  N N   . MET A 121 ? 0.2459 0.2449 0.2459 0.0302  -0.0294 -0.0294 195 MET A N   
943  C CA  . MET A 121 ? 0.2562 0.2563 0.2589 0.0315  -0.0318 -0.0307 195 MET A CA  
944  C C   . MET A 121 ? 0.2646 0.2660 0.2724 0.0309  -0.0344 -0.0324 195 MET A C   
945  O O   . MET A 121 ? 0.3027 0.3062 0.3149 0.0311  -0.0359 -0.0333 195 MET A O   
946  C CB  . MET A 121 ? 0.2708 0.2682 0.2678 0.0345  -0.0333 -0.0311 195 MET A CB  
947  C CG  . MET A 121 ? 0.3082 0.3046 0.3013 0.0353  -0.0309 -0.0296 195 MET A CG  
948  S SD  . MET A 121 ? 0.3886 0.3813 0.3743 0.0388  -0.0322 -0.0297 195 MET A SD  
949  C CE  . MET A 121 ? 0.4005 0.3942 0.3890 0.0407  -0.0360 -0.0317 195 MET A CE  
950  N N   . ASN A 122 ? 0.2624 0.2626 0.2696 0.0302  -0.0351 -0.0327 196 ASN A N   
951  C CA  . ASN A 122 ? 0.2563 0.2576 0.2685 0.0293  -0.0375 -0.0342 196 ASN A CA  
952  C C   . ASN A 122 ? 0.2678 0.2714 0.2854 0.0264  -0.0355 -0.0334 196 ASN A C   
953  O O   . ASN A 122 ? 0.2756 0.2796 0.2969 0.0254  -0.0370 -0.0343 196 ASN A O   
954  C CB  . ASN A 122 ? 0.2827 0.2809 0.2908 0.0306  -0.0398 -0.0353 196 ASN A CB  
955  C CG  . ASN A 122 ? 0.3031 0.2995 0.3077 0.0336  -0.0426 -0.0366 196 ASN A CG  
956  O OD1 . ASN A 122 ? 0.3165 0.3140 0.3248 0.0341  -0.0456 -0.0382 196 ASN A OD1 
957  N ND2 . ASN A 122 ? 0.2908 0.2847 0.2885 0.0356  -0.0418 -0.0358 196 ASN A ND2 
958  N N   . ASN A 123 ? 0.2636 0.2685 0.2814 0.0251  -0.0322 -0.0317 197 ASN A N   
959  C CA  . ASN A 123 ? 0.2480 0.2553 0.2710 0.0226  -0.0302 -0.0309 197 ASN A CA  
960  C C   . ASN A 123 ? 0.2551 0.2615 0.2779 0.0212  -0.0298 -0.0306 197 ASN A C   
961  O O   . ASN A 123 ? 0.2820 0.2901 0.3101 0.0193  -0.0293 -0.0304 197 ASN A O   
962  C CB  . ASN A 123 ? 0.2806 0.2908 0.3108 0.0221  -0.0314 -0.0318 197 ASN A CB  
963  C CG  . ASN A 123 ? 0.3223 0.3333 0.3522 0.0237  -0.0318 -0.0320 197 ASN A CG  
964  O OD1 . ASN A 123 ? 0.3477 0.3587 0.3750 0.0238  -0.0294 -0.0308 197 ASN A OD1 
965  N ND2 . ASN A 123 ? 0.3769 0.3881 0.4087 0.0251  -0.0350 -0.0336 197 ASN A ND2 
966  N N   . LYS A 124 ? 0.2365 0.2401 0.2533 0.0221  -0.0295 -0.0302 198 LYS A N   
967  C CA  . LYS A 124 ? 0.2356 0.2381 0.2519 0.0210  -0.0291 -0.0298 198 LYS A CA  
968  C C   . LYS A 124 ? 0.2197 0.2226 0.2347 0.0194  -0.0257 -0.0278 198 LYS A C   
969  O O   . LYS A 124 ? 0.2356 0.2392 0.2492 0.0194  -0.0238 -0.0267 198 LYS A O   
970  C CB  . LYS A 124 ? 0.2592 0.2583 0.2699 0.0229  -0.0308 -0.0305 198 LYS A CB  
971  C CG  . LYS A 124 ? 0.2781 0.2762 0.2890 0.0248  -0.0345 -0.0326 198 LYS A CG  
972  C CD  . LYS A 124 ? 0.2857 0.2852 0.3030 0.0236  -0.0366 -0.0340 198 LYS A CD  
973  C CE  . LYS A 124 ? 0.3280 0.3262 0.3449 0.0255  -0.0406 -0.0363 198 LYS A CE  
974  N NZ  . LYS A 124 ? 0.3371 0.3368 0.3610 0.0242  -0.0426 -0.0376 198 LYS A NZ  
975  N N   . ILE A 125 ? 0.2233 0.2260 0.2395 0.0180  -0.0251 -0.0273 199 ILE A N   
976  C CA  . ILE A 125 ? 0.2148 0.2174 0.2288 0.0169  -0.0224 -0.0254 199 ILE A CA  
977  C C   . ILE A 125 ? 0.2097 0.2094 0.2174 0.0184  -0.0225 -0.0251 199 ILE A C   
978  O O   . ILE A 125 ? 0.2161 0.2139 0.2223 0.0195  -0.0242 -0.0260 199 ILE A O   
979  C CB  . ILE A 125 ? 0.2497 0.2530 0.2674 0.0149  -0.0216 -0.0249 199 ILE A CB  
980  C CG1 . ILE A 125 ? 0.3065 0.3127 0.3305 0.0134  -0.0211 -0.0251 199 ILE A CG1 
981  C CG2 . ILE A 125 ? 0.2694 0.2724 0.2843 0.0139  -0.0190 -0.0230 199 ILE A CG2 
982  C CD1 . ILE A 125 ? 0.3630 0.3702 0.3912 0.0115  -0.0201 -0.0244 199 ILE A CD1 
983  N N   . VAL A 126 ? 0.1944 0.1939 0.1985 0.0187  -0.0206 -0.0238 200 VAL A N   
984  C CA  . VAL A 126 ? 0.2045 0.2015 0.2029 0.0203  -0.0204 -0.0232 200 VAL A CA  
985  C C   . VAL A 126 ? 0.1930 0.1900 0.1901 0.0190  -0.0180 -0.0213 200 VAL A C   
986  O O   . VAL A 126 ? 0.1932 0.1915 0.1906 0.0178  -0.0160 -0.0201 200 VAL A O   
987  C CB  . VAL A 126 ? 0.2063 0.2029 0.2019 0.0217  -0.0201 -0.0231 200 VAL A CB  
988  C CG1 . VAL A 126 ? 0.2263 0.2203 0.2163 0.0236  -0.0200 -0.0225 200 VAL A CG1 
989  C CG2 . VAL A 126 ? 0.2424 0.2397 0.2403 0.0228  -0.0223 -0.0248 200 VAL A CG2 
990  N N   . ALA A 127 ? 0.1802 0.1757 0.1761 0.0192  -0.0184 -0.0213 201 ALA A N   
991  C CA  . ALA A 127 ? 0.1775 0.1728 0.1721 0.0182  -0.0165 -0.0195 201 ALA A CA  
992  C C   . ALA A 127 ? 0.1645 0.1580 0.1540 0.0198  -0.0158 -0.0186 201 ALA A C   
993  O O   . ALA A 127 ? 0.1877 0.1789 0.1740 0.0216  -0.0167 -0.0190 201 ALA A O   
994  C CB  . ALA A 127 ? 0.1773 0.1718 0.1733 0.0178  -0.0173 -0.0199 201 ALA A CB  
995  N N   . LEU A 128 ? 0.1660 0.1604 0.1546 0.0193  -0.0142 -0.0175 202 LEU A N   
996  C CA  . LEU A 128 ? 0.1781 0.1711 0.1627 0.0208  -0.0136 -0.0168 202 LEU A CA  
997  C C   . LEU A 128 ? 0.1765 0.1690 0.1591 0.0204  -0.0118 -0.0148 202 LEU A C   
998  O O   . LEU A 128 ? 0.1766 0.1707 0.1605 0.0187  -0.0103 -0.0137 202 LEU A O   
999  C CB  . LEU A 128 ? 0.1871 0.1811 0.1721 0.0206  -0.0131 -0.0168 202 LEU A CB  
1000 C CG  . LEU A 128 ? 0.1976 0.1901 0.1788 0.0223  -0.0126 -0.0162 202 LEU A CG  
1001 C CD1 . LEU A 128 ? 0.2142 0.2044 0.1923 0.0249  -0.0141 -0.0171 202 LEU A CD1 
1002 C CD2 . LEU A 128 ? 0.2212 0.2149 0.2036 0.0219  -0.0123 -0.0165 202 LEU A CD2 
1003 N N   . ALA A 129 ? 0.1731 0.1636 0.1526 0.0220  -0.0119 -0.0145 203 ALA A N   
1004 C CA  . ALA A 129 ? 0.1721 0.1621 0.1496 0.0220  -0.0101 -0.0125 203 ALA A CA  
1005 C C   . ALA A 129 ? 0.1893 0.1784 0.1640 0.0231  -0.0092 -0.0116 203 ALA A C   
1006 O O   . ALA A 129 ? 0.1846 0.1742 0.1589 0.0224  -0.0075 -0.0099 203 ALA A O   
1007 C CB  . ALA A 129 ? 0.1924 0.1806 0.1682 0.0232  -0.0103 -0.0123 203 ALA A CB  
1008 N N   . ASN A 130 ? 0.1998 0.1876 0.1725 0.0251  -0.0103 -0.0127 204 ASN A N   
1009 C CA  . ASN A 130 ? 0.2024 0.1889 0.1721 0.0265  -0.0095 -0.0119 204 ASN A CA  
1010 C C   . ASN A 130 ? 0.2104 0.1986 0.1819 0.0249  -0.0084 -0.0113 204 ASN A C   
1011 O O   . ASN A 130 ? 0.2480 0.2375 0.2217 0.0240  -0.0092 -0.0124 204 ASN A O   
1012 C CB  . ASN A 130 ? 0.2016 0.1863 0.1690 0.0290  -0.0112 -0.0134 204 ASN A CB  
1013 C CG  . ASN A 130 ? 0.2068 0.1902 0.1712 0.0306  -0.0103 -0.0126 204 ASN A CG  
1014 O OD1 . ASN A 130 ? 0.2467 0.2312 0.2124 0.0298  -0.0099 -0.0125 204 ASN A OD1 
1015 N ND2 . ASN A 130 ? 0.2189 0.2000 0.1796 0.0327  -0.0098 -0.0117 204 ASN A ND2 
1016 N N   . LYS A 131 ? 0.1873 0.1755 0.1581 0.0244  -0.0067 -0.0095 205 LYS A N   
1017 C CA  . LYS A 131 ? 0.1888 0.1783 0.1610 0.0227  -0.0057 -0.0089 205 LYS A CA  
1018 C C   . LYS A 131 ? 0.1798 0.1679 0.1498 0.0242  -0.0053 -0.0087 205 LYS A C   
1019 O O   . LYS A 131 ? 0.1849 0.1738 0.1559 0.0232  -0.0050 -0.0089 205 LYS A O   
1020 C CB  . LYS A 131 ? 0.1804 0.1709 0.1535 0.0210  -0.0042 -0.0071 205 LYS A CB  
1021 C CG  . LYS A 131 ? 0.1839 0.1731 0.1550 0.0220  -0.0030 -0.0053 205 LYS A CG  
1022 C CD  . LYS A 131 ? 0.1787 0.1691 0.1512 0.0204  -0.0019 -0.0037 205 LYS A CD  
1023 C CE  . LYS A 131 ? 0.1787 0.1692 0.1515 0.0206  -0.0024 -0.0039 205 LYS A CE  
1024 N NZ  . LYS A 131 ? 0.1749 0.1668 0.1495 0.0190  -0.0016 -0.0024 205 LYS A NZ  
1025 N N   . GLU A 132 ? 0.1823 0.1683 0.1491 0.0266  -0.0053 -0.0083 206 GLU A N   
1026 C CA  . GLU A 132 ? 0.1955 0.1799 0.1600 0.0281  -0.0047 -0.0078 206 GLU A CA  
1027 C C   . GLU A 132 ? 0.1937 0.1783 0.1587 0.0286  -0.0061 -0.0096 206 GLU A C   
1028 O O   . GLU A 132 ? 0.2012 0.1855 0.1659 0.0288  -0.0055 -0.0093 206 GLU A O   
1029 C CB  . GLU A 132 ? 0.1947 0.1767 0.1555 0.0309  -0.0044 -0.0071 206 GLU A CB  
1030 C CG  . GLU A 132 ? 0.2149 0.1965 0.1751 0.0307  -0.0027 -0.0050 206 GLU A CG  
1031 C CD  . GLU A 132 ? 0.2117 0.1936 0.1723 0.0305  -0.0030 -0.0050 206 GLU A CD  
1032 O OE1 . GLU A 132 ? 0.2302 0.2130 0.1923 0.0297  -0.0045 -0.0066 206 GLU A OE1 
1033 O OE2 . GLU A 132 ? 0.2361 0.2172 0.1955 0.0312  -0.0016 -0.0033 206 GLU A OE2 
1034 N N   . SER A 133 ? 0.1880 0.1732 0.1541 0.0288  -0.0079 -0.0113 207 SER A N   
1035 C CA  . SER A 133 ? 0.1939 0.1798 0.1613 0.0292  -0.0093 -0.0129 207 SER A CA  
1036 C C   . SER A 133 ? 0.1893 0.1770 0.1594 0.0270  -0.0085 -0.0129 207 SER A C   
1037 O O   . SER A 133 ? 0.1979 0.1854 0.1680 0.0275  -0.0085 -0.0133 207 SER A O   
1038 C CB  . SER A 133 ? 0.2116 0.1980 0.1804 0.0293  -0.0113 -0.0146 207 SER A CB  
1039 O OG  . SER A 133 ? 0.2286 0.2169 0.2005 0.0271  -0.0110 -0.0145 207 SER A OG  
1040 N N   . ILE A 134 ? 0.1850 0.1744 0.1576 0.0246  -0.0078 -0.0125 208 ILE A N   
1041 C CA  . ILE A 134 ? 0.1794 0.1704 0.1544 0.0226  -0.0070 -0.0125 208 ILE A CA  
1042 C C   . ILE A 134 ? 0.1828 0.1728 0.1562 0.0224  -0.0055 -0.0112 208 ILE A C   
1043 O O   . ILE A 134 ? 0.1915 0.1817 0.1655 0.0220  -0.0051 -0.0116 208 ILE A O   
1044 C CB  . ILE A 134 ? 0.1939 0.1866 0.1712 0.0204  -0.0066 -0.0121 208 ILE A CB  
1045 C CG1 . ILE A 134 ? 0.2265 0.2200 0.2057 0.0205  -0.0080 -0.0134 208 ILE A CG1 
1046 C CG2 . ILE A 134 ? 0.1918 0.1859 0.1709 0.0184  -0.0056 -0.0120 208 ILE A CG2 
1047 C CD1 . ILE A 134 ? 0.2553 0.2501 0.2363 0.0187  -0.0076 -0.0128 208 ILE A CD1 
1048 N N   . VAL A 135 ? 0.1749 0.1639 0.1466 0.0227  -0.0045 -0.0096 209 VAL A N   
1049 C CA  . VAL A 135 ? 0.1731 0.1612 0.1438 0.0224  -0.0031 -0.0084 209 VAL A CA  
1050 C C   . VAL A 135 ? 0.1911 0.1775 0.1599 0.0243  -0.0032 -0.0087 209 VAL A C   
1051 O O   . VAL A 135 ? 0.2025 0.1886 0.1716 0.0237  -0.0025 -0.0085 209 VAL A O   
1052 C CB  . VAL A 135 ? 0.1746 0.1620 0.1442 0.0225  -0.0020 -0.0065 209 VAL A CB  
1053 C CG1 . VAL A 135 ? 0.1801 0.1662 0.1488 0.0224  -0.0006 -0.0051 209 VAL A CG1 
1054 C CG2 . VAL A 135 ? 0.1835 0.1726 0.1550 0.0204  -0.0018 -0.0060 209 VAL A CG2 
1055 N N   . SER A 136 ? 0.1824 0.1675 0.1492 0.0267  -0.0041 -0.0092 210 SER A N   
1056 C CA  . SER A 136 ? 0.1997 0.1830 0.1642 0.0289  -0.0042 -0.0092 210 SER A CA  
1057 C C   . SER A 136 ? 0.2028 0.1868 0.1685 0.0292  -0.0053 -0.0108 210 SER A C   
1058 O O   . SER A 136 ? 0.2189 0.2016 0.1833 0.0305  -0.0050 -0.0108 210 SER A O   
1059 C CB  . SER A 136 ? 0.2143 0.1959 0.1759 0.0315  -0.0048 -0.0091 210 SER A CB  
1060 O OG  . SER A 136 ? 0.3036 0.2843 0.2638 0.0316  -0.0035 -0.0074 210 SER A OG  
1061 N N   . ALA A 137 ? 0.1922 0.1781 0.1605 0.0281  -0.0065 -0.0122 211 ALA A N   
1062 C CA  . ALA A 137 ? 0.2000 0.1866 0.1697 0.0288  -0.0077 -0.0138 211 ALA A CA  
1063 C C   . ALA A 137 ? 0.1982 0.1873 0.1717 0.0266  -0.0078 -0.0146 211 ALA A C   
1064 O O   . ALA A 137 ? 0.2076 0.1979 0.1832 0.0268  -0.0091 -0.0160 211 ALA A O   
1065 C CB  . ALA A 137 ? 0.2060 0.1920 0.1746 0.0309  -0.0097 -0.0149 211 ALA A CB  
1066 N N   . GLY A 138 ? 0.2224 0.2123 0.1968 0.0244  -0.0064 -0.0138 212 GLY A N   
1067 C CA  . GLY A 138 ? 0.2185 0.2105 0.1960 0.0223  -0.0062 -0.0144 212 GLY A CA  
1068 C C   . GLY A 138 ? 0.2241 0.2169 0.2035 0.0225  -0.0065 -0.0156 212 GLY A C   
1069 O O   . GLY A 138 ? 0.2274 0.2220 0.2095 0.0219  -0.0072 -0.0165 212 GLY A O   
1070 N N   . PHE A 139 ? 0.2396 0.2312 0.2176 0.0231  -0.0058 -0.0153 213 PHE A N   
1071 C CA  . PHE A 139 ? 0.2530 0.2453 0.2327 0.0234  -0.0058 -0.0163 213 PHE A CA  
1072 C C   . PHE A 139 ? 0.2357 0.2286 0.2166 0.0252  -0.0076 -0.0175 213 PHE A C   
1073 O O   . PHE A 139 ? 0.2426 0.2373 0.2266 0.0249  -0.0081 -0.0185 213 PHE A O   
1074 C CB  . PHE A 139 ? 0.2743 0.2649 0.2522 0.0238  -0.0046 -0.0159 213 PHE A CB  
1075 C CG  . PHE A 139 ? 0.3152 0.3062 0.2945 0.0245  -0.0046 -0.0168 213 PHE A CG  
1076 C CD1 . PHE A 139 ? 0.3456 0.3379 0.3270 0.0230  -0.0037 -0.0173 213 PHE A CD1 
1077 C CD2 . PHE A 139 ? 0.3531 0.3432 0.3316 0.0268  -0.0055 -0.0172 213 PHE A CD2 
1078 C CE1 . PHE A 139 ? 0.3492 0.3419 0.3320 0.0238  -0.0035 -0.0181 213 PHE A CE1 
1079 C CE2 . PHE A 139 ? 0.3608 0.3514 0.3408 0.0276  -0.0055 -0.0180 213 PHE A CE2 
1080 C CZ  . PHE A 139 ? 0.3465 0.3384 0.3288 0.0261  -0.0045 -0.0185 213 PHE A CZ  
1081 N N   . PHE A 140 ? 0.2308 0.2223 0.2094 0.0272  -0.0087 -0.0174 214 PHE A N   
1082 C CA  . PHE A 140 ? 0.2253 0.2172 0.2047 0.0290  -0.0108 -0.0186 214 PHE A CA  
1083 C C   . PHE A 140 ? 0.2327 0.2267 0.2153 0.0278  -0.0119 -0.0195 214 PHE A C   
1084 O O   . PHE A 140 ? 0.2300 0.2254 0.2156 0.0282  -0.0132 -0.0207 214 PHE A O   
1085 C CB  . PHE A 140 ? 0.2444 0.2340 0.2198 0.0312  -0.0115 -0.0181 214 PHE A CB  
1086 C CG  . PHE A 140 ? 0.2736 0.2631 0.2490 0.0331  -0.0139 -0.0194 214 PHE A CG  
1087 C CD1 . PHE A 140 ? 0.3364 0.3257 0.3118 0.0351  -0.0152 -0.0202 214 PHE A CD1 
1088 C CD2 . PHE A 140 ? 0.3299 0.3197 0.3056 0.0330  -0.0152 -0.0199 214 PHE A CD2 
1089 C CE1 . PHE A 140 ? 0.3377 0.3270 0.3131 0.0369  -0.0178 -0.0215 214 PHE A CE1 
1090 C CE2 . PHE A 140 ? 0.3475 0.3372 0.3233 0.0347  -0.0177 -0.0212 214 PHE A CE2 
1091 C CZ  . PHE A 140 ? 0.3427 0.3321 0.3183 0.0366  -0.0191 -0.0220 214 PHE A CZ  
1092 N N   . LEU A 141 ? 0.2322 0.2262 0.2145 0.0266  -0.0115 -0.0189 215 LEU A N   
1093 C CA  . LEU A 141 ? 0.2127 0.2084 0.1980 0.0255  -0.0125 -0.0196 215 LEU A CA  
1094 C C   . LEU A 141 ? 0.2057 0.2038 0.1951 0.0237  -0.0117 -0.0200 215 LEU A C   
1095 O O   . LEU A 141 ? 0.2121 0.2119 0.2051 0.0234  -0.0128 -0.0209 215 LEU A O   
1096 C CB  . LEU A 141 ? 0.2072 0.2024 0.1912 0.0244  -0.0118 -0.0186 215 LEU A CB  
1097 C CG  . LEU A 141 ? 0.2254 0.2184 0.2057 0.0263  -0.0127 -0.0184 215 LEU A CG  
1098 C CD1 . LEU A 141 ? 0.2470 0.2396 0.2262 0.0252  -0.0117 -0.0172 215 LEU A CD1 
1099 C CD2 . LEU A 141 ? 0.2369 0.2297 0.2176 0.0280  -0.0151 -0.0198 215 LEU A CD2 
1100 N N   . LYS A 142 ? 0.2078 0.2059 0.1967 0.0225  -0.0098 -0.0192 216 LYS A N   
1101 C CA  . LYS A 142 ? 0.2129 0.2128 0.2050 0.0211  -0.0088 -0.0194 216 LYS A CA  
1102 C C   . LYS A 142 ? 0.2422 0.2432 0.2370 0.0223  -0.0097 -0.0206 216 LYS A C   
1103 O O   . LYS A 142 ? 0.2366 0.2397 0.2354 0.0216  -0.0100 -0.0212 216 LYS A O   
1104 C CB  . LYS A 142 ? 0.2341 0.2333 0.2245 0.0200  -0.0067 -0.0186 216 LYS A CB  
1105 C CG  . LYS A 142 ? 0.2517 0.2525 0.2447 0.0186  -0.0054 -0.0187 216 LYS A CG  
1106 C CD  . LYS A 142 ? 0.3210 0.3208 0.3118 0.0177  -0.0036 -0.0181 216 LYS A CD  
1107 C CE  . LYS A 142 ? 0.3695 0.3680 0.3592 0.0191  -0.0035 -0.0185 216 LYS A CE  
1108 N NZ  . LYS A 142 ? 0.4185 0.4158 0.4061 0.0181  -0.0018 -0.0180 216 LYS A NZ  
1109 N N   . LYS A 143 ? 0.2280 0.2276 0.2207 0.0242  -0.0102 -0.0207 217 LYS A N   
1110 C CA  . LYS A 143 ? 0.2592 0.2597 0.2542 0.0256  -0.0113 -0.0217 217 LYS A CA  
1111 C C   . LYS A 143 ? 0.2457 0.2476 0.2436 0.0262  -0.0136 -0.0228 217 LYS A C   
1112 O O   . LYS A 143 ? 0.2528 0.2568 0.2550 0.0262  -0.0142 -0.0236 217 LYS A O   
1113 C CB  . LYS A 143 ? 0.3065 0.3050 0.2981 0.0276  -0.0113 -0.0215 217 LYS A CB  
1114 C CG  . LYS A 143 ? 0.3881 0.3854 0.3778 0.0270  -0.0091 -0.0207 217 LYS A CG  
1115 C CD  . LYS A 143 ? 0.4521 0.4507 0.4445 0.0262  -0.0077 -0.0210 217 LYS A CD  
1116 C CE  . LYS A 143 ? 0.5211 0.5198 0.5144 0.0282  -0.0085 -0.0217 217 LYS A CE  
1117 N NZ  . LYS A 143 ? 0.5672 0.5668 0.5627 0.0276  -0.0069 -0.0218 217 LYS A NZ  
1118 N N   . LEU A 144 ? 0.2374 0.2381 0.2331 0.0269  -0.0150 -0.0229 218 LEU A N   
1119 C CA  . LEU A 144 ? 0.2481 0.2496 0.2460 0.0275  -0.0174 -0.0240 218 LEU A CA  
1120 C C   . LEU A 144 ? 0.2336 0.2374 0.2362 0.0253  -0.0171 -0.0242 218 LEU A C   
1121 O O   . LEU A 144 ? 0.2415 0.2470 0.2484 0.0254  -0.0187 -0.0253 218 LEU A O   
1122 C CB  . LEU A 144 ? 0.3011 0.3004 0.2951 0.0284  -0.0185 -0.0239 218 LEU A CB  
1123 C CG  . LEU A 144 ? 0.3744 0.3717 0.3650 0.0312  -0.0205 -0.0245 218 LEU A CG  
1124 C CD1 . LEU A 144 ? 0.3414 0.3373 0.3300 0.0313  -0.0215 -0.0246 218 LEU A CD1 
1125 C CD2 . LEU A 144 ? 0.3230 0.3213 0.3163 0.0326  -0.0228 -0.0259 218 LEU A CD2 
1126 N N   . LEU A 145 ? 0.2285 0.2323 0.2304 0.0234  -0.0152 -0.0232 219 LEU A N   
1127 C CA  . LEU A 145 ? 0.2232 0.2290 0.2292 0.0214  -0.0146 -0.0231 219 LEU A CA  
1128 C C   . LEU A 145 ? 0.2220 0.2300 0.2322 0.0208  -0.0135 -0.0233 219 LEU A C   
1129 O O   . LEU A 145 ? 0.2181 0.2281 0.2329 0.0197  -0.0136 -0.0236 219 LEU A O   
1130 C CB  . LEU A 145 ? 0.2024 0.2075 0.2062 0.0198  -0.0128 -0.0219 219 LEU A CB  
1131 C CG  . LEU A 145 ? 0.2005 0.2040 0.2017 0.0201  -0.0138 -0.0217 219 LEU A CG  
1132 C CD1 . LEU A 145 ? 0.2180 0.2205 0.2160 0.0189  -0.0118 -0.0202 219 LEU A CD1 
1133 C CD2 . LEU A 145 ? 0.2156 0.2203 0.2204 0.0194  -0.0151 -0.0224 219 LEU A CD2 
1134 N N   . ASN A 146 ? 0.2276 0.2351 0.2362 0.0214  -0.0123 -0.0230 220 ASN A N   
1135 C CA  . ASN A 146 ? 0.2428 0.2523 0.2552 0.0212  -0.0113 -0.0232 220 ASN A CA  
1136 C C   . ASN A 146 ? 0.2535 0.2647 0.2704 0.0223  -0.0134 -0.0244 220 ASN A C   
1137 O O   . ASN A 146 ? 0.3165 0.3300 0.3382 0.0215  -0.0128 -0.0245 220 ASN A O   
1138 C CB  . ASN A 146 ? 0.2573 0.2656 0.2669 0.0219  -0.0098 -0.0228 220 ASN A CB  
1139 C CG  . ASN A 146 ? 0.2742 0.2813 0.2805 0.0205  -0.0075 -0.0218 220 ASN A CG  
1140 O OD1 . ASN A 146 ? 0.2765 0.2839 0.2829 0.0189  -0.0066 -0.0212 220 ASN A OD1 
1141 N ND2 . ASN A 146 ? 0.2944 0.2998 0.2976 0.0212  -0.0065 -0.0215 220 ASN A ND2 
1142 N N   . ILE A 147 ? 0.2461 0.2562 0.2613 0.0241  -0.0158 -0.0252 221 ILE A N   
1143 C CA  . ILE A 147 ? 0.2705 0.2819 0.2895 0.0254  -0.0183 -0.0264 221 ILE A CA  
1144 C C   . ILE A 147 ? 0.2794 0.2920 0.3021 0.0244  -0.0199 -0.0271 221 ILE A C   
1145 O O   . ILE A 147 ? 0.3023 0.3174 0.3308 0.0242  -0.0209 -0.0277 221 ILE A O   
1146 C CB  . ILE A 147 ? 0.3247 0.3341 0.3397 0.0279  -0.0202 -0.0269 221 ILE A CB  
1147 C CG1 . ILE A 147 ? 0.3972 0.4056 0.4095 0.0289  -0.0186 -0.0263 221 ILE A CG1 
1148 C CG2 . ILE A 147 ? 0.3466 0.3569 0.3646 0.0293  -0.0235 -0.0283 221 ILE A CG2 
1149 C CD1 . ILE A 147 ? 0.4547 0.4606 0.4622 0.0313  -0.0199 -0.0264 221 ILE A CD1 
1150 N N   . HIS A 148 ? 0.2476 0.2586 0.2673 0.0239  -0.0203 -0.0269 222 HIS A N   
1151 C CA  . HIS A 148 ? 0.2520 0.2635 0.2744 0.0232  -0.0222 -0.0276 222 HIS A CA  
1152 C C   . HIS A 148 ? 0.2890 0.3019 0.3142 0.0208  -0.0200 -0.0267 222 HIS A C   
1153 O O   . HIS A 148 ? 0.2584 0.2700 0.2807 0.0198  -0.0189 -0.0259 222 HIS A O   
1154 C CB  . HIS A 148 ? 0.2566 0.2654 0.2740 0.0244  -0.0238 -0.0280 222 HIS A CB  
1155 C CG  . HIS A 148 ? 0.2514 0.2588 0.2662 0.0270  -0.0260 -0.0289 222 HIS A CG  
1156 N ND1 . HIS A 148 ? 0.3053 0.3135 0.3231 0.0280  -0.0292 -0.0304 222 HIS A ND1 
1157 C CD2 . HIS A 148 ? 0.2633 0.2690 0.2734 0.0287  -0.0256 -0.0285 222 HIS A CD2 
1158 C CE1 . HIS A 148 ? 0.2849 0.2917 0.2994 0.0304  -0.0306 -0.0309 222 HIS A CE1 
1159 N NE2 . HIS A 148 ? 0.2935 0.2987 0.3033 0.0309  -0.0285 -0.0297 222 HIS A NE2 
1160 N N   . LYS A 149 ? 0.2756 0.2911 0.3067 0.0199  -0.0194 -0.0268 223 LYS A N   
1161 C CA  . LYS A 149 ? 0.3026 0.3195 0.3363 0.0178  -0.0168 -0.0257 223 LYS A CA  
1162 C C   . LYS A 149 ? 0.2695 0.2859 0.3035 0.0165  -0.0172 -0.0255 223 LYS A C   
1163 O O   . LYS A 149 ? 0.2727 0.2887 0.3049 0.0151  -0.0150 -0.0243 223 LYS A O   
1164 C CB  . LYS A 149 ? 0.3617 0.3817 0.4024 0.0173  -0.0164 -0.0258 223 LYS A CB  
1165 C CG  . LYS A 149 ? 0.4695 0.4905 0.5111 0.0184  -0.0157 -0.0259 223 LYS A CG  
1166 C CD  . LYS A 149 ? 0.5466 0.5663 0.5834 0.0186  -0.0131 -0.0249 223 LYS A CD  
1167 C CE  . LYS A 149 ? 0.5983 0.6196 0.6380 0.0193  -0.0120 -0.0249 223 LYS A CE  
1168 N NZ  . LYS A 149 ? 0.6407 0.6601 0.6752 0.0203  -0.0106 -0.0245 223 LYS A NZ  
1169 N N   . ASN A 150 ? 0.2716 0.2877 0.3073 0.0169  -0.0200 -0.0267 224 ASN A N   
1170 C CA  . ASN A 150 ? 0.2790 0.2946 0.3157 0.0156  -0.0204 -0.0266 224 ASN A CA  
1171 C C   . ASN A 150 ? 0.2591 0.2718 0.2894 0.0163  -0.0208 -0.0265 224 ASN A C   
1172 O O   . ASN A 150 ? 0.2852 0.2972 0.3155 0.0153  -0.0209 -0.0262 224 ASN A O   
1173 C CB  . ASN A 150 ? 0.3253 0.3420 0.3677 0.0156  -0.0231 -0.0280 224 ASN A CB  
1174 C CG  . ASN A 150 ? 0.3708 0.3907 0.4203 0.0147  -0.0223 -0.0279 224 ASN A CG  
1175 O OD1 . ASN A 150 ? 0.4674 0.4885 0.5212 0.0154  -0.0246 -0.0291 224 ASN A OD1 
1176 N ND2 . ASN A 150 ? 0.3842 0.4054 0.4351 0.0133  -0.0191 -0.0264 224 ASN A ND2 
1177 N N   . ALA A 151 ? 0.2453 0.2563 0.2706 0.0179  -0.0211 -0.0265 225 ALA A N   
1178 C CA  . ALA A 151 ? 0.2309 0.2393 0.2502 0.0185  -0.0209 -0.0260 225 ALA A CA  
1179 C C   . ALA A 151 ? 0.2127 0.2211 0.2301 0.0169  -0.0180 -0.0243 225 ALA A C   
1180 O O   . ALA A 151 ? 0.2082 0.2179 0.2266 0.0162  -0.0160 -0.0235 225 ALA A O   
1181 C CB  . ALA A 151 ? 0.2337 0.2404 0.2482 0.0206  -0.0217 -0.0263 225 ALA A CB  
1182 N N   . LYS A 152 ? 0.1985 0.2055 0.2133 0.0165  -0.0178 -0.0237 226 LYS A N   
1183 C CA  . LYS A 152 ? 0.2076 0.2144 0.2203 0.0152  -0.0152 -0.0221 226 LYS A CA  
1184 C C   . LYS A 152 ? 0.2277 0.2322 0.2354 0.0159  -0.0154 -0.0215 226 LYS A C   
1185 O O   . LYS A 152 ? 0.2435 0.2468 0.2508 0.0166  -0.0170 -0.0222 226 LYS A O   
1186 C CB  . LYS A 152 ? 0.2277 0.2359 0.2442 0.0132  -0.0142 -0.0215 226 LYS A CB  
1187 C CG  . LYS A 152 ? 0.2832 0.2939 0.3050 0.0122  -0.0134 -0.0216 226 LYS A CG  
1188 C CD  . LYS A 152 ? 0.3404 0.3521 0.3657 0.0104  -0.0125 -0.0209 226 LYS A CD  
1189 C CE  . LYS A 152 ? 0.4229 0.4369 0.4527 0.0094  -0.0109 -0.0205 226 LYS A CE  
1190 N NZ  . LYS A 152 ? 0.4897 0.5051 0.5243 0.0100  -0.0127 -0.0219 226 LYS A NZ  
1191 N N   . ILE A 153 ? 0.1927 0.1965 0.1969 0.0157  -0.0136 -0.0203 227 ILE A N   
1192 C CA  . ILE A 153 ? 0.1937 0.1958 0.1941 0.0159  -0.0131 -0.0193 227 ILE A CA  
1193 C C   . ILE A 153 ? 0.1925 0.1954 0.1941 0.0140  -0.0116 -0.0181 227 ILE A C   
1194 O O   . ILE A 153 ? 0.2029 0.2072 0.2056 0.0126  -0.0100 -0.0173 227 ILE A O   
1195 C CB  . ILE A 153 ? 0.1988 0.1997 0.1950 0.0167  -0.0121 -0.0184 227 ILE A CB  
1196 C CG1 . ILE A 153 ? 0.2234 0.2231 0.2178 0.0189  -0.0136 -0.0194 227 ILE A CG1 
1197 C CG2 . ILE A 153 ? 0.2062 0.2059 0.1994 0.0164  -0.0111 -0.0170 227 ILE A CG2 
1198 C CD1 . ILE A 153 ? 0.2501 0.2487 0.2411 0.0197  -0.0125 -0.0187 227 ILE A CD1 
1199 N N   . ILE A 154 ? 0.1806 0.1827 0.1818 0.0139  -0.0121 -0.0179 228 ILE A N   
1200 C CA  . ILE A 154 ? 0.1858 0.1884 0.1877 0.0124  -0.0108 -0.0167 228 ILE A CA  
1201 C C   . ILE A 154 ? 0.1734 0.1743 0.1711 0.0130  -0.0103 -0.0156 228 ILE A C   
1202 O O   . ILE A 154 ? 0.1852 0.1843 0.1809 0.0145  -0.0115 -0.0161 228 ILE A O   
1203 C CB  . ILE A 154 ? 0.2064 0.2094 0.2118 0.0117  -0.0116 -0.0172 228 ILE A CB  
1204 C CG1 . ILE A 154 ? 0.2265 0.2311 0.2366 0.0112  -0.0124 -0.0184 228 ILE A CG1 
1205 C CG2 . ILE A 154 ? 0.2076 0.2111 0.2134 0.0101  -0.0100 -0.0157 228 ILE A CG2 
1206 C CD1 . ILE A 154 ? 0.2288 0.2354 0.2411 0.0099  -0.0106 -0.0177 228 ILE A CD1 
1207 N N   . PRO A 155 ? 0.1723 0.1736 0.1684 0.0121  -0.0086 -0.0141 229 PRO A N   
1208 C CA  . PRO A 155 ? 0.1730 0.1728 0.1655 0.0128  -0.0081 -0.0130 229 PRO A CA  
1209 C C   . PRO A 155 ? 0.1694 0.1685 0.1615 0.0129  -0.0082 -0.0123 229 PRO A C   
1210 O O   . PRO A 155 ? 0.1858 0.1859 0.1802 0.0115  -0.0077 -0.0119 229 PRO A O   
1211 C CB  . PRO A 155 ? 0.1913 0.1919 0.1829 0.0116  -0.0065 -0.0117 229 PRO A CB  
1212 C CG  . PRO A 155 ? 0.2335 0.2359 0.2282 0.0100  -0.0060 -0.0119 229 PRO A CG  
1213 C CD  . PRO A 155 ? 0.1790 0.1819 0.1765 0.0105  -0.0072 -0.0134 229 PRO A CD  
1214 N N   . VAL A 156 ? 0.1593 0.1565 0.1486 0.0145  -0.0087 -0.0122 230 VAL A N   
1215 C CA  . VAL A 156 ? 0.1598 0.1560 0.1482 0.0149  -0.0086 -0.0115 230 VAL A CA  
1216 C C   . VAL A 156 ? 0.1631 0.1590 0.1491 0.0149  -0.0071 -0.0096 230 VAL A C   
1217 O O   . VAL A 156 ? 0.1753 0.1712 0.1614 0.0144  -0.0065 -0.0085 230 VAL A O   
1218 C CB  . VAL A 156 ? 0.1672 0.1613 0.1540 0.0169  -0.0102 -0.0128 230 VAL A CB  
1219 C CG1 . VAL A 156 ? 0.1812 0.1737 0.1662 0.0177  -0.0099 -0.0120 230 VAL A CG1 
1220 C CG2 . VAL A 156 ? 0.1892 0.1836 0.1789 0.0167  -0.0118 -0.0147 230 VAL A CG2 
1221 N N   . ASP A 157 ? 0.1506 0.1463 0.1348 0.0153  -0.0065 -0.0091 231 ASP A N   
1222 C CA  . ASP A 157 ? 0.1551 0.1508 0.1378 0.0150  -0.0052 -0.0072 231 ASP A CA  
1223 C C   . ASP A 157 ? 0.1551 0.1526 0.1399 0.0129  -0.0044 -0.0061 231 ASP A C   
1224 O O   . ASP A 157 ? 0.1612 0.1601 0.1480 0.0115  -0.0044 -0.0066 231 ASP A O   
1225 C CB  . ASP A 157 ? 0.1540 0.1496 0.1354 0.0153  -0.0047 -0.0070 231 ASP A CB  
1226 C CG  . ASP A 157 ? 0.1542 0.1494 0.1340 0.0155  -0.0035 -0.0052 231 ASP A CG  
1227 O OD1 . ASP A 157 ? 0.1629 0.1580 0.1426 0.0155  -0.0030 -0.0041 231 ASP A OD1 
1228 O OD2 . ASP A 157 ? 0.1595 0.1543 0.1382 0.0158  -0.0031 -0.0050 231 ASP A OD2 
1229 N N   . SER A 158 ? 0.1502 0.1477 0.1346 0.0128  -0.0036 -0.0046 232 SER A N   
1230 C CA  . SER A 158 ? 0.1537 0.1526 0.1401 0.0111  -0.0031 -0.0037 232 SER A CA  
1231 C C   . SER A 158 ? 0.1400 0.1406 0.1274 0.0092  -0.0026 -0.0032 232 SER A C   
1232 O O   . SER A 158 ? 0.1480 0.1498 0.1372 0.0079  -0.0025 -0.0033 232 SER A O   
1233 C CB  . SER A 158 ? 0.1563 0.1549 0.1421 0.0115  -0.0025 -0.0020 232 SER A CB  
1234 O OG  . SER A 158 ? 0.1692 0.1682 0.1541 0.0112  -0.0016 -0.0005 232 SER A OG  
