data_8VMM
# 
_entry.id   8VMM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8VMM         pdb_00008vmm 10.2210/pdb8vmm/pdb 
WWPDB D_1000280596 ?            ?                   
# 
_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       2025-01-15 
# 
_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                        8VMM 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yxf423@med.miami.edu 
_pdbx_contact_author.name_first         Yangbo 
_pdbx_contact_author.name_last          Feng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5894-9476 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Park, H.' 1 ? 
'Feng, Y.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'A structural study of selectivity mechanisms for JNK3 and p38 alpha with indazole scaffold probing compounds' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Park, H.' 1 ? 
primary 'Feng, Y.' 2 ? 
# 
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 'Mitogen-activated protein kinase 14'                                                           42238.117 1   
2.7.11.24 ? ? ? 
2 non-polymer syn 'octyl beta-D-glucopyranoside'                                                                  292.369   2   ? 
? ? ? 
3 non-polymer syn '(4P)-4-[6-fluoro-5-(2-methoxyanilino)-1H-indazol-1-yl]-N-(oxetan-3-yl)thiophene-2-carboxamide' 438.475   1   ? 
? ? ? 
4 water       nat water                                                                                           18.015    103 ? 
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'MAP kinase 14,MAPK 14,CRK1,Mitogen-activated protein kinase p38 alpha,MAP kinase p38 alpha' 
# 
_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       
;MAHHHHHHSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELR
LLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKP
SNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLK
LILRLVGTPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD
PDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELR
LLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKP
SNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLK
LILRLVGTPGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHD
PDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
;
_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 'octyl beta-D-glucopyranoside'                                                                  BOG   
3 '(4P)-4-[6-fluoro-5-(2-methoxyanilino)-1H-indazol-1-yl]-N-(oxetan-3-yl)thiophene-2-carboxamide' A1ACP 
4 water                                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   SER n 
1 10  GLN n 
1 11  GLU n 
1 12  ARG n 
1 13  PRO n 
1 14  THR n 
1 15  PHE n 
1 16  TYR n 
1 17  ARG n 
1 18  GLN n 
1 19  GLU n 
1 20  LEU n 
1 21  ASN n 
1 22  LYS n 
1 23  THR n 
1 24  ILE n 
1 25  TRP n 
1 26  GLU n 
1 27  VAL n 
1 28  PRO n 
1 29  GLU n 
1 30  ARG n 
1 31  TYR n 
1 32  GLN n 
1 33  ASN n 
1 34  LEU n 
1 35  SER n 
1 36  PRO n 
1 37  VAL n 
1 38  GLY n 
1 39  SER n 
1 40  GLY n 
1 41  ALA n 
1 42  TYR n 
1 43  GLY n 
1 44  SER n 
1 45  VAL n 
1 46  CYS n 
1 47  ALA n 
1 48  ALA n 
1 49  PHE n 
1 50  ASP n 
1 51  THR n 
1 52  LYS n 
1 53  THR n 
1 54  GLY n 
1 55  HIS n 
1 56  ARG n 
1 57  VAL n 
1 58  ALA n 
1 59  VAL n 
1 60  LYS n 
1 61  LYS n 
1 62  LEU n 
1 63  SER n 
1 64  ARG n 
1 65  PRO n 
1 66  PHE n 
1 67  GLN n 
1 68  SER n 
1 69  ILE n 
1 70  ILE n 
1 71  HIS n 
1 72  ALA n 
1 73  LYS n 
1 74  ARG n 
1 75  THR n 
1 76  TYR n 
1 77  ARG n 
1 78  GLU n 
1 79  LEU n 
1 80  ARG n 
1 81  LEU n 
1 82  LEU n 
1 83  LYS n 
1 84  HIS n 
1 85  MET n 
1 86  LYS n 
1 87  HIS n 
1 88  GLU n 
1 89  ASN n 
1 90  VAL n 
1 91  ILE n 
1 92  GLY n 
1 93  LEU n 
1 94  LEU n 
1 95  ASP n 
1 96  VAL n 
1 97  PHE n 
1 98  THR n 
1 99  PRO n 
1 100 ALA n 
1 101 ARG n 
1 102 SER n 
1 103 LEU n 
1 104 GLU n 
1 105 GLU n 
1 106 PHE n 
1 107 ASN n 
1 108 ASP n 
1 109 VAL n 
1 110 TYR n 
1 111 LEU n 
1 112 VAL n 
1 113 THR n 
1 114 HIS n 
1 115 LEU n 
1 116 MET n 
1 117 GLY n 
1 118 ALA n 
1 119 ASP n 
1 120 LEU n 
1 121 ASN n 
1 122 ASN n 
1 123 ILE n 
1 124 VAL n 
1 125 LYS n 
1 126 CYS n 
1 127 GLN n 
1 128 LYS n 
1 129 LEU n 
1 130 THR n 
1 131 ASP n 
1 132 ASP n 
1 133 HIS n 
1 134 VAL n 
1 135 GLN n 
1 136 PHE n 
1 137 LEU n 
1 138 ILE n 
1 139 TYR n 
1 140 GLN n 
1 141 ILE n 
1 142 LEU n 
1 143 ARG n 
1 144 GLY n 
1 145 LEU n 
1 146 LYS n 
1 147 TYR n 
1 148 ILE n 
1 149 HIS n 
1 150 SER n 
1 151 ALA n 
1 152 ASP n 
1 153 ILE n 
1 154 ILE n 
1 155 HIS n 
1 156 ARG n 
1 157 ASP n 
1 158 LEU n 
1 159 LYS n 
1 160 PRO n 
1 161 SER n 
1 162 ASN n 
1 163 LEU n 
1 164 ALA n 
1 165 VAL n 
1 166 ASN n 
1 167 GLU n 
1 168 ASP n 
1 169 CYS n 
1 170 GLU n 
1 171 LEU n 
1 172 LYS n 
1 173 ILE n 
1 174 LEU n 
1 175 ASP n 
1 176 PHE n 
1 177 GLY n 
1 178 LEU n 
1 179 ALA n 
1 180 ARG n 
1 181 HIS n 
1 182 THR n 
1 183 ASP n 
1 184 ASP n 
1 185 GLU n 
1 186 MET n 
1 187 THR n 
1 188 GLY n 
1 189 TYR n 
1 190 VAL n 
1 191 ALA n 
1 192 THR n 
1 193 ARG n 
1 194 TRP n 
1 195 TYR n 
1 196 ARG n 
1 197 ALA n 
1 198 PRO n 
1 199 GLU n 
1 200 ILE n 
1 201 MET n 
1 202 LEU n 
1 203 ASN n 
1 204 TRP n 
1 205 MET n 
1 206 HIS n 
1 207 TYR n 
1 208 ASN n 
1 209 GLN n 
1 210 THR n 
1 211 VAL n 
1 212 ASP n 
1 213 ILE n 
1 214 TRP n 
1 215 SER n 
1 216 VAL n 
1 217 GLY n 
1 218 CYS n 
1 219 ILE n 
1 220 MET n 
1 221 ALA n 
1 222 GLU n 
1 223 LEU n 
1 224 LEU n 
1 225 THR n 
1 226 GLY n 
1 227 ARG n 
1 228 THR n 
1 229 LEU n 
1 230 PHE n 
1 231 PRO n 
1 232 GLY n 
1 233 THR n 
1 234 ASP n 
1 235 HIS n 
1 236 ILE n 
1 237 ASP n 
1 238 GLN n 
1 239 LEU n 
1 240 LYS n 
1 241 LEU n 
1 242 ILE n 
1 243 LEU n 
1 244 ARG n 
1 245 LEU n 
1 246 VAL n 
1 247 GLY n 
1 248 THR n 
1 249 PRO n 
1 250 GLY n 
1 251 ALA n 
1 252 GLU n 
1 253 LEU n 
1 254 LEU n 
1 255 LYS n 
1 256 LYS n 
1 257 ILE n 
1 258 SER n 
1 259 SER n 
1 260 GLU n 
1 261 SER n 
1 262 ALA n 
1 263 ARG n 
1 264 ASN n 
1 265 TYR n 
1 266 ILE n 
1 267 GLN n 
1 268 SER n 
1 269 LEU n 
1 270 ALA n 
1 271 GLN n 
1 272 MET n 
1 273 PRO n 
1 274 LYS n 
1 275 MET n 
1 276 ASN n 
1 277 PHE n 
1 278 ALA n 
1 279 ASN n 
1 280 VAL n 
1 281 PHE n 
1 282 ILE n 
1 283 GLY n 
1 284 ALA n 
1 285 ASN n 
1 286 PRO n 
1 287 LEU n 
1 288 ALA n 
1 289 VAL n 
1 290 ASP n 
1 291 LEU n 
1 292 LEU n 
1 293 GLU n 
1 294 LYS n 
1 295 MET n 
1 296 LEU n 
1 297 VAL n 
1 298 LEU n 
1 299 ASP n 
1 300 SER n 
1 301 ASP n 
1 302 LYS n 
1 303 ARG n 
1 304 ILE n 
1 305 THR n 
1 306 ALA n 
1 307 ALA n 
1 308 GLN n 
1 309 ALA n 
1 310 LEU n 
1 311 ALA n 
1 312 HIS n 
1 313 ALA n 
1 314 TYR n 
1 315 PHE n 
1 316 ALA n 
1 317 GLN n 
1 318 TYR n 
1 319 HIS n 
1 320 ASP n 
1 321 PRO n 
1 322 ASP n 
1 323 ASP n 
1 324 GLU n 
1 325 PRO n 
1 326 VAL n 
1 327 ALA n 
1 328 ASP n 
1 329 PRO n 
1 330 TYR n 
1 331 ASP n 
1 332 GLN n 
1 333 SER n 
1 334 PHE n 
1 335 GLU n 
1 336 SER n 
1 337 ARG n 
1 338 ASP n 
1 339 LEU n 
1 340 LEU n 
1 341 ILE n 
1 342 ASP n 
1 343 GLU n 
1 344 TRP n 
1 345 LYS n 
1 346 SER n 
1 347 LEU n 
1 348 THR n 
1 349 TYR n 
1 350 ASP n 
1 351 GLU n 
1 352 VAL n 
1 353 ILE n 
1 354 SER n 
1 355 PHE n 
1 356 VAL n 
1 357 PRO n 
1 358 PRO n 
1 359 PRO n 
1 360 LEU n 
1 361 ASP n 
1 362 GLN n 
1 363 GLU n 
1 364 GLU n 
1 365 MET n 
1 366 GLU n 
1 367 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                   367 
_entity_src_gen.gene_src_common_name               'house mouse' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Mapk14, Crk1, Csbp1, Csbp2' 
_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      'Mus musculus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10090 
_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 
A1ACP non-polymer         . '(4P)-4-[6-fluoro-5-(2-methoxyanilino)-1H-indazol-1-yl]-N-(oxetan-3-yl)thiophene-2-carboxamide' ? 
'C22 H19 F N4 O3 S' 438.475 
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 
BOG   D-saccharide        n 'octyl beta-D-glucopyranoside'                                                                  
'Beta-Octylglucoside; octyl beta-D-glucoside; octyl D-glucoside; octyl glucoside' 'C14 H28 O6'        292.369 
CYS   'L-peptide linking' y CYSTEINE                                                                                        ? 
'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                       ? 
'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                 ? 
'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE                                                                                         ? 
'C2 H5 N O2'        75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                       ? 
'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER                                                                                           ? 
'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                      ? 
'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                         ? 
'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE                                                                                          ? 
'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE                                                                                      ? 
'C5 H11 N O2 S'     149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                   ? 
'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE                                                                                         ? 
'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE                                                                                          ? 
'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE                                                                                       ? 
'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                      ? 
'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                        ? 
'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE                                                                                          ? 
'C5 H11 N O2'       117.146 
# 
_pdbx_chem_comp_identifier.comp_id           BOG 
_pdbx_chem_comp_identifier.type              'IUPAC CARBOHYDRATE SYMBOL' 
_pdbx_chem_comp_identifier.program           PDB-CARE 
_pdbx_chem_comp_identifier.program_version   1.0 
_pdbx_chem_comp_identifier.identifier        b-octylglucoside 
# 
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   MET 1   -6  ?   ?   ?   A . n 
A 1 2   ALA 2   -5  ?   ?   ?   A . n 
A 1 3   HIS 3   -4  ?   ?   ?   A . n 
A 1 4   HIS 4   -3  ?   ?   ?   A . n 
A 1 5   HIS 5   -2  ?   ?   ?   A . n 
A 1 6   HIS 6   -1  ?   ?   ?   A . n 
A 1 7   HIS 7   0   ?   ?   ?   A . n 
A 1 8   HIS 8   1   ?   ?   ?   A . n 
A 1 9   SER 9   2   ?   ?   ?   A . n 
A 1 10  GLN 10  3   ?   ?   ?   A . n 
A 1 11  GLU 11  4   ?   ?   ?   A . n 
A 1 12  ARG 12  5   5   ARG ARG A . n 
A 1 13  PRO 13  6   6   PRO PRO A . n 
A 1 14  THR 14  7   7   THR THR A . n 
A 1 15  PHE 15  8   8   PHE PHE A . n 
A 1 16  TYR 16  9   9   TYR TYR A . n 
A 1 17  ARG 17  10  10  ARG ARG A . n 
A 1 18  GLN 18  11  11  GLN GLN A . n 
A 1 19  GLU 19  12  12  GLU GLU A . n 
A 1 20  LEU 20  13  13  LEU LEU A . n 
A 1 21  ASN 21  14  14  ASN ASN A . n 
A 1 22  LYS 22  15  15  LYS LYS A . n 
A 1 23  THR 23  16  16  THR THR A . n 
A 1 24  ILE 24  17  17  ILE ILE A . n 
A 1 25  TRP 25  18  18  TRP TRP A . n 
A 1 26  GLU 26  19  19  GLU GLU A . n 
A 1 27  VAL 27  20  20  VAL VAL A . n 
A 1 28  PRO 28  21  21  PRO PRO A . n 
A 1 29  GLU 29  22  22  GLU GLU A . n 
A 1 30  ARG 30  23  23  ARG ARG A . n 
A 1 31  TYR 31  24  24  TYR TYR A . n 
A 1 32  GLN 32  25  25  GLN GLN A . n 
A 1 33  ASN 33  26  26  ASN ASN A . n 
A 1 34  LEU 34  27  27  LEU LEU A . n 
A 1 35  SER 35  28  28  SER SER A . n 
A 1 36  PRO 36  29  29  PRO PRO A . n 
A 1 37  VAL 37  30  30  VAL VAL A . n 
A 1 38  GLY 38  31  31  GLY GLY A . n 
A 1 39  SER 39  32  32  SER SER A . n 
A 1 40  GLY 40  33  33  GLY GLY A . n 
A 1 41  ALA 41  34  34  ALA ALA A . n 
A 1 42  TYR 42  35  35  TYR TYR A . n 
A 1 43  GLY 43  36  36  GLY GLY A . n 
A 1 44  SER 44  37  37  SER SER A . n 
A 1 45  VAL 45  38  38  VAL VAL A . n 
A 1 46  CYS 46  39  39  CYS CYS A . n 
A 1 47  ALA 47  40  40  ALA ALA A . n 
A 1 48  ALA 48  41  41  ALA ALA A . n 
A 1 49  PHE 49  42  42  PHE PHE A . n 
A 1 50  ASP 50  43  43  ASP ASP A . n 
A 1 51  THR 51  44  44  THR THR A . n 
A 1 52  LYS 52  45  45  LYS LYS A . n 
A 1 53  THR 53  46  46  THR THR A . n 
A 1 54  GLY 54  47  47  GLY GLY A . n 
A 1 55  HIS 55  48  48  HIS HIS A . n 
A 1 56  ARG 56  49  49  ARG ARG A . n 
A 1 57  VAL 57  50  50  VAL VAL A . n 
A 1 58  ALA 58  51  51  ALA ALA A . n 
A 1 59  VAL 59  52  52  VAL VAL A . n 
A 1 60  LYS 60  53  53  LYS LYS A . n 
A 1 61  LYS 61  54  54  LYS LYS A . n 
A 1 62  LEU 62  55  55  LEU LEU A . n 
A 1 63  SER 63  56  56  SER SER A . n 
A 1 64  ARG 64  57  57  ARG ARG A . n 
A 1 65  PRO 65  58  58  PRO PRO A . n 
A 1 66  PHE 66  59  59  PHE PHE A . n 
A 1 67  GLN 67  60  60  GLN GLN A . n 
A 1 68  SER 68  61  61  SER SER A . n 
A 1 69  ILE 69  62  62  ILE ILE A . n 
A 1 70  ILE 70  63  63  ILE ILE A . n 
A 1 71  HIS 71  64  64  HIS HIS A . n 
A 1 72  ALA 72  65  65  ALA ALA A . n 
A 1 73  LYS 73  66  66  LYS LYS A . n 
A 1 74  ARG 74  67  67  ARG ARG A . n 
A 1 75  THR 75  68  68  THR THR A . n 
A 1 76  TYR 76  69  69  TYR TYR A . n 
A 1 77  ARG 77  70  70  ARG ARG A . n 
A 1 78  GLU 78  71  71  GLU GLU A . n 
A 1 79  LEU 79  72  72  LEU LEU A . n 
A 1 80  ARG 80  73  73  ARG ARG A . n 
A 1 81  LEU 81  74  74  LEU LEU A . n 
A 1 82  LEU 82  75  75  LEU LEU A . n 
A 1 83  LYS 83  76  76  LYS LYS A . n 
A 1 84  HIS 84  77  77  HIS HIS A . n 
A 1 85  MET 85  78  78  MET MET A . n 
A 1 86  LYS 86  79  79  LYS LYS A . n 
A 1 87  HIS 87  80  80  HIS HIS A . n 
A 1 88  GLU 88  81  81  GLU GLU A . n 
A 1 89  ASN 89  82  82  ASN ASN A . n 
A 1 90  VAL 90  83  83  VAL VAL A . n 
A 1 91  ILE 91  84  84  ILE ILE A . n 
A 1 92  GLY 92  85  85  GLY GLY A . n 
A 1 93  LEU 93  86  86  LEU LEU A . n 
A 1 94  LEU 94  87  87  LEU LEU A . n 
A 1 95  ASP 95  88  88  ASP ASP A . n 
A 1 96  VAL 96  89  89  VAL VAL A . n 
A 1 97  PHE 97  90  90  PHE PHE A . n 
A 1 98  THR 98  91  91  THR THR A . n 
A 1 99  PRO 99  92  92  PRO PRO A . n 
A 1 100 ALA 100 93  93  ALA ALA A . n 
A 1 101 ARG 101 94  94  ARG ARG A . n 
A 1 102 SER 102 95  95  SER SER A . n 
A 1 103 LEU 103 96  96  LEU LEU A . n 
A 1 104 GLU 104 97  97  GLU GLU A . n 
A 1 105 GLU 105 98  98  GLU GLU A . n 
A 1 106 PHE 106 99  99  PHE PHE A . n 
A 1 107 ASN 107 100 100 ASN ASN A . n 
A 1 108 ASP 108 101 101 ASP ASP A . n 
A 1 109 VAL 109 102 102 VAL VAL A . n 
A 1 110 TYR 110 103 103 TYR TYR A . n 
A 1 111 LEU 111 104 104 LEU LEU A . n 
A 1 112 VAL 112 105 105 VAL VAL A . n 
A 1 113 THR 113 106 106 THR THR A . n 
A 1 114 HIS 114 107 107 HIS HIS A . n 
A 1 115 LEU 115 108 108 LEU LEU A . n 
A 1 116 MET 116 109 109 MET MET A . n 
A 1 117 GLY 117 110 110 GLY GLY A . n 
A 1 118 ALA 118 111 111 ALA ALA A . n 
A 1 119 ASP 119 112 112 ASP ASP A . n 
A 1 120 LEU 120 113 113 LEU LEU A . n 
A 1 121 ASN 121 114 114 ASN ASN A . n 
A 1 122 ASN 122 115 115 ASN ASN A . n 
A 1 123 ILE 123 116 116 ILE ILE A . n 
A 1 124 VAL 124 117 117 VAL VAL A . n 
A 1 125 LYS 125 118 118 LYS LYS A . n 
A 1 126 CYS 126 119 119 CYS CYS A . n 
A 1 127 GLN 127 120 120 GLN GLN A . n 
A 1 128 LYS 128 121 121 LYS LYS A . n 
A 1 129 LEU 129 122 122 LEU LEU A . n 
A 1 130 THR 130 123 123 THR THR A . n 
A 1 131 ASP 131 124 124 ASP ASP A . n 
A 1 132 ASP 132 125 125 ASP ASP A . n 
A 1 133 HIS 133 126 126 HIS HIS A . n 
A 1 134 VAL 134 127 127 VAL VAL A . n 
A 1 135 GLN 135 128 128 GLN GLN A . n 
A 1 136 PHE 136 129 129 PHE PHE A . n 
A 1 137 LEU 137 130 130 LEU LEU A . n 
A 1 138 ILE 138 131 131 ILE ILE A . n 
A 1 139 TYR 139 132 132 TYR TYR A . n 
A 1 140 GLN 140 133 133 GLN GLN A . n 
A 1 141 ILE 141 134 134 ILE ILE A . n 
A 1 142 LEU 142 135 135 LEU LEU A . n 
A 1 143 ARG 143 136 136 ARG ARG A . n 
A 1 144 GLY 144 137 137 GLY GLY A . n 
A 1 145 LEU 145 138 138 LEU LEU A . n 
A 1 146 LYS 146 139 139 LYS LYS A . n 
A 1 147 TYR 147 140 140 TYR TYR A . n 
A 1 148 ILE 148 141 141 ILE ILE A . n 
A 1 149 HIS 149 142 142 HIS HIS A . n 
A 1 150 SER 150 143 143 SER SER A . n 
A 1 151 ALA 151 144 144 ALA ALA A . n 
A 1 152 ASP 152 145 145 ASP ASP A . n 
A 1 153 ILE 153 146 146 ILE ILE A . n 
A 1 154 ILE 154 147 147 ILE ILE A . n 
A 1 155 HIS 155 148 148 HIS HIS A . n 
A 1 156 ARG 156 149 149 ARG ARG A . n 
A 1 157 ASP 157 150 150 ASP ASP A . n 
A 1 158 LEU 158 151 151 LEU LEU A . n 
A 1 159 LYS 159 152 152 LYS LYS A . n 
A 1 160 PRO 160 153 153 PRO PRO A . n 
A 1 161 SER 161 154 154 SER SER A . n 
A 1 162 ASN 162 155 155 ASN ASN A . n 
A 1 163 LEU 163 156 156 LEU LEU A . n 
A 1 164 ALA 164 157 157 ALA ALA A . n 
A 1 165 VAL 165 158 158 VAL VAL A . n 
A 1 166 ASN 166 159 159 ASN ASN A . n 
A 1 167 GLU 167 160 160 GLU GLU A . n 
A 1 168 ASP 168 161 161 ASP ASP A . n 
A 1 169 CYS 169 162 162 CYS CYS A . n 
A 1 170 GLU 170 163 163 GLU GLU A . n 
A 1 171 LEU 171 164 164 LEU LEU A . n 
A 1 172 LYS 172 165 165 LYS LYS A . n 
A 1 173 ILE 173 166 166 ILE ILE A . n 
A 1 174 LEU 174 167 167 LEU LEU A . n 
A 1 175 ASP 175 168 168 ASP ASP A . n 
A 1 176 PHE 176 169 169 PHE PHE A . n 
A 1 177 GLY 177 170 170 GLY GLY A . n 
A 1 178 LEU 178 171 171 LEU LEU A . n 
A 1 179 ALA 179 172 172 ALA ALA A . n 
A 1 180 ARG 180 173 173 ARG ARG A . n 
A 1 181 HIS 181 174 ?   ?   ?   A . n 
A 1 182 THR 182 175 ?   ?   ?   A . n 
A 1 183 ASP 183 176 ?   ?   ?   A . n 
A 1 184 ASP 184 177 ?   ?   ?   A . n 
A 1 185 GLU 185 178 ?   ?   ?   A . n 
A 1 186 MET 186 179 ?   ?   ?   A . n 
A 1 187 THR 187 180 ?   ?   ?   A . n 
A 1 188 GLY 188 181 ?   ?   ?   A . n 
A 1 189 TYR 189 182 ?   ?   ?   A . n 
A 1 190 VAL 190 183 183 VAL VAL A . n 
A 1 191 ALA 191 184 184 ALA ALA A . n 
A 1 192 THR 192 185 185 THR THR A . n 
A 1 193 ARG 193 186 186 ARG ARG A . n 
A 1 194 TRP 194 187 187 TRP TRP A . n 
A 1 195 TYR 195 188 188 TYR TYR A . n 
A 1 196 ARG 196 189 189 ARG ARG A . n 
A 1 197 ALA 197 190 190 ALA ALA A . n 
A 1 198 PRO 198 191 191 PRO PRO A . n 
A 1 199 GLU 199 192 192 GLU GLU A . n 
A 1 200 ILE 200 193 193 ILE ILE A . n 
A 1 201 MET 201 194 194 MET MET A . n 
A 1 202 LEU 202 195 195 LEU LEU A . n 
A 1 203 ASN 203 196 196 ASN ASN A . n 
A 1 204 TRP 204 197 197 TRP TRP A . n 
A 1 205 MET 205 198 198 MET MET A . n 
A 1 206 HIS 206 199 199 HIS HIS A . n 
A 1 207 TYR 207 200 200 TYR TYR A . n 
A 1 208 ASN 208 201 201 ASN ASN A . n 
A 1 209 GLN 209 202 202 GLN GLN A . n 
A 1 210 THR 210 203 203 THR THR A . n 
A 1 211 VAL 211 204 204 VAL VAL A . n 
A 1 212 ASP 212 205 205 ASP ASP A . n 
A 1 213 ILE 213 206 206 ILE ILE A . n 
A 1 214 TRP 214 207 207 TRP TRP A . n 
A 1 215 SER 215 208 208 SER SER A . n 
A 1 216 VAL 216 209 209 VAL VAL A . n 
A 1 217 GLY 217 210 210 GLY GLY A . n 
A 1 218 CYS 218 211 211 CYS CYS A . n 
A 1 219 ILE 219 212 212 ILE ILE A . n 
A 1 220 MET 220 213 213 MET MET A . n 
A 1 221 ALA 221 214 214 ALA ALA A . n 
A 1 222 GLU 222 215 215 GLU GLU A . n 
A 1 223 LEU 223 216 216 LEU LEU A . n 
A 1 224 LEU 224 217 217 LEU LEU A . n 
A 1 225 THR 225 218 218 THR THR A . n 
A 1 226 GLY 226 219 219 GLY GLY A . n 
A 1 227 ARG 227 220 220 ARG ARG A . n 
A 1 228 THR 228 221 221 THR THR A . n 
A 1 229 LEU 229 222 222 LEU LEU A . n 
A 1 230 PHE 230 223 223 PHE PHE A . n 
A 1 231 PRO 231 224 224 PRO PRO A . n 
A 1 232 GLY 232 225 225 GLY GLY A . n 
A 1 233 THR 233 226 226 THR THR A . n 
A 1 234 ASP 234 227 227 ASP ASP A . n 
A 1 235 HIS 235 228 228 HIS HIS A . n 
A 1 236 ILE 236 229 229 ILE ILE A . n 
A 1 237 ASP 237 230 230 ASP ASP A . n 
A 1 238 GLN 238 231 231 GLN GLN A . n 
A 1 239 LEU 239 232 232 LEU LEU A . n 
A 1 240 LYS 240 233 233 LYS LYS A . n 
A 1 241 LEU 241 234 234 LEU LEU A . n 
A 1 242 ILE 242 235 235 ILE ILE A . n 
A 1 243 LEU 243 236 236 LEU LEU A . n 
A 1 244 ARG 244 237 237 ARG ARG A . n 
A 1 245 LEU 245 238 238 LEU LEU A . n 
A 1 246 VAL 246 239 239 VAL VAL A . n 
A 1 247 GLY 247 240 240 GLY GLY A . n 
A 1 248 THR 248 241 241 THR THR A . n 
A 1 249 PRO 249 242 242 PRO PRO A . n 
A 1 250 GLY 250 243 243 GLY GLY A . n 
A 1 251 ALA 251 244 244 ALA ALA A . n 
A 1 252 GLU 252 245 245 GLU GLU A . n 
A 1 253 LEU 253 246 246 LEU LEU A . n 
A 1 254 LEU 254 247 247 LEU LEU A . n 
A 1 255 LYS 255 248 248 LYS LYS A . n 
A 1 256 LYS 256 249 249 LYS LYS A . n 
A 1 257 ILE 257 250 250 ILE ILE A . n 
A 1 258 SER 258 251 251 SER SER A . n 
A 1 259 SER 259 252 252 SER SER A . n 
A 1 260 GLU 260 253 253 GLU GLU A . n 
A 1 261 SER 261 254 254 SER SER A . n 
A 1 262 ALA 262 255 255 ALA ALA A . n 
A 1 263 ARG 263 256 256 ARG ARG A . n 
A 1 264 ASN 264 257 257 ASN ASN A . n 
A 1 265 TYR 265 258 258 TYR TYR A . n 
A 1 266 ILE 266 259 259 ILE ILE A . n 
A 1 267 GLN 267 260 260 GLN GLN A . n 
A 1 268 SER 268 261 261 SER SER A . n 
A 1 269 LEU 269 262 262 LEU LEU A . n 
A 1 270 ALA 270 263 263 ALA ALA A . n 
A 1 271 GLN 271 264 264 GLN GLN A . n 
A 1 272 MET 272 265 265 MET MET A . n 
A 1 273 PRO 273 266 266 PRO PRO A . n 
A 1 274 LYS 274 267 267 LYS LYS A . n 
A 1 275 MET 275 268 268 MET MET A . n 
A 1 276 ASN 276 269 269 ASN ASN A . n 
A 1 277 PHE 277 270 270 PHE PHE A . n 
A 1 278 ALA 278 271 271 ALA ALA A . n 
A 1 279 ASN 279 272 272 ASN ASN A . n 
A 1 280 VAL 280 273 273 VAL VAL A . n 
A 1 281 PHE 281 274 274 PHE PHE A . n 
A 1 282 ILE 282 275 275 ILE ILE A . n 
A 1 283 GLY 283 276 276 GLY GLY A . n 
A 1 284 ALA 284 277 277 ALA ALA A . n 
A 1 285 ASN 285 278 278 ASN ASN A . n 
A 1 286 PRO 286 279 279 PRO PRO A . n 
A 1 287 LEU 287 280 280 LEU LEU A . n 
A 1 288 ALA 288 281 281 ALA ALA A . n 
A 1 289 VAL 289 282 282 VAL VAL A . n 
A 1 290 ASP 290 283 283 ASP ASP A . n 
A 1 291 LEU 291 284 284 LEU LEU A . n 
A 1 292 LEU 292 285 285 LEU LEU A . n 
A 1 293 GLU 293 286 286 GLU GLU A . n 
A 1 294 LYS 294 287 287 LYS LYS A . n 
A 1 295 MET 295 288 288 MET MET A . n 
A 1 296 LEU 296 289 289 LEU LEU A . n 
A 1 297 VAL 297 290 290 VAL VAL A . n 
A 1 298 LEU 298 291 291 LEU LEU A . n 
A 1 299 ASP 299 292 292 ASP ASP A . n 
A 1 300 SER 300 293 293 SER SER A . n 
A 1 301 ASP 301 294 294 ASP ASP A . n 
A 1 302 LYS 302 295 295 LYS LYS A . n 
A 1 303 ARG 303 296 296 ARG ARG A . n 
A 1 304 ILE 304 297 297 ILE ILE A . n 
A 1 305 THR 305 298 298 THR THR A . n 
A 1 306 ALA 306 299 299 ALA ALA A . n 
A 1 307 ALA 307 300 300 ALA ALA A . n 
A 1 308 GLN 308 301 301 GLN GLN A . n 
A 1 309 ALA 309 302 302 ALA ALA A . n 
A 1 310 LEU 310 303 303 LEU LEU A . n 
A 1 311 ALA 311 304 304 ALA ALA A . n 
A 1 312 HIS 312 305 305 HIS HIS A . n 
A 1 313 ALA 313 306 306 ALA ALA A . n 
A 1 314 TYR 314 307 307 TYR TYR A . n 
A 1 315 PHE 315 308 308 PHE PHE A . n 
A 1 316 ALA 316 309 309 ALA ALA A . n 
A 1 317 GLN 317 310 310 GLN GLN A . n 
A 1 318 TYR 318 311 311 TYR TYR A . n 
A 1 319 HIS 319 312 312 HIS HIS A . n 
A 1 320 ASP 320 313 313 ASP ASP A . n 
A 1 321 PRO 321 314 314 PRO PRO A . n 
A 1 322 ASP 322 315 315 ASP ASP A . n 
A 1 323 ASP 323 316 316 ASP ASP A . n 
A 1 324 GLU 324 317 317 GLU GLU A . n 
A 1 325 PRO 325 318 318 PRO PRO A . n 
A 1 326 VAL 326 319 319 VAL VAL A . n 
A 1 327 ALA 327 320 320 ALA ALA A . n 
A 1 328 ASP 328 321 321 ASP ASP A . n 
A 1 329 PRO 329 322 322 PRO PRO A . n 
A 1 330 TYR 330 323 323 TYR TYR A . n 
A 1 331 ASP 331 324 324 ASP ASP A . n 
A 1 332 GLN 332 325 325 GLN GLN A . n 
A 1 333 SER 333 326 326 SER SER A . n 
A 1 334 PHE 334 327 327 PHE PHE A . n 
A 1 335 GLU 335 328 328 GLU GLU A . n 
A 1 336 SER 336 329 329 SER SER A . n 
A 1 337 ARG 337 330 330 ARG ARG A . n 
A 1 338 ASP 338 331 331 ASP ASP A . n 
A 1 339 LEU 339 332 332 LEU LEU A . n 
A 1 340 LEU 340 333 333 LEU LEU A . n 
A 1 341 ILE 341 334 334 ILE ILE A . n 
A 1 342 ASP 342 335 335 ASP ASP A . n 
A 1 343 GLU 343 336 336 GLU GLU A . n 
A 1 344 TRP 344 337 337 TRP TRP A . n 
A 1 345 LYS 345 338 338 LYS LYS A . n 
A 1 346 SER 346 339 339 SER SER A . n 
A 1 347 LEU 347 340 340 LEU LEU A . n 
A 1 348 THR 348 341 341 THR THR A . n 
A 1 349 TYR 349 342 342 TYR TYR A . n 
A 1 350 ASP 350 343 343 ASP ASP A . n 
A 1 351 GLU 351 344 344 GLU GLU A . n 
A 1 352 VAL 352 345 345 VAL VAL A . n 
A 1 353 ILE 353 346 346 ILE ILE A . n 
A 1 354 SER 354 347 347 SER SER A . n 
A 1 355 PHE 355 348 348 PHE PHE A . n 
A 1 356 VAL 356 349 349 VAL VAL A . n 
A 1 357 PRO 357 350 350 PRO PRO A . n 
A 1 358 PRO 358 351 351 PRO PRO A . n 
A 1 359 PRO 359 352 352 PRO PRO A . n 
A 1 360 LEU 360 353 353 LEU LEU A . n 
A 1 361 ASP 361 354 354 ASP ASP A . n 
A 1 362 GLN 362 355 ?   ?   ?   A . n 
A 1 363 GLU 363 356 ?   ?   ?   A . n 
A 1 364 GLU 364 357 ?   ?   ?   A . n 
A 1 365 MET 365 358 ?   ?   ?   A . n 
A 1 366 GLU 366 359 ?   ?   ?   A . n 
A 1 367 SER 367 360 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ACP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ACP 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 BOG   1   601 601 BOG   BOG A . 
C 3 A1ACP 1   602 701 A1ACP 23M A . 
D 2 BOG   1   603 801 BOG   BOG A . 
E 4 HOH   1   701 42  HOH   HOH A . 
E 4 HOH   2   702 36  HOH   HOH A . 
E 4 HOH   3   703 100 HOH   HOH A . 
E 4 HOH   4   704 88  HOH   HOH A . 
E 4 HOH   5   705 102 HOH   HOH A . 
E 4 HOH   6   706 99  HOH   HOH A . 
E 4 HOH   7   707 48  HOH   HOH A . 
E 4 HOH   8   708 7   HOH   HOH A . 
E 4 HOH   9   709 14  HOH   HOH A . 
E 4 HOH   10  710 80  HOH   HOH A . 
E 4 HOH   11  711 45  HOH   HOH A . 
E 4 HOH   12  712 46  HOH   HOH A . 
E 4 HOH   13  713 41  HOH   HOH A . 
E 4 HOH   14  714 17  HOH   HOH A . 
E 4 HOH   15  715 40  HOH   HOH A . 
E 4 HOH   16  716 93  HOH   HOH A . 
E 4 HOH   17  717 103 HOH   HOH A . 
E 4 HOH   18  718 35  HOH   HOH A . 
E 4 HOH   19  719 6   HOH   HOH A . 
E 4 HOH   20  720 64  HOH   HOH A . 
E 4 HOH   21  721 4   HOH   HOH A . 
E 4 HOH   22  722 52  HOH   HOH A . 
E 4 HOH   23  723 29  HOH   HOH A . 
E 4 HOH   24  724 37  HOH   HOH A . 
E 4 HOH   25  725 19  HOH   HOH A . 
E 4 HOH   26  726 67  HOH   HOH A . 
E 4 HOH   27  727 26  HOH   HOH A . 
E 4 HOH   28  728 1   HOH   HOH A . 
E 4 HOH   29  729 23  HOH   HOH A . 
E 4 HOH   30  730 79  HOH   HOH A . 
E 4 HOH   31  731 2   HOH   HOH A . 
E 4 HOH   32  732 70  HOH   HOH A . 
E 4 HOH   33  733 56  HOH   HOH A . 
E 4 HOH   34  734 86  HOH   HOH A . 
E 4 HOH   35  735 49  HOH   HOH A . 
E 4 HOH   36  736 33  HOH   HOH A . 
E 4 HOH   37  737 12  HOH   HOH A . 
E 4 HOH   38  738 15  HOH   HOH A . 
E 4 HOH   39  739 20  HOH   HOH A . 
E 4 HOH   40  740 39  HOH   HOH A . 
E 4 HOH   41  741 34  HOH   HOH A . 
E 4 HOH   42  742 3   HOH   HOH A . 
E 4 HOH   43  743 81  HOH   HOH A . 
E 4 HOH   44  744 44  HOH   HOH A . 
E 4 HOH   45  745 16  HOH   HOH A . 
E 4 HOH   46  746 66  HOH   HOH A . 
E 4 HOH   47  747 92  HOH   HOH A . 
E 4 HOH   48  748 32  HOH   HOH A . 
E 4 HOH   49  749 13  HOH   HOH A . 
E 4 HOH   50  750 31  HOH   HOH A . 
E 4 HOH   51  751 5   HOH   HOH A . 
E 4 HOH   52  752 10  HOH   HOH A . 
E 4 HOH   53  753 53  HOH   HOH A . 
E 4 HOH   54  754 38  HOH   HOH A . 
E 4 HOH   55  755 69  HOH   HOH A . 
E 4 HOH   56  756 11  HOH   HOH A . 
E 4 HOH   57  757 60  HOH   HOH A . 
E 4 HOH   58  758 58  HOH   HOH A . 
E 4 HOH   59  759 9   HOH   HOH A . 
E 4 HOH   60  760 97  HOH   HOH A . 
E 4 HOH   61  761 85  HOH   HOH A . 
E 4 HOH   62  762 8   HOH   HOH A . 
E 4 HOH   63  763 51  HOH   HOH A . 
E 4 HOH   64  764 62  HOH   HOH A . 
E 4 HOH   65  765 63  HOH   HOH A . 
E 4 HOH   66  766 78  HOH   HOH A . 
E 4 HOH   67  767 24  HOH   HOH A . 
E 4 HOH   68  768 54  HOH   HOH A . 
E 4 HOH   69  769 30  HOH   HOH A . 
E 4 HOH   70  770 50  HOH   HOH A . 
E 4 HOH   71  771 59  HOH   HOH A . 
E 4 HOH   72  772 98  HOH   HOH A . 
E 4 HOH   73  773 94  HOH   HOH A . 
E 4 HOH   74  774 84  HOH   HOH A . 
E 4 HOH   75  775 71  HOH   HOH A . 
E 4 HOH   76  776 96  HOH   HOH A . 
E 4 HOH   77  777 27  HOH   HOH A . 
E 4 HOH   78  778 74  HOH   HOH A . 
E 4 HOH   79  779 83  HOH   HOH A . 
E 4 HOH   80  780 18  HOH   HOH A . 
E 4 HOH   81  781 101 HOH   HOH A . 
E 4 HOH   82  782 47  HOH   HOH A . 
E 4 HOH   83  783 57  HOH   HOH A . 
E 4 HOH   84  784 25  HOH   HOH A . 
E 4 HOH   85  785 68  HOH   HOH A . 
E 4 HOH   86  786 28  HOH   HOH A . 
E 4 HOH   87  787 95  HOH   HOH A . 
E 4 HOH   88  788 89  HOH   HOH A . 
E 4 HOH   89  789 75  HOH   HOH A . 
E 4 HOH   90  790 76  HOH   HOH A . 
E 4 HOH   91  791 55  HOH   HOH A . 
E 4 HOH   92  792 65  HOH   HOH A . 
E 4 HOH   93  793 22  HOH   HOH A . 
E 4 HOH   94  794 77  HOH   HOH A . 
E 4 HOH   95  795 73  HOH   HOH A . 
E 4 HOH   96  796 61  HOH   HOH A . 
E 4 HOH   97  797 72  HOH   HOH A . 
E 4 HOH   98  798 90  HOH   HOH A . 
E 4 HOH   99  799 21  HOH   HOH A . 
E 4 HOH   100 800 82  HOH   HOH A . 
E 4 HOH   101 801 87  HOH   HOH A . 
E 4 HOH   102 802 91  HOH   HOH A . 
E 4 HOH   103 803 43  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8VMM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.350 
_cell.length_a_esd                 ? 
_cell.length_b                     74.330 
_cell.length_b_esd                 ? 
_cell.length_c                     78.710 
_cell.length_c_esd                 ? 
_cell.volume                       388181.624 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8VMM 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8VMM 
_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             2.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.11 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    'PEG 4000, Na cacodylate, n-octyl-b-D-glucoside (b-OG)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-09-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          39.82 
_reflns.entry_id                                       8VMM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.4 
_reflns.d_resolution_low                               39.36 
_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                                     15741 
_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                                6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.77 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.4 
_reflns_shell.d_res_low                                     2.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2570 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.9 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               45.65 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8VMM 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.4 
_refine.ls_d_res_low                             39.35 
_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                     15741 
_refine.ls_number_reflns_R_free                  770 
_refine.ls_number_reflns_R_work                  14971 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 4.89 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2070 
_refine.ls_R_factor_R_free                       0.2632 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2042 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 24.7391 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.3300 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.4 
_refine_hist.d_res_low                        39.35 
_refine_hist.number_atoms_solvent             103 
_refine_hist.number_atoms_total               2925 
_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        2751 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         71 
_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' ? 0.0014  ? 2890 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.4775  ? 3921 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0378  ? 440  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0026  ? 493  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 22.1104 ? 390  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.4  2.55  . . 131 2439 99.65  . . . . 0.2696 . . . . . . . . . . . 0.3322 
'X-RAY DIFFRACTION' 2.55 2.75  . . 134 2415 99.77  . . . . 0.2339 . . . . . . . . . . . 0.3101 
'X-RAY DIFFRACTION' 2.75 3.02  . . 127 2489 99.77  . . . . 0.2339 . . . . . . . . . . . 0.3162 
'X-RAY DIFFRACTION' 3.02 3.46  . . 129 2471 100.00 . . . . 0.2249 . . . . . . . . . . . 0.2738 
'X-RAY DIFFRACTION' 3.46 4.36  . . 131 2506 100.00 . . . . 0.1776 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 4.36 39.35 . . 118 2651 100.00 . . . . 0.1851 . . . . . . . . . . . 0.2471 
# 
_struct.entry_id                     8VMM 
_struct.title                        
'A structural study of selectivity mechanisms for JNK3 and p38 alpha with indazole scaffold probing compounds' 
_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        8VMM 
_struct_keywords.text            'C-Jun terminal kinase 3, JNK3, p38 alpha, Kinase, selectivity, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK14_MOUSE 
_struct_ref.pdbx_db_accession          P47811 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGHRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHE
NVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNED
CELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGT
PGAELLKKISSESARNYIQSLAQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVAD
PYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8VMM 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 9 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 367 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P47811 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  360 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       360 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8VMM MET A 1 ? UNP P47811 ? ? 'initiating methionine' -6 1 
1 8VMM ALA A 2 ? UNP P47811 ? ? 'expression tag'        -5 2 
1 8VMM HIS A 3 ? UNP P47811 ? ? 'expression tag'        -4 3 
1 8VMM HIS A 4 ? UNP P47811 ? ? 'expression tag'        -3 4 
1 8VMM HIS A 5 ? UNP P47811 ? ? 'expression tag'        -2 5 
1 8VMM HIS A 6 ? UNP P47811 ? ? 'expression tag'        -1 6 
1 8VMM HIS A 7 ? UNP P47811 ? ? 'expression tag'        0  7 
1 8VMM HIS A 8 ? UNP P47811 ? ? 'expression tag'        1  8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 68  ? MET A 85  ? SER A 61  MET A 78  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 120 ? GLN A 127 ? LEU A 113 GLN A 120 1 ? 8  
HELX_P HELX_P3  AA3 THR A 130 ? ALA A 151 ? THR A 123 ALA A 144 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 159 ? SER A 161 ? LYS A 152 SER A 154 5 ? 3  
HELX_P HELX_P5  AA5 THR A 192 ? ARG A 196 ? THR A 185 ARG A 189 5 ? 5  
HELX_P HELX_P6  AA6 ALA A 197 ? LEU A 202 ? ALA A 190 LEU A 195 1 ? 6  
HELX_P HELX_P7  AA7 GLN A 209 ? GLY A 226 ? GLN A 202 GLY A 219 1 ? 18 
HELX_P HELX_P8  AA8 ASP A 234 ? GLY A 247 ? ASP A 227 GLY A 240 1 ? 14 
HELX_P HELX_P9  AA9 GLY A 250 ? LYS A 256 ? GLY A 243 LYS A 249 1 ? 7  
HELX_P HELX_P10 AB1 SER A 259 ? LEU A 269 ? SER A 252 LEU A 262 1 ? 11 
HELX_P HELX_P11 AB2 ASN A 276 ? PHE A 281 ? ASN A 269 PHE A 274 1 ? 6  
HELX_P HELX_P12 AB3 ASN A 285 ? LEU A 296 ? ASN A 278 LEU A 289 1 ? 12 
HELX_P HELX_P13 AB4 THR A 305 ? ALA A 311 ? THR A 298 ALA A 304 1 ? 7  
HELX_P HELX_P14 AB5 HIS A 312 ? ALA A 316 ? HIS A 305 ALA A 309 5 ? 5  
HELX_P HELX_P15 AB6 ASP A 320 ? GLU A 324 ? ASP A 313 GLU A 317 5 ? 5  
HELX_P HELX_P16 AB7 GLN A 332 ? ARG A 337 ? GLN A 325 ARG A 330 5 ? 6  
HELX_P HELX_P17 AB8 LEU A 340 ? SER A 354 ? LEU A 333 SER A 347 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 15  ? LEU A 20  ? PHE A 8   LEU A 13  
AA1 2 THR A 23  ? PRO A 28  ? THR A 16  PRO A 21  
AA2 1 TYR A 31  ? SER A 39  ? TYR A 24  SER A 32  
AA2 2 GLY A 43  ? ASP A 50  ? GLY A 36  ASP A 43  
AA2 3 ARG A 56  ? LEU A 62  ? ARG A 49  LEU A 55  
AA2 4 TYR A 110 ? HIS A 114 ? TYR A 103 HIS A 107 
AA2 5 ASP A 95  ? PHE A 97  ? ASP A 88  PHE A 90  
AA3 1 ALA A 118 ? ASP A 119 ? ALA A 111 ASP A 112 
AA3 2 LEU A 163 ? VAL A 165 ? LEU A 156 VAL A 158 
AA3 3 LEU A 171 ? ILE A 173 ? LEU A 164 ILE A 166 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLN A 18  ? N GLN A 11  O TRP A 25  ? O TRP A 18  
AA2 1 2 N SER A 35  ? N SER A 28  O ALA A 47  ? O ALA A 40  
AA2 2 3 N CYS A 46  ? N CYS A 39  O VAL A 59  ? O VAL A 52  
AA2 3 4 N ALA A 58  ? N ALA A 51  O THR A 113 ? O THR A 106 
AA2 4 5 O VAL A 112 ? O VAL A 105 N ASP A 95  ? N ASP A 88  
AA3 1 2 N ALA A 118 ? N ALA A 111 O VAL A 165 ? O VAL A 158 
AA3 2 3 N ALA A 164 ? N ALA A 157 O LYS A 172 ? O LYS A 165 
# 
_pdbx_entry_details.entry_id                   8VMM 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OH  A TYR 323 ? ? O A HOH 701 ? ? 1.87 
2  1 OD2 A ASP 343 ? ? O A HOH 702 ? ? 1.89 
3  1 O   A HOH 775 ? ? O A HOH 789 ? ? 1.91 
4  1 O   A HOH 798 ? ? O A HOH 801 ? ? 1.91 
5  1 OE1 A GLU 19  ? ? O A HOH 703 ? ? 1.92 
6  1 O   A HOH 767 ? ? O A HOH 793 ? ? 1.94 
7  1 O   A HOH 753 ? ? O A HOH 782 ? ? 1.96 
8  1 O   A HOH 762 ? ? O A HOH 783 ? ? 2.00 
9  1 OE2 A GLU 163 ? ? O A HOH 704 ? ? 2.02 
10 1 O   A HOH 743 ? ? O A HOH 790 ? ? 2.04 
11 1 NH2 A ARG 237 ? ? O A HOH 705 ? ? 2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 99  ? ? -58.07  109.90  
2 1 ASN A 100 ? ? -147.87 -4.07   
3 1 ALA A 111 ? ? -175.13 -178.84 
4 1 ARG A 149 ? ? 76.36   -7.57   
5 1 THR A 185 ? ? 77.98   -40.95  
6 1 HIS A 199 ? ? -175.13 104.94  
7 1 ASP A 227 ? ? -164.82 -162.24 
8 1 GLN A 264 ? ? 78.18   132.33  
9 1 LEU A 289 ? ? -103.00 55.12   
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -9.15398282587 -1.08811991606 -17.6051215619 0.303119200984 ? 0.0119473618127  ? 0.000366044298786 
? 0.223858620403 ? -0.0179242871701 ? 0.300136457844 ? 2.00557011952 ? -0.206790175498 ? 0.857657802505  ? 3.66123070445 ? 
-1.61705810152  ? 3.05679962235 ? 0.173243762632   ? 0.195249595874   ? -0.0586529152651 ? -0.298753444101  ? 0.0663929589205 ? 
0.434681122741  ? 0.23473070354    ? 0.0599352419648 ? -0.168473449187 ? 
2 'X-RAY DIFFRACTION' ? refined 12.4318669682  -1.27336421254 -17.451860541  0.243384235815 ? 0.00413868218302 ? 0.0144264505626   
? 0.284403425357 ? 0.0870968110924  ? 0.250896167192 ? 3.14078651633 ? 0.033402568462  ? -0.508670273888 ? 3.4547100713  ? 
0.0738844046953 ? 1.50834793644 ? -0.0548389919086 ? -0.0681784150151 ? -0.233027928137  ? -0.0661171244591 ? -0.138547399489 ? 
-0.28744922587  ? 0.0177943763998  ? 0.363688997422  ? 0.140786554046  ? 
3 'X-RAY DIFFRACTION' ? refined 26.631121446   -15.9699750384 -18.9000749817 0.275715929691 ? 0.109637938645   ? 0.0758661442197   
? 0.373174536343 ? 0.0365026819828  ? 0.383693731143 ? 2.00603640829 ? -1.16990043094  ? 3.32905975287   ? 2.88407461902 ? 
-1.59966451381  ? 5.6120812019  ? 0.602206699077   ? 0.49662539753    ? -0.307086781867  ? -0.0100935661376 ? -0.450911719767 ? 
0.107597851383  ? 0.150833817806   ? 0.965177855253  ? -0.15956044892  ? 
4 'X-RAY DIFFRACTION' ? refined 12.6543973872  0.212447884654 -10.9520135308 0.371714093214 ? -0.0624344222077 ? -0.00188787058893 
? 0.342921244859 ? 0.0456747500012  ? 0.203973898509 ? 3.02020675702 ? 0.792022911961  ? -0.246044071685 ? 2.0626727534  ? 
-1.2877007823   ? 1.48701174133 ? 0.0987512970414  ? -0.326717248422  ? 0.0506850795653  ? -0.0140748490211 ? -0.307340376017 ? 
-0.278885688885 ? -0.0134378649408 ? 0.356320763303  ? 0.155503562832  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1   A 5   ? A 119 A 123 ? ? 
;chain 'A' and (resid 5 through 123 )
;
2 'X-RAY DIFFRACTION' 2 A 120 A 124 ? A 205 A 218 ? ? 
;chain 'A' and (resid 124 through 218 )
;
3 'X-RAY DIFFRACTION' 3 A 206 A 219 ? A 248 A 261 ? ? 
;chain 'A' and (resid 219 through 261 )
;
4 'X-RAY DIFFRACTION' 4 A 249 A 262 ? A 341 A 354 ? ? 
;chain 'A' and (resid 262 through 354 )
;
# 
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 MET -6  ? A MET 1   
2  1 Y 1 A ALA -5  ? A ALA 2   
3  1 Y 1 A HIS -4  ? A HIS 3   
4  1 Y 1 A HIS -3  ? A HIS 4   
5  1 Y 1 A HIS -2  ? A HIS 5   
6  1 Y 1 A HIS -1  ? A HIS 6   
7  1 Y 1 A HIS 0   ? A HIS 7   
8  1 Y 1 A HIS 1   ? A HIS 8   
9  1 Y 1 A SER 2   ? A SER 9   
10 1 Y 1 A GLN 3   ? A GLN 10  
11 1 Y 1 A GLU 4   ? A GLU 11  
12 1 Y 1 A HIS 174 ? A HIS 181 
13 1 Y 1 A THR 175 ? A THR 182 
14 1 Y 1 A ASP 176 ? A ASP 183 
15 1 Y 1 A ASP 177 ? A ASP 184 
16 1 Y 1 A GLU 178 ? A GLU 185 
17 1 Y 1 A MET 179 ? A MET 186 
18 1 Y 1 A THR 180 ? A THR 187 
19 1 Y 1 A GLY 181 ? A GLY 188 
20 1 Y 1 A TYR 182 ? A TYR 189 
21 1 Y 1 A GLN 355 ? A GLN 362 
22 1 Y 1 A GLU 356 ? A GLU 363 
23 1 Y 1 A GLU 357 ? A GLU 364 
24 1 Y 1 A MET 358 ? A MET 365 
25 1 Y 1 A GLU 359 ? A GLU 366 
26 1 Y 1 A SER 360 ? A SER 367 
# 
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 
A1ACP C1     C Y N 1   
A1ACP C2     C Y N 2   
A1ACP N3     N N N 3   
A1ACP C4     C Y N 4   
A1ACP C5     C Y N 5   
A1ACP C6     C Y N 6   
A1ACP C7     C Y N 7   
A1ACP C8     C Y N 8   
A1ACP C9     C Y N 9   
A1ACP C10    C Y N 10  
A1ACP C11    C Y N 11  
A1ACP C12    C Y N 12  
A1ACP C13    C N N 13  
A1ACP C14    C N N 14  
A1ACP C15    C Y N 15  
A1ACP C16    C Y N 16  
A1ACP C17    C Y N 17  
A1ACP C18    C Y N 18  
A1ACP C19    C Y N 19  
A1ACP C20    C N N 20  
A1ACP C21    C N N 21  
A1ACP C22    C N N 22  
A1ACP C3     C Y N 23  
A1ACP F1     F N N 24  
A1ACP N1     N Y N 25  
A1ACP N2     N Y N 26  
A1ACP N4     N N N 27  
A1ACP O1     O N N 28  
A1ACP O2     O N N 29  
A1ACP O3     O N N 30  
A1ACP S1     S Y N 31  
A1ACP H4     H N N 32  
A1ACP H1     H N N 33  
A1ACP H2     H N N 34  
A1ACP H3     H N N 35  
A1ACP H5     H N N 36  
A1ACP H6     H N N 37  
A1ACP H8     H N N 38  
A1ACP H9     H N N 39  
A1ACP H10    H N N 40  
A1ACP H11    H N N 41  
A1ACP H12    H N N 42  
A1ACP H13    H N N 43  
A1ACP H14    H N N 44  
A1ACP H16    H N N 45  
A1ACP H15    H N N 46  
A1ACP H17    H N N 47  
A1ACP H18    H N N 48  
A1ACP H19    H N N 49  
A1ACP H7     H N N 50  
ALA   N      N N N 51  
ALA   CA     C N S 52  
ALA   C      C N N 53  
ALA   O      O N N 54  
ALA   CB     C N N 55  
ALA   OXT    O N N 56  
ALA   H      H N N 57  
ALA   H2     H N N 58  
ALA   HA     H N N 59  
ALA   HB1    H N N 60  
ALA   HB2    H N N 61  
ALA   HB3    H N N 62  
ALA   HXT    H N N 63  
ARG   N      N N N 64  
ARG   CA     C N S 65  
ARG   C      C N N 66  
ARG   O      O N N 67  
ARG   CB     C N N 68  
ARG   CG     C N N 69  
ARG   CD     C N N 70  
ARG   NE     N N N 71  
ARG   CZ     C N N 72  
ARG   NH1    N N N 73  
ARG   NH2    N N N 74  
ARG   OXT    O N N 75  
ARG   H      H N N 76  
ARG   H2     H N N 77  
ARG   HA     H N N 78  
ARG   HB2    H N N 79  
ARG   HB3    H N N 80  
ARG   HG2    H N N 81  
ARG   HG3    H N N 82  
ARG   HD2    H N N 83  
ARG   HD3    H N N 84  
ARG   HE     H N N 85  
ARG   HH11   H N N 86  
ARG   HH12   H N N 87  
ARG   HH21   H N N 88  
ARG   HH22   H N N 89  
ARG   HXT    H N N 90  
ASN   N      N N N 91  
ASN   CA     C N S 92  
ASN   C      C N N 93  
ASN   O      O N N 94  
ASN   CB     C N N 95  
ASN   CG     C N N 96  
ASN   OD1    O N N 97  
ASN   ND2    N N N 98  
ASN   OXT    O N N 99  
ASN   H      H N N 100 
ASN   H2     H N N 101 
ASN   HA     H N N 102 
ASN   HB2    H N N 103 
ASN   HB3    H N N 104 
ASN   HD21   H N N 105 
ASN   HD22   H N N 106 
ASN   HXT    H N N 107 
ASP   N      N N N 108 
ASP   CA     C N S 109 
ASP   C      C N N 110 
ASP   O      O N N 111 
ASP   CB     C N N 112 
ASP   CG     C N N 113 
ASP   OD1    O N N 114 
ASP   OD2    O N N 115 
ASP   OXT    O N N 116 
ASP   H      H N N 117 
ASP   H2     H N N 118 
ASP   HA     H N N 119 
ASP   HB2    H N N 120 
ASP   HB3    H N N 121 
ASP   HD2    H N N 122 
ASP   HXT    H N N 123 
BOG   C1     C N R 124 
BOG   O1     O N N 125 
BOG   C2     C N R 126 
BOG   O2     O N N 127 
BOG   C3     C N S 128 
BOG   O3     O N N 129 
BOG   C4     C N S 130 
BOG   O4     O N N 131 
BOG   C5     C N R 132 
BOG   O5     O N N 133 
BOG   C6     C N N 134 
BOG   O6     O N N 135 
BOG   "C1'"  C N N 136 
BOG   "C2'"  C N N 137 
BOG   "C3'"  C N N 138 
BOG   "C4'"  C N N 139 
BOG   "C5'"  C N N 140 
BOG   "C6'"  C N N 141 
BOG   "C7'"  C N N 142 
BOG   "C8'"  C N N 143 
BOG   H1     H N N 144 
BOG   H2     H N N 145 
BOG   HO2    H N N 146 
BOG   H3     H N N 147 
BOG   HO3    H N N 148 
BOG   H4     H N N 149 
BOG   HO4    H N N 150 
BOG   H5     H N N 151 
BOG   H61    H N N 152 
BOG   H62    H N N 153 
BOG   HO6    H N N 154 
BOG   "H1'1" H N N 155 
BOG   "H1'2" H N N 156 
BOG   "H2'1" H N N 157 
BOG   "H2'2" H N N 158 
BOG   "H3'1" H N N 159 
BOG   "H3'2" H N N 160 
BOG   "H4'1" H N N 161 
BOG   "H4'2" H N N 162 
BOG   "H5'1" H N N 163 
BOG   "H5'2" H N N 164 
BOG   "H6'1" H N N 165 
BOG   "H6'2" H N N 166 
BOG   "H7'1" H N N 167 
BOG   "H7'2" H N N 168 
BOG   "H8'1" H N N 169 
BOG   "H8'2" H N N 170 
BOG   "H8'3" H N N 171 
CYS   N      N N N 172 
CYS   CA     C N R 173 
CYS   C      C N N 174 
CYS   O      O N N 175 
CYS   CB     C N N 176 
CYS   SG     S N N 177 
CYS   OXT    O N N 178 
CYS   H      H N N 179 
CYS   H2     H N N 180 
CYS   HA     H N N 181 
CYS   HB2    H N N 182 
CYS   HB3    H N N 183 
CYS   HG     H N N 184 
CYS   HXT    H N N 185 
GLN   N      N N N 186 
GLN   CA     C N S 187 
GLN   C      C N N 188 
GLN   O      O N N 189 
GLN   CB     C N N 190 
GLN   CG     C N N 191 
GLN   CD     C N N 192 
GLN   OE1    O N N 193 
GLN   NE2    N N N 194 
GLN   OXT    O N N 195 
GLN   H      H N N 196 
GLN   H2     H N N 197 
GLN   HA     H N N 198 
GLN   HB2    H N N 199 
GLN   HB3    H N N 200 
GLN   HG2    H N N 201 
GLN   HG3    H N N 202 
GLN   HE21   H N N 203 
GLN   HE22   H N N 204 
GLN   HXT    H N N 205 
GLU   N      N N N 206 
GLU   CA     C N S 207 
GLU   C      C N N 208 
GLU   O      O N N 209 
GLU   CB     C N N 210 
GLU   CG     C N N 211 
GLU   CD     C N N 212 
GLU   OE1    O N N 213 
GLU   OE2    O N N 214 
GLU   OXT    O N N 215 
GLU   H      H N N 216 
GLU   H2     H N N 217 
GLU   HA     H N N 218 
GLU   HB2    H N N 219 
GLU   HB3    H N N 220 
GLU   HG2    H N N 221 
GLU   HG3    H N N 222 
GLU   HE2    H N N 223 
GLU   HXT    H N N 224 
GLY   N      N N N 225 
GLY   CA     C N N 226 
GLY   C      C N N 227 
GLY   O      O N N 228 
GLY   OXT    O N N 229 
GLY   H      H N N 230 
GLY   H2     H N N 231 
GLY   HA2    H N N 232 
GLY   HA3    H N N 233 
GLY   HXT    H N N 234 
HIS   N      N N N 235 
HIS   CA     C N S 236 
HIS   C      C N N 237 
HIS   O      O N N 238 
HIS   CB     C N N 239 
HIS   CG     C Y N 240 
HIS   ND1    N Y N 241 
HIS   CD2    C Y N 242 
HIS   CE1    C Y N 243 
HIS   NE2    N Y N 244 
HIS   OXT    O N N 245 
HIS   H      H N N 246 
HIS   H2     H N N 247 
HIS   HA     H N N 248 
HIS   HB2    H N N 249 
HIS   HB3    H N N 250 
HIS   HD1    H N N 251 
HIS   HD2    H N N 252 
HIS   HE1    H N N 253 
HIS   HE2    H N N 254 
HIS   HXT    H N N 255 
HOH   O      O N N 256 
HOH   H1     H N N 257 
HOH   H2     H N N 258 
ILE   N      N N N 259 
ILE   CA     C N S 260 
ILE   C      C N N 261 
ILE   O      O N N 262 
ILE   CB     C N S 263 
ILE   CG1    C N N 264 
ILE   CG2    C N N 265 
ILE   CD1    C N N 266 
ILE   OXT    O N N 267 
ILE   H      H N N 268 
ILE   H2     H N N 269 
ILE   HA     H N N 270 
ILE   HB     H N N 271 
ILE   HG12   H N N 272 
ILE   HG13   H N N 273 
ILE   HG21   H N N 274 
ILE   HG22   H N N 275 
ILE   HG23   H N N 276 
ILE   HD11   H N N 277 
ILE   HD12   H N N 278 
ILE   HD13   H N N 279 
ILE   HXT    H N N 280 
LEU   N      N N N 281 
LEU   CA     C N S 282 
LEU   C      C N N 283 
LEU   O      O N N 284 
LEU   CB     C N N 285 
LEU   CG     C N N 286 
LEU   CD1    C N N 287 
LEU   CD2    C N N 288 
LEU   OXT    O N N 289 
LEU   H      H N N 290 
LEU   H2     H N N 291 
LEU   HA     H N N 292 
LEU   HB2    H N N 293 
LEU   HB3    H N N 294 
LEU   HG     H N N 295 
LEU   HD11   H N N 296 
LEU   HD12   H N N 297 
LEU   HD13   H N N 298 
LEU   HD21   H N N 299 
LEU   HD22   H N N 300 
LEU   HD23   H N N 301 
LEU   HXT    H N N 302 
LYS   N      N N N 303 
LYS   CA     C N S 304 
LYS   C      C N N 305 
LYS   O      O N N 306 
LYS   CB     C N N 307 
LYS   CG     C N N 308 
LYS   CD     C N N 309 
LYS   CE     C N N 310 
LYS   NZ     N N N 311 
LYS   OXT    O N N 312 
LYS   H      H N N 313 
LYS   H2     H N N 314 
LYS   HA     H N N 315 
LYS   HB2    H N N 316 
LYS   HB3    H N N 317 
LYS   HG2    H N N 318 
LYS   HG3    H N N 319 
LYS   HD2    H N N 320 
LYS   HD3    H N N 321 
LYS   HE2    H N N 322 
LYS   HE3    H N N 323 
LYS   HZ1    H N N 324 
LYS   HZ2    H N N 325 
LYS   HZ3    H N N 326 
LYS   HXT    H N N 327 
MET   N      N N N 328 
MET   CA     C N S 329 
MET   C      C N N 330 
MET   O      O N N 331 
MET   CB     C N N 332 
MET   CG     C N N 333 
MET   SD     S N N 334 
MET   CE     C N N 335 
MET   OXT    O N N 336 
MET   H      H N N 337 
MET   H2     H N N 338 
MET   HA     H N N 339 
MET   HB2    H N N 340 
MET   HB3    H N N 341 
MET   HG2    H N N 342 
MET   HG3    H N N 343 
MET   HE1    H N N 344 
MET   HE2    H N N 345 
MET   HE3    H N N 346 
MET   HXT    H N N 347 
PHE   N      N N N 348 
PHE   CA     C N S 349 
PHE   C      C N N 350 
PHE   O      O N N 351 
PHE   CB     C N N 352 
PHE   CG     C Y N 353 
PHE   CD1    C Y N 354 
PHE   CD2    C Y N 355 
PHE   CE1    C Y N 356 
PHE   CE2    C Y N 357 
PHE   CZ     C Y N 358 
PHE   OXT    O N N 359 
PHE   H      H N N 360 
PHE   H2     H N N 361 
PHE   HA     H N N 362 
PHE   HB2    H N N 363 
PHE   HB3    H N N 364 
PHE   HD1    H N N 365 
PHE   HD2    H N N 366 
PHE   HE1    H N N 367 
PHE   HE2    H N N 368 
PHE   HZ     H N N 369 
PHE   HXT    H N N 370 
PRO   N      N N N 371 
PRO   CA     C N S 372 
PRO   C      C N N 373 
PRO   O      O N N 374 
PRO   CB     C N N 375 
PRO   CG     C N N 376 
PRO   CD     C N N 377 
PRO   OXT    O N N 378 
PRO   H      H N N 379 
PRO   HA     H N N 380 
PRO   HB2    H N N 381 
PRO   HB3    H N N 382 
PRO   HG2    H N N 383 
PRO   HG3    H N N 384 
PRO   HD2    H N N 385 
PRO   HD3    H N N 386 
PRO   HXT    H N N 387 
SER   N      N N N 388 
SER   CA     C N S 389 
SER   C      C N N 390 
SER   O      O N N 391 
SER   CB     C N N 392 
SER   OG     O N N 393 
SER   OXT    O N N 394 
SER   H      H N N 395 
SER   H2     H N N 396 
SER   HA     H N N 397 
SER   HB2    H N N 398 
SER   HB3    H N N 399 
SER   HG     H N N 400 
SER   HXT    H N N 401 
THR   N      N N N 402 
THR   CA     C N S 403 
THR   C      C N N 404 
THR   O      O N N 405 
THR   CB     C N R 406 
THR   OG1    O N N 407 
THR   CG2    C N N 408 
THR   OXT    O N N 409 
THR   H      H N N 410 
THR   H2     H N N 411 
THR   HA     H N N 412 
THR   HB     H N N 413 
THR   HG1    H N N 414 
THR   HG21   H N N 415 
THR   HG22   H N N 416 
THR   HG23   H N N 417 
THR   HXT    H N N 418 
TRP   N      N N N 419 
TRP   CA     C N S 420 
TRP   C      C N N 421 
TRP   O      O N N 422 
TRP   CB     C N N 423 
TRP   CG     C Y N 424 
TRP   CD1    C Y N 425 
TRP   CD2    C Y N 426 
TRP   NE1    N Y N 427 
TRP   CE2    C Y N 428 
TRP   CE3    C Y N 429 
TRP   CZ2    C Y N 430 
TRP   CZ3    C Y N 431 
TRP   CH2    C Y N 432 
TRP   OXT    O N N 433 
TRP   H      H N N 434 
TRP   H2     H N N 435 
TRP   HA     H N N 436 
TRP   HB2    H N N 437 
TRP   HB3    H N N 438 
TRP   HD1    H N N 439 
TRP   HE1    H N N 440 
TRP   HE3    H N N 441 
TRP   HZ2    H N N 442 
TRP   HZ3    H N N 443 
TRP   HH2    H N N 444 
TRP   HXT    H N N 445 
TYR   N      N N N 446 
TYR   CA     C N S 447 
TYR   C      C N N 448 
TYR   O      O N N 449 
TYR   CB     C N N 450 
TYR   CG     C Y N 451 
TYR   CD1    C Y N 452 
TYR   CD2    C Y N 453 
TYR   CE1    C Y N 454 
TYR   CE2    C Y N 455 
TYR   CZ     C Y N 456 
TYR   OH     O N N 457 
TYR   OXT    O N N 458 
TYR   H      H N N 459 
TYR   H2     H N N 460 
TYR   HA     H N N 461 
TYR   HB2    H N N 462 
TYR   HB3    H N N 463 
TYR   HD1    H N N 464 
TYR   HD2    H N N 465 
TYR   HE1    H N N 466 
TYR   HE2    H N N 467 
TYR   HH     H N N 468 
TYR   HXT    H N N 469 
VAL   N      N N N 470 
VAL   CA     C N S 471 
VAL   C      C N N 472 
VAL   O      O N N 473 
VAL   CB     C N N 474 
VAL   CG1    C N N 475 
VAL   CG2    C N N 476 
VAL   OXT    O N N 477 
VAL   H      H N N 478 
VAL   H2     H N N 479 
VAL   HA     H N N 480 
VAL   HB     H N N 481 
VAL   HG11   H N N 482 
VAL   HG12   H N N 483 
VAL   HG13   H N N 484 
VAL   HG21   H N N 485 
VAL   HG22   H N N 486 
VAL   HG23   H N N 487 
VAL   HXT    H N N 488 
# 
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 
A1ACP C1    N1     sing N N 1   
A1ACP C1    C10    sing Y N 2   
A1ACP C1    C12    doub Y N 3   
A1ACP N1    C2     sing Y N 4   
A1ACP N1    N2     sing Y N 5   
A1ACP C2    C3     doub Y N 6   
A1ACP C2    C5     sing Y N 7   
A1ACP C3    C4     sing Y N 8   
A1ACP C3    C8     sing Y N 9   
A1ACP C4    N2     doub Y N 10  
A1ACP C5    C6     doub Y N 11  
A1ACP C6    C7     sing Y N 12  
A1ACP C6    F1     sing N N 13  
A1ACP C7    C8     doub Y N 14  
A1ACP C7    N3     sing N N 15  
A1ACP N3    C9     sing N N 16  
A1ACP C9    C15    doub Y N 17  
A1ACP C9    C19    sing Y N 18  
A1ACP C10   C11    doub Y N 19  
A1ACP C11   S1     sing Y N 20  
A1ACP C11   C13    sing N N 21  
A1ACP S1    C12    sing Y N 22  
A1ACP C13   O1     doub N N 23  
A1ACP C13   N4     sing N N 24  
A1ACP N4    C14    sing N N 25  
A1ACP C14   C20    sing N N 26  
A1ACP C14   C21    sing N N 27  
A1ACP C15   O3     sing N N 28  
A1ACP C15   C16    sing Y N 29  
A1ACP C16   C17    doub Y N 30  
A1ACP C17   C18    sing Y N 31  
A1ACP C18   C19    doub Y N 32  
A1ACP C20   O2     sing N N 33  
A1ACP O2    C21    sing N N 34  
A1ACP O3    C22    sing N N 35  
A1ACP N3    H4     sing N N 36  
A1ACP C4    H1     sing N N 37  
A1ACP C5    H2     sing N N 38  
A1ACP C8    H3     sing N N 39  
A1ACP C10   H5     sing N N 40  
A1ACP C12   H6     sing N N 41  
A1ACP C14   H8     sing N N 42  
A1ACP C16   H9     sing N N 43  
A1ACP C17   H10    sing N N 44  
A1ACP C18   H11    sing N N 45  
A1ACP C19   H12    sing N N 46  
A1ACP C20   H13    sing N N 47  
A1ACP C20   H14    sing N N 48  
A1ACP C21   H16    sing N N 49  
A1ACP C21   H15    sing N N 50  
A1ACP C22   H17    sing N N 51  
A1ACP C22   H18    sing N N 52  
A1ACP C22   H19    sing N N 53  
A1ACP N4    H7     sing N N 54  
ALA   N     CA     sing N N 55  
ALA   N     H      sing N N 56  
ALA   N     H2     sing N N 57  
ALA   CA    C      sing N N 58  
ALA   CA    CB     sing N N 59  
ALA   CA    HA     sing N N 60  
ALA   C     O      doub N N 61  
ALA   C     OXT    sing N N 62  
ALA   CB    HB1    sing N N 63  
ALA   CB    HB2    sing N N 64  
ALA   CB    HB3    sing N N 65  
ALA   OXT   HXT    sing N N 66  
ARG   N     CA     sing N N 67  
ARG   N     H      sing N N 68  
ARG   N     H2     sing N N 69  
ARG   CA    C      sing N N 70  
ARG   CA    CB     sing N N 71  
ARG   CA    HA     sing N N 72  
ARG   C     O      doub N N 73  
ARG   C     OXT    sing N N 74  
ARG   CB    CG     sing N N 75  
ARG   CB    HB2    sing N N 76  
ARG   CB    HB3    sing N N 77  
ARG   CG    CD     sing N N 78  
ARG   CG    HG2    sing N N 79  
ARG   CG    HG3    sing N N 80  
ARG   CD    NE     sing N N 81  
ARG   CD    HD2    sing N N 82  
ARG   CD    HD3    sing N N 83  
ARG   NE    CZ     sing N N 84  
ARG   NE    HE     sing N N 85  
ARG   CZ    NH1    sing N N 86  
ARG   CZ    NH2    doub N N 87  
ARG   NH1   HH11   sing N N 88  
ARG   NH1   HH12   sing N N 89  
ARG   NH2   HH21   sing N N 90  
ARG   NH2   HH22   sing N N 91  
ARG   OXT   HXT    sing N N 92  
ASN   N     CA     sing N N 93  
ASN   N     H      sing N N 94  
ASN   N     H2     sing N N 95  
ASN   CA    C      sing N N 96  
ASN   CA    CB     sing N N 97  
ASN   CA    HA     sing N N 98  
ASN   C     O      doub N N 99  
ASN   C     OXT    sing N N 100 
ASN   CB    CG     sing N N 101 
ASN   CB    HB2    sing N N 102 
ASN   CB    HB3    sing N N 103 
ASN   CG    OD1    doub N N 104 
ASN   CG    ND2    sing N N 105 
ASN   ND2   HD21   sing N N 106 
ASN   ND2   HD22   sing N N 107 
ASN   OXT   HXT    sing N N 108 
ASP   N     CA     sing N N 109 
ASP   N     H      sing N N 110 
ASP   N     H2     sing N N 111 
ASP   CA    C      sing N N 112 
ASP   CA    CB     sing N N 113 
ASP   CA    HA     sing N N 114 
ASP   C     O      doub N N 115 
ASP   C     OXT    sing N N 116 
ASP   CB    CG     sing N N 117 
ASP   CB    HB2    sing N N 118 
ASP   CB    HB3    sing N N 119 
ASP   CG    OD1    doub N N 120 
ASP   CG    OD2    sing N N 121 
ASP   OD2   HD2    sing N N 122 
ASP   OXT   HXT    sing N N 123 
BOG   C1    O1     sing N N 124 
BOG   C1    C2     sing N N 125 
BOG   C1    O5     sing N N 126 
BOG   C1    H1     sing N N 127 
BOG   O1    "C1'"  sing N N 128 
BOG   C2    O2     sing N N 129 
BOG   C2    C3     sing N N 130 
BOG   C2    H2     sing N N 131 
BOG   O2    HO2    sing N N 132 
BOG   C3    O3     sing N N 133 
BOG   C3    C4     sing N N 134 
BOG   C3    H3     sing N N 135 
BOG   O3    HO3    sing N N 136 
BOG   C4    O4     sing N N 137 
BOG   C4    C5     sing N N 138 
BOG   C4    H4     sing N N 139 
BOG   O4    HO4    sing N N 140 
BOG   C5    O5     sing N N 141 
BOG   C5    C6     sing N N 142 
BOG   C5    H5     sing N N 143 
BOG   C6    O6     sing N N 144 
BOG   C6    H61    sing N N 145 
BOG   C6    H62    sing N N 146 
BOG   O6    HO6    sing N N 147 
BOG   "C1'" "C2'"  sing N N 148 
BOG   "C1'" "H1'1" sing N N 149 
BOG   "C1'" "H1'2" sing N N 150 
BOG   "C2'" "C3'"  sing N N 151 
BOG   "C2'" "H2'1" sing N N 152 
BOG   "C2'" "H2'2" sing N N 153 
BOG   "C3'" "C4'"  sing N N 154 
BOG   "C3'" "H3'1" sing N N 155 
BOG   "C3'" "H3'2" sing N N 156 
BOG   "C4'" "C5'"  sing N N 157 
BOG   "C4'" "H4'1" sing N N 158 
BOG   "C4'" "H4'2" sing N N 159 
BOG   "C5'" "C6'"  sing N N 160 
BOG   "C5'" "H5'1" sing N N 161 
BOG   "C5'" "H5'2" sing N N 162 
BOG   "C6'" "C7'"  sing N N 163 
BOG   "C6'" "H6'1" sing N N 164 
BOG   "C6'" "H6'2" sing N N 165 
BOG   "C7'" "C8'"  sing N N 166 
BOG   "C7'" "H7'1" sing N N 167 
BOG   "C7'" "H7'2" sing N N 168 
BOG   "C8'" "H8'1" sing N N 169 
BOG   "C8'" "H8'2" sing N N 170 
BOG   "C8'" "H8'3" sing N N 171 
CYS   N     CA     sing N N 172 
CYS   N     H      sing N N 173 
CYS   N     H2     sing N N 174 
CYS   CA    C      sing N N 175 
CYS   CA    CB     sing N N 176 
CYS   CA    HA     sing N N 177 
CYS   C     O      doub N N 178 
CYS   C     OXT    sing N N 179 
CYS   CB    SG     sing N N 180 
CYS   CB    HB2    sing N N 181 
CYS   CB    HB3    sing N N 182 
CYS   SG    HG     sing N N 183 
CYS   OXT   HXT    sing N N 184 
GLN   N     CA     sing N N 185 
GLN   N     H      sing N N 186 
GLN   N     H2     sing N N 187 
GLN   CA    C      sing N N 188 
GLN   CA    CB     sing N N 189 
GLN   CA    HA     sing N N 190 
GLN   C     O      doub N N 191 
GLN   C     OXT    sing N N 192 
GLN   CB    CG     sing N N 193 
GLN   CB    HB2    sing N N 194 
GLN   CB    HB3    sing N N 195 
GLN   CG    CD     sing N N 196 
GLN   CG    HG2    sing N N 197 
GLN   CG    HG3    sing N N 198 
GLN   CD    OE1    doub N N 199 
GLN   CD    NE2    sing N N 200 
GLN   NE2   HE21   sing N N 201 
GLN   NE2   HE22   sing N N 202 
GLN   OXT   HXT    sing N N 203 
GLU   N     CA     sing N N 204 
GLU   N     H      sing N N 205 
GLU   N     H2     sing N N 206 
GLU   CA    C      sing N N 207 
GLU   CA    CB     sing N N 208 
GLU   CA    HA     sing N N 209 
GLU   C     O      doub N N 210 
GLU   C     OXT    sing N N 211 
GLU   CB    CG     sing N N 212 
GLU   CB    HB2    sing N N 213 
GLU   CB    HB3    sing N N 214 
GLU   CG    CD     sing N N 215 
GLU   CG    HG2    sing N N 216 
GLU   CG    HG3    sing N N 217 
GLU   CD    OE1    doub N N 218 
GLU   CD    OE2    sing N N 219 
GLU   OE2   HE2    sing N N 220 
GLU   OXT   HXT    sing N N 221 
GLY   N     CA     sing N N 222 
GLY   N     H      sing N N 223 
GLY   N     H2     sing N N 224 
GLY   CA    C      sing N N 225 
GLY   CA    HA2    sing N N 226 
GLY   CA    HA3    sing N N 227 
GLY   C     O      doub N N 228 
GLY   C     OXT    sing N N 229 
GLY   OXT   HXT    sing N N 230 
HIS   N     CA     sing N N 231 
HIS   N     H      sing N N 232 
HIS   N     H2     sing N N 233 
HIS   CA    C      sing N N 234 
HIS   CA    CB     sing N N 235 
HIS   CA    HA     sing N N 236 
HIS   C     O      doub N N 237 
HIS   C     OXT    sing N N 238 
HIS   CB    CG     sing N N 239 
HIS   CB    HB2    sing N N 240 
HIS   CB    HB3    sing N N 241 
HIS   CG    ND1    sing Y N 242 
HIS   CG    CD2    doub Y N 243 
HIS   ND1   CE1    doub Y N 244 
HIS   ND1   HD1    sing N N 245 
HIS   CD2   NE2    sing Y N 246 
HIS   CD2   HD2    sing N N 247 
HIS   CE1   NE2    sing Y N 248 
HIS   CE1   HE1    sing N N 249 
HIS   NE2   HE2    sing N N 250 
HIS   OXT   HXT    sing N N 251 
HOH   O     H1     sing N N 252 
HOH   O     H2     sing N N 253 
ILE   N     CA     sing N N 254 
ILE   N     H      sing N N 255 
ILE   N     H2     sing N N 256 
ILE   CA    C      sing N N 257 
ILE   CA    CB     sing N N 258 
ILE   CA    HA     sing N N 259 
ILE   C     O      doub N N 260 
ILE   C     OXT    sing N N 261 
ILE   CB    CG1    sing N N 262 
ILE   CB    CG2    sing N N 263 
ILE   CB    HB     sing N N 264 
ILE   CG1   CD1    sing N N 265 
ILE   CG1   HG12   sing N N 266 
ILE   CG1   HG13   sing N N 267 
ILE   CG2   HG21   sing N N 268 
ILE   CG2   HG22   sing N N 269 
ILE   CG2   HG23   sing N N 270 
ILE   CD1   HD11   sing N N 271 
ILE   CD1   HD12   sing N N 272 
ILE   CD1   HD13   sing N N 273 
ILE   OXT   HXT    sing N N 274 
LEU   N     CA     sing N N 275 
LEU   N     H      sing N N 276 
LEU   N     H2     sing N N 277 
LEU   CA    C      sing N N 278 
LEU   CA    CB     sing N N 279 
LEU   CA    HA     sing N N 280 
LEU   C     O      doub N N 281 
LEU   C     OXT    sing N N 282 
LEU   CB    CG     sing N N 283 
LEU   CB    HB2    sing N N 284 
LEU   CB    HB3    sing N N 285 
LEU   CG    CD1    sing N N 286 
LEU   CG    CD2    sing N N 287 
LEU   CG    HG     sing N N 288 
LEU   CD1   HD11   sing N N 289 
LEU   CD1   HD12   sing N N 290 
LEU   CD1   HD13   sing N N 291 
LEU   CD2   HD21   sing N N 292 
LEU   CD2   HD22   sing N N 293 
LEU   CD2   HD23   sing N N 294 
LEU   OXT   HXT    sing N N 295 
LYS   N     CA     sing N N 296 
LYS   N     H      sing N N 297 
LYS   N     H2     sing N N 298 
LYS   CA    C      sing N N 299 
LYS   CA    CB     sing N N 300 
LYS   CA    HA     sing N N 301 
LYS   C     O      doub N N 302 
LYS   C     OXT    sing N N 303 
LYS   CB    CG     sing N N 304 
LYS   CB    HB2    sing N N 305 
LYS   CB    HB3    sing N N 306 
LYS   CG    CD     sing N N 307 
LYS   CG    HG2    sing N N 308 
LYS   CG    HG3    sing N N 309 
LYS   CD    CE     sing N N 310 
LYS   CD    HD2    sing N N 311 
LYS   CD    HD3    sing N N 312 
LYS   CE    NZ     sing N N 313 
LYS   CE    HE2    sing N N 314 
LYS   CE    HE3    sing N N 315 
LYS   NZ    HZ1    sing N N 316 
LYS   NZ    HZ2    sing N N 317 
LYS   NZ    HZ3    sing N N 318 
LYS   OXT   HXT    sing N N 319 
MET   N     CA     sing N N 320 
MET   N     H      sing N N 321 
MET   N     H2     sing N N 322 
MET   CA    C      sing N N 323 
MET   CA    CB     sing N N 324 
MET   CA    HA     sing N N 325 
MET   C     O      doub N N 326 
MET   C     OXT    sing N N 327 
MET   CB    CG     sing N N 328 
MET   CB    HB2    sing N N 329 
MET   CB    HB3    sing N N 330 
MET   CG    SD     sing N N 331 
MET   CG    HG2    sing N N 332 
MET   CG    HG3    sing N N 333 
MET   SD    CE     sing N N 334 
MET   CE    HE1    sing N N 335 
MET   CE    HE2    sing N N 336 
MET   CE    HE3    sing N N 337 
MET   OXT   HXT    sing N N 338 
PHE   N     CA     sing N N 339 
PHE   N     H      sing N N 340 
PHE   N     H2     sing N N 341 
PHE   CA    C      sing N N 342 
PHE   CA    CB     sing N N 343 
PHE   CA    HA     sing N N 344 
PHE   C     O      doub N N 345 
PHE   C     OXT    sing N N 346 
PHE   CB    CG     sing N N 347 
PHE   CB    HB2    sing N N 348 
PHE   CB    HB3    sing N N 349 
PHE   CG    CD1    doub Y N 350 
PHE   CG    CD2    sing Y N 351 
PHE   CD1   CE1    sing Y N 352 
PHE   CD1   HD1    sing N N 353 
PHE   CD2   CE2    doub Y N 354 
PHE   CD2   HD2    sing N N 355 
PHE   CE1   CZ     doub Y N 356 
PHE   CE1   HE1    sing N N 357 
PHE   CE2   CZ     sing Y N 358 
PHE   CE2   HE2    sing N N 359 
PHE   CZ    HZ     sing N N 360 
PHE   OXT   HXT    sing N N 361 
PRO   N     CA     sing N N 362 
PRO   N     CD     sing N N 363 
PRO   N     H      sing N N 364 
PRO   CA    C      sing N N 365 
PRO   CA    CB     sing N N 366 
PRO   CA    HA     sing N N 367 
PRO   C     O      doub N N 368 
PRO   C     OXT    sing N N 369 
PRO   CB    CG     sing N N 370 
PRO   CB    HB2    sing N N 371 
PRO   CB    HB3    sing N N 372 
PRO   CG    CD     sing N N 373 
PRO   CG    HG2    sing N N 374 
PRO   CG    HG3    sing N N 375 
PRO   CD    HD2    sing N N 376 
PRO   CD    HD3    sing N N 377 
PRO   OXT   HXT    sing N N 378 
SER   N     CA     sing N N 379 
SER   N     H      sing N N 380 
SER   N     H2     sing N N 381 
SER   CA    C      sing N N 382 
SER   CA    CB     sing N N 383 
SER   CA    HA     sing N N 384 
SER   C     O      doub N N 385 
SER   C     OXT    sing N N 386 
SER   CB    OG     sing N N 387 
SER   CB    HB2    sing N N 388 
SER   CB    HB3    sing N N 389 
SER   OG    HG     sing N N 390 
SER   OXT   HXT    sing N N 391 
THR   N     CA     sing N N 392 
THR   N     H      sing N N 393 
THR   N     H2     sing N N 394 
THR   CA    C      sing N N 395 
THR   CA    CB     sing N N 396 
THR   CA    HA     sing N N 397 
THR   C     O      doub N N 398 
THR   C     OXT    sing N N 399 
THR   CB    OG1    sing N N 400 
THR   CB    CG2    sing N N 401 
THR   CB    HB     sing N N 402 
THR   OG1   HG1    sing N N 403 
THR   CG2   HG21   sing N N 404 
THR   CG2   HG22   sing N N 405 
THR   CG2   HG23   sing N N 406 
THR   OXT   HXT    sing N N 407 
TRP   N     CA     sing N N 408 
TRP   N     H      sing N N 409 
TRP   N     H2     sing N N 410 
TRP   CA    C      sing N N 411 
TRP   CA    CB     sing N N 412 
TRP   CA    HA     sing N N 413 
TRP   C     O      doub N N 414 
TRP   C     OXT    sing N N 415 
TRP   CB    CG     sing N N 416 
TRP   CB    HB2    sing N N 417 
TRP   CB    HB3    sing N N 418 
TRP   CG    CD1    doub Y N 419 
TRP   CG    CD2    sing Y N 420 
TRP   CD1   NE1    sing Y N 421 
TRP   CD1   HD1    sing N N 422 
TRP   CD2   CE2    doub Y N 423 
TRP   CD2   CE3    sing Y N 424 
TRP   NE1   CE2    sing Y N 425 
TRP   NE1   HE1    sing N N 426 
TRP   CE2   CZ2    sing Y N 427 
TRP   CE3   CZ3    doub Y N 428 
TRP   CE3   HE3    sing N N 429 
TRP   CZ2   CH2    doub Y N 430 
TRP   CZ2   HZ2    sing N N 431 
TRP   CZ3   CH2    sing Y N 432 
TRP   CZ3   HZ3    sing N N 433 
TRP   CH2   HH2    sing N N 434 
TRP   OXT   HXT    sing N N 435 
TYR   N     CA     sing N N 436 
TYR   N     H      sing N N 437 
TYR   N     H2     sing N N 438 
TYR   CA    C      sing N N 439 
TYR   CA    CB     sing N N 440 
TYR   CA    HA     sing N N 441 
TYR   C     O      doub N N 442 
TYR   C     OXT    sing N N 443 
TYR   CB    CG     sing N N 444 
TYR   CB    HB2    sing N N 445 
TYR   CB    HB3    sing N N 446 
TYR   CG    CD1    doub Y N 447 
TYR   CG    CD2    sing Y N 448 
TYR   CD1   CE1    sing Y N 449 
TYR   CD1   HD1    sing N N 450 
TYR   CD2   CE2    doub Y N 451 
TYR   CD2   HD2    sing N N 452 
TYR   CE1   CZ     doub Y N 453 
TYR   CE1   HE1    sing N N 454 
TYR   CE2   CZ     sing Y N 455 
TYR   CE2   HE2    sing N N 456 
TYR   CZ    OH     sing N N 457 
TYR   OH    HH     sing N N 458 
TYR   OXT   HXT    sing N N 459 
VAL   N     CA     sing N N 460 
VAL   N     H      sing N N 461 
VAL   N     H2     sing N N 462 
VAL   CA    C      sing N N 463 
VAL   CA    CB     sing N N 464 
VAL   CA    HA     sing N N 465 
VAL   C     O      doub N N 466 
VAL   C     OXT    sing N N 467 
VAL   CB    CG1    sing N N 468 
VAL   CB    CG2    sing N N 469 
VAL   CB    HB     sing N N 470 
VAL   CG1   HG11   sing N N 471 
VAL   CG1   HG12   sing N N 472 
VAL   CG1   HG13   sing N N 473 
VAL   CG2   HG21   sing N N 474 
VAL   CG2   HG22   sing N N 475 
VAL   CG2   HG23   sing N N 476 
VAL   OXT   HXT    sing N N 477 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Institute on Aging (NIH/NIA)' 
_pdbx_audit_support.country                'United States' 
_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   8EFJ 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8VMM 
_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]   0.015072 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013454 
_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]   0.012705 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F ? ? 8.95735 ?       ? ? 7.27484  ?        ? ? 0.0 
;1-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
H ? ? 0.51345 0.48472 ? ? 24.73122 6.32584  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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      . ARG   A 1 12  ? -25.46876 4.52946   -7.36321  1.000 74.65634  ? 5   ARG   A N      1 
ATOM   2    C CA     . ARG   A 1 12  ? -24.51494 4.01850   -8.34107  1.000 67.68986  ? 5   ARG   A CA     1 
ATOM   3    C C      . ARG   A 1 12  ? -24.85037 4.51655   -9.74322  1.000 60.85292  ? 5   ARG   A C      1 
ATOM   4    O O      . ARG   A 1 12  ? -26.00660 4.81657   -10.04068 1.000 77.36163  ? 5   ARG   A O      1 
ATOM   5    C CB     . ARG   A 1 12  ? -24.48804 2.48871   -8.31621  1.000 72.96393  ? 5   ARG   A CB     1 
ATOM   6    C CG     . ARG   A 1 12  ? -25.39528 1.83698   -9.34583  1.000 73.67139  ? 5   ARG   A CG     1 
ATOM   7    C CD     . ARG   A 1 12  ? -25.50225 0.33777   -9.12027  1.000 70.28284  ? 5   ARG   A CD     1 
ATOM   8    N NE     . ARG   A 1 12  ? -25.95603 -0.35974  -10.31747 1.000 67.46967  ? 5   ARG   A NE     1 
ATOM   9    C CZ     . ARG   A 1 12  ? -25.15202 -0.95880  -11.18537 1.000 61.40964  ? 5   ARG   A CZ     1 
ATOM   10   N NH1    . ARG   A 1 12  ? -23.83965 -0.96965  -11.01844 1.000 64.45156  ? 5   ARG   A NH1    1 
ATOM   11   N NH2    . ARG   A 1 12  ? -25.67778 -1.56154  -12.24796 1.000 57.94283  ? 5   ARG   A NH2    1 
ATOM   12   N N      . PRO   A 1 13  ? -23.83999 4.60144   -10.60365 1.000 55.49668  ? 6   PRO   A N      1 
ATOM   13   C CA     . PRO   A 1 13  ? -24.05867 5.12374   -11.95713 1.000 58.70890  ? 6   PRO   A CA     1 
ATOM   14   C C      . PRO   A 1 13  ? -24.84225 4.14451   -12.81977 1.000 60.36574  ? 6   PRO   A C      1 
ATOM   15   O O      . PRO   A 1 13  ? -25.04715 2.97804   -12.47747 1.000 56.01951  ? 6   PRO   A O      1 
ATOM   16   C CB     . PRO   A 1 13  ? -22.63850 5.32475   -12.49250 1.000 58.66051  ? 6   PRO   A CB     1 
ATOM   17   C CG     . PRO   A 1 13  ? -21.81292 4.34029   -11.73146 1.000 48.21712  ? 6   PRO   A CG     1 
ATOM   18   C CD     . PRO   A 1 13  ? -22.42921 4.25195   -10.36178 1.000 54.36270  ? 6   PRO   A CD     1 
ATOM   19   N N      . THR   A 1 14  ? -25.28506 4.65067   -13.96833 1.000 57.06524  ? 7   THR   A N      1 
ATOM   20   C CA     . THR   A 1 14  ? -25.98956 3.84605   -14.95577 1.000 49.61372  ? 7   THR   A CA     1 
ATOM   21   C C      . THR   A 1 14  ? -24.99684 3.25146   -15.94615 1.000 52.25406  ? 7   THR   A C      1 
ATOM   22   O O      . THR   A 1 14  ? -24.08026 3.93467   -16.41231 1.000 58.96043  ? 7   THR   A O      1 
ATOM   23   C CB     . THR   A 1 14  ? -27.03024 4.68643   -15.69972 1.000 57.25395  ? 7   THR   A CB     1 
ATOM   24   O OG1    . THR   A 1 14  ? -27.91175 5.30612   -14.75492 1.000 53.40767  ? 7   THR   A OG1    1 
ATOM   25   C CG2    . THR   A 1 14  ? -27.84293 3.81568   -16.64743 1.000 52.64856  ? 7   THR   A CG2    1 
ATOM   26   N N      . PHE   A 1 15  ? -25.18644 1.97456   -16.26302 1.000 48.64016  ? 8   PHE   A N      1 
ATOM   27   C CA     . PHE   A 1 15  ? -24.29980 1.23169   -17.14481 1.000 48.17213  ? 8   PHE   A CA     1 
ATOM   28   C C      . PHE   A 1 15  ? -24.95730 1.00953   -18.50130 1.000 52.03852  ? 8   PHE   A C      1 
ATOM   29   O O      . PHE   A 1 15  ? -26.18115 1.07863   -18.64452 1.000 44.35271  ? 8   PHE   A O      1 
ATOM   30   C CB     . PHE   A 1 15  ? -23.92633 -0.12261  -16.52936 1.000 42.59076  ? 8   PHE   A CB     1 
ATOM   31   C CG     . PHE   A 1 15  ? -22.83189 -0.04704  -15.50308 1.000 48.75465  ? 8   PHE   A CG     1 
ATOM   32   C CD1    . PHE   A 1 15  ? -23.08599 0.44064   -14.23198 1.000 48.42057  ? 8   PHE   A CD1    1 
ATOM   33   C CD2    . PHE   A 1 15  ? -21.55065 -0.47638  -15.80630 1.000 50.69423  ? 8   PHE   A CD2    1 
ATOM   34   C CE1    . PHE   A 1 15  ? -22.07991 0.50590   -13.28551 1.000 46.06813  ? 8   PHE   A CE1    1 
ATOM   35   C CE2    . PHE   A 1 15  ? -20.54128 -0.41352  -14.86493 1.000 41.99819  ? 8   PHE   A CE2    1 
ATOM   36   C CZ     . PHE   A 1 15  ? -20.80614 0.07831   -13.60310 1.000 35.95311  ? 8   PHE   A CZ     1 
ATOM   37   N N      . TYR   A 1 16  ? -24.12205 0.73693   -19.50322 1.000 55.49962  ? 9   TYR   A N      1 
ATOM   38   C CA     . TYR   A 1 16  ? -24.59684 0.33148   -20.81809 1.000 58.20755  ? 9   TYR   A CA     1 
ATOM   39   C C      . TYR   A 1 16  ? -23.68192 -0.75735  -21.35979 1.000 52.23567  ? 9   TYR   A C      1 
ATOM   40   O O      . TYR   A 1 16  ? -22.48137 -0.78075  -21.07545 1.000 49.50124  ? 9   TYR   A O      1 
ATOM   41   C CB     . TYR   A 1 16  ? -24.68011 1.51640   -21.79704 1.000 47.56464  ? 9   TYR   A CB     1 
ATOM   42   C CG     . TYR   A 1 16  ? -23.35413 2.12100   -22.20481 1.000 47.94349  ? 9   TYR   A CG     1 
ATOM   43   C CD1    . TYR   A 1 16  ? -22.72672 3.07156   -21.41003 1.000 47.61480  ? 9   TYR   A CD1    1 
ATOM   44   C CD2    . TYR   A 1 16  ? -22.74310 1.76014   -23.39784 1.000 49.04594  ? 9   TYR   A CD2    1 
ATOM   45   C CE1    . TYR   A 1 16  ? -21.52004 3.63470   -21.78517 1.000 41.85567  ? 9   TYR   A CE1    1 
ATOM   46   C CE2    . TYR   A 1 16  ? -21.53782 2.31665   -23.78017 1.000 48.59552  ? 9   TYR   A CE2    1 
ATOM   47   C CZ     . TYR   A 1 16  ? -20.93021 3.25371   -22.97110 1.000 42.09983  ? 9   TYR   A CZ     1 
ATOM   48   O OH     . TYR   A 1 16  ? -19.72912 3.81119   -23.34974 1.000 47.36960  ? 9   TYR   A OH     1 
ATOM   49   N N      . ARG   A 1 17  ? -24.26600 -1.66474  -22.13739 1.000 51.74540  ? 10  ARG   A N      1 
ATOM   50   C CA     . ARG   A 1 17  ? -23.58839 -2.86796  -22.59430 1.000 57.23303  ? 10  ARG   A CA     1 
ATOM   51   C C      . ARG   A 1 17  ? -23.30439 -2.80231  -24.08957 1.000 52.52022  ? 10  ARG   A C      1 
ATOM   52   O O      . ARG   A 1 17  ? -24.05031 -2.18850  -24.85835 1.000 56.28403  ? 10  ARG   A O      1 
ATOM   53   C CB     . ARG   A 1 17  ? -24.42424 -4.11540  -22.28654 1.000 48.51915  ? 10  ARG   A CB     1 
ATOM   54   C CG     . ARG   A 1 17  ? -24.81563 -4.25996  -20.82487 1.000 58.94467  ? 10  ARG   A CG     1 
ATOM   55   C CD     . ARG   A 1 17  ? -25.87754 -5.33279  -20.64136 1.000 72.93804  ? 10  ARG   A CD     1 
ATOM   56   N NE     . ARG   A 1 17  ? -25.31982 -6.57943  -20.13026 1.000 81.64683  ? 10  ARG   A NE     1 
ATOM   57   C CZ     . ARG   A 1 17  ? -24.84840 -7.55786  -20.89111 1.000 75.51061  ? 10  ARG   A CZ     1 
ATOM   58   N NH1    . ARG   A 1 17  ? -24.84157 -7.46528  -22.21085 1.000 55.22867  ? 10  ARG   A NH1    1 
ATOM   59   N NH2    . ARG   A 1 17  ? -24.37517 -8.65857  -20.31334 1.000 72.55799  ? 10  ARG   A NH2    1 
ATOM   60   N N      . GLN   A 1 18  ? -22.21585 -3.45341  -24.49097 1.000 54.35009  ? 11  GLN   A N      1 
ATOM   61   C CA     . GLN   A 1 18  ? -21.83511 -3.54817  -25.89331 1.000 63.06391  ? 11  GLN   A CA     1 
ATOM   62   C C      . GLN   A 1 18  ? -20.83757 -4.68863  -26.03853 1.000 57.25439  ? 11  GLN   A C      1 
ATOM   63   O O      . GLN   A 1 18  ? -20.28098 -5.18230  -25.05487 1.000 56.45080  ? 11  GLN   A O      1 
ATOM   64   C CB     . GLN   A 1 18  ? -21.24609 -2.23038  -26.40682 1.000 50.64580  ? 11  GLN   A CB     1 
ATOM   65   C CG     . GLN   A 1 18  ? -20.07526 -1.71507  -25.58608 1.000 51.85605  ? 11  GLN   A CG     1 
ATOM   66   C CD     . GLN   A 1 18  ? -19.54138 -0.39425  -26.10100 1.000 57.25506  ? 11  GLN   A CD     1 
ATOM   67   O OE1    . GLN   A 1 18  ? -19.10055 0.45518   -25.32675 1.000 66.41023  ? 11  GLN   A OE1    1 
ATOM   68   N NE2    . GLN   A 1 18  ? -19.57688 -0.21469  -27.41590 1.000 48.61950  ? 11  GLN   A NE2    1 
ATOM   69   N N      . GLU   A 1 19  ? -20.62061 -5.10512  -27.28246 1.000 56.43872  ? 12  GLU   A N      1 
ATOM   70   C CA     . GLU   A 1 19  ? -19.68167 -6.17122  -27.60209 1.000 58.16558  ? 12  GLU   A CA     1 
ATOM   71   C C      . GLU   A 1 19  ? -18.53231 -5.60937  -28.42652 1.000 57.57428  ? 12  GLU   A C      1 
ATOM   72   O O      . GLU   A 1 19  ? -18.75782 -4.93056  -29.43383 1.000 65.15493  ? 12  GLU   A O      1 
ATOM   73   C CB     . GLU   A 1 19  ? -20.37103 -7.30785  -28.36137 1.000 70.76371  ? 12  GLU   A CB     1 
ATOM   74   C CG     . GLU   A 1 19  ? -19.51175 -8.55690  -28.50379 1.000 66.52082  ? 12  GLU   A CG     1 
ATOM   75   C CD     . GLU   A 1 19  ? -20.30154 -9.76738  -28.96406 1.000 67.62393  ? 12  GLU   A CD     1 
ATOM   76   O OE1    . GLU   A 1 19  ? -21.39924 -9.58397  -29.53066 1.000 68.07904  ? 12  GLU   A OE1    1 
ATOM   77   O OE2    . GLU   A 1 19  ? -19.82305 -10.90358 -28.75868 1.000 76.21028  ? 12  GLU   A OE2    1 
ATOM   78   N N      . LEU   A 1 20  ? -17.30526 -5.89401  -27.99560 1.000 63.05182  ? 13  LEU   A N      1 
ATOM   79   C CA     . LEU   A 1 20  ? -16.10540 -5.46963  -28.70770 1.000 69.46252  ? 13  LEU   A CA     1 
ATOM   80   C C      . LEU   A 1 20  ? -15.11635 -6.62332  -28.70998 1.000 70.66164  ? 13  LEU   A C      1 
ATOM   81   O O      . LEU   A 1 20  ? -14.75833 -7.13546  -27.64494 1.000 67.87864  ? 13  LEU   A O      1 
ATOM   82   C CB     . LEU   A 1 20  ? -15.48160 -4.22770  -28.06220 1.000 62.22298  ? 13  LEU   A CB     1 
ATOM   83   C CG     . LEU   A 1 20  ? -16.33163 -2.95614  -28.03094 1.000 64.57450  ? 13  LEU   A CG     1 
ATOM   84   C CD1    . LEU   A 1 20  ? -17.28366 -2.97606  -26.84571 1.000 67.55518  ? 13  LEU   A CD1    1 
ATOM   85   C CD2    . LEU   A 1 20  ? -15.44595 -1.71991  -27.99023 1.000 54.01676  ? 13  LEU   A CD2    1 
ATOM   86   N N      . ASN   A 1 21  ? -14.67862 -7.03110  -29.90136 1.000 78.98594  ? 14  ASN   A N      1 
ATOM   87   C CA     . ASN   A 1 21  ? -13.72227 -8.12749  -30.04825 1.000 78.05860  ? 14  ASN   A CA     1 
ATOM   88   C C      . ASN   A 1 21  ? -14.27548 -9.41636  -29.44200 1.000 72.68121  ? 14  ASN   A C      1 
ATOM   89   O O      . ASN   A 1 21  ? -13.58986 -10.13406 -28.71067 1.000 75.24535  ? 14  ASN   A O      1 
ATOM   90   C CB     . ASN   A 1 21  ? -12.37274 -7.76250  -29.42542 1.000 75.80115  ? 14  ASN   A CB     1 
ATOM   91   C CG     . ASN   A 1 21  ? -11.64617 -6.68214  -30.20129 1.000 82.24487  ? 14  ASN   A CG     1 
ATOM   92   O OD1    . ASN   A 1 21  ? -12.24208 -5.98172  -31.01986 1.000 74.09348  ? 14  ASN   A OD1    1 
ATOM   93   N ND2    . ASN   A 1 21  ? -10.35063 -6.54073  -29.94639 1.000 86.73658  ? 14  ASN   A ND2    1 
ATOM   94   N N      . LYS   A 1 22  ? -15.53739 -9.70755  -29.75461 1.000 65.62023  ? 15  LYS   A N      1 
ATOM   95   C CA     . LYS   A 1 22  ? -16.23497 -10.87921 -29.23165 1.000 67.92406  ? 15  LYS   A CA     1 
ATOM   96   C C      . LYS   A 1 22  ? -16.30401 -10.87352 -27.70762 1.000 67.78894  ? 15  LYS   A C      1 
ATOM   97   O O      . LYS   A 1 22  ? -16.46036 -11.92890 -27.08419 1.000 70.43870  ? 15  LYS   A O      1 
ATOM   98   C CB     . LYS   A 1 22  ? -15.58724 -12.17620 -29.73146 1.000 62.89088  ? 15  LYS   A CB     1 
ATOM   99   C CG     . LYS   A 1 22  ? -14.92667 -12.04823 -31.09573 1.000 65.10447  ? 15  LYS   A CG     1 
ATOM   100  C CD     . LYS   A 1 22  ? -13.82536 -13.07767 -31.28019 1.000 72.02219  ? 15  LYS   A CD     1 
ATOM   101  C CE     . LYS   A 1 22  ? -14.39257 -14.48445 -31.31671 1.000 60.74215  ? 15  LYS   A CE     1 
ATOM   102  N NZ     . LYS   A 1 22  ? -14.92368 -14.82337 -32.66648 1.000 62.93879  ? 15  LYS   A NZ     1 
ATOM   103  N N      . THR   A 1 23  ? -16.19066 -9.69557  -27.09902 1.000 57.63500  ? 16  THR   A N      1 
ATOM   104  C CA     . THR   A 1 23  ? -16.25519 -9.52465  -25.65654 1.000 58.14131  ? 16  THR   A CA     1 
ATOM   105  C C      . THR   A 1 23  ? -17.39533 -8.57563  -25.30715 1.000 63.80750  ? 16  THR   A C      1 
ATOM   106  O O      . THR   A 1 23  ? -17.81907 -7.75436  -26.12474 1.000 66.32769  ? 16  THR   A O      1 
ATOM   107  C CB     . THR   A 1 23  ? -14.92958 -8.98057  -25.10081 1.000 61.99092  ? 16  THR   A CB     1 
ATOM   108  O OG1    . THR   A 1 23  ? -13.84811 -9.81788  -25.52927 1.000 68.55222  ? 16  THR   A OG1    1 
ATOM   109  C CG2    . THR   A 1 23  ? -14.95849 -8.93678  -23.58029 1.000 51.02995  ? 16  THR   A CG2    1 
ATOM   110  N N      . ILE   A 1 24  ? -17.89167 -8.69381  -24.07838 1.000 53.84476  ? 17  ILE   A N      1 
ATOM   111  C CA     . ILE   A 1 24  ? -19.00285 -7.88270  -23.59105 1.000 62.98760  ? 17  ILE   A CA     1 
ATOM   112  C C      . ILE   A 1 24  ? -18.45659 -6.86833  -22.59540 1.000 57.62019  ? 17  ILE   A C      1 
ATOM   113  O O      . ILE   A 1 24  ? -17.83288 -7.24316  -21.59441 1.000 54.76404  ? 17  ILE   A O      1 
ATOM   114  C CB     . ILE   A 1 24  ? -20.09976 -8.74743  -22.95138 1.000 53.81841  ? 17  ILE   A CB     1 
ATOM   115  C CG1    . ILE   A 1 24  ? -21.05248 -7.87670  -22.12954 1.000 59.77688  ? 17  ILE   A CG1    1 
ATOM   116  C CG2    . ILE   A 1 24  ? -19.48511 -9.83279  -22.08323 1.000 50.54116  ? 17  ILE   A CG2    1 
ATOM   117  C CD1    . ILE   A 1 24  ? -21.79437 -6.84596  -22.95112 1.000 65.24363  ? 17  ILE   A CD1    1 
ATOM   118  N N      . TRP   A 1 25  ? -18.70062 -5.58785  -22.86306 1.000 52.24916  ? 18  TRP   A N      1 
ATOM   119  C CA     . TRP   A 1 25  ? -18.25490 -4.49603  -22.00725 1.000 50.48875  ? 18  TRP   A CA     1 
ATOM   120  C C      . TRP   A 1 25  ? -19.46127 -3.81560  -21.37329 1.000 53.08580  ? 18  TRP   A C      1 
ATOM   121  O O      . TRP   A 1 25  ? -20.38749 -3.40048  -22.07849 1.000 52.51887  ? 18  TRP   A O      1 
ATOM   122  C CB     . TRP   A 1 25  ? -17.43298 -3.47541  -22.79972 1.000 46.37987  ? 18  TRP   A CB     1 
ATOM   123  C CG     . TRP   A 1 25  ? -16.07080 -3.96307  -23.19299 1.000 51.08110  ? 18  TRP   A CG     1 
ATOM   124  C CD1    . TRP   A 1 25  ? -15.78186 -4.97249  -24.06394 1.000 53.01441  ? 18  TRP   A CD1    1 
ATOM   125  C CD2    . TRP   A 1 25  ? -14.81028 -3.45922  -22.73062 1.000 47.57648  ? 18  TRP   A CD2    1 
ATOM   126  N NE1    . TRP   A 1 25  ? -14.42139 -5.12986  -24.17220 1.000 53.76578  ? 18  TRP   A NE1    1 
ATOM   127  C CE2    . TRP   A 1 25  ? -13.80213 -4.21331  -23.36376 1.000 49.30728  ? 18  TRP   A CE2    1 
ATOM   128  C CE3    . TRP   A 1 25  ? -14.43700 -2.44516  -21.84296 1.000 33.08871  ? 18  TRP   A CE3    1 
ATOM   129  C CZ2    . TRP   A 1 25  ? -12.44599 -3.98565  -23.13804 1.000 41.76680  ? 18  TRP   A CZ2    1 
ATOM   130  C CZ3    . TRP   A 1 25  ? -13.08981 -2.22104  -21.61988 1.000 40.92827  ? 18  TRP   A CZ3    1 
ATOM   131  C CH2    . TRP   A 1 25  ? -12.11122 -2.98771  -22.26467 1.000 40.69513  ? 18  TRP   A CH2    1 
ATOM   132  N N      . GLU   A 1 26  ? -19.44567 -3.70540  -20.04547 1.000 46.95788  ? 19  GLU   A N      1 
ATOM   133  C CA     . GLU   A 1 26  ? -20.47916 -3.01104  -19.28182 1.000 48.99181  ? 19  GLU   A CA     1 
ATOM   134  C C      . GLU   A 1 26  ? -19.79680 -1.91337  -18.47585 1.000 43.29563  ? 19  GLU   A C      1 
ATOM   135  O O      . GLU   A 1 26  ? -19.07964 -2.20209  -17.51150 1.000 43.52092  ? 19  GLU   A O      1 
ATOM   136  C CB     . GLU   A 1 26  ? -21.23512 -3.97624  -18.36777 1.000 57.75180  ? 19  GLU   A CB     1 
ATOM   137  C CG     . GLU   A 1 26  ? -22.09017 -5.00165  -19.09788 1.000 67.38850  ? 19  GLU   A CG     1 
ATOM   138  C CD     . GLU   A 1 26  ? -22.67273 -6.04702  -18.16350 1.000 74.92214  ? 19  GLU   A CD     1 
ATOM   139  O OE1    . GLU   A 1 26  ? -23.68491 -5.75442  -17.49485 1.000 76.78567  ? 19  GLU   A OE1    1 
ATOM   140  O OE2    . GLU   A 1 26  ? -22.11870 -7.16383  -18.09647 1.000 63.01879  ? 19  GLU   A OE2    1 
ATOM   141  N N      . VAL   A 1 27  ? -20.01662 -0.66103  -18.86474 1.000 48.54320  ? 20  VAL   A N      1 
ATOM   142  C CA     . VAL   A 1 27  ? -19.28581 0.46264   -18.27972 1.000 39.49896  ? 20  VAL   A CA     1 
ATOM   143  C C      . VAL   A 1 27  ? -20.25222 1.59305   -17.96530 1.000 41.82783  ? 20  VAL   A C      1 
ATOM   144  O O      . VAL   A 1 27  ? -21.32710 1.70876   -18.56976 1.000 48.48068  ? 20  VAL   A O      1 
ATOM   145  C CB     . VAL   A 1 27  ? -18.17085 0.96988   -19.21413 1.000 35.40381  ? 20  VAL   A CB     1 
ATOM   146  C CG1    . VAL   A 1 27  ? -17.28091 -0.18372  -19.65276 1.000 33.34591  ? 20  VAL   A CG1    1 
ATOM   147  C CG2    . VAL   A 1 27  ? -18.77142 1.67549   -20.41994 1.000 40.50827  ? 20  VAL   A CG2    1 
ATOM   148  N N      . PRO   A 1 28  ? -19.89007 2.44614   -17.00790 1.000 43.12695  ? 21  PRO   A N      1 
ATOM   149  C CA     . PRO   A 1 28  ? -20.73093 3.60485   -16.68915 1.000 41.70407  ? 21  PRO   A CA     1 
ATOM   150  C C      . PRO   A 1 28  ? -20.92356 4.51803   -17.89237 1.000 44.11525  ? 21  PRO   A C      1 
ATOM   151  O O      . PRO   A 1 28  ? -20.11346 4.55683   -18.82122 1.000 39.06594  ? 21  PRO   A O      1 
ATOM   152  C CB     . PRO   A 1 28  ? -19.95199 4.31029   -15.57266 1.000 34.16246  ? 21  PRO   A CB     1 
ATOM   153  C CG     . PRO   A 1 28  ? -19.15058 3.21962   -14.93469 1.000 32.53849  ? 21  PRO   A CG     1 
ATOM   154  C CD     . PRO   A 1 28  ? -18.77631 2.28873   -16.05658 1.000 36.53281  ? 21  PRO   A CD     1 
ATOM   155  N N      . GLU   A 1 29  ? -22.02574 5.27261   -17.85476 1.000 48.00995  ? 22  GLU   A N      1 
ATOM   156  C CA     . GLU   A 1 29  ? -22.38209 6.13569   -18.97647 1.000 44.20386  ? 22  GLU   A CA     1 
ATOM   157  C C      . GLU   A 1 29  ? -21.32007 7.19120   -19.25106 1.000 38.68602  ? 22  GLU   A C      1 
ATOM   158  O O      . GLU   A 1 29  ? -21.20507 7.67109   -20.38445 1.000 34.66332  ? 22  GLU   A O      1 
ATOM   159  C CB     . GLU   A 1 29  ? -23.72062 6.82007   -18.70937 1.000 43.73432  ? 22  GLU   A CB     1 
ATOM   160  C CG     . GLU   A 1 29  ? -24.92086 5.89973   -18.69684 1.000 51.21042  ? 22  GLU   A CG     1 
ATOM   161  C CD     . GLU   A 1 29  ? -26.20282 6.65402   -18.42051 1.000 59.43156  ? 22  GLU   A CD     1 
ATOM   162  O OE1    . GLU   A 1 29  ? -26.11860 7.79509   -17.91879 1.000 53.41254  ? 22  GLU   A OE1    1 
ATOM   163  O OE2    . GLU   A 1 29  ? -27.29069 6.11136   -18.70448 1.000 65.67652  ? 22  GLU   A OE2    1 
ATOM   164  N N      . ARG   A 1 30  ? -20.54901 7.58130   -18.23335 1.000 37.07115  ? 23  ARG   A N      1 
ATOM   165  C CA     . ARG   A 1 30  ? -19.61364 8.68669   -18.41404 1.000 40.31456  ? 23  ARG   A CA     1 
ATOM   166  C C      . ARG   A 1 30  ? -18.55683 8.37115   -19.46484 1.000 37.85022  ? 23  ARG   A C      1 
ATOM   167  O O      . ARG   A 1 30  ? -18.07092 9.28161   -20.14543 1.000 35.72661  ? 23  ARG   A O      1 
ATOM   168  C CB     . ARG   A 1 30  ? -18.95342 9.04606   -17.08297 1.000 41.29034  ? 23  ARG   A CB     1 
ATOM   169  C CG     . ARG   A 1 30  ? -18.27859 7.88651   -16.37681 1.000 41.27817  ? 23  ARG   A CG     1 
ATOM   170  C CD     . ARG   A 1 30  ? -17.60328 8.35497   -15.09760 1.000 48.88002  ? 23  ARG   A CD     1 
ATOM   171  N NE     . ARG   A 1 30  ? -16.49162 9.26145   -15.36149 1.000 40.19705  ? 23  ARG   A NE     1 
ATOM   172  C CZ     . ARG   A 1 30  ? -15.59941 9.63359   -14.45326 1.000 42.23908  ? 23  ARG   A CZ     1 
ATOM   173  N NH1    . ARG   A 1 30  ? -15.66657 9.20725   -13.20283 1.000 49.01243  ? 23  ARG   A NH1    1 
ATOM   174  N NH2    . ARG   A 1 30  ? -14.61575 10.45428  -14.80757 1.000 38.69900  ? 23  ARG   A NH2    1 
ATOM   175  N N      . TYR   A 1 31  ? -18.18914 7.10177   -19.61661 1.000 37.43061  ? 24  TYR   A N      1 
ATOM   176  C CA     . TYR   A 1 31  ? -17.19115 6.69936   -20.60017 1.000 36.63438  ? 24  TYR   A CA     1 
ATOM   177  C C      . TYR   A 1 31  ? -17.88842 6.36950   -21.91475 1.000 37.14565  ? 24  TYR   A C      1 
ATOM   178  O O      . TYR   A 1 31  ? -18.68231 5.42460   -21.98379 1.000 38.94494  ? 24  TYR   A O      1 
ATOM   179  C CB     . TYR   A 1 31  ? -16.38243 5.50807   -20.09068 1.000 34.90542  ? 24  TYR   A CB     1 
ATOM   180  C CG     . TYR   A 1 31  ? -15.80220 5.73058   -18.71336 1.000 34.27260  ? 24  TYR   A CG     1 
ATOM   181  C CD1    . TYR   A 1 31  ? -14.83970 6.70767   -18.49382 1.000 35.89907  ? 24  TYR   A CD1    1 
ATOM   182  C CD2    . TYR   A 1 31  ? -16.22535 4.97372   -17.63047 1.000 36.40509  ? 24  TYR   A CD2    1 
ATOM   183  C CE1    . TYR   A 1 31  ? -14.31065 6.91877   -17.23488 1.000 39.05548  ? 24  TYR   A CE1    1 
ATOM   184  C CE2    . TYR   A 1 31  ? -15.70256 5.17710   -16.36910 1.000 35.08397  ? 24  TYR   A CE2    1 
ATOM   185  C CZ     . TYR   A 1 31  ? -14.74610 6.15012   -16.17637 1.000 38.34607  ? 24  TYR   A CZ     1 
ATOM   186  O OH     . TYR   A 1 31  ? -14.22449 6.35363   -14.91969 1.000 42.62438  ? 24  TYR   A OH     1 
ATOM   187  N N      . GLN   A 1 32  ? -17.58873 7.14662   -22.95227 1.000 38.34541  ? 25  GLN   A N      1 
ATOM   188  C CA     . GLN   A 1 32  ? -18.26682 7.05251   -24.23458 1.000 39.05127  ? 25  GLN   A CA     1 
ATOM   189  C C      . GLN   A 1 32  ? -17.27776 6.71749   -25.34305 1.000 41.17457  ? 25  GLN   A C      1 
ATOM   190  O O      . GLN   A 1 32  ? -16.06784 6.92522   -25.21473 1.000 47.67645  ? 25  GLN   A O      1 
ATOM   191  C CB     . GLN   A 1 32  ? -18.98974 8.36302   -24.57445 1.000 34.38407  ? 25  GLN   A CB     1 
ATOM   192  C CG     . GLN   A 1 32  ? -20.07845 8.74746   -23.59132 1.000 34.79563  ? 25  GLN   A CG     1 
ATOM   193  C CD     . GLN   A 1 32  ? -21.36911 7.99620   -23.83805 1.000 36.62220  ? 25  GLN   A CD     1 
ATOM   194  O OE1    . GLN   A 1 32  ? -21.92323 8.03618   -24.93615 1.000 45.24379  ? 25  GLN   A OE1    1 
ATOM   195  N NE2    . GLN   A 1 32  ? -21.85458 7.30245   -22.81586 1.000 36.62643  ? 25  GLN   A NE2    1 
ATOM   196  N N      . ASN   A 1 33  ? -17.81821 6.19491   -26.44398 1.000 37.47024  ? 26  ASN   A N      1 
ATOM   197  C CA     . ASN   A 1 33  ? -17.04436 5.93714   -27.65750 1.000 39.86128  ? 26  ASN   A CA     1 
ATOM   198  C C      . ASN   A 1 33  ? -15.88914 4.97430   -27.38604 1.000 48.83623  ? 26  ASN   A C      1 
ATOM   199  O O      . ASN   A 1 33  ? -14.72473 5.26470   -27.66821 1.000 42.58158  ? 26  ASN   A O      1 
ATOM   200  C CB     . ASN   A 1 33  ? -16.53883 7.24728   -28.26518 1.000 37.63169  ? 26  ASN   A CB     1 
ATOM   201  C CG     . ASN   A 1 33  ? -17.66529 8.21171   -28.58401 1.000 58.04912  ? 26  ASN   A CG     1 
ATOM   202  O OD1    . ASN   A 1 33  ? -18.23538 8.83625   -27.68897 1.000 55.77929  ? 26  ASN   A OD1    1 
ATOM   203  N ND2    . ASN   A 1 33  ? -17.99542 8.33410   -29.86454 1.000 68.52297  ? 26  ASN   A ND2    1 
ATOM   204  N N      . LEU   A 1 34  ? -16.22329 3.81010   -26.83565 1.000 44.56565  ? 27  LEU   A N      1 
ATOM   205  C CA     . LEU   A 1 34  ? -15.20902 2.80185   -26.56455 1.000 40.77930  ? 27  LEU   A CA     1 
ATOM   206  C C      . LEU   A 1 34  ? -14.57584 2.32775   -27.86632 1.000 43.71548  ? 27  LEU   A C      1 
ATOM   207  O O      . LEU   A 1 34  ? -15.27264 2.04793   -28.84626 1.000 40.92633  ? 27  LEU   A O      1 
ATOM   208  C CB     . LEU   A 1 34  ? -15.82247 1.62495   -25.80743 1.000 41.61498  ? 27  LEU   A CB     1 
ATOM   209  C CG     . LEU   A 1 34  ? -15.60954 1.64982   -24.29285 1.000 49.44830  ? 27  LEU   A CG     1 
ATOM   210  C CD1    . LEU   A 1 34  ? -16.28707 2.86576   -23.67704 1.000 38.93896  ? 27  LEU   A CD1    1 
ATOM   211  C CD2    . LEU   A 1 34  ? -16.10928 0.36356   -23.65131 1.000 41.66388  ? 27  LEU   A CD2    1 
ATOM   212  N N      . SER   A 1 35  ? -13.24763 2.24566   -27.87433 1.000 36.74925  ? 28  SER   A N      1 
ATOM   213  C CA     . SER   A 1 35  ? -12.50948 1.82114   -29.05608 1.000 40.30924  ? 28  SER   A CA     1 
ATOM   214  C C      . SER   A 1 35  ? -11.33823 0.93785   -28.64510 1.000 40.72898  ? 28  SER   A C      1 
ATOM   215  O O      . SER   A 1 35  ? -10.49325 1.35658   -27.84191 1.000 35.66859  ? 28  SER   A O      1 
ATOM   216  C CB     . SER   A 1 35  ? -12.01834 3.03330   -29.84910 1.000 41.19458  ? 28  SER   A CB     1 
ATOM   217  O OG     . SER   A 1 35  ? -11.35497 2.63361   -31.03547 1.000 50.57209  ? 28  SER   A OG     1 
ATOM   218  N N      . PRO   A 1 36  ? -11.25242 -0.28284  -29.16912 1.000 43.38768  ? 29  PRO   A N      1 
ATOM   219  C CA     . PRO   A 1 36  ? -10.17788 -1.18538  -28.74725 1.000 36.34867  ? 29  PRO   A CA     1 
ATOM   220  C C      . PRO   A 1 36  ? -8.81566  -0.63241  -29.13164 1.000 34.30629  ? 29  PRO   A C      1 
ATOM   221  O O      . PRO   A 1 36  ? -8.62373  -0.10205  -30.22912 1.000 36.94303  ? 29  PRO   A O      1 
ATOM   222  C CB     . PRO   A 1 36  ? -10.49123 -2.48951  -29.49205 1.000 42.28845  ? 29  PRO   A CB     1 
ATOM   223  C CG     . PRO   A 1 36  ? -11.92460 -2.36248  -29.92288 1.000 48.66709  ? 29  PRO   A CG     1 
ATOM   224  C CD     . PRO   A 1 36  ? -12.13690 -0.90380  -30.16514 1.000 35.51701  ? 29  PRO   A CD     1 
ATOM   225  N N      . VAL   A 1 37  ? -7.87021  -0.75276  -28.19977 1.000 37.07895  ? 30  VAL   A N      1 
ATOM   226  C CA     . VAL   A 1 37  ? -6.47438  -0.38907  -28.43220 1.000 35.33883  ? 30  VAL   A CA     1 
ATOM   227  C C      . VAL   A 1 37  ? -5.61120  -1.63882  -28.63119 1.000 44.01388  ? 30  VAL   A C      1 
ATOM   228  O O      . VAL   A 1 37  ? -4.91623  -1.77415  -29.64263 1.000 51.81457  ? 30  VAL   A O      1 
ATOM   229  C CB     . VAL   A 1 37  ? -5.92961  0.49156   -27.28562 1.000 34.65644  ? 30  VAL   A CB     1 
ATOM   230  C CG1    . VAL   A 1 37  ? -4.51456  0.94422   -27.59554 1.000 36.70826  ? 30  VAL   A CG1    1 
ATOM   231  C CG2    . VAL   A 1 37  ? -6.85978  1.65886   -27.03084 1.000 30.69582  ? 30  VAL   A CG2    1 
ATOM   232  N N      . GLY   A 1 38  ? -5.63782  -2.55952  -27.67306 1.000 40.00086  ? 31  GLY   A N      1 
ATOM   233  C CA     . GLY   A 1 38  ? -4.86235  -3.77552  -27.77455 1.000 49.17001  ? 31  GLY   A CA     1 
ATOM   234  C C      . GLY   A 1 38  ? -5.32358  -4.76094  -26.72939 1.000 42.97232  ? 31  GLY   A C      1 
ATOM   235  O O      . GLY   A 1 38  ? -6.37766  -4.59212  -26.11090 1.000 40.18816  ? 31  GLY   A O      1 
ATOM   236  N N      . SER   A 1 39  ? -4.51192  -5.79353  -26.53395 1.000 41.91895  ? 32  SER   A N      1 
ATOM   237  C CA     . SER   A 1 39  ? -4.85178  -6.83557  -25.58323 1.000 44.19603  ? 32  SER   A CA     1 
ATOM   238  C C      . SER   A 1 39  ? -3.58365  -7.40362  -24.96926 1.000 51.67812  ? 32  SER   A C      1 
ATOM   239  O O      . SER   A 1 39  ? -2.52098  -7.42229  -25.59688 1.000 51.90163  ? 32  SER   A O      1 
ATOM   240  C CB     . SER   A 1 39  ? -5.66121  -7.95579  -26.24221 1.000 42.63282  ? 32  SER   A CB     1 
ATOM   241  O OG     . SER   A 1 39  ? -6.34735  -8.71713  -25.26389 1.000 54.50246  ? 32  SER   A OG     1 
ATOM   242  N N      . GLY   A 1 40  ? -3.71431  -7.86294  -23.72841 1.000 54.79793  ? 33  GLY   A N      1 
ATOM   243  C CA     . GLY   A 1 40  ? -2.65427  -8.57863  -23.05014 1.000 51.05573  ? 33  GLY   A CA     1 
ATOM   244  C C      . GLY   A 1 40  ? -3.09353  -9.98135  -22.68577 1.000 52.50220  ? 33  GLY   A C      1 
ATOM   245  O O      . GLY   A 1 40  ? -4.08932  -10.47954 -23.21940 1.000 50.65528  ? 33  GLY   A O      1 
ATOM   246  N N      . ALA   A 1 41  ? -2.36698  -10.63075 -21.77506 1.000 61.69650  ? 34  ALA   A N      1 
ATOM   247  C CA     . ALA   A 1 41  ? -2.72886  -11.98590 -21.37657 1.000 53.65691  ? 34  ALA   A CA     1 
ATOM   248  C C      . ALA   A 1 41  ? -3.78432  -12.00128 -20.27794 1.000 57.64788  ? 34  ALA   A C      1 
ATOM   249  O O      . ALA   A 1 41  ? -4.53761  -12.97493 -20.16475 1.000 64.68077  ? 34  ALA   A O      1 
ATOM   250  C CB     . ALA   A 1 41  ? -1.48579  -12.75154 -20.92065 1.000 54.81265  ? 34  ALA   A CB     1 
ATOM   251  N N      . TYR   A 1 42  ? -3.86077  -10.94455 -19.46882 1.000 52.36552  ? 35  TYR   A N      1 
ATOM   252  C CA     . TYR   A 1 42  ? -4.80094  -10.87968 -18.35755 1.000 45.84015  ? 35  TYR   A CA     1 
ATOM   253  C C      . TYR   A 1 42  ? -5.91136  -9.85994  -18.57928 1.000 48.66880  ? 35  TYR   A C      1 
ATOM   254  O O      . TYR   A 1 42  ? -6.68614  -9.59384  -17.65443 1.000 46.05355  ? 35  TYR   A O      1 
ATOM   255  C CB     . TYR   A 1 42  ? -4.06091  -10.56765 -17.05454 1.000 50.81082  ? 35  TYR   A CB     1 
ATOM   256  C CG     . TYR   A 1 42  ? -2.81375  -11.39519 -16.84045 1.000 53.32899  ? 35  TYR   A CG     1 
ATOM   257  C CD1    . TYR   A 1 42  ? -2.79076  -12.74783 -17.15416 1.000 51.38160  ? 35  TYR   A CD1    1 
ATOM   258  C CD2    . TYR   A 1 42  ? -1.65898  -10.82378 -16.32308 1.000 47.12840  ? 35  TYR   A CD2    1 
ATOM   259  C CE1    . TYR   A 1 42  ? -1.65168  -13.50697 -16.96043 1.000 58.00434  ? 35  TYR   A CE1    1 
ATOM   260  C CE2    . TYR   A 1 42  ? -0.51507  -11.57493 -16.12599 1.000 47.63138  ? 35  TYR   A CE2    1 
ATOM   261  C CZ     . TYR   A 1 42  ? -0.51698  -12.91572 -16.44604 1.000 62.60661  ? 35  TYR   A CZ     1 
ATOM   262  O OH     . TYR   A 1 42  ? 0.61881   -13.66793 -16.25106 1.000 55.91275  ? 35  TYR   A OH     1 
ATOM   263  N N      . GLY   A 1 43  ? -6.01212  -9.28363  -19.77417 1.000 46.69951  ? 36  GLY   A N      1 
ATOM   264  C CA     . GLY   A 1 43  ? -7.06067  -8.31823  -20.03756 1.000 45.46135  ? 36  GLY   A CA     1 
ATOM   265  C C      . GLY   A 1 43  ? -6.90489  -7.56797  -21.34333 1.000 49.73572  ? 36  GLY   A C      1 
ATOM   266  O O      . GLY   A 1 43  ? -5.82018  -7.54091  -21.93242 1.000 54.98257  ? 36  GLY   A O      1 
ATOM   267  N N      . SER   A 1 44  ? -7.99142  -6.95723  -21.80541 1.000 39.78676  ? 37  SER   A N      1 
ATOM   268  C CA     . SER   A 1 44  ? -7.99848  -6.15403  -23.01694 1.000 36.92050  ? 37  SER   A CA     1 
ATOM   269  C C      . SER   A 1 44  ? -8.27462  -4.69797  -22.66702 1.000 38.12929  ? 37  SER   A C      1 
ATOM   270  O O      . SER   A 1 44  ? -8.93281  -4.39667  -21.66714 1.000 38.68769  ? 37  SER   A O      1 
ATOM   271  C CB     . SER   A 1 44  ? -9.04656  -6.66389  -24.00940 1.000 38.31462  ? 37  SER   A CB     1 
ATOM   272  O OG     . SER   A 1 44  ? -10.33647 -6.68582  -23.42334 1.000 38.13917  ? 37  SER   A OG     1 
ATOM   273  N N      . VAL   A 1 45  ? -7.76935  -3.79450  -23.50218 1.000 32.81532  ? 38  VAL   A N      1 
ATOM   274  C CA     . VAL   A 1 45  ? -7.79934  -2.36560  -23.22299 1.000 28.17078  ? 38  VAL   A CA     1 
ATOM   275  C C      . VAL   A 1 45  ? -8.57133  -1.65128  -24.32205 1.000 27.00020  ? 38  VAL   A C      1 
ATOM   276  O O      . VAL   A 1 45  ? -8.39650  -1.94026  -25.51101 1.000 31.22772  ? 38  VAL   A O      1 
ATOM   277  C CB     . VAL   A 1 45  ? -6.37547  -1.78750  -23.09408 1.000 33.49194  ? 38  VAL   A CB     1 
ATOM   278  C CG1    . VAL   A 1 45  ? -6.43213  -0.31179  -22.73315 1.000 30.86866  ? 38  VAL   A CG1    1 
ATOM   279  C CG2    . VAL   A 1 45  ? -5.58347  -2.56777  -22.05699 1.000 33.41613  ? 38  VAL   A CG2    1 
ATOM   280  N N      . CYS   A 1 46  ? -9.42056  -0.71281  -23.91591 1.000 32.21981  ? 39  CYS   A N      1 
ATOM   281  C CA     . CYS   A 1 46  ? -10.17203 0.13540   -24.82608 1.000 37.95818  ? 39  CYS   A CA     1 
ATOM   282  C C      . CYS   A 1 46  ? -9.90847  1.59782   -24.50015 1.000 32.57620  ? 39  CYS   A C      1 
ATOM   283  O O      . CYS   A 1 46  ? -9.71054  1.96594   -23.33816 1.000 33.41248  ? 39  CYS   A O      1 
ATOM   284  C CB     . CYS   A 1 46  ? -11.67863 -0.14044  -24.73685 1.000 33.89975  ? 39  CYS   A CB     1 
ATOM   285  S SG     . CYS   A 1 46  ? -12.29550 -1.37856  -25.89451 1.000 37.69735  ? 39  CYS   A SG     1 
ATOM   286  N N      . ALA   A 1 47  ? -9.90017  2.42678   -25.53723 1.000 38.72714  ? 40  ALA   A N      1 
ATOM   287  C CA     . ALA   A 1 47  ? -9.89763  3.86988   -25.36517 1.000 31.22178  ? 40  ALA   A CA     1 
ATOM   288  C C      . ALA   A 1 47  ? -11.33150 4.36030   -25.21282 1.000 31.10272  ? 40  ALA   A C      1 
ATOM   289  O O      . ALA   A 1 47  ? -12.26019 3.80948   -25.80980 1.000 31.81266  ? 40  ALA   A O      1 
ATOM   290  C CB     . ALA   A 1 47  ? -9.22463  4.56001   -26.55249 1.000 27.94327  ? 40  ALA   A CB     1 
ATOM   291  N N      . ALA   A 1 48  ? -11.51013 5.39672   -24.39690 1.000 39.82267  ? 41  ALA   A N      1 
ATOM   292  C CA     . ALA   A 1 48  ? -12.84534 5.91499   -24.13829 1.000 41.58185  ? 41  ALA   A CA     1 
ATOM   293  C C      . ALA   A 1 48  ? -12.78070 7.41710   -23.90986 1.000 41.82573  ? 41  ALA   A C      1 
ATOM   294  O O      . ALA   A 1 48  ? -11.71491 7.98571   -23.65738 1.000 31.27781  ? 41  ALA   A O      1 
ATOM   295  C CB     . ALA   A 1 48  ? -13.49566 5.22310   -22.93439 1.000 35.30218  ? 41  ALA   A CB     1 
ATOM   296  N N      . PHE   A 1 49  ? -13.94642 8.05226   -24.00207 1.000 40.34683  ? 42  PHE   A N      1 
ATOM   297  C CA     . PHE   A 1 49  ? -14.10369 9.47918   -23.75302 1.000 39.36454  ? 42  PHE   A CA     1 
ATOM   298  C C      . PHE   A 1 49  ? -14.77771 9.65838   -22.39994 1.000 38.29508  ? 42  PHE   A C      1 
ATOM   299  O O      . PHE   A 1 49  ? -15.93431 9.26137   -22.22242 1.000 37.35294  ? 42  PHE   A O      1 
ATOM   300  C CB     . PHE   A 1 49  ? -14.92260 10.14210  -24.86213 1.000 42.87260  ? 42  PHE   A CB     1 
ATOM   301  C CG     . PHE   A 1 49  ? -14.93400 11.64637  -24.79882 1.000 42.98442  ? 42  PHE   A CG     1 
ATOM   302  C CD1    . PHE   A 1 49  ? -14.29181 12.39812  -25.76962 1.000 50.55289  ? 42  PHE   A CD1    1 
ATOM   303  C CD2    . PHE   A 1 49  ? -15.59650 12.30902  -23.77784 1.000 48.20682  ? 42  PHE   A CD2    1 
ATOM   304  C CE1    . PHE   A 1 49  ? -14.30400 13.78126  -25.71704 1.000 51.99695  ? 42  PHE   A CE1    1 
ATOM   305  C CE2    . PHE   A 1 49  ? -15.61047 13.68951  -23.71981 1.000 53.41720  ? 42  PHE   A CE2    1 
ATOM   306  C CZ     . PHE   A 1 49  ? -14.96470 14.42621  -24.69028 1.000 50.47160  ? 42  PHE   A CZ     1 
ATOM   307  N N      . ASP   A 1 50  ? -14.05627 10.25537  -21.45411 1.000 35.21240  ? 43  ASP   A N      1 
ATOM   308  C CA     . ASP   A 1 50  ? -14.56976 10.49516  -20.10652 1.000 39.16866  ? 43  ASP   A CA     1 
ATOM   309  C C      . ASP   A 1 50  ? -15.33207 11.81521  -20.11385 1.000 41.55545  ? 43  ASP   A C      1 
ATOM   310  O O      . ASP   A 1 50  ? -14.73386 12.89234  -20.06022 1.000 40.40758  ? 43  ASP   A O      1 
ATOM   311  C CB     . ASP   A 1 50  ? -13.42888 10.50860  -19.09598 1.000 38.16605  ? 43  ASP   A CB     1 
ATOM   312  C CG     . ASP   A 1 50  ? -13.91729 10.59533  -17.66532 1.000 43.21104  ? 43  ASP   A CG     1 
ATOM   313  O OD1    . ASP   A 1 50  ? -15.10933 10.90310  -17.45610 1.000 42.39020  ? 43  ASP   A OD1    1 
ATOM   314  O OD2    . ASP   A 1 50  ? -13.10799 10.35383  -16.74490 1.000 41.35065  ? 43  ASP   A OD2    1 
ATOM   315  N N      . THR   A 1 51  ? -16.66399 11.73219  -20.16831 1.000 37.68444  ? 44  THR   A N      1 
ATOM   316  C CA     . THR   A 1 51  ? -17.47978 12.93729  -20.27387 1.000 40.70151  ? 44  THR   A CA     1 
ATOM   317  C C      . THR   A 1 51  ? -17.36235 13.83418  -19.04854 1.000 43.34146  ? 44  THR   A C      1 
ATOM   318  O O      . THR   A 1 51  ? -17.66283 15.02890  -19.14028 1.000 46.28399  ? 44  THR   A O      1 
ATOM   319  C CB     . THR   A 1 51  ? -18.94855 12.56982  -20.50107 1.000 35.68856  ? 44  THR   A CB     1 
ATOM   320  O OG1    . THR   A 1 51  ? -19.41055 11.73620  -19.43031 1.000 37.29174  ? 44  THR   A OG1    1 
ATOM   321  C CG2    . THR   A 1 51  ? -19.11833 11.83579  -21.82291 1.000 34.14670  ? 44  THR   A CG2    1 
ATOM   322  N N      . LYS   A 1 52  ? -16.93761 13.29336  -17.90553 1.000 46.72125  ? 45  LYS   A N      1 
ATOM   323  C CA     . LYS   A 1 52  ? -16.82884 14.11822  -16.70734 1.000 48.06412  ? 45  LYS   A CA     1 
ATOM   324  C C      . LYS   A 1 52  ? -15.64609 15.07555  -16.78386 1.000 49.40323  ? 45  LYS   A C      1 
ATOM   325  O O      . LYS   A 1 52  ? -15.67946 16.14893  -16.17109 1.000 51.85938  ? 45  LYS   A O      1 
ATOM   326  C CB     . LYS   A 1 52  ? -16.71710 13.23188  -15.46602 1.000 40.17491  ? 45  LYS   A CB     1 
ATOM   327  C CG     . LYS   A 1 52  ? -18.00289 12.50037  -15.11242 1.000 49.04229  ? 45  LYS   A CG     1 
ATOM   328  C CD     . LYS   A 1 52  ? -18.25772 12.50635  -13.61208 1.000 56.42592  ? 45  LYS   A CD     1 
ATOM   329  C CE     . LYS   A 1 52  ? -16.96238 12.38623  -12.82666 1.000 61.73285  ? 45  LYS   A CE     1 
ATOM   330  N NZ     . LYS   A 1 52  ? -17.10573 11.48054  -11.65171 1.000 58.99920  ? 45  LYS   A NZ     1 
ATOM   331  N N      . THR   A 1 53  ? -14.60016 14.71401  -17.52887 1.000 48.79972  ? 46  THR   A N      1 
ATOM   332  C CA     . THR   A 1 53  ? -13.39320 15.52252  -17.61018 1.000 47.19226  ? 46  THR   A CA     1 
ATOM   333  C C      . THR   A 1 53  ? -13.08305 16.04667  -19.00351 1.000 46.65363  ? 46  THR   A C      1 
ATOM   334  O O      . THR   A 1 53  ? -12.27399 16.97337  -19.12371 1.000 50.70610  ? 46  THR   A O      1 
ATOM   335  C CB     . THR   A 1 53  ? -12.17592 14.72389  -17.11597 1.000 47.40427  ? 46  THR   A CB     1 
ATOM   336  O OG1    . THR   A 1 53  ? -11.83381 13.72440  -18.08445 1.000 52.16284  ? 46  THR   A OG1    1 
ATOM   337  C CG2    . THR   A 1 53  ? -12.48549 14.04847  -15.79030 1.000 49.68033  ? 46  THR   A CG2    1 
ATOM   338  N N      . GLY   A 1 54  ? -13.69383 15.49535  -20.04902 1.000 45.18802  ? 47  GLY   A N      1 
ATOM   339  C CA     . GLY   A 1 54  ? -13.34993 15.87470  -21.40245 1.000 43.31668  ? 47  GLY   A CA     1 
ATOM   340  C C      . GLY   A 1 54  ? -12.06528 15.27257  -21.92082 1.000 49.10960  ? 47  GLY   A C      1 
ATOM   341  O O      . GLY   A 1 54  ? -11.59529 15.67885  -22.98982 1.000 38.81463  ? 47  GLY   A O      1 
ATOM   342  N N      . HIS   A 1 55  ? -11.48001 14.32248  -21.19864 1.000 40.24662  ? 48  HIS   A N      1 
ATOM   343  C CA     . HIS   A 1 55  ? -10.25255 13.65977  -21.60583 1.000 45.01379  ? 48  HIS   A CA     1 
ATOM   344  C C      . HIS   A 1 55  ? -10.55105 12.23770  -22.05843 1.000 37.35163  ? 48  HIS   A C      1 
ATOM   345  O O      . HIS   A 1 55  ? -11.51086 11.60989  -21.60233 1.000 35.78182  ? 48  HIS   A O      1 
ATOM   346  C CB     . HIS   A 1 55  ? -9.23385  13.62347  -20.46118 1.000 41.92207  ? 48  HIS   A CB     1 
ATOM   347  C CG     . HIS   A 1 55  ? -8.78466  14.97584  -20.00385 1.000 49.06188  ? 48  HIS   A CG     1 
ATOM   348  N ND1    . HIS   A 1 55  ? -8.71109  15.32345  -18.67184 1.000 52.47767  ? 48  HIS   A ND1    1 
ATOM   349  C CD2    . HIS   A 1 55  ? -8.38090  16.06493  -20.69994 1.000 43.94484  ? 48  HIS   A CD2    1 
ATOM   350  C CE1    . HIS   A 1 55  ? -8.28367  16.56914  -18.56717 1.000 53.17543  ? 48  HIS   A CE1    1 
ATOM   351  N NE2    . HIS   A 1 55  ? -8.07602  17.04184  -19.78317 1.000 54.58426  ? 48  HIS   A NE2    1 
ATOM   352  N N      . ARG   A 1 56  ? -9.72036  11.73695  -22.96668 1.000 44.12010  ? 49  ARG   A N      1 
ATOM   353  C CA     . ARG   A 1 56  ? -9.75500  10.32651  -23.31593 1.000 37.24386  ? 49  ARG   A CA     1 
ATOM   354  C C      . ARG   A 1 56  ? -8.99304  9.52871   -22.26769 1.000 40.52814  ? 49  ARG   A C      1 
ATOM   355  O O      . ARG   A 1 56  ? -7.93586  9.95238   -21.79171 1.000 44.58429  ? 49  ARG   A O      1 
ATOM   356  C CB     . ARG   A 1 56  ? -9.15015  10.09454  -24.70048 1.000 35.58193  ? 49  ARG   A CB     1 
ATOM   357  C CG     . ARG   A 1 56  ? -9.98610  10.64003  -25.84769 1.000 46.87805  ? 49  ARG   A CG     1 
ATOM   358  C CD     . ARG   A 1 56  ? -9.67726  9.91580   -27.15043 1.000 50.92554  ? 49  ARG   A CD     1 
ATOM   359  N NE     . ARG   A 1 56  ? -8.29193  10.10474  -27.56460 1.000 58.06418  ? 49  ARG   A NE     1 
ATOM   360  C CZ     . ARG   A 1 56  ? -7.62038  9.26558   -28.34188 1.000 65.16817  ? 49  ARG   A CZ     1 
ATOM   361  N NH1    . ARG   A 1 56  ? -8.18002  8.16448   -28.81724 1.000 57.83403  ? 49  ARG   A NH1    1 
ATOM   362  N NH2    . ARG   A 1 56  ? -6.35534  9.53780   -28.65023 1.000 50.54996  ? 49  ARG   A NH2    1 
ATOM   363  N N      . VAL   A 1 57  ? -9.54330  8.37611   -21.89522 1.000 36.66149  ? 50  VAL   A N      1 
ATOM   364  C CA     . VAL   A 1 57  ? -8.90559  7.51851   -20.90370 1.000 32.80001  ? 50  VAL   A CA     1 
ATOM   365  C C      . VAL   A 1 57  ? -8.68988  6.13660   -21.50182 1.000 31.72936  ? 50  VAL   A C      1 
ATOM   366  O O      . VAL   A 1 57  ? -9.01204  5.89311   -22.67007 1.000 31.84169  ? 50  VAL   A O      1 
ATOM   367  C CB     . VAL   A 1 57  ? -9.73999  7.43150   -19.61217 1.000 36.24273  ? 50  VAL   A CB     1 
ATOM   368  C CG1    . VAL   A 1 57  ? -9.88148  8.80460   -18.97245 1.000 28.42908  ? 50  VAL   A CG1    1 
ATOM   369  C CG2    . VAL   A 1 57  ? -11.10464 6.81968   -19.90023 1.000 32.68408  ? 50  VAL   A CG2    1 
ATOM   370  N N      . ALA   A 1 58  ? -8.14162  5.22655   -20.70329 1.000 30.73424  ? 51  ALA   A N      1 
ATOM   371  C CA     . ALA   A 1 58  ? -7.95547  3.83695   -21.09149 1.000 35.60643  ? 51  ALA   A CA     1 
ATOM   372  C C      . ALA   A 1 58  ? -8.69738  2.95411   -20.10050 1.000 29.95421  ? 51  ALA   A C      1 
ATOM   373  O O      . ALA   A 1 58  ? -8.52163  3.09624   -18.88562 1.000 27.23633  ? 51  ALA   A O      1 
ATOM   374  C CB     . ALA   A 1 58  ? -6.47008  3.46712   -21.13775 1.000 32.17963  ? 51  ALA   A CB     1 
ATOM   375  N N      . VAL   A 1 59  ? -9.53265  2.05774   -20.61801 1.000 28.08982  ? 52  VAL   A N      1 
ATOM   376  C CA     . VAL   A 1 59  ? -10.34301 1.16270   -19.80003 1.000 31.43055  ? 52  VAL   A CA     1 
ATOM   377  C C      . VAL   A 1 59  ? -9.89973  -0.26445  -20.08293 1.000 29.61036  ? 52  VAL   A C      1 
ATOM   378  O O      . VAL   A 1 59  ? -9.90791  -0.70582  -21.23904 1.000 30.38849  ? 52  VAL   A O      1 
ATOM   379  C CB     . VAL   A 1 59  ? -11.84466 1.33426   -20.07671 1.000 32.85048  ? 52  VAL   A CB     1 
ATOM   380  C CG1    . VAL   A 1 59  ? -12.65714 0.46111   -19.13314 1.000 26.66401  ? 52  VAL   A CG1    1 
ATOM   381  C CG2    . VAL   A 1 59  ? -12.24548 2.79517   -19.94086 1.000 29.98857  ? 52  VAL   A CG2    1 
ATOM   382  N N      . LYS   A 1 60  ? -9.52220  -0.98540  -19.03123 1.000 29.52850  ? 53  LYS   A N      1 
ATOM   383  C CA     . LYS   A 1 60  ? -9.02840  -2.35155  -19.14563 1.000 34.39150  ? 53  LYS   A CA     1 
ATOM   384  C C      . LYS   A 1 60  ? -9.97683  -3.28382  -18.40817 1.000 36.42173  ? 53  LYS   A C      1 
ATOM   385  O O      . LYS   A 1 60  ? -10.12950 -3.18052  -17.18592 1.000 32.58284  ? 53  LYS   A O      1 
ATOM   386  C CB     . LYS   A 1 60  ? -7.60972  -2.46925  -18.58399 1.000 32.83070  ? 53  LYS   A CB     1 
ATOM   387  C CG     . LYS   A 1 60  ? -7.16160  -3.89173  -18.28251 1.000 34.44728  ? 53  LYS   A CG     1 
ATOM   388  C CD     . LYS   A 1 60  ? -5.85172  -3.88389  -17.50871 1.000 44.44524  ? 53  LYS   A CD     1 
ATOM   389  C CE     . LYS   A 1 60  ? -5.28720  -5.28332  -17.33023 1.000 38.03161  ? 53  LYS   A CE     1 
ATOM   390  N NZ     . LYS   A 1 60  ? -3.94367  -5.24756  -16.68591 1.000 43.90425  ? 53  LYS   A NZ     1 
ATOM   391  N N      . LYS   A 1 61  ? -10.61509 -4.18366  -19.15011 1.000 33.45414  ? 54  LYS   A N      1 
ATOM   392  C CA     . LYS   A 1 61  ? -11.45389 -5.21763  -18.56152 1.000 35.89005  ? 54  LYS   A CA     1 
ATOM   393  C C      . LYS   A 1 61  ? -10.59351 -6.43956  -18.26840 1.000 32.65966  ? 54  LYS   A C      1 
ATOM   394  O O      . LYS   A 1 61  ? -9.99451  -7.01633  -19.18271 1.000 33.12482  ? 54  LYS   A O      1 
ATOM   395  C CB     . LYS   A 1 61  ? -12.60848 -5.58744  -19.49227 1.000 35.10314  ? 54  LYS   A CB     1 
ATOM   396  C CG     . LYS   A 1 61  ? -13.41442 -6.78724  -19.01142 1.000 34.61190  ? 54  LYS   A CG     1 
ATOM   397  C CD     . LYS   A 1 61  ? -14.50579 -7.17203  -19.99603 1.000 41.88468  ? 54  LYS   A CD     1 
ATOM   398  C CE     . LYS   A 1 61  ? -15.40829 -8.24867  -19.41502 1.000 36.48641  ? 54  LYS   A CE     1 
ATOM   399  N NZ     . LYS   A 1 61  ? -16.38553 -8.75784  -20.41557 1.000 48.99124  ? 54  LYS   A NZ     1 
ATOM   400  N N      . LEU   A 1 62  ? -10.52358 -6.82556  -16.99798 1.000 30.50593  ? 55  LEU   A N      1 
ATOM   401  C CA     . LEU   A 1 62  ? -9.78930  -8.02913  -16.63845 1.000 39.10761  ? 55  LEU   A CA     1 
ATOM   402  C C      . LEU   A 1 62  ? -10.46114 -9.25121  -17.25073 1.000 36.64042  ? 55  LEU   A C      1 
ATOM   403  O O      . LEU   A 1 62  ? -11.69039 -9.35921  -17.27613 1.000 32.98877  ? 55  LEU   A O      1 
ATOM   404  C CB     . LEU   A 1 62  ? -9.70502  -8.16963  -15.11771 1.000 35.85963  ? 55  LEU   A CB     1 
ATOM   405  C CG     . LEU   A 1 62  ? -8.58341  -7.38056  -14.43714 1.000 38.22486  ? 55  LEU   A CG     1 
ATOM   406  C CD1    . LEU   A 1 62  ? -8.76608  -5.88549  -14.65515 1.000 32.24707  ? 55  LEU   A CD1    1 
ATOM   407  C CD2    . LEU   A 1 62  ? -8.51290  -7.70549  -12.95222 1.000 29.63689  ? 55  LEU   A CD2    1 
ATOM   408  N N      . SER   A 1 63  ? -9.64487  -10.16878 -17.76021 1.000 40.75277  ? 56  SER   A N      1 
ATOM   409  C CA     . SER   A 1 63  ? -10.13898 -11.38718 -18.38817 1.000 37.35962  ? 56  SER   A CA     1 
ATOM   410  C C      . SER   A 1 63  ? -10.21089 -12.49496 -17.34441 1.000 36.87964  ? 56  SER   A C      1 
ATOM   411  O O      . SER   A 1 63  ? -9.20259  -12.81661 -16.70629 1.000 42.25271  ? 56  SER   A O      1 
ATOM   412  C CB     . SER   A 1 63  ? -9.23526  -11.79712 -19.55003 1.000 39.97585  ? 56  SER   A CB     1 
ATOM   413  O OG     . SER   A 1 63  ? -9.82519  -12.83088 -20.31806 1.000 56.40391  ? 56  SER   A OG     1 
ATOM   414  N N      . ARG   A 1 64  ? -11.39871 -13.07441 -17.17365 1.000 40.97217  ? 57  ARG   A N      1 
ATOM   415  C CA     . ARG   A 1 64  ? -11.65946 -14.15361 -16.22455 1.000 49.22525  ? 57  ARG   A CA     1 
ATOM   416  C C      . ARG   A 1 64  ? -10.98876 -13.84559 -14.87855 1.000 42.24138  ? 57  ARG   A C      1 
ATOM   417  O O      . ARG   A 1 64  ? -10.10778 -14.58734 -14.43765 1.000 40.90327  ? 57  ARG   A O      1 
ATOM   418  C CB     . ARG   A 1 64  ? -11.19179 -15.49741 -16.77300 1.000 50.42259  ? 57  ARG   A CB     1 
ATOM   419  C CG     . ARG   A 1 64  ? -11.62291 -15.77273 -18.20536 1.000 54.28757  ? 57  ARG   A CG     1 
ATOM   420  C CD     . ARG   A 1 64  ? -12.69281 -16.85103 -18.26230 1.000 51.28909  ? 57  ARG   A CD     1 
ATOM   421  N NE     . ARG   A 1 64  ? -13.58098 -16.68080 -19.40585 1.000 63.30417  ? 57  ARG   A NE     1 
ATOM   422  C CZ     . ARG   A 1 64  ? -13.24359 -16.94179 -20.66145 1.000 71.83130  ? 57  ARG   A CZ     1 
ATOM   423  N NH1    . ARG   A 1 64  ? -12.03813 -17.38885 -20.97478 1.000 67.16043  ? 57  ARG   A NH1    1 
ATOM   424  N NH2    . ARG   A 1 64  ? -14.13876 -16.75154 -21.62690 1.000 61.50964  ? 57  ARG   A NH2    1 
ATOM   425  N N      . PRO   A 1 65  ? -11.39232 -12.76409 -14.20905 1.000 38.70163  ? 58  PRO   A N      1 
ATOM   426  C CA     . PRO   A 1 65  ? -10.65365 -12.33452 -13.00995 1.000 37.15428  ? 58  PRO   A CA     1 
ATOM   427  C C      . PRO   A 1 65  ? -10.70352 -13.32997 -11.86389 1.000 38.21163  ? 58  PRO   A C      1 
ATOM   428  O O      . PRO   A 1 65  ? -9.74709  -13.40126 -11.08123 1.000 29.95354  ? 58  PRO   A O      1 
ATOM   429  C CB     . PRO   A 1 65  ? -11.33584 -11.00991 -12.63961 1.000 37.07876  ? 58  PRO   A CB     1 
ATOM   430  C CG     . PRO   A 1 65  ? -12.70784 -11.11910 -13.21996 1.000 38.71996  ? 58  PRO   A CG     1 
ATOM   431  C CD     . PRO   A 1 65  ? -12.54941 -11.89792 -14.49295 1.000 32.06124  ? 58  PRO   A CD     1 
ATOM   432  N N      . PHE   A 1 66  ? -11.78353 -14.10185 -11.73550 1.000 40.79535  ? 59  PHE   A N      1 
ATOM   433  C CA     . PHE   A 1 66  ? -11.96162 -15.01724 -10.61376 1.000 36.75766  ? 59  PHE   A CA     1 
ATOM   434  C C      . PHE   A 1 66  ? -12.20610 -16.44847 -11.08260 1.000 44.05996  ? 59  PHE   A C      1 
ATOM   435  O O      . PHE   A 1 66  ? -12.91784 -17.21118 -10.42678 1.000 38.70710  ? 59  PHE   A O      1 
ATOM   436  C CB     . PHE   A 1 66  ? -13.10392 -14.54598 -9.71466  1.000 32.27136  ? 59  PHE   A CB     1 
ATOM   437  C CG     . PHE   A 1 66  ? -13.00754 -13.09826 -9.32368  1.000 40.92323  ? 59  PHE   A CG     1 
ATOM   438  C CD1    . PHE   A 1 66  ? -11.98418 -12.65639 -8.50134  1.000 39.97011  ? 59  PHE   A CD1    1 
ATOM   439  C CD2    . PHE   A 1 66  ? -13.93612 -12.17822 -9.78192  1.000 39.99954  ? 59  PHE   A CD2    1 
ATOM   440  C CE1    . PHE   A 1 66  ? -11.89026 -11.32545 -8.14110  1.000 36.60935  ? 59  PHE   A CE1    1 
ATOM   441  C CE2    . PHE   A 1 66  ? -13.84698 -10.84563 -9.42477  1.000 43.81235  ? 59  PHE   A CE2    1 
ATOM   442  C CZ     . PHE   A 1 66  ? -12.82214 -10.41960 -8.60361  1.000 34.87787  ? 59  PHE   A CZ     1 
ATOM   443  N N      . GLN   A 1 67  ? -11.61255 -16.83012 -12.21463 1.000 45.88752  ? 60  GLN   A N      1 
ATOM   444  C CA     . GLN   A 1 67  ? -11.81257 -18.17480 -12.74061 1.000 47.75036  ? 60  GLN   A CA     1 
ATOM   445  C C      . GLN   A 1 67  ? -11.10455 -19.23764 -11.91099 1.000 50.95911  ? 60  GLN   A C      1 
ATOM   446  O O      . GLN   A 1 67  ? -11.50038 -20.40700 -11.95838 1.000 50.24677  ? 60  GLN   A O      1 
ATOM   447  C CB     . GLN   A 1 67  ? -11.33682 -18.24349 -14.19139 1.000 46.44973  ? 60  GLN   A CB     1 
ATOM   448  C CG     . GLN   A 1 67  ? -11.62289 -19.56473 -14.87797 1.000 50.91545  ? 60  GLN   A CG     1 
ATOM   449  C CD     . GLN   A 1 67  ? -11.13104 -19.58705 -16.30947 1.000 52.76797  ? 60  GLN   A CD     1 
ATOM   450  O OE1    . GLN   A 1 67  ? -11.91687 -19.71423 -17.24950 1.000 50.99794  ? 60  GLN   A OE1    1 
ATOM   451  N NE2    . GLN   A 1 67  ? -9.82263  -19.46073 -16.48326 1.000 45.40742  ? 60  GLN   A NE2    1 
ATOM   452  N N      . SER   A 1 68  ? -10.07439 -18.86363 -11.15664 1.000 47.45280  ? 61  SER   A N      1 
ATOM   453  C CA     . SER   A 1 68  ? -9.33491  -19.81016 -10.33572 1.000 45.00511  ? 61  SER   A CA     1 
ATOM   454  C C      . SER   A 1 68  ? -8.69802  -19.05598 -9.17578  1.000 39.88525  ? 61  SER   A C      1 
ATOM   455  O O      . SER   A 1 68  ? -8.78554  -17.82844 -9.08202  1.000 42.79977  ? 61  SER   A O      1 
ATOM   456  C CB     . SER   A 1 68  ? -8.28043  -20.55144 -11.16395 1.000 47.18322  ? 61  SER   A CB     1 
ATOM   457  O OG     . SER   A 1 68  ? -7.35453  -19.64331 -11.73585 1.000 46.84749  ? 61  SER   A OG     1 
ATOM   458  N N      . ILE   A 1 69  ? -8.05351  -19.80749 -8.28099  1.000 43.64258  ? 62  ILE   A N      1 
ATOM   459  C CA     . ILE   A 1 69  ? -7.31528  -19.18236 -7.18777  1.000 42.14924  ? 62  ILE   A CA     1 
ATOM   460  C C      . ILE   A 1 69  ? -6.19787  -18.30786 -7.73955  1.000 37.62650  ? 62  ILE   A C      1 
ATOM   461  O O      . ILE   A 1 69  ? -5.96065  -17.19421 -7.25588  1.000 34.68369  ? 62  ILE   A O      1 
ATOM   462  C CB     . ILE   A 1 69  ? -6.77150  -20.25579 -6.22687  1.000 44.15988  ? 62  ILE   A CB     1 
ATOM   463  C CG1    . ILE   A 1 69  ? -7.89796  -20.81004 -5.35314  1.000 38.16506  ? 62  ILE   A CG1    1 
ATOM   464  C CG2    . ILE   A 1 69  ? -5.65269  -19.68574 -5.36799  1.000 41.51846  ? 62  ILE   A CG2    1 
ATOM   465  C CD1    . ILE   A 1 69  ? -7.47663  -21.97291 -4.48368  1.000 46.34743  ? 62  ILE   A CD1    1 
ATOM   466  N N      . ILE   A 1 70  ? -5.50077  -18.79516 -8.76716  1.000 39.16817  ? 63  ILE   A N      1 
ATOM   467  C CA     . ILE   A 1 70  ? -4.39814  -18.03847 -9.35437  1.000 41.29051  ? 63  ILE   A CA     1 
ATOM   468  C C      . ILE   A 1 70  ? -4.91107  -16.73344 -9.94890  1.000 31.77770  ? 63  ILE   A C      1 
ATOM   469  O O      . ILE   A 1 70  ? -4.39200  -15.64938 -9.65674  1.000 39.23348  ? 63  ILE   A O      1 
ATOM   470  C CB     . ILE   A 1 70  ? -3.66389  -18.89044 -10.40596 1.000 46.92836  ? 63  ILE   A CB     1 
ATOM   471  C CG1    . ILE   A 1 70  ? -3.06772  -20.14340 -9.75936  1.000 43.95486  ? 63  ILE   A CG1    1 
ATOM   472  C CG2    . ILE   A 1 70  ? -2.57948  -18.07593 -11.09154 1.000 39.42726  ? 63  ILE   A CG2    1 
ATOM   473  C CD1    . ILE   A 1 70  ? -4.08704  -21.21648 -9.43677  1.000 50.19876  ? 63  ILE   A CD1    1 
ATOM   474  N N      . HIS   A 1 71  ? -5.94075  -16.81998 -10.79462 1.000 34.09520  ? 64  HIS   A N      1 
ATOM   475  C CA     . HIS   A 1 71  ? -6.53836  -15.61554 -11.36152 1.000 37.30511  ? 64  HIS   A CA     1 
ATOM   476  C C      . HIS   A 1 71  ? -7.04926  -14.68673 -10.26738 1.000 33.97640  ? 64  HIS   A C      1 
ATOM   477  O O      . HIS   A 1 71  ? -6.89916  -13.46265 -10.35981 1.000 33.38117  ? 64  HIS   A O      1 
ATOM   478  C CB     . HIS   A 1 71  ? -7.67859  -15.99024 -12.30909 1.000 39.21505  ? 64  HIS   A CB     1 
ATOM   479  C CG     . HIS   A 1 71  ? -7.22448  -16.44057 -13.66253 1.000 47.69642  ? 64  HIS   A CG     1 
ATOM   480  N ND1    . HIS   A 1 71  ? -7.95759  -16.20841 -14.80664 1.000 50.51176  ? 64  HIS   A ND1    1 
ATOM   481  C CD2    . HIS   A 1 71  ? -6.11817  -17.11529 -14.05523 1.000 54.92395  ? 64  HIS   A CD2    1 
ATOM   482  C CE1    . HIS   A 1 71  ? -7.32073  -16.71724 -15.84616 1.000 51.99746  ? 64  HIS   A CE1    1 
ATOM   483  N NE2    . HIS   A 1 71  ? -6.20167  -17.27305 -15.41760 1.000 58.62146  ? 64  HIS   A NE2    1 
ATOM   484  N N      . ALA   A 1 72  ? -7.66048  -15.25216 -9.22382  1.000 33.08751  ? 65  ALA   A N      1 
ATOM   485  C CA     . ALA   A 1 72  ? -8.24803  -14.43232 -8.16902  1.000 31.55093  ? 65  ALA   A CA     1 
ATOM   486  C C      . ALA   A 1 72  ? -7.17827  -13.65476 -7.41320  1.000 27.55506  ? 65  ALA   A C      1 
ATOM   487  O O      . ALA   A 1 72  ? -7.33097  -12.45402 -7.16037  1.000 26.43414  ? 65  ALA   A O      1 
ATOM   488  C CB     . ALA   A 1 72  ? -9.05585  -15.31025 -7.21291  1.000 36.18859  ? 65  ALA   A CB     1 
ATOM   489  N N      . LYS   A 1 73  ? -6.08982  -14.32679 -7.03343  1.000 36.18946  ? 66  LYS   A N      1 
ATOM   490  C CA     . LYS   A 1 73  ? -4.99612  -13.63488 -6.36034  1.000 27.20656  ? 66  LYS   A CA     1 
ATOM   491  C C      . LYS   A 1 73  ? -4.36539  -12.59269 -7.27441  1.000 31.83085  ? 66  LYS   A C      1 
ATOM   492  O O      . LYS   A 1 73  ? -4.10021  -11.46143 -6.85020  1.000 30.05209  ? 66  LYS   A O      1 
ATOM   493  C CB     . LYS   A 1 73  ? -3.94986  -14.64493 -5.88903  1.000 29.62081  ? 66  LYS   A CB     1 
ATOM   494  C CG     . LYS   A 1 73  ? -3.13754  -14.19191 -4.68731  1.000 35.26654  ? 66  LYS   A CG     1 
ATOM   495  C CD     . LYS   A 1 73  ? -2.09813  -15.23375 -4.30708  1.000 29.45519  ? 66  LYS   A CD     1 
ATOM   496  C CE     . LYS   A 1 73  ? -1.30713  -14.80696 -3.08108  1.000 33.71898  ? 66  LYS   A CE     1 
ATOM   497  N NZ     . LYS   A 1 73  ? -0.10968  -15.66718 -2.86704  1.000 41.00834  ? 66  LYS   A NZ     1 
ATOM   498  N N      . ARG   A 1 74  ? -4.12425  -12.95447 -8.53728  1.000 32.87324  ? 67  ARG   A N      1 
ATOM   499  C CA     . ARG   A 1 74  ? -3.55693  -12.00114 -9.48544  1.000 36.58932  ? 67  ARG   A CA     1 
ATOM   500  C C      . ARG   A 1 74  ? -4.43372  -10.76139 -9.61252  1.000 30.86326  ? 67  ARG   A C      1 
ATOM   501  O O      . ARG   A 1 74  ? -3.92420  -9.63876  -9.71076  1.000 33.21754  ? 67  ARG   A O      1 
ATOM   502  C CB     . ARG   A 1 74  ? -3.36595  -12.66717 -10.84877 1.000 37.71702  ? 67  ARG   A CB     1 
ATOM   503  C CG     . ARG   A 1 74  ? -2.64805  -11.79512 -11.86655 1.000 48.28783  ? 67  ARG   A CG     1 
ATOM   504  C CD     . ARG   A 1 74  ? -2.76802  -12.35876 -13.27342 1.000 41.99268  ? 67  ARG   A CD     1 
ATOM   505  N NE     . ARG   A 1 74  ? -2.55380  -13.80034 -13.31298 1.000 54.84126  ? 67  ARG   A NE     1 
ATOM   506  C CZ     . ARG   A 1 74  ? -3.35831  -14.65948 -13.92389 1.000 64.29476  ? 67  ARG   A CZ     1 
ATOM   507  N NH1    . ARG   A 1 74  ? -4.45084  -14.25632 -14.55288 1.000 55.67866  ? 67  ARG   A NH1    1 
ATOM   508  N NH2    . ARG   A 1 74  ? -3.05888  -15.95535 -13.90449 1.000 61.04250  ? 67  ARG   A NH2    1 
ATOM   509  N N      . THR   A 1 75  ? -5.75614  -10.94379 -9.61358  1.000 24.56754  ? 68  THR   A N      1 
ATOM   510  C CA     . THR   A 1 75  ? -6.66137  -9.80070  -9.67891  1.000 30.99599  ? 68  THR   A CA     1 
ATOM   511  C C      . THR   A 1 75  ? -6.52192  -8.92351  -8.43955  1.000 24.82608  ? 68  THR   A C      1 
ATOM   512  O O      . THR   A 1 75  ? -6.37946  -7.69965  -8.54142  1.000 24.41915  ? 68  THR   A O      1 
ATOM   513  C CB     . THR   A 1 75  ? -8.10323  -10.28542 -9.84408  1.000 31.62732  ? 68  THR   A CB     1 
ATOM   514  O OG1    . THR   A 1 75  ? -8.25667  -10.90039 -11.12967 1.000 28.55617  ? 68  THR   A OG1    1 
ATOM   515  C CG2    . THR   A 1 75  ? -9.07942  -9.12255  -9.72279  1.000 24.27406  ? 68  THR   A CG2    1 
ATOM   516  N N      . TYR   A 1 76  ? -6.55837  -9.53821  -7.25479  1.000 27.82149  ? 69  TYR   A N      1 
ATOM   517  C CA     . TYR   A 1 76  ? -6.36914  -8.78659  -6.01775  1.000 27.52336  ? 69  TYR   A CA     1 
ATOM   518  C C      . TYR   A 1 76  ? -5.01110  -8.09606  -5.99809  1.000 28.38234  ? 69  TYR   A C      1 
ATOM   519  O O      . TYR   A 1 76  ? -4.87793  -6.98186  -5.47842  1.000 30.19138  ? 69  TYR   A O      1 
ATOM   520  C CB     . TYR   A 1 76  ? -6.52027  -9.72620  -4.81941  1.000 29.96982  ? 69  TYR   A CB     1 
ATOM   521  C CG     . TYR   A 1 76  ? -6.31860  -9.08515  -3.46237  1.000 29.13611  ? 69  TYR   A CG     1 
ATOM   522  C CD1    . TYR   A 1 76  ? -7.26485  -8.21802  -2.93123  1.000 31.92098  ? 69  TYR   A CD1    1 
ATOM   523  C CD2    . TYR   A 1 76  ? -5.19095  -9.36806  -2.70159  1.000 32.19290  ? 69  TYR   A CD2    1 
ATOM   524  C CE1    . TYR   A 1 76  ? -7.08636  -7.63984  -1.68617  1.000 31.73504  ? 69  TYR   A CE1    1 
ATOM   525  C CE2    . TYR   A 1 76  ? -5.00418  -8.79550  -1.45736  1.000 26.01930  ? 69  TYR   A CE2    1 
ATOM   526  C CZ     . TYR   A 1 76  ? -5.95551  -7.93513  -0.95364  1.000 34.37744  ? 69  TYR   A CZ     1 
ATOM   527  O OH     . TYR   A 1 76  ? -5.76946  -7.36224  0.28488   1.000 30.53331  ? 69  TYR   A OH     1 
ATOM   528  N N      . ARG   A 1 77  ? -3.99295  -8.74060  -6.57090  1.000 27.79042  ? 70  ARG   A N      1 
ATOM   529  C CA     . ARG   A 1 77  ? -2.65113  -8.16823  -6.57638  1.000 31.48362  ? 70  ARG   A CA     1 
ATOM   530  C C      . ARG   A 1 77  ? -2.59354  -6.90134  -7.42125  1.000 28.62179  ? 70  ARG   A C      1 
ATOM   531  O O      . ARG   A 1 77  ? -2.08200  -5.86780  -6.97408  1.000 23.19215  ? 70  ARG   A O      1 
ATOM   532  C CB     . ARG   A 1 77  ? -1.64771  -9.20421  -7.08455  1.000 31.30678  ? 70  ARG   A CB     1 
ATOM   533  C CG     . ARG   A 1 77  ? -0.28881  -8.63657  -7.46214  1.000 29.28228  ? 70  ARG   A CG     1 
ATOM   534  C CD     . ARG   A 1 77  ? 0.59257   -9.70768  -8.08866  1.000 27.88135  ? 70  ARG   A CD     1 
ATOM   535  N NE     . ARG   A 1 77  ? 0.73049   -10.87284 -7.22346  1.000 31.62216  ? 70  ARG   A NE     1 
ATOM   536  C CZ     . ARG   A 1 77  ? 0.39632   -12.10880 -7.56967  1.000 31.41636  ? 70  ARG   A CZ     1 
ATOM   537  N NH1    . ARG   A 1 77  ? -0.09765  -12.38193 -8.76587  1.000 28.98089  ? 70  ARG   A NH1    1 
ATOM   538  N NH2    . ARG   A 1 77  ? 0.56122   -13.09573 -6.69278  1.000 27.81124  ? 70  ARG   A NH2    1 
ATOM   539  N N      . GLU   A 1 78  ? -3.11207  -6.96031  -8.64999  1.000 26.46139  ? 71  GLU   A N      1 
ATOM   540  C CA     . GLU   A 1 78  ? -3.04251  -5.79427  -9.52433  1.000 29.90785  ? 71  GLU   A CA     1 
ATOM   541  C C      . GLU   A 1 78  ? -3.85761  -4.63526  -8.96511  1.000 33.04045  ? 71  GLU   A C      1 
ATOM   542  O O      . GLU   A 1 78  ? -3.43032  -3.47682  -9.03409  1.000 33.90936  ? 71  GLU   A O      1 
ATOM   543  C CB     . GLU   A 1 78  ? -3.51701  -6.15398  -10.93324 1.000 31.53408  ? 71  GLU   A CB     1 
ATOM   544  C CG     . GLU   A 1 78  ? -2.83425  -5.33920  -12.02282 1.000 40.18079  ? 71  GLU   A CG     1 
ATOM   545  C CD     . GLU   A 1 78  ? -3.61471  -5.31332  -13.32208 1.000 41.19112  ? 71  GLU   A CD     1 
ATOM   546  O OE1    . GLU   A 1 78  ? -3.05641  -4.85340  -14.34061 1.000 40.76419  ? 71  GLU   A OE1    1 
ATOM   547  O OE2    . GLU   A 1 78  ? -4.78297  -5.75359  -13.32931 1.000 44.08671  ? 71  GLU   A OE2    1 
ATOM   548  N N      . LEU   A 1 79  ? -5.03252  -4.92448  -8.40346  1.000 26.27154  ? 72  LEU   A N      1 
ATOM   549  C CA     . LEU   A 1 79  ? -5.87079  -3.85705  -7.86608  1.000 31.59440  ? 72  LEU   A CA     1 
ATOM   550  C C      . LEU   A 1 79  ? -5.20709  -3.18601  -6.66896  1.000 25.44272  ? 72  LEU   A C      1 
ATOM   551  O O      . LEU   A 1 79  ? -5.12489  -1.95396  -6.60133  1.000 30.16215  ? 72  LEU   A O      1 
ATOM   552  C CB     . LEU   A 1 79  ? -7.24626  -4.40699  -7.48617  1.000 26.25896  ? 72  LEU   A CB     1 
ATOM   553  C CG     . LEU   A 1 79  ? -8.26121  -3.36124  -7.01928  1.000 29.29497  ? 72  LEU   A CG     1 
ATOM   554  C CD1    . LEU   A 1 79  ? -8.11180  -2.07417  -7.81882  1.000 21.28956  ? 72  LEU   A CD1    1 
ATOM   555  C CD2    . LEU   A 1 79  ? -9.67908  -3.90138  -7.12755  1.000 36.76982  ? 72  LEU   A CD2    1 
ATOM   556  N N      . ARG   A 1 80  ? -4.72713  -3.98175  -5.71107  1.000 28.86086  ? 73  ARG   A N      1 
ATOM   557  C CA     . ARG   A 1 80  ? -4.05963  -3.40790  -4.54758  1.000 33.12622  ? 73  ARG   A CA     1 
ATOM   558  C C      . ARG   A 1 80  ? -2.80466  -2.64476  -4.95128  1.000 27.54788  ? 73  ARG   A C      1 
ATOM   559  O O      . ARG   A 1 80  ? -2.50504  -1.58411  -4.39004  1.000 26.92233  ? 73  ARG   A O      1 
ATOM   560  C CB     . ARG   A 1 80  ? -3.72074  -4.50681  -3.54149  1.000 28.76333  ? 73  ARG   A CB     1 
ATOM   561  C CG     . ARG   A 1 80  ? -4.76645  -4.69221  -2.45834  1.000 41.46118  ? 73  ARG   A CG     1 
ATOM   562  C CD     . ARG   A 1 80  ? -4.18871  -5.39507  -1.24478  1.000 37.94334  ? 73  ARG   A CD     1 
ATOM   563  N NE     . ARG   A 1 80  ? -3.72849  -4.46351  -0.22344  1.000 36.90047  ? 73  ARG   A NE     1 
ATOM   564  C CZ     . ARG   A 1 80  ? -2.45858  -4.29955  0.11822   1.000 52.94162  ? 73  ARG   A CZ     1 
ATOM   565  N NH1    . ARG   A 1 80  ? -1.49175  -4.98288  -0.47180  1.000 43.48090  ? 73  ARG   A NH1    1 
ATOM   566  N NH2    . ARG   A 1 80  ? -2.15145  -3.43214  1.07872   1.000 44.83625  ? 73  ARG   A NH2    1 
ATOM   567  N N      . LEU   A 1 81  ? -2.05953  -3.16664  -5.92610  1.000 26.79705  ? 74  LEU   A N      1 
ATOM   568  C CA     . LEU   A 1 81  ? -0.84509  -2.49097  -6.36800  1.000 32.15435  ? 74  LEU   A CA     1 
ATOM   569  C C      . LEU   A 1 81  ? -1.17150  -1.17804  -7.06899  1.000 31.12588  ? 74  LEU   A C      1 
ATOM   570  O O      . LEU   A 1 81  ? -0.62018  -0.12561  -6.72543  1.000 36.50316  ? 74  LEU   A O      1 
ATOM   571  C CB     . LEU   A 1 81  ? -0.03915  -3.40838  -7.28684  1.000 36.12855  ? 74  LEU   A CB     1 
ATOM   572  C CG     . LEU   A 1 81  ? 1.08783   -2.73742  -8.07274  1.000 36.10729  ? 74  LEU   A CG     1 
ATOM   573  C CD1    . LEU   A 1 81  ? 2.32653   -2.58768  -7.20395  1.000 38.04279  ? 74  LEU   A CD1    1 
ATOM   574  C CD2    . LEU   A 1 81  ? 1.40025   -3.52328  -9.33446  1.000 34.77101  ? 74  LEU   A CD2    1 
ATOM   575  N N      . LEU   A 1 82  ? -2.07337  -1.21861  -8.05286  1.000 27.83195  ? 75  LEU   A N      1 
ATOM   576  C CA     . LEU   A 1 82  ? -2.39691  -0.00988  -8.80508  1.000 28.12934  ? 75  LEU   A CA     1 
ATOM   577  C C      . LEU   A 1 82  ? -2.98014  1.06967   -7.90132  1.000 29.09142  ? 75  LEU   A C      1 
ATOM   578  O O      . LEU   A 1 82  ? -2.66435  2.25512   -8.05645  1.000 35.24991  ? 75  LEU   A O      1 
ATOM   579  C CB     . LEU   A 1 82  ? -3.36105  -0.34201  -9.94269  1.000 25.45640  ? 75  LEU   A CB     1 
ATOM   580  C CG     . LEU   A 1 82  ? -2.76369  -1.16275  -11.08759 1.000 39.21415  ? 75  LEU   A CG     1 
ATOM   581  C CD1    . LEU   A 1 82  ? -3.77393  -1.33210  -12.20897 1.000 38.14785  ? 75  LEU   A CD1    1 
ATOM   582  C CD2    . LEU   A 1 82  ? -1.48351  -0.51916  -11.60186 1.000 37.81915  ? 75  LEU   A CD2    1 
ATOM   583  N N      . LYS   A 1 83  ? -3.83243  0.68256   -6.94902  1.000 30.50378  ? 76  LYS   A N      1 
ATOM   584  C CA     . LYS   A 1 83  ? -4.39096  1.65974   -6.02072  1.000 28.44265  ? 76  LYS   A CA     1 
ATOM   585  C C      . LYS   A 1 83  ? -3.31213  2.36072   -5.20498  1.000 35.43169  ? 76  LYS   A C      1 
ATOM   586  O O      . LYS   A 1 83  ? -3.55330  3.45783   -4.68883  1.000 31.58431  ? 76  LYS   A O      1 
ATOM   587  C CB     . LYS   A 1 83  ? -5.39622  0.98559   -5.08337  1.000 28.91715  ? 76  LYS   A CB     1 
ATOM   588  C CG     . LYS   A 1 83  ? -6.74324  0.68028   -5.72393  1.000 29.81495  ? 76  LYS   A CG     1 
ATOM   589  C CD     . LYS   A 1 83  ? -7.68566  -0.00749  -4.74521  1.000 35.84269  ? 76  LYS   A CD     1 
ATOM   590  C CE     . LYS   A 1 83  ? -7.96669  0.86781   -3.53330  1.000 33.96021  ? 76  LYS   A CE     1 
ATOM   591  N NZ     . LYS   A 1 83  ? -8.96456  0.24756   -2.61699  1.000 36.12194  ? 76  LYS   A NZ     1 
ATOM   592  N N      . HIS   A 1 84  ? -2.13130  1.75500   -5.08085  1.000 29.82476  ? 77  HIS   A N      1 
ATOM   593  C CA     . HIS   A 1 84  ? -1.04066  2.32261   -4.30071  1.000 34.04321  ? 77  HIS   A CA     1 
ATOM   594  C C      . HIS   A 1 84  ? -0.11476  3.20984   -5.12350  1.000 33.23115  ? 77  HIS   A C      1 
ATOM   595  O O      . HIS   A 1 84  ? 0.57035   4.06395   -4.54915  1.000 29.85691  ? 77  HIS   A O      1 
ATOM   596  C CB     . HIS   A 1 84  ? -0.22671  1.19434   -3.65542  1.000 34.87110  ? 77  HIS   A CB     1 
ATOM   597  C CG     . HIS   A 1 84  ? 0.72612   1.65573   -2.59632  1.000 45.22309  ? 77  HIS   A CG     1 
ATOM   598  N ND1    . HIS   A 1 84  ? 0.31511   2.02377   -1.33309  1.000 50.24587  ? 77  HIS   A ND1    1 
ATOM   599  C CD2    . HIS   A 1 84  ? 2.07356   1.79272   -2.60784  1.000 45.76455  ? 77  HIS   A CD2    1 
ATOM   600  C CE1    . HIS   A 1 84  ? 1.36693   2.37577   -0.61499  1.000 48.10905  ? 77  HIS   A CE1    1 
ATOM   601  N NE2    . HIS   A 1 84  ? 2.44635   2.24461   -1.36506  1.000 46.71243  ? 77  HIS   A NE2    1 
ATOM   602  N N      . MET   A 1 85  ? -0.08590  3.03780   -6.44558  1.000 31.56330  ? 78  MET   A N      1 
ATOM   603  C CA     . MET   A 1 85  ? 0.84630   3.75769   -7.31091  1.000 31.71237  ? 78  MET   A CA     1 
ATOM   604  C C      . MET   A 1 85  ? 0.32614   5.17197   -7.55588  1.000 32.85335  ? 78  MET   A C      1 
ATOM   605  O O      . MET   A 1 85  ? -0.64185  5.36672   -8.30004  1.000 32.10750  ? 78  MET   A O      1 
ATOM   606  C CB     . MET   A 1 85  ? 1.02175   3.00644   -8.62749  1.000 28.01888  ? 78  MET   A CB     1 
ATOM   607  C CG     . MET   A 1 85  ? 1.81711   1.69881   -8.54352  1.000 25.11396  ? 78  MET   A CG     1 
ATOM   608  S SD     . MET   A 1 85  ? 3.35464   1.77153   -7.60362  1.000 30.14825  ? 78  MET   A SD     1 
ATOM   609  C CE     . MET   A 1 85  ? 2.75133   1.76292   -5.91930  1.000 32.38655  ? 78  MET   A CE     1 
ATOM   610  N N      . LYS   A 1 86  ? 0.97913   6.16802   -6.94345  1.000 29.80979  ? 79  LYS   A N      1 
ATOM   611  C CA     . LYS   A 1 86  ? 0.62249   7.58324   -7.10504  1.000 36.49243  ? 79  LYS   A CA     1 
ATOM   612  C C      . LYS   A 1 86  ? 1.88709   8.35002   -7.49766  1.000 35.71646  ? 79  LYS   A C      1 
ATOM   613  O O      . LYS   A 1 86  ? 2.54273   8.96423   -6.65234  1.000 31.97026  ? 79  LYS   A O      1 
ATOM   614  C CB     . LYS   A 1 86  ? -0.00784  8.14452   -5.82444  1.000 35.62138  ? 79  LYS   A CB     1 
ATOM   615  C CG     . LYS   A 1 86  ? -1.15498  7.31660   -5.27129  1.000 42.39177  ? 79  LYS   A CG     1 
ATOM   616  C CD     . LYS   A 1 86  ? -2.49579  7.80746   -5.78906  1.000 42.55862  ? 79  LYS   A CD     1 
ATOM   617  C CE     . LYS   A 1 86  ? -3.64709  7.23418   -4.97544  1.000 40.62025  ? 79  LYS   A CE     1 
ATOM   618  N NZ     . LYS   A 1 86  ? -3.53611  7.57951   -3.53092  1.000 45.36736  ? 79  LYS   A NZ     1 
ATOM   619  N N      . HIS   A 1 87  ? 2.21570   8.32853   -8.78893  1.000 34.76891  ? 80  HIS   A N      1 
ATOM   620  C CA     . HIS   A 1 87  ? 3.44393   8.94596   -9.27119  1.000 30.56669  ? 80  HIS   A CA     1 
ATOM   621  C C      . HIS   A 1 87  ? 3.31950   9.20812   -10.76659 1.000 30.99758  ? 80  HIS   A C      1 
ATOM   622  O O      . HIS   A 1 87  ? 2.71748   8.41388   -11.49229 1.000 31.41220  ? 80  HIS   A O      1 
ATOM   623  C CB     . HIS   A 1 87  ? 4.65587   8.05471   -8.97371  1.000 28.50749  ? 80  HIS   A CB     1 
ATOM   624  C CG     . HIS   A 1 87  ? 5.97165   8.67904   -9.32015  1.000 30.93296  ? 80  HIS   A CG     1 
ATOM   625  N ND1    . HIS   A 1 87  ? 6.45219   8.73355   -10.61062 1.000 30.61813  ? 80  HIS   A ND1    1 
ATOM   626  C CD2    . HIS   A 1 87  ? 6.91335   9.26511   -8.54308  1.000 32.30150  ? 80  HIS   A CD2    1 
ATOM   627  C CE1    . HIS   A 1 87  ? 7.63055   9.33043   -10.61474 1.000 36.61379  ? 80  HIS   A CE1    1 
ATOM   628  N NE2    . HIS   A 1 87  ? 7.93337   9.66309   -9.37278  1.000 37.08778  ? 80  HIS   A NE2    1 
ATOM   629  N N      . GLU   A 1 88  ? 3.91260   10.31738  -11.21927 1.000 35.72133  ? 81  GLU   A N      1 
ATOM   630  C CA     . GLU   A 1 88  ? 3.68983   10.78111  -12.58690 1.000 35.85407  ? 81  GLU   A CA     1 
ATOM   631  C C      . GLU   A 1 88  ? 4.22423   9.80420   -13.62683 1.000 30.87339  ? 81  GLU   A C      1 
ATOM   632  O O      . GLU   A 1 88  ? 3.66842   9.70935   -14.72716 1.000 30.43353  ? 81  GLU   A O      1 
ATOM   633  C CB     . GLU   A 1 88  ? 4.32968   12.15478  -12.78801 1.000 34.80296  ? 81  GLU   A CB     1 
ATOM   634  C CG     . GLU   A 1 88  ? 3.63746   13.28265  -12.04977 1.000 39.97968  ? 81  GLU   A CG     1 
ATOM   635  C CD     . GLU   A 1 88  ? 4.59970   14.37756  -11.64200 1.000 53.31801  ? 81  GLU   A CD     1 
ATOM   636  O OE1    . GLU   A 1 88  ? 4.60319   14.75468  -10.45165 1.000 54.14310  ? 81  GLU   A OE1    1 
ATOM   637  O OE2    . GLU   A 1 88  ? 5.35675   14.85777  -12.51220 1.000 55.40418  ? 81  GLU   A OE2    1 
ATOM   638  N N      . ASN   A 1 89  ? 5.30556   9.08960   -13.31911 1.000 33.99681  ? 82  ASN   A N      1 
ATOM   639  C CA     . ASN   A 1 89  ? 5.90350   8.15743   -14.26595 1.000 29.33545  ? 82  ASN   A CA     1 
ATOM   640  C C      . ASN   A 1 89  ? 5.50861   6.71137   -13.98756 1.000 31.08569  ? 82  ASN   A C      1 
ATOM   641  O O      . ASN   A 1 89  ? 6.17649   5.78646   -14.46306 1.000 29.15587  ? 82  ASN   A O      1 
ATOM   642  C CB     . ASN   A 1 89  ? 7.42433   8.30987   -14.26918 1.000 31.47625  ? 82  ASN   A CB     1 
ATOM   643  C CG     . ASN   A 1 89  ? 7.86221   9.73922   -14.52816 1.000 33.13367  ? 82  ASN   A CG     1 
ATOM   644  O OD1    . ASN   A 1 89  ? 8.45001   10.38627  -13.66248 1.000 34.45539  ? 82  ASN   A OD1    1 
ATOM   645  N ND2    . ASN   A 1 89  ? 7.56780   10.24192  -15.72195 1.000 33.28309  ? 82  ASN   A ND2    1 
ATOM   646  N N      . VAL   A 1 90  ? 4.43347   6.50026   -13.23400 1.000 31.99861  ? 83  VAL   A N      1 
ATOM   647  C CA     . VAL   A 1 90  ? 3.90085   5.17215   -12.96263 1.000 30.83858  ? 83  VAL   A CA     1 
ATOM   648  C C      . VAL   A 1 90  ? 2.41346   5.19042   -13.27828 1.000 34.93956  ? 83  VAL   A C      1 
ATOM   649  O O      . VAL   A 1 90  ? 1.70479   6.12470   -12.88640 1.000 33.27126  ? 83  VAL   A O      1 
ATOM   650  C CB     . VAL   A 1 90  ? 4.14052   4.74331   -11.50279 1.000 32.45195  ? 83  VAL   A CB     1 
ATOM   651  C CG1    . VAL   A 1 90  ? 3.58533   3.34835   -11.26455 1.000 27.62800  ? 83  VAL   A CG1    1 
ATOM   652  C CG2    . VAL   A 1 90  ? 5.62499   4.80175   -11.16929 1.000 28.01960  ? 83  VAL   A CG2    1 
ATOM   653  N N      . ILE   A 1 91  ? 1.94460   4.16763   -13.99791 1.000 32.48791  ? 84  ILE   A N      1 
ATOM   654  C CA     . ILE   A 1 91  ? 0.52499   4.07565   -14.30958 1.000 36.53902  ? 84  ILE   A CA     1 
ATOM   655  C C      . ILE   A 1 91  ? -0.27903  4.18789   -13.02241 1.000 27.81637  ? 84  ILE   A C      1 
ATOM   656  O O      . ILE   A 1 91  ? 0.11029   3.65709   -11.97673 1.000 28.67076  ? 84  ILE   A O      1 
ATOM   657  C CB     . ILE   A 1 91  ? 0.22215   2.76483   -15.05871 1.000 35.03135  ? 84  ILE   A CB     1 
ATOM   658  C CG1    . ILE   A 1 91  ? -1.12505  2.85793   -15.77894 1.000 36.20473  ? 84  ILE   A CG1    1 
ATOM   659  C CG2    . ILE   A 1 91  ? 0.24702   1.58115   -14.10303 1.000 29.29367  ? 84  ILE   A CG2    1 
ATOM   660  C CD1    . ILE   A 1 91  ? -1.13895  3.84863   -16.92473 1.000 31.64841  ? 84  ILE   A CD1    1 
ATOM   661  N N      . GLY   A 1 92  ? -1.40242  4.90090   -13.09355 1.000 31.56337  ? 85  GLY   A N      1 
ATOM   662  C CA     . GLY   A 1 92  ? -2.21379  5.14567   -11.92009 1.000 35.77881  ? 85  GLY   A CA     1 
ATOM   663  C C      . GLY   A 1 92  ? -3.68836  4.99070   -12.23253 1.000 34.43410  ? 85  GLY   A C      1 
ATOM   664  O O      . GLY   A 1 92  ? -4.12669  5.13422   -13.37652 1.000 34.06157  ? 85  GLY   A O      1 
ATOM   665  N N      . LEU   A 1 93  ? -4.45204  4.70467   -11.18167 1.000 29.66866  ? 86  LEU   A N      1 
ATOM   666  C CA     . LEU   A 1 93  ? -5.87629  4.42270   -11.30397 1.000 34.52832  ? 86  LEU   A CA     1 
ATOM   667  C C      . LEU   A 1 93  ? -6.67758  5.71593   -11.22039 1.000 34.12621  ? 86  LEU   A C      1 
ATOM   668  O O      . LEU   A 1 93  ? -6.63996  6.41115   -10.19911 1.000 48.01266  ? 86  LEU   A O      1 
ATOM   669  C CB     . LEU   A 1 93  ? -6.32669  3.45496   -10.21154 1.000 30.69554  ? 86  LEU   A CB     1 
ATOM   670  C CG     . LEU   A 1 93  ? -6.25644  1.96105   -10.52326 1.000 31.45947  ? 86  LEU   A CG     1 
ATOM   671  C CD1    . LEU   A 1 93  ? -6.91928  1.16446   -9.41120  1.000 31.07522  ? 86  LEU   A CD1    1 
ATOM   672  C CD2    . LEU   A 1 93  ? -6.90061  1.65624   -11.86691 1.000 30.11056  ? 86  LEU   A CD2    1 
ATOM   673  N N      . LEU   A 1 94  ? -7.40637  6.03198   -12.28967 1.000 32.88010  ? 87  LEU   A N      1 
ATOM   674  C CA     . LEU   A 1 94  ? -8.39016  7.10371   -12.24191 1.000 29.30529  ? 87  LEU   A CA     1 
ATOM   675  C C      . LEU   A 1 94  ? -9.75816  6.62204   -11.78144 1.000 38.11352  ? 87  LEU   A C      1 
ATOM   676  O O      . LEU   A 1 94  ? -10.55219 7.43390   -11.29166 1.000 34.45097  ? 87  LEU   A O      1 
ATOM   677  C CB     . LEU   A 1 94  ? -8.53319  7.76873   -13.61544 1.000 25.49095  ? 87  LEU   A CB     1 
ATOM   678  C CG     . LEU   A 1 94  ? -7.27185  8.28644   -14.30755 1.000 38.99762  ? 87  LEU   A CG     1 
ATOM   679  C CD1    . LEU   A 1 94  ? -7.58616  8.65599   -15.74833 1.000 38.91960  ? 87  LEU   A CD1    1 
ATOM   680  C CD2    . LEU   A 1 94  ? -6.68693  9.47527   -13.56148 1.000 39.61320  ? 87  LEU   A CD2    1 
ATOM   681  N N      . ASP   A 1 95  ? -10.05025 5.33008   -11.92054 1.000 31.15200  ? 88  ASP   A N      1 
ATOM   682  C CA     . ASP   A 1 95  ? -11.35716 4.80454   -11.54995 1.000 33.30050  ? 88  ASP   A CA     1 
ATOM   683  C C      . ASP   A 1 95  ? -11.32077 3.28339   -11.58736 1.000 35.21365  ? 88  ASP   A C      1 
ATOM   684  O O      . ASP   A 1 95  ? -10.54727 2.68621   -12.34192 1.000 33.62278  ? 88  ASP   A O      1 
ATOM   685  C CB     . ASP   A 1 95  ? -12.45341 5.33329   -12.48332 1.000 32.49260  ? 88  ASP   A CB     1 
ATOM   686  C CG     . ASP   A 1 95  ? -13.84805 5.04207   -11.96667 1.000 39.98469  ? 88  ASP   A CG     1 
ATOM   687  O OD1    . ASP   A 1 95  ? -14.00614 4.87969   -10.73833 1.000 41.58164  ? 88  ASP   A OD1    1 
ATOM   688  O OD2    . ASP   A 1 95  ? -14.78650 4.97891   -12.78844 1.000 34.67410  ? 88  ASP   A OD2    1 
ATOM   689  N N      . VAL   A 1 96  ? -12.16538 2.67089   -10.75938 1.000 30.00075  ? 89  VAL   A N      1 
ATOM   690  C CA     . VAL   A 1 96  ? -12.36077 1.22435   -10.72946 1.000 32.94412  ? 89  VAL   A CA     1 
ATOM   691  C C      . VAL   A 1 96  ? -13.85186 0.96374   -10.57980 1.000 39.50105  ? 89  VAL   A C      1 
ATOM   692  O O      . VAL   A 1 96  ? -14.49890 1.54235   -9.70065  1.000 33.57231  ? 89  VAL   A O      1 
ATOM   693  C CB     . VAL   A 1 96  ? -11.58325 0.55412   -9.57867  1.000 32.52791  ? 89  VAL   A CB     1 
ATOM   694  C CG1    . VAL   A 1 96  ? -11.53985 -0.95466  -9.77390  1.000 31.09808  ? 89  VAL   A CG1    1 
ATOM   695  C CG2    . VAL   A 1 96  ? -10.17943 1.12857   -9.47067  1.000 40.44759  ? 89  VAL   A CG2    1 
ATOM   696  N N      . PHE   A 1 97  ? -14.40262 0.10121   -11.43145 1.000 34.49783  ? 90  PHE   A N      1 
ATOM   697  C CA     . PHE   A 1 97  ? -15.83331 -0.15565  -11.37406 1.000 38.06670  ? 90  PHE   A CA     1 
ATOM   698  C C      . PHE   A 1 97  ? -16.12560 -1.60675  -11.72803 1.000 37.75745  ? 90  PHE   A C      1 
ATOM   699  O O      . PHE   A 1 97  ? -15.34909 -2.27572  -12.41615 1.000 35.58730  ? 90  PHE   A O      1 
ATOM   700  C CB     . PHE   A 1 97  ? -16.61747 0.79632   -12.29397 1.000 34.85243  ? 90  PHE   A CB     1 
ATOM   701  C CG     . PHE   A 1 97  ? -16.34824 0.60030   -13.76378 1.000 33.03616  ? 90  PHE   A CG     1 
ATOM   702  C CD1    . PHE   A 1 97  ? -17.02277 -0.37199  -14.48464 1.000 28.61544  ? 90  PHE   A CD1    1 
ATOM   703  C CD2    . PHE   A 1 97  ? -15.44022 1.40771   -14.42915 1.000 31.73440  ? 90  PHE   A CD2    1 
ATOM   704  C CE1    . PHE   A 1 97  ? -16.78545 -0.54505  -15.83524 1.000 32.46166  ? 90  PHE   A CE1    1 
ATOM   705  C CE2    . PHE   A 1 97  ? -15.19875 1.23833   -15.78081 1.000 34.33487  ? 90  PHE   A CE2    1 
ATOM   706  C CZ     . PHE   A 1 97  ? -15.87256 0.26115   -16.48417 1.000 29.91611  ? 90  PHE   A CZ     1 
ATOM   707  N N      . THR   A 1 98  ? -17.26661 -2.08205  -11.23199 1.000 30.64223  ? 91  THR   A N      1 
ATOM   708  C CA     . THR   A 1 98  ? -17.81958 -3.38510  -11.54696 1.000 30.50849  ? 91  THR   A CA     1 
ATOM   709  C C      . THR   A 1 98  ? -19.31344 -3.20004  -11.76875 1.000 38.66002  ? 91  THR   A C      1 
ATOM   710  O O      . THR   A 1 98  ? -19.95702 -2.44154  -11.02926 1.000 44.71906  ? 91  THR   A O      1 
ATOM   711  C CB     . THR   A 1 98  ? -17.58736 -4.41324  -10.42925 1.000 38.99873  ? 91  THR   A CB     1 
ATOM   712  O OG1    . THR   A 1 98  ? -18.15700 -5.67303  -10.80972 1.000 33.05987  ? 91  THR   A OG1    1 
ATOM   713  C CG2    . THR   A 1 98  ? -18.23453 -3.94665  -9.13136  1.000 30.76658  ? 91  THR   A CG2    1 
ATOM   714  N N      . PRO   A 1 99  ? -19.89038 -3.85720  -12.77984 1.000 44.41737  ? 92  PRO   A N      1 
ATOM   715  C CA     . PRO   A 1 99  ? -21.34891 -3.78569  -12.96256 1.000 42.01907  ? 92  PRO   A CA     1 
ATOM   716  C C      . PRO   A 1 99  ? -22.12683 -4.41552  -11.82439 1.000 45.59022  ? 92  PRO   A C      1 
ATOM   717  O O      . PRO   A 1 99  ? -23.33508 -4.17038  -11.71414 1.000 47.84177  ? 92  PRO   A O      1 
ATOM   718  C CB     . PRO   A 1 99  ? -21.58223 -4.54513  -14.27737 1.000 43.82500  ? 92  PRO   A CB     1 
ATOM   719  C CG     . PRO   A 1 99  ? -20.23248 -4.63881  -14.93262 1.000 50.49487  ? 92  PRO   A CG     1 
ATOM   720  C CD     . PRO   A 1 99  ? -19.24378 -4.68105  -13.81260 1.000 44.21276  ? 92  PRO   A CD     1 
ATOM   721  N N      . ALA   A 1 100 ? -21.47379 -5.19869  -10.97003 1.000 50.49420  ? 93  ALA   A N      1 
ATOM   722  C CA     . ALA   A 1 100 ? -22.17309 -5.90032  -9.90523  1.000 57.85769  ? 93  ALA   A CA     1 
ATOM   723  C C      . ALA   A 1 100 ? -22.56551 -4.94159  -8.78912  1.000 52.39193  ? 93  ALA   A C      1 
ATOM   724  O O      . ALA   A 1 100 ? -21.81819 -4.02315  -8.44099  1.000 49.81982  ? 93  ALA   A O      1 
ATOM   725  C CB     . ALA   A 1 100 ? -21.29821 -7.02344  -9.34973  1.000 56.58360  ? 93  ALA   A CB     1 
ATOM   726  N N      . ARG   A 1 101 ? -23.75436 -5.16048  -8.23081  1.000 54.04315  ? 94  ARG   A N      1 
ATOM   727  C CA     . ARG   A 1 101 ? -24.23244 -4.41258  -7.07668  1.000 61.62412  ? 94  ARG   A CA     1 
ATOM   728  C C      . ARG   A 1 101 ? -24.22041 -5.25126  -5.80577  1.000 55.54249  ? 94  ARG   A C      1 
ATOM   729  O O      . ARG   A 1 101 ? -24.76872 -4.82338  -4.78453  1.000 49.65682  ? 94  ARG   A O      1 
ATOM   730  C CB     . ARG   A 1 101 ? -25.63821 -3.87148  -7.34311  1.000 59.30036  ? 94  ARG   A CB     1 
ATOM   731  C CG     . ARG   A 1 101 ? -26.55078 -4.86008  -8.04097  1.000 64.18393  ? 94  ARG   A CG     1 
ATOM   732  C CD     . ARG   A 1 101 ? -27.53718 -4.15792  -8.95661  1.000 73.94746  ? 94  ARG   A CD     1 
ATOM   733  N NE     . ARG   A 1 101 ? -28.29390 -5.11380  -9.75572  1.000 81.50352  ? 94  ARG   A NE     1 
ATOM   734  C CZ     . ARG   A 1 101 ? -29.39342 -5.73024  -9.34355  1.000 89.59100  ? 94  ARG   A CZ     1 
ATOM   735  N NH1    . ARG   A 1 101 ? -30.01722 -6.61375  -10.10542 1.000 93.74349  ? 94  ARG   A NH1    1 
ATOM   736  N NH2    . ARG   A 1 101 ? -29.87813 -5.45530  -8.13551  1.000 92.86623  ? 94  ARG   A NH2    1 
ATOM   737  N N      . SER   A 1 102 ? -23.61485 -6.43627  -5.84947  1.000 55.66573  ? 95  SER   A N      1 
ATOM   738  C CA     . SER   A 1 102 ? -23.47742 -7.29370  -4.68048  1.000 49.70279  ? 95  SER   A CA     1 
ATOM   739  C C      . SER   A 1 102 ? -22.29059 -8.22072  -4.90278  1.000 54.33304  ? 95  SER   A C      1 
ATOM   740  O O      . SER   A 1 102 ? -21.82024 -8.39463  -6.02993  1.000 52.95090  ? 95  SER   A O      1 
ATOM   741  C CB     . SER   A 1 102 ? -24.75583 -8.09609  -4.41409  1.000 49.19063  ? 95  SER   A CB     1 
ATOM   742  O OG     . SER   A 1 102 ? -24.85971 -9.20259  -5.29317  1.000 58.90073  ? 95  SER   A OG     1 
ATOM   743  N N      . LEU   A 1 103 ? -21.81153 -8.81776  -3.80770  1.000 55.51499  ? 96  LEU   A N      1 
ATOM   744  C CA     . LEU   A 1 103 ? -20.63969 -9.68622  -3.89312  1.000 50.38259  ? 96  LEU   A CA     1 
ATOM   745  C C      . LEU   A 1 103 ? -20.95272 -10.97080 -4.65262  1.000 53.69826  ? 96  LEU   A C      1 
ATOM   746  O O      . LEU   A 1 103 ? -20.09478 -11.50237 -5.36889  1.000 50.07403  ? 96  LEU   A O      1 
ATOM   747  C CB     . LEU   A 1 103 ? -20.11906 -9.99877  -2.48784  1.000 51.59467  ? 96  LEU   A CB     1 
ATOM   748  C CG     . LEU   A 1 103 ? -18.94467 -10.97555 -2.38718  1.000 51.88424  ? 96  LEU   A CG     1 
ATOM   749  C CD1    . LEU   A 1 103 ? -17.75988 -10.49560 -3.21246  1.000 44.16228  ? 96  LEU   A CD1    1 
ATOM   750  C CD2    . LEU   A 1 103 ? -18.54294 -11.17392 -0.93504  1.000 42.50446  ? 96  LEU   A CD2    1 
ATOM   751  N N      . GLU   A 1 104 ? -22.17166 -11.48984 -4.49998  1.000 56.74570  ? 97  GLU   A N      1 
ATOM   752  C CA     . GLU   A 1 104 ? -22.56310 -12.68647 -5.23629  1.000 59.87862  ? 97  GLU   A CA     1 
ATOM   753  C C      . GLU   A 1 104 ? -22.67595 -12.40602 -6.72925  1.000 57.99413  ? 97  GLU   A C      1 
ATOM   754  O O      . GLU   A 1 104 ? -22.51810 -13.32020 -7.54706  1.000 65.71392  ? 97  GLU   A O      1 
ATOM   755  C CB     . GLU   A 1 104 ? -23.88426 -13.23775 -4.69405  1.000 63.89598  ? 97  GLU   A CB     1 
ATOM   756  C CG     . GLU   A 1 104 ? -24.91851 -12.17775 -4.32605  1.000 76.05689  ? 97  GLU   A CG     1 
ATOM   757  C CD     . GLU   A 1 104 ? -24.58743 -11.44537 -3.03668  1.000 81.60531  ? 97  GLU   A CD     1 
ATOM   758  O OE1    . GLU   A 1 104 ? -25.48546 -11.28836 -2.18362  1.000 86.49636  ? 97  GLU   A OE1    1 
ATOM   759  O OE2    . GLU   A 1 104 ? -23.42619 -11.01599 -2.88071  1.000 81.62253  ? 97  GLU   A OE2    1 
ATOM   760  N N      . GLU   A 1 105 ? -22.94998 -11.15472 -7.09949  1.000 44.70377  ? 98  GLU   A N      1 
ATOM   761  C CA     . GLU   A 1 105 ? -22.92771 -10.74255 -8.49618  1.000 60.06708  ? 98  GLU   A CA     1 
ATOM   762  C C      . GLU   A 1 105 ? -21.52232 -10.42300 -8.98643  1.000 55.34346  ? 98  GLU   A C      1 
ATOM   763  O O      . GLU   A 1 105 ? -21.26859 -10.49709 -10.19351 1.000 64.40776  ? 98  GLU   A O      1 
ATOM   764  C CB     . GLU   A 1 105 ? -23.82012 -9.51417  -8.69407  1.000 66.31507  ? 98  GLU   A CB     1 
ATOM   765  C CG     . GLU   A 1 105 ? -25.21139 -9.81157  -9.22247  1.000 49.81716  ? 98  GLU   A CG     1 
ATOM   766  C CD     . GLU   A 1 105 ? -25.79851 -8.63917  -9.98502  1.000 70.27405  ? 98  GLU   A CD     1 
ATOM   767  O OE1    . GLU   A 1 105 ? -25.58790 -7.48415  -9.55671  1.000 68.90107  ? 98  GLU   A OE1    1 
ATOM   768  O OE2    . GLU   A 1 105 ? -26.46899 -8.87137  -11.01261 1.000 78.12613  ? 98  GLU   A OE2    1 
ATOM   769  N N      . PHE   A 1 106 ? -20.61123 -10.07392 -8.07810  1.000 51.73410  ? 99  PHE   A N      1 
ATOM   770  C CA     . PHE   A 1 106 ? -19.27193 -9.61646  -8.43048  1.000 49.10530  ? 99  PHE   A CA     1 
ATOM   771  C C      . PHE   A 1 106 ? -18.51349 -10.64797 -9.25549  1.000 41.18134  ? 99  PHE   A C      1 
ATOM   772  O O      . PHE   A 1 106 ? -18.11993 -11.69535 -8.73620  1.000 43.18148  ? 99  PHE   A O      1 
ATOM   773  C CB     . PHE   A 1 106 ? -18.48540 -9.28033  -7.16017  1.000 42.20262  ? 99  PHE   A CB     1 
ATOM   774  C CG     . PHE   A 1 106 ? -17.13823 -8.66834  -7.42124  1.000 41.27577  ? 99  PHE   A CG     1 
ATOM   775  C CD1    . PHE   A 1 106 ? -16.96170 -7.76007  -8.45100  1.000 38.42107  ? 99  PHE   A CD1    1 
ATOM   776  C CD2    . PHE   A 1 106 ? -16.04892 -8.99783  -6.63132  1.000 41.97593  ? 99  PHE   A CD2    1 
ATOM   777  C CE1    . PHE   A 1 106 ? -15.72288 -7.19426  -8.69047  1.000 41.83235  ? 99  PHE   A CE1    1 
ATOM   778  C CE2    . PHE   A 1 106 ? -14.80842 -8.43540  -6.86507  1.000 43.36727  ? 99  PHE   A CE2    1 
ATOM   779  C CZ     . PHE   A 1 106 ? -14.64507 -7.53266  -7.89641  1.000 38.51667  ? 99  PHE   A CZ     1 
ATOM   780  N N      . ASN   A 1 107 ? -18.29327 -10.36051 -10.53508 1.000 48.68866  ? 100 ASN   A N      1 
ATOM   781  C CA     . ASN   A 1 107 ? -17.51250 -11.26804 -11.36692 1.000 51.12558  ? 100 ASN   A CA     1 
ATOM   782  C C      . ASN   A 1 107 ? -16.70582 -10.56914 -12.45133 1.000 47.17095  ? 100 ASN   A C      1 
ATOM   783  O O      . ASN   A 1 107 ? -15.95285 -11.24840 -13.15434 1.000 44.09862  ? 100 ASN   A O      1 
ATOM   784  C CB     . ASN   A 1 107 ? -18.43239 -12.32243 -12.00517 1.000 53.64013  ? 100 ASN   A CB     1 
ATOM   785  C CG     . ASN   A 1 107 ? -17.76416 -13.67879 -12.12609 1.000 69.12394  ? 100 ASN   A CG     1 
ATOM   786  O OD1    . ASN   A 1 107 ? -17.27358 -14.23191 -11.14141 1.000 67.55873  ? 100 ASN   A OD1    1 
ATOM   787  N ND2    . ASN   A 1 107 ? -17.73908 -14.22061 -13.33786 1.000 72.81125  ? 100 ASN   A ND2    1 
ATOM   788  N N      . ASP   A 1 108 ? -16.82434 -9.25372  -12.61709 1.000 45.84178  ? 101 ASP   A N      1 
ATOM   789  C CA     . ASP   A 1 108 ? -16.07675 -8.52260  -13.62916 1.000 47.66052  ? 101 ASP   A CA     1 
ATOM   790  C C      . ASP   A 1 108 ? -15.46490 -7.27629  -13.00763 1.000 44.68588  ? 101 ASP   A C      1 
ATOM   791  O O      . ASP   A 1 108 ? -16.09021 -6.61776  -12.17073 1.000 38.68436  ? 101 ASP   A O      1 
ATOM   792  C CB     . ASP   A 1 108 ? -16.97181 -8.14016  -14.81362 1.000 50.00343  ? 101 ASP   A CB     1 
ATOM   793  C CG     . ASP   A 1 108 ? -17.06769 -9.24362  -15.84920 1.000 53.65554  ? 101 ASP   A CG     1 
ATOM   794  O OD1    . ASP   A 1 108 ? -18.15527 -9.84259  -15.98515 1.000 55.07271  ? 101 ASP   A OD1    1 
ATOM   795  O OD2    . ASP   A 1 108 ? -16.05365 -9.51410  -16.52578 1.000 58.84067  ? 101 ASP   A OD2    1 
ATOM   796  N N      . VAL   A 1 109 ? -14.23939 -6.95825  -13.42030 1.000 39.29091  ? 102 VAL   A N      1 
ATOM   797  C CA     . VAL   A 1 109 ? -13.49061 -5.82969  -12.88130 1.000 38.65236  ? 102 VAL   A CA     1 
ATOM   798  C C      . VAL   A 1 109 ? -12.94941 -5.00414  -14.03908 1.000 33.99687  ? 102 VAL   A C      1 
ATOM   799  O O      . VAL   A 1 109 ? -12.35769 -5.55229  -14.97579 1.000 35.93615  ? 102 VAL   A O      1 
ATOM   800  C CB     . VAL   A 1 109 ? -12.33869 -6.28914  -11.96661 1.000 37.80482  ? 102 VAL   A CB     1 
ATOM   801  C CG1    . VAL   A 1 109 ? -11.59673 -5.08484  -11.40508 1.000 41.47776  ? 102 VAL   A CG1    1 
ATOM   802  C CG2    . VAL   A 1 109 ? -12.86605 -7.17011  -10.84520 1.000 35.61623  ? 102 VAL   A CG2    1 
ATOM   803  N N      . TYR   A 1 110 ? -13.14965 -3.69083  -13.97128 1.000 32.47523  ? 103 TYR   A N      1 
ATOM   804  C CA     . TYR   A 1 110 ? -12.60846 -2.75438  -14.94318 1.000 35.58867  ? 103 TYR   A CA     1 
ATOM   805  C C      . TYR   A 1 110 ? -11.69424 -1.76050  -14.24109 1.000 27.87005  ? 103 TYR   A C      1 