1235 N N   . GLU A 159 ? 0.1324 0.1330 0.1186 0.0091  -0.0022 -0.0027 233 GLU A N   
1236 C CA  . GLU A 159 ? 0.1337 0.1356 0.1204 0.0074  -0.0017 -0.0023 233 GLU A CA  
1237 C C   . GLU A 159 ? 0.1392 0.1415 0.1267 0.0070  -0.0020 -0.0039 233 GLU A C   
1238 O O   . GLU A 159 ? 0.1429 0.1463 0.1314 0.0056  -0.0017 -0.0038 233 GLU A O   
1239 C CB  . GLU A 159 ? 0.1413 0.1428 0.1266 0.0076  -0.0013 -0.0015 233 GLU A CB  
1240 C CG  . GLU A 159 ? 0.1557 0.1570 0.1406 0.0080  -0.0009 0.0001  233 GLU A CG  
1241 C CD  . GLU A 159 ? 0.1527 0.1524 0.1362 0.0101  -0.0009 0.0001  233 GLU A CD  
1242 O OE1 . GLU A 159 ? 0.1591 0.1578 0.1419 0.0113  -0.0015 -0.0013 233 GLU A OE1 
1243 O OE2 . GLU A 159 ? 0.1705 0.1700 0.1537 0.0106  -0.0002 0.0016  233 GLU A OE2 
1244 N N   . HIS A 160 ? 0.1390 0.1403 0.1261 0.0084  -0.0027 -0.0052 234 HIS A N   
1245 C CA  . HIS A 160 ? 0.1458 0.1476 0.1341 0.0082  -0.0030 -0.0067 234 HIS A CA  
1246 C C   . HIS A 160 ? 0.1357 0.1382 0.1265 0.0078  -0.0034 -0.0074 234 HIS A C   
1247 O O   . HIS A 160 ? 0.1420 0.1456 0.1344 0.0068  -0.0031 -0.0079 234 HIS A O   
1248 C CB  . HIS A 160 ? 0.1495 0.1501 0.1366 0.0099  -0.0037 -0.0078 234 HIS A CB  
1249 C CG  . HIS A 160 ? 0.1460 0.1456 0.1308 0.0103  -0.0031 -0.0068 234 HIS A CG  
1250 N ND1 . HIS A 160 ? 0.1598 0.1586 0.1433 0.0110  -0.0029 -0.0057 234 HIS A ND1 
1251 C CD2 . HIS A 160 ? 0.1579 0.1574 0.1418 0.0099  -0.0026 -0.0067 234 HIS A CD2 
1252 C CE1 . HIS A 160 ? 0.1622 0.1606 0.1445 0.0110  -0.0023 -0.0048 234 HIS A CE1 
1253 N NE2 . HIS A 160 ? 0.1626 0.1612 0.1450 0.0103  -0.0022 -0.0054 234 HIS A NE2 
1254 N N   . SER A 161 ? 0.1430 0.1450 0.1342 0.0084  -0.0038 -0.0073 235 SER A N   
1255 C CA  . SER A 161 ? 0.1387 0.1413 0.1324 0.0077  -0.0040 -0.0076 235 SER A CA  
1256 C C   . SER A 161 ? 0.1451 0.1491 0.1396 0.0060  -0.0029 -0.0063 235 SER A C   
1257 O O   . SER A 161 ? 0.1480 0.1530 0.1447 0.0050  -0.0025 -0.0066 235 SER A O   
1258 C CB  . SER A 161 ? 0.1512 0.1526 0.1446 0.0087  -0.0046 -0.0075 235 SER A CB  
1259 O OG  . SER A 161 ? 0.1568 0.1587 0.1529 0.0079  -0.0047 -0.0077 235 SER A OG  
1260 N N   . ALA A 162 ? 0.1354 0.1395 0.1283 0.0056  -0.0023 -0.0048 236 ALA A N   
1261 C CA  . ALA A 162 ? 0.1441 0.1494 0.1374 0.0041  -0.0014 -0.0036 236 ALA A CA  
1262 C C   . ALA A 162 ? 0.1348 0.1409 0.1282 0.0032  -0.0009 -0.0041 236 ALA A C   
1263 O O   . ALA A 162 ? 0.1339 0.1408 0.1287 0.0022  -0.0003 -0.0039 236 ALA A O   
1264 C CB  . ALA A 162 ? 0.1496 0.1547 0.1411 0.0039  -0.0011 -0.0020 236 ALA A CB  
1265 N N   . ILE A 163 ? 0.1402 0.1458 0.1321 0.0035  -0.0010 -0.0046 237 ILE A N   
1266 C CA  . ILE A 163 ? 0.1435 0.1495 0.1352 0.0029  -0.0005 -0.0052 237 ILE A CA  
1267 C C   . ILE A 163 ? 0.1424 0.1491 0.1366 0.0029  -0.0004 -0.0063 237 ILE A C   
1268 O O   . ILE A 163 ? 0.1509 0.1584 0.1459 0.0020  0.0004  -0.0061 237 ILE A O   
1269 C CB  . ILE A 163 ? 0.1506 0.1557 0.1405 0.0036  -0.0008 -0.0058 237 ILE A CB  
1270 C CG1 . ILE A 163 ? 0.1614 0.1661 0.1494 0.0032  -0.0007 -0.0046 237 ILE A CG1 
1271 C CG2 . ILE A 163 ? 0.1637 0.1691 0.1538 0.0033  -0.0003 -0.0068 237 ILE A CG2 
1272 C CD1 . ILE A 163 ? 0.1756 0.1791 0.1621 0.0042  -0.0010 -0.0049 237 ILE A CD1 
1273 N N   . PHE A 164 ? 0.1449 0.1511 0.1404 0.0040  -0.0013 -0.0073 238 PHE A N   
1274 C CA  . PHE A 164 ? 0.1486 0.1556 0.1471 0.0040  -0.0014 -0.0084 238 PHE A CA  
1275 C C   . PHE A 164 ? 0.1515 0.1594 0.1523 0.0030  -0.0007 -0.0077 238 PHE A C   
1276 O O   . PHE A 164 ? 0.1644 0.1733 0.1673 0.0024  0.0000  -0.0079 238 PHE A O   
1277 C CB  . PHE A 164 ? 0.1602 0.1663 0.1594 0.0055  -0.0028 -0.0096 238 PHE A CB  
1278 C CG  . PHE A 164 ? 0.1719 0.1788 0.1744 0.0057  -0.0034 -0.0110 238 PHE A CG  
1279 C CD1 . PHE A 164 ? 0.1862 0.1936 0.1890 0.0058  -0.0029 -0.0116 238 PHE A CD1 
1280 C CD2 . PHE A 164 ? 0.1988 0.2056 0.2038 0.0060  -0.0043 -0.0117 238 PHE A CD2 
1281 C CE1 . PHE A 164 ? 0.2113 0.2197 0.2176 0.0060  -0.0034 -0.0128 238 PHE A CE1 
1282 C CE2 . PHE A 164 ? 0.2114 0.2191 0.2199 0.0061  -0.0050 -0.0129 238 PHE A CE2 
1283 C CZ  . PHE A 164 ? 0.2103 0.2188 0.2193 0.0062  -0.0045 -0.0134 238 PHE A CZ  
1284 N N   . GLN A 165 ? 0.1590 0.1665 0.1594 0.0029  -0.0009 -0.0067 239 GLN A N   
1285 C CA  . GLN A 165 ? 0.1533 0.1615 0.1556 0.0020  -0.0002 -0.0058 239 GLN A CA  
1286 C C   . GLN A 165 ? 0.1661 0.1751 0.1676 0.0008  0.0011  -0.0047 239 GLN A C   
1287 O O   . GLN A 165 ? 0.2195 0.2292 0.2229 0.0001  0.0020  -0.0041 239 GLN A O   
1288 C CB  . GLN A 165 ? 0.1477 0.1550 0.1493 0.0022  -0.0006 -0.0049 239 GLN A CB  
1289 C CG  . GLN A 165 ? 0.1408 0.1470 0.1435 0.0034  -0.0019 -0.0061 239 GLN A CG  
1290 C CD  . GLN A 165 ? 0.1554 0.1607 0.1573 0.0037  -0.0021 -0.0052 239 GLN A CD  
1291 O OE1 . GLN A 165 ? 0.1606 0.1662 0.1638 0.0029  -0.0015 -0.0042 239 GLN A OE1 
1292 N NE2 . GLN A 165 ? 0.1604 0.1645 0.1600 0.0049  -0.0028 -0.0053 239 GLN A NE2 
1293 N N   . CYS A 166 ? 0.1562 0.1650 0.1548 0.0007  0.0013  -0.0043 240 CYS A N   
1294 C CA  . CYS A 166 ? 0.1758 0.1852 0.1729 -0.0002 0.0024  -0.0034 240 CYS A CA  
1295 C C   . CYS A 166 ? 0.1842 0.1940 0.1821 -0.0004 0.0033  -0.0042 240 CYS A C   
1296 O O   . CYS A 166 ? 0.2059 0.2160 0.2023 -0.0010 0.0044  -0.0036 240 CYS A O   
1297 C CB  . CYS A 166 ? 0.1741 0.1829 0.1680 -0.0004 0.0021  -0.0029 240 CYS A CB  
1298 S SG  . CYS A 166 ? 0.2227 0.2313 0.2157 -0.0003 0.0015  -0.0015 240 CYS A SG  
1299 N N   . LEU A 167 ? 0.1931 0.2031 0.1930 0.0002  0.0030  -0.0055 241 LEU A N   
1300 C CA  . LEU A 167 ? 0.1976 0.2080 0.1985 0.0002  0.0038  -0.0063 241 LEU A CA  
1301 C C   . LEU A 167 ? 0.2212 0.2327 0.2258 -0.0001 0.0047  -0.0061 241 LEU A C   
1302 O O   . LEU A 167 ? 0.2894 0.3011 0.2962 -0.0002 0.0043  -0.0058 241 LEU A O   
1303 C CB  . LEU A 167 ? 0.1934 0.2034 0.1947 0.0013  0.0029  -0.0078 241 LEU A CB  
1304 C CG  . LEU A 167 ? 0.1871 0.1960 0.1851 0.0018  0.0021  -0.0079 241 LEU A CG  
1305 C CD1 . LEU A 167 ? 0.1960 0.2045 0.1945 0.0029  0.0012  -0.0094 241 LEU A CD1 
1306 C CD2 . LEU A 167 ? 0.2029 0.2114 0.1977 0.0011  0.0029  -0.0074 241 LEU A CD2 
1307 N N   . ASP A 168 ? 0.2183 0.2304 0.2234 -0.0002 0.0061  -0.0061 242 ASP A N   
1308 C CA  . ASP A 168 ? 0.2438 0.2569 0.2526 -0.0006 0.0073  -0.0058 242 ASP A CA  
1309 C C   . ASP A 168 ? 0.2318 0.2457 0.2446 0.0000  0.0066  -0.0072 242 ASP A C   
1310 O O   . ASP A 168 ? 0.2198 0.2337 0.2321 0.0006  0.0066  -0.0081 242 ASP A O   
1311 C CB  . ASP A 168 ? 0.2714 0.2847 0.2784 -0.0009 0.0093  -0.0051 242 ASP A CB  
1312 C CG  . ASP A 168 ? 0.3501 0.3646 0.3608 -0.0011 0.0111  -0.0045 242 ASP A CG  
1313 O OD1 . ASP A 168 ? 0.3212 0.3364 0.3361 -0.0013 0.0107  -0.0046 242 ASP A OD1 
1314 O OD2 . ASP A 168 ? 0.4012 0.4157 0.4102 -0.0011 0.0129  -0.0040 242 ASP A OD2 
1315 N N   . ASN A 169 ? 0.2243 0.2387 0.2409 0.0000  0.0059  -0.0073 243 ASN A N   
1316 C CA  . ASN A 169 ? 0.2255 0.2404 0.2459 0.0005  0.0047  -0.0087 243 ASN A CA  
1317 C C   . ASN A 169 ? 0.2588 0.2752 0.2824 0.0005  0.0061  -0.0089 243 ASN A C   
1318 O O   . ASN A 169 ? 0.2633 0.2802 0.2893 0.0012  0.0053  -0.0101 243 ASN A O   
1319 C CB  . ASN A 169 ? 0.2446 0.2595 0.2683 0.0004  0.0033  -0.0091 243 ASN A CB  
1320 C CG  . ASN A 169 ? 0.2494 0.2627 0.2700 0.0009  0.0016  -0.0094 243 ASN A CG  
1321 O OD1 . ASN A 169 ? 0.3242 0.3370 0.3455 0.0006  0.0011  -0.0089 243 ASN A OD1 
1322 N ND2 . ASN A 169 ? 0.2712 0.2838 0.2889 0.0018  0.0006  -0.0102 243 ASN A ND2 
1323 N N   . ASN A 170 ? 0.2678 0.2846 0.2912 -0.0001 0.0084  -0.0076 244 ASN A N   
1324 C CA  . ASN A 170 ? 0.2867 0.3047 0.3125 0.0000  0.0102  -0.0075 244 ASN A CA  
1325 C C   . ASN A 170 ? 0.2960 0.3136 0.3192 0.0009  0.0099  -0.0086 244 ASN A C   
1326 O O   . ASN A 170 ? 0.3163 0.3349 0.3422 0.0014  0.0105  -0.0092 244 ASN A O   
1327 C CB  . ASN A 170 ? 0.3188 0.3368 0.3432 -0.0006 0.0127  -0.0058 244 ASN A CB  
1328 C CG  . ASN A 170 ? 0.4062 0.4255 0.4335 -0.0004 0.0150  -0.0054 244 ASN A CG  
1329 O OD1 . ASN A 170 ? 0.3911 0.4118 0.4241 -0.0003 0.0149  -0.0059 244 ASN A OD1 
1330 N ND2 . ASN A 170 ? 0.4081 0.4267 0.4317 -0.0003 0.0170  -0.0046 244 ASN A ND2 
1331 N N   . LYS A 171 ? 0.2624 0.2785 0.2803 0.0011  0.0093  -0.0087 245 LYS A N   
1332 C CA  . LYS A 171 ? 0.2400 0.2554 0.2552 0.0019  0.0089  -0.0097 245 LYS A CA  
1333 C C   . LYS A 171 ? 0.2282 0.2433 0.2440 0.0027  0.0066  -0.0110 245 LYS A C   
1334 O O   . LYS A 171 ? 0.2358 0.2510 0.2524 0.0036  0.0062  -0.0120 245 LYS A O   
1335 C CB  . LYS A 171 ? 0.2613 0.2752 0.2707 0.0016  0.0093  -0.0092 245 LYS A CB  
1336 C CG  . LYS A 171 ? 0.3205 0.3343 0.3282 0.0010  0.0115  -0.0080 245 LYS A CG  
1337 C CD  . LYS A 171 ? 0.4064 0.4207 0.4150 0.0016  0.0134  -0.0082 245 LYS A CD  
1338 C CE  . LYS A 171 ? 0.4910 0.5048 0.4971 0.0012  0.0157  -0.0069 245 LYS A CE  
1339 N NZ  . LYS A 171 ? 0.5353 0.5479 0.5368 0.0005  0.0151  -0.0062 245 LYS A NZ  
1340 N N   . VAL A 172 ? 0.2139 0.2284 0.2292 0.0026  0.0050  -0.0110 246 VAL A N   
1341 C CA  . VAL A 172 ? 0.2168 0.2307 0.2321 0.0035  0.0028  -0.0122 246 VAL A CA  
1342 C C   . VAL A 172 ? 0.2331 0.2482 0.2532 0.0042  0.0021  -0.0133 246 VAL A C   
1343 O O   . VAL A 172 ? 0.2264 0.2412 0.2461 0.0053  0.0009  -0.0144 246 VAL A O   
1344 C CB  . VAL A 172 ? 0.2071 0.2202 0.2217 0.0034  0.0014  -0.0119 246 VAL A CB  
1345 C CG1 . VAL A 172 ? 0.2017 0.2140 0.2163 0.0045  -0.0007 -0.0132 246 VAL A CG1 
1346 C CG2 . VAL A 172 ? 0.2031 0.2150 0.2132 0.0029  0.0019  -0.0108 246 VAL A CG2 
1347 N N   . LEU A 173 ? 0.2453 0.2618 0.2699 0.0035  0.0028  -0.0129 247 LEU A N   
1348 C CA  . LEU A 173 ? 0.2489 0.2668 0.2789 0.0039  0.0018  -0.0139 247 LEU A CA  
1349 C C   . LEU A 173 ? 0.2602 0.2791 0.2913 0.0047  0.0026  -0.0144 247 LEU A C   
1350 O O   . LEU A 173 ? 0.2917 0.3117 0.3269 0.0053  0.0014  -0.0155 247 LEU A O   
1351 C CB  . LEU A 173 ? 0.2759 0.2951 0.3109 0.0029  0.0024  -0.0133 247 LEU A CB  
1352 C CG  . LEU A 173 ? 0.3070 0.3251 0.3419 0.0024  0.0009  -0.0133 247 LEU A CG  
1353 C CD1 . LEU A 173 ? 0.3257 0.3449 0.3650 0.0013  0.0021  -0.0123 247 LEU A CD1 
1354 C CD2 . LEU A 173 ? 0.3161 0.3339 0.3527 0.0033  -0.0019 -0.0149 247 LEU A CD2 
1355 N N   . LYS A 174 ? 0.2472 0.2655 0.2748 0.0047  0.0044  -0.0139 248 LYS A N   
1356 C CA  . LYS A 174 ? 0.2585 0.2773 0.2864 0.0055  0.0053  -0.0144 248 LYS A CA  
1357 C C   . LYS A 174 ? 0.2664 0.2839 0.2913 0.0067  0.0036  -0.0155 248 LYS A C   
1358 O O   . LYS A 174 ? 0.2966 0.3144 0.3221 0.0077  0.0039  -0.0161 248 LYS A O   
1359 C CB  . LYS A 174 ? 0.2767 0.2950 0.3015 0.0052  0.0079  -0.0134 248 LYS A CB  
1360 C CG  . LYS A 174 ? 0.3153 0.3346 0.3423 0.0042  0.0100  -0.0121 248 LYS A CG  
1361 C CD  . LYS A 174 ? 0.4163 0.4347 0.4391 0.0039  0.0124  -0.0111 248 LYS A CD  
1362 C CE  . LYS A 174 ? 0.5269 0.5463 0.5519 0.0035  0.0150  -0.0099 248 LYS A CE  
1363 N NZ  . LYS A 174 ? 0.5950 0.6158 0.6251 0.0027  0.0149  -0.0092 248 LYS A NZ  
1364 N N   . THR A 175 ? 0.2317 0.2478 0.2535 0.0068  0.0019  -0.0157 249 THR A N   
1365 C CA  . THR A 175 ? 0.2373 0.2520 0.2560 0.0080  0.0005  -0.0165 249 THR A CA  
1366 C C   . THR A 175 ? 0.2137 0.2277 0.2321 0.0083  -0.0017 -0.0169 249 THR A C   
1367 O O   . THR A 175 ? 0.2197 0.2345 0.2416 0.0080  -0.0025 -0.0171 249 THR A O   
1368 C CB  . THR A 175 ? 0.2630 0.2760 0.2764 0.0078  0.0017  -0.0159 249 THR A CB  
1369 O OG1 . THR A 175 ? 0.2943 0.3059 0.3048 0.0090  0.0006  -0.0165 249 THR A OG1 
1370 C CG2 . THR A 175 ? 0.2499 0.2622 0.2605 0.0067  0.0023  -0.0148 249 THR A CG2 
1371 N N   . LYS A 176 ? 0.1948 0.2069 0.2088 0.0090  -0.0025 -0.0170 250 LYS A N   
1372 C CA  . LYS A 176 ? 0.1962 0.2072 0.2089 0.0095  -0.0043 -0.0172 250 LYS A CA  
1373 C C   . LYS A 176 ? 0.1705 0.1796 0.1781 0.0100  -0.0043 -0.0168 250 LYS A C   
1374 O O   . LYS A 176 ? 0.1808 0.1894 0.1864 0.0102  -0.0033 -0.0167 250 LYS A O   
1375 C CB  . LYS A 176 ? 0.1857 0.1970 0.2011 0.0107  -0.0066 -0.0186 250 LYS A CB  
1376 C CG  . LYS A 176 ? 0.2026 0.2136 0.2173 0.0123  -0.0074 -0.0195 250 LYS A CG  
1377 C CD  . LYS A 176 ? 0.1979 0.2094 0.2155 0.0135  -0.0098 -0.0208 250 LYS A CD  
1378 C CE  . LYS A 176 ? 0.2068 0.2178 0.2230 0.0152  -0.0106 -0.0216 250 LYS A CE  
1379 N NZ  . LYS A 176 ? 0.2142 0.2258 0.2335 0.0164  -0.0131 -0.0229 250 LYS A NZ  
1380 N N   . CYS A 177 ? 0.1706 0.1785 0.1761 0.0102  -0.0052 -0.0165 251 CYS A N   
1381 C CA  . CYS A 177 ? 0.1821 0.1882 0.1831 0.0107  -0.0050 -0.0159 251 CYS A CA  
1382 C C   . CYS A 177 ? 0.1872 0.1925 0.1867 0.0123  -0.0057 -0.0167 251 CYS A C   
1383 O O   . CYS A 177 ? 0.1863 0.1919 0.1876 0.0134  -0.0070 -0.0178 251 CYS A O   
1384 C CB  . CYS A 177 ? 0.1885 0.1936 0.1878 0.0109  -0.0059 -0.0154 251 CYS A CB  
1385 S SG  . CYS A 177 ? 0.2063 0.2122 0.2066 0.0091  -0.0049 -0.0142 251 CYS A SG  
1386 N N   . LEU A 178 ? 0.1934 0.1973 0.1895 0.0123  -0.0049 -0.0160 252 LEU A N   
1387 C CA  . LEU A 178 ? 0.2050 0.2076 0.1990 0.0138  -0.0054 -0.0164 252 LEU A CA  
1388 C C   . LEU A 178 ? 0.2048 0.2083 0.2008 0.0142  -0.0051 -0.0173 252 LEU A C   
1389 O O   . LEU A 178 ? 0.2340 0.2374 0.2306 0.0158  -0.0062 -0.0182 252 LEU A O   
1390 C CB  . LEU A 178 ? 0.2175 0.2190 0.2103 0.0155  -0.0070 -0.0168 252 LEU A CB  
1391 C CG  . LEU A 178 ? 0.2405 0.2399 0.2293 0.0165  -0.0067 -0.0160 252 LEU A CG  
1392 C CD1 . LEU A 178 ? 0.2642 0.2623 0.2513 0.0182  -0.0081 -0.0162 252 LEU A CD1 
1393 C CD2 . LEU A 178 ? 0.2505 0.2493 0.2383 0.0172  -0.0062 -0.0163 252 LEU A CD2 
1394 N N   . GLN A 179 ? 0.2027 0.2071 0.1996 0.0130  -0.0036 -0.0170 253 GLN A N   
1395 C CA  . GLN A 179 ? 0.2134 0.2186 0.2122 0.0132  -0.0028 -0.0176 253 GLN A CA  
1396 C C   . GLN A 179 ? 0.2293 0.2338 0.2259 0.0123  -0.0010 -0.0171 253 GLN A C   
1397 O O   . GLN A 179 ? 0.2219 0.2261 0.2169 0.0110  -0.0002 -0.0162 253 GLN A O   
1398 C CB  . GLN A 179 ? 0.2173 0.2248 0.2205 0.0125  -0.0026 -0.0179 253 GLN A CB  
1399 C CG  . GLN A 179 ? 0.2315 0.2397 0.2375 0.0133  -0.0046 -0.0186 253 GLN A CG  
1400 C CD  . GLN A 179 ? 0.2383 0.2467 0.2455 0.0150  -0.0058 -0.0197 253 GLN A CD  
1401 O OE1 . GLN A 179 ? 0.2765 0.2834 0.2812 0.0164  -0.0070 -0.0200 253 GLN A OE1 
1402 N NE2 . GLN A 179 ? 0.2340 0.2442 0.2451 0.0149  -0.0053 -0.0201 253 GLN A NE2 
1403 N N   . ASP A 180 ? 0.2177 0.2217 0.2140 0.0131  -0.0005 -0.0176 254 ASP A N   
1404 C CA  . ASP A 180 ? 0.2297 0.2330 0.2241 0.0124  0.0011  -0.0174 254 ASP A CA  
1405 C C   . ASP A 180 ? 0.2090 0.2137 0.2051 0.0111  0.0024  -0.0170 254 ASP A C   
1406 O O   . ASP A 180 ? 0.2346 0.2411 0.2342 0.0110  0.0023  -0.0172 254 ASP A O   
1407 C CB  . ASP A 180 ? 0.2594 0.2622 0.2541 0.0137  0.0015  -0.0181 254 ASP A CB  
1408 C CG  . ASP A 180 ? 0.3263 0.3272 0.3187 0.0150  0.0007  -0.0183 254 ASP A CG  
1409 O OD1 . ASP A 180 ? 0.3826 0.3822 0.3724 0.0148  0.0002  -0.0177 254 ASP A OD1 
1410 O OD2 . ASP A 180 ? 0.4454 0.4463 0.4387 0.0164  0.0006  -0.0190 254 ASP A OD2 
1411 N N   . ASN A 181 ? 0.2391 0.2427 0.2322 0.0099  0.0035  -0.0164 255 ASN A N   
1412 C CA  . ASN A 181 ? 0.2811 0.2854 0.2746 0.0088  0.0050  -0.0160 255 ASN A CA  
1413 C C   . ASN A 181 ? 0.2310 0.2365 0.2256 0.0077  0.0046  -0.0152 255 ASN A C   
1414 O O   . ASN A 181 ? 0.2303 0.2366 0.2255 0.0069  0.0059  -0.0147 255 ASN A O   
1415 C CB  . ASN A 181 ? 0.3048 0.3104 0.3011 0.0094  0.0062  -0.0165 255 ASN A CB  
1416 C CG  . ASN A 181 ? 0.4059 0.4101 0.4006 0.0104  0.0068  -0.0172 255 ASN A CG  
1417 O OD1 . ASN A 181 ? 0.4954 0.4976 0.4863 0.0101  0.0072  -0.0172 255 ASN A OD1 
1418 N ND2 . ASN A 181 ? 0.4446 0.4499 0.4423 0.0117  0.0067  -0.0178 255 ASN A ND2 
1419 N N   . PHE A 182 ? 0.2099 0.2155 0.2049 0.0078  0.0032  -0.0150 256 PHE A N   
1420 C CA  . PHE A 182 ? 0.2010 0.2076 0.1973 0.0069  0.0028  -0.0143 256 PHE A CA  
1421 C C   . PHE A 182 ? 0.1973 0.2034 0.1911 0.0056  0.0038  -0.0133 256 PHE A C   
1422 O O   . PHE A 182 ? 0.1885 0.1957 0.1838 0.0048  0.0045  -0.0127 256 PHE A O   
1423 C CB  . PHE A 182 ? 0.1953 0.2015 0.1914 0.0075  0.0012  -0.0143 256 PHE A CB  
1424 C CG  . PHE A 182 ? 0.1825 0.1894 0.1800 0.0068  0.0007  -0.0136 256 PHE A CG  
1425 C CD1 . PHE A 182 ? 0.1729 0.1793 0.1682 0.0058  0.0010  -0.0125 256 PHE A CD1 
1426 C CD2 . PHE A 182 ? 0.1840 0.1921 0.1851 0.0072  0.0000  -0.0142 256 PHE A CD2 
1427 C CE1 . PHE A 182 ? 0.1721 0.1792 0.1688 0.0052  0.0006  -0.0119 256 PHE A CE1 
1428 C CE2 . PHE A 182 ? 0.1761 0.1847 0.1784 0.0066  -0.0004 -0.0136 256 PHE A CE2 
1429 C CZ  . PHE A 182 ? 0.1861 0.1942 0.1862 0.0056  0.0000  -0.0125 256 PHE A CZ  
1430 N N   . SER A 183 ? 0.1874 0.1919 0.1777 0.0053  0.0038  -0.0131 257 SER A N   
1431 C CA  . SER A 183 ? 0.1927 0.1968 0.1806 0.0040  0.0044  -0.0122 257 SER A CA  
1432 C C   . SER A 183 ? 0.2064 0.2107 0.1939 0.0036  0.0060  -0.0122 257 SER A C   
1433 O O   . SER A 183 ? 0.2001 0.2048 0.1869 0.0027  0.0066  -0.0114 257 SER A O   
1434 C CB  . SER A 183 ? 0.2041 0.2066 0.1889 0.0038  0.0038  -0.0120 257 SER A CB  
1435 O OG  . SER A 183 ? 0.2809 0.2820 0.2643 0.0044  0.0041  -0.0128 257 SER A OG  
1436 N N   . LYS A 184 ? 0.2133 0.2173 0.2011 0.0044  0.0068  -0.0131 258 LYS A N   
1437 C CA  . LYS A 184 ? 0.2212 0.2253 0.2085 0.0042  0.0085  -0.0131 258 LYS A CA  
1438 C C   . LYS A 184 ? 0.2079 0.2140 0.1987 0.0040  0.0093  -0.0126 258 LYS A C   
1439 O O   . LYS A 184 ? 0.2152 0.2215 0.2050 0.0034  0.0106  -0.0118 258 LYS A O   
1440 C CB  . LYS A 184 ? 0.2696 0.2730 0.2569 0.0054  0.0092  -0.0142 258 LYS A CB  
1441 C CG  . LYS A 184 ? 0.3810 0.3844 0.3679 0.0055  0.0113  -0.0142 258 LYS A CG  
1442 C CD  . LYS A 184 ? 0.4609 0.4631 0.4470 0.0066  0.0119  -0.0152 258 LYS A CD  
1443 C CE  . LYS A 184 ? 0.5466 0.5477 0.5303 0.0067  0.0139  -0.0153 258 LYS A CE  
1444 N NZ  . LYS A 184 ? 0.6378 0.6408 0.6238 0.0065  0.0155  -0.0145 258 LYS A NZ  
1445 N N   . ILE A 185 ? 0.1946 0.2021 0.1893 0.0046  0.0087  -0.0129 259 ILE A N   
1446 C CA  . ILE A 185 ? 0.2035 0.2130 0.2023 0.0044  0.0093  -0.0125 259 ILE A CA  
1447 C C   . ILE A 185 ? 0.2006 0.2103 0.1989 0.0033  0.0092  -0.0113 259 ILE A C   
1448 O O   . ILE A 185 ? 0.2136 0.2242 0.2134 0.0028  0.0105  -0.0105 259 ILE A O   
1449 C CB  . ILE A 185 ? 0.2311 0.2418 0.2342 0.0052  0.0081  -0.0132 259 ILE A CB  
1450 C CG1 . ILE A 185 ? 0.2654 0.2761 0.2694 0.0065  0.0085  -0.0142 259 ILE A CG1 
1451 C CG2 . ILE A 185 ? 0.2612 0.2738 0.2690 0.0048  0.0084  -0.0127 259 ILE A CG2 
1452 C CD1 . ILE A 185 ? 0.3290 0.3405 0.3362 0.0075  0.0068  -0.0151 259 ILE A CD1 
1453 N N   . ASN A 186 ? 0.1867 0.1955 0.1829 0.0030  0.0077  -0.0111 260 ASN A N   
1454 C CA  . ASN A 186 ? 0.1892 0.1983 0.1852 0.0021  0.0074  -0.0100 260 ASN A CA  
1455 C C   . ASN A 186 ? 0.1808 0.1888 0.1726 0.0012  0.0080  -0.0092 260 ASN A C   
1456 O O   . ASN A 186 ? 0.1934 0.2017 0.1846 0.0005  0.0077  -0.0082 260 ASN A O   
1457 C CB  . ASN A 186 ? 0.1800 0.1890 0.1765 0.0023  0.0055  -0.0101 260 ASN A CB  
1458 C CG  . ASN A 186 ? 0.1859 0.1961 0.1867 0.0029  0.0049  -0.0107 260 ASN A CG  
1459 O OD1 . ASN A 186 ? 0.2095 0.2206 0.2128 0.0023  0.0051  -0.0101 260 ASN A OD1 
1460 N ND2 . ASN A 186 ? 0.1888 0.1988 0.1904 0.0039  0.0040  -0.0118 260 ASN A ND2 
1461 N N   . ASN A 187 ? 0.1819 0.1888 0.1709 0.0014  0.0087  -0.0097 261 ASN A N   
1462 C CA  . ASN A 187 ? 0.1864 0.1921 0.1712 0.0006  0.0090  -0.0091 261 ASN A CA  
1463 C C   . ASN A 187 ? 0.1674 0.1725 0.1504 0.0000  0.0074  -0.0086 261 ASN A C   
1464 O O   . ASN A 187 ? 0.1677 0.1725 0.1484 -0.0007 0.0073  -0.0077 261 ASN A O   
1465 C CB  . ASN A 187 ? 0.2089 0.2153 0.1937 0.0001  0.0104  -0.0080 261 ASN A CB  
1466 C CG  . ASN A 187 ? 0.2611 0.2680 0.2473 0.0007  0.0124  -0.0083 261 ASN A CG  
1467 O OD1 . ASN A 187 ? 0.2895 0.2956 0.2747 0.0014  0.0129  -0.0092 261 ASN A OD1 
1468 N ND2 . ASN A 187 ? 0.3275 0.3358 0.3165 0.0006  0.0135  -0.0074 261 ASN A ND2 
1469 N N   . ILE A 188 ? 0.1620 0.1668 0.1457 0.0005  0.0062  -0.0091 262 ILE A N   
1470 C CA  . ILE A 188 ? 0.1672 0.1714 0.1496 0.0001  0.0048  -0.0086 262 ILE A CA  
1471 C C   . ILE A 188 ? 0.1677 0.1703 0.1468 -0.0001 0.0046  -0.0089 262 ILE A C   
1472 O O   . ILE A 188 ? 0.1858 0.1873 0.1643 0.0004  0.0048  -0.0099 262 ILE A O   
1473 C CB  . ILE A 188 ? 0.1703 0.1748 0.1548 0.0009  0.0038  -0.0089 262 ILE A CB  
1474 C CG1 . ILE A 188 ? 0.1797 0.1856 0.1674 0.0012  0.0038  -0.0087 262 ILE A CG1 
1475 C CG2 . ILE A 188 ? 0.1802 0.1839 0.1632 0.0006  0.0027  -0.0082 262 ILE A CG2 
1476 C CD1 . ILE A 188 ? 0.1813 0.1873 0.1709 0.0022  0.0027  -0.0093 262 ILE A CD1 
1477 N N   . ASN A 189 ? 0.1598 0.1619 0.1368 -0.0011 0.0039  -0.0081 263 ASN A N   
1478 C CA  . ASN A 189 ? 0.1611 0.1616 0.1353 -0.0016 0.0034  -0.0084 263 ASN A CA  
1479 C C   . ASN A 189 ? 0.1673 0.1675 0.1419 -0.0017 0.0021  -0.0079 263 ASN A C   
1480 O O   . ASN A 189 ? 0.1936 0.1923 0.1671 -0.0016 0.0017  -0.0085 263 ASN A O   
1481 C CB  . ASN A 189 ? 0.1822 0.1823 0.1538 -0.0026 0.0034  -0.0079 263 ASN A CB  
1482 C CG  . ASN A 189 ? 0.2313 0.2295 0.1998 -0.0030 0.0028  -0.0086 263 ASN A CG  
1483 O OD1 . ASN A 189 ? 0.2774 0.2742 0.2450 -0.0024 0.0035  -0.0098 263 ASN A OD1 
1484 N ND2 . ASN A 189 ? 0.2458 0.2436 0.2129 -0.0040 0.0016  -0.0079 263 ASN A ND2 
1485 N N   . LYS A 190 ? 0.1525 0.1539 0.1286 -0.0019 0.0016  -0.0068 264 LYS A N   
1486 C CA  . LYS A 190 ? 0.1530 0.1541 0.1294 -0.0021 0.0006  -0.0061 264 LYS A CA  
1487 C C   . LYS A 190 ? 0.1407 0.1432 0.1193 -0.0017 0.0004  -0.0051 264 LYS A C   
1488 O O   . LYS A 190 ? 0.1529 0.1565 0.1324 -0.0018 0.0008  -0.0048 264 LYS A O   
1489 C CB  . LYS A 190 ? 0.1798 0.1804 0.1543 -0.0033 0.0000  -0.0055 264 LYS A CB  
1490 C CG  . LYS A 190 ? 0.1925 0.1931 0.1676 -0.0038 -0.0010 -0.0044 264 LYS A CG  
1491 C CD  . LYS A 190 ? 0.2033 0.2056 0.1796 -0.0042 -0.0013 -0.0029 264 LYS A CD  
1492 C CE  . LYS A 190 ? 0.2210 0.2235 0.1983 -0.0045 -0.0021 -0.0017 264 LYS A CE  
1493 N NZ  . LYS A 190 ? 0.2575 0.2593 0.2335 -0.0057 -0.0030 -0.0017 264 LYS A NZ  
1494 N N   . ILE A 191 ? 0.1433 0.1456 0.1227 -0.0012 0.0000  -0.0047 265 ILE A N   
1495 C CA  . ILE A 191 ? 0.1367 0.1398 0.1177 -0.0006 -0.0002 -0.0038 265 ILE A CA  
1496 C C   . ILE A 191 ? 0.1398 0.1432 0.1209 -0.0012 -0.0007 -0.0024 265 ILE A C   
1497 O O   . ILE A 191 ? 0.1456 0.1481 0.1261 -0.0013 -0.0010 -0.0022 265 ILE A O   
1498 C CB  . ILE A 191 ? 0.1521 0.1547 0.1340 0.0008  -0.0002 -0.0045 265 ILE A CB  
1499 C CG1 . ILE A 191 ? 0.1733 0.1761 0.1560 0.0013  0.0001  -0.0059 265 ILE A CG1 
1500 C CG2 . ILE A 191 ? 0.1512 0.1543 0.1344 0.0015  -0.0004 -0.0037 265 ILE A CG2 
1501 C CD1 . ILE A 191 ? 0.1762 0.1802 0.1604 0.0011  0.0004  -0.0058 265 ILE A CD1 
1502 N N   . PHE A 192 ? 0.1390 0.1434 0.1209 -0.0014 -0.0008 -0.0012 266 PHE A N   
1503 C CA  . PHE A 192 ? 0.1445 0.1494 0.1272 -0.0015 -0.0012 0.0002  266 PHE A CA  
1504 C C   . PHE A 192 ? 0.1415 0.1463 0.1253 -0.0001 -0.0010 0.0003  266 PHE A C   
1505 O O   . PHE A 192 ? 0.1477 0.1531 0.1325 0.0002  -0.0008 0.0003  266 PHE A O   
1506 C CB  . PHE A 192 ? 0.1581 0.1642 0.1411 -0.0025 -0.0014 0.0014  266 PHE A CB  
1507 C CG  . PHE A 192 ? 0.2077 0.2138 0.1892 -0.0039 -0.0019 0.0015  266 PHE A CG  
1508 C CD1 . PHE A 192 ? 0.2292 0.2352 0.2106 -0.0046 -0.0027 0.0022  266 PHE A CD1 
1509 C CD2 . PHE A 192 ? 0.2216 0.2278 0.2019 -0.0044 -0.0017 0.0009  266 PHE A CD2 
1510 C CE1 . PHE A 192 ? 0.2686 0.2745 0.2486 -0.0058 -0.0035 0.0022  266 PHE A CE1 
1511 C CE2 . PHE A 192 ? 0.2375 0.2435 0.2159 -0.0055 -0.0023 0.0010  266 PHE A CE2 
1512 C CZ  . PHE A 192 ? 0.2464 0.2522 0.2246 -0.0062 -0.0033 0.0015  266 PHE A CZ  
1513 N N   . LEU A 193 ? 0.1319 0.1358 0.1156 0.0006  -0.0010 0.0006  267 LEU A N   
1514 C CA  . LEU A 193 ? 0.1387 0.1421 0.1229 0.0022  -0.0008 0.0007  267 LEU A CA  
1515 C C   . LEU A 193 ? 0.1359 0.1399 0.1209 0.0023  -0.0007 0.0025  267 LEU A C   
1516 O O   . LEU A 193 ? 0.1452 0.1490 0.1303 0.0020  -0.0006 0.0035  267 LEU A O   
1517 C CB  . LEU A 193 ? 0.1582 0.1602 0.1415 0.0032  -0.0006 0.0000  267 LEU A CB  
1518 C CG  . LEU A 193 ? 0.1693 0.1703 0.1523 0.0051  -0.0005 -0.0001 267 LEU A CG  
1519 C CD1 . LEU A 193 ? 0.1937 0.1950 0.1772 0.0058  -0.0008 -0.0014 267 LEU A CD1 
1520 C CD2 . LEU A 193 ? 0.1798 0.1794 0.1617 0.0061  -0.0003 -0.0006 267 LEU A CD2 
1521 N N   . CYS A 194 ? 0.1324 0.1371 0.1182 0.0025  -0.0006 0.0030  268 CYS A N   
1522 C CA  . CYS A 194 ? 0.1471 0.1524 0.1338 0.0027  -0.0004 0.0048  268 CYS A CA  
1523 C C   . CYS A 194 ? 0.1537 0.1579 0.1402 0.0044  0.0000  0.0052  268 CYS A C   
1524 O O   . CYS A 194 ? 0.1665 0.1695 0.1520 0.0058  0.0000  0.0040  268 CYS A O   
1525 C CB  . CYS A 194 ? 0.1549 0.1611 0.1424 0.0025  -0.0004 0.0052  268 CYS A CB  
1526 S SG  . CYS A 194 ? 0.1856 0.1931 0.1732 0.0005  -0.0008 0.0053  268 CYS A SG  
1527 N N   . SER A 195 ? 0.1484 0.1531 0.1357 0.0045  0.0004  0.0070  269 SER A N   
1528 C CA  . SER A 195 ? 0.1500 0.1537 0.1371 0.0063  0.0011  0.0079  269 SER A CA  
1529 C C   . SER A 195 ? 0.1548 0.1594 0.1432 0.0065  0.0016  0.0098  269 SER A C   
1530 O O   . SER A 195 ? 0.1499 0.1560 0.1398 0.0051  0.0014  0.0110  269 SER A O   
1531 C CB  . SER A 195 ? 0.1573 0.1604 0.1443 0.0062  0.0015  0.0084  269 SER A CB  
1532 O OG  . SER A 195 ? 0.1816 0.1836 0.1682 0.0082  0.0025  0.0095  269 SER A OG  
1533 N N   . SER A 196 ? 0.1470 0.1505 0.1347 0.0084  0.0023  0.0101  270 SER A N   
1534 C CA  . SER A 196 ? 0.1444 0.1485 0.1333 0.0090  0.0030  0.0120  270 SER A CA  
1535 C C   . SER A 196 ? 0.1512 0.1560 0.1416 0.0087  0.0037  0.0140  270 SER A C   
1536 O O   . SER A 196 ? 0.1541 0.1602 0.1463 0.0086  0.0041  0.0158  270 SER A O   
1537 C CB  . SER A 196 ? 0.1549 0.1573 0.1423 0.0114  0.0037  0.0119  270 SER A CB  
1538 O OG  . SER A 196 ? 0.1581 0.1590 0.1442 0.0130  0.0046  0.0124  270 SER A OG  
1539 N N   . GLY A 197 ? 0.1497 0.1538 0.1395 0.0088  0.0038  0.0136  271 GLY A N   
1540 C CA  . GLY A 197 ? 0.1516 0.1560 0.1430 0.0087  0.0046  0.0154  271 GLY A CA  
1541 C C   . GLY A 197 ? 0.1542 0.1573 0.1450 0.0110  0.0061  0.0166  271 GLY A C   
1542 O O   . GLY A 197 ? 0.1648 0.1678 0.1567 0.0111  0.0070  0.0179  271 GLY A O   
1543 N N   . GLY A 198 ? 0.1592 0.1612 0.1482 0.0128  0.0065  0.0162  272 GLY A N   
1544 C CA  . GLY A 198 ? 0.1733 0.1736 0.1610 0.0153  0.0081  0.0172  272 GLY A CA  
1545 C C   . GLY A 198 ? 0.1815 0.1829 0.1715 0.0157  0.0094  0.0199  272 GLY A C   
1546 O O   . GLY A 198 ? 0.1984 0.2021 0.1914 0.0140  0.0090  0.0211  272 GLY A O   
1547 N N   . PRO A 199 ? 0.2022 0.2020 0.1908 0.0183  0.0111  0.0209  273 PRO A N   
1548 C CA  . PRO A 199 ? 0.2151 0.2159 0.2059 0.0191  0.0126  0.0236  273 PRO A CA  
1549 C C   . PRO A 199 ? 0.2308 0.2333 0.2252 0.0179  0.0134  0.0257  273 PRO A C   
1550 O O   . PRO A 199 ? 0.2538 0.2578 0.2510 0.0180  0.0144  0.0280  273 PRO A O   
1551 C CB  . PRO A 199 ? 0.2433 0.2413 0.2307 0.0223  0.0142  0.0237  273 PRO A CB  
1552 C CG  . PRO A 199 ? 0.2497 0.2456 0.2340 0.0230  0.0136  0.0218  273 PRO A CG  
1553 C CD  . PRO A 199 ? 0.2160 0.2130 0.2006 0.0206  0.0113  0.0195  273 PRO A CD  
1554 N N   . PHE A 200 ? 0.2072 0.2093 0.2016 0.0169  0.0129  0.0250  274 PHE A N   
1555 C CA  . PHE A 200 ? 0.2164 0.2197 0.2142 0.0159  0.0136  0.0270  274 PHE A CA  
1556 C C   . PHE A 200 ? 0.1982 0.2039 0.1991 0.0127  0.0118  0.0267  274 PHE A C   
1557 O O   . PHE A 200 ? 0.2162 0.2228 0.2200 0.0114  0.0118  0.0278  274 PHE A O   
1558 C CB  . PHE A 200 ? 0.2170 0.2182 0.2130 0.0170  0.0146  0.0268  274 PHE A CB  
1559 C CG  . PHE A 200 ? 0.2342 0.2328 0.2268 0.0203  0.0164  0.0271  274 PHE A CG  
1560 C CD1 . PHE A 200 ? 0.2600 0.2585 0.2522 0.0222  0.0177  0.0284  274 PHE A CD1 
1561 C CD2 . PHE A 200 ? 0.2326 0.2288 0.2221 0.0217  0.0168  0.0261  274 PHE A CD2 
1562 C CE1 . PHE A 200 ? 0.2810 0.2768 0.2695 0.0254  0.0194  0.0287  274 PHE A CE1 
1563 C CE2 . PHE A 200 ? 0.2679 0.2615 0.2538 0.0249  0.0184  0.0265  274 PHE A CE2 
1564 C CZ  . PHE A 200 ? 0.2863 0.2797 0.2715 0.0267  0.0196  0.0276  274 PHE A CZ  
1565 N N   . GLN A 201 ? 0.2064 0.2128 0.2065 0.0114  0.0101  0.0251  275 GLN A N   
1566 C CA  . GLN A 201 ? 0.2160 0.2241 0.2178 0.0087  0.0082  0.0243  275 GLN A CA  
1567 C C   . GLN A 201 ? 0.2100 0.2205 0.2162 0.0071  0.0080  0.0265  275 GLN A C   
1568 O O   . GLN A 201 ? 0.2439 0.2551 0.2515 0.0049  0.0066  0.0260  275 GLN A O   
1569 C CB  . GLN A 201 ? 0.1985 0.2070 0.1986 0.0080  0.0068  0.0226  275 GLN A CB  
1570 C CG  . GLN A 201 ? 0.1901 0.1996 0.1907 0.0055  0.0049  0.0214  275 GLN A CG  
1571 C CD  . GLN A 201 ? 0.1884 0.1964 0.1873 0.0049  0.0044  0.0196  275 GLN A CD  
1572 O OE1 . GLN A 201 ? 0.1954 0.2014 0.1919 0.0063  0.0050  0.0185  275 GLN A OE1 
1573 N NE2 . GLN A 201 ? 0.1710 0.1800 0.1713 0.0027  0.0031  0.0194  275 GLN A NE2 
1574 N N   . ASN A 202 ? 0.2281 0.2398 0.2366 0.0080  0.0091  0.0287  276 ASN A N   
1575 C CA  . ASN A 202 ? 0.2463 0.2606 0.2596 0.0065  0.0087  0.0309  276 ASN A CA  
1576 C C   . ASN A 202 ? 0.2786 0.2932 0.2952 0.0072  0.0105  0.0332  276 ASN A C   
1577 O O   . ASN A 202 ? 0.2807 0.2977 0.3018 0.0062  0.0105  0.0354  276 ASN A O   
1578 C CB  . ASN A 202 ? 0.2976 0.3137 0.3122 0.0068  0.0087  0.0320  276 ASN A CB  
1579 C CG  . ASN A 202 ? 0.3475 0.3636 0.3596 0.0059  0.0070  0.0300  276 ASN A CG  
1580 O OD1 . ASN A 202 ? 0.3706 0.3865 0.3814 0.0043  0.0054  0.0282  276 ASN A OD1 
1581 N ND2 . ASN A 202 ? 0.4614 0.4774 0.4724 0.0072  0.0076  0.0303  276 ASN A ND2 
1582 N N   . LEU A 203 ? 0.2411 0.2534 0.2555 0.0088  0.0120  0.0330  277 LEU A N   
1583 C CA  . LEU A 203 ? 0.2536 0.2658 0.2707 0.0097  0.0141  0.0354  277 LEU A CA  
1584 C C   . LEU A 203 ? 0.2719 0.2847 0.2921 0.0074  0.0131  0.0355  277 LEU A C   
1585 O O   . LEU A 203 ? 0.2762 0.2881 0.2946 0.0060  0.0115  0.0334  277 LEU A O   
1586 C CB  . LEU A 203 ? 0.2513 0.2605 0.2645 0.0126  0.0162  0.0352  277 LEU A CB  
1587 C CG  . LEU A 203 ? 0.2602 0.2683 0.2702 0.0152  0.0173  0.0351  277 LEU A CG  
1588 C CD1 . LEU A 203 ? 0.2583 0.2634 0.2645 0.0180  0.0192  0.0349  277 LEU A CD1 
1589 C CD2 . LEU A 203 ? 0.2758 0.2860 0.2892 0.0158  0.0184  0.0377  277 LEU A CD2 
1590 N N   . THR A 204 ? 0.2883 0.3024 0.3132 0.0073  0.0144  0.0382  278 THR A N   
1591 C CA  . THR A 204 ? 0.2782 0.2924 0.3063 0.0053  0.0138  0.0386  278 THR A CA  
1592 C C   . THR A 204 ? 0.2441 0.2553 0.2695 0.0068  0.0154  0.0381  278 THR A C   
1593 O O   . THR A 204 ? 0.2433 0.2525 0.2650 0.0095  0.0172  0.0380  278 THR A O   
1594 C CB  . THR A 204 ? 0.2957 0.3125 0.3305 0.0047  0.0147  0.0418  278 THR A CB  
1595 O OG1 . THR A 204 ? 0.3070 0.3228 0.3416 0.0075  0.0179  0.0439  278 THR A OG1 
1596 C CG2 . THR A 204 ? 0.3009 0.3208 0.3385 0.0037  0.0133  0.0426  278 THR A CG2 
1597 N N   . MET A 205 ? 0.2501 0.2609 0.2774 0.0050  0.0146  0.0377  279 MET A N   
1598 C CA  . MET A 205 ? 0.2701 0.2781 0.2957 0.0062  0.0163  0.0377  279 MET A CA  
1599 C C   . MET A 205 ? 0.2741 0.2817 0.3010 0.0087  0.0196  0.0406  279 MET A C   
1600 O O   . MET A 205 ? 0.2779 0.2829 0.3008 0.0112  0.0213  0.0404  279 MET A O   
1601 C CB  . MET A 205 ? 0.2849 0.2926 0.3133 0.0037  0.0150  0.0373  279 MET A CB  
1602 C CG  . MET A 205 ? 0.2907 0.2979 0.3164 0.0017  0.0122  0.0342  279 MET A CG  
1603 S SD  . MET A 205 ? 0.2745 0.2786 0.2929 0.0035  0.0123  0.0312  279 MET A SD  
1604 C CE  . MET A 205 ? 0.2826 0.2840 0.3012 0.0042  0.0140  0.0319  279 MET A CE  
1605 N N   . ASP A 206 ? 0.2829 0.2930 0.3154 0.0082  0.0204  0.0434  280 ASP A N   
1606 C CA  . ASP A 206 ? 0.2901 0.2998 0.3242 0.0107  0.0238  0.0465  280 ASP A CA  
1607 C C   . ASP A 206 ? 0.2778 0.2862 0.3069 0.0139  0.0253  0.0463  280 ASP A C   
1608 O O   . ASP A 206 ? 0.2961 0.3023 0.3226 0.0167  0.0279  0.0473  280 ASP A O   
1609 C CB  . ASP A 206 ? 0.3420 0.3550 0.3835 0.0094  0.0242  0.0494  280 ASP A CB  
1610 C CG  . ASP A 206 ? 0.3898 0.4039 0.4372 0.0067  0.0234  0.0504  280 ASP A CG  
1611 O OD1 . ASP A 206 ? 0.4018 0.4136 0.4474 0.0064  0.0233  0.0492  280 ASP A OD1 
1612 O OD2 . ASP A 206 ? 0.4288 0.4460 0.4825 0.0050  0.0227  0.0522  280 ASP A OD2 
1613 N N   . GLU A 207 ? 0.2541 0.2637 0.2815 0.0135  0.0235  0.0448  281 GLU A N   
1614 C CA  . GLU A 207 ? 0.2541 0.2623 0.2767 0.0163  0.0246  0.0443  281 GLU A CA  
1615 C C   . GLU A 207 ? 0.2495 0.2543 0.2656 0.0179  0.0245  0.0417  281 GLU A C   
1616 O O   . GLU A 207 ? 0.2706 0.2731 0.2828 0.0209  0.0264  0.0420  281 GLU A O   
1617 C CB  . GLU A 207 ? 0.2719 0.2822 0.2947 0.0152  0.0227  0.0433  281 GLU A CB  
1618 C CG  . GLU A 207 ? 0.2983 0.3117 0.3270 0.0147  0.0233  0.0462  281 GLU A CG  
1619 C CD  . GLU A 207 ? 0.3182 0.3337 0.3471 0.0136  0.0213  0.0453  281 GLU A CD  
1620 O OE1 . GLU A 207 ? 0.3053 0.3211 0.3331 0.0115  0.0186  0.0430  281 GLU A OE1 
1621 O OE2 . GLU A 207 ? 0.3759 0.3924 0.4060 0.0151  0.0226  0.0471  281 GLU A OE2 
1622 N N   . LEU A 208 ? 0.2553 0.2596 0.2699 0.0159  0.0221  0.0391  282 LEU A N   
1623 C CA  . LEU A 208 ? 0.2645 0.2659 0.2735 0.0172  0.0218  0.0367  282 LEU A CA  
1624 C C   . LEU A 208 ? 0.2801 0.2789 0.2875 0.0194  0.0242  0.0379  282 LEU A C   
1625 O O   . LEU A 208 ? 0.2976 0.2937 0.2998 0.0219  0.0250  0.0368  282 LEU A O   
1626 C CB  . LEU A 208 ? 0.2629 0.2643 0.2713 0.0147  0.0192  0.0341  282 LEU A CB  
1627 C CG  . LEU A 208 ? 0.2518 0.2548 0.2595 0.0130  0.0168  0.0321  282 LEU A CG  
1628 C CD1 . LEU A 208 ? 0.2494 0.2525 0.2574 0.0104  0.0145  0.0301  282 LEU A CD1 
1629 C CD2 . LEU A 208 ? 0.2408 0.2421 0.2434 0.0151  0.0167  0.0303  282 LEU A CD2 
1630 N N   . LYS A 209 ? 0.2872 0.2867 0.2991 0.0185  0.0255  0.0402  283 LYS A N   
1631 C CA  . LYS A 209 ? 0.2935 0.2906 0.3042 0.0206  0.0279  0.0415  283 LYS A CA  
1632 C C   . LYS A 209 ? 0.2959 0.2910 0.3023 0.0244  0.0303  0.0424  283 LYS A C   
1633 O O   . LYS A 209 ? 0.3091 0.3012 0.3111 0.0267  0.0315  0.0420  283 LYS A O   
1634 C CB  . LYS A 209 ? 0.3299 0.3284 0.3470 0.0192  0.0293  0.0444  283 LYS A CB  
1635 C CG  . LYS A 209 ? 0.4345 0.4304 0.4509 0.0210  0.0320  0.0461  283 LYS A CG  
1636 C CD  . LYS A 209 ? 0.4621 0.4595 0.4856 0.0197  0.0335  0.0492  283 LYS A CD  
1637 C CE  . LYS A 209 ? 0.5316 0.5315 0.5604 0.0156  0.0308  0.0485  283 LYS A CE  
1638 N NZ  . LYS A 209 ? 0.5891 0.5901 0.6248 0.0142  0.0322  0.0514  283 LYS A NZ  
1639 N N   . ASN A 210 ? 0.2888 0.2854 0.2964 0.0252  0.0310  0.0437  284 ASN A N   
1640 C CA  . ASN A 210 ? 0.2878 0.2827 0.2922 0.0289  0.0336  0.0451  284 ASN A CA  
1641 C C   . ASN A 210 ? 0.2983 0.2923 0.2978 0.0304  0.0326  0.0431  284 ASN A C   
1642 O O   . ASN A 210 ? 0.3084 0.3009 0.3050 0.0334  0.0345  0.0441  284 ASN A O   
1643 C CB  . ASN A 210 ? 0.3486 0.3457 0.3586 0.0291  0.0360  0.0488  284 ASN A CB  
1644 C CG  . ASN A 210 ? 0.3854 0.3823 0.3993 0.0285  0.0377  0.0510  284 ASN A CG  
1645 O OD1 . ASN A 210 ? 0.4767 0.4765 0.4971 0.0256  0.0370  0.0522  284 ASN A OD1 
1646 N ND2 . ASN A 210 ? 0.3865 0.3802 0.3963 0.0308  0.0395  0.0512  284 ASN A ND2 
1647 N N   . VAL A 211 ? 0.2609 0.2554 0.2590 0.0285  0.0295  0.0401  285 VAL A N   
1648 C CA  . VAL A 211 ? 0.2634 0.2570 0.2571 0.0298  0.0284  0.0380  285 VAL A CA  
1649 C C   . VAL A 211 ? 0.2629 0.2526 0.2501 0.0332  0.0294  0.0370  285 VAL A C   
1650 O O   . VAL A 211 ? 0.2717 0.2597 0.2571 0.0337  0.0297  0.0365  285 VAL A O   
1651 C CB  . VAL A 211 ? 0.2641 0.2590 0.2578 0.0271  0.0251  0.0351  285 VAL A CB  
1652 C CG1 . VAL A 211 ? 0.2916 0.2901 0.2906 0.0243  0.0240  0.0360  285 VAL A CG1 
1653 C CG2 . VAL A 211 ? 0.2543 0.2482 0.2464 0.0259  0.0236  0.0330  285 VAL A CG2 
1654 N N   . THR A 212 ? 0.2871 0.2755 0.2706 0.0352  0.0294  0.0361  286 THR A N   
1655 C CA  . THR A 212 ? 0.3037 0.2885 0.2808 0.0386  0.0300  0.0349  286 THR A CA  
1656 C C   . THR A 212 ? 0.2713 0.2552 0.2448 0.0384  0.0272  0.0315  286 THR A C   
1657 O O   . THR A 212 ? 0.2750 0.2611 0.2509 0.0361  0.0254  0.0305  286 THR A O   
1658 C CB  . THR A 212 ? 0.3453 0.3286 0.3205 0.0419  0.0328  0.0371  286 THR A CB  
1659 O OG1 . THR A 212 ? 0.3819 0.3663 0.3577 0.0415  0.0318  0.0364  286 THR A OG1 
1660 C CG2 . THR A 212 ? 0.3820 0.3666 0.3618 0.0420  0.0357  0.0408  286 THR A CG2 
1661 N N   . SER A 213 ? 0.2672 0.2478 0.2349 0.0409  0.0270  0.0299  287 SER A N   
1662 C CA  . SER A 213 ? 0.2726 0.2523 0.2371 0.0410  0.0245  0.0267  287 SER A CA  
1663 C C   . SER A 213 ? 0.2804 0.2600 0.2442 0.0419  0.0245  0.0266  287 SER A C   
1664 O O   . SER A 213 ? 0.2780 0.2583 0.2419 0.0404  0.0223  0.0245  287 SER A O   
1665 C CB  . SER A 213 ? 0.3011 0.2774 0.2599 0.0435  0.0240  0.0250  287 SER A CB  
1666 O OG  . SER A 213 ? 0.3013 0.2748 0.2561 0.0472  0.0262  0.0264  287 SER A OG  
1667 N N   . GLU A 214 ? 0.2993 0.2781 0.2627 0.0441  0.0271  0.0290  288 GLU A N   
1668 C CA  . GLU A 214 ? 0.3153 0.2941 0.2785 0.0448  0.0272  0.0291  288 GLU A CA  
1669 C C   . GLU A 214 ? 0.3129 0.2956 0.2817 0.0413  0.0258  0.0292  288 GLU A C   
1670 O O   . GLU A 214 ? 0.3019 0.2847 0.2702 0.0407  0.0242  0.0275  288 GLU A O   
1671 C CB  . GLU A 214 ? 0.3536 0.3313 0.3162 0.0477  0.0305  0.0320  288 GLU A CB  
1672 C CG  . GLU A 214 ? 0.4444 0.4221 0.4070 0.0486  0.0310  0.0324  288 GLU A CG  
1673 C CD  . GLU A 214 ? 0.5211 0.4979 0.4834 0.0514  0.0345  0.0355  288 GLU A CD  
1674 O OE1 . GLU A 214 ? 0.5571 0.5330 0.5190 0.0530  0.0368  0.0375  288 GLU A OE1 
1675 O OE2 . GLU A 214 ? 0.6539 0.6308 0.6166 0.0521  0.0350  0.0360  288 GLU A OE2 
1676 N N   . ASN A 215 ? 0.2888 0.2743 0.2626 0.0389  0.0263  0.0309  289 ASN A N   
1677 C CA  . ASN A 215 ? 0.2952 0.2843 0.2741 0.0356  0.0249  0.0311  289 ASN A CA  
1678 C C   . ASN A 215 ? 0.2941 0.2836 0.2721 0.0335  0.0218  0.0279  289 ASN A C   
1679 O O   . ASN A 215 ? 0.3158 0.3070 0.2958 0.0317  0.0204  0.0272  289 ASN A O   
1680 C CB  . ASN A 215 ? 0.3309 0.3226 0.3150 0.0334  0.0255  0.0332  289 ASN A CB  
1681 C CG  . ASN A 215 ? 0.3650 0.3571 0.3515 0.0349  0.0285  0.0366  289 ASN A CG  
1682 O OD1 . ASN A 215 ? 0.4017 0.3934 0.3878 0.0369  0.0302  0.0381  289 ASN A OD1 
1683 N ND2 . ASN A 215 ? 0.3137 0.3069 0.3035 0.0336  0.0293  0.0381  289 ASN A ND2 
1684 N N   . ALA A 216 ? 0.2730 0.2608 0.2483 0.0337  0.0209  0.0261  290 ALA A N   
1685 C CA  . ALA A 216 ? 0.2817 0.2699 0.2564 0.0318  0.0182  0.0233  290 ALA A CA  
1686 C C   . ALA A 216 ? 0.2897 0.2763 0.2612 0.0330  0.0169  0.0211  290 ALA A C   
1687 O O   . ALA A 216 ? 0.3066 0.2943 0.2790 0.0310  0.0149  0.0193  290 ALA A O   
1688 C CB  . ALA A 216 ? 0.2887 0.2756 0.2616 0.0319  0.0177  0.0222  290 ALA A CB  
1689 N N   . LEU A 217 ? 0.3069 0.2907 0.2745 0.0361  0.0181  0.0212  291 LEU A N   
1690 C CA  . LEU A 217 ? 0.3295 0.3111 0.2935 0.0375  0.0167  0.0189  291 LEU A CA  
1691 C C   . LEU A 217 ? 0.3700 0.3522 0.3352 0.0375  0.0169  0.0194  291 LEU A C   
1692 O O   . LEU A 217 ? 0.3734 0.3544 0.3368 0.0378  0.0153  0.0174  291 LEU A O   
1693 C CB  . LEU A 217 ? 0.3370 0.3148 0.2955 0.0412  0.0175  0.0185  291 LEU A CB  
1694 C CG  . LEU A 217 ? 0.3579 0.3344 0.3141 0.0417  0.0170  0.0175  291 LEU A CG  
1695 C CD1 . LEU A 217 ? 0.4185 0.3912 0.3691 0.0456  0.0181  0.0175  291 LEU A CD1 
1696 C CD2 . LEU A 217 ? 0.3622 0.3391 0.3182 0.0401  0.0141  0.0145  291 LEU A CD2 
1697 N N   . LYS A 218 ? 0.4042 0.3880 0.3723 0.0374  0.0188  0.0222  292 LYS A N   
1698 C CA  . LYS A 218 ? 0.4607 0.4444 0.4292 0.0382  0.0194  0.0229  292 LYS A CA  
1699 C C   . LYS A 218 ? 0.5186 0.5045 0.4899 0.0354  0.0175  0.0218  292 LYS A C   
1700 O O   . LYS A 218 ? 0.4713 0.4599 0.4460 0.0326  0.0163  0.0216  292 LYS A O   
1701 C CB  . LYS A 218 ? 0.5533 0.5383 0.5245 0.0389  0.0221  0.0264  292 LYS A CB  
1702 C CG  . LYS A 218 ? 0.6231 0.6122 0.6002 0.0357  0.0219  0.0280  292 LYS A CG  
1703 C CD  . LYS A 218 ? 0.7137 0.7045 0.6943 0.0361  0.0244  0.0315  292 LYS A CD  
1704 C CE  . LYS A 218 ? 0.7736 0.7683 0.7599 0.0328  0.0235  0.0326  292 LYS A CE  
1705 N NZ  . LYS A 218 ? 0.7703 0.7665 0.7601 0.0327  0.0254  0.0354  292 LYS A NZ  
1706 N N   . HIS A 219 ? 0.5117 0.4961 0.4815 0.0364  0.0171  0.0209  293 HIS A N   
1707 C CA  . HIS A 219 ? 0.5975 0.5837 0.5701 0.0344  0.0158  0.0204  293 HIS A CA  
1708 C C   . HIS A 219 ? 0.5556 0.5433 0.5296 0.0316  0.0135  0.0184  293 HIS A C   
1709 O O   . HIS A 219 ? 0.5923 0.5830 0.5700 0.0290  0.0129  0.0191  293 HIS A O   
1710 C CB  . HIS A 219 ? 0.6789 0.6679 0.6557 0.0335  0.0173  0.0234  293 HIS A CB  
1711 C CG  . HIS A 219 ? 0.7937 0.7812 0.7693 0.0364  0.0198  0.0255  293 HIS A CG  
1712 N ND1 . HIS A 219 ? 0.8605 0.8502 0.8394 0.0365  0.0218  0.0286  293 HIS A ND1 
1713 C CD2 . HIS A 219 ? 0.8384 0.8225 0.8098 0.0394  0.0207  0.0249  293 HIS A CD2 
1714 C CE1 . HIS A 219 ? 0.8178 0.8054 0.7946 0.0395  0.0240  0.0299  293 HIS A CE1 
1715 N NE2 . HIS A 219 ? 0.8615 0.8455 0.8335 0.0414  0.0233  0.0277  293 HIS A NE2 
1716 N N   . PRO A 220 ? 0.5355 0.5212 0.5064 0.0321  0.0120  0.0158  294 PRO A N   
1717 C CA  . PRO A 220 ? 0.5256 0.5126 0.4979 0.0296  0.0099  0.0138  294 PRO A CA  
1718 C C   . PRO A 220 ? 0.5223 0.5100 0.4962 0.0282  0.0087  0.0129  294 PRO A C   
1719 O O   . PRO A 220 ? 0.4821 0.4681 0.4548 0.0297  0.0090  0.0128  294 PRO A O   
1720 C CB  . PRO A 220 ? 0.5079 0.4922 0.4764 0.0312  0.0088  0.0115  294 PRO A CB  
1721 C CG  . PRO A 220 ? 0.5196 0.5007 0.4844 0.0345  0.0098  0.0116  294 PRO A CG  
1722 C CD  . PRO A 220 ? 0.5215 0.5036 0.4877 0.0352  0.0123  0.0147  294 PRO A CD  
1723 N N   . LYS A 221 ? 0.4578 0.4478 0.4344 0.0255  0.0075  0.0122  295 LYS A N   
1724 C CA  . LYS A 221 ? 0.4167 0.4073 0.3949 0.0242  0.0064  0.0114  295 LYS A CA  
1725 C C   . LYS A 221 ? 0.4455 0.4332 0.4211 0.0255  0.0052  0.0089  295 LYS A C   
1726 O O   . LYS A 221 ? 0.5181 0.5046 0.4935 0.0261  0.0052  0.0087  295 LYS A O   
1727 C CB  . LYS A 221 ? 0.4177 0.4109 0.3985 0.0213  0.0054  0.0109  295 LYS A CB  
1728 C CG  . LYS A 221 ? 0.4400 0.4341 0.4227 0.0197  0.0046  0.0104  295 LYS A CG  
1729 C CD  . LYS A 221 ? 0.4532 0.4486 0.4379 0.0194  0.0055  0.0126  295 LYS A CD  
1730 C CE  . LYS A 221 ? 0.4993 0.4952 0.4856 0.0181  0.0048  0.0120  295 LYS A CE  
1731 N NZ  . LYS A 221 ? 0.5158 0.5089 0.5004 0.0196  0.0044  0.0105  295 LYS A NZ  
1732 N N   . TRP A 222 ? 0.4230 0.4098 0.3969 0.0258  0.0041  0.0070  296 TRP A N   
1733 C CA  . TRP A 222 ? 0.4212 0.4049 0.3921 0.0277  0.0030  0.0048  296 TRP A CA  
1734 C C   . TRP A 222 ? 0.4212 0.4034 0.3890 0.0295  0.0034  0.0047  296 TRP A C   
1735 O O   . TRP A 222 ? 0.4525 0.4365 0.4213 0.0285  0.0038  0.0054  296 TRP A O   
1736 C CB  . TRP A 222 ? 0.3859 0.3698 0.3581 0.0262  0.0010  0.0024  296 TRP A CB  
1737 C CG  . TRP A 222 ? 0.3586 0.3442 0.3319 0.0247  0.0002  0.0016  296 TRP A CG  
1738 C CD1 . TRP A 222 ? 0.3483 0.3328 0.3198 0.0255  -0.0009 -0.0001 296 TRP A CD1 
1739 C CD2 . TRP A 222 ? 0.3701 0.3589 0.3465 0.0221  0.0004  0.0025  296 TRP A CD2 
1740 N NE1 . TRP A 222 ? 0.3314 0.3179 0.3047 0.0237  -0.0012 -0.0004 296 TRP A NE1 
1741 C CE2 . TRP A 222 ? 0.3582 0.3472 0.3343 0.0216  -0.0003 0.0011  296 TRP A CE2 
1742 C CE3 . TRP A 222 ? 0.3599 0.3510 0.3390 0.0202  0.0012  0.0042  296 TRP A CE3 
1743 C CZ2 . TRP A 222 ? 0.3831 0.3746 0.3615 0.0194  -0.0003 0.0014  296 TRP A CZ2 
1744 C CZ3 . TRP A 222 ? 0.3919 0.3854 0.3731 0.0180  0.0011  0.0044  296 TRP A CZ3 
1745 C CH2 . TRP A 222 ? 0.3738 0.3674 0.3545 0.0176  0.0002  0.0030  296 TRP A CH2 
1746 N N   . LYS A 223 ? 0.4118 0.3909 0.3758 0.0323  0.0033  0.0037  297 LYS A N   
1747 C CA  . LYS A 223 ? 0.4219 0.3992 0.3824 0.0344  0.0038  0.0037  297 LYS A CA  
1748 C C   . LYS A 223 ? 0.3831 0.3609 0.3438 0.0335  0.0020  0.0018  297 LYS A C   
1749 O O   . LYS A 223 ? 0.3803 0.3574 0.3409 0.0332  0.0000  -0.0004 297 LYS A O   
1750 C CB  . LYS A 223 ? 0.4591 0.4325 0.4149 0.0378  0.0039  0.0030  297 LYS A CB  
1751 C CG  . LYS A 223 ? 0.5299 0.5015 0.4819 0.0402  0.0048  0.0035  297 LYS A CG  
1752 C CD  . LYS A 223 ? 0.6426 0.6100 0.5892 0.0438  0.0048  0.0026  297 LYS A CD  
1753 C CE  . LYS A 223 ? 0.7123 0.6776 0.6571 0.0442  0.0019  -0.0005 297 LYS A CE  
1754 N NZ  . LYS A 223 ? 0.7567 0.7178 0.6956 0.0477  0.0015  -0.0016 297 LYS A NZ  
1755 N N   . MET A 224 ? 0.2797 0.2590 0.2411 0.0328  0.0028  0.0029  298 MET A N   
1756 C CA  . MET A 224 ? 0.2498 0.2293 0.2109 0.0323  0.0014  0.0013  298 MET A CA  
1757 C C   . MET A 224 ? 0.2397 0.2168 0.1967 0.0351  0.0020  0.0014  298 MET A C   
1758 O O   . MET A 224 ? 0.2629 0.2386 0.2179 0.0370  0.0038  0.0031  298 MET A O   
1759 C CB  . MET A 224 ? 0.2222 0.2047 0.1867 0.0297  0.0019  0.0023  298 MET A CB  
1760 C CG  . MET A 224 ? 0.2335 0.2185 0.2017 0.0271  0.0016  0.0024  298 MET A CG  
1761 S SD  . MET A 224 ? 0.2597 0.2479 0.2313 0.0241  0.0015  0.0029  298 MET A SD  
1762 C CE  . MET A 224 ? 0.2478 0.2364 0.2194 0.0245  0.0036  0.0056  298 MET A CE  
1763 N N   . GLY A 225 ? 0.2350 0.2114 0.1907 0.0355  0.0006  -0.0002 299 GLY A N   
1764 C CA  . GLY A 225 ? 0.2363 0.2104 0.1881 0.0381  0.0011  0.0000  299 GLY A CA  
1765 C C   . GLY A 225 ? 0.2250 0.1999 0.1772 0.0381  0.0035  0.0025  299 GLY A C   
1766 O O   . GLY A 225 ? 0.2205 0.1982 0.1766 0.0357  0.0043  0.0039  299 GLY A O   
1767 N N   . LYS A 226 ? 0.2327 0.2052 0.1811 0.0410  0.0047  0.0034  300 LYS A N   
1768 C CA  . LYS A 226 ? 0.2294 0.2023 0.1782 0.0413  0.0072  0.0061  300 LYS A CA  
1769 C C   . LYS A 226 ? 0.2158 0.1908 0.1673 0.0392  0.0071  0.0063  300 LYS A C   
1770 O O   . LYS A 226 ? 0.2286 0.2054 0.1831 0.0377  0.0087  0.0084  300 LYS A O   
1771 C CB  . LYS A 226 ? 0.2645 0.2340 0.2082 0.0450  0.0086  0.0069  300 LYS A CB  
1772 C CG  . LYS A 226 ? 0.3064 0.2738 0.2474 0.0472  0.0093  0.0072  300 LYS A CG  
1773 C CD  . LYS A 226 ? 0.3669 0.3307 0.3023 0.0511  0.0106  0.0079  300 LYS A CD  
1774 C CE  . LYS A 226 ? 0.4462 0.4072 0.3779 0.0537  0.0111  0.0078  300 LYS A CE  
1775 N NZ  . LYS A 226 ? 0.4819 0.4447 0.4169 0.0528  0.0134  0.0103  300 LYS A NZ  
1776 N N   . LYS A 227 ? 0.2107 0.1853 0.1614 0.0391  0.0053  0.0043  301 LYS A N   
1777 C CA  . LYS A 227 ? 0.2132 0.1893 0.1659 0.0374  0.0054  0.0045  301 LYS A CA  
1778 C C   . LYS A 227 ? 0.1882 0.1675 0.1457 0.0339  0.0052  0.0048  301 LYS A C   
1779 O O   . LYS A 227 ? 0.1924 0.1731 0.1523 0.0325  0.0065  0.0065  301 LYS A O   
1780 C CB  . LYS A 227 ? 0.2294 0.2042 0.1798 0.0385  0.0035  0.0022  301 LYS A CB  
1781 C CG  . LYS A 227 ? 0.2568 0.2319 0.2077 0.0380  0.0038  0.0025  301 LYS A CG  
1782 C CD  . LYS A 227 ? 0.2461 0.2241 0.2014 0.0347  0.0032  0.0020  301 LYS A CD  
1783 C CE  . LYS A 227 ? 0.2338 0.2116 0.1889 0.0346  0.0032  0.0018  301 LYS A CE  
1784 N NZ  . LYS A 227 ? 0.2127 0.1930 0.1715 0.0316  0.0024  0.0010  301 LYS A NZ  
1785 N N   . ILE A 228 ? 0.1822 0.1627 0.1413 0.0325  0.0036  0.0032  302 ILE A N   
1786 C CA  . ILE A 228 ? 0.1779 0.1613 0.1412 0.0293  0.0033  0.0034  302 ILE A CA  
1787 C C   . ILE A 228 ? 0.1861 0.1706 0.1512 0.0286  0.0050  0.0058  302 ILE A C   
1788 O O   . ILE A 228 ? 0.1892 0.1760 0.1575 0.0263  0.0054  0.0068  302 ILE A O   
1789 C CB  . ILE A 228 ? 0.1793 0.1636 0.1440 0.0280  0.0014  0.0013  302 ILE A CB  
1790 C CG1 . ILE A 228 ? 0.2107 0.1979 0.1793 0.0249  0.0013  0.0016  302 ILE A CG1 
1791 C CG2 . ILE A 228 ? 0.1973 0.1806 0.1610 0.0291  0.0012  0.0011  302 ILE A CG2 
1792 C CD1 . ILE A 228 ? 0.2224 0.2105 0.1924 0.0236  -0.0003 -0.0004 302 ILE A CD1 
1793 N N   . THR A 229 ? 0.1851 0.1682 0.1485 0.0306  0.0060  0.0068  303 THR A N   
1794 C CA  . THR A 229 ? 0.1899 0.1744 0.1555 0.0300  0.0076  0.0092  303 THR A CA  
1795 C C   . THR A 229 ? 0.1840 0.1692 0.1509 0.0295  0.0092  0.0113  303 THR A C   
1796 O O   . THR A 229 ? 0.1853 0.1727 0.1557 0.0275  0.0098  0.0128  303 THR A O   
1797 C CB  . THR A 229 ? 0.2226 0.2050 0.1856 0.0325  0.0086  0.0098  303 THR A CB  
1798 O OG1 . THR A 229 ? 0.2355 0.2173 0.1978 0.0325  0.0069  0.0077  303 THR A OG1 
1799 C CG2 . THR A 229 ? 0.2358 0.2197 0.2014 0.0319  0.0103  0.0123  303 THR A CG2 
1800 N N   . ILE A 230 ? 0.1858 0.1690 0.1500 0.0315  0.0100  0.0115  304 ILE A N   
1801 C CA  . ILE A 230 ? 0.1834 0.1671 0.1491 0.0310  0.0115  0.0134  304 ILE A CA  
1802 C C   . ILE A 230 ? 0.1785 0.1642 0.1472 0.0281  0.0104  0.0126  304 ILE A C   
1803 O O   . ILE A 230 ? 0.1814 0.1687 0.1532 0.0263  0.0112  0.0143  304 ILE A O   
1804 C CB  . ILE A 230 ? 0.2038 0.1846 0.1658 0.0340  0.0126  0.0138  304 ILE A CB  
1805 C CG1 . ILE A 230 ? 0.2277 0.2062 0.1864 0.0371  0.0141  0.0149  304 ILE A CG1 
1806 C CG2 . ILE A 230 ? 0.2024 0.1836 0.1661 0.0333  0.0140  0.0155  304 ILE A CG2 
1807 C CD1 . ILE A 230 ? 0.2526 0.2324 0.2139 0.0369  0.0162  0.0176  304 ILE A CD1 
1808 N N   . ASP A 231 ? 0.1712 0.1566 0.1388 0.0276  0.0086  0.0102  305 ASP A N   
1809 C CA  . ASP A 231 ? 0.1697 0.1569 0.1398 0.0249  0.0076  0.0094  305 ASP A CA  
1810 C C   . ASP A 231 ? 0.1576 0.1474 0.1312 0.0222  0.0072  0.0099  305 ASP A C   
1811 O O   . ASP A 231 ? 0.1630 0.1543 0.1390 0.0201  0.0071  0.0103  305 ASP A O   
1812 C CB  . ASP A 231 ? 0.1760 0.1625 0.1445 0.0251  0.0059  0.0068  305 ASP A CB  
1813 C CG  . ASP A 231 ? 0.1900 0.1744 0.1557 0.0270  0.0059  0.0061  305 ASP A CG  
1814 O OD1 . ASP A 231 ? 0.1932 0.1766 0.1583 0.0281  0.0074  0.0078  305 ASP A OD1 
1815 O OD2 . ASP A 231 ? 0.2164 0.2003 0.1809 0.0275  0.0043  0.0040  305 ASP A OD2 
1816 N N   . SER A 232 ? 0.1571 0.1475 0.1311 0.0223  0.0070  0.0099  306 SER A N   
1817 C CA  . SER A 232 ? 0.1574 0.1502 0.1345 0.0201  0.0068  0.0107  306 SER A CA  
1818 C C   . SER A 232 ? 0.1561 0.1500 0.1355 0.0195  0.0082  0.0133  306 SER A C   
1819 O O   . SER A 232 ? 0.1610 0.1569 0.1432 0.0172  0.0079  0.0140  306 SER A O   
1820 C CB  . SER A 232 ? 0.1598 0.1526 0.1365 0.0207  0.0064  0.0103  306 SER A CB  