ATOM   806  O O      . TYR   A 1 110 ? -11.93520 -1.37431  -13.09368 1.000 27.64455  ? 103 TYR   A O      1 
ATOM   807  C CB     . TYR   A 1 110 ? -13.71690 -1.99195  -15.67517 1.000 26.10156  ? 103 TYR   A CB     1 
ATOM   808  C CG     . TYR   A 1 110 ? -14.60886 -2.84764  -16.54279 1.000 34.01593  ? 103 TYR   A CG     1 
ATOM   809  C CD1    . TYR   A 1 110 ? -15.57800 -3.66659  -15.98003 1.000 39.44205  ? 103 TYR   A CD1    1 
ATOM   810  C CD2    . TYR   A 1 110 ? -14.49599 -2.82056  -17.92631 1.000 32.49444  ? 103 TYR   A CD2    1 
ATOM   811  C CE1    . TYR   A 1 110 ? -16.40175 -4.44363  -16.76931 1.000 37.48985  ? 103 TYR   A CE1    1 
ATOM   812  C CE2    . TYR   A 1 110 ? -15.31547 -3.59378  -18.72416 1.000 37.41218  ? 103 TYR   A CE2    1 
ATOM   813  C CZ     . TYR   A 1 110 ? -16.26665 -4.40345  -18.14046 1.000 35.76652  ? 103 TYR   A CZ     1 
ATOM   814  O OH     . TYR   A 1 110 ? -17.08615 -5.17592  -18.92992 1.000 40.27376  ? 103 TYR   A OH     1 
ATOM   815  N N      . LEU   A 1 111 ? -10.64522 -1.34271  -14.94532 1.000 31.80302  ? 104 LEU   A N      1 
ATOM   816  C CA     . LEU   A 1 111 ? -9.68265  -0.38005  -14.42740 1.000 30.72707  ? 104 LEU   A CA     1 
ATOM   817  C C      . LEU   A 1 111 ? -9.53650  0.75837   -15.42504 1.000 30.63155  ? 104 LEU   A C      1 
ATOM   818  O O      . LEU   A 1 111 ? -9.40492  0.51732   -16.62918 1.000 27.86500  ? 104 LEU   A O      1 
ATOM   819  C CB     . LEU   A 1 111 ? -8.32571  -1.04209  -14.16649 1.000 32.48561  ? 104 LEU   A CB     1 
ATOM   820  C CG     . LEU   A 1 111 ? -8.35255  -2.29156  -13.28243 1.000 33.39551  ? 104 LEU   A CG     1 
ATOM   821  C CD1    . LEU   A 1 111 ? -6.96018  -2.88819  -13.14704 1.000 35.79180  ? 104 LEU   A CD1    1 
ATOM   822  C CD2    . LEU   A 1 111 ? -8.93654  -1.96877  -11.91552 1.000 33.22229  ? 104 LEU   A CD2    1 
ATOM   823  N N      . VAL   A 1 112 ? -9.56211  1.99269   -14.92571 1.000 28.81256  ? 105 VAL   A N      1 
ATOM   824  C CA     . VAL   A 1 112 ? -9.46493  3.18669   -15.75723 1.000 29.97277  ? 105 VAL   A CA     1 
ATOM   825  C C      . VAL   A 1 112 ? -8.16562  3.91002   -15.43605 1.000 31.08352  ? 105 VAL   A C      1 
ATOM   826  O O      . VAL   A 1 112 ? -7.78557  4.04114   -14.26609 1.000 29.42313  ? 105 VAL   A O      1 
ATOM   827  C CB     . VAL   A 1 112 ? -10.66927 4.12704   -15.55611 1.000 29.33964  ? 105 VAL   A CB     1 
ATOM   828  C CG1    . VAL   A 1 112 ? -10.52132 5.36255   -16.43202 1.000 30.44077  ? 105 VAL   A CG1    1 
ATOM   829  C CG2    . VAL   A 1 112 ? -11.97025 3.40337   -15.85960 1.000 28.08318  ? 105 VAL   A CG2    1 
ATOM   830  N N      . THR   A 1 113 ? -7.49185  4.38861   -16.47887 1.000 27.33115  ? 106 THR   A N      1 
ATOM   831  C CA     . THR   A 1 113 ? -6.25595  5.14071   -16.32606 1.000 30.18510  ? 106 THR   A CA     1 
ATOM   832  C C      . THR   A 1 113 ? -6.13857  6.12043   -17.48543 1.000 33.21049  ? 106 THR   A C      1 
ATOM   833  O O      . THR   A 1 113 ? -6.96858  6.13681   -18.39952 1.000 32.38402  ? 106 THR   A O      1 
ATOM   834  C CB     . THR   A 1 113 ? -5.03871  4.21152   -16.27194 1.000 34.58472  ? 106 THR   A CB     1 
ATOM   835  O OG1    . THR   A 1 113 ? -3.88659  4.95639   -15.85664 1.000 47.57071  ? 106 THR   A OG1    1 
ATOM   836  C CG2    . THR   A 1 113 ? -4.77256  3.61314   -17.64052 1.000 21.69342  ? 106 THR   A CG2    1 
ATOM   837  N N      . HIS   A 1 114 ? -5.09567  6.94530   -17.44036 1.000 32.21698  ? 107 HIS   A N      1 
ATOM   838  C CA     . HIS   A 1 114 ? -4.81847  7.83998   -18.55292 1.000 29.76345  ? 107 HIS   A CA     1 
ATOM   839  C C      . HIS   A 1 114 ? -4.57478  7.03741   -19.82377 1.000 31.68950  ? 107 HIS   A C      1 
ATOM   840  O O      . HIS   A 1 114 ? -4.05950  5.91673   -19.78983 1.000 33.33903  ? 107 HIS   A O      1 
ATOM   841  C CB     . HIS   A 1 114 ? -3.60094  8.71558   -18.25511 1.000 33.84094  ? 107 HIS   A CB     1 
ATOM   842  C CG     . HIS   A 1 114 ? -3.70510  9.48426   -16.97612 1.000 41.91220  ? 107 HIS   A CG     1 
ATOM   843  N ND1    . HIS   A 1 114 ? -4.08816  10.80775  -16.93062 1.000 37.17628  ? 107 HIS   A ND1    1 
ATOM   844  C CD2    . HIS   A 1 114 ? -3.47346  9.11520   -15.69481 1.000 43.54860  ? 107 HIS   A CD2    1 
ATOM   845  C CE1    . HIS   A 1 114 ? -4.08691  11.22052  -15.67555 1.000 44.30389  ? 107 HIS   A CE1    1 
ATOM   846  N NE2    . HIS   A 1 114 ? -3.71522  10.21327  -14.90605 1.000 46.18423  ? 107 HIS   A NE2    1 
ATOM   847  N N      . LEU   A 1 115 ? -4.95818  7.61948   -20.95496 1.000 30.49847  ? 108 LEU   A N      1 
ATOM   848  C CA     . LEU   A 1 115 ? -4.68153  7.02984   -22.25742 1.000 31.92374  ? 108 LEU   A CA     1 
ATOM   849  C C      . LEU   A 1 115 ? -3.38416  7.61931   -22.79596 1.000 25.29222  ? 108 LEU   A C      1 
ATOM   850  O O      . LEU   A 1 115 ? -3.29885  8.82934   -23.02922 1.000 32.71595  ? 108 LEU   A O      1 
ATOM   851  C CB     . LEU   A 1 115 ? -5.83299  7.28136   -23.22971 1.000 32.00694  ? 108 LEU   A CB     1 
ATOM   852  C CG     . LEU   A 1 115 ? -5.58334  6.76820   -24.64877 1.000 35.43984  ? 108 LEU   A CG     1 
ATOM   853  C CD1    . LEU   A 1 115 ? -5.41247  5.25576   -24.64517 1.000 34.65638  ? 108 LEU   A CD1    1 
ATOM   854  C CD2    . LEU   A 1 115 ? -6.70553  7.18536   -25.58545 1.000 32.14534  ? 108 LEU   A CD2    1 
ATOM   855  N N      . MET   A 1 116 ? -2.37573  6.77069   -22.98008 1.000 30.76894  ? 109 MET   A N      1 
ATOM   856  C CA     . MET   A 1 116 ? -1.09596  7.21029   -23.50820 1.000 33.15837  ? 109 MET   A CA     1 
ATOM   857  C C      . MET   A 1 116 ? -1.11639  7.14184   -25.03560 1.000 37.68746  ? 109 MET   A C      1 
ATOM   858  O O      . MET   A 1 116 ? -2.10443  6.73995   -25.65592 1.000 33.33256  ? 109 MET   A O      1 
ATOM   859  C CB     . MET   A 1 116 ? 0.03849   6.36897   -22.92459 1.000 30.01813  ? 109 MET   A CB     1 
ATOM   860  C CG     . MET   A 1 116 ? 0.28701   6.59442   -21.43634 1.000 31.40573  ? 109 MET   A CG     1 
ATOM   861  S SD     . MET   A 1 116 ? 0.55661   8.31957   -20.98758 1.000 39.74019  ? 109 MET   A SD     1 
ATOM   862  C CE     . MET   A 1 116 ? 2.35159   8.39369   -20.99726 1.000 33.25244  ? 109 MET   A CE     1 
ATOM   863  N N      . GLY   A 1 117 ? -0.00853  7.54189   -25.65303 1.000 39.21254  ? 110 GLY   A N      1 
ATOM   864  C CA     . GLY   A 1 117 ? 0.04883   7.64087   -27.09713 1.000 33.41945  ? 110 GLY   A CA     1 
ATOM   865  C C      . GLY   A 1 117 ? 0.44278   6.36149   -27.80467 1.000 49.18119  ? 110 GLY   A C      1 
ATOM   866  O O      . GLY   A 1 117 ? -0.08331  6.05093   -28.87933 1.000 41.55813  ? 110 GLY   A O      1 
ATOM   867  N N      . ALA   A 1 118 ? 1.37417   5.61500   -27.21577 1.000 43.55841  ? 111 ALA   A N      1 
ATOM   868  C CA     . ALA   A 1 118 ? 1.89486   4.41461   -27.85762 1.000 47.96870  ? 111 ALA   A CA     1 
ATOM   869  C C      . ALA   A 1 118 ? 2.85264   3.68573   -26.92867 1.000 36.31468  ? 111 ALA   A C      1 
ATOM   870  O O      . ALA   A 1 118 ? 3.06112   4.11689   -25.79568 1.000 37.95031  ? 111 ALA   A O      1 
ATOM   871  C CB     . ALA   A 1 118 ? 2.59235   4.76865   -29.16350 1.000 48.43863  ? 111 ALA   A CB     1 
ATOM   872  N N      . ASP   A 1 119 ? 3.42453   2.57934   -27.39580 1.000 48.33557  ? 112 ASP   A N      1 
ATOM   873  C CA     . ASP   A 1 119 ? 4.42997   1.83145   -26.66147 1.000 50.09618  ? 112 ASP   A CA     1 
ATOM   874  C C      . ASP   A 1 119 ? 5.82520   2.29867   -27.06160 1.000 55.45617  ? 112 ASP   A C      1 
ATOM   875  O O      . ASP   A 1 119 ? 6.01298   3.01222   -28.04980 1.000 60.58617  ? 112 ASP   A O      1 
ATOM   876  C CB     . ASP   A 1 119 ? 4.27931   0.33598   -26.93422 1.000 43.63561  ? 112 ASP   A CB     1 
ATOM   877  C CG     . ASP   A 1 119 ? 3.08094   -0.26728  -26.23594 1.000 49.65562  ? 112 ASP   A CG     1 
ATOM   878  O OD1    . ASP   A 1 119 ? 2.77182   0.16183   -25.10579 1.000 61.45180  ? 112 ASP   A OD1    1 
ATOM   879  O OD2    . ASP   A 1 119 ? 2.45564   -1.18349  -26.81241 1.000 55.82372  ? 112 ASP   A OD2    1 
ATOM   880  N N      . LEU   A 1 120 ? 6.82111   1.87140   -26.28381 1.000 47.66936  ? 113 LEU   A N      1 
ATOM   881  C CA     . LEU   A 1 120 ? 8.19480   2.20531   -26.62990 1.000 58.48887  ? 113 LEU   A CA     1 
ATOM   882  C C      . LEU   A 1 120 ? 8.69210   1.41359   -27.83116 1.000 64.95186  ? 113 LEU   A C      1 
ATOM   883  O O      . LEU   A 1 120 ? 9.70646   1.79160   -28.42501 1.000 72.97685  ? 113 LEU   A O      1 
ATOM   884  C CB     . LEU   A 1 120 ? 9.12158   1.98587   -25.43498 1.000 46.35126  ? 113 LEU   A CB     1 
ATOM   885  C CG     . LEU   A 1 120 ? 10.24892  3.01929   -25.36982 1.000 57.55037  ? 113 LEU   A CG     1 
ATOM   886  C CD1    . LEU   A 1 120 ? 9.69900   4.41525   -25.64077 1.000 57.36221  ? 113 LEU   A CD1    1 
ATOM   887  C CD2    . LEU   A 1 120 ? 10.97234  2.97279   -24.03283 1.000 52.44084  ? 113 LEU   A CD2    1 
ATOM   888  N N      . ASN   A 1 121 ? 8.00958   0.32653   -28.20107 1.000 61.32263  ? 114 ASN   A N      1 
ATOM   889  C CA     . ASN   A 1 121 ? 8.33286   -0.34399  -29.45627 1.000 73.63549  ? 114 ASN   A CA     1 
ATOM   890  C C      . ASN   A 1 121 ? 8.02872   0.55764   -30.64465 1.000 79.86505  ? 114 ASN   A C      1 
ATOM   891  O O      . ASN   A 1 121 ? 8.78181   0.58135   -31.62571 1.000 84.81974  ? 114 ASN   A O      1 
ATOM   892  C CB     . ASN   A 1 121 ? 7.55728   -1.65620  -29.57488 1.000 71.47111  ? 114 ASN   A CB     1 
ATOM   893  C CG     . ASN   A 1 121 ? 7.37739   -2.35160  -28.24201 1.000 64.64070  ? 114 ASN   A CG     1 
ATOM   894  O OD1    . ASN   A 1 121 ? 6.52968   -1.96630  -27.43682 1.000 56.50300  ? 114 ASN   A OD1    1 
ATOM   895  N ND2    . ASN   A 1 121 ? 8.17243   -3.38809  -28.00417 1.000 54.12367  ? 114 ASN   A ND2    1 
ATOM   896  N N      . ASN   A 1 122 ? 6.92640   1.30832   -30.57091 1.000 73.49232  ? 115 ASN   A N      1 
ATOM   897  C CA     . ASN   A 1 122 ? 6.56797   2.21682   -31.65388 1.000 81.65218  ? 115 ASN   A CA     1 
ATOM   898  C C      . ASN   A 1 122 ? 7.54730   3.37979   -31.76190 1.000 90.88097  ? 115 ASN   A C      1 
ATOM   899  O O      . ASN   A 1 122 ? 7.82113   3.85264   -32.87132 1.000 94.06108  ? 115 ASN   A O      1 
ATOM   900  C CB     . ASN   A 1 122 ? 5.14123   2.72747   -31.45139 1.000 77.27493  ? 115 ASN   A CB     1 
ATOM   901  C CG     . ASN   A 1 122 ? 4.20440   1.64608   -30.94951 1.000 80.61722  ? 115 ASN   A CG     1 
ATOM   902  O OD1    . ASN   A 1 122 ? 4.48219   0.45366   -31.08913 1.000 79.76745  ? 115 ASN   A OD1    1 
ATOM   903  N ND2    . ASN   A 1 122 ? 3.09154   2.05622   -30.35578 1.000 64.92556  ? 115 ASN   A ND2    1 
ATOM   904  N N      . ILE   A 1 123 ? 8.08251   3.85327   -30.63269 1.000 87.42296  ? 116 ILE   A N      1 
ATOM   905  C CA     . ILE   A 1 123 ? 9.09344   4.90461   -30.68731 1.000 84.96991  ? 116 ILE   A CA     1 
ATOM   906  C C      . ILE   A 1 123 ? 10.43044  4.33721   -31.14729 1.000 95.12126  ? 116 ILE   A C      1 
ATOM   907  O O      . ILE   A 1 123 ? 11.20878  5.03439   -31.80815 1.000 101.52447 ? 116 ILE   A O      1 
ATOM   908  C CB     . ILE   A 1 123 ? 9.21890   5.62063   -29.33187 1.000 78.51492  ? 116 ILE   A CB     1 
ATOM   909  C CG1    . ILE   A 1 123 ? 8.12688   6.68515   -29.19195 1.000 75.50997  ? 116 ILE   A CG1    1 
ATOM   910  C CG2    . ILE   A 1 123 ? 10.59030  6.25632   -29.20766 1.000 74.93829  ? 116 ILE   A CG2    1 
ATOM   911  C CD1    . ILE   A 1 123 ? 6.71897   6.14655   -29.28320 1.000 70.73755  ? 116 ILE   A CD1    1 
ATOM   912  N N      . VAL   A 1 124 ? 10.70849  3.06688   -30.84074 1.000 93.09646  ? 117 VAL   A N      1 
ATOM   913  C CA     . VAL   A 1 124 ? 11.89326  2.41696   -31.38576 1.000 98.30986  ? 117 VAL   A CA     1 
ATOM   914  C C      . VAL   A 1 124 ? 11.69989  2.06893   -32.85394 1.000 105.80290 ? 117 VAL   A C      1 
ATOM   915  O O      . VAL   A 1 124 ? 12.68382  1.86856   -33.57571 1.000 112.73576 ? 117 VAL   A O      1 
ATOM   916  C CB     . VAL   A 1 124 ? 12.25094  1.15889   -30.57004 1.000 93.09788  ? 117 VAL   A CB     1 
ATOM   917  C CG1    . VAL   A 1 124 ? 13.45209  0.45197   -31.17916 1.000 87.15915  ? 117 VAL   A CG1    1 
ATOM   918  C CG2    . VAL   A 1 124 ? 12.52849  1.52464   -29.11807 1.000 86.53073  ? 117 VAL   A CG2    1 
ATOM   919  N N      . LYS   A 1 125 ? 10.44967  1.99857   -33.31891 1.000 100.25756 ? 118 LYS   A N      1 
ATOM   920  C CA     . LYS   A 1 125 ? 10.19989  1.70789   -34.72692 1.000 105.76087 ? 118 LYS   A CA     1 
ATOM   921  C C      . LYS   A 1 125 ? 10.78070  2.79308   -35.62357 1.000 120.29305 ? 118 LYS   A C      1 
ATOM   922  O O      . LYS   A 1 125 ? 11.29770  2.50225   -36.70836 1.000 129.50431 ? 118 LYS   A O      1 
ATOM   923  C CB     . LYS   A 1 125 ? 8.69918   1.54976   -34.97414 1.000 104.01649 ? 118 LYS   A CB     1 
ATOM   924  C CG     . LYS   A 1 125 ? 8.30138   1.55546   -36.44446 1.000 103.14556 ? 118 LYS   A CG     1 
ATOM   925  C CD     . LYS   A 1 125 ? 7.88861   2.94651   -36.90402 1.000 105.87299 ? 118 LYS   A CD     1 
ATOM   926  C CE     . LYS   A 1 125 ? 6.67076   3.44428   -36.14147 1.000 103.51871 ? 118 LYS   A CE     1 
ATOM   927  N NZ     . LYS   A 1 125 ? 6.26096   4.80864   -36.57690 1.000 90.88639  ? 118 LYS   A NZ     1 
ATOM   928  N N      . CYS   A 1 126 ? 10.69836  4.05275   -35.19268 1.000 117.30417 ? 119 CYS   A N      1 
ATOM   929  C CA     . CYS   A 1 126 ? 11.32155  5.12877   -35.95473 1.000 120.13265 ? 119 CYS   A CA     1 
ATOM   930  C C      . CYS   A 1 126 ? 12.83299  4.93658   -36.03334 1.000 128.72529 ? 119 CYS   A C      1 
ATOM   931  O O      . CYS   A 1 126 ? 13.45315  5.22445   -37.06453 1.000 123.26306 ? 119 CYS   A O      1 
ATOM   932  C CB     . CYS   A 1 126 ? 10.97175  6.47714   -35.32773 1.000 111.56324 ? 119 CYS   A CB     1 
ATOM   933  S SG     . CYS   A 1 126 ? 9.24060   6.95833   -35.45505 1.000 106.66714 ? 119 CYS   A SG     1 
ATOM   934  N N      . GLN   A 1 127 ? 13.44082  4.44667   -34.95337 1.000 129.09546 ? 120 GLN   A N      1 
ATOM   935  C CA     . GLN   A 1 127 ? 14.83568  4.01058   -34.88895 1.000 132.80982 ? 120 GLN   A CA     1 
ATOM   936  C C      . GLN   A 1 127 ? 15.83607  5.15871   -34.84854 1.000 131.96727 ? 120 GLN   A C      1 
ATOM   937  O O      . GLN   A 1 127 ? 17.04802  4.90324   -34.93120 1.000 127.47063 ? 120 GLN   A O      1 
ATOM   938  C CB     . GLN   A 1 127 ? 15.19382  3.08964   -36.06056 1.000 140.59207 ? 120 GLN   A CB     1 
ATOM   939  C CG     . GLN   A 1 127 ? 14.39822  1.79365   -36.09630 1.000 137.50842 ? 120 GLN   A CG     1 
ATOM   940  C CD     . GLN   A 1 127 ? 14.04674  1.36207   -37.50722 1.000 141.34060 ? 120 GLN   A CD     1 
ATOM   941  O OE1    . GLN   A 1 127 ? 14.08526  2.16250   -38.44175 1.000 139.27121 ? 120 GLN   A OE1    1 
ATOM   942  N NE2    . GLN   A 1 127 ? 13.70037  0.08996   -37.66787 1.000 139.13918 ? 120 GLN   A NE2    1 
ATOM   943  N N      . LYS   A 1 128 ? 15.38575  6.41501   -34.72040 1.000 120.66988 ? 121 LYS   A N      1 
ATOM   944  C CA     . LYS   A 1 128 ? 16.29332  7.56610   -34.66959 1.000 111.15657 ? 121 LYS   A CA     1 
ATOM   945  C C      . LYS   A 1 128 ? 15.81712  8.50365   -33.55767 1.000 102.21686 ? 121 LYS   A C      1 
ATOM   946  O O      . LYS   A 1 128 ? 15.13838  9.50413   -33.80081 1.000 102.79071 ? 121 LYS   A O      1 
ATOM   947  C CB     . LYS   A 1 128 ? 16.37093  8.28243   -36.01731 1.000 112.92533 ? 121 LYS   A CB     1 
ATOM   948  C CG     . LYS   A 1 128 ? 17.22180  9.54453   -35.99672 1.000 110.25575 ? 121 LYS   A CG     1 
ATOM   949  C CD     . LYS   A 1 128 ? 17.63938  9.95940   -37.39915 1.000 106.78219 ? 121 LYS   A CD     1 
ATOM   950  C CE     . LYS   A 1 128 ? 18.77073  9.08811   -37.92052 1.000 113.25791 ? 121 LYS   A CE     1 
ATOM   951  N NZ     . LYS   A 1 128 ? 19.59370  9.79151   -38.94363 1.000 100.16077 ? 121 LYS   A NZ     1 
ATOM   952  N N      . LEU   A 1 129 ? 16.18443  8.17340   -32.32323 1.000 89.30714  ? 122 LEU   A N      1 
ATOM   953  C CA     . LEU   A 1 129 ? 15.89758  9.02354   -31.17715 1.000 77.30756  ? 122 LEU   A CA     1 
ATOM   954  C C      . LEU   A 1 129 ? 17.08398  9.94287   -30.91981 1.000 77.99571  ? 122 LEU   A C      1 
ATOM   955  O O      . LEU   A 1 129 ? 18.23467  9.49313   -30.91275 1.000 71.74313  ? 122 LEU   A O      1 
ATOM   956  C CB     . LEU   A 1 129 ? 15.60196  8.18183   -29.93479 1.000 62.06602  ? 122 LEU   A CB     1 
ATOM   957  C CG     . LEU   A 1 129 ? 14.13286  8.02464   -29.54052 1.000 71.23983  ? 122 LEU   A CG     1 
ATOM   958  C CD1    . LEU   A 1 129 ? 13.32351  7.46873   -30.70131 1.000 79.28157  ? 122 LEU   A CD1    1 
ATOM   959  C CD2    . LEU   A 1 129 ? 13.99854  7.13784   -28.31197 1.000 70.52663  ? 122 LEU   A CD2    1 
ATOM   960  N N      . THR   A 1 130 ? 16.80344  11.22781  -30.72131 1.000 74.74883  ? 123 THR   A N      1 
ATOM   961  C CA     . THR   A 1 130 ? 17.85730  12.16918  -30.37637 1.000 71.47073  ? 123 THR   A CA     1 
ATOM   962  C C      . THR   A 1 130 ? 18.39515  11.86842  -28.98214 1.000 69.19813  ? 123 THR   A C      1 
ATOM   963  O O      . THR   A 1 130 ? 17.68780  11.34254  -28.11846 1.000 65.64528  ? 123 THR   A O      1 
ATOM   964  C CB     . THR   A 1 130 ? 17.34066  13.60745  -30.43747 1.000 69.64113  ? 123 THR   A CB     1 
ATOM   965  O OG1    . THR   A 1 130 ? 16.06281  13.68778  -29.79300 1.000 73.07994  ? 123 THR   A OG1    1 
ATOM   966  C CG2    . THR   A 1 130 ? 17.20458  14.06495  -31.88280 1.000 71.98081  ? 123 THR   A CG2    1 
ATOM   967  N N      . ASP   A 1 131 ? 19.67025  12.20189  -28.76909 1.000 52.33138  ? 124 ASP   A N      1 
ATOM   968  C CA     . ASP   A 1 131 ? 20.27322  11.97787  -27.46004 1.000 49.71088  ? 124 ASP   A CA     1 
ATOM   969  C C      . ASP   A 1 131 ? 19.48567  12.67386  -26.35819 1.000 49.04165  ? 124 ASP   A C      1 
ATOM   970  O O      . ASP   A 1 131 ? 19.43520  12.18126  -25.22487 1.000 40.14280  ? 124 ASP   A O      1 
ATOM   971  C CB     . ASP   A 1 131 ? 21.72622  12.45187  -27.45954 1.000 42.40551  ? 124 ASP   A CB     1 
ATOM   972  C CG     . ASP   A 1 131 ? 22.36923  12.35067  -26.09081 1.000 45.74413  ? 124 ASP   A CG     1 
ATOM   973  O OD1    . ASP   A 1 131 ? 22.51208  11.21908  -25.58128 1.000 40.44942  ? 124 ASP   A OD1    1 
ATOM   974  O OD2    . ASP   A 1 131 ? 22.73103  13.40246  -25.52412 1.000 47.61195  ? 124 ASP   A OD2    1 
ATOM   975  N N      . ASP   A 1 132 ? 18.86671  13.81631  -26.66825 1.000 45.66076  ? 125 ASP   A N      1 
ATOM   976  C CA     . ASP   A 1 132 ? 18.00484  14.47648  -25.69447 1.000 42.44191  ? 125 ASP   A CA     1 
ATOM   977  C C      . ASP   A 1 132 ? 16.72618  13.68498  -25.45436 1.000 43.74569  ? 125 ASP   A C      1 
ATOM   978  O O      . ASP   A 1 132 ? 16.15550  13.74803  -24.35935 1.000 37.34187  ? 125 ASP   A O      1 
ATOM   979  C CB     . ASP   A 1 132 ? 17.67492  15.89449  -26.15956 1.000 55.25568  ? 125 ASP   A CB     1 
ATOM   980  C CG     . ASP   A 1 132 ? 16.66288  16.58029  -25.26366 1.000 64.70379  ? 125 ASP   A CG     1 
ATOM   981  O OD1    . ASP   A 1 132 ? 15.47853  16.65741  -25.65257 1.000 61.01131  ? 125 ASP   A OD1    1 
ATOM   982  O OD2    . ASP   A 1 132 ? 17.05085  17.04159  -24.17004 1.000 65.41525  ? 125 ASP   A OD2    1 
ATOM   983  N N      . HIS   A 1 133 ? 16.25887  12.94359  -26.46140 1.000 43.48095  ? 126 HIS   A N      1 
ATOM   984  C CA     . HIS   A 1 133 ? 15.11688  12.05965  -26.25603 1.000 46.46370  ? 126 HIS   A CA     1 
ATOM   985  C C      . HIS   A 1 133 ? 15.47390  10.91512  -25.31727 1.000 42.64646  ? 126 HIS   A C      1 
ATOM   986  O O      . HIS   A 1 133 ? 14.63817  10.47371  -24.51942 1.000 38.72865  ? 126 HIS   A O      1 
ATOM   987  C CB     . HIS   A 1 133 ? 14.62271  11.51427  -27.59608 1.000 50.55930  ? 126 HIS   A CB     1 
ATOM   988  C CG     . HIS   A 1 133 ? 13.68868  12.43416  -28.31830 1.000 55.65725  ? 126 HIS   A CG     1 
ATOM   989  N ND1    . HIS   A 1 133 ? 13.30156  13.65425  -27.80782 1.000 51.03786  ? 126 HIS   A ND1    1 
ATOM   990  C CD2    . HIS   A 1 133 ? 13.06366  12.31104  -29.51326 1.000 65.79942  ? 126 HIS   A CD2    1 
ATOM   991  C CE1    . HIS   A 1 133 ? 12.47924  14.24358  -28.65742 1.000 57.68775  ? 126 HIS   A CE1    1 
ATOM   992  N NE2    . HIS   A 1 133 ? 12.31810  13.44950  -29.70040 1.000 56.21320  ? 126 HIS   A NE2    1 
ATOM   993  N N      . VAL   A 1 134 ? 16.71130  10.42146  -25.39836 1.000 37.87885  ? 127 VAL   A N      1 
ATOM   994  C CA     . VAL   A 1 134 ? 17.12445  9.31599   -24.54050 1.000 37.40553  ? 127 VAL   A CA     1 
ATOM   995  C C      . VAL   A 1 134 ? 17.30647  9.79255   -23.10544 1.000 31.45011  ? 127 VAL   A C      1 
ATOM   996  O O      . VAL   A 1 134 ? 16.89399  9.11546   -22.15611 1.000 38.84503  ? 127 VAL   A O      1 
ATOM   997  C CB     . VAL   A 1 134 ? 18.40444  8.66294   -25.09137 1.000 35.01673  ? 127 VAL   A CB     1 
ATOM   998  C CG1    . VAL   A 1 134 ? 18.80173  7.47181   -24.23503 1.000 36.72517  ? 127 VAL   A CG1    1 
ATOM   999  C CG2    . VAL   A 1 134 ? 18.20005  8.24111   -26.53891 1.000 41.18580  ? 127 VAL   A CG2    1 
ATOM   1000 N N      . GLN   A 1 135 ? 17.92644  10.96079  -22.92124 1.000 39.31871  ? 128 GLN   A N      1 
ATOM   1001 C CA     . GLN   A 1 135 ? 18.05289  11.52934  -21.58316 1.000 36.96286  ? 128 GLN   A CA     1 
ATOM   1002 C C      . GLN   A 1 135 ? 16.69090  11.64231  -20.90949 1.000 30.71514  ? 128 GLN   A C      1 
ATOM   1003 O O      . GLN   A 1 135 ? 16.50849  11.20855  -19.76672 1.000 37.80708  ? 128 GLN   A O      1 
ATOM   1004 C CB     . GLN   A 1 135 ? 18.72530  12.90287  -21.65341 1.000 34.16883  ? 128 GLN   A CB     1 
ATOM   1005 C CG     . GLN   A 1 135 ? 20.06985  12.92154  -22.35860 1.000 42.45093  ? 128 GLN   A CG     1 
ATOM   1006 C CD     . GLN   A 1 135 ? 20.66540  14.31613  -22.43565 1.000 38.74905  ? 128 GLN   A CD     1 
ATOM   1007 O OE1    . GLN   A 1 135 ? 19.98199  15.31109  -22.19122 1.000 45.81560  ? 128 GLN   A OE1    1 
ATOM   1008 N NE2    . GLN   A 1 135 ? 21.94551  14.39396  -22.77569 1.000 36.69434  ? 128 GLN   A NE2    1 
ATOM   1009 N N      . PHE   A 1 136 ? 15.71514  12.21648  -21.61704 1.000 33.28775  ? 129 PHE   A N      1 
ATOM   1010 C CA     . PHE   A 1 136 ? 14.40941  12.47531  -21.01844 1.000 32.42036  ? 129 PHE   A CA     1 
ATOM   1011 C C      . PHE   A 1 136 ? 13.62407  11.18558  -20.80777 1.000 29.48594  ? 129 PHE   A C      1 
ATOM   1012 O O      . PHE   A 1 136 ? 12.96477  11.01644  -19.77477 1.000 24.86238  ? 129 PHE   A O      1 
ATOM   1013 C CB     . PHE   A 1 136 ? 13.62668  13.45461  -21.89547 1.000 32.23889  ? 129 PHE   A CB     1 
ATOM   1014 C CG     . PHE   A 1 136 ? 12.30993  13.88123  -21.31047 1.000 30.52590  ? 129 PHE   A CG     1 
ATOM   1015 C CD1    . PHE   A 1 136 ? 12.22041  14.29768  -19.99238 1.000 31.18914  ? 129 PHE   A CD1    1 
ATOM   1016 C CD2    . PHE   A 1 136 ? 11.16238  13.87774  -22.08531 1.000 37.63597  ? 129 PHE   A CD2    1 
ATOM   1017 C CE1    . PHE   A 1 136 ? 11.00698  14.69319  -19.45684 1.000 35.37662  ? 129 PHE   A CE1    1 
ATOM   1018 C CE2    . PHE   A 1 136 ? 9.94807   14.27191  -21.55664 1.000 37.29440  ? 129 PHE   A CE2    1 
ATOM   1019 C CZ     . PHE   A 1 136 ? 9.86993   14.68038  -20.24112 1.000 32.95518  ? 129 PHE   A CZ     1 
ATOM   1020 N N      . LEU   A 1 137 ? 13.68244  10.26336  -21.77063 1.000 30.67375  ? 130 LEU   A N      1 
ATOM   1021 C CA     . LEU   A 1 137 ? 12.92717  9.01976   -21.64794 1.000 28.55845  ? 130 LEU   A CA     1 
ATOM   1022 C C      . LEU   A 1 137 ? 13.48347  8.14296   -20.53217 1.000 32.10665  ? 130 LEU   A C      1 
ATOM   1023 O O      . LEU   A 1 137 ? 12.72958  7.63887   -19.69101 1.000 28.85689  ? 130 LEU   A O      1 
ATOM   1024 C CB     . LEU   A 1 137 ? 12.93314  8.26634   -22.97842 1.000 29.31975  ? 130 LEU   A CB     1 
ATOM   1025 C CG     . LEU   A 1 137 ? 12.02713  8.81293   -24.08302 1.000 26.62771  ? 130 LEU   A CG     1 
ATOM   1026 C CD1    . LEU   A 1 137 ? 12.30954  8.10377   -25.39816 1.000 32.97484  ? 130 LEU   A CD1    1 
ATOM   1027 C CD2    . LEU   A 1 137 ? 10.56052  8.67863   -23.70045 1.000 24.07290  ? 130 LEU   A CD2    1 
ATOM   1028 N N      . ILE   A 1 138 ? 14.80393  7.94461   -20.50951 1.000 32.06756  ? 131 ILE   A N      1 
ATOM   1029 C CA     . ILE   A 1 138 ? 15.39498  7.10018   -19.47653 1.000 32.72327  ? 131 ILE   A CA     1 
ATOM   1030 C C      . ILE   A 1 138 ? 15.31509  7.77297   -18.11297 1.000 28.68979  ? 131 ILE   A C      1 
ATOM   1031 O O      . ILE   A 1 138 ? 15.22543  7.09253   -17.08354 1.000 28.02475  ? 131 ILE   A O      1 
ATOM   1032 C CB     . ILE   A 1 138 ? 16.84694  6.73595   -19.83670 1.000 35.90459  ? 131 ILE   A CB     1 
ATOM   1033 C CG1    . ILE   A 1 138 ? 16.89905  6.00297   -21.17982 1.000 34.96139  ? 131 ILE   A CG1    1 
ATOM   1034 C CG2    . ILE   A 1 138 ? 17.46926  5.88842   -18.73434 1.000 24.80217  ? 131 ILE   A CG2    1 
ATOM   1035 C CD1    . ILE   A 1 138 ? 16.09728  4.71444   -21.21157 1.000 32.44631  ? 131 ILE   A CD1    1 
ATOM   1036 N N      . TYR   A 1 139 ? 15.34930  9.10761   -18.07127 1.000 33.49983  ? 132 TYR   A N      1 
ATOM   1037 C CA     . TYR   A 1 139 ? 15.22020  9.79544   -16.79072 1.000 33.38165  ? 132 TYR   A CA     1 
ATOM   1038 C C      . TYR   A 1 139 ? 13.86259  9.52313   -16.15663 1.000 25.83548  ? 132 TYR   A C      1 
ATOM   1039 O O      . TYR   A 1 139 ? 13.76341  9.33660   -14.93804 1.000 23.64004  ? 132 TYR   A O      1 
ATOM   1040 C CB     . TYR   A 1 139 ? 15.43110  11.29927  -16.96183 1.000 28.49442  ? 132 TYR   A CB     1 
ATOM   1041 C CG     . TYR   A 1 139 ? 15.06322  12.08221  -15.72171 1.000 31.32183  ? 132 TYR   A CG     1 
ATOM   1042 C CD1    . TYR   A 1 139 ? 15.94984  12.19041  -14.65843 1.000 27.17339  ? 132 TYR   A CD1    1 
ATOM   1043 C CD2    . TYR   A 1 139 ? 13.82190  12.69501  -15.60446 1.000 31.82063  ? 132 TYR   A CD2    1 
ATOM   1044 C CE1    . TYR   A 1 139 ? 15.61671  12.89543  -13.51872 1.000 28.75281  ? 132 TYR   A CE1    1 
ATOM   1045 C CE2    . TYR   A 1 139 ? 13.47898  13.40170  -14.46717 1.000 29.67323  ? 132 TYR   A CE2    1 
ATOM   1046 C CZ     . TYR   A 1 139 ? 14.38055  13.49904  -13.42804 1.000 33.95232  ? 132 TYR   A CZ     1 
ATOM   1047 O OH     . TYR   A 1 139 ? 14.04513  14.20211  -12.29360 1.000 41.16952  ? 132 TYR   A OH     1 
ATOM   1048 N N      . GLN   A 1 140 ? 12.80241  9.50238   -16.96679 1.000 25.81365  ? 133 GLN   A N      1 
ATOM   1049 C CA     . GLN   A 1 140 ? 11.47435  9.22750   -16.42946 1.000 27.16889  ? 133 GLN   A CA     1 
ATOM   1050 C C      . GLN   A 1 140 ? 11.35476  7.78139   -15.96500 1.000 29.69639  ? 133 GLN   A C      1 
ATOM   1051 O O      . GLN   A 1 140 ? 10.76371  7.50966   -14.91279 1.000 23.92738  ? 133 GLN   A O      1 
ATOM   1052 C CB     . GLN   A 1 140 ? 10.40821  9.55254   -17.47396 1.000 26.99144  ? 133 GLN   A CB     1 
ATOM   1053 C CG     . GLN   A 1 140 ? 10.26332  11.03822  -17.75850 1.000 24.84238  ? 133 GLN   A CG     1 
ATOM   1054 C CD     . GLN   A 1 140 ? 9.34530   11.31878  -18.92910 1.000 27.42248  ? 133 GLN   A CD     1 
ATOM   1055 O OE1    . GLN   A 1 140 ? 8.14597   11.53194  -18.75416 1.000 35.08089  ? 133 GLN   A OE1    1 
ATOM   1056 N NE2    . GLN   A 1 140 ? 9.90433   11.31750  -20.13351 1.000 28.95340  ? 133 GLN   A NE2    1 
ATOM   1057 N N      . ILE   A 1 141 ? 11.90464  6.83935   -16.73505 1.000 22.44625  ? 134 ILE   A N      1 
ATOM   1058 C CA     . ILE   A 1 141 ? 11.92194  5.44555   -16.29748 1.000 30.95785  ? 134 ILE   A CA     1 
ATOM   1059 C C      . ILE   A 1 141 ? 12.58585  5.33396   -14.93173 1.000 25.79119  ? 134 ILE   A C      1 
ATOM   1060 O O      . ILE   A 1 141 ? 12.01989  4.77006   -13.98737 1.000 26.02496  ? 134 ILE   A O      1 
ATOM   1061 C CB     . ILE   A 1 141 ? 12.63159  4.55878   -17.33676 1.000 26.26555  ? 134 ILE   A CB     1 
ATOM   1062 C CG1    . ILE   A 1 141 ? 11.83458  4.50374   -18.64008 1.000 22.95440  ? 134 ILE   A CG1    1 
ATOM   1063 C CG2    . ILE   A 1 141 ? 12.83968  3.15717   -16.78198 1.000 21.72857  ? 134 ILE   A CG2    1 
ATOM   1064 C CD1    . ILE   A 1 141 ? 12.54533  3.76187   -19.75300 1.000 30.90624  ? 134 ILE   A CD1    1 
ATOM   1065 N N      . LEU   A 1 142 ? 13.80011  5.87563   -14.80874 1.000 23.79944  ? 135 LEU   A N      1 
ATOM   1066 C CA     . LEU   A 1 142 ? 14.51114  5.82349   -13.53600 1.000 24.90570  ? 135 LEU   A CA     1 
ATOM   1067 C C      . LEU   A 1 142 ? 13.72641  6.52761   -12.43694 1.000 25.96617  ? 135 LEU   A C      1 
ATOM   1068 O O      . LEU   A 1 142 ? 13.68225  6.05547   -11.29456 1.000 23.63841  ? 135 LEU   A O      1 
ATOM   1069 C CB     . LEU   A 1 142 ? 15.89851  6.44840   -13.68695 1.000 27.81614  ? 135 LEU   A CB     1 
ATOM   1070 C CG     . LEU   A 1 142 ? 16.85500  5.77167   -14.67155 1.000 34.39262  ? 135 LEU   A CG     1 
ATOM   1071 C CD1    . LEU   A 1 142 ? 18.15704  6.55223   -14.78093 1.000 28.59159  ? 135 LEU   A CD1    1 
ATOM   1072 C CD2    . LEU   A 1 142 ? 17.12060  4.33219   -14.25774 1.000 24.68567  ? 135 LEU   A CD2    1 
ATOM   1073 N N      . ARG   A 1 143 ? 13.10075  7.66083   -12.76439 1.000 30.27076  ? 136 ARG   A N      1 
ATOM   1074 C CA     . ARG   A 1 143 ? 12.33995  8.40939   -11.76867 1.000 29.48991  ? 136 ARG   A CA     1 
ATOM   1075 C C      . ARG   A 1 143 ? 11.17760  7.58193   -11.23298 1.000 28.52612  ? 136 ARG   A C      1 
ATOM   1076 O O      . ARG   A 1 143 ? 10.95353  7.51492   -10.01840 1.000 23.32630  ? 136 ARG   A O      1 
ATOM   1077 C CB     . ARG   A 1 143 ? 11.84014  9.71889   -12.37853 1.000 29.87231  ? 136 ARG   A CB     1 
ATOM   1078 C CG     . ARG   A 1 143 ? 11.22543  10.68796  -11.38479 1.000 27.19421  ? 136 ARG   A CG     1 
ATOM   1079 C CD     . ARG   A 1 143 ? 10.93687  12.02291  -12.05155 1.000 37.44043  ? 136 ARG   A CD     1 
ATOM   1080 N NE     . ARG   A 1 143 ? 10.27059  12.95822  -11.15403 1.000 44.39087  ? 136 ARG   A NE     1 
ATOM   1081 C CZ     . ARG   A 1 143 ? 9.02557   13.38640  -11.31061 1.000 48.90046  ? 136 ARG   A CZ     1 
ATOM   1082 N NH1    . ARG   A 1 143 ? 8.27590   12.97711  -12.32114 1.000 42.66037  ? 136 ARG   A NH1    1 
ATOM   1083 N NH2    . ARG   A 1 143 ? 8.52036   14.24786  -10.43209 1.000 44.85226  ? 136 ARG   A NH2    1 
ATOM   1084 N N      . GLY   A 1 144 ? 10.41750  6.94965   -12.12960 1.000 26.47452  ? 137 GLY   A N      1 
ATOM   1085 C CA     . GLY   A 1 144 ? 9.37074   6.04700   -11.68610 1.000 25.60657  ? 137 GLY   A CA     1 
ATOM   1086 C C      . GLY   A 1 144 ? 9.91578   4.80796   -11.00752 1.000 28.84741  ? 137 GLY   A C      1 
ATOM   1087 O O      . GLY   A 1 144 ? 9.28222   4.26535   -10.09755 1.000 27.47925  ? 137 GLY   A O      1 
ATOM   1088 N N      . LEU   A 1 145 ? 11.09750  4.34892   -11.42906 1.000 25.85242  ? 138 LEU   A N      1 
ATOM   1089 C CA     . LEU   A 1 145 ? 11.69379  3.16287   -10.82286 1.000 25.43838  ? 138 LEU   A CA     1 
ATOM   1090 C C      . LEU   A 1 145 ? 12.14991  3.43813   -9.39489  1.000 28.60986  ? 138 LEU   A C      1 
ATOM   1091 O O      . LEU   A 1 145 ? 12.07707  2.55314   -8.53357  1.000 30.33487  ? 138 LEU   A O      1 
ATOM   1092 C CB     . LEU   A 1 145 ? 12.86240  2.67052   -11.67902 1.000 24.36841  ? 138 LEU   A CB     1 
ATOM   1093 C CG     . LEU   A 1 145 ? 12.96675  1.15703   -11.87528 1.000 32.86491  ? 138 LEU   A CG     1 
ATOM   1094 C CD1    . LEU   A 1 145 ? 11.58946  0.53421   -12.04488 1.000 36.46319  ? 138 LEU   A CD1    1 
ATOM   1095 C CD2    . LEU   A 1 145 ? 13.85366  0.83620   -13.06738 1.000 32.62025  ? 138 LEU   A CD2    1 
ATOM   1096 N N      . LYS   A 1 146 ? 12.63648  4.65101   -9.12314  1.000 26.90365  ? 139 LYS   A N      1 
ATOM   1097 C CA     . LYS   A 1 146 ? 12.99393  4.99240   -7.75003  1.000 25.91942  ? 139 LYS   A CA     1 
ATOM   1098 C C      . LYS   A 1 146 ? 11.76539  4.97963   -6.85130  1.000 27.45445  ? 139 LYS   A C      1 
ATOM   1099 O O      . LYS   A 1 146 ? 11.82116  4.49848   -5.71323  1.000 29.83475  ? 139 LYS   A O      1 
ATOM   1100 C CB     . LYS   A 1 146 ? 13.67763  6.35887   -7.69290  1.000 27.99306  ? 139 LYS   A CB     1 
ATOM   1101 C CG     . LYS   A 1 146 ? 13.85212  6.88633   -6.27218  1.000 28.67080  ? 139 LYS   A CG     1 
ATOM   1102 C CD     . LYS   A 1 146 ? 14.28852  8.34251   -6.25188  1.000 33.91844  ? 139 LYS   A CD     1 
ATOM   1103 C CE     . LYS   A 1 146 ? 14.19920  8.91739   -4.84576  1.000 36.34799  ? 139 LYS   A CE     1 
ATOM   1104 N NZ     . LYS   A 1 146 ? 14.97592  10.17875  -4.69886  1.000 36.60372  ? 139 LYS   A NZ     1 
ATOM   1105 N N      . TYR   A 1 147 ? 10.64602  5.51114   -7.34587  1.000 30.69519  ? 140 TYR   A N      1 
ATOM   1106 C CA     . TYR   A 1 147 ? 9.40118   5.46726   -6.58753  1.000 25.10454  ? 140 TYR   A CA     1 
ATOM   1107 C C      . TYR   A 1 147 ? 8.96263   4.02792   -6.34758  1.000 27.85187  ? 140 TYR   A C      1 
ATOM   1108 O O      . TYR   A 1 147 ? 8.62439   3.64727   -5.22068  1.000 26.71134  ? 140 TYR   A O      1 
ATOM   1109 C CB     . TYR   A 1 147 ? 8.31897   6.25290   -7.33017  1.000 29.36471  ? 140 TYR   A CB     1 
ATOM   1110 C CG     . TYR   A 1 147 ? 6.94000   6.16165   -6.71598  1.000 30.56091  ? 140 TYR   A CG     1 
ATOM   1111 C CD1    . TYR   A 1 147 ? 6.51796   7.08427   -5.76742  1.000 32.57826  ? 140 TYR   A CD1    1 
ATOM   1112 C CD2    . TYR   A 1 147 ? 6.05581   5.15934   -7.09322  1.000 32.02591  ? 140 TYR   A CD2    1 
ATOM   1113 C CE1    . TYR   A 1 147 ? 5.25637   7.00683   -5.20739  1.000 35.00725  ? 140 TYR   A CE1    1 
ATOM   1114 C CE2    . TYR   A 1 147 ? 4.79420   5.07286   -6.53832  1.000 34.10786  ? 140 TYR   A CE2    1 
ATOM   1115 C CZ     . TYR   A 1 147 ? 4.39914   5.99823   -5.59678  1.000 35.90230  ? 140 TYR   A CZ     1 
ATOM   1116 O OH     . TYR   A 1 147 ? 3.14206   5.91353   -5.04378  1.000 32.62668  ? 140 TYR   A OH     1 
ATOM   1117 N N      . ILE   A 1 148 ? 8.97040   3.20867   -7.40137  1.000 23.64778  ? 141 ILE   A N      1 
ATOM   1118 C CA     . ILE   A 1 148 ? 8.56282   1.81241   -7.26503  1.000 30.22323  ? 141 ILE   A CA     1 
ATOM   1119 C C      . ILE   A 1 148 ? 9.47582   1.08639   -6.28566  1.000 33.68412  ? 141 ILE   A C      1 
ATOM   1120 O O      . ILE   A 1 148 ? 9.01341   0.37498   -5.38542  1.000 30.88470  ? 141 ILE   A O      1 
ATOM   1121 C CB     . ILE   A 1 148 ? 8.55042   1.12021   -8.63959  1.000 32.93166  ? 141 ILE   A CB     1 
ATOM   1122 C CG1    . ILE   A 1 148 ? 7.41642   1.67044   -9.50665  1.000 33.15383  ? 141 ILE   A CG1    1 
ATOM   1123 C CG2    . ILE   A 1 148 ? 8.42431   -0.38766  -8.47607  1.000 29.98701  ? 141 ILE   A CG2    1 
ATOM   1124 C CD1    . ILE   A 1 148 ? 7.50077   1.24954   -10.95679 1.000 34.04728  ? 141 ILE   A CD1    1 
ATOM   1125 N N      . HIS   A 1 149 ? 10.79036  1.25357   -6.44895  1.000 36.29743  ? 142 HIS   A N      1 
ATOM   1126 C CA     . HIS   A 1 149 ? 11.73380  0.55584   -5.58284  1.000 29.14128  ? 142 HIS   A CA     1 
ATOM   1127 C C      . HIS   A 1 149 ? 11.65772  1.05640   -4.14646  1.000 31.93073  ? 142 HIS   A C      1 
ATOM   1128 O O      . HIS   A 1 149 ? 11.97372  0.30791   -3.21446  1.000 34.41649  ? 142 HIS   A O      1 
ATOM   1129 C CB     . HIS   A 1 149 ? 13.15200  0.70148   -6.13148  1.000 29.33866  ? 142 HIS   A CB     1 
ATOM   1130 C CG     . HIS   A 1 149 ? 13.41491  -0.13724  -7.34331  1.000 42.46135  ? 142 HIS   A CG     1 
ATOM   1131 N ND1    . HIS   A 1 149 ? 14.54716  0.00340   -8.11739  1.000 33.53100  ? 142 HIS   A ND1    1 
ATOM   1132 C CD2    . HIS   A 1 149 ? 12.68883  -1.12784  -7.91447  1.000 26.16345  ? 142 HIS   A CD2    1 
ATOM   1133 C CE1    . HIS   A 1 149 ? 14.50685  -0.86473  -9.11281  1.000 33.08841  ? 142 HIS   A CE1    1 
ATOM   1134 N NE2    . HIS   A 1 149 ? 13.38988  -1.56308  -9.01247  1.000 30.40098  ? 142 HIS   A NE2    1 
ATOM   1135 N N      . SER   A 1 150 ? 11.24421  2.30943   -3.94449  1.000 34.50284  ? 143 SER   A N      1 
ATOM   1136 C CA     . SER   A 1 150 ? 11.05831  2.81379   -2.58972  1.000 39.05857  ? 143 SER   A CA     1 
ATOM   1137 C C      . SER   A 1 150 ? 9.88914   2.13953   -1.88515  1.000 37.56798  ? 143 SER   A C      1 
ATOM   1138 O O      . SER   A 1 150 ? 9.84853   2.12663   -0.64989  1.000 45.45333  ? 143 SER   A O      1 
ATOM   1139 C CB     . SER   A 1 150 ? 10.85808  4.33051   -2.61234  1.000 34.42109  ? 143 SER   A CB     1 
ATOM   1140 O OG     . SER   A 1 150 ? 9.65613   4.68044   -3.27581  1.000 35.10530  ? 143 SER   A OG     1 
ATOM   1141 N N      . ALA   A 1 151 ? 8.94414   1.58117   -2.63863  1.000 38.04566  ? 144 ALA   A N      1 
ATOM   1142 C CA     . ALA   A 1 151 ? 7.84423   0.80991   -2.07503  1.000 44.89119  ? 144 ALA   A CA     1 
ATOM   1143 C C      . ALA   A 1 151 ? 8.21951   -0.64242  -1.81325  1.000 43.67111  ? 144 ALA   A C      1 
ATOM   1144 O O      . ALA   A 1 151 ? 7.34654   -1.43625  -1.44457  1.000 41.40997  ? 144 ALA   A O      1 
ATOM   1145 C CB     . ALA   A 1 151 ? 6.62870   0.87042   -3.00462  1.000 38.56567  ? 144 ALA   A CB     1 
ATOM   1146 N N      . ASP   A 1 152 ? 9.49289   -1.00261  -1.98668  1.000 35.73456  ? 145 ASP   A N      1 
ATOM   1147 C CA     . ASP   A 1 152 ? 9.96421   -2.37774  -1.83595  1.000 43.47433  ? 145 ASP   A CA     1 
ATOM   1148 C C      . ASP   A 1 152 ? 9.43266   -3.28589  -2.94148  1.000 35.98331  ? 145 ASP   A C      1 
ATOM   1149 O O      . ASP   A 1 152 ? 9.32649   -4.50066  -2.75849  1.000 37.05358  ? 145 ASP   A O      1 
ATOM   1150 C CB     . ASP   A 1 152 ? 9.60197   -2.95348  -0.46089  1.000 46.34580  ? 145 ASP   A CB     1 
ATOM   1151 C CG     . ASP   A 1 152 ? 9.65849   -1.91692  0.64503   1.000 64.39415  ? 145 ASP   A CG     1 
ATOM   1152 O OD1    . ASP   A 1 152 ? 10.69647  -1.23312  0.77392   1.000 58.02181  ? 145 ASP   A OD1    1 
ATOM   1153 O OD2    . ASP   A 1 152 ? 8.66174   -1.79031  1.38770   1.000 67.12761  ? 145 ASP   A OD2    1 
ATOM   1154 N N      . ILE   A 1 153 ? 9.09918   -2.71134  -4.09471  1.000 32.72784  ? 146 ILE   A N      1 
ATOM   1155 C CA     . ILE   A 1 153 ? 8.52055   -3.44487  -5.21485  1.000 32.17783  ? 146 ILE   A CA     1 
ATOM   1156 C C      . ILE   A 1 153 ? 9.58214   -3.61704  -6.29140  1.000 38.05273  ? 146 ILE   A C      1 
ATOM   1157 O O      . ILE   A 1 153 ? 10.29431  -2.66357  -6.62936  1.000 33.41486  ? 146 ILE   A O      1 
ATOM   1158 C CB     . ILE   A 1 153 ? 7.28481   -2.72552  -5.78381  1.000 32.67609  ? 146 ILE   A CB     1 
ATOM   1159 C CG1    . ILE   A 1 153 ? 6.13944   -2.73717  -4.77081  1.000 29.06771  ? 146 ILE   A CG1    1 
ATOM   1160 C CG2    . ILE   A 1 153 ? 6.85009   -3.36698  -7.09618  1.000 24.27886  ? 146 ILE   A CG2    1 
ATOM   1161 C CD1    . ILE   A 1 153 ? 4.96236   -1.87945  -5.17945  1.000 38.54121  ? 146 ILE   A CD1    1 
ATOM   1162 N N      . ILE   A 1 154 ? 9.67996   -4.82925  -6.83281  1.000 29.93761  ? 147 ILE   A N      1 
ATOM   1163 C CA     . ILE   A 1 154 ? 10.53376  -5.13196  -7.97637  1.000 30.75576  ? 147 ILE   A CA     1 
ATOM   1164 C C      . ILE   A 1 154 ? 9.63441   -5.44243  -9.16437  1.000 32.28421  ? 147 ILE   A C      1 
ATOM   1165 O O      . ILE   A 1 154 ? 8.66326   -6.19791  -9.03289  1.000 33.06387  ? 147 ILE   A O      1 
ATOM   1166 C CB     . ILE   A 1 154 ? 11.48023  -6.30936  -7.68403  1.000 32.36792  ? 147 ILE   A CB     1 
ATOM   1167 C CG1    . ILE   A 1 154 ? 12.35806  -6.00648  -6.46857  1.000 33.53160  ? 147 ILE   A CG1    1 
ATOM   1168 C CG2    . ILE   A 1 154 ? 12.33500  -6.62075  -8.90451  1.000 34.19502  ? 147 ILE   A CG2    1 
ATOM   1169 C CD1    . ILE   A 1 154 ? 13.35170  -7.10241  -6.14776  1.000 35.95969  ? 147 ILE   A CD1    1 
ATOM   1170 N N      . HIS   A 1 155 ? 9.95401   -4.86073  -10.32194 1.000 24.35075  ? 148 HIS   A N      1 
ATOM   1171 C CA     . HIS   A 1 155 ? 9.14080   -5.08078  -11.51458 1.000 28.63744  ? 148 HIS   A CA     1 
ATOM   1172 C C      . HIS   A 1 155 ? 9.38566   -6.46754  -12.10127 1.000 38.01655  ? 148 HIS   A C      1 
ATOM   1173 O O      . HIS   A 1 155 ? 8.45031   -7.25764  -12.26919 1.000 38.84760  ? 148 HIS   A O      1 
ATOM   1174 C CB     . HIS   A 1 155 ? 9.42404   -3.99389  -12.55472 1.000 33.37656  ? 148 HIS   A CB     1 
ATOM   1175 C CG     . HIS   A 1 155 ? 8.41731   -3.94259  -13.66101 1.000 27.98442  ? 148 HIS   A CG     1 
ATOM   1176 N ND1    . HIS   A 1 155 ? 8.38163   -4.87130  -14.67854 1.000 32.10049  ? 148 HIS   A ND1    1 
ATOM   1177 C CD2    . HIS   A 1 155 ? 7.40679   -3.07580  -13.90761 1.000 27.86800  ? 148 HIS   A CD2    1 
ATOM   1178 C CE1    . HIS   A 1 155 ? 7.39343   -4.57783  -15.50508 1.000 34.21742  ? 148 HIS   A CE1    1 
ATOM   1179 N NE2    . HIS   A 1 155 ? 6.78580   -3.49300  -15.05973 1.000 23.72647  ? 148 HIS   A NE2    1 
ATOM   1180 N N      . ARG   A 1 156 ? 10.63894  -6.77508  -12.42702 1.000 33.31207  ? 149 ARG   A N      1 
ATOM   1181 C CA     . ARG   A 1 156 ? 11.12739  -8.07343  -12.87305 1.000 31.42166  ? 149 ARG   A CA     1 
ATOM   1182 C C      . ARG   A 1 156 ? 10.76782  -8.37412  -14.32729 1.000 30.72292  ? 149 ARG   A C      1 
ATOM   1183 O O      . ARG   A 1 156 ? 11.24584  -9.37451  -14.86270 1.000 37.01330  ? 149 ARG   A O      1 
ATOM   1184 C CB     . ARG   A 1 156 ? 10.63029  -9.23774  -11.99372 1.000 42.28046  ? 149 ARG   A CB     1 
ATOM   1185 C CG     . ARG   A 1 156 ? 11.67603  -9.78351  -11.03492 1.000 54.19971  ? 149 ARG   A CG     1 
ATOM   1186 C CD     . ARG   A 1 156 ? 11.15447  -11.00263 -10.29149 1.000 55.56417  ? 149 ARG   A CD     1 
ATOM   1187 N NE     . ARG   A 1 156 ? 11.09184  -12.17789 -11.15213 1.000 52.69373  ? 149 ARG   A NE     1 
ATOM   1188 C CZ     . ARG   A 1 156 ? 11.03065  -13.42704 -10.71186 1.000 61.67813  ? 149 ARG   A CZ     1 
ATOM   1189 N NH1    . ARG   A 1 156 ? 11.01769  -13.70436 -9.41820  1.000 64.29872  ? 149 ARG   A NH1    1 
ATOM   1190 N NH2    . ARG   A 1 156 ? 10.98238  -14.42322 -11.59163 1.000 70.41795  ? 149 ARG   A NH2    1 
ATOM   1191 N N      . ASP   A 1 157 ? 9.94902   -7.55271  -14.99071 1.000 29.99115  ? 150 ASP   A N      1 
ATOM   1192 C CA     . ASP   A 1 157 ? 9.55852   -7.83029  -16.36879 1.000 32.65881  ? 150 ASP   A CA     1 
ATOM   1193 C C      . ASP   A 1 157 ? 9.63230   -6.58047  -17.23951 1.000 34.24848  ? 150 ASP   A C      1 
ATOM   1194 O O      . ASP   A 1 157 ? 8.87637   -6.45105  -18.20860 1.000 34.06174  ? 150 ASP   A O      1 
ATOM   1195 C CB     . ASP   A 1 157 ? 8.14923   -8.42678  -16.42927 1.000 47.12507  ? 150 ASP   A CB     1 
ATOM   1196 C CG     . ASP   A 1 157 ? 7.96153   -9.36291  -17.60893 1.000 51.83951  ? 150 ASP   A CG     1 
ATOM   1197 O OD1    . ASP   A 1 157 ? 8.73666   -10.33523 -17.72921 1.000 55.77551  ? 150 ASP   A OD1    1 
ATOM   1198 O OD2    . ASP   A 1 157 ? 7.03742   -9.12926  -18.41567 1.000 50.28793  ? 150 ASP   A OD2    1 
ATOM   1199 N N      . LEU   A 1 158 ? 10.53718  -5.65804  -16.91694 1.000 37.77872  ? 151 LEU   A N      1 
ATOM   1200 C CA     . LEU   A 1 158 ? 10.64301  -4.41486  -17.67051 1.000 34.20364  ? 151 LEU   A CA     1 
ATOM   1201 C C      . LEU   A 1 158 ? 11.02987  -4.69127  -19.11826 1.000 37.41562  ? 151 LEU   A C      1 
ATOM   1202 O O      . LEU   A 1 158 ? 11.96998  -5.44307  -19.39105 1.000 34.95479  ? 151 LEU   A O      1 
ATOM   1203 C CB     . LEU   A 1 158 ? 11.67074  -3.48926  -17.01954 1.000 32.45050  ? 151 LEU   A CB     1 
ATOM   1204 C CG     . LEU   A 1 158 ? 11.17542  -2.54656  -15.92094 1.000 40.02762  ? 151 LEU   A CG     1 
ATOM   1205 C CD1    . LEU   A 1 158 ? 12.25224  -1.53000  -15.56864 1.000 30.92785  ? 151 LEU   A CD1    1 
ATOM   1206 C CD2    . LEU   A 1 158 ? 9.88917   -1.84783  -16.33903 1.000 39.84734  ? 151 LEU   A CD2    1 
ATOM   1207 N N      . LYS   A 1 159 ? 10.30581  -4.07263  -20.04467 1.000 36.94197  ? 152 LYS   A N      1 
ATOM   1208 C CA     . LYS   A 1 159 ? 10.55900  -4.23917  -21.46950 1.000 29.46483  ? 152 LYS   A CA     1 
ATOM   1209 C C      . LYS   A 1 159 ? 9.89085   -3.08773  -22.20594 1.000 32.65904  ? 152 LYS   A C      1 
ATOM   1210 O O      . LYS   A 1 159 ? 9.12670   -2.31789  -21.60810 1.000 34.32304  ? 152 LYS   A O      1 
ATOM   1211 C CB     . LYS   A 1 159 ? 10.04243  -5.59628  -21.97641 1.000 30.20546  ? 152 LYS   A CB     1 
ATOM   1212 C CG     . LYS   A 1 159 ? 8.55786   -5.62105  -22.28767 1.000 35.07347  ? 152 LYS   A CG     1 
ATOM   1213 C CD     . LYS   A 1 159 ? 8.12499   -6.98994  -22.78545 1.000 48.62614  ? 152 LYS   A CD     1 
ATOM   1214 C CE     . LYS   A 1 159 ? 7.85742   -7.93882  -21.62981 1.000 37.46671  ? 152 LYS   A CE     1 
ATOM   1215 N NZ     . LYS   A 1 159 ? 6.75713   -7.44639  -20.75494 1.000 39.20106  ? 152 LYS   A NZ     1 
ATOM   1216 N N      . PRO   A 1 160 ? 10.15580  -2.94082  -23.50775 1.000 37.23186  ? 153 PRO   A N      1 
ATOM   1217 C CA     . PRO   A 1 160 ? 9.62485   -1.76989  -24.22899 1.000 37.41817  ? 153 PRO   A CA     1 
ATOM   1218 C C      . PRO   A 1 160 ? 8.11307   -1.62774  -24.15353 1.000 33.89539  ? 153 PRO   A C      1 
ATOM   1219 O O      . PRO   A 1 160 ? 7.61492   -0.50833  -23.98143 1.000 34.21415  ? 153 PRO   A O      1 
ATOM   1220 C CB     . PRO   A 1 160 ? 10.10749  -2.00670  -25.66686 1.000 39.34094  ? 153 PRO   A CB     1 
ATOM   1221 C CG     . PRO   A 1 160 ? 11.34001  -2.83760  -25.50926 1.000 37.18691  ? 153 PRO   A CG     1 
ATOM   1222 C CD     . PRO   A 1 160 ? 11.05108  -3.75105  -24.35170 1.000 37.63431  ? 153 PRO   A CD     1 
ATOM   1223 N N      . SER   A 1 161 ? 7.36143   -2.72441  -24.27848 1.000 33.71575  ? 154 SER   A N      1 
ATOM   1224 C CA     . SER   A 1 161 ? 5.90630   -2.61712  -24.24541 1.000 36.27297  ? 154 SER   A CA     1 
ATOM   1225 C C      . SER   A 1 161 ? 5.39320   -2.12211  -22.89876 1.000 31.28959  ? 154 SER   A C      1 
ATOM   1226 O O      . SER   A 1 161 ? 4.23484   -1.70092  -22.80704 1.000 34.16693  ? 154 SER   A O      1 
ATOM   1227 C CB     . SER   A 1 161 ? 5.26474   -3.96298  -24.59183 1.000 35.37759  ? 154 SER   A CB     1 
ATOM   1228 O OG     . SER   A 1 161 ? 5.70977   -4.98832  -23.72102 1.000 43.90618  ? 154 SER   A OG     1 
ATOM   1229 N N      . ASN   A 1 162 ? 6.22517   -2.15455  -21.85851 1.000 27.96566  ? 155 ASN   A N      1 
ATOM   1230 C CA     . ASN   A 1 162 ? 5.84277   -1.66410  -20.54006 1.000 33.18776  ? 155 ASN   A CA     1 
ATOM   1231 C C      . ASN   A 1 162 ? 5.99217   -0.15564  -20.39455 1.000 32.74640  ? 155 ASN   A C      1 
ATOM   1232 O O      . ASN   A 1 162 ? 5.64857   0.38348   -19.33679 1.000 26.63011  ? 155 ASN   A O      1 
ATOM   1233 C CB     . ASN   A 1 162 ? 6.67450   -2.35678  -19.45764 1.000 31.49789  ? 155 ASN   A CB     1 
ATOM   1234 C CG     . ASN   A 1 162 ? 6.26616   -3.79660  -19.24172 1.000 34.50142  ? 155 ASN   A CG     1 
ATOM   1235 O OD1    . ASN   A 1 162 ? 7.06015   -4.71416  -19.44341 1.000 38.70701  ? 155 ASN   A OD1    1 
ATOM   1236 N ND2    . ASN   A 1 162 ? 5.02149   -4.00368  -18.82717 1.000 31.00269  ? 155 ASN   A ND2    1 
ATOM   1237 N N      . LEU   A 1 163 ? 6.49721   0.53383   -21.41157 1.000 30.69728  ? 156 LEU   A N      1 
ATOM   1238 C CA     . LEU   A 1 163 ? 6.72251   1.97514   -21.35682 1.000 33.96346  ? 156 LEU   A CA     1 
ATOM   1239 C C      . LEU   A 1 163 ? 5.74608   2.65096   -22.31452 1.000 38.55531  ? 156 LEU   A C      1 
ATOM   1240 O O      . LEU   A 1 163 ? 5.95364   2.64982   -23.53135 1.000 38.11529  ? 156 LEU   A O      1 
ATOM   1241 C CB     . LEU   A 1 163 ? 8.17021   2.31634   -21.70230 1.000 32.78373  ? 156 LEU   A CB     1 
ATOM   1242 C CG     . LEU   A 1 163 ? 9.26956   1.81038   -20.76206 1.000 35.67727  ? 156 LEU   A CG     1 
ATOM   1243 C CD1    . LEU   A 1 163 ? 8.79649   1.78645   -19.31446 1.000 23.54282  ? 156 LEU   A CD1    1 
ATOM   1244 C CD2    . LEU   A 1 163 ? 9.76267   0.44001   -21.19233 1.000 36.78859  ? 156 LEU   A CD2    1 
ATOM   1245 N N      . ALA   A 1 164 ? 4.67927   3.22225   -21.76111 1.000 31.94056  ? 157 ALA   A N      1 
ATOM   1246 C CA     . ALA   A 1 164 ? 3.72515   3.99913   -22.53977 1.000 34.92327  ? 157 ALA   A CA     1 
ATOM   1247 C C      . ALA   A 1 164 ? 4.18393   5.45010   -22.59044 1.000 32.58489  ? 157 ALA   A C      1 
ATOM   1248 O O      . ALA   A 1 164 ? 4.56818   6.02275   -21.56514 1.000 24.73534  ? 157 ALA   A O      1 
ATOM   1249 C CB     . ALA   A 1 164 ? 2.32284   3.90306   -21.93809 1.000 32.92556  ? 157 ALA   A CB     1 
ATOM   1250 N N      . VAL   A 1 165 ? 4.14825   6.03862   -23.78238 1.000 29.39608  ? 158 VAL   A N      1 
ATOM   1251 C CA     . VAL   A 1 165 ? 4.62665   7.39712   -23.99144 1.000 37.30153  ? 158 VAL   A CA     1 
ATOM   1252 C C      . VAL   A 1 165 ? 3.61450   8.16484   -24.82701 1.000 34.57229  ? 158 VAL   A C      1 
ATOM   1253 O O      . VAL   A 1 165 ? 2.92401   7.60049   -25.68138 1.000 25.82235  ? 158 VAL   A O      1 
ATOM   1254 C CB     . VAL   A 1 165 ? 6.01362   7.41989   -24.67299 1.000 37.13182  ? 158 VAL   A CB     1 
ATOM   1255 C CG1    . VAL   A 1 165 ? 7.07304   6.84882   -23.74324 1.000 39.18577  ? 158 VAL   A CG1    1 
ATOM   1256 C CG2    . VAL   A 1 165 ? 5.97259   6.64914   -25.98371 1.000 37.61346  ? 158 VAL   A CG2    1 
ATOM   1257 N N      . ASN   A 1 166 ? 3.52373   9.46247   -24.56367 1.000 41.61436  ? 159 ASN   A N      1 
ATOM   1258 C CA     . ASN   A 1 166 ? 2.76294   10.37059  -25.40358 1.000 39.85880  ? 159 ASN   A CA     1 
ATOM   1259 C C      . ASN   A 1 166 ? 3.68659   11.00763  -26.43707 1.000 43.12596  ? 159 ASN   A C      1 
ATOM   1260 O O      . ASN   A 1 166 ? 4.91079   10.86743  -26.38636 1.000 43.11663  ? 159 ASN   A O      1 
ATOM   1261 C CB     . ASN   A 1 166 ? 2.08600   11.44995  -24.55738 1.000 38.49052  ? 159 ASN   A CB     1 
ATOM   1262 C CG     . ASN   A 1 166 ? 1.02126   10.88893  -23.63684 1.000 44.75863  ? 159 ASN   A CG     1 
ATOM   1263 O OD1    . ASN   A 1 166 ? 0.45863   9.82550   -23.89528 1.000 48.54724  ? 159 ASN   A OD1    1 
ATOM   1264 N ND2    . ASN   A 1 166 ? 0.73761   11.60473  -22.55422 1.000 42.26561  ? 159 ASN   A ND2    1 
ATOM   1265 N N      . GLU   A 1 167 ? 3.08584   11.71642  -27.39362 1.000 39.73039  ? 160 GLU   A N      1 
ATOM   1266 C CA     . GLU   A 1 167 ? 3.89827   12.50279  -28.31142 1.000 44.28977  ? 160 GLU   A CA     1 
ATOM   1267 C C      . GLU   A 1 167 ? 4.63991   13.61366  -27.58192 1.000 42.09172  ? 160 GLU   A C      1 
ATOM   1268 O O      . GLU   A 1 167 ? 5.66579   14.09257  -28.07678 1.000 49.49014  ? 160 GLU   A O      1 
ATOM   1269 C CB     . GLU   A 1 167 ? 3.03188   13.07962  -29.43161 1.000 56.05086  ? 160 GLU   A CB     1 
ATOM   1270 C CG     . GLU   A 1 167 ? 3.14227   12.33412  -30.75914 1.000 66.96154  ? 160 GLU   A CG     1 
ATOM   1271 C CD     . GLU   A 1 167 ? 4.57883   12.04058  -31.16769 1.000 77.36397  ? 160 GLU   A CD     1 
ATOM   1272 O OE1    . GLU   A 1 167 ? 4.77455   11.27354  -32.13333 1.000 79.68991  ? 160 GLU   A OE1    1 
ATOM   1273 O OE2    . GLU   A 1 167 ? 5.51367   12.57378  -30.53314 1.000 80.56015  ? 160 GLU   A OE2    1 
ATOM   1274 N N      . ASP   A 1 168 ? 4.14497   14.02557  -26.41208 1.000 42.55679  ? 161 ASP   A N      1 
ATOM   1275 C CA     . ASP   A 1 168 ? 4.89839   14.92339  -25.54606 1.000 49.35484  ? 161 ASP   A CA     1 
ATOM   1276 C C      . ASP   A 1 168 ? 6.22335   14.31576  -25.11027 1.000 48.94405  ? 161 ASP   A C      1 
ATOM   1277 O O      . ASP   A 1 168 ? 7.10071   15.04379  -24.63167 1.000 32.22192  ? 161 ASP   A O      1 
ATOM   1278 C CB     . ASP   A 1 168 ? 4.06846   15.27455  -24.30865 1.000 44.55633  ? 161 ASP   A CB     1 
ATOM   1279 C CG     . ASP   A 1 168 ? 3.55952   16.69855  -24.33018 1.000 56.24231  ? 161 ASP   A CG     1 
ATOM   1280 O OD1    . ASP   A 1 168 ? 3.39775   17.25621  -25.43484 1.000 66.00927  ? 161 ASP   A OD1    1 
ATOM   1281 O OD2    . ASP   A 1 168 ? 3.32017   17.26029  -23.23982 1.000 71.29555  ? 161 ASP   A OD2    1 
ATOM   1282 N N      . CYS   A 1 169 ? 6.38196   13.00149  -25.26384 1.000 41.40126  ? 162 CYS   A N      1 
ATOM   1283 C CA     . CYS   A 1 169 ? 7.51292   12.21155  -24.78587 1.000 40.54412  ? 162 CYS   A CA     1 
ATOM   1284 C C      . CYS   A 1 169 ? 7.38530   11.92245  -23.29642 1.000 36.23665  ? 162 CYS   A C      1 
ATOM   1285 O O      . CYS   A 1 169 ? 8.35790   11.46877  -22.67403 1.000 39.27191  ? 162 CYS   A O      1 
ATOM   1286 C CB     . CYS   A 1 169 ? 8.86211   12.87942  -25.07230 1.000 43.81341  ? 162 CYS   A CB     1 
ATOM   1287 S SG     . CYS   A 1 169 ? 9.55373   12.47091  -26.69536 1.000 58.29991  ? 162 CYS   A SG     1 
ATOM   1288 N N      . GLU   A 1 170 ? 6.22014   12.16839  -22.70280 1.000 38.71109  ? 163 GLU   A N      1 
ATOM   1289 C CA     . GLU   A 1 170 ? 5.98696   11.81887  -21.30956 1.000 39.67958  ? 163 GLU   A CA     1 
ATOM   1290 C C      . GLU   A 1 170 ? 5.73428   10.32178  -21.18619 1.000 32.30508  ? 163 GLU   A C      1 
ATOM   1291 O O      . GLU   A 1 170 ? 4.99579   9.73375   -21.98185 1.000 26.70008  ? 163 GLU   A O      1 
ATOM   1292 C CB     . GLU   A 1 170 ? 4.80573   12.61278  -20.75098 1.000 33.37935  ? 163 GLU   A CB     1 
ATOM   1293 C CG     . GLU   A 1 170 ? 5.13545   14.07326  -20.47191 1.000 54.09174  ? 163 GLU   A CG     1 
ATOM   1294 C CD     . GLU   A 1 170 ? 3.90789   14.96106  -20.43698 1.000 64.36339  ? 163 GLU   A CD     1 
ATOM   1295 O OE1    . GLU   A 1 170 ? 3.84664   15.85404  -19.56722 1.000 68.36692  ? 163 GLU   A OE1    1 
ATOM   1296 O OE2    . GLU   A 1 170 ? 3.00576   14.76916  -21.27876 1.000 67.85972  ? 163 GLU   A OE2    1 
ATOM   1297 N N      . LEU   A 1 171 ? 6.35431   9.70624   -20.18262 1.000 25.67102  ? 164 LEU   A N      1 
ATOM   1298 C CA     . LEU   A 1 171 ? 6.40193   8.25688   -20.05989 1.000 24.70451  ? 164 LEU   A CA     1 
ATOM   1299 C C      . LEU   A 1 171 ? 5.78949   7.80509   -18.74172 1.000 24.40448  ? 164 LEU   A C      1 
ATOM   1300 O O      . LEU   A 1 171 ? 5.96702   8.45256   -17.70553 1.000 23.04592  ? 164 LEU   A O      1 
ATOM   1301 C CB     . LEU   A 1 171 ? 7.84655   7.75264   -20.16171 1.000 24.46634  ? 164 LEU   A CB     1 
ATOM   1302 C CG     . LEU   A 1 171 ? 8.10814   6.26994   -19.88631 1.000 30.40578  ? 164 LEU   A CG     1 
ATOM   1303 C CD1    . LEU   A 1 171 ? 9.30279   5.77971   -20.69264 1.000 25.47043  ? 164 LEU   A CD1    1 
ATOM   1304 C CD2    . LEU   A 1 171 ? 8.32377   6.02187   -18.40066 1.000 22.51139  ? 164 LEU   A CD2    1 
ATOM   1305 N N      . LYS   A 1 172 ? 5.07352   6.68509   -18.79102 1.000 26.49316  ? 165 LYS   A N      1 
ATOM   1306 C CA     . LYS   A 1 172 ? 4.56287   6.01245   -17.60626 1.000 26.69118  ? 165 LYS   A CA     1 
ATOM   1307 C C      . LYS   A 1 172 ? 4.94249   4.54288   -17.67927 1.000 26.65996  ? 165 LYS   A C      1 
ATOM   1308 O O      . LYS   A 1 172 ? 4.89059   3.93478   -18.75198 1.000 24.60440  ? 165 LYS   A O      1 
ATOM   1309 C CB     . LYS   A 1 172 ? 3.03982   6.14633   -17.48421 1.000 27.47237  ? 165 LYS   A CB     1 
ATOM   1310 C CG     . LYS   A 1 172 ? 2.56621   7.48576   -16.95414 1.000 27.91287  ? 165 LYS   A CG     1 
ATOM   1311 C CD     . LYS   A 1 172 ? 1.21464   7.85530   -17.54023 1.000 39.11098  ? 165 LYS   A CD     1 
ATOM   1312 C CE     . LYS   A 1 172 ? 0.48724   8.84321   -16.65070 1.000 39.50447  ? 165 LYS   A CE     1 
ATOM   1313 N NZ     . LYS   A 1 172 ? 1.39023   9.94583   -16.22767 1.000 35.65166  ? 165 LYS   A NZ     1 
ATOM   1314 N N      . ILE   A 1 173 ? 5.32691   3.97750   -16.54174 1.000 28.68717  ? 166 ILE   A N      1 
ATOM   1315 C CA     . ILE   A 1 173 ? 5.63620   2.55622   -16.45787 1.000 24.54174  ? 166 ILE   A CA     1 
ATOM   1316 C C      . ILE   A 1 173 ? 4.34226   1.79246   -16.22522 1.000 27.53422  ? 166 ILE   A C      1 
ATOM   1317 O O      . ILE   A 1 173 ? 3.57745   2.10998   -15.30638 1.000 27.18024  ? 166 ILE   A O      1 
ATOM   1318 C CB     . ILE   A 1 173 ? 6.65421   2.27315   -15.34130 1.000 24.12901  ? 166 ILE   A CB     1 
ATOM   1319 C CG1    . ILE   A 1 173 ? 7.96510   3.01170   -15.61453 1.000 21.44876  ? 166 ILE   A CG1    1 
ATOM   1320 C CG2    . ILE   A 1 173 ? 6.90068   0.77189   -15.22012 1.000 21.05234  ? 166 ILE   A CG2    1 
ATOM   1321 C CD1    . ILE   A 1 173 ? 8.95280   2.94235   -14.47115 1.000 26.24209  ? 166 ILE   A CD1    1 
ATOM   1322 N N      . LEU   A 1 174 ? 4.09279   0.79109   -17.06236 1.000 24.42949  ? 167 LEU   A N      1 
ATOM   1323 C CA     . LEU   A 1 174 ? 2.92176   -0.06330  -16.94281 1.000 24.50670  ? 167 LEU   A CA     1 
ATOM   1324 C C      . LEU   A 1 174 ? 3.29524   -1.35251  -16.22363 1.000 32.14187  ? 167 LEU   A C      1 
ATOM   1325 O O      . LEU   A 1 174 ? 4.39767   -1.88040  -16.40412 1.000 24.27377  ? 167 LEU   A O      1 
ATOM   1326 C CB     . LEU   A 1 174 ? 2.34025   -0.39358  -18.31922 1.000 28.10510  ? 167 LEU   A CB     1 
ATOM   1327 C CG     . LEU   A 1 174 ? 1.83173   0.75593   -19.19016 1.000 30.64146  ? 167 LEU   A CG     1 
ATOM   1328 C CD1    . LEU   A 1 174 ? 1.38023   0.22278   -20.54050 1.000 31.59447  ? 167 LEU   A CD1    1 
ATOM   1329 C CD2    . LEU   A 1 174 ? 0.70029   1.50294   -18.50017 1.000 29.10814  ? 167 LEU   A CD2    1 
ATOM   1330 N N      . ASP   A 1 175 ? 2.37270   -1.85730  -15.40156 1.000 21.01760  ? 168 ASP   A N      1 
ATOM   1331 C CA     . ASP   A 1 175 ? 2.59679   -3.15954  -14.78299 1.000 30.64671  ? 168 ASP   A CA     1 
ATOM   1332 C C      . ASP   A 1 175 ? 2.56853   -4.26691  -15.82886 1.000 28.19179  ? 168 ASP   A C      1 
ATOM   1333 O O      . ASP   A 1 175 ? 3.40702   -5.17530  -15.80366 1.000 26.17388  ? 168 ASP   A O      1 
ATOM   1334 C CB     . ASP   A 1 175 ? 1.56205   -3.41285  -13.68349 1.000 29.26151  ? 168 ASP   A CB     1 
ATOM   1335 C CG     . ASP   A 1 175 ? 0.14845   -3.53915  -14.22184 1.000 36.90872  ? 168 ASP   A CG     1 
ATOM   1336 O OD1    . ASP   A 1 175 ? -0.16401  -2.89835  -15.24720 1.000 29.91926  ? 168 ASP   A OD1    1 
ATOM   1337 O OD2    . ASP   A 1 175 ? -0.65342  -4.27768  -13.61366 1.000 38.27017  ? 168 ASP   A OD2    1 
ATOM   1338 N N      . PHE   A 1 176 ? 1.62487   -4.19522  -16.76576 1.000 26.45748  ? 169 PHE   A N      1 
ATOM   1339 C CA     . PHE   A 1 176 ? 1.53049   -5.14497  -17.86814 1.000 32.17443  ? 169 PHE   A CA     1 
ATOM   1340 C C      . PHE   A 1 176 ? 1.19180   -4.37390  -19.13300 1.000 30.34821  ? 169 PHE   A C      1 
ATOM   1341 O O      . PHE   A 1 176 ? 0.17579   -3.67384  -19.17912 1.000 33.98274  ? 169 PHE   A O      1 
ATOM   1342 C CB     . PHE   A 1 176 ? 0.47072   -6.21738  -17.59477 1.000 31.99446  ? 169 PHE   A CB     1 
ATOM   1343 C CG     . PHE   A 1 176 ? 0.79177   -7.10663  -16.42842 1.000 32.37773  ? 169 PHE   A CG     1 
ATOM   1344 C CD1    . PHE   A 1 176 ? 1.73508   -8.11404  -16.54646 1.000 35.36784  ? 169 PHE   A CD1    1 
ATOM   1345 C CD2    . PHE   A 1 176 ? 0.14674   -6.93845  -15.21478 1.000 39.20406  ? 169 PHE   A CD2    1 
ATOM   1346 C CE1    . PHE   A 1 176 ? 2.03027   -8.93557  -15.47495 1.000 39.12898  ? 169 PHE   A CE1    1 
ATOM   1347 C CE2    . PHE   A 1 176 ? 0.43786   -7.75684  -14.13944 1.000 48.26386  ? 169 PHE   A CE2    1 
ATOM   1348 C CZ     . PHE   A 1 176 ? 1.38076   -8.75651  -14.27001 1.000 34.37610  ? 169 PHE   A CZ     1 
ATOM   1349 N N      . GLY   A 1 177 ? 2.04136   -4.49807  -20.15384 1.000 35.66108  ? 170 GLY   A N      1 
ATOM   1350 C CA     . GLY   A 1 177 ? 1.81877   -3.82674  -21.41553 1.000 36.39119  ? 170 GLY   A CA     1 
ATOM   1351 C C      . GLY   A 1 177 ? 0.91793   -4.62138  -22.34421 1.000 38.46538  ? 170 GLY   A C      1 
ATOM   1352 O O      . GLY   A 1 177 ? 0.47190   -5.72707  -22.04172 1.000 43.59669  ? 170 GLY   A O      1 
ATOM   1353 N N      . LEU   A 1 178 ? 0.64994   -4.02943  -23.50450 1.000 37.47936  ? 171 LEU   A N      1 
ATOM   1354 C CA     . LEU   A 1 178 ? -0.18599  -4.67448  -24.50645 1.000 44.08532  ? 171 LEU   A CA     1 
ATOM   1355 C C      . LEU   A 1 178 ? 0.64751   -5.63500  -25.34400 1.000 46.50075  ? 171 LEU   A C      1 
ATOM   1356 O O      . LEU   A 1 178 ? 1.66777   -5.24585  -25.92156 1.000 43.06372  ? 171 LEU   A O      1 
ATOM   1357 C CB     . LEU   A 1 178 ? -0.84804  -3.63193  -25.40639 1.000 46.00172  ? 171 LEU   A CB     1 
ATOM   1358 C CG     . LEU   A 1 178 ? -1.74911  -2.59610  -24.73267 1.000 45.08505  ? 171 LEU   A CG     1 
ATOM   1359 C CD1    . LEU   A 1 178 ? -2.07507  -1.47032  -25.70141 1.000 45.54150  ? 171 LEU   A CD1    1 
ATOM   1360 C CD2    . LEU   A 1 178 ? -3.02205  -3.24362  -24.20946 1.000 35.19074  ? 171 LEU   A CD2    1 
ATOM   1361 N N      . ALA   A 1 179 ? 0.21476   -6.89243  -25.40345 1.000 45.84697  ? 172 ALA   A N      1 
ATOM   1362 C CA     . ALA   A 1 179 ? 0.84396   -7.87258  -26.27757 1.000 50.61575  ? 172 ALA   A CA     1 
ATOM   1363 C C      . ALA   A 1 179 ? 0.33928   -7.78716  -27.71099 1.000 49.98373  ? 172 ALA   A C      1 
ATOM   1364 O O      . ALA   A 1 179 ? 0.80980   -8.55194  -28.55974 1.000 57.97729  ? 172 ALA   A O      1 
ATOM   1365 C CB     . ALA   A 1 179 ? 0.62139   -9.28731  -25.73508 1.000 46.05277  ? 172 ALA   A CB     1 
ATOM   1366 N N      . ARG   A 1 180 ? -0.59303  -6.87928  -27.99393 1.000 59.72711  ? 173 ARG   A N      1 
ATOM   1367 C CA     . ARG   A 1 180 ? -1.17929  -6.72552  -29.32355 1.000 52.08479  ? 173 ARG   A CA     1 
ATOM   1368 C C      . ARG   A 1 180 ? -0.14080  -6.82986  -30.43513 1.000 65.84454  ? 173 ARG   A C      1 
ATOM   1369 O O      . ARG   A 1 180 ? -0.21945  -7.71336  -31.28897 1.000 66.50529  ? 173 ARG   A O      1 
ATOM   1370 C CB     . ARG   A 1 180 ? -1.90859  -5.38411  -29.42811 1.000 43.27677  ? 173 ARG   A CB     1 
ATOM   1371 C CG     . ARG   A 1 180 ? -2.08620  -4.89604  -30.85610 1.000 57.93718  ? 173 ARG   A CG     1 
ATOM   1372 C CD     . ARG   A 1 180 ? -3.02870  -3.70707  -30.93019 1.000 64.07175  ? 173 ARG   A CD     1 
ATOM   1373 N NE     . ARG   A 1 180 ? -3.59200  -3.54706  -32.26549 1.000 64.20228  ? 173 ARG   A NE     1 
ATOM   1374 C CZ     . ARG   A 1 180 ? -4.70576  -4.13343  -32.68346 1.000 66.86377  ? 173 ARG   A CZ     1 
ATOM   1375 N NH1    . ARG   A 1 180 ? -5.16118  -3.95621  -33.91305 1.000 67.90564  ? 173 ARG   A NH1    1 
ATOM   1376 N NH2    . ARG   A 1 180 ? -5.37976  -4.91776  -31.84680 1.000 71.49492  ? 173 ARG   A NH2    1 
ATOM   1377 N N      . VAL   A 1 190 ? 9.13333   -9.25903  -29.51162 1.000 56.61629  ? 183 VAL   A N      1 
ATOM   1378 C CA     . VAL   A 1 190 ? 9.85491   -8.94289  -28.28501 1.000 71.50001  ? 183 VAL   A CA     1 
ATOM   1379 C C      . VAL   A 1 190 ? 9.68757   -10.07662 -27.28115 1.000 73.60225  ? 183 VAL   A C      1 
ATOM   1380 O O      . VAL   A 1 190 ? 8.64446   -10.20827 -26.64375 1.000 79.63425  ? 183 VAL   A O      1 
ATOM   1381 C CB     . VAL   A 1 190 ? 9.38301   -7.60784  -27.69163 1.000 69.74570  ? 183 VAL   A CB     1 
ATOM   1382 C CG1    . VAL   A 1 190 ? 9.96662   -7.41007  -26.30237 1.000 65.39183  ? 183 VAL   A CG1    1 
ATOM   1383 C CG2    . VAL   A 1 190 ? 9.77042   -6.45785  -28.60895 1.000 60.09498  ? 183 VAL   A CG2    1 
ATOM   1384 N N      . ALA   A 1 191 ? 10.73257  -10.89197 -27.13963 1.000 64.68486  ? 184 ALA   A N      1 
ATOM   1385 C CA     . ALA   A 1 191 ? 10.64873  -12.11484 -26.35059 1.000 81.92409  ? 184 ALA   A CA     1 
ATOM   1386 C C      . ALA   A 1 191 ? 10.67531  -11.87557 -24.84633 1.000 77.17600  ? 184 ALA   A C      1 
ATOM   1387 O O      . ALA   A 1 191 ? 10.39895  -12.81419 -24.09097 1.000 90.76539  ? 184 ALA   A O      1 
ATOM   1388 C CB     . ALA   A 1 191 ? 11.78889  -13.06246 -26.73280 1.000 70.28362  ? 184 ALA   A CB     1 
ATOM   1389 N N      . THR   A 1 192 ? 10.99721  -10.66067 -24.39593 1.000 46.67269  ? 185 THR   A N      1 
ATOM   1390 C CA     . THR   A 1 192 ? 11.13630  -10.36403 -22.97298 1.000 48.12172  ? 185 THR   A CA     1 
ATOM   1391 C C      . THR   A 1 192 ? 12.47460  -10.87572 -22.45826 1.000 46.43277  ? 185 THR   A C      1 
ATOM   1392 O O      . THR   A 1 192 ? 13.14451  -10.20400 -21.66554 1.000 45.10015  ? 185 THR   A O      1 
ATOM   1393 C CB     . THR   A 1 192 ? 9.99247   -10.97924 -22.16213 1.000 58.10452  ? 185 THR   A CB     1 
ATOM   1394 O OG1    . THR   A 1 192 ? 8.73778   -10.65682 -22.77485 1.000 62.21077  ? 185 THR   A OG1    1 
ATOM   1395 C CG2    . THR   A 1 192 ? 10.01041  -10.45638 -20.73412 1.000 58.44198  ? 185 THR   A CG2    1 
ATOM   1396 N N      . ARG   A 1 193 ? 12.86510  -12.07170 -22.90816 1.000 51.74061  ? 186 ARG   A N      1 
ATOM   1397 C CA     . ARG   A 1 193 ? 14.16408  -12.62664 -22.54483 1.000 43.70930  ? 186 ARG   A CA     1 
ATOM   1398 C C      . ARG   A 1 193 ? 15.29743  -11.65900 -22.85312 1.000 40.77653  ? 186 ARG   A C      1 
ATOM   1399 O O      . ARG   A 1 193 ? 16.34127  -11.69475 -22.19336 1.000 36.42707  ? 186 ARG   A O      1 
ATOM   1400 C CB     . ARG   A 1 193 ? 14.38029  -13.95673 -23.27488 1.000 46.95097  ? 186 ARG   A CB     1 
ATOM   1401 C CG     . ARG   A 1 193 ? 14.97742  -13.82249 -24.67883 1.000 55.54730  ? 186 ARG   A CG     1 
ATOM   1402 C CD     . ARG   A 1 193 ? 15.20438  -15.18580 -25.31070 1.000 50.60578  ? 186 ARG   A CD     1 
ATOM   1403 N NE     . ARG   A 1 193 ? 14.81558  -15.22582 -26.71613 1.000 51.91293  ? 186 ARG   A NE     1 
ATOM   1404 C CZ     . ARG   A 1 193 ? 13.76204  -15.87863 -27.18736 1.000 62.42839  ? 186 ARG   A CZ     1 
ATOM   1405 N NH1    . ARG   A 1 193 ? 13.49753  -15.92047 -28.48339 1.000 61.80969  ? 186 ARG   A NH1    1 
ATOM   1406 N NH2    . ARG   A 1 193 ? 12.95510  -16.50708 -26.33761 1.000 67.73670  ? 186 ARG   A NH2    1 
ATOM   1407 N N      . TRP   A 1 194 ? 15.10547  -10.77524 -23.83442 1.000 41.47736  ? 187 TRP   A N      1 
ATOM   1408 C CA     . TRP   A 1 194 ? 16.16747  -9.86728  -24.24973 1.000 36.74320  ? 187 TRP   A CA     1 
ATOM   1409 C C      . TRP   A 1 194 ? 16.50119  -8.82077  -23.19176 1.000 36.55841  ? 187 TRP   A C      1 
ATOM   1410 O O      . TRP   A 1 194 ? 17.56048  -8.19092  -23.27863 1.000 42.63610  ? 187 TRP   A O      1 
ATOM   1411 C CB     . TRP   A 1 194 ? 15.77569  -9.18073  -25.56067 1.000 39.06944  ? 187 TRP   A CB     1 
ATOM   1412 C CG     . TRP   A 1 194 ? 15.49016  -10.14514 -26.67659 1.000 42.63132  ? 187 TRP   A CG     1 
ATOM   1413 C CD1    . TRP   A 1 194 ? 15.83420  -11.46468 -26.72572 1.000 46.79835  ? 187 TRP   A CD1    1 
ATOM   1414 C CD2    . TRP   A 1 194 ? 14.80293  -9.86512  -27.90332 1.000 39.52320  ? 187 TRP   A CD2    1 
ATOM   1415 N NE1    . TRP   A 1 194 ? 15.40399  -12.02392 -27.90398 1.000 44.62720  ? 187 TRP   A NE1    1 
ATOM   1416 C CE2    . TRP   A 1 194 ? 14.76853  -11.06322 -28.64527 1.000 45.22850  ? 187 TRP   A CE2    1 
ATOM   1417 C CE3    . TRP   A 1 194 ? 14.21455  -8.71919  -28.44612 1.000 39.11022  ? 187 TRP   A CE3    1 
ATOM   1418 C CZ2    . TRP   A 1 194 ? 14.16955  -11.14774 -29.90043 1.000 45.63005  ? 187 TRP   A CZ2    1 
ATOM   1419 C CZ3    . TRP   A 1 194 ? 13.61999  -8.80518  -29.69305 1.000 36.83903  ? 187 TRP   A CZ3    1 
ATOM   1420 C CH2    . TRP   A 1 194 ? 13.60197  -10.01030 -30.40569 1.000 50.63568  ? 187 TRP   A CH2    1 
ATOM   1421 N N      . TYR   A 1 195 ? 15.63833  -8.62615  -22.19324 1.000 37.99980  ? 188 TYR   A N      1 
ATOM   1422 C CA     . TYR   A 1 195 ? 15.82655  -7.57067  -21.20382 1.000 30.62254  ? 188 TYR   A CA     1 
ATOM   1423 C C      . TYR   A 1 195 ? 15.97570  -8.10106  -19.78247 1.000 38.20056  ? 188 TYR   A C      1 
ATOM   1424 O O      . TYR   A 1 195 ? 15.99161  -7.30485  -18.83587 1.000 30.97436  ? 188 TYR   A O      1 
ATOM   1425 C CB     . TYR   A 1 195 ? 14.66497  -6.57349  -21.27807 1.000 32.07605  ? 188 TYR   A CB     1 
ATOM   1426 C CG     . TYR   A 1 195 ? 14.38734  -6.10307  -22.68728 1.000 31.51863  ? 188 TYR   A CG     1 
ATOM   1427 C CD1    . TYR   A 1 195 ? 13.54264  -6.81901  -23.52537 1.000 28.97526  ? 188 TYR   A CD1    1 
ATOM   1428 C CD2    . TYR   A 1 195 ? 14.98874  -4.95655  -23.18777 1.000 30.89327  ? 188 TYR   A CD2    1 
ATOM   1429 C CE1    . TYR   A 1 195 ? 13.29620  -6.40013  -24.81795 1.000 28.23345  ? 188 TYR   A CE1    1 
ATOM   1430 C CE2    . TYR   A 1 195 ? 14.74802  -4.52945  -24.47925 1.000 35.23350  ? 188 TYR   A CE2    1 
ATOM   1431 C CZ     . TYR   A 1 195 ? 13.90099  -5.25506  -25.28977 1.000 36.76066  ? 188 TYR   A CZ     1 
ATOM   1432 O OH     . TYR   A 1 195 ? 13.65814  -4.83366  -26.57673 1.000 42.13620  ? 188 TYR   A OH     1 
ATOM   1433 N N      . ARG   A 1 196 ? 16.10407  -9.41396  -19.60580 1.000 35.56543  ? 189 ARG   A N      1 
ATOM   1434 C CA     . ARG   A 1 196 ? 16.17882  -10.01219 -18.28015 1.000 29.44631  ? 189 ARG   A CA     1 
ATOM   1435 C C      . ARG   A 1 196 ? 17.61902  -10.07349 -17.78831 1.000 33.69669  ? 189 ARG   A C      1 
ATOM   1436 O O      . ARG   A 1 196 ? 18.53126  -10.44019 -18.53589 1.000 30.89192  ? 189 ARG   A O      1 
ATOM   1437 C CB     . ARG   A 1 196 ? 15.57848  -11.41913 -18.28924 1.000 37.90746  ? 189 ARG   A CB     1 
ATOM   1438 C CG     . ARG   A 1 196 ? 14.06869  -11.45108 -18.45571 1.000 51.22484  ? 189 ARG   A CG     1 
ATOM   1439 C CD     . ARG   A 1 196 ? 13.39297  -12.14728 -17.28303 1.000 53.86988  ? 189 ARG   A CD     1 
ATOM   1440 N NE     . ARG   A 1 196 ? 11.96752  -11.84518 -17.22343 1.000 56.43407  ? 189 ARG   A NE     1 
ATOM   1441 C CZ     . ARG   A 1 196 ? 11.14206  -12.29616 -16.28843 1.000 53.92694  ? 189 ARG   A CZ     1 
ATOM   1442 N NH1    . ARG   A 1 196 ? 11.56723  -13.07582 -15.30768 1.000 47.83895  ? 189 ARG   A NH1    1 
ATOM   1443 N NH2    . ARG   A 1 196 ? 9.85717   -11.95591 -16.33849 1.000 57.25044  ? 189 ARG   A NH2    1 
ATOM   1444 N N      . ALA   A 1 197 ? 17.81369  -9.71807  -16.52021 1.000 29.59232  ? 190 ALA   A N      1 
ATOM   1445 C CA     . ALA   A 1 197 ? 19.12976  -9.82381  -15.91545 1.000 37.28240  ? 190 ALA   A CA     1 
ATOM   1446 C C      . ALA   A 1 197 ? 19.59417  -11.28011 -15.93111 1.000 38.28779  ? 190 ALA   A C      1 
ATOM   1447 O O      . ALA   A 1 197 ? 18.77454  -12.20331 -15.89844 1.000 33.12869  ? 190 ALA   A O      1 
ATOM   1448 C CB     . ALA   A 1 197 ? 19.10739  -9.29302  -14.48379 1.000 40.81410  ? 190 ALA   A CB     1 
ATOM   1449 N N      . PRO   A 1 198 ? 20.90737  -11.51572 -15.98345 1.000 37.32508  ? 191 PRO   A N      1 
ATOM   1450 C CA     . PRO   A 1 198 ? 21.38791  -12.90564 -16.06686 1.000 38.35254  ? 191 PRO   A CA     1 
ATOM   1451 C C      . PRO   A 1 198 ? 20.99673  -13.75481 -14.86980 1.000 47.39716  ? 191 PRO   A C      1 
ATOM   1452 O O      . PRO   A 1 198 ? 20.65124  -14.93048 -15.04234 1.000 41.47148  ? 191 PRO   A O      1 
ATOM   1453 C CB     . PRO   A 1 198 ? 22.91103  -12.74255 -16.18352 1.000 42.62045  ? 191 PRO   A CB     1 
ATOM   1454 C CG     . PRO   A 1 198 ? 23.19847  -11.37263 -15.65095 1.000 44.43068  ? 191 PRO   A CG     1 
ATOM   1455 C CD     . PRO   A 1 198 ? 22.00907  -10.53989 -16.00972 1.000 39.24304  ? 191 PRO   A CD     1 
ATOM   1456 N N      . GLU   A 1 199 ? 21.03838  -13.19521 -13.65729 1.000 40.76633  ? 192 GLU   A N      1 
ATOM   1457 C CA     . GLU   A 1 199 ? 20.69233  -13.97859 -12.47480 1.000 49.34017  ? 192 GLU   A CA     1 
ATOM   1458 C C      . GLU   A 1 199 ? 19.29882  -14.58252 -12.60038 1.000 47.28191  ? 192 GLU   A C      1 
ATOM   1459 O O      . GLU   A 1 199 ? 19.08074  -15.74228 -12.22916 1.000 52.16104  ? 192 GLU   A O      1 
ATOM   1460 C CB     . GLU   A 1 199 ? 20.79147  -13.11295 -11.21888 1.000 38.86011  ? 192 GLU   A CB     1 
ATOM   1461 C CG     . GLU   A 1 199 ? 19.92151  -11.86949 -11.24691 1.000 42.32100  ? 192 GLU   A CG     1 
ATOM   1462 C CD     . GLU   A 1 199 ? 20.67747  -10.64318 -11.71523 1.000 42.61772  ? 192 GLU   A CD     1 
ATOM   1463 O OE1    . GLU   A 1 199 ? 21.34961  -10.72360 -12.76359 1.000 37.04005  ? 192 GLU   A OE1    1 
ATOM   1464 O OE2    . GLU   A 1 199 ? 20.60305  -9.59964  -11.03293 1.000 48.66576  ? 192 GLU   A OE2    1 
ATOM   1465 N N      . ILE   A 1 200 ? 18.34271  -13.81242 -13.12330 1.000 40.43179  ? 193 ILE   A N      1 
ATOM   1466 C CA     . ILE   A 1 200 ? 16.99393  -14.33577 -13.32541 1.000 46.83672  ? 193 ILE   A CA     1 
ATOM   1467 C C      . ILE   A 1 200 ? 17.03765  -15.58328 -14.19771 1.000 50.11752  ? 193 ILE   A C      1 
ATOM   1468 O O      . ILE   A 1 200 ? 16.47669  -16.62923 -13.84899 1.000 48.85732  ? 193 ILE   A O      1 
ATOM   1469 C CB     . ILE   A 1 200 ? 16.08215  -13.25636 -13.93578 1.000 46.27119  ? 193 ILE   A CB     1 
ATOM   1470 C CG1    . ILE   A 1 200 ? 15.85639  -12.11611 -12.94140 1.000 44.40615  ? 193 ILE   A CG1    1 
ATOM   1471 C CG2    . ILE   A 1 200 ? 14.75679  -13.86387 -14.36863 1.000 40.63473  ? 193 ILE   A CG2    1 
ATOM   1472 C CD1    . ILE   A 1 200 ? 15.33347  -10.84694 -13.58119 1.000 40.67785  ? 193 ILE   A CD1    1 
ATOM   1473 N N      . MET   A 1 201 ? 17.70981  -15.49143 -15.34765 1.000 49.83161  ? 194 MET   A N      1 
ATOM   1474 C CA     . MET   A 1 201 ? 17.80215  -16.63420 -16.24778 1.000 52.95183  ? 194 MET   A CA     1 
ATOM   1475 C C      . MET   A 1 201 ? 18.58528  -17.78769 -15.63827 1.000 49.35608  ? 194 MET   A C      1 
ATOM   1476 O O      . MET   A 1 201 ? 18.43672  -18.92774 -16.09028 1.000 53.57329  ? 194 MET   A O      1 
ATOM   1477 C CB     . MET   A 1 201 ? 18.43389  -16.20948 -17.57171 1.000 54.36608  ? 194 MET   A CB     1 
ATOM   1478 C CG     . MET   A 1 201 ? 17.47959  -15.46889 -18.49042 1.000 39.15754  ? 194 MET   A CG     1 
ATOM   1479 S SD     . MET   A 1 201 ? 18.29571  -14.85901 -19.97477 1.000 56.22327  ? 194 MET   A SD     1 
ATOM   1480 C CE     . MET   A 1 201 ? 17.18871  -15.46824 -21.24248 1.000 56.62539  ? 194 MET   A CE     1 
ATOM   1481 N N      . LEU   A 1 202 ? 19.41896  -17.51971 -14.63419 1.000 49.47344  ? 195 LEU   A N      1 
ATOM   1482 C CA     . LEU   A 1 202 ? 20.03900  -18.58877 -13.86580 1.000 55.23168  ? 195 LEU   A CA     1 
ATOM   1483 C C      . LEU   A 1 202 ? 19.10986  -19.14793 -12.79873 1.000 54.08942  ? 195 LEU   A C      1 
ATOM   1484 O O      . LEU   A 1 202 ? 19.46324  -20.13517 -12.14685 1.000 47.69314  ? 195 LEU   A O      1 
ATOM   1485 C CB     . LEU   A 1 202 ? 21.33164  -18.09256 -13.21211 1.000 57.33667  ? 195 LEU   A CB     1 
ATOM   1486 C CG     . LEU   A 1 202 ? 22.56367  -17.96364 -14.10986 1.000 48.76654  ? 195 LEU   A CG     1 
ATOM   1487 C CD1    . LEU   A 1 202 ? 23.73058  -17.38399 -13.32641 1.000 51.38247  ? 195 LEU   A CD1    1 
ATOM   1488 C CD2    . LEU   A 1 202 ? 22.93786  -19.30662 -14.71783 1.000 48.24195  ? 195 LEU   A CD2    1 
ATOM   1489 N N      . ASN   A 1 203 ? 17.93666  -18.54380 -12.60735 1.000 59.56847  ? 196 ASN   A N      1 
ATOM   1490 C CA     . ASN   A 1 203 ? 16.97708  -18.99032 -11.59974 1.000 54.23351  ? 196 ASN   A CA     1 
ATOM   1491 C C      . ASN   A 1 203 ? 17.52294  -18.79103 -10.18665 1.000 53.37591  ? 196 ASN   A C      1 
ATOM   1492 O O      . ASN   A 1 203 ? 17.29541  -19.61356 -9.29920  1.000 54.09191  ? 196 ASN   A O      1 
ATOM   1493 C CB     . ASN   A 1 203 ? 16.57603  -20.45012 -11.82388 1.000 55.24386  ? 196 ASN   A CB     1 
ATOM   1494 C CG     . ASN   A 1 203 ? 15.19279  -20.76148 -11.29069 1.000 53.32335  ? 196 ASN   A CG     1 
ATOM   1495 O OD1    . ASN   A 1 203 ? 15.04292  -21.48358 -10.30569 1.000 60.39715  ? 196 ASN   A OD1    1 
ATOM   1496 N ND2    . ASN   A 1 203 ? 14.17108  -20.21538 -11.94099 1.000 55.76359  ? 196 ASN   A ND2    1 
ATOM   1497 N N      . TRP   A 1 204 ? 18.24667  -17.68741 -9.97667  1.000 56.43096  ? 197 TRP   A N      1 
ATOM   1498 C CA     . TRP   A 1 204 ? 18.81074  -17.40876 -8.65939  1.000 52.79818  ? 197 TRP   A CA     1 
ATOM   1499 C C      . TRP   A 1 204 ? 17.73530  -17.41318 -7.57837  1.000 55.09845  ? 197 TRP   A C      1 
ATOM   1500 O O      . TRP   A 1 204 ? 18.00831  -17.78271 -6.43073  1.000 56.14485  ? 197 TRP   A O      1 
ATOM   1501 C CB     . TRP   A 1 204 ? 19.55199  -16.07003 -8.68306  1.000 49.99313  ? 197 TRP   A CB     1 
ATOM   1502 C CG     . TRP   A 1 204 ? 20.85517  -16.07761 -7.93321  1.000 45.97939  ? 197 TRP   A CG     1 
ATOM   1503 C CD1    . TRP   A 1 204 ? 21.02182  -16.18757 -6.58374  1.000 50.85104  ? 197 TRP   A CD1    1 
ATOM   1504 C CD2    . TRP   A 1 204 ? 22.17251  -15.96336 -8.49114  1.000 46.73202  ? 197 TRP   A CD2    1 
ATOM   1505 N NE1    . TRP   A 1 204 ? 22.35798  -16.15084 -6.26585  1.000 49.85014  ? 197 TRP   A NE1    1 
ATOM   1506 C CE2    . TRP   A 1 204 ? 23.08544  -16.01419 -7.41850  1.000 49.35245  ? 197 TRP   A CE2    1 
ATOM   1507 C CE3    . TRP   A 1 204 ? 22.66789  -15.82512 -9.79183  1.000 46.00085  ? 197 TRP   A CE3    1 
ATOM   1508 C CZ2    . TRP   A 1 204 ? 24.46404  -15.93104 -7.60553  1.000 51.21488  ? 197 TRP   A CZ2    1 
ATOM   1509 C CZ3    . TRP   A 1 204 ? 24.03875  -15.74325 -9.97519  1.000 47.83240  ? 197 TRP   A CZ3    1 
ATOM   1510 C CH2    . TRP   A 1 204 ? 24.91963  -15.79638 -8.88779  1.000 50.38876  ? 197 TRP   A CH2    1 
ATOM   1511 N N      . MET   A 1 205 ? 16.51417  -16.99932 -7.92254  1.000 60.51204  ? 198 MET   A N      1 
ATOM   1512 C CA     . MET   A 1 205 ? 15.33343  -17.15980 -7.07184  1.000 64.95520  ? 198 MET   A CA     1 
ATOM   1513 C C      . MET   A 1 205 ? 15.33024  -16.21524 -5.87254  1.000 67.25194  ? 198 MET   A C      1 
ATOM   1514 O O      . MET   A 1 205 ? 14.71932  -16.51141 -4.84290  1.000 76.88373  ? 198 MET   A O      1 
ATOM   1515 C CB     . MET   A 1 205 ? 15.17722  -18.60705 -6.59816  1.000 68.16775  ? 198 MET   A CB     1 
ATOM   1516 C CG     . MET   A 1 205 ? 13.72750  -19.02355 -6.42526  1.000 62.66054  ? 198 MET   A CG     1 
ATOM   1517 S SD     . MET   A 1 205 ? 12.68371  -18.42514 -7.77204  1.000 87.25226  ? 198 MET   A SD     1 
ATOM   1518 C CE     . MET   A 1 205 ? 12.16063  -16.83327 -7.13337  1.000 67.06255  ? 198 MET   A CE     1 
ATOM   1519 N N      . HIS   A 1 206 ? 16.00569  -15.07696 -5.99302  1.000 56.40303  ? 199 HIS   A N      1 
ATOM   1520 C CA     . HIS   A 1 206 ? 15.90924  -14.00552 -5.00909  1.000 60.55119  ? 199 HIS   A CA     1 
ATOM   1521 C C      . HIS   A 1 206 ? 16.71393  -12.82395 -5.53139  1.000 62.72215  ? 199 HIS   A C      1 
ATOM   1522 O O      . HIS   A 1 206 ? 17.94940  -12.84090 -5.51421  1.000 57.04601  ? 199 HIS   A O      1 
ATOM   1523 C CB     . HIS   A 1 206 ? 16.40111  -14.45527 -3.62999  1.000 57.96150  ? 199 HIS   A CB     1 
ATOM   1524 C CG     . HIS   A 1 206 ? 17.84790  -14.82762 -3.60114  1.000 68.06313  ? 199 HIS   A CG     1 
ATOM   1525 N ND1    . HIS   A 1 206 ? 18.85338  -13.88629 -3.63500  1.000 76.35337  ? 199 HIS   A ND1    1 
ATOM   1526 C CD2    . HIS   A 1 206 ? 18.46097  -16.03336 -3.55272  1.000 64.30142  ? 199 HIS   A CD2    1 
ATOM   1527 C CE1    . HIS   A 1 206 ? 20.02426  -14.49592 -3.61297  1.000 75.72358  ? 199 HIS   A CE1    1 
ATOM   1528 N NE2    . HIS   A 1 206 ? 19.81461  -15.79899 -3.55623  1.000 72.31572  ? 199 HIS   A NE2    1 
ATOM   1529 N N      . TYR   A 1 207 ? 16.02404  -11.80004 -6.01465  1.000 39.60053  ? 200 TYR   A N      1 
ATOM   1530 C CA     . TYR   A 1 207 ? 16.63263  -10.80515 -6.87890  1.000 38.03104  ? 200 TYR   A CA     1 
ATOM   1531 C C      . TYR   A 1 207 ? 16.72227  -9.45331  -6.18914  1.000 41.72315  ? 200 TYR   A C      1 
ATOM   1532 O O      . TYR   A 1 207 ? 15.83951  -9.07408  -5.41270  1.000 39.06479  ? 200 TYR   A O      1 
ATOM   1533 C CB     . TYR   A 1 207 ? 15.84359  -10.69273 -8.18396  1.000 48.11360  ? 200 TYR   A CB     1 
ATOM   1534 C CG     . TYR   A 1 207 ? 15.67872  -12.03326 -8.86124  1.000 49.50030  ? 200 TYR   A CG     1 
ATOM   1535 C CD1    . TYR   A 1 207 ? 16.77628  -12.69951 -9.38971  1.000 45.34549  ? 200 TYR   A CD1    1 
ATOM   1536 C CD2    . TYR   A 1 207 ? 14.43574  -12.64727 -8.94699  1.000 48.64106  ? 200 TYR   A CD2    1 
ATOM   1537 C CE1    . TYR   A 1 207 ? 16.64120  -13.93069 -9.99962  1.000 48.84787  ? 200 TYR   A CE1    1 
ATOM   1538 C CE2    . TYR   A 1 207 ? 14.29038  -13.88196 -9.55686  1.000 54.24194  ? 200 TYR   A CE2    1 
ATOM   1539 C CZ     . TYR   A 1 207 ? 15.39795  -14.51793 -10.08118 1.000 54.06425  ? 200 TYR   A CZ     1 
ATOM   1540 O OH     . TYR   A 1 207 ? 15.26511  -15.74464 -10.68973 1.000 45.21065  ? 200 TYR   A OH     1 
ATOM   1541 N N      . ASN   A 1 208 ? 17.81531  -8.75043  -6.46360  1.000 35.68125  ? 201 ASN   A N      1 
ATOM   1542 C CA     . ASN   A 1 208 ? 17.96081  -7.36160  -6.07403  1.000 35.28248  ? 201 ASN   A CA     1 
ATOM   1543 C C      . ASN   A 1 208 ? 17.02036  -6.49228  -6.90312  1.000 32.67142  ? 201 ASN   A C      1 
ATOM   1544 O O      . ASN   A 1 208 ? 16.54763  -6.88633  -7.97337  1.000 31.26014  ? 201 ASN   A O      1 
ATOM   1545 C CB     . ASN   A 1 208 ? 19.41367  -6.91748  -6.26586  1.000 42.22238  ? 201 ASN   A CB     1 
ATOM   1546 C CG     . ASN   A 1 208 ? 19.69171  -5.53900  -5.70151  1.000 43.09014  ? 201 ASN   A CG     1 
ATOM   1547 O OD1    . ASN   A 1 208 ? 19.00566  -4.57061  -6.02526  1.000 47.60536  ? 201 ASN   A OD1    1 
ATOM   1548 N ND2    . ASN   A 1 208 ? 20.71648  -5.44194  -4.86086  1.000 50.53207  ? 201 ASN   A ND2    1 
ATOM   1549 N N      . GLN   A 1 209 ? 16.73622  -5.29474  -6.38889  1.000 34.78339  ? 202 GLN   A N      1 
ATOM   1550 C CA     . GLN   A 1 209 ? 15.99968  -4.32663  -7.19257  1.000 34.17772  ? 202 GLN   A CA     1 
ATOM   1551 C C      . GLN   A 1 209 ? 16.74451  -4.00503  -8.48119  1.000 32.77604  ? 202 GLN   A C      1 
ATOM   1552 O O      . GLN   A 1 209 ? 16.11978  -3.67017  -9.49396  1.000 27.63833  ? 202 GLN   A O      1 
ATOM   1553 C CB     . GLN   A 1 209 ? 15.74969  -3.05028  -6.38884  1.000 34.92947  ? 202 GLN   A CB     1 
ATOM   1554 C CG     . GLN   A 1 209 ? 15.12938  -3.28724  -5.02128  1.000 43.37547  ? 202 GLN   A CG     1 
ATOM   1555 C CD     . GLN   A 1 209 ? 14.79338  -1.99517  -4.30140  1.000 45.87536  ? 202 GLN   A CD     1 
ATOM   1556 O OE1    . GLN   A 1 209 ? 15.56723  -1.03794  -4.32622  1.000 41.88620  ? 202 GLN   A OE1    1 
ATOM   1557 N NE2    . GLN   A 1 209 ? 13.63322  -1.96163  -3.65513  1.000 44.20492  ? 202 GLN   A NE2    1 
ATOM   1558 N N      . THR   A 1 210 ? 18.07528  -4.12153  -8.46894  1.000 33.23183  ? 203 THR   A N      1 
ATOM   1559 C CA     . THR   A 1 210 ? 18.88569  -3.78230  -9.63219  1.000 34.41395  ? 203 THR   A CA     1 
ATOM   1560 C C      . THR   A 1 210 ? 18.63184  -4.69319  -10.82657 1.000 34.15010  ? 203 THR   A C      1 
ATOM   1561 O O      . THR   A 1 210 ? 19.18522  -4.43632  -11.90119 1.000 33.32647  ? 203 THR   A O      1 
ATOM   1562 C CB     . THR   A 1 210 ? 20.37168  -3.81468  -9.26803  1.000 33.96584  ? 203 THR   A CB     1 
ATOM   1563 O OG1    . THR   A 1 210 ? 20.69375  -5.07447  -8.66448  1.000 42.86793  ? 203 THR   A OG1    1 
ATOM   1564 C CG2    . THR   A 1 210 ? 20.70413  -2.69049  -8.29727  1.000 36.97939  ? 203 THR   A CG2    1 
ATOM   1565 N N      . VAL   A 1 211 ? 17.82573  -5.74672  -10.67393 1.000 32.40476  ? 204 VAL   A N      1 
ATOM   1566 C CA     . VAL   A 1 211 ? 17.41172  -6.51843  -11.84248 1.000 30.64995  ? 204 VAL   A CA     1 
ATOM   1567 C C      . VAL   A 1 211 ? 16.67551  -5.62020  -12.82718 1.000 27.88899  ? 204 VAL   A C      1 
ATOM   1568 O O      . VAL   A 1 211 ? 16.81152  -5.76725  -14.04815 1.000 29.26389  ? 204 VAL   A O      1 
ATOM   1569 C CB     . VAL   A 1 211 ? 16.55206  -7.72576  -11.42175 1.000 35.55987  ? 204 VAL   A CB     1 
ATOM   1570 C CG1    . VAL   A 1 211 ? 17.28908  -8.57369  -10.39756 1.000 31.28187  ? 204 VAL   A CG1    1 
ATOM   1571 C CG2    . VAL   A 1 211 ? 15.20609  -7.26353  -10.87991 1.000 27.67826  ? 204 VAL   A CG2    1 
ATOM   1572 N N      . ASP   A 1 212 ? 15.88764  -4.67090  -12.31232 1.000 25.82813  ? 205 ASP   A N      1 
ATOM   1573 C CA     . ASP   A 1 212 ? 15.23164  -3.70114  -13.18295 1.000 25.02516  ? 205 ASP   A CA     1 
ATOM   1574 C C      . ASP   A 1 212 ? 16.23494  -2.73704  -13.80204 1.000 29.19412  ? 205 ASP   A C      1 
ATOM   1575 O O      . ASP   A 1 212 ? 16.04574  -2.29489  -14.94101 1.000 23.86713  ? 205 ASP   A O      1 
ATOM   1576 C CB     . ASP   A 1 212 ? 14.16861  -2.92251  -12.40663 1.000 28.44586  ? 205 ASP   A CB     1 
ATOM   1577 C CG     . ASP   A 1 212 ? 12.99630  -3.78946  -11.98517 1.000 28.98068  ? 205 ASP   A CG     1 
ATOM   1578 O OD1    . ASP   A 1 212 ? 12.71637  -4.79781  -12.66747 1.000 25.46436  ? 205 ASP   A OD1    1 
ATOM   1579 O OD2    . ASP   A 1 212 ? 12.35088  -3.45685  -10.96976 1.000 23.62795  ? 205 ASP   A OD2    1 
ATOM   1580 N N      . ILE   A 1 213 ? 17.29762  -2.39368  -13.06999 1.000 31.60221  ? 206 ILE   A N      1 
ATOM   1581 C CA     . ILE   A 1 213 ? 18.32949  -1.52205  -13.62474 1.000 28.73406  ? 206 ILE   A CA     1 
ATOM   1582 C C      . ILE   A 1 213 ? 18.98050  -2.17799  -14.83446 1.000 32.32773  ? 206 ILE   A C      1 
ATOM   1583 O O      . ILE   A 1 213 ? 19.28148  -1.51405  -15.83412 1.000 34.96862  ? 206 ILE   A O      1 
ATOM   1584 C CB     . ILE   A 1 213 ? 19.36831  -1.16515  -12.54558 1.000 32.61610  ? 206 ILE   A CB     1 
ATOM   1585 C CG1    . ILE   A 1 213 ? 18.72501  -0.32081  -11.44320 1.000 28.55064  ? 206 ILE   A CG1    1 
ATOM   1586 C CG2    . ILE   A 1 213 ? 20.54931  -0.43366  -13.16470 1.000 29.73965  ? 206 ILE   A CG2    1 
ATOM   1587 C CD1    . ILE   A 1 213 ? 18.30530  1.06124   -11.89593 1.000 31.78918  ? 206 ILE   A CD1    1 
ATOM   1588 N N      . TRP   A 1 214 ? 19.20993  -3.49089  -14.76444 1.000 30.43827  ? 207 TRP   A N      1 
ATOM   1589 C CA     . TRP   A 1 214 ? 19.73154  -4.21020  -15.92131 1.000 28.21403  ? 207 TRP   A CA     1 
ATOM   1590 C C      . TRP   A 1 214 ? 18.79037  -4.07599  -17.11168 1.000 31.63479  ? 207 TRP   A C      1 
ATOM   1591 O O      . TRP   A 1 214 ? 19.22463  -3.79420  -18.23481 1.000 27.20576  ? 207 TRP   A O      1 
ATOM   1592 C CB     . TRP   A 1 214 ? 19.95168  -5.68243  -15.57140 1.000 32.06711  ? 207 TRP   A CB     1 
ATOM   1593 C CG     . TRP   A 1 214 ? 20.43275  -6.49607  -16.73193 1.000 33.44602  ? 207 TRP   A CG     1 
ATOM   1594 C CD1    . TRP   A 1 214 ? 19.66720  -7.07371  -17.70348 1.000 29.50479  ? 207 TRP   A CD1    1 
ATOM   1595 C CD2    . TRP   A 1 214 ? 21.79245  -6.81702  -17.04884 1.000 37.86284  ? 207 TRP   A CD2    1 
ATOM   1596 N NE1    . TRP   A 1 214 ? 20.46548  -7.73555  -18.60407 1.000 31.35719  ? 207 TRP   A NE1    1 
ATOM   1597 C CE2    . TRP   A 1 214 ? 21.77477  -7.59357  -18.22462 1.000 37.44650  ? 207 TRP   A CE2    1 
ATOM   1598 C CE3    . TRP   A 1 214 ? 23.02249  -6.52469  -16.45175 1.000 34.75509  ? 207 TRP   A CE3    1 
ATOM   1599 C CZ2    . TRP   A 1 214 ? 22.93872  -8.08081  -18.81440 1.000 34.47409  ? 207 TRP   A CZ2    1 
ATOM   1600 C CZ3    . TRP   A 1 214 ? 24.17681  -7.00967  -17.03916 1.000 35.64536  ? 207 TRP   A CZ3    1 
ATOM   1601 C CH2    . TRP   A 1 214 ? 24.12667  -7.77881  -18.20808 1.000 36.15111  ? 207 TRP   A CH2    1 
ATOM   1602 N N      . SER   A 1 215 ? 17.49087  -4.28121  -16.88290 1.000 25.62106  ? 208 SER   A N      1 
ATOM   1603 C CA     . SER   A 1 215 ? 16.51411  -4.11768  -17.95465 1.000 28.02985  ? 208 SER   A CA     1 
ATOM   1604 C C      . SER   A 1 215 ? 16.58022  -2.71359  -18.54115 1.000 30.58710  ? 208 SER   A C      1 
ATOM   1605 O O      . SER   A 1 215 ? 16.58549  -2.53725  -19.76485 1.000 31.08158  ? 208 SER   A O      1 
ATOM   1606 C CB     . SER   A 1 215 ? 15.10746  -4.41695  -17.43366 1.000 30.18193  ? 208 SER   A CB     1 
ATOM   1607 O OG     . SER   A 1 215 ? 15.03814  -5.70546  -16.84842 1.000 30.35905  ? 208 SER   A OG     1 
ATOM   1608 N N      . VAL   A 1 216 ? 16.63031  -1.69752  -17.67672 1.000 31.60046  ? 209 VAL   A N      1 
ATOM   1609 C CA     . VAL   A 1 216 ? 16.72162  -0.32056  -18.15269 1.000 30.06658  ? 209 VAL   A CA     1 
ATOM   1610 C C      . VAL   A 1 216 ? 17.96504  -0.13805  -19.01265 1.000 33.58267  ? 209 VAL   A C      1 
ATOM   1611 O O      . VAL   A 1 216 ? 17.91805  0.49838   -20.07279 1.000 29.12358  ? 209 VAL   A O      1 
ATOM   1612 C CB     . VAL   A 1 216 ? 16.70395  0.65679   -16.96288 1.000 39.13652  ? 209 VAL   A CB     1 
ATOM   1613 C CG1    . VAL   A 1 216 ? 17.03314  2.06850   -17.42632 1.000 27.95407  ? 209 VAL   A CG1    1 
ATOM   1614 C CG2    . VAL   A 1 216 ? 15.35173  0.61428   -16.26176 1.000 28.81787  ? 209 VAL   A CG2    1 
ATOM   1615 N N      . GLY   A 1 217 ? 19.09502  -0.69683  -18.57450 1.000 32.58558  ? 210 GLY   A N      1 
ATOM   1616 C CA     . GLY   A 1 217 ? 20.30634  -0.61149  -19.37370 1.000 32.41771  ? 210 GLY   A CA     1 
ATOM   1617 C C      . GLY   A 1 217 ? 20.14086  -1.22067  -20.75260 1.000 32.19381  ? 210 GLY   A C      1 
ATOM   1618 O O      . GLY   A 1 217 ? 20.67420  -0.70484  -21.73788 1.000 34.76167  ? 210 GLY   A O      1 
ATOM   1619 N N      . CYS   A 1 218 ? 19.40107  -2.32885  -20.84218 1.000 31.23297  ? 211 CYS   A N      1 
ATOM   1620 C CA     . CYS   A 1 218 ? 19.14290  -2.93906  -22.14249 1.000 29.46857  ? 211 CYS   A CA     1 
ATOM   1621 C C      . CYS   A 1 218 ? 18.23925  -2.05676  -22.99448 1.000 32.49371  ? 211 CYS   A C      1 
ATOM   1622 O O      . CYS   A 1 218 ? 18.40497  -1.98470  -24.21765 1.000 30.47832  ? 211 CYS   A O      1 
ATOM   1623 C CB     . CYS   A 1 218 ? 18.51842  -4.32273  -21.96139 1.000 29.89339  ? 211 CYS   A CB     1 
ATOM   1624 S SG     . CYS   A 1 218 ? 19.65945  -5.60662  -21.39870 1.000 32.32281  ? 211 CYS   A SG     1 
ATOM   1625 N N      . ILE   A 1 219 ? 17.27584  -1.38155  -22.36670 1.000 31.99753  ? 212 ILE   A N      1 
ATOM   1626 C CA     . ILE   A 1 219 ? 16.35953  -0.52496  -23.11221 1.000 27.77080  ? 212 ILE   A CA     1 
ATOM   1627 C C      . ILE   A 1 219 ? 17.08997  0.70540   -23.63483 1.000 28.99370  ? 212 ILE   A C      1 
ATOM   1628 O O      . ILE   A 1 219 ? 16.95673  1.07761   -24.80660 1.000 29.03312  ? 212 ILE   A O      1 
ATOM   1629 C CB     . ILE   A 1 219 ? 15.15686  -0.13714  -22.23338 1.000 31.86173  ? 212 ILE   A CB     1 
ATOM   1630 C CG1    . ILE   A 1 219 ? 14.32642  -1.37450  -21.88812 1.000 29.21473  ? 212 ILE   A CG1    1 
ATOM   1631 C CG2    . ILE   A 1 219 ? 14.30116  0.90840   -22.93147 1.000 31.82874  ? 212 ILE   A CG2    1 
ATOM   1632 C CD1    . ILE   A 1 219 ? 13.08567  -1.06851  -21.07654 1.000 28.36202  ? 212 ILE   A CD1    1 
ATOM   1633 N N      . MET   A 1 220 ? 17.87764  1.35145   -22.77242 1.000 27.54741  ? 213 MET   A N      1 
ATOM   1634 C CA     . MET   A 1 220 ? 18.59238  2.55769   -23.17592 1.000 31.31181  ? 213 MET   A CA     1 
ATOM   1635 C C      . MET   A 1 220 ? 19.52922  2.28387   -24.34631 1.000 34.42231  ? 213 MET   A C      1 
ATOM   1636 O O      . MET   A 1 220 ? 19.66964  3.11927   -25.24794 1.000 29.37767  ? 213 MET   A O      1 
ATOM   1637 C CB     . MET   A 1 220 ? 19.36569  3.12164   -21.98420 1.000 32.84268  ? 213 MET   A CB     1 
ATOM   1638 C CG     . MET   A 1 220 ? 20.39950  4.17134   -22.34372 1.000 30.39653  ? 213 MET   A CG     1 
ATOM   1639 S SD     . MET   A 1 220 ? 21.01671  5.03279   -20.88464 1.000 34.96895  ? 213 MET   A SD     1 
ATOM   1640 C CE     . MET   A 1 220 ? 22.11403  6.23042   -21.63637 1.000 33.36412  ? 213 MET   A CE     1 
ATOM   1641 N N      . ALA   A 1 221 ? 20.18016  1.11782   -24.35013 1.000 34.31622  ? 214 ALA   A N      1 
ATOM   1642 C CA     . ALA   A 1 221 ? 21.10183  0.79033   -25.43363 1.000 36.42748  ? 214 ALA   A CA     1 
ATOM   1643 C C      . ALA   A 1 221 ? 20.37089  0.67804   -26.76553 1.000 31.75379  ? 214 ALA   A C      1 
ATOM   1644 O O      . ALA   A 1 221 ? 20.89443  1.09001   -27.80729 1.000 35.34026  ? 214 ALA   A O      1 
ATOM   1645 C CB     . ALA   A 1 221 ? 21.84495  -0.50735  -25.11698 1.000 32.00300  ? 214 ALA   A CB     1 
ATOM   1646 N N      . GLU   A 1 222 ? 19.16138  0.11529   -26.75318 1.000 33.02399  ? 215 GLU   A N      1 
ATOM   1647 C CA     . GLU   A 1 222 ? 18.36785  0.03513   -27.97478 1.000 36.82680  ? 215 GLU   A CA     1 
ATOM   1648 C C      . GLU   A 1 222 ? 18.01202  1.42651   -28.48461 1.000 35.34994  ? 215 GLU   A C      1 
ATOM   1649 O O      . GLU   A 1 222 ? 18.15424  1.72085   -29.67721 1.000 35.29269  ? 215 GLU   A O      1 
ATOM   1650 C CB     . GLU   A 1 222 ? 17.10502  -0.78755  -27.71901 1.000 31.68919  ? 215 GLU   A CB     1 
ATOM   1651 C CG     . GLU   A 1 222 ? 16.53028  -1.46638  -28.94923 1.000 39.58120  ? 215 GLU   A CG     1 
ATOM   1652 C CD     . GLU   A 1 222 ? 15.53432  -2.55200  -28.59328 1.000 50.11615  ? 215 GLU   A CD     1 
ATOM   1653 O OE1    . GLU   A 1 222 ? 14.46189  -2.61349  -29.23027 1.000 53.78307  ? 215 GLU   A OE1    1 
ATOM   1654 O OE2    . GLU   A 1 222 ? 15.82335  -3.34216  -27.67096 1.000 41.84462  ? 215 GLU   A OE2    1 
ATOM   1655 N N      . LEU   A 1 223 ? 17.55029  2.30119   -27.58660 1.000 33.41963  ? 216 LEU   A N      1 
ATOM   1656 C CA     . LEU   A 1 223 ? 17.16250  3.64810   -27.99229 1.000 38.59605  ? 216 LEU   A CA     1 
ATOM   1657 C C      . LEU   A 1 223 ? 18.32064  4.40218   -28.63207 1.000 34.87361  ? 216 LEU   A C      1 
ATOM   1658 O O      . LEU   A 1 223 ? 18.10580  5.20989   -29.54258 1.000 37.65799  ? 216 LEU   A O      1 
ATOM   1659 C CB     . LEU   A 1 223 ? 16.62757  4.42476   -26.78833 1.000 38.68064  ? 216 LEU   A CB     1 
ATOM   1660 C CG     . LEU   A 1 223 ? 15.46125  3.79559   -26.02386 1.000 39.18362  ? 216 LEU   A CG     1 
ATOM   1661 C CD1    . LEU   A 1 223 ? 14.91846  4.76179   -24.98083 1.000 32.69612  ? 216 LEU   A CD1    1 
ATOM   1662 C CD2    . LEU   A 1 223 ? 14.36325  3.36306   -26.98309 1.000 37.43515  ? 216 LEU   A CD2    1 
ATOM   1663 N N      . LEU   A 1 224 ? 19.54977  4.15554   -28.17434 1.000 33.23822  ? 217 LEU   A N      1 
ATOM   1664 C CA     . LEU   A 1 224 ? 20.70225  4.87465   -28.70748 1.000 34.12851  ? 217 LEU   A CA     1 
ATOM   1665 C C      . LEU   A 1 224 ? 21.15732  4.30685   -30.04666 1.000 37.97007  ? 217 LEU   A C      1 
ATOM   1666 O O      . LEU   A 1 224 ? 21.46002  5.06627   -30.97387 1.000 44.35031  ? 217 LEU   A O      1 
ATOM   1667 C CB     . LEU   A 1 224 ? 21.85601  4.83809   -27.70397 1.000 35.75153  ? 217 LEU   A CB     1 
ATOM   1668 C CG     . LEU   A 1 224 ? 21.72198  5.70721   -26.45257 1.000 38.97210  ? 217 LEU   A CG     1 
ATOM   1669 C CD1    . LEU   A 1 224 ? 22.68931  5.24200   -25.37556 1.000 33.56501  ? 217 LEU   A CD1    1 
ATOM   1670 C CD2    . LEU   A 1 224 ? 21.95252  7.17224   -26.78810 1.000 37.66055  ? 217 LEU   A CD2    1 
ATOM   1671 N N      . THR   A 1 225 ? 21.21322  2.98103   -30.16756 1.000 36.43742  ? 218 THR   A N      1 
ATOM   1672 C CA     . THR   A 1 225 ? 21.76092  2.34776   -31.36118 1.000 39.20355  ? 218 THR   A CA     1 
ATOM   1673 C C      . THR   A 1 225 ? 20.70668  2.03002   -32.41195 1.000 38.65439  ? 218 THR   A C      1 
ATOM   1674 O O      . THR   A 1 225 ? 21.02351  2.01070   -33.60719 1.000 40.90194  ? 218 THR   A O      1 
ATOM   1675 C CB     . THR   A 1 225 ? 22.49099  1.05436   -30.98527 1.000 41.35869  ? 218 THR   A CB     1 
ATOM   1676 O OG1    . THR   A 1 225 ? 21.59491  0.18670   -30.27845 1.000 36.79101  ? 218 THR   A OG1    1 
ATOM   1677 C CG2    . THR   A 1 225 ? 23.69406  1.35716   -30.10596 1.000 39.23419  ? 218 THR   A CG2    1 
ATOM   1678 N N      . GLY   A 1 226 ? 19.46716  1.78143   -32.00035 1.000 41.39016  ? 219 GLY   A N      1 
ATOM   1679 C CA     . GLY   A 1 226 ? 18.44261  1.31594   -32.90983 1.000 42.62070  ? 219 GLY   A CA     1 
ATOM   1680 C C      . GLY   A 1 226 ? 18.38284  -0.18446  -33.08268 1.000 46.57846  ? 219 GLY   A C      1 
ATOM   1681 O O      . GLY   A 1 226 ? 17.70483  -0.65912  -34.00197 1.000 49.39863  ? 219 GLY   A O      1 
ATOM   1682 N N      . ARG   A 1 227 ? 19.06801  -0.94606  -32.23149 1.000 46.26421  ? 220 ARG   A N      1 
ATOM   1683 C CA     . ARG   A 1 227 ? 19.10912  -2.39628  -32.33830 1.000 43.26394  ? 220 ARG   A CA     1 
ATOM   1684 C C      . ARG   A 1 227 ? 18.99044  -3.00596  -30.94878 1.000 41.00939  ? 220 ARG   A C      1 
ATOM   1685 O O      . ARG   A 1 227 ? 19.28324  -2.36283  -29.93732 1.000 42.73112  ? 220 ARG   A O      1 
ATOM   1686 C CB     . ARG   A 1 227 ? 20.40250  -2.87716  -33.01352 1.000 46.95149  ? 220 ARG   A CB     1 
ATOM   1687 C CG     . ARG   A 1 227 ? 21.02644  -1.86302  -33.95989 1.000 57.16194  ? 220 ARG   A CG     1 
ATOM   1688 C CD     . ARG   A 1 227 ? 22.54662  -1.92132  -33.91933 1.000 59.63611  ? 220 ARG   A CD     1 
ATOM   1689 N NE     . ARG   A 1 227 ? 23.06361  -3.19452  -34.40670 1.000 71.06952  ? 220 ARG   A NE     1 
ATOM   1690 C CZ     . ARG   A 1 227 ? 23.20380  -3.50680  -35.68802 1.000 74.66731  ? 220 ARG   A CZ     1 
ATOM   1691 N NH1    . ARG   A 1 227 ? 22.86414  -2.66113  -36.64757 1.000 68.49908  ? 220 ARG   A NH1    1 
ATOM   1692 N NH2    . ARG   A 1 227 ? 23.69641  -4.69820  -36.01503 1.000 70.85151  ? 220 ARG   A NH2    1 
ATOM   1693 N N      . THR   A 1 228 ? 18.55164  -4.26157  -30.90900 1.000 47.23540  ? 221 THR   A N      1 
ATOM   1694 C CA     . THR   A 1 228 ? 18.50010  -4.98960  -29.64877 1.000 41.54127  ? 221 THR   A CA     1 
ATOM   1695 C C      . THR   A 1 228 ? 19.91553  -5.28251  -29.16602 1.000 35.65224  ? 221 THR   A C      1 
ATOM   1696 O O      . THR   A 1 228 ? 20.75052  -5.78601  -29.92435 1.000 32.22174  ? 221 THR   A O      1 
ATOM   1697 C CB     . THR   A 1 228 ? 17.71530  -6.29132  -29.81007 1.000 35.79855  ? 221 THR   A CB     1 
ATOM   1698 O OG1    . THR   A 1 228 ? 16.39804  -6.00330  -30.29499 1.000 38.79076  ? 221 THR   A OG1    1 
ATOM   1699 C CG2    . THR   A 1 228 ? 17.60809  -7.01540  -28.47541 1.000 38.08979  ? 221 THR   A CG2    1 
ATOM   1700 N N      . LEU   A 1 229 ? 20.18867  -4.95890  -27.90100 1.000 33.71706  ? 222 LEU   A N      1 
ATOM   1701 C CA     . LEU   A 1 229 ? 21.52199  -5.19137  -27.35525 1.000 37.90133  ? 222 LEU   A CA     1 
ATOM   1702 C C      . LEU   A 1 229 ? 21.83763  -6.68113  -27.29338 1.000 39.42989  ? 222 LEU   A C      1 
ATOM   1703 O O      . LEU   A 1 229 ? 22.88108  -7.12608  -27.78524 1.000 38.31758  ? 222 LEU   A O      1 
ATOM   1704 C CB     . LEU   A 1 229 ? 21.64252  -4.55670  -25.96974 1.000 34.48599  ? 222 LEU   A CB     1 
ATOM   1705 C CG     . LEU   A 1 229 ? 23.00748  -4.71373  -25.29646 1.000 30.58397  ? 222 LEU   A CG     1 
ATOM   1706 C CD1    . LEU   A 1 229 ? 24.10710  -4.16905  -26.19360 1.000 37.35571  ? 222 LEU   A CD1    1 
ATOM   1707 C CD2    . LEU   A 1 229 ? 23.02936  -4.02773  -23.93873 1.000 28.93096  ? 222 LEU   A CD2    1 
ATOM   1708 N N      . PHE   A 1 230 ? 20.94380  -7.46968  -26.69022 1.000 42.17921  ? 223 PHE   A N      1 
ATOM   1709 C CA     . PHE   A 1 230 ? 21.11148  -8.91375  -26.53775 1.000 29.28059  ? 223 PHE   A CA     1 
ATOM   1710 C C      . PHE   A 1 230 ? 19.91002  -9.61296  -27.16478 1.000 36.32789  ? 223 PHE   A C      1 
ATOM   1711 O O      . PHE   A 1 230 ? 18.98671  -10.03803 -26.45361 1.000 41.28063  ? 223 PHE   A O      1 
ATOM   1712 C CB     . PHE   A 1 230 ? 21.25907  -9.30957  -25.06889 1.000 33.75206  ? 223 PHE   A CB     1 
ATOM   1713 C CG     . PHE   A 1 230 ? 22.35383  -8.57721  -24.34340 1.000 32.37127  ? 223 PHE   A CG     1 
ATOM   1714 C CD1    . PHE   A 1 230 ? 23.67513  -8.70749  -24.73696 1.000 33.49620  ? 223 PHE   A CD1    1 
ATOM   1715 C CD2    . PHE   A 1 230 ? 22.06087  -7.76950  -23.25701 1.000 28.31359  ? 223 PHE   A CD2    1 
ATOM   1716 C CE1    . PHE   A 1 230 ? 24.68300  -8.03843  -24.06537 1.000 32.71728  ? 223 PHE   A CE1    1 
ATOM   1717 C CE2    . PHE   A 1 230 ? 23.06360  -7.09832  -22.58187 1.000 44.56576  ? 223 PHE   A CE2    1 
ATOM   1718 C CZ     . PHE   A 1 230 ? 24.37625  -7.23284  -22.98654 1.000 36.09359  ? 223 PHE   A CZ     1 
ATOM   1719 N N      . PRO   A 1 231 ? 19.88263  -9.74959  -28.49314 1.000 38.97778  ? 224 PRO   A N      1 
ATOM   1720 C CA     . PRO   A 1 231 ? 18.77963  -10.46721 -29.15917 1.000 43.59983  ? 224 PRO   A CA     1 
ATOM   1721 C C      . PRO   A 1 231 ? 18.98954  -11.97918 -29.16566 1.000 39.31671  ? 224 PRO   A C      1 
ATOM   1722 O O      . PRO   A 1 231 ? 19.07483  -12.62209 -30.21546 1.000 45.24867  ? 224 PRO   A O      1 
ATOM   1723 C CB     . PRO   A 1 231 ? 18.80541  -9.86171  -30.56782 1.000 42.16195  ? 224 PRO   A CB     1 
ATOM   1724 C CG     . PRO   A 1 231 ? 20.24966  -9.56733  -30.80250 1.000 38.49303  ? 224 PRO   A CG     1 
ATOM   1725 C CD     . PRO   A 1 231 ? 20.83365  -9.17622  -29.46248 1.000 41.84031  ? 224 PRO   A CD     1 
ATOM   1726 N N      . GLY   A 1 232 ? 19.07092  -12.56159 -27.97226 1.000 42.80654  ? 225 GLY   A N      1 
ATOM   1727 C CA     . GLY   A 1 232 ? 19.33232  -13.98344 -27.86750 1.000 49.22126  ? 225 GLY   A CA     1 
ATOM   1728 C C      . GLY   A 1 232 ? 18.15894  -14.82364 -28.33445 1.000 54.33059  ? 225 GLY   A C      1 
ATOM   1729 O O      . GLY   A 1 232 ? 16.99957  -14.41104 -28.28201 1.000 55.01318  ? 225 GLY   A O      1 
ATOM   1730 N N      . THR   A 1 233 ? 18.47738  -16.03242 -28.80223 1.000 50.41845  ? 226 THR   A N      1 
ATOM   1731 C CA     . THR   A 1 233 ? 17.45038  -16.96676 -29.24363 1.000 49.71760  ? 226 THR   A CA     1 
ATOM   1732 C C      . THR   A 1 233 ? 16.80262  -17.72154 -28.08772 1.000 48.69709  ? 226 THR   A C      1 
ATOM   1733 O O      . THR   A 1 233 ? 15.68942  -18.22873 -28.24962 1.000 50.72306  ? 226 THR   A O      1 
ATOM   1734 C CB     . THR   A 1 233 ? 18.03701  -17.97100 -30.24162 1.000 56.45743  ? 226 THR   A CB     1 
ATOM   1735 O OG1    . THR   A 1 233 ? 19.28755  -18.46571 -29.74693 1.000 52.32035  ? 226 THR   A OG1    1 
ATOM   1736 C CG2    . THR   A 1 233 ? 18.25940  -17.31405 -31.59897 1.000 57.15608  ? 226 THR   A CG2    1 
ATOM   1737 N N      . ASP   A 1 234 ? 17.46193  -17.80560 -26.93608 1.000 46.09962  ? 227 ASP   A N      1 
ATOM   1738 C CA     . ASP   A 1 234 ? 16.92605  -18.51546 -25.78277 1.000 45.04318  ? 227 ASP   A CA     1 
ATOM   1739 C C      . ASP   A 1 234 ? 17.73189  -18.10010 -24.55325 1.000 46.83383  ? 227 ASP   A C      1 
ATOM   1740 O O      . ASP   A 1 234 ? 18.44346  -17.08995 -24.57890 1.000 49.60428  ? 227 ASP   A O      1 
ATOM   1741 C CB     . ASP   A 1 234 ? 16.94829  -20.03386 -26.02168 1.000 41.02638  ? 227 ASP   A CB     1 
ATOM   1742 C CG     . ASP   A 1 234 ? 18.26632  -20.50955 -26.57770 1.000 40.19876  ? 227 ASP   A CG     1 
ATOM   1743 O OD1    . ASP   A 1 234 ? 19.24444  -20.58787 -25.80332 1.000 41.31235  ? 227 ASP   A OD1    1 
ATOM   1744 O OD2    . ASP   A 1 234 ? 18.32811  -20.78872 -27.78907 1.000 49.03766  ? 227 ASP   A OD2    1 
ATOM   1745 N N      . HIS   A 1 235 ? 17.64341  -18.89363 -23.48737 1.000 47.37357  ? 228 HIS   A N      1 
ATOM   1746 C CA     . HIS   A 1 235 ? 18.23168  -18.49756 -22.21474 1.000 50.00804  ? 228 HIS   A CA     1 
ATOM   1747 C C      . HIS   A 1 235 ? 19.73739  -18.72786 -22.18555 1.000 45.88402  ? 228 HIS   A C      1 
ATOM   1748 O O      . HIS   A 1 235 ? 20.47568  -17.88997 -21.65881 1.000 48.27599  ? 228 HIS   A O      1 
ATOM   1749 C CB     . HIS   A 1 235 ? 17.53898  -19.23287 -21.06518 1.000 43.11499  ? 228 HIS   A CB     1 
ATOM   1750 C CG     . HIS   A 1 235 ? 16.23357  -18.61650 -20.66507 1.000 53.19028  ? 228 HIS   A CG     1 
ATOM   1751 N ND1    . HIS   A 1 235 ? 15.79068  -18.58156 -19.36012 1.000 44.82096  ? 228 HIS   A ND1    1 
ATOM   1752 C CD2    . HIS   A 1 235 ? 15.27615  -18.00606 -21.40331 1.000 48.07642  ? 228 HIS   A CD2    1 
ATOM   1753 C CE1    . HIS   A 1 235 ? 14.61663  -17.97725 -19.31230 1.000 43.36246  ? 228 HIS   A CE1    1 
ATOM   1754 N NE2    . HIS   A 1 235 ? 14.28232  -17.61770 -20.53853 1.000 41.86930  ? 228 HIS   A NE2    1 
ATOM   1755 N N      . ILE   A 1 236 ? 20.21936  -19.84083 -22.74366 1.000 40.38840  ? 229 ILE   A N      1 
ATOM   1756 C CA     . ILE   A 1 236 ? 21.66272  -20.06231 -22.79396 1.000 49.21809  ? 229 ILE   A CA     1 
ATOM   1757 C C      . ILE   A 1 236 ? 22.30758  -19.11631 -23.79998 1.000 44.72703  ? 229 ILE   A C      1 
ATOM   1758 O O      . ILE   A 1 236 ? 23.31736  -18.46528 -23.50632 1.000 45.98035  ? 229 ILE   A O      1 
ATOM   1759 C CB     . ILE   A 1 236 ? 21.98121  -21.53476 -23.11451 1.000 53.05950  ? 229 ILE   A CB     1 
ATOM   1760 C CG1    . ILE   A 1 236 ? 21.23777  -21.99142 -24.37145 1.000 53.69584  ? 229 ILE   A CG1    1 
ATOM   1761 C CG2    . ILE   A 1 236 ? 21.64235  -22.42762 -21.92866 1.000 49.39315  ? 229 ILE   A CG2    1 
ATOM   1762 C CD1    . ILE   A 1 236 ? 22.10340  -22.03062 -25.61303 1.000 53.05355  ? 229 ILE   A CD1    1 
ATOM   1763 N N      . ASP   A 1 237 ? 21.73312  -19.02500 -25.00272 1.000 37.42084  ? 230 ASP   A N      1 
ATOM   1764 C CA     . ASP   A 1 237 ? 22.23850  -18.07622 -25.98912 1.000 43.52026  ? 230 ASP   A CA     1 
ATOM   1765 C C      . ASP   A 1 237 ? 22.20613  -16.65004 -25.45604 1.000 45.67182  ? 230 ASP   A C      1 
ATOM   1766 O O      . ASP   A 1 237 ? 23.09195  -15.84802 -25.77354 1.000 51.08971  ? 230 ASP   A O      1 
ATOM   1767 C CB     . ASP   A 1 237 ? 21.42931  -18.17942 -27.28269 1.000 39.30193  ? 230 ASP   A CB     1 
ATOM   1768 C CG     . ASP   A 1 237 ? 21.91382  -17.21828 -28.35047 1.000 49.11367  ? 230 ASP   A CG     1 
ATOM   1769 O OD1    . ASP   A 1 237 ? 23.08591  -17.33106 -28.76746 1.000 44.55991  ? 230 ASP   A OD1    1 
ATOM   1770 O OD2    . ASP   A 1 237 ? 21.12107  -16.35169 -28.77532 1.000 51.91963  ? 230 ASP   A OD2    1 
ATOM   1771 N N      . GLN   A 1 238 ? 21.19746  -16.31591 -24.64801 1.000 40.70284  ? 231 GLN   A N      1 
ATOM   1772 C CA     . GLN   A 1 238 ? 21.13727  -14.98885 -24.04374 1.000 45.49374  ? 231 GLN   A CA     1 
ATOM   1773 C C      . GLN   A 1 238 ? 22.33498  -14.75135 -23.13234 1.000 44.36724  ? 231 GLN   A C      1 
ATOM   1774 O O      . GLN   A 1 238 ? 23.03637  -13.74018 -23.25657 1.000 37.05949  ? 231 GLN   A O      1 
ATOM   1775 C CB     . GLN   A 1 238 ? 19.82814  -14.82617 -23.27012 1.000 46.48003  ? 231 GLN   A CB     1 
ATOM   1776 C CG     . GLN   A 1 238 ? 19.50251  -13.39158 -22.89512 1.000 45.87413  ? 231 GLN   A CG     1 
ATOM   1777 C CD     . GLN   A 1 238 ? 18.88895  -12.61620 -24.04354 1.000 45.05859  ? 231 GLN   A CD     1 
ATOM   1778 O OE1    . GLN   A 1 238 ? 18.29963  -13.19714 -24.95542 1.000 43.67889  ? 231 GLN   A OE1    1 
ATOM   1779 N NE2    . GLN   A 1 238 ? 19.02288  -11.29582 -24.00431 1.000 46.42110  ? 231 GLN   A NE2    1 
ATOM   1780 N N      . LEU   A 1 239 ? 22.58637  -15.68149 -22.20728 1.000 40.94347  ? 232 LEU   A N      1 
ATOM   1781 C CA     . LEU   A 1 239 ? 23.73542  -15.54883 -21.31862 1.000 44.85697  ? 232 LEU   A CA     1 
ATOM   1782 C C      . LEU   A 1 239 ? 25.04262  -15.49725 -22.09768 1.000 46.89825  ? 232 LEU   A C      1 
ATOM   1783 O O      . LEU   A 1 239 ? 26.00985  -14.87423 -21.64507 1.000 49.84362  ? 232 LEU   A O      1 
ATOM   1784 C CB     . LEU   A 1 239 ? 23.76053  -16.70386 -20.31664 1.000 47.71903  ? 232 LEU   A CB     1 
ATOM   1785 C CG     . LEU   A 1 239 ? 22.60527  -16.76342 -19.31458 1.000 48.39744  ? 232 LEU   A CG     1 
ATOM   1786 C CD1    . LEU   A 1 239 ? 22.55472  -18.12198 -18.63465 1.000 55.88789  ? 232 LEU   A CD1    1 
ATOM   1787 C CD2    . LEU   A 1 239 ? 22.72922  -15.65110 -18.28545 1.000 43.06188  ? 232 LEU   A CD2    1 
ATOM   1788 N N      . LYS   A 1 240 ? 25.09360  -16.14280 -23.26576 1.000 38.58334  ? 233 LYS   A N      1 
ATOM   1789 C CA     . LYS   A 1 240 ? 26.30959  -16.11352 -24.07162 1.000 43.46426  ? 233 LYS   A CA     1 
ATOM   1790 C C      . LYS   A 1 240 ? 26.52979  -14.73737 -24.68783 1.000 52.76395  ? 233 LYS   A C      1 
ATOM   1791 O O      . LYS   A 1 240 ? 27.66880  -14.26126 -24.76624 1.000 49.45815  ? 233 LYS   A O      1 
ATOM   1792 C CB     . LYS   A 1 240 ? 26.24509  -17.18798 -25.15636 1.000 47.96202  ? 233 LYS   A CB     1 
ATOM   1793 C CG     . LYS   A 1 240 ? 27.09696  -16.89335 -26.38002 1.000 57.56522  ? 233 LYS   A CG     1 
ATOM   1794 C CD     . LYS   A 1 240 ? 26.35808  -17.25433 -27.65899 1.000 64.67276  ? 233 LYS   A CD     1 
ATOM   1795 C CE     . LYS   A 1 240 ? 27.29673  -17.29259 -28.85375 1.000 62.19663  ? 233 LYS   A CE     1 
ATOM   1796 N NZ     . LYS   A 1 240 ? 26.63595  -17.87711 -30.05368 1.000 65.63068  ? 233 LYS   A NZ     1 
ATOM   1797 N N      . LEU   A 1 241 ? 25.45326  -14.08296 -25.13145 1.000 42.26623  ? 234 LEU   A N      1 
ATOM   1798 C CA     . LEU   A 1 241 ? 25.58401  -12.73341 -25.67064 1.000 40.30737  ? 234 LEU   A CA     1 
ATOM   1799 C C      . LEU   A 1 241 ? 25.99717  -11.74753 -24.58575 1.000 43.67977  ? 234 LEU   A C      1 
ATOM   1800 O O      . LEU   A 1 241 ? 26.83193  -10.86645 -24.82288 1.000 46.21758  ? 234 LEU   A O      1 
ATOM   1801 C CB     . LEU   A 1 241 ? 24.27186  -12.29806 -26.32221 1.000 41.02548  ? 234 LEU   A CB     1 
ATOM   1802 C CG     . LEU   A 1 241 ? 23.69895  -13.22716 -27.39487 1.000 43.81569  ? 234 LEU   A CG     1 
ATOM   1803 C CD1    . LEU   A 1 241 ? 22.50485  -12.58248 -28.08372 1.000 33.06171  ? 234 LEU   A CD1    1 
ATOM   1804 C CD2    . LEU   A 1 241 ? 24.76901  -13.60372 -28.40845 1.000 43.63741  ? 234 LEU   A CD2    1 
ATOM   1805 N N      . ILE   A 1 242 ? 25.42459  -11.88145 -23.38838 1.000 39.23150  ? 235 ILE   A N      1 
ATOM   1806 C CA     . ILE   A 1 242 ? 25.80377  -11.00958 -22.28009 1.000 35.08364  ? 235 ILE   A CA     1 
ATOM   1807 C C      . ILE   A 1 242 ? 27.28655  -11.16683 -21.96788 1.000 49.03076  ? 235 ILE   A C      1 
ATOM   1808 O O      . ILE   A 1 242 ? 28.00925  -10.18089 -21.77918 1.000 45.03318  ? 235 ILE   A O      1 
ATOM   1809 C CB     . ILE   A 1 242 ? 24.93217  -11.30310 -21.04613 1.000 35.35778  ? 235 ILE   A CB     1 
ATOM   1810 C CG1    . ILE   A 1 242 ? 23.50058  -10.81073 -21.27601 1.000 39.83793  ? 235 ILE   A CG1    1 
ATOM   1811 C CG2    . ILE   A 1 242 ? 25.53603  -10.66718 -19.80081 1.000 31.59013  ? 235 ILE   A CG2    1 
ATOM   1812 C CD1    . ILE   A 1 242 ? 22.47071  -11.48856 -20.40057 1.000 33.77509  ? 235 ILE   A CD1    1 
ATOM   1813 N N      . LEU   A 1 243 ? 27.76284  -12.41390 -21.91308 1.000 46.10131  ? 236 LEU   A N      1 
ATOM   1814 C CA     . LEU   A 1 243 ? 29.16531  -12.65706 -21.59278 1.000 45.50890  ? 236 LEU   A CA     1 
ATOM   1815 C C      . LEU   A 1 243 ? 30.09718  -12.01216 -22.61087 1.000 48.81153  ? 236 LEU   A C      1 
ATOM   1816 O O      . LEU   A 1 243 ? 31.19464  -11.56929 -22.25281 1.000 50.87126  ? 236 LEU   A O      1 
ATOM   1817 C CB     . LEU   A 1 243 ? 29.43044  -14.16033 -21.50770 1.000 48.77955  ? 236 LEU   A CB     1 
ATOM   1818 C CG     . LEU   A 1 243 ? 28.92534  -14.86476 -20.24653 1.000 49.12981  ? 236 LEU   A CG     1 
ATOM   1819 C CD1    . LEU   A 1 243 ? 28.75642  -16.35526 -20.49301 1.000 53.83848  ? 236 LEU   A CD1    1 
ATOM   1820 C CD2    . LEU   A 1 243 ? 29.86719  -14.61548 -19.08069 1.000 51.54426  ? 236 LEU   A CD2    1 
ATOM   1821 N N      . ARG   A 1 244 ? 29.68402  -11.94765 -23.87900 1.000 42.28892  ? 237 ARG   A N      1 
ATOM   1822 C CA     . ARG   A 1 244 ? 30.53768  -11.34342 -24.89693 1.000 52.04522  ? 237 ARG   A CA     1 
ATOM   1823 C C      . ARG   A 1 244 ? 30.78151  -9.86697  -24.60857 1.000 52.11438  ? 237 ARG   A C      1 
ATOM   1824 O O      . ARG   A 1 244 ? 31.90986  -9.37953  -24.74216 1.000 47.10781  ? 237 ARG   A O      1 
ATOM   1825 C CB     . ARG   A 1 244 ? 29.91813  -11.52049 -26.28389 1.000 49.40010  ? 237 ARG   A CB     1 
ATOM   1826 C CG     . ARG   A 1 244 ? 30.42394  -10.51662 -27.30944 1.000 63.41107  ? 237 ARG   A CG     1 
ATOM   1827 C CD     . ARG   A 1 244 ? 29.38134  -10.21669 -28.37495 1.000 70.75462  ? 237 ARG   A CD     1 
ATOM   1828 N NE     . ARG   A 1 244 ? 29.03427  -11.39368 -29.16215 1.000 85.42964  ? 237 ARG   A NE     1 
ATOM   1829 C CZ     . ARG   A 1 244 ? 28.31521  -11.36258 -30.27633 1.000 81.85099  ? 237 ARG   A CZ     1 
ATOM   1830 N NH1    . ARG   A 1 244 ? 27.84472  -10.22623 -30.76458 1.000 61.98327  ? 237 ARG   A NH1    1 
ATOM   1831 N NH2    . ARG   A 1 244 ? 28.06279  -12.49984 -30.91778 1.000 68.61664  ? 237 ARG   A NH2    1 
ATOM   1832 N N      . LEU   A 1 245 ? 29.73586  -9.13639  -24.21529 1.000 44.33888  ? 238 LEU   A N      1 
ATOM   1833 C CA     . LEU   A 1 245 ? 29.88699  -7.70847  -23.95589 1.000 47.33177  ? 238 LEU   A CA     1 
ATOM   1834 C C      . LEU   A 1 245 ? 30.56124  -7.44990  -22.61341 1.000 47.08510  ? 238 LEU   A C      1 
ATOM   1835 O O      . LEU   A 1 245 ? 31.56631  -6.73400  -22.54407 1.000 49.89454  ? 238 LEU   A O      1 
ATOM   1836 C CB     . LEU   A 1 245 ? 28.52504  -7.01177  -24.00590 1.000 49.63653  ? 238 LEU   A CB     1 
ATOM   1837 C CG     . LEU   A 1 245 ? 28.52298  -5.56319  -23.50547 1.000 43.59934  ? 238 LEU   A CG     1 
ATOM   1838 C CD1    . LEU   A 1 245 ? 29.36954  -4.68128  -24.41042 1.000 48.37165  ? 238 LEU   A CD1    1 
ATOM   1839 C CD2    . LEU   A 1 245 ? 27.10722  -5.01712  -23.39052 1.000 39.95443  ? 238 LEU   A CD2    1 
ATOM   1840 N N      . VAL   A 1 246 ? 30.02026  -8.02366  -21.53326 1.000 38.02494  ? 239 VAL   A N      1 
ATOM   1841 C CA     . VAL   A 1 246 ? 30.50636  -7.71705  -20.18936 1.000 42.94420  ? 239 VAL   A CA     1 
ATOM   1842 C C      . VAL   A 1 246 ? 31.69290  -8.57219  -19.76764 1.000 49.08752  ? 239 VAL   A C      1 
ATOM   1843 O O      . VAL   A 1 246 ? 32.36892  -8.23033  -18.78458 1.000 48.41612  ? 239 VAL   A O      1 
ATOM   1844 C CB     . VAL   A 1 246 ? 29.37718  -7.86945  -19.15042 1.000 47.01563  ? 239 VAL   A CB     1 
ATOM   1845 C CG1    . VAL   A 1 246 ? 28.21850  -6.94051  -19.48633 1.000 43.94133  ? 239 VAL   A CG1    1 
ATOM   1846 C CG2    . VAL   A 1 246 ? 28.90773  -9.31359  -19.08193 1.000 45.45564  ? 239 VAL   A CG2    1 
ATOM   1847 N N      . GLY   A 1 247 ? 31.97115  -9.66428  -20.46940 1.000 53.70724  ? 240 GLY   A N      1 
ATOM   1848 C CA     . GLY   A 1 247 ? 33.09025  -10.51960 -20.13742 1.000 53.21067  ? 240 GLY   A CA     1 
ATOM   1849 C C      . GLY   A 1 247 ? 32.69880  -11.67265 -19.22799 1.000 53.78173  ? 240 GLY   A C      1 
ATOM   1850 O O      . GLY   A 1 247 ? 31.64502  -11.68070 -18.59332 1.000 56.23786  ? 240 GLY   A O      1 
ATOM   1851 N N      . THR   A 1 248 ? 33.58164  -12.66659 -19.17219 1.000 62.55242  ? 241 THR   A N      1 
ATOM   1852 C CA     . THR   A 1 248 ? 33.33472  -13.83533 -18.34455 1.000 54.70100  ? 241 THR   A CA     1 
ATOM   1853 C C      . THR   A 1 248 ? 33.24393  -13.42906 -16.87321 1.000 50.02874  ? 241 THR   A C      1 
ATOM   1854 O O      . THR   A 1 248 ? 33.93187  -12.50377 -16.43039 1.000 39.46475  ? 241 THR   A O      1 
ATOM   1855 C CB     . THR   A 1 248 ? 34.44246  -14.87124 -18.53411 1.000 62.31421  ? 241 THR   A CB     1 
ATOM   1856 O OG1    . THR   A 1 248 ? 34.90498  -14.83762 -19.88998 1.000 70.73099  ? 241 THR   A OG1    1 
ATOM   1857 C CG2    . THR   A 1 248 ? 33.92832  -16.26922 -18.21830 1.000 60.25883  ? 241 THR   A CG2    1 
ATOM   1858 N N      . PRO   A 1 249 ? 32.40086  -14.10344 -16.09277 1.000 49.18688  ? 242 PRO   A N      1 
ATOM   1859 C CA     . PRO   A 1 249 ? 32.25021  -13.73079 -14.68136 1.000 47.93075  ? 242 PRO   A CA     1 
ATOM   1860 C C      . PRO   A 1 249 ? 33.55744  -13.89606 -13.92016 1.000 56.31333  ? 242 PRO   A C      1 
ATOM   1861 O O      . PRO   A 1 249 ? 34.32504  -14.83138 -14.15734 1.000 46.45418  ? 242 PRO   A O      1 
ATOM   1862 C CB     . PRO   A 1 249 ? 31.17462  -14.69740 -14.17031 1.000 44.06040  ? 242 PRO   A CB     1 
ATOM   1863 C CG     . PRO   A 1 249 ? 30.46805  -15.17820 -15.40019 1.000 51.67098  ? 242 PRO   A CG     1 
ATOM   1864 C CD     . PRO   A 1 249 ? 31.51399  -15.21564 -16.46859 1.000 47.73849  ? 242 PRO   A CD     1 
ATOM   1865 N N      . GLY   A 1 250 ? 33.80244  -12.97309 -12.99506 1.000 61.24595  ? 243 GLY   A N      1 
ATOM   1866 C CA     . GLY   A 1 250 ? 35.00326  -13.02263 -12.18915 1.000 47.17391  ? 243 GLY   A CA     1 
ATOM   1867 C C      . GLY   A 1 250 ? 34.94217  -14.09959 -11.12198 1.000 57.46802  ? 243 GLY   A C      1 
ATOM   1868 O O      . GLY   A 1 250 ? 33.90383  -14.70284 -10.84542 1.000 49.69688  ? 243 GLY   A O      1 
ATOM   1869 N N      . ALA   A 1 251 ? 36.10113  -14.33882 -10.50293 1.000 52.29444  ? 244 ALA   A N      1 
ATOM   1870 C CA     . ALA   A 1 251 ? 36.19344  -15.38076 -9.48567  1.000 54.41099  ? 244 ALA   A CA     1 
ATOM   1871 C C      . ALA   A 1 251 ? 35.30642  -15.08107 -8.28429  1.000 55.16707  ? 244 ALA   A C      1 
ATOM   1872 O O      . ALA   A 1 251 ? 34.76561  -16.00686 -7.66828  1.000 43.45552  ? 244 ALA   A O      1 
ATOM   1873 C CB     . ALA   A 1 251 ? 37.64593  -15.55598 -9.04279  1.000 50.72893  ? 244 ALA   A CB     1 
ATOM   1874 N N      . GLU   A 1 252 ? 35.14600  -13.80271 -7.93187  1.000 55.05795  ? 245 GLU   A N      1 
ATOM   1875 C CA     . GLU   A 1 252 ? 34.30919  -13.45072 -6.79061  1.000 51.34122  ? 245 GLU   A CA     1 
ATOM   1876 C C      . GLU   A 1 252 ? 32.82516  -13.62449 -7.08791  1.000 47.34505  ? 245 GLU   A C      1 
ATOM   1877 O O      . GLU   A 1 252 ? 32.03037  -13.76698 -6.15227  1.000 47.61861  ? 245 GLU   A O      1 
ATOM   1878 C CB     . GLU   A 1 252 ? 34.59472  -12.01421 -6.34800  1.000 47.27416  ? 245 GLU   A CB     1 
ATOM   1879 C CG     . GLU   A 1 252 ? 33.72163  -10.96412 -7.01341  1.000 52.51473  ? 245 GLU   A CG     1 
ATOM   1880 C CD     . GLU   A 1 252 ? 34.26442  -10.51535 -8.35648  1.000 54.89894  ? 245 GLU   A CD     1 
ATOM   1881 O OE1    . GLU   A 1 252 ? 33.52972  -9.82930  -9.09755  1.000 57.60183  ? 245 GLU   A OE1    1 
ATOM   1882 O OE2    . GLU   A 1 252 ? 35.42580  -10.84795 -8.67287  1.000 58.40116  ? 245 GLU   A OE2    1 
ATOM   1883 N N      . LEU   A 1 253 ? 32.43425  -13.61750 -8.36345  1.000 45.04959  ? 246 LEU   A N      1 
ATOM   1884 C CA     . LEU   A 1 253 ? 31.04719  -13.90131 -8.71294  1.000 43.54506  ? 246 LEU   A CA     1 
ATOM   1885 C C      . LEU   A 1 253 ? 30.80110  -15.40020 -8.82479  1.000 38.12310  ? 246 LEU   A C      1 
ATOM   1886 O O      . LEU   A 1 253 ? 29.72269  -15.88446 -8.46336  1.000 37.05933  ? 246 LEU   A O      1 
ATOM   1887 C CB     . LEU   A 1 253 ? 30.67858  -13.20067 -10.02076 1.000 42.39563  ? 246 LEU   A CB     1 
ATOM   1888 C CG     . LEU   A 1 253 ? 30.41768  -11.69771 -9.92674  1.000 44.18069  ? 246 LEU   A CG     1 
ATOM   1889 C CD1    . LEU   A 1 253 ? 29.40801  -11.26273 -10.97707 1.000 47.43634  ? 246 LEU   A CD1    1 
ATOM   1890 C CD2    . LEU   A 1 253 ? 29.94283  -11.32377 -8.53126  1.000 48.72284  ? 246 LEU   A CD2    1 
ATOM   1891 N N      . LEU   A 1 254 ? 31.79036  -16.14812 -9.31905  1.000 38.40995  ? 247 LEU   A N      1 
ATOM   1892 C CA     . LEU   A 1 254 ? 31.63893  -17.59481 -9.42308  1.000 41.95314  ? 247 LEU   A CA     1 
ATOM   1893 C C      . LEU   A 1 254 ? 31.49365  -18.24205 -8.05260  1.000 36.64032  ? 247 LEU   A C      1 
ATOM   1894 O O      . LEU   A 1 254 ? 30.84122  -19.28448 -7.92583  1.000 34.47753  ? 247 LEU   A O      1 
ATOM   1895 C CB     . LEU   A 1 254 ? 32.82765  -18.19254 -10.17670 1.000 48.06494  ? 247 LEU   A CB     1 
ATOM   1896 C CG     . LEU   A 1 254 ? 32.98624  -17.71607 -11.62248 1.000 53.87601  ? 247 LEU   A CG     1 
ATOM   1897 C CD1    . LEU   A 1 254 ? 34.38231  -18.01564 -12.15132 1.000 46.08374  ? 247 LEU   A CD1    1 
ATOM   1898 C CD2    . LEU   A 1 254 ? 31.92292  -18.34476 -12.51044 1.000 46.57793  ? 247 LEU   A CD2    1 
ATOM   1899 N N      . LYS   A 1 255 ? 32.08832  -17.64264 -7.01752  1.000 40.35572  ? 248 LYS   A N      1 
ATOM   1900 C CA     . LYS   A 1 255 ? 31.94151  -18.18289 -5.66941  1.000 41.89976  ? 248 LYS   A CA     1 
ATOM   1901 C C      . LYS   A 1 255 ? 30.48319  -18.18091 -5.23077  1.000 41.67944  ? 248 LYS   A C      1 
ATOM   1902 O O      . LYS   A 1 255 ? 30.01681  -19.13083 -4.59099  1.000 45.02545  ? 248 LYS   A O      1 
ATOM   1903 C CB     . LYS   A 1 255 ? 32.78893  -17.38002 -4.68263  1.000 40.99152  ? 248 LYS   A CB     1 
ATOM   1904 C CG     . LYS   A 1 255 ? 34.27785  -17.38283 -4.97651  1.000 46.61108  ? 248 LYS   A CG     1 
ATOM   1905 C CD     . LYS   A 1 255 ? 34.91342  -16.06002 -4.57400  1.000 55.13438  ? 248 LYS   A CD     1 
ATOM   1906 C CE     . LYS   A 1 255 ? 34.66422  -15.74966 -3.10519  1.000 43.20664  ? 248 LYS   A CE     1 
ATOM   1907 N NZ     . LYS   A 1 255 ? 35.61318  -16.47038 -2.21283  1.000 55.27183  ? 248 LYS   A NZ     1 
ATOM   1908 N N      . LYS   A 1 256 ? 29.74719  -17.11968 -5.56563  1.000 41.44192  ? 249 LYS   A N      1 
ATOM   1909 C CA     . LYS   A 1 256 ? 28.36759  -16.97567 -5.11910  1.000 40.45073  ? 249 LYS   A CA     1 
ATOM   1910 C C      . LYS   A 1 256 ? 27.40441  -17.90764 -5.84095  1.000 34.98600  ? 249 LYS   A C      1 
ATOM   1911 O O      . LYS   A 1 256 ? 26.24626  -18.01130 -5.42329  1.000 43.66889  ? 249 LYS   A O      1 
ATOM   1912 C CB     . LYS   A 1 256 ? 27.91054  -15.52734 -5.29926  1.000 43.40135  ? 249 LYS   A CB     1 
ATOM   1913 C CG     . LYS   A 1 256 ? 28.79836  -14.50622 -4.60959  1.000 32.56388  ? 249 LYS   A CG     1 
ATOM   1914 C CD     . LYS   A 1 256 ? 28.20936  -13.11019 -4.71732  1.000 43.07734  ? 249 LYS   A CD     1 
ATOM   1915 C CE     . LYS   A 1 256 ? 29.19375  -12.05431 -4.24501  1.000 41.76363  ? 249 LYS   A CE     1 
ATOM   1916 N NZ     . LYS   A 1 256 ? 28.59165  -10.69256 -4.26674  1.000 48.60787  ? 249 LYS   A NZ     1 
ATOM   1917 N N      . ILE   A 1 257 ? 27.84060  -18.57780 -6.90268  1.000 32.46787  ? 250 ILE   A N      1 
ATOM   1918 C CA     . ILE   A 1 257 ? 26.97208  -19.49286 -7.63604  1.000 39.70348  ? 250 ILE   A CA     1 
ATOM   1919 C C      . ILE   A 1 257 ? 26.99645  -20.84857 -6.94205  1.000 38.87962  ? 250 ILE   A C      1 
ATOM   1920 O O      . ILE   A 1 257 ? 28.04784  -21.49066 -6.84582  1.000 45.04090  ? 250 ILE   A O      1 
ATOM   1921 C CB     . ILE   A 1 257 ? 27.40315  -19.61386 -9.10445  1.000 37.44848  ? 250 ILE   A CB     1 
ATOM   1922 C CG1    . ILE   A 1 257 ? 27.34235  -18.24863 -9.79238  1.000 37.14136  ? 250 ILE   A CG1    1 
ATOM   1923 C CG2    . ILE   A 1 257 ? 26.52251  -20.61575 -9.83694  1.000 28.34773  ? 250 ILE   A CG2    1 
ATOM   1924 C CD1    . ILE   A 1 257 ? 27.88125  -18.25327 -11.20687 1.000 28.04652  ? 250 ILE   A CD1    1 
ATOM   1925 N N      . SER   A 1 258 ? 25.83566  -21.28455 -6.45111  1.000 40.72220  ? 251 SER   A N      1 
ATOM   1926 C CA     . SER   A 1 258 ? 25.75858  -22.57459 -5.77517  1.000 48.52256  ? 251 SER   A CA     1 
ATOM   1927 C C      . SER   A 1 258 ? 25.60357  -23.71962 -6.76864  1.000 46.38789  ? 251 SER   A C      1 
ATOM   1928 O O      . SER   A 1 258 ? 26.24640  -24.76468 -6.61853  1.000 42.56906  ? 251 SER   A O      1 
ATOM   1929 C CB     . SER   A 1 258 ? 24.60199  -22.57662 -4.77584  1.000 45.06973  ? 251 SER   A CB     1 
ATOM   1930 O OG     . SER   A 1 258 ? 24.53384  -23.81178 -4.08590  1.000 49.40536  ? 251 SER   A OG     1 
ATOM   1931 N N      . SER   A 1 259 ? 24.76199  -23.54019 -7.78472  1.000 41.77046  ? 252 SER   A N      1 
ATOM   1932 C CA     . SER   A 1 259 ? 24.53970  -24.58332 -8.77801  1.000 52.01609  ? 252 SER   A CA     1 
ATOM   1933 C C      . SER   A 1 259 ? 25.85321  -24.97509 -9.44236  1.000 58.49272  ? 252 SER   A C      1 
ATOM   1934 O O      . SER   A 1 259 ? 26.49478  -24.15298 -10.10422 1.000 51.82713  ? 252 SER   A O      1 
ATOM   1935 C CB     . SER   A 1 259 ? 23.53508  -24.10191 -9.82348  1.000 45.59839  ? 252 SER   A CB     1 
ATOM   1936 O OG     . SER   A 1 259 ? 23.44356  -25.01593 -10.90225 1.000 52.94716  ? 252 SER   A OG     1 
ATOM   1937 N N      . GLU   A 1 260 ? 26.25219  -26.23735 -9.26755  1.000 49.70193  ? 253 GLU   A N      1 
ATOM   1938 C CA     . GLU   A 1 260 ? 27.50409  -26.69693 -9.85998  1.000 58.61361  ? 253 GLU   A CA     1 
ATOM   1939 C C      . GLU   A 1 260 ? 27.40309  -26.77994 -11.37837 1.000 61.04715  ? 253 GLU   A C      1 
ATOM   1940 O O      . GLU   A 1 260 ? 28.34406  -26.40503 -12.08797 1.000 61.05832  ? 253 GLU   A O      1 
ATOM   1941 C CB     . GLU   A 1 260 ? 27.90341  -28.04974 -9.27127  1.000 61.88615  ? 253 GLU   A CB     1 
ATOM   1942 C CG     . GLU   A 1 260 ? 29.37573  -28.38517 -9.45850  1.000 64.46805  ? 253 GLU   A CG     1 
ATOM   1943 C CD     . GLU   A 1 260 ? 29.97436  -29.09266 -8.25991  1.000 72.49225  ? 253 GLU   A CD     1 
ATOM   1944 O OE1    . GLU   A 1 260 ? 29.54166  -30.22480 -7.96138  1.000 81.63560  ? 253 GLU   A OE1    1 
ATOM   1945 O OE2    . GLU   A 1 260 ? 30.87815  -28.51644 -7.61643  1.000 74.39870  ? 253 GLU   A OE2    1 
ATOM   1946 N N      . SER   A 1 261 ? 26.27526  -27.27280 -11.89804 1.000 56.35799  ? 254 SER   A N      1 
ATOM   1947 C CA     . SER   A 1 261 ? 26.10085  -27.31831 -13.34668 1.000 46.95839  ? 254 SER   A CA     1 
ATOM   1948 C C      . SER   A 1 261 ? 26.16781  -25.92159 -13.94736 1.000 48.70253  ? 254 SER   A C      1 
ATOM   1949 O O      . SER   A 1 261 ? 26.73140  -25.72963 -15.03117 1.000 53.28056  ? 254 SER   A O      1 
ATOM   1950 C CB     . SER   A 1 261 ? 24.77653  -27.99267 -13.70512 1.000 57.57369  ? 254 SER   A CB     1 
ATOM   1951 O OG     . SER   A 1 261 ? 24.82798  -29.38527 -13.44965 1.000 57.88408  ? 254 SER   A OG     1 
ATOM   1952 N N      . ALA   A 1 262 ? 25.59589  -24.93200 -13.25845 1.000 51.39991  ? 255 ALA   A N      1 
ATOM   1953 C CA     . ALA   A 1 262 ? 25.72120  -23.55058 -13.71053 1.000 47.97039  ? 255 ALA   A CA     1 
ATOM   1954 C C      . ALA   A 1 262 ? 27.17833  -23.10698 -13.69614 1.000 44.97651  ? 255 ALA   A C      1 
ATOM   1955 O O      . ALA   A 1 262 ? 27.69701  -22.59995 -14.69754 1.000 53.59881  ? 255 ALA   A O      1 
ATOM   1956 C CB     . ALA   A 1 262 ? 24.86503  -22.63241 -12.83784 1.000 48.66071  ? 255 ALA   A CB     1 
ATOM   1957 N N      . ARG   A 1 263 ? 27.85571  -23.29167 -12.56102 1.000 45.82593  ? 256 ARG   A N      1 
ATOM   1958 C CA     . ARG   A 1 263 ? 29.27818  -22.97605 -12.48255 1.000 55.77744  ? 256 ARG   A CA     1 
ATOM   1959 C C      . ARG   A 1 263 ? 30.06032  -23.71089 -13.56312 1.000 51.68505  ? 256 ARG   A C      1 
ATOM   1960 O O      . ARG   A 1 263 ? 30.85445  -23.10755 -14.29406 1.000 51.84670  ? 256 ARG   A O      1 
ATOM   1961 C CB     . ARG   A 1 263 ? 29.81887  -23.33567 -11.09733 1.000 59.69605  ? 256 ARG   A CB     1 
ATOM   1962 C CG     . ARG   A 1 263 ? 29.70558  -22.23380 -10.05671 1.000 45.67239  ? 256 ARG   A CG     1 
ATOM   1963 C CD     . ARG   A 1 263 ? 30.69907  -22.45762 -8.92424  1.000 41.19606  ? 256 ARG   A CD     1 
ATOM   1964 N NE     . ARG   A 1 263 ? 30.99425  -23.87310 -8.73311  1.000 50.88937  ? 256 ARG   A NE     1 
ATOM   1965 C CZ     . ARG   A 1 263 ? 30.26445  -24.69842 -7.99536  1.000 49.69633  ? 256 ARG   A CZ     1 
ATOM   1966 N NH1    . ARG   A 1 263 ? 30.56874  -25.98122 -7.88706  1.000 61.67249  ? 256 ARG   A NH1    1 
ATOM   1967 N NH2    . ARG   A 1 263 ? 29.20484  -24.22400 -7.34701  1.000 51.64411  ? 256 ARG   A NH2    1 
ATOM   1968 N N      . ASN   A 1 264 ? 29.84245  -25.02264 -13.67919 1.000 56.86859  ? 257 ASN   A N      1 
ATOM   1969 C CA     . ASN   A 1 264 ? 30.60272  -25.81939 -14.63587 1.000 61.07274  ? 257 ASN   A CA     1 
ATOM   1970 C C      . ASN   A 1 264 ? 30.42539  -25.30179 -16.05697 1.000 56.84194  ? 257 ASN   A C      1 
ATOM   1971 O O      . ASN   A 1 264 ? 31.38995  -25.24557 -16.82846 1.000 63.09131  ? 257 ASN   A O      1 
ATOM   1972 C CB     . ASN   A 1 264 ? 30.18556  -27.28669 -14.54298 1.000 62.84290  ? 257 ASN   A CB     1 
ATOM   1973 C CG     . ASN   A 1 264 ? 31.04805  -28.07614 -13.57887 1.000 63.71760  ? 257 ASN   A CG     1 
ATOM   1974 O OD1    . ASN   A 1 264 ? 30.98274  -27.87875 -12.36533 1.000 73.06162  ? 257 ASN   A OD1    1 
ATOM   1975 N ND2    . ASN   A 1 264 ? 31.86464  -28.97566 -14.11508 1.000 63.10978  ? 257 ASN   A ND2    1 
ATOM   1976 N N      . TYR   A 1 265 ? 29.20108  -24.91815 -16.42492 1.000 54.75725  ? 258 TYR   A N      1 
ATOM   1977 C CA     . TYR   A 1 265 ? 28.96861  -24.45637 -17.78922 1.000 55.18301  ? 258 TYR   A CA     1 
ATOM   1978 C C      . TYR   A 1 265 ? 29.53768  -23.05991 -18.00807 1.000 56.85447  ? 258 TYR   A C      1 
ATOM   1979 O O      . TYR   A 1 265 ? 30.09558  -22.77243 -19.07364 1.000 60.61517  ? 258 TYR   A O      1 
ATOM   1980 C CB     . TYR   A 1 265 ? 27.47730  -24.48599 -18.11810 1.000 49.60422  ? 258 TYR   A CB     1 
ATOM   1981 C CG     . TYR   A 1 265 ? 27.20366  -24.28772 -19.59049 1.000 56.46177  ? 258 TYR   A CG     1 
ATOM   1982 C CD1    . TYR   A 1 265 ? 27.26819  -25.35385 -20.47781 1.000 45.34420  ? 258 TYR   A CD1    1 
ATOM   1983 C CD2    . TYR   A 1 265 ? 26.90148  -23.03116 -20.09698 1.000 52.92017  ? 258 TYR   A CD2    1 
ATOM   1984 C CE1    . TYR   A 1 265 ? 27.02822  -25.17574 -21.82704 1.000 50.89808  ? 258 TYR   A CE1    1 
ATOM   1985 C CE2    . TYR   A 1 265 ? 26.65979  -22.84326 -21.44405 1.000 55.01580  ? 258 TYR   A CE2    1 
ATOM   1986 C CZ     . TYR   A 1 265 ? 26.72447  -23.91846 -22.30465 1.000 62.01799  ? 258 TYR   A CZ     1 
ATOM   1987 O OH     . TYR   A 1 265 ? 26.48453  -23.73638 -23.64733 1.000 62.21839  ? 258 TYR   A OH     1 
ATOM   1988 N N      . ILE   A 1 266 ? 29.40274  -22.17593 -17.01791 1.000 52.56460  ? 259 ILE   A N      1 
ATOM   1989 C CA     . ILE   A 1 266 ? 29.99395  -20.84520 -17.13283 1.000 53.66301  ? 259 ILE   A CA     1 
ATOM   1990 C C      . ILE   A 1 266 ? 31.51293  -20.94806 -17.19070 1.000 56.44565  ? 259 ILE   A C      1 
ATOM   1991 O O      . ILE   A 1 266 ? 32.16667  -20.31409 -18.02768 1.000 58.79331  ? 259 ILE   A O      1 
ATOM   1992 C CB     . ILE   A 1 266 ? 29.53316  -19.94696 -15.97095 1.000 56.21488  ? 259 ILE   A CB     1 
ATOM   1993 C CG1    . ILE   A 1 266 ? 28.01531  -19.76034 -16.00752 1.000 55.53785  ? 259 ILE   A CG1    1 
ATOM   1994 C CG2    . ILE   A 1 266 ? 30.23826  -18.60003 -16.02799 1.000 51.18693  ? 259 ILE   A CG2    1 
ATOM   1995 C CD1    . ILE   A 1 266 ? 27.45765  -19.06815 -14.78256 1.000 51.42618  ? 259 ILE   A CD1    1 
ATOM   1996 N N      . GLN   A 1 267 ? 32.09686  -21.75673 -16.30287 1.000 49.72065  ? 260 GLN   A N      1 
ATOM   1997 C CA     . GLN   A 1 267 ? 33.54858  -21.90624 -16.28147 1.000 60.91247  ? 260 GLN   A CA     1 
ATOM   1998 C C      . GLN   A 1 267 ? 34.05489  -22.60497 -17.53719 1.000 68.02578  ? 260 GLN   A C      1 
ATOM   1999 O O      . GLN   A 1 267 ? 35.08831  -22.21813 -18.09559 1.000 72.83766  ? 260 GLN   A O      1 
ATOM   2000 C CB     . GLN   A 1 267 ? 33.98143  -22.68025 -15.03608 1.000 54.31802  ? 260 GLN   A CB     1 
ATOM   2001 C CG     . GLN   A 1 267 ? 33.54723  -22.06277 -13.71883 1.000 43.25443  ? 260 GLN   A CG     1 
ATOM   2002 C CD     . GLN   A 1 267 ? 34.10292  -22.81099 -12.52236 1.000 50.81100  ? 260 GLN   A CD     1 
ATOM   2003 O OE1    . GLN   A 1 267 ? 33.36946  -23.48950 -11.80350 1.000 55.42517  ? 260 GLN   A OE1    1 
ATOM   2004 N NE2    . GLN   A 1 267 ? 35.40798  -22.69423 -12.30605 1.000 47.32218  ? 260 GLN   A NE2    1 
ATOM   2005 N N      . SER   A 1 268 ? 33.34502  -23.63888 -17.99339 1.000 64.80261  ? 261 SER   A N      1 
ATOM   2006 C CA     . SER   A 1 268 ? 33.79945  -24.42124 -19.13591 1.000 67.08228  ? 261 SER   A CA     1 
ATOM   2007 C C      . SER   A 1 268 ? 33.74587  -23.64721 -20.44529 1.000 65.08788  ? 261 SER   A C      1 
ATOM   2008 O O      . SER   A 1 268 ? 34.29943  -24.11947 -21.44405 1.000 80.32261  ? 261 SER   A O      1 
ATOM   2009 C CB     . SER   A 1 268 ? 32.97201  -25.70171 -19.25639 1.000 67.33614  ? 261 SER   A CB     1 
ATOM   2010 O OG     . SER   A 1 268 ? 33.39224  -26.66655 -18.30695 1.000 60.60821  ? 261 SER   A OG     1 
ATOM   2011 N N      . LEU   A 1 269 ? 33.09794  -22.48607 -20.47166 1.000 75.82711  ? 262 LEU   A N      1 
ATOM   2012 C CA     . LEU   A 1 269 ? 33.09919  -21.67178 -21.67564 1.000 78.65089  ? 262 LEU   A CA     1 
ATOM   2013 C C      . LEU   A 1 269 ? 34.52318  -21.23571 -22.01499 1.000 88.52059  ? 262 LEU   A C      1 
ATOM   2014 O O      . LEU   A 1 269 ? 35.41788  -21.21744 -21.16546 1.000 89.31028  ? 262 LEU   A O      1 
ATOM   2015 C CB     . LEU   A 1 269 ? 32.19273  -20.45233 -21.50137 1.000 73.70913  ? 262 LEU   A CB     1 
ATOM   2016 C CG     . LEU   A 1 269 ? 30.68630  -20.71915 -21.58161 1.000 76.47246  ? 262 LEU   A CG     1 
ATOM   2017 C CD1    . LEU   A 1 269 ? 29.89574  -19.62906 -20.87253 1.000 66.91834  ? 262 LEU   A CD1    1 
ATOM   2018 C CD2    . LEU   A 1 269 ? 30.23593  -20.85468 -23.03136 1.000 74.32182  ? 262 LEU   A CD2    1 
ATOM   2019 N N      . ALA   A 1 270 ? 34.72807  -20.88211 -23.28606 1.000 99.02208  ? 263 ALA   A N      1 
ATOM   2020 C CA     . ALA   A 1 270 ? 36.06072  -20.51740 -23.75555 1.000 101.05099 ? 263 ALA   A CA     1 
ATOM   2021 C C      . ALA   A 1 270 ? 36.60584  -19.27232 -23.06723 1.000 97.20616  ? 263 ALA   A C      1 
ATOM   2022 O O      . ALA   A 1 270 ? 37.81939  -19.03775 -23.11047 1.000 107.16685 ? 263 ALA   A O      1 
ATOM   2023 C CB     . ALA   A 1 270 ? 36.04026  -20.30845 -25.27012 1.000 111.58566 ? 263 ALA   A CB     1 
ATOM   2024 N N      . GLN   A 1 271 ? 35.74011  -18.47064 -22.44418 1.000 95.01640  ? 264 GLN   A N      1 
ATOM   2025 C CA     . GLN   A 1 271 ? 36.14860  -17.25726 -21.74378 1.000 97.39682  ? 264 GLN   A CA     1 
ATOM   2026 C C      . GLN   A 1 271 ? 36.41472  -16.11982 -22.72272 1.000 93.46324  ? 264 GLN   A C      1 
ATOM   2027 O O      . GLN   A 1 271 ? 37.11240  -16.30548 -23.72508 1.000 91.34756  ? 264 GLN   A O      1 
ATOM   2028 C CB     . GLN   A 1 271 ? 37.38804  -17.52267 -20.88401 1.000 87.97137  ? 264 GLN   A CB     1 
ATOM   2029 C CG     . GLN   A 1 271 ? 37.55289  -16.57085 -19.71093 1.000 94.63714  ? 264 GLN   A CG     1 
ATOM   2030 C CD     . GLN   A 1 271 ? 38.36313  -15.33698 -20.06705 1.000 96.67319  ? 264 GLN   A CD     1 
ATOM   2031 O OE1    . GLN   A 1 271 ? 38.59556  -15.05069 -21.24141 1.000 99.86850  ? 264 GLN   A OE1    1 
ATOM   2032 N NE2    . GLN   A 1 271 ? 38.79763  -14.59896 -19.05062 1.000 89.57982  ? 264 GLN   A NE2    1 
ATOM   2033 N N      . MET   A 1 272 ? 35.86618  -14.94187 -22.43864 1.000 84.83518  ? 265 MET   A N      1 
ATOM   2034 C CA     . MET   A 1 272 ? 36.04335  -13.75970 -23.26756 1.000 83.18603  ? 265 MET   A CA     1 
ATOM   2035 C C      . MET   A 1 272 ? 36.27677  -12.54797 -22.37931 1.000 77.94987  ? 265 MET   A C      1 
ATOM   2036 O O      . MET   A 1 272 ? 35.77128  -12.49285 -21.25149 1.000 69.91411  ? 265 MET   A O      1 
ATOM   2037 C CB     . MET   A 1 272 ? 34.82431  -13.50102 -24.16786 1.000 88.61130  ? 265 MET   A CB     1 
ATOM   2038 C CG     . MET   A 1 272 ? 34.20636  -14.75173 -24.76642 1.000 97.78372  ? 265 MET   A CG     1 
ATOM   2039 S SD     . MET   A 1 272 ? 33.03341  -15.54470 -23.65092 1.000 100.80761 ? 265 MET   A SD     1 
ATOM   2040 C CE     . MET   A 1 272 ? 31.47606  -14.99573 -24.34571 1.000 72.29041  ? 265 MET   A CE     1 
ATOM   2041 N N      . PRO   A 1 273 ? 37.03310  -11.56620 -22.85869 1.000 80.15573  ? 266 PRO   A N      1 
ATOM   2042 C CA     . PRO   A 1 273 ? 37.25388  -10.34827 -22.07651 1.000 74.10989  ? 266 PRO   A CA     1 
ATOM   2043 C C      . PRO   A 1 273 ? 36.08457  -9.38122  -22.19324 1.000 75.04748  ? 266 PRO   A C      1 
ATOM   2044 O O      . PRO   A 1 273 ? 35.29097  -9.42272  -23.13540 1.000 75.27123  ? 266 PRO   A O      1 
ATOM   2045 C CB     . PRO   A 1 273 ? 38.51751  -9.75543  -22.70728 1.000 76.60096  ? 266 PRO   A CB     1 
ATOM   2046 C CG     . PRO   A 1 273 ? 38.43678  -10.18873 -24.13387 1.000 76.07617  ? 266 PRO   A CG     1 
ATOM   2047 C CD     . PRO   A 1 273 ? 37.79008  -11.55656 -24.12355 1.000 82.66327  ? 266 PRO   A CD     1 
ATOM   2048 N N      . LYS   A 1 274 ? 35.99324  -8.49510  -21.20475 1.000 72.06631  ? 267 LYS   A N      1 
ATOM   2049 C CA     . LYS   A 1 274 ? 34.98959  -7.44108  -21.24332 1.000 57.32403  ? 267 LYS   A CA     1 
ATOM   2050 C C      . LYS   A 1 274 ? 35.31031  -6.46325  -22.36566 1.000 65.00950  ? 267 LYS   A C      1 
ATOM   2051 O O      . LYS   A 1 274 ? 36.43542  -5.96389  -22.46675 1.000 76.60109  ? 267 LYS   A O      1 
ATOM   2052 C CB     . LYS   A 1 274 ? 34.92933  -6.70605  -19.90488 1.000 58.08849  ? 267 LYS   A CB     1 
ATOM   2053 C CG     . LYS   A 1 274 ? 34.08167  -5.43821  -19.93608 1.000 65.24067  ? 267 LYS   A CG     1 
ATOM   2054 C CD     . LYS   A 1 274 ? 34.18987  -4.65709  -18.63455 1.000 53.26053  ? 267 LYS   A CD     1 
ATOM   2055 C CE     . LYS   A 1 274 ? 33.08659  -3.61327  -18.51814 1.000 61.57208  ? 267 LYS   A CE     1 
ATOM   2056 N NZ     . LYS   A 1 274 ? 33.35713  -2.41237  -19.35807 1.000 69.05795  ? 267 LYS   A NZ     1 
ATOM   2057 N N      . MET   A 1 275 ? 34.32436  -6.19751  -23.21525 1.000 62.11007  ? 268 MET   A N      1 
ATOM   2058 C CA     . MET   A 1 275 ? 34.50084  -5.23149  -24.28684 1.000 59.45343  ? 268 MET   A CA     1 
ATOM   2059 C C      . MET   A 1 275 ? 34.40724  -3.81320  -23.73949 1.000 54.75399  ? 268 MET   A C      1 
ATOM   2060 O O      . MET   A 1 275 ? 33.75665  -3.55764  -22.72259 1.000 66.14282  ? 268 MET   A O      1 
ATOM   2061 C CB     . MET   A 1 275 ? 33.45304  -5.44089  -25.38080 1.000 58.57656  ? 268 MET   A CB     1 
ATOM   2062 C CG     . MET   A 1 275 ? 33.15728  -6.90022  -25.68680 1.000 59.70005  ? 268 MET   A CG     1 
ATOM   2063 S SD     . MET   A 1 275 ? 32.67664  -7.17266  -27.40377 1.000 72.85392  ? 268 MET   A SD     1 
ATOM   2064 C CE     . MET   A 1 275 ? 30.99706  -6.54901  -27.39080 1.000 54.68069  ? 268 MET   A CE     1 
ATOM   2065 N N      . ASN   A 1 276 ? 35.07423  -2.88705  -24.42165 1.000 74.85826  ? 269 ASN   A N      1 
ATOM   2066 C CA     . ASN   A 1 276 ? 35.01881  -1.48197  -24.04074 1.000 75.63957  ? 269 ASN   A CA     1 
ATOM   2067 C C      . ASN   A 1 276 ? 33.74601  -0.86149  -24.60133 1.000 53.05163  ? 269 ASN   A C      1 
ATOM   2068 O O      . ASN   A 1 276 ? 33.57576  -0.77583  -25.82229 1.000 58.01053  ? 269 ASN   A O      1 
ATOM   2069 C CB     . ASN   A 1 276 ? 36.25301  -0.73580  -24.54184 1.000 73.39816  ? 269 ASN   A CB     1 
ATOM   2070 C CG     . ASN   A 1 276 ? 36.55780  0.50032   -23.71644 1.000 84.83669  ? 269 ASN   A CG     1 
ATOM   2071 O OD1    . ASN   A 1 276 ? 35.93676  0.73664   -22.68006 1.000 85.43199  ? 269 ASN   A OD1    1 
ATOM   2072 N ND2    . ASN   A 1 276 ? 37.51731  1.29662   -24.17334 1.000 81.59304  ? 269 ASN   A ND2    1 
ATOM   2073 N N      . PHE   A 1 277 ? 32.85107  -0.43279  -23.70832 1.000 62.92719  ? 270 PHE   A N      1 
ATOM   2074 C CA     . PHE   A 1 277 ? 31.58369  0.13939   -24.14997 1.000 59.85489  ? 270 PHE   A CA     1 
ATOM   2075 C C      . PHE   A 1 277 ? 31.79945  1.31739   -25.08963 1.000 54.85537  ? 270 PHE   A C      1 
ATOM   2076 O O      . PHE   A 1 277 ? 30.98384  1.55129   -25.98929 1.000 52.29269  ? 270 PHE   A O      1 
ATOM   2077 C CB     . PHE   A 1 277 ? 30.74913  0.56726   -22.94216 1.000 46.12603  ? 270 PHE   A CB     1 
ATOM   2078 C CG     . PHE   A 1 277 ? 30.12893  -0.58012  -22.19142 1.000 57.77753  ? 270 PHE   A CG     1 
ATOM   2079 C CD1    . PHE   A 1 277 ? 30.76742  -1.80762  -22.11572 1.000 57.57132  ? 270 PHE   A CD1    1 
ATOM   2080 C CD2    . PHE   A 1 277 ? 28.90605  -0.42895  -21.55909 1.000 45.30459  ? 270 PHE   A CD2    1 
ATOM   2081 C CE1    . PHE   A 1 277 ? 30.19982  -2.86013  -21.42608 1.000 53.05211  ? 270 PHE   A CE1    1 
ATOM   2082 C CE2    . PHE   A 1 277 ? 28.33335  -1.47890  -20.86664 1.000 45.48955  ? 270 PHE   A CE2    1 
ATOM   2083 C CZ     . PHE   A 1 277 ? 28.98122  -2.69597  -20.80069 1.000 47.46517  ? 270 PHE   A CZ     1 
ATOM   2084 N N      . ALA   A 1 278 ? 32.88755  2.06793   -24.89995 1.000 54.41274  ? 271 ALA   A N      1 
ATOM   2085 C CA     . ALA   A 1 278 ? 33.18414  3.17532   -25.80130 1.000 58.71889  ? 271 ALA   A CA     1 
ATOM   2086 C C      . ALA   A 1 278 ? 33.25921  2.71202   -27.24975 1.000 67.30038  ? 271 ALA   A C      1 
ATOM   2087 O O      . ALA   A 1 278 ? 32.88871  3.46102   -28.16064 1.000 67.46476  ? 271 ALA   A O      1 
ATOM   2088 C CB     . ALA   A 1 278 ? 34.49110  3.85300   -25.38917 1.000 55.05491  ? 271 ALA   A CB     1 
ATOM   2089 N N      . ASN   A 1 279 ? 33.72789  1.48456   -27.48302 1.000 68.58941  ? 272 ASN   A N      1 
ATOM   2090 C CA     . ASN   A 1 279 ? 33.80514  0.95936   -28.84181 1.000 66.11597  ? 272 ASN   A CA     1 
ATOM   2091 C C      . ASN   A 1 279 ? 32.43856  0.50544   -29.34199 1.000 65.92982  ? 272 ASN   A C      1 
ATOM   2092 O O      . ASN   A 1 279 ? 31.99962  0.90882   -30.42484 1.000 63.48422  ? 272 ASN   A O      1 
ATOM   2093 C CB     . ASN   A 1 279 ? 34.80447  -0.19769  -28.90242 1.000 68.09461  ? 272 ASN   A CB     1 
ATOM   2094 C CG     . ASN   A 1 279 ? 36.23444  0.27392   -29.06608 1.000 60.20638  ? 272 ASN   A CG     1 
ATOM   2095 O OD1    . ASN   A 1 279 ? 36.61527  1.32735   -28.55663 1.000 73.95270  ? 272 ASN   A OD1    1 
ATOM   2096 N ND2    . ASN   A 1 279 ? 37.03609  -0.50670  -29.78165 1.000 76.15572  ? 272 ASN   A ND2    1 
ATOM   2097 N N      . VAL   A 1 280 ? 31.75102  -0.33279  -28.56272 1.000 56.00821  ? 273 VAL   A N      1 
ATOM   2098 C CA     . VAL   A 1 280 ? 30.48314  -0.89428  -29.01775 1.000 58.38129  ? 273 VAL   A CA     1 
ATOM   2099 C C      . VAL   A 1 280 ? 29.42629  0.19099   -29.17758 1.000 53.70550  ? 273 VAL   A C      1 
ATOM   2100 O O      . VAL   A 1 280 ? 28.55053  0.08837   -30.04531 1.000 48.88594  ? 273 VAL   A O      1 
ATOM   2101 C CB     . VAL   A 1 280 ? 30.01574  -2.00262  -28.05565 1.000 55.35176  ? 273 VAL   A CB     1 
ATOM   2102 C CG1    . VAL   A 1 280 ? 29.87880  -1.45925  -26.64366 1.000 56.71897  ? 273 VAL   A CG1    1 
ATOM   2103 C CG2    . VAL   A 1 280 ? 28.70167  -2.60185  -28.53344 1.000 49.01899  ? 273 VAL   A CG2    1 
ATOM   2104 N N      . PHE   A 1 281 ? 29.48096  1.24037   -28.35711 1.000 52.25371  ? 274 PHE   A N      1 
ATOM   2105 C CA     . PHE   A 1 281 ? 28.53203  2.34491   -28.42983 1.000 58.73377  ? 274 PHE   A CA     1 
ATOM   2106 C C      . PHE   A 1 281 ? 29.17816  3.61982   -28.96809 1.000 63.87229  ? 274 PHE   A C      1 
ATOM   2107 O O      . PHE   A 1 281 ? 28.81711  4.72534   -28.55710 1.000 57.73655  ? 274 PHE   A O      1 
ATOM   2108 C CB     . PHE   A 1 281 ? 27.90424  2.60645   -27.06098 1.000 49.15938  ? 274 PHE   A CB     1 
ATOM   2109 C CG     . PHE   A 1 281 ? 27.24267  1.40074   -26.45398 1.000 56.79136  ? 274 PHE   A CG     1 
ATOM   2110 C CD1    . PHE   A 1 281 ? 26.02459  0.94567   -26.93190 1.000 46.32060  ? 274 PHE   A CD1    1 
ATOM   2111 C CD2    . PHE   A 1 281 ? 27.83723  0.72555   -25.40114 1.000 54.72442  ? 274 PHE   A CD2    1 
ATOM   2112 C CE1    . PHE   A 1 281 ? 25.41464  -0.16258  -26.37322 1.000 45.39442  ? 274 PHE   A CE1    1 
ATOM   2113 C CE2    . PHE   A 1 281 ? 27.23285  -0.38340  -24.83900 1.000 50.26380  ? 274 PHE   A CE2    1 
ATOM   2114 C CZ     . PHE   A 1 281 ? 26.01995  -0.82774  -25.32551 1.000 44.37603  ? 274 PHE   A CZ     1 
ATOM   2115 N N      . ILE   A 1 282 ? 30.13444  3.48069   -29.89066 1.000 58.58987  ? 275 ILE   A N      1 
ATOM   2116 C CA     . ILE   A 1 282 ? 30.79847  4.65199   -30.44527 1.000 62.07619  ? 275 ILE   A CA     1 
ATOM   2117 C C      . ILE   A 1 282 ? 29.77410  5.54929   -31.13334 1.000 63.97900  ? 275 ILE   A C      1 
ATOM   2118 O O      . ILE   A 1 282 ? 28.79700  5.07932   -31.73060 1.000 66.51154  ? 275 ILE   A O      1 
ATOM   2119 C CB     . ILE   A 1 282 ? 31.91634  4.24575   -31.42069 1.000 68.60520  ? 275 ILE   A CB     1 
ATOM   2120 C CG1    . ILE   A 1 282 ? 32.63478  5.48691   -31.95734 1.000 70.09475  ? 275 ILE   A CG1    1 
ATOM   2121 C CG2    . ILE   A 1 282 ? 31.35126  3.41810   -32.56453 1.000 64.83597  ? 275 ILE   A CG2    1 
ATOM   2122 C CD1    . ILE   A 1 282 ? 33.30178  6.32272   -30.88426 1.000 65.52580  ? 275 ILE   A CD1    1 
ATOM   2123 N N      . GLY   A 1 283 ? 30.00644  6.85902   -31.05307 1.000 59.06305  ? 276 GLY   A N      1 
ATOM   2124 C CA     . GLY   A 1 283 ? 29.07122  7.84261   -31.54281 1.000 51.58289  ? 276 GLY   A CA     1 
ATOM   2125 C C      . GLY   A 1 283 ? 28.05499  8.30895   -30.52293 1.000 57.68128  ? 276 GLY   A C      1 
ATOM   2126 O O      . GLY   A 1 283 ? 27.50973  9.40852   -30.66917 1.000 65.58133  ? 276 GLY   A O      1 
ATOM   2127 N N      . ALA   A 1 284 ? 27.78828  7.50884   -29.49535 1.000 52.24541  ? 277 ALA   A N      1 
ATOM   2128 C CA     . ALA   A 1 284 ? 26.85712  7.89465   -28.45023 1.000 55.36819  ? 277 ALA   A CA     1 
ATOM   2129 C C      . ALA   A 1 284 ? 27.49580  8.91059   -27.50775 1.000 45.51929  ? 277 ALA   A C      1 
ATOM   2130 O O      . ALA   A 1 284 ? 28.72038  9.03252   -27.41515 1.000 44.70374  ? 277 ALA   A O      1 
ATOM   2131 C CB     . ALA   A 1 284 ? 26.39365  6.66887   -27.66172 1.000 43.45597  ? 277 ALA   A CB     1 
ATOM   2132 N N      . ASN   A 1 285 ? 26.64091  9.64815   -26.80810 1.000 44.71848  ? 278 ASN   A N      1 
ATOM   2133 C CA     . ASN   A 1 285 ? 27.08098  10.59885  -25.80123 1.000 41.81664  ? 278 ASN   A CA     1 
ATOM   2134 C C      . ASN   A 1 285 ? 27.97671  9.89611   -24.78153 1.000 42.09494  ? 278 ASN   A C      1 
ATOM   2135 O O      . ASN   A 1 285 ? 27.54129  8.91692   -24.15662 1.000 48.27462  ? 278 ASN   A O      1 
ATOM   2136 C CB     . ASN   A 1 285 ? 25.86859  11.22018  -25.10830 1.000 41.26456  ? 278 ASN   A CB     1 
ATOM   2137 C CG     . ASN   A 1 285 ? 26.24254  12.33774  -24.14944 1.000 40.59105  ? 278 ASN   A CG     1 
ATOM   2138 O OD1    . ASN   A 1 285 ? 27.34375  12.36499  -23.60046 1.000 44.42622  ? 278 ASN   A OD1    1 
ATOM   2139 N ND2    . ASN   A 1 285 ? 25.31614  13.26599  -23.93933 1.000 39.94958  ? 278 ASN   A ND2    1 
ATOM   2140 N N      . PRO   A 1 286 ? 29.21689  10.34883  -24.59103 1.000 43.74403  ? 279 PRO   A N      1 
ATOM   2141 C CA     . PRO   A 1 286 ? 30.09138  9.68764   -23.60844 1.000 44.68808  ? 279 PRO   A CA     1 
ATOM   2142 C C      . PRO   A 1 286 ? 29.46657  9.57230   -22.23068 1.000 47.02610  ? 279 PRO   A C      1 
ATOM   2143 O O      . PRO   A 1 286 ? 29.72073  8.58919   -21.52233 1.000 42.61575  ? 279 PRO   A O      1 
ATOM   2144 C CB     . PRO   A 1 286 ? 31.33855  10.58226  -23.59492 1.000 46.29463  ? 279 PRO   A CB     1 
ATOM   2145 C CG     . PRO   A 1 286 ? 31.33506  11.25582  -24.92794 1.000 48.59106  ? 279 PRO   A CG     1 
ATOM   2146 C CD     . PRO   A 1 286 ? 29.89034  11.46517  -25.27635 1.000 45.40999  ? 279 PRO   A CD     1 
ATOM   2147 N N      . LEU   A 1 287 ? 28.65132  10.54866  -21.82542 1.000 44.87630  ? 280 LEU   A N      1 
ATOM   2148 C CA     . LEU   A 1 287 ? 27.96094  10.44137  -20.54542 1.000 40.56141  ? 280 LEU   A CA     1 
ATOM   2149 C C      . LEU   A 1 287 ? 26.95886  9.29422   -20.54735 1.000 41.99814  ? 280 LEU   A C      1 
ATOM   2150 O O      . LEU   A 1 287 ? 26.70723  8.69048   -19.49781 1.000 43.47515  ? 280 LEU   A O      1 
ATOM   2151 C CB     . LEU   A 1 287 ? 27.26833  11.76227  -20.21040 1.000 40.23227  ? 280 LEU   A CB     1 
ATOM   2152 C CG     . LEU   A 1 287 ? 28.20616  12.92440  -19.87503 1.000 44.82329  ? 280 LEU   A CG     1 
ATOM   2153 C CD1    . LEU   A 1 287 ? 27.41940  14.18969  -19.56560 1.000 41.82124  ? 280 LEU   A CD1    1 
ATOM   2154 C CD2    . LEU   A 1 287 ? 29.12019  12.55794  -18.71488 1.000 48.17602  ? 280 LEU   A CD2    1 
ATOM   2155 N N      . ALA   A 1 288 ? 26.38031  8.97797   -21.70891 1.000 38.40963  ? 281 ALA   A N      1 
ATOM   2156 C CA     . ALA   A 1 288 ? 25.50069  7.81806   -21.79931 1.000 39.28988  ? 281 ALA   A CA     1 
ATOM   2157 C C      . ALA   A 1 288 ? 26.29015  6.51609   -21.76365 1.000 37.81052  ? 281 ALA   A C      1 
ATOM   2158 O O      . ALA   A 1 288 ? 25.81108  5.51740   -21.21485 1.000 41.77951  ? 281 ALA   A O      1 
ATOM   2159 C CB     . ALA   A 1 288 ? 24.65417  7.89309   -23.06982 1.000 36.69907  ? 281 ALA   A CB     1 
ATOM   2160 N N      . VAL   A 1 289 ? 27.49523  6.50534   -22.33793 1.000 39.58767  ? 282 VAL   A N      1 
ATOM   2161 C CA     . VAL   A 1 289 ? 28.32773  5.30720   -22.28788 1.000 40.87977  ? 282 VAL   A CA     1 
ATOM   2162 C C      . VAL   A 1 289 ? 28.73458  5.00477   -20.85160 1.000 41.84040  ? 282 VAL   A C      1 
ATOM   2163 O O      . VAL   A 1 289 ? 28.70012  3.84957   -20.41019 1.000 40.43864  ? 282 VAL   A O      1 
ATOM   2164 C CB     . VAL   A 1 289 ? 29.55437  5.46744   -23.20528 1.000 42.79926  ? 282 VAL   A CB     1 
ATOM   2165 C CG1    . VAL   A 1 289 ? 30.38138  4.19189   -23.21270 1.000 44.11491  ? 282 VAL   A CG1    1 
ATOM   2166 C CG2    . VAL   A 1 289 ? 29.11589  5.83108   -24.61575 1.000 43.15233  ? 282 VAL   A CG2    1 
ATOM   2167 N N      . ASP   A 1 290 ? 29.12116  6.03663   -20.09746 1.000 41.64031  ? 283 ASP   A N      1 
ATOM   2168 C CA     . ASP   A 1 290 ? 29.47797  5.83060   -18.69779 1.000 41.12799  ? 283 ASP   A CA     1 
ATOM   2169 C C      . ASP   A 1 290 ? 28.29579  5.29314   -17.90211 1.000 39.30423  ? 283 ASP   A C      1 
ATOM   2170 O O      . ASP   A 1 290 ? 28.45577  4.39119   -17.07149 1.000 44.42945  ? 283 ASP   A O      1 
ATOM   2171 C CB     . ASP   A 1 290 ? 29.98677  7.13475   -18.08298 1.000 41.97357  ? 283 ASP   A CB     1 
ATOM   2172 C CG     . ASP   A 1 290 ? 30.69435  6.91695   -16.75753 1.000 46.24961  ? 283 ASP   A CG     1 
ATOM   2173 O OD1    . ASP   A 1 290 ? 31.86688  6.48689   -16.77175 1.000 53.86964  ? 283 ASP   A OD1    1 
ATOM   2174 O OD2    . ASP   A 1 290 ? 30.07803  7.17436   -15.70156 1.000 42.15120  ? 283 ASP   A OD2    1 
ATOM   2175 N N      . LEU   A 1 291 ? 27.09877  5.83511   -18.13893 1.000 40.14458  ? 284 LEU   A N      1 
ATOM   2176 C CA     . LEU   A 1 291 ? 25.92374  5.35194   -17.42106 1.000 42.36851  ? 284 LEU   A CA     1 
ATOM   2177 C C      . LEU   A 1 291 ? 25.63952  3.89306   -17.74987 1.000 37.35080  ? 284 LEU   A C      1 
ATOM   2178 O O      . LEU   A 1 291 ? 25.35736  3.09135   -16.85258 1.000 35.26437  ? 284 LEU   A O      1 
ATOM   2179 C CB     . LEU   A 1 291 ? 24.70675  6.21591   -17.74452 1.000 36.58360  ? 284 LEU   A CB     1 
ATOM   2180 C CG     . LEU   A 1 291 ? 23.39981  5.70967   -17.12928 1.000 45.02644  ? 284 LEU   A CG     1 
ATOM   2181 C CD1    . LEU   A 1 291 ? 23.55215  5.54711   -15.62277 1.000 33.35272  ? 284 LEU   A CD1    1 
ATOM   2182 C CD2    . LEU   A 1 291 ? 22.23518  6.63161   -17.46077 1.000 38.99007  ? 284 LEU   A CD2    1 
ATOM   2183 N N      . LEU   A 1 292 ? 25.70456  3.53012   -19.03367 1.000 36.73120  ? 285 LEU   A N      1 
ATOM   2184 C CA     . LEU   A 1 292 ? 25.48684  2.13942   -19.41794 1.000 38.41631  ? 285 LEU   A CA     1 
ATOM   2185 C C      . LEU   A 1 292 ? 26.45727  1.21230   -18.69818 1.000 45.39773  ? 285 LEU   A C      1 
ATOM   2186 O O      . LEU   A 1 292 ? 26.05998  0.15534   -18.19345 1.000 36.80324  ? 285 LEU   A O      1 
ATOM   2187 C CB     . LEU   A 1 292 ? 25.62272  1.98581   -20.93250 1.000 42.07298  ? 285 LEU   A CB     1 
ATOM   2188 C CG     . LEU   A 1 292 ? 24.45168  2.48278   -21.78195 1.000 38.51878  ? 285 LEU   A CG     1 
ATOM   2189 C CD1    . LEU   A 1 292 ? 24.69556  2.18490   -23.25403 1.000 36.83337  ? 285 LEU   A CD1    1 
ATOM   2190 C CD2    . LEU   A 1 292 ? 23.14412  1.86349   -21.31304 1.000 34.02226  ? 285 LEU   A CD2    1 
ATOM   2191 N N      . GLU   A 1 293 ? 27.73561  1.59498   -18.63400 1.000 42.34296  ? 286 GLU   A N      1 
ATOM   2192 C CA     . GLU   A 1 293 ? 28.72394  0.74801   -17.97531 1.000 45.39816  ? 286 GLU   A CA     1 
ATOM   2193 C C      . GLU   A 1 293 ? 28.38038  0.52051   -16.50876 1.000 43.69662  ? 286 GLU   A C      1 
ATOM   2194 O O      . GLU   A 1 293 ? 28.67360  -0.54931  -15.96279 1.000 41.27460  ? 286 GLU   A O      1 
ATOM   2195 C CB     . GLU   A 1 293 ? 30.11752  1.36247   -18.11405 1.000 47.87668  ? 286 GLU   A CB     1 
ATOM   2196 C CG     . GLU   A 1 293 ? 30.85155  0.92578   -19.37422 1.000 55.04474  ? 286 GLU   A CG     1 
ATOM   2197 C CD     . GLU   A 1 293 ? 32.27130  1.45084   -19.44491 1.000 64.75144  ? 286 GLU   A CD     1 
ATOM   2198 O OE1    . GLU   A 1 293 ? 33.21247  0.64123   -19.30747 1.000 74.44734  ? 286 GLU   A OE1    1 
ATOM   2199 O OE2    . GLU   A 1 293 ? 32.44745  2.67080   -19.64509 1.000 59.53140  ? 286 GLU   A OE2    1 
ATOM   2200 N N      . LYS   A 1 294 ? 27.75648  1.50378   -15.85778 1.000 43.09696  ? 287 LYS   A N      1 
ATOM   2201 C CA     . LYS   A 1 294 ? 27.34654  1.35829   -14.46660 1.000 38.80651  ? 287 LYS   A CA     1 
ATOM   2202 C C      . LYS   A 1 294 ? 26.04992  0.57537   -14.30669 1.000 40.02707  ? 287 LYS   A C      1 
ATOM   2203 O O      . LYS   A 1 294 ? 25.70431  0.20768   -13.17833 1.000 39.51564  ? 287 LYS   A O      1 
ATOM   2204 C CB     . LYS   A 1 294 ? 27.19307  2.73497   -13.81418 1.000 37.78785  ? 287 LYS   A CB     1 
ATOM   2205 C CG     . LYS   A 1 294 ? 28.39832  3.64598   -13.98550 1.000 39.46058  ? 287 LYS   A CG     1 
ATOM   2206 C CD     . LYS   A 1 294 ? 28.78439  4.29986   -12.66769 1.000 40.46967  ? 287 LYS   A CD     1 
ATOM   2207 C CE     . LYS   A 1 294 ? 29.55721  5.59105   -12.89159 1.000 48.04177  ? 287 LYS   A CE     1 
ATOM   2208 N NZ     . LYS   A 1 294 ? 30.72106  5.39629   -13.80003 1.000 43.10073  ? 287 LYS   A NZ     1 
ATOM   2209 N N      . MET   A 1 295 ? 25.32844  0.31471   -15.39602 1.000 39.20185  ? 288 MET   A N      1 
ATOM   2210 C CA     . MET   A 1 295 ? 24.07459  -0.42858  -15.35005 1.000 38.28988  ? 288 MET   A CA     1 
ATOM   2211 C C      . MET   A 1 295 ? 24.24221  -1.89925  -15.70295 1.000 36.63645  ? 288 MET   A C      1 
ATOM   2212 O O      . MET   A 1 295 ? 23.57086  -2.75151  -15.11360 1.000 37.53020  ? 288 MET   A O      1 
ATOM   2213 C CB     . MET   A 1 295 ? 23.04712  0.19909   -16.30050 1.000 32.72818  ? 288 MET   A CB     1 
ATOM   2214 C CG     . MET   A 1 295 ? 22.50695  1.54894   -15.85254 1.000 31.91049  ? 288 MET   A CG     1 
ATOM   2215 S SD     . MET   A 1 295 ? 21.24763  2.20002   -16.97239 1.000 36.37445  ? 288 MET   A SD     1 
ATOM   2216 C CE     . MET   A 1 295 ? 20.44975  3.41551   -15.92611 1.000 38.59936  ? 288 MET   A CE     1 
ATOM   2217 N N      . LEU   A 1 296 ? 25.12672  -2.21741  -16.64112 1.000 36.02777  ? 289 LEU   A N      1 
ATOM   2218 C CA     . LEU   A 1 296 ? 25.23910  -3.56900  -17.19237 1.000 36.89827  ? 289 LEU   A CA     1 
ATOM   2219 C C      . LEU   A 1 296 ? 26.43768  -4.31788  -16.62091 1.000 41.42546  ? 289 LEU   A C      1 
ATOM   2220 O O      . LEU   A 1 296 ? 27.29206  -4.81346  -17.35653 1.000 45.47783  ? 289 LEU   A O      1 
ATOM   2221 C CB     . LEU   A 1 296 ? 25.31079  -3.50367  -18.71352 1.000 37.43229  ? 289 LEU   A CB     1 
ATOM   2222 C CG     . LEU   A 1 296 ? 24.06740  -2.95493  -19.41862 1.000 37.61063  ? 289 LEU   A CG     1 
ATOM   2223 C CD1    . LEU   A 1 296 ? 24.31928  -2.78020  -20.90909 1.000 36.78439  ? 289 LEU   A CD1    1 
ATOM   2224 C CD2    . LEU   A 1 296 ? 22.86760  -3.85868  -19.17610 1.000 34.74655  ? 289 LEU   A CD2    1 
ATOM   2225 N N      . VAL   A 1 297 ? 26.51304  -4.41372  -15.29657 1.000 38.74886  ? 290 VAL   A N      1 
ATOM   2226 C CA     . VAL   A 1 297 ? 27.52042  -5.22350  -14.62036 1.000 43.00698  ? 290 VAL   A CA     1 
ATOM   2227 C C      . VAL   A 1 297 ? 26.85249  -6.49256  -14.11451 1.000 40.39771  ? 290 VAL   A C      1 
ATOM   2228 O O      . VAL   A 1 297 ? 25.69385  -6.46867  -13.67947 1.000 41.59806  ? 290 VAL   A O      1 
ATOM   2229 C CB     . VAL   A 1 297 ? 28.19043  -4.44885  -13.46887 1.000 43.87039  ? 290 VAL   A CB     1 
ATOM   2230 C CG1    . VAL   A 1 297 ? 28.82117  -3.16519  -13.98859 1.000 41.47777  ? 290 VAL   A CG1    1 
ATOM   2231 C CG2    . VAL   A 1 297 ? 27.18439  -4.15013  -12.36951 1.000 48.53328  ? 290 VAL   A CG2    1 
ATOM   2232 N N      . LEU   A 1 298 ? 27.58072  -7.60879  -14.17483 1.000 46.92400  ? 291 LEU   A N      1 
ATOM   2233 C CA     . LEU   A 1 298 ? 26.99079  -8.89084  -13.80237 1.000 42.48550  ? 291 LEU   A CA     1 
ATOM   2234 C C      . LEU   A 1 298 ? 26.57366  -8.90885  -12.33681 1.000 44.15862  ? 291 LEU   A C      1 
ATOM   2235 O O      . LEU   A 1 298 ? 25.49890  -9.41755  -11.99655 1.000 40.62149  ? 291 LEU   A O      1 
ATOM   2236 C CB     . LEU   A 1 298 ? 27.97118  -10.02437 -14.09974 1.000 44.94143  ? 291 LEU   A CB     1 
ATOM   2237 C CG     . LEU   A 1 298 ? 28.19941  -10.30980 -15.58546 1.000 51.58717  ? 291 LEU   A CG     1 
ATOM   2238 C CD1    . LEU   A 1 298 ? 28.92081  -11.63513 -15.78109 1.000 52.98857  ? 291 LEU   A CD1    1 
ATOM   2239 C CD2    . LEU   A 1 298 ? 26.87692  -10.29488 -16.33790 1.000 44.00302  ? 291 LEU   A CD2    1 
ATOM   2240 N N      . ASP   A 1 299 ? 27.40611  -8.36156  -11.45474 1.000 43.50796  ? 292 ASP   A N      1 
ATOM   2241 C CA     . ASP   A 1 299 ? 27.09594  -8.34830  -10.02839 1.000 51.52632  ? 292 ASP   A CA     1 