1821 O OG  . SER A 232 ? 0.1738 0.1688 0.1533 0.0188  0.0064  0.0114  306 SER A OG  
1822 N N   . ALA A 233 ? 0.1766 0.1690 0.1548 0.0217  0.0098  0.0149  307 ALA A N   
1823 C CA  . ALA A 233 ? 0.1786 0.1722 0.1595 0.0213  0.0114  0.0175  307 ALA A CA  
1824 C C   . ALA A 233 ? 0.1752 0.1692 0.1579 0.0197  0.0114  0.0180  307 ALA A C   
1825 O O   . ALA A 233 ? 0.1742 0.1701 0.1603 0.0180  0.0117  0.0195  307 ALA A O   
1826 C CB  . ALA A 233 ? 0.1916 0.1833 0.1706 0.0242  0.0133  0.0191  307 ALA A CB  
1827 N N   . THR A 234 ? 0.1728 0.1652 0.1532 0.0204  0.0111  0.0166  308 THR A N   
1828 C CA  . THR A 234 ? 0.1747 0.1671 0.1565 0.0191  0.0111  0.0168  308 THR A CA  
1829 C C   . THR A 234 ? 0.1603 0.1541 0.1434 0.0164  0.0093  0.0151  308 THR A C   
1830 O O   . THR A 234 ? 0.1690 0.1629 0.1534 0.0149  0.0091  0.0151  308 THR A O   
1831 C CB  . THR A 234 ? 0.1849 0.1748 0.1637 0.0211  0.0118  0.0163  308 THR A CB  
1832 O OG1 . THR A 234 ? 0.1834 0.1724 0.1595 0.0216  0.0103  0.0138  308 THR A OG1 
1833 C CG2 . THR A 234 ? 0.2035 0.1915 0.1804 0.0241  0.0138  0.0180  308 THR A CG2 
1834 N N   . MET A 235 ? 0.1616 0.1561 0.1439 0.0159  0.0080  0.0135  309 MET A N   
1835 C CA  . MET A 235 ? 0.1568 0.1522 0.1395 0.0139  0.0064  0.0116  309 MET A CA  
1836 C C   . MET A 235 ? 0.1522 0.1459 0.1327 0.0145  0.0059  0.0098  309 MET A C   
1837 O O   . MET A 235 ? 0.1644 0.1587 0.1451 0.0131  0.0048  0.0083  309 MET A O   
1838 C CB  . MET A 235 ? 0.1539 0.1513 0.1395 0.0112  0.0058  0.0122  309 MET A CB  
1839 C CG  . MET A 235 ? 0.1680 0.1672 0.1557 0.0105  0.0059  0.0137  309 MET A CG  
1840 S SD  . MET A 235 ? 0.1781 0.1796 0.1685 0.0074  0.0045  0.0138  309 MET A SD  
1841 C CE  . MET A 235 ? 0.1858 0.1873 0.1742 0.0068  0.0032  0.0112  309 MET A CE  
1842 N N   . MET A 236 ? 0.1534 0.1451 0.1317 0.0169  0.0068  0.0100  310 MET A N   
1843 C CA  . MET A 236 ? 0.1539 0.1441 0.1300 0.0177  0.0061  0.0081  310 MET A CA  
1844 C C   . MET A 236 ? 0.1555 0.1461 0.1306 0.0178  0.0047  0.0060  310 MET A C   
1845 O O   . MET A 236 ? 0.1643 0.1548 0.1389 0.0175  0.0038  0.0043  310 MET A O   
1846 C CB  . MET A 236 ? 0.1693 0.1572 0.1428 0.0204  0.0072  0.0087  310 MET A CB  
1847 C CG  . MET A 236 ? 0.1996 0.1862 0.1712 0.0212  0.0064  0.0068  310 MET A CG  
1848 S SD  . MET A 236 ? 0.2138 0.2009 0.1871 0.0187  0.0058  0.0059  310 MET A SD  
1849 C CE  . MET A 236 ? 0.2344 0.2196 0.2074 0.0198  0.0076  0.0078  310 MET A CE  
1850 N N   . ASN A 237 ? 0.1492 0.1404 0.1244 0.0182  0.0046  0.0062  311 ASN A N   
1851 C CA  . ASN A 237 ? 0.1566 0.1483 0.1315 0.0180  0.0032  0.0043  311 ASN A CA  
1852 C C   . ASN A 237 ? 0.1473 0.1406 0.1240 0.0155  0.0024  0.0034  311 ASN A C   
1853 O O   . ASN A 237 ? 0.1509 0.1442 0.1273 0.0154  0.0014  0.0015  311 ASN A O   
1854 C CB  . ASN A 237 ? 0.1522 0.1442 0.1273 0.0185  0.0032  0.0048  311 ASN A CB  
1855 C CG  . ASN A 237 ? 0.1684 0.1607 0.1434 0.0183  0.0018  0.0028  311 ASN A CG  
1856 O OD1 . ASN A 237 ? 0.1801 0.1711 0.1533 0.0197  0.0010  0.0012  311 ASN A OD1 
1857 N ND2 . ASN A 237 ? 0.1738 0.1679 0.1508 0.0166  0.0014  0.0028  311 ASN A ND2 
1858 N N   . LYS A 238 ? 0.1491 0.1439 0.1279 0.0136  0.0027  0.0046  312 LYS A N   
1859 C CA  . LYS A 238 ? 0.1478 0.1440 0.1279 0.0114  0.0019  0.0037  312 LYS A CA  
1860 C C   . LYS A 238 ? 0.1510 0.1463 0.1304 0.0111  0.0018  0.0027  312 LYS A C   
1861 O O   . LYS A 238 ? 0.1533 0.1490 0.1328 0.0102  0.0011  0.0013  312 LYS A O   
1862 C CB  . LYS A 238 ? 0.1491 0.1468 0.1312 0.0095  0.0021  0.0053  312 LYS A CB  
1863 C CG  . LYS A 238 ? 0.1694 0.1686 0.1524 0.0077  0.0012  0.0044  312 LYS A CG  
1864 C CD  . LYS A 238 ? 0.1533 0.1529 0.1361 0.0081  0.0008  0.0035  312 LYS A CD  
1865 C CE  . LYS A 238 ? 0.1628 0.1622 0.1456 0.0096  0.0012  0.0045  312 LYS A CE  
1866 N NZ  . LYS A 238 ? 0.1504 0.1502 0.1334 0.0096  0.0007  0.0037  312 LYS A NZ  
1867 N N   . GLY A 239 ? 0.1540 0.1480 0.1328 0.0120  0.0026  0.0036  313 GLY A N   
1868 C CA  . GLY A 239 ? 0.1560 0.1488 0.1340 0.0120  0.0025  0.0026  313 GLY A CA  
1869 C C   . GLY A 239 ? 0.1483 0.1404 0.1248 0.0134  0.0018  0.0007  313 GLY A C   
1870 O O   . GLY A 239 ? 0.1567 0.1489 0.1332 0.0127  0.0013  -0.0006 313 GLY A O   
1871 N N   . LEU A 240 ? 0.1459 0.1372 0.1210 0.0155  0.0018  0.0006  314 LEU A N   
1872 C CA  . LEU A 240 ? 0.1496 0.1404 0.1235 0.0167  0.0008  -0.0011 314 LEU A CA  
1873 C C   . LEU A 240 ? 0.1444 0.1368 0.1199 0.0152  0.0000  -0.0024 314 LEU A C   
1874 O O   . LEU A 240 ? 0.1452 0.1377 0.1207 0.0152  -0.0007 -0.0040 314 LEU A O   
1875 C CB  . LEU A 240 ? 0.1611 0.1507 0.1332 0.0191  0.0007  -0.0010 314 LEU A CB  
1876 C CG  . LEU A 240 ? 0.1760 0.1636 0.1460 0.0211  0.0018  0.0002  314 LEU A CG  
1877 C CD1 . LEU A 240 ? 0.2161 0.2024 0.1839 0.0234  0.0017  0.0003  314 LEU A CD1 
1878 C CD2 . LEU A 240 ? 0.2075 0.1937 0.1762 0.0220  0.0018  -0.0004 314 LEU A CD2 
1879 N N   . GLU A 241 ? 0.1350 0.1288 0.1118 0.0139  0.0000  -0.0017 315 GLU A N   
1880 C CA  . GLU A 241 ? 0.1383 0.1337 0.1167 0.0125  -0.0006 -0.0027 315 GLU A CA  
1881 C C   . GLU A 241 ? 0.1336 0.1298 0.1128 0.0107  -0.0006 -0.0032 315 GLU A C   
1882 O O   . GLU A 241 ? 0.1443 0.1413 0.1243 0.0101  -0.0011 -0.0043 315 GLU A O   
1883 C CB  . GLU A 241 ? 0.1373 0.1337 0.1166 0.0118  -0.0005 -0.0016 315 GLU A CB  
1884 C CG  . GLU A 241 ? 0.1535 0.1490 0.1320 0.0136  -0.0007 -0.0015 315 GLU A CG  
1885 C CD  . GLU A 241 ? 0.1467 0.1433 0.1264 0.0130  -0.0005 -0.0006 315 GLU A CD  
1886 O OE1 . GLU A 241 ? 0.1571 0.1550 0.1381 0.0111  -0.0002 0.0002  315 GLU A OE1 
1887 O OE2 . GLU A 241 ? 0.1520 0.1478 0.1310 0.0144  -0.0007 -0.0008 315 GLU A OE2 
1888 N N   . VAL A 242 ? 0.1352 0.1309 0.1141 0.0100  -0.0001 -0.0024 316 VAL A N   
1889 C CA  . VAL A 242 ? 0.1377 0.1336 0.1168 0.0085  -0.0001 -0.0030 316 VAL A CA  
1890 C C   . VAL A 242 ? 0.1322 0.1273 0.1107 0.0095  -0.0003 -0.0046 316 VAL A C   
1891 O O   . VAL A 242 ? 0.1387 0.1344 0.1175 0.0088  -0.0005 -0.0058 316 VAL A O   
1892 C CB  . VAL A 242 ? 0.1490 0.1443 0.1280 0.0076  0.0003  -0.0018 316 VAL A CB  
1893 C CG1 . VAL A 242 ? 0.1538 0.1485 0.1324 0.0066  0.0002  -0.0028 316 VAL A CG1 
1894 C CG2 . VAL A 242 ? 0.1449 0.1414 0.1251 0.0063  0.0003  -0.0004 316 VAL A CG2 
1895 N N   . ILE A 243 ? 0.1413 0.1349 0.1185 0.0114  -0.0002 -0.0046 317 ILE A N   
1896 C CA  . ILE A 243 ? 0.1349 0.1277 0.1115 0.0126  -0.0005 -0.0060 317 ILE A CA  
1897 C C   . ILE A 243 ? 0.1389 0.1328 0.1164 0.0131  -0.0014 -0.0073 317 ILE A C   
1898 O O   . ILE A 243 ? 0.1467 0.1410 0.1249 0.0130  -0.0017 -0.0086 317 ILE A O   
1899 C CB  . ILE A 243 ? 0.1442 0.1352 0.1191 0.0146  -0.0002 -0.0055 317 ILE A CB  
1900 C CG1 . ILE A 243 ? 0.1595 0.1495 0.1341 0.0139  0.0006  -0.0043 317 ILE A CG1 
1901 C CG2 . ILE A 243 ? 0.1503 0.1405 0.1245 0.0162  -0.0008 -0.0070 317 ILE A CG2 
1902 C CD1 . ILE A 243 ? 0.1641 0.1522 0.1371 0.0158  0.0012  -0.0033 317 ILE A CD1 
1903 N N   . GLU A 244 ? 0.1405 0.1347 0.1182 0.0136  -0.0018 -0.0070 318 GLU A N   
1904 C CA  . GLU A 244 ? 0.1443 0.1395 0.1233 0.0138  -0.0026 -0.0081 318 GLU A CA  
1905 C C   . GLU A 244 ? 0.1404 0.1373 0.1213 0.0120  -0.0025 -0.0086 318 GLU A C   
1906 O O   . GLU A 244 ? 0.1530 0.1506 0.1353 0.0120  -0.0030 -0.0098 318 GLU A O   
1907 C CB  . GLU A 244 ? 0.1484 0.1435 0.1272 0.0145  -0.0029 -0.0075 318 GLU A CB  
1908 C CG  . GLU A 244 ? 0.1602 0.1560 0.1403 0.0148  -0.0040 -0.0087 318 GLU A CG  
1909 C CD  . GLU A 244 ? 0.1633 0.1588 0.1433 0.0153  -0.0042 -0.0081 318 GLU A CD  
1910 O OE1 . GLU A 244 ? 0.1658 0.1610 0.1448 0.0152  -0.0033 -0.0066 318 GLU A OE1 
1911 O OE2 . GLU A 244 ? 0.1840 0.1797 0.1649 0.0158  -0.0052 -0.0091 318 GLU A OE2 
1912 N N   . THR A 245 ? 0.1419 0.1394 0.1230 0.0103  -0.0018 -0.0076 319 THR A N   
1913 C CA  . THR A 245 ? 0.1350 0.1338 0.1173 0.0086  -0.0016 -0.0078 319 THR A CA  
1914 C C   . THR A 245 ? 0.1501 0.1487 0.1323 0.0085  -0.0013 -0.0089 319 THR A C   
1915 O O   . THR A 245 ? 0.1532 0.1527 0.1367 0.0080  -0.0012 -0.0097 319 THR A O   
1916 C CB  . THR A 245 ? 0.1418 0.1410 0.1238 0.0070  -0.0011 -0.0064 319 THR A CB  
1917 O OG1 . THR A 245 ? 0.1568 0.1564 0.1392 0.0072  -0.0012 -0.0054 319 THR A OG1 
1918 C CG2 . THR A 245 ? 0.1444 0.1447 0.1269 0.0054  -0.0008 -0.0066 319 THR A CG2 
1919 N N   . HIS A 246 ? 0.1443 0.1416 0.1251 0.0088  -0.0010 -0.0087 320 HIS A N   
1920 C CA  . HIS A 246 ? 0.1521 0.1488 0.1325 0.0089  -0.0007 -0.0097 320 HIS A CA  
1921 C C   . HIS A 246 ? 0.1515 0.1486 0.1330 0.0101  -0.0012 -0.0110 320 HIS A C   
1922 O O   . HIS A 246 ? 0.1672 0.1650 0.1497 0.0097  -0.0008 -0.0118 320 HIS A O   
1923 C CB  . HIS A 246 ? 0.1578 0.1527 0.1365 0.0094  -0.0004 -0.0093 320 HIS A CB  
1924 C CG  . HIS A 246 ? 0.1649 0.1589 0.1431 0.0100  -0.0002 -0.0103 320 HIS A CG  
1925 N ND1 . HIS A 246 ? 0.1799 0.1738 0.1579 0.0088  0.0002  -0.0108 320 HIS A ND1 
1926 C CD2 . HIS A 246 ? 0.1903 0.1832 0.1680 0.0117  -0.0003 -0.0109 320 HIS A CD2 
1927 C CE1 . HIS A 246 ? 0.1987 0.1917 0.1764 0.0098  0.0005  -0.0117 320 HIS A CE1 
1928 N NE2 . HIS A 246 ? 0.2116 0.2040 0.1891 0.0115  0.0000  -0.0118 320 HIS A NE2 
1929 N N   . PHE A 247 ? 0.1501 0.1468 0.1315 0.0118  -0.0019 -0.0112 321 PHE A N   
1930 C CA  . PHE A 247 ? 0.1640 0.1610 0.1466 0.0131  -0.0026 -0.0124 321 PHE A CA  
1931 C C   . PHE A 247 ? 0.1640 0.1628 0.1492 0.0124  -0.0031 -0.0130 321 PHE A C   
1932 O O   . PHE A 247 ? 0.1788 0.1786 0.1659 0.0125  -0.0031 -0.0139 321 PHE A O   
1933 C CB  . PHE A 247 ? 0.1730 0.1688 0.1544 0.0151  -0.0035 -0.0125 321 PHE A CB  
1934 C CG  . PHE A 247 ? 0.1895 0.1836 0.1689 0.0161  -0.0031 -0.0123 321 PHE A CG  
1935 C CD1 . PHE A 247 ? 0.2351 0.2290 0.2148 0.0165  -0.0029 -0.0132 321 PHE A CD1 
1936 C CD2 . PHE A 247 ? 0.2212 0.2137 0.1984 0.0168  -0.0028 -0.0112 321 PHE A CD2 
1937 C CE1 . PHE A 247 ? 0.2443 0.2364 0.2222 0.0175  -0.0025 -0.0129 321 PHE A CE1 
1938 C CE2 . PHE A 247 ? 0.2490 0.2398 0.2246 0.0177  -0.0022 -0.0108 321 PHE A CE2 
1939 C CZ  . PHE A 247 ? 0.2635 0.2541 0.2393 0.0180  -0.0021 -0.0118 321 PHE A CZ  
1940 N N   . LEU A 248 ? 0.1562 0.1554 0.1418 0.0119  -0.0033 -0.0123 322 LEU A N   
1941 C CA  . LEU A 248 ? 0.1549 0.1557 0.1432 0.0114  -0.0037 -0.0128 322 LEU A CA  
1942 C C   . LEU A 248 ? 0.1667 0.1688 0.1565 0.0098  -0.0027 -0.0128 322 LEU A C   
1943 O O   . LEU A 248 ? 0.1808 0.1841 0.1732 0.0097  -0.0028 -0.0135 322 LEU A O   
1944 C CB  . LEU A 248 ? 0.1686 0.1695 0.1569 0.0110  -0.0039 -0.0120 322 LEU A CB  
1945 C CG  . LEU A 248 ? 0.1597 0.1593 0.1468 0.0127  -0.0050 -0.0122 322 LEU A CG  
1946 C CD1 . LEU A 248 ? 0.1640 0.1636 0.1509 0.0122  -0.0049 -0.0111 322 LEU A CD1 
1947 C CD2 . LEU A 248 ? 0.1903 0.1904 0.1795 0.0137  -0.0064 -0.0137 322 LEU A CD2 
1948 N N   . PHE A 249 ? 0.1605 0.1624 0.1487 0.0086  -0.0017 -0.0120 323 PHE A N   
1949 C CA  . PHE A 249 ? 0.1632 0.1661 0.1522 0.0072  -0.0007 -0.0118 323 PHE A CA  
1950 C C   . PHE A 249 ? 0.1805 0.1827 0.1681 0.0069  0.0001  -0.0121 323 PHE A C   
1951 O O   . PHE A 249 ? 0.1934 0.1962 0.1810 0.0058  0.0010  -0.0119 323 PHE A O   
1952 C CB  . PHE A 249 ? 0.1734 0.1765 0.1616 0.0059  -0.0005 -0.0105 323 PHE A CB  
1953 C CG  . PHE A 249 ? 0.1642 0.1677 0.1536 0.0063  -0.0012 -0.0101 323 PHE A CG  
1954 C CD1 . PHE A 249 ? 0.1698 0.1743 0.1619 0.0064  -0.0015 -0.0108 323 PHE A CD1 
1955 C CD2 . PHE A 249 ? 0.1688 0.1716 0.1568 0.0065  -0.0015 -0.0092 323 PHE A CD2 
1956 C CE1 . PHE A 249 ? 0.1747 0.1793 0.1678 0.0068  -0.0023 -0.0105 323 PHE A CE1 
1957 C CE2 . PHE A 249 ? 0.1605 0.1634 0.1493 0.0069  -0.0021 -0.0089 323 PHE A CE2 
1958 C CZ  . PHE A 249 ? 0.1638 0.1675 0.1550 0.0071  -0.0025 -0.0096 323 PHE A CZ  
1959 N N   . ASP A 250 ? 0.1801 0.1811 0.1664 0.0079  -0.0001 -0.0126 324 ASP A N   
1960 C CA  . ASP A 250 ? 0.1873 0.1874 0.1724 0.0078  0.0006  -0.0130 324 ASP A CA  
1961 C C   . ASP A 250 ? 0.1804 0.1798 0.1634 0.0063  0.0013  -0.0123 324 ASP A C   
1962 O O   . ASP A 250 ? 0.2011 0.2004 0.1834 0.0057  0.0021  -0.0126 324 ASP A O   
1963 C CB  . ASP A 250 ? 0.2421 0.2434 0.2294 0.0080  0.0012  -0.0139 324 ASP A CB  
1964 C CG  . ASP A 250 ? 0.3452 0.3459 0.3316 0.0080  0.0023  -0.0145 324 ASP A CG  
1965 O OD1 . ASP A 250 ? 0.3376 0.3367 0.3224 0.0088  0.0021  -0.0148 324 ASP A OD1 
1966 O OD2 . ASP A 250 ? 0.3381 0.3397 0.3253 0.0073  0.0033  -0.0145 324 ASP A OD2 
1967 N N   . VAL A 251 ? 0.1653 0.1642 0.1471 0.0059  0.0008  -0.0113 325 VAL A N   
1968 C CA  . VAL A 251 ? 0.1722 0.1706 0.1523 0.0044  0.0011  -0.0106 325 VAL A CA  
1969 C C   . VAL A 251 ? 0.1583 0.1549 0.1367 0.0046  0.0009  -0.0104 325 VAL A C   
1970 O O   . VAL A 251 ? 0.1710 0.1671 0.1496 0.0056  0.0005  -0.0100 325 VAL A O   
1971 C CB  . VAL A 251 ? 0.1792 0.1787 0.1599 0.0036  0.0007  -0.0094 325 VAL A CB  
1972 C CG1 . VAL A 251 ? 0.1878 0.1868 0.1668 0.0021  0.0007  -0.0086 325 VAL A CG1 
1973 C CG2 . VAL A 251 ? 0.2247 0.2258 0.2071 0.0034  0.0010  -0.0095 325 VAL A CG2 
1974 N N   . ASP A 252 ? 0.1654 0.1609 0.1422 0.0037  0.0012  -0.0106 326 ASP A N   
1975 C CA  . ASP A 252 ? 0.1773 0.1710 0.1527 0.0036  0.0011  -0.0105 326 ASP A CA  
1976 C C   . ASP A 252 ? 0.1729 0.1667 0.1485 0.0030  0.0006  -0.0091 326 ASP A C   
1977 O O   . ASP A 252 ? 0.1627 0.1577 0.1387 0.0021  0.0003  -0.0083 326 ASP A O   
1978 C CB  . ASP A 252 ? 0.1964 0.1888 0.1700 0.0026  0.0014  -0.0111 326 ASP A CB  
1979 C CG  . ASP A 252 ? 0.2474 0.2391 0.2204 0.0033  0.0022  -0.0124 326 ASP A CG  
1980 O OD1 . ASP A 252 ? 0.2787 0.2711 0.2531 0.0047  0.0024  -0.0129 326 ASP A OD1 
1981 O OD2 . ASP A 252 ? 0.2981 0.2887 0.2693 0.0025  0.0025  -0.0130 326 ASP A OD2 
1982 N N   . TYR A 253 ? 0.1681 0.1606 0.1435 0.0035  0.0005  -0.0086 327 TYR A N   
1983 C CA  . TYR A 253 ? 0.1624 0.1550 0.1382 0.0031  0.0002  -0.0071 327 TYR A CA  
1984 C C   . TYR A 253 ? 0.1722 0.1650 0.1478 0.0011  -0.0001 -0.0066 327 TYR A C   
1985 O O   . TYR A 253 ? 0.1677 0.1615 0.1442 0.0005  -0.0005 -0.0053 327 TYR A O   
1986 C CB  . TYR A 253 ? 0.1609 0.1518 0.1366 0.0040  0.0004  -0.0067 327 TYR A CB  
1987 C CG  . TYR A 253 ? 0.1571 0.1479 0.1329 0.0061  0.0006  -0.0068 327 TYR A CG  
1988 C CD1 . TYR A 253 ? 0.1575 0.1492 0.1340 0.0068  0.0005  -0.0058 327 TYR A CD1 
1989 C CD2 . TYR A 253 ? 0.1623 0.1522 0.1375 0.0074  0.0008  -0.0080 327 TYR A CD2 
1990 C CE1 . TYR A 253 ? 0.1602 0.1517 0.1365 0.0088  0.0005  -0.0062 327 TYR A CE1 
1991 C CE2 . TYR A 253 ? 0.1687 0.1587 0.1440 0.0093  0.0007  -0.0083 327 TYR A CE2 
1992 C CZ  . TYR A 253 ? 0.1538 0.1445 0.1295 0.0100  0.0005  -0.0074 327 TYR A CZ  
1993 O OH  . TYR A 253 ? 0.1704 0.1609 0.1458 0.0120  0.0001  -0.0077 327 TYR A OH  
1994 N N   . ASN A 254 ? 0.1736 0.1653 0.1478 0.0002  -0.0002 -0.0075 328 ASN A N   
1995 C CA  . ASN A 254 ? 0.1901 0.1819 0.1637 -0.0014 -0.0009 -0.0071 328 ASN A CA  
1996 C C   . ASN A 254 ? 0.1774 0.1711 0.1511 -0.0020 -0.0010 -0.0068 328 ASN A C   
1997 O O   . ASN A 254 ? 0.2014 0.1954 0.1748 -0.0034 -0.0018 -0.0062 328 ASN A O   
1998 C CB  . ASN A 254 ? 0.2254 0.2153 0.1971 -0.0020 -0.0009 -0.0084 328 ASN A CB  
1999 C CG  . ASN A 254 ? 0.2985 0.2862 0.2701 -0.0019 -0.0009 -0.0085 328 ASN A CG  
2000 O OD1 . ASN A 254 ? 0.3417 0.3295 0.3148 -0.0016 -0.0009 -0.0073 328 ASN A OD1 
2001 N ND2 . ASN A 254 ? 0.3828 0.3685 0.3525 -0.0022 -0.0008 -0.0098 328 ASN A ND2 
2002 N N   . ASP A 255 ? 0.1634 0.1581 0.1377 -0.0011 -0.0005 -0.0072 329 ASP A N   
2003 C CA  . ASP A 255 ? 0.1647 0.1611 0.1393 -0.0015 -0.0004 -0.0069 329 ASP A CA  
2004 C C   . ASP A 255 ? 0.1559 0.1538 0.1324 -0.0009 -0.0005 -0.0059 329 ASP A C   
2005 O O   . ASP A 255 ? 0.1549 0.1542 0.1322 -0.0009 -0.0003 -0.0057 329 ASP A O   
2006 C CB  . ASP A 255 ? 0.1741 0.1706 0.1482 -0.0010 0.0002  -0.0081 329 ASP A CB  
2007 C CG  . ASP A 255 ? 0.2080 0.2028 0.1797 -0.0015 0.0004  -0.0092 329 ASP A CG  
2008 O OD1 . ASP A 255 ? 0.2470 0.2411 0.2173 -0.0027 -0.0001 -0.0089 329 ASP A OD1 
2009 O OD2 . ASP A 255 ? 0.2225 0.2168 0.1940 -0.0007 0.0012  -0.0103 329 ASP A OD2 
2010 N N   . ILE A 256 ? 0.1443 0.1420 0.1217 -0.0004 -0.0007 -0.0051 330 ILE A N   
2011 C CA  . ILE A 256 ? 0.1407 0.1395 0.1196 0.0002  -0.0008 -0.0040 330 ILE A CA  
2012 C C   . ILE A 256 ? 0.1477 0.1466 0.1271 -0.0005 -0.0012 -0.0025 330 ILE A C   
2013 O O   . ILE A 256 ? 0.1523 0.1502 0.1317 -0.0006 -0.0012 -0.0022 330 ILE A O   
2014 C CB  . ILE A 256 ? 0.1398 0.1379 0.1191 0.0020  -0.0005 -0.0043 330 ILE A CB  
2015 C CG1 . ILE A 256 ? 0.1498 0.1478 0.1290 0.0028  -0.0002 -0.0058 330 ILE A CG1 
2016 C CG2 . ILE A 256 ? 0.1482 0.1472 0.1286 0.0027  -0.0005 -0.0032 330 ILE A CG2 
2017 C CD1 . ILE A 256 ? 0.1582 0.1553 0.1373 0.0046  -0.0002 -0.0064 330 ILE A CD1 
2018 N N   . GLU A 257 ? 0.1419 0.1423 0.1222 -0.0012 -0.0014 -0.0014 331 GLU A N   
2019 C CA  . GLU A 257 ? 0.1472 0.1481 0.1283 -0.0021 -0.0019 0.0000  331 GLU A CA  
2020 C C   . GLU A 257 ? 0.1567 0.1586 0.1393 -0.0012 -0.0016 0.0013  331 GLU A C   
2021 O O   . GLU A 257 ? 0.1730 0.1759 0.1559 -0.0009 -0.0015 0.0013  331 GLU A O   
2022 C CB  . GLU A 257 ? 0.1636 0.1654 0.1443 -0.0037 -0.0026 0.0002  331 GLU A CB  
2023 C CG  . GLU A 257 ? 0.2028 0.2054 0.1847 -0.0047 -0.0033 0.0018  331 GLU A CG  
2024 C CD  . GLU A 257 ? 0.2413 0.2445 0.2225 -0.0062 -0.0043 0.0021  331 GLU A CD  
2025 O OE1 . GLU A 257 ? 0.2569 0.2598 0.2362 -0.0066 -0.0044 0.0010  331 GLU A OE1 
2026 O OE2 . GLU A 257 ? 0.3180 0.3222 0.3007 -0.0069 -0.0050 0.0035  331 GLU A OE2 
2027 N N   . VAL A 258 ? 0.1491 0.1507 0.1327 -0.0007 -0.0014 0.0025  332 VAL A N   
2028 C CA  . VAL A 258 ? 0.1473 0.1497 0.1321 0.0002  -0.0010 0.0038  332 VAL A CA  
2029 C C   . VAL A 258 ? 0.1506 0.1546 0.1368 -0.0009 -0.0014 0.0054  332 VAL A C   
2030 O O   . VAL A 258 ? 0.1721 0.1763 0.1590 -0.0022 -0.0020 0.0060  332 VAL A O   
2031 C CB  . VAL A 258 ? 0.1543 0.1556 0.1394 0.0014  -0.0003 0.0046  332 VAL A CB  
2032 C CG1 . VAL A 258 ? 0.1751 0.1772 0.1614 0.0025  0.0002  0.0062  332 VAL A CG1 
2033 C CG2 . VAL A 258 ? 0.1630 0.1628 0.1466 0.0029  0.0000  0.0032  332 VAL A CG2 
2034 N N   . ILE A 259 ? 0.1353 0.1403 0.1220 -0.0005 -0.0013 0.0060  333 ILE A N   
2035 C CA  . ILE A 259 ? 0.1454 0.1520 0.1335 -0.0015 -0.0017 0.0075  333 ILE A CA  
2036 C C   . ILE A 259 ? 0.1420 0.1490 0.1313 -0.0001 -0.0010 0.0089  333 ILE A C   
2037 O O   . ILE A 259 ? 0.1524 0.1590 0.1410 0.0010  -0.0005 0.0082  333 ILE A O   
2038 C CB  . ILE A 259 ? 0.1814 0.1889 0.1688 -0.0025 -0.0023 0.0070  333 ILE A CB  
2039 C CG1 . ILE A 259 ? 0.2162 0.2253 0.2048 -0.0037 -0.0030 0.0086  333 ILE A CG1 
2040 C CG2 . ILE A 259 ? 0.2078 0.2152 0.1946 -0.0017 -0.0018 0.0062  333 ILE A CG2 
2041 C CD1 . ILE A 259 ? 0.2606 0.2695 0.2492 -0.0051 -0.0040 0.0087  333 ILE A CD1 
2042 N N   . VAL A 260 ? 0.1304 0.1384 0.1215 -0.0003 -0.0009 0.0107  334 VAL A N   
2043 C CA  . VAL A 260 ? 0.1226 0.1310 0.1149 0.0009  -0.0001 0.0122  334 VAL A CA  
2044 C C   . VAL A 260 ? 0.1297 0.1396 0.1226 0.0003  -0.0005 0.0128  334 VAL A C   
2045 O O   . VAL A 260 ? 0.1318 0.1430 0.1256 -0.0010 -0.0013 0.0136  334 VAL A O   
2046 C CB  . VAL A 260 ? 0.1390 0.1479 0.1334 0.0011  0.0003  0.0141  334 VAL A CB  
2047 C CG1 . VAL A 260 ? 0.1465 0.1557 0.1418 0.0026  0.0014  0.0156  334 VAL A CG1 
2048 C CG2 . VAL A 260 ? 0.1632 0.1704 0.1568 0.0017  0.0009  0.0136  334 VAL A CG2 
2049 N N   . HIS A 261 ? 0.1273 0.1367 0.1195 0.0015  0.0000  0.0124  335 HIS A N   
2050 C CA  . HIS A 261 ? 0.1255 0.1359 0.1181 0.0013  -0.0001 0.0129  335 HIS A CA  
2051 C C   . HIS A 261 ? 0.1331 0.1431 0.1263 0.0030  0.0007  0.0139  335 HIS A C   
2052 O O   . HIS A 261 ? 0.1394 0.1481 0.1315 0.0043  0.0011  0.0128  335 HIS A O   
2053 C CB  . HIS A 261 ? 0.1318 0.1416 0.1230 0.0010  -0.0004 0.0110  335 HIS A CB  
2054 C CG  . HIS A 261 ? 0.1317 0.1422 0.1233 0.0009  -0.0003 0.0115  335 HIS A CG  
2055 N ND1 . HIS A 261 ? 0.1406 0.1525 0.1333 0.0002  -0.0006 0.0131  335 HIS A ND1 
2056 C CD2 . HIS A 261 ? 0.1315 0.1412 0.1228 0.0016  0.0000  0.0106  335 HIS A CD2 
2057 C CE1 . HIS A 261 ? 0.1401 0.1521 0.1330 0.0005  -0.0003 0.0132  335 HIS A CE1 
2058 N NE2 . HIS A 261 ? 0.1414 0.1520 0.1335 0.0013  0.0000  0.0117  335 HIS A NE2 
2059 N N   . LYS A 262 ? 0.1344 0.1455 0.1294 0.0031  0.0010  0.0159  336 LYS A N   
2060 C CA  . LYS A 262 ? 0.1465 0.1570 0.1419 0.0050  0.0022  0.0170  336 LYS A CA  
2061 C C   . LYS A 262 ? 0.1420 0.1520 0.1369 0.0059  0.0025  0.0168  336 LYS A C   
2062 O O   . LYS A 262 ? 0.1609 0.1696 0.1552 0.0077  0.0033  0.0169  336 LYS A O   
2063 C CB  . LYS A 262 ? 0.1743 0.1862 0.1722 0.0048  0.0026  0.0194  336 LYS A CB  
2064 C CG  . LYS A 262 ? 0.1976 0.2116 0.1974 0.0038  0.0020  0.0207  336 LYS A CG  
2065 C CD  . LYS A 262 ? 0.2480 0.2637 0.2508 0.0036  0.0022  0.0232  336 LYS A CD  
2066 C CE  . LYS A 262 ? 0.3190 0.3365 0.3235 0.0032  0.0019  0.0247  336 LYS A CE  
2067 N NZ  . LYS A 262 ? 0.3787 0.3973 0.3831 0.0012  0.0003  0.0243  336 LYS A NZ  
2068 N N   . GLU A 263 ? 0.1356 0.1465 0.1308 0.0047  0.0018  0.0166  337 GLU A N   
2069 C CA  . GLU A 263 ? 0.1381 0.1485 0.1331 0.0054  0.0021  0.0165  337 GLU A CA  
2070 C C   . GLU A 263 ? 0.1341 0.1426 0.1274 0.0061  0.0020  0.0143  337 GLU A C   
2071 O O   . GLU A 263 ? 0.1476 0.1551 0.1407 0.0071  0.0023  0.0139  337 GLU A O   
2072 C CB  . GLU A 263 ? 0.1516 0.1635 0.1475 0.0041  0.0015  0.0172  337 GLU A CB  
2073 C CG  . GLU A 263 ? 0.1572 0.1711 0.1550 0.0033  0.0013  0.0193  337 GLU A CG  
2074 C CD  . GLU A 263 ? 0.1782 0.1932 0.1762 0.0018  0.0003  0.0194  337 GLU A CD  
2075 O OE1 . GLU A 263 ? 0.1665 0.1808 0.1630 0.0011  0.0000  0.0177  337 GLU A OE1 
2076 O OE2 . GLU A 263 ? 0.2208 0.2375 0.2207 0.0012  0.0000  0.0211  337 GLU A OE2 
2077 N N   . CYS A 264 ? 0.1379 0.1459 0.1301 0.0057  0.0016  0.0127  338 CYS A N   
2078 C CA  . CYS A 264 ? 0.1496 0.1560 0.1405 0.0064  0.0014  0.0106  338 CYS A CA  
2079 C C   . CYS A 264 ? 0.1425 0.1489 0.1339 0.0060  0.0011  0.0099  338 CYS A C   
2080 O O   . CYS A 264 ? 0.1495 0.1545 0.1405 0.0070  0.0011  0.0087  338 CYS A O   
2081 C CB  . CYS A 264 ? 0.1535 0.1581 0.1433 0.0085  0.0019  0.0104  338 CYS A CB  
2082 S SG  . CYS A 264 ? 0.2053 0.2095 0.1944 0.0093  0.0024  0.0112  338 CYS A SG  
2083 N N   . ILE A 265 ? 0.1339 0.1418 0.1261 0.0044  0.0009  0.0105  339 ILE A N   
2084 C CA  . ILE A 265 ? 0.1387 0.1467 0.1314 0.0037  0.0008  0.0099  339 ILE A CA  
2085 C C   . ILE A 265 ? 0.1381 0.1462 0.1304 0.0028  0.0005  0.0084  339 ILE A C   
2086 O O   . ILE A 265 ? 0.1450 0.1524 0.1376 0.0030  0.0004  0.0070  339 ILE A O   
2087 C CB  . ILE A 265 ? 0.1362 0.1456 0.1299 0.0029  0.0010  0.0117  339 ILE A CB  
2088 C CG1 . ILE A 265 ? 0.1481 0.1574 0.1425 0.0040  0.0014  0.0133  339 ILE A CG1 
2089 C CG2 . ILE A 265 ? 0.1469 0.1564 0.1411 0.0022  0.0011  0.0113  339 ILE A CG2 
2090 C CD1 . ILE A 265 ? 0.1554 0.1630 0.1499 0.0054  0.0018  0.0127  339 ILE A CD1 
2091 N N   . ILE A 266 ? 0.1313 0.1404 0.1230 0.0017  0.0002  0.0085  340 ILE A N   
2092 C CA  . ILE A 266 ? 0.1470 0.1559 0.1379 0.0010  0.0000  0.0070  340 ILE A CA  
2093 C C   . ILE A 266 ? 0.1386 0.1463 0.1288 0.0020  -0.0001 0.0057  340 ILE A C   
2094 O O   . ILE A 266 ? 0.1705 0.1780 0.1602 0.0024  -0.0001 0.0063  340 ILE A O   
2095 C CB  . ILE A 266 ? 0.1466 0.1565 0.1367 -0.0003 -0.0002 0.0076  340 ILE A CB  
2096 C CG1 . ILE A 266 ? 0.1851 0.1960 0.1756 -0.0011 -0.0001 0.0088  340 ILE A CG1 
2097 C CG2 . ILE A 266 ? 0.1736 0.1831 0.1627 -0.0007 -0.0003 0.0060  340 ILE A CG2 
2098 C CD1 . ILE A 266 ? 0.2410 0.2528 0.2303 -0.0024 -0.0006 0.0093  340 ILE A CD1 
2099 N N   . HIS A 267 ? 0.1373 0.1443 0.1277 0.0025  -0.0001 0.0041  341 HIS A N   
2100 C CA  . HIS A 267 ? 0.1379 0.1436 0.1274 0.0038  -0.0004 0.0029  341 HIS A CA  
2101 C C   . HIS A 267 ? 0.1404 0.1460 0.1291 0.0034  -0.0005 0.0020  341 HIS A C   
2102 O O   . HIS A 267 ? 0.1594 0.1640 0.1472 0.0045  -0.0007 0.0014  341 HIS A O   
2103 C CB  . HIS A 267 ? 0.1538 0.1586 0.1441 0.0048  -0.0006 0.0017  341 HIS A CB  
2104 C CG  . HIS A 267 ? 0.1718 0.1761 0.1625 0.0056  -0.0005 0.0027  341 HIS A CG  
2105 N ND1 . HIS A 267 ? 0.2829 0.2871 0.2730 0.0062  -0.0001 0.0042  341 HIS A ND1 
2106 C CD2 . HIS A 267 ? 0.2008 0.2050 0.1927 0.0055  -0.0005 0.0026  341 HIS A CD2 
2107 C CE1 . HIS A 267 ? 0.1937 0.1974 0.1844 0.0068  0.0000  0.0047  341 HIS A CE1 
2108 N NE2 . HIS A 267 ? 0.2128 0.2164 0.2045 0.0064  -0.0002 0.0038  341 HIS A NE2 
2109 N N   . SER A 268 ? 0.1372 0.1436 0.1259 0.0021  -0.0004 0.0018  342 SER A N   
2110 C CA  . SER A 268 ? 0.1390 0.1453 0.1266 0.0015  -0.0005 0.0011  342 SER A CA  
2111 C C   . SER A 268 ? 0.1385 0.1456 0.1263 0.0003  -0.0002 0.0008  342 SER A C   
2112 O O   . SER A 268 ? 0.1472 0.1549 0.1361 0.0001  0.0000  0.0010  342 SER A O   
2113 C CB  . SER A 268 ? 0.1371 0.1423 0.1241 0.0025  -0.0007 -0.0003 342 SER A CB  