ATOM   2242 C C      . ASP   A 1 299 ? 25.95863  -7.36834  -9.76552  1.000 48.63732  ? 292 ASP   A C      1 
ATOM   2243 O O      . ASP   A 1 299 ? 26.11457  -6.15687  -9.95209  1.000 47.68568  ? 292 ASP   A O      1 
ATOM   2244 C CB     . ASP   A 1 299 ? 28.33482  -7.97818  -9.21809  1.000 47.59025  ? 292 ASP   A CB     1 
ATOM   2245 C CG     . ASP   A 1 299 ? 28.12559  -8.14082  -7.72078  1.000 51.84114  ? 292 ASP   A CG     1 
ATOM   2246 O OD1    . ASP   A 1 299 ? 29.09778  -8.48632  -7.01674  1.000 62.48169  ? 292 ASP   A OD1    1 
ATOM   2247 O OD2    . ASP   A 1 299 ? 26.99255  -7.92144  -7.24384  1.000 51.96339  ? 292 ASP   A OD2    1 
ATOM   2248 N N      . SER   A 1 300 ? 24.81385  -7.89214  -9.32039  1.000 39.01039  ? 293 SER   A N      1 
ATOM   2249 C CA     . SER   A 1 300 ? 23.67780  -7.03255  -9.00887  1.000 37.05796  ? 293 SER   A CA     1 
ATOM   2250 C C      . SER   A 1 300 ? 23.99272  -6.07770  -7.86577  1.000 43.23667  ? 293 SER   A C      1 
ATOM   2251 O O      . SER   A 1 300 ? 23.41365  -4.98812  -7.78972  1.000 44.67539  ? 293 SER   A O      1 
ATOM   2252 C CB     . SER   A 1 300 ? 22.45674  -7.88385  -8.66404  1.000 40.20851  ? 293 SER   A CB     1 
ATOM   2253 O OG     . SER   A 1 300 ? 22.61456  -8.50801  -7.40126  1.000 39.68366  ? 293 SER   A OG     1 
ATOM   2254 N N      . ASP   A 1 301 ? 24.89903  -6.46590  -6.96655  1.000 46.73776  ? 294 ASP   A N      1 
ATOM   2255 C CA     . ASP   A 1 301 ? 25.25017  -5.60180  -5.84678  1.000 49.39774  ? 294 ASP   A CA     1 
ATOM   2256 C C      . ASP   A 1 301 ? 26.06786  -4.39351  -6.28193  1.000 49.38446  ? 294 ASP   A C      1 
ATOM   2257 O O      . ASP   A 1 301 ? 26.14837  -3.41423  -5.53279  1.000 46.48883  ? 294 ASP   A O      1 
ATOM   2258 C CB     . ASP   A 1 301 ? 26.01769  -6.39723  -4.79007  1.000 47.21611  ? 294 ASP   A CB     1 
ATOM   2259 C CG     . ASP   A 1 301 ? 25.18693  -7.50884  -4.18207  1.000 59.42356  ? 294 ASP   A CG     1 
ATOM   2260 O OD1    . ASP   A 1 301 ? 23.96421  -7.31565  -4.01493  1.000 56.00920  ? 294 ASP   A OD1    1 
ATOM   2261 O OD2    . ASP   A 1 301 ? 25.75563  -8.57702  -3.87285  1.000 63.60175  ? 294 ASP   A OD2    1 
ATOM   2262 N N      . LYS   A 1 302 ? 26.67112  -4.43712  -7.46984  1.000 42.43661  ? 295 LYS   A N      1 
ATOM   2263 C CA     . LYS   A 1 302 ? 27.47962  -3.33507  -7.97162  1.000 48.35806  ? 295 LYS   A CA     1 
ATOM   2264 C C      . LYS   A 1 302 ? 26.74643  -2.46288  -8.98205  1.000 49.54413  ? 295 LYS   A C      1 
ATOM   2265 O O      . LYS   A 1 302 ? 27.24132  -1.37970  -9.31373  1.000 41.02986  ? 295 LYS   A O      1 
ATOM   2266 C CB     . LYS   A 1 302 ? 28.76992  -3.87011  -8.60688  1.000 47.23181  ? 295 LYS   A CB     1 
ATOM   2267 C CG     . LYS   A 1 302 ? 29.61845  -4.72267  -7.67542  1.000 50.16502  ? 295 LYS   A CG     1 
ATOM   2268 C CD     . LYS   A 1 302 ? 30.07104  -3.93292  -6.45797  1.000 48.87050  ? 295 LYS   A CD     1 
ATOM   2269 C CE     . LYS   A 1 302 ? 30.76329  -4.82963  -5.44287  1.000 62.84832  ? 295 LYS   A CE     1 
ATOM   2270 N NZ     . LYS   A 1 302 ? 31.93058  -5.54435  -6.03042  1.000 61.13904  ? 295 LYS   A NZ     1 
ATOM   2271 N N      . ARG   A 1 303 ? 25.59295  -2.90302  -9.47931  1.000 40.08281  ? 296 ARG   A N      1 
ATOM   2272 C CA     . ARG   A 1 303 ? 24.84287  -2.10167  -10.43464 1.000 38.79202  ? 296 ARG   A CA     1 
ATOM   2273 C C      . ARG   A 1 303 ? 24.36973  -0.80530  -9.79013  1.000 35.46641  ? 296 ARG   A C      1 
ATOM   2274 O O      . ARG   A 1 303 ? 24.06666  -0.75085  -8.59557  1.000 39.18750  ? 296 ARG   A O      1 
ATOM   2275 C CB     . ARG   A 1 303 ? 23.64162  -2.88231  -10.96678 1.000 44.85153  ? 296 ARG   A CB     1 
ATOM   2276 C CG     . ARG   A 1 303 ? 23.99337  -4.01398  -11.91281 1.000 41.28416  ? 296 ARG   A CG     1 
ATOM   2277 C CD     . ARG   A 1 303 ? 22.76145  -4.83742  -12.25111 1.000 36.75875  ? 296 ARG   A CD     1 
ATOM   2278 N NE     . ARG   A 1 303 ? 23.10971  -6.17648  -12.70989 1.000 40.98393  ? 296 ARG   A NE     1 
ATOM   2279 C CZ     . ARG   A 1 303 ? 22.30599  -7.22817  -12.63123 1.000 36.04809  ? 296 ARG   A CZ     1 
ATOM   2280 N NH1    . ARG   A 1 303 ? 22.68316  -8.42003  -13.06443 1.000 36.04335  ? 296 ARG   A NH1    1 
ATOM   2281 N NH2    . ARG   A 1 303 ? 21.09278  -7.08025  -12.10576 1.000 33.25957  ? 296 ARG   A NH2    1 
ATOM   2282 N N      . ILE   A 1 304 ? 24.30334  0.24908   -10.60206 1.000 37.83564  ? 297 ILE   A N      1 
ATOM   2283 C CA     . ILE   A 1 304 ? 23.82305  1.53503   -10.11855 1.000 40.73965  ? 297 ILE   A CA     1 
ATOM   2284 C C      . ILE   A 1 304 ? 22.33733  1.43833   -9.80057  1.000 41.84817  ? 297 ILE   A C      1 
ATOM   2285 O O      . ILE   A 1 304 ? 21.55889  0.82864   -10.54737 1.000 31.75236  ? 297 ILE   A O      1 
ATOM   2286 C CB     . ILE   A 1 304 ? 24.10212  2.63257   -11.15876 1.000 40.16432  ? 297 ILE   A CB     1 
ATOM   2287 C CG1    . ILE   A 1 304 ? 23.91134  4.01909   -10.54172 1.000 37.60888  ? 297 ILE   A CG1    1 
ATOM   2288 C CG2    . ILE   A 1 304 ? 23.20678  2.45110   -12.37637 1.000 33.06526  ? 297 ILE   A CG2    1 
ATOM   2289 C CD1    . ILE   A 1 304 ? 24.33700  5.14987   -11.45180 1.000 37.27804  ? 297 ILE   A CD1    1 
ATOM   2290 N N      . THR   A 1 305 ? 21.93736  2.03315   -8.68060  1.000 35.88856  ? 298 THR   A N      1 
ATOM   2291 C CA     . THR   A 1 305 ? 20.53273  2.07060   -8.31180  1.000 31.81488  ? 298 THR   A CA     1 
ATOM   2292 C C      . THR   A 1 305 ? 19.81647  3.19230   -9.05803  1.000 39.59777  ? 298 THR   A C      1 
ATOM   2293 O O      . THR   A 1 305 ? 20.43686  4.10911   -9.60460  1.000 36.89306  ? 298 THR   A O      1 
ATOM   2294 C CB     . THR   A 1 305 ? 20.37029  2.26567   -6.80414  1.000 33.54863  ? 298 THR   A CB     1 
ATOM   2295 O OG1    . THR   A 1 305 ? 20.93150  3.52744   -6.42112  1.000 35.58749  ? 298 THR   A OG1    1 
ATOM   2296 C CG2    . THR   A 1 305 ? 21.07105  1.14918   -6.04014  1.000 38.95527  ? 298 THR   A CG2    1 
ATOM   2297 N N      . ALA   A 1 306 ? 18.48442  3.10762   -9.07486  1.000 33.29039  ? 299 ALA   A N      1 
ATOM   2298 C CA     . ALA   A 1 306 ? 17.69161  4.14664   -9.72319  1.000 32.79409  ? 299 ALA   A CA     1 
ATOM   2299 C C      . ALA   A 1 306 ? 17.97625  5.51489   -9.11656  1.000 30.68122  ? 299 ALA   A C      1 
ATOM   2300 O O      . ALA   A 1 306 ? 18.14577  6.50127   -9.84292  1.000 30.13742  ? 299 ALA   A O      1 
ATOM   2301 C CB     . ALA   A 1 306 ? 16.20262  3.81204   -9.62408  1.000 28.75527  ? 299 ALA   A CB     1 
ATOM   2302 N N      . ALA   A 1 307 ? 18.03558  5.59476   -7.78544  1.000 30.87460  ? 300 ALA   A N      1 
ATOM   2303 C CA     . ALA   A 1 307 ? 18.30390  6.87196   -7.13150  1.000 32.20180  ? 300 ALA   A CA     1 
ATOM   2304 C C      . ALA   A 1 307 ? 19.65460  7.43468   -7.55874  1.000 39.85118  ? 300 ALA   A C      1 
ATOM   2305 O O      . ALA   A 1 307 ? 19.75974  8.60387   -7.94809  1.000 35.73502  ? 300 ALA   A O      1 
ATOM   2306 C CB     . ALA   A 1 307 ? 18.24119  6.70828   -5.61266  1.000 33.30113  ? 300 ALA   A CB     1 
ATOM   2307 N N      . GLN   A 1 308 ? 20.70403  6.61264   -7.49469  1.000 33.96818  ? 301 GLN   A N      1 
ATOM   2308 C CA     . GLN   A 1 308 ? 22.02810  7.08215   -7.88865  1.000 38.75277  ? 301 GLN   A CA     1 
ATOM   2309 C C      . GLN   A 1 308 ? 22.05914  7.47515   -9.36039  1.000 38.68359  ? 301 GLN   A C      1 
ATOM   2310 O O      . GLN   A 1 308 ? 22.62018  8.51727   -9.72060  1.000 35.42450  ? 301 GLN   A O      1 
ATOM   2311 C CB     . GLN   A 1 308 ? 23.07551  6.00742   -7.59485  1.000 36.10011  ? 301 GLN   A CB     1 
ATOM   2312 C CG     . GLN   A 1 308 ? 23.31222  5.76465   -6.11252  1.000 37.42128  ? 301 GLN   A CG     1 
ATOM   2313 C CD     . GLN   A 1 308 ? 23.98660  4.43451   -5.83632  1.000 38.20229  ? 301 GLN   A CD     1 
ATOM   2314 O OE1    . GLN   A 1 308 ? 23.97593  3.53272   -6.67429  1.000 37.61585  ? 301 GLN   A OE1    1 
ATOM   2315 N NE2    . GLN   A 1 308 ? 24.57761  4.30612   -4.65413  1.000 41.26106  ? 301 GLN   A NE2    1 
ATOM   2316 N N      . ALA   A 1 309 ? 21.45450  6.65672   -10.22595 1.000 33.02816  ? 302 ALA   A N      1 
ATOM   2317 C CA     . ALA   A 1 309 ? 21.48228  6.94263   -11.65661 1.000 32.52050  ? 302 ALA   A CA     1 
ATOM   2318 C C      . ALA   A 1 309 ? 20.84127  8.28634   -11.97696 1.000 33.11071  ? 302 ALA   A C      1 
ATOM   2319 O O      . ALA   A 1 309 ? 21.25257  8.95791   -12.93011 1.000 35.37241  ? 302 ALA   A O      1 
ATOM   2320 C CB     . ALA   A 1 309 ? 20.78654  5.82326   -12.43054 1.000 31.13892  ? 302 ALA   A CB     1 
ATOM   2321 N N      . LEU   A 1 310 ? 19.83395  8.69433   -11.20162 1.000 36.79421  ? 303 LEU   A N      1 
ATOM   2322 C CA     . LEU   A 1 310 ? 19.22223  9.99965   -11.42298 1.000 36.63837  ? 303 LEU   A CA     1 
ATOM   2323 C C      . LEU   A 1 310 ? 20.22297  11.12613  -11.20238 1.000 40.61893  ? 303 LEU   A C      1 
ATOM   2324 O O      . LEU   A 1 310 ? 20.11939  12.18230  -11.83658 1.000 34.40000  ? 303 LEU   A O      1 
ATOM   2325 C CB     . LEU   A 1 310 ? 18.00934  10.17414  -10.50826 1.000 32.34960  ? 303 LEU   A CB     1 
ATOM   2326 C CG     . LEU   A 1 310 ? 16.79658  9.29842   -10.83337 1.000 33.98632  ? 303 LEU   A CG     1 
ATOM   2327 C CD1    . LEU   A 1 310 ? 15.76091  9.36535   -9.72080  1.000 34.06143  ? 303 LEU   A CD1    1 
ATOM   2328 C CD2    . LEU   A 1 310 ? 16.18486  9.70605   -12.16426 1.000 30.17457  ? 303 LEU   A CD2    1 
ATOM   2329 N N      . ALA   A 1 311 ? 21.19764  10.91923  -10.31803 1.000 43.46056  ? 304 ALA   A N      1 
ATOM   2330 C CA     . ALA   A 1 311 ? 22.22459  11.91488  -10.04200 1.000 42.08126  ? 304 ALA   A CA     1 
ATOM   2331 C C      . ALA   A 1 311 ? 23.38417  11.86549  -11.02886 1.000 42.14447  ? 304 ALA   A C      1 
ATOM   2332 O O      . ALA   A 1 311 ? 24.30082  12.68784  -10.92187 1.000 39.36500  ? 304 ALA   A O      1 
ATOM   2333 C CB     . ALA   A 1 311 ? 22.75371  11.74014  -8.61590  1.000 40.43069  ? 304 ALA   A CB     1 
ATOM   2334 N N      . HIS   A 1 312 ? 23.37060  10.92989  -11.97598 1.000 44.58074  ? 305 HIS   A N      1 
ATOM   2335 C CA     . HIS   A 1 312 ? 24.43208  10.85580  -12.96942 1.000 39.35331  ? 305 HIS   A CA     1 
ATOM   2336 C C      . HIS   A 1 312 ? 24.44070  12.11170  -13.83332 1.000 37.71358  ? 305 HIS   A C      1 
ATOM   2337 O O      . HIS   A 1 312 ? 23.39633  12.70079  -14.12566 1.000 36.94307  ? 305 HIS   A O      1 
ATOM   2338 C CB     . HIS   A 1 312 ? 24.25429  9.61274   -13.84332 1.000 35.95432  ? 305 HIS   A CB     1 
ATOM   2339 C CG     . HIS   A 1 312 ? 25.46789  9.25527   -14.64447 1.000 41.61039  ? 305 HIS   A CG     1 
ATOM   2340 N ND1    . HIS   A 1 312 ? 25.78327  9.87473   -15.83497 1.000 39.54664  ? 305 HIS   A ND1    1 
ATOM   2341 C CD2    . HIS   A 1 312 ? 26.44080  8.33824   -14.42845 1.000 39.52993  ? 305 HIS   A CD2    1 
ATOM   2342 C CE1    . HIS   A 1 312 ? 26.89921  9.35677   -16.31617 1.000 39.02687  ? 305 HIS   A CE1    1 
ATOM   2343 N NE2    . HIS   A 1 312 ? 27.31862  8.42243   -15.48188 1.000 39.29502  ? 305 HIS   A NE2    1 
ATOM   2344 N N      . ALA   A 1 313 ? 25.64329  12.52095  -14.24481 1.000 41.39668  ? 306 ALA   A N      1 
ATOM   2345 C CA     . ALA   A 1 313 ? 25.78244  13.72348  -15.05873 1.000 40.77784  ? 306 ALA   A CA     1 
ATOM   2346 C C      . ALA   A 1 313 ? 24.96151  13.65490  -16.33878 1.000 38.76852  ? 306 ALA   A C      1 
ATOM   2347 O O      . ALA   A 1 313 ? 24.59737  14.70222  -16.88487 1.000 39.12403  ? 306 ALA   A O      1 
ATOM   2348 C CB     . ALA   A 1 313 ? 27.25471  13.96249  -15.39894 1.000 41.86596  ? 306 ALA   A CB     1 
ATOM   2349 N N      . TYR   A 1 314 ? 24.65577  12.44877  -16.82447 1.000 37.50267  ? 307 TYR   A N      1 
ATOM   2350 C CA     . TYR   A 1 314 ? 23.89927  12.31552  -18.06592 1.000 40.61261  ? 307 TYR   A CA     1 
ATOM   2351 C C      . TYR   A 1 314 ? 22.52665  12.97138  -17.97155 1.000 37.71035  ? 307 TYR   A C      1 
ATOM   2352 O O      . TYR   A 1 314 ? 21.95602  13.36250  -18.99653 1.000 36.31934  ? 307 TYR   A O      1 
ATOM   2353 C CB     . TYR   A 1 314 ? 23.75506  10.83785  -18.43134 1.000 35.53228  ? 307 TYR   A CB     1 
ATOM   2354 C CG     . TYR   A 1 314 ? 23.08796  10.59785  -19.76501 1.000 41.72409  ? 307 TYR   A CG     1 
ATOM   2355 C CD1    . TYR   A 1 314 ? 23.61835  11.12803  -20.93343 1.000 39.67792  ? 307 TYR   A CD1    1 
ATOM   2356 C CD2    . TYR   A 1 314 ? 21.92828  9.83934   -19.85696 1.000 33.39649  ? 307 TYR   A CD2    1 
ATOM   2357 C CE1    . TYR   A 1 314 ? 23.01256  10.91064  -22.15601 1.000 35.59822  ? 307 TYR   A CE1    1 
ATOM   2358 C CE2    . TYR   A 1 314 ? 21.31523  9.61615   -21.07518 1.000 33.03783  ? 307 TYR   A CE2    1 
ATOM   2359 C CZ     . TYR   A 1 314 ? 21.86174  10.15354  -22.22168 1.000 35.90180  ? 307 TYR   A CZ     1 
ATOM   2360 O OH     . TYR   A 1 314 ? 21.25726  9.93566   -23.43858 1.000 34.06674  ? 307 TYR   A OH     1 
ATOM   2361 N N      . PHE   A 1 315 ? 21.98048  13.10091  -16.76121 1.000 35.27681  ? 308 PHE   A N      1 
ATOM   2362 C CA     . PHE   A 1 315 ? 20.65304  13.66780  -16.55532 1.000 35.34375  ? 308 PHE   A CA     1 
ATOM   2363 C C      . PHE   A 1 315 ? 20.70132  15.05955  -15.93207 1.000 44.96021  ? 308 PHE   A C      1 
ATOM   2364 O O      . PHE   A 1 315 ? 19.72154  15.49183  -15.31651 1.000 42.68676  ? 308 PHE   A O      1 
ATOM   2365 C CB     . PHE   A 1 315 ? 19.80609  12.73689  -15.68610 1.000 36.14830  ? 308 PHE   A CB     1 
ATOM   2366 C CG     . PHE   A 1 315 ? 19.71341  11.33268  -16.20902 1.000 32.70301  ? 308 PHE   A CG     1 
ATOM   2367 C CD1    . PHE   A 1 315 ? 19.08600  11.06758  -17.41408 1.000 34.24779  ? 308 PHE   A CD1    1 
ATOM   2368 C CD2    . PHE   A 1 315 ? 20.25121  10.27661  -15.49252 1.000 32.79831  ? 308 PHE   A CD2    1 
ATOM   2369 C CE1    . PHE   A 1 315 ? 18.99826  9.77582   -17.89647 1.000 32.28421  ? 308 PHE   A CE1    1 
ATOM   2370 C CE2    . PHE   A 1 315 ? 20.16696  8.98188   -15.96979 1.000 32.94059  ? 308 PHE   A CE2    1 
ATOM   2371 C CZ     . PHE   A 1 315 ? 19.53954  8.73142   -17.17309 1.000 30.45036  ? 308 PHE   A CZ     1 
ATOM   2372 N N      . ALA   A 1 316 ? 21.81869  15.77422  -16.08477 1.000 37.53595  ? 309 ALA   A N      1 
ATOM   2373 C CA     . ALA   A 1 316 ? 21.95003  17.08130  -15.44911 1.000 43.53788  ? 309 ALA   A CA     1 
ATOM   2374 C C      . ALA   A 1 316 ? 20.84131  18.03610  -15.87423 1.000 45.37849  ? 309 ALA   A C      1 
ATOM   2375 O O      . ALA   A 1 316 ? 20.42072  18.88777  -15.08272 1.000 40.95048  ? 309 ALA   A O      1 
ATOM   2376 C CB     . ALA   A 1 316 ? 23.31892  17.68413  -15.76614 1.000 40.95310  ? 309 ALA   A CB     1 
ATOM   2377 N N      . GLN   A 1 317 ? 20.35326  17.91267  -17.10898 1.000 42.15142  ? 310 GLN   A N      1 
ATOM   2378 C CA     . GLN   A 1 317 ? 19.33763  18.82631  -17.61677 1.000 46.15879  ? 310 GLN   A CA     1 
ATOM   2379 C C      . GLN   A 1 317 ? 17.94653  18.54888  -17.05990 1.000 47.11736  ? 310 GLN   A C      1 
ATOM   2380 O O      . GLN   A 1 317 ? 17.06115  19.39854  -17.20629 1.000 46.37197  ? 310 GLN   A O      1 
ATOM   2381 C CB     . GLN   A 1 317 ? 19.29589  18.76813  -19.14635 1.000 45.48722  ? 310 GLN   A CB     1 
ATOM   2382 C CG     . GLN   A 1 317 ? 20.61588  19.11329  -19.81913 1.000 50.26171  ? 310 GLN   A CG     1 
ATOM   2383 C CD     . GLN   A 1 317 ? 20.96798  20.58372  -19.69979 1.000 66.69221  ? 310 GLN   A CD     1 
ATOM   2384 O OE1    . GLN   A 1 317 ? 21.26663  21.07651  -18.61217 1.000 69.81725  ? 310 GLN   A OE1    1 
ATOM   2385 N NE2    . GLN   A 1 317 ? 20.93418  21.29340  -20.82247 1.000 67.85028  ? 310 GLN   A NE2    1 
ATOM   2386 N N      . TYR   A 1 318 ? 17.73090  17.39496  -16.42534 1.000 43.33854  ? 311 TYR   A N      1 
ATOM   2387 C CA     . TYR   A 1 318 ? 16.42506  17.03465  -15.89318 1.000 41.99127  ? 311 TYR   A CA     1 
ATOM   2388 C C      . TYR   A 1 318 ? 16.42520  16.71949  -14.40508 1.000 40.36287  ? 311 TYR   A C      1 
ATOM   2389 O O      . TYR   A 1 318 ? 15.35079  16.72573  -13.79452 1.000 38.71690  ? 311 TYR   A O      1 
ATOM   2390 C CB     . TYR   A 1 318 ? 15.85544  15.82249  -16.64953 1.000 35.57539  ? 311 TYR   A CB     1 
ATOM   2391 C CG     . TYR   A 1 318 ? 15.74258  16.03483  -18.14246 1.000 41.68330  ? 311 TYR   A CG     1 
ATOM   2392 C CD1    . TYR   A 1 318 ? 14.70130  16.77993  -18.67880 1.000 38.99298  ? 311 TYR   A CD1    1 
ATOM   2393 C CD2    . TYR   A 1 318 ? 16.67922  15.49518  -19.01545 1.000 41.19679  ? 311 TYR   A CD2    1 
ATOM   2394 C CE1    . TYR   A 1 318 ? 14.59345  16.98126  -20.04169 1.000 43.63968  ? 311 TYR   A CE1    1 
ATOM   2395 C CE2    . TYR   A 1 318 ? 16.57936  15.69112  -20.38194 1.000 38.89653  ? 311 TYR   A CE2    1 
ATOM   2396 C CZ     . TYR   A 1 318 ? 15.53372  16.43534  -20.88843 1.000 44.93232  ? 311 TYR   A CZ     1 
ATOM   2397 O OH     . TYR   A 1 318 ? 15.42583  16.63575  -22.24553 1.000 41.10628  ? 311 TYR   A OH     1 
ATOM   2398 N N      . HIS   A 1 319 ? 17.58448  16.46106  -13.80697 1.000 41.90155  ? 312 HIS   A N      1 
ATOM   2399 C CA     . HIS   A 1 319 ? 17.64113  16.01300  -12.42237 1.000 44.94648  ? 312 HIS   A CA     1 
ATOM   2400 C C      . HIS   A 1 319 ? 17.20205  17.11549  -11.46354 1.000 46.34952  ? 312 HIS   A C      1 
ATOM   2401 O O      . HIS   A 1 319 ? 17.60500  18.27520  -11.59265 1.000 45.14944  ? 312 HIS   A O      1 
ATOM   2402 C CB     . HIS   A 1 319 ? 19.05945  15.55134  -12.08436 1.000 40.77364  ? 312 HIS   A CB     1 
ATOM   2403 C CG     . HIS   A 1 319 ? 19.27570  15.25779  -10.63258 1.000 40.02190  ? 312 HIS   A CG     1 
ATOM   2404 N ND1    . HIS   A 1 319 ? 18.46751  14.40187  -9.91590  1.000 36.26344  ? 312 HIS   A ND1    1 
ATOM   2405 C CD2    . HIS   A 1 319 ? 20.21669  15.70090  -9.76543  1.000 41.33128  ? 312 HIS   A CD2    1 
ATOM   2406 C CE1    . HIS   A 1 319 ? 18.89833  14.33356  -8.66888  1.000 37.92107  ? 312 HIS   A CE1    1 
ATOM   2407 N NE2    . HIS   A 1 319 ? 19.95866  15.11252  -8.55126  1.000 44.48409  ? 312 HIS   A NE2    1 
ATOM   2408 N N      . ASP   A 1 320 ? 16.36696  16.74077  -10.49333 1.000 44.83040  ? 313 ASP   A N      1 
ATOM   2409 C CA     . ASP   A 1 320 ? 15.94717  17.64650  -9.42373  1.000 43.79390  ? 313 ASP   A CA     1 
ATOM   2410 C C      . ASP   A 1 320 ? 15.71423  16.80751  -8.17537  1.000 44.03038  ? 313 ASP   A C      1 
ATOM   2411 O O      . ASP   A 1 320 ? 14.69803  16.10349  -8.06653  1.000 48.46808  ? 313 ASP   A O      1 
ATOM   2412 C CB     . ASP   A 1 320 ? 14.69527  18.43694  -9.79516  1.000 52.88253  ? 313 ASP   A CB     1 
ATOM   2413 C CG     . ASP   A 1 320 ? 14.23740  19.36531  -8.68088  1.000 51.48181  ? 313 ASP   A CG     1 
ATOM   2414 O OD1    . ASP   A 1 320 ? 14.97904  19.52338  -7.68765  1.000 46.40202  ? 313 ASP   A OD1    1 
ATOM   2415 O OD2    . ASP   A 1 320 ? 13.13299  19.93697  -8.79929  1.000 57.21664  ? 313 ASP   A OD2    1 
ATOM   2416 N N      . PRO   A 1 321 ? 16.63106  16.85608  -7.20610  1.000 49.13099  ? 314 PRO   A N      1 
ATOM   2417 C CA     . PRO   A 1 321 ? 16.47218  16.00911  -6.01221  1.000 51.36405  ? 314 PRO   A CA     1 
ATOM   2418 C C      . PRO   A 1 321 ? 15.19294  16.27995  -5.24095  1.000 52.22454  ? 314 PRO   A C      1 
ATOM   2419 O O      . PRO   A 1 321 ? 14.67485  15.37078  -4.58035  1.000 52.96148  ? 314 PRO   A O      1 
ATOM   2420 C CB     . PRO   A 1 321 ? 17.71744  16.34311  -5.17695  1.000 54.45419  ? 314 PRO   A CB     1 
ATOM   2421 C CG     . PRO   A 1 321 ? 18.16994  17.67985  -5.67286  1.000 45.73072  ? 314 PRO   A CG     1 
ATOM   2422 C CD     . PRO   A 1 321 ? 17.83420  17.70198  -7.13336  1.000 49.45124  ? 314 PRO   A CD     1 
ATOM   2423 N N      . ASP   A 1 322 ? 14.66650  17.50114  -5.30026  1.000 55.36434  ? 315 ASP   A N      1 
ATOM   2424 C CA     . ASP   A 1 322 ? 13.45342  17.84841  -4.57202  1.000 51.62535  ? 315 ASP   A CA     1 
ATOM   2425 C C      . ASP   A 1 322 ? 12.18068  17.41833  -5.29134  1.000 49.72493  ? 315 ASP   A C      1 
ATOM   2426 O O      . ASP   A 1 322 ? 11.09025  17.58200  -4.73282  1.000 52.30681  ? 315 ASP   A O      1 
ATOM   2427 C CB     . ASP   A 1 322 ? 13.41468  19.35764  -4.31153  1.000 54.77721  ? 315 ASP   A CB     1 
ATOM   2428 C CG     . ASP   A 1 322 ? 14.63939  19.85304  -3.56353  1.000 57.59513  ? 315 ASP   A CG     1 
ATOM   2429 O OD1    . ASP   A 1 322 ? 14.79407  19.50536  -2.37387  1.000 59.90384  ? 315 ASP   A OD1    1 
ATOM   2430 O OD2    . ASP   A 1 322 ? 15.44753  20.59214  -4.16469  1.000 65.23185  ? 315 ASP   A OD2    1 
ATOM   2431 N N      . ASP   A 1 323 ? 12.28760  16.87065  -6.50450  1.000 49.58519  ? 316 ASP   A N      1 
ATOM   2432 C CA     . ASP   A 1 323 ? 11.12525  16.47438  -7.29208  1.000 44.89789  ? 316 ASP   A CA     1 
ATOM   2433 C C      . ASP   A 1 323 ? 11.25022  15.03457  -7.77989  1.000 46.09079  ? 316 ASP   A C      1 
ATOM   2434 O O      . ASP   A 1 323 ? 10.79698  14.70105  -8.87817  1.000 40.98504  ? 316 ASP   A O      1 
ATOM   2435 C CB     . ASP   A 1 323 ? 10.91826  17.42444  -8.47190  1.000 45.41205  ? 316 ASP   A CB     1 
ATOM   2436 C CG     . ASP   A 1 323 ? 9.56187   17.25251  -9.12949  1.000 52.01260  ? 316 ASP   A CG     1 
ATOM   2437 O OD1    . ASP   A 1 323 ? 8.62660   16.77186  -8.45486  1.000 42.41562  ? 316 ASP   A OD1    1 
ATOM   2438 O OD2    . ASP   A 1 323 ? 9.43284   17.59755  -10.32290 1.000 46.99796  ? 316 ASP   A OD2    1 
ATOM   2439 N N      . GLU   A 1 324 ? 11.86520  14.17108  -6.97637  1.000 44.78015  ? 317 GLU   A N      1 
ATOM   2440 C CA     . GLU   A 1 324 ? 11.99059  12.74521  -7.27651  1.000 33.42299  ? 317 GLU   A CA     1 
ATOM   2441 C C      . GLU   A 1 324 ? 11.48730  11.96418  -6.07057  1.000 43.40495  ? 317 GLU   A C      1 
ATOM   2442 O O      . GLU   A 1 324 ? 12.27160  11.37194  -5.31903  1.000 43.36322  ? 317 GLU   A O      1 
ATOM   2443 C CB     . GLU   A 1 324 ? 13.43549  12.38237  -7.61982  1.000 40.60961  ? 317 GLU   A CB     1 
ATOM   2444 C CG     . GLU   A 1 324 ? 13.90611  12.94697  -8.95249  1.000 41.12611  ? 317 GLU   A CG     1 
ATOM   2445 C CD     . GLU   A 1 324 ? 15.41122  13.10358  -9.02795  1.000 44.15121  ? 317 GLU   A CD     1 
ATOM   2446 O OE1    . GLU   A 1 324 ? 15.90261  13.62161  -10.05247 1.000 45.26617  ? 317 GLU   A OE1    1 
ATOM   2447 O OE2    . GLU   A 1 324 ? 16.10307  12.70967  -8.06612  1.000 42.92078  ? 317 GLU   A OE2    1 
ATOM   2448 N N      . PRO   A 1 325 ? 10.17582  11.94019  -5.86079  1.000 41.36860  ? 318 PRO   A N      1 
ATOM   2449 C CA     . PRO   A 1 325 ? 9.62711   11.46693  -4.58813  1.000 38.72206  ? 318 PRO   A CA     1 
ATOM   2450 C C      . PRO   A 1 325 ? 9.69347   9.95116   -4.45195  1.000 44.26763  ? 318 PRO   A C      1 
ATOM   2451 O O      . PRO   A 1 325 ? 9.90203   9.21016   -5.41432  1.000 37.59640  ? 318 PRO   A O      1 
ATOM   2452 C CB     . PRO   A 1 325 ? 8.17569   11.95417  -4.63624  1.000 39.88383  ? 318 PRO   A CB     1 
ATOM   2453 C CG     . PRO   A 1 325 ? 7.84697   11.98808  -6.08811  1.000 37.28355  ? 318 PRO   A CG     1 
ATOM   2454 C CD     . PRO   A 1 325 ? 9.12278   12.35251  -6.80420  1.000 38.52511  ? 318 PRO   A CD     1 
ATOM   2455 N N      . VAL   A 1 326 ? 9.51093   9.50387   -3.21366  1.000 44.36783  ? 319 VAL   A N      1 
ATOM   2456 C CA     . VAL   A 1 326 ? 9.45628   8.08918   -2.88779  1.000 37.97132  ? 319 VAL   A CA     1 
ATOM   2457 C C      . VAL   A 1 326 ? 8.02466   7.73877   -2.48964  1.000 39.24499  ? 319 VAL   A C      1 
ATOM   2458 O O      . VAL   A 1 326 ? 7.18382   8.60989   -2.26620  1.000 37.44677  ? 319 VAL   A O      1 
ATOM   2459 C CB     . VAL   A 1 326 ? 10.45561  7.71268   -1.77649  1.000 37.89695  ? 319 VAL   A CB     1 
ATOM   2460 C CG1    . VAL   A 1 326 ? 11.87837  8.02544   -2.21497  1.000 37.19761  ? 319 VAL   A CG1    1 
ATOM   2461 C CG2    . VAL   A 1 326 ? 10.11642  8.44339   -0.48510  1.000 36.09054  ? 319 VAL   A CG2    1 
ATOM   2462 N N      . ALA   A 1 327 ? 7.75377   6.44255   -2.39946  1.000 43.04651  ? 320 ALA   A N      1 
ATOM   2463 C CA     . ALA   A 1 327 ? 6.41861   5.94471   -2.10969  1.000 37.69781  ? 320 ALA   A CA     1 
ATOM   2464 C C      . ALA   A 1 327 ? 6.29607   5.52537   -0.65008  1.000 43.46728  ? 320 ALA   A C      1 
ATOM   2465 O O      . ALA   A 1 327 ? 7.28267   5.21061   0.02048   1.000 45.26249  ? 320 ALA   A O      1 
ATOM   2466 C CB     . ALA   A 1 327 ? 6.07353   4.76243   -3.01903  1.000 32.03409  ? 320 ALA   A CB     1 
ATOM   2467 N N      . ASP   A 1 328 ? 5.05578   5.53167   -0.16125  1.000 56.13216  ? 321 ASP   A N      1 
ATOM   2468 C CA     . ASP   A 1 328 ? 4.77295   4.97046   1.14535   1.000 56.49651  ? 321 ASP   A CA     1 
ATOM   2469 C C      . ASP   A 1 328 ? 5.05819   3.47118   1.12745   1.000 50.11488  ? 321 ASP   A C      1 
ATOM   2470 O O      . ASP   A 1 328 ? 5.04046   2.83846   0.06846   1.000 43.93310  ? 321 ASP   A O      1 
ATOM   2471 C CB     . ASP   A 1 328 ? 3.31790   5.22475   1.53500   1.000 52.67581  ? 321 ASP   A CB     1 
ATOM   2472 C CG     . ASP   A 1 328 ? 3.02642   6.69123   1.77914   1.000 64.76325  ? 321 ASP   A CG     1 
ATOM   2473 O OD1    . ASP   A 1 328 ? 3.68868   7.29220   2.65056   1.000 69.00725  ? 321 ASP   A OD1    1 
ATOM   2474 O OD2    . ASP   A 1 328 ? 2.13308   7.24240   1.10131   1.000 62.87544  ? 321 ASP   A OD2    1 
ATOM   2475 N N      . PRO   A 1 329 ? 5.32489   2.87958   2.28920   1.000 61.94894  ? 322 PRO   A N      1 
ATOM   2476 C CA     . PRO   A 1 329 ? 5.58111   1.43598   2.32789   1.000 55.35794  ? 322 PRO   A CA     1 
ATOM   2477 C C      . PRO   A 1 329 ? 4.37114   0.66285   1.82796   1.000 47.29706  ? 322 PRO   A C      1 
ATOM   2478 O O      . PRO   A 1 329 ? 3.23020   0.95861   2.18874   1.000 50.75656  ? 322 PRO   A O      1 
ATOM   2479 C CB     . PRO   A 1 329 ? 5.85761   1.16355   3.81055   1.000 61.61638  ? 322 PRO   A CB     1 
ATOM   2480 C CG     . PRO   A 1 329 ? 5.16598   2.27645   4.53104   1.000 59.68343  ? 322 PRO   A CG     1 
ATOM   2481 C CD     . PRO   A 1 329 ? 5.29007   3.47503   3.63561   1.000 60.41851  ? 322 PRO   A CD     1 
ATOM   2482 N N      . TYR   A 1 330 ? 4.62805   -0.32849  0.97943   1.000 49.08640  ? 323 TYR   A N      1 
ATOM   2483 C CA     . TYR   A 1 330 ? 3.57876   -1.15024  0.38932   1.000 45.95183  ? 323 TYR   A CA     1 
ATOM   2484 C C      . TYR   A 1 330 ? 3.58441   -2.51958  1.05400   1.000 47.97030  ? 323 TYR   A C      1 
ATOM   2485 O O      . TYR   A 1 330 ? 4.59853   -3.22555  1.01969   1.000 44.53381  ? 323 TYR   A O      1 
ATOM   2486 C CB     . TYR   A 1 330 ? 3.76502   -1.28926  -1.12076  1.000 37.24186  ? 323 TYR   A CB     1 
ATOM   2487 C CG     . TYR   A 1 330 ? 2.67074   -2.09918  -1.77266  1.000 36.04252  ? 323 TYR   A CG     1 
ATOM   2488 C CD1    . TYR   A 1 330 ? 1.34120   -1.71312  -1.66449  1.000 39.82940  ? 323 TYR   A CD1    1 
ATOM   2489 C CD2    . TYR   A 1 330 ? 2.96121   -3.25650  -2.48128  1.000 39.92308  ? 323 TYR   A CD2    1 
ATOM   2490 C CE1    . TYR   A 1 330 ? 0.33286   -2.45087  -2.25069  1.000 40.74635  ? 323 TYR   A CE1    1 
ATOM   2491 C CE2    . TYR   A 1 330 ? 1.95815   -4.00202  -3.07158  1.000 36.05974  ? 323 TYR   A CE2    1 
ATOM   2492 C CZ     . TYR   A 1 330 ? 0.64614   -3.59384  -2.95259  1.000 40.34834  ? 323 TYR   A CZ     1 
ATOM   2493 O OH     . TYR   A 1 330 ? -0.35801  -4.32954  -3.53720  1.000 41.53231  ? 323 TYR   A OH     1 
ATOM   2494 N N      . ASP   A 1 331 ? 2.45029   -2.89430  1.64286   1.000 40.54228  ? 324 ASP   A N      1 
ATOM   2495 C CA     . ASP   A 1 331 ? 2.32493   -4.15259  2.37065   1.000 46.08172  ? 324 ASP   A CA     1 
ATOM   2496 C C      . ASP   A 1 331 ? 1.98463   -5.26593  1.38630   1.000 46.53391  ? 324 ASP   A C      1 
ATOM   2497 O O      . ASP   A 1 331 ? 0.86763   -5.32229  0.86110   1.000 41.84906  ? 324 ASP   A O      1 
ATOM   2498 C CB     . ASP   A 1 331 ? 1.26233   -4.03727  3.46063   1.000 47.06677  ? 324 ASP   A CB     1 
ATOM   2499 C CG     . ASP   A 1 331 ? 0.81442   -5.38668  3.98115   1.000 54.55044  ? 324 ASP   A CG     1 
ATOM   2500 O OD1    . ASP   A 1 331 ? 1.67467   -6.27768  4.14312   1.000 55.30299  ? 324 ASP   A OD1    1 
ATOM   2501 O OD2    . ASP   A 1 331 ? -0.39730  -5.55685  4.22780   1.000 56.12251  ? 324 ASP   A OD2    1 
ATOM   2502 N N      . GLN   A 1 332 ? 2.94895   -6.15290  1.13634   1.000 46.77440  ? 325 GLN   A N      1 
ATOM   2503 C CA     . GLN   A 1 332 ? 2.74687   -7.32555  0.29383   1.000 46.62075  ? 325 GLN   A CA     1 
ATOM   2504 C C      . GLN   A 1 332 ? 2.62947   -8.60866  1.11159   1.000 41.59744  ? 325 GLN   A C      1 
ATOM   2505 O O      . GLN   A 1 332 ? 3.02244   -9.68232  0.64282   1.000 36.11324  ? 325 GLN   A O      1 
ATOM   2506 C CB     . GLN   A 1 332 ? 3.87908   -7.45201  -0.72616  1.000 44.55279  ? 325 GLN   A CB     1 
ATOM   2507 C CG     . GLN   A 1 332 ? 3.96795   -6.30260  -1.71587  1.000 48.79028  ? 325 GLN   A CG     1 
ATOM   2508 C CD     . GLN   A 1 332 ? 5.18767   -6.40238  -2.61225  1.000 51.86835  ? 325 GLN   A CD     1 
ATOM   2509 O OE1    . GLN   A 1 332 ? 6.03589   -5.51056  -2.62761  1.000 46.82328  ? 325 GLN   A OE1    1 
ATOM   2510 N NE2    . GLN   A 1 332 ? 5.28226   -7.49338  -3.36384  1.000 47.01440  ? 325 GLN   A NE2    1 
ATOM   2511 N N      . SER   A 1 333 ? 2.09634   -8.51650  2.33230   1.000 38.37328  ? 326 SER   A N      1 
ATOM   2512 C CA     . SER   A 1 333 ? 1.98666   -9.69789  3.18276   1.000 51.10295  ? 326 SER   A CA     1 
ATOM   2513 C C      . SER   A 1 333 ? 1.07248   -10.74639 2.56163   1.000 41.89601  ? 326 SER   A C      1 
ATOM   2514 O O      . SER   A 1 333 ? 1.35074   -11.94882 2.64069   1.000 43.53317  ? 326 SER   A O      1 
ATOM   2515 C CB     . SER   A 1 333 ? 1.48013   -9.30082  4.56948   1.000 46.85907  ? 326 SER   A CB     1 
ATOM   2516 O OG     . SER   A 1 333 ? 2.40751   -8.45770  5.22979   1.000 60.19323  ? 326 SER   A OG     1 
ATOM   2517 N N      . PHE   A 1 334 ? -0.02180  -10.30948 1.93319   1.000 36.09293  ? 327 PHE   A N      1 
ATOM   2518 C CA     . PHE   A 1 334 ? -0.97386  -11.24082 1.33788   1.000 38.00320  ? 327 PHE   A CA     1 
ATOM   2519 C C      . PHE   A 1 334 ? -0.31509  -12.21849 0.37390   1.000 40.32694  ? 327 PHE   A C      1 
ATOM   2520 O O      . PHE   A 1 334 ? -0.91456  -13.24849 0.04498   1.000 45.34731  ? 327 PHE   A O      1 
ATOM   2521 C CB     . PHE   A 1 334 ? -2.07273  -10.46513 0.60639   1.000 28.79297  ? 327 PHE   A CB     1 
ATOM   2522 C CG     . PHE   A 1 334 ? -1.62330  -9.86614  -0.69798  1.000 36.19428  ? 327 PHE   A CG     1 
ATOM   2523 C CD1    . PHE   A 1 334 ? -1.04496  -8.60827  -0.73519  1.000 27.05587  ? 327 PHE   A CD1    1 
ATOM   2524 C CD2    . PHE   A 1 334 ? -1.77557  -10.56260 -1.88646  1.000 33.28839  ? 327 PHE   A CD2    1 
ATOM   2525 C CE1    . PHE   A 1 334 ? -0.62863  -8.05599  -1.93188  1.000 31.49753  ? 327 PHE   A CE1    1 
ATOM   2526 C CE2    . PHE   A 1 334 ? -1.35961  -10.01614 -3.08605  1.000 33.60859  ? 327 PHE   A CE2    1 
ATOM   2527 C CZ     . PHE   A 1 334 ? -0.78602  -8.76073  -3.10899  1.000 33.58343  ? 327 PHE   A CZ     1 
ATOM   2528 N N      . GLU   A 1 335 ? 0.90081   -11.92138 -0.08997  1.000 36.11936  ? 328 GLU   A N      1 
ATOM   2529 C CA     . GLU   A 1 335 ? 1.53640   -12.76489 -1.09636  1.000 36.91780  ? 328 GLU   A CA     1 
ATOM   2530 C C      . GLU   A 1 335 ? 1.83740   -14.16240 -0.56772  1.000 37.82495  ? 328 GLU   A C      1 
ATOM   2531 O O      . GLU   A 1 335 ? 1.89427   -15.11711 -1.35069  1.000 38.42499  ? 328 GLU   A O      1 
ATOM   2532 C CB     . GLU   A 1 335 ? 2.81747   -12.10074 -1.60027  1.000 31.10931  ? 328 GLU   A CB     1 
ATOM   2533 C CG     . GLU   A 1 335 ? 2.57735   -10.91376 -2.52043  1.000 38.10111  ? 328 GLU   A CG     1 
ATOM   2534 C CD     . GLU   A 1 335 ? 2.04380   -11.32840 -3.87813  1.000 33.39194  ? 328 GLU   A CD     1 
ATOM   2535 O OE1    . GLU   A 1 335 ? 1.89403   -12.54579 -4.11238  1.000 40.16193  ? 328 GLU   A OE1    1 
ATOM   2536 O OE2    . GLU   A 1 335 ? 1.77305   -10.43741 -4.71063  1.000 35.19848  ? 328 GLU   A OE2    1 
ATOM   2537 N N      . SER   A 1 336 ? 2.03375   -14.30756 0.74177   1.000 39.90908  ? 329 SER   A N      1 
ATOM   2538 C CA     . SER   A 1 336 ? 2.37049   -15.60044 1.32337   1.000 47.06534  ? 329 SER   A CA     1 
ATOM   2539 C C      . SER   A 1 336 ? 1.15099   -16.39153 1.77718   1.000 49.24977  ? 329 SER   A C      1 
ATOM   2540 O O      . SER   A 1 336 ? 1.28955   -17.57329 2.11190   1.000 52.53999  ? 329 SER   A O      1 
ATOM   2541 C CB     . SER   A 1 336 ? 3.32542   -15.41711 2.50898   1.000 49.78615  ? 329 SER   A CB     1 
ATOM   2542 O OG     . SER   A 1 336 ? 2.77173   -14.55181 3.48516   1.000 48.80817  ? 329 SER   A OG     1 
ATOM   2543 N N      . ARG   A 1 337 ? -0.02955  -15.77994 1.79573   1.000 44.52944  ? 330 ARG   A N      1 
ATOM   2544 C CA     . ARG   A 1 337 ? -1.23311  -16.47412 2.22651   1.000 39.68669  ? 330 ARG   A CA     1 
ATOM   2545 C C      . ARG   A 1 337 ? -1.78514  -17.33578 1.09862   1.000 39.52070  ? 330 ARG   A C      1 
ATOM   2546 O O      . ARG   A 1 337 ? -1.71580  -16.96791 -0.07777  1.000 37.30576  ? 330 ARG   A O      1 
ATOM   2547 C CB     . ARG   A 1 337 ? -2.29285  -15.47247 2.68495   1.000 41.79858  ? 330 ARG   A CB     1 
ATOM   2548 C CG     . ARG   A 1 337 ? -1.73124  -14.26717 3.41906   1.000 42.72324  ? 330 ARG   A CG     1 
ATOM   2549 C CD     . ARG   A 1 337 ? -1.68371  -14.50207 4.91935   1.000 47.49880  ? 330 ARG   A CD     1 
ATOM   2550 N NE     . ARG   A 1 337 ? -0.65898  -13.69050 5.56508   1.000 65.71017  ? 330 ARG   A NE     1 
ATOM   2551 C CZ     . ARG   A 1 337 ? -0.65486  -12.36440 5.58323   1.000 61.11062  ? 330 ARG   A CZ     1 
ATOM   2552 N NH1    . ARG   A 1 337 ? -1.61579  -11.66177 5.00525   1.000 49.69446  ? 330 ARG   A NH1    1 
ATOM   2553 N NH2    . ARG   A 1 337 ? 0.33758   -11.72712 6.19759   1.000 53.29986  ? 330 ARG   A NH2    1 
ATOM   2554 N N      . ASP   A 1 338 ? -2.32567  -18.49351 1.46548   1.000 39.22330  ? 331 ASP   A N      1 
ATOM   2555 C CA     . ASP   A 1 338 ? -2.99341  -19.39592 0.53134   1.000 41.27344  ? 331 ASP   A CA     1 
ATOM   2556 C C      . ASP   A 1 338 ? -4.46679  -19.43071 0.92098   1.000 43.17074  ? 331 ASP   A C      1 
ATOM   2557 O O      . ASP   A 1 338 ? -4.84666  -20.08614 1.89580   1.000 42.87353  ? 331 ASP   A O      1 
ATOM   2558 C CB     . ASP   A 1 338 ? -2.36454  -20.78604 0.55786   1.000 52.81184  ? 331 ASP   A CB     1 
ATOM   2559 C CG     . ASP   A 1 338 ? -1.09352  -20.86446 -0.26692  1.000 60.43544  ? 331 ASP   A CG     1 
ATOM   2560 O OD1    . ASP   A 1 338 ? -1.09799  -20.38130 -1.41925  1.000 51.23372  ? 331 ASP   A OD1    1 
ATOM   2561 O OD2    . ASP   A 1 338 ? -0.08894  -21.40893 0.23617   1.000 50.82662  ? 331 ASP   A OD2    1 
ATOM   2562 N N      . LEU   A 1 339 ? -5.29046  -18.71574 0.16319   1.000 36.04839  ? 332 LEU   A N      1 
ATOM   2563 C CA     . LEU   A 1 339 ? -6.70184  -18.55210 0.46987   1.000 43.81975  ? 332 LEU   A CA     1 
ATOM   2564 C C      . LEU   A 1 339 ? -7.54936  -19.15963 -0.63966  1.000 44.39234  ? 332 LEU   A C      1 
ATOM   2565 O O      . LEU   A 1 339 ? -7.04616  -19.58977 -1.68075  1.000 44.81804  ? 332 LEU   A O      1 
ATOM   2566 C CB     . LEU   A 1 339 ? -7.05114  -17.07108 0.66179   1.000 40.01399  ? 332 LEU   A CB     1 
ATOM   2567 C CG     . LEU   A 1 339 ? -6.23907  -16.34986 1.73856   1.000 41.42441  ? 332 LEU   A CG     1 
ATOM   2568 C CD1    . LEU   A 1 339 ? -6.38956  -14.84245 1.61061   1.000 33.60698  ? 332 LEU   A CD1    1 
ATOM   2569 C CD2    . LEU   A 1 339 ? -6.65363  -16.82290 3.12461   1.000 40.69099  ? 332 LEU   A CD2    1 
ATOM   2570 N N      . LEU   A 1 340 ? -8.85339  -19.19218 -0.40275  1.000 40.95369  ? 333 LEU   A N      1 
ATOM   2571 C CA     . LEU   A 1 340 ? -9.77990  -19.75941 -1.36592  1.000 50.47260  ? 333 LEU   A CA     1 
ATOM   2572 C C      . LEU   A 1 340 ? -10.27545 -18.68920 -2.33058  1.000 43.57333  ? 333 LEU   A C      1 
ATOM   2573 O O      . LEU   A 1 340 ? -10.17182 -17.48660 -2.07684  1.000 39.72539  ? 333 LEU   A O      1 
ATOM   2574 C CB     . LEU   A 1 340 ? -10.95617 -20.42218 -0.65441  1.000 36.43833  ? 333 LEU   A CB     1 
ATOM   2575 C CG     . LEU   A 1 340 ? -10.53598 -21.54454 0.29543   1.000 55.42029  ? 333 LEU   A CG     1 
ATOM   2576 C CD1    . LEU   A 1 340 ? -11.73708 -22.07394 1.02804   1.000 39.22953  ? 333 LEU   A CD1    1 
ATOM   2577 C CD2    . LEU   A 1 340 ? -9.83646  -22.66536 -0.45978  1.000 43.74188  ? 333 LEU   A CD2    1 
ATOM   2578 N N      . ILE   A 1 341 ? -10.82542 -19.15371 -3.45394  1.000 39.93772  ? 334 ILE   A N      1 
ATOM   2579 C CA     . ILE   A 1 341 ? -11.22617 -18.25063 -4.52692  1.000 47.72641  ? 334 ILE   A CA     1 
ATOM   2580 C C      . ILE   A 1 341 ? -12.22071 -17.21126 -4.03046  1.000 44.17585  ? 334 ILE   A C      1 
ATOM   2581 O O      . ILE   A 1 341 ? -12.20811 -16.06136 -4.48735  1.000 40.39725  ? 334 ILE   A O      1 
ATOM   2582 C CB     . ILE   A 1 341 ? -11.79331 -19.06404 -5.70566  1.000 47.87165  ? 334 ILE   A CB     1 
ATOM   2583 C CG1    . ILE   A 1 341 ? -12.16712 -18.14008 -6.86397  1.000 38.73497  ? 334 ILE   A CG1    1 
ATOM   2584 C CG2    . ILE   A 1 341 ? -12.98691 -19.89615 -5.25423  1.000 44.12772  ? 334 ILE   A CG2    1 
ATOM   2585 C CD1    . ILE   A 1 341 ? -12.16116 -18.83125 -8.20599  1.000 57.67554  ? 334 ILE   A CD1    1 
ATOM   2586 N N      . ASP   A 1 342 ? -13.09177 -17.58606 -3.09154  1.000 38.96114  ? 335 ASP   A N      1 
ATOM   2587 C CA     . ASP   A 1 342 ? -14.08633 -16.64027 -2.59621  1.000 45.68490  ? 335 ASP   A CA     1 
ATOM   2588 C C      . ASP   A 1 342 ? -13.45597 -15.60848 -1.67033  1.000 44.52606  ? 335 ASP   A C      1 
ATOM   2589 O O      . ASP   A 1 342 ? -13.86530 -14.44159 -1.66083  1.000 44.75330  ? 335 ASP   A O      1 
ATOM   2590 C CB     . ASP   A 1 342 ? -15.21451 -17.38939 -1.88643  1.000 46.52831  ? 335 ASP   A CB     1 
ATOM   2591 C CG     . ASP   A 1 342 ? -16.20620 -17.99466 -2.85655  1.000 54.43575  ? 335 ASP   A CG     1 
ATOM   2592 O OD1    . ASP   A 1 342 ? -16.60134 -17.29631 -3.81441  1.000 57.20968  ? 335 ASP   A OD1    1 
ATOM   2593 O OD2    . ASP   A 1 342 ? -16.58808 -19.16700 -2.66544  1.000 65.19118  ? 335 ASP   A OD2    1 
ATOM   2594 N N      . GLU   A 1 343 ? -12.46204 -16.01881 -0.88247  1.000 38.15873  ? 336 GLU   A N      1 
ATOM   2595 C CA     . GLU   A 1 343 ? -11.76722 -15.06868 -0.02126  1.000 37.16392  ? 336 GLU   A CA     1 
ATOM   2596 C C      . GLU   A 1 343 ? -10.99234 -14.04911 -0.85007  1.000 37.97994  ? 336 GLU   A C      1 
ATOM   2597 O O      . GLU   A 1 343 ? -11.06011 -12.84264 -0.58815  1.000 42.17700  ? 336 GLU   A O      1 
ATOM   2598 C CB     . GLU   A 1 343 ? -10.85078 -15.81930 0.94585   1.000 41.52854  ? 336 GLU   A CB     1 
ATOM   2599 C CG     . GLU   A 1 343 ? -11.57593 -16.91720 1.71948   1.000 40.03796  ? 336 GLU   A CG     1 
ATOM   2600 C CD     . GLU   A 1 343 ? -10.65358 -17.75276 2.58567   1.000 46.47591  ? 336 GLU   A CD     1 
ATOM   2601 O OE1    . GLU   A 1 343 ? -10.79767 -17.70551 3.82565   1.000 47.71981  ? 336 GLU   A OE1    1 
ATOM   2602 O OE2    . GLU   A 1 343 ? -9.79177  -18.46464 2.02848   1.000 48.09853  ? 336 GLU   A OE2    1 
ATOM   2603 N N      . TRP   A 1 344 ? -10.25627 -14.51373 -1.86478  1.000 31.33146  ? 337 TRP   A N      1 
ATOM   2604 C CA     . TRP   A 1 344 ? -9.64983  -13.58353 -2.81248  1.000 37.14487  ? 337 TRP   A CA     1 
ATOM   2605 C C      . TRP   A 1 344 ? -10.70860 -12.73427 -3.50044  1.000 40.96497  ? 337 TRP   A C      1 
ATOM   2606 O O      . TRP   A 1 344 ? -10.46606 -11.56160 -3.80908  1.000 35.22562  ? 337 TRP   A O      1 
ATOM   2607 C CB     . TRP   A 1 344 ? -8.83393  -14.34127 -3.86245  1.000 32.52701  ? 337 TRP   A CB     1 
ATOM   2608 C CG     . TRP   A 1 344 ? -7.58643  -14.98930 -3.34145  1.000 38.53736  ? 337 TRP   A CG     1 
ATOM   2609 C CD1    . TRP   A 1 344 ? -7.24450  -16.30605 -3.44659  1.000 34.55359  ? 337 TRP   A CD1    1 
ATOM   2610 C CD2    . TRP   A 1 344 ? -6.50841  -14.34984 -2.64557  1.000 39.59192  ? 337 TRP   A CD2    1 
ATOM   2611 N NE1    . TRP   A 1 344 ? -6.02537  -16.52793 -2.85551  1.000 34.58752  ? 337 TRP   A NE1    1 
ATOM   2612 C CE2    . TRP   A 1 344 ? -5.55184  -15.34358 -2.35555  1.000 35.29498  ? 337 TRP   A CE2    1 
ATOM   2613 C CE3    . TRP   A 1 344 ? -6.26066  -13.03541 -2.23727  1.000 29.22709  ? 337 TRP   A CE3    1 
ATOM   2614 C CZ2    . TRP   A 1 344 ? -4.36742  -15.06487 -1.67631  1.000 33.25463  ? 337 TRP   A CZ2    1 
ATOM   2615 C CZ3    . TRP   A 1 344 ? -5.08354  -12.76070 -1.56220  1.000 32.76062  ? 337 TRP   A CZ3    1 
ATOM   2616 C CH2    . TRP   A 1 344 ? -4.15239  -13.77068 -1.28876  1.000 38.86857  ? 337 TRP   A CH2    1 
ATOM   2617 N N      . LYS   A 1 345 ? -11.88526 -13.31193 -3.74860  1.000 37.62674  ? 338 LYS   A N      1 
ATOM   2618 C CA     . LYS   A 1 345 ? -12.95523 -12.58408 -4.42029  1.000 37.38775  ? 338 LYS   A CA     1 
ATOM   2619 C C      . LYS   A 1 345 ? -13.50479 -11.46920 -3.53924  1.000 41.43040  ? 338 LYS   A C      1 
ATOM   2620 O O      . LYS   A 1 345 ? -13.77592 -10.36361 -4.02258  1.000 36.80074  ? 338 LYS   A O      1 
ATOM   2621 C CB     . LYS   A 1 345 ? -14.06270 -13.56039 -4.81153  1.000 42.06784  ? 338 LYS   A CB     1 
ATOM   2622 C CG     . LYS   A 1 345 ? -15.09129 -13.02118 -5.78274  1.000 43.23753  ? 338 LYS   A CG     1 
ATOM   2623 C CD     . LYS   A 1 345 ? -15.79615 -14.17712 -6.47135  1.000 43.17001  ? 338 LYS   A CD     1 
ATOM   2624 C CE     . LYS   A 1 345 ? -16.98729 -13.71091 -7.27885  1.000 48.24258  ? 338 LYS   A CE     1 
ATOM   2625 N NZ     . LYS   A 1 345 ? -17.45608 -14.76004 -8.22598  1.000 48.52114  ? 338 LYS   A NZ     1 
ATOM   2626 N N      . SER   A 1 346 ? -13.67402 -11.74018 -2.24292  1.000 37.19581  ? 339 SER   A N      1 
ATOM   2627 C CA     . SER   A 1 346 ? -14.24296 -10.73943 -1.34612  1.000 37.92703  ? 339 SER   A CA     1 
ATOM   2628 C C      . SER   A 1 346 ? -13.24832 -9.62098  -1.05886  1.000 37.68386  ? 339 SER   A C      1 
ATOM   2629 O O      . SER   A 1 346 ? -13.62575 -8.44396  -1.01350  1.000 32.04900  ? 339 SER   A O      1 
ATOM   2630 C CB     . SER   A 1 346 ? -14.70017 -11.40243 -0.04728  1.000 40.70573  ? 339 SER   A CB     1 
ATOM   2631 O OG     . SER   A 1 346 ? -15.31662 -10.46325 0.81510   1.000 42.27611  ? 339 SER   A OG     1 
ATOM   2632 N N      . LEU   A 1 347 ? -11.97486 -9.96653  -0.85538  1.000 36.50768  ? 340 LEU   A N      1 
ATOM   2633 C CA     . LEU   A 1 347 ? -10.96033 -8.93843  -0.64742  1.000 38.33779  ? 340 LEU   A CA     1 
ATOM   2634 C C      . LEU   A 1 347 ? -10.88407 -7.99596  -1.84172  1.000 31.30844  ? 340 LEU   A C      1 
ATOM   2635 O O      . LEU   A 1 347 ? -10.75860 -6.77701  -1.67450  1.000 31.90598  ? 340 LEU   A O      1 
ATOM   2636 C CB     . LEU   A 1 347 ? -9.60170  -9.58696  -0.38424  1.000 32.61967  ? 340 LEU   A CB     1 
ATOM   2637 C CG     . LEU   A 1 347 ? -9.51452  -10.48196 0.85350   1.000 34.97475  ? 340 LEU   A CG     1 
ATOM   2638 C CD1    . LEU   A 1 347 ? -8.19303  -11.23423 0.88232   1.000 35.84571  ? 340 LEU   A CD1    1 
ATOM   2639 C CD2    . LEU   A 1 347 ? -9.69797  -9.66348  2.12216   1.000 32.39264  ? 340 LEU   A CD2    1 
ATOM   2640 N N      . THR   A 1 348 ? -10.95923 -8.54296  -3.05748  1.000 28.53863  ? 341 THR   A N      1 
ATOM   2641 C CA     . THR   A 1 348 ? -10.96844 -7.69807  -4.24669  1.000 29.72518  ? 341 THR   A CA     1 
ATOM   2642 C C      . THR   A 1 348 ? -12.21082 -6.81926  -4.28398  1.000 38.05017  ? 341 THR   A C      1 
ATOM   2643 O O      . THR   A 1 348 ? -12.12994 -5.62857  -4.60876  1.000 33.90829  ? 341 THR   A O      1 
ATOM   2644 C CB     . THR   A 1 348 ? -10.88923 -8.55728  -5.50726  1.000 31.73466  ? 341 THR   A CB     1 
ATOM   2645 O OG1    . THR   A 1 348 ? -9.67365  -9.31531  -5.49563  1.000 30.78933  ? 341 THR   A OG1    1 
ATOM   2646 C CG2    . THR   A 1 348 ? -10.92949 -7.67953  -6.75256  1.000 26.51460  ? 341 THR   A CG2    1 
ATOM   2647 N N      . TYR   A 1 349 ? -13.37378 -7.39184  -3.96491  1.000 38.97843  ? 342 TYR   A N      1 
ATOM   2648 C CA     . TYR   A 1 349 ? -14.58851 -6.58845  -3.88713  1.000 41.57132  ? 342 TYR   A CA     1 
ATOM   2649 C C      . TYR   A 1 349 ? -14.43509 -5.47151  -2.86428  1.000 35.72641  ? 342 TYR   A C      1 
ATOM   2650 O O      . TYR   A 1 349 ? -14.85140 -4.33272  -3.10789  1.000 34.32416  ? 342 TYR   A O      1 
ATOM   2651 C CB     . TYR   A 1 349 ? -15.78380 -7.47712  -3.54375  1.000 40.41330  ? 342 TYR   A CB     1 
ATOM   2652 C CG     . TYR   A 1 349 ? -17.11731 -6.77111  -3.62865  1.000 41.84093  ? 342 TYR   A CG     1 
ATOM   2653 C CD1    . TYR   A 1 349 ? -17.69472 -6.48185  -4.85784  1.000 46.47874  ? 342 TYR   A CD1    1 
ATOM   2654 C CD2    . TYR   A 1 349 ? -17.80061 -6.39571  -2.47963  1.000 44.10452  ? 342 TYR   A CD2    1 
ATOM   2655 C CE1    . TYR   A 1 349 ? -18.91432 -5.83725  -4.94056  1.000 46.33779  ? 342 TYR   A CE1    1 
ATOM   2656 C CE2    . TYR   A 1 349 ? -19.02031 -5.75093  -2.55227  1.000 46.54800  ? 342 TYR   A CE2    1 
ATOM   2657 C CZ     . TYR   A 1 349 ? -19.57242 -5.47413  -3.78488  1.000 48.77788  ? 342 TYR   A CZ     1 
ATOM   2658 O OH     . TYR   A 1 349 ? -20.78674 -4.83237  -3.86306  1.000 42.10063  ? 342 TYR   A OH     1 
ATOM   2659 N N      . ASP   A 1 350 ? -13.83216 -5.77950  -1.71351  1.000 36.27654  ? 343 ASP   A N      1 
ATOM   2660 C CA     . ASP   A 1 350 ? -13.56920 -4.74993  -0.71405  1.000 33.16184  ? 343 ASP   A CA     1 
ATOM   2661 C C      . ASP   A 1 350 ? -12.72448 -3.62283  -1.29245  1.000 38.52350  ? 343 ASP   A C      1 
ATOM   2662 O O      . ASP   A 1 350 ? -12.95925 -2.44510  -0.99677  1.000 42.48264  ? 343 ASP   A O      1 
ATOM   2663 C CB     . ASP   A 1 350 ? -12.87350 -5.36307  0.50134   1.000 34.52370  ? 343 ASP   A CB     1 
ATOM   2664 C CG     . ASP   A 1 350 ? -13.82471 -6.13465  1.39110   1.000 40.46544  ? 343 ASP   A CG     1 
ATOM   2665 O OD1    . ASP   A 1 350 ? -15.05201 -5.94028  1.26443   1.000 40.91863  ? 343 ASP   A OD1    1 
ATOM   2666 O OD2    . ASP   A 1 350 ? -13.34318 -6.93444  2.22069   1.000 43.50335  ? 343 ASP   A OD2    1 
ATOM   2667 N N      . GLU   A 1 351 ? -11.73317 -3.96410  -2.11880  1.000 37.78128  ? 344 GLU   A N      1 
ATOM   2668 C CA     . GLU   A 1 351 ? -10.85678 -2.94089  -2.67787  1.000 36.06893  ? 344 GLU   A CA     1 
ATOM   2669 C C      . GLU   A 1 351 ? -11.57391 -2.09093  -3.71880  1.000 36.19512  ? 344 GLU   A C      1 
ATOM   2670 O O      . GLU   A 1 351 ? -11.26083 -0.90420  -3.86797  1.000 37.32053  ? 344 GLU   A O      1 
ATOM   2671 C CB     . GLU   A 1 351 ? -9.60934  -3.58731  -3.28156  1.000 30.61994  ? 344 GLU   A CB     1 
ATOM   2672 C CG     . GLU   A 1 351 ? -8.68439  -4.22741  -2.25533  1.000 31.03815  ? 344 GLU   A CG     1 
ATOM   2673 C CD     . GLU   A 1 351 ? -8.09222  -3.21841  -1.28624  1.000 38.25584  ? 344 GLU   A CD     1 
ATOM   2674 O OE1    . GLU   A 1 351 ? -7.70327  -2.11799  -1.73155  1.000 31.54958  ? 344 GLU   A OE1    1 
ATOM   2675 O OE2    . GLU   A 1 351 ? -8.01560  -3.52725  -0.07775  1.000 39.35378  ? 344 GLU   A OE2    1 
ATOM   2676 N N      . VAL   A 1 352 ? -12.53002 -2.67037  -4.44718  1.000 34.60545  ? 345 VAL   A N      1 
ATOM   2677 C CA     . VAL   A 1 352 ? -13.30457 -1.87810  -5.39675  1.000 39.71216  ? 345 VAL   A CA     1 
ATOM   2678 C C      . VAL   A 1 352 ? -14.18034 -0.87343  -4.65874  1.000 45.27506  ? 345 VAL   A C      1 
ATOM   2679 O O      . VAL   A 1 352 ? -14.27620 0.29529   -5.05169  1.000 45.61722  ? 345 VAL   A O      1 
ATOM   2680 C CB     . VAL   A 1 352 ? -14.14070 -2.79513  -6.30770  1.000 36.33273  ? 345 VAL   A CB     1 
ATOM   2681 C CG1    . VAL   A 1 352 ? -14.93332 -1.96638  -7.31024  1.000 30.04302  ? 345 VAL   A CG1    1 
ATOM   2682 C CG2    . VAL   A 1 352 ? -13.24605 -3.79664  -7.02223  1.000 34.30732  ? 345 VAL   A CG2    1 
ATOM   2683 N N      . ILE   A 1 353 ? -14.82168 -1.30682  -3.57182  1.000 40.16703  ? 346 ILE   A N      1 
ATOM   2684 C CA     . ILE   A 1 353 ? -15.73195 -0.42942  -2.84342  1.000 42.09114  ? 346 ILE   A CA     1 
ATOM   2685 C C      . ILE   A 1 353 ? -14.96642 0.69355   -2.15419  1.000 42.72782  ? 346 ILE   A C      1 
ATOM   2686 O O      . ILE   A 1 353 ? -15.45789 1.82359   -2.04949  1.000 52.91947  ? 346 ILE   A O      1 
ATOM   2687 C CB     . ILE   A 1 353 ? -16.56498 -1.24451  -1.83766  1.000 53.12869  ? 346 ILE   A CB     1 
ATOM   2688 C CG1    . ILE   A 1 353 ? -17.09498 -2.52255  -2.49208  1.000 44.80940  ? 346 ILE   A CG1    1 
ATOM   2689 C CG2    . ILE   A 1 353 ? -17.70795 -0.40426  -1.28860  1.000 52.91453  ? 346 ILE   A CG2    1 
ATOM   2690 C CD1    . ILE   A 1 353 ? -18.43237 -2.34987  -3.17691  1.000 51.21455  ? 346 ILE   A CD1    1 
ATOM   2691 N N      . SER   A 1 354 ? -13.75771 0.40810   -1.67438  1.000 46.00465  ? 347 SER   A N      1 
ATOM   2692 C CA     . SER   A 1 354 ? -12.98743 1.38521   -0.91385  1.000 39.48283  ? 347 SER   A CA     1 
ATOM   2693 C C      . SER   A 1 354 ? -12.21236 2.36166   -1.79098  1.000 40.89657  ? 347 SER   A C      1 
ATOM   2694 O O      . SER   A 1 354 ? -11.51953 3.23092   -1.25146  1.000 41.85301  ? 347 SER   A O      1 
ATOM   2695 C CB     . SER   A 1 354 ? -12.01784 0.66706   0.02870   1.000 34.38070  ? 347 SER   A CB     1 
ATOM   2696 O OG     . SER   A 1 354 ? -11.15058 -0.19162  -0.69150  1.000 34.86862  ? 347 SER   A OG     1 
ATOM   2697 N N      . PHE   A 1 355 ? -12.31005 2.25173   -3.11343  1.000 41.02012  ? 348 PHE   A N      1 
ATOM   2698 C CA     . PHE   A 1 355 ? -11.52878 3.11335   -3.99025  1.000 40.06578  ? 348 PHE   A CA     1 
ATOM   2699 C C      . PHE   A 1 355 ? -11.97848 4.56447   -3.87049  1.000 34.16349  ? 348 PHE   A C      1 
ATOM   2700 O O      . PHE   A 1 355 ? -13.17417 4.85975   -3.79314  1.000 43.64850  ? 348 PHE   A O      1 
ATOM   2701 C CB     . PHE   A 1 355 ? -11.64801 2.64945   -5.44239  1.000 33.80707  ? 348 PHE   A CB     1 
ATOM   2702 C CG     . PHE   A 1 355 ? -10.91098 3.52432   -6.42078  1.000 36.48255  ? 348 PHE   A CG     1 
ATOM   2703 C CD1    . PHE   A 1 355 ? -9.53638  3.42418   -6.56196  1.000 31.25530  ? 348 PHE   A CD1    1 
ATOM   2704 C CD2    . PHE   A 1 355 ? -11.59265 4.44893   -7.19632  1.000 32.54495  ? 348 PHE   A CD2    1 
ATOM   2705 C CE1    . PHE   A 1 355 ? -8.85527  4.22830   -7.45929  1.000 33.40750  ? 348 PHE   A CE1    1 
ATOM   2706 C CE2    . PHE   A 1 355 ? -10.91669 5.25605   -8.09563  1.000 34.04339  ? 348 PHE   A CE2    1 
ATOM   2707 C CZ     . PHE   A 1 355 ? -9.54638  5.14494   -8.22696  1.000 30.46659  ? 348 PHE   A CZ     1 
ATOM   2708 N N      . VAL   A 1 356 ? -11.00804 5.47099   -3.85478  1.000 42.92772  ? 349 VAL   A N      1 
ATOM   2709 C CA     . VAL   A 1 356 ? -11.25039 6.90690   -3.86242  1.000 44.93410  ? 349 VAL   A CA     1 
ATOM   2710 C C      . VAL   A 1 356 ? -10.55689 7.48444   -5.09082  1.000 38.53548  ? 349 VAL   A C      1 
ATOM   2711 O O      . VAL   A 1 356 ? -9.32758  7.43039   -5.18746  1.000 41.16671  ? 349 VAL   A O      1 
ATOM   2712 C CB     . VAL   A 1 356 ? -10.74501 7.59358   -2.58246  1.000 47.20774  ? 349 VAL   A CB     1 
ATOM   2713 C CG1    . VAL   A 1 356 ? -11.06046 9.08392   -2.62025  1.000 38.34961  ? 349 VAL   A CG1    1 
ATOM   2714 C CG2    . VAL   A 1 356 ? -11.35844 6.94280   -1.35132  1.000 46.55531  ? 349 VAL   A CG2    1 
ATOM   2715 N N      . PRO   A 1 357 ? -11.29034 8.03795   -6.05401  1.000 42.43410  ? 350 PRO   A N      1 
ATOM   2716 C CA     . PRO   A 1 357 ? -10.63758 8.58201   -7.23877  1.000 48.55239  ? 350 PRO   A CA     1 
ATOM   2717 C C      . PRO   A 1 357 ? -9.74399  9.74725   -6.87034  1.000 46.76389  ? 350 PRO   A C      1 
ATOM   2718 O O      . PRO   A 1 357 ? -10.00349 10.46792  -5.88792  1.000 48.17424  ? 350 PRO   A O      1 
ATOM   2719 C CB     . PRO   A 1 357 ? -11.81569 9.03086   -8.11551  1.000 45.57757  ? 350 PRO   A CB     1 
ATOM   2720 C CG     . PRO   A 1 357 ? -12.94626 9.22818   -7.15935  1.000 46.53249  ? 350 PRO   A CG     1 
ATOM   2721 C CD     . PRO   A 1 357 ? -12.75476 8.17516   -6.11306  1.000 41.08707  ? 350 PRO   A CD     1 
ATOM   2722 N N      . PRO   A 1 358 ? -8.66901  9.97019   -7.62906  1.000 48.55749  ? 351 PRO   A N      1 
ATOM   2723 C CA     . PRO   A 1 358 ? -7.85717  11.16065  -7.40062  1.000 61.80070  ? 351 PRO   A CA     1 
ATOM   2724 C C      . PRO   A 1 358 ? -8.61027  12.40565  -7.82541  1.000 63.28877  ? 351 PRO   A C      1 
ATOM   2725 O O      . PRO   A 1 358 ? -9.48987  12.34879  -8.70290  1.000 52.45675  ? 351 PRO   A O      1 
ATOM   2726 C CB     . PRO   A 1 358 ? -6.62012  10.92068  -8.28526  1.000 55.66154  ? 351 PRO   A CB     1 
ATOM   2727 C CG     . PRO   A 1 358 ? -7.10028  10.00635  -9.35570  1.000 50.56054  ? 351 PRO   A CG     1 
ATOM   2728 C CD     . PRO   A 1 358 ? -8.13767  9.12797   -8.71467  1.000 48.87928  ? 351 PRO   A CD     1 
ATOM   2729 N N      . PRO   A 1 359 ? -8.30668  13.55818  -7.22983  1.000 69.89684  ? 352 PRO   A N      1 
ATOM   2730 C CA     . PRO   A 1 359 ? -9.03162  14.78477  -7.58693  1.000 78.85329  ? 352 PRO   A CA     1 
ATOM   2731 C C      . PRO   A 1 359 ? -8.62796  15.27631  -8.96963  1.000 83.31936  ? 352 PRO   A C      1 
ATOM   2732 O O      . PRO   A 1 359 ? -7.44059  15.37243  -9.28829  1.000 83.41070  ? 352 PRO   A O      1 
ATOM   2733 C CB     . PRO   A 1 359 ? -8.61618  15.77318  -6.49223  1.000 80.63283  ? 352 PRO   A CB     1 
ATOM   2734 C CG     . PRO   A 1 359 ? -7.27177  15.29195  -6.05293  1.000 79.27386  ? 352 PRO   A CG     1 
ATOM   2735 C CD     . PRO   A 1 359 ? -7.29395  13.79142  -6.18516  1.000 70.48357  ? 352 PRO   A CD     1 
ATOM   2736 N N      . LEU   A 1 360 ? -9.62830  15.58726  -9.79077  1.000 74.97818  ? 353 LEU   A N      1 
ATOM   2737 C CA     . LEU   A 1 360 ? -9.36417  16.12800  -11.11757 1.000 82.79285  ? 353 LEU   A CA     1 
ATOM   2738 C C      . LEU   A 1 360 ? -8.65877  17.47288  -11.00018 1.000 86.63983  ? 353 LEU   A C      1 
ATOM   2739 O O      . LEU   A 1 360 ? -9.19428  18.41211  -10.40269 1.000 82.18784  ? 353 LEU   A O      1 
ATOM   2740 C CB     . LEU   A 1 360 ? -10.66886 16.27250  -11.89881 1.000 80.89522  ? 353 LEU   A CB     1 
ATOM   2741 C CG     . LEU   A 1 360 ? -10.52252 16.78263  -13.33388 1.000 87.13780  ? 353 LEU   A CG     1 
ATOM   2742 C CD1    . LEU   A 1 360 ? -9.40187  16.04482  -14.05334 1.000 76.29579  ? 353 LEU   A CD1    1 
ATOM   2743 C CD2    . LEU   A 1 360 ? -11.83397 16.65325  -14.09152 1.000 72.66656  ? 353 LEU   A CD2    1 
ATOM   2744 N N      . ASP   A 1 361 ? -7.45917  17.55552  -11.57328 1.000 88.79463  ? 354 ASP   A N      1 
ATOM   2745 C CA     . ASP   A 1 361 ? -6.59677  18.73743  -11.49042 1.000 80.90115  ? 354 ASP   A CA     1 
ATOM   2746 C C      . ASP   A 1 361 ? -7.36336  20.05401  -11.38941 1.000 70.89195  ? 354 ASP   A C      1 
ATOM   2747 O O      . ASP   A 1 361 ? -8.28663  20.30881  -12.16163 1.000 84.95115  ? 354 ASP   A O      1 
ATOM   2748 C CB     . ASP   A 1 361 ? -5.66480  18.78801  -12.70408 1.000 81.33525  ? 354 ASP   A CB     1 
ATOM   2749 C CG     . ASP   A 1 361 ? -4.67361  17.64071  -12.72749 1.000 72.24641  ? 354 ASP   A CG     1 
ATOM   2750 O OD1    . ASP   A 1 361 ? -5.10196  16.47818  -12.56845 1.000 66.30306  ? 354 ASP   A OD1    1 
ATOM   2751 O OD2    . ASP   A 1 361 ? -3.46601  17.90191  -12.90758 1.000 77.47076  ? 354 ASP   A OD2    1 
HETATM 2752 C C1     . BOG   B 2 .   ? 24.23670  -11.63110 -8.00696  1.000 45.09504  ? 601 BOG   A C1     1 
HETATM 2753 O O1     . BOG   B 2 .   ? 24.63247  -10.98320 -9.17947  1.000 34.71184  ? 601 BOG   A O1     1 
HETATM 2754 C C2     . BOG   B 2 .   ? 24.95234  -11.01063 -6.80873  1.000 44.60847  ? 601 BOG   A C2     1 
HETATM 2755 O O2     . BOG   B 2 .   ? 26.33707  -11.05357 -6.98794  1.000 51.36505  ? 601 BOG   A O2     1 
HETATM 2756 C C3     . BOG   B 2 .   ? 24.56532  -11.80570 -5.56415  1.000 42.85798  ? 601 BOG   A C3     1 
HETATM 2757 O O3     . BOG   B 2 .   ? 25.09057  -11.18673 -4.42541  1.000 42.46941  ? 601 BOG   A O3     1 
HETATM 2758 C C4     . BOG   B 2 .   ? 23.04284  -11.85974 -5.46192  1.000 45.24291  ? 601 BOG   A C4     1 
HETATM 2759 O O4     . BOG   B 2 .   ? 22.67565  -12.75566 -4.44582  1.000 52.27672  ? 601 BOG   A O4     1 
HETATM 2760 C C5     . BOG   B 2 .   ? 22.41821  -12.31132 -6.78402  1.000 48.26482  ? 601 BOG   A C5     1 
HETATM 2761 O O5     . BOG   B 2 .   ? 22.85187  -11.49775 -7.83704  1.000 45.64667  ? 601 BOG   A O5     1 
HETATM 2762 C C6     . BOG   B 2 .   ? 20.89805  -12.21144 -6.63699  1.000 44.73097  ? 601 BOG   A C6     1 
HETATM 2763 O O6     . BOG   B 2 .   ? 20.27961  -12.28124 -7.89181  1.000 54.77425  ? 601 BOG   A O6     1 
HETATM 2764 C "C1'"  . BOG   B 2 .   ? 24.21737  -11.63856 -10.34374 1.000 39.95789  ? 601 BOG   A "C1'"  1 
HETATM 2765 C "C2'"  . BOG   B 2 .   ? 25.39732  -12.37988 -10.96687 1.000 37.58898  ? 601 BOG   A "C2'"  1 
HETATM 2766 C "C3'"  . BOG   B 2 .   ? 25.00636  -12.89039 -12.35250 1.000 44.87074  ? 601 BOG   A "C3'"  1 
HETATM 2767 C "C4'"  . BOG   B 2 .   ? 26.21951  -13.54461 -13.01071 1.000 44.58931  ? 601 BOG   A "C4'"  1 
HETATM 2768 C "C5'"  . BOG   B 2 .   ? 25.77058  -14.35794 -14.22317 1.000 50.78569  ? 601 BOG   A "C5'"  1 
HETATM 2769 C "C6'"  . BOG   B 2 .   ? 26.99894  -14.87503 -14.96898 1.000 47.46410  ? 601 BOG   A "C6'"  1 
HETATM 2770 C "C7'"  . BOG   B 2 .   ? 26.67599  -15.02109 -16.45450 1.000 51.46269  ? 601 BOG   A "C7'"  1 
HETATM 2771 C "C8'"  . BOG   B 2 .   ? 25.82564  -16.26934 -16.67687 1.000 47.13711  ? 601 BOG   A "C8'"  1 
HETATM 2772 H H1     . BOG   B 2 .   ? 24.46674  -12.57121 -8.07159  1.000 54.14517  ? 601 BOG   A H1     1 
HETATM 2773 H H2     . BOG   B 2 .   ? 24.69110  -10.08129 -6.71402  1.000 53.56129  ? 601 BOG   A H2     1 
HETATM 2774 H HO2    . BOG   B 2 .   ? 26.70318  -11.24559 -6.24737  1.000 61.66918  ? 601 BOG   A HO2    1 
HETATM 2775 H H3     . BOG   B 2 .   ? 24.92216  -12.70541 -5.62817  1.000 51.46070  ? 601 BOG   A H3     1 
HETATM 2776 H HO3    . BOG   B 2 .   ? 25.68220  -10.62661 -4.66407  1.000 50.99441  ? 601 BOG   A HO3    1 
HETATM 2777 H H4     . BOG   B 2 .   ? 22.71816  -10.96903 -5.25668  1.000 54.32262  ? 601 BOG   A H4     1 
HETATM 2778 H HO4    . BOG   B 2 .   ? 23.36785  -13.00397 -4.01726  1.000 62.76319  ? 601 BOG   A HO4    1 
HETATM 2779 H H5     . BOG   B 2 .   ? 22.68445  -13.22219 -6.98483  1.000 57.94891  ? 601 BOG   A H5     1 
HETATM 2780 H H61    . BOG   B 2 .   ? 20.67259  -11.36703 -6.21624  1.000 53.70829  ? 601 BOG   A H61    1 
HETATM 2781 H H62    . BOG   B 2 .   ? 20.58186  -12.94287 -6.08387  1.000 53.70829  ? 601 BOG   A H62    1 
HETATM 2782 H HO6    . BOG   B 2 .   ? 19.87837  -13.02679 -7.96708  1.000 65.76023  ? 601 BOG   A HO6    1 
HETATM 2783 H "H1'1" . BOG   B 2 .   ? 23.87596  -10.98697 -10.97602 1.000 47.98059  ? 601 BOG   A "H1'1" 1 
HETATM 2784 H "H1'2" . BOG   B 2 .   ? 23.51762  -12.27340 -10.12413 1.000 47.98059  ? 601 BOG   A "H1'2" 1 
HETATM 2785 H "H2'1" . BOG   B 2 .   ? 25.64130  -13.13054 -10.40306 1.000 45.13791  ? 601 BOG   A "H2'1" 1 
HETATM 2786 H "H2'2" . BOG   B 2 .   ? 26.15247  -11.77627 -11.04625 1.000 45.13791  ? 601 BOG   A "H2'2" 1 
HETATM 2787 H "H3'1" . BOG   B 2 .   ? 24.29279  -13.54202 -12.26823 1.000 53.87601  ? 601 BOG   A "H3'1" 1 
HETATM 2788 H "H3'2" . BOG   B 2 .   ? 24.70318  -12.14764 -12.89776 1.000 53.87601  ? 601 BOG   A "H3'2" 1 
HETATM 2789 H "H4'1" . BOG   B 2 .   ? 26.65565  -14.13078 -12.37268 1.000 53.53830  ? 601 BOG   A "H4'1" 1 
HETATM 2790 H "H4'2" . BOG   B 2 .   ? 26.84158  -12.85714 -13.29589 1.000 53.53830  ? 601 BOG   A "H4'2" 1 
HETATM 2791 H "H5'1" . BOG   B 2 .   ? 25.24600  -13.79542 -14.81417 1.000 60.97395  ? 601 BOG   A "H5'1" 1 
HETATM 2792 H "H5'2" . BOG   B 2 .   ? 25.23134  -15.10829 -13.92806 1.000 60.97395  ? 601 BOG   A "H5'2" 1 
HETATM 2793 H "H6'1" . BOG   B 2 .   ? 27.25529  -15.73826 -14.60841 1.000 56.98805  ? 601 BOG   A "H6'1" 1 
HETATM 2794 H "H6'2" . BOG   B 2 .   ? 27.73084  -14.24815 -14.85830 1.000 56.98805  ? 601 BOG   A "H6'2" 1 
HETATM 2795 H "H7'1" . BOG   B 2 .   ? 27.50159  -15.09972 -16.95758 1.000 61.78636  ? 601 BOG   A "H7'1" 1 
HETATM 2796 H "H7'2" . BOG   B 2 .   ? 26.18665  -14.23981 -16.75626 1.000 61.78636  ? 601 BOG   A "H7'2" 1 
HETATM 2797 H "H8'1" . BOG   B 2 .   ? 25.53662  -16.30303 -17.60220 1.000 56.59566  ? 601 BOG   A "H8'1" 1 
HETATM 2798 H "H8'2" . BOG   B 2 .   ? 26.35100  -17.05892 -16.47325 1.000 56.59566  ? 601 BOG   A "H8'2" 1 
HETATM 2799 H "H8'3" . BOG   B 2 .   ? 25.04905  -16.23913 -16.09645 1.000 56.59566  ? 601 BOG   A "H8'3" 1 
HETATM 2800 C C1     . A1ACP C 3 .   ? -1.35258  2.43535   -24.24764 1.000 41.22218  ? 602 A1ACP A C1     1 
HETATM 2801 C C2     . A1ACP C 3 .   ? -1.99430  1.43549   -22.14522 1.000 45.23908  ? 602 A1ACP A C2     1 
HETATM 2802 N N3     . A1ACP C 3 .   ? -2.83981  -1.38163  -19.06762 1.000 41.42542  ? 602 A1ACP A N3     1 
HETATM 2803 C C4     . A1ACP C 3 .   ? -2.52875  3.35905   -21.05632 1.000 41.51903  ? 602 A1ACP A C4     1 
HETATM 2804 C C5     . A1ACP C 3 .   ? -1.80845  0.08064   -22.36884 1.000 37.36623  ? 602 A1ACP A C5     1 
HETATM 2805 C C6     . A1ACP C 3 .   ? -2.09227  -0.81502  -21.34481 1.000 37.08476  ? 602 A1ACP A C6     1 
HETATM 2806 C C7     . A1ACP C 3 .   ? -2.56263  -0.37378  -20.10355 1.000 36.06567  ? 602 A1ACP A C7     1 
HETATM 2807 C C8     . A1ACP C 3 .   ? -2.75380  0.99991   -19.86510 1.000 34.74193  ? 602 A1ACP A C8     1 
HETATM 2808 C C9     . A1ACP C 3 .   ? -3.53358  -1.03371  -17.81943 1.000 40.14319  ? 602 A1ACP A C9     1 
HETATM 2809 C C10    . A1ACP C 3 .   ? -1.98466  3.14898   -25.28395 1.000 44.90810  ? 602 A1ACP A C10    1 
HETATM 2810 C C11    . A1ACP C 3 .   ? -1.40434  2.94354   -26.52643 1.000 38.88371  ? 602 A1ACP A C11    1 
HETATM 2811 C C12    . A1ACP C 3 .   ? -0.26485  1.66133   -24.71878 1.000 47.94829  ? 602 A1ACP A C12    1 
HETATM 2812 C C13    . A1ACP C 3 .   ? -1.92318  3.62629   -27.80392 1.000 51.13618  ? 602 A1ACP A C13    1 
HETATM 2813 C C14    . A1ACP C 3 .   ? -3.30080  5.60311   -28.91135 1.000 52.89701  ? 602 A1ACP A C14    1 
HETATM 2814 C C15    . A1ACP C 3 .   ? -4.85164  -0.55623  -17.84504 1.000 34.85805  ? 602 A1ACP A C15    1 
HETATM 2815 C C16    . A1ACP C 3 .   ? -5.50040  -0.23380  -16.64183 1.000 32.52055  ? 602 A1ACP A C16    1 
HETATM 2816 C C17    . A1ACP C 3 .   ? -4.83078  -0.39144  -15.42482 1.000 33.41107  ? 602 A1ACP A C17    1 
HETATM 2817 C C18    . A1ACP C 3 .   ? -3.52416  -0.86798  -15.40662 1.000 38.89991  ? 602 A1ACP A C18    1 
HETATM 2818 C C19    . A1ACP C 3 .   ? -2.88774  -1.18602  -16.59547 1.000 35.02543  ? 602 A1ACP A C19    1 
HETATM 2819 C C20    . A1ACP C 3 .   ? -4.27446  4.83462   -29.53885 1.000 41.71036  ? 602 A1ACP A C20    1 
HETATM 2820 C C21    . A1ACP C 3 .   ? -4.02252  6.72577   -28.51590 1.000 50.53176  ? 602 A1ACP A C21    1 
HETATM 2821 C C22    . A1ACP C 3 .   ? -6.20417  0.82275   -19.22646 1.000 34.48146  ? 602 A1ACP A C22    1 
HETATM 2822 C C3     . A1ACP C 3 .   ? -2.47188  1.91831   -20.88688 1.000 35.57166  ? 602 A1ACP A C3     1 
HETATM 2823 F F1     . A1ACP C 3 .   ? -1.91261  -2.15440  -21.55369 1.000 41.33052  ? 602 A1ACP A F1     1 
HETATM 2824 N N1     . A1ACP C 3 .   ? -1.82339  2.50562   -22.85953 1.000 41.42764  ? 602 A1ACP A N1     1 
HETATM 2825 N N2     . A1ACP C 3 .   ? -2.12439  3.63770   -22.28121 1.000 40.88825  ? 602 A1ACP A N2     1 
HETATM 2826 N N4     . A1ACP C 3 .   ? -2.72909  4.84336   -27.65280 1.000 39.99374  ? 602 A1ACP A N4     1 
HETATM 2827 O O1     . A1ACP C 3 .   ? -1.68099  3.17443   -28.87681 1.000 49.07947  ? 602 A1ACP A O1     1 
HETATM 2828 O O2     . A1ACP C 3 .   ? -5.36671  5.87193   -28.89273 1.000 47.25903  ? 602 A1ACP A O2     1 
HETATM 2829 O O3     . A1ACP C 3 .   ? -5.51501  -0.40330  -19.08120 1.000 43.07780  ? 602 A1ACP A O3     1 
HETATM 2830 S S1     . A1ACP C 3 .   ? -0.08201  1.87094   -26.42568 1.000 37.20595  ? 602 A1ACP A S1     1 
HETATM 2831 H H4     . A1ACP C 3 .   ? -2.58963  -2.19440  -19.19577 1.000 49.74163  ? 602 A1ACP A H4     1 
HETATM 2832 H H1     . A1ACP C 3 .   ? -2.80152  3.97570   -20.41581 1.000 49.85396  ? 602 A1ACP A H1     1 
HETATM 2833 H H2     . A1ACP C 3 .   ? -1.49876  -0.22447  -23.19097 1.000 44.87060  ? 602 A1ACP A H2     1 
HETATM 2834 H H3     . A1ACP C 3 .   ? -3.06354  1.29532   -19.03945 1.000 41.72144  ? 602 A1ACP A H3     1 
HETATM 2835 H H5     . A1ACP C 3 .   ? -2.71893  3.70340   -25.14845 1.000 53.92085  ? 602 A1ACP A H5     1 
HETATM 2836 H H6     . A1ACP C 3 .   ? 0.27290   1.11926   -24.18787 1.000 57.56907  ? 602 A1ACP A H6     1 
HETATM 2837 H H8     . A1ACP C 3 .   ? -2.59126  5.84300   -29.52772 1.000 63.50754  ? 602 A1ACP A H8     1 
HETATM 2838 H H9     . A1ACP C 3 .   ? -6.37426  0.08415   -16.65469 1.000 39.05579  ? 602 A1ACP A H9     1 
HETATM 2839 H H10    . A1ACP C 3 .   ? -5.25894  -0.17769  -14.62740 1.000 40.12441  ? 602 A1ACP A H10    1 
HETATM 2840 H H11    . A1ACP C 3 .   ? -3.07821  -0.97300  -14.59731 1.000 46.71102  ? 602 A1ACP A H11    1 
HETATM 2841 H H12    . A1ACP C 3 .   ? -2.01492  -1.50646  -16.57550 1.000 42.06165  ? 602 A1ACP A H12    1 
HETATM 2842 H H13    . A1ACP C 3 .   ? -4.34225  3.93670   -29.17823 1.000 50.08356  ? 602 A1ACP A H13    1 
HETATM 2843 H H14    . A1ACP C 3 .   ? -4.23134  4.88100   -30.50678 1.000 50.08356  ? 602 A1ACP A H14    1 
HETATM 2844 H H16    . A1ACP C 3 .   ? -3.88309  7.49175   -29.09447 1.000 60.66924  ? 602 A1ACP A H16    1 
HETATM 2845 H H15    . A1ACP C 3 .   ? -3.94445  6.91450   -27.56765 1.000 60.66924  ? 602 A1ACP A H15    1 
HETATM 2846 H H17    . A1ACP C 3 .   ? -6.42733  0.95951   -20.16049 1.000 41.40888  ? 602 A1ACP A H17    1 
HETATM 2847 H H18    . A1ACP C 3 .   ? -5.63973  1.54929   -18.91913 1.000 41.40888  ? 602 A1ACP A H18    1 
HETATM 2848 H H19    . A1ACP C 3 .   ? -7.01819  0.80050   -18.69942 1.000 41.40888  ? 602 A1ACP A H19    1 
HETATM 2849 H H7     . A1ACP C 3 .   ? -2.89236  5.14738   -26.86508 1.000 48.02361  ? 602 A1ACP A H7     1 
HETATM 2850 C C1     . BOG   D 2 .   ? 4.66450   -9.32742  -12.51383 1.000 62.58137  ? 603 BOG   A C1     1 
HETATM 2851 O O1     . BOG   D 2 .   ? 5.43403   -8.17566  -12.74095 1.000 62.50680  ? 603 BOG   A O1     1 
HETATM 2852 C C2     . BOG   D 2 .   ? 5.23018   -10.47869 -13.34293 1.000 65.35548  ? 603 BOG   A C2     1 
HETATM 2853 O O2     . BOG   D 2 .   ? 4.23716   -11.46931 -13.42577 1.000 70.96190  ? 603 BOG   A O2     1 
HETATM 2854 C C3     . BOG   D 2 .   ? 6.49705   -11.08645 -12.76348 1.000 71.95251  ? 603 BOG   A C3     1 
HETATM 2855 O O3     . BOG   D 2 .   ? 7.49913   -11.05478 -13.73973 1.000 68.65434  ? 603 BOG   A O3     1 
HETATM 2856 C C4     . BOG   D 2 .   ? 6.93277   -10.28517 -11.55451 1.000 71.39324  ? 603 BOG   A C4     1 
HETATM 2857 O O4     . BOG   D 2 .   ? 7.98738   -10.95826 -10.92888 1.000 70.41931  ? 603 BOG   A O4     1 
HETATM 2858 C C5     . BOG   D 2 .   ? 5.74935   -10.21175 -10.60219 1.000 80.42459  ? 603 BOG   A C5     1 
HETATM 2859 O O5     . BOG   D 2 .   ? 4.62250   -9.58189  -11.14053 1.000 84.79452  ? 603 BOG   A O5     1 
HETATM 2860 C C6     . BOG   D 2 .   ? 6.18567   -9.42946  -9.35785  1.000 71.24483  ? 603 BOG   A C6     1 
HETATM 2861 O O6     . BOG   D 2 .   ? 7.57978   -9.50980  -9.19768  1.000 69.14000  ? 603 BOG   A O6     1 
HETATM 2862 C "C1'"  . BOG   D 2 .   ? 4.75576   -7.08470  -13.29461 1.000 47.45988  ? 603 BOG   A "C1'"  1 
HETATM 2863 C "C2'"  . BOG   D 2 .   ? 3.79825   -6.48827  -12.26464 1.000 56.43264  ? 603 BOG   A "C2'"  1 
HETATM 2864 C "C3'"  . BOG   D 2 .   ? 4.56185   -6.02514  -11.02541 1.000 45.51231  ? 603 BOG   A "C3'"  1 
HETATM 2865 C "C4'"  . BOG   D 2 .   ? 5.36599   -4.76877  -11.35263 1.000 43.99547  ? 603 BOG   A "C4'"  1 
HETATM 2866 C "C5'"  . BOG   D 2 .   ? 4.75081   -3.55222  -10.66326 1.000 33.07062  ? 603 BOG   A "C5'"  1 
HETATM 2867 C "C6'"  . BOG   D 2 .   ? 4.69394   -2.38930  -11.65323 1.000 31.31955  ? 603 BOG   A "C6'"  1 
HETATM 2868 C "C7'"  . BOG   D 2 .   ? 4.47607   -1.07892  -10.89796 1.000 30.96972  ? 603 BOG   A "C7'"  1 
HETATM 2869 C "C8'"  . BOG   D 2 .   ? 3.68289   -0.10774  -11.77005 1.000 30.30294  ? 603 BOG   A "C8'"  1 
HETATM 2870 H H1     . BOG   D 2 .   ? 3.74583   -9.20815  -12.80145 1.000 75.12877  ? 603 BOG   A H1     1 
HETATM 2871 H H2     . BOG   D 2 .   ? 5.47503   -10.12571 -14.21262 1.000 78.45771  ? 603 BOG   A H2     1 
HETATM 2872 H HO2    . BOG   D 2 .   ? 3.57597   -11.26805 -12.92179 1.000 85.18541  ? 603 BOG   A HO2    1 
HETATM 2873 H H3     . BOG   D 2 .   ? 6.33295   -12.00344 -12.49310 1.000 86.37414  ? 603 BOG   A H3     1 
HETATM 2874 H HO3    . BOG   D 2 .   ? 7.54292   -10.27839 -14.08424 1.000 82.41633  ? 603 BOG   A HO3    1 
HETATM 2875 H H4     . BOG   D 2 .   ? 7.22147   -9.39483  -11.80918 1.000 85.70301  ? 603 BOG   A H4     1 
HETATM 2876 H HO4    . BOG   D 2 .   ? 8.07023   -11.73624 -11.26283 1.000 84.53429  ? 603 BOG   A HO4    1 
HETATM 2877 H H5     . BOG   D 2 .   ? 5.49189   -11.12536 -10.40238 1.000 96.54063  ? 603 BOG   A H5     1 
HETATM 2878 H H61    . BOG   D 2 .   ? 5.75122   -9.80373  -8.57550  1.000 85.52493  ? 603 BOG   A H61    1 
HETATM 2879 H H62    . BOG   D 2 .   ? 5.92767   -8.49969  -9.45719  1.000 85.52493  ? 603 BOG   A H62    1 
HETATM 2880 H HO6    . BOG   D 2 .   ? 7.91491   -8.73055  -9.11951  1.000 82.99912  ? 603 BOG   A HO6    1 
HETATM 2881 H "H1'1" . BOG   D 2 .   ? 4.25168   -7.37921  -14.06925 1.000 56.98298  ? 603 BOG   A "H1'1" 1 
HETATM 2882 H "H1'2" . BOG   D 2 .   ? 5.39839   -6.41007  -13.56442 1.000 56.98298  ? 603 BOG   A "H1'2" 1 
HETATM 2883 H "H2'1" . BOG   D 2 .   ? 3.14889   -7.16086  -12.00606 1.000 67.75029  ? 603 BOG   A "H2'1" 1 
HETATM 2884 H "H2'2" . BOG   D 2 .   ? 3.33899   -5.72983  -12.65802 1.000 67.75029  ? 603 BOG   A "H2'2" 1 
HETATM 2885 H "H3'1" . BOG   D 2 .   ? 3.93234   -5.82837  -10.31414 1.000 54.64590  ? 603 BOG   A "H3'1" 1 
HETATM 2886 H "H3'2" . BOG   D 2 .   ? 5.16538   -6.72791  -10.73775 1.000 54.64590  ? 603 BOG   A "H3'2" 1 
HETATM 2887 H "H4'1" . BOG   D 2 .   ? 5.36368   -4.62810  -12.31238 1.000 52.82570  ? 603 BOG   A "H4'1" 1 
HETATM 2888 H "H4'2" . BOG   D 2 .   ? 6.27869   -4.88364  -11.04490 1.000 52.82570  ? 603 BOG   A "H4'2" 1 
HETATM 2889 H "H5'1" . BOG   D 2 .   ? 5.29471   -3.30226  -9.89997  1.000 39.71588  ? 603 BOG   A "H5'1" 1 
HETATM 2890 H "H5'2" . BOG   D 2 .   ? 3.85364   -3.76792  -10.36419 1.000 39.71588  ? 603 BOG   A "H5'2" 1 
HETATM 2891 H "H6'1" . BOG   D 2 .   ? 5.52907   -2.34312  -12.14450 1.000 37.61458  ? 603 BOG   A "H6'1" 1 
HETATM 2892 H "H6'2" . BOG   D 2 .   ? 3.96137   -2.52950  -12.27337 1.000 37.61458  ? 603 BOG   A "H6'2" 1 
HETATM 2893 H "H7'1" . BOG   D 2 .   ? 5.33558   -0.68669  -10.67820 1.000 37.19479  ? 603 BOG   A "H7'1" 1 
HETATM 2894 H "H7'2" . BOG   D 2 .   ? 3.98302   -1.25551  -10.08149 1.000 37.19479  ? 603 BOG   A "H7'2" 1 
HETATM 2895 H "H8'1" . BOG   D 2 .   ? 2.80914   0.04102   -11.37594 1.000 36.39465  ? 603 BOG   A "H8'1" 1 
HETATM 2896 H "H8'2" . BOG   D 2 .   ? 4.15850   0.73554   -11.82977 1.000 36.39465  ? 603 BOG   A "H8'2" 1 
HETATM 2897 H "H8'3" . BOG   D 2 .   ? 3.57733   -0.48305  -12.65825 1.000 36.39465  ? 603 BOG   A "H8'3" 1 
HETATM 2898 O O      . HOH   E 4 .   ? 0.09614   -5.67568  -4.75081  1.000 34.11106  ? 701 HOH   A O      1 
HETATM 2899 O O      . HOH   E 4 .   ? -11.61125 -6.38773  2.73299   1.000 46.79117  ? 702 HOH   A O      1 
HETATM 2900 O O      . HOH   E 4 .   ? -24.67799 -4.16033  -17.09662 1.000 57.06397  ? 703 HOH   A O      1 
HETATM 2901 O O      . HOH   E 4 .   ? 1.32032   14.14469  -22.19155 1.000 42.12412  ? 704 HOH   A O      1 
HETATM 2902 O O      . HOH   E 4 .   ? 28.47655  -14.25930 -29.82407 1.000 63.76477  ? 705 HOH   A O      1 
HETATM 2903 O O      . HOH   E 4 .   ? 33.62224  -25.44195 -10.80817 1.000 48.08200  ? 706 HOH   A O      1 
HETATM 2904 O O      . HOH   E 4 .   ? 1.59841   -1.43003  -24.11601 1.000 35.72522  ? 707 HOH   A O      1 
HETATM 2905 O O      . HOH   E 4 .   ? -16.55853 -8.66256  0.44039   1.000 36.25739  ? 708 HOH   A O      1 
HETATM 2906 O O      . HOH   E 4 .   ? -7.16878  -3.78549  -31.10604 1.000 51.36865  ? 709 HOH   A O      1 
HETATM 2907 O O      . HOH   E 4 .   ? 30.54984  7.77817   -27.86501 1.000 52.07247  ? 710 HOH   A O      1 
HETATM 2908 O O      . HOH   E 4 .   ? 17.18763  -20.17598 -17.52627 1.000 49.52825  ? 711 HOH   A O      1 
HETATM 2909 O O      . HOH   E 4 .   ? -19.55295 3.12382   -25.52130 1.000 50.67585  ? 712 HOH   A O      1 
HETATM 2910 O O      . HOH   E 4 .   ? 19.34169  -9.50803  -8.05464  1.000 36.85491  ? 713 HOH   A O      1 
HETATM 2911 O O      . HOH   E 4 .   ? -9.01513  4.50875   -3.03725  1.000 40.75559  ? 714 HOH   A O      1 
HETATM 2912 O O      . HOH   E 4 .   ? -22.28219 -1.11553  -9.23203  1.000 44.12184  ? 715 HOH   A O      1 
HETATM 2913 O O      . HOH   E 4 .   ? -9.96737  -1.19882  1.12111   1.000 48.61839  ? 716 HOH   A O      1 
HETATM 2914 O O      . HOH   E 4 .   ? 0.92357   -10.19762 7.96393   1.000 58.31348  ? 717 HOH   A O      1 
HETATM 2915 O O      . HOH   E 4 .   ? 27.69728  11.79415  -13.19423 1.000 41.47179  ? 718 HOH   A O      1 
HETATM 2916 O O      . HOH   E 4 .   ? 17.81245  -3.86486  -26.35769 1.000 31.39711  ? 719 HOH   A O      1 
HETATM 2917 O O      . HOH   E 4 .   ? 28.78785  -8.34953  -3.56109  1.000 50.62687  ? 720 HOH   A O      1 
HETATM 2918 O O      . HOH   E 4 .   ? -13.35789 -8.58264  -15.61324 1.000 27.46358  ? 721 HOH   A O      1 
HETATM 2919 O O      . HOH   E 4 .   ? 35.95015  -3.51856  -26.65996 1.000 52.91107  ? 722 HOH   A O      1 
HETATM 2920 O O      . HOH   E 4 .   ? 28.73291  14.44093  -23.61916 1.000 44.26197  ? 723 HOH   A O      1 
HETATM 2921 O O      . HOH   E 4 .   ? 23.73647  9.82253   -27.27436 1.000 40.72275  ? 724 HOH   A O      1 
HETATM 2922 O O      . HOH   E 4 .   ? 2.23438   -7.94805  -4.72783  1.000 33.17847  ? 725 HOH   A O      1 
HETATM 2923 O O      . HOH   E 4 .   ? 10.968    -16.010   -28.533   1.000 48.46579  ? 726 HOH   A O      1 
HETATM 2924 O O      . HOH   E 4 .   ? -13.40238 -9.45093  2.65318   1.000 45.24323  ? 727 HOH   A O      1 
HETATM 2925 O O      . HOH   E 4 .   ? 13.15568  -5.76772  -15.01994 1.000 22.43181  ? 728 HOH   A O      1 
HETATM 2926 O O      . HOH   E 4 .   ? 22.04221  -1.89860  -28.79137 1.000 32.27555  ? 729 HOH   A O      1 
HETATM 2927 O O      . HOH   E 4 .   ? -18.10155 1.21759   -29.02068 1.000 40.98546  ? 730 HOH   A O      1 
HETATM 2928 O O      . HOH   E 4 .   ? 0.34745   6.42257   -10.48197 1.000 26.34523  ? 731 HOH   A O      1 
HETATM 2929 O O      . HOH   E 4 .   ? 23.93850  -28.42635 -11.17626 1.000 50.89486  ? 732 HOH   A O      1 
HETATM 2930 O O      . HOH   E 4 .   ? -3.25013  4.98433   -8.47650  1.000 25.11142  ? 733 HOH   A O      1 
HETATM 2931 O O      . HOH   E 4 .   ? 24.664    -16.881   -3.621    1.000 41.11746  ? 734 HOH   A O      1 
HETATM 2932 O O      . HOH   E 4 .   ? 20.75428  15.92892  -19.71667 1.000 43.46032  ? 735 HOH   A O      1 
HETATM 2933 O O      . HOH   E 4 .   ? 28.03561  -20.14512 -30.21381 1.000 46.37894  ? 736 HOH   A O      1 
HETATM 2934 O O      . HOH   E 4 .   ? -18.38952 -10.35533 -18.59790 1.000 49.45805  ? 737 HOH   A O      1 
HETATM 2935 O O      . HOH   E 4 .   ? 8.13406   -6.57061  -5.51323  1.000 29.38659  ? 738 HOH   A O      1 
HETATM 2936 O O      . HOH   E 4 .   ? 23.84097  -19.48812 -6.31207  1.000 41.23337  ? 739 HOH   A O      1 
HETATM 2937 O O      . HOH   E 4 .   ? 32.30476  -7.66163  -7.71299  1.000 57.32126  ? 740 HOH   A O      1 
HETATM 2938 O O      . HOH   E 4 .   ? 26.96179  -31.00351 -7.35824  1.000 49.65910  ? 741 HOH   A O      1 
HETATM 2939 O O      . HOH   E 4 .   ? 16.89787  1.22267   -7.29404  1.000 19.94770  ? 742 HOH   A O      1 
HETATM 2940 O O      . HOH   E 4 .   ? -2.37431  -4.66164  -19.66636 1.000 54.33173  ? 743 HOH   A O      1 
HETATM 2941 O O      . HOH   E 4 .   ? 27.80239  0.79225   -10.99126 1.000 48.30526  ? 744 HOH   A O      1 
HETATM 2942 O O      . HOH   E 4 .   ? -5.45202  10.48960  -20.59818 1.000 42.61320  ? 745 HOH   A O      1 
HETATM 2943 O O      . HOH   E 4 .   ? -5.11024  6.25505   -7.84693  1.000 41.05112  ? 746 HOH   A O      1 
HETATM 2944 O O      . HOH   E 4 .   ? 12.07728  14.52360  -3.90789  1.000 46.77244  ? 747 HOH   A O      1 
HETATM 2945 O O      . HOH   E 4 .   ? -2.23505  -8.64879  -19.64352 1.000 44.25032  ? 748 HOH   A O      1 
HETATM 2946 O O      . HOH   E 4 .   ? 18.62545  -6.51015  -25.28440 1.000 31.02814  ? 749 HOH   A O      1 
HETATM 2947 O O      . HOH   E 4 .   ? 0.26716   11.52014  -27.43514 1.000 40.47242  ? 750 HOH   A O      1 
HETATM 2948 O O      . HOH   E 4 .   ? 10.71921  9.83639   -8.05531  1.000 31.85996  ? 751 HOH   A O      1 
HETATM 2949 O O      . HOH   E 4 .   ? 24.44796  -9.41058  -28.44316 1.000 42.72834  ? 752 HOH   A O      1 
HETATM 2950 O O      . HOH   E 4 .   ? 12.53244  -8.23372  -19.08692 1.000 43.48823  ? 753 HOH   A O      1 
HETATM 2951 O O      . HOH   E 4 .   ? -4.01497  -8.47004  -13.90931 1.000 45.96310  ? 754 HOH   A O      1 
HETATM 2952 O O      . HOH   E 4 .   ? -8.25323  -6.00675  1.38408   1.000 44.07211  ? 755 HOH   A O      1 
HETATM 2953 O O      . HOH   E 4 .   ? -2.80092  -0.70502  -1.65412  1.000 36.46471  ? 756 HOH   A O      1 
HETATM 2954 O O      . HOH   E 4 .   ? 5.81828   -5.00624  -28.56794 1.000 48.25350  ? 757 HOH   A O      1 
HETATM 2955 O O      . HOH   E 4 .   ? 15.71131  -8.30483  -15.07578 1.000 33.93828  ? 758 HOH   A O      1 
HETATM 2956 O O      . HOH   E 4 .   ? 19.42027  -9.04089  -20.99648 1.000 25.04806  ? 759 HOH   A O      1 
HETATM 2957 O O      . HOH   E 4 .   ? -22.66275 -8.12864  -1.09647  1.000 56.42814  ? 760 HOH   A O      1 
HETATM 2958 O O      . HOH   E 4 .   ? 8.25613   13.58870  -30.67061 1.000 54.22464  ? 761 HOH   A O      1 
HETATM 2959 O O      . HOH   E 4 .   ? 0.34905   8.87896   -13.68317 1.000 37.16209  ? 762 HOH   A O      1 
HETATM 2960 O O      . HOH   E 4 .   ? 5.04625   -6.97062  -17.48927 1.000 35.71320  ? 763 HOH   A O      1 
HETATM 2961 O O      . HOH   E 4 .   ? -3.98145  -18.69379 -2.76255  1.000 36.37962  ? 764 HOH   A O      1 
HETATM 2962 O O      . HOH   E 4 .   ? 20.78226  4.72130   -3.69247  1.000 44.11058  ? 765 HOH   A O      1 
HETATM 2963 O O      . HOH   E 4 .   ? 11.23199  16.32576  -12.35108 1.000 44.42273  ? 766 HOH   A O      1 
HETATM 2964 O O      . HOH   E 4 .   ? 14.36928  3.90128   -4.22406  1.000 33.09246  ? 767 HOH   A O      1 
HETATM 2965 O O      . HOH   E 4 .   ? 0.42369   5.71937   -2.03047  1.000 38.92614  ? 768 HOH   A O      1 
HETATM 2966 O O      . HOH   E 4 .   ? -22.17250 7.22544   -15.53598 1.000 39.63025  ? 769 HOH   A O      1 
HETATM 2967 O O      . HOH   E 4 .   ? -2.10356  11.02685  -21.30613 1.000 36.85236  ? 770 HOH   A O      1 
HETATM 2968 O O      . HOH   E 4 .   ? 15.32479  -1.90193  -32.54216 1.000 46.36161  ? 771 HOH   A O      1 
HETATM 2969 O O      . HOH   E 4 .   ? 14.55183  16.73766  -28.57252 1.000 55.00038  ? 772 HOH   A O      1 
HETATM 2970 O O      . HOH   E 4 .   ? 4.99434   10.63680  -5.88642  1.000 37.86959  ? 773 HOH   A O      1 
HETATM 2971 O O      . HOH   E 4 .   ? 30.09602  -3.61027  -17.65540 1.000 42.49287  ? 774 HOH   A O      1 
HETATM 2972 O O      . HOH   E 4 .   ? -9.86130  -4.44564  -26.50042 1.000 44.94822  ? 775 HOH   A O      1 
HETATM 2973 O O      . HOH   E 4 .   ? 21.63799  -24.83210 -4.00281  1.000 51.65347  ? 776 HOH   A O      1 
HETATM 2974 O O      . HOH   E 4 .   ? -1.42410  -15.25980 -8.94084  1.000 31.79935  ? 777 HOH   A O      1 
HETATM 2975 O O      . HOH   E 4 .   ? -1.32488  -8.88018  -11.18627 1.000 40.50105  ? 778 HOH   A O      1 
HETATM 2976 O O      . HOH   E 4 .   ? 17.11117  -5.04828  -3.32987  1.000 42.03705  ? 779 HOH   A O      1 
HETATM 2977 O O      . HOH   E 4 .   ? 16.89230  3.38955   -5.94204  1.000 28.10539  ? 780 HOH   A O      1 
HETATM 2978 O O      . HOH   E 4 .   ? -6.30380  -11.36530 -13.53267 1.000 50.60994  ? 781 HOH   A O      1 
HETATM 2979 O O      . HOH   E 4 .   ? 13.12148  -8.61905  -17.25716 1.000 43.69773  ? 782 HOH   A O      1 
HETATM 2980 O O      . HOH   E 4 .   ? -1.53279  8.22631   -13.80622 1.000 49.74780  ? 783 HOH   A O      1 
HETATM 2981 O O      . HOH   E 4 .   ? -6.53144  4.48888   -4.64438  1.000 28.89244  ? 784 HOH   A O      1 
HETATM 2982 O O      . HOH   E 4 .   ? 16.86906  9.78811   -2.19119  1.000 48.30324  ? 785 HOH   A O      1 
HETATM 2983 O O      . HOH   E 4 .   ? 24.87127  -6.06012  -30.01235 1.000 42.83186  ? 786 HOH   A O      1 
HETATM 2984 O O      . HOH   E 4 .   ? -14.09693 -12.00176 -18.51476 1.000 47.22015  ? 787 HOH   A O      1 
HETATM 2985 O O      . HOH   E 4 .   ? 5.77217   -7.01741  2.36593   1.000 47.50966  ? 788 HOH   A O      1 
HETATM 2986 O O      . HOH   E 4 .   ? -11.39983 -5.38884  -27.12324 1.000 62.01316  ? 789 HOH   A O      1 
HETATM 2987 O O      . HOH   E 4 .   ? -3.35221  -6.40243  -20.08841 1.000 50.13076  ? 790 HOH   A O      1 
HETATM 2988 O O      . HOH   E 4 .   ? 22.82262  -4.43039  -2.41724  1.000 51.99307  ? 791 HOH   A O      1 
HETATM 2989 O O      . HOH   E 4 .   ? 24.33273  -10.23143 -30.96691 1.000 46.27956  ? 792 HOH   A O      1 
HETATM 2990 O O      . HOH   E 4 .   ? 14.93320  2.30504   -3.27179  1.000 43.37968  ? 793 HOH   A O      1 
HETATM 2991 O O      . HOH   E 4 .   ? 18.53796  0.87547   -2.91640  1.000 40.43107  ? 794 HOH   A O      1 
HETATM 2992 O O      . HOH   E 4 .   ? 0.09594   -6.83636  -10.84411 1.000 39.47782  ? 795 HOH   A O      1 
HETATM 2993 O O      . HOH   E 4 .   ? 22.07433  -1.89730  -4.04674  1.000 49.96859  ? 796 HOH   A O      1 
HETATM 2994 O O      . HOH   E 4 .   ? 18.25953  3.51306   -3.59005  1.000 42.82204  ? 797 HOH   A O      1 
HETATM 2995 O O      . HOH   E 4 .   ? -1.30398  9.02155   -10.72327 1.000 38.36246  ? 798 HOH   A O      1 
HETATM 2996 O O      . HOH   E 4 .   ? 24.09952  -3.11032  -30.18684 1.000 31.09805  ? 799 HOH   A O      1 
HETATM 2997 O O      . HOH   E 4 .   ? 8.99481   8.34165   -33.19882 1.000 47.97844  ? 800 HOH   A O      1 
HETATM 2998 O O      . HOH   E 4 .   ? -3.05177  9.00222   -9.94472  1.000 39.38301  ? 801 HOH   A O      1 
HETATM 2999 O O      . HOH   E 4 .   ? -20.42885 8.40288   -13.25348 1.000 45.23004  ? 802 HOH   A O      1 
HETATM 3000 O O      . HOH   E 4 .   ? 27.83978  3.36197   -9.75565  1.000 45.33007  ? 803 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   . ARG A 12  ? 0.73750 0.89192 1.20717 0.10578  0.24442  0.17770  5   ARG A N   
2    C CA  . ARG A 12  ? 0.65580 0.79961 1.11649 0.08730  0.21491  0.16681  5   ARG A CA  
3    C C   . ARG A 12  ? 0.55564 0.70794 1.04855 0.08523  0.18854  0.17229  5   ARG A C   
4    O O   . ARG A 12  ? 0.73544 0.91970 1.28425 0.09259  0.19033  0.19377  5   ARG A O   
5    C CB  . ARG A 12  ? 0.71492 0.87165 1.18573 0.06341  0.19709  0.17584  5   ARG A CB  
6    C CG  . ARG A 12  ? 0.69198 0.88208 1.22512 0.04787  0.16867  0.19846  5   ARG A CG  
7    C CD  . ARG A 12  ? 0.64191 0.84201 1.18651 0.02539  0.15466  0.20985  5   ARG A CD  
8    N NE  . ARG A 12  ? 0.59007 0.80230 1.17118 0.00520  0.11541  0.22210  5   ARG A NE  
9    C CZ  . ARG A 12  ? 0.53517 0.71705 1.08106 -0.01037 0.08209  0.20603  5   ARG A CZ  
10   N NH1 . ARG A 12  ? 0.60832 0.75181 1.08874 -0.00842 0.08330  0.17906  5   ARG A NH1 
11   N NH2 . ARG A 12  ? 0.47833 0.66829 1.05494 -0.02778 0.04641  0.21787  5   ARG A NH2 
12   N N   . PRO A 13  ? 0.51089 0.63327 0.96446 0.07472  0.16278  0.15362  6   PRO A N   
13   C CA  . PRO A 13  ? 0.54390 0.66902 1.01775 0.07271  0.13746  0.15774  6   PRO A CA  
14   C C   . PRO A 13  ? 0.53885 0.69362 1.06115 0.05468  0.10801  0.17782  6   PRO A C   
15   O O   . PRO A 13  ? 0.47517 0.64309 1.01022 0.04044  0.10279  0.18601  6   PRO A O   
16   C CB  . PRO A 13  ? 0.57737 0.66247 0.98900 0.06515  0.12173  0.13247  6   PRO A CB  
17   C CG  . PRO A 13  ? 0.46194 0.53371 0.83639 0.05457  0.12511  0.12039  6   PRO A CG  
18   C CD  . PRO A 13  ? 0.53025 0.61636 0.91892 0.06525  0.15685  0.12931  6   PRO A CD  
19   N N   . THR A 14  ? 0.48612 0.64832 1.03378 0.05446  0.08631  0.18645  7   THR A N   
20   C CA  . THR A 14  ? 0.37129 0.55495 0.95886 0.03605  0.05172  0.20426  7   THR A CA  
21   C C   . THR A 14  ? 0.43280 0.58337 0.96925 0.01843  0.01942  0.18611  7   THR A C   
22   O O   . THR A 14  ? 0.54278 0.66440 1.03305 0.02355  0.01760  0.16776  7   THR A O   
23   C CB  . THR A 14  ? 0.44159 0.65077 1.08304 0.04512  0.04265  0.22505  7   THR A CB  
24   O OG1 . THR A 14  ? 0.37041 0.60651 1.05233 0.06549  0.07667  0.23998  7   THR A OG1 
25   C CG2 . THR A 14  ? 0.36089 0.59327 1.04625 0.02390  0.00405  0.24595  7   THR A CG2 
26   N N   . PHE A 15  ? 0.38318 0.53722 0.92771 -0.00193 -0.00550 0.19215  8   PHE A N   
27   C CA  . PHE A 15  ? 0.40508 0.52588 0.89937 -0.01694 -0.03479 0.17495  8   PHE A CA  
28   C C   . PHE A 15  ? 0.44628 0.57041 0.96054 -0.02987 -0.07422 0.18733  8   PHE A C   
29   O O   . PHE A 15  ? 0.31734 0.47447 0.89340 -0.03302 -0.08334 0.21278  8   PHE A O   
30   C CB  . PHE A 15  ? 0.34344 0.45410 0.82072 -0.03014 -0.03710 0.16950  8   PHE A CB  
31   C CG  . PHE A 15  ? 0.44269 0.53477 0.87499 -0.02083 -0.00885 0.14974  8   PHE A CG  
32   C CD1 . PHE A 15  ? 0.42763 0.53624 0.87589 -0.00797 0.02630  0.15501  8   PHE A CD1 
33   C CD2 . PHE A 15  ? 0.49830 0.55630 0.87156 -0.02430 -0.01778 0.12667  8   PHE A CD2 
34   C CE1 . PHE A 15  ? 0.41950 0.50805 0.82283 -0.00107 0.04855  0.13720  8   PHE A CE1 
35   C CE2 . PHE A 15  ? 0.40552 0.44888 0.74135 -0.01704 0.00499  0.11070  8   PHE A CE2 
36   C CZ  . PHE A 15  ? 0.31976 0.37699 0.66930 -0.00662 0.03643  0.11580  8   PHE A CZ  
37   N N   . TYR A 16  ? 0.51954 0.60933 0.97986 -0.03698 -0.09781 0.16985  9   TYR A N   
38   C CA  . TYR A 16  ? 0.55584 0.63784 1.01794 -0.05138 -0.13908 0.17751  9   TYR A CA  
39   C C   . TYR A 16  ? 0.51420 0.55573 0.91478 -0.06275 -0.15991 0.15699  9   TYR A C   
40   O O   . TYR A 16  ? 0.50392 0.52287 0.85403 -0.05499 -0.14276 0.13492  9   TYR A O   
41   C CB  . TYR A 16  ? 0.42304 0.50353 0.88067 -0.04272 -0.14738 0.18034  9   TYR A CB  
42   C CG  . TYR A 16  ? 0.46066 0.50928 0.85169 -0.03327 -0.13761 0.15647  9   TYR A CG  
43   C CD1 . TYR A 16  ? 0.45955 0.50896 0.84064 -0.01700 -0.10261 0.14726  9   TYR A CD1 
44   C CD2 . TYR A 16  ? 0.50286 0.52018 0.84048 -0.04083 -0.16372 0.14441  9   TYR A CD2 
45   C CE1 . TYR A 16  ? 0.41351 0.43722 0.73960 -0.01100 -0.09526 0.12881  9   TYR A CE1 
46   C CE2 . TYR A 16  ? 0.52360 0.51755 0.80525 -0.03233 -0.15274 0.12606  9   TYR A CE2 
47   C CZ  . TYR A 16  ? 0.44029 0.43957 0.71974 -0.01862 -0.11921 0.11948  9   TYR A CZ  
48   O OH  . TYR A 16  ? 0.53053 0.50966 0.75964 -0.01274 -0.10978 0.10429  9   TYR A OH  
49   N N   . ARG A 17  ? 0.50958 0.54122 0.91529 -0.08078 -0.19790 0.16505  10  ARG A N   
50   C CA  . ARG A 17  ? 0.61113 0.60119 0.96228 -0.09153 -0.21993 0.14738  10  ARG A CA  
51   C C   . ARG A 17  ? 0.57904 0.53631 0.88019 -0.09437 -0.25072 0.13758  10  ARG A C   
52   O O   . ARG A 17  ? 0.61543 0.58442 0.93869 -0.09749 -0.26966 0.15237  10  ARG A O   
53   C CB  . ARG A 17  ? 0.48812 0.48142 0.87396 -0.11189 -0.24237 0.16231  10  ARG A CB  
54   C CG  . ARG A 17  ? 0.59177 0.61952 1.02833 -0.11067 -0.21256 0.17601  10  ARG A CG  
55   C CD  . ARG A 17  ? 0.74880 0.78858 1.23393 -0.13363 -0.23757 0.19907  10  ARG A CD  
56   N NE  . ARG A 17  ? 0.87930 0.88916 1.33374 -0.14257 -0.24066 0.18800  10  ARG A NE  
57   C CZ  . ARG A 17  ? 0.83559 0.79565 1.23782 -0.15317 -0.27283 0.17211  10  ARG A CZ  
58   N NH1 . ARG A 17  ? 0.59874 0.53167 0.96802 -0.15680 -0.30467 0.16429  10  ARG A NH1 
59   N NH2 . ARG A 17  ? 0.81449 0.74851 1.19387 -0.15923 -0.27310 0.16391  10  ARG A NH2 
60   N N   . GLN A 18  ? 0.63896 0.55482 0.87128 -0.09208 -0.25504 0.11323  11  GLN A N   
61   C CA  . GLN A 18  ? 0.78169 0.66025 0.95421 -0.09314 -0.28181 0.10123  11  GLN A CA  
62   C C   . GLN A 18  ? 0.74431 0.57841 0.85269 -0.09172 -0.28639 0.07705  11  GLN A C   
63   O O   . GLN A 18  ? 0.73335 0.56867 0.84285 -0.08725 -0.26486 0.06896  11  GLN A O   
64   C CB  . GLN A 18  ? 0.62997 0.51460 0.77974 -0.07776 -0.26417 0.09655  11  GLN A CB  
65   C CG  . GLN A 18  ? 0.64828 0.54030 0.78172 -0.06125 -0.22265 0.08210  11  GLN A CG  
66   C CD  . GLN A 18  ? 0.72108 0.61839 0.83596 -0.04924 -0.20788 0.08053  11  GLN A CD  
67   O OE1 . GLN A 18  ? 0.82579 0.74191 0.95558 -0.03891 -0.17692 0.07972  11  GLN A OE1 
68   N NE2 . GLN A 18  ? 0.63022 0.50778 0.70931 -0.05144 -0.23134 0.08061  11  GLN A NE2 
69   N N   . GLU A 19  ? 0.76724 0.56001 0.81717 -0.09428 -0.31490 0.06579  12  GLU A N   
70   C CA  . GLU A 19  ? 0.82786 0.57249 0.80968 -0.08932 -0.32069 0.04165  12  GLU A CA  
71   C C   . GLU A 19  ? 0.84775 0.57530 0.76451 -0.07088 -0.30571 0.02380  12  GLU A C   
72   O O   . GLU A 19  ? 0.95133 0.67519 0.84906 -0.07095 -0.31873 0.02832  12  GLU A O   
73   C CB  . GLU A 19  ? 1.00960 0.71089 0.96821 -0.10707 -0.36779 0.04152  12  GLU A CB  
74   C CG  . GLU A 19  ? 0.99555 0.64291 0.88903 -0.10124 -0.37385 0.01701  12  GLU A CG  
75   C CD  . GLU A 19  ? 1.02651 0.63435 0.90854 -0.11696 -0.41051 0.02146  12  GLU A CD  
76   O OE1 . GLU A 19  ? 1.02153 0.63636 0.92881 -0.13071 -0.43362 0.04061  12  GLU A OE1 
77   O OE2 . GLU A 19  ? 1.15783 0.73037 1.00744 -0.11195 -0.40983 0.00859  12  GLU A OE2 
78   N N   . LEU A 20  ? 0.93054 0.64977 0.81538 -0.05539 -0.27853 0.00572  13  LEU A N   
79   C CA  . LEU A 20  ? 1.03547 0.74235 0.86143 -0.03715 -0.26084 -0.00991 13  LEU A CA  
80   C C   . LEU A 20  ? 1.08041 0.75043 0.85398 -0.02550 -0.25684 -0.03190 13  LEU A C   
81   O O   . LEU A 20  ? 1.03507 0.71340 0.83061 -0.02303 -0.24143 -0.03519 13  LEU A O   
82   C CB  . LEU A 20  ? 0.91993 0.66996 0.77431 -0.02682 -0.22281 -0.00484 13  LEU A CB  
83   C CG  . LEU A 20  ? 0.92195 0.70631 0.82528 -0.03347 -0.22182 0.01564  13  LEU A CG  
84   C CD1 . LEU A 20  ? 0.92624 0.73983 0.90072 -0.04351 -0.21911 0.03078  13  LEU A CD1 
85   C CD2 . LEU A 20  ? 0.78265 0.58902 0.68073 -0.02118 -0.19113 0.01531  13  LEU A CD2 
86   N N   . ASN A 21  ? 1.22364 0.85149 0.92597 -0.01696 -0.27032 -0.04657 14  ASN A N   
87   C CA  . ASN A 21  ? 1.24411 0.83186 0.88990 -0.00151 -0.26628 -0.06866 14  ASN A CA  
88   C C   . ASN A 21  ? 1.18101 0.74041 0.84014 -0.01325 -0.28911 -0.07105 14  ASN A C   
89   O O   . ASN A 21  ? 1.21645 0.76888 0.87364 -0.00367 -0.27462 -0.08073 14  ASN A O   
90   C CB  . ASN A 21  ? 1.20513 0.82183 0.85314 0.01845  -0.22381 -0.07546 14  ASN A CB  
91   C CG  . ASN A 21  ? 1.28952 0.92451 0.91090 0.03104  -0.20299 -0.07489 14  ASN A CG  
92   O OD1 . ASN A 21  ? 1.18887 0.82408 0.80227 0.02344  -0.21681 -0.06591 14  ASN A OD1 
93   N ND2 . ASN A 21  ? 1.34470 0.99649 0.95440 0.04959  -0.17049 -0.08238 14  ASN A ND2 
94   N N   . LYS A 22  ? 1.09160 0.63509 0.76659 -0.03531 -0.32681 -0.06006 15  LYS A N   
95   C CA  . LYS A 22  ? 1.12017 0.64264 0.81800 -0.05041 -0.34910 -0.05511 15  LYS A CA  
96   C C   . LYS A 22  ? 1.08359 0.64453 0.84755 -0.05674 -0.33034 -0.04491 15  LYS A C   
97   O O   . LYS A 22  ? 1.12029 0.66202 0.89404 -0.06367 -0.33975 -0.04496 15  LYS A O   
98   C CB  . LYS A 22  ? 1.09359 0.56486 0.73112 -0.03495 -0.35038 -0.07181 15  LYS A CB  
99   C CG  . LYS A 22  ? 1.15540 0.59757 0.72070 -0.01611 -0.34601 -0.08616 15  LYS A CG  
100  C CD  . LYS A 22  ? 1.27190 0.67932 0.78529 0.00792  -0.33088 -0.10512 15  LYS A CD  
101  C CE  . LYS A 22  ? 1.14611 0.51059 0.65122 -0.00047 -0.35756 -0.10370 15  LYS A CE  
102  N NZ  . LYS A 22  ? 1.20442 0.52506 0.66191 -0.00368 -0.38385 -0.10480 15  LYS A NZ  
103  N N   . THR A 23  ? 0.92082 0.53826 0.73079 -0.05245 -0.29922 -0.03331 16  THR A N   
104  C CA  . THR A 23  ? 0.89317 0.55203 0.76390 -0.05542 -0.27469 -0.02160 16  THR A CA  
105  C C   . THR A 23  ? 0.92687 0.63233 0.86519 -0.06954 -0.27446 0.00304  16  THR A C   
106  O O   . THR A 23  ? 0.95566 0.67027 0.89422 -0.07143 -0.28346 0.00965  16  THR A O   
107  C CB  . THR A 23  ? 0.93821 0.61893 0.79823 -0.03425 -0.23423 -0.03217 16  THR A CB  
108  O OG1 . THR A 23  ? 1.05484 0.69590 0.85394 -0.01783 -0.23307 -0.05376 16  THR A OG1 
109  C CG2 . THR A 23  ? 0.77081 0.48519 0.68291 -0.03748 -0.21196 -0.02212 16  THR A CG2 
110  N N   . ILE A 24  ? 0.77199 0.50678 0.76709 -0.07806 -0.26314 0.01753  17  ILE A N   
111  C CA  . ILE A 24  ? 0.84932 0.63054 0.91339 -0.08860 -0.25870 0.04210  17  ILE A CA  
112  C C   . ILE A 24  ? 0.76073 0.58085 0.84773 -0.07464 -0.21646 0.04309  17  ILE A C   
113  O O   . ILE A 24  ? 0.72419 0.54648 0.81012 -0.06911 -0.19588 0.03725  17  ILE A O   
114  C CB  . ILE A 24  ? 0.71468 0.50205 0.82813 -0.10931 -0.27693 0.06118  17  ILE A CB  
115  C CG1 . ILE A 24  ? 0.74610 0.59018 0.93497 -0.11368 -0.25872 0.08655  17  ILE A CG1 
116  C CG2 . ILE A 24  ? 0.68514 0.45175 0.78345 -0.10830 -0.26903 0.05221  17  ILE A CG2 
117  C CD1 . ILE A 24  ? 0.80036 0.66602 1.01258 -0.11506 -0.26941 0.09915  17  ILE A CD1 
118  N N   . TRP A 25  ? 0.67733 0.52476 0.78314 -0.06945 -0.20565 0.05085  18  TRP A N   
119  C CA  . TRP A 25  ? 0.63841 0.51710 0.76283 -0.05704 -0.16898 0.05178  18  TRP A CA  
120  C C   . TRP A 25  ? 0.63612 0.55375 0.82715 -0.06213 -0.16138 0.07493  18  TRP A C   
121  O O   . TRP A 25  ? 0.61699 0.54510 0.83338 -0.06829 -0.17970 0.08908  18  TRP A O   
122  C CB  . TRP A 25  ? 0.59944 0.47475 0.68803 -0.04443 -0.15938 0.04148  18  TRP A CB  
123  C CG  . TRP A 25  ? 0.68822 0.53582 0.71681 -0.03435 -0.15488 0.02002  18  TRP A CG  
124  C CD1 . TRP A 25  ? 0.74045 0.55089 0.72297 -0.03497 -0.17713 0.00797  18  TRP A CD1 
125  C CD2 . TRP A 25  ? 0.64781 0.50295 0.65693 -0.02113 -0.12627 0.00897  18  TRP A CD2 
126  N NE1 . TRP A 25  ? 0.76919 0.56671 0.70695 -0.02037 -0.16105 -0.00945 18  TRP A NE1 
127  C CE2 . TRP A 25  ? 0.69663 0.52382 0.65300 -0.01301 -0.13077 -0.00789 18  TRP A CE2 
128  C CE3 . TRP A 25  ? 0.44857 0.32968 0.47896 -0.01544 -0.09845 0.01203  18  TRP A CE3 
129  C CZ2 . TRP A 25  ? 0.60773 0.43937 0.53985 0.00007  -0.10787 -0.01899 18  TRP A CZ2 
130  C CZ3 . TRP A 25  ? 0.55704 0.43812 0.55992 -0.00524 -0.07922 0.00015  18  TRP A CZ3 
131  C CH2 . TRP A 25  ? 0.57606 0.43612 0.53405 0.00217  -0.08373 -0.01387 18  TRP A CH2 
132  N N   . GLU A 26  ? 0.54246 0.48123 0.76049 -0.05834 -0.13414 0.07936  19  GLU A N   
133  C CA  . GLU A 26  ? 0.53564 0.51234 0.81348 -0.05792 -0.11834 0.10000  19  GLU A CA  
134  C C   . GLU A 26  ? 0.46252 0.44999 0.73253 -0.04167 -0.08257 0.09228  19  GLU A C   
135  O O   . GLU A 26  ? 0.47284 0.45519 0.72556 -0.03759 -0.06343 0.08293  19  GLU A O   
136  C CB  . GLU A 26  ? 0.62936 0.61927 0.94567 -0.06952 -0.11901 0.11507  19  GLU A CB  
137  C CG  . GLU A 26  ? 0.74870 0.72951 1.08225 -0.08916 -0.15746 0.12718  19  GLU A CG  
138  C CD  . GLU A 26  ? 0.82976 0.82002 1.19692 -0.10261 -0.15813 0.14218  19  GLU A CD  
139  O OE1 . GLU A 26  ? 0.81994 0.85011 1.24746 -0.10539 -0.14546 0.16604  19  GLU A OE1 
140  O OE2 . GLU A 26  ? 0.70100 0.65881 1.03462 -0.10958 -0.17048 0.13127  19  GLU A OE2 
141  N N   . VAL A 27  ? 0.52138 0.52062 0.80242 -0.03311 -0.07574 0.09664  20  VAL A N   
142  C CA  . VAL A 27  ? 0.41163 0.41202 0.67714 -0.01891 -0.04685 0.08746  20  VAL A CA  
143  C C   . VAL A 27  ? 0.41801 0.44299 0.72827 -0.01016 -0.03253 0.10336  20  VAL A C   
144  O O   . VAL A 27  ? 0.48388 0.52534 0.83283 -0.01378 -0.04847 0.12065  20  VAL A O   
145  C CB  . VAL A 27  ? 0.38302 0.36208 0.60008 -0.01471 -0.05196 0.07191  20  VAL A CB  
146  C CG1 . VAL A 27  ? 0.37911 0.33461 0.55327 -0.02005 -0.06606 0.05717  20  VAL A CG1 
147  C CG2 . VAL A 27  ? 0.44358 0.42521 0.67034 -0.01521 -0.06983 0.08165  20  VAL A CG2 
148  N N   . PRO A 28  ? 0.43576 0.46194 0.74092 0.00222  -0.00317 0.09805  21  PRO A N   
149  C CA  . PRO A 28  ? 0.39988 0.44333 0.74136 0.01489  0.01333  0.11071  21  PRO A CA  
150  C C   . PRO A 28  ? 0.43033 0.47084 0.77500 0.01776  -0.00216 0.11552  21  PRO A C   
151  O O   . PRO A 28  ? 0.38568 0.40657 0.69207 0.01275  -0.01761 0.10496  21  PRO A O   
152  C CB  . PRO A 28  ? 0.31837 0.34810 0.63155 0.02649  0.04327  0.09711  21  PRO A CB  
153  C CG  . PRO A 28  ? 0.31098 0.33054 0.59480 0.01821  0.04495  0.08551  21  PRO A CG  
154  C CD  . PRO A 28  ? 0.36986 0.38075 0.63747 0.00522  0.01559  0.08143  21  PRO A CD  
155  N N   . GLU A 29  ? 0.45695 0.51843 0.84877 0.02727  0.00347  0.13324  22  GLU A N   
156  C CA  . GLU A 29  ? 0.40556 0.46653 0.80745 0.03033  -0.01313 0.14208  22  GLU A CA  
157  C C   . GLU A 29  ? 0.36032 0.39308 0.71649 0.03705  -0.00566 0.12724  22  GLU A C   
158  O O   . GLU A 29  ? 0.31641 0.34004 0.66060 0.03452  -0.02431 0.13017  22  GLU A O   
159  C CB  . GLU A 29  ? 0.36907 0.45907 0.83356 0.04319  -0.00396 0.16444  22  GLU A CB  
160  C CG  . GLU A 29  ? 0.43301 0.55801 0.95475 0.03427  -0.01698 0.18623  22  GLU A CG  
161  C CD  . GLU A 29  ? 0.50350 0.66252 1.09211 0.04998  -0.00467 0.21036  22  GLU A CD  
162  O OE1 . GLU A 29  ? 0.43100 0.58232 1.01611 0.07072  0.02140  0.20640  22  GLU A OE1 
163  O OE2 . GLU A 29  ? 0.55251 0.74513 1.19777 0.04194  -0.02162 0.23385  22  GLU A OE2 
164  N N   . ARG A 30  ? 0.35355 0.37156 0.68343 0.04443  0.02004  0.11287  23  ARG A N   
165  C CA  . ARG A 30  ? 0.41561 0.40758 0.70858 0.04939  0.02659  0.10190  23  ARG A CA  
166  C C   . ARG A 30  ? 0.40339 0.38070 0.65404 0.03683  0.00743  0.09259  23  ARG A C   
167  O O   . ARG A 30  ? 0.38797 0.35061 0.61887 0.03777  0.00317  0.09212  23  ARG A O   
168  C CB  . ARG A 30  ? 0.44098 0.41725 0.71061 0.05662  0.05372  0.08793  23  ARG A CB  
169  C CG  . ARG A 30  ? 0.44812 0.42450 0.69576 0.04763  0.05788  0.07624  23  ARG A CG  
170  C CD  . ARG A 30  ? 0.55988 0.51738 0.77996 0.05409  0.08152  0.06314  23  ARG A CD  
171  N NE  . ARG A 30  ? 0.47079 0.40267 0.65384 0.05208  0.08003  0.05236  23  ARG A NE  
172  C CZ  . ARG A 30  ? 0.51481 0.42525 0.66483 0.05226  0.09247  0.03931  23  ARG A CZ  
173  N NH1 . ARG A 30  ? 0.60328 0.51201 0.74695 0.05590  0.10845  0.03394  23  ARG A NH1 
174  N NH2 . ARG A 30  ? 0.48610 0.37605 0.60824 0.04744  0.08754  0.03290  23  ARG A NH2 
175  N N   . TYR A 31  ? 0.40228 0.38220 0.63771 0.02602  -0.00329 0.08598  24  TYR A N   
176  C CA  . TYR A 31  ? 0.41072 0.37719 0.60403 0.01735  -0.01854 0.07668  24  TYR A CA  
177  C C   . TYR A 31  ? 0.41368 0.38355 0.61413 0.01128  -0.04653 0.08756  24  TYR A C   
178  O O   . TYR A 31  ? 0.42573 0.40575 0.64825 0.00525  -0.06085 0.09398  24  TYR A O   
179  C CB  . TYR A 31  ? 0.39829 0.36076 0.56720 0.01172  -0.01553 0.06278  24  TYR A CB  
180  C CG  . TYR A 31  ? 0.39322 0.35275 0.55623 0.01633  0.00887  0.05377  24  TYR A CG  
181  C CD1 . TYR A 31  ? 0.42610 0.37291 0.56499 0.01918  0.02091  0.04636  24  TYR A CD1 
182  C CD2 . TYR A 31  ? 0.41175 0.37967 0.59181 0.01647  0.01831  0.05399  24  TYR A CD2 
183  C CE1 . TYR A 31  ? 0.47159 0.41156 0.60078 0.02193  0.03952  0.03790  24  TYR A CE1 
184  C CE2 . TYR A 31  ? 0.40082 0.36287 0.56935 0.02057  0.03924  0.04585  24  TYR A CE2 
185  C CZ  . TYR A 31  ? 0.45613 0.40293 0.59792 0.02326  0.04872  0.03709  24  TYR A CZ  
186  O OH  . TYR A 31  ? 0.51880 0.45577 0.64496 0.02590  0.06597  0.02872  24  TYR A OH  
187  N N   . GLN A 32  ? 0.43900 0.39874 0.61922 0.01151  -0.05587 0.09067  25  GLN A N   
188  C CA  . GLN A 32  ? 0.44730 0.40678 0.62969 0.00645  -0.08353 0.10239  25  GLN A CA  
189  C C   . GLN A 32  ? 0.49904 0.43997 0.62544 0.00100  -0.09544 0.09303  25  GLN A C   
190  O O   . GLN A 32  ? 0.59529 0.52783 0.68837 0.00282  -0.07999 0.08153  25  GLN A O   
191  C CB  . GLN A 32  ? 0.37752 0.34143 0.58749 0.01341  -0.08554 0.11897  25  GLN A CB  
192  C CG  . GLN A 32  ? 0.35700 0.34065 0.62443 0.02278  -0.07271 0.13038  25  GLN A CG  
193  C CD  . GLN A 32  ? 0.35808 0.36367 0.66973 0.01750  -0.09340 0.14620  25  GLN A CD  
194  O OE1 . GLN A 32  ? 0.46523 0.47172 0.78210 0.01205  -0.12063 0.15871  25  GLN A OE1 
195  N NE2 . GLN A 32  ? 0.34147 0.36501 0.68515 0.01777  -0.08188 0.14733  25  GLN A NE2 
196  N N   . ASN A 33  ? 0.45756 0.39243 0.57371 -0.00555 -0.12352 0.09912  26  ASN A N   
197  C CA  . ASN A 33  ? 0.51376 0.42842 0.57237 -0.00852 -0.13602 0.09220  26  ASN A CA  
198  C C   . ASN A 33  ? 0.64364 0.54839 0.66352 -0.00764 -0.12449 0.07245  26  ASN A C   
199  O O   . ASN A 33  ? 0.57876 0.47747 0.56168 -0.00374 -0.11085 0.06474  26  ASN A O   
200  C CB  . ASN A 33  ? 0.49294 0.40319 0.53370 -0.00466 -0.12898 0.09912  26  ASN A CB  
201  C CG  . ASN A 33  ? 0.73671 0.65407 0.81482 -0.00358 -0.14168 0.11948  26  ASN A CG  
202  O OD1 . ASN A 33  ? 0.68776 0.61892 0.81268 0.00224  -0.12914 0.12653  26  ASN A OD1 
203  N ND2 . ASN A 33  ? 0.88042 0.78705 0.93609 -0.00780 -0.16661 0.12934  26  ASN A ND2 
204  N N   . LEU A 34  ? 0.58585 0.49025 0.61719 -0.01127 -0.13037 0.06616  27  LEU A N   
205  C CA  . LEU A 34  ? 0.55301 0.44614 0.55027 -0.00906 -0.12181 0.04828  27  LEU A CA  
206  C C   . LEU A 34  ? 0.61824 0.48742 0.55533 -0.00739 -0.13490 0.03972  27  LEU A C   
207  O O   . LEU A 34  ? 0.59311 0.44690 0.51500 -0.01270 -0.16183 0.04457  27  LEU A O   
208  C CB  . LEU A 34  ? 0.55555 0.44890 0.57673 -0.01459 -0.12969 0.04587  27  LEU A CB  
209  C CG  . LEU A 34  ? 0.63883 0.54908 0.69089 -0.01167 -0.10455 0.04342  27  LEU A CG  
210  C CD1 . LEU A 34  ? 0.48368 0.41520 0.58063 -0.00911 -0.09138 0.05707  27  LEU A CD1 
211  C CD2 . LEU A 34  ? 0.53573 0.44328 0.60403 -0.01809 -0.11323 0.04189  27  LEU A CD2 
212  N N   . SER A 35  ? 0.54268 0.40890 0.44473 0.00054  -0.11577 0.02775  28  SER A N   
213  C CA  . SER A 35  ? 0.61486 0.46026 0.45645 0.00623  -0.12120 0.01912  28  SER A CA  
214  C C   . SER A 35  ? 0.62967 0.47114 0.44671 0.01554  -0.10456 0.00268  28  SER A C   
215  O O   . SER A 35  ? 0.55348 0.41521 0.38655 0.01935  -0.08033 0.00153  28  SER A O   
216  C CB  . SER A 35  ? 0.63015 0.48204 0.45302 0.00871  -0.11232 0.02846  28  SER A CB  
217  O OG  . SER A 35  ? 0.77591 0.60845 0.53715 0.01545  -0.11558 0.02169  28  SER A OG  
218  N N   . PRO A 36  ? 0.68569 0.49941 0.46343 0.01968  -0.11832 -0.00992 29  PRO A N   
219  C CA  . PRO A 36  ? 0.60493 0.41380 0.36235 0.03102  -0.10305 -0.02503 29  PRO A CA  
220  C C   . PRO A 36  ? 0.58276 0.40641 0.31432 0.04313  -0.07748 -0.02643 29  PRO A C   
221  O O   . PRO A 36  ? 0.62888 0.44794 0.32685 0.04623  -0.07780 -0.02202 29  PRO A O   
222  C CB  . PRO A 36  ? 0.70902 0.47639 0.42136 0.03378  -0.12710 -0.03753 29  PRO A CB  
223  C CG  . PRO A 36  ? 0.78891 0.54473 0.51549 0.01846  -0.15793 -0.02711 29  PRO A CG  
224  C CD  . PRO A 36  ? 0.60628 0.38831 0.35490 0.01435  -0.15052 -0.01093 29  PRO A CD  
225  N N   . VAL A 37  ? 0.60541 0.44873 0.35469 0.04906  -0.05575 -0.03053 30  VAL A N   
226  C CA  . VAL A 37  ? 0.58249 0.44517 0.31505 0.06034  -0.03098 -0.03046 30  VAL A CA  
227  C C   . VAL A 37  ? 0.70901 0.55733 0.40599 0.07790  -0.02471 -0.04559 30  VAL A C   
228  O O   . VAL A 37  ? 0.82459 0.66680 0.47733 0.09159  -0.01612 -0.04896 30  VAL A O   
229  C CB  . VAL A 37  ? 0.54701 0.44393 0.32585 0.05410  -0.01227 -0.02191 30  VAL A CB  
230  C CG1 . VAL A 37  ? 0.56873 0.48981 0.33621 0.06249  0.01066  -0.01762 30  VAL A CG1 
231  C CG2 . VAL A 37  ? 0.48366 0.38752 0.29512 0.03967  -0.01871 -0.00905 30  VAL A CG2 
232  N N   . GLY A 38  ? 0.65449 0.49643 0.36892 0.07918  -0.02775 -0.05411 31  GLY A N   
233  C CA  . GLY A 38  ? 0.78643 0.61153 0.47027 0.09720  -0.02303 -0.06830 31  GLY A CA  
234  C C   . GLY A 38  ? 0.70571 0.51576 0.41129 0.09281  -0.03508 -0.07496 31  GLY A C   
235  O O   . GLY A 38  ? 0.65986 0.46920 0.39790 0.07588  -0.04889 -0.06887 31  GLY A O   
236  N N   . SER A 39  ? 0.70172 0.50086 0.39015 0.10929  -0.02852 -0.08604 32  SER A N   
237  C CA  . SER A 39  ? 0.73143 0.51239 0.43543 0.10638  -0.04020 -0.09185 32  SER A CA  
238  C C   . SER A 39  ? 0.82050 0.61455 0.52848 0.12364  -0.02224 -0.09647 32  SER A C   
239  O O   . SER A 39  ? 0.82834 0.63141 0.51227 0.14313  -0.00518 -0.10001 32  SER A O   
240  C CB  . SER A 39  ? 0.74219 0.46990 0.40777 0.10694  -0.06704 -0.10342 32  SER A CB  
241  O OG  . SER A 39  ? 0.88835 0.60201 0.58049 0.09519  -0.08245 -0.10281 32  SER A OG  
242  N N   . GLY A 40  ? 0.84840 0.64532 0.58835 0.11666  -0.02585 -0.09463 33  GLY A N   
243  C CA  . GLY A 40  ? 0.79693 0.60068 0.54228 0.13186  -0.01480 -0.09834 33  GLY A CA  
244  C C   . GLY A 40  ? 0.83352 0.59483 0.56649 0.13434  -0.03328 -0.10745 33  GLY A C   
245  O O   . GLY A 40  ? 0.83021 0.55308 0.54138 0.12705  -0.05472 -0.11294 33  GLY A O   
246  N N   . ALA A 41  ? 0.94341 0.71001 0.69077 0.14325  -0.02748 -0.10772 34  ALA A N   
247  C CA  . ALA A 41  ? 0.85952 0.58363 0.59557 0.14547  -0.04538 -0.11478 34  ALA A CA  
248  C C   . ALA A 41  ? 0.89861 0.62262 0.66913 0.12005  -0.05863 -0.10455 34  ALA A C   
249  O O   . ALA A 41  ? 1.00370 0.68863 0.76525 0.11335  -0.07926 -0.10739 34  ALA A O   
250  C CB  . ALA A 41  ? 0.87362 0.60059 0.60842 0.16835  -0.03442 -0.11845 34  ALA A CB  
251  N N   . TYR A 42  ? 0.80537 0.57063 0.61365 0.10588  -0.04704 -0.09212 35  TYR A N   
252  C CA  . TYR A 42  ? 0.71072 0.48016 0.55083 0.08469  -0.05407 -0.08141 35  TYR A CA  
253  C C   . TYR A 42  ? 0.73613 0.51916 0.59390 0.06656  -0.05643 -0.07341 35  TYR A C   
254  O O   . TYR A 42  ? 0.68950 0.48348 0.57684 0.05076  -0.05689 -0.06287 35  TYR A O   
255  C CB  . TYR A 42  ? 0.75492 0.55464 0.62102 0.08393  -0.03970 -0.07369 35  TYR A CB  
256  C CG  . TYR A 42  ? 0.79179 0.58755 0.64692 0.10372  -0.03552 -0.07889 35  TYR A CG  
257  C CD1 . TYR A 42  ? 0.78890 0.54374 0.61963 0.11568  -0.04890 -0.08759 35  TYR A CD1 
258  C CD2 . TYR A 42  ? 0.69616 0.52794 0.56656 0.11050  -0.01973 -0.07419 35  TYR A CD2 
259  C CE1 . TYR A 42  ? 0.87676 0.62772 0.69941 0.13678  -0.04441 -0.09169 35  TYR A CE1 
260  C CE2 . TYR A 42  ? 0.70353 0.53636 0.56989 0.12970  -0.01632 -0.07652 35  TYR A CE2 
261  C CZ  . TYR A 42  ? 0.91433 0.70721 0.75722 0.14424  -0.02757 -0.08537 35  TYR A CZ  
262  O OH  . TYR A 42  ? 0.83010 0.62362 0.67072 0.16624  -0.02353 -0.08711 35  TYR A OH  
263  N N   . GLY A 43  ? 0.71729 0.49994 0.55714 0.06971  -0.05715 -0.07715 36  GLY A N   
264  C CA  . GLY A 43  ? 0.69157 0.48642 0.54934 0.05419  -0.06090 -0.06845 36  GLY A CA  
265  C C   . GLY A 43  ? 0.75227 0.55021 0.58726 0.05983  -0.05890 -0.07143 36  GLY A C   
266  O O   . GLY A 43  ? 0.82604 0.62741 0.63564 0.07604  -0.04753 -0.07845 36  GLY A O   
267  N N   . SER A 44  ? 0.62270 0.42116 0.46786 0.04699  -0.06948 -0.06430 37  SER A N   
268  C CA  . SER A 44  ? 0.59237 0.39330 0.41714 0.04961  -0.06975 -0.06413 37  SER A CA  
269  C C   . SER A 44  ? 0.58521 0.41991 0.44362 0.04030  -0.05749 -0.05144 37  SER A C   
270  O O   . SER A 44  ? 0.57533 0.42351 0.47111 0.02956  -0.05548 -0.04286 37  SER A O   
271  C CB  . SER A 44  ? 0.62823 0.39593 0.43162 0.04297  -0.09715 -0.06598 37  SER A CB  
272  O OG  . SER A 44  ? 0.61199 0.38274 0.45439 0.02490  -0.11145 -0.05455 37  SER A OG  
273  N N   . VAL A 45  ? 0.51934 0.36546 0.36203 0.04532  -0.04862 -0.04985 38  VAL A N   
274  C CA  . VAL A 45  ? 0.44244 0.31642 0.31150 0.03853  -0.03594 -0.03872 38  VAL A CA  
275  C C   . VAL A 45  ? 0.43212 0.30078 0.29298 0.03351  -0.04741 -0.03181 38  VAL A C   
276  O O   . VAL A 45  ? 0.50436 0.35597 0.32618 0.03993  -0.05542 -0.03659 38  VAL A O   
277  C CB  . VAL A 45  ? 0.50389 0.40061 0.36804 0.04652  -0.01423 -0.03886 38  VAL A CB  
278  C CG1 . VAL A 45  ? 0.45479 0.37335 0.34473 0.03737  -0.00413 -0.02755 38  VAL A CG1 
279  C CG2 . VAL A 45  ? 0.49881 0.40046 0.37039 0.05214  -0.00611 -0.04472 38  VAL A CG2 
280  N N   . CYS A 46  ? 0.48232 0.36408 0.37781 0.02339  -0.04791 -0.02033 39  CYS A N   
281  C CA  . CYS A 46  ? 0.55527 0.43595 0.45102 0.01848  -0.05833 -0.01059 39  CYS A CA  
282  C C   . CYS A 46  ? 0.47326 0.37487 0.38962 0.01639  -0.04204 -0.00106 39  CYS A C   
283  O O   . CYS A 46  ? 0.47095 0.38544 0.41313 0.01467  -0.02808 -0.00021 39  CYS A O   
284  C CB  . CYS A 46  ? 0.49688 0.37104 0.42011 0.00871  -0.07879 -0.00300 39  CYS A CB  
285  S SG  . CYS A 46  ? 0.56782 0.40814 0.45637 0.00612  -0.11066 -0.00863 39  CYS A SG  
286  N N   . ALA A 47  ? 0.55654 0.45752 0.45740 0.01621  -0.04515 0.00617  40  ALA A N   
287  C CA  . ALA A 47  ? 0.45050 0.36441 0.37137 0.01252  -0.03527 0.01745  40  ALA A CA  
288  C C   . ALA A 47  ? 0.43796 0.35106 0.39274 0.00722  -0.04722 0.02800  40  ALA A C   
289  O O   . ALA A 47  ? 0.45023 0.35392 0.40459 0.00475  -0.06745 0.03068  40  ALA A O   
290  C CB  . ALA A 47  ? 0.41935 0.33328 0.30909 0.01434  -0.03284 0.02327  40  ALA A CB  
291  N N   . ALA A 48  ? 0.53545 0.45763 0.51999 0.00592  -0.03525 0.03445  41  ALA A N   
292  C CA  . ALA A 48  ? 0.54450 0.46927 0.56615 0.00461  -0.04207 0.04536  41  ALA A CA  
293  C C   . ALA A 48  ? 0.54291 0.46869 0.57759 0.00590  -0.03091 0.05372  41  ALA A C   
294  O O   . ALA A 48  ? 0.41459 0.33943 0.43439 0.00521  -0.01741 0.05021  41  ALA A O   
295  C CB  . ALA A 48  ? 0.45255 0.38384 0.50493 0.00462  -0.03782 0.04253  41  ALA A CB  
296  N N   . PHE A 49  ? 0.51382 0.44085 0.57833 0.00767  -0.03804 0.06593  42  PHE A N   
297  C CA  . PHE A 49  ? 0.49775 0.42038 0.57754 0.01120  -0.02919 0.07441  42  PHE A CA  
298  C C   . PHE A 49  ? 0.47138 0.39808 0.58558 0.01759  -0.01512 0.07340  42  PHE A C   
299  O O   . PHE A 49  ? 0.44491 0.38262 0.59170 0.02073  -0.02076 0.08037  42  PHE A O   
300  C CB  . PHE A 49  ? 0.54036 0.46023 0.62837 0.01183  -0.04644 0.09035  42  PHE A CB  
301  C CG  . PHE A 49  ? 0.54237 0.45190 0.63894 0.01575  -0.03929 0.09955  42  PHE A CG  
302  C CD1 . PHE A 49  ? 0.65077 0.54992 0.72009 0.01131  -0.04441 0.10664  42  PHE A CD1 
303  C CD2 . PHE A 49  ? 0.59808 0.50581 0.72774 0.02463  -0.02703 0.10173  42  PHE A CD2 
304  C CE1 . PHE A 49  ? 0.67133 0.55646 0.74786 0.01378  -0.03992 0.11607  42  PHE A CE1 
305  C CE2 . PHE A 49  ? 0.66816 0.55939 0.80206 0.02958  -0.02159 0.10898  42  PHE A CE2 
306  C CZ  . PHE A 49  ? 0.64354 0.52242 0.75172 0.02323  -0.02936 0.11637  42  PHE A CZ  
307  N N   . ASP A 50  ? 0.43803 0.35579 0.54409 0.01919  0.00283  0.06577  43  ASP A N   
308  C CA  . ASP A 50  ? 0.48152 0.39749 0.60923 0.02687  0.01918  0.06282  43  ASP A CA  
309  C C   . ASP A 50  ? 0.50844 0.41404 0.65643 0.03635  0.02263  0.07325  43  ASP A C   
310  O O   . ASP A 50  ? 0.50618 0.39154 0.63759 0.03634  0.02764  0.07207  43  ASP A O   
311  C CB  . ASP A 50  ? 0.48037 0.38617 0.58360 0.02373  0.03360  0.04911  43  ASP A CB  
312  C CG  . ASP A 50  ? 0.54174 0.44259 0.65749 0.03182  0.05074  0.04432  43  ASP A CG  
313  O OD1 . ASP A 50  ? 0.52013 0.42502 0.66549 0.04213  0.05534  0.05268  43  ASP A OD1 
314  O OD2 . ASP A 50  ? 0.52728 0.42097 0.62288 0.02860  0.05998  0.03315  43  ASP A OD2 
315  N N   . THR A 51  ? 0.44211 0.36140 0.62833 0.04455  0.01923  0.08474  44  THR A N   
316  C CA  . THR A 51  ? 0.47486 0.38650 0.68511 0.05660  0.02148  0.09671  44  THR A CA  
317  C C   . THR A 51  ? 0.51709 0.40708 0.72262 0.06812  0.04445  0.08889  44  THR A C   
318  O O   . THR A 51  ? 0.55867 0.43002 0.76988 0.07804  0.04717  0.09500  44  THR A O   
319  C CB  . THR A 51  ? 0.38646 0.32370 0.64585 0.06372  0.01376  0.11265  44  THR A CB  
320  O OG1 . THR A 51  ? 0.39429 0.34847 0.67415 0.06727  0.02787  0.10927  44  THR A OG1 
321  C CG2 . THR A 51  ? 0.36288 0.31312 0.62142 0.05156  -0.01410 0.12094  44  THR A CG2 
322  N N   . LYS A 52  ? 0.56513 0.45316 0.75690 0.06753  0.05991  0.07544  45  LYS A N   
323  C CA  . LYS A 52  ? 0.59518 0.45698 0.77407 0.07861  0.08064  0.06643  45  LYS A CA  
324  C C   . LYS A 52  ? 0.63649 0.46439 0.77622 0.07076  0.07777  0.05825  45  LYS A C   
325  O O   . LYS A 52  ? 0.68199 0.47798 0.81045 0.08044  0.08809  0.05421  45  LYS A O   
326  C CB  . LYS A 52  ? 0.49563 0.36390 0.66693 0.07910  0.09624  0.05565  45  LYS A CB  
327  C CG  . LYS A 52  ? 0.58375 0.48233 0.79730 0.08890  0.10451  0.06605  45  LYS A CG  
328  C CD  . LYS A 52  ? 0.68237 0.57244 0.88912 0.10132  0.13096  0.05873  45  LYS A CD  
329  C CE  . LYS A 52  ? 0.77513 0.63946 0.93098 0.09156  0.13495  0.04015  45  LYS A CE  
330  N NZ  . LYS A 52  ? 0.73903 0.61255 0.89013 0.09328  0.15068  0.03578  45  LYS A NZ  
331  N N   . THR A 53  ? 0.63409 0.46732 0.75275 0.05362  0.06396  0.05651  46  THR A N   
332  C CA  . THR A 53  ? 0.63299 0.44083 0.71927 0.04275  0.06050  0.05182  46  THR A CA  
333  C C   . THR A 53  ? 0.62684 0.43544 0.71035 0.03438  0.04458  0.06433  46  THR A C   
334  O O   . THR A 53  ? 0.69264 0.47804 0.75592 0.02622  0.04170  0.06527  46  THR A O   
335  C CB  . THR A 53  ? 0.64177 0.45624 0.70314 0.02937  0.06164  0.03998  46  THR A CB  
336  O OG1 . THR A 53  ? 0.69179 0.53515 0.75500 0.02086  0.05074  0.04380  46  THR A OG1 
337  C CG2 . THR A 53  ? 0.67013 0.48591 0.73158 0.03640  0.07583  0.02920  46  THR A CG2 
338  N N   . GLY A 54  ? 0.59446 0.42698 0.69550 0.03498  0.03307  0.07488  47  GLY A N   
339  C CA  . GLY A 54  ? 0.57368 0.40723 0.66492 0.02660  0.01809  0.08683  47  GLY A CA  
340  C C   . GLY A 54  ? 0.65244 0.49780 0.71571 0.01184  0.01431  0.08304  47  GLY A C   
341  O O   . GLY A 54  ? 0.52699 0.37177 0.57602 0.00433  0.00535  0.09331  47  GLY A O   
342  N N   . HIS A 55  ? 0.53909 0.39583 0.59427 0.00860  0.02180  0.06994  48  HIS A N   
343  C CA  . HIS A 55  ? 0.60220 0.47338 0.63474 -0.00200 0.02053  0.06624  48  HIS A CA  
344  C C   . HIS A 55  ? 0.49787 0.39046 0.53086 0.00060  0.01490  0.06235  48  HIS A C   
345  O O   . HIS A 55  ? 0.46999 0.36745 0.52210 0.00744  0.01456  0.05918  48  HIS A O   
346  C CB  . HIS A 55  ? 0.56823 0.43466 0.58995 -0.00792 0.03072  0.05506  48  HIS A CB  
347  C CG  . HIS A 55  ? 0.66978 0.50962 0.68473 -0.01366 0.03293  0.05760  48  HIS A CG  
348  N ND1 . HIS A 55  ? 0.72147 0.54006 0.73238 -0.01245 0.04053  0.04727  48  HIS A ND1 
349  C CD2 . HIS A 55  ? 0.61150 0.43853 0.61968 -0.02149 0.02714  0.06957  48  HIS A CD2 
350  C CE1 . HIS A 55  ? 0.74287 0.53373 0.74382 -0.01944 0.03783  0.05143  48  HIS A CE1 
351  N NE2 . HIS A 55  ? 0.75868 0.55511 0.76017 -0.02560 0.02971  0.06582  48  HIS A NE2 
352  N N   . ARG A 56  ? 0.58711 0.49117 0.59808 -0.00468 0.01071  0.06339  49  ARG A N   
353  C CA  . ARG A 56  ? 0.49844 0.41581 0.50084 -0.00208 0.00578  0.05633  49  ARG A CA  
354  C C   . ARG A 56  ? 0.53851 0.46299 0.53839 -0.00259 0.01600  0.04337  49  ARG A C   
355  O O   . ARG A 56  ? 0.59170 0.51756 0.58474 -0.00779 0.02464  0.04171  49  ARG A O   
356  C CB  . ARG A 56  ? 0.48506 0.40815 0.45874 -0.00409 -0.00052 0.06139  49  ARG A CB  
357  C CG  . ARG A 56  ? 0.63172 0.54699 0.60245 -0.00363 -0.01468 0.07447  49  ARG A CG  
358  C CD  . ARG A 56  ? 0.69383 0.61157 0.62954 -0.00271 -0.02324 0.07508  49  ARG A CD  
359  N NE  . ARG A 56  ? 0.78986 0.71645 0.69986 -0.00529 -0.01093 0.07695  49  ARG A NE  
360  C CZ  . ARG A 56  ? 0.88903 0.82137 0.76569 -0.00103 -0.00894 0.07243  49  ARG A CZ  
361  N NH1 . ARG A 56  ? 0.80490 0.72866 0.66387 0.00497  -0.02103 0.06381  49  ARG A NH1 
362  N NH2 . ARG A 56  ? 0.70465 0.65080 0.56522 -0.00255 0.00546  0.07731  49  ARG A NH2 
363  N N   . VAL A 57  ? 0.48586 0.41441 0.49271 0.00161  0.01310  0.03583  50  VAL A N   
364  C CA  . VAL A 57  ? 0.43607 0.36992 0.44027 0.00179  0.02095  0.02469  50  VAL A CA  
365  C C   . VAL A 57  ? 0.42588 0.36532 0.41437 0.00493  0.01379  0.01852  50  VAL A C   
366  O O   . VAL A 57  ? 0.43242 0.36927 0.40814 0.00648  0.00280  0.02184  50  VAL A O   
367  C CB  . VAL A 57  ? 0.47395 0.40295 0.50016 0.00423  0.02674  0.02142  50  VAL A CB  
368  C CG1 . VAL A 57  ? 0.37648 0.29304 0.41066 0.00396  0.03521  0.02486  50  VAL A CG1 
369  C CG2 . VAL A 57  ? 0.42164 0.35300 0.46721 0.00771  0.01718  0.02574  50  VAL A CG2 
370  N N   . ALA A 58  ? 0.41285 0.35615 0.39876 0.00635  0.01881  0.00934  51  ALA A N   
371  C CA  . ALA A 58  ? 0.47982 0.42255 0.45051 0.01105  0.01215  0.00189  51  ALA A CA  
372  C C   . ALA A 58  ? 0.40427 0.34244 0.39141 0.01084  0.00967  -0.00232 51  ALA A C   
373  O O   . ALA A 58  ? 0.36526 0.30593 0.36367 0.00919  0.01946  -0.00414 51  ALA A O   
374  C CB  . ALA A 58  ? 0.43918 0.39200 0.39150 0.01463  0.02053  -0.00318 51  ALA A CB  
375  N N   . VAL A 59  ? 0.38354 0.31346 0.37028 0.01137  -0.00447 -0.00279 52  VAL A N   
376  C CA  . VAL A 59  ? 0.42089 0.34733 0.42600 0.00903  -0.00887 -0.00330 52  VAL A CA  
377  C C   . VAL A 59  ? 0.40907 0.32388 0.39211 0.01217  -0.01819 -0.01243 52  VAL A C   
378  O O   . VAL A 59  ? 0.43056 0.33340 0.39066 0.01462  -0.03124 -0.01543 52  VAL A O   
379  C CB  . VAL A 59  ? 0.43003 0.35668 0.46145 0.00461  -0.02032 0.00727  52  VAL A CB  
380  C CG1 . VAL A 59  ? 0.34309 0.27122 0.39881 0.00077  -0.02210 0.01024  52  VAL A CG1 
381  C CG2 . VAL A 59  ? 0.38464 0.31955 0.43524 0.00517  -0.01100 0.01609  52  VAL A CG2 
382  N N   . LYS A 60  ? 0.40698 0.32160 0.39337 0.01286  -0.01219 -0.01695 53  LYS A N   
383  C CA  . LYS A 60  ? 0.47997 0.38057 0.44618 0.01756  -0.02002 -0.02569 53  LYS A CA  
384  C C   . LYS A 60  ? 0.50246 0.39432 0.48708 0.01086  -0.02884 -0.02215 53  LYS A C   
385  O O   . LYS A 60  ? 0.44441 0.34527 0.44832 0.00744  -0.01826 -0.01785 53  LYS A O   
386  C CB  . LYS A 60  ? 0.46154 0.37007 0.41581 0.02469  -0.00681 -0.03199 53  LYS A CB  
387  C CG  . LYS A 60  ? 0.49102 0.38549 0.43233 0.03070  -0.01250 -0.03939 53  LYS A CG  
388  C CD  . LYS A 60  ? 0.61372 0.52178 0.55321 0.03659  0.00034  -0.04189 53  LYS A CD  
389  C CE  . LYS A 60  ? 0.54201 0.43553 0.46748 0.04595  -0.00534 -0.04883 53  LYS A CE  
390  N NZ  . LYS A 60  ? 0.61015 0.52104 0.53697 0.05281  0.00559  -0.04924 53  LYS A NZ  
391  N N   . LYS A 61  ? 0.47395 0.34665 0.45050 0.00816  -0.04883 -0.02308 54  LYS A N   
392  C CA  . LYS A 61  ? 0.50273 0.36491 0.49601 -0.00021 -0.06048 -0.01816 54  LYS A CA  
393  C C   . LYS A 61  ? 0.47640 0.31893 0.44558 0.00620  -0.06330 -0.02835 54  LYS A C   
394  O O   . LYS A 61  ? 0.50069 0.32217 0.43574 0.01495  -0.07241 -0.03940 54  LYS A O   
395  C CB  . LYS A 61  ? 0.49556 0.34409 0.49411 -0.00922 -0.08514 -0.01240 54  LYS A CB  
396  C CG  . LYS A 61  ? 0.48855 0.32323 0.50332 -0.02026 -0.10122 -0.00602 54  LYS A CG  
397  C CD  . LYS A 61  ? 0.58423 0.40359 0.60361 -0.03162 -0.13042 0.00040  54  LYS A CD  
398  C CE  . LYS A 61  ? 0.51002 0.32081 0.55548 -0.04649 -0.14647 0.01156  54  LYS A CE  
399  N NZ  . LYS A 61  ? 0.67468 0.46537 0.72140 -0.05994 -0.18065 0.01749  54  LYS A NZ  
400  N N   . LEU A 62  ? 0.44228 0.29011 0.42670 0.00341  -0.05484 -0.02438 55  LEU A N   
401  C CA  . LEU A 62  ? 0.56423 0.39223 0.52945 0.00930  -0.05928 -0.03171 55  LEU A CA  
402  C C   . LEU A 62  ? 0.54740 0.34237 0.50240 0.00401  -0.08455 -0.03297 55  LEU A C   
403  O O   . LEU A 62  ? 0.49355 0.28775 0.47212 -0.01023 -0.09707 -0.02186 55  LEU A O   
404  C CB  . LEU A 62  ? 0.51347 0.35255 0.49648 0.00529  -0.04705 -0.02455 55  LEU A CB  
405  C CG  . LEU A 62  ? 0.53836 0.39725 0.51676 0.01284  -0.02730 -0.02788 55  LEU A CG  
406  C CD1 . LEU A 62  ? 0.45182 0.33239 0.44103 0.01107  -0.01528 -0.02516 55  LEU A CD1 
407  C CD2 . LEU A 62  ? 0.42557 0.28770 0.41280 0.00862  -0.01941 -0.02142 55  LEU A CD2 
408  N N   . SER A 63  ? 0.62054 0.38729 0.54059 0.01591  -0.09272 -0.04599 56  SER A N   
409  C CA  . SER A 63  ? 0.59810 0.32304 0.49836 0.01247  -0.11900 -0.05041 56  SER A CA  
410  C C   . SER A 63  ? 0.59424 0.30317 0.50385 0.00720  -0.12480 -0.04535 56  SER A C   
411  O O   . SER A 63  ? 0.66505 0.37475 0.56560 0.01913  -0.11309 -0.05012 56  SER A O   
412  C CB  . SER A 63  ? 0.65720 0.35370 0.50800 0.03124  -0.12386 -0.06848 56  SER A CB  
413  O OG  . SER A 63  ? 0.88977 0.53906 0.71425 0.02709  -0.15228 -0.07443 56  SER A OG  
414  N N   . ARG A 64  ? 0.64372 0.33953 0.57351 -0.01143 -0.14382 -0.03361 57  ARG A N   
415  C CA  . ARG A 64  ? 0.75005 0.42899 0.69129 -0.02059 -0.15211 -0.02477 57  ARG A CA  
416  C C   . ARG A 64  ? 0.64753 0.35447 0.60297 -0.01526 -0.12673 -0.01947 57  ARG A C   
417  O O   . ARG A 64  ? 0.64266 0.33205 0.57943 -0.00479 -0.12574 -0.02546 57  ARG A O   
418  C CB  . ARG A 64  ? 0.79686 0.42116 0.69780 -0.01248 -0.17384 -0.03814 57  ARG A CB  
419  C CG  . ARG A 64  ? 0.86772 0.45605 0.73891 -0.01385 -0.19928 -0.04840 57  ARG A CG  
420  C CD  . ARG A 64  ? 0.84012 0.39077 0.71787 -0.03517 -0.23223 -0.03912 57  ARG A CD  
421  N NE  . ARG A 64  ? 0.99634 0.54009 0.86884 -0.04587 -0.25384 -0.03788 57  ARG A NE  
422  C CZ  . ARG A 64  ? 1.13078 0.64464 0.95385 -0.03299 -0.26536 -0.05422 57  ARG A CZ  
423  N NH1 . ARG A 64  ? 1.09413 0.58589 0.87177 -0.00772 -0.25496 -0.07279 57  ARG A NH1 
424  N NH2 . ARG A 64  ? 1.00309 0.51085 0.82315 -0.04494 -0.28698 -0.04997 57  ARG A NH2 
425  N N   . PRO A 65  ? 0.57894 0.32654 0.56500 -0.02157 -0.10719 -0.00828 58  PRO A N   
426  C CA  . PRO A 65  ? 0.55046 0.32070 0.54053 -0.01548 -0.08405 -0.00601 58  PRO A CA  
427  C C   . PRO A 65  ? 0.56642 0.32431 0.56114 -0.02187 -0.08652 0.00415  58  PRO A C   
428  O O   . PRO A 65  ? 0.46476 0.22578 0.44756 -0.01297 -0.07579 0.00136  58  PRO A O   
429  C CB  . PRO A 65  ? 0.52767 0.33502 0.54614 -0.02201 -0.06603 0.00378  58  PRO A CB  
430  C CG  . PRO A 65  ? 0.54037 0.34718 0.58363 -0.03610 -0.08088 0.01475  58  PRO A CG  
431  C CD  . PRO A 65  ? 0.47640 0.24842 0.49336 -0.03361 -0.10633 0.00305  58  PRO A CD  
432  N N   . PHE A 66  ? 0.59759 0.34209 0.61035 -0.03821 -0.10167 0.01777  59  PHE A N   
433  C CA  . PHE A 66  ? 0.54749 0.28171 0.56742 -0.04713 -0.10353 0.03159  59  PHE A CA  
434  C C   . PHE A 66  ? 0.65882 0.34751 0.66775 -0.05400 -0.13297 0.03201  59  PHE A C   
435  O O   . PHE A 66  ? 0.58802 0.26800 0.61467 -0.07018 -0.14137 0.04983  59  PHE A O   
436  C CB  . PHE A 66  ? 0.46742 0.23352 0.52522 -0.06284 -0.08940 0.05380  59  PHE A CB  
437  C CG  . PHE A 66  ? 0.56180 0.36557 0.62753 -0.05576 -0.06207 0.05239  59  PHE A CG  
438  C CD1 . PHE A 66  ? 0.55406 0.36524 0.59938 -0.04461 -0.04441 0.04555  59  PHE A CD1 
439  C CD2 . PHE A 66  ? 0.53258 0.36163 0.62559 -0.06040 -0.05620 0.05832  59  PHE A CD2 
440  C CE1 . PHE A 66  ? 0.50143 0.33995 0.54961 -0.03920 -0.02207 0.04332  59  PHE A CE1 
441  C CE2 . PHE A 66  ? 0.56998 0.42730 0.66739 -0.05269 -0.03194 0.05626  59  PHE A CE2 
442  C CZ  . PHE A 66  ? 0.46416 0.32387 0.53717 -0.04256 -0.01521 0.04805  59  PHE A CZ  
443  N N   . GLN A 67  ? 0.70315 0.35998 0.68038 -0.04156 -0.14868 0.01285  60  GLN A N   
444  C CA  . GLN A 67  ? 0.75048 0.35466 0.70915 -0.04630 -0.17871 0.00997  60  GLN A CA  
445  C C   . GLN A 67  ? 0.80543 0.38203 0.74875 -0.04013 -0.18199 0.01143  60  GLN A C   
446  O O   . GLN A 67  ? 0.80906 0.35307 0.74702 -0.04905 -0.20319 0.01638  60  GLN A O   
447  C CB  . GLN A 67  ? 0.75668 0.33073 0.67747 -0.03118 -0.19208 -0.01285 60  GLN A CB  
448  C CG  . GLN A 67  ? 0.83663 0.36487 0.73306 -0.03423 -0.22051 -0.01766 60  GLN A CG  
449  C CD  . GLN A 67  ? 0.88209 0.38743 0.73543 -0.01651 -0.22819 -0.03969 60  GLN A CD  
450  O OE1 . GLN A 67  ? 0.86611 0.35922 0.71235 -0.02629 -0.24755 -0.04002 60  GLN A OE1 
451  N NE2 . GLN A 67  ? 0.79979 0.30126 0.62422 0.01015  -0.21254 -0.05647 60  GLN A NE2 
452  N N   . SER A 68  ? 0.75585 0.35394 0.69320 -0.02489 -0.16037 0.00811  61  SER A N   
453  C CA  . SER A 68  ? 0.73705 0.31203 0.66091 -0.01750 -0.16354 0.01081  61  SER A CA  
454  C C   . SER A 68  ? 0.65541 0.27128 0.58876 -0.01247 -0.13784 0.01729  61  SER A C   
455  O O   . SER A 68  ? 0.67433 0.33094 0.62093 -0.01343 -0.11838 0.01721  61  SER A O   
456  C CB  . SER A 68  ? 0.79094 0.32492 0.67689 0.00679  -0.17544 -0.01015 61  SER A CB  
457  O OG  . SER A 68  ? 0.78153 0.34203 0.65643 0.02739  -0.15786 -0.02602 61  SER A OG  
458  N N   . ILE A 69  ? 0.71108 0.31201 0.63512 -0.00735 -0.13990 0.02315  62  ILE A N   
459  C CA  . ILE A 69  ? 0.68077 0.31398 0.60672 -0.00188 -0.12004 0.02818  62  ILE A CA  
460  C C   . ILE A 69  ? 0.61890 0.27544 0.53530 0.01845  -0.10768 0.01066  62  ILE A C   
461  O O   . ILE A 69  ? 0.56667 0.26039 0.49076 0.01739  -0.08933 0.01207  62  ILE A O   
462  C CB  . ILE A 69  ? 0.71813 0.32649 0.63325 0.00089  -0.12900 0.03808  62  ILE A CB  
463  C CG1 . ILE A 69  ? 0.64041 0.24004 0.56964 -0.02331 -0.13361 0.06166  62  ILE A CG1 
464  C CG2 . ILE A 69  ? 0.67762 0.31316 0.58673 0.01243  -0.11429 0.03789  62  ILE A CG2 
465  C CD1 . ILE A 69  ? 0.75843 0.32708 0.67548 -0.02278 -0.14582 0.07364  62  ILE A CD1 
466  N N   . ILE A 70  ? 0.65210 0.28571 0.55041 0.03732  -0.11734 -0.00548 63  ILE A N   
467  C CA  . ILE A 70  ? 0.67304 0.33113 0.56468 0.05726  -0.10469 -0.01959 63  ILE A CA  
468  C C   . ILE A 70  ? 0.53858 0.22797 0.44086 0.04963  -0.09210 -0.02341 63  ILE A C   
469  O O   . ILE A 70  ? 0.61805 0.34422 0.52842 0.05153  -0.07559 -0.02347 63  ILE A O   
470  C CB  . ILE A 70  ? 0.76354 0.38834 0.63119 0.08096  -0.11534 -0.03542 63  ILE A CB  
471  C CG1 . ILE A 70  ? 0.73943 0.33279 0.59786 0.09147  -0.12726 -0.03106 63  ILE A CG1 
472  C CG2 . ILE A 70  ? 0.65942 0.31502 0.52361 0.10117  -0.09952 -0.04725 63  ILE A CG2 
473  C CD1 . ILE A 70  ? 0.83428 0.38355 0.68949 0.07436  -0.14770 -0.02138 63  ILE A CD1 
474  N N   . HIS A 71  ? 0.57337 0.24642 0.47568 0.04009  -0.10199 -0.02577 64  HIS A N   
475  C CA  . HIS A 71  ? 0.60079 0.30155 0.51509 0.03231  -0.09223 -0.02718 64  HIS A CA  
476  C C   . HIS A 71  ? 0.53910 0.27435 0.47750 0.01748  -0.07614 -0.01330 64  HIS A C   
477  O O   . HIS A 71  ? 0.51914 0.28485 0.46435 0.01843  -0.06092 -0.01576 64  HIS A O   
478  C CB  . HIS A 71  ? 0.63370 0.30932 0.54698 0.02148  -0.11008 -0.02811 64  HIS A CB  
479  C CG  . HIS A 71  ? 0.76182 0.40686 0.64356 0.03756  -0.12195 -0.04592 64  HIS A CG  
480  N ND1 . HIS A 71  ? 0.80371 0.43761 0.67789 0.03208  -0.13301 -0.05136 64  HIS A ND1 
481  C CD2 . HIS A 71  ? 0.87048 0.49254 0.72384 0.06046  -0.12394 -0.05921 64  HIS A CD2 
482  C CE1 . HIS A 71  ? 0.84542 0.44780 0.68245 0.05063  -0.14092 -0.06841 64  HIS A CE1 
483  N NE2 . HIS A 71  ? 0.93564 0.53114 0.76056 0.06926  -0.13415 -0.07358 64  HIS A NE2 
484  N N   . ALA A 72  ? 0.52665 0.25499 0.47554 0.00419  -0.07880 0.00172  65  ALA A N   
485  C CA  . ALA A 72  ? 0.49167 0.24869 0.45844 -0.00822 -0.06165 0.01506  65  ALA A CA  
486  C C   . ALA A 72  ? 0.43710 0.21569 0.39418 0.00046  -0.04598 0.01155  65  ALA A C   
487  O O   . ALA A 72  ? 0.41233 0.21628 0.37577 -0.00240 -0.03009 0.01185  65  ALA A O   
488  C CB  . ALA A 72  ? 0.55135 0.29558 0.52807 -0.02317 -0.06675 0.03360  65  ALA A CB  
489  N N   . LYS A 73  ? 0.55538 0.32239 0.49726 0.01093  -0.05197 0.00891  66  LYS A N   
490  C CA  . LYS A 73  ? 0.43727 0.22484 0.37162 0.01779  -0.04174 0.00676  66  LYS A CA  
491  C C   . LYS A 73  ? 0.48813 0.29747 0.42382 0.02694  -0.03432 -0.00573 66  LYS A C   
492  O O   . LYS A 73  ? 0.45762 0.28955 0.39468 0.02363  -0.02232 -0.00564 66  LYS A O   
493  C CB  . LYS A 73  ? 0.47678 0.24913 0.39954 0.02841  -0.05256 0.00818  66  LYS A CB  
494  C CG  . LYS A 73  ? 0.54517 0.33361 0.46118 0.02763  -0.04673 0.01426  66  LYS A CG  
495  C CD  . LYS A 73  ? 0.47857 0.25335 0.38724 0.03957  -0.05980 0.01726  66  LYS A CD  
496  C CE  . LYS A 73  ? 0.53018 0.31984 0.43115 0.03669  -0.05809 0.02504  66  LYS A CE  
497  N NZ  . LYS A 73  ? 0.62469 0.40888 0.52455 0.05143  -0.07143 0.02789  66  LYS A NZ  
498  N N   . ARG A 74  ? 0.50562 0.30556 0.43785 0.03823  -0.04160 -0.01621 67  ARG A N   
499  C CA  . ARG A 74  ? 0.54557 0.36651 0.47814 0.04664  -0.03362 -0.02595 67  ARG A CA  
500  C C   . ARG A 74  ? 0.46374 0.30183 0.40709 0.03426  -0.02325 -0.02401 67  ARG A C   
501  O O   . ARG A 74  ? 0.48507 0.34609 0.43096 0.03519  -0.01296 -0.02649 67  ARG A O   
502  C CB  . ARG A 74  ? 0.57003 0.37238 0.49066 0.06075  -0.04234 -0.03706 67  ARG A CB  
503  C CG  . ARG A 74  ? 0.69747 0.52191 0.61534 0.07159  -0.03274 -0.04545 67  ARG A CG  
504  C CD  . ARG A 74  ? 0.63178 0.43305 0.53071 0.08364  -0.04020 -0.05664 67  ARG A CD  
505  N NE  . ARG A 74  ? 0.81170 0.57734 0.69467 0.09536  -0.05331 -0.06102 67  ARG A NE  
506  C CZ  . ARG A 74  ? 0.95007 0.67604 0.81680 0.09355  -0.06931 -0.06619 67  ARG A CZ  
507  N NH1 . ARG A 74  ? 0.84273 0.56297 0.70983 0.07998  -0.07512 -0.06643 67  ARG A NH1 
508  N NH2 . ARG A 74  ? 0.92670 0.61603 0.77661 0.10533  -0.08171 -0.07054 67  ARG A NH2 
509  N N   . THR A 75  ? 0.38461 0.21208 0.33676 0.02253  -0.02651 -0.01813 68  THR A N   
510  C CA  . THR A 75  ? 0.45574 0.30007 0.42190 0.01290  -0.01611 -0.01448 68  THR A CA  
511  C C   . THR A 75  ? 0.37201 0.23223 0.33904 0.00768  -0.00110 -0.00892 68  THR A C   
512  O O   . THR A 75  ? 0.36109 0.23714 0.32959 0.00754  0.00930  -0.01197 68  THR A O   
513  C CB  . THR A 75  ? 0.46219 0.29576 0.44374 0.00153  -0.02349 -0.00582 68  THR A CB  
514  O OG1 . THR A 75  ? 0.43149 0.24661 0.40690 0.00519  -0.03983 -0.01298 68  THR A OG1 
515  C CG2 . THR A 75  ? 0.35568 0.20987 0.35675 -0.00641 -0.01058 0.00087  68  THR A CG2 
516  N N   . TYR A 76  ? 0.41422 0.26643 0.37643 0.00321  -0.00077 -0.00066 69  TYR A N   
517  C CA  . TYR A 76  ? 0.41056 0.27125 0.36395 -0.00098 0.01203  0.00351  69  TYR A CA  
518  C C   . TYR A 76  ? 0.42180 0.29304 0.36357 0.00519  0.01249  -0.00452 69  TYR A C   
519  O O   . TYR A 76  ? 0.44441 0.32345 0.37928 0.00153  0.02220  -0.00561 69  TYR A O   
520  C CB  . TYR A 76  ? 0.44885 0.29626 0.39361 -0.00603 0.00997  0.01449  69  TYR A CB  
521  C CG  . TYR A 76  ? 0.44365 0.29342 0.36996 -0.01003 0.02168  0.01876  69  TYR A CG  
522  C CD1 . TYR A 76  ? 0.47703 0.33230 0.40352 -0.01510 0.03919  0.02312  69  TYR A CD1 
523  C CD2 . TYR A 76  ? 0.49066 0.33517 0.39736 -0.00774 0.01459  0.01878  69  TYR A CD2 
524  C CE1 . TYR A 76  ? 0.48477 0.33542 0.38560 -0.01730 0.05003  0.02521  69  TYR A CE1 
525  C CE2 . TYR A 76  ? 0.42139 0.26281 0.30442 -0.01242 0.02231  0.02212  69  TYR A CE2 
526  C CZ  . TYR A 76  ? 0.52913 0.37115 0.40591 -0.01700 0.04035  0.02432  69  TYR A CZ  
527  O OH  . TYR A 76  ? 0.49425 0.32683 0.33904 -0.02020 0.04824  0.02579  69  TYR A OH  
528  N N   . ARG A 77  ? 0.41493 0.28593 0.35505 0.01485  0.00181  -0.00947 70  ARG A N   
529  C CA  . ARG A 77  ? 0.45761 0.34459 0.39403 0.02023  0.00144  -0.01351 70  ARG A CA  
530  C C   . ARG A 77  ? 0.41373 0.31707 0.35670 0.01958  0.00912  -0.01915 70  ARG A C   
531  O O   . ARG A 77  ? 0.34264 0.25650 0.28206 0.01438  0.01348  -0.01899 70  ARG A O   
532  C CB  . ARG A 77  ? 0.45523 0.34135 0.39293 0.03406  -0.00906 -0.01588 70  ARG A CB  
533  C CG  . ARG A 77  ? 0.41943 0.33019 0.36297 0.04174  -0.00824 -0.01827 70  ARG A CG  
534  C CD  . ARG A 77  ? 0.40059 0.31142 0.34736 0.05996  -0.01503 -0.02050 70  ARG A CD  
535  N NE  . ARG A 77  ? 0.45589 0.34857 0.39704 0.06308  -0.02526 -0.01498 70  ARG A NE  
536  C CZ  . ARG A 77  ? 0.46395 0.33055 0.39918 0.07213  -0.03293 -0.01726 70  ARG A CZ  
537  N NH1 . ARG A 77  ? 0.43867 0.29248 0.36999 0.07903  -0.03267 -0.02611 70  ARG A NH1 
538  N NH2 . ARG A 77  ? 0.42568 0.27505 0.35596 0.07363  -0.04291 -0.01018 70  ARG A NH2 
539  N N   . GLU A 78  ? 0.38420 0.28680 0.33441 0.02384  0.00893  -0.02361 71  GLU A N   
540  C CA  . GLU A 78  ? 0.42137 0.33841 0.37658 0.02347  0.01532  -0.02733 71  GLU A CA  
541  C C   . GLU A 78  ? 0.46053 0.37754 0.41731 0.01289  0.02483  -0.02471 71  GLU A C   
542  O O   . GLU A 78  ? 0.46851 0.39529 0.42460 0.00976  0.02984  -0.02588 71  GLU A O   
543  C CB  . GLU A 78  ? 0.44298 0.35499 0.40018 0.02994  0.01142  -0.03199 71  GLU A CB  
544  C CG  . GLU A 78  ? 0.54686 0.47575 0.50407 0.03528  0.01570  -0.03552 71  GLU A CG  
545  C CD  . GLU A 78  ? 0.56306 0.48437 0.51765 0.03761  0.01284  -0.03896 71  GLU A CD  
546  O OE1 . GLU A 78  ? 0.55567 0.48786 0.50532 0.04381  0.01597  -0.04141 71  GLU A OE1 
547  O OE2 . GLU A 78  ? 0.60405 0.50935 0.56169 0.03248  0.00675  -0.03770 71  GLU A OE2 
548  N N   . LEU A 79  ? 0.37774 0.28328 0.33718 0.00784  0.02789  -0.02018 72  LEU A N   
549  C CA  . LEU A 79  ? 0.44482 0.34985 0.40577 0.00178  0.03993  -0.01753 72  LEU A CA  
550  C C   . LEU A 79  ? 0.37428 0.27573 0.31670 -0.00210 0.04503  -0.01815 72  LEU A C   
551  O O   . LEU A 79  ? 0.43585 0.33725 0.37293 -0.00461 0.05129  -0.02102 72  LEU A O   
552  C CB  . LEU A 79  ? 0.37577 0.27436 0.34759 -0.00157 0.04399  -0.00963 72  LEU A CB  
553  C CG  . LEU A 79  ? 0.41169 0.31210 0.38929 -0.00375 0.05958  -0.00563 72  LEU A CG  
554  C CD1 . LEU A 79  ? 0.30735 0.21353 0.28802 -0.00156 0.06242  -0.01131 72  LEU A CD1 
555  C CD2 . LEU A 79  ? 0.49723 0.40111 0.49875 -0.00625 0.06204  0.00490  72  LEU A CD2 
556  N N   . ARG A 80  ? 0.42401 0.31877 0.35380 -0.00316 0.04040  -0.01524 73  ARG A N   
557  C CA  . ARG A 80  ? 0.48793 0.37574 0.39498 -0.00804 0.04141  -0.01566 73  ARG A CA  
558  C C   . ARG A 80  ? 0.41364 0.31258 0.32048 -0.00944 0.03413  -0.01994 73  ARG A C   
559  O O   . ARG A 80  ? 0.41327 0.30500 0.30466 -0.01586 0.03570  -0.02222 73  ARG A O   
560  C CB  . ARG A 80  ? 0.43994 0.31914 0.33379 -0.00889 0.03466  -0.00995 73  ARG A CB  
561  C CG  . ARG A 80  ? 0.61052 0.47481 0.49000 -0.01238 0.04590  -0.00362 73  ARG A CG  
562  C CD  . ARG A 80  ? 0.57783 0.43044 0.43341 -0.01537 0.03887  0.00211  73  ARG A CD  
563  N NE  . ARG A 80  ? 0.57964 0.41983 0.40258 -0.02041 0.04077  -0.00099 73  ARG A NE  
564  C CZ  . ARG A 80  ? 0.78701 0.62727 0.59726 -0.02383 0.02573  -0.00272 73  ARG A CZ  
565  N NH1 . ARG A 80  ? 0.65499 0.51139 0.48570 -0.02036 0.01076  -0.00096 73  ARG A NH1 
566  N NH2 . ARG A 80  ? 0.70158 0.52453 0.47746 -0.03037 0.02523  -0.00581 73  ARG A NH2 
567  N N   . LEU A 81  ? 0.39322 0.30864 0.31630 -0.00343 0.02624  -0.02039 74  LEU A N   
568  C CA  . LEU A 81  ? 0.45329 0.38603 0.38240 -0.00480 0.02092  -0.02087 74  LEU A CA  
569  C C   . LEU A 81  ? 0.43808 0.37317 0.37139 -0.00892 0.02789  -0.02360 74  LEU A C   
570  O O   . LEU A 81  ? 0.50874 0.44295 0.43527 -0.01758 0.02584  -0.02332 74  LEU A O   
571  C CB  . LEU A 81  ? 0.49212 0.44330 0.43730 0.00629  0.01508  -0.01985 74  LEU A CB  
572  C CG  . LEU A 81  ? 0.47867 0.45555 0.43769 0.00711  0.01392  -0.01778 74  LEU A CG  
573  C CD1 . LEU A 81  ? 0.49849 0.48758 0.45938 0.00110  0.00403  -0.01127 74  LEU A CD1 
574  C CD2 . LEU A 81  ? 0.45322 0.44390 0.42402 0.02229  0.01562  -0.01917 74  LEU A CD2 
575  N N   . LEU A 82  ? 0.39277 0.32830 0.33642 -0.00376 0.03391  -0.02545 75  LEU A N   
576  C CA  . LEU A 82  ? 0.39423 0.33169 0.34287 -0.00663 0.03932  -0.02648 75  LEU A CA  
577  C C   . LEU A 82  ? 0.41745 0.33558 0.35230 -0.01363 0.04581  -0.02792 75  LEU A C   
578  O O   . LEU A 82  ? 0.49749 0.41269 0.42915 -0.01941 0.04601  -0.02841 75  LEU A O   
579  C CB  . LEU A 82  ? 0.35600 0.29494 0.31629 -0.00009 0.04194  -0.02711 75  LEU A CB  
580  C CG  . LEU A 82  ? 0.52382 0.47617 0.48997 0.00853  0.03641  -0.02797 75  LEU A CG  
581  C CD1 . LEU A 82  ? 0.51018 0.45801 0.48126 0.01259  0.03594  -0.02908 75  LEU A CD1 
582  C CD2 . LEU A 82  ? 0.49857 0.47059 0.46780 0.00800  0.03620  -0.02568 75  LEU A CD2 
583  N N   . LYS A 83  ? 0.44378 0.34662 0.36860 -0.01260 0.05182  -0.02809 76  LYS A N   
584  C CA  . LYS A 83  ? 0.43115 0.31244 0.33710 -0.01561 0.06093  -0.03047 76  LYS A CA  
585  C C   . LYS A 83  ? 0.53166 0.40086 0.41372 -0.02444 0.05324  -0.03330 76  LYS A C   
586  O O   . LYS A 83  ? 0.49706 0.34361 0.35940 -0.02744 0.05800  -0.03745 76  LYS A O   
587  C CB  . LYS A 83  ? 0.44325 0.31398 0.34148 -0.01195 0.07083  -0.02795 76  LYS A CB  
588  C CG  . LYS A 83  ? 0.44363 0.32247 0.36673 -0.00588 0.07963  -0.02328 76  LYS A CG  
589  C CD  . LYS A 83  ? 0.52306 0.39615 0.44265 -0.00388 0.09035  -0.01712 76  LYS A CD  
590  C CE  . LYS A 83  ? 0.51592 0.36805 0.40637 -0.00221 0.10490  -0.01976 76  LYS A CE  
591  N NZ  . LYS A 83  ? 0.54482 0.39493 0.43272 0.00112  0.11967  -0.01137 76  LYS A NZ  
592  N N   . HIS A 84  ? 0.45584 0.33807 0.33930 -0.02835 0.04021  -0.03071 77  HIS A N   
593  C CA  . HIS A 84  ? 0.51833 0.39214 0.38301 -0.03913 0.02827  -0.03088 77  HIS A CA  
594  C C   . HIS A 84  ? 0.49807 0.38654 0.37802 -0.04672 0.01999  -0.02826 77  HIS A C   
595  O O   . HIS A 84  ? 0.46500 0.34023 0.32919 -0.05883 0.00980  -0.02836 77  HIS A O   
596  C CB  . HIS A 84  ? 0.52640 0.40969 0.38885 -0.03962 0.01690  -0.02626 77  HIS A CB  
597  C CG  . HIS A 84  ? 0.66979 0.54013 0.50835 -0.05177 0.00222  -0.02531 77  HIS A CG  
598  N ND1 . HIS A 84  ? 0.75872 0.59409 0.55630 -0.05629 0.00354  -0.03002 77  HIS A ND1 
599  C CD2 . HIS A 84  ? 0.66727 0.55495 0.51663 -0.06064 -0.01517 -0.01918 77  HIS A CD2 
600  C CE1 . HIS A 84  ? 0.74012 0.56756 0.52025 -0.06868 -0.01507 -0.02809 77  HIS A CE1 
601  N NE2 . HIS A 84  ? 0.69963 0.56081 0.51441 -0.07234 -0.02739 -0.02045 77  HIS A NE2 
602  N N   . MET A 85  ? 0.45929 0.37280 0.36717 -0.04084 0.02341  -0.02510 78  MET A N   
603  C CA  . MET A 85  ? 0.44876 0.38220 0.37397 -0.04747 0.01757  -0.01933 78  MET A CA  
604  C C   . MET A 85  ? 0.47286 0.38555 0.38987 -0.05389 0.02146  -0.02160 78  MET A C   
605  O O   . MET A 85  ? 0.46241 0.37191 0.38563 -0.04632 0.03179  -0.02351 78  MET A O   
606  C CB  . MET A 85  ? 0.38323 0.34746 0.33390 -0.03651 0.02194  -0.01545 78  MET A CB  
607  C CG  . MET A 85  ? 0.33567 0.32155 0.29700 -0.02859 0.01684  -0.01216 78  MET A CG  
608  S SD  . MET A 85  ? 0.39306 0.39362 0.35881 -0.03961 0.00099  -0.00369 78  MET A SD  
609  C CE  . MET A 85  ? 0.44630 0.40755 0.37669 -0.04688 -0.00446 -0.01027 78  MET A CE  
610  N N   . LYS A 86  ? 0.44439 0.34089 0.34736 -0.06832 0.01104  -0.02069 79  LYS A N   
611  C CA  . LYS A 86  ? 0.54144 0.41166 0.43345 -0.07542 0.01186  -0.02271 79  LYS A CA  
612  C C   . LYS A 86  ? 0.52236 0.40680 0.42791 -0.09219 -0.00244 -0.01242 79  LYS A C   
613  O O   . LYS A 86  ? 0.48729 0.35183 0.37561 -0.10734 -0.01724 -0.01215 79  LYS A O   
614  C CB  . LYS A 86  ? 0.55925 0.38241 0.41179 -0.07676 0.01308  -0.03322 79  LYS A CB  
615  C CG  . LYS A 86  ? 0.65168 0.46599 0.49303 -0.06161 0.02808  -0.03985 79  LYS A CG  
616  C CD  . LYS A 86  ? 0.65603 0.45879 0.50221 -0.04976 0.04462  -0.04294 79  LYS A CD  
617  C CE  . LYS A 86  ? 0.64053 0.43002 0.47283 -0.03718 0.06001  -0.04773 79  LYS A CE  
618  N NZ  . LYS A 86  ? 0.72779 0.48018 0.51578 -0.04029 0.05942  -0.05523 79  LYS A NZ  
619  N N   . HIS A 87  ? 0.48933 0.40730 0.42444 -0.09025 0.00147  -0.00292 80  HIS A N   
620  C CA  . HIS A 87  ? 0.42164 0.36282 0.37693 -0.10568 -0.00934 0.01101  80  HIS A CA  
621  C C   . HIS A 87  ? 0.41221 0.37676 0.38880 -0.10074 0.00096  0.01934  80  HIS A C   
622  O O   . HIS A 87  ? 0.41074 0.38943 0.39336 -0.08401 0.01337  0.01614  80  HIS A O   
623  C CB  . HIS A 87  ? 0.37687 0.35474 0.35155 -0.10811 -0.01820 0.01951  80  HIS A CB  
624  C CG  . HIS A 87  ? 0.38923 0.39596 0.39012 -0.12558 -0.03008 0.03701  80  HIS A CG  
625  N ND1 . HIS A 87  ? 0.36177 0.40848 0.39310 -0.12290 -0.02119 0.05052  80  HIS A ND1 
626  C CD2 . HIS A 87  ? 0.40761 0.41019 0.40951 -0.14689 -0.05074 0.04495  80  HIS A CD2 
627  C CE1 . HIS A 87  ? 0.42221 0.49224 0.47671 -0.14175 -0.03394 0.06766  80  HIS A CE1 
628  N NE2 . HIS A 87  ? 0.44227 0.48596 0.48093 -0.15761 -0.05376 0.06476  80  HIS A NE2 
629  N N   . GLU A 88  ? 0.46832 0.43485 0.45407 -0.11664 -0.00591 0.03097  81  GLU A N   
630  C CA  . GLU A 88  ? 0.46107 0.44143 0.45979 -0.11376 0.00341  0.03970  81  GLU A CA  
631  C C   . GLU A 88  ? 0.37364 0.40368 0.39573 -0.10164 0.01393  0.04822  81  GLU A C   
632  O O   . GLU A 88  ? 0.36566 0.40256 0.38812 -0.09064 0.02510  0.04918  81  GLU A O   
633  C CB  . GLU A 88  ? 0.44852 0.42088 0.45295 -0.13578 -0.00758 0.05326  81  GLU A CB  
634  C CG  . GLU A 88  ? 0.54313 0.45716 0.51876 -0.14441 -0.01602 0.04379  81  GLU A CG  
635  C CD  . GLU A 88  ? 0.71668 0.61624 0.69292 -0.17114 -0.03578 0.05466  81  GLU A CD  
636  O OE1 . GLU A 88  ? 0.74956 0.60838 0.69925 -0.18020 -0.04929 0.04464  81  GLU A OE1 
637  O OE2 . GLU A 88  ? 0.72526 0.65301 0.72684 -0.18379 -0.03837 0.07402  81  GLU A OE2 
638  N N   . ASN A 89  ? 0.39610 0.45957 0.43605 -0.10246 0.01020  0.05480  82  ASN A N   
639  C CA  . ASN A 89  ? 0.31499 0.42426 0.37536 -0.08789 0.02191  0.06260  82  ASN A CA  
640  C C   . ASN A 89  ? 0.33959 0.44942 0.39210 -0.06731 0.02731  0.04924  82  ASN A C   
641  O O   . ASN A 89  ? 0.29883 0.44273 0.36623 -0.05389 0.03434  0.05391  82  ASN A O   
642  C CB  . ASN A 89  ? 0.31687 0.46963 0.40946 -0.09961 0.01637  0.08242  82  ASN A CB  
643  C CG  . ASN A 89  ? 0.33486 0.48653 0.43754 -0.12345 0.00859  0.09835  82  ASN A CG  
644  O OD1 . ASN A 89  ? 0.35249 0.49561 0.46104 -0.14477 -0.00940 0.10460  82  ASN A OD1 
645  N ND2 . ASN A 89  ? 0.33515 0.49209 0.43736 -0.12104 0.02016  0.10551  82  ASN A ND2 
646  N N   . VAL A 90  ? 0.37139 0.44347 0.40093 -0.06387 0.02490  0.03371  83  VAL A N   
647  C CA  . VAL A 90  ? 0.36120 0.42835 0.38218 -0.04678 0.02885  0.02216  83  VAL A CA  
648  C C   . VAL A 90  ? 0.42889 0.46644 0.43222 -0.03930 0.03515  0.01125  83  VAL A C   
649  O O   . VAL A 90  ? 0.42086 0.43029 0.41301 -0.04779 0.03330  0.00801  83  VAL A O   
650  C CB  . VAL A 90  ? 0.38793 0.44299 0.40211 -0.05158 0.01821  0.01765  83  VAL A CB  
651  C CG1 . VAL A 90  ? 0.33137 0.38062 0.33775 -0.03486 0.02203  0.00807  83  VAL A CG1 
652  C CG2 . VAL A 90  ? 0.31410 0.40042 0.35010 -0.06106 0.00829  0.03098  83  VAL A CG2 
653  N N   . ILE A 91  ? 0.39676 0.43964 0.39799 -0.02307 0.04168  0.00621  84  ILE A N   
654  C CA  . ILE A 91  ? 0.46000 0.47870 0.44962 -0.01707 0.04482  -0.00185 84  ILE A CA  
655  C C   . ILE A 91  ? 0.36196 0.35281 0.34212 -0.02175 0.04221  -0.00896 84  ILE A C   
656  O O   . ILE A 91  ? 0.37463 0.36338 0.35134 -0.02320 0.03819  -0.01131 84  ILE A O   
657  C CB  . ILE A 91  ? 0.44045 0.46420 0.42638 -0.00085 0.04742  -0.00702 84  ILE A CB  
658  C CG1 . ILE A 91  ? 0.46383 0.46938 0.44240 0.00268  0.04804  -0.01079 84  ILE A CG1 
659  C CG2 . ILE A 91  ? 0.37039 0.38838 0.35425 0.00477  0.04366  -0.01315 84  ILE A CG2 
660  C CD1 . ILE A 91  ? 0.40450 0.41565 0.38234 -0.00027 0.05074  -0.00363 84  ILE A CD1 
661  N N   . GLY A 92  ? 0.41808 0.38780 0.39339 -0.02309 0.04523  -0.01128 85  GLY A N   
662  C CA  . GLY A 92  ? 0.48355 0.42726 0.44863 -0.02517 0.04691  -0.01704 85  GLY A CA  
663  C C   . GLY A 92  ? 0.46894 0.40167 0.43772 -0.01709 0.05260  -0.01931 85  GLY A C   
664  O O   . GLY A 92  ? 0.45943 0.39838 0.43637 -0.01345 0.05261  -0.01604 85  GLY A O   
665  N N   . LEU A 93  ? 0.41567 0.33301 0.37860 -0.01475 0.05715  -0.02335 86  LEU A N   
666  C CA  . LEU A 93  ? 0.47560 0.38781 0.44851 -0.00756 0.06292  -0.02271 86  LEU A CA  
667  C C   . LEU A 93  ? 0.47573 0.37145 0.44945 -0.00649 0.06998  -0.02154 86  LEU A C   
668  O O   . LEU A 93  ? 0.66364 0.53926 0.62137 -0.00817 0.07546  -0.02528 86  LEU A O   
669  C CB  . LEU A 93  ? 0.43002 0.33725 0.39903 -0.00505 0.06679  -0.02452 86  LEU A CB  
670  C CG  . LEU A 93  ? 0.43338 0.35262 0.40932 -0.00211 0.06015  -0.02380 86  LEU A CG  
671  C CD1 . LEU A 93  ? 0.43167 0.34346 0.40559 -0.00119 0.06503  -0.02245 86  LEU A CD1 
672  C CD2 . LEU A 93  ? 0.40841 0.33592 0.39974 0.00167  0.05500  -0.02105 86  LEU A CD2 
673  N N   . LEU A 94  ? 0.45282 0.35401 0.44246 -0.00275 0.06899  -0.01651 87  LEU A N   
674  C CA  . LEU A 94  ? 0.41007 0.29703 0.40636 0.00195  0.07612  -0.01378 87  LEU A CA  
675  C C   . LEU A 94  ? 0.51531 0.40449 0.52834 0.01048  0.08482  -0.01071 87  LEU A C   
676  O O   . LEU A 94  ? 0.47214 0.34829 0.48855 0.01754  0.09574  -0.00942 87  LEU A O   
677  C CB  . LEU A 94  ? 0.35642 0.24862 0.36350 0.00168  0.06950  -0.00709 87  LEU A CB  
678  C CG  . LEU A 94  ? 0.53004 0.42573 0.52596 -0.00702 0.06223  -0.00558 87  LEU A CG  
679  C CD1 . LEU A 94  ? 0.52344 0.42681 0.52852 -0.00600 0.05613  0.00277  87  LEU A CD1 
680  C CD2 . LEU A 94  ? 0.55038 0.42366 0.53108 -0.01353 0.06422  -0.00788 87  LEU A CD2 
681  N N   . ASP A 95  ? 0.41816 0.32297 0.44251 0.01039  0.08053  -0.00852 88  ASP A N   
682  C CA  . ASP A 95  ? 0.43568 0.34748 0.48211 0.01576  0.08723  -0.00184 88  ASP A CA  
683  C C   . ASP A 95  ? 0.45461 0.37759 0.50575 0.01167  0.07878  -0.00071 88  ASP A C   
684  O O   . ASP A 95  ? 0.43606 0.36266 0.47878 0.00792  0.06603  -0.00432 88  ASP A O   
685  C CB  . ASP A 95  ? 0.41337 0.33326 0.48794 0.02046  0.08473  0.00762  88  ASP A CB  
686  C CG  . ASP A 95  ? 0.49477 0.42556 0.59890 0.02665  0.09454  0.01770  88  ASP A CG  
687  O OD1 . ASP A 95  ? 0.51881 0.44512 0.61598 0.03007  0.10970  0.01645  88  ASP A OD1 
688  O OD2 . ASP A 95  ? 0.41260 0.35762 0.54723 0.02782  0.08689  0.02832  88  ASP A OD2 
689  N N   . VAL A 96  ? 0.38303 0.31008 0.44678 0.01328  0.08694  0.00506  89  VAL A N   
690  C CA  . VAL A 96  ? 0.41509 0.34952 0.48712 0.00847  0.07832  0.00893  89  VAL A CA  
691  C C   . VAL A 96  ? 0.48200 0.42989 0.58898 0.00956  0.08350  0.02298  89  VAL A C   
692  O O   . VAL A 96  ? 0.40375 0.35366 0.51818 0.01583  0.10235  0.02804  89  VAL A O   
693  C CB  . VAL A 96  ? 0.42068 0.34649 0.46874 0.00613  0.08260  0.00390  89  VAL A CB  
694  C CG1 . VAL A 96  ? 0.40026 0.32848 0.45284 0.00107  0.06922  0.00655  89  VAL A CG1 
695  C CG2 . VAL A 96  ? 0.53409 0.44986 0.55287 0.00536  0.08071  -0.00713 89  VAL A CG2 
696  N N   . PHE A 97  ? 0.40868 0.36530 0.53677 0.00378  0.06679  0.02998  90  PHE A N   
697  C CA  . PHE A 97  ? 0.43451 0.40860 0.60325 0.00225  0.06842  0.04673  90  PHE A CA  
698  C C   . PHE A 97  ? 0.42651 0.40164 0.60646 -0.00884 0.04890  0.05289  90  PHE A C   
699  O O   . PHE A 97  ? 0.41150 0.37201 0.56865 -0.01280 0.03112  0.04305  90  PHE A O   
700  C CB  . PHE A 97  ? 0.38139 0.36633 0.57652 0.00651  0.06490  0.05395  90  PHE A CB  
701  C CG  . PHE A 97  ? 0.36221 0.34176 0.55126 0.00109  0.03981  0.05029  90  PHE A CG  
702  C CD1 . PHE A 97  ? 0.29816 0.28247 0.50663 -0.00832 0.01806  0.05895  90  PHE A CD1 
703  C CD2 . PHE A 97  ? 0.35861 0.32665 0.52051 0.00481  0.03754  0.03919  90  PHE A CD2 
704  C CE1 . PHE A 97  ? 0.35493 0.32903 0.54943 -0.01223 -0.00512 0.05437  90  PHE A CE1 
705  C CE2 . PHE A 97  ? 0.39684 0.35947 0.54825 0.00119  0.01700  0.03658  90  PHE A CE2 
706  C CZ  . PHE A 97  ? 0.33602 0.29996 0.50069 -0.00645 -0.00415 0.04312  90  PHE A CZ  
707  N N   . THR A 98  ? 0.31899 0.31077 0.53450 -0.01327 0.05308  0.07020  91  THR A N   
708  C CA  . THR A 98  ? 0.31032 0.30364 0.54523 -0.02645 0.03283  0.08073  91  THR A CA  
709  C C   . THR A 98  ? 0.38605 0.40722 0.67564 -0.03020 0.03162  0.10283  91  THR A C   
710  O O   . THR A 98  ? 0.44804 0.48989 0.76119 -0.02138 0.05628  0.11312  91  THR A O   
711  C CB  . THR A 98  ? 0.42338 0.41025 0.64815 -0.03180 0.03917  0.08388  91  THR A CB  
712  O OG1 . THR A 98  ? 0.34253 0.32669 0.58690 -0.04634 0.01631  0.09509  91  THR A OG1 
713  C CG2 . THR A 98  ? 0.30701 0.31297 0.54901 -0.02614 0.06913  0.09655  91  THR A CG2 
714  N N   . PRO A 99  ? 0.45189 0.47360 0.76216 -0.04233 0.00301  0.11090  92  PRO A N   
715  C CA  . PRO A 99  ? 0.39134 0.44399 0.76120 -0.04851 -0.00161 0.13584  92  PRO A CA  
716  C C   . PRO A 99  ? 0.41745 0.49235 0.82241 -0.05467 0.01329  0.15660  92  PRO A C   
717  O O   . PRO A 99  ? 0.41587 0.52542 0.87648 -0.05602 0.01921  0.18018  92  PRO A O   
718  C CB  . PRO A 99  ? 0.41826 0.45675 0.79014 -0.06350 -0.04154 0.13703  92  PRO A CB  
719  C CG  . PRO A 99  ? 0.53545 0.53733 0.84579 -0.05878 -0.05176 0.11028  92  PRO A CG  
720  C CD  . PRO A 99  ? 0.46937 0.46220 0.74831 -0.05026 -0.02706 0.09796  92  PRO A CD  
721  N N   . ALA A 100 ? 0.49481 0.55304 0.87070 -0.05784 0.02037  0.15047  93  ALA A N   
722  C CA  . ALA A 100 ? 0.57201 0.64914 0.97718 -0.06562 0.03345  0.17191  93  ALA A CA  
723  C C   . ALA A 100 ? 0.49002 0.59269 0.90794 -0.04927 0.07422  0.17991  93  ALA A C   
724  O O   . ALA A 100 ? 0.47440 0.56380 0.85473 -0.03314 0.09328  0.16155  93  ALA A O   
725  C CB  . ALA A 100 ? 0.57905 0.62638 0.94449 -0.07323 0.02709  0.16289  93  ALA A CB  
726  N N   . ARG A 101 ? 0.48134 0.61990 0.95215 -0.05347 0.08744  0.20826  94  ARG A N   
727  C CA  . ARG A 101 ? 0.56538 0.72831 1.04775 -0.03662 0.12934  0.21854  94  ARG A CA  
728  C C   . ARG A 101 ? 0.49153 0.65557 0.96326 -0.04233 0.14726  0.22985  94  ARG A C   
729  O O   . ARG A 101 ? 0.41173 0.59212 0.88288 -0.02738 0.17768  0.23727  94  ARG A O   
730  C CB  . ARG A 101 ? 0.50136 0.70597 1.04582 -0.03013 0.13502  0.24141  94  ARG A CB  
731  C CG  . ARG A 101 ? 0.54346 0.76386 1.13138 -0.05036 0.10092  0.26147  94  ARG A CG  
732  C CD  . ARG A 101 ? 0.64334 0.88882 1.27751 -0.04511 0.08915  0.27359  94  ARG A CD  
733  N NE  . ARG A 101 ? 0.72525 0.97833 1.39318 -0.06647 0.05079  0.29048  94  ARG A NE  
734  C CZ  . ARG A 101 ? 0.80702 1.08556 1.51148 -0.07270 0.04944  0.31543  94  ARG A CZ  
735  N NH1 . ARG A 101 ? 0.85057 1.13054 1.58072 -0.09316 0.01180  0.32964  94  ARG A NH1 
736  N NH2 . ARG A 101 ? 0.83837 1.13923 1.55089 -0.05801 0.08623  0.32637  94  ARG A NH2 
737  N N   . SER A 102 ? 0.50966 0.64795 0.95744 -0.05962 0.12360  0.22545  95  SER A N   
738  C CA  . SER A 102 ? 0.44132 0.57458 0.87258 -0.06632 0.13664  0.23554  95  SER A CA  
739  C C   . SER A 102 ? 0.53102 0.62012 0.91327 -0.07666 0.10920  0.21629  95  SER A C   
740  O O   . SER A 102 ? 0.52376 0.59198 0.89615 -0.08150 0.07879  0.20079  95  SER A O   
741  C CB  . SER A 102 ? 0.41097 0.57307 0.88497 -0.07649 0.12991  0.26139  95  SER A CB  
742  O OG  . SER A 102 ? 0.53266 0.68251 1.02280 -0.09872 0.08930  0.26625  95  SER A OG  
743  N N   . LEU A 103 ? 0.56153 0.63617 0.91161 -0.07850 0.12103  0.21810  96  LEU A N   
744  C CA  . LEU A 103 ? 0.52570 0.55912 0.82949 -0.08502 0.09766  0.20089  96  LEU A CA  
745  C C   . LEU A 103 ? 0.56345 0.58535 0.89149 -0.10638 0.06144  0.21154  96  LEU A C   
746  O O   . LEU A 103 ? 0.53904 0.52621 0.83734 -0.10881 0.03398  0.19257  96  LEU A O   
747  C CB  . LEU A 103 ? 0.55793 0.57942 0.82301 -0.08197 0.11815  0.20324  96  LEU A CB  
748  C CG  . LEU A 103 ? 0.58946 0.57120 0.81071 -0.08767 0.09594  0.19007  96  LEU A CG  
749  C CD1 . LEU A 103 ? 0.51114 0.46899 0.69783 -0.07701 0.08056  0.15887  96  LEU A CD1 
750  C CD2 . LEU A 103 ? 0.48565 0.45896 0.67036 -0.08455 0.11713  0.19566  96  LEU A CD2 
751  N N   . GLU A 104 ? 0.57531 0.62474 0.95603 -0.12148 0.06069  0.24197  97  GLU A N   
752  C CA  . GLU A 104 ? 0.61455 0.64977 1.01080 -0.14028 0.02181  0.24773  97  GLU A CA  
753  C C   . GLU A 104 ? 0.58818 0.61679 0.99854 -0.14311 -0.00668 0.23700  97  GLU A C   
754  O O   . GLU A 104 ? 0.69984 0.69748 1.09950 -0.15506 -0.04283 0.23031  97  GLU A O   
755  C CB  . GLU A 104 ? 0.64065 0.70948 1.07762 -0.14925 0.02536  0.27463  97  GLU A CB  
756  C CG  . GLU A 104 ? 0.76510 0.88402 1.24069 -0.13615 0.05581  0.28871  97  GLU A CG  
757  C CD  . GLU A 104 ? 0.84126 0.96935 1.29003 -0.11853 0.09929  0.28685  97  GLU A CD  
758  O OE1 . GLU A 104 ? 0.88552 1.04588 1.35507 -0.11259 0.12387  0.30475  97  GLU A OE1 
759  O OE2 . GLU A 104 ? 0.86532 0.96639 1.26958 -0.10987 0.10835  0.26727  97  GLU A OE2 
760  N N   . GLU A 105 ? 0.40477 0.45910 0.83466 -0.13107 0.00877  0.23454  98  GLU A N   
761  C CA  . GLU A 105 ? 0.60069 0.64663 1.03495 -0.13114 -0.01631 0.22189  98  GLU A CA  
762  C C   . GLU A 105 ? 0.57454 0.58286 0.94540 -0.11637 -0.02169 0.18653  98  GLU A C   
763  O O   . GLU A 105 ? 0.70085 0.68807 1.05828 -0.11833 -0.04912 0.17264  98  GLU A O   
764  C CB  . GLU A 105 ? 0.65060 0.74012 1.12895 -0.12105 0.00180  0.23294  98  GLU A CB  
765  C CG  . GLU A 105 ? 0.41559 0.53340 0.94383 -0.13035 -0.01799 0.25406  98  GLU A CG  
766  C CD  . GLU A 105 ? 0.65528 0.79949 1.21532 -0.12023 -0.01608 0.25684  98  GLU A CD  
767  O OE1 . GLU A 105 ? 0.63328 0.79276 1.19189 -0.10149 0.01654  0.25163  98  GLU A OE1 
768  O OE2 . GLU A 105 ? 0.74609 0.89283 1.32952 -0.13041 -0.04813 0.26420  98  GLU A OE2 
769  N N   . PHE A 106 ? 0.54461 0.54482 0.87622 -0.10210 0.00347  0.17314  99  PHE A N   
770  C CA  . PHE A 106 ? 0.53781 0.51139 0.81657 -0.08746 0.00271  0.14307  99  PHE A CA  
771  C C   . PHE A 106 ? 0.46100 0.39477 0.70893 -0.09325 -0.02975 0.12825  99  PHE A C   
772  O O   . PHE A 106 ? 0.49934 0.41110 0.73026 -0.09924 -0.03717 0.12982  99  PHE A O   
773  C CB  . PHE A 106 ? 0.46261 0.43323 0.70767 -0.07585 0.03082  0.13597  99  PHE A CB  
774  C CG  . PHE A 106 ? 0.47300 0.42381 0.67148 -0.06176 0.03209  0.10881  99  PHE A CG  
775  C CD1 . PHE A 106 ? 0.43650 0.38988 0.63345 -0.05411 0.02729  0.09587  99  PHE A CD1 
776  C CD2 . PHE A 106 ? 0.50163 0.43311 0.66015 -0.05709 0.03731  0.09864  99  PHE A CD2 
777  C CE1 . PHE A 106 ? 0.49743 0.43621 0.65579 -0.04292 0.02898  0.07416  99  PHE A CE1 
778  C CE2 . PHE A 106 ? 0.53570 0.45401 0.65805 -0.04568 0.03755  0.07687  99  PHE A CE2 
779  C CZ  . PHE A 106 ? 0.47243 0.39532 0.59571 -0.03901 0.03407  0.06506  99  PHE A CZ  
780  N N   . ASN A 107 ? 0.56345 0.48549 0.80101 -0.09004 -0.04848 0.11393  100 ASN A N   
781  C CA  . ASN A 107 ? 0.62016 0.50128 0.82110 -0.09097 -0.07608 0.09714  100 ASN A CA  
782  C C   . ASN A 107 ? 0.58416 0.45452 0.75360 -0.07728 -0.08050 0.07448  100 ASN A C   
783  O O   . ASN A 107 ? 0.56837 0.40501 0.70217 -0.07356 -0.09893 0.05867  100 ASN A O   
784  C CB  . ASN A 107 ? 0.64991 0.51537 0.87280 -0.11068 -0.10889 0.11043  100 ASN A CB  
785  C CG  . ASN A 107 ? 0.87356 0.69181 1.06103 -0.11421 -0.13155 0.10072  100 ASN A CG  
786  O OD1 . ASN A 107 ? 0.86045 0.67043 1.03604 -0.11271 -0.12147 0.10284  100 ASN A OD1 
787  N ND2 . ASN A 107 ? 0.93852 0.72232 1.10566 -0.11787 -0.16286 0.08985  100 ASN A ND2 
788  N N   . ASP A 108 ? 0.55531 0.45139 0.73508 -0.06879 -0.06366 0.07296  101 ASP A N   
789  C CA  . ASP A 108 ? 0.59031 0.47871 0.74186 -0.05714 -0.06637 0.05463  101 ASP A CA  
790  C C   . ASP A 108 ? 0.54875 0.45615 0.69296 -0.04418 -0.03734 0.04843  101 ASP A C   
791  O O   . ASP A 108 ? 0.45608 0.38736 0.62639 -0.04396 -0.01737 0.06030  101 ASP A O   
792  C CB  . ASP A 108 ? 0.61148 0.50564 0.78278 -0.06315 -0.08461 0.06057  101 ASP A CB  
793  C CG  . ASP A 108 ? 0.67538 0.53528 0.82801 -0.07202 -0.11911 0.05568  101 ASP A CG  
794  O OD1 . ASP A 108 ? 0.68289 0.54326 0.86636 -0.08853 -0.13905 0.07206  101 ASP A OD1 
795  O OD2 . ASP A 108 ? 0.76584 0.59748 0.87236 -0.06229 -0.12645 0.03598  101 ASP A OD2 
796  N N   . VAL A 109 ? 0.49643 0.39204 0.60441 -0.03318 -0.03513 0.03040  102 VAL A N   
797  C CA  . VAL A 109 ? 0.48805 0.39603 0.58453 -0.02317 -0.01232 0.02353  102 VAL A CA  
798  C C   . VAL A 109 ? 0.43475 0.34190 0.51508 -0.01618 -0.01594 0.01302  102 VAL A C   
799  O O   . VAL A 109 ? 0.47288 0.36332 0.52921 -0.01321 -0.03068 0.00316  102 VAL A O   
800  C CB  . VAL A 109 ? 0.48925 0.38757 0.55959 -0.01841 -0.00429 0.01550  102 VAL A CB  
801  C CG1 . VAL A 109 ? 0.53619 0.44510 0.59468 -0.01112 0.01534  0.00943  102 VAL A CG1 
802  C CG2 . VAL A 109 ? 0.45812 0.35464 0.54049 -0.02603 -0.00174 0.02748  102 VAL A CG2 
803  N N   . TYR A 110 ? 0.40661 0.32960 0.49770 -0.01265 -0.00176 0.01554  103 TYR A N   
804  C CA  . TYR A 110 ? 0.45068 0.37428 0.52724 -0.00697 -0.00248 0.00824  103 TYR A CA  
805  C C   . TYR A 110 ? 0.35564 0.28428 0.41902 -0.00129 0.01651  0.00234  103 TYR A C   
806  O O   . TYR A 110 ? 0.34834 0.28191 0.42012 -0.00118 0.03169  0.00617  103 TYR A O   
807  C CB  . TYR A 110 ? 0.31868 0.25251 0.42055 -0.00912 -0.00761 0.01830  103 TYR A CB  
808  C CG  . TYR A 110 ? 0.41685 0.34472 0.53088 -0.01704 -0.03165 0.02497  103 TYR A CG  
809  C CD1 . TYR A 110 ? 0.47444 0.40697 0.61720 -0.02591 -0.03737 0.03714  103 TYR A CD1 
810  C CD2 . TYR A 110 ? 0.40757 0.32406 0.50301 -0.01684 -0.04970 0.02040  103 TYR A CD2 
811  C CE1 . TYR A 110 ? 0.44808 0.37318 0.60319 -0.03614 -0.06325 0.04453  103 TYR A CE1 