2114 O OG  . SER A 268 ? 0.1475 0.1519 0.1338 0.0034  -0.0008 0.0002  342 SER A OG  
2115 N N   . CYS A 269 ? 0.1324 0.1393 0.1189 -0.0003 -0.0002 0.0003  343 CYS A N   
2116 C CA  . CYS A 269 ? 0.1442 0.1517 0.1302 -0.0013 0.0001  0.0002  343 CYS A CA  
2117 C C   . CYS A 269 ? 0.1405 0.1474 0.1256 -0.0013 0.0003  -0.0012 343 CYS A C   
2118 O O   . CYS A 269 ? 0.1591 0.1651 0.1433 -0.0010 0.0000  -0.0017 343 CYS A O   
2119 C CB  . CYS A 269 ? 0.1666 0.1746 0.1514 -0.0024 -0.0001 0.0014  343 CYS A CB  
2120 S SG  . CYS A 269 ? 0.1811 0.1898 0.1668 -0.0024 -0.0005 0.0033  343 CYS A SG  
2121 N N   . VAL A 270 ? 0.1404 0.1476 0.1255 -0.0017 0.0010  -0.0016 344 VAL A N   
2122 C CA  . VAL A 270 ? 0.1374 0.1440 0.1217 -0.0016 0.0014  -0.0029 344 VAL A CA  
2123 C C   . VAL A 270 ? 0.1333 0.1400 0.1157 -0.0026 0.0019  -0.0026 344 VAL A C   
2124 O O   . VAL A 270 ? 0.1409 0.1483 0.1235 -0.0030 0.0025  -0.0018 344 VAL A O   
2125 C CB  . VAL A 270 ? 0.1452 0.1523 0.1318 -0.0010 0.0020  -0.0038 344 VAL A CB  
2126 C CG1 . VAL A 270 ? 0.1607 0.1673 0.1466 -0.0008 0.0026  -0.0051 344 VAL A CG1 
2127 C CG2 . VAL A 270 ? 0.1682 0.1751 0.1564 0.0000  0.0013  -0.0043 344 VAL A CG2 
2128 N N   . GLU A 271 ? 0.1339 0.1395 0.1140 -0.0029 0.0017  -0.0031 345 GLU A N   
2129 C CA  . GLU A 271 ? 0.1374 0.1426 0.1150 -0.0036 0.0020  -0.0032 345 GLU A CA  
2130 C C   . GLU A 271 ? 0.1395 0.1442 0.1170 -0.0030 0.0032  -0.0044 345 GLU A C   
2131 O O   . GLU A 271 ? 0.1480 0.1520 0.1257 -0.0024 0.0031  -0.0055 345 GLU A O   
2132 C CB  . GLU A 271 ? 0.1463 0.1504 0.1216 -0.0042 0.0010  -0.0033 345 GLU A CB  
2133 C CG  . GLU A 271 ? 0.1667 0.1699 0.1389 -0.0048 0.0012  -0.0035 345 GLU A CG  
2134 C CD  . GLU A 271 ? 0.2147 0.2167 0.1850 -0.0054 0.0000  -0.0038 345 GLU A CD  
2135 O OE1 . GLU A 271 ? 0.2804 0.2829 0.2507 -0.0062 -0.0010 -0.0028 345 GLU A OE1 
2136 O OE2 . GLU A 271 ? 0.2315 0.2321 0.2011 -0.0051 0.0001  -0.0050 345 GLU A OE2 
2137 N N   . PHE A 272 ? 0.1419 0.1470 0.1192 -0.0031 0.0043  -0.0042 346 PHE A N   
2138 C CA  . PHE A 272 ? 0.1475 0.1523 0.1248 -0.0026 0.0056  -0.0051 346 PHE A CA  
2139 C C   . PHE A 272 ? 0.1549 0.1582 0.1283 -0.0029 0.0058  -0.0057 346 PHE A C   
2140 O O   . PHE A 272 ? 0.1624 0.1649 0.1332 -0.0036 0.0048  -0.0053 346 PHE A O   
2141 C CB  . PHE A 272 ? 0.1557 0.1618 0.1351 -0.0025 0.0069  -0.0045 346 PHE A CB  
2142 C CG  . PHE A 272 ? 0.1562 0.1634 0.1394 -0.0022 0.0065  -0.0043 346 PHE A CG  
2143 C CD1 . PHE A 272 ? 0.1626 0.1701 0.1485 -0.0014 0.0067  -0.0054 346 PHE A CD1 
2144 C CD2 . PHE A 272 ? 0.1659 0.1737 0.1500 -0.0025 0.0059  -0.0032 346 PHE A CD2 
2145 C CE1 . PHE A 272 ? 0.1631 0.1715 0.1522 -0.0010 0.0060  -0.0054 346 PHE A CE1 
2146 C CE2 . PHE A 272 ? 0.1714 0.1800 0.1587 -0.0021 0.0054  -0.0032 346 PHE A CE2 
2147 C CZ  . PHE A 272 ? 0.1695 0.1782 0.1591 -0.0014 0.0054  -0.0044 346 PHE A CZ  
2148 N N   . ILE A 273 ? 0.1679 0.1706 0.1409 -0.0022 0.0071  -0.0066 347 ILE A N   
2149 C CA  . ILE A 273 ? 0.1724 0.1732 0.1415 -0.0023 0.0073  -0.0074 347 ILE A CA  
2150 C C   . ILE A 273 ? 0.1751 0.1753 0.1407 -0.0028 0.0076  -0.0067 347 ILE A C   
2151 O O   . ILE A 273 ? 0.1774 0.1757 0.1393 -0.0030 0.0071  -0.0074 347 ILE A O   
2152 C CB  . ILE A 273 ? 0.1929 0.1933 0.1626 -0.0013 0.0088  -0.0086 347 ILE A CB  
2153 C CG1 . ILE A 273 ? 0.1922 0.1939 0.1639 -0.0008 0.0107  -0.0080 347 ILE A CG1 
2154 C CG2 . ILE A 273 ? 0.1936 0.1941 0.1658 -0.0007 0.0081  -0.0094 347 ILE A CG2 
2155 C CD1 . ILE A 273 ? 0.2123 0.2137 0.1846 0.0001  0.0123  -0.0090 347 ILE A CD1 
2156 N N   . ASP A 274 ? 0.1643 0.1658 0.1310 -0.0030 0.0082  -0.0055 348 ASP A N   
2157 C CA  . ASP A 274 ? 0.1685 0.1694 0.1318 -0.0034 0.0083  -0.0046 348 ASP A CA  
2158 C C   . ASP A 274 ? 0.1603 0.1614 0.1226 -0.0043 0.0062  -0.0038 348 ASP A C   
2159 O O   . ASP A 274 ? 0.1831 0.1837 0.1423 -0.0047 0.0059  -0.0031 348 ASP A O   
2160 C CB  . ASP A 274 ? 0.1813 0.1835 0.1461 -0.0031 0.0100  -0.0034 348 ASP A CB  
2161 C CG  . ASP A 274 ? 0.2061 0.2102 0.1755 -0.0032 0.0098  -0.0025 348 ASP A CG  
2162 O OD1 . ASP A 274 ? 0.1944 0.1990 0.1658 -0.0035 0.0084  -0.0027 348 ASP A OD1 
2163 O OD2 . ASP A 274 ? 0.2360 0.2411 0.2070 -0.0030 0.0114  -0.0015 348 ASP A OD2 
2164 N N   . LYS A 275 ? 0.1548 0.1565 0.1197 -0.0046 0.0050  -0.0038 349 LYS A N   
2165 C CA  . LYS A 275 ? 0.1610 0.1632 0.1261 -0.0054 0.0031  -0.0030 349 LYS A CA  
2166 C C   . LYS A 275 ? 0.1587 0.1626 0.1262 -0.0055 0.0032  -0.0014 349 LYS A C   
2167 O O   . LYS A 275 ? 0.1569 0.1614 0.1250 -0.0060 0.0018  -0.0006 349 LYS A O   
2168 C CB  . LYS A 275 ? 0.1819 0.1828 0.1431 -0.0061 0.0018  -0.0030 349 LYS A CB  
2169 C CG  . LYS A 275 ? 0.2312 0.2299 0.1897 -0.0060 0.0017  -0.0047 349 LYS A CG  
2170 C CD  . LYS A 275 ? 0.2237 0.2221 0.1844 -0.0058 0.0014  -0.0056 349 LYS A CD  
2171 C CE  . LYS A 275 ? 0.3201 0.3161 0.2778 -0.0056 0.0015  -0.0072 349 LYS A CE  
2172 N NZ  . LYS A 275 ? 0.3722 0.3668 0.3268 -0.0065 0.0000  -0.0074 349 LYS A NZ  
2173 N N   . SER A 276 ? 0.1505 0.1553 0.1197 -0.0050 0.0047  -0.0011 350 SER A N   
2174 C CA  . SER A 276 ? 0.1522 0.1584 0.1243 -0.0050 0.0048  0.0001  350 SER A CA  
2175 C C   . SER A 276 ? 0.1428 0.1496 0.1180 -0.0048 0.0039  -0.0001 350 SER A C   
2176 O O   . SER A 276 ? 0.1501 0.1566 0.1263 -0.0043 0.0041  -0.0013 350 SER A O   
2177 C CB  . SER A 276 ? 0.1440 0.1509 0.1176 -0.0046 0.0066  0.0005  350 SER A CB  
2178 O OG  . SER A 276 ? 0.1664 0.1744 0.1421 -0.0047 0.0066  0.0019  350 SER A OG  
2179 N N   . VAL A 277 ? 0.1390 0.1467 0.1156 -0.0050 0.0031  0.0010  351 VAL A N   
2180 C CA  . VAL A 277 ? 0.1306 0.1387 0.1098 -0.0047 0.0025  0.0008  351 VAL A CA  
2181 C C   . VAL A 277 ? 0.1372 0.1462 0.1192 -0.0043 0.0030  0.0015  351 VAL A C   
2182 O O   . VAL A 277 ? 0.1498 0.1593 0.1317 -0.0046 0.0033  0.0028  351 VAL A O   
2183 C CB  . VAL A 277 ? 0.1351 0.1432 0.1135 -0.0051 0.0010  0.0015  351 VAL A CB  
2184 C CG1 . VAL A 277 ? 0.1466 0.1549 0.1274 -0.0045 0.0006  0.0016  351 VAL A CG1 
2185 C CG2 . VAL A 277 ? 0.1414 0.1484 0.1173 -0.0055 0.0004  0.0007  351 VAL A CG2 
2186 N N   . ILE A 278 ? 0.1292 0.1383 0.1136 -0.0036 0.0031  0.0007  352 ILE A N   
2187 C CA  . ILE A 278 ? 0.1321 0.1417 0.1192 -0.0032 0.0033  0.0011  352 ILE A CA  
2188 C C   . ILE A 278 ? 0.1352 0.1447 0.1233 -0.0027 0.0023  0.0011  352 ILE A C   
2189 O O   . ILE A 278 ? 0.1447 0.1535 0.1321 -0.0023 0.0018  0.0002  352 ILE A O   
2190 C CB  . ILE A 278 ? 0.1365 0.1463 0.1259 -0.0029 0.0043  0.0001  352 ILE A CB  
2191 C CG1 . ILE A 278 ? 0.1492 0.1592 0.1376 -0.0033 0.0056  0.0003  352 ILE A CG1 
2192 C CG2 . ILE A 278 ? 0.1426 0.1528 0.1351 -0.0026 0.0043  0.0004  352 ILE A CG2 
2193 C CD1 . ILE A 278 ? 0.1684 0.1788 0.1566 -0.0037 0.0063  0.0019  352 ILE A CD1 
2194 N N   . SER A 279 ? 0.1322 0.1419 0.1215 -0.0025 0.0021  0.0021  353 SER A N   
2195 C CA  . SER A 279 ? 0.1406 0.1500 0.1305 -0.0018 0.0014  0.0022  353 SER A CA  
2196 C C   . SER A 279 ? 0.1327 0.1421 0.1249 -0.0012 0.0015  0.0022  353 SER A C   
2197 O O   . SER A 279 ? 0.1395 0.1492 0.1329 -0.0016 0.0021  0.0027  353 SER A O   
2198 C CB  . SER A 279 ? 0.1721 0.1818 0.1609 -0.0021 0.0009  0.0036  353 SER A CB  
2199 O OG  . SER A 279 ? 0.2489 0.2593 0.2383 -0.0024 0.0011  0.0051  353 SER A OG  
2200 N N   . GLN A 280 ? 0.1309 0.1395 0.1236 -0.0002 0.0009  0.0017  354 GLN A N   
2201 C CA  . GLN A 280 ? 0.1366 0.1448 0.1310 0.0004  0.0008  0.0017  354 GLN A CA  
2202 C C   . GLN A 280 ? 0.1353 0.1432 0.1291 0.0009  0.0005  0.0029  354 GLN A C   
2203 O O   . GLN A 280 ? 0.1432 0.1510 0.1357 0.0012  0.0002  0.0032  354 GLN A O   
2204 C CB  . GLN A 280 ? 0.1474 0.1547 0.1428 0.0013  0.0002  0.0000  354 GLN A CB  
2205 C CG  . GLN A 280 ? 0.1521 0.1588 0.1493 0.0021  0.0000  -0.0004 354 GLN A CG  
2206 C CD  . GLN A 280 ? 0.1858 0.1912 0.1818 0.0033  -0.0006 -0.0003 354 GLN A CD  
2207 O OE1 . GLN A 280 ? 0.2078 0.2129 0.2021 0.0039  -0.0009 -0.0004 354 GLN A OE1 
2208 N NE2 . GLN A 280 ? 0.1886 0.1933 0.1858 0.0039  -0.0008 -0.0002 354 GLN A NE2 
2209 N N   . MET A 281 ? 0.1284 0.1362 0.1234 0.0010  0.0007  0.0037  355 MET A N   
2210 C CA  . MET A 281 ? 0.1489 0.1567 0.1436 0.0015  0.0007  0.0052  355 MET A CA  
2211 C C   . MET A 281 ? 0.1453 0.1520 0.1413 0.0024  0.0007  0.0049  355 MET A C   
2212 O O   . MET A 281 ? 0.1510 0.1575 0.1486 0.0022  0.0008  0.0044  355 MET A O   
2213 C CB  . MET A 281 ? 0.1844 0.1933 0.1791 0.0004  0.0012  0.0070  355 MET A CB  
2214 C CG  . MET A 281 ? 0.2142 0.2241 0.2075 -0.0005 0.0012  0.0072  355 MET A CG  
2215 S SD  . MET A 281 ? 0.3034 0.3144 0.2963 -0.0017 0.0016  0.0089  355 MET A SD  
2216 C CE  . MET A 281 ? 0.2283 0.2395 0.2215 -0.0010 0.0012  0.0104  355 MET A CE  
2217 N N   . TYR A 282 ? 0.1459 0.1518 0.1411 0.0035  0.0005  0.0055  356 TYR A N   
2218 C CA  . TYR A 282 ? 0.1565 0.1610 0.1523 0.0046  0.0005  0.0055  356 TYR A CA  
2219 C C   . TYR A 282 ? 0.1675 0.1716 0.1620 0.0058  0.0007  0.0066  356 TYR A C   
2220 O O   . TYR A 282 ? 0.1792 0.1839 0.1727 0.0057  0.0007  0.0071  356 TYR A O   
2221 C CB  . TYR A 282 ? 0.1556 0.1587 0.1520 0.0054  -0.0001 0.0034  356 TYR A CB  
2222 C CG  . TYR A 282 ? 0.1519 0.1534 0.1490 0.0063  -0.0002 0.0033  356 TYR A CG  
2223 C CD1 . TYR A 282 ? 0.1611 0.1629 0.1600 0.0056  0.0002  0.0042  356 TYR A CD1 
2224 C CD2 . TYR A 282 ? 0.1614 0.1611 0.1572 0.0080  -0.0007 0.0024  356 TYR A CD2 
2225 C CE1 . TYR A 282 ? 0.1639 0.1640 0.1633 0.0065  0.0002  0.0042  356 TYR A CE1 
2226 C CE2 . TYR A 282 ? 0.1762 0.1741 0.1722 0.0090  -0.0008 0.0024  356 TYR A CE2 
2227 C CZ  . TYR A 282 ? 0.1659 0.1641 0.1638 0.0081  -0.0004 0.0032  356 TYR A CZ  
2228 O OH  . TYR A 282 ? 0.1803 0.1766 0.1784 0.0091  -0.0004 0.0032  356 TYR A OH  
2229 N N   . TYR A 283 ? 0.1549 0.1577 0.1495 0.0070  0.0009  0.0070  357 TYR A N   
2230 C CA  . TYR A 283 ? 0.1721 0.1742 0.1654 0.0084  0.0012  0.0078  357 TYR A CA  
2231 C C   . TYR A 283 ? 0.1901 0.1912 0.1818 0.0094  0.0007  0.0064  357 TYR A C   
2232 O O   . TYR A 283 ? 0.2005 0.2010 0.1922 0.0093  0.0000  0.0046  357 TYR A O   
2233 C CB  . TYR A 283 ? 0.1706 0.1710 0.1640 0.0097  0.0014  0.0081  357 TYR A CB  
2234 C CG  . TYR A 283 ? 0.1541 0.1554 0.1491 0.0089  0.0020  0.0097  357 TYR A CG  
2235 C CD1 . TYR A 283 ? 0.1675 0.1707 0.1630 0.0083  0.0025  0.0118  357 TYR A CD1 
2236 C CD2 . TYR A 283 ? 0.1619 0.1623 0.1582 0.0087  0.0018  0.0090  357 TYR A CD2 
2237 C CE1 . TYR A 283 ? 0.1596 0.1635 0.1564 0.0076  0.0029  0.0133  357 TYR A CE1 
2238 C CE2 . TYR A 283 ? 0.1710 0.1721 0.1687 0.0080  0.0024  0.0105  357 TYR A CE2 
2239 C CZ  . TYR A 283 ? 0.1640 0.1668 0.1617 0.0075  0.0030  0.0127  357 TYR A CZ  
2240 O OH  . TYR A 283 ? 0.1902 0.1938 0.1893 0.0069  0.0035  0.0142  357 TYR A OH  
2241 N N   . PRO A 284 ? 0.2016 0.2024 0.1920 0.0105  0.0012  0.0073  358 PRO A N   
2242 C CA  . PRO A 284 ? 0.2186 0.2181 0.2071 0.0117  0.0009  0.0062  358 PRO A CA  
2243 C C   . PRO A 284 ? 0.2655 0.2627 0.2529 0.0133  0.0003  0.0045  358 PRO A C   
2244 O O   . PRO A 284 ? 0.3111 0.3072 0.2984 0.0143  0.0006  0.0050  358 PRO A O   
2245 C CB  . PRO A 284 ? 0.2496 0.2494 0.2375 0.0125  0.0018  0.0080  358 PRO A CB  
2246 C CG  . PRO A 284 ? 0.2382 0.2393 0.2276 0.0119  0.0024  0.0099  358 PRO A CG  
2247 C CD  . PRO A 284 ? 0.2118 0.2136 0.2026 0.0105  0.0020  0.0096  358 PRO A CD  
2248 N N   . ASP A 285 ? 0.2535 0.2500 0.2406 0.0133  -0.0006 0.0025  359 ASP A N   
2249 C CA  . ASP A 285 ? 0.3114 0.3057 0.2980 0.0145  -0.0016 0.0006  359 ASP A CA  
2250 C C   . ASP A 285 ? 0.2915 0.2858 0.2777 0.0145  -0.0026 -0.0011 359 ASP A C   
2251 O O   . ASP A 285 ? 0.3047 0.3007 0.2916 0.0132  -0.0024 -0.0009 359 ASP A O   
2252 C CB  . ASP A 285 ? 0.3988 0.3929 0.3873 0.0139  -0.0017 0.0006  359 ASP A CB  
2253 C CG  . ASP A 285 ? 0.4499 0.4414 0.4380 0.0152  -0.0027 -0.0009 359 ASP A CG  
2254 O OD1 . ASP A 285 ? 0.4227 0.4137 0.4120 0.0149  -0.0024 -0.0003 359 ASP A OD1 
2255 O OD2 . ASP A 285 ? 0.3728 0.3626 0.3596 0.0164  -0.0039 -0.0028 359 ASP A OD2 
2256 N N   . MET A 286 ? 0.2207 0.2128 0.2054 0.0161  -0.0036 -0.0027 360 MET A N   
2257 C CA  . MET A 286 ? 0.2013 0.1933 0.1861 0.0162  -0.0049 -0.0047 360 MET A CA  
2258 C C   . MET A 286 ? 0.1922 0.1837 0.1791 0.0158  -0.0062 -0.0065 360 MET A C   
2259 O O   . MET A 286 ? 0.1991 0.1908 0.1868 0.0157  -0.0074 -0.0081 360 MET A O   
2260 C CB  . MET A 286 ? 0.2063 0.1964 0.1878 0.0185  -0.0053 -0.0054 360 MET A CB  
2261 C CG  . MET A 286 ? 0.2300 0.2209 0.2101 0.0185  -0.0041 -0.0039 360 MET A CG  
2262 S SD  . MET A 286 ? 0.2154 0.2086 0.1975 0.0165  -0.0042 -0.0043 360 MET A SD  
2263 C CE  . MET A 286 ? 0.2416 0.2337 0.2232 0.0176  -0.0060 -0.0069 360 MET A CE  
2264 N N   . GLN A 287 ? 0.2044 0.1954 0.1926 0.0154  -0.0061 -0.0061 361 GLN A N   
2265 C CA  . GLN A 287 ? 0.2017 0.1921 0.1922 0.0150  -0.0074 -0.0077 361 GLN A CA  
2266 C C   . GLN A 287 ? 0.1843 0.1771 0.1783 0.0129  -0.0073 -0.0080 361 GLN A C   
2267 O O   . GLN A 287 ? 0.1859 0.1786 0.1817 0.0127  -0.0086 -0.0097 361 GLN A O   
2268 C CB  . GLN A 287 ? 0.2440 0.2331 0.2351 0.0151  -0.0072 -0.0073 361 GLN A CB  
2269 C CG  . GLN A 287 ? 0.3130 0.2992 0.3006 0.0175  -0.0074 -0.0076 361 GLN A CG  
2270 C CD  . GLN A 287 ? 0.3315 0.3163 0.3198 0.0177  -0.0071 -0.0071 361 GLN A CD  
2271 O OE1 . GLN A 287 ? 0.4156 0.4013 0.4044 0.0171  -0.0056 -0.0051 361 GLN A OE1 
2272 N NE2 . GLN A 287 ? 0.3685 0.3513 0.3574 0.0181  -0.0087 -0.0091 361 GLN A NE2 
2273 N N   . ILE A 288 ? 0.1697 0.1646 0.1647 0.0114  -0.0059 -0.0063 362 ILE A N   
2274 C CA  . ILE A 288 ? 0.1706 0.1675 0.1685 0.0096  -0.0057 -0.0065 362 ILE A CA  
2275 C C   . ILE A 288 ? 0.1519 0.1495 0.1494 0.0098  -0.0063 -0.0077 362 ILE A C   
2276 O O   . ILE A 288 ? 0.1773 0.1755 0.1773 0.0092  -0.0070 -0.0089 362 ILE A O   
2277 C CB  . ILE A 288 ? 0.1901 0.1890 0.1889 0.0080  -0.0041 -0.0045 362 ILE A CB  
2278 C CG1 . ILE A 288 ? 0.2166 0.2149 0.2166 0.0077  -0.0037 -0.0035 362 ILE A CG1 
2279 C CG2 . ILE A 288 ? 0.2194 0.2201 0.2203 0.0065  -0.0038 -0.0048 362 ILE A CG2 
2280 C CD1 . ILE A 288 ? 0.2309 0.2308 0.2315 0.0063  -0.0023 -0.0015 362 ILE A CD1 
2281 N N   . PRO A 289 ? 0.1588 0.1562 0.1534 0.0106  -0.0060 -0.0072 363 PRO A N   
2282 C CA  . PRO A 289 ? 0.1674 0.1652 0.1617 0.0109  -0.0066 -0.0084 363 PRO A CA  
2283 C C   . PRO A 289 ? 0.1702 0.1667 0.1650 0.0121  -0.0084 -0.0105 363 PRO A C   
2284 O O   . PRO A 289 ? 0.1739 0.1713 0.1705 0.0117  -0.0090 -0.0117 363 PRO A O   
2285 C CB  . PRO A 289 ? 0.1914 0.1887 0.1824 0.0119  -0.0060 -0.0074 363 PRO A CB  
2286 C CG  . PRO A 289 ? 0.1833 0.1812 0.1741 0.0111  -0.0047 -0.0054 363 PRO A CG  
2287 C CD  . PRO A 289 ? 0.1576 0.1550 0.1500 0.0109  -0.0049 -0.0054 363 PRO A CD  
2288 N N   . ILE A 290 ? 0.1697 0.1641 0.1627 0.0137  -0.0092 -0.0110 364 ILE A N   
2289 C CA  . ILE A 290 ? 0.1782 0.1711 0.1714 0.0149  -0.0112 -0.0131 364 ILE A CA  
2290 C C   . ILE A 290 ? 0.1904 0.1842 0.1880 0.0135  -0.0120 -0.0142 364 ILE A C   
2291 O O   . ILE A 290 ? 0.1957 0.1901 0.1954 0.0134  -0.0132 -0.0156 364 ILE A O   
2292 C CB  . ILE A 290 ? 0.1900 0.1800 0.1798 0.0170  -0.0119 -0.0135 364 ILE A CB  
2293 C CG1 . ILE A 290 ? 0.1859 0.1751 0.1716 0.0185  -0.0111 -0.0126 364 ILE A CG1 
2294 C CG2 . ILE A 290 ? 0.2208 0.2092 0.2111 0.0181  -0.0143 -0.0159 364 ILE A CG2 
2295 C CD1 . ILE A 290 ? 0.2108 0.1974 0.1931 0.0205  -0.0110 -0.0123 364 ILE A CD1 
2296 N N   . LEU A 291 ? 0.1843 0.1783 0.1837 0.0124  -0.0112 -0.0132 365 LEU A N   
2297 C CA  . LEU A 291 ? 0.1979 0.1925 0.2016 0.0112  -0.0118 -0.0140 365 LEU A CA  
2298 C C   . LEU A 291 ? 0.1932 0.1904 0.2001 0.0096  -0.0112 -0.0139 365 LEU A C   
2299 O O   . LEU A 291 ? 0.2024 0.2002 0.2127 0.0092  -0.0123 -0.0153 365 LEU A O   
2300 C CB  . LEU A 291 ? 0.2239 0.2182 0.2288 0.0103  -0.0107 -0.0127 365 LEU A CB  
2301 C CG  . LEU A 291 ? 0.2335 0.2284 0.2433 0.0089  -0.0111 -0.0133 365 LEU A CG  
2302 C CD1 . LEU A 291 ? 0.2471 0.2403 0.2581 0.0097  -0.0135 -0.0156 365 LEU A CD1 
2303 C CD2 . LEU A 291 ? 0.2517 0.2463 0.2622 0.0081  -0.0098 -0.0117 365 LEU A CD2 
2304 N N   . TYR A 292 ? 0.1777 0.1765 0.1837 0.0088  -0.0094 -0.0123 366 TYR A N   
2305 C CA  . TYR A 292 ? 0.1880 0.1890 0.1965 0.0075  -0.0086 -0.0122 366 TYR A CA  
2306 C C   . TYR A 292 ? 0.1884 0.1897 0.1972 0.0083  -0.0098 -0.0138 366 TYR A C   
2307 O O   . TYR A 292 ? 0.1958 0.1985 0.2080 0.0075  -0.0098 -0.0144 366 TYR A O   
2308 C CB  . TYR A 292 ? 0.1916 0.1938 0.1982 0.0066  -0.0067 -0.0104 366 TYR A CB  
2309 C CG  . TYR A 292 ? 0.1850 0.1892 0.1939 0.0052  -0.0056 -0.0100 366 TYR A CG  
2310 C CD1 . TYR A 292 ? 0.2077 0.2130 0.2200 0.0039  -0.0047 -0.0095 366 TYR A CD1 
2311 C CD2 . TYR A 292 ? 0.2047 0.2097 0.2125 0.0053  -0.0052 -0.0103 366 TYR A CD2 
2312 C CE1 . TYR A 292 ? 0.2190 0.2260 0.2332 0.0029  -0.0035 -0.0091 366 TYR A CE1 
2313 C CE2 . TYR A 292 ? 0.1905 0.1972 0.2001 0.0042  -0.0041 -0.0100 366 TYR A CE2 
2314 C CZ  . TYR A 292 ? 0.2052 0.2129 0.2179 0.0030  -0.0031 -0.0094 366 TYR A CZ  
2315 O OH  . TYR A 292 ? 0.2300 0.2392 0.2443 0.0021  -0.0018 -0.0090 366 TYR A OH  
2316 N N   . SER A 293 ? 0.1864 0.1862 0.1916 0.0099  -0.0107 -0.0143 367 SER A N   
2317 C CA  . SER A 293 ? 0.1892 0.1892 0.1945 0.0108  -0.0119 -0.0158 367 SER A CA  
2318 C C   . SER A 293 ? 0.2001 0.1999 0.2089 0.0110  -0.0139 -0.0176 367 SER A C   
2319 O O   . SER A 293 ? 0.2119 0.2128 0.2228 0.0112  -0.0147 -0.0187 367 SER A O   
2320 C CB  . SER A 293 ? 0.1987 0.1969 0.1995 0.0128  -0.0125 -0.0160 367 SER A CB  
2321 O OG  . SER A 293 ? 0.1954 0.1914 0.1943 0.0143  -0.0139 -0.0169 367 SER A OG  
2322 N N   . LEU A 294 ? 0.1984 0.1968 0.2078 0.0112  -0.0147 -0.0180 368 LEU A N   
2323 C CA  . LEU A 294 ? 0.2086 0.2066 0.2215 0.0113  -0.0168 -0.0199 368 LEU A CA  
2324 C C   . LEU A 294 ? 0.2253 0.2251 0.2438 0.0093  -0.0161 -0.0195 368 LEU A C   
2325 O O   . LEU A 294 ? 0.2418 0.2419 0.2644 0.0091  -0.0178 -0.0210 368 LEU A O   
2326 C CB  . LEU A 294 ? 0.2216 0.2168 0.2320 0.0126  -0.0182 -0.0206 368 LEU A CB  
2327 C CG  . LEU A 294 ? 0.2446 0.2376 0.2494 0.0149  -0.0191 -0.0211 368 LEU A CG  
2328 C CD1 . LEU A 294 ? 0.2675 0.2576 0.2694 0.0163  -0.0200 -0.0216 368 LEU A CD1 
2329 C CD2 . LEU A 294 ? 0.2610 0.2543 0.2660 0.0160  -0.0209 -0.0227 368 LEU A CD2 
2330 N N   . THR A 295 ? 0.2152 0.2162 0.2343 0.0078  -0.0138 -0.0177 369 THR A N   
2331 C CA  . THR A 295 ? 0.2165 0.2191 0.2408 0.0061  -0.0129 -0.0171 369 THR A CA  
2332 C C   . THR A 295 ? 0.2186 0.2237 0.2448 0.0051  -0.0112 -0.0163 369 THR A C   
2333 O O   . THR A 295 ? 0.2137 0.2203 0.2446 0.0039  -0.0106 -0.0162 369 THR A O   
2334 C CB  . THR A 295 ? 0.2409 0.2429 0.2650 0.0052  -0.0114 -0.0155 369 THR A CB  
2335 O OG1 . THR A 295 ? 0.2237 0.2262 0.2443 0.0050  -0.0095 -0.0137 369 THR A OG1 
2336 C CG2 . THR A 295 ? 0.2676 0.2669 0.2903 0.0061  -0.0130 -0.0164 369 THR A CG2 
2337 N N   . TRP A 296 ? 0.1992 0.2046 0.2216 0.0055  -0.0103 -0.0157 370 TRP A N   
2338 C CA  . TRP A 296 ? 0.1943 0.2018 0.2178 0.0047  -0.0086 -0.0150 370 TRP A CA  
2339 C C   . TRP A 296 ? 0.2154 0.2244 0.2439 0.0045  -0.0094 -0.0162 370 TRP A C   
2340 O O   . TRP A 296 ? 0.2287 0.2371 0.2577 0.0056  -0.0115 -0.0178 370 TRP A O   
2341 C CB  . TRP A 296 ? 0.1981 0.2053 0.2170 0.0057  -0.0084 -0.0149 370 TRP A CB  
2342 C CG  . TRP A 296 ? 0.1915 0.2004 0.2112 0.0051  -0.0069 -0.0144 370 TRP A CG  
2343 C CD1 . TRP A 296 ? 0.2078 0.2175 0.2262 0.0041  -0.0048 -0.0129 370 TRP A CD1 
2344 C CD2 . TRP A 296 ? 0.2018 0.2119 0.2239 0.0055  -0.0073 -0.0155 370 TRP A CD2 
2345 N NE1 . TRP A 296 ? 0.2226 0.2337 0.2424 0.0038  -0.0038 -0.0131 370 TRP A NE1 
2346 C CE2 . TRP A 296 ? 0.2123 0.2237 0.2344 0.0047  -0.0053 -0.0146 370 TRP A CE2 
2347 C CE3 . TRP A 296 ? 0.2203 0.2304 0.2445 0.0065  -0.0094 -0.0172 370 TRP A CE3 
2348 C CZ2 . TRP A 296 ? 0.2242 0.2369 0.2485 0.0049  -0.0050 -0.0152 370 TRP A CZ2 
2349 C CZ3 . TRP A 296 ? 0.2264 0.2380 0.2531 0.0066  -0.0092 -0.0178 370 TRP A CZ3 
2350 C CH2 . TRP A 296 ? 0.2285 0.2414 0.2554 0.0058  -0.0070 -0.0168 370 TRP A CH2 
2351 N N   . PRO A 297 ? 0.2064 0.2173 0.2385 0.0033  -0.0076 -0.0154 371 PRO A N   
2352 C CA  . PRO A 297 ? 0.2171 0.2288 0.2481 0.0022  -0.0050 -0.0135 371 PRO A CA  
2353 C C   . PRO A 297 ? 0.2247 0.2361 0.2571 0.0011  -0.0040 -0.0122 371 PRO A C   
2354 O O   . PRO A 297 ? 0.2642 0.2763 0.2961 0.0002  -0.0019 -0.0106 371 PRO A O   
2355 C CB  . PRO A 297 ? 0.2582 0.2719 0.2925 0.0017  -0.0038 -0.0134 371 PRO A CB  
2356 C CG  . PRO A 297 ? 0.2639 0.2782 0.3036 0.0018  -0.0055 -0.0148 371 PRO A CG  
2357 C CD  . PRO A 297 ? 0.2251 0.2377 0.2625 0.0031  -0.0082 -0.0164 371 PRO A CD  
2358 N N   . ASP A 298 ? 0.2151 0.2252 0.2487 0.0013  -0.0056 -0.0129 372 ASP A N   
2359 C CA  . ASP A 298 ? 0.2179 0.2274 0.2527 0.0004  -0.0048 -0.0117 372 ASP A CA  
2360 C C   . ASP A 298 ? 0.2154 0.2231 0.2455 0.0010  -0.0050 -0.0111 372 ASP A C   
2361 O O   . ASP A 298 ? 0.2157 0.2223 0.2419 0.0022  -0.0061 -0.0118 372 ASP A O   
2362 C CB  . ASP A 298 ? 0.2535 0.2628 0.2937 0.0000  -0.0062 -0.0129 372 ASP A CB  
2363 C CG  . ASP A 298 ? 0.3441 0.3555 0.3898 -0.0006 -0.0056 -0.0131 372 ASP A CG  
2364 O OD1 . ASP A 298 ? 0.3837 0.3967 0.4300 -0.0014 -0.0032 -0.0117 372 ASP A OD1 
2365 O OD2 . ASP A 298 ? 0.4694 0.4808 0.5189 -0.0005 -0.0076 -0.0147 372 ASP A OD2 
2366 N N   . ARG A 299 ? 0.1889 0.1960 0.2196 0.0003  -0.0041 -0.0099 373 ARG A N   
2367 C CA  . ARG A 299 ? 0.1893 0.1946 0.2168 0.0009  -0.0045 -0.0094 373 ARG A CA  
2368 C C   . ARG A 299 ? 0.2018 0.2058 0.2324 0.0006  -0.0053 -0.0098 373 ARG A C   
2369 O O   . ARG A 299 ? 0.2263 0.2312 0.2617 -0.0004 -0.0047 -0.0096 373 ARG A O   
2370 C CB  . ARG A 299 ? 0.1844 0.1901 0.2091 0.0003  -0.0025 -0.0072 373 ARG A CB  
2371 C CG  . ARG A 299 ? 0.1813 0.1879 0.2023 0.0006  -0.0018 -0.0067 373 ARG A CG  
2372 C CD  . ARG A 299 ? 0.1812 0.1883 0.1997 0.0000  -0.0001 -0.0046 373 ARG A CD  
2373 N NE  . ARG A 299 ? 0.1797 0.1875 0.1950 0.0001  0.0003  -0.0042 373 ARG A NE  
2374 C CZ  . ARG A 299 ? 0.1814 0.1886 0.1932 0.0009  -0.0003 -0.0044 373 ARG A CZ  
2375 N NH1 . ARG A 299 ? 0.1801 0.1858 0.1908 0.0019  -0.0015 -0.0050 373 ARG A NH1 
2376 N NH2 . ARG A 299 ? 0.1934 0.2012 0.2027 0.0008  0.0001  -0.0041 373 ARG A NH2 
2377 N N   . ILE A 300 ? 0.1811 0.1829 0.2094 0.0016  -0.0065 -0.0103 374 ILE A N   
2378 C CA  . ILE A 300 ? 0.1955 0.1955 0.2263 0.0014  -0.0073 -0.0108 374 ILE A CA  
2379 C C   . ILE A 300 ? 0.1816 0.1804 0.2096 0.0017  -0.0063 -0.0092 374 ILE A C   
2380 O O   . ILE A 300 ? 0.1911 0.1897 0.2146 0.0024  -0.0058 -0.0083 374 ILE A O   
2381 C CB  . ILE A 300 ? 0.2094 0.2077 0.2405 0.0026  -0.0101 -0.0133 374 ILE A CB  
2382 C CG1 . ILE A 300 ? 0.2207 0.2170 0.2461 0.0044  -0.0111 -0.0138 374 ILE A CG1 
2383 C CG2 . ILE A 300 ? 0.2240 0.2238 0.2581 0.0024  -0.0112 -0.0148 374 ILE A CG2 
2384 C CD1 . ILE A 300 ? 0.2506 0.2446 0.2754 0.0058  -0.0139 -0.0162 374 ILE A CD1 
2385 N N   . LYS A 301 ? 0.1880 0.1855 0.2185 0.0012  -0.0063 -0.0090 375 LYS A N   
2386 C CA  . LYS A 301 ? 0.1941 0.1902 0.2224 0.0015  -0.0055 -0.0075 375 LYS A CA  
2387 C C   . LYS A 301 ? 0.2202 0.2140 0.2442 0.0033  -0.0068 -0.0084 375 LYS A C   
2388 O O   . LYS A 301 ? 0.2363 0.2285 0.2601 0.0043  -0.0088 -0.0106 375 LYS A O   
2389 C CB  . LYS A 301 ? 0.2290 0.2239 0.2613 0.0006  -0.0053 -0.0073 375 LYS A CB  
2390 C CG  . LYS A 301 ? 0.2844 0.2779 0.3149 0.0009  -0.0042 -0.0056 375 LYS A CG  
2391 C CD  . LYS A 301 ? 0.3730 0.3653 0.4077 0.0000  -0.0037 -0.0052 375 LYS A CD  
2392 C CE  . LYS A 301 ? 0.4630 0.4537 0.4954 0.0005  -0.0027 -0.0036 375 LYS A CE  
2393 N NZ  . LYS A 301 ? 0.5504 0.5392 0.5863 0.0000  -0.0027 -0.0035 375 LYS A NZ  
2394 N N   . THR A 302 ? 0.1950 0.1887 0.2152 0.0039  -0.0056 -0.0068 376 THR A N   
2395 C CA  . THR A 302 ? 0.1972 0.1886 0.2136 0.0056  -0.0064 -0.0071 376 THR A CA  
2396 C C   . THR A 302 ? 0.1939 0.1845 0.2096 0.0057  -0.0050 -0.0052 376 THR A C   
2397 O O   . THR A 302 ? 0.2249 0.2169 0.2425 0.0044  -0.0035 -0.0035 376 THR A O   
2398 C CB  . THR A 302 ? 0.1976 0.1896 0.2098 0.0067  -0.0063 -0.0070 376 THR A CB  
2399 O OG1 . THR A 302 ? 0.1898 0.1836 0.2008 0.0061  -0.0045 -0.0046 376 THR A OG1 
2400 C CG2 . THR A 302 ? 0.1967 0.1899 0.2093 0.0067  -0.0073 -0.0084 376 THR A CG2 
2401 N N   . ASN A 303 ? 0.2144 0.2027 0.2271 0.0073  -0.0055 -0.0054 377 ASN A N   
2402 C CA  . ASN A 303 ? 0.2315 0.2189 0.2431 0.0076  -0.0042 -0.0035 377 ASN A CA  
2403 C C   . ASN A 303 ? 0.2278 0.2158 0.2354 0.0088  -0.0034 -0.0022 377 ASN A C   
2404 O O   . ASN A 303 ? 0.2316 0.2183 0.2373 0.0100  -0.0028 -0.0012 377 ASN A O   
2405 C CB  . ASN A 303 ? 0.2890 0.2732 0.3012 0.0084  -0.0050 -0.0045 377 ASN A CB  
2406 C CG  . ASN A 303 ? 0.3472 0.3314 0.3643 0.0069  -0.0052 -0.0050 377 ASN A CG  