812  C CE2 . TYR A 110 ? 0.47139 0.37717 0.57294 -0.02555 -0.07542 0.02589  103 TYR A CE2 
813  C CZ  . TYR A 110 ? 0.43881 0.34856 0.57159 -0.03608 -0.08352 0.03798  103 TYR A CZ  
814  O OH  . TYR A 110 ? 0.49766 0.39484 0.63771 -0.04765 -0.11290 0.04465  103 TYR A OH  
815  N N   . LEU A 111 ? 0.41365 0.33997 0.45475 0.00301  0.01520  -0.00625 104 LEU A N   
816  C CA  . LEU A 111 ? 0.40269 0.33296 0.43184 0.00551  0.02861  -0.01066 104 LEU A CA  
817  C C   . LEU A 111 ? 0.40109 0.33507 0.42771 0.00680  0.02835  -0.00988 104 LEU A C   
818  O O   . LEU A 111 ? 0.36954 0.30220 0.38700 0.00838  0.01773  -0.01113 104 LEU A O   
819  C CB  . LEU A 111 ? 0.43266 0.36096 0.44068 0.00823  0.02790  -0.01860 104 LEU A CB  
820  C CG  . LEU A 111 ? 0.44687 0.36818 0.45383 0.00744  0.02523  -0.01886 104 LEU A CG  
821  C CD1 . LEU A 111 ? 0.48342 0.40435 0.47215 0.01252  0.02335  -0.02559 104 LEU A CD1 
822  C CD2 . LEU A 111 ? 0.44141 0.36323 0.45766 0.00345  0.03715  -0.01331 104 LEU A CD2 
823  N N   . VAL A 112 ? 0.37629 0.31123 0.40722 0.00637  0.03961  -0.00772 105 VAL A N   
824  C CA  . VAL A 112 ? 0.39113 0.32679 0.42091 0.00656  0.03959  -0.00489 105 VAL A CA  
825  C C   . VAL A 112 ? 0.41094 0.34601 0.42408 0.00420  0.04596  -0.00894 105 VAL A C   
826  O O   . VAL A 112 ? 0.39335 0.32341 0.40119 0.00235  0.05329  -0.01233 105 VAL A O   
827  C CB  . VAL A 112 ? 0.37673 0.31023 0.42781 0.00841  0.04517  0.00277  105 VAL A CB  
828  C CG1 . VAL A 112 ? 0.39255 0.32321 0.44085 0.00848  0.04341  0.00666  105 VAL A CG1 
829  C CG2 . VAL A 112 ? 0.35065 0.29051 0.42588 0.00890  0.03724  0.01033  105 VAL A CG2 
830  N N   . THR A 113 ? 0.36467 0.30478 0.36901 0.00322  0.04225  -0.00713 106 THR A N   
831  C CA  . THR A 113 ? 0.40305 0.34659 0.39726 -0.00153 0.04640  -0.00712 106 THR A CA  
832  C C   . THR A 113 ? 0.44136 0.38694 0.43355 -0.00365 0.04420  0.00027  106 THR A C   
833  O O   . THR A 113 ? 0.43040 0.37412 0.42593 -0.00048 0.03868  0.00430  106 THR A O   
834  C CB  . THR A 113 ? 0.45761 0.41409 0.44236 -0.00028 0.04548  -0.01110 106 THR A CB  
835  O OG1 . THR A 113 ? 0.62097 0.58362 0.60288 -0.00729 0.04849  -0.00872 106 THR A OG1 
836  C CG2 . THR A 113 ? 0.29409 0.25992 0.27024 0.00590  0.04108  -0.01039 106 THR A CG2 
837  N N   . HIS A 114 ? 0.42929 0.37851 0.41630 -0.01048 0.04692  0.00372  107 HIS A N   
838  C CA  . HIS A 114 ? 0.39805 0.35090 0.38192 -0.01404 0.04534  0.01317  107 HIS A CA  
839  C C   . HIS A 114 ? 0.42100 0.38851 0.39454 -0.00770 0.04285  0.01474  107 HIS A C   
840  O O   . HIS A 114 ? 0.44047 0.41833 0.40794 -0.00188 0.04381  0.00866  107 HIS A O   
841  C CB  . HIS A 114 ? 0.44859 0.40610 0.43111 -0.02490 0.04754  0.01869  107 HIS A CB  
842  C CG  . HIS A 114 ? 0.55765 0.49371 0.54111 -0.03153 0.04792  0.01504  107 HIS A CG  
843  N ND1 . HIS A 114 ? 0.50543 0.41888 0.48822 -0.03667 0.04665  0.01951  107 HIS A ND1 
844  C CD2 . HIS A 114 ? 0.58166 0.51118 0.56180 -0.03301 0.04893  0.00691  107 HIS A CD2 
845  C CE1 . HIS A 114 ? 0.60513 0.49675 0.58147 -0.04022 0.04742  0.01275  107 HIS A CE1 
846  N NE2 . HIS A 114 ? 0.62645 0.52814 0.60021 -0.03866 0.04870  0.00537  107 HIS A NE2 
847  N N   . LEU A 115 ? 0.40857 0.37354 0.37669 -0.00774 0.03929  0.02283  108 LEU A N   
848  C CA  . LEU A 115 ? 0.42978 0.40401 0.37916 -0.00161 0.03737  0.02481  108 LEU A CA  
849  C C   . LEU A 115 ? 0.34203 0.33442 0.28454 -0.00598 0.04551  0.03464  108 LEU A C   
850  O O   . LEU A 115 ? 0.43550 0.42525 0.38231 -0.01495 0.04572  0.04597  108 LEU A O   
851  C CB  . LEU A 115 ? 0.43702 0.39819 0.38090 0.00030  0.02713  0.02973  108 LEU A CB  
852  C CG  . LEU A 115 ? 0.48918 0.45335 0.40402 0.00643  0.02375  0.03157  108 LEU A CG  
853  C CD1 . LEU A 115 ? 0.48436 0.44780 0.38462 0.01610  0.02216  0.01854  108 LEU A CD1 
854  C CD2 . LEU A 115 ? 0.45425 0.40405 0.36308 0.00573  0.01030  0.03884  108 LEU A CD2 
855  N N   . MET A 116 ? 0.40795 0.41919 0.34194 0.00065  0.05248  0.03180  109 MET A N   
856  C CA  . MET A 116 ? 0.43045 0.46659 0.36283 -0.00215 0.06260  0.04365  109 MET A CA  
857  C C   . MET A 116 ? 0.49587 0.53470 0.40139 0.00545  0.06539  0.04981  109 MET A C   
858  O O   . MET A 116 ? 0.45364 0.47245 0.34040 0.01184  0.05653  0.04383  109 MET A O   
859  C CB  . MET A 116 ? 0.38032 0.43943 0.32081 0.00340  0.07042  0.03979  109 MET A CB  
860  C CG  . MET A 116 ? 0.39061 0.44874 0.35392 -0.00675 0.06694  0.03702  109 MET A CG  
861  S SD  . MET A 116 ? 0.49225 0.54630 0.47140 -0.02828 0.06365  0.05063  109 MET A SD  
862  C CE  . MET A 116 ? 0.39019 0.48626 0.38698 -0.03455 0.07128  0.06528  109 MET A CE  
863  N N   . GLY A 117 ? 0.50757 0.57183 0.41050 0.00409  0.07731  0.06329  110 GLY A N   
864  C CA  . GLY A 117 ? 0.44315 0.51012 0.31652 0.01048  0.08241  0.07178  110 GLY A CA  
865  C C   . GLY A 117 ? 0.65081 0.72343 0.49442 0.03084  0.09095  0.06239  110 GLY A C   
866  O O   . GLY A 117 ? 0.57231 0.62757 0.37914 0.03972  0.08748  0.05947  110 GLY A O   
867  N N   . ALA A 118 ? 0.56804 0.66213 0.42486 0.03911  0.10106  0.05761  111 ALA A N   
868  C CA  . ALA A 118 ? 0.63157 0.73071 0.46031 0.06164  0.11188  0.04894  111 ALA A CA  
869  C C   . ALA A 118 ? 0.46748 0.59028 0.32203 0.06915  0.12010  0.04490  111 ALA A C   
870  O O   . ALA A 118 ? 0.47242 0.60592 0.36360 0.05499  0.11530  0.04864  111 ALA A O   
871  C CB  . ALA A 118 ? 0.63954 0.75787 0.44304 0.06905  0.12896  0.06331  111 ALA A CB  
872  N N   . ASP A 119 ? 0.62520 0.75311 0.45823 0.09227  0.13148  0.03705  112 ASP A N   
873  C CA  . ASP A 119 ? 0.63106 0.78427 0.48810 0.10336  0.14063  0.03536  112 ASP A CA  
874  C C   . ASP A 119 ? 0.67533 0.87971 0.55204 0.10721  0.16314  0.05620  112 ASP A C   
875  O O   . ASP A 119 ? 0.74083 0.95765 0.60352 0.10508  0.17410  0.07005  112 ASP A O   
876  C CB  . ASP A 119 ? 0.56888 0.69650 0.39257 0.12882  0.14055  0.01553  112 ASP A CB  
877  C CG  . ASP A 119 ? 0.66105 0.74628 0.47936 0.12281  0.11769  -0.00197 112 ASP A CG  
878  O OD1 . ASP A 119 ? 0.79849 0.88590 0.65050 0.10476  0.10726  0.00027  112 ASP A OD1 
879  O OD2 . ASP A 119 ? 0.76444 0.81315 0.54346 0.13603  0.11006  -0.01738 112 ASP A OD2 
880  N N   . LEU A 120 ? 0.55451 0.79081 0.46590 0.11279  0.16981  0.06044  113 LEU A N   
881  C CA  . LEU A 120 ? 0.66432 0.95591 0.60208 0.11769  0.19160  0.08260  113 LEU A CA  
882  C C   . LEU A 120 ? 0.75677 1.04953 0.66157 0.14615  0.20993  0.07860  113 LEU A C   
883  O O   . LEU A 120 ? 0.84152 1.16814 0.76313 0.14698  0.22395  0.09588  113 LEU A O   
884  C CB  . LEU A 120 ? 0.48222 0.80786 0.47106 0.11395  0.18937  0.08984  113 LEU A CB  
885  C CG  . LEU A 120 ? 0.58986 0.97137 0.62543 0.09709  0.19860  0.11973  113 LEU A CG  
886  C CD1 . LEU A 120 ? 0.59267 0.96184 0.62499 0.06894  0.19009  0.13065  113 LEU A CD1 
887  C CD2 . LEU A 120 ? 0.49978 0.90698 0.58576 0.08554  0.18716  0.12681  113 LEU A CD2 
888  N N   . ASN A 121 ? 0.74070 0.98930 0.59998 0.16616  0.20505  0.05503  114 ASN A N   
889  C CA  . ASN A 121 ? 0.91449 1.14862 0.73471 0.18840  0.21615  0.04853  114 ASN A CA  
890  C C   . ASN A 121 ? 1.00471 1.23434 0.79545 0.18008  0.22154  0.05825  114 ASN A C   
891  O O   . ASN A 121 ? 1.06583 1.31095 0.84599 0.19059  0.23789  0.06678  114 ASN A O   
892  C CB  . ASN A 121 ? 0.92014 1.09997 0.69547 0.20697  0.20434  0.02119  114 ASN A CB  
893  C CG  . ASN A 121 ? 0.82799 1.00052 0.62754 0.20775  0.19203  0.01055  114 ASN A CG  
894  O OD1 . ASN A 121 ? 0.72570 0.88747 0.53369 0.19178  0.17844  0.00725  114 ASN A OD1 
895  N ND2 . ASN A 121 ? 0.68976 0.86731 0.49938 0.22726  0.19714  0.00579  114 ASN A ND2 
896  N N   . ASN A 122 ? 0.93576 1.14423 0.71239 0.16190  0.20820  0.05817  115 ASN A N   
897  C CA  . ASN A 122 ? 1.05068 1.25270 0.79903 0.15247  0.21059  0.06923  115 ASN A CA  
898  C C   . ASN A 122 ? 1.13751 1.38862 0.92693 0.13629  0.22400  0.09769  115 ASN A C   
899  O O   . ASN A 122 ? 1.18279 1.43923 0.95187 0.13663  0.23440  0.10890  115 ASN A O   
900  C CB  . ASN A 122 ? 1.01373 1.18112 0.74125 0.13733  0.19076  0.06421  115 ASN A CB  
901  C CG  . ASN A 122 ? 1.07706 1.19842 0.78760 0.14418  0.16965  0.03734  115 ASN A CG  
902  O OD1 . ASN A 122 ? 1.07847 1.18718 0.76516 0.16796  0.17526  0.02201  115 ASN A OD1 
903  N ND2 . ASN A 122 ? 0.88221 0.97778 0.60688 0.12343  0.14525  0.03259  115 ASN A ND2 
904  N N   . ILE A 123 ? 1.06355 1.34863 0.90950 0.12075  0.22223  0.11004  116 ILE A N   
905  C CA  . ILE A 123 ? 1.00347 1.33322 0.89179 0.10350  0.23120  0.13742  116 ILE A CA  
906  C C   . ILE A 123 ? 1.11585 1.47956 1.01876 0.12208  0.25016  0.14403  116 ILE A C   
907  O O   . ILE A 123 ? 1.18261 1.57580 1.09905 0.11591  0.26235  0.16487  116 ILE A O   
908  C CB  . ILE A 123 ? 0.89730 1.24720 0.83871 0.07816  0.21895  0.14853  116 ILE A CB  
909  C CG1 . ILE A 123 ? 0.87089 1.19559 0.80256 0.05443  0.20472  0.15353  116 ILE A CG1 
910  C CG2 . ILE A 123 ? 0.81879 1.21783 0.81069 0.06608  0.22634  0.17333  116 ILE A CG2 
911  C CD1 . ILE A 123 ? 0.84360 1.11181 0.73229 0.06208  0.18848  0.12739  116 ILE A CD1 
912  N N   . VAL A 124 ? 1.09294 1.45186 0.99244 0.14571  0.25310  0.12749  117 VAL A N   
913  C CA  . VAL A 124 ? 1.14774 1.53353 1.05405 0.16800  0.27223  0.13256  117 VAL A CA  
914  C C   . VAL A 124 ? 1.27050 1.63116 1.11836 0.18691  0.28487  0.12486  117 VAL A C   
915  O O   . VAL A 124 ? 1.34923 1.73538 1.19883 0.20229  0.30475  0.13469  117 VAL A O   
916  C CB  . VAL A 124 ? 1.07721 1.46228 0.99780 0.18766  0.27005  0.11826  117 VAL A CB  
917  C CG1 . VAL A 124 ? 0.99188 1.40258 0.91719 0.21342  0.29077  0.12395  117 VAL A CG1 
918  C CG2 . VAL A 124 ? 0.96575 1.37825 0.94378 0.16826  0.25740  0.12770  117 VAL A CG2 
919  N N   . LYS A 125 ? 1.23436 1.54542 1.02955 0.18600  0.27321  0.10825  118 LYS A N   
920  C CA  . LYS A 125 ? 1.33364 1.61642 1.06838 0.20145  0.28173  0.10077  118 LYS A CA  
921  C C   . LYS A 125 ? 1.50600 1.81940 1.24518 0.19088  0.29727  0.12577  118 LYS A C   
922  O O   . LYS A 125 ? 1.63185 1.94748 1.34124 0.20834  0.31510  0.12760  118 LYS A O   
923  C CB  . LYS A 125 ? 1.34848 1.57340 1.03027 0.19763  0.26116  0.08116  118 LYS A CB  
924  C CG  . LYS A 125 ? 1.36893 1.56329 0.98685 0.20560  0.26487  0.07718  118 LYS A CG  
925  C CD  . LYS A 125 ? 1.40227 1.60337 1.01705 0.18137  0.26187  0.09670  118 LYS A CD  
926  C CE  . LYS A 125 ? 1.37865 1.55634 0.99825 0.16118  0.23732  0.09302  118 LYS A CE  
927  N NZ  . LYS A 125 ? 1.21834 1.39965 0.83529 0.13825  0.23305  0.11371  118 LYS A NZ  
928  N N   . CYS A 126 ? 1.44921 1.78407 1.22374 0.16214  0.29052  0.14556  119 CYS A N   
929  C CA  . CYS A 126 ? 1.47139 1.83659 1.25651 0.14941  0.30376  0.17191  119 CYS A CA  
930  C C   . CYS A 126 ? 1.54972 1.96681 1.37445 0.16089  0.32556  0.18806  119 CYS A C   
931  O O   . CYS A 126 ? 1.47853 1.91399 1.29092 0.16674  0.34453  0.20238  119 CYS A O   
932  C CB  . CYS A 126 ? 1.34823 1.72249 1.16817 0.11534  0.28896  0.18978  119 CYS A CB  
933  S SG  . CYS A 126 ? 1.32013 1.63864 1.09409 0.10111  0.26604  0.17881  119 CYS A SG  
934  N N   . GLN A 127 ? 1.53026 1.97221 1.40257 0.16451  0.32303  0.18719  120 GLN A N   
935  C CA  . GLN A 127 ? 1.54872 2.03782 1.45964 0.17991  0.34116  0.19989  120 GLN A CA  
936  C C   . GLN A 127 ? 1.50190 2.04497 1.46729 0.15848  0.34790  0.23366  120 GLN A C   
937  O O   . GLN A 127 ? 1.41906 2.00634 1.41791 0.17056  0.36443  0.24870  120 GLN A O   
938  C CB  . GLN A 127 ? 1.66591 2.14533 1.53061 0.21330  0.36336  0.19066  120 GLN A CB  
939  C CG  . GLN A 127 ? 1.66200 2.08763 1.47507 0.23692  0.35584  0.15751  120 GLN A CG  
940  C CD  . GLN A 127 ? 1.74668 2.13606 1.48756 0.25679  0.36733  0.14523  120 GLN A CD  
941  O OE1 . GLN A 127 ? 1.72442 2.12091 1.44634 0.24855  0.37728  0.15941  120 GLN A OE1 
942  N NE2 . GLN A 127 ? 1.74690 2.09454 1.44522 0.28226  0.36465  0.11906  120 GLN A NE2 
943  N N   . LYS A 128 ? 1.35608 1.89631 1.33251 0.12699  0.33473  0.24716  121 LYS A N   
944  C CA  . LYS A 128 ? 1.20343 1.78927 1.23075 0.10332  0.33710  0.27967  121 LYS A CA  
945  C C   . LYS A 128 ? 1.08176 1.65975 1.14227 0.06921  0.31030  0.28509  121 LYS A C   
946  O O   . LYS A 128 ? 1.10114 1.65712 1.14732 0.04733  0.30012  0.29130  121 LYS A O   
947  C CB  . LYS A 128 ? 1.23478 1.82290 1.23297 0.10043  0.35251  0.29530  121 LYS A CB  
948  C CG  . LYS A 128 ? 1.16998 1.80047 1.21876 0.07329  0.35257  0.32975  121 LYS A CG  
949  C CD  . LYS A 128 ? 1.12948 1.77420 1.15356 0.07878  0.37560  0.34726  121 LYS A CD  
950  C CE  . LYS A 128 ? 1.19564 1.87995 1.22769 0.10904  0.40383  0.35282  121 LYS A CE  
951  N NZ  . LYS A 128 ? 1.01531 1.73601 1.05433 0.10546  0.42535  0.38222  121 LYS A NZ  
952  N N   . LEU A 129 ? 0.89859 1.49257 1.00211 0.06503  0.29829  0.28297  122 LEU A N   
953  C CA  . LEU A 129 ? 0.73714 1.32565 0.87454 0.03298  0.27288  0.28877  122 LEU A CA  
954  C C   . LEU A 129 ? 0.71140 1.34587 0.90620 0.01054  0.26956  0.32006  122 LEU A C   
955  O O   . LEU A 129 ? 0.60649 1.28489 0.83452 0.02257  0.28128  0.33253  122 LEU A O   
956  C CB  . LEU A 129 ? 0.54404 1.12124 0.69295 0.03869  0.25939  0.26928  122 LEU A CB  
957  C CG  . LEU A 129 ? 0.69026 1.21524 0.80129 0.03608  0.24523  0.24493  122 LEU A CG  
958  C CD1 . LEU A 129 ? 0.82425 1.31562 0.87247 0.05878  0.25779  0.22789  122 LEU A CD1 
959  C CD2 . LEU A 129 ? 0.67776 1.19797 0.80396 0.04294  0.23440  0.22830  122 LEU A CD2 
960  N N   . THR A 130 ? 0.67057 1.29308 0.87646 -0.02174 0.25262  0.33332  123 THR A N   
961  C CA  . THR A 130 ? 0.59907 1.25812 0.85837 -0.04700 0.24365  0.36235  123 THR A CA  
962  C C   . THR A 130 ? 0.54977 1.22560 0.85384 -0.05547 0.22569  0.36210  123 THR A C   
963  O O   . THR A 130 ? 0.51780 1.16570 0.81072 -0.05297 0.21335  0.34020  123 THR A O   
964  C CB  . THR A 130 ? 0.58632 1.21808 0.84165 -0.07966 0.22624  0.37370  123 THR A CB  
965  O OG1 . THR A 130 ? 0.65626 1.23611 0.88434 -0.08762 0.20824  0.35160  123 THR A OG1 
966  C CG2 . THR A 130 ? 0.62733 1.25685 0.85076 -0.07485 0.24457  0.38442  123 THR A CG2 
967  N N   . ASP A 131 ? 0.68313 0.66751 0.63771 -0.08695 0.13617  0.19575  124 ASP A N   
968  C CA  . ASP A 131 ? 0.62571 0.63530 0.62778 -0.09290 0.12706  0.18465  124 ASP A CA  
969  C C   . ASP A 131 ? 0.61802 0.61634 0.62899 -0.09737 0.10403  0.17698  124 ASP A C   
970  O O   . ASP A 131 ? 0.49374 0.50759 0.52392 -0.09666 0.08961  0.16385  124 ASP A O   
971  C CB  . ASP A 131 ? 0.51236 0.54153 0.55732 -0.10592 0.14445  0.19267  124 ASP A CB  
972  C CG  . ASP A 131 ? 0.52911 0.58530 0.62366 -0.11329 0.13116  0.18185  124 ASP A CG  
973  O OD1 . ASP A 131 ? 0.45189 0.52922 0.55578 -0.10479 0.12494  0.17210  124 ASP A OD1 
974  O OD2 . ASP A 131 ? 0.54328 0.59877 0.66699 -0.12765 0.12629  0.18316  124 ASP A OD2 
975  N N   . ASP A 132 ? 0.58925 0.55978 0.58587 -0.10144 0.10118  0.18541  125 ASP A N   
976  C CA  . ASP A 132 ? 0.55099 0.50763 0.55398 -0.10400 0.08141  0.17655  125 ASP A CA  
977  C C   . ASP A 132 ? 0.57833 0.52915 0.55466 -0.09018 0.06579  0.16544  125 ASP A C   
978  O O   . ASP A 132 ? 0.49375 0.44448 0.48060 -0.09065 0.05053  0.15273  125 ASP A O   
979  C CB  . ASP A 132 ? 0.72493 0.65143 0.72310 -0.11048 0.08401  0.18962  125 ASP A CB  
980  C CG  . ASP A 132 ? 0.84891 0.75752 0.85202 -0.11092 0.06561  0.17958  125 ASP A CG  
981  O OD1 . ASP A 132 ? 0.81814 0.70628 0.79373 -0.10031 0.05725  0.18181  125 ASP A OD1 
982  O OD2 . ASP A 132 ? 0.84483 0.76058 0.88008 -0.12183 0.05940  0.16855  125 ASP A OD2 
983  N N   . HIS A 133 ? 0.58810 0.53395 0.53003 -0.07851 0.06998  0.16914  126 HIS A N   
984  C CA  . HIS A 133 ? 0.63311 0.57683 0.55547 -0.06638 0.05597  0.15734  126 HIS A CA  
985  C C   . HIS A 133 ? 0.56998 0.53866 0.51173 -0.06414 0.05265  0.14375  126 HIS A C   
986  O O   . HIS A 133 ? 0.52028 0.48896 0.46227 -0.05932 0.03907  0.13230  126 HIS A O   
987  C CB  . HIS A 133 ? 0.70188 0.63560 0.58355 -0.05585 0.06048  0.16275  126 HIS A CB  
988  C CG  . HIS A 133 ? 0.78406 0.69077 0.63989 -0.05295 0.05337  0.17354  126 HIS A CG  
989  N ND1 . HIS A 133 ? 0.72559 0.61633 0.59729 -0.05852 0.04544  0.17804  126 HIS A ND1 
990  C CD2 . HIS A 133 ? 0.93063 0.82332 0.74613 -0.04448 0.05195  0.18088  126 HIS A CD2 
991  C CE1 . HIS A 133 ? 0.82616 0.69426 0.67145 -0.05266 0.03959  0.18957  126 HIS A CE1 
992  N NE2 . HIS A 133 ? 0.81895 0.68863 0.62827 -0.04424 0.04221  0.19191  126 HIS A NE2 
993  N N   . VAL A 134 ? 0.49639 0.48656 0.45627 -0.06716 0.06573  0.14605  127 VAL A N   
994  C CA  . VAL A 134 ? 0.47562 0.48966 0.45596 -0.06372 0.06226  0.13613  127 VAL A CA  
995  C C   . VAL A 134 ? 0.38762 0.41113 0.39621 -0.07237 0.04903  0.12986  127 VAL A C   
996  O O   . VAL A 134 ? 0.47785 0.50866 0.48942 -0.06797 0.03753  0.12037  127 VAL A O   
997  C CB  . VAL A 134 ? 0.43321 0.46830 0.42896 -0.06304 0.08048  0.14097  127 VAL A CB  
998  C CG1 . VAL A 134 ? 0.43942 0.49798 0.45799 -0.05733 0.07589  0.13277  127 VAL A CG1 
999  C CG2 . VAL A 134 ? 0.52687 0.55009 0.48792 -0.05503 0.09499  0.14517  127 VAL A CG2 
1000 N N   . GLN A 135 ? 0.48095 0.50359 0.50939 -0.08532 0.05085  0.13474  128 GLN A N   
1001 C CA  . GLN A 135 ? 0.44144 0.47040 0.49258 -0.09491 0.03709  0.12613  128 GLN A CA  
1002 C C   . GLN A 135 ? 0.37487 0.38574 0.40643 -0.09028 0.02286  0.11598  128 GLN A C   
1003 O O   . GLN A 135 ? 0.45974 0.48073 0.49603 -0.08961 0.01159  0.10574  128 GLN A O   
1004 C CB  . GLN A 135 ? 0.40065 0.42397 0.47364 -0.11029 0.04172  0.13160  128 GLN A CB  
1005 C CG  . GLN A 135 ? 0.49163 0.53260 0.58872 -0.11654 0.05875  0.14264  128 GLN A CG  
1006 C CD  . GLN A 135 ? 0.43936 0.47212 0.56081 -0.13309 0.06433  0.14848  128 GLN A CD  
1007 O OE1 . GLN A 135 ? 0.53934 0.54734 0.65411 -0.13825 0.05736  0.14598  128 GLN A OE1 
1008 N NE2 . GLN A 135 ? 0.39578 0.44899 0.54945 -0.14157 0.07808  0.15607  128 GLN A NE2 
1009 N N   . PHE A 136 ? 0.42356 0.40803 0.43320 -0.08651 0.02368  0.11964  129 PHE A N   
1010 C CA  . PHE A 136 ? 0.42225 0.38953 0.42004 -0.08249 0.01186  0.11023  129 PHE A CA  
1011 C C   . PHE A 136 ? 0.38809 0.36138 0.37086 -0.07022 0.00683  0.10316  129 PHE A C   
1012 O O   . PHE A 136 ? 0.32937 0.30245 0.31284 -0.06898 -0.00199 0.09239  129 PHE A O   
1013 C CB  . PHE A 136 ? 0.43401 0.37303 0.41789 -0.08075 0.01322  0.11822  129 PHE A CB  
1014 C CG  . PHE A 136 ? 0.41966 0.34103 0.39915 -0.07669 0.00244  0.10890  129 PHE A CG  
1015 C CD1 . PHE A 136 ? 0.42264 0.34512 0.41729 -0.08346 -0.00400 0.09537  129 PHE A CD1 
1016 C CD2 . PHE A 136 ? 0.52160 0.42607 0.48233 -0.06603 -0.00120 0.11304  129 PHE A CD2 
1017 C CE1 . PHE A 136 ? 0.48184 0.38815 0.47417 -0.07929 -0.01067 0.08582  129 PHE A CE1 
1018 C CE2 . PHE A 136 ? 0.52116 0.41154 0.48432 -0.06162 -0.01000 0.10451  129 PHE A CE2 
1019 C CZ  . PHE A 136 ? 0.46055 0.35142 0.44017 -0.06809 -0.01311 0.09076  129 PHE A CZ  
1020 N N   . LEU A 137 ? 0.40623 0.38391 0.37532 -0.06161 0.01368  0.10839  130 LEU A N   
1021 C CA  . LEU A 137 ? 0.38202 0.36321 0.33985 -0.05079 0.00974  0.10116  130 LEU A CA  
1022 C C   . LEU A 137 ? 0.41453 0.41686 0.38851 -0.05103 0.00737  0.09561  130 LEU A C   
1023 O O   . LEU A 137 ? 0.37430 0.37610 0.34603 -0.04726 0.00026  0.08778  130 LEU A O   
1024 C CB  . LEU A 137 ? 0.39848 0.37803 0.33750 -0.04259 0.01799  0.10584  130 LEU A CB  
1025 C CG  . LEU A 137 ? 0.37993 0.33794 0.29386 -0.03847 0.01570  0.11043  130 LEU A CG  
1026 C CD1 . LEU A 137 ? 0.46763 0.42618 0.35908 -0.03236 0.02534  0.11439  130 LEU A CD1 
1027 C CD2 . LEU A 137 ? 0.35278 0.30013 0.26175 -0.03243 0.00249  0.10142  130 LEU A CD2 
1028 N N   . ILE A 138 ? 0.40171 0.42337 0.39334 -0.05511 0.01357  0.10081  131 ILE A N   
1029 C CA  . ILE A 138 ? 0.39733 0.44048 0.40552 -0.05408 0.00929  0.09818  131 ILE A CA  
1030 C C   . ILE A 138 ? 0.34316 0.38862 0.35830 -0.06253 -0.00291 0.09182  131 ILE A C   
1031 O O   . ILE A 138 ? 0.33115 0.38643 0.34723 -0.05983 -0.01012 0.08809  131 ILE A O   
1032 C CB  . ILE A 138 ? 0.42252 0.48820 0.45350 -0.05543 0.01841  0.10569  131 ILE A CB  
1033 C CG1 . ILE A 138 ? 0.41553 0.47743 0.43541 -0.04646 0.03295  0.10945  131 ILE A CG1 
1034 C CG2 . ILE A 138 ? 0.26761 0.35653 0.31823 -0.05320 0.01111  0.10510  131 ILE A CG2 
1035 C CD1 . ILE A 138 ? 0.38995 0.44666 0.39621 -0.03429 0.03190  0.10361  131 ILE A CD1 
1036 N N   . TYR A 139 ? 0.40638 0.44149 0.42498 -0.07291 -0.00486 0.09038  132 TYR A N   
1037 C CA  . TYR A 139 ? 0.40387 0.43840 0.42608 -0.08150 -0.01581 0.08083  132 TYR A CA  
1038 C C   . TYR A 139 ? 0.31961 0.34000 0.32202 -0.07508 -0.02059 0.07201  132 TYR A C   
1039 O O   . TYR A 139 ? 0.29071 0.31773 0.28978 -0.07708 -0.02811 0.06470  132 TYR A O   
1040 C CB  . TYR A 139 ? 0.34321 0.36463 0.37482 -0.09370 -0.01518 0.07958  132 TYR A CB  
1041 C CG  . TYR A 139 ? 0.38171 0.39593 0.41244 -0.10200 -0.02520 0.06582  132 TYR A CG  
1042 C CD1 . TYR A 139 ? 0.31838 0.35191 0.36217 -0.11176 -0.03466 0.05932  132 TYR A CD1 
1043 C CD2 . TYR A 139 ? 0.40105 0.38992 0.41806 -0.09969 -0.02552 0.05833  132 TYR A CD2 
1044 C CE1 . TYR A 139 ? 0.34285 0.36887 0.38076 -0.11980 -0.04351 0.04427  132 TYR A CE1 
1045 C CE2 . TYR A 139 ? 0.37707 0.35813 0.39225 -0.10692 -0.03204 0.04356  132 TYR A CE2 
1046 C CZ  . TYR A 139 ? 0.42276 0.42159 0.44569 -0.11733 -0.04070 0.03584  132 TYR A CZ  
1047 O OH  . TYR A 139 ? 0.51931 0.50939 0.53556 -0.12505 -0.04691 0.01879  132 TYR A OH  
1048 N N   . GLN A 140 ? 0.32998 0.33165 0.31917 -0.06750 -0.01632 0.07277  133 GLN A N   
1049 C CA  . GLN A 140 ? 0.35517 0.34519 0.33193 -0.06138 -0.01930 0.06447  133 GLN A CA  
1050 C C   . GLN A 140 ? 0.38435 0.38705 0.35693 -0.05351 -0.01920 0.06472  133 GLN A C   
1051 O O   . GLN A 140 ? 0.31352 0.31563 0.27998 -0.05272 -0.02198 0.05814  133 GLN A O   
1052 C CB  . GLN A 140 ? 0.36224 0.33223 0.33109 -0.05507 -0.01708 0.06593  133 GLN A CB  
1053 C CG  . GLN A 140 ? 0.33950 0.29175 0.31265 -0.06137 -0.01773 0.06629  133 GLN A CG  
1054 C CD  . GLN A 140 ? 0.38075 0.31537 0.34581 -0.05377 -0.01757 0.07187  133 GLN A CD  
1055 O OE1 . GLN A 140 ? 0.48193 0.40430 0.44668 -0.04866 -0.02133 0.06584  133 GLN A OE1 
1056 N NE2 . GLN A 140 ? 0.40248 0.33665 0.36096 -0.05272 -0.01321 0.08372  133 GLN A NE2 
1057 N N   . ILE A 141 ? 0.28813 0.30084 0.26388 -0.04752 -0.01437 0.07239  134 ILE A N   
1058 C CA  . ILE A 141 ? 0.39213 0.41568 0.36845 -0.04001 -0.01345 0.07394  134 ILE A CA  
1059 C C   . ILE A 141 ? 0.31994 0.35905 0.30095 -0.04454 -0.02012 0.07429  134 ILE A C   
1060 O O   . ILE A 141 ? 0.32591 0.36434 0.29858 -0.04167 -0.02229 0.07195  134 ILE A O   
1061 C CB  . ILE A 141 ? 0.32764 0.35978 0.31055 -0.03363 -0.00591 0.08096  134 ILE A CB  
1062 C CG1 . ILE A 141 ? 0.29516 0.31122 0.26578 -0.02833 -0.00105 0.07903  134 ILE A CG1 
1063 C CG2 . ILE A 141 ? 0.26428 0.30760 0.25370 -0.02612 -0.00483 0.08379  134 ILE A CG2 
1064 C CD1 . ILE A 141 ? 0.39341 0.41546 0.36543 -0.02295 0.00839  0.08340  134 ILE A CD1 
1065 N N   . LEU A 142 ? 0.28535 0.33925 0.27967 -0.05209 -0.02370 0.07767  135 LEU A N   
1066 C CA  . LEU A 142 ? 0.29216 0.36349 0.29066 -0.05704 -0.03372 0.07774  135 LEU A CA  
1067 C C   . LEU A 142 ? 0.31534 0.37533 0.29592 -0.06311 -0.03981 0.06674  135 LEU A C   
1068 O O   . LEU A 142 ? 0.28717 0.35431 0.25668 -0.06240 -0.04589 0.06611  135 LEU A O   
1069 C CB  . LEU A 142 ? 0.31539 0.40499 0.33651 -0.06595 -0.03751 0.08120  135 LEU A CB  
1070 C CG  . LEU A 142 ? 0.38643 0.49115 0.42919 -0.06042 -0.02929 0.09176  135 LEU A CG  
1071 C CD1 . LEU A 142 ? 0.29785 0.42085 0.36765 -0.07121 -0.03165 0.09429  135 LEU A CD1 
1072 C CD2 . LEU A 142 ? 0.25690 0.37603 0.30501 -0.04927 -0.03059 0.09904  135 LEU A CD2 
1073 N N   . ARG A 143 ? 0.37737 0.41869 0.35409 -0.06860 -0.03740 0.05843  136 ARG A N   
1074 C CA  . ARG A 143 ? 0.37658 0.40524 0.33867 -0.07411 -0.04052 0.04564  136 ARG A CA  
1075 C C   . ARG A 143 ? 0.37255 0.39336 0.31795 -0.06555 -0.03592 0.04350  136 ARG A C   
1076 O O   . ARG A 143 ? 0.31147 0.33379 0.24103 -0.06793 -0.03874 0.03766  136 ARG A O   
1077 C CB  . ARG A 143 ? 0.38681 0.39469 0.35352 -0.07921 -0.03703 0.03884  136 ARG A CB  
1078 C CG  . ARG A 143 ? 0.36074 0.35473 0.31779 -0.08618 -0.03894 0.02325  136 ARG A CG  
1079 C CD  . ARG A 143 ? 0.49364 0.46699 0.46193 -0.09109 -0.03582 0.01883  136 ARG A CD  
1080 N NE  . ARG A 143 ? 0.58920 0.54626 0.55119 -0.09653 -0.03539 0.00203  136 ARG A NE  
1081 C CZ  . ARG A 143 ? 0.65332 0.58954 0.61514 -0.09081 -0.02872 -0.00398 136 ARG A CZ  
1082 N NH1 . ARG A 143 ? 0.57480 0.50476 0.54134 -0.07997 -0.02453 0.00555  136 ARG A NH1 
1083 N NH2 . ARG A 143 ? 0.60807 0.53000 0.56610 -0.09596 -0.02658 -0.02094 136 ARG A NH2 
1084 N N   . GLY A 144 ? 0.34849 0.36073 0.29669 -0.05616 -0.02839 0.04778  137 GLY A N   
1085 C CA  . GLY A 144 ? 0.34243 0.34909 0.28141 -0.04868 -0.02294 0.04680  137 GLY A CA  
1086 C C   . GLY A 144 ? 0.37982 0.40156 0.31469 -0.04449 -0.02431 0.05606  137 GLY A C   
1087 O O   . GLY A 144 ? 0.36765 0.38655 0.28989 -0.04211 -0.02095 0.05544  137 GLY A O   
1088 N N   . LEU A 145 ? 0.33258 0.37024 0.27946 -0.04311 -0.02816 0.06582  138 LEU A N   
1089 C CA  . LEU A 145 ? 0.32222 0.37452 0.26980 -0.03754 -0.03048 0.07681  138 LEU A CA  
1090 C C   . LEU A 145 ? 0.36395 0.42672 0.29637 -0.04361 -0.04055 0.07649  138 LEU A C   
1091 O O   . LEU A 145 ? 0.38818 0.45516 0.30924 -0.03883 -0.04139 0.08429  138 LEU A O   
1092 C CB  . LEU A 145 ? 0.29632 0.36387 0.26570 -0.03379 -0.03106 0.08635  138 LEU A CB  
1093 C CG  . LEU A 145 ? 0.39956 0.47100 0.37815 -0.02222 -0.02552 0.09684  138 LEU A CG  
1094 C CD1 . LEU A 145 ? 0.45452 0.50637 0.42455 -0.01671 -0.01614 0.09288  138 LEU A CD1 
1095 C CD2 . LEU A 145 ? 0.38619 0.46652 0.38671 -0.01808 -0.02078 0.10136  138 LEU A CD2 
1096 N N   . LYS A 146 ? 0.34163 0.40798 0.27260 -0.05444 -0.04861 0.06773  139 LYS A N   
1097 C CA  . LYS A 146 ? 0.33261 0.40767 0.24454 -0.06151 -0.05970 0.06370  139 LYS A CA  
1098 C C   . LYS A 146 ? 0.36723 0.42565 0.25026 -0.06091 -0.05254 0.05605  139 LYS A C   
1099 O O   . LYS A 146 ? 0.40300 0.46740 0.26318 -0.06028 -0.05686 0.06008  139 LYS A O   
1100 C CB  . LYS A 146 ? 0.35520 0.43448 0.27393 -0.07478 -0.06896 0.05228  139 LYS A CB  
1101 C CG  . LYS A 146 ? 0.37053 0.45447 0.26436 -0.08392 -0.08058 0.04213  139 LYS A CG  
1102 C CD  . LYS A 146 ? 0.43515 0.51661 0.33698 -0.09838 -0.08734 0.02629  139 LYS A CD  
1103 C CE  . LYS A 146 ? 0.47669 0.55678 0.34758 -0.10771 -0.09657 0.01094  139 LYS A CE  
1104 N NZ  . LYS A 146 ? 0.47450 0.55850 0.35778 -0.12334 -0.10791 -0.00398 139 LYS A NZ  
1105 N N   . TYR A 147 ? 0.41475 0.45273 0.29879 -0.06075 -0.04118 0.04580  140 TYR A N   
1106 C CA  . TYR A 147 ? 0.35592 0.37873 0.21921 -0.05936 -0.03080 0.03826  140 TYR A CA  
1107 C C   . TYR A 147 ? 0.39199 0.41585 0.25040 -0.04961 -0.02317 0.05172  140 TYR A C   
1108 O O   . TYR A 147 ? 0.38627 0.40885 0.21979 -0.04944 -0.01970 0.05345  140 TYR A O   
1109 C CB  . TYR A 147 ? 0.41235 0.41575 0.28762 -0.05926 -0.02104 0.02659  140 TYR A CB  
1110 C CG  . TYR A 147 ? 0.43616 0.42517 0.29985 -0.05655 -0.00748 0.01878  140 TYR A CG  
1111 C CD1 . TYR A 147 ? 0.47080 0.45061 0.31642 -0.06319 -0.00380 0.00315  140 TYR A CD1 
1112 C CD2 . TYR A 147 ? 0.45296 0.43753 0.32635 -0.04787 0.00290  0.02565  140 TYR A CD2 
1113 C CE1 . TYR A 147 ? 0.50822 0.47584 0.34606 -0.06045 0.01162  -0.00437 140 TYR A CE1 
1114 C CE2 . TYR A 147 ? 0.48468 0.45803 0.35324 -0.04601 0.01694  0.01877  140 TYR A CE2 
1115 C CZ  . TYR A 147 ? 0.51590 0.48132 0.36691 -0.05193 0.02215  0.00428  140 TYR A CZ  
1116 O OH  . TYR A 147 ? 0.47856 0.43376 0.32735 -0.04980 0.03903  -0.00290 140 TYR A OH  
1117 N N   . ILE A 148 ? 0.33091 0.35575 0.21185 -0.04173 -0.01958 0.06127  141 ILE A N   
1118 C CA  . ILE A 148 ? 0.41434 0.43770 0.29630 -0.03286 -0.01151 0.07348  141 ILE A CA  
1119 C C   . ILE A 148 ? 0.45803 0.49582 0.32600 -0.03096 -0.01952 0.08792  141 ILE A C   
1120 O O   . ILE A 148 ? 0.42995 0.46347 0.28006 -0.02792 -0.01329 0.09557  141 ILE A O   
1121 C CB  . ILE A 148 ? 0.44015 0.46191 0.34919 -0.02569 -0.00774 0.07817  141 ILE A CB  
1122 C CG1 . ILE A 148 ? 0.44464 0.45130 0.36375 -0.02609 -0.00079 0.06579  141 ILE A CG1 
1123 C CG2 . ILE A 148 ? 0.40126 0.42255 0.31556 -0.01707 -0.00109 0.09155  141 ILE A CG2 
1124 C CD1 . ILE A 148 ? 0.44959 0.45505 0.38901 -0.02087 -0.00020 0.06732  141 ILE A CD1 
1125 N N   . HIS A 149 ? 0.48201 0.53772 0.35940 -0.03253 -0.03343 0.09313  142 HIS A N   
1126 C CA  . HIS A 149 ? 0.38853 0.46109 0.25762 -0.02943 -0.04442 0.10848  142 HIS A CA  
1127 C C   . HIS A 149 ? 0.43592 0.50998 0.26732 -0.03634 -0.05136 0.10446  142 HIS A C   
1128 O O   . HIS A 149 ? 0.47104 0.55252 0.28411 -0.03221 -0.05692 0.11897  142 HIS A O   
1129 C CB  . HIS A 149 ? 0.37531 0.46949 0.26994 -0.02995 -0.05781 0.11342  142 HIS A CB  
1130 C CG  . HIS A 149 ? 0.53043 0.62569 0.45722 -0.02064 -0.05019 0.12147  142 HIS A CG  
1131 N ND1 . HIS A 149 ? 0.40233 0.51438 0.35732 -0.02048 -0.05584 0.12408  142 HIS A ND1 
1132 C CD2 . HIS A 149 ? 0.32581 0.40704 0.26124 -0.01174 -0.03632 0.12589  142 HIS A CD2 
1133 C CE1 . HIS A 149 ? 0.39122 0.49869 0.36730 -0.01123 -0.04492 0.12923  142 HIS A CE1 
1134 N NE2 . HIS A 149 ? 0.36728 0.45581 0.33201 -0.00609 -0.03408 0.12976  142 HIS A NE2 
1135 N N   . SER A 150 ? 0.47566 0.54165 0.29364 -0.04647 -0.05096 0.08505  143 SER A N   
1136 C CA  . SER A 150 ? 0.54725 0.61152 0.32527 -0.05348 -0.05486 0.07723  143 SER A CA  
1137 C C   . SER A 150 ? 0.54219 0.59059 0.29463 -0.04866 -0.03759 0.08158  143 SER A C   
1138 O O   . SER A 150 ? 0.65493 0.70391 0.36818 -0.05146 -0.03973 0.08253  143 SER A O   
1139 C CB  . SER A 150 ? 0.49244 0.54869 0.26671 -0.06520 -0.05603 0.05318  143 SER A CB  
1140 O OG  . SER A 150 ? 0.50408 0.53965 0.29011 -0.06364 -0.03830 0.04282  143 SER A OG  
1141 N N   . ALA A 151 ? 0.54585 0.58056 0.31915 -0.04208 -0.02044 0.08403  144 ALA A N   
1142 C CA  . ALA A 151 ? 0.64214 0.66294 0.40057 -0.03754 -0.00202 0.09022  144 ALA A CA  
1143 C C   . ALA A 151 ? 0.62495 0.65081 0.38354 -0.02830 -0.00220 0.11545  144 ALA A C   
1144 O O   . ALA A 151 ? 0.60262 0.61605 0.35472 -0.02421 0.01462  0.12389  144 ALA A O   
1145 C CB  . ALA A 151 ? 0.55795 0.56317 0.34419 -0.03547 0.01494  0.08037  144 ALA A CB  
1146 N N   . ASP A 152 ? 0.51496 0.55851 0.28428 -0.02483 -0.01986 0.12811  145 ASP A N   
1147 C CA  . ASP A 152 ? 0.60892 0.65733 0.38557 -0.01436 -0.02135 0.15317  145 ASP A CA  
1148 C C   . ASP A 152 ? 0.50522 0.54227 0.31971 -0.00659 -0.00685 0.15749  145 ASP A C   
1149 O O   . ASP A 152 ? 0.51879 0.54999 0.33909 0.00171  0.00048  0.17584  145 ASP A O   
1150 C CB  . ASP A 152 ? 0.66102 0.70331 0.39661 -0.01268 -0.01595 0.16771  145 ASP A CB  
1151 C CG  . ASP A 152 ? 0.90370 0.94990 0.59308 -0.02255 -0.02397 0.15558  145 ASP A CG  
1152 O OD1 . ASP A 152 ? 0.81826 0.88256 0.50375 -0.02746 -0.04590 0.15004  145 ASP A OD1 
1153 O OD2 . ASP A 152 ? 0.95374 0.98491 0.61189 -0.02587 -0.00747 0.15047  145 ASP A OD2 
1154 N N   . ILE A 153 ? 0.45698 0.48985 0.29668 -0.00933 -0.00312 0.14076  146 ILE A N   
1155 C CA  . ILE A 153 ? 0.44280 0.46470 0.31511 -0.00356 0.00895  0.14007  146 ILE A CA  
1156 C C   . ILE A 153 ? 0.50356 0.53753 0.40473 0.00083  -0.00049 0.14225  146 ILE A C   
1157 O O   . ILE A 153 ? 0.44015 0.48606 0.34340 -0.00426 -0.01175 0.13398  146 ILE A O   
1158 C CB  . ILE A 153 ? 0.45160 0.45989 0.33005 -0.00883 0.01976  0.12031  146 ILE A CB  
1159 C CG1 . ILE A 153 ? 0.41713 0.41307 0.27425 -0.01184 0.03421  0.11859  146 ILE A CG1 
1160 C CG2 . ILE A 153 ? 0.33663 0.33719 0.24866 -0.00384 0.02665  0.11701  146 ILE A CG2 
1161 C CD1 . ILE A 153 ? 0.53777 0.52344 0.40318 -0.01679 0.04342  0.09868  146 ILE A CD1 
1162 N N   . ILE A 154 ? 0.39430 0.42408 0.31911 0.00989  0.00593  0.15272  147 ILE A N   
1163 C CA  . ILE A 154 ? 0.39213 0.43008 0.34637 0.01518  0.00244  0.15281  147 ILE A CA  
1164 C C   . ILE A 154 ? 0.41063 0.43270 0.38333 0.01640  0.01468  0.14039  147 ILE A C   
1165 O O   . ILE A 154 ? 0.42450 0.43099 0.40079 0.01839  0.02632  0.14151  147 ILE A O   
1166 C CB  . ILE A 154 ? 0.40483 0.45098 0.37402 0.02578  -0.00054 0.17351  147 ILE A CB  
1167 C CG1 . ILE A 154 ? 0.42010 0.48431 0.36963 0.02476  -0.01645 0.18665  147 ILE A CG1 
1168 C CG2 . ILE A 154 ? 0.41448 0.46858 0.41620 0.03165  -0.00055 0.17130  147 ILE A CG2 
1169 C CD1 . ILE A 154 ? 0.44145 0.51633 0.40853 0.03652  -0.02244 0.20930  147 ILE A CD1 
1170 N N   . HIS A 155 ? 0.30498 0.33116 0.28907 0.01469  0.01186  0.12878  148 HIS A N   
1171 C CA  . HIS A 155 ? 0.35949 0.37207 0.35653 0.01556  0.02020  0.11595  148 HIS A CA  
1172 C C   . HIS A 155 ? 0.47254 0.47957 0.49234 0.02472  0.02798  0.12115  148 HIS A C   
1173 O O   . HIS A 155 ? 0.48523 0.47675 0.51405 0.02644  0.03724  0.11764  148 HIS A O   
1174 C CB  . HIS A 155 ? 0.41816 0.43556 0.41443 0.01105  0.01487  0.10395  148 HIS A CB  
1175 C CG  . HIS A 155 ? 0.35293 0.35668 0.35367 0.01045  0.01960  0.08994  148 HIS A CG  
1176 N ND1 . HIS A 155 ? 0.40241 0.39970 0.41757 0.01619  0.02548  0.08600  148 HIS A ND1 
1177 C CD2 . HIS A 155 ? 0.35657 0.35240 0.34989 0.00514  0.01804  0.07850  148 HIS A CD2 
1178 C CE1 . HIS A 155 ? 0.43307 0.42016 0.44688 0.01379  0.02549  0.07266  148 HIS A CE1 
1179 N NE2 . HIS A 155 ? 0.30412 0.29071 0.30666 0.00768  0.02073  0.06904  148 HIS A NE2 
1180 N N   . ARG A 156 ? 0.40444 0.42395 0.43731 0.03045  0.02510  0.12845  149 ARG A N   
1181 C CA  . ARG A 156 ? 0.37356 0.38954 0.43078 0.04061  0.03274  0.13457  149 ARG A CA  
1182 C C   . ARG A 156 ? 0.36493 0.36962 0.43278 0.04192  0.04092  0.11789  149 ARG A C   
1183 O O   . ARG A 156 ? 0.43898 0.44000 0.52735 0.05011  0.04857  0.11891  149 ARG A O   
1184 C CB  . ARG A 156 ? 0.51332 0.51660 0.57655 0.04578  0.03953  0.14753  149 ARG A CB  
1185 C CG  . ARG A 156 ? 0.65822 0.67353 0.72759 0.05353  0.03414  0.17013  149 ARG A CG  
1186 C CD  . ARG A 156 ? 0.67891 0.67761 0.75467 0.05939  0.04304  0.18499  149 ARG A CD  
1187 N NE  . ARG A 156 ? 0.63742 0.62088 0.74382 0.06707  0.05546  0.18126  149 ARG A NE  
1188 C CZ  . ARG A 156 ? 0.75005 0.71940 0.87404 0.07520  0.06403  0.19645  149 ARG A CZ  
1189 N NH1 . ARG A 156 ? 0.78763 0.75636 0.89906 0.07735  0.06163  0.21903  149 ARG A NH1 
1190 N NH2 . ARG A 156 ? 0.85601 0.81006 1.00950 0.08124  0.07570  0.18882  149 ARG A NH2 
1191 N N   . ASP A 157 ? 0.36223 0.36091 0.41639 0.03466  0.03915  0.10236  150 ASP A N   
1192 C CA  . ASP A 157 ? 0.39804 0.38623 0.45661 0.03565  0.04437  0.08632  150 ASP A CA  
1193 C C   . ASP A 157 ? 0.42202 0.41561 0.46365 0.02998  0.03844  0.07665  150 ASP A C   
1194 O O   . ASP A 157 ? 0.42527 0.40883 0.46009 0.02799  0.03833  0.06272  150 ASP A O   
1195 C CB  . ASP A 157 ? 0.58569 0.55582 0.64903 0.03367  0.04850  0.07675  150 ASP A CB  
1196 C CG  . ASP A 157 ? 0.64528 0.60317 0.72122 0.03753  0.05533  0.06292  150 ASP A CG  
1197 O OD1 . ASP A 157 ? 0.69021 0.64636 0.78264 0.04516  0.06324  0.06745  150 ASP A OD1 
1198 O OD2 . ASP A 157 ? 0.63023 0.58025 0.70023 0.03320  0.05219  0.04686  150 ASP A OD2 
1199 N N   . LEU A 158 ? 0.46362 0.47274 0.49906 0.02712  0.03276  0.08438  151 LEU A N   
1200 C CA  . LEU A 158 ? 0.42212 0.43454 0.44292 0.02116  0.02832  0.07799  151 LEU A CA  
1201 C C   . LEU A 158 ? 0.46390 0.47343 0.48429 0.02477  0.03549  0.07005  151 LEU A C   
1202 O O   . LEU A 158 ? 0.42576 0.44163 0.46073 0.03114  0.04356  0.07347  151 LEU A O   
1203 C CB  . LEU A 158 ? 0.39427 0.42413 0.41457 0.01670  0.02211  0.08772  151 LEU A CB  
1204 C CG  . LEU A 158 ? 0.49415 0.52468 0.50204 0.00909  0.01310  0.08912  151 LEU A CG  
1205 C CD1 . LEU A 158 ? 0.37330 0.42022 0.38159 0.00297  0.00625  0.09447  151 LEU A CD1 
1206 C CD2 . LEU A 158 ? 0.50138 0.51677 0.49587 0.00472  0.01145  0.07779  151 LEU A CD2 
1207 N N   . LYS A 159 ? 0.46687 0.46687 0.46988 0.02123  0.03273  0.05965  152 LYS A N   
1208 C CA  . LYS A 159 ? 0.37695 0.37241 0.37018 0.02386  0.03896  0.05117  152 LYS A CA  
1209 C C   . LYS A 159 ? 0.42750 0.41627 0.39712 0.01840  0.03119  0.04621  152 LYS A C   
1210 O O   . LYS A 159 ? 0.45043 0.43667 0.41702 0.01369  0.02182  0.04749  152 LYS A O   
1211 C CB  . LYS A 159 ? 0.38819 0.37129 0.38819 0.02971  0.04505  0.03966  152 LYS A CB  
1212 C CG  . LYS A 159 ? 0.45737 0.42656 0.44870 0.02678  0.03686  0.02729  152 LYS A CG  
1213 C CD  . LYS A 159 ? 0.62962 0.58669 0.63126 0.03107  0.04273  0.01409  152 LYS A CD  
1214 C CE  . LYS A 159 ? 0.48040 0.43433 0.50883 0.03306  0.04673  0.01989  152 LYS A CE  
1215 N NZ  . LYS A 159 ? 0.50198 0.45461 0.53287 0.02744  0.03837  0.02266  152 LYS A NZ  
1216 N N   . PRO A 160 ? 0.49259 0.47761 0.44444 0.01949  0.03552  0.04104  153 PRO A N   
1217 C CA  . PRO A 160 ? 0.50520 0.48367 0.43284 0.01512  0.02742  0.04044  153 PRO A CA  
1218 C C   . PRO A 160 ? 0.46538 0.43323 0.38926 0.01396  0.01422  0.03261  153 PRO A C   
1219 O O   . PRO A 160 ? 0.47212 0.43769 0.39017 0.01007  0.00517  0.03687  153 PRO A O   
1220 C CB  . PRO A 160 ? 0.53812 0.51263 0.44403 0.01810  0.03622  0.03514  153 PRO A CB  
1221 C CG  . PRO A 160 ? 0.50120 0.48613 0.42560 0.02230  0.05165  0.03760  153 PRO A CG  
1222 C CD  . PRO A 160 ? 0.49703 0.48386 0.44904 0.02503  0.04936  0.03715  153 PRO A CD  
1223 N N   . SER A 161 ? 0.46287 0.42417 0.39400 0.01714  0.01328  0.02084  154 SER A N   
1224 C CA  . SER A 161 ? 0.49680 0.45077 0.43063 0.01565  0.00072  0.01266  154 SER A CA  
1225 C C   . SER A 161 ? 0.42651 0.38379 0.37856 0.01240  -0.00275 0.01910  154 SER A C   
1226 O O   . SER A 161 ? 0.46269 0.41603 0.41946 0.01086  -0.01238 0.01454  154 SER A O   
1227 C CB  . SER A 161 ? 0.48446 0.43147 0.42826 0.01822  0.00153  -0.00226 154 SER A CB  
1228 O OG  . SER A 161 ? 0.58413 0.53288 0.55123 0.02026  0.01280  0.00034  154 SER A OG  
1229 N N   . ASN A 162 ? 0.37839 0.34355 0.34063 0.01155  0.00469  0.02911  155 ASN A N   
1230 C CA  . ASN A 162 ? 0.44002 0.40800 0.41296 0.00808  0.00269  0.03451  155 ASN A CA  
1231 C C   . ASN A 162 ? 0.43727 0.40681 0.40013 0.00350  -0.00303 0.04001  155 ASN A C   
1232 O O   . ASN A 162 ? 0.35753 0.32798 0.32631 0.00017  -0.00444 0.04199  155 ASN A O   
1233 C CB  . ASN A 162 ? 0.41216 0.38800 0.39662 0.00917  0.01073  0.04320  155 ASN A CB  
1234 C CG  . ASN A 162 ? 0.44670 0.41734 0.44686 0.01322  0.01699  0.03962  155 ASN A CG  
1235 O OD1 . ASN A 162 ? 0.49713 0.46955 0.50401 0.01787  0.02419  0.04201  155 ASN A OD1 
1236 N ND2 . ASN A 162 ? 0.40148 0.36524 0.41124 0.01151  0.01553  0.03396  155 ASN A ND2 
1237 N N   . LEU A 163 ? 0.41688 0.38526 0.36421 0.00302  -0.00492 0.04241  156 LEU A N   
1238 C CA  . LEU A 163 ? 0.46103 0.42829 0.40114 -0.00172 -0.00902 0.04878  156 LEU A CA  
1239 C C   . LEU A 163 ? 0.52650 0.48271 0.45572 -0.00024 -0.01851 0.04556  156 LEU A C   
1240 O O   . LEU A 163 ? 0.52810 0.48063 0.43948 0.00199  -0.01942 0.04639  156 LEU A O   
1241 C CB  . LEU A 163 ? 0.44556 0.42041 0.37967 -0.00414 -0.00228 0.05759  156 LEU A CB  
1242 C CG  . LEU A 163 ? 0.47264 0.46187 0.42107 -0.00540 0.00416  0.06280  156 LEU A CG  
1243 C CD1 . LEU A 163 ? 0.31486 0.30617 0.27349 -0.00758 0.00034  0.06177  156 LEU A CD1 
1244 C CD2 . LEU A 163 ? 0.48349 0.47755 0.43676 0.00108  0.01247  0.06116  156 LEU A CD2 
1245 N N   . ALA A 164 ? 0.44092 0.39215 0.38052 -0.00093 -0.02538 0.04223  157 ALA A N   
1246 C CA  . ALA A 164 ? 0.48334 0.42536 0.41822 0.00138  -0.03655 0.04121  157 ALA A CA  
1247 C C   . ALA A 164 ? 0.45797 0.39391 0.38620 -0.00207 -0.03764 0.05096  157 ALA A C   
1248 O O   . ALA A 164 ? 0.35484 0.29229 0.29270 -0.00704 -0.03301 0.05267  157 ALA A O   
1249 C CB  . ALA A 164 ? 0.45129 0.39189 0.40784 0.00315  -0.04215 0.03261  157 ALA A CB  
1250 N N   . VAL A 165 ? 0.42609 0.35411 0.33671 0.00018  -0.04379 0.05732  158 VAL A N   
1251 C CA  . VAL A 165 ? 0.53124 0.45053 0.43552 -0.00317 -0.04350 0.06885  158 VAL A CA  
1252 C C   . VAL A 165 ? 0.50269 0.40967 0.40123 0.00220  -0.05685 0.07319  158 VAL A C   
1253 O O   . VAL A 165 ? 0.39538 0.30247 0.28328 0.00804  -0.06649 0.06969  158 VAL A O   
1254 C CB  . VAL A 165 ? 0.53450 0.45634 0.42000 -0.00661 -0.03337 0.07845  158 VAL A CB  
1255 C CG1 . VAL A 165 ? 0.55165 0.48743 0.44980 -0.01162 -0.02214 0.07613  158 VAL A CG1 
1256 C CG2 . VAL A 165 ? 0.54926 0.47061 0.40926 -0.00121 -0.03466 0.07777  158 VAL A CG2 
1257 N N   . ASN A 166 ? 0.59262 0.48875 0.49979 0.00030  -0.05843 0.08052  159 ASN A N   
1258 C CA  . ASN A 166 ? 0.57664 0.45913 0.47868 0.00601  -0.07066 0.08959  159 ASN A CA  
1259 C C   . ASN A 166 ? 0.63036 0.50337 0.50486 0.00399  -0.06666 0.10657  159 ASN A C   
1260 O O   . ASN A 166 ? 0.63149 0.50926 0.49749 -0.00275 -0.05306 0.11008  159 ASN A O   
1261 C CB  . ASN A 166 ? 0.55306 0.42601 0.48339 0.00618  -0.07315 0.08835  159 ASN A CB  
1262 C CG  . ASN A 166 ? 0.62070 0.50210 0.57782 0.00905  -0.07564 0.07262  159 ASN A CG  
1263 O OD1 . ASN A 166 ? 0.66528 0.55698 0.62231 0.01284  -0.08097 0.06489  159 ASN A OD1 
1264 N ND2 . ASN A 166 ? 0.58295 0.45927 0.56369 0.00667  -0.07042 0.06700  159 ASN A ND2 
1265 N N   . GLU A 167 ? 0.59598 0.45595 0.45765 0.01018  -0.07844 0.11841  160 GLU A N   
1266 C CA  . GLU A 167 ? 0.66654 0.51384 0.50243 0.00799  -0.07291 0.13775  160 GLU A CA  
1267 C C   . GLU A 167 ? 0.63524 0.47303 0.49102 -0.00058 -0.06111 0.14473  160 GLU A C   
1268 O O   . GLU A 167 ? 0.73588 0.56742 0.57709 -0.00644 -0.04972 0.15841  160 GLU A O   
1269 C CB  . GLU A 167 ? 0.82625 0.66007 0.64336 0.01732  -0.08987 0.15141  160 GLU A CB  
1270 C CG  . GLU A 167 ? 0.97832 0.81528 0.75063 0.02144  -0.09457 0.15511  160 GLU A CG  
1271 C CD  . GLU A 167 ? 1.11804 0.95739 0.86405 0.01407  -0.07360 0.16060  160 GLU A CD  
1272 O OE1 . GLU A 167 ? 1.15839 1.00172 0.86774 0.01659  -0.07306 0.15904  160 GLU A OE1 
1273 O OE2 . GLU A 167 ? 1.15324 0.99113 0.91654 0.00558  -0.05745 0.16533  160 GLU A OE2 
1274 N N   . ASP A 168 ? 0.63039 0.46687 0.51970 -0.00211 -0.06259 0.13445  161 ASP A N   
1275 C CA  . ASP A 168 ? 0.71204 0.54181 0.62141 -0.01210 -0.05143 0.13494  161 ASP A CA  
1276 C C   . ASP A 168 ? 0.70239 0.54817 0.60909 -0.02211 -0.03763 0.13027  161 ASP A C   
1277 O O   . ASP A 168 ? 0.48756 0.32976 0.40697 -0.03214 -0.02857 0.13291  161 ASP A O   
1278 C CB  . ASP A 168 ? 0.64134 0.46881 0.58279 -0.01150 -0.05470 0.12008  161 ASP A CB  
1279 C CG  . ASP A 168 ? 0.79138 0.59527 0.75031 -0.00934 -0.05819 0.12816  161 ASP A CG  
1280 O OD1 . ASP A 168 ? 0.92425 0.71401 0.86979 -0.00381 -0.06419 0.14660  161 ASP A OD1 
1281 O OD2 . ASP A 168 ? 0.97518 0.77353 0.96019 -0.01282 -0.05451 0.11618  161 ASP A OD2 
1282 N N   . CYS A 169 ? 0.60524 0.46868 0.49913 -0.01954 -0.03645 0.12302  162 CYS A N   
1283 C CA  . CYS A 169 ? 0.58756 0.46928 0.48366 -0.02620 -0.02516 0.11745  162 CYS A CA  
1284 C C   . CYS A 169 ? 0.52180 0.41365 0.44137 -0.02979 -0.02559 0.10222  162 CYS A C   
1285 O O   . CYS A 169 ? 0.55300 0.45975 0.47941 -0.03602 -0.01836 0.09864  162 CYS A O   
1286 C CB  . CYS A 169 ? 0.62942 0.51003 0.52527 -0.03573 -0.01260 0.12958  162 CYS A CB  
1287 S SG  . CYS A 169 ? 0.82407 0.70512 0.68593 -0.03290 -0.00298 0.14424  162 CYS A SG  
1288 N N   . GLU A 170 ? 0.55130 0.43620 0.48334 -0.02569 -0.03356 0.09369  163 GLU A N   
1289 C CA  . GLU A 170 ? 0.55525 0.44884 0.50356 -0.02833 -0.03240 0.07920  163 GLU A CA  
1290 C C   . GLU A 170 ? 0.45829 0.36728 0.40188 -0.02327 -0.03248 0.07202  163 GLU A C   
1291 O O   . GLU A 170 ? 0.39009 0.29828 0.32610 -0.01554 -0.03814 0.07198  163 GLU A O   
1292 C CB  . GLU A 170 ? 0.47443 0.35462 0.43921 -0.02534 -0.03743 0.07216  163 GLU A CB  
1293 C CG  . GLU A 170 ? 0.73853 0.60241 0.71430 -0.03209 -0.03502 0.07500  163 GLU A CG  
1294 C CD  . GLU A 170 ? 0.86919 0.71523 0.86109 -0.02562 -0.04031 0.07269  163 GLU A CD  
1295 O OE1 . GLU A 170 ? 0.91811 0.75351 0.92601 -0.03062 -0.03641 0.06435  163 GLU A OE1 
1296 O OE2 . GLU A 170 ? 0.91515 0.75811 0.90510 -0.01537 -0.04886 0.07837  163 GLU A OE2 
1297 N N   . LEU A 171 ? 0.36804 0.29058 0.31676 -0.02785 -0.02705 0.06608  164 LEU A N   
1298 C CA  . LEU A 171 ? 0.35224 0.28848 0.29795 -0.02388 -0.02476 0.06224  164 LEU A CA  
1299 C C   . LEU A 171 ? 0.34352 0.28418 0.29956 -0.02397 -0.02382 0.05221  164 LEU A C   
1300 O O   . LEU A 171 ? 0.32487 0.26480 0.28598 -0.02993 -0.02241 0.04822  164 LEU A O   
1301 C CB  . LEU A 171 ? 0.34585 0.29583 0.28793 -0.02761 -0.01801 0.06824  164 LEU A CB  
1302 C CG  . LEU A 171 ? 0.41605 0.37977 0.35946 -0.02352 -0.01421 0.06548  164 LEU A CG  
1303 C CD1 . LEU A 171 ? 0.35182 0.32506 0.29088 -0.02306 -0.00717 0.07257  164 LEU A CD1 
1304 C CD2 . LEU A 171 ? 0.30980 0.28286 0.26267 -0.02714 -0.01376 0.06168  164 LEU A CD2 
1305 N N   . LYS A 172 ? 0.36802 0.31247 0.32612 -0.01795 -0.02381 0.04770  165 LYS A N   
1306 C CA  . LYS A 172 ? 0.36624 0.31555 0.33235 -0.01778 -0.01980 0.04079  165 LYS A CA  
1307 C C   . LYS A 172 ? 0.36300 0.32218 0.32777 -0.01452 -0.01582 0.04263  165 LYS A C   
1308 O O   . LYS A 172 ? 0.33814 0.29680 0.29991 -0.01006 -0.01738 0.04331  165 LYS A O   
1309 C CB  . LYS A 172 ? 0.37440 0.31596 0.35346 -0.01377 -0.02175 0.03277  165 LYS A CB  
1310 C CG  . LYS A 172 ? 0.38092 0.31259 0.36706 -0.01634 -0.02225 0.02852  165 LYS A CG  
1311 C CD  . LYS A 172 ? 0.52010 0.44377 0.52217 -0.00996 -0.02807 0.02471  165 LYS A CD  
1312 C CE  . LYS A 172 ? 0.52300 0.43829 0.53969 -0.01091 -0.02391 0.01678  165 LYS A CE  
1313 N NZ  . LYS A 172 ? 0.47962 0.38764 0.48733 -0.01782 -0.02198 0.01793  165 LYS A NZ  
1314 N N   . ILE A 173 ? 0.38572 0.35273 0.35153 -0.01648 -0.01080 0.04340  166 ILE A N   
1315 C CA  . ILE A 173 ? 0.32994 0.30419 0.29834 -0.01253 -0.00616 0.04650  166 ILE A CA  
1316 C C   . ILE A 173 ? 0.36624 0.33492 0.34501 -0.00905 -0.00297 0.04024  166 ILE A C   
1317 O O   . ILE A 173 ? 0.36157 0.32710 0.34406 -0.01106 -0.00005 0.03624  166 ILE A O   
1318 C CB  . ILE A 173 ? 0.32204 0.30750 0.28726 -0.01532 -0.00380 0.05313  166 ILE A CB  
1319 C CG1 . ILE A 173 ? 0.28636 0.28017 0.24842 -0.01978 -0.00738 0.05849  166 ILE A CG1 
1320 C CG2 . ILE A 173 ? 0.27935 0.26992 0.25062 -0.00966 0.00142  0.05827  166 ILE A CG2 
1321 C CD1 . ILE A 173 ? 0.34295 0.35029 0.30385 -0.02359 -0.00934 0.06392  166 ILE A CD1 
1322 N N   . LEU A 174 ? 0.32539 0.29266 0.31015 -0.00441 -0.00240 0.03821  167 LEU A N   
1323 C CA  . LEU A 174 ? 0.32275 0.28557 0.32282 -0.00216 0.00072  0.03174  167 LEU A CA  
1324 C C   . LEU A 174 ? 0.41676 0.38222 0.42227 -0.00058 0.00989  0.03724  167 LEU A C   
1325 O O   . LEU A 174 ? 0.31709 0.28740 0.31780 0.00162  0.01155  0.04385  167 LEU A O   
1326 C CB  . LEU A 174 ? 0.36829 0.32672 0.37285 0.00107  -0.00598 0.02396  167 LEU A CB  
1327 C CG  . LEU A 174 ? 0.40346 0.35802 0.40275 0.00132  -0.01715 0.02057  167 LEU A CG  
1328 C CD1 . LEU A 174 ? 0.41691 0.36863 0.41490 0.00471  -0.02531 0.01331  167 LEU A CD1 
1329 C CD2 . LEU A 174 ? 0.37975 0.33191 0.39431 0.00009  -0.01839 0.01642  167 LEU A CD2 
1330 N N   . ASP A 175 ? 0.27292 0.23497 0.29068 -0.00129 0.01694  0.03560  168 ASP A N   
1331 C CA  . ASP A 175 ? 0.39285 0.35412 0.41747 0.00075  0.02640  0.04272  168 ASP A CA  
1332 C C   . ASP A 175 ? 0.35881 0.31551 0.39684 0.00451  0.02672  0.03784  168 ASP A C   
1333 O O   . ASP A 175 ? 0.33266 0.28968 0.37215 0.00815  0.03139  0.04487  168 ASP A O   
1334 C CB  . ASP A 175 ? 0.37354 0.33067 0.40759 -0.00166 0.03650  0.04303  168 ASP A CB  
1335 C CG  . ASP A 175 ? 0.46400 0.41616 0.52220 -0.00267 0.03696  0.03066  168 ASP A CG  
1336 O OD1 . ASP A 175 ? 0.37430 0.32719 0.43531 -0.00220 0.02593  0.02143  168 ASP A OD1 
1337 O OD2 . ASP A 175 ? 0.47684 0.42490 0.55235 -0.00402 0.04811  0.03105  168 ASP A OD2 
1338 N N   . PHE A 176 ? 0.33473 0.28726 0.38327 0.00396  0.02099  0.02508  169 PHE A N   
1339 C CA  . PHE A 176 ? 0.40574 0.35319 0.46355 0.00639  0.01922  0.01615  169 PHE A CA  
1340 C C   . PHE A 176 ? 0.38556 0.33353 0.43400 0.00636  0.00576  0.00579  169 PHE A C   
1341 O O   . PHE A 176 ? 0.42885 0.37752 0.48482 0.00438  -0.00133 0.00023  169 PHE A O   
1342 C CB  . PHE A 176 ? 0.39644 0.33693 0.48227 0.00477  0.02609  0.01006  169 PHE A CB  
1343 C CG  . PHE A 176 ? 0.39986 0.33684 0.49351 0.00550  0.04041  0.02279  169 PHE A CG  
1344 C CD1 . PHE A 176 ? 0.43872 0.37165 0.53344 0.01003  0.04620  0.02886  169 PHE A CD1 
1345 C CD2 . PHE A 176 ? 0.48434 0.42140 0.58384 0.00233  0.04890  0.02943  169 PHE A CD2 
1346 C CE1 . PHE A 176 ? 0.48534 0.41413 0.58725 0.01188  0.05808  0.04349  169 PHE A CE1 
1347 C CE2 . PHE A 176 ? 0.59979 0.53250 0.70151 0.00332  0.06191  0.04365  169 PHE A CE2 
1348 C CZ  . PHE A 176 ? 0.42485 0.35329 0.52800 0.00836  0.06543  0.05178  169 PHE A CZ  
1349 N N   . GLY A 177 ? 0.45841 0.40607 0.49047 0.00914  0.00287  0.00408  170 GLY A N   
1350 C CA  . GLY A 177 ? 0.47321 0.42007 0.48942 0.00961  -0.00942 -0.00346 170 GLY A CA  
1351 C C   . GLY A 177 ? 0.49810 0.43961 0.52380 0.00974  -0.01632 -0.01958 170 GLY A C   
1352 O O   . GLY A 177 ? 0.55687 0.49430 0.60531 0.00878  -0.01034 -0.02603 170 GLY A O   
1353 N N   . LEU A 178 ? 0.49187 0.43287 0.49930 0.01054  -0.02983 -0.02589 171 LEU A N   
1354 C CA  . LEU A 178 ? 0.57545 0.51284 0.58676 0.01018  -0.04068 -0.04293 171 LEU A CA  
1355 C C   . LEU A 178 ? 0.61375 0.54494 0.60813 0.01220  -0.03410 -0.05116 171 LEU A C   
1356 O O   . LEU A 178 ? 0.58013 0.51122 0.54487 0.01485  -0.03049 -0.04548 171 LEU A O   
1357 C CB  . LEU A 178 ? 0.60419 0.54387 0.59979 0.01104  -0.06018 -0.04508 171 LEU A CB  
1358 C CG  . LEU A 178 ? 0.58430 0.52930 0.59943 0.01044  -0.06754 -0.03869 171 LEU A CG  
1359 C CD1 . LEU A 178 ? 0.59690 0.54229 0.59118 0.01337  -0.08593 -0.03578 171 LEU A CD1 
1360 C CD2 . LEU A 178 ? 0.44393 0.39240 0.50076 0.00755  -0.06945 -0.04934 171 LEU A CD2 
1361 N N   . ALA A 179 ? 0.60035 0.52564 0.61599 0.01071  -0.03078 -0.06509 172 ALA A N   
1362 C CA  . ALA A 179 ? 0.66789 0.58488 0.67040 0.01267  -0.02464 -0.07763 172 ALA A CA  
1363 C C   . ALA A 179 ? 0.66921 0.58366 0.64628 0.01189  -0.04137 -0.09510 172 ALA A C   
1364 O O   . ALA A 179 ? 0.77864 0.68509 0.73915 0.01321  -0.03665 -0.10894 172 ALA A O   
1365 C CB  . ALA A 179 ? 0.60117 0.50977 0.63885 0.01117  -0.01312 -0.08580 172 ALA A CB  
1366 N N   . ARG A 180 ? 0.79184 0.71270 0.76482 0.01033  -0.06081 -0.09484 173 ARG A N   
1367 C CA  . ARG A 180 ? 0.70383 0.62399 0.65116 0.00994  -0.08121 -0.10950 173 ARG A CA  
1368 C C   . ARG A 180 ? 0.89642 0.80967 0.79570 0.01315  -0.07556 -0.11368 173 ARG A C   
1369 O O   . ARG A 180 ? 0.91133 0.81731 0.79827 0.01205  -0.07791 -0.13451 173 ARG A O   
1370 C CB  . ARG A 180 ? 0.59128 0.52000 0.53304 0.01097  -0.10052 -0.09892 173 ARG A CB  
1371 C CG  . ARG A 180 ? 0.79170 0.71945 0.69019 0.01307  -0.12047 -0.10459 173 ARG A CG  
1372 C CD  . ARG A 180 ? 0.86500 0.80084 0.76859 0.01495  -0.14245 -0.09487 173 ARG A CD  
1373 N NE  . ARG A 180 ? 0.87691 0.81334 0.74915 0.01639  -0.16773 -0.10451 173 ARG A NE  
1374 C CZ  . ARG A 180 ? 0.90218 0.84431 0.79403 0.01347  -0.18843 -0.12396 173 ARG A CZ  
1375 N NH1 . ARG A 180 ? 0.92607 0.86964 0.78439 0.01499  -0.21381 -0.13217 173 ARG A NH1 
1376 N NH2 . ARG A 180 ? 0.94109 0.88791 0.88748 0.00848  -0.18389 -0.13508 173 ARG A NH2 
1377 N N   . VAL A 190 ? 0.77819 0.69429 0.67868 0.04381  0.07531  -0.06762 183 VAL A N   
1378 C CA  . VAL A 190 ? 0.95213 0.88208 0.88247 0.04533  0.08006  -0.04518 183 VAL A CA  
1379 C C   . VAL A 190 ? 0.96648 0.89198 0.93810 0.04864  0.08376  -0.04473 183 VAL A C   
1380 O O   . VAL A 190 ? 1.04027 0.96089 1.02458 0.04476  0.07221  -0.04539 183 VAL A O   
1381 C CB  . VAL A 190 ? 0.92948 0.86826 0.85228 0.03907  0.06418  -0.02962 183 VAL A CB  
1382 C CG1 . VAL A 190 ? 0.85989 0.81152 0.81318 0.03958  0.06634  -0.01010 183 VAL A CG1 
1383 C CG2 . VAL A 190 ? 0.81822 0.76074 0.70438 0.03662  0.06361  -0.02487 183 VAL A CG2 
1384 N N   . ALA A 191 ? 0.84534 0.77254 0.83985 0.05629  0.10107  -0.04229 184 ALA A N   
1385 C CA  . ALA A 191 ? 1.05357 0.97265 1.08652 0.06112  0.10691  -0.04173 184 ALA A CA  
1386 C C   . ALA A 191 ? 0.98185 0.91141 1.03908 0.06073  0.10039  -0.01837 184 ALA A C   
1387 O O   . ALA A 191 ? 1.14732 1.06836 1.23299 0.06367  0.10313  -0.01485 184 ALA A O   
1388 C CB  . ALA A 191 ? 0.90056 0.81745 0.95244 0.07115  0.12786  -0.04615 184 ALA A CB  
1389 N N   . THR A 192 ? 0.59385 0.54014 0.63937 0.05687  0.09241  -0.00268 185 THR A N   
1390 C CA  . THR A 192 ? 0.60271 0.56012 0.66558 0.05617  0.08607  0.01814  185 THR A CA  
1391 C C   . THR A 192 ? 0.56820 0.53766 0.65838 0.06490  0.09619  0.03248  185 THR A C   
1392 O O   . THR A 192 ? 0.54360 0.53102 0.63897 0.06405  0.09084  0.04966  185 THR A O   
1393 C CB  . THR A 192 ? 0.72880 0.67369 0.80522 0.05394  0.08079  0.01793  185 THR A CB  
1394 O OG1 . THR A 192 ? 0.79014 0.72492 0.84867 0.04682  0.07176  0.00195  185 THR A OG1 
1395 C CG2 . THR A 192 ? 0.72743 0.68336 0.80974 0.05165  0.07339  0.03831  185 THR A CG2 
1396 N N   . ARG A 193 ? 0.63203 0.59185 0.74203 0.07345  0.11013  0.02459  186 ARG A N   
1397 C CA  . ARG A 193 ? 0.51591 0.48754 0.65731 0.08380  0.12057  0.03750  186 ARG A CA  
1398 C C   . ARG A 193 ? 0.47267 0.46745 0.60920 0.08318  0.12273  0.04469  186 ARG A C   
1399 O O   . ARG A 193 ? 0.40236 0.41576 0.56594 0.08885  0.12380  0.06137  186 ARG A O   
1400 C CB  . ARG A 193 ? 0.55597 0.51094 0.71701 0.09307  0.13790  0.02276  186 ARG A CB  
1401 C CG  . ARG A 193 ? 0.66977 0.62544 0.81533 0.09482  0.15195  0.00523  186 ARG A CG  
1402 C CD  . ARG A 193 ? 0.60614 0.54374 0.77291 0.10445  0.17049  -0.01127 186 ARG A CD  
1403 N NE  . ARG A 193 ? 0.63850 0.56162 0.77233 0.10086  0.17807  -0.03904 186 ARG A NE  
1404 C CZ  . ARG A 193 ? 0.78319 0.68251 0.90630 0.09712  0.17577  -0.06061 186 ARG A CZ  
1405 N NH1 . ARG A 193 ? 0.79021 0.67788 0.88040 0.09419  0.18136  -0.08648 186 ARG A NH1 
1406 N NH2 . ARG A 193 ? 0.84699 0.73414 0.99255 0.09576  0.16766  -0.05621 186 ARG A NH2 
1407 N N   . TRP A 194 ? 0.49256 0.48704 0.59635 0.07608  0.12269  0.03351  187 TRP A N   
1408 C CA  . TRP A 194 ? 0.42736 0.44142 0.52730 0.07444  0.12811  0.03983  187 TRP A CA  
1409 C C   . TRP A 194 ? 0.41651 0.45059 0.52196 0.06823  0.11377  0.05901  187 TRP A C   
1410 O O   . TRP A 194 ? 0.48343 0.53735 0.59920 0.06719  0.11802  0.06738  187 TRP A O   
1411 C CB  . TRP A 194 ? 0.47349 0.47864 0.53233 0.06815  0.13150  0.02512  187 TRP A CB  
1412 C CG  . TRP A 194 ? 0.52885 0.51487 0.57608 0.07316  0.14478  0.00326  187 TRP A CG  
1413 C CD1 . TRP A 194 ? 0.57492 0.55318 0.65002 0.08314  0.15851  -0.00442 187 TRP A CD1 
1414 C CD2 . TRP A 194 ? 0.50882 0.48020 0.51268 0.06846  0.14479  -0.01458 187 TRP A CD2 
1415 N NE1 . TRP A 194 ? 0.56171 0.52072 0.61320 0.08403  0.16789  -0.02847 187 TRP A NE1 
1416 C CE2 . TRP A 194 ? 0.58580 0.54125 0.59143 0.07503  0.15867  -0.03493 187 TRP A CE2 
1417 C CE3 . TRP A 194 ? 0.51762 0.48714 0.48125 0.05976  0.13365  -0.01496 187 TRP A CE3 
1418 C CZ2 . TRP A 194 ? 0.60989 0.54908 0.57476 0.07232  0.16040  -0.05695 187 TRP A CZ2 
1419 C CZ3 . TRP A 194 ? 0.50723 0.46116 0.43133 0.05817  0.13467  -0.03385 187 TRP A CZ3 
1420 C CH2 . TRP A 194 ? 0.68706 0.62669 0.61017 0.06400  0.14732  -0.05529 187 TRP A CH2 
1421 N N   . TYR A 195 ? 0.43807 0.46760 0.53815 0.06359  0.09797  0.06505  188 TYR A N   
1422 C CA  . TYR A 195 ? 0.33977 0.38523 0.43852 0.05638  0.08376  0.07932  188 TYR A CA  
1423 C C   . TYR A 195 ? 0.42591 0.47874 0.54679 0.06039  0.07532  0.09443  188 TYR A C   
1424 O O   . TYR A 195 ? 0.33252 0.39627 0.44809 0.05399  0.06203  0.10427  188 TYR A O   
1425 C CB  . TYR A 195 ? 0.37283 0.40722 0.43870 0.04602  0.07245  0.07301  188 TYR A CB  
1426 C CG  . TYR A 195 ? 0.37781 0.40250 0.41726 0.04296  0.07831  0.05996  188 TYR A CG  
1427 C CD1 . TYR A 195 ? 0.35656 0.36210 0.38228 0.04564  0.08227  0.04406  188 TYR A CD1 
1428 C CD2 . TYR A 195 ? 0.37057 0.40491 0.39832 0.03708  0.07965  0.06391  188 TYR A CD2 
1429 C CE1 . TYR A 195 ? 0.35980 0.35689 0.35605 0.04320  0.08565  0.03272  188 TYR A CE1 
1430 C CE2 . TYR A 195 ? 0.43842 0.46274 0.43755 0.03484  0.08530  0.05480  188 TYR A CE2 
1431 C CZ  . TYR A 195 ? 0.46984 0.47596 0.45094 0.03829  0.08745  0.03935  188 TYR A CZ  
1432 O OH  . TYR A 195 ? 0.55239 0.54889 0.49971 0.03632  0.09102  0.03077  188 TYR A OH  
1433 N N   . ARG A 196 ? 0.38700 0.43312 0.53120 0.07089  0.08284  0.09677  189 ARG A N   
1434 C CA  . ARG A 196 ? 0.30234 0.35228 0.46421 0.07583  0.07520  0.11364  189 ARG A CA  
1435 C C   . ARG A 196 ? 0.33715 0.41334 0.52982 0.08258  0.07306  0.12987  189 ARG A C   
1436 O O   . ARG A 196 ? 0.29098 0.37543 0.50735 0.08979  0.08544  0.12718  189 ARG A O   
1437 C CB  . ARG A 196 ? 0.41251 0.44000 0.58779 0.08403  0.08430  0.11056  189 ARG A CB  
1438 C CG  . ARG A 196 ? 0.59663 0.60089 0.74878 0.07674  0.08295  0.09734  189 ARG A CG  
1439 C CD  . ARG A 196 ? 0.63146 0.62478 0.79057 0.07830  0.07970  0.10965  189 ARG A CD  
1440 N NE  . ARG A 196 ? 0.67589 0.65412 0.81423 0.06888  0.07606  0.09946  189 ARG A NE  
1441 C CZ  . ARG A 196 ? 0.64734 0.61436 0.78729 0.06741  0.07545  0.10749  189 ARG A CZ  
1442 N NH1 . ARG A 196 ? 0.56479 0.53174 0.72112 0.07480  0.07731  0.12745  189 ARG A NH1 
1443 N NH2 . ARG A 196 ? 0.69781 0.65380 0.82364 0.05865  0.07335  0.09636  189 ARG A NH2 
1444 N N   . ALA A 197 ? 0.28051 0.37064 0.47322 0.08026  0.05722  0.14608  190 ALA A N   
1445 C CA  . ALA A 197 ? 0.35836 0.47569 0.58252 0.08681  0.05057  0.16286  190 ALA A CA  
1446 C C   . ALA A 197 ? 0.36056 0.47345 0.62075 0.10317  0.06070  0.17130  190 ALA A C   
1447 O O   . ALA A 197 ? 0.30478 0.39247 0.56149 0.10790  0.06771  0.16935  190 ALA A O   
1448 C CB  . ALA A 197 ? 0.40323 0.53308 0.61445 0.08142  0.02965  0.17765  190 ALA A CB  
1449 N N   . PRO A 198 ? 0.32726 0.46418 0.62674 0.11211  0.06226  0.18071  191 PRO A N   
1450 C CA  . PRO A 198 ? 0.32886 0.46046 0.66790 0.12936  0.07361  0.18833  191 PRO A CA  
1451 C C   . PRO A 198 ? 0.44611 0.56710 0.78767 0.13679  0.06356  0.20804  191 PRO A C   
1452 O O   . PRO A 198 ? 0.37381 0.47143 0.73050 0.14692  0.07619  0.20832  191 PRO A O   
1453 C CB  . PRO A 198 ? 0.35678 0.52299 0.73961 0.13610  0.07339  0.19682  191 PRO A CB  
1454 C CG  . PRO A 198 ? 0.37692 0.56807 0.74318 0.12214  0.05434  0.20065  191 PRO A CG  
1455 C CD  . PRO A 198 ? 0.33549 0.50527 0.65029 0.10696  0.05503  0.18409  191 PRO A CD  
1456 N N   . GLU A 199 ? 0.36237 0.49847 0.68809 0.13168  0.04186  0.22442  192 GLU A N   
1457 C CA  . GLU A 199 ? 0.47534 0.60138 0.79798 0.13877  0.03277  0.24596  192 GLU A CA  
1458 C C   . GLU A 199 ? 0.46963 0.55775 0.76912 0.13617  0.04534  0.23766  192 GLU A C   
1459 O O   . GLU A 199 ? 0.53364 0.60327 0.84497 0.14397  0.05153  0.24718  192 GLU A O   
1460 C CB  . GLU A 199 ? 0.34497 0.49079 0.64075 0.13047  0.00800  0.25986  192 GLU A CB  
1461 C CG  . GLU A 199 ? 0.40595 0.54651 0.65555 0.11196  0.00388  0.24274  192 GLU A CG  
1462 C CD  . GLU A 199 ? 0.39963 0.56640 0.65325 0.10235  -0.00271 0.23170  192 GLU A CD  
1463 O OE1 . GLU A 199 ? 0.31638 0.49109 0.59988 0.10635  0.00963  0.22316  192 GLU A OE1 
1464 O OE2 . GLU A 199 ? 0.48115 0.65955 0.70838 0.09045  -0.01880 0.23116  192 GLU A OE2 
1465 N N   . ILE A 200 ? 0.39828 0.47435 0.66360 0.12209  0.04907  0.21675  193 ILE A N   
1466 C CA  . ILE A 200 ? 0.49597 0.53908 0.74453 0.11842  0.06032  0.20638  193 ILE A CA  
1467 C C   . ILE A 200 ? 0.53339 0.55645 0.81440 0.12938  0.07941  0.19848  193 ILE A C   
1468 O O   . ILE A 200 ? 0.52177 0.52145 0.81314 0.13491  0.08679  0.20579  193 ILE A O   
1469 C CB  . ILE A 200 ? 0.50232 0.53976 0.71601 0.10299  0.06024  0.18372  193 ILE A CB  
1470 C CG1 . ILE A 200 ? 0.48487 0.53579 0.66657 0.09222  0.04335  0.19062  193 ILE A CG1 
1471 C CG2 . ILE A 200 ? 0.44388 0.45026 0.64979 0.09980  0.07215  0.16971  193 ILE A CG2 
1472 C CD1 . ILE A 200 ? 0.44611 0.49830 0.60116 0.07876  0.04121  0.17072  193 ILE A CD1 
1473 N N   . MET A 201 ? 0.52174 0.55238 0.81925 0.13227  0.08920  0.18289  194 MET A N   
1474 C CA  . MET A 201 ? 0.55806 0.56923 0.88464 0.14245  0.10884  0.17128  194 MET A CA  
1475 C C   . MET A 201 ? 0.49913 0.51064 0.86554 0.15742  0.11121  0.19167  194 MET A C   
1476 O O   . MET A 201 ? 0.55444 0.54325 0.93785 0.16128  0.12548  0.18210  194 MET A O   
1477 C CB  . MET A 201 ? 0.57132 0.59261 0.90173 0.14188  0.11999  0.15051  194 MET A CB  
1478 C CG  . MET A 201 ? 0.39597 0.40544 0.68639 0.12784  0.12224  0.12538  194 MET A CG  
1479 S SD  . MET A 201 ? 0.60889 0.63143 0.89591 0.12678  0.13543  0.10560  194 MET A SD  
1480 C CE  . MET A 201 ? 0.63253 0.62063 0.89835 0.12339  0.14966  0.07442  194 MET A CE  
1481 N N   . LEU A 202 ? 0.49027 0.52755 0.86195 0.15937  0.09476  0.21411  195 LEU A N   
1482 C CA  . LEU A 202 ? 0.55563 0.59300 0.94992 0.16692  0.09179  0.23171  195 LEU A CA  
1483 C C   . LEU A 202 ? 0.55436 0.57214 0.92866 0.16348  0.08690  0.24531  195 LEU A C   
1484 O O   . LEU A 202 ? 0.46927 0.48271 0.86014 0.17008  0.08610  0.26052  195 LEU A O   
1485 C CB  . LEU A 202 ? 0.56557 0.63938 0.97358 0.17022  0.07454  0.24881  195 LEU A CB  
1486 C CG  . LEU A 202 ? 0.43831 0.53312 0.88148 0.17625  0.08211  0.24025  195 LEU A CG  
1487 C CD1 . LEU A 202 ? 0.45462 0.58668 0.91101 0.17695  0.06164  0.25727  195 LEU A CD1 
1488 C CD2 . LEU A 202 ? 0.42657 0.50318 0.90323 0.18641  0.10073  0.23383  195 LEU A CD2 
1489 N N   . ASN A 203 ? 0.63910 0.64509 0.97914 0.15346  0.08467  0.24049  196 ASN A N   
1490 C CA  . ASN A 203 ? 0.58446 0.57264 0.90353 0.14856  0.08271  0.25192  196 ASN A CA  
1491 C C   . ASN A 203 ? 0.57193 0.58010 0.87601 0.14935  0.06383  0.27658  196 ASN A C   
1492 O O   . ASN A 203 ? 0.58563 0.58271 0.88691 0.15164  0.06374  0.29172  196 ASN A O   
1493 C CB  . ASN A 203 ? 0.59880 0.55860 0.94161 0.15280  0.09936  0.24888  196 ASN A CB  
1494 C CG  . ASN A 203 ? 0.58919 0.52503 0.91183 0.14426  0.10464  0.24963  196 ASN A CG  
1495 O OD1 . ASN A 203 ? 0.68137 0.61047 1.00298 0.14599  0.10387  0.26761  196 ASN A OD1 
1496 N ND2 . ASN A 203 ? 0.62932 0.55249 0.93695 0.13510  0.11037  0.23018  196 ASN A ND2 
1497 N N   . TRP A 204 ? 0.60428 0.64192 0.89793 0.14701  0.04746  0.27977  197 TRP A N   
1498 C CA  . TRP A 204 ? 0.55730 0.61509 0.83370 0.14653  0.02694  0.29938  197 TRP A CA  
1499 C C   . TRP A 204 ? 0.60543 0.64719 0.84087 0.13906  0.02431  0.30730  197 TRP A C   
1500 O O   . TRP A 204 ? 0.62159 0.66695 0.84471 0.14181  0.01369  0.32545  197 TRP A O   
1501 C CB  . TRP A 204 ? 0.51356 0.60368 0.78227 0.14125  0.01011  0.29614  197 TRP A CB  
1502 C CG  . TRP A 204 ? 0.44861 0.56693 0.73147 0.14654  -0.00867 0.31142  197 TRP A CG  
1503 C CD1 . TRP A 204 ? 0.51602 0.64005 0.77604 0.14635  -0.02563 0.32830  197 TRP A CD1 
1504 C CD2 . TRP A 204 ? 0.43590 0.58047 0.75923 0.15277  -0.01245 0.31036  197 TRP A CD2 
1505 N NE1 . TRP A 204 ? 0.48589 0.63815 0.77005 0.15225  -0.04188 0.33780  197 TRP A NE1 
1506 C CE2 . TRP A 204 ? 0.46122 0.62724 0.78671 0.15593  -0.03364 0.32712  197 TRP A CE2 
1507 C CE3 . TRP A 204 ? 0.41286 0.56462 0.77034 0.15596  0.00094  0.29617  197 TRP A CE3 
1508 C CZ2 . TRP A 204 ? 0.46194 0.65727 0.82672 0.16173  -0.04250 0.33022  197 TRP A CZ2 
1509 C CZ3 . TRP A 204 ? 0.41391 0.59441 0.80910 0.16142  -0.00541 0.29927  197 TRP A CZ3 
1510 C CH2 . TRP A 204 ? 0.43714 0.63957 0.83783 0.16407  -0.02732 0.31625  197 TRP A CH2 
1511 N N   . MET A 205 ? 0.68716 0.71103 0.90099 0.12979  0.03421  0.29377  198 MET A N   
1512 C CA  . MET A 205 ? 0.76065 0.76483 0.94252 0.12268  0.03859  0.29821  198 MET A CA  
1513 C C   . MET A 205 ? 0.79949 0.81847 0.93731 0.11507  0.02130  0.30613  198 MET A C   
1514 O O   . MET A 205 ? 0.93440 0.94134 1.04550 0.11226  0.02231  0.31624  198 MET A O   
1515 C CB  . MET A 205 ? 0.80242 0.78711 1.00054 0.13002  0.04850  0.31196  198 MET A CB  
1516 C CG  . MET A 205 ? 0.74631 0.70290 0.93160 0.12284  0.06441  0.30769  198 MET A CG  
1517 S SD  . MET A 205 ? 1.06058 1.00406 1.25055 0.11368  0.07753  0.27919  198 MET A SD  
1518 C CE  . MET A 205 ? 0.81694 0.77375 0.95739 0.10120  0.06557  0.27588  198 MET A CE  
1519 N N   . HIS A 206 ? 0.65640 0.70064 0.78602 0.11118  0.00620  0.30062  199 HIS A N   
1520 C CA  . HIS A 206 ? 0.71929 0.77600 0.80538 0.10143  -0.00937 0.30141  199 HIS A CA  
1521 C C   . HIS A 206 ? 0.73581 0.81992 0.82742 0.09715  -0.02296 0.29154  199 HIS A C   
1522 O O   . HIS A 206 ? 0.64853 0.75595 0.76302 0.10288  -0.03577 0.29811  199 HIS A O   
1523 C CB  . HIS A 206 ? 0.69111 0.75263 0.75853 0.10542  -0.02256 0.32068  199 HIS A CB  
1524 C CG  . HIS A 206 ? 0.80126 0.88517 0.89966 0.11568  -0.03667 0.33194  199 HIS A CG  
1525 N ND1 . HIS A 206 ? 0.89465 1.00896 0.99747 0.11295  -0.05545 0.32780  199 HIS A ND1 
1526 C CD2 . HIS A 206 ? 0.74412 0.82495 0.87410 0.12841  -0.03434 0.34673  199 HIS A CD2 
1527 C CE1 . HIS A 206 ? 0.86999 1.00009 1.00707 0.12372  -0.06405 0.33947  199 HIS A CE1 
1528 N NE2 . HIS A 206 ? 0.82823 0.93805 0.98139 0.13368  -0.05159 0.35137  199 HIS A NE2 
1529 N N   . TYR A 207 ? 0.44968 0.53145 0.52351 0.08687  -0.01981 0.27600  200 TYR A N   
1530 C CA  . TYR A 207 ? 0.41842 0.52065 0.50594 0.08328  -0.02654 0.26534  200 TYR A CA  
1531 C C   . TYR A 207 ? 0.47088 0.58994 0.52447 0.07062  -0.04353 0.25945  200 TYR A C   
1532 O O   . TYR A 207 ? 0.45433 0.56118 0.46877 0.06253  -0.04294 0.25611  200 TYR A O   
1533 C CB  . TYR A 207 ? 0.54911 0.63327 0.64571 0.07958  -0.00846 0.24432  200 TYR A CB  
1534 C CG  . TYR A 207 ? 0.56253 0.62743 0.69083 0.09115  0.00855  0.24754  200 TYR A CG  
1535 C CD1 . TYR A 207 ? 0.49269 0.56874 0.66149 0.10345  0.00981  0.25441  200 TYR A CD1 
1536 C CD2 . TYR A 207 ? 0.56374 0.59942 0.68498 0.08964  0.02396  0.24299  200 TYR A CD2 
1537 C CE1 . TYR A 207 ? 0.53367 0.58990 0.73242 0.11414  0.02639  0.25527  200 TYR A CE1 
1538 C CE2 . TYR A 207 ? 0.63077 0.64721 0.78297 0.09910  0.03924  0.24392  200 TYR A CE2 
1539 C CZ  . TYR A 207 ? 0.61302 0.63865 0.80253 0.11148  0.04055  0.24953  200 TYR A CZ  
1540 O OH  . TYR A 207 ? 0.49760 0.50248 0.71771 0.12000  0.05675  0.24659  200 TYR A OH  
1541 N N   . ASN A 208 ? 0.37912 0.52607 0.45054 0.06855  -0.05743 0.25666  201 ASN A N   
1542 C CA  . ASN A 208 ? 0.37729 0.53907 0.42421 0.05418  -0.07182 0.24409  201 ASN A CA  
1543 C C   . ASN A 208 ? 0.35438 0.49890 0.38809 0.04277  -0.05841 0.21919  201 ASN A C   
1544 O O   . ASN A 208 ? 0.33641 0.46504 0.38629 0.04602  -0.04129 0.21067  201 ASN A O   
1545 C CB  . ASN A 208 ? 0.44310 0.63884 0.52231 0.05416  -0.08797 0.24596  201 ASN A CB  
1546 C CG  . ASN A 208 ? 0.45589 0.66834 0.51300 0.03881  -0.10583 0.23446  201 ASN A CG  
1547 O OD1 . ASN A 208 ? 0.52400 0.72395 0.56084 0.02657  -0.09927 0.21477  201 ASN A OD1 
1548 N ND2 . ASN A 208 ? 0.53965 0.77788 0.60246 0.03891  -0.12781 0.24339  201 ASN A ND2 
1549 N N   . GLN A 209 ? 0.39030 0.53746 0.39384 0.02951  -0.06714 0.20713  202 GLN A N   
1550 C CA  . GLN A 209 ? 0.38955 0.52349 0.38556 0.01925  -0.05734 0.18487  202 GLN A CA  
1551 C C   . GLN A 209 ? 0.35705 0.50149 0.38680 0.01897  -0.05384 0.17706  202 GLN A C   
1552 O O   . GLN A 209 ? 0.29665 0.42609 0.32739 0.01590  -0.04125 0.16329  202 GLN A O   
1553 C CB  . GLN A 209 ? 0.40920 0.54549 0.37247 0.00562  -0.06802 0.17327  202 GLN A CB  
1554 C CG  . GLN A 209 ? 0.53179 0.66004 0.45624 0.00516  -0.07114 0.18065  202 GLN A CG  
1555 C CD  . GLN A 209 ? 0.57505 0.70223 0.46578 -0.00857 -0.07843 0.16466  202 GLN A CD  
1556 O OE1 . GLN A 209 ? 0.51713 0.66054 0.41382 -0.01720 -0.09208 0.15549  202 GLN A OE1 
1557 N NE2 . GLN A 209 ? 0.57150 0.67897 0.42911 -0.01099 -0.06791 0.16034  202 GLN A NE2 
1558 N N   . THR A 210 ? 0.34461 0.51536 0.40268 0.02252  -0.06450 0.18648  203 THR A N   
1559 C CA  . THR A 210 ? 0.34438 0.52759 0.43561 0.02164  -0.05919 0.18013  203 THR A CA  
1560 C C   . THR A 210 ? 0.33963 0.50809 0.44982 0.03182  -0.03896 0.17855  203 THR A C   
1561 O O   . THR A 210 ? 0.31972 0.49477 0.45176 0.03127  -0.03048 0.17202  203 THR A O   
1562 C CB  . THR A 210 ? 0.31648 0.53388 0.44019 0.02405  -0.07450 0.19167  203 THR A CB  
1563 O OG1 . THR A 210 ? 0.42319 0.64626 0.55933 0.03845  -0.07887 0.21125  203 THR A OG1 
1564 C CG2 . THR A 210 ? 0.35494 0.58840 0.46170 0.01058  -0.09560 0.18740  203 THR A CG2 
1565 N N   . VAL A 211 ? 0.32692 0.47516 0.42915 0.04045  -0.03020 0.18370  204 VAL A N   
1566 C CA  . VAL A 211 ? 0.30617 0.43652 0.42187 0.04765  -0.01127 0.17692  204 VAL A CA  
1567 C C   . VAL A 211 ? 0.28144 0.39804 0.38018 0.03811  -0.00339 0.15755  204 VAL A C   
1568 O O   . VAL A 211 ? 0.29631 0.40845 0.40713 0.04068  0.00872  0.14906  204 VAL A O   
1569 C CB  . VAL A 211 ? 0.37735 0.48608 0.48769 0.05600  -0.00381 0.18438  204 VAL A CB  
1570 C CG1 . VAL A 211 ? 0.31424 0.43535 0.43898 0.06622  -0.01285 0.20720  204 VAL A CG1 
1571 C CG2 . VAL A 211 ? 0.29565 0.38577 0.37023 0.04713  -0.00379 0.17728  204 VAL A CG2 
1572 N N   . ASP A 212 ? 0.26752 0.37677 0.33706 0.02750  -0.01000 0.15050  205 ASP A N   
1573 C CA  . ASP A 212 ? 0.26601 0.36346 0.32138 0.01899  -0.00516 0.13448  205 ASP A CA  
1574 C C   . ASP A 212 ? 0.30935 0.42330 0.37659 0.01284  -0.00761 0.13150  205 ASP A C   
1575 O O   . ASP A 212 ? 0.24545 0.35110 0.31029 0.01031  0.00093  0.12228  205 ASP A O   
1576 C CB  . ASP A 212 ? 0.32289 0.40863 0.34929 0.01032  -0.01069 0.12807  205 ASP A CB  
1577 C CG  . ASP A 212 ? 0.33934 0.40631 0.35548 0.01485  -0.00389 0.12900  205 ASP A CG  
1578 O OD1 . ASP A 212 ? 0.29384 0.35052 0.32317 0.02248  0.00632  0.12870  205 ASP A OD1 
1579 O OD2 . ASP A 212 ? 0.28005 0.34207 0.27563 0.01018  -0.00758 0.12910  205 ASP A OD2 
1580 N N   . ILE A 213 ? 0.32772 0.46521 0.40781 0.00991  -0.01950 0.13967  206 ILE A N   
1581 C CA  . ILE A 213 ? 0.27933 0.43451 0.37793 0.00314  -0.02068 0.13771  206 ILE A CA  
1582 C C   . ILE A 213 ? 0.31472 0.47446 0.43912 0.01150  -0.00530 0.13915  206 ILE A C   
1583 O O   . ILE A 213 ? 0.34670 0.50680 0.47514 0.00647  0.00356  0.13333  206 ILE A O   
1584 C CB  . ILE A 213 ? 0.31460 0.49712 0.42754 -0.00147 -0.03844 0.14575  206 ILE A CB  
1585 C CG1 . ILE A 213 ? 0.27573 0.45170 0.35736 -0.01189 -0.05204 0.13995  206 ILE A CG1 
1586 C CG2 . ILE A 213 ? 0.26107 0.46490 0.40399 -0.00803 -0.03768 0.14493  206 ILE A CG2 
1587 C CD1 . ILE A 213 ? 0.32504 0.48921 0.39360 -0.02486 -0.04984 0.12596  206 ILE A CD1 
1588 N N   . TRP A 214 ? 0.28436 0.44618 0.42597 0.02456  -0.00043 0.14712  207 TRP A N   
1589 C CA  . TRP A 214 ? 0.24831 0.41090 0.41279 0.03359  0.01695  0.14564  207 TRP A CA  
1590 C C   . TRP A 214 ? 0.30833 0.44551 0.44814 0.03179  0.03073  0.13144  207 TRP A C   
1591 O O   . TRP A 214 ? 0.25023 0.38892 0.39455 0.03083  0.04333  0.12594  207 TRP A O   
1592 C CB  . TRP A 214 ? 0.28965 0.45293 0.47583 0.04851  0.02007  0.15550  207 TRP A CB  
1593 C CG  . TRP A 214 ? 0.29996 0.46113 0.50971 0.05863  0.03986  0.15128  207 TRP A CG  
1594 C CD1 . TRP A 214 ? 0.26303 0.39921 0.45881 0.06259  0.05537  0.13880  207 TRP A CD1 
1595 C CD2 . TRP A 214 ? 0.33361 0.51910 0.58590 0.06592  0.04682  0.15781  207 TRP A CD2 
1596 N NE1 . TRP A 214 ? 0.27578 0.41718 0.49847 0.07181  0.07259  0.13602  207 TRP A NE1 
1597 C CE2 . TRP A 214 ? 0.33052 0.50228 0.59000 0.07449  0.06897  0.14804  207 TRP A CE2 
1598 C CE3 . TRP A 214 ? 0.27157 0.49028 0.55869 0.06590  0.03620  0.16999  207 TRP A CE3 
1599 C CZ2 . TRP A 214 ? 0.27359 0.46261 0.57366 0.08369  0.08361  0.15010  207 TRP A CZ2 
1600 C CZ3 . TRP A 214 ? 0.26140 0.49954 0.59342 0.07502  0.04922  0.17329  207 TRP A CZ3 
1601 C CH2 . TRP A 214 ? 0.27091 0.49363 0.60904 0.08416  0.07410  0.16343  207 TRP A CH2 
1602 N N   . SER A 215 ? 0.24852 0.36294 0.36202 0.03129  0.02845  0.12575  208 SER A N   
1603 C CA  . SER A 215 ? 0.29422 0.38629 0.38450 0.02926  0.03715  0.11212  208 SER A CA  
1604 C C   . SER A 215 ? 0.33115 0.42434 0.40668 0.01855  0.03588  0.10740  208 SER A C   
1605 O O   . SER A 215 ? 0.34270 0.42866 0.40960 0.01852  0.04657  0.10079  208 SER A O   
1606 C CB  . SER A 215 ? 0.33475 0.40663 0.40539 0.02877  0.03233  0.10761  208 SER A CB  
1607 O OG  . SER A 215 ? 0.33330 0.40191 0.41830 0.03795  0.03471  0.11414  208 SER A OG  
1608 N N   . VAL A 216 ? 0.34301 0.44373 0.41394 0.00925  0.02322  0.11079  209 VAL A N   
1609 C CA  . VAL A 216 ? 0.32720 0.42702 0.38817 -0.00140 0.02215  0.10753  209 VAL A CA  
1610 C C   . VAL A 216 ? 0.35995 0.47509 0.44094 -0.00190 0.03313  0.11140  209 VAL A C   
1611 O O   . VAL A 216 ? 0.31041 0.41695 0.37921 -0.00571 0.04202  0.10823  209 VAL A O   
1612 C CB  . VAL A 216 ? 0.44108 0.54716 0.49877 -0.01139 0.00712  0.10897  209 VAL A CB  
1613 C CG1 . VAL A 216 ? 0.29990 0.40617 0.35606 -0.02276 0.00708  0.10694  209 VAL A CG1 
1614 C CG2 . VAL A 216 ? 0.32406 0.41222 0.35867 -0.01149 0.00069  0.10345  209 VAL A CG2 
1615 N N   . GLY A 217 ? 0.32891 0.46739 0.44181 0.00234  0.03325  0.11940  210 GLY A N   
1616 C CA  . GLY A 217 ? 0.31254 0.46811 0.45107 0.00261  0.04639  0.12297  210 GLY A CA  
1617 C C   . GLY A 217 ? 0.31783 0.45965 0.44574 0.01018  0.06644  0.11678  210 GLY A C   
1618 O O   . GLY A 217 ? 0.34948 0.49365 0.47765 0.00659  0.08028  0.11646  210 GLY A O   
1619 N N   . CYS A 218 ? 0.31426 0.44075 0.43169 0.02013  0.06896  0.11132  211 CYS A N   
1620 C CA  . CYS A 218 ? 0.30194 0.41305 0.40468 0.02664  0.08630  0.10180  211 CYS A CA  
1621 C C   . CYS A 218 ? 0.36040 0.45118 0.42303 0.01939  0.08624  0.09459  211 CYS A C   
1622 O O   . CYS A 218 ? 0.34226 0.42642 0.38936 0.02022  0.10091  0.08987  211 CYS A O   
1623 C CB  . CYS A 218 ? 0.31112 0.40929 0.41541 0.03755  0.08733  0.09625  211 CYS A CB  
1624 S SG  . CYS A 218 ? 0.31931 0.43670 0.47211 0.05059  0.09374  0.10510  211 CYS A SG  
1625 N N   . ILE A 219 ? 0.36345 0.44397 0.40835 0.01289  0.07019  0.09410  212 ILE A N   
1626 C CA  . ILE A 219 ? 0.32763 0.38913 0.33841 0.00736  0.06762  0.08896  212 ILE A CA  
1627 C C   . ILE A 219 ? 0.34175 0.40919 0.35068 -0.00132 0.07325  0.09608  212 ILE A C   
1628 O O   . ILE A 219 ? 0.35414 0.41019 0.33879 -0.00214 0.08230  0.09470  212 ILE A O   
1629 C CB  . ILE A 219 ? 0.38699 0.43725 0.38636 0.00365  0.05056  0.08650  212 ILE A CB  
1630 C CG1 . ILE A 219 ? 0.35617 0.39756 0.35630 0.01148  0.04815  0.07958  212 ILE A CG1 
1631 C CG2 . ILE A 219 ? 0.40168 0.43493 0.37273 -0.00168 0.04611  0.08367  212 ILE A CG2 
1632 C CD1 . ILE A 219 ? 0.35208 0.38269 0.34286 0.00820  0.03497  0.07655  212 ILE A CD1 
1633 N N   . MET A 220 ? 0.30920 0.39419 0.34328 -0.00840 0.06777  0.10407  213 MET A N   
1634 C CA  . MET A 220 ? 0.35355 0.44397 0.39218 -0.01848 0.07335  0.11106  213 MET A CA  
1635 C C   . MET A 220 ? 0.38887 0.48640 0.43262 -0.01555 0.09557  0.11386  213 MET A C   
1636 O O   . MET A 220 ? 0.33302 0.42247 0.36073 -0.02130 0.10560  0.11818  213 MET A O   
1637 C CB  . MET A 220 ? 0.35535 0.46650 0.42602 -0.02682 0.06267  0.11654  213 MET A CB  
1638 C CG  . MET A 220 ? 0.31426 0.43686 0.40381 -0.03773 0.07089  0.12382  213 MET A CG  
1639 S SD  . MET A 220 ? 0.35509 0.49728 0.47630 -0.05051 0.05241  0.12573  213 MET A SD  
1640 C CE  . MET A 220 ? 0.32439 0.47493 0.46836 -0.06398 0.06676  0.13350  213 MET A CE  
1641 N N   . ALA A 221 ? 0.37534 0.48698 0.44154 -0.00620 0.10500  0.11210  214 ALA A N   
1642 C CA  . ALA A 221 ? 0.39706 0.51631 0.47071 -0.00248 0.12925  0.11300  214 ALA A CA  
1643 C C   . ALA A 221 ? 0.36171 0.45625 0.38853 0.00098  0.14043  0.10571  214 ALA A C   
1644 O O   . ALA A 221 ? 0.41167 0.50487 0.42622 -0.00157 0.15919  0.10901  214 ALA A O   
1645 C CB  . ALA A 221 ? 0.32296 0.46023 0.43278 0.00877  0.13655  0.11132  214 ALA A CB  
1646 N N   . GLU A 222 ? 0.39315 0.46853 0.39308 0.00642  0.12909  0.09585  215 GLU A N   
1647 C CA  . GLU A 222 ? 0.46432 0.51702 0.41790 0.00908  0.13444  0.08767  215 GLU A CA  
1648 C C   . GLU A 222 ? 0.45934 0.50005 0.38374 -0.00008 0.13047  0.09618  215 GLU A C   
1649 O O   . GLU A 222 ? 0.47186 0.50338 0.36572 -0.00052 0.14442  0.09788  215 GLU A O   
1650 C CB  . GLU A 222 ? 0.40928 0.44654 0.34823 0.01508  0.11975  0.07527  215 GLU A CB  
1651 C CG  . GLU A 222 ? 0.52736 0.54694 0.42961 0.02105  0.12727  0.06145  215 GLU A CG  
1652 C CD  . GLU A 222 ? 0.66384 0.67295 0.56740 0.02707  0.11613  0.04770  215 GLU A CD  
1653 O OE1 . GLU A 222 ? 0.72697 0.71881 0.59773 0.02734  0.10721  0.03753  215 GLU A OE1 
1654 O OE2 . GLU A 222 ? 0.54418 0.56261 0.48311 0.03136  0.11576  0.04789  215 GLU A OE2 
1655 N N   . LEU A 223 ? 0.43266 0.47201 0.36512 -0.00716 0.11231  0.10198  216 LEU A N   
1656 C CA  . LEU A 223 ? 0.51049 0.53595 0.42003 -0.01514 0.10767  0.11079  216 LEU A CA  
1657 C C   . LEU A 223 ? 0.45888 0.49169 0.37447 -0.02200 0.12711  0.12307  216 LEU A C   
1658 O O   . LEU A 223 ? 0.50974 0.52685 0.39424 -0.02537 0.13228  0.13095  216 LEU A O   
1659 C CB  . LEU A 223 ? 0.50667 0.53103 0.43198 -0.02160 0.08767  0.11305  216 LEU A CB  
1660 C CG  . LEU A 223 ? 0.51603 0.53386 0.43891 -0.01623 0.07018  0.10247  216 LEU A CG  
1661 C CD1 . LEU A 223 ? 0.43202 0.44590 0.36438 -0.02325 0.05414  0.10452  216 LEU A CD1 
1662 C CD2 . LEU A 223 ? 0.51209 0.51128 0.39899 -0.00937 0.06684  0.09462  216 LEU A CD2 
1663 N N   . LEU A 224 ? 0.41632 0.47328 0.37330 -0.02407 0.13808  0.12605  217 LEU A N   
1664 C CA  . LEU A 224 ? 0.41935 0.48640 0.39098 -0.03190 0.15806  0.13776  217 LEU A CA  
1665 C C   . LEU A 224 ? 0.47654 0.54103 0.42512 -0.02574 0.18436  0.13665  217 LEU A C   
1666 O O   . LEU A 224 ? 0.56718 0.62317 0.49476 -0.03117 0.20033  0.14693  217 LEU A O   
1667 C CB  . LEU A 224 ? 0.41041 0.50764 0.44034 -0.03675 0.15838  0.14076  217 LEU A CB  
1668 C CG  . LEU A 224 ? 0.44191 0.54379 0.49507 -0.04690 0.13643  0.14327  217 LEU A CG  
1669 C CD1 . LEU A 224 ? 0.34553 0.47899 0.45080 -0.04763 0.13088  0.14238  217 LEU A CD1 
1670 C CD2 . LEU A 224 ? 0.42871 0.52152 0.48070 -0.06049 0.14126  0.15427  217 LEU A CD2 
1671 N N   . THR A 225 ? 0.45440 0.52455 0.40551 -0.01450 0.19053  0.12429  218 THR A N   