2407 O OD1 . ASN A 303 ? 0.5275 0.5096 0.5462 0.0071  -0.0069 -0.0071 377 ASN A OD1 
2408 N ND2 . ASN A 303 ? 0.3825 0.3687 0.4020 0.0053  -0.0035 -0.0030 377 ASN A ND2 
2409 N N   . LEU A 304 ? 0.1903 0.1803 0.1967 0.0086  -0.0034 -0.0021 378 LEU A N   
2410 C CA  . LEU A 304 ? 0.1888 0.1797 0.1921 0.0094  -0.0026 -0.0008 378 LEU A CA  
2411 C C   . LEU A 304 ? 0.1736 0.1657 0.1771 0.0087  -0.0010 0.0017  378 LEU A C   
2412 O O   . LEU A 304 ? 0.1868 0.1801 0.1928 0.0073  -0.0003 0.0026  378 LEU A O   
2413 C CB  . LEU A 304 ? 0.2020 0.1947 0.2044 0.0090  -0.0028 -0.0013 378 LEU A CB  
2414 C CG  . LEU A 304 ? 0.2487 0.2401 0.2498 0.0101  -0.0044 -0.0036 378 LEU A CG  
2415 C CD1 . LEU A 304 ? 0.2480 0.2415 0.2488 0.0095  -0.0044 -0.0037 378 LEU A CD1 
2416 C CD2 . LEU A 304 ? 0.3014 0.2905 0.2990 0.0123  -0.0048 -0.0039 378 LEU A CD2 
2417 N N   . LYS A 305 ? 0.1757 0.1677 0.1767 0.0099  -0.0004 0.0030  379 LYS A N   
2418 C CA  . LYS A 305 ? 0.1773 0.1708 0.1784 0.0095  0.0009  0.0056  379 LYS A CA  
2419 C C   . LYS A 305 ? 0.1769 0.1733 0.1791 0.0077  0.0014  0.0065  379 LYS A C   
2420 O O   . LYS A 305 ? 0.1734 0.1709 0.1745 0.0074  0.0010  0.0060  379 LYS A O   
2421 C CB  . LYS A 305 ? 0.1869 0.1802 0.1853 0.0110  0.0013  0.0066  379 LYS A CB  
2422 C CG  . LYS A 305 ? 0.1849 0.1795 0.1834 0.0110  0.0025  0.0092  379 LYS A CG  
2423 C CD  . LYS A 305 ? 0.1832 0.1780 0.1796 0.0123  0.0030  0.0102  379 LYS A CD  
2424 C CE  . LYS A 305 ? 0.1992 0.1911 0.1937 0.0145  0.0028  0.0092  379 LYS A CE  
2425 N NZ  . LYS A 305 ? 0.2193 0.2114 0.2119 0.0159  0.0036  0.0104  379 LYS A NZ  
2426 N N   . PRO A 306 ? 0.1646 0.1621 0.1685 0.0065  0.0022  0.0080  380 PRO A N   
2427 C CA  . PRO A 306 ? 0.1667 0.1666 0.1711 0.0050  0.0026  0.0088  380 PRO A CA  
2428 C C   . PRO A 306 ? 0.1656 0.1671 0.1681 0.0050  0.0029  0.0103  380 PRO A C   
2429 O O   . PRO A 306 ? 0.1690 0.1706 0.1708 0.0058  0.0033  0.0119  380 PRO A O   
2430 C CB  . PRO A 306 ? 0.2046 0.2048 0.2109 0.0040  0.0035  0.0101  380 PRO A CB  
2431 C CG  . PRO A 306 ? 0.2425 0.2405 0.2496 0.0050  0.0036  0.0102  380 PRO A CG  
2432 C CD  . PRO A 306 ? 0.2005 0.1966 0.2059 0.0066  0.0027  0.0088  380 PRO A CD  
2433 N N   . LEU A 307 ? 0.1500 0.1531 0.1519 0.0041  0.0027  0.0100  381 LEU A N   
2434 C CA  . LEU A 307 ? 0.1479 0.1527 0.1484 0.0038  0.0029  0.0114  381 LEU A CA  
2435 C C   . LEU A 307 ? 0.1436 0.1496 0.1446 0.0031  0.0035  0.0136  381 LEU A C   
2436 O O   . LEU A 307 ? 0.1732 0.1793 0.1753 0.0023  0.0040  0.0139  381 LEU A O   
2437 C CB  . LEU A 307 ? 0.1532 0.1592 0.1530 0.0028  0.0025  0.0104  381 LEU A CB  
2438 C CG  . LEU A 307 ? 0.1572 0.1647 0.1555 0.0024  0.0024  0.0115  381 LEU A CG  
2439 C CD1 . LEU A 307 ? 0.1634 0.1705 0.1607 0.0035  0.0022  0.0118  381 LEU A CD1 
2440 C CD2 . LEU A 307 ? 0.1727 0.1810 0.1703 0.0014  0.0022  0.0104  381 LEU A CD2 
2441 N N   . ASP A 308 ? 0.1415 0.1484 0.1418 0.0035  0.0036  0.0152  382 ASP A N   
2442 C CA  . ASP A 308 ? 0.1523 0.1603 0.1530 0.0031  0.0041  0.0175  382 ASP A CA  
2443 C C   . ASP A 308 ? 0.1473 0.1572 0.1469 0.0026  0.0036  0.0185  382 ASP A C   
2444 O O   . ASP A 308 ? 0.1588 0.1691 0.1582 0.0032  0.0034  0.0190  382 ASP A O   
2445 C CB  . ASP A 308 ? 0.1589 0.1659 0.1603 0.0044  0.0045  0.0185  382 ASP A CB  
2446 C CG  . ASP A 308 ? 0.1852 0.1932 0.1872 0.0043  0.0050  0.0210  382 ASP A CG  
2447 O OD1 . ASP A 308 ? 0.1797 0.1896 0.1813 0.0034  0.0047  0.0221  382 ASP A OD1 
2448 O OD2 . ASP A 308 ? 0.2100 0.2168 0.2128 0.0053  0.0055  0.0217  382 ASP A OD2 
2449 N N   . LEU A 309 ? 0.1459 0.1571 0.1449 0.0013  0.0034  0.0187  383 LEU A N   
2450 C CA  . LEU A 309 ? 0.1575 0.1703 0.1554 0.0006  0.0027  0.0193  383 LEU A CA  
2451 C C   . LEU A 309 ? 0.1443 0.1584 0.1425 0.0008  0.0025  0.0216  383 LEU A C   
2452 O O   . LEU A 309 ? 0.1617 0.1768 0.1597 0.0007  0.0019  0.0220  383 LEU A O   
2453 C CB  . LEU A 309 ? 0.1741 0.1874 0.1707 -0.0005 0.0026  0.0188  383 LEU A CB  
2454 C CG  . LEU A 309 ? 0.1961 0.2086 0.1924 -0.0008 0.0027  0.0166  383 LEU A CG  
2455 C CD1 . LEU A 309 ? 0.2073 0.2204 0.2023 -0.0018 0.0028  0.0165  383 LEU A CD1 
2456 C CD2 . LEU A 309 ? 0.2168 0.2291 0.2126 -0.0005 0.0021  0.0154  383 LEU A CD2 
2457 N N   . ALA A 310 ? 0.1547 0.1688 0.1537 0.0010  0.0030  0.0230  384 ALA A N   
2458 C CA  . ALA A 310 ? 0.1690 0.1844 0.1687 0.0014  0.0028  0.0253  384 ALA A CA  
2459 C C   . ALA A 310 ? 0.1636 0.1787 0.1644 0.0026  0.0030  0.0256  384 ALA A C   
2460 O O   . ALA A 310 ? 0.1809 0.1975 0.1824 0.0028  0.0026  0.0271  384 ALA A O   
2461 C CB  . ALA A 310 ? 0.1875 0.2027 0.1878 0.0016  0.0034  0.0268  384 ALA A CB  
2462 N N   . GLN A 311 ? 0.1588 0.1720 0.1597 0.0036  0.0036  0.0243  385 GLN A N   
2463 C CA  . GLN A 311 ? 0.1612 0.1737 0.1626 0.0050  0.0040  0.0244  385 GLN A CA  
2464 C C   . GLN A 311 ? 0.1649 0.1782 0.1658 0.0048  0.0034  0.0239  385 GLN A C   
2465 O O   . GLN A 311 ? 0.1779 0.1919 0.1795 0.0055  0.0035  0.0252  385 GLN A O   
2466 C CB  . GLN A 311 ? 0.1641 0.1741 0.1653 0.0060  0.0045  0.0228  385 GLN A CB  
2467 C CG  . GLN A 311 ? 0.1831 0.1917 0.1842 0.0078  0.0050  0.0228  385 GLN A CG  
2468 C CD  . GLN A 311 ? 0.1804 0.1863 0.1807 0.0086  0.0051  0.0207  385 GLN A CD  
2469 O OE1 . GLN A 311 ? 0.2069 0.2116 0.2077 0.0084  0.0052  0.0200  385 GLN A OE1 
2470 N NE2 . GLN A 311 ? 0.1904 0.1954 0.1896 0.0097  0.0051  0.0197  385 GLN A NE2 
2471 N N   . VAL A 312 ? 0.1638 0.1768 0.1635 0.0039  0.0029  0.0221  386 VAL A N   
2472 C CA  . VAL A 312 ? 0.1759 0.1895 0.1751 0.0036  0.0024  0.0215  386 VAL A CA  
2473 C C   . VAL A 312 ? 0.1675 0.1833 0.1673 0.0027  0.0017  0.0232  386 VAL A C   
2474 O O   . VAL A 312 ? 0.1776 0.1942 0.1782 0.0029  0.0015  0.0239  386 VAL A O   
2475 C CB  . VAL A 312 ? 0.2020 0.2149 0.1999 0.0027  0.0020  0.0193  386 VAL A CB  
2476 C CG1 . VAL A 312 ? 0.2266 0.2402 0.2238 0.0021  0.0014  0.0187  386 VAL A CG1 
2477 C CG2 . VAL A 312 ? 0.2007 0.2115 0.1982 0.0037  0.0024  0.0175  386 VAL A CG2 
2478 N N   . SER A 313 ? 0.1519 0.1688 0.1515 0.0016  0.0012  0.0238  387 SER A N   
2479 C CA  . SER A 313 ? 0.1535 0.1725 0.1536 0.0007  0.0002  0.0254  387 SER A CA  
2480 C C   . SER A 313 ? 0.1516 0.1713 0.1509 -0.0004 -0.0008 0.0247  387 SER A C   
2481 O O   . SER A 313 ? 0.1661 0.1866 0.1643 -0.0015 -0.0017 0.0248  387 SER A O   
2482 C CB  . SER A 313 ? 0.1737 0.1937 0.1759 0.0016  0.0005  0.0276  387 SER A CB  
2483 O OG  . SER A 313 ? 0.2053 0.2274 0.2083 0.0008  -0.0005 0.0292  387 SER A OG  
2484 N N   . THR A 314 ? 0.1634 0.1826 0.1629 -0.0001 -0.0007 0.0239  388 THR A N   
2485 C CA  . THR A 314 ? 0.1724 0.1922 0.1715 -0.0011 -0.0017 0.0233  388 THR A CA  
2486 C C   . THR A 314 ? 0.1700 0.1882 0.1681 -0.0008 -0.0012 0.0213  388 THR A C   
2487 O O   . THR A 314 ? 0.1899 0.2070 0.1883 0.0005  -0.0002 0.0210  388 THR A O   
2488 C CB  . THR A 314 ? 0.2226 0.2441 0.2240 -0.0012 -0.0022 0.0250  388 THR A CB  
2489 O OG1 . THR A 314 ? 0.2908 0.3140 0.2931 -0.0017 -0.0030 0.0268  388 THR A OG1 
2490 C CG2 . THR A 314 ? 0.3007 0.3226 0.3018 -0.0025 -0.0034 0.0244  388 THR A CG2 
2491 N N   . LEU A 315 ? 0.1579 0.1758 0.1544 -0.0018 -0.0019 0.0199  389 LEU A N   
2492 C CA  . LEU A 315 ? 0.1604 0.1769 0.1559 -0.0017 -0.0017 0.0181  389 LEU A CA  
2493 C C   . LEU A 315 ? 0.1633 0.1805 0.1589 -0.0027 -0.0026 0.0181  389 LEU A C   
2494 O O   . LEU A 315 ? 0.1804 0.1985 0.1755 -0.0039 -0.0037 0.0184  389 LEU A O   
2495 C CB  . LEU A 315 ? 0.1670 0.1824 0.1606 -0.0020 -0.0015 0.0162  389 LEU A CB  
2496 C CG  . LEU A 315 ? 0.1855 0.2003 0.1793 -0.0012 -0.0007 0.0160  389 LEU A CG  
2497 C CD1 . LEU A 315 ? 0.2292 0.2433 0.2216 -0.0018 -0.0005 0.0144  389 LEU A CD1 
2498 C CD2 . LEU A 315 ? 0.2185 0.2321 0.2130 0.0001  0.0000  0.0158  389 LEU A CD2 
2499 N N   . THR A 316 ? 0.1469 0.1635 0.1430 -0.0022 -0.0023 0.0178  390 THR A N   
2500 C CA  . THR A 316 ? 0.1474 0.1644 0.1441 -0.0031 -0.0031 0.0180  390 THR A CA  
2501 C C   . THR A 316 ? 0.1400 0.1554 0.1353 -0.0031 -0.0029 0.0161  390 THR A C   
2502 O O   . THR A 316 ? 0.1447 0.1588 0.1392 -0.0019 -0.0020 0.0152  390 THR A O   
2503 C CB  . THR A 316 ? 0.1639 0.1819 0.1633 -0.0027 -0.0029 0.0199  390 THR A CB  
2504 O OG1 . THR A 316 ? 0.1943 0.2112 0.1940 -0.0010 -0.0015 0.0200  390 THR A OG1 
2505 C CG2 . THR A 316 ? 0.2005 0.2202 0.2017 -0.0025 -0.0030 0.0219  390 THR A CG2 
2506 N N   . PHE A 317 ? 0.1385 0.1539 0.1334 -0.0043 -0.0039 0.0157  391 PHE A N   
2507 C CA  . PHE A 317 ? 0.1431 0.1570 0.1366 -0.0044 -0.0038 0.0140  391 PHE A CA  
2508 C C   . PHE A 317 ? 0.1508 0.1649 0.1456 -0.0053 -0.0046 0.0145  391 PHE A C   
2509 O O   . PHE A 317 ? 0.1630 0.1781 0.1583 -0.0067 -0.0059 0.0151  391 PHE A O   
2510 C CB  . PHE A 317 ? 0.1615 0.1747 0.1525 -0.0052 -0.0043 0.0123  391 PHE A CB  
2511 C CG  . PHE A 317 ? 0.1858 0.1989 0.1760 -0.0045 -0.0036 0.0119  391 PHE A CG  
2512 C CD1 . PHE A 317 ? 0.1923 0.2043 0.1820 -0.0034 -0.0027 0.0108  391 PHE A CD1 
2513 C CD2 . PHE A 317 ? 0.2165 0.2308 0.2069 -0.0049 -0.0040 0.0131  391 PHE A CD2 
2514 C CE1 . PHE A 317 ? 0.2122 0.2242 0.2016 -0.0029 -0.0021 0.0105  391 PHE A CE1 
2515 C CE2 . PHE A 317 ? 0.2673 0.2816 0.2576 -0.0043 -0.0032 0.0130  391 PHE A CE2 
2516 C CZ  . PHE A 317 ? 0.2499 0.2631 0.2398 -0.0034 -0.0023 0.0117  391 PHE A CZ  
2517 N N   . HIS A 318 ? 0.1442 0.1571 0.1393 -0.0046 -0.0038 0.0142  392 HIS A N   
2518 C CA  . HIS A 318 ? 0.1516 0.1644 0.1480 -0.0055 -0.0044 0.0145  392 HIS A CA  
2519 C C   . HIS A 318 ? 0.1548 0.1656 0.1499 -0.0049 -0.0037 0.0132  392 HIS A C   
2520 O O   . HIS A 318 ? 0.1694 0.1793 0.1634 -0.0034 -0.0026 0.0125  392 HIS A O   
2521 C CB  . HIS A 318 ? 0.1829 0.1971 0.1828 -0.0054 -0.0042 0.0168  392 HIS A CB  
2522 C CG  . HIS A 318 ? 0.2133 0.2271 0.2141 -0.0036 -0.0025 0.0178  392 HIS A CG  
2523 N ND1 . HIS A 318 ? 0.2392 0.2537 0.2405 -0.0023 -0.0016 0.0188  392 HIS A ND1 
2524 C CD2 . HIS A 318 ? 0.2033 0.2159 0.2046 -0.0028 -0.0015 0.0180  392 HIS A CD2 
2525 C CE1 . HIS A 318 ? 0.2394 0.2531 0.2412 -0.0007 -0.0001 0.0196  392 HIS A CE1 
2526 N NE2 . HIS A 318 ? 0.2239 0.2364 0.2257 -0.0009 0.0000  0.0192  392 HIS A NE2 
2527 N N   . LYS A 319 ? 0.1725 0.1827 0.1680 -0.0060 -0.0044 0.0128  393 LYS A N   
2528 C CA  . LYS A 319 ? 0.1862 0.1944 0.1806 -0.0053 -0.0037 0.0117  393 LYS A CA  
2529 C C   . LYS A 319 ? 0.1838 0.1919 0.1802 -0.0041 -0.0024 0.0132  393 LYS A C   
2530 O O   . LYS A 319 ? 0.1966 0.2060 0.1958 -0.0044 -0.0024 0.0151  393 LYS A O   
2531 C CB  . LYS A 319 ? 0.2600 0.2672 0.2539 -0.0068 -0.0047 0.0107  393 LYS A CB  
2532 C CG  . LYS A 319 ? 0.3274 0.3341 0.3182 -0.0074 -0.0055 0.0087  393 LYS A CG  
2533 C CD  . LYS A 319 ? 0.3358 0.3413 0.3241 -0.0062 -0.0045 0.0071  393 LYS A CD  
2534 C CE  . LYS A 319 ? 0.4242 0.4277 0.4111 -0.0057 -0.0041 0.0056  393 LYS A CE  
2535 N NZ  . LYS A 319 ? 0.3820 0.3845 0.3693 -0.0042 -0.0029 0.0059  393 LYS A NZ  
2536 N N   . PRO A 320 ? 0.1786 0.1850 0.1736 -0.0025 -0.0012 0.0126  394 PRO A N   
2537 C CA  . PRO A 320 ? 0.1807 0.1867 0.1771 -0.0011 0.0001  0.0140  394 PRO A CA  
2538 C C   . PRO A 320 ? 0.1847 0.1900 0.1828 -0.0022 0.0000  0.0146  394 PRO A C   
2539 O O   . PRO A 320 ? 0.2096 0.2139 0.2066 -0.0033 -0.0008 0.0131  394 PRO A O   
2540 C CB  . PRO A 320 ? 0.2104 0.2146 0.2041 0.0007  0.0011  0.0127  394 PRO A CB  
2541 C CG  . PRO A 320 ? 0.2092 0.2126 0.2008 0.0000  0.0002  0.0106  394 PRO A CG  
2542 C CD  . PRO A 320 ? 0.2178 0.2228 0.2099 -0.0018 -0.0010 0.0104  394 PRO A CD  
2543 N N   . SER A 321 ? 0.1879 0.1937 0.1887 -0.0017 0.0009  0.0167  395 SER A N   
2544 C CA  . SER A 321 ? 0.2002 0.2054 0.2033 -0.0024 0.0012  0.0175  395 SER A CA  
2545 C C   . SER A 321 ? 0.1911 0.1938 0.1921 -0.0007 0.0025  0.0169  395 SER A C   
2546 O O   . SER A 321 ? 0.1948 0.1969 0.1950 0.0013  0.0041  0.0177  395 SER A O   
2547 C CB  . SER A 321 ? 0.2330 0.2397 0.2399 -0.0023 0.0019  0.0202  395 SER A CB  
2548 O OG  . SER A 321 ? 0.2795 0.2853 0.2886 -0.0026 0.0026  0.0211  395 SER A OG  
2549 N N   . LEU A 322 ? 0.2056 0.2067 0.2056 -0.0016 0.0020  0.0155  396 LEU A N   
2550 C CA  . LEU A 322 ? 0.2210 0.2198 0.2192 -0.0001 0.0032  0.0149  396 LEU A CA  
2551 C C   . LEU A 322 ? 0.2094 0.2076 0.2101 0.0005  0.0047  0.0172  396 LEU A C   
2552 O O   . LEU A 322 ? 0.2352 0.2317 0.2343 0.0025  0.0062  0.0173  396 LEU A O   
2553 C CB  . LEU A 322 ? 0.2378 0.2350 0.2344 -0.0013 0.0022  0.0129  396 LEU A CB  
2554 C CG  . LEU A 322 ? 0.2877 0.2851 0.2815 -0.0017 0.0009  0.0107  396 LEU A CG  
2555 C CD1 . LEU A 322 ? 0.3202 0.3160 0.3124 -0.0026 0.0002  0.0088  396 LEU A CD1 
2556 C CD2 . LEU A 322 ? 0.2870 0.2843 0.2784 0.0002  0.0017  0.0100  396 LEU A CD2 
2557 N N   . GLU A 323 ? 0.1979 0.1978 0.2027 -0.0008 0.0045  0.0190  397 GLU A N   
2558 C CA  . GLU A 323 ? 0.2313 0.2309 0.2391 -0.0001 0.0063  0.0215  397 GLU A CA  
2559 C C   . GLU A 323 ? 0.2026 0.2026 0.2097 0.0023  0.0081  0.0229  397 GLU A C   
2560 O O   . GLU A 323 ? 0.2183 0.2169 0.2251 0.0042  0.0101  0.0243  397 GLU A O   
2561 C CB  . GLU A 323 ? 0.2546 0.2562 0.2674 -0.0024 0.0053  0.0230  397 GLU A CB  
2562 C CG  . GLU A 323 ? 0.3203 0.3219 0.3371 -0.0019 0.0071  0.0257  397 GLU A CG  
2563 C CD  . GLU A 323 ? 0.3901 0.3941 0.4124 -0.0040 0.0062  0.0275  397 GLU A CD  
2564 O OE1 . GLU A 323 ? 0.4632 0.4694 0.4864 -0.0053 0.0045  0.0272  397 GLU A OE1 
2565 O OE2 . GLU A 323 ? 0.4537 0.4574 0.4797 -0.0043 0.0073  0.0293  397 GLU A OE2 
2566 N N   . HIS A 324 ? 0.1799 0.1817 0.1866 0.0025  0.0075  0.0229  398 HIS A N   
2567 C CA  . HIS A 324 ? 0.1868 0.1888 0.1925 0.0048  0.0091  0.0241  398 HIS A CA  
2568 C C   . HIS A 324 ? 0.1758 0.1757 0.1766 0.0070  0.0096  0.0224  398 HIS A C   
2569 O O   . HIS A 324 ? 0.1907 0.1897 0.1902 0.0095  0.0113  0.0233  398 HIS A O   
2570 C CB  . HIS A 324 ? 0.1965 0.2010 0.2037 0.0041  0.0082  0.0246  398 HIS A CB  
2571 C CG  . HIS A 324 ? 0.2201 0.2268 0.2324 0.0024  0.0079  0.0267  398 HIS A CG  
2572 N ND1 . HIS A 324 ? 0.2616 0.2690 0.2761 -0.0001 0.0061  0.0262  398 HIS A ND1 
2573 C CD2 . HIS A 324 ? 0.3123 0.3207 0.3279 0.0029  0.0090  0.0293  398 HIS A CD2 
2574 C CE1 . HIS A 324 ? 0.2763 0.2860 0.2955 -0.0012 0.0060  0.0284  398 HIS A CE1 
2575 N NE2 . HIS A 324 ? 0.2974 0.3078 0.3176 0.0006  0.0078  0.0303  398 HIS A NE2 
2576 N N   . PHE A 325 ? 0.1712 0.1704 0.1696 0.0062  0.0081  0.0199  399 PHE A N   
2577 C CA  . PHE A 325 ? 0.1729 0.1705 0.1672 0.0080  0.0081  0.0180  399 PHE A CA  
2578 C C   . PHE A 325 ? 0.1807 0.1765 0.1732 0.0077  0.0077  0.0163  399 PHE A C   
2579 O O   . PHE A 325 ? 0.1729 0.1685 0.1636 0.0070  0.0064  0.0141  399 PHE A O   
2580 C CB  . PHE A 325 ? 0.1615 0.1604 0.1546 0.0075  0.0068  0.0165  399 PHE A CB  
2581 C CG  . PHE A 325 ? 0.1645 0.1650 0.1592 0.0080  0.0074  0.0183  399 PHE A CG  
2582 C CD1 . PHE A 325 ? 0.1729 0.1724 0.1660 0.0105  0.0088  0.0190  399 PHE A CD1 
2583 C CD2 . PHE A 325 ? 0.1699 0.1727 0.1675 0.0061  0.0065  0.0192  399 PHE A CD2 
2584 C CE1 . PHE A 325 ? 0.1814 0.1820 0.1759 0.0112  0.0096  0.0207  399 PHE A CE1 
2585 C CE2 . PHE A 325 ? 0.1762 0.1804 0.1754 0.0068  0.0072  0.0209  399 PHE A CE2 
2586 C CZ  . PHE A 325 ? 0.1820 0.1851 0.1798 0.0093  0.0088  0.0217  399 PHE A CZ  
2587 N N   . PRO A 326 ? 0.1838 0.1780 0.1768 0.0085  0.0090  0.0174  400 PRO A N   
2588 C CA  . PRO A 326 ? 0.1922 0.1845 0.1838 0.0083  0.0088  0.0160  400 PRO A CA  
2589 C C   . PRO A 326 ? 0.1791 0.1699 0.1668 0.0100  0.0085  0.0140  400 PRO A C   
2590 O O   . PRO A 326 ? 0.1814 0.1711 0.1678 0.0095  0.0079  0.0124  400 PRO A O   
2591 C CB  . PRO A 326 ? 0.2014 0.1924 0.1947 0.0091  0.0106  0.0182  400 PRO A CB  
2592 C CG  . PRO A 326 ? 0.2069 0.1986 0.2006 0.0109  0.0121  0.0202  400 PRO A CG  
2593 C CD  . PRO A 326 ? 0.1840 0.1782 0.1792 0.0095  0.0109  0.0201  400 PRO A CD  
2594 N N   . CYS A 327 ? 0.1686 0.1594 0.1543 0.0120  0.0089  0.0139  401 CYS A N   
2595 C CA  . CYS A 327 ? 0.1681 0.1577 0.1503 0.0135  0.0083  0.0119  401 CYS A CA  
2596 C C   . CYS A 327 ? 0.1697 0.1602 0.1518 0.0118  0.0066  0.0097  401 CYS A C   
2597 O O   . CYS A 327 ? 0.1692 0.1587 0.1492 0.0124  0.0061  0.0079  401 CYS A O   
2598 C CB  . CYS A 327 ? 0.1756 0.1651 0.1560 0.0158  0.0087  0.0121  401 CYS A CB  
2599 S SG  . CYS A 327 ? 0.1989 0.1861 0.1775 0.0189  0.0109  0.0141  401 CYS A SG  
2600 N N   . ILE A 328 ? 0.1675 0.1600 0.1515 0.0097  0.0057  0.0098  402 ILE A N   
2601 C CA  . ILE A 328 ? 0.1721 0.1653 0.1556 0.0082  0.0043  0.0078  402 ILE A CA  
2602 C C   . ILE A 328 ? 0.1613 0.1533 0.1445 0.0073  0.0040  0.0067  402 ILE A C   
2603 O O   . ILE A 328 ? 0.1642 0.1557 0.1458 0.0074  0.0034  0.0048  402 ILE A O   
2604 C CB  . ILE A 328 ? 0.1741 0.1696 0.1597 0.0062  0.0035  0.0083  402 ILE A CB  
2605 C CG1 . ILE A 328 ? 0.1791 0.1757 0.1651 0.0070  0.0038  0.0093  402 ILE A CG1 
2606 C CG2 . ILE A 328 ? 0.1854 0.1814 0.1702 0.0047  0.0022  0.0064  402 ILE A CG2 
2607 C CD1 . ILE A 328 ? 0.1919 0.1907 0.1802 0.0052  0.0032  0.0103  402 ILE A CD1 
2608 N N   . LYS A 329 ? 0.1702 0.1619 0.1552 0.0062  0.0044  0.0079  403 LYS A N   
2609 C CA  . LYS A 329 ? 0.1839 0.1741 0.1686 0.0052  0.0040  0.0069  403 LYS A CA  
2610 C C   . LYS A 329 ? 0.1774 0.1655 0.1599 0.0073  0.0048  0.0062  403 LYS A C   
2611 O O   . LYS A 329 ? 0.1738 0.1610 0.1550 0.0070  0.0042  0.0045  403 LYS A O   
2612 C CB  . LYS A 329 ? 0.2154 0.2054 0.2028 0.0039  0.0043  0.0086  403 LYS A CB  
2613 C CG  . LYS A 329 ? 0.2789 0.2672 0.2662 0.0028  0.0040  0.0076  403 LYS A CG  
2614 C CD  . LYS A 329 ? 0.3445 0.3329 0.3308 0.0010  0.0025  0.0056  403 LYS A CD  
2615 C CE  . LYS A 329 ? 0.3837 0.3702 0.3705 -0.0001 0.0022  0.0051  403 LYS A CE  
2616 N NZ  . LYS A 329 ? 0.4372 0.4234 0.4221 -0.0011 0.0011  0.0029  403 LYS A NZ  
2617 N N   . LEU A 330 ? 0.1647 0.1520 0.1465 0.0094  0.0060  0.0074  404 LEU A N   
2618 C CA  . LEU A 330 ? 0.1633 0.1485 0.1427 0.0116  0.0066  0.0068  404 LEU A CA  
2619 C C   . LEU A 330 ? 0.1535 0.1390 0.1309 0.0123  0.0055  0.0046  404 LEU A C   
2620 O O   . LEU A 330 ? 0.1719 0.1561 0.1478 0.0130  0.0053  0.0033  404 LEU A O   
2621 C CB  . LEU A 330 ? 0.1745 0.1588 0.1531 0.0140  0.0080  0.0085  404 LEU A CB  
2622 C CG  . LEU A 330 ? 0.1800 0.1639 0.1608 0.0136  0.0094  0.0109  404 LEU A CG  
2623 C CD1 . LEU A 330 ? 0.1991 0.1822 0.1787 0.0162  0.0109  0.0126  404 LEU A CD1 
2624 C CD2 . LEU A 330 ? 0.2044 0.1865 0.1857 0.0131  0.0098  0.0109  404 LEU A CD2 
2625 N N   . ALA A 331 ? 0.1581 0.1453 0.1356 0.0121  0.0048  0.0042  405 ALA A N   
2626 C CA  . ALA A 331 ? 0.1527 0.1404 0.1288 0.0127  0.0039  0.0022  405 ALA A CA  
2627 C C   . ALA A 331 ? 0.1502 0.1382 0.1267 0.0109  0.0031  0.0006  405 ALA A C   
2628 O O   . ALA A 331 ? 0.1580 0.1454 0.1333 0.0116  0.0027  -0.0008 405 ALA A O   
2629 C CB  . ALA A 331 ? 0.1578 0.1471 0.1343 0.0127  0.0034  0.0023  405 ALA A CB  
2630 N N   . TYR A 332 ? 0.1580 0.1470 0.1360 0.0086  0.0028  0.0010  406 TYR A N   
2631 C CA  . TYR A 332 ? 0.1574 0.1463 0.1353 0.0071  0.0021  -0.0003 406 TYR A CA  
2632 C C   . TYR A 332 ? 0.1648 0.1515 0.1418 0.0076  0.0026  -0.0009 406 TYR A C   
2633 O O   . TYR A 332 ? 0.1740 0.1602 0.1499 0.0078  0.0023  -0.0024 406 TYR A O   
2634 C CB  . TYR A 332 ? 0.1503 0.1401 0.1295 0.0047  0.0016  0.0000  406 TYR A CB  
2635 C CG  . TYR A 332 ? 0.1546 0.1465 0.1343 0.0038  0.0009  0.0000  406 TYR A CG  
2636 C CD1 . TYR A 332 ? 0.1577 0.1510 0.1386 0.0038  0.0010  0.0013  406 TYR A CD1 
2637 C CD2 . TYR A 332 ? 0.1550 0.1474 0.1340 0.0029  0.0004  -0.0015 406 TYR A CD2 
2638 C CE1 . TYR A 332 ? 0.1581 0.1532 0.1395 0.0029  0.0004  0.0012  406 TYR A CE1 
2639 C CE2 . TYR A 332 ? 0.1547 0.1488 0.1340 0.0021  0.0000  -0.0016 406 TYR A CE2 
2640 C CZ  . TYR A 332 ? 0.1569 0.1524 0.1374 0.0020  -0.0001 -0.0002 406 TYR A CZ  
2641 O OH  . TYR A 332 ? 0.1649 0.1621 0.1460 0.0012  -0.0005 0.0000  406 TYR A OH  
2642 N N   . GLN A 333 ? 0.1601 0.1455 0.1376 0.0080  0.0034  0.0005  407 GLN A N   
2643 C CA  . GLN A 333 ? 0.1768 0.1599 0.1535 0.0084  0.0039  0.0001  407 GLN A CA  
2644 C C   . GLN A 333 ? 0.1784 0.1607 0.1532 0.0107  0.0041  -0.0008 407 GLN A C   
2645 O O   . GLN A 333 ? 0.1805 0.1616 0.1544 0.0109  0.0039  -0.0021 407 GLN A O   
2646 C CB  . GLN A 333 ? 0.1917 0.1737 0.1696 0.0085  0.0049  0.0021  407 GLN A CB  
2647 C CG  . GLN A 333 ? 0.1987 0.1813 0.1790 0.0060  0.0044  0.0028  407 GLN A CG  
2648 C CD  . GLN A 333 ? 0.2474 0.2293 0.2296 0.0060  0.0055  0.0050  407 GLN A CD  
2649 O OE1 . GLN A 333 ? 0.2638 0.2455 0.2459 0.0078  0.0066  0.0065  407 GLN A OE1 
2650 N NE2 . GLN A 333 ? 0.3262 0.3073 0.3101 0.0041  0.0052  0.0052  407 GLN A NE2 
2651 N N   . ALA A 334 ? 0.1584 0.1410 0.1325 0.0126  0.0043  -0.0003 408 ALA A N   
2652 C CA  . ALA A 334 ? 0.1623 0.1442 0.1345 0.0149  0.0041  -0.0013 408 ALA A CA  
2653 C C   . ALA A 334 ? 0.1664 0.1495 0.1386 0.0145  0.0031  -0.0033 408 ALA A C   
2654 O O   . ALA A 334 ? 0.1715 0.1538 0.1428 0.0155  0.0030  -0.0045 408 ALA A O   
2655 C CB  . ALA A 334 ? 0.1695 0.1514 0.1408 0.0169  0.0044  -0.0004 408 ALA A CB  
2656 N N   . GLY A 335 ? 0.1675 0.1526 0.1408 0.0131  0.0025  -0.0036 409 GLY A N   
2657 C CA  . GLY A 335 ? 0.1627 0.1490 0.1362 0.0126  0.0017  -0.0053 409 GLY A CA  
2658 C C   . GLY A 335 ? 0.1598 0.1453 0.1332 0.0115  0.0019  -0.0063 409 GLY A C   
2659 O O   . GLY A 335 ? 0.1731 0.1586 0.1461 0.0122  0.0017  -0.0076 409 GLY A O   
2660 N N   . ILE A 336 ? 0.1688 0.1537 0.1425 0.0099  0.0021  -0.0057 410 ILE A N   
2661 C CA  . ILE A 336 ? 0.1821 0.1659 0.1554 0.0088  0.0022  -0.0067 410 ILE A CA  
2662 C C   . ILE A 336 ? 0.1900 0.1717 0.1623 0.0103  0.0027  -0.0071 410 ILE A C   
2663 O O   . ILE A 336 ? 0.2133 0.1945 0.1850 0.0104  0.0027  -0.0085 410 ILE A O   
2664 C CB  . ILE A 336 ? 0.1846 0.1681 0.1585 0.0067  0.0021  -0.0059 410 ILE A CB  
2665 C CG1 . ILE A 336 ? 0.1929 0.1785 0.1675 0.0052  0.0014  -0.0059 410 ILE A CG1 
2666 C CG2 . ILE A 336 ? 0.2062 0.1878 0.1793 0.0058  0.0022  -0.0069 410 ILE A CG2 
2667 C CD1 . ILE A 336 ? 0.2069 0.1927 0.1824 0.0033  0.0011  -0.0048 410 ILE A CD1 
2668 N N   . LYS A 337 ? 0.1821 0.1626 0.1541 0.0116  0.0032  -0.0059 411 LYS A N   
2669 C CA  . LYS A 337 ? 0.1982 0.1767 0.1691 0.0133  0.0038  -0.0062 411 LYS A CA  
2670 C C   . LYS A 337 ? 0.2125 0.1917 0.1828 0.0151  0.0033  -0.0074 411 LYS A C   
2671 O O   . LYS A 337 ? 0.2437 0.2216 0.2133 0.0162  0.0035  -0.0083 411 LYS A O   
2672 C CB  . LYS A 337 ? 0.2334 0.2105 0.2040 0.0145  0.0045  -0.0045 411 LYS A CB  
2673 C CG  . LYS A 337 ? 0.2894 0.2653 0.2610 0.0130  0.0051  -0.0033 411 LYS A CG  
2674 C CD  . LYS A 337 ? 0.3932 0.3672 0.3644 0.0146  0.0062  -0.0016 411 LYS A CD  
2675 C CE  . LYS A 337 ? 0.4796 0.4526 0.4524 0.0131  0.0069  -0.0001 411 LYS A CE  
2676 N NZ  . LYS A 337 ? 0.5847 0.5566 0.5580 0.0111  0.0065  -0.0012 411 LYS A NZ  
2677 N N   . GLY A 338 ? 0.1962 0.1772 0.1669 0.0157  0.0027  -0.0075 412 GLY A N   
2678 C CA  . GLY A 338 ? 0.1861 0.1680 0.1567 0.0172  0.0020  -0.0087 412 GLY A CA  
2679 C C   . GLY A 338 ? 0.1900 0.1703 0.1592 0.0198  0.0021  -0.0085 412 GLY A C   
2680 O O   . GLY A 338 ? 0.1837 0.1628 0.1518 0.0207  0.0026  -0.0071 412 GLY A O   
2681 N N   . ASN A 339 ? 0.2052 0.1855 0.1743 0.0211  0.0017  -0.0097 413 ASN A N   
2682 C CA  . ASN A 339 ? 0.1997 0.1788 0.1674 0.0237  0.0015  -0.0097 413 ASN A CA  
2683 C C   . ASN A 339 ? 0.1935 0.1729 0.1603 0.0250  0.0009  -0.0090 413 ASN A C   
2684 O O   . ASN A 339 ? 0.2188 0.2000 0.1866 0.0244  0.0001  -0.0095 413 ASN A O   
2685 C CB  . ASN A 339 ? 0.1920 0.1684 0.1584 0.0242  0.0026  -0.0088 413 ASN A CB  
2686 C CG  . ASN A 339 ? 0.1926 0.1674 0.1574 0.0269  0.0026  -0.0088 413 ASN A CG  
2687 O OD1 . ASN A 339 ? 0.1928 0.1662 0.1560 0.0285  0.0029  -0.0076 413 ASN A OD1 
2688 N ND2 . ASN A 339 ? 0.2353 0.2104 0.2007 0.0276  0.0021  -0.0101 413 ASN A ND2 
2689 N N   . PHE A 340 ? 0.1807 0.1582 0.1455 0.0268  0.0014  -0.0078 414 PHE A N   
2690 C CA  . PHE A 340 ? 0.1783 0.1556 0.1417 0.0283  0.0010  -0.0071 414 PHE A CA  
2691 C C   . PHE A 340 ? 0.1772 0.1543 0.1405 0.0273  0.0021  -0.0053 414 PHE A C   
2692 O O   . PHE A 340 ? 0.1796 0.1561 0.1415 0.0288  0.0022  -0.0044 414 PHE A O   
2693 C CB  . PHE A 340 ? 0.2053 0.1808 0.1661 0.0314  0.0008  -0.0069 414 PHE A CB  
2694 C CG  . PHE A 340 ? 0.2222 0.1983 0.1833 0.0327  -0.0005 -0.0086 414 PHE A CG  
2695 C CD1 . PHE A 340 ? 0.2541 0.2317 0.2156 0.0334  -0.0023 -0.0099 414 PHE A CD1 
2696 C CD2 . PHE A 340 ? 0.2299 0.2052 0.1912 0.0331  -0.0002 -0.0091 414 PHE A CD2 
2697 C CE1 . PHE A 340 ? 0.3000 0.2785 0.2625 0.0343  -0.0037 -0.0115 414 PHE A CE1 
2698 C CE2 . PHE A 340 ? 0.2544 0.2305 0.2165 0.0342  -0.0015 -0.0106 414 PHE A CE2 
2699 C CZ  . PHE A 340 ? 0.2874 0.2652 0.2501 0.0348  -0.0032 -0.0118 414 PHE A CZ  
2700 N N   . TYR A 341 ? 0.1604 0.1377 0.1253 0.0249  0.0029  -0.0048 415 TYR A N   
2701 C CA  . TYR A 341 ? 0.1605 0.1379 0.1260 0.0239  0.0039  -0.0031 415 TYR A CA  
2702 C C   . TYR A 341 ? 0.1651 0.1441 0.1309 0.0237  0.0032  -0.0030 415 TYR A C   
2703 O O   . TYR A 341 ? 0.1667 0.1452 0.1318 0.0244  0.0040  -0.0015 415 TYR A O   
2704 C CB  . TYR A 341 ? 0.1662 0.1436 0.1335 0.0212  0.0045  -0.0027 415 TYR A CB  
2705 C CG  . TYR A 341 ? 0.1706 0.1456 0.1374 0.0215  0.0055  -0.0021 415 TYR A CG  
2706 C CD1 . TYR A 341 ? 0.1766 0.1503 0.1435 0.0217  0.0068  -0.0001 415 TYR A CD1 
2707 C CD2 . TYR A 341 ? 0.1780 0.1522 0.1446 0.0216  0.0054  -0.0033 415 TYR A CD2 
2708 C CE1 . TYR A 341 ? 0.1982 0.1696 0.1650 0.0218  0.0078  0.0006  415 TYR A CE1 
2709 C CE2 . TYR A 341 ? 0.1924 0.1642 0.1586 0.0218  0.0064  -0.0027 415 TYR A CE2 
2710 C CZ  . TYR A 341 ? 0.2015 0.1720 0.1681 0.0217  0.0075  -0.0007 415 TYR A CZ  
2711 O OH  . TYR A 341 ? 0.2310 0.1990 0.1976 0.0216  0.0086  0.0000  415 TYR A OH  
2712 N N   . PRO A 342 ? 0.1630 0.1439 0.1299 0.0228  0.0020  -0.0045 416 PRO A N   
2713 C CA  . PRO A 342 ? 0.1654 0.1477 0.1326 0.0228  0.0015  -0.0044 416 PRO A CA  
2714 C C   . PRO A 342 ? 0.1737 0.1548 0.1385 0.0256  0.0011  -0.0042 416 PRO A C   
2715 O O   . PRO A 342 ? 0.1732 0.1543 0.1375 0.0261  0.0014  -0.0033 416 PRO A O   
2716 C CB  . PRO A 342 ? 0.1665 0.1508 0.1354 0.0214  0.0004  -0.0061 416 PRO A CB  
2717 C CG  . PRO A 342 ? 0.1657 0.1500 0.1357 0.0197  0.0008  -0.0064 416 PRO A CG  
2718 C CD  . PRO A 342 ? 0.1746 0.1567 0.1430 0.0213  0.0014  -0.0061 416 PRO A CD  
2719 N N   . THR A 343 ? 0.1682 0.1482 0.1315 0.0276  0.0005  -0.0052 417 THR A N   
2720 C CA  . THR A 343 ? 0.1743 0.1528 0.1348 0.0305  0.0001  -0.0050 417 THR A CA  
2721 C C   . THR A 343 ? 0.1701 0.1467 0.1287 0.0316  0.0018  -0.0028 417 THR A C   
2722 O O   . THR A 343 ? 0.1871 0.1630 0.1439 0.0331  0.0019  -0.0021 417 THR A O   
2723 C CB  . THR A 343 ? 0.1848 0.1622 0.1440 0.0324  -0.0007 -0.0062 417 THR A CB  
2724 O OG1 . THR A 343 ? 0.2012 0.1805 0.1626 0.0312  -0.0020 -0.0080 417 THR A OG1 
2725 C CG2 . THR A 343 ? 0.2130 0.1888 0.1690 0.0355  -0.0015 -0.0063 417 THR A CG2 
2726 N N   . VAL A 344 ? 0.1702 0.1458 0.1293 0.0308  0.0032  -0.0017 418 VAL A N   
2727 C CA  . VAL A 344 ? 0.1679 0.1419 0.1260 0.0317  0.0050  0.0004  418 VAL A CA  
2728 C C   . VAL A 344 ? 0.1692 0.1444 0.1288 0.0303  0.0057  0.0018  418 VAL A C   
2729 O O   . VAL A 344 ? 0.1814 0.1555 0.1395 0.0318  0.0068  0.0034  418 VAL A O   
2730 C CB  . VAL A 344 ? 0.1757 0.1485 0.1346 0.0309  0.0061  0.0012  418 VAL A CB  
2731 C CG1 . VAL A 344 ? 0.1865 0.1578 0.1452 0.0313  0.0082  0.0037  418 VAL A CG1 
2732 C CG2 . VAL A 344 ? 0.1853 0.1568 0.1424 0.0328  0.0055  0.0001  418 VAL A CG2 
2733 N N   . LEU A 345 ? 0.1654 0.1427 0.1278 0.0275  0.0052  0.0012  419 LEU A N   
2734 C CA  . LEU A 345 ? 0.1615 0.1402 0.1256 0.0260  0.0057  0.0023  419 LEU A CA  
2735 C C   . LEU A 345 ? 0.1575 0.1363 0.1200 0.0277  0.0052  0.0022  419 LEU A C   
2736 O O   . LEU A 345 ? 0.1717 0.1502 0.1338 0.0284  0.0063  0.0039  419 LEU A O   
2737 C CB  . LEU A 345 ? 0.1661 0.1471 0.1330 0.0230  0.0048  0.0013  419 LEU A CB  
2738 C CG  . LEU A 345 ? 0.1667 0.1494 0.1356 0.0214  0.0050  0.0023  419 LEU A CG  
2739 C CD1 . LEU A 345 ? 0.1756 0.1583 0.1463 0.0198  0.0061  0.0041  419 LEU A CD1 
2740 C CD2 . LEU A 345 ? 0.1777 0.1626 0.1482 0.0194  0.0037  0.0007  419 LEU A CD2 
2741 N N   . ASN A 346 ? 0.1631 0.1424 0.1248 0.0283  0.0035  0.0002  420 ASN A N   
2742 C CA  . ASN A 346 ? 0.1704 0.1496 0.1306 0.0298  0.0028  -0.0001 420 ASN A CA  
2743 C C   . ASN A 346 ? 0.1783 0.1551 0.1350 0.0329  0.0037  0.0009  420 ASN A C   
2744 O O   . ASN A 346 ? 0.1849 0.1612 0.1405 0.0338  0.0043  0.0019  420 ASN A O   
2745 C CB  . ASN A 346 ? 0.1792 0.1592 0.1395 0.0299  0.0008  -0.0025 420 ASN A CB  
2746 C CG  . ASN A 346 ? 0.2000 0.1798 0.1590 0.0312  -0.0001 -0.0031 420 ASN A CG  
2747 O OD1 . ASN A 346 ? 0.2365 0.2145 0.1925 0.0338  -0.0008 -0.0037 420 ASN A OD1 
2748 N ND2 . ASN A 346 ? 0.1851 0.1664 0.1459 0.0296  0.0000  -0.0027 420 ASN A ND2 
2749 N N   . ALA A 347 ? 0.1772 0.1522 0.1319 0.0346  0.0037  0.0007  421 ALA A N   
2750 C CA  . ALA A 347 ? 0.1872 0.1595 0.1379 0.0379  0.0044  0.0016  421 ALA A CA  
2751 C C   . ALA A 347 ? 0.1878 0.1593 0.1384 0.0382  0.0069  0.0043  421 ALA A C   
2752 O O   . ALA A 347 ? 0.1925 0.1626 0.1406 0.0403  0.0077  0.0054  421 ALA A O   
2753 C CB  . ALA A 347 ? 0.2039 0.1748 0.1530 0.0394  0.0041  0.0010  421 ALA A CB  
2754 N N   . SER A 348 ? 0.1859 0.1579 0.1392 0.0362  0.0082  0.0056  422 SER A N   
2755 C CA  . SER A 348 ? 0.1895 0.1609 0.1434 0.0363  0.0105  0.0082  422 SER A CA  
2756 C C   . SER A 348 ? 0.1946 0.1674 0.1499 0.0355  0.0108  0.0090  422 SER A C   
2757 O O   . SER A 348 ? 0.1983 0.1702 0.1527 0.0370  0.0126  0.0110  422 SER A O   
2758 C CB  . SER A 348 ? 0.1911 0.1627 0.1479 0.0343  0.0115  0.0092  422 SER A CB  
2759 O OG  . SER A 348 ? 0.1955 0.1695 0.1558 0.0310  0.0104  0.0081  422 SER A OG  
2760 N N   . ASN A 349 ? 0.1819 0.1572 0.1397 0.0331  0.0093  0.0076  423 ASN A N   
2761 C CA  . ASN A 349 ? 0.1808 0.1575 0.1399 0.0324  0.0095  0.0083  423 ASN A CA  
2762 C C   . ASN A 349 ? 0.1840 0.1591 0.1393 0.0353  0.0093  0.0079  423 ASN A C   
2763 O O   . ASN A 349 ? 0.1916 0.1667 0.1468 0.0360  0.0104  0.0094  423 ASN A O   
2764 C CB  . ASN A 349 ? 0.1805 0.1597 0.1426 0.0295  0.0080  0.0069  423 ASN A CB  
2765 C CG  . ASN A 349 ? 0.1725 0.1531 0.1359 0.0288  0.0082  0.0077  423 ASN A CG  
2766 O OD1 . ASN A 349 ? 0.1878 0.1690 0.1530 0.0282  0.0098  0.0098  423 ASN A OD1 
2767 N ND2 . ASN A 349 ? 0.1853 0.1665 0.1481 0.0289  0.0067  0.0060  423 ASN A ND2 
2768 N N   . GLU A 350 ? 0.1864 0.1604 0.1390 0.0369  0.0076  0.0059  424 GLU A N   
2769 C CA  . GLU A 350 ? 0.1973 0.1695 0.1462 0.0397  0.0073  0.0055  424 GLU A CA  
2770 C C   . GLU A 350 ? 0.2102 0.1801 0.1562 0.0423  0.0096  0.0078  424 GLU A C   
2771 O O   . GLU A 350 ? 0.2132 0.1823 0.1577 0.0437  0.0103  0.0086  424 GLU A O   
2772 C CB  . GLU A 350 ? 0.2118 0.1829 0.1580 0.0413  0.0050  0.0030  424 GLU A CB  
2773 C CG  . GLU A 350 ? 0.2320 0.2052 0.1808 0.0391  0.0028  0.0007  424 GLU A CG  
2774 C CD  . GLU A 350 ? 0.2633 0.2358 0.2102 0.0406  0.0004  -0.0016 424 GLU A CD  
2775 O OE1 . GLU A 350 ? 0.2918 0.2618 0.2346 0.0436  0.0002  -0.0017 424 GLU A OE1 
2776 O OE2 . GLU A 350 ? 0.2721 0.2465 0.2216 0.0387  -0.0012 -0.0034 424 GLU A OE2 
2777 N N   . ILE A 351 ? 0.2036 0.1723 0.1491 0.0431  0.0109  0.0090  425 ILE A N   
2778 C CA  . ILE A 351 ? 0.2090 0.1755 0.1521 0.0455  0.0134  0.0116  425 ILE A CA  
2779 C C   . ILE A 351 ? 0.2102 0.1781 0.1567 0.0440  0.0155  0.0140  425 ILE A C   
2780 O O   . ILE A 351 ? 0.2259 0.1927 0.1706 0.0460  0.0171  0.0156  425 ILE A O   
2781 C CB  . ILE A 351 ? 0.2246 0.1894 0.1666 0.0465  0.0144  0.0124  425 ILE A CB  
2782 C CG1 . ILE A 351 ? 0.2336 0.1967 0.1716 0.0487  0.0125  0.0103  425 ILE A CG1 
2783 C CG2 . ILE A 351 ? 0.2282 0.1911 0.1689 0.0485  0.0175  0.0154  425 ILE A CG2 
2784 C CD1 . ILE A 351 ? 0.2679 0.2283 0.2003 0.0525  0.0123  0.0101  425 ILE A CD1 
2785 N N   . ALA A 352 ? 0.1996 0.1699 0.1509 0.0407  0.0156  0.0144  426 ALA A N   
2786 C CA  . ALA A 352 ? 0.2060 0.1778 0.1610 0.0392  0.0174  0.0168  426 ALA A CA  
2787 C C   . ALA A 352 ? 0.2029 0.1759 0.1583 0.0391  0.0171  0.0168  426 ALA A C   
2788 O O   . ALA A 352 ? 0.2159 0.1890 0.1721 0.0398  0.0191  0.0190  426 ALA A O   
2789 C CB  . ALA A 352 ? 0.2223 0.1962 0.1819 0.0357  0.0170  0.0169  426 ALA A CB  
2790 N N   . ASN A 353 ? 0.1978 0.1720 0.1532 0.0380  0.0148  0.0143  427 ASN A N   
2791 C CA  . ASN A 353 ? 0.2054 0.1805 0.1610 0.0379  0.0143  0.0140  427 ASN A CA  
2792 C C   . ASN A 353 ? 0.2079 0.1803 0.1591 0.0416  0.0155  0.0148  427 ASN A C   
2793 O O   . ASN A 353 ? 0.2152 0.1878 0.1670 0.0421  0.0171  0.0166  427 ASN A O   
2794 C CB  . ASN A 353 ? 0.2008 0.1768 0.1564 0.0366  0.0115  0.0111  427 ASN A CB  
2795 C CG  . ASN A 353 ? 0.2063 0.1828 0.1616 0.0368  0.0107  0.0103  427 ASN A CG  
2796 O OD1 . ASN A 353 ? 0.2289 0.2036 0.1812 0.0393  0.0114  0.0107  427 ASN A OD1 
2797 N ND2 . ASN A 353 ? 0.2043 0.1831 0.1625 0.0342  0.0091  0.0089  427 ASN A ND2 
2798 N N   . ASN A 354 ? 0.2212 0.1910 0.1678 0.0442  0.0149  0.0136  428 ASN A N   
2799 C CA  . ASN A 354 ? 0.2493 0.2161 0.1908 0.0479  0.0158  0.0141  428 ASN A CA  
2800 C C   . ASN A 354 ? 0.2403 0.2059 0.1815 0.0495  0.0191  0.0174  428 ASN A C   
2801 O O   . ASN A 354 ? 0.2509 0.2153 0.1901 0.0516  0.0206  0.0186  428 ASN A O   
2802 C CB  . ASN A 354 ? 0.2563 0.2206 0.1930 0.0503  0.0140  0.0120  428 ASN A CB  
2803 C CG  . ASN A 354 ? 0.3202 0.2817 0.2517 0.0536  0.0140  0.0115  428 ASN A CG  
2804 O OD1 . ASN A 354 ? 0.3334 0.2921 0.2608 0.0568  0.0156  0.0128  428 ASN A OD1 
2805 N ND2 . ASN A 354 ? 0.3081 0.2702 0.2400 0.0530  0.0123  0.0099  428 ASN A ND2 
2806 N N   . LEU A 355 ? 0.2327 0.1989 0.1763 0.0485  0.0205  0.0190  429 LEU A N   
2807 C CA  . LEU A 355 ? 0.2364 0.2017 0.1805 0.0498  0.0237  0.0223  429 LEU A CA  
2808 C C   . LEU A 355 ? 0.2376 0.2053 0.1860 0.0482  0.0250  0.0240  429 LEU A C   
2809 O O   . LEU A 355 ? 0.2535 0.2202 0.2008 0.0503  0.0273  0.0262  429 LEU A O   
2810 C CB  . LEU A 355 ? 0.2435 0.2091 0.1901 0.0486  0.0247  0.0235  429 LEU A CB  
2811 C CG  . LEU A 355 ? 0.2481 0.2109 0.1904 0.0508  0.0244  0.0226  429 LEU A CG  
2812 C CD1 . LEU A 355 ? 0.2479 0.2115 0.1936 0.0488  0.0248  0.0233  429 LEU A CD1 
2813 C CD2 . LEU A 355 ? 0.2714 0.2307 0.2080 0.0553  0.0265  0.0242  429 LEU A CD2 
2814 N N   . PHE A 356 ? 0.2239 0.1947 0.1770 0.0446  0.0235  0.0232  430 PHE A N   
2815 C CA  . PHE A 356 ? 0.2170 0.1903 0.1742 0.0430  0.0244  0.0249  430 PHE A CA  
2816 C C   . PHE A 356 ? 0.2304 0.2028 0.1848 0.0449  0.0241  0.0242  430 PHE A C   
2817 O O   . PHE A 356 ? 0.2415 0.2142 0.1968 0.0459  0.0262  0.0264  430 PHE A O   
2818 C CB  . PHE A 356 ? 0.2153 0.1918 0.1774 0.0389  0.0224  0.0237  430 PHE A CB  
2819 C CG  . PHE A 356 ? 0.2243 0.2034 0.1907 0.0372  0.0230  0.0253  430 PHE A CG  
2820 C CD1 . PHE A 356 ? 0.2209 0.2013 0.1912 0.0366  0.0251  0.0282  430 PHE A CD1 
2821 C CD2 . PHE A 356 ? 0.2177 0.1984 0.1848 0.0360  0.0212  0.0238  430 PHE A CD2 
2822 C CE1 . PHE A 356 ? 0.2364 0.2194 0.2110 0.0350  0.0256  0.0297  430 PHE A CE1 
2823 C CE2 . PHE A 356 ? 0.2214 0.2046 0.1926 0.0344  0.0217  0.0253  430 PHE A CE2 
2824 C CZ  . PHE A 356 ? 0.2239 0.2083 0.1988 0.0339  0.0238  0.0282  430 PHE A CZ  
2825 N N   . LEU A 357 ? 0.2302 0.2017 0.1814 0.0454  0.0217  0.0213  431 LEU A N   
2826 C CA  . LEU A 357 ? 0.2371 0.2074 0.1854 0.0472  0.0212  0.0204  431 LEU A CA  
2827 C C   . LEU A 357 ? 0.2559 0.2232 0.2000 0.0510  0.0239  0.0223  431 LEU A C   
2828 O O   . LEU A 357 ? 0.2786 0.2457 0.2226 0.0521  0.0251  0.0234  431 LEU A O   
2829 C CB  . LEU A 357 ? 0.2388 0.2079 0.1838 0.0476  0.0183  0.0170  431 LEU A CB  
2830 C CG  . LEU A 357 ? 0.2764 0.2437 0.2180 0.0494  0.0173  0.0155  431 LEU A CG  
2831 C CD1 . LEU A 357 ? 0.2991 0.2687 0.2443 0.0474  0.0172  0.0158  431 LEU A CD1 
2832 C CD2 . LEU A 357 ? 0.3064 0.2724 0.2451 0.0498  0.0143  0.0122  431 LEU A CD2 
2833 N N   . ASN A 358 ? 0.2620 0.2270 0.2029 0.0532  0.0249  0.0229  432 ASN A N   
2834 C CA  . ASN A 358 ? 0.2780 0.2396 0.2140 0.0573  0.0274  0.0246  432 ASN A CA  
2835 C C   . ASN A 358 ? 0.2954 0.2578 0.2347 0.0573  0.0309  0.0284  432 ASN A C   
2836 O O   . ASN A 358 ? 0.3069 0.2665 0.2424 0.0607  0.0334  0.0302  432 ASN A O   
2837 C CB  . ASN A 358 ? 0.2994 0.2578 0.2297 0.0598  0.0263  0.0230  432 ASN A CB  
2838 C CG  . ASN A 358 ? 0.3448 0.3020 0.2714 0.0605  0.0232  0.0196  432 ASN A CG  
2839 O OD1 . ASN A 358 ? 0.3792 0.3373 0.3066 0.0588  0.0204  0.0171  432 ASN A OD1 
2840 N ND2 . ASN A 358 ? 0.3486 0.3038 0.2718 0.0628  0.0235  0.0194  432 ASN A ND2 
2841 N N   . ASN A 359 ? 0.2740 0.2400 0.2200 0.0539  0.0313  0.0297  433 ASN A N   
2842 C CA  . ASN A 359 ? 0.2866 0.2539 0.2368 0.0537  0.0345  0.0334  433 ASN A CA  
2843 C C   . ASN A 359 ? 0.3018 0.2675 0.2514 0.0548  0.0364  0.0351  433 ASN A C   
2844 O O   . ASN A 359 ? 0.3328 0.2980 0.2834 0.0563  0.0396  0.0382  433 ASN A O   
2845 C CB  . ASN A 359 ? 0.3114 0.2776 0.2599 0.0564  0.0370  0.0353  433 ASN A CB  
2846 C CG  . ASN A 359 ? 0.3756 0.3427 0.3240 0.0558  0.0352  0.0336  433 ASN A CG  
2847 O OD1 . ASN A 359 ? 0.4882 0.4526 0.4312 0.0586  0.0350  0.0325  433 ASN A OD1 
2848 N ND2 . ASN A 359 ? 0.3231 0.2939 0.2772 0.0521  0.0337  0.0333  433 ASN A ND2 
2849 N N   . LYS A 360 ? 0.2726 0.2379 0.2213 0.0538  0.0345  0.0332  434 LYS A N   
2850 C CA  . LYS A 360 ? 0.2834 0.2470 0.2314 0.0549  0.0362  0.0347  434 LYS A CA  
2851 C C   . LYS A 360 ? 0.2776 0.2438 0.2322 0.0513  0.0363  0.0358  434 LYS A C   
2852 O O   . LYS A 360 ? 0.3010 0.2662 0.2563 0.0518  0.0382  0.0377  434 LYS A O   
2853 C CB  . LYS A 360 ? 0.2949 0.2559 0.2373 0.0566  0.0343  0.0322  434 LYS A CB  
2854 C CG  . LYS A 360 ? 0.3423 0.3002 0.2775 0.0602  0.0336  0.0306  434 LYS A CG  
2855 C CD  . LYS A 360 ? 0.3940 0.3491 0.3254 0.0641  0.0370  0.0332  434 LYS A CD  
2856 C CE  . LYS A 360 ? 0.4553 0.4072 0.3793 0.0677  0.0358  0.0313  434 LYS A CE  
2857 N NZ  . LYS A 360 ? 0.5250 0.4744 0.4456 0.0713  0.0393  0.0340  434 LYS A NZ  
2858 N N   . ILE A 361 ? 0.2520 0.2213 0.2107 0.0476  0.0338  0.0341  435 ILE A N   
2859 C CA  . ILE A 361 ? 0.2387 0.2105 0.2034 0.0440  0.0334  0.0347  435 ILE A CA  
2860 C C   . ILE A 361 ? 0.2391 0.2144 0.2089 0.0411  0.0325  0.0348  435 ILE A C   
2861 O O   . ILE A 361 ? 0.2531 0.2288 0.2214 0.0418  0.0318  0.0340  435 ILE A O   
2862 C CB  . ILE A 361 ? 0.2466 0.2181 0.2105 0.0424  0.0308  0.0320  435 ILE A CB  
2863 C CG1 . ILE A 361 ? 0.2495 0.2224 0.2124 0.0409  0.0276  0.0287  435 ILE A CG1 
2864 C CG2 . ILE A 361 ? 0.2599 0.2280 0.2189 0.0453  0.0316  0.0318  435 ILE A CG2 
2865 C CD1 . ILE A 361 ? 0.2338 0.2067 0.1964 0.0392  0.0252  0.0261  435 ILE A CD1 
2866 N N   . LYS A 362 ? 0.2395 0.2171 0.2152 0.0380  0.0325  0.0360  436 LYS A N   
2867 C CA  . LYS A 362 ? 0.2448 0.2258 0.2255 0.0350  0.0314  0.0361  436 LYS A CA  
2868 C C   . LYS A 362 ? 0.2350 0.2176 0.2165 0.0320  0.0280  0.0331  436 LYS A C   
2869 O O   . LYS A 362 ? 0.2259 0.2071 0.2050 0.0319  0.0267  0.0311  436 LYS A O   
2870 C CB  . LYS A 362 ? 0.2827 0.2654 0.2696 0.0333  0.0330  0.0390  436 LYS A CB  
2871 C CG  . LYS A 362 ? 0.3345 0.3160 0.3215 0.0361  0.0367  0.0424  436 LYS A CG  
2872 C CD  . LYS A 362 ? 0.4229 0.4066 0.4171 0.0341  0.0382  0.0454  436 LYS A CD  
2873 C CE  . LYS A 362 ? 0.5246 0.5074 0.5194 0.0369  0.0421  0.0490  436 LYS A CE  
2874 N NZ  . LYS A 362 ? 0.6001 0.5837 0.6006 0.0354  0.0437  0.0515  436 LYS A NZ  
2875 N N   . TYR A 363 ? 0.2244 0.2098 0.2093 0.0297  0.0268  0.0329  437 TYR A N   
2876 C CA  . TYR A 363 ? 0.2185 0.2055 0.2041 0.0270  0.0237  0.0303  437 TYR A CA  
2877 C C   . TYR A 363 ? 0.2181 0.2048 0.2048 0.0250  0.0226  0.0292  437 TYR A C   
2878 O O   . TYR A 363 ? 0.2188 0.2048 0.2029 0.0246  0.0208  0.0265  437 TYR A O   
2879 C CB  . TYR A 363 ? 0.2191 0.2093 0.2091 0.0249  0.0231  0.0311  437 TYR A CB  
2880 C CG  . TYR A 363 ? 0.1999 0.1918 0.1908 0.0220  0.0202  0.0287  437 TYR A CG  
2881 C CD1 . TYR A 363 ? 0.2085 0.2004 0.1965 0.0224  0.0187  0.0265  437 TYR A CD1 
2882 C CD2 . TYR A 363 ? 0.1966 0.1900 0.1912 0.0190  0.0191  0.0286  437 TYR A CD2 
2883 C CE1 . TYR A 363 ? 0.2030 0.1964 0.1918 0.0199  0.0163  0.0245  437 TYR A CE1 
2884 C CE2 . TYR A 363 ? 0.1924 0.1873 0.1874 0.0166  0.0166  0.0265  437 TYR A CE2 
2885 C CZ  . TYR A 363 ? 0.1966 0.1915 0.1887 0.0171  0.0153  0.0245  437 TYR A CZ  
2886 O OH  . TYR A 363 ? 0.2141 0.2102 0.2065 0.0149  0.0131  0.0225  437 TYR A OH  
2887 N N   . PHE A 364 ? 0.2204 0.2079 0.2114 0.0235  0.0236  0.0311  438 PHE A N   
2888 C CA  . PHE A 364 ? 0.2186 0.2058 0.2109 0.0214  0.0224  0.0300  438 PHE A CA  
2889 C C   . PHE A 364 ? 0.2175 0.2016 0.2061 0.0234  0.0233  0.0295  438 PHE A C   
2890 O O   . PHE A 364 ? 0.2360 0.2193 0.2243 0.0221  0.0221  0.0280  438 PHE A O   
2891 C CB  . PHE A 364 ? 0.2254 0.2143 0.2236 0.0188  0.0228  0.0319  438 PHE A CB  
2892 C CG  . PHE A 364 ? 0.2280 0.2199 0.2296 0.0161  0.0209  0.0315  438 PHE A CG  
2893 C CD1 . PHE A 364 ? 0.2304 0.2232 0.2315 0.0140  0.0182  0.0289  438 PHE A CD1 
2894 C CD2 . PHE A 364 ? 0.2336 0.2278 0.2393 0.0159  0.0219  0.0340  438 PHE A CD2 
2895 C CE1 . PHE A 364 ? 0.2416 0.2370 0.2453 0.0117  0.0166  0.0286  438 PHE A CE1 
2896 C CE2 . PHE A 364 ? 0.2444 0.2413 0.2529 0.0136  0.0201  0.0337  438 PHE A CE2 
2897 C CZ  . PHE A 364 ? 0.2484 0.2459 0.2560 0.0115  0.0175  0.0310  438 PHE A CZ  
2898 N N   . ASP A 365 ? 0.2135 0.1955 0.1985 0.0268  0.0253  0.0306  439 ASP A N   
2899 C CA  . ASP A 365 ? 0.2145 0.1935 0.1953 0.0291  0.0259  0.0299  439 ASP A CA  
2900 C C   . ASP A 365 ? 0.2190 0.1974 0.1958 0.0294  0.0234  0.0266  439 ASP A C   
2901 O O   . ASP A 365 ? 0.2222 0.1987 0.1964 0.0303  0.0231  0.0254  439 ASP A O   
2902 C CB  . ASP A 365 ? 0.2265 0.2034 0.2042 0.0328  0.0285  0.0320  439 ASP A CB  
2903 C CG  . ASP A 365 ? 0.2646 0.2418 0.2462 0.0331  0.0314  0.0356  439 ASP A CG  
2904 O OD1 . ASP A 365 ? 0.3161 0.2940 0.3020 0.0308  0.0316  0.0365  439 ASP A OD1 
2905 O OD2 . ASP A 365 ? 0.2731 0.2495 0.2528 0.0358  0.0335  0.0373  439 ASP A OD2 
2906 N N   . ILE A 366 ? 0.2021 0.1822 0.1786 0.0287  0.0218  0.0251  440 ILE A N   
2907 C CA  . ILE A 366 ? 0.1962 0.1759 0.1694 0.0289  0.0195  0.0221  440 ILE A CA  
2908 C C   . ILE A 366 ? 0.1992 0.1793 0.1738 0.0264  0.0180  0.0204  440 ILE A C   
2909 O O   . ILE A 366 ? 0.2057 0.1841 0.1776 0.0274  0.0173  0.0189  440 ILE A O   
2910 C CB  . ILE A 366 ? 0.2014 0.1829 0.1748 0.0282  0.0183  0.0211  440 ILE A CB  
2911 C CG1 . ILE A 366 ? 0.2053 0.1860 0.1769 0.0309  0.0198  0.0226  440 ILE A CG1 
2912 C CG2 . ILE A 366 ? 0.2098 0.1913 0.1809 0.0279  0.0158  0.0179  440 ILE A CG2 
2913 C CD1 . ILE A 366 ? 0.2031 0.1858 0.1758 0.0299  0.0188  0.0220  440 ILE A CD1 
2914 N N   . SER A 367 ? 0.1874 0.1697 0.1663 0.0234  0.0173  0.0207  441 SER A N   
2915 C CA  . SER A 367 ? 0.2006 0.1832 0.1810 0.0209  0.0159  0.0192  441 SER A CA  
2916 C C   . SER A 367 ? 0.1945 0.1751 0.1751 0.0214  0.0171  0.0201  441 SER A C   
2917 O O   . SER A 367 ? 0.2002 0.1798 0.1797 0.0209  0.0162  0.0185  441 SER A O   
2918 C CB  . SER A 367 ? 0.2104 0.1957 0.1949 0.0177  0.0148  0.0194  441 SER A CB  
2919 O OG  . SER A 367 ? 0.2230 0.2093 0.2106 0.0176  0.0163  0.0221  441 SER A OG  
2920 N N   . SER A 368 ? 0.1971 0.1770 0.1790 0.0225  0.0194  0.0228  442 SER A N   
2921 C CA  . SER A 368 ? 0.2171 0.1947 0.1991 0.0230  0.0207  0.0239  442 SER A CA  
2922 C C   . SER A 368 ? 0.2134 0.1885 0.1905 0.0257  0.0208  0.0226  442 SER A C   
2923 O O   . SER A 368 ? 0.2172 0.1909 0.1938 0.0253  0.0204  0.0217  442 SER A O   
2924 C CB  . SER A 368 ? 0.2392 0.2166 0.2237 0.0239  0.0234  0.0272  442 SER A CB  
2925 O OG  . SER A 368 ? 0.2639 0.2388 0.2482 0.0247  0.0248  0.0282  442 SER A OG  
2926 N N   . ILE A 369 ? 0.2064 0.1808 0.1798 0.0285  0.0211  0.0225  443 ILE A N   
2927 C CA  . ILE A 369 ? 0.2098 0.1817 0.1783 0.0312  0.0209  0.0212  443 ILE A CA  
2928 C C   . ILE A 369 ? 0.1924 0.1648 0.1600 0.0299  0.0184  0.0182  443 ILE A C   
2929 O O   . ILE A 369 ? 0.2053 0.1761 0.1713 0.0305  0.0181  0.0172  443 ILE A O   
2930 C CB  . ILE A 369 ? 0.2163 0.1873 0.1808 0.0343  0.0214  0.0214  443 ILE A CB  
2931 C CG1 . ILE A 369 ? 0.2356 0.2053 0.2000 0.0363  0.0244  0.0246  443 ILE A CG1 
2932 C CG2 . ILE A 369 ? 0.2310 0.2001 0.1906 0.0368  0.0202  0.0194  443 ILE A CG2 
2933 C CD1 . ILE A 369 ? 0.2750 0.2439 0.2359 0.0392  0.0251  0.0251  443 ILE A CD1 
2934 N N   . ILE A 370 ? 0.1931 0.1679 0.1619 0.0281  0.0166  0.0166  444 ILE A N   
2935 C CA  . ILE A 370 ? 0.1877 0.1631 0.1559 0.0270  0.0144  0.0138  444 ILE A CA  
2936 C C   . ILE A 370 ? 0.1832 0.1584 0.1535 0.0248  0.0141  0.0134  444 ILE A C   
2937 O O   . ILE A 370 ? 0.1832 0.1573 0.1519 0.0253  0.0134  0.0118  444 ILE A O   
2938 C CB  . ILE A 370 ? 0.1802 0.1582 0.1497 0.0252  0.0128  0.0126  444 ILE A CB  
2939 C CG1 . ILE A 370 ? 0.1909 0.1688 0.1580 0.0275  0.0128  0.0126  444 ILE A CG1 
2940 C CG2 . ILE A 370 ? 0.1877 0.1665 0.1573 0.0237  0.0108  0.0100  444 ILE A CG2 
2941 C CD1 . ILE A 370 ? 0.1896 0.1698 0.1585 0.0259  0.0120  0.0123  444 ILE A CD1 
2942 N N   . SER A 371 ? 0.1827 0.1588 0.1567 0.0226  0.0148  0.0148  445 SER A N   
2943 C CA  . SER A 371 ? 0.1870 0.1626 0.1631 0.0205  0.0145  0.0145  445 SER A CA  
2944 C C   . SER A 371 ? 0.1905 0.1633 0.1649 0.0223  0.0157  0.0150  445 SER A C   
2945 O O   . SER A 371 ? 0.1940 0.1658 0.1678 0.0217  0.0149  0.0135  445 SER A O   
2946 C CB  . SER A 371 ? 0.1981 0.1750 0.1784 0.0182  0.0150  0.0162  445 SER A CB  
2947 O OG  . SER A 371 ? 0.2370 0.2132 0.2194 0.0161  0.0146  0.0157  445 SER A OG  
2948 N N   . GLN A 372 ? 0.1836 0.1550 0.1570 0.0246  0.0177  0.0171  446 GLN A N   
2949 C CA  . GLN A 372 ? 0.2058 0.1744 0.1776 0.0264  0.0190  0.0179  446 GLN A CA  
2950 C C   . GLN A 372 ? 0.2005 0.1678 0.1680 0.0285  0.0179  0.0159  446 GLN A C   
2951 O O   . GLN A 372 ? 0.2154 0.1809 0.1821 0.0289  0.0180  0.0153  446 GLN A O   
2952 C CB  . GLN A 372 ? 0.2210 0.1883 0.1923 0.0286  0.0215  0.0209  446 GLN A CB  
2953 C CG  . GLN A 372 ? 0.2379 0.2060 0.2140 0.0266  0.0230  0.0233  446 GLN A CG  
2954 C CD  . GLN A 372 ? 0.2852 0.2522 0.2609 0.0291  0.0257  0.0263  446 GLN A CD  
2955 O OE1 . GLN A 372 ? 0.3094 0.2737 0.2827 0.0315  0.0273  0.0273  446 GLN A OE1 
2956 N NE2 . GLN A 372 ? 0.2824 0.2510 0.2595 0.0292  0.0265  0.0277  446 GLN A NE2 
2957 N N   . VAL A 373 ? 0.1977 0.1659 0.1627 0.0299  0.0168  0.0146  447 VAL A N   
2958 C CA  . VAL A 373 ? 0.1884 0.1557 0.1499 0.0318  0.0156  0.0126  447 VAL A CA  
2959 C C   . VAL A 373 ? 0.1914 0.1596 0.1544 0.0296  0.0139  0.0104  447 VAL A C   
2960 O O   . VAL A 373 ? 0.1875 0.1543 0.1489 0.0305  0.0135  0.0093  447 VAL A O   
2961 C CB  . VAL A 373 ? 0.1988 0.1666 0.1575 0.0337  0.0146  0.0118  447 VAL A CB  
2962 C CG1 . VAL A 373 ? 0.2011 0.1680 0.1567 0.0355  0.0131  0.0097  447 VAL A CG1 
2963 C CG2 . VAL A 373 ? 0.2096 0.1761 0.1665 0.0361  0.0165  0.0141  447 VAL A CG2 
2964 N N   . LEU A 374 ? 0.1847 0.1552 0.1503 0.0268  0.0128  0.0095  448 LEU A N   
2965 C CA  . LEU A 374 ? 0.1806 0.1519 0.1475 0.0247  0.0114  0.0075  448 LEU A CA  
2966 C C   . LEU A 374 ? 0.1798 0.1492 0.1476 0.0239  0.0122  0.0079  448 LEU A C   
2967 O O   . LEU A 374 ? 0.1880 0.1567 0.1550 0.0240  0.0114  0.0062  448 LEU A O   
2968 C CB  . LEU A 374 ? 0.1740 0.1479 0.1435 0.0218  0.0104  0.0070  448 LEU A CB  
2969 C CG  . LEU A 374 ? 0.1908 0.1666 0.1596 0.0222  0.0093  0.0061  448 LEU A CG  
2970 C CD1 . LEU A 374 ? 0.2086 0.1867 0.1801 0.0196  0.0089  0.0064  448 LEU A CD1 
2971 C CD2 . LEU A 374 ? 0.1861 0.1623 0.1535 0.0227  0.0078  0.0036  448 LEU A CD2 
2972 N N   . GLU A 375 ? 0.1880 0.1568 0.1579 0.0231  0.0137  0.0100  449 GLU A N   
2973 C CA  . GLU A 375 ? 0.1936 0.1604 0.1647 0.0222  0.0144  0.0104  449 GLU A CA  
2974 C C   . GLU A 375 ? 0.2015 0.1656 0.1698 0.0250  0.0152  0.0105  449 GLU A C   
2975 O O   . GLU A 375 ? 0.2236 0.1861 0.1921 0.0244  0.0153  0.0099  449 GLU A O   
2976 C CB  . GLU A 375 ? 0.2186 0.1852 0.1929 0.0208  0.0158  0.0128  449 GLU A CB  
2977 C CG  . GLU A 375 ? 0.2618 0.2309 0.2395 0.0177  0.0147  0.0126  449 GLU A CG  
2978 C CD  . GLU A 375 ? 0.3271 0.2966 0.3052 0.0154  0.0130  0.0102  449 GLU A CD  
2979 O OE1 . GLU A 375 ? 0.3721 0.3396 0.3506 0.0148  0.0132  0.0098  449 GLU A OE1 
2980 O OE2 . GLU A 375 ? 0.4069 0.3784 0.3846 0.0146  0.0115  0.0087  449 GLU A OE2 
2981 N N   . SER A 376 ? 0.1952 0.1587 0.1606 0.0279  0.0158  0.0113  450 SER A N   
2982 C CA  . SER A 376 ? 0.1922 0.1531 0.1546 0.0309  0.0166  0.0117  450 SER A CA  
2983 C C   . SER A 376 ? 0.1990 0.1600 0.1592 0.0318  0.0149  0.0091  450 SER A C   
2984 O O   . SER A 376 ? 0.2095 0.1684 0.1677 0.0337  0.0153  0.0091  450 SER A O   
2985 C CB  . SER A 376 ? 0.2185 0.1786 0.1784 0.0337  0.0179  0.0135  450 SER A CB  
2986 O OG  . SER A 376 ? 0.2417 0.2029 0.1991 0.0352  0.0165  0.0121  450 SER A OG  
2987 N N   . PHE A 377 ? 0.1920 0.1554 0.1526 0.0306  0.0130  0.0071  451 PHE A N   
2988 C CA  . PHE A 377 ? 0.1899 0.1538 0.1490 0.0316  0.0114  0.0048  451 PHE A CA  
2989 C C   . PHE A 377 ? 0.1926 0.1562 0.1531 0.0299  0.0110  0.0035  451 PHE A C   
2990 O O   . PHE A 377 ? 0.1998 0.1639 0.1628 0.0271  0.0111  0.0034  451 PHE A O   
2991 C CB  . PHE A 377 ? 0.1937 0.1604 0.1532 0.0307  0.0098  0.0034  451 PHE A CB  
2992 C CG  . PHE A 377 ? 0.1903 0.1577 0.1487 0.0317  0.0080  0.0011  451 PHE A CG  
2993 C CD1 . PHE A 377 ? 0.2007 0.1670 0.1562 0.0348  0.0076  0.0009  451 PHE A CD1 
2994 C CD2 . PHE A 377 ? 0.1995 0.1687 0.1599 0.0295  0.0069  -0.0005 451 PHE A CD2 
2995 C CE1 . PHE A 377 ? 0.2106 0.1777 0.1657 0.0355  0.0059  -0.0011 451 PHE A CE1 
2996 C CE2 . PHE A 377 ? 0.2081 0.1782 0.1681 0.0303  0.0055  -0.0025 451 PHE A CE2 
2997 C CZ  . PHE A 377 ? 0.2182 0.1873 0.1757 0.0333  0.0050  -0.0027 451 PHE A CZ  
2998 N N   . ASN A 378 ? 0.1957 0.1584 0.1545 0.0316  0.0104  0.0023  452 ASN A N   
2999 C CA  . ASN A 378 ? 0.1897 0.1520 0.1495 0.0305  0.0100  0.0008  452 ASN A CA  
3000 C C   . ASN A 378 ? 0.1870 0.1512 0.1464 0.0309  0.0082  -0.0013 452 ASN A C   
3001 O O   . ASN A 378 ? 0.2040 0.1684 0.1615 0.0333  0.0075  -0.0017 452 ASN A O   
3002 C CB  . ASN A 378 ? 0.1962 0.1555 0.1547 0.0322  0.0111  0.0015  452 ASN A CB  
3003 C CG  . ASN A 378 ? 0.2147 0.1730 0.1747 0.0303  0.0113  0.0006  452 ASN A CG  
3004 O OD1 . ASN A 378 ? 0.2383 0.1961 0.1975 0.0312  0.0108  -0.0007 452 ASN A OD1 
3005 N ND2 . ASN A 378 ? 0.2037 0.1617 0.1657 0.0278  0.0119  0.0012  452 ASN A ND2 
3006 N N   . SER A 379 ? 0.1879 0.1533 0.1490 0.0287  0.0076  -0.0028 453 SER A N   
3007 C CA  . SER A 379 ? 0.1982 0.1656 0.1597 0.0289  0.0061  -0.0048 453 SER A CA  
3008 C C   . SER A 379 ? 0.2102 0.1766 0.1700 0.0317  0.0057  -0.0054 453 SER A C   
3009 O O   . SER A 379 ? 0.2249 0.1890 0.1840 0.0326  0.0066  -0.0049 453 SER A O   
3010 C CB  . SER A 379 ? 0.2323 0.2005 0.1955 0.0265  0.0060  -0.0062 453 SER A CB  
3011 O OG  . SER A 379 ? 0.2992 0.2686 0.2638 0.0240  0.0060  -0.0058 453 SER A OG  
3012 N N   . GLN A 380 ? 0.2109 0.1792 0.1707 0.0329  0.0042  -0.0066 454 GLN A N   
3013 C CA  . GLN A 380 ? 0.2091 0.1769 0.1678 0.0354  0.0034  -0.0075 454 GLN A CA  
3014 C C   . GLN A 380 ? 0.2305 0.2004 0.1913 0.0346  0.0024  -0.0094 454 GLN A C   
3015 O O   . GLN A 380 ? 0.2629 0.2350 0.2255 0.0327  0.0019  -0.0101 454 GLN A O   
3016 C CB  . GLN A 380 ? 0.2324 0.2004 0.1891 0.0378  0.0024  -0.0072 454 GLN A CB  
3017 C CG  . GLN A 380 ? 0.2497 0.2153 0.2039 0.0393  0.0036  -0.0051 454 GLN A CG  
3018 C CD  . GLN A 380 ? 0.2723 0.2375 0.2237 0.0421  0.0026  -0.0049 454 GLN A CD  
3019 O OE1 . GLN A 380 ? 0.3157 0.2823 0.2672 0.0432  0.0007  -0.0065 454 GLN A OE1 
3020 N NE2 . GLN A 380 ? 0.2912 0.2545 0.2404 0.0433  0.0039  -0.0030 454 GLN A NE2 
3021 N N   . LYS A 381 ? 0.2539 0.2233 0.2145 0.0363  0.0021  -0.0101 455 LYS A N   
3022 C CA  . LYS A 381 ? 0.2953 0.2671 0.2582 0.0359  0.0010  -0.0119 455 LYS A CA  
3023 C C   . LYS A 381 ? 0.2482 0.2223 0.2119 0.0365  -0.0007 -0.0126 455 LYS A C   
3024 O O   . LYS A 381 ? 0.2620 0.2356 0.2238 0.0385  -0.0015 -0.0122 455 LYS A O   
3025 C CB  . LYS A 381 ? 0.3739 0.3448 0.3368 0.0378  0.0010  -0.0124 455 LYS A CB  
3026 C CG  . LYS A 381 ? 0.4593 0.4319 0.4248 0.0368  0.0009  -0.0139 455 LYS A CG  
3027 C CD  . LYS A 381 ? 0.5092 0.4802 0.4746 0.0381  0.0016  -0.0142 455 LYS A CD  
3028 C CE  . LYS A 381 ? 0.5961 0.5665 0.5603 0.0413  0.0006  -0.0139 455 LYS A CE  
3029 N NZ  . LYS A 381 ? 0.6233 0.5935 0.5886 0.0425  0.0008  -0.0147 455 LYS A NZ  
3030 N N   . VAL A 382 ? 0.2877 0.2643 0.2539 0.0346  -0.0012 -0.0137 456 VAL A N   
3031 C CA  . VAL A 382 ? 0.3047 0.2836 0.2721 0.0347  -0.0028 -0.0144 456 VAL A CA  
3032 C C   . VAL A 382 ? 0.2999 0.2800 0.2685 0.0367  -0.0044 -0.0156 456 VAL A C   
3033 O O   . VAL A 382 ? 0.3432 0.3241 0.3139 0.0365  -0.0042 -0.0164 456 VAL A O   
3034 C CB  . VAL A 382 ? 0.3183 0.2994 0.2882 0.0320  -0.0026 -0.0150 456 VAL A CB  
3035 C CG1 . VAL A 382 ? 0.3208 0.3041 0.2922 0.0321  -0.0043 -0.0157 456 VAL A CG1 
3036 C CG2 . VAL A 382 ? 0.3150 0.2951 0.2839 0.0300  -0.0012 -0.0138 456 VAL A CG2 
3037 N N   . SER A 383 ? 0.2833 0.2632 0.2505 0.0388  -0.0060 -0.0157 457 SER A N   
3038 C CA  . SER A 383 ? 0.3170 0.2980 0.2853 0.0408  -0.0079 -0.0168 457 SER A CA  
3039 C C   . SER A 383 ? 0.3618 0.3459 0.3345 0.0392  -0.0086 -0.0182 457 SER A C   
3040 O O   . SER A 383 ? 0.3581 0.3437 0.3323 0.0372  -0.0086 -0.0184 457 SER A O   
3041 C CB  . SER A 383 ? 0.3270 0.3075 0.2932 0.0428  -0.0097 -0.0169 457 SER A CB  
3042 O OG  . SER A 383 ? 0.3810 0.3585 0.3429 0.0447  -0.0091 -0.0156 457 SER A OG  
3043 N N   . GLU A 384 ? 0.3826 0.3678 0.3574 0.0405  -0.0094 -0.0191 458 GLU A N   
3044 C CA  . GLU A 384 ? 0.4038 0.3919 0.3831 0.0391  -0.0096 -0.0201 458 GLU A CA  
3045 C C   . GLU A 384 ? 0.3853 0.3757 0.3671 0.0397  -0.0121 -0.0212 458 GLU A C   
3046 O O   . GLU A 384 ? 0.5205 0.5135 0.5064 0.0382  -0.0123 -0.0220 458 GLU A O   
3047 C CB  . GLU A 384 ? 0.4578 0.4457 0.4382 0.0401  -0.0089 -0.0203 458 GLU A CB  
3048 C CG  . GLU A 384 ? 0.5303 0.5159 0.5086 0.0392  -0.0064 -0.0194 458 GLU A CG  
3049 C CD  . GLU A 384 ? 0.5955 0.5801 0.5740 0.0405  -0.0054 -0.0195 458 GLU A CD  
3050 O OE1 . GLU A 384 ? 0.6004 0.5866 0.5814 0.0420  -0.0065 -0.0202 458 GLU A OE1 
3051 O OE2 . GLU A 384 ? 0.6606 0.6429 0.6371 0.0399  -0.0036 -0.0188 458 GLU A OE2 
3052 N N   . ASN A 385 ? 0.3416 0.3309 0.3211 0.0418  -0.0139 -0.0213 459 ASN A N   
3053 C CA  . ASN A 385 ? 0.3969 0.3875 0.3779 0.0428  -0.0167 -0.0224 459 ASN A CA  
3054 C C   . ASN A 385 ? 0.3891 0.3791 0.3680 0.0420  -0.0171 -0.0222 459 ASN A C   
3055 O O   . ASN A 385 ? 0.3697 0.3572 0.3444 0.0425  -0.0161 -0.0211 459 ASN A O   
3056 C CB  . ASN A 385 ? 0.4336 0.4230 0.4126 0.0460  -0.0183 -0.0226 459 ASN A CB  
3057 C CG  . ASN A 385 ? 0.5021 0.4918 0.4807 0.0477  -0.0214 -0.0236 459 ASN A CG  
3058 O OD1 . ASN A 385 ? 0.4754 0.4631 0.4501 0.0485  -0.0220 -0.0233 459 ASN A OD1 
3059 N ND2 . ASN A 385 ? 0.5950 0.5869 0.5775 0.0485  -0.0235 -0.0248 459 ASN A ND2 
3060 N N   . SER A 386 ? 0.3677 0.3598 0.3498 0.0409  -0.0186 -0.0232 460 SER A N   
3061 C CA  . SER A 386 ? 0.3716 0.3631 0.3521 0.0401  -0.0190 -0.0230 460 SER A CA  
3062 C C   . SER A 386 ? 0.3834 0.3722 0.3589 0.0425  -0.0202 -0.0228 460 SER A C   
3063 O O   . SER A 386 ? 0.3602 0.3473 0.3324 0.0423  -0.0191 -0.0218 460 SER A O   
3064 C CB  . SER A 386 ? 0.3658 0.3599 0.3508 0.0387  -0.0205 -0.0243 460 SER A CB  
3065 O OG  . SER A 386 ? 0.3960 0.3895 0.3795 0.0377  -0.0206 -0.0240 460 SER A OG  
3066 N N   . GLU A 387 ? 0.3732 0.3616 0.3479 0.0451  -0.0224 -0.0236 461 GLU A N   
3067 C CA  . GLU A 387 ? 0.3655 0.3511 0.3350 0.0477  -0.0237 -0.0234 461 GLU A CA  
3068 C C   . GLU A 387 ? 0.3501 0.3328 0.3149 0.0487  -0.0213 -0.0216 461 GLU A C   
3069 O O   . GLU A 387 ? 0.3670 0.3475 0.3276 0.0496  -0.0208 -0.0208 461 GLU A O   
3070 C CB  . GLU A 387 ? 0.4693 0.4553 0.4394 0.0502  -0.0267 -0.0248 461 GLU A CB  
3071 C CG  . GLU A 387 ? 0.5376 0.5204 0.5017 0.0534  -0.0281 -0.0246 461 GLU A CG  
3072 C CD  . GLU A 387 ? 0.6618 0.6448 0.6260 0.0559  -0.0317 -0.0261 461 GLU A CD  
3073 O OE1 . GLU A 387 ? 0.7469 0.7322 0.7152 0.0551  -0.0341 -0.0278 461 GLU A OE1 
3074 O OE2 . GLU A 387 ? 0.7175 0.6986 0.6780 0.0587  -0.0321 -0.0257 461 GLU A OE2 
3075 N N   . ASP A 388 ? 0.3388 0.3215 0.3044 0.0487  -0.0198 -0.0210 462 ASP A N   
3076 C CA  . ASP A 388 ? 0.3333 0.3133 0.2951 0.0494  -0.0174 -0.0192 462 ASP A CA  
3077 C C   . ASP A 388 ? 0.2846 0.2644 0.2461 0.0469  -0.0150 -0.0181 462 ASP A C   
3078 O O   . ASP A 388 ? 0.3056 0.2829 0.2634 0.0476  -0.0135 -0.0166 462 ASP A O   
3079 C CB  . ASP A 388 ? 0.3499 0.3299 0.3128 0.0499  -0.0164 -0.0190 462 ASP A CB  
3080 C CG  . ASP A 388 ? 0.4155 0.3950 0.3774 0.0530  -0.0185 -0.0196 462 ASP A CG  
3081 O OD1 . ASP A 388 ? 0.4385 0.4169 0.3975 0.0551  -0.0204 -0.0199 462 ASP A OD1 
3082 O OD2 . ASP A 388 ? 0.4786 0.4590 0.4428 0.0532  -0.0182 -0.0198 462 ASP A OD2 
3083 N N   . LEU A 389 ? 0.3033 0.2855 0.2688 0.0441  -0.0147 -0.0187 463 LEU A N   
3084 C CA  . LEU A 389 ? 0.2817 0.2639 0.2473 0.0417  -0.0127 -0.0177 463 LEU A CA  
3085 C C   . LEU A 389 ? 0.2808 0.2620 0.2439 0.0420  -0.0131 -0.0172 463 LEU A C   
3086 O O   . LEU A 389 ? 0.2681 0.2477 0.2288 0.0417  -0.0114 -0.0157 463 LEU A O   
3087 C CB  . LEU A 389 ? 0.2622 0.2472 0.2323 0.0389  -0.0123 -0.0184 463 LEU A CB  
3088 C CG  . LEU A 389 ? 0.2641 0.2494 0.2345 0.0363  -0.0105 -0.0175 463 LEU A CG  
3089 C CD1 . LEU A 389 ? 0.2659 0.2490 0.2339 0.0361  -0.0083 -0.0159 463 LEU A CD1 
3090 C CD2 . LEU A 389 ? 0.2616 0.2494 0.2361 0.0339  -0.0101 -0.0182 463 LEU A CD2 
3091 N N   . MET A 390 ? 0.2830 0.2648 0.2463 0.0430  -0.0154 -0.0184 464 MET A N   
3092 C CA  . MET A 390 ? 0.2859 0.2663 0.2462 0.0438  -0.0159 -0.0181 464 MET A CA  
3093 C C   . MET A 390 ? 0.2795 0.2567 0.2346 0.0465  -0.0152 -0.0168 464 MET A C   
3094 O O   . MET A 390 ? 0.2782 0.2538 0.2306 0.0467  -0.0139 -0.0155 464 MET A O   
3095 C CB  . MET A 390 ? 0.3148 0.2961 0.2762 0.0445  -0.0188 -0.0199 464 MET A CB  
3096 C CG  . MET A 390 ? 0.3566 0.3366 0.3153 0.0450  -0.0192 -0.0197 464 MET A CG  
3097 S SD  . MET A 390 ? 0.3830 0.3632 0.3420 0.0424  -0.0166 -0.0181 464 MET A SD  
3098 C CE  . MET A 390 ? 0.4177 0.4014 0.3828 0.0388  -0.0164 -0.0189 464 MET A CE  
3099 N N   . LYS A 391 ? 0.2962 0.2723 0.2496 0.0489  -0.0160 -0.0171 465 LYS A N   
3100 C CA  . LYS A 391 ? 0.2747 0.2476 0.2230 0.0516  -0.0151 -0.0157 465 LYS A CA  
3101 C C   . LYS A 391 ? 0.2483 0.2199 0.1958 0.0504  -0.0119 -0.0136 465 LYS A C   
3102 O O   . LYS A 391 ? 0.2659 0.2353 0.2098 0.0517  -0.0106 -0.0121 465 LYS A O   
3103 C CB  . LYS A 391 ? 0.3345 0.3065 0.2814 0.0542  -0.0164 -0.0161 465 LYS A CB  
3104 C CG  . LYS A 391 ? 0.4151 0.3873 0.3612 0.0563  -0.0198 -0.0179 465 LYS A CG  
3105 C CD  . LYS A 391 ? 0.5011 0.4721 0.4453 0.0593  -0.0210 -0.0181 465 LYS A CD  
3106 C CE  . LYS A 391 ? 0.5764 0.5482 0.5209 0.0609  -0.0247 -0.0201 465 LYS A CE  
3107 N NZ  . LYS A 391 ? 0.6133 0.5842 0.5563 0.0637  -0.0260 -0.0203 465 LYS A NZ  
3108 N N   . GLN A 392 ? 0.2593 0.2326 0.2103 0.0481  -0.0108 -0.0136 466 GLN A N   
3109 C CA  . GLN A 392 ? 0.2589 0.2312 0.2099 0.0467  -0.0080 -0.0119 466 GLN A CA  
3110 C C   . GLN A 392 ? 0.2444 0.2171 0.1957 0.0447  -0.0069 -0.0109 466 GLN A C   
3111 O O   . GLN A 392 ? 0.2259 0.1968 0.1751 0.0450  -0.0050 -0.0091 466 GLN A O   
3112 C CB  . GLN A 392 ? 0.2626 0.2366 0.2174 0.0446  -0.0075 -0.0125 466 GLN A CB  
3113 C CG  . GLN A 392 ? 0.2790 0.2520 0.2340 0.0429  -0.0050 -0.0110 466 GLN A CG  
3114 C CD  . GLN A 392 ? 0.2917 0.2657 0.2495 0.0417  -0.0046 -0.0118 466 GLN A CD  
3115 O OE1 . GLN A 392 ? 0.2803 0.2566 0.2410 0.0408  -0.0058 -0.0133 466 GLN A OE1 
3116 N NE2 . GLN A 392 ? 0.2766 0.2490 0.2339 0.0411  -0.0027 -0.0107 466 GLN A NE2 
3117 N N   . ILE A 393 ? 0.2431 0.2181 0.1969 0.0430  -0.0080 -0.0121 467 ILE A N   
3118 C CA  . ILE A 393 ? 0.2298 0.2051 0.1838 0.0414  -0.0072 -0.0113 467 ILE A CA  
3119 C C   . ILE A 393 ? 0.2320 0.2051 0.1819 0.0438  -0.0070 -0.0103 467 ILE A C   
3120 O O   . ILE A 393 ? 0.2355 0.2076 0.1843 0.0434  -0.0051 -0.0086 467 ILE A O   
3121 C CB  . ILE A 393 ? 0.2274 0.2054 0.1847 0.0395  -0.0086 -0.0128 467 ILE A CB  
3122 C CG1 . ILE A 393 ? 0.2382 0.2182 0.1993 0.0370  -0.0080 -0.0133 467 ILE A CG1 
3123 C CG2 . ILE A 393 ? 0.2377 0.2159 0.1948 0.0384  -0.0080 -0.0121 467 ILE A CG2 
3124 C CD1 . ILE A 393 ? 0.2420 0.2247 0.2067 0.0355  -0.0095 -0.0149 467 ILE A CD1 
3125 N N   . LEU A 394 ? 0.2491 0.2212 0.1966 0.0464  -0.0090 -0.0114 468 LEU A N   
3126 C CA  . LEU A 394 ? 0.2631 0.2327 0.2061 0.0489  -0.0089 -0.0106 468 LEU A CA  
3127 C C   . LEU A 394 ? 0.2404 0.2075 0.1802 0.0505  -0.0066 -0.0084 468 LEU A C   
3128 O O   . LEU A 394 ? 0.2495 0.2150 0.1869 0.0513  -0.0051 -0.0068 468 LEU A O   
3129 C CB  . LEU A 394 ? 0.2924 0.2614 0.2333 0.0515  -0.0118 -0.0123 468 LEU A CB  
3130 C CG  . LEU A 394 ? 0.3878 0.3588 0.3314 0.0504  -0.0143 -0.0144 468 LEU A CG  
3131 C CD1 . LEU A 394 ? 0.4114 0.3820 0.3538 0.0527  -0.0174 -0.0164 468 LEU A CD1 
3132 C CD2 . LEU A 394 ? 0.4270 0.3972 0.3689 0.0503  -0.0139 -0.0140 468 LEU A CD2 
3133 N N   . GLN A 395 ? 0.2513 0.2178 0.1912 0.0512  -0.0064 -0.0083 469 GLN A N   
3134 C CA  . GLN A 395 ? 0.2624 0.2263 0.1995 0.0528  -0.0042 -0.0062 469 GLN A CA  
3135 C C   . GLN A 395 ? 0.2189 0.1831 0.1580 0.0503  -0.0015 -0.0043 469 GLN A C   
3136 O O   . GLN A 395 ? 0.2289 0.1911 0.1656 0.0514  0.0003  -0.0023 469 GLN A O   
3137 C CB  . GLN A 395 ? 0.2853 0.2487 0.2226 0.0538  -0.0045 -0.0066 469 GLN A CB  
3138 C CG  . GLN A 395 ? 0.2976 0.2583 0.2325 0.0552  -0.0021 -0.0043 469 GLN A CG  
3139 C CD  . GLN A 395 ? 0.2837 0.2449 0.2218 0.0524  0.0000  -0.0032 469 GLN A CD  
3140 O OE1 . GLN A 395 ? 0.3278 0.2909 0.2693 0.0503  -0.0004 -0.0044 469 GLN A OE1 
3141 N NE2 . GLN A 395 ? 0.3003 0.2596 0.2372 0.0525  0.0025  -0.0009 469 GLN A NE2 
3142 N N   . ILE A 396 ? 0.2296 0.1962 0.1730 0.0471  -0.0014 -0.0050 470 ILE A N   
3143 C CA  . ILE A 396 ? 0.2260 0.1930 0.1715 0.0446  0.0006  -0.0034 470 ILE A CA  
3144 C C   . ILE A 396 ? 0.2054 0.1727 0.1506 0.0441  0.0012  -0.0025 470 ILE A C   
3145 O O   . ILE A 396 ? 0.2098 0.1761 0.1546 0.0439  0.0032  -0.0005 470 ILE A O   
3146 C CB  . ILE A 396 ? 0.2169 0.1861 0.1666 0.0415  0.0004  -0.0045 470 ILE A CB  
3147 C CG1 . ILE A 396 ? 0.2219 0.1903 0.1717 0.0421  0.0005  -0.0049 470 ILE A CG1 
3148 C CG2 . ILE A 396 ? 0.2173 0.1872 0.1693 0.0387  0.0021  -0.0032 470 ILE A CG2 
3149 C CD1 . ILE A 396 ? 0.2412 0.2117 0.1946 0.0396  0.0000  -0.0063 470 ILE A CD1 
3150 N N   . HIS A 397 ? 0.2134 0.1820 0.1587 0.0441  -0.0005 -0.0040 471 HIS A N   
3151 C CA  . HIS A 397 ? 0.2194 0.1882 0.1642 0.0439  -0.0001 -0.0033 471 HIS A CA  
3152 C C   . HIS A 397 ? 0.2225 0.1885 0.1630 0.0469  0.0011  -0.0015 471 HIS A C   
3153 O O   . HIS A 397 ? 0.2170 0.1824 0.1573 0.0466  0.0030  0.0002  471 HIS A O   
3154 C CB  . HIS A 397 ? 0.2404 0.2106 0.1856 0.0438  -0.0025 -0.0053 471 HIS A CB  
3155 C CG  . HIS A 397 ? 0.3125 0.2819 0.2556 0.0449  -0.0025 -0.0050 471 HIS A CG  
3156 N ND1 . HIS A 397 ? 0.2693 0.2402 0.2150 0.0425  -0.0016 -0.0042 471 HIS A ND1 
3157 C CD2 . HIS A 397 ? 0.3406 0.3081 0.2800 0.0476  -0.0033 -0.0052 471 HIS A CD2 
3158 C CE1 . HIS A 397 ? 0.2926 0.2630 0.2366 0.0435  -0.0017 -0.0040 471 HIS A CE1 
3159 N NE2 . HIS A 397 ? 0.3243 0.2923 0.2642 0.0467  -0.0027 -0.0046 471 HIS A NE2 
3160 N N   . SER A 398 ? 0.2363 0.2002 0.1730 0.0500  0.0001  -0.0021 472 SER A N   
3161 C CA  . SER A 398 ? 0.2508 0.2117 0.1828 0.0532  0.0013  -0.0005 472 SER A CA  
3162 C C   . SER A 398 ? 0.2310 0.1905 0.1629 0.0533  0.0043  0.0020  472 SER A C   
3163 O O   . SER A 398 ? 0.2386 0.1966 0.1687 0.0544  0.0063  0.0040  472 SER A O   
3164 C CB  . SER A 398 ? 0.3025 0.2617 0.2307 0.0564  -0.0005 -0.0018 472 SER A CB  
3165 O OG  . SER A 398 ? 0.3980 0.3582 0.3262 0.0564  -0.0031 -0.0040 472 SER A OG  
3166 N N   . TRP A 399 ? 0.2216 0.1815 0.1557 0.0521  0.0046  0.0019  473 TRP A N   
3167 C CA  . TRP A 399 ? 0.2371 0.1957 0.1718 0.0518  0.0072  0.0042  473 TRP A CA  
3168 C C   . TRP A 399 ? 0.2220 0.1819 0.1598 0.0492  0.0090  0.0058  473 TRP A C   
3169 O O   . TRP A 399 ? 0.2260 0.1845 0.1634 0.0498  0.0113  0.0082  473 TRP A O   
3170 C CB  . TRP A 399 ? 0.2362 0.1951 0.1732 0.0505  0.0070  0.0036  473 TRP A CB  
3171 C CG  . TRP A 399 ? 0.2469 0.2051 0.1860 0.0489  0.0095  0.0057  473 TRP A CG  
3172 C CD1 . TRP A 399 ? 0.2393 0.1948 0.1764 0.0508  0.0117  0.0079  473 TRP A CD1 
3173 C CD2 . TRP A 399 ? 0.2272 0.1873 0.1708 0.0453  0.0102  0.0059  473 TRP A CD2 
3174 N NE1 . TRP A 399 ? 0.2344 0.1901 0.1748 0.0485  0.0137  0.0095  473 TRP A NE1 
3175 C CE2 . TRP A 399 ? 0.2228 0.1814 0.1672 0.0450  0.0127  0.0083  473 TRP A CE2 
3176 C CE3 . TRP A 399 ? 0.2167 0.1796 0.1636 0.0422  0.0090  0.0044  473 TRP A CE3 
3177 C CZ2 . TRP A 399 ? 0.2280 0.1876 0.1763 0.0419  0.0137  0.0091  473 TRP A CZ2 
3178 C CZ3 . TRP A 399 ? 0.2253 0.1892 0.1758 0.0393  0.0100  0.0052  473 TRP A CZ3 
3179 C CH2 . TRP A 399 ? 0.2278 0.1901 0.1790 0.0390  0.0122  0.0075  473 TRP A CH2 
3180 N N   . ALA A 400 ? 0.2135 0.1762 0.1550 0.0462  0.0078  0.0044  474 ALA A N   
3181 C CA  . ALA A 400 ? 0.2135 0.1777 0.1583 0.0435  0.0091  0.0057  474 ALA A CA  
3182 C C   . ALA A 400 ? 0.2009 0.1646 0.1439 0.0449  0.0102  0.0071  474 ALA A C   
3183 O O   . ALA A 400 ? 0.2158 0.1794 0.1603 0.0442  0.0122  0.0093  474 ALA A O   
3184 C CB  . ALA A 400 ? 0.2071 0.1742 0.1555 0.0403  0.0076  0.0039  474 ALA A CB  
3185 N N   . LYS A 401 ? 0.2151 0.1782 0.1549 0.0471  0.0087  0.0059  475 LYS A N   
3186 C CA  . LYS A 401 ? 0.2378 0.1997 0.1751 0.0489  0.0098  0.0072  475 LYS A CA  
3187 C C   . LYS A 401 ? 0.2307 0.1897 0.1650 0.0516  0.0123  0.0097  475 LYS A C   
3188 O O   . LYS A 401 ? 0.2541 0.2126 0.1885 0.0519  0.0145  0.0120  475 LYS A O   
3189 C CB  . LYS A 401 ? 0.2598 0.2212 0.1939 0.0508  0.0076  0.0052  475 LYS A CB  
3190 C CG  . LYS A 401 ? 0.2692 0.2334 0.2064 0.0483  0.0055  0.0031  475 LYS A CG  
3191 C CD  . LYS A 401 ? 0.3221 0.2857 0.2567 0.0499  0.0037  0.0016  475 LYS A CD  
3192 C CE  . LYS A 401 ? 0.4222 0.3839 0.3528 0.0528  0.0017  0.0000  475 LYS A CE  
3193 N NZ  . LYS A 401 ? 0.5023 0.4629 0.4299 0.0546  0.0004  -0.0010 475 LYS A NZ  
3194 N N   . ASP A 402 ? 0.2442 0.2013 0.1758 0.0536  0.0120  0.0094  476 ASP A N   
3195 C CA  . ASP A 402 ? 0.2686 0.2227 0.1971 0.0564  0.0144  0.0118  476 ASP A CA  
3196 C C   . ASP A 402 ? 0.2427 0.1973 0.1750 0.0543  0.0170  0.0142  476 ASP A C   
3197 O O   . ASP A 402 ? 0.2862 0.2394 0.2179 0.0556  0.0196  0.0169  476 ASP A O   
3198 C CB  . ASP A 402 ? 0.2928 0.2449 0.2180 0.0588  0.0135  0.0110  476 ASP A CB  
3199 C CG  . ASP A 402 ? 0.3355 0.2863 0.2558 0.0618  0.0111  0.0091  476 ASP A CG  
3200 O OD1 . ASP A 402 ? 0.3726 0.3233 0.2911 0.0627  0.0106  0.0087  476 ASP A OD1 
3201 O OD2 . ASP A 402 ? 0.3829 0.3329 0.3017 0.0631  0.0096  0.0079  476 ASP A OD2 
3202 N N   . LYS A 403 ? 0.2409 0.1975 0.1777 0.0510  0.0163  0.0133  477 LYS A N   
3203 C CA  . LYS A 403 ? 0.2403 0.1973 0.1811 0.0487  0.0183  0.0153  477 LYS A CA  
3204 C C   . LYS A 403 ? 0.2480 0.2065 0.1915 0.0472  0.0197  0.0169  477 LYS A C   
3205 O O   . LYS A 403 ? 0.2601 0.2180 0.2052 0.0471  0.0222  0.0196  477 LYS A O   
3206 C CB  . LYS A 403 ? 0.2447 0.2035 0.1893 0.0455  0.0169  0.0136  477 LYS A CB  
3207 C CG  . LYS A 403 ? 0.2497 0.2086 0.1983 0.0431  0.0185  0.0152  477 LYS A CG  
3208 C CD  . LYS A 403 ? 0.3304 0.2864 0.2779 0.0446  0.0205  0.0169  477 LYS A CD  
3209 C CE  . LYS A 403 ? 0.3521 0.3086 0.3043 0.0420  0.0222  0.0188  477 LYS A CE  
3210 N NZ  . LYS A 403 ? 0.3913 0.3450 0.3434 0.0429  0.0242  0.0206  477 LYS A NZ  
3211 N N   . ALA A 404 ? 0.2380 0.1987 0.1825 0.0459  0.0180  0.0154  478 ALA A N   
3212 C CA  . ALA A 404 ? 0.2317 0.1938 0.1784 0.0448  0.0192  0.0169  478 ALA A CA  
3213 C C   . ALA A 404 ? 0.2333 0.1933 0.1770 0.0480  0.0215  0.0193  478 ALA A C   
3214 O O   . ALA A 404 ? 0.2531 0.2135 0.1993 0.0473  0.0237  0.0217  478 ALA A O   
3215 C CB  . ALA A 404 ? 0.2173 0.1818 0.1649 0.0433  0.0169  0.0148  478 ALA A CB  
3216 N N   . THR A 405 ? 0.2498 0.2077 0.1880 0.0513  0.0208  0.0184  479 THR A N   
3217 C CA  . THR A 405 ? 0.2715 0.2269 0.2059 0.0548  0.0230  0.0205  479 THR A CA  
3218 C C   . THR A 405 ? 0.2896 0.2430 0.2241 0.0559  0.0260  0.0233  479 THR A C   
3219 O O   . THR A 405 ? 0.3063 0.2590 0.2410 0.0570  0.0287  0.0261  479 THR A O   
3220 C CB  . THR A 405 ? 0.2887 0.2420 0.2170 0.0581  0.0212  0.0186  479 THR A CB  
3221 O OG1 . THR A 405 ? 0.3033 0.2585 0.2321 0.0569  0.0188  0.0163  479 THR A OG1 
3222 C CG2 . THR A 405 ? 0.3150 0.2652 0.2381 0.0621  0.0234  0.0205  479 THR A CG2 
3223 N N   . ASP A 406 ? 0.2857 0.2385 0.2206 0.0554  0.0254  0.0227  480 ASP A N   
3224 C CA  . ASP A 406 ? 0.3347 0.2855 0.2699 0.0563  0.0281  0.0253  480 ASP A CA  
3225 C C   . ASP A 406 ? 0.3179 0.2704 0.2591 0.0534  0.0302  0.0276  480 ASP A C   
3226 O O   . ASP A 406 ? 0.3560 0.3072 0.2977 0.0546  0.0332  0.0306  480 ASP A O   
3227 C CB  . ASP A 406 ? 0.3784 0.3281 0.3129 0.0563  0.0269  0.0240  480 ASP A CB  
3228 C CG  . ASP A 406 ? 0.4911 0.4378 0.4239 0.0585  0.0294  0.0264  480 ASP A CG  
3229 O OD1 . ASP A 406 ? 0.5241 0.4684 0.4526 0.0620  0.0313  0.0282  480 ASP A OD1 
3230 O OD2 . ASP A 406 ? 0.5574 0.5040 0.4927 0.0568  0.0294  0.0262  480 ASP A OD2 
3231 N N   . ILE A 407 ? 0.3063 0.2619 0.2524 0.0495  0.0285  0.0263  481 ILE A N   
3232 C CA  . ILE A 407 ? 0.2988 0.2563 0.2508 0.0465  0.0299  0.0281  481 ILE A CA  
3233 C C   . ILE A 407 ? 0.3125 0.2704 0.2649 0.0476  0.0319  0.0304  481 ILE A C   
3234 O O   . ILE A 407 ? 0.3410 0.2989 0.2965 0.0473  0.0345  0.0333  481 ILE A O   
3235 C CB  . ILE A 407 ? 0.3041 0.2647 0.2604 0.0425  0.0274  0.0259  481 ILE A CB  
3236 C CG1 . ILE A 407 ? 0.2930 0.2529 0.2497 0.0413  0.0261  0.0243  481 ILE A CG1 
3237 C CG2 . ILE A 407 ? 0.2991 0.2619 0.2612 0.0395  0.0283  0.0276  481 ILE A CG2 
3238 C CD1 . ILE A 407 ? 0.3081 0.2704 0.2666 0.0384  0.0232  0.0214  481 ILE A CD1 
3239 N N   . TYR A 408 ? 0.2987 0.2572 0.2482 0.0488  0.0306  0.0290  482 TYR A N   
3240 C CA  . TYR A 408 ? 0.2958 0.2543 0.2447 0.0504  0.0325  0.0309  482 TYR A CA  
3241 C C   . TYR A 408 ? 0.3314 0.2867 0.2771 0.0540  0.0358  0.0338  482 TYR A C   
3242 O O   . TYR A 408 ? 0.3706 0.3264 0.3191 0.0540  0.0385  0.0367  482 TYR A O   
3243 C CB  . TYR A 408 ? 0.2920 0.2510 0.2375 0.0515  0.0304  0.0287  482 TYR A CB  
3244 C CG  . TYR A 408 ? 0.2995 0.2574 0.2426 0.0541  0.0325  0.0305  482 TYR A CG  
3245 C CD1 . TYR A 408 ? 0.2976 0.2576 0.2450 0.0527  0.0341  0.0326  482 TYR A CD1 
3246 C CD2 . TYR A 408 ? 0.3185 0.2732 0.2549 0.0583  0.0329  0.0303  482 TYR A CD2 
3247 C CE1 . TYR A 408 ? 0.3049 0.2638 0.2502 0.0553  0.0363  0.0344  482 TYR A CE1 
3248 C CE2 . TYR A 408 ? 0.3316 0.2850 0.2652 0.0610  0.0350  0.0320  482 TYR A CE2 
3249 C CZ  . TYR A 408 ? 0.3227 0.2783 0.2609 0.0595  0.0367  0.0341  482 TYR A CZ  
3250 O OH  . TYR A 408 ? 0.3414 0.2957 0.2772 0.0622  0.0390  0.0359  482 TYR A OH  
3251 N N   . ASN A 409 ? 0.3362 0.2886 0.2760 0.0571  0.0354  0.0329  483 ASN A N   
3252 C CA  . ASN A 409 ? 0.3602 0.3092 0.2957 0.0611  0.0383  0.0354  483 ASN A CA  
3253 C C   . ASN A 409 ? 0.4221 0.3708 0.3620 0.0601  0.0413  0.0385  483 ASN A C   
3254 O O   . ASN A 409 ? 0.4383 0.3853 0.3772 0.0625  0.0446  0.0416  483 ASN A O   
3255 C CB  . ASN A 409 ? 0.3936 0.3396 0.3225 0.0642  0.0369  0.0336  483 ASN A CB  
3256 C CG  . ASN A 409 ? 0.3613 0.3067 0.2851 0.0663  0.0348  0.0314  483 ASN A CG  
3257 O OD1 . ASN A 409 ? 0.4254 0.3716 0.3492 0.0666  0.0355  0.0319  483 ASN A OD1 
3258 N ND2 . ASN A 409 ? 0.4467 0.3906 0.3660 0.0679  0.0323  0.0289  483 ASN A ND2 
3259 N N   . LYS A 410 ? 0.4888 0.4390 0.4334 0.0567  0.0401  0.0377  484 LYS A N   
3260 C CA  . LYS A 410 ? 0.5770 0.5266 0.5257 0.0555  0.0425  0.0403  484 LYS A CA  
3261 C C   . LYS A 410 ? 0.6976 0.6495 0.6526 0.0533  0.0444  0.0428  484 LYS A C   
3262 O O   . LYS A 410 ? 0.7836 0.7343 0.7406 0.0542  0.0477  0.0461  484 LYS A O   
3263 C CB  . LYS A 410 ? 0.5888 0.5388 0.5399 0.0528  0.0404  0.0383  484 LYS A CB  
3264 C CG  . LYS A 410 ? 0.6725 0.6225 0.6293 0.0505  0.0422  0.0405  484 LYS A CG  
3265 C CD  . LYS A 410 ? 0.7542 0.7023 0.7104 0.0503  0.0416  0.0396  484 LYS A CD  
3266 C CE  . LYS A 410 ? 0.7849 0.7315 0.7448 0.0498  0.0445  0.0426  484 LYS A CE  
3267 N NZ  . LYS A 410 ? 0.8359 0.7796 0.7932 0.0511  0.0446  0.0422  484 LYS A NZ  
3268 N N   . HIS A 411 ? 0.7368 0.6920 0.6952 0.0506  0.0426  0.0415  485 HIS A N   
3269 C CA  . HIS A 411 ? 0.8053 0.7629 0.7700 0.0483  0.0441  0.0438  485 HIS A CA  
3270 C C   . HIS A 411 ? 0.8550 0.8119 0.8180 0.0514  0.0470  0.0465  485 HIS A C   
3271 O O   . HIS A 411 ? 0.9672 0.9255 0.9351 0.0504  0.0493  0.0493  485 HIS A O   
3272 C CB  . HIS A 411 ? 0.8981 0.8594 0.8668 0.0445  0.0411  0.0416  485 HIS A CB  
3273 C CG  . HIS A 411 ? 1.0230 0.9870 0.9993 0.0413  0.0419  0.0435  485 HIS A CG  
3274 N ND1 . HIS A 411 ? 1.0672 1.0316 1.0483 0.0385  0.0417  0.0439  485 HIS A ND1 
3275 C CD2 . HIS A 411 ? 1.0380 1.0044 1.0179 0.0405  0.0427  0.0451  485 HIS A CD2 
3276 C CE1 . HIS A 411 ? 1.0317 0.9986 1.0192 0.0360  0.0423  0.0457  485 HIS A CE1 
3277 N NE2 . HIS A 411 ? 1.0300 0.9983 1.0170 0.0371  0.0429  0.0464  485 HIS A NE2 
3278 N N   . ASN A 412 ? 0.8390 0.7937 0.7948 0.0551  0.0469  0.0455  486 ASN A N   
3279 C CA  . ASN A 412 ? 0.8833 0.8362 0.8357 0.0588  0.0500  0.0480  486 ASN A CA  
3280 C C   . ASN A 412 ? 0.9595 0.9092 0.9100 0.0617  0.0535  0.0510  486 ASN A C   
3281 O O   . ASN A 412 ? 0.9748 0.9230 0.9248 0.0614  0.0529  0.0504  486 ASN A O   
3282 C CB  . ASN A 412 ? 0.8370 0.7883 0.7820 0.0618  0.0484  0.0457  486 ASN A CB  
3283 C CG  . ASN A 412 ? 0.7830 0.7370 0.7297 0.0603  0.0467  0.0443  486 ASN A CG  
3284 O OD1 . ASN A 412 ? 0.8272 0.7845 0.7800 0.0564  0.0455  0.0440  486 ASN A OD1 
3285 N ND2 . ASN A 412 ? 0.8143 0.7667 0.7553 0.0633  0.0466  0.0436  486 ASN A ND2 
# 