1672 C CA  . THR A 225 ? 0.49557 0.56505 0.42894 -0.00823 0.21812  0.11994  218 THR A CA  
1673 C C   . THR A 225 ? 0.51862 0.56107 0.38900 -0.00237 0.21680  0.11051  218 THR A C   
1674 O O   . THR A 225 ? 0.56064 0.59563 0.39782 -0.00096 0.23900  0.11057  218 THR A O   
1675 C CB  . THR A 225 ? 0.50252 0.59213 0.47679 0.00145  0.22816  0.11041  218 THR A CB  
1676 O OG1 . THR A 225 ? 0.44704 0.52976 0.42109 0.00889  0.20715  0.09904  218 THR A OG1 
1677 C CG2 . THR A 225 ? 0.44414 0.56458 0.48200 -0.00386 0.23089  0.12070  218 THR A CG2 
1678 N N   . GLY A 226 ? 0.71451 0.42599 0.43213 0.02954  0.02629  0.08740  219 GLY A N   
1679 C CA  . GLY A 226 ? 0.72711 0.43229 0.46000 0.06484  0.02692  0.06466  219 GLY A CA  
1680 C C   . GLY A 226 ? 0.74206 0.50305 0.52465 0.09292  0.04314  0.05041  219 GLY A C   
1681 O O   . GLY A 226 ? 0.77466 0.53487 0.56740 0.12055  0.04013  0.03508  219 GLY A O   
1682 N N   . ARG A 227 ? 0.71482 0.51806 0.52494 0.08702  0.05635  0.05483  220 ARG A N   
1683 C CA  . ARG A 227 ? 0.64759 0.49752 0.49872 0.11285  0.06692  0.04227  220 ARG A CA  
1684 C C   . ARG A 227 ? 0.60786 0.45996 0.49035 0.11041  0.07500  0.03498  220 ARG A C   
1685 O O   . ARG A 227 ? 0.63998 0.47404 0.50957 0.08646  0.07602  0.04465  220 ARG A O   
1686 C CB  . ARG A 227 ? 0.67273 0.59075 0.52046 0.11227  0.07497  0.05957  220 ARG A CB  
1687 C CG  . ARG A 227 ? 0.81244 0.73980 0.61966 0.09347  0.07039  0.08362  220 ARG A CG  
1688 C CD  . ARG A 227 ? 0.81973 0.82062 0.62555 0.07291  0.08081  0.11343  220 ARG A CD  
1689 N NE  . ARG A 227 ? 0.93523 1.00240 0.76269 0.10581  0.09282  0.10680  220 ARG A NE  
1690 C CZ  . ARG A 227 ? 0.97514 1.07423 0.78765 0.13248  0.09495  0.10639  220 ARG A CZ  
1691 N NH1 . ARG A 227 ? 0.91663 0.99047 0.69556 0.12758  0.08715  0.11362  220 ARG A NH1 
1692 N NH2 . ARG A 227 ? 0.90385 1.05776 0.73043 0.16744  0.10334  0.09776  220 ARG A NH2 
1693 N N   . THR A 228 ? 0.66836 0.53812 0.58826 0.13511  0.07781  0.01860  221 THR A N   
1694 C CA  . THR A 228 ? 0.58345 0.46110 0.53382 0.13236  0.08517  0.01420  221 THR A CA  
1695 C C   . THR A 228 ? 0.49448 0.41704 0.44310 0.11601  0.09363  0.03067  221 THR A C   
1696 O O   . THR A 228 ? 0.43660 0.40403 0.38365 0.12548  0.09512  0.03656  221 THR A O   
1697 C CB  . THR A 228 ? 0.49624 0.37910 0.48484 0.15911  0.08032  -0.00362 221 THR A CB  
1698 O OG1 . THR A 228 ? 0.54163 0.39413 0.53812 0.16737  0.06808  -0.01633 221 THR A OG1 
1699 C CG2 . THR A 228 ? 0.51319 0.40233 0.53171 0.15279  0.08677  -0.00504 221 THR A CG2 
1700 N N   . LEU A 229 ? 0.47393 0.38616 0.42101 0.09401  0.09863  0.03820  222 LEU A N   
1701 C CA  . LEU A 229 ? 0.51295 0.46671 0.46042 0.07618  0.10438  0.05506  222 LEU A CA  
1702 C C   . LEU A 229 ? 0.50777 0.50250 0.48789 0.09737  0.10805  0.04631  222 LEU A C   
1703 O O   . LEU A 229 ? 0.47613 0.52292 0.45685 0.10301  0.11040  0.05529  222 LEU A O   
1704 C CB  . LEU A 229 ? 0.48409 0.40723 0.41899 0.05032  0.10522  0.06258  222 LEU A CB  
1705 C CG  . LEU A 229 ? 0.42176 0.38309 0.35721 0.02805  0.10793  0.08161  222 LEU A CG  
1706 C CD1 . LEU A 229 ? 0.49891 0.50247 0.41797 0.01188  0.10471  0.10543  222 LEU A CD1 
1707 C CD2 . LEU A 229 ? 0.42209 0.34006 0.33710 0.00431  0.10466  0.08718  222 LEU A CD2 
1708 N N   . PHE A 230 ? 0.54115 0.51427 0.54719 0.11019  0.10698  0.03010  223 PHE A N   
1709 C CA  . PHE A 230 ? 0.36089 0.35763 0.39401 0.12880  0.10400  0.02112  223 PHE A CA  
1710 C C   . PHE A 230 ? 0.45179 0.42505 0.50346 0.15380  0.09252  0.00315  223 PHE A C   
1711 O O   . PHE A 230 ? 0.51410 0.46535 0.58902 0.15080  0.08865  -0.00348 223 PHE A O   
1712 C CB  . PHE A 230 ? 0.41420 0.40665 0.46158 0.11360  0.10890  0.02415  223 PHE A CB  
1713 C CG  . PHE A 230 ? 0.39828 0.40491 0.42677 0.08636  0.11598  0.04218  223 PHE A CG  
1714 C CD1 . PHE A 230 ? 0.39742 0.45463 0.42065 0.08425  0.11682  0.05495  223 PHE A CD1 
1715 C CD2 . PHE A 230 ? 0.36341 0.33417 0.37821 0.06445  0.12003  0.04724  223 PHE A CD2 
1716 C CE1 . PHE A 230 ? 0.38685 0.45948 0.39677 0.05531  0.11962  0.07501  223 PHE A CE1 
1717 C CE2 . PHE A 230 ? 0.57475 0.55002 0.56853 0.03788  0.12070  0.06440  223 PHE A CE2 
1718 C CZ  . PHE A 230 ? 0.45021 0.47693 0.44426 0.03056  0.11951  0.07957  223 PHE A CZ  
1719 N N   . PRO A 231 ? 0.48678 0.46650 0.52769 0.17591  0.08407  -0.00327 224 PRO A N   
1720 C CA  . PRO A 231 ? 0.54638 0.50574 0.60447 0.17804  0.05919  -0.02050 224 PRO A CA  
1721 C C   . PRO A 231 ? 0.48350 0.45177 0.55858 0.18287  0.04330  -0.02809 224 PRO A C   
1722 O O   . PRO A 231 ? 0.56180 0.53086 0.62659 0.19535  0.03078  -0.03339 224 PRO A O   
1723 C CB  . PRO A 231 ? 0.53739 0.49577 0.56880 0.19148  0.05676  -0.02110 224 PRO A CB  
1724 C CG  . PRO A 231 ? 0.48600 0.48620 0.49036 0.20577  0.07392  -0.00718 224 PRO A CG  
1725 C CD  . PRO A 231 ? 0.52212 0.53386 0.53377 0.17856  0.08852  0.00693  224 PRO A CD  
1726 N N   . GLY A 232 ? 0.52107 0.49026 0.61512 0.17447  0.04412  -0.02675 225 GLY A N   
1727 C CA  . GLY A 232 ? 0.59835 0.56804 0.70379 0.17994  0.03034  -0.03016 225 GLY A CA  
1728 C C   . GLY A 232 ? 0.66730 0.60841 0.78860 0.17827  0.01608  -0.03015 225 GLY A C   
1729 O O   . GLY A 232 ? 0.67702 0.60155 0.81168 0.16931  0.02087  -0.02454 225 GLY A O   
1730 N N   . THR A 233 ? 0.62464 0.56097 0.73006 0.19073  -0.00089 -0.03393 226 THR A N   
1731 C CA  . THR A 233 ? 0.62543 0.53415 0.72946 0.19215  -0.02047 -0.03484 226 THR A CA  
1732 C C   . THR A 233 ? 0.61233 0.50537 0.73257 0.18263  -0.02719 -0.02764 226 THR A C   
1733 O O   . THR A 233 ? 0.64275 0.51556 0.76893 0.17828  -0.04487 -0.02761 226 THR A O   
1734 C CB  . THR A 233 ? 0.72292 0.62693 0.79527 0.21135  -0.04325 -0.04732 226 THR A CB  
1735 O OG1 . THR A 233 ? 0.66864 0.59013 0.72916 0.22106  -0.04292 -0.05013 226 THR A OG1 
1736 C CG2 . THR A 233 ? 0.73747 0.64989 0.78430 0.22419  -0.04204 -0.05419 226 THR A CG2 
1737 N N   . ASP A 234 ? 0.57372 0.47649 0.70137 0.17896  -0.01789 -0.02298 227 ASP A N   
1738 C CA  . ASP A 234 ? 0.56082 0.44891 0.70171 0.16932  -0.02888 -0.01812 227 ASP A CA  
1739 C C   . ASP A 234 ? 0.57701 0.48030 0.72216 0.16543  -0.01156 -0.01383 227 ASP A C   
1740 O O   . ASP A 234 ? 0.60841 0.53199 0.74434 0.16978  0.00984  -0.01342 227 ASP A O   
1741 C CB  . ASP A 234 ? 0.51916 0.38569 0.65397 0.17344  -0.06192 -0.02442 227 ASP A CB  
1742 C CG  . ASP A 234 ? 0.51450 0.39032 0.62255 0.19134  -0.06694 -0.03453 227 ASP A CG  
1743 O OD1 . ASP A 234 ? 0.52396 0.41413 0.63159 0.19378  -0.05904 -0.03312 227 ASP A OD1 
1744 O OD2 . ASP A 234 ? 0.63589 0.50612 0.72120 0.20445  -0.08025 -0.04499 227 ASP A OD2 
1745 N N   . HIS A 235 ? 0.58143 0.47427 0.74428 0.15507  -0.02384 -0.01039 228 HIS A N   
1746 C CA  . HIS A 235 ? 0.60514 0.51078 0.78416 0.14432  -0.00750 -0.00494 228 HIS A CA  
1747 C C   . HIS A 235 ? 0.55468 0.47527 0.71343 0.16055  -0.00523 -0.00973 228 HIS A C   
1748 O O   . HIS A 235 ? 0.57510 0.51895 0.74022 0.15558  0.01781  -0.00604 228 HIS A O   
1749 C CB  . HIS A 235 ? 0.51079 0.40133 0.72606 0.12366  -0.01660 0.00781  228 HIS A CB  
1750 C CG  . HIS A 235 ? 0.62434 0.52087 0.87578 0.10597  -0.00234 0.02023  228 HIS A CG  
1751 N ND1 . HIS A 235 ? 0.50715 0.41134 0.78450 0.08401  0.01323  0.03817  228 HIS A ND1 
1752 C CD2 . HIS A 235 ? 0.55612 0.45804 0.81253 0.10730  0.00006  0.01780  228 HIS A CD2 
1753 C CE1 . HIS A 235 ? 0.47565 0.39374 0.77818 0.07666  0.02609  0.04659  228 HIS A CE1 
1754 N NE2 . HIS A 235 ? 0.45950 0.37338 0.75797 0.09229  0.01729  0.03439  228 HIS A NE2 
1755 N N   . ILE A 236 ? 0.49301 0.40609 0.63547 0.17397  -0.02583 -0.01524 229 ILE A N   
1756 C CA  . ILE A 236 ? 0.60139 0.53936 0.72931 0.18844  -0.02519 -0.02093 229 ILE A CA  
1757 C C   . ILE A 236 ? 0.53676 0.51001 0.65266 0.19757  -0.00956 -0.02549 229 ILE A C   
1758 O O   . ILE A 236 ? 0.54235 0.55214 0.65256 0.20057  0.00681  -0.02259 229 ILE A O   
1759 C CB  . ILE A 236 ? 0.66391 0.58230 0.76981 0.20086  -0.05571 -0.02983 229 ILE A CB  
1760 C CG1 . ILE A 236 ? 0.68387 0.58163 0.77469 0.20686  -0.07365 -0.03791 229 ILE A CG1 
1761 C CG2 . ILE A 236 ? 0.62468 0.51168 0.74036 0.18855  -0.07394 -0.02451 229 ILE A CG2 
1762 C CD1 . ILE A 236 ? 0.67956 0.59749 0.73874 0.23007  -0.07576 -0.05034 229 ILE A CD1 
1763 N N   . ASP A 237 ? 0.45022 0.41475 0.55685 0.20176  -0.01521 -0.03037 230 ASP A N   
1764 C CA  . ASP A 237 ? 0.52295 0.51690 0.61372 0.20957  -0.00240 -0.03305 230 ASP A CA  
1765 C C   . ASP A 237 ? 0.54038 0.55230 0.64264 0.19568  0.02255  -0.02485 230 ASP A C   
1766 O O   . ASP A 237 ? 0.60220 0.65126 0.68772 0.20080  0.03821  -0.01911 230 ASP A O   
1767 C CB  . ASP A 237 ? 0.48000 0.45381 0.55948 0.21494  -0.01397 -0.03915 230 ASP A CB  
1768 C CG  . ASP A 237 ? 0.60231 0.60336 0.66043 0.22496  -0.00255 -0.04057 230 ASP A CG  
1769 O OD1 . ASP A 237 ? 0.54209 0.57662 0.57437 0.24313  -0.00011 -0.04176 230 ASP A OD1 
1770 O OD2 . ASP A 237 ? 0.63870 0.62998 0.70403 0.21611  0.00405  -0.03883 230 ASP A OD2 
1771 N N   . GLN A 238 ? 0.47762 0.46584 0.60307 0.17916  0.02699  -0.02153 231 GLN A N   
1772 C CA  . GLN A 238 ? 0.53666 0.53290 0.65900 0.16563  0.05308  -0.01052 231 GLN A CA  
1773 C C   . GLN A 238 ? 0.51542 0.53880 0.63154 0.15683  0.07010  0.00227  231 GLN A C   
1774 O O   . GLN A 238 ? 0.41968 0.46798 0.52043 0.14567  0.08494  0.01221  231 GLN A O   
1775 C CB  . GLN A 238 ? 0.55262 0.51948 0.69393 0.14766  0.05542  -0.00690 231 GLN A CB  
1776 C CG  . GLN A 238 ? 0.54751 0.51039 0.68511 0.13195  0.08047  0.00212  231 GLN A CG  
1777 C CD  . GLN A 238 ? 0.54322 0.50018 0.66862 0.13710  0.07555  -0.00452 231 GLN A CD  
1778 O OE1 . GLN A 238 ? 0.52687 0.47838 0.65435 0.14778  0.05271  -0.01613 231 GLN A OE1 
1779 N NE2 . GLN A 238 ? 0.56717 0.51917 0.67745 0.13065  0.09511  0.00263  231 GLN A NE2 
1780 N N   . LEU A 239 ? 0.47096 0.48854 0.59617 0.15332  0.06181  0.00273  232 LEU A N   
1781 C CA  . LEU A 239 ? 0.51468 0.55713 0.63255 0.13910  0.07098  0.01302  232 LEU A CA  
1782 C C   . LEU A 239 ? 0.52822 0.62132 0.63238 0.15719  0.07201  0.01474  232 LEU A C   
1783 O O   . LEU A 239 ? 0.55688 0.68186 0.65509 0.13997  0.08370  0.02877  232 LEU A O   
1784 C CB  . LEU A 239 ? 0.55372 0.57803 0.68136 0.13667  0.05753  0.01161  232 LEU A CB  
1785 C CG  . LEU A 239 ? 0.56956 0.55713 0.71219 0.11415  0.06017  0.01669  232 LEU A CG  
1786 C CD1 . LEU A 239 ? 0.66820 0.63571 0.81958 0.11526  0.03953  0.01568  232 LEU A CD1 
1787 C CD2 . LEU A 239 ? 0.50518 0.49284 0.63814 0.08633  0.08307  0.02905  232 LEU A CD2 
1788 N N   . LYS A 240 ? 0.42155 0.52498 0.51946 0.19258  0.05880  0.00213  233 LYS A N   
1789 C CA  . LYS A 240 ? 0.47142 0.62763 0.55240 0.20717  0.06000  0.00465  233 LYS A CA  
1790 C C   . LYS A 240 ? 0.57964 0.77095 0.65420 0.19784  0.08099  0.01954  233 LYS A C   
1791 O O   . LYS A 240 ? 0.51920 0.76969 0.59030 0.19321  0.09248  0.03589  233 LYS A O   
1792 C CB  . LYS A 240 ? 0.54060 0.67935 0.60239 0.22991  0.03613  -0.01270 233 LYS A CB  
1793 C CG  . LYS A 240 ? 0.65522 0.84018 0.69182 0.24719  0.04101  -0.00948 233 LYS A CG  
1794 C CD  . LYS A 240 ? 0.76292 0.91521 0.77914 0.26158  0.02611  -0.02323 233 LYS A CD  
1795 C CE  . LYS A 240 ? 0.72770 0.92482 0.71066 0.28728  0.02733  -0.02186 233 LYS A CE  
1796 N NZ  . LYS A 240 ? 0.79222 0.95332 0.74813 0.30554  0.00904  -0.03750 233 LYS A NZ  
1797 N N   . LEU A 241 ? 0.45898 0.61499 0.53196 0.19142  0.08399  0.01629  234 LEU A N   
1798 C CA  . LEU A 241 ? 0.43287 0.60576 0.49287 0.17326  0.09814  0.03075  234 LEU A CA  
1799 C C   . LEU A 241 ? 0.47597 0.64851 0.53515 0.13134  0.10922  0.05018  234 LEU A C   
1800 O O   . LEU A 241 ? 0.49942 0.70913 0.54751 0.11373  0.11680  0.07000  234 LEU A O   
1801 C CB  . LEU A 241 ? 0.45879 0.58493 0.51506 0.17626  0.09468  0.02055  234 LEU A CB  
1802 C CG  . LEU A 241 ? 0.50263 0.60837 0.55380 0.20325  0.07375  0.00065  234 LEU A CG  
1803 C CD1 . LEU A 241 ? 0.37995 0.44792 0.42832 0.20022  0.07048  -0.00541 234 LEU A CD1 
1804 C CD2 . LEU A 241 ? 0.49293 0.64342 0.52167 0.22402  0.06980  0.00171  234 LEU A CD2 
1805 N N   . ILE A 242 ? 0.43081 0.56079 0.49902 0.11445  0.10823  0.04657  235 ILE A N   
1806 C CA  . ILE A 242 ? 0.38447 0.50429 0.44426 0.07875  0.11517  0.06248  235 ILE A CA  
1807 C C   . ILE A 242 ? 0.54240 0.71654 0.60401 0.07085  0.11548  0.07824  235 ILE A C   
1808 O O   . ILE A 242 ? 0.49002 0.68131 0.53973 0.04301  0.11839  0.09907  235 ILE A O   
1809 C CB  . ILE A 242 ? 0.40218 0.47225 0.46900 0.06926  0.11505  0.05475  235 ILE A CB  
1810 C CG1 . ILE A 242 ? 0.47398 0.50009 0.53959 0.07172  0.11741  0.04535  235 ILE A CG1 
1811 C CG2 . ILE A 242 ? 0.36242 0.42262 0.41524 0.03887  0.11887  0.06917  235 ILE A CG2 
1812 C CD1 . ILE A 242 ? 0.40177 0.39669 0.48484 0.07359  0.11688  0.03696  235 ILE A CD1 
1813 N N   . LEU A 243 ? 0.49161 0.69259 0.56745 0.09524  0.10920  0.06956  236 LEU A N   
1814 C CA  . LEU A 243 ? 0.46299 0.72181 0.54433 0.09250  0.10878  0.08356  236 LEU A CA  
1815 C C   . LEU A 243 ? 0.48288 0.81145 0.56029 0.09313  0.11552  0.10237  236 LEU A C   
1816 O O   . LEU A 243 ? 0.49172 0.86794 0.57322 0.07131  0.11752  0.12552  236 LEU A O   
1817 C CB  . LEU A 243 ? 0.49675 0.76771 0.58894 0.12699  0.09757  0.06729  236 LEU A CB  
1818 C CG  . LEU A 243 ? 0.51711 0.73469 0.61491 0.11812  0.08905  0.05801  236 LEU A CG  
1819 C CD1 . LEU A 243 ? 0.57885 0.78599 0.68078 0.15558  0.07119  0.03794  236 LEU A CD1 
1820 C CD2 . LEU A 243 ? 0.54223 0.77510 0.64112 0.09121  0.09051  0.07410  236 LEU A CD2 
1821 N N   . ARG A 244 ? 0.39967 0.73771 0.46940 0.11637  0.11805  0.09530  237 ARG A N   
1822 C CA  . ARG A 244 ? 0.50171 0.91019 0.56559 0.11713  0.12557  0.11572  237 ARG A CA  
1823 C C   . ARG A 244 ? 0.50699 0.91157 0.56155 0.06712  0.12888  0.14406  237 ARG A C   
1824 O O   . ARG A 244 ? 0.42749 0.87839 0.48401 0.04765  0.12274  0.16580  237 ARG A O   
1825 C CB  . ARG A 244 ? 0.47598 0.87601 0.52499 0.14940  0.12341  0.10030  237 ARG A CB  
1826 C CG  . ARG A 244 ? 0.64448 1.08524 0.67962 0.13634  0.12769  0.12222  237 ARG A CG  
1827 C CD  . ARG A 244 ? 0.75402 1.16290 0.77143 0.15325  0.13023  0.11054  237 ARG A CD  
1828 N NE  . ARG A 244 ? 0.94793 1.34172 0.95628 0.19982  0.11814  0.08329  237 ARG A NE  
1829 C CZ  . ARG A 244 ? 0.91685 1.28683 0.90628 0.22121  0.11400  0.07129  237 ARG A CZ  
1830 N NH1 . ARG A 244 ? 0.67018 1.03504 0.64986 0.20587  0.12473  0.08288  237 ARG A NH1 
1831 N NH2 . ARG A 244 ? 0.76299 1.10741 0.73671 0.25540  0.09639  0.04801  237 ARG A NH2 
1832 N N   . LEU A 245 ? 0.43945 0.76572 0.47950 0.04540  0.12605  0.13777  238 LEU A N   
1833 C CA  . LEU A 245 ? 0.49084 0.79605 0.51151 0.00076  0.12262  0.16187  238 LEU A CA  
1834 C C   . LEU A 245 ? 0.49011 0.78695 0.51196 -0.03259 0.11580  0.17702  238 LEU A C   
1835 O O   . LEU A 245 ? 0.51947 0.83798 0.53831 -0.06054 0.10339  0.19669  238 LEU A O   
1836 C CB  . LEU A 245 ? 0.55523 0.77653 0.55420 -0.00382 0.11957  0.14704  238 LEU A CB  
1837 C CG  . LEU A 245 ? 0.50464 0.67852 0.47341 -0.04650 0.10972  0.16602  238 LEU A CG  
1838 C CD1 . LEU A 245 ? 0.55362 0.77380 0.51048 -0.06961 0.10533  0.19699  238 LEU A CD1 
1839 C CD2 . LEU A 245 ? 0.49375 0.58336 0.44098 -0.04164 0.10677  0.14608  238 LEU A CD2 
1840 N N   . VAL A 246 ? 0.39101 0.63754 0.41622 -0.02734 0.11416  0.15786  239 VAL A N   
1841 C CA  . VAL A 246 ? 0.46366 0.68632 0.48170 -0.05793 0.10619  0.16942  239 VAL A CA  
1842 C C   . VAL A 246 ? 0.51174 0.79863 0.55473 -0.05383 0.10482  0.17839  239 VAL A C   
1843 O O   . VAL A 246 ? 0.50908 0.78403 0.54649 -0.08106 0.09315  0.19004  239 VAL A O   
1844 C CB  . VAL A 246 ? 0.54657 0.68752 0.55229 -0.05472 0.10635  0.14745  239 VAL A CB  
1845 C CG1 . VAL A 246 ? 0.53632 0.61664 0.51661 -0.05681 0.10683  0.13926  239 VAL A CG1 
1846 C CG2 . VAL A 246 ? 0.51626 0.66369 0.54716 -0.02008 0.11194  0.12391  239 VAL A CG2 
1847 N N   . GLY A 247 ? 0.54361 0.88759 0.60944 -0.01632 0.11095  0.16775  240 GLY A N   
1848 C CA  . GLY A 247 ? 0.50872 0.91642 0.59662 -0.00501 0.10850  0.17389  240 GLY A CA  
1849 C C   . GLY A 247 ? 0.52769 0.89452 0.62125 0.01425  0.10365  0.14968  240 GLY A C   
1850 O O   . GLY A 247 ? 0.58808 0.87893 0.66978 0.00880  0.10278  0.13425  240 GLY A O   
1851 N N   . THR A 248 ? 0.61435 1.03662 0.72574 0.03807  0.09975  0.14807  241 THR A N   
1852 C CA  . THR A 248 ? 0.52614 0.91150 0.64074 0.05615  0.09088  0.12740  241 THR A CA  
1853 C C   . THR A 248 ? 0.48886 0.81848 0.59353 0.01842  0.08591  0.13439  241 THR A C   
1854 O O   . THR A 248 ? 0.35174 0.69551 0.45223 -0.01612 0.08397  0.15794  241 THR A O   
1855 C CB  . THR A 248 ? 0.59359 1.04981 0.72425 0.08936  0.08432  0.12601  241 THR A CB  
1856 O OG1 . THR A 248 ? 0.67339 1.20466 0.80941 0.11773  0.09209  0.13074  241 THR A OG1 
1857 C CG2 . THR A 248 ? 0.58373 0.99474 0.71109 0.12263  0.07117  0.09781  241 THR A CG2 
1858 N N   . PRO A 249 ? 0.50194 0.76682 0.60012 0.02360  0.08182  0.11607  242 PRO A N   
1859 C CA  . PRO A 249 ? 0.50946 0.71973 0.59196 -0.00797 0.07882  0.12183  242 PRO A CA  
1860 C C   . PRO A 249 ? 0.60209 0.84725 0.69031 -0.02065 0.06837  0.13673  242 PRO A C   
1861 O O   . PRO A 249 ? 0.45430 0.75011 0.56064 0.00427  0.06154  0.13345  242 PRO A O   
1862 C CB  . PRO A 249 ? 0.47983 0.63383 0.56043 0.00695  0.07680  0.10123  242 PRO A CB  
1863 C CG  . PRO A 249 ? 0.56983 0.73217 0.66126 0.03751  0.07863  0.08596  242 PRO A CG  
1864 C CD  . PRO A 249 ? 0.49151 0.72849 0.59385 0.05698  0.07776  0.09161  242 PRO A CD  
1865 N N   . GLY A 250 ? 0.68096 0.89562 0.75049 -0.05751 0.06454  0.15258  243 GLY A N   
1866 C CA  . GLY A 250 ? 0.49267 0.73344 0.56628 -0.07478 0.05146  0.16887  243 GLY A CA  
1867 C C   . GLY A 250 ? 0.63593 0.84178 0.70582 -0.06472 0.04344  0.15536  243 GLY A C   
1868 O O   . GLY A 250 ? 0.55780 0.71173 0.61872 -0.05144 0.04772  0.13669  243 GLY A O   
1869 N N   . ALA A 251 ? 0.55704 0.79481 0.63510 -0.07339 0.02979  0.16782  244 ALA A N   
1870 C CA  . ALA A 251 ? 0.59588 0.80275 0.66874 -0.06444 0.01882  0.15687  244 ALA A CA  
1871 C C   . ALA A 251 ? 0.64798 0.76330 0.68481 -0.08595 0.02019  0.15238  244 ALA A C   
1872 O O   . ALA A 251 ? 0.51566 0.59071 0.54474 -0.07424 0.01793  0.13855  244 ALA A O   
1873 C CB  . ALA A 251 ? 0.52635 0.78663 0.61449 -0.07146 0.00252  0.17308  244 ALA A CB  
1874 N N   . GLU A 252 ? 0.66682 0.74744 0.67769 -0.11613 0.02219  0.16484  245 GLU A N   
1875 C CA  . GLU A 252 ? 0.66162 0.65778 0.63134 -0.13034 0.02467  0.15996  245 GLU A CA  
1876 C C   . GLU A 252 ? 0.62434 0.58570 0.58886 -0.11335 0.04318  0.14296  245 GLU A C   
1877 O O   . GLU A 252 ? 0.65497 0.56055 0.59377 -0.11505 0.04853  0.13673  245 GLU A O   
1878 C CB  . GLU A 252 ? 0.63310 0.59491 0.56819 -0.16281 0.01613  0.17659  245 GLU A CB  
1879 C CG  . GLU A 252 ? 0.71308 0.65056 0.63168 -0.16443 0.02730  0.17367  245 GLU A CG  
1880 C CD  . GLU A 252 ? 0.71133 0.71525 0.65933 -0.16754 0.02702  0.18606  245 GLU A CD  
1881 O OE1 . GLU A 252 ? 0.75235 0.74309 0.69317 -0.16203 0.03621  0.17949  245 GLU A OE1 
1882 O OE2 . GLU A 252 ? 0.72237 0.79533 0.70128 -0.17191 0.01774  0.20101  245 GLU A OE2 
1883 N N   . LEU A 253 ? 0.57547 0.57213 0.56408 -0.09681 0.05280  0.13703  246 LEU A N   
1884 C CA  . LEU A 253 ? 0.56432 0.53493 0.55526 -0.08001 0.06716  0.12198  246 LEU A CA  
1885 C C   . LEU A 253 ? 0.48428 0.46534 0.49888 -0.05671 0.06257  0.10965  246 LEU A C   
1886 O O   . LEU A 253 ? 0.48360 0.42930 0.49519 -0.05195 0.06833  0.10223  246 LEU A O   
1887 C CB  . LEU A 253 ? 0.53825 0.53281 0.53978 -0.07320 0.07610  0.12078  246 LEU A CB  
1888 C CG  . LEU A 253 ? 0.58282 0.54344 0.55241 -0.09394 0.07966  0.12929  246 LEU A CG  
1889 C CD1 . LEU A 253 ? 0.62289 0.58167 0.59781 -0.08085 0.09168  0.12067  246 LEU A CD1 
1890 C CD2 . LEU A 253 ? 0.67600 0.56990 0.60534 -0.10636 0.08030  0.12894  246 LEU A CD2 
1891 N N   . LEU A 254 ? 0.46427 0.49420 0.50093 -0.04142 0.05002  0.10875  247 LEU A N   
1892 C CA  . LEU A 254 ? 0.50449 0.53425 0.55529 -0.01682 0.03826  0.09587  247 LEU A CA  
1893 C C   . LEU A 254 ? 0.45870 0.44096 0.49250 -0.02854 0.02981  0.09696  247 LEU A C   
1894 O O   . LEU A 254 ? 0.43872 0.39524 0.47603 -0.01778 0.02166  0.08886  247 LEU A O   
1895 C CB  . LEU A 254 ? 0.55445 0.64692 0.62488 0.00771  0.02523  0.09372  247 LEU A CB  
1896 C CG  . LEU A 254 ? 0.60458 0.75161 0.69086 0.02444  0.03390  0.09332  247 LEU A CG  
1897 C CD1 . LEU A 254 ? 0.47476 0.69872 0.57749 0.04431  0.02545  0.09847  247 LEU A CD1 
1898 C CD2 . LEU A 254 ? 0.51661 0.64486 0.60828 0.05030  0.03367  0.07596  247 LEU A CD2 
1899 N N   . LYS A 255 ? 0.51790 0.48483 0.53060 -0.05206 0.02887  0.10852  248 LYS A N   
1900 C CA  . LYS A 255 ? 0.56080 0.47987 0.55133 -0.06374 0.02201  0.11068  248 LYS A CA  
1901 C C   . LYS A 255 ? 0.57774 0.45088 0.55501 -0.06938 0.03684  0.10904  248 LYS A C   
1902 O O   . LYS A 255 ? 0.63070 0.47615 0.60391 -0.06942 0.03040  0.10861  248 LYS A O   
1903 C CB  . LYS A 255 ? 0.56256 0.46793 0.52700 -0.08783 0.01755  0.12341  248 LYS A CB  
1904 C CG  . LYS A 255 ? 0.60990 0.56901 0.59210 -0.08662 0.00149  0.13048  248 LYS A CG  
1905 C CD  . LYS A 255 ? 0.72536 0.68105 0.68844 -0.11507 -0.00038 0.14699  248 LYS A CD  
1906 C CE  . LYS A 255 ? 0.61345 0.49725 0.53096 -0.13566 -0.00378 0.15097  248 LYS A CE  
1907 N NZ  . LYS A 255 ? 0.76838 0.64957 0.68213 -0.13959 -0.02456 0.15502  248 LYS A NZ  
1908 N N   . LYS A 256 ? 0.57891 0.44629 0.54941 -0.07419 0.05570  0.10996  249 LYS A N   
1909 C CA  . LYS A 256 ? 0.58132 0.41555 0.54007 -0.07720 0.07257  0.11037  249 LYS A CA  
1910 C C   . LYS A 256 ? 0.49807 0.34276 0.48848 -0.06296 0.07211  0.10438  249 LYS A C   
1911 O O   . LYS A 256 ? 0.61460 0.44135 0.60327 -0.06668 0.08401  0.10856  249 LYS A O   
1912 C CB  . LYS A 256 ? 0.62884 0.45258 0.56764 -0.08186 0.08955  0.11142  249 LYS A CB  
1913 C CG  . LYS A 256 ? 0.51138 0.31340 0.41250 -0.09850 0.08395  0.11880  249 LYS A CG  
1914 C CD  . LYS A 256 ? 0.65913 0.44218 0.53543 -0.09855 0.09297  0.11673  249 LYS A CD  
1915 C CE  . LYS A 256 ? 0.65684 0.42523 0.50477 -0.11216 0.07655  0.12225  249 LYS A CE  
1916 N NZ  . LYS A 256 ? 0.76267 0.50355 0.58066 -0.10871 0.07882  0.11731  249 LYS A NZ  
1917 N N   . ILE A 257 ? 0.44733 0.32149 0.46482 -0.04588 0.05736  0.09599  250 ILE A N   
1918 C CA  . ILE A 257 ? 0.53027 0.40530 0.57297 -0.03200 0.04952  0.08984  250 ILE A CA  
1919 C C   . ILE A 257 ? 0.52853 0.37882 0.56989 -0.03429 0.02791  0.09257  250 ILE A C   
1920 O O   . ILE A 257 ? 0.60678 0.46087 0.64370 -0.02585 0.00777  0.08829  250 ILE A O   
1921 C CB  . ILE A 257 ? 0.48334 0.39337 0.54616 -0.00787 0.04046  0.07801  250 ILE A CB  
1922 C CG1 . ILE A 257 ? 0.47256 0.40420 0.53444 -0.00938 0.06036  0.07826  250 ILE A CG1 
1923 C CG2 . ILE A 257 ? 0.36501 0.26461 0.44746 0.00722  0.02551  0.07084  250 ILE A CG2 
1924 C CD1 . ILE A 257 ? 0.33867 0.31111 0.41585 0.01346  0.05442  0.06966  250 ILE A CD1 
1925 N N   . SER A 258 ? 0.55830 0.38546 0.60350 -0.04601 0.03079  0.10155  251 SER A N   
1926 C CA  . SER A 258 ? 0.66766 0.46641 0.70957 -0.05343 0.00741  0.10831  251 SER A CA  
1927 C C   . SER A 258 ? 0.63617 0.42885 0.69751 -0.03593 -0.02378 0.09946  251 SER A C   
1928 O O   . SER A 258 ? 0.59775 0.36989 0.64979 -0.02823 -0.05424 0.09528  251 SER A O   
1929 C CB  . SER A 258 ? 0.63079 0.41336 0.66830 -0.07651 0.02279  0.12716  251 SER A CB  
1930 O OG  . SER A 258 ? 0.69701 0.45086 0.72931 -0.08865 -0.00149 0.13785  251 SER A OG  
1931 N N   . SER A 259 ? 0.56609 0.37104 0.64996 -0.02743 -0.01992 0.09556  252 SER A N   
1932 C CA  . SER A 259 ? 0.69632 0.48721 0.79284 -0.00920 -0.05311 0.08638  252 SER A CA  
1933 C C   . SER A 259 ? 0.77954 0.57916 0.86376 0.02257  -0.07377 0.06714  252 SER A C   
1934 O O   . SER A 259 ? 0.68190 0.51974 0.76755 0.03871  -0.05700 0.05756  252 SER A O   
1935 C CB  . SER A 259 ? 0.60189 0.40831 0.72233 -0.00320 -0.04291 0.08380  252 SER A CB  
1936 O OG  . SER A 259 ? 0.69885 0.48804 0.82486 0.01918  -0.07749 0.07178  252 SER A OG  
1937 N N   . GLU A 260 ? 0.68388 0.44992 0.75465 0.03245  -0.11149 0.06291  253 GLU A N   
1938 C CA  . GLU A 260 ? 0.79742 0.57551 0.85412 0.06943  -0.13258 0.04386  253 GLU A CA  
1939 C C   . GLU A 260 ? 0.82156 0.61395 0.88400 0.10466  -0.14260 0.02660  253 GLU A C   
1940 O O   . GLU A 260 ? 0.80791 0.64451 0.86751 0.13404  -0.13490 0.01411  253 GLU A O   
1941 C CB  . GLU A 260 ? 0.86220 0.59242 0.89677 0.07489  -0.17449 0.04197  253 GLU A CB  
1942 C CG  . GLU A 260 ? 0.89347 0.64490 0.91112 0.11099  -0.18989 0.02536  253 GLU A CG  
1943 C CD  . GLU A 260 ? 1.01299 0.73165 1.00974 0.10035  -0.21089 0.03087  253 GLU A CD  
1944 O OE1 . GLU A 260 ? 1.15481 0.81200 1.13497 0.09630  -0.24879 0.03279  253 GLU A OE1 
1945 O OE2 . GLU A 260 ? 1.02667 0.77797 1.02217 0.09432  -0.19251 0.03462  253 GLU A OE2 
1946 N N   . SER A 261 ? 0.77110 0.52902 0.84123 0.10196  -0.16081 0.02759  254 SER A N   
1947 C CA  . SER A 261 ? 0.64933 0.41432 0.72055 0.13557  -0.17153 0.01093  254 SER A CA  
1948 C C   . SER A 261 ? 0.64701 0.46954 0.73392 0.13702  -0.12889 0.01008  254 SER A C   
1949 O O   . SER A 261 ? 0.69699 0.54992 0.77751 0.17172  -0.12820 -0.00488 254 SER A O   
1950 C CB  . SER A 261 ? 0.79655 0.51585 0.87514 0.12279  -0.19717 0.01589  254 SER A CB  
1951 O OG  . SER A 261 ? 0.82215 0.50210 0.87509 0.11927  -0.23534 0.01106  254 SER A OG  
1952 N N   . ALA A 262 ? 0.67096 0.50767 0.77433 0.10124  -0.09440 0.02655  255 ALA A N   
1953 C CA  . ALA A 262 ? 0.60941 0.49206 0.72118 0.09977  -0.05771 0.02697  255 ALA A CA  
1954 C C   . ALA A 262 ? 0.56058 0.48713 0.66119 0.11293  -0.04714 0.02326  255 ALA A C   
1955 O O   . ALA A 262 ? 0.65612 0.62335 0.75705 0.13482  -0.03838 0.01595  255 ALA A O   
1956 C CB  . ALA A 262 ? 0.61525 0.49587 0.73777 0.06304  -0.02763 0.04396  255 ALA A CB  
1957 N N   . ARG A 263 ? 0.57583 0.49800 0.66735 0.09848  -0.04858 0.03065  256 ARG A N   
1958 C CA  . ARG A 263 ? 0.68898 0.65616 0.77415 0.10918  -0.04339 0.03004  256 ARG A CA  
1959 C C   . ARG A 263 ? 0.62966 0.62445 0.70969 0.15569  -0.06450 0.01348  256 ARG A C   
1960 O O   . ARG A 263 ? 0.61046 0.66472 0.69476 0.17261  -0.05095 0.01269  256 ARG A O   
1961 C CB  . ARG A 263 ? 0.74889 0.69635 0.82294 0.09013  -0.05073 0.03855  256 ARG A CB  
1962 C CG  . ARG A 263 ? 0.57333 0.51821 0.64380 0.05207  -0.02391 0.05492  256 ARG A CG  
1963 C CD  . ARG A 263 ? 0.52237 0.46379 0.57911 0.04145  -0.03241 0.06140  256 ARG A CD  
1964 N NE  . ARG A 263 ? 0.65587 0.57251 0.70518 0.06007  -0.06508 0.05291  256 ARG A NE  
1965 C CZ  . ARG A 263 ? 0.66240 0.52405 0.70178 0.04657  -0.08050 0.05661  256 ARG A CZ  
1966 N NH1 . ARG A 263 ? 0.82756 0.66016 0.85556 0.06390  -0.11565 0.04884  256 ARG A NH1 
1967 N NH2 . ARG A 263 ? 0.69568 0.53197 0.73459 0.01580  -0.06141 0.06970  256 ARG A NH2 
1968 N N   . ASN A 264 ? 0.71385 0.66547 0.78142 0.17794  -0.09964 0.00126  257 ASN A N   
1969 C CA  . ASN A 264 ? 0.76600 0.73583 0.81866 0.23014  -0.12418 -0.01760 257 ASN A CA  
1970 C C   . ASN A 264 ? 0.69939 0.70482 0.75553 0.25582  -0.11193 -0.02583 257 ASN A C   
1971 O O   . ASN A 264 ? 0.76360 0.82302 0.81056 0.27679  -0.10295 -0.03177 257 ASN A O   
1972 C CB  . ASN A 264 ? 0.81921 0.71929 0.84924 0.24183  -0.16667 -0.02920 257 ASN A CB  
1973 C CG  . ASN A 264 ? 0.84046 0.72585 0.85467 0.24520  -0.18783 -0.03019 257 ASN A CG  
1974 O OD1 . ASN A 264 ? 0.96260 0.82967 0.98374 0.21263  -0.18352 -0.01484 257 ASN A OD1 
1975 N ND2 . ASN A 264 ? 0.83853 0.73345 0.82590 0.27259  -0.20213 -0.04813 257 ASN A ND2 
1976 N N   . TYR A 265 ? 0.67950 0.65585 0.74517 0.23758  -0.10440 -0.02319 258 TYR A N   
1977 C CA  . TYR A 265 ? 0.67693 0.67940 0.74037 0.25047  -0.09122 -0.02981 258 TYR A CA  
1978 C C   . TYR A 265 ? 0.66969 0.74180 0.74872 0.24816  -0.05614 -0.01881 258 TYR A C   
1979 O O   . TYR A 265 ? 0.70581 0.82174 0.77555 0.26278  -0.04592 -0.02248 258 TYR A O   
1980 C CB  . TYR A 265 ? 0.62037 0.57323 0.69113 0.23371  -0.09700 -0.02953 258 TYR A CB  
1981 C CG  . TYR A 265 ? 0.70624 0.67306 0.76600 0.24485  -0.09117 -0.03819 258 TYR A CG  
1982 C CD1 . TYR A 265 ? 0.58291 0.52865 0.61132 0.26269  -0.11510 -0.05360 258 TYR A CD1 
1983 C CD2 . TYR A 265 ? 0.64612 0.64329 0.72132 0.23847  -0.06389 -0.03199 258 TYR A CD2 
1984 C CE1 . TYR A 265 ? 0.65550 0.60959 0.66880 0.27438  -0.11230 -0.06184 258 TYR A CE1 
1985 C CE2 . TYR A 265 ? 0.67427 0.67953 0.73655 0.24753  -0.06124 -0.03910 258 TYR A CE2 
1986 C CZ  . TYR A 265 ? 0.78030 0.76429 0.81181 0.26597  -0.08535 -0.05362 258 TYR A CZ  
1987 O OH  . TYR A 265 ? 0.78703 0.77609 0.80090 0.27719  -0.08452 -0.06109 258 TYR A OH  
1988 N N   . ILE A 266 ? 0.61045 0.68379 0.70298 0.20316  -0.03282 -0.00113 259 ILE A N   
1989 C CA  . ILE A 266 ? 0.60310 0.73239 0.70346 0.18564  -0.00260 0.01333  259 ILE A CA  
1990 C C   . ILE A 266 ? 0.61650 0.81216 0.71602 0.20482  -0.00312 0.01724  259 ILE A C   
1991 O O   . ILE A 266 ? 0.62351 0.88360 0.72677 0.21654  0.01104  0.02361  259 ILE A O   
1992 C CB  . ILE A 266 ? 0.64226 0.74598 0.74767 0.13727  0.01584  0.02939  259 ILE A CB  
1993 C CG1 . ILE A 266 ? 0.64872 0.70277 0.75869 0.12285  0.02007  0.02728  259 ILE A CG1 
1994 C CG2 . ILE A 266 ? 0.56232 0.71325 0.66930 0.11710  0.03851  0.04561  259 ILE A CG2 
1995 C CD1 . ILE A 266 ? 0.60672 0.63154 0.71571 0.08415  0.03607  0.04036  259 ILE A CD1 
1996 N N   . GLN A 267 ? 0.53623 0.72113 0.63180 0.20809  -0.02006 0.01545  260 GLN A N   
1997 C CA  . GLN A 267 ? 0.65433 0.90725 0.75281 0.22777  -0.02217 0.01998  260 GLN A CA  
1998 C C   . GLN A 267 ? 0.73760 1.02488 0.82219 0.27800  -0.03268 0.00367  260 GLN A C   
1999 O O   . GLN A 267 ? 0.77541 1.13202 0.86007 0.28406  -0.01940 0.01167  260 GLN A O   
2000 C CB  . GLN A 267 ? 0.58243 0.80564 0.67577 0.22051  -0.04117 0.01952  260 GLN A CB  
2001 C CG  . GLN A 267 ? 0.45614 0.63575 0.55159 0.16738  -0.03066 0.03472  260 GLN A CG  
2002 C CD  . GLN A 267 ? 0.56261 0.71790 0.65008 0.16174  -0.04968 0.03551  260 GLN A CD  
2003 O OE1 . GLN A 267 ? 0.64781 0.73468 0.72342 0.15076  -0.06415 0.03091  260 GLN A OE1 
2004 N NE2 . GLN A 267 ? 0.49623 0.71060 0.59120 0.16804  -0.05077 0.04362  260 GLN A NE2 
2005 N N   . SER A 268 ? 0.72758 0.94719 0.78743 0.29299  -0.05466 -0.01744 261 SER A N   
2006 C CA  . SER A 268 ? 0.76600 0.98978 0.79304 0.32229  -0.06442 -0.03448 261 SER A CA  
2007 C C   . SER A 268 ? 0.73029 0.99196 0.75079 0.32687  -0.04466 -0.03169 261 SER A C   
2008 O O   . SER A 268 ? 0.92682 1.20821 0.91687 0.35456  -0.04854 -0.04228 261 SER A O   
2009 C CB  . SER A 268 ? 0.80594 0.94617 0.80636 0.33123  -0.09563 -0.05436 261 SER A CB  
2010 O OG  . SER A 268 ? 0.73316 0.84488 0.72480 0.33611  -0.11842 -0.05986 261 SER A OG  
2011 N N   . LEU A 269 ? 0.84400 0.75074 1.28634 0.34241  0.45350  0.30684  262 LEU A N   
2012 C CA  . LEU A 269 ? 0.89968 0.79482 1.29387 0.34428  0.46718  0.28241  262 LEU A CA  
2013 C C   . LEU A 269 ? 1.00091 0.93351 1.42896 0.35254  0.48238  0.30780  262 LEU A C   
2014 O O   . LEU A 269 ? 0.97709 0.95360 1.46269 0.35246  0.47491  0.34725  262 LEU A O   
2015 C CB  . LEU A 269 ? 0.84687 0.75307 1.20068 0.32969  0.44397  0.27217  262 LEU A CB  
2016 C CG  . LEU A 269 ? 0.91483 0.77397 1.21680 0.32176  0.43343  0.23788  262 LEU A CG  
2017 C CD1 . LEU A 269 ? 0.79157 0.67367 1.07735 0.30763  0.40483  0.24202  262 LEU A CD1 
2018 C CD2 . LEU A 269 ? 0.92465 0.73498 1.16426 0.32386  0.45353  0.19582  262 LEU A CD2 
2019 N N   . ALA A 270 ? 1.15223 1.06772 1.54244 0.35819  0.50280  0.28534  263 ALA A N   
2020 C CA  . ALA A 270 ? 1.15838 1.10428 1.57681 0.36713  0.51953  0.30667  263 ALA A CA  
2021 C C   . ALA A 270 ? 1.08059 1.08643 1.52636 0.35669  0.49784  0.34061  263 ALA A C   
2022 O O   . ALA A 270 ? 1.18251 1.22189 1.66745 0.36233  0.50583  0.36902  263 ALA A O   
2023 C CB  . ALA A 270 ? 1.31915 1.23591 1.68469 0.37261  0.54267  0.27367  263 ALA A CB  
2024 N N   . GLN A 271 ? 1.05480 1.07445 1.48094 0.34103  0.47040  0.33806  264 GLN A N   
2025 C CA  . GLN A 271 ? 1.05852 1.13441 1.50770 0.32791  0.44665  0.36728  264 GLN A CA  
2026 C C   . GLN A 271 ? 1.01530 1.10236 1.43352 0.32485  0.45272  0.35807  264 GLN A C   
2027 O O   . GLN A 271 ? 0.99364 1.06978 1.40738 0.33673  0.47755  0.35287  264 GLN A O   
2028 C CB  . GLN A 271 ? 0.90155 1.02058 1.42038 0.32961  0.44191  0.41277  264 GLN A CB  
2029 C CG  . GLN A 271 ? 0.95859 1.13265 1.50454 0.31066  0.40789  0.44377  264 GLN A CG  
2030 C CD  . GLN A 271 ? 0.97042 1.18194 1.52078 0.30424  0.40336  0.45879  264 GLN A CD  
2031 O OE1 . GLN A 271 ? 1.02484 1.22042 1.54929 0.31286  0.42402  0.44194  264 GLN A OE1 
2032 N NE2 . GLN A 271 ? 0.85353 1.11497 1.43513 0.28725  0.37465  0.49028  264 GLN A NE2 
2033 N N   . MET A 272 ? 0.90529 1.01519 1.30287 0.30810  0.43009  0.35640  265 MET A N   
2034 C CA  . MET A 272 ? 0.88928 1.01315 1.25826 0.30094  0.43110  0.34972  265 MET A CA  
2035 C C   . MET A 272 ? 0.79722 0.97419 1.19033 0.28159  0.40123  0.37610  265 MET A C   
2036 O O   . MET A 272 ? 0.68532 0.87836 1.09274 0.26998  0.37813  0.38535  265 MET A O   
2037 C CB  . MET A 272 ? 0.99565 1.07858 1.29260 0.29585  0.43588  0.30779  265 MET A CB  
2038 C CG  . MET A 272 ? 1.14163 1.16657 1.40713 0.30826  0.45589  0.27642  265 MET A CG  
2039 S SD  . MET A 272 ? 1.18742 1.18872 1.45410 0.30482  0.43913  0.26828  265 MET A SD  
2040 C CE  . MET A 272 ? 0.86656 0.82938 1.05076 0.29147  0.43259  0.22566  265 MET A CE  
2041 N N   . PRO A 273 ? 0.81447 1.01921 1.21188 0.27626  0.39987  0.38799  266 PRO A N   
2042 C CA  . PRO A 273 ? 0.71618 0.96744 1.13222 0.25451  0.36941  0.40982  266 PRO A CA  
2043 C C   . PRO A 273 ? 0.74824 0.99016 1.11307 0.23483  0.35393  0.38556  266 PRO A C   
2044 O O   . PRO A 273 ? 0.78093 0.98537 1.09367 0.23828  0.36799  0.35435  266 PRO A O   
2045 C CB  . PRO A 273 ? 0.73170 1.00891 1.16988 0.25830  0.37682  0.42926  266 PRO A CB  
2046 C CG  . PRO A 273 ? 0.75014 0.98922 1.15119 0.27512  0.40912  0.40312  266 PRO A CG  
2047 C CD  . PRO A 273 ? 0.85241 1.04797 1.24044 0.28930  0.42564  0.38309  266 PRO A CD  
2048 N N   . LYS A 274 ? 0.69519 0.97006 1.07294 0.21169  0.32290  0.40053  267 LYS A N   
2049 C CA  . LYS A 274 ? 0.52805 0.79231 0.85769 0.18900  0.30324  0.38011  267 LYS A CA  
2050 C C   . LYS A 274 ? 0.63095 0.89835 0.94077 0.18682  0.31104  0.37489  267 LYS A C   
2051 O O   . LYS A 274 ? 0.75579 1.05479 1.09991 0.18698  0.30854  0.39713  267 LYS A O   
2052 C CB  . LYS A 274 ? 0.52297 0.81593 0.86820 0.16287  0.26471  0.39470  267 LYS A CB  
2053 C CG  . LYS A 274 ? 0.63221 0.91407 0.93257 0.13843  0.24103  0.37481  267 LYS A CG  
2054 C CD  . LYS A 274 ? 0.46428 0.77664 0.78273 0.11261  0.20602  0.38960  267 LYS A CD  
2055 C CE  . LYS A 274 ? 0.59279 0.88321 0.86345 0.09026  0.18317  0.36386  267 LYS A CE  
2056 N NZ  . LYS A 274 ? 0.68747 0.98565 0.95076 0.08279  0.18565  0.36441  267 LYS A NZ  
2057 N N   . MET A 275 ? 0.62438 0.85776 0.87775 0.18408  0.31791  0.34571  268 MET A N   
2058 C CA  . MET A 275 ? 0.59814 0.83261 0.82822 0.17944  0.32110  0.33945  268 MET A CA  
2059 C C   . MET A 275 ? 0.52936 0.78809 0.76295 0.15305  0.29024  0.34876  268 MET A C   
2060 O O   . MET A 275 ? 0.67470 0.93376 0.90466 0.13620  0.26686  0.34749  268 MET A O   
2061 C CB  . MET A 275 ? 0.62278 0.81295 0.78991 0.18367  0.33592  0.30590  268 MET A CB  
2062 C CG  . MET A 275 ? 0.65347 0.80803 0.80683 0.20461  0.36043  0.28831  268 MET A CG  
2063 S SD  . MET A 275 ? 0.85518 0.96739 0.94555 0.21349  0.38416  0.25487  268 MET A SD  
2064 C CE  . MET A 275 ? 0.65451 0.73908 0.68403 0.19244  0.36291  0.22975  268 MET A CE  
2065 N N   . ASN A 276 ? 0.77558 1.05276 1.01593 0.14902  0.28980  0.35740  269 ASN A N   
2066 C CA  . ASN A 276 ? 0.77803 1.07412 1.02180 0.12437  0.26220  0.36421  269 ASN A CA  
2067 C C   . ASN A 276 ? 0.52062 0.78557 0.70953 0.11288  0.25677  0.33889  269 ASN A C   
2068 O O   . ASN A 276 ? 0.59858 0.84795 0.75761 0.12022  0.27296  0.32687  269 ASN A O   
2069 C CB  . ASN A 276 ? 0.72806 1.05643 1.00431 0.12465  0.26362  0.38546  269 ASN A CB  
2070 C CG  . ASN A 276 ? 0.85540 1.21156 1.15645 0.09997  0.23248  0.40041  269 ASN A CG  
2071 O OD1 . ASN A 276 ? 0.86538 1.21856 1.16209 0.08290  0.20999  0.39578  269 ASN A OD1 
2072 N ND2 . ASN A 276 ? 0.79744 1.17940 1.12332 0.09734  0.23110  0.41773  269 ASN A ND2 
2073 N N   . PHE A 277 ? 0.65326 0.90929 0.82840 0.09434  0.23321  0.33139  270 PHE A N   
2074 C CA  . PHE A 277 ? 0.64135 0.86594 0.76692 0.08365  0.22489  0.30771  270 PHE A CA  
2075 C C   . PHE A 277 ? 0.57705 0.81030 0.69690 0.07588  0.22414  0.31162  270 PHE A C   
2076 O O   . PHE A 277 ? 0.56636 0.77549 0.64503 0.07529  0.22895  0.29495  270 PHE A O   
2077 C CB  . PHE A 277 ? 0.47314 0.68762 0.59182 0.06393  0.19302  0.29672  270 PHE A CB  
2078 C CG  . PHE A 277 ? 0.63110 0.82478 0.73940 0.07023  0.18967  0.28273  270 PHE A CG  
2079 C CD1 . PHE A 277 ? 0.61917 0.81892 0.74935 0.08914  0.20793  0.29207  270 PHE A CD1 
2080 C CD2 . PHE A 277 ? 0.49108 0.65964 0.57065 0.05761  0.16904  0.26159  270 PHE A CD2 
2081 C CE1 . PHE A 277 ? 0.57050 0.75115 0.69409 0.09442  0.20438  0.28130  270 PHE A CE1 
2082 C CE2 . PHE A 277 ? 0.50185 0.65320 0.57335 0.06269  0.16580  0.25076  270 PHE A CE2 
2083 C CZ  . PHE A 277 ? 0.51761 0.67473 0.61113 0.08066  0.18284  0.26096  270 PHE A CZ  
2084 N N   . ALA A 278 ? 0.54634 0.81362 0.70748 0.06916  0.21593  0.33339  271 ALA A N   
2085 C CA  . ALA A 278 ? 0.59805 0.87461 0.75839 0.06237  0.21476  0.33876  271 ALA A CA  
2086 C C   . ALA A 278 ? 0.71920 0.98459 0.85331 0.07972  0.24142  0.33100  271 ALA A C   
2087 O O   . ALA A 278 ? 0.73166 0.98987 0.84183 0.07355  0.24117  0.32560  271 ALA A O   
2088 C CB  . ALA A 278 ? 0.52127 0.83711 0.73346 0.05559  0.20462  0.36503  271 ALA A CB  
2089 N N   . ASN A 279 ? 0.73496 0.99812 0.87301 0.10078  0.26442  0.33027  272 ASN A N   
2090 C CA  . ASN A 279 ? 0.71770 0.96728 0.82713 0.11670  0.29091  0.31973  272 ASN A CA  
2091 C C   . ASN A 279 ? 0.74840 0.95726 0.79937 0.11678  0.29512  0.29064  272 ASN A C   
2092 O O   . ASN A 279 ? 0.73311 0.93067 0.74834 0.11322  0.29938  0.28011  272 ASN A O   
2093 C CB  . ASN A 279 ? 0.73111 0.98922 0.86695 0.13943  0.31483  0.32819  272 ASN A CB  
2094 C CG  . ASN A 279 ? 0.60277 0.89937 0.78542 0.14306  0.31840  0.35580  272 ASN A CG  
2095 O OD1 . ASN A 279 ? 0.75875 1.08114 0.96997 0.12726  0.29699  0.37316  272 ASN A OD1 
2096 N ND2 . ASN A 279 ? 0.80135 1.10042 0.99180 0.16360  0.34548  0.35949  272 ASN A ND2 
2097 N N   . VAL A 280 ? 0.63313 0.82078 0.67415 0.11985  0.29273  0.27855  273 VAL A N   
2098 C CA  . VAL A 280 ? 0.69480 0.84232 0.68111 0.12105  0.29692  0.25075  273 VAL A CA  
2099 C C   . VAL A 280 ? 0.64894 0.78618 0.60545 0.10116  0.27547  0.24293  273 VAL A C   
2100 O O   . VAL A 280 ? 0.61204 0.72374 0.52166 0.09961  0.27871  0.22384  273 VAL A O   
2101 C CB  . VAL A 280 ? 0.66245 0.79102 0.64965 0.12828  0.29794  0.24223  273 VAL A CB  
2102 C CG1 . VAL A 280 ? 0.66509 0.80850 0.68147 0.11283  0.26958  0.25338  273 VAL A CG1 
2103 C CG2 . VAL A 280 ? 0.61566 0.70074 0.54610 0.12876  0.30054  0.21258  273 VAL A CG2 
2104 N N   . PHE A 281 ? 0.61521 0.77131 0.59889 0.08496  0.25260  0.25729  274 PHE A N   
2105 C CA  . PHE A 281 ? 0.70717 0.85388 0.67056 0.06652  0.23212  0.25224  274 PHE A CA  
2106 C C   . PHE A 281 ? 0.75692 0.92865 0.74129 0.05669  0.22600  0.26918  274 PHE A C   
2107 O O   . PHE A 281 ? 0.67491 0.84999 0.66883 0.03972  0.20527  0.27445  274 PHE A O   
2108 C CB  . PHE A 281 ? 0.58451 0.72451 0.55881 0.05338  0.20684  0.24829  274 PHE A CB  
2109 C CG  . PHE A 281 ? 0.69535 0.80944 0.65302 0.06088  0.20583  0.22854  274 PHE A CG  
2110 C CD1 . PHE A 281 ? 0.58947 0.66892 0.50158 0.06177  0.20539  0.20464  274 PHE A CD1 
2111 C CD2 . PHE A 281 ? 0.65458 0.78064 0.64406 0.06593  0.20421  0.23598  274 PHE A CD2 
2112 C CE1 . PHE A 281 ? 0.58999 0.64566 0.48913 0.06775  0.20395  0.18779  274 PHE A CE1 
2113 C CE2 . PHE A 281 ? 0.60995 0.71308 0.58676 0.07248  0.20307  0.22019  274 PHE A CE2 
2114 C CZ  . PHE A 281 ? 0.56237 0.62948 0.49424 0.07346  0.20320  0.19568  274 PHE A CZ  
2115 N N   . ILE A 282 ? 0.68180 0.87005 0.67430 0.06736  0.24447  0.27777  275 ILE A N   
2116 C CA  . ILE A 282 ? 0.71076 0.92364 0.72421 0.05892  0.23976  0.29536  275 ILE A CA  
2117 C C   . ILE A 282 ? 0.75058 0.94824 0.73209 0.04531  0.22830  0.28789  275 ILE A C   
2118 O O   . ILE A 282 ? 0.80635 0.97817 0.74261 0.04723  0.23288  0.26936  275 ILE A O   
2119 C CB  . ILE A 282 ? 0.78460 1.01566 0.80642 0.07413  0.26400  0.30438  275 ILE A CB  
2120 C CG1 . ILE A 282 ? 0.78622 1.04465 0.83240 0.06505  0.25826  0.32481  275 ILE A CG1 
2121 C CG2 . ILE A 282 ? 0.76213 0.96864 0.73270 0.08434  0.28377  0.28366  275 ILE A CG2 
2122 C CD1 . ILE A 282 ? 0.70304 0.98608 0.80056 0.05361  0.23841  0.34479  275 ILE A CD1 
2123 N N   . GLY A 283 ? 0.67433 0.88829 0.68151 0.03097  0.21249  0.30331  276 GLY A N   
2124 C CA  . GLY A 283 ? 0.59016 0.79186 0.57789 0.01717  0.19887  0.30052  276 GLY A CA  
2125 C C   . GLY A 283 ? 0.67343 0.85680 0.66140 0.00385  0.17687  0.29308  276 GLY A C   
2126 O O   . GLY A 283 ? 0.77398 0.95310 0.76471 -0.00952 0.16210  0.29714  276 GLY A O   
2127 N N   . ALA A 284 ? 0.60862 0.78111 0.59536 0.00738  0.17481  0.28306  277 ALA A N   
2128 C CA  . ALA A 284 ? 0.65359 0.80959 0.64056 -0.00511 0.15503  0.27576  277 ALA A CA  
2129 C C   . ALA A 284 ? 0.50775 0.68202 0.53975 -0.01967 0.13837  0.29038  277 ALA A C   
2130 O O   . ALA A 284 ? 0.47756 0.67841 0.54257 -0.01810 0.14187  0.30569  277 ALA A O   
2131 C CB  . ALA A 284 ? 0.51396 0.65254 0.48463 0.00322  0.15699  0.25862  277 ALA A CB  
2132 N N   . ASN A 285 ? 0.50271 0.66057 0.53582 -0.03425 0.11879  0.28282  278 ASN A N   
2133 C CA  . ASN A 285 ? 0.45030 0.61803 0.52051 -0.05065 0.10072  0.29011  278 ASN A CA  
2134 C C   . ASN A 285 ? 0.44064 0.62632 0.53246 -0.04843 0.10029  0.29372  278 ASN A C   
2135 O O   . ASN A 285 ? 0.52888 0.70172 0.60362 -0.04151 0.09999  0.27731  278 ASN A O   
2136 C CB  . ASN A 285 ? 0.45610 0.59497 0.51680 -0.06284 0.08113  0.27024  278 ASN A CB  
2137 C CG  . ASN A 285 ? 0.43438 0.57841 0.52948 -0.08181 0.06290  0.27460  278 ASN A CG  
2138 O OD1 . ASN A 285 ? 0.46556 0.63355 0.58889 -0.08687 0.06069  0.28769  278 ASN A OD1 
2139 N ND2 . ASN A 285 ? 0.43438 0.55544 0.52808 -0.09289 0.04977  0.26354  278 ASN A ND2 
2140 N N   . PRO A 286 ? 0.43831 0.65473 0.56903 -0.05447 0.09929  0.31611  279 PRO A N   
2141 C CA  . PRO A 286 ? 0.43523 0.67283 0.58989 -0.05354 0.09729  0.32334  279 PRO A CA  
2142 C C   . PRO A 286 ? 0.47238 0.69399 0.62041 -0.06433 0.07771  0.30412  279 PRO A C   
2143 O O   . PRO A 286 ? 0.41336 0.64233 0.56352 -0.05793 0.07886  0.30241  279 PRO A O   
2144 C CB  . PRO A 286 ? 0.43173 0.69868 0.62858 -0.06282 0.08978  0.34354  279 PRO A CB  
2145 C CG  . PRO A 286 ? 0.46314 0.72845 0.65465 -0.05849 0.09829  0.34858  279 PRO A CG  
2146 C CD  . PRO A 286 ? 0.44624 0.67800 0.60113 -0.06082 0.09664  0.33123  279 PRO A CD  
2147 N N   . LEU A 287 ? 0.45471 0.65480 0.59558 -0.08017 0.06048  0.28982  280 LEU A N   
2148 C CA  . LEU A 287 ? 0.40946 0.59268 0.53900 -0.08981 0.04397  0.26868  280 LEU A CA  
2149 C C   . LEU A 287 ? 0.44717 0.60787 0.54070 -0.07495 0.05136  0.24877  280 LEU A C   
2150 O O   . LEU A 287 ? 0.46915 0.62655 0.55616 -0.07693 0.04354  0.23765  280 LEU A O   
2151 C CB  . LEU A 287 ? 0.41208 0.57442 0.54215 -0.10812 0.02763  0.25646  280 LEU A CB  
2152 C CG  . LEU A 287 ? 0.45199 0.63229 0.61880 -0.12772 0.01539  0.27205  280 LEU A CG  
2153 C CD1 . LEU A 287 ? 0.42316 0.57628 0.58957 -0.14424 0.00143  0.25667  280 LEU A CD1 
2154 C CD2 . LEU A 287 ? 0.47989 0.68513 0.66545 -0.13735 0.00515  0.27886  280 LEU A CD2 
2155 N N   . ALA A 288 ? 0.41465 0.56063 0.48411 -0.06136 0.06563  0.24481  281 ALA A N   
2156 C CA  . ALA A 288 ? 0.44384 0.56893 0.48007 -0.04767 0.07315  0.22727  281 ALA A CA  
2157 C C   . ALA A 288 ? 0.41796 0.55889 0.45978 -0.03241 0.08745  0.23570  281 ALA A C   
2158 O O   . ALA A 288 ? 0.47712 0.60624 0.50407 -0.02575 0.08756  0.22315  281 ALA A O   
2159 C CB  . ALA A 288 ? 0.42724 0.53250 0.43466 -0.04029 0.08250  0.22077  281 ALA A CB  
2160 N N   . VAL A 289 ? 0.42344 0.59137 0.48934 -0.02628 0.10034  0.25805  282 VAL A N   
2161 C CA  . VAL A 289 ? 0.43009 0.61467 0.50849 -0.01060 0.11570  0.26843  282 VAL A CA  
2162 C C   . VAL A 289 ? 0.42935 0.62922 0.53117 -0.01840 0.10113  0.27279  282 VAL A C   
2163 O O   . VAL A 289 ? 0.41328 0.61081 0.51240 -0.00769 0.10628  0.26944  282 VAL A O   
2164 C CB  . VAL A 289 ? 0.43653 0.64984 0.53980 -0.00263 0.13364  0.29338  282 VAL A CB  
2165 C CG1 . VAL A 289 ? 0.44295 0.67165 0.56157 0.01625  0.15282  0.30388  282 VAL A CG1 
2166 C CG2 . VAL A 289 ? 0.45433 0.65452 0.53074 0.00265  0.14678  0.28968  282 VAL A CG2 
2167 N N   . ASP A 290 ? 0.41392 0.62948 0.53874 -0.03825 0.08220  0.28068  283 ASP A N   
2168 C CA  . ASP A 290 ? 0.39601 0.62770 0.53896 -0.04933 0.06585  0.28451  283 ASP A CA  
2169 C C   . ASP A 290 ? 0.39185 0.59717 0.50436 -0.05080 0.05659  0.25997  283 ASP A C   
2170 O O   . ASP A 290 ? 0.45174 0.66641 0.56996 -0.04785 0.05376  0.26273  283 ASP A O   
2171 C CB  . ASP A 290 ? 0.39340 0.64151 0.55990 -0.07344 0.04609  0.29302  283 ASP A CB  
2172 C CG  . ASP A 290 ? 0.43065 0.70575 0.62087 -0.08613 0.03029  0.30416  283 ASP A CG  
2173 O OD1 . ASP A 290 ? 0.50452 0.81365 0.72863 -0.08089 0.03624  0.33042  283 ASP A OD1 
2174 O OD2 . ASP A 290 ? 0.38750 0.65133 0.56272 -0.10160 0.01223  0.28752  283 ASP A OD2 
2175 N N   . LEU A 291 ? 0.42287 0.59700 0.50544 -0.05535 0.05185  0.23792  284 LEU A N   
2176 C CA  . LEU A 291 ? 0.46831 0.61841 0.52310 -0.05648 0.04415  0.21541  284 LEU A CA  
2177 C C   . LEU A 291 ? 0.41300 0.55324 0.45292 -0.03649 0.05903  0.21191  284 LEU A C   
2178 O O   . LEU A 291 ? 0.38827 0.52752 0.42410 -0.03579 0.05371  0.20696  284 LEU A O   
2179 C CB  . LEU A 291 ? 0.41321 0.53335 0.44345 -0.06319 0.03855  0.19530  284 LEU A CB  
2180 C CG  . LEU A 291 ? 0.53792 0.63315 0.53972 -0.06274 0.03289  0.17264  284 LEU A CG  
2181 C CD1 . LEU A 291 ? 0.38356 0.49144 0.39225 -0.07483 0.01860  0.17039  284 LEU A CD1 
2182 C CD2 . LEU A 291 ? 0.47624 0.54488 0.46032 -0.06896 0.02791  0.15589  284 LEU A CD2 
2183 N N   . LEU A 292 ? 0.41082 0.54308 0.44172 -0.02084 0.07794  0.21420  285 LEU A N   
2184 C CA  . LEU A 292 ? 0.44118 0.56071 0.45775 -0.00208 0.09368  0.20927  285 LEU A CA  
2185 C C   . LEU A 292 ? 0.51174 0.65541 0.55776 0.00480  0.09726  0.22614  285 LEU A C   
2186 O O   . LEU A 292 ? 0.40852 0.54217 0.44767 0.01184  0.09816  0.21987  285 LEU A O   
2187 C CB  . LEU A 292 ? 0.49470 0.60594 0.49795 0.01188  0.11475  0.21047  285 LEU A CB  
2188 C CG  . LEU A 292 ? 0.47106 0.55416 0.43832 0.00897  0.11360  0.19292  285 LEU A CG  
2189 C CD1 . LEU A 292 ? 0.45650 0.53509 0.40790 0.02232  0.13536  0.19541  285 LEU A CD1 
2190 C CD2 . LEU A 292 ? 0.43285 0.48754 0.37230 0.00844  0.10553  0.17126  285 LEU A CD2 
2191 N N   . GLU A 293 ? 0.44989 0.62698 0.53198 0.00244  0.09875  0.24986  286 GLU A N   
2192 C CA  . GLU A 293 ? 0.46808 0.67262 0.58422 0.00900  0.10187  0.27041  286 GLU A CA  
2193 C C   . GLU A 293 ? 0.44414 0.65393 0.56220 -0.00389 0.08103  0.26758  286 GLU A C   
2194 O O   . GLU A 293 ? 0.40513 0.62461 0.53851 0.00473  0.08408  0.27739  286 GLU A O   
2195 C CB  . GLU A 293 ? 0.47306 0.71595 0.63008 0.00528  0.10388  0.29822  286 GLU A CB  
2196 C CG  . GLU A 293 ? 0.55795 0.80717 0.72633 0.02613  0.13200  0.31039  286 GLU A CG  
2197 C CD  . GLU A 293 ? 0.65145 0.94297 0.86584 0.02319  0.13463  0.34138  286 GLU A CD  
2198 O OE1 . GLU A 293 ? 0.75446 1.07056 1.00364 0.03611  0.14663  0.36271  286 GLU A OE1 
2199 O OE2 . GLU A 293 ? 0.58090 0.88147 0.79955 0.00807  0.12490  0.34575  286 GLU A OE2 
2200 N N   . LYS A 294 ? 0.44363 0.64715 0.54670 -0.02434 0.06072  0.25460  287 LYS A N   
2201 C CA  . LYS A 294 ? 0.38937 0.59717 0.48793 -0.03815 0.04160  0.24921  287 LYS A CA  
2202 C C   . LYS A 294 ? 0.42618 0.60265 0.49202 -0.03126 0.04308  0.22750  287 LYS A C   
2203 O O   . LYS A 294 ? 0.41935 0.60061 0.48146 -0.03946 0.03045  0.22497  287 LYS A O   
2204 C CB  . LYS A 294 ? 0.37667 0.58816 0.47094 -0.06297 0.02127  0.24150  287 LYS A CB  
2205 C CG  . LYS A 294 ? 0.37777 0.61773 0.50382 -0.07317 0.01734  0.26179  287 LYS A CG  
2206 C CD  . LYS A 294 ? 0.37960 0.64160 0.51647 -0.09867 -0.00632 0.26602  287 LYS A CD  
2207 C CE  . LYS A 294 ? 0.46367 0.74020 0.62150 -0.11455 -0.01402 0.27587  287 LYS A CE  
2208 N NZ  . LYS A 294 ? 0.38123 0.68275 0.57364 -0.10181 0.00052  0.30350  287 LYS A NZ  
2209 N N   . MET A 295 ? 0.43376 0.58012 0.47561 -0.01777 0.05743  0.21289  288 MET A N   
2210 C CA  . MET A 295 ? 0.44236 0.55838 0.45410 -0.01181 0.05869  0.19305  288 MET A CA  
2211 C C   . MET A 295 ? 0.42225 0.53132 0.43844 0.00813  0.07508  0.19826  288 MET A C   
2212 O O   . MET A 295 ? 0.44062 0.53806 0.44729 0.01031  0.07160  0.19142  288 MET A O   
2213 C CB  . MET A 295 ? 0.39237 0.47810 0.37306 -0.01192 0.06172  0.17297  288 MET A CB  
2214 C CG  . MET A 295 ? 0.38551 0.46841 0.35854 -0.03065 0.04555  0.16257  288 MET A CG  
2215 S SD  . MET A 295 ? 0.46350 0.51290 0.40566 -0.02943 0.04893  0.14326  288 MET A SD  
2216 C CE  . MET A 295 ? 0.49486 0.53913 0.43261 -0.04980 0.02959  0.12927  288 MET A CE  
2217 N N   . LEU A 296 ? 0.40723 0.52277 0.43889 0.02279  0.09377  0.21033  289 LEU A N   
2218 C CA  . LEU A 296 ? 0.42247 0.52408 0.45543 0.04356  0.11360  0.21111  289 LEU A CA  
2219 C C   . LEU A 296 ? 0.45529 0.58689 0.53180 0.05194  0.11910  0.23736  289 LEU A C   
2220 O O   . LEU A 296 ? 0.49809 0.63580 0.59406 0.06857  0.13994  0.24913  289 LEU A O   
2221 C CB  . LEU A 296 ? 0.44052 0.52508 0.45666 0.05586  0.13429  0.20382  289 LEU A CB  
2222 C CG  . LEU A 296 ? 0.46743 0.52120 0.44041 0.04957  0.13032  0.17981  289 LEU A CG  
2223 C CD1 . LEU A 296 ? 0.46493 0.50989 0.42282 0.05923  0.14971  0.17714  289 LEU A CD1 
2224 C CD2 . LEU A 296 ? 0.45012 0.47304 0.39705 0.05173  0.12686  0.16110  289 LEU A CD2 
2225 N N   . VAL A 297 ? 0.40906 0.56115 0.50207 0.04048  0.10096  0.24782  290 VAL A N   
2226 C CA  . VAL A 297 ? 0.43885 0.62070 0.57452 0.04714  0.10303  0.27502  290 VAL A CA  
2227 C C   . VAL A 297 ? 0.41341 0.57723 0.54429 0.05508  0.10389  0.27042  290 VAL A C   
2228 O O   . VAL A 297 ? 0.44573 0.58915 0.54565 0.04564  0.09166  0.25148  290 VAL A O   
2229 C CB  . VAL A 297 ? 0.42805 0.65101 0.58782 0.02648  0.08055  0.29426  290 VAL A CB  
2230 C CG1 . VAL A 297 ? 0.39063 0.62889 0.55645 0.01730  0.07893  0.29853  290 VAL A CG1 
2231 C CG2 . VAL A 297 ? 0.49797 0.71474 0.63133 0.00718  0.05767  0.27955  290 VAL A CG2 
2232 N N   . LEU A 298 ? 0.48235 0.65380 0.64675 0.07290  0.11914  0.28888  291 LEU A N   
2233 C CA  . LEU A 298 ? 0.43299 0.58433 0.59694 0.08226  0.12230  0.28587  291 LEU A CA  
2234 C C   . LEU A 298 ? 0.44730 0.61727 0.61326 0.06450  0.09695  0.29349  291 LEU A C   
2235 O O   . LEU A 298 ? 0.41829 0.56449 0.56064 0.06212  0.09114  0.27867  291 LEU A O   
2236 C CB  . LEU A 298 ? 0.44743 0.60569 0.65445 0.10508  0.14425  0.30725  291 LEU A CB  
2237 C CG  . LEU A 298 ? 0.54361 0.67450 0.74197 0.12571  0.17413  0.29457  291 LEU A CG  
2238 C CD1 . LEU A 298 ? 0.54906 0.67711 0.78716 0.14985  0.19760  0.31062  291 LEU A CD1 
2239 C CD2 . LEU A 298 ? 0.48207 0.56523 0.62462 0.12425  0.17664  0.25842  291 LEU A CD2 
2240 N N   . ASP A 299 ? 0.41550 0.62908 0.60853 0.05081  0.08144  0.31693  292 ASP A N   
2241 C CA  . ASP A 299 ? 0.50981 0.74537 0.70258 0.03203  0.05727  0.32528  292 ASP A CA  
2242 C C   . ASP A 299 ? 0.49476 0.71309 0.64015 0.01301  0.04192  0.29673  292 ASP A C   
2243 O O   . ASP A 299 ? 0.48444 0.70894 0.61846 0.00072  0.03544  0.28891  292 ASP A O   
2244 C CB  . ASP A 299 ? 0.42942 0.71721 0.66158 0.02039  0.04412  0.35774  292 ASP A CB  
2245 C CG  . ASP A 299 ? 0.47388 0.78841 0.70744 0.00142  0.02020  0.37023  292 ASP A CG  
2246 O OD1 . ASP A 299 ? 0.58126 0.93716 0.85560 -0.00185 0.01253  0.40375  292 ASP A OD1 
2247 O OD2 . ASP A 299 ? 0.49455 0.79082 0.68901 -0.01058 0.00920  0.34785  292 ASP A OD2 
2248 N N   . SER A 300 ? 0.38816 0.58516 0.50889 0.01076  0.03662  0.28227  293 SER A N   
2249 C CA  . SER A 300 ? 0.38247 0.56392 0.46165 -0.00582 0.02366  0.25630  293 SER A CA  
2250 C C   . SER A 300 ? 0.44948 0.66494 0.52837 -0.03011 0.00220  0.26299  293 SER A C   
2251 O O   . SER A 300 ? 0.48016 0.68636 0.53094 -0.04421 -0.00604 0.24236  293 SER A O   
2252 C CB  . SER A 300 ? 0.43718 0.59457 0.49599 -0.00332 0.02239  0.24418  293 SER A CB  
2253 O OG  . SER A 300 ? 0.41562 0.60080 0.49138 -0.01095 0.01007  0.26439  293 SER A OG  
2254 N N   . ASP A 301 ? 0.47037 0.72496 0.58050 -0.03596 -0.00714 0.29169  294 ASP A N   
2255 C CA  . ASP A 301 ? 0.49364 0.78205 0.60119 -0.06153 -0.02880 0.29828  294 ASP A CA  
2256 C C   . ASP A 301 ? 0.48701 0.78728 0.60209 -0.07027 -0.03122 0.29870  294 ASP A C   
2257 O O   . ASP A 301 ? 0.44899 0.76567 0.55170 -0.09358 -0.04851 0.29389  294 ASP A O   
2258 C CB  . ASP A 301 ? 0.44120 0.77149 0.58131 -0.06654 -0.03957 0.33225  294 ASP A CB  
2259 C CG  . ASP A 301 ? 0.60079 0.92326 0.73377 -0.06193 -0.04046 0.33399  294 ASP A CG  
2260 O OD1 . ASP A 301 ? 0.57883 0.87580 0.67347 -0.06734 -0.04270 0.30784  294 ASP A OD1 
2261 O OD2 . ASP A 301 ? 0.63511 0.97769 0.80378 -0.05267 -0.03860 0.36308  294 ASP A OD2 
2262 N N   . LYS A 302 ? 0.39535 0.68725 0.52980 -0.05282 -0.01387 0.30395  295 LYS A N   
2263 C CA  . LYS A 302 ? 0.46260 0.76669 0.60810 -0.05983 -0.01469 0.30731  295 LYS A CA  
2264 C C   . LYS A 302 ? 0.50007 0.76738 0.61501 -0.05742 -0.00628 0.27835  295 LYS A C   
2265 O O   . LYS A 302 ? 0.38833 0.66285 0.50777 -0.06687 -0.00957 0.27802  295 LYS A O   
2266 C CB  . LYS A 302 ? 0.42550 0.75184 0.61726 -0.04308 -0.00052 0.33673  295 LYS A CB  
2267 C CG  . LYS A 302 ? 0.43598 0.80295 0.66711 -0.04420 -0.00837 0.37112  295 LYS A CG  
2268 C CD  . LYS A 302 ? 0.40592 0.81101 0.63993 -0.07407 -0.03560 0.38259  295 LYS A CD  
2269 C CE  . LYS A 302 ? 0.55719 1.00416 0.82659 -0.07739 -0.04625 0.41772  295 LYS A CE  
2270 N NZ  . LYS A 302 ? 0.50988 0.97890 0.83422 -0.05670 -0.03050 0.45075  295 LYS A NZ  
2271 N N   . ARG A 303 ? 0.40234 0.63198 0.48864 -0.04593 0.00355  0.25615  296 ARG A N   
2272 C CA  . ARG A 303 ? 0.40622 0.60310 0.46460 -0.04424 0.01024  0.23118  296 ARG A CA  
2273 C C   . ARG A 303 ? 0.37106 0.56734 0.40917 -0.06726 -0.00680 0.21505  296 ARG A C   
2274 O O   . ARG A 303 ? 0.41739 0.62503 0.44652 -0.08256 -0.02177 0.21233  296 ARG A O   
2275 C CB  . ARG A 303 ? 0.50428 0.66371 0.53617 -0.03020 0.02098  0.21209  296 ARG A CB  
2276 C CG  . ARG A 303 ? 0.45835 0.60674 0.50351 -0.00655 0.04164  0.22039  296 ARG A CG  
2277 C CD  . ARG A 303 ? 0.42226 0.53419 0.44022 0.00318  0.04836  0.20132  296 ARG A CD  
2278 N NE  . ARG A 303 ? 0.47314 0.57683 0.50723 0.02318  0.06500  0.21093  296 ARG A NE  
2279 C CZ  . ARG A 303 ? 0.42200 0.50248 0.44518 0.03075  0.06844  0.20302  296 ARG A CZ  
2280 N NH1 . ARG A 303 ? 0.41957 0.49006 0.45986 0.04895  0.08466  0.21113  296 ARG A NH1 
2281 N NH2 . ARG A 303 ? 0.40039 0.46674 0.39658 0.01986  0.05605  0.18672  296 ARG A NH2 
2282 N N   . ILE A 304 ? 0.40813 0.59047 0.43898 -0.06970 -0.00353 0.20422  297 ILE A N   
2283 C CA  . ILE A 304 ? 0.45273 0.62859 0.46661 -0.08978 -0.01698 0.18702  297 ILE A CA  
2284 C C   . ILE A 304 ? 0.48730 0.63481 0.46793 -0.09067 -0.01867 0.16214  297 ILE A C   
2285 O O   . ILE A 304 ? 0.37228 0.49490 0.33927 -0.07518 -0.00718 0.15332  297 ILE A O   
2286 C CB  . ILE A 304 ? 0.44683 0.61358 0.46565 -0.09030 -0.01177 0.18436  297 ILE A CB  
2287 C CG1 . ILE A 304 ? 0.41764 0.58231 0.42902 -0.11304 -0.02666 0.17114  297 ILE A CG1 
2288 C CG2 . ILE A 304 ? 0.37451 0.50798 0.37384 -0.07379 0.00313  0.17041  297 ILE A CG2 
2289 C CD1 . ILE A 304 ? 0.41099 0.57116 0.43424 -0.11605 -0.02378 0.17323  297 ILE A CD1 
2290 N N   . THR A 305 ? 0.41488 0.56667 0.38205 -0.10951 -0.03279 0.15069  298 THR A N   
2291 C CA  . THR A 305 ? 0.38108 0.50867 0.31907 -0.11139 -0.03374 0.12744  298 THR A CA  
2292 C C   . THR A 305 ? 0.49302 0.59231 0.41921 -0.11235 -0.02993 0.10810  298 THR A C   
2293 O O   . THR A 305 ? 0.45401 0.55475 0.39301 -0.11672 -0.03008 0.11153  298 THR A O   
2294 C CB  . THR A 305 ? 0.40154 0.54529 0.32786 -0.13093 -0.04807 0.12183  298 THR A CB  
2295 O OG1 . THR A 305 ? 0.42338 0.57577 0.35301 -0.15032 -0.05814 0.11734  298 THR A OG1 
2296 C CG2 . THR A 305 ? 0.45492 0.63012 0.39509 -0.13100 -0.05342 0.14471  298 THR A CG2 
2297 N N   . ALA A 306 ? 0.42861 0.50331 0.33296 -0.10831 -0.02670 0.08971  299 ALA A N   
2298 C CA  . ALA A 306 ? 0.43382 0.48251 0.32970 -0.10892 -0.02351 0.07303  299 ALA A CA  
2299 C C   . ALA A 306 ? 0.40489 0.45654 0.30431 -0.12782 -0.03243 0.06413  299 ALA A C   
2300 O O   . ALA A 306 ? 0.39828 0.43958 0.30723 -0.12954 -0.03072 0.06257  299 ALA A O   
2301 C CB  . ALA A 306 ? 0.39691 0.42367 0.27199 -0.10348 -0.02023 0.05665  299 ALA A CB  
2302 N N   . ALA A 307 ? 0.40548 0.47086 0.29675 -0.14311 -0.04208 0.05826  300 ALA A N   
2303 C CA  . ALA A 307 ? 0.42218 0.48788 0.31346 -0.16319 -0.05072 0.04669  300 ALA A CA  
2304 C C   . ALA A 307 ? 0.50563 0.58715 0.42139 -0.16987 -0.05546 0.06314  300 ALA A C   
2305 O O   . ALA A 307 ? 0.45505 0.52346 0.37926 -0.17702 -0.05629 0.05644  300 ALA A O   
2306 C CB  . ALA A 307 ? 0.43637 0.51814 0.31078 -0.17960 -0.06041 0.03903  300 ALA A CB  
2307 N N   . GLN A 308 ? 0.41644 0.52699 0.34720 -0.16742 -0.05829 0.08652  301 GLN A N   
2308 C CA  . GLN A 308 ? 0.46158 0.59155 0.41930 -0.17334 -0.06235 0.10541  301 GLN A CA  
2309 C C   . GLN A 308 ? 0.46179 0.57559 0.43242 -0.15938 -0.05070 0.11009  301 GLN A C   
2310 O O   . GLN A 308 ? 0.41522 0.52914 0.40160 -0.16858 -0.05389 0.11327  301 GLN A O   
2311 C CB  . GLN A 308 ? 0.41034 0.57563 0.38567 -0.16997 -0.06524 0.13211  301 GLN A CB  
2312 C CG  . GLN A 308 ? 0.42170 0.61141 0.38873 -0.18846 -0.08030 0.13355  301 GLN A CG  
2313 C CD  . GLN A 308 ? 0.41596 0.63647 0.39908 -0.17995 -0.08074 0.16002  301 GLN A CD  
2314 O OE1 . GLN A 308 ? 0.40652 0.62239 0.40032 -0.15756 -0.06722 0.17098  301 GLN A OE1 
2315 N NE2 . GLN A 308 ? 0.44354 0.69545 0.42874 -0.19839 -0.09631 0.17063  301 GLN A NE2 
2316 N N   . ALA A 309 ? 0.39719 0.49718 0.36055 -0.13839 -0.03763 0.11089  302 ALA A N   
2317 C CA  . ALA A 309 ? 0.39233 0.47951 0.36379 -0.12560 -0.02634 0.11639  302 ALA A CA  
2318 C C   . ALA A 309 ? 0.40873 0.47215 0.37717 -0.13358 -0.02813 0.10119  302 ALA A C   
2319 O O   . ALA A 309 ? 0.43303 0.49456 0.41640 -0.13186 -0.02416 0.11015  302 ALA A O   
2320 C CB  . ALA A 309 ? 0.38420 0.45737 0.34157 -0.10461 -0.01343 0.11547  302 ALA A CB  
2321 N N   . LEU A 310 ? 0.46700 0.51273 0.41828 -0.14184 -0.03305 0.07935  303 LEU A N   
2322 C CA  . LEU A 310 ? 0.47234 0.49441 0.42533 -0.14912 -0.03395 0.06502  303 LEU A CA  
2323 C C   . LEU A 310 ? 0.51278 0.54390 0.48665 -0.16679 -0.04267 0.07015  303 LEU A C   
2324 O O   . LEU A 310 ? 0.43485 0.45066 0.42154 -0.16964 -0.04141 0.06873  303 LEU A O   
2325 C CB  . LEU A 310 ? 0.43105 0.43445 0.36364 -0.15426 -0.03574 0.04045  303 LEU A CB  
2326 C CG  . LEU A 310 ? 0.46235 0.45184 0.37713 -0.13808 -0.02749 0.03409  303 LEU A CG  
2327 C CD1 . LEU A 310 ? 0.47290 0.45170 0.36958 -0.14440 -0.02922 0.01258  303 LEU A CD1 
2328 C CD2 . LEU A 310 ? 0.41879 0.38867 0.33903 -0.12671 -0.01980 0.03633  303 LEU A CD2 
2329 N N   . ALA A 311 ? 0.53841 0.59514 0.51776 -0.17968 -0.05245 0.07783  304 ALA A N   
2330 C CA  . ALA A 311 ? 0.51033 0.57855 0.51001 -0.19905 -0.06297 0.08415  304 ALA A CA  
2331 C C   . ALA A 311 ? 0.49461 0.58412 0.52257 -0.19312 -0.05978 0.11233  304 ALA A C   
2332 O O   . ALA A 311 ? 0.44835 0.54962 0.49773 -0.20894 -0.06855 0.12144  304 ALA A O   
2333 C CB  . ALA A 311 ? 0.48495 0.57416 0.47708 -0.21838 -0.07691 0.08101  304 ALA A CB  
2334 N N   . HIS A 312 ? 0.52366 0.61820 0.55200 -0.17149 -0.04701 0.12585  305 HIS A N   
2335 C CA  . HIS A 312 ? 0.44231 0.55700 0.49593 -0.16392 -0.04051 0.15186  305 HIS A CA  
2336 C C   . HIS A 312 ? 0.42117 0.52213 0.48964 -0.16842 -0.03911 0.15383  305 HIS A C   
2337 O O   . HIS A 312 ? 0.42501 0.49676 0.48190 -0.16698 -0.03682 0.13744  305 HIS A O   
2338 C CB  . HIS A 312 ? 0.40150 0.51784 0.44676 -0.13934 -0.02462 0.16060  305 HIS A CB  
2339 C CG  . HIS A 312 ? 0.45606 0.59888 0.52607 -0.13022 -0.01575 0.18778  305 HIS A CG  
2340 N ND1 . HIS A 312 ? 0.42587 0.56790 0.50883 -0.12553 -0.00728 0.19916  305 HIS A ND1 
2341 C CD2 . HIS A 312 ? 0.41455 0.58675 0.50065 -0.12431 -0.01285 0.20714  305 HIS A CD2 
2342 C CE1 . HIS A 312 ? 0.40294 0.57268 0.50722 -0.11692 0.00154  0.22307  305 HIS A CE1 
2343 N NE2 . HIS A 312 ? 0.39895 0.58689 0.50720 -0.11547 -0.00138 0.22843  305 HIS A NE2 
2344 N N   . ALA A 313 ? 0.45034 0.57451 0.54804 -0.17391 -0.04053 0.17653  306 ALA A N   
2345 C CA  . ALA A 313 ? 0.43927 0.55432 0.55578 -0.17954 -0.03998 0.18283  306 ALA A CA  
2346 C C   . ALA A 313 ? 0.42394 0.51993 0.52915 -0.16125 -0.02558 0.18225  306 ALA A C   
2347 O O   . ALA A 313 ? 0.43120 0.51018 0.54515 -0.16594 -0.02622 0.18081  306 ALA A O   
2348 C CB  . ALA A 313 ? 0.43045 0.57882 0.58145 -0.18551 -0.04155 0.21183  306 ALA A CB  
2349 N N   . TYR A 314 ? 0.41346 0.51163 0.49985 -0.14153 -0.01325 0.18376  307 TYR A N   
2350 C CA  . TYR A 314 ? 0.46306 0.54507 0.53497 -0.12595 -0.00062 0.18352  307 TYR A CA  
2351 C C   . TYR A 314 ? 0.44212 0.49128 0.49942 -0.12939 -0.00503 0.16249  307 TYR A C   
2352 O O   . TYR A 314 ? 0.42968 0.46623 0.48407 -0.12312 0.00082  0.16560  307 TYR A O   
2353 C CB  . TYR A 314 ? 0.40432 0.49053 0.45522 -0.10651 0.01206  0.18424  307 TYR A CB  
2354 C CG  . TYR A 314 ? 0.49348 0.56588 0.52597 -0.09190 0.02494  0.18480  307 TYR A CG  
2355 C CD1 . TYR A 314 ? 0.46022 0.54255 0.50481 -0.08930 0.03292  0.20300  307 TYR A CD1 
2356 C CD2 . TYR A 314 ? 0.40516 0.45625 0.40751 -0.08212 0.02841  0.16815  307 TYR A CD2 
2357 C CE1 . TYR A 314 ? 0.41892 0.49067 0.44298 -0.07796 0.04379  0.20391  307 TYR A CE1 
2358 C CE2 . TYR A 314 ? 0.41086 0.45031 0.39411 -0.07129 0.03829  0.16874  307 TYR A CE2 
2359 C CZ  . TYR A 314 ? 0.44049 0.49051 0.43311 -0.06955 0.04584  0.18630  307 TYR A CZ  
2360 O OH  . TYR A 314 ? 0.42795 0.46838 0.39804 -0.06069 0.05484  0.18728  307 TYR A OH  
2361 N N   . PHE A 315 ? 0.41832 0.45499 0.46704 -0.13933 -0.01475 0.14222  308 PHE A N   
2362 C CA  . PHE A 315 ? 0.43317 0.43945 0.47028 -0.14137 -0.01712 0.12151  308 PHE A CA  
2363 C C   . PHE A 315 ? 0.55287 0.54667 0.60874 -0.16020 -0.02714 0.11268  308 PHE A C   
2364 O O   . PHE A 315 ? 0.53477 0.50492 0.58221 -0.16459 -0.02977 0.09145  308 PHE A O   
2365 C CB  . PHE A 315 ? 0.45499 0.45305 0.46544 -0.13670 -0.01751 0.10257  308 PHE A CB  
2366 C CG  . PHE A 315 ? 0.41462 0.42079 0.40716 -0.11927 -0.00819 0.10897  308 PHE A CG  
2367 C CD1 . PHE A 315 ? 0.44125 0.43683 0.42318 -0.10579 0.00097  0.11291  308 PHE A CD1 
2368 C CD2 . PHE A 315 ? 0.41188 0.43579 0.39852 -0.11727 -0.00896 0.11134  308 PHE A CD2 
2369 C CE1 . PHE A 315 ? 0.42124 0.42062 0.38480 -0.09103 0.00985  0.11612  308 PHE A CE1 
2370 C CE2 . PHE A 315 ? 0.41706 0.44485 0.38968 -0.10100 0.00056  0.11634  308 PHE A CE2 
2371 C CZ  . PHE A 315 ? 0.39438 0.40827 0.35432 -0.08807 0.01031  0.11722  308 PHE A CZ  
2372 N N   . ALA A 316 ? 0.44512 0.45360 0.52747 -0.17150 -0.03199 0.12839  309 ALA A N   
2373 C CA  . ALA A 316 ? 0.51954 0.51435 0.62035 -0.19147 -0.04227 0.11901  309 ALA A CA  
2374 C C   . ALA A 316 ? 0.55178 0.51422 0.65817 -0.18987 -0.03936 0.10846  309 ALA A C   
2375 O O   . ALA A 316 ? 0.50176 0.44169 0.61248 -0.20257 -0.04488 0.08879  309 ALA A O   
2376 C CB  . ALA A 316 ? 0.46913 0.48581 0.60110 -0.20302 -0.04757 0.14198  309 ALA A CB  
2377 N N   . GLN A 317 ? 0.51169 0.47149 0.61838 -0.17479 -0.03044 0.12138  310 GLN A N   
2378 C CA  . GLN A 317 ? 0.56770 0.50091 0.68522 -0.17282 -0.02826 0.11719  310 GLN A CA  
2379 C C   . GLN A 317 ? 0.59445 0.50450 0.69129 -0.16630 -0.02558 0.09312  310 GLN A C   
2380 O O   . GLN A 317 ? 0.58864 0.47473 0.69856 -0.16639 -0.02435 0.08651  310 GLN A O   
2381 C CB  . GLN A 317 ? 0.55426 0.49662 0.67743 -0.16059 -0.02097 0.14174  310 GLN A CB  
2382 C CG  . GLN A 317 ? 0.59900 0.56560 0.74512 -0.16588 -0.02133 0.16817  310 GLN A CG  
2383 C CD  . GLN A 317 ? 0.79861 0.75416 0.98123 -0.18236 -0.02895 0.17293  310 GLN A CD  
2384 O OE1 . GLN A 317 ? 0.83837 0.78481 1.02955 -0.19761 -0.03745 0.15778  310 GLN A OE1 
2385 N NE2 . GLN A 317 ? 0.80604 0.76208 1.00989 -0.18044 -0.02623 0.19428  310 GLN A NE2 
2386 N N   . TYR A 318 ? 0.55364 0.47111 0.62192 -0.16048 -0.02426 0.08164  311 TYR A N   
2387 C CA  . TYR A 318 ? 0.54916 0.44839 0.59793 -0.15400 -0.02118 0.06087  311 TYR A CA  
2388 C C   . TYR A 318 ? 0.53431 0.43286 0.56643 -0.16319 -0.02536 0.03877  311 TYR A C   
2389 O O   . TYR A 318 ? 0.52310 0.40409 0.54387 -0.16121 -0.02258 0.01916  311 TYR A O   
2390 C CB  . TYR A 318 ? 0.47286 0.37956 0.49929 -0.13653 -0.01463 0.06822  311 TYR A CB  
2391 C CG  . TYR A 318 ? 0.54657 0.45516 0.58204 -0.12796 -0.01036 0.08901  311 TYR A CG  
2392 C CD1 . TYR A 318 ? 0.51474 0.40476 0.56205 -0.12515 -0.00921 0.08953  311 TYR A CD1 
2393 C CD2 . TYR A 318 ? 0.53401 0.46451 0.56677 -0.12285 -0.00691 0.10919  311 TYR A CD2 
2394 C CE1 . TYR A 318 ? 0.56976 0.46445 0.62390 -0.11907 -0.00669 0.11057  311 TYR A CE1 
2395 C CE2 . TYR A 318 ? 0.50236 0.43630 0.53922 -0.11630 -0.00253 0.12794  311 TYR A CE2 
2396 C CZ  . TYR A 318 ? 0.58133 0.49805 0.62784 -0.11525 -0.00343 0.12904  311 TYR A CZ  
2397 O OH  . TYR A 318 ? 0.52988 0.45283 0.57913 -0.11039 -0.00044 0.14966  311 TYR A OH  
2398 N N   . HIS A 319 ? 0.54729 0.46631 0.57846 -0.17366 -0.03191 0.04275  312 HIS A N   
2399 C CA  . HIS A 319 ? 0.59060 0.51486 0.60230 -0.18304 -0.03699 0.02523  312 HIS A CA  
2400 C C   . HIS A 319 ? 0.61555 0.51576 0.62976 -0.19832 -0.04005 0.00044  312 HIS A C   
2401 O O   . HIS A 319 ? 0.59656 0.48528 0.63363 -0.20988 -0.04360 0.00061  312 HIS A O   
2402 C CB  . HIS A 319 ? 0.52634 0.48146 0.54141 -0.19197 -0.04474 0.03984  312 HIS A CB  
2403 C CG  . HIS A 319 ? 0.51955 0.48375 0.51735 -0.20616 -0.05294 0.02504  312 HIS A CG  
2404 N ND1 . HIS A 319 ? 0.48127 0.44424 0.45234 -0.20047 -0.05021 0.01119  312 HIS A ND1 
2405 C CD2 . HIS A 319 ? 0.53032 0.50701 0.53307 -0.22723 -0.06467 0.02331  312 HIS A CD2 
2406 C CE1 . HIS A 319 ? 0.50223 0.47733 0.46127 -0.21710 -0.05936 0.00182  312 HIS A CE1 
2407 N NE2 . HIS A 319 ? 0.57660 0.56007 0.55353 -0.23407 -0.06878 0.00845  312 HIS A NE2 
2408 N N   . ASP A 320 ? 0.60691 0.49886 0.59758 -0.19843 -0.03773 -0.02131 313 ASP A N   
2409 C CA  . ASP A 320 ? 0.60254 0.47247 0.58897 -0.21300 -0.03841 -0.04879 313 ASP A CA  
2410 C C   . ASP A 320 ? 0.61253 0.49391 0.56652 -0.21768 -0.03996 -0.06433 313 ASP A C   
2411 O O   . ASP A 320 ? 0.67510 0.55344 0.61302 -0.20466 -0.03235 -0.07065 313 ASP A O   
2412 C CB  . ASP A 320 ? 0.72435 0.56180 0.72315 -0.20413 -0.02805 -0.06087 313 ASP A CB  
2413 C CG  . ASP A 320 ? 0.71655 0.52837 0.71115 -0.21766 -0.02543 -0.09174 313 ASP A CG  
2414 O OD1 . ASP A 320 ? 0.65450 0.47272 0.63585 -0.23682 -0.03344 -0.10381 313 ASP A OD1 
2415 O OD2 . ASP A 320 ? 0.79457 0.58015 0.79926 -0.20945 -0.01501 -0.10383 313 ASP A OD2 
2416 N N   . PRO A 321 ? 0.67538 0.57190 0.61948 -0.23730 -0.05057 -0.06926 314 PRO A N   
2417 C CA  . PRO A 321 ? 0.70894 0.62128 0.62138 -0.24303 -0.05325 -0.08044 314 PRO A CA  
2418 C C   . PRO A 321 ? 0.73410 0.62296 0.62723 -0.24234 -0.04349 -0.10959 314 PRO A C   
2419 O O   . PRO A 321 ? 0.74764 0.64843 0.61623 -0.23829 -0.04104 -0.11465 314 PRO A O   
2420 C CB  . PRO A 321 ? 0.74313 0.67322 0.65267 -0.26836 -0.06811 -0.08054 314 PRO A CB  
2421 C CG  . PRO A 321 ? 0.63030 0.54044 0.56683 -0.27847 -0.07069 -0.08203 314 PRO A CG  
2422 C CD  . PRO A 321 ? 0.67197 0.57324 0.63371 -0.25680 -0.06166 -0.06373 314 PRO A CD  
2423 N N   . ASP A 322 ? 0.78057 0.63673 0.68630 -0.24573 -0.03686 -0.12796 315 ASP A N   
2424 C CA  . ASP A 322 ? 0.74596 0.57849 0.63708 -0.24415 -0.02483 -0.15643 315 ASP A CA  
2425 C C   . ASP A 322 ? 0.72253 0.54566 0.62113 -0.21973 -0.01197 -0.15127 315 ASP A C   
2426 O O   . ASP A 322 ? 0.76371 0.57082 0.65289 -0.21547 -0.00040 -0.17169 315 ASP A O   
2427 C CB  . ASP A 322 ? 0.79253 0.59132 0.69743 -0.25748 -0.02146 -0.17913 315 ASP A CB  
2428 C CG  . ASP A 322 ? 0.82610 0.63625 0.72600 -0.27795 -0.03554 -0.18222 315 ASP A CG  
2429 O OD1 . ASP A 322 ? 0.85945 0.68611 0.73052 -0.28528 -0.03937 -0.19281 315 ASP A OD1 
2430 O OD2 . ASP A 322 ? 0.91617 0.72015 0.84219 -0.28659 -0.04298 -0.17205 315 ASP A OD2 
2431 N N   . ASP A 323 ? 0.71196 0.54547 0.62658 -0.20439 -0.01347 -0.12460 316 ASP A N   
2432 C CA  . ASP A 323 ? 0.65266 0.47841 0.57485 -0.18338 -0.00380 -0.11739 316 ASP A CA  
2433 C C   . ASP A 323 ? 0.66329 0.51457 0.57338 -0.17154 -0.00732 -0.09629 316 ASP A C   
2434 O O   . ASP A 323 ? 0.59558 0.44514 0.51653 -0.15639 -0.00425 -0.08071 316 ASP A O   
2435 C CB  . ASP A 323 ? 0.65443 0.46031 0.61071 -0.17610 -0.00045 -0.10719 316 ASP A CB  
2436 C CG  . ASP A 323 ? 0.73848 0.53348 0.70428 -0.15765 0.00928  -0.10318 316 ASP A CG  
2437 O OD1 . ASP A 323 ? 0.62255 0.41661 0.57244 -0.15262 0.01623  -0.11634 316 ASP A OD1 
2438 O OD2 . ASP A 323 ? 0.66884 0.45834 0.65853 -0.14901 0.00946  -0.08531 316 ASP A OD2 
2439 N N   . GLU A 324 ? 0.64625 0.52102 0.53417 -0.17899 -0.01391 -0.09529 317 GLU A N   
2440 C CA  . GLU A 324 ? 0.49857 0.39586 0.37549 -0.16826 -0.01628 -0.07719 317 GLU A CA  
2441 C C   . GLU A 324 ? 0.63007 0.53847 0.48065 -0.17144 -0.01531 -0.08875 317 GLU A C   
2442 O O   . GLU A 324 ? 0.62641 0.55791 0.46329 -0.18126 -0.02326 -0.08437 317 GLU A O   
2443 C CB  . GLU A 324 ? 0.57987 0.49973 0.46338 -0.17296 -0.02573 -0.05679 317 GLU A CB  
2444 C CG  . GLU A 324 ? 0.58022 0.49363 0.48875 -0.16717 -0.02525 -0.04084 317 GLU A CG  
2445 C CD  . GLU A 324 ? 0.60812 0.54104 0.52838 -0.17782 -0.03412 -0.02593 317 GLU A CD  
2446 O OE1 . GLU A 324 ? 0.61599 0.54655 0.55736 -0.17494 -0.03371 -0.01185 317 GLU A OE1 
2447 O OE2 . GLU A 324 ? 0.58945 0.54229 0.49905 -0.18956 -0.04180 -0.02643 317 GLU A OE2 
2448 N N   . PRO A 325 ? 0.61073 0.50548 0.45561 -0.16348 -0.00572 -0.10141 318 PRO A N   
2449 C CA  . PRO A 325 ? 0.58250 0.48599 0.40277 -0.16897 -0.00294 -0.11578 318 PRO A CA  
2450 C C   . PRO A 325 ? 0.64908 0.57700 0.45588 -0.16270 -0.00714 -0.09955 318 PRO A C   
2451 O O   . PRO A 325 ? 0.55983 0.49279 0.37588 -0.15093 -0.00939 -0.08001 318 PRO A O   
2452 C CB  . PRO A 325 ? 0.60276 0.48373 0.42891 -0.15944 0.01039  -0.13044 318 PRO A CB  
2453 C CG  . PRO A 325 ? 0.56559 0.43546 0.41555 -0.14420 0.01179  -0.11409 318 PRO A CG  
2454 C CD  . PRO A 325 ? 0.57597 0.44910 0.43871 -0.14926 0.00300  -0.10078 318 PRO A CD  
2455 N N   . VAL A 326 ? 0.65302 0.59561 0.43715 -0.17139 -0.00758 -0.10841 319 VAL A N   
2456 C CA  . VAL A 326 ? 0.56836 0.53382 0.34055 -0.16675 -0.01096 -0.09393 319 VAL A CA  
2457 C C   . VAL A 326 ? 0.58945 0.54931 0.35236 -0.15903 -0.00075 -0.10345 319 VAL A C   
2458 O O   . VAL A 326 ? 0.57250 0.51433 0.33597 -0.15916 0.00915  -0.12254 319 VAL A O   
2459 C CB  . VAL A 326 ? 0.56356 0.55730 0.31905 -0.18368 -0.02150 -0.09006 319 VAL A CB  
2460 C CG1 . VAL A 326 ? 0.54725 0.54939 0.31670 -0.19089 -0.03190 -0.07734 319 VAL A CG1 
2461 C CG2 . VAL A 326 ? 0.54854 0.54145 0.28128 -0.20022 -0.01849 -0.11495 319 VAL A CG2 
2462 N N   . ALA A 327 ? 0.63430 0.60992 0.39135 -0.15202 -0.00259 -0.08897 320 ALA A N   
2463 C CA  . ALA A 327 ? 0.56907 0.54272 0.32056 -0.14413 0.00591  -0.09299 320 ALA A CA  
2464 C C   . ALA A 327 ? 0.64269 0.63859 0.37028 -0.15571 0.00595  -0.09876 320 ALA A C   
2465 O O   . ALA A 327 ? 0.66208 0.67967 0.37802 -0.16790 -0.00353 -0.09225 320 ALA A O   
2466 C CB  . ALA A 327 ? 0.49388 0.46792 0.25535 -0.12926 0.00397  -0.07312 320 ALA A CB  
2467 N N   . ASP A 328 ? 0.80630 0.79885 0.52761 -0.15214 0.01687  -0.10954 321 ASP A N   
2468 C CA  . ASP A 328 ? 0.81042 0.82639 0.50980 -0.16069 0.01835  -0.11149 321 ASP A CA  
2469 C C   . ASP A 328 ? 0.72218 0.76030 0.42166 -0.15733 0.00886  -0.08575 321 ASP A C   
2470 O O   . ASP A 328 ? 0.64079 0.67044 0.35803 -0.14459 0.00563  -0.07024 321 ASP A O   
2471 C CB  . ASP A 328 ? 0.76514 0.77344 0.46285 -0.15463 0.03390  -0.12535 321 ASP A CB  
2472 C CG  . ASP A 328 ? 0.92450 0.91193 0.62427 -0.15749 0.04536  -0.15110 321 ASP A CG  
2473 O OD1 . ASP A 328 ? 0.97939 0.97253 0.67005 -0.16862 0.04315  -0.16051 321 ASP A OD1 
2474 O OD2 . ASP A 328 ? 0.90281 0.86789 0.61828 -0.14727 0.05622  -0.15940 321 ASP A OD2 
2475 N N   . PRO A 329 ? 0.86565 0.93020 0.55793 -0.16418 0.00470  -0.07742 322 PRO A N   
2476 C CA  . PRO A 329 ? 0.77379 0.85855 0.47101 -0.16061 -0.00367 -0.05186 322 PRO A CA  
2477 C C   . PRO A 329 ? 0.67274 0.75002 0.37431 -0.14859 0.00245  -0.04564 322 PRO A C   
2478 O O   . PRO A 329 ? 0.71953 0.79259 0.41640 -0.14657 0.01325  -0.05756 322 PRO A O   
2479 C CB  . PRO A 329 ? 0.84662 0.95946 0.53507 -0.17171 -0.00678 -0.04803 322 PRO A CB  
2480 C CG  . PRO A 329 ? 0.82927 0.93368 0.50475 -0.17691 0.00459  -0.07336 322 PRO A CG  
2481 C CD  . PRO A 329 ? 0.84682 0.92260 0.52621 -0.17524 0.00860  -0.09103 322 PRO A CD  
2482 N N   . TYR A 330 ? 0.69227 0.76711 0.40568 -0.14002 -0.00396 -0.02629 323 TYR A N   
2483 C CA  . TYR A 330 ? 0.65191 0.71647 0.37758 -0.12732 -0.00048 -0.01754 323 TYR A CA  
2484 C C   . TYR A 330 ? 0.67004 0.75788 0.39473 -0.12924 -0.00597 0.00328  323 TYR A C   
2485 O O   . TYR A 330 ? 0.62098 0.71970 0.35140 -0.13022 -0.01486 0.02013  323 TYR A O   
2486 C CB  . TYR A 330 ? 0.54385 0.58360 0.28757 -0.11467 -0.00276 -0.01201 323 TYR A CB  
2487 C CG  . TYR A 330 ? 0.52922 0.55675 0.28348 -0.10402 -0.00078 -0.00438 323 TYR A CG  
2488 C CD1 . TYR A 330 ? 0.57869 0.60030 0.33434 -0.10176 0.00726  -0.01376 323 TYR A CD1 
2489 C CD2 . TYR A 330 ? 0.57704 0.59886 0.34099 -0.09676 -0.00664 0.01224  323 TYR A CD2 
2490 C CE1 . TYR A 330 ? 0.58970 0.60217 0.35631 -0.09399 0.00727  -0.00524 323 TYR A CE1 
2491 C CE2 . TYR A 330 ? 0.52964 0.53884 0.30163 -0.08942 -0.00620 0.01814  323 TYR A CE2 
2492 C CZ  . TYR A 330 ? 0.58467 0.59037 0.35801 -0.08882 -0.00031 0.01015  323 TYR A CZ  
2493 O OH  . TYR A 330 ? 0.60010 0.59514 0.38280 -0.08335 -0.00161 0.01754  323 TYR A OH  
2494 N N   . ASP A 331 ? 0.57454 0.67061 0.29527 -0.12927 -0.00014 0.00382  324 ASP A N   
2495 C CA  . ASP A 331 ? 0.63584 0.75426 0.36079 -0.13075 -0.00469 0.02420  324 ASP A CA  
2496 C C   . ASP A 331 ? 0.64084 0.74435 0.38289 -0.11981 -0.00833 0.04062  324 ASP A C   
2497 O O   . ASP A 331 ? 0.58410 0.67201 0.33396 -0.11268 -0.00325 0.03681  324 ASP A O   
2498 C CB  . ASP A 331 ? 0.64566 0.77965 0.36301 -0.13490 0.00385  0.01796  324 ASP A CB  
2499 C CG  . ASP A 331 ? 0.73121 0.88345 0.45801 -0.13407 0.00030  0.04021  324 ASP A CG  
2500 O OD1 . ASP A 331 ? 0.73344 0.89698 0.47084 -0.13489 -0.00966 0.05889  324 ASP A OD1 
2501 O OD2 . ASP A 331 ? 0.75017 0.90621 0.47602 -0.13271 0.00794  0.04010  324 ASP A OD2 
2502 N N   . GLN A 332 ? 0.63931 0.74631 0.39160 -0.11770 -0.01695 0.05869  325 GLN A N   
2503 C CA  . GLN A 332 ? 0.63664 0.72735 0.40739 -0.10722 -0.02009 0.07351  325 GLN A CA  
2504 C C   . GLN A 332 ? 0.56343 0.67567 0.34141 -0.11048 -0.02470 0.09655  325 GLN A C   
2505 O O   . GLN A 332 ? 0.49104 0.59517 0.28593 -0.10402 -0.02928 0.11296  325 GLN A O   
2506 C CB  . GLN A 332 ? 0.61255 0.68666 0.39359 -0.09981 -0.02363 0.07694  325 GLN A CB  
2507 C CG  . GLN A 332 ? 0.67513 0.72624 0.45243 -0.09558 -0.01961 0.05780  325 GLN A CG  
2508 C CD  . GLN A 332 ? 0.71472 0.75504 0.50100 -0.08925 -0.02191 0.06268  325 GLN A CD  
2509 O OE1 . GLN A 332 ? 0.65043 0.69536 0.43328 -0.09299 -0.02234 0.05623  325 GLN A OE1 
2510 N NE2 . GLN A 332 ? 0.65419 0.67959 0.45255 -0.07986 -0.02265 0.07388  325 GLN A NE2 
2511 N N   . SER A 333 ? 0.51682 0.65470 0.28650 -0.11905 -0.02247 0.09688  326 SER A N   
2512 C CA  . SER A 333 ? 0.66623 0.82533 0.45012 -0.12095 -0.02674 0.11790  326 SER A CA  
2513 C C   . SER A 333 ? 0.55057 0.69417 0.34711 -0.11482 -0.02737 0.13127  326 SER A C   
2514 O O   . SER A 333 ? 0.56390 0.71065 0.37951 -0.11232 -0.03311 0.15206  326 SER A O   
2515 C CB  . SER A 333 ? 0.60665 0.79329 0.38048 -0.13012 -0.02257 0.11190  326 SER A CB  
2516 O OG  . SER A 333 ? 0.77446 0.97519 0.53742 -0.13806 -0.02396 0.10163  326 SER A OG  
2517 N N   . PHE A 334 ? 0.48494 0.60964 0.27680 -0.11159 -0.02165 0.11849  327 PHE A N   
2518 C CA  . PHE A 334 ? 0.50923 0.61659 0.31813 -0.10601 -0.02322 0.12764  327 PHE A CA  
2519 C C   . PHE A 334 ? 0.54147 0.62397 0.36679 -0.09817 -0.02970 0.13774  327 PHE A C   
2520 O O   . PHE A 334 ? 0.60422 0.67415 0.44461 -0.09577 -0.03297 0.14924  327 PHE A O   
2521 C CB  . PHE A 334 ? 0.39979 0.48720 0.20701 -0.10194 -0.01725 0.10949  327 PHE A CB  
2522 C CG  . PHE A 334 ? 0.50415 0.56061 0.31046 -0.09446 -0.01776 0.09444  327 PHE A CG  
2523 C CD1 . PHE A 334 ? 0.39269 0.44911 0.18620 -0.09504 -0.01344 0.07728  327 PHE A CD1 
2524 C CD2 . PHE A 334 ? 0.47340 0.50075 0.29066 -0.08792 -0.02256 0.09749  327 PHE A CD2 
2525 C CE1 . PHE A 334 ? 0.45751 0.48792 0.25133 -0.08862 -0.01387 0.06592  327 PHE A CE1 
2526 C CE2 . PHE A 334 ? 0.48725 0.48873 0.30099 -0.08188 -0.02254 0.08457  327 PHE A CE2 
2527 C CZ  . PHE A 334 ? 0.48956 0.49381 0.29264 -0.08191 -0.01818 0.07001  327 PHE A CZ  
2528 N N   . GLU A 335 ? 0.49149 0.56597 0.31490 -0.09431 -0.03087 0.13337  328 GLU A N   
2529 C CA  . GLU A 335 ? 0.50550 0.55370 0.34350 -0.08520 -0.03370 0.13975  328 GLU A CA  
2530 C C   . GLU A 335 ? 0.50713 0.56519 0.36485 -0.08530 -0.03848 0.16553  328 GLU A C   
2531 O O   . GLU A 335 ? 0.51853 0.55017 0.39127 -0.07803 -0.03956 0.17124  328 GLU A O   
2532 C CB  . GLU A 335 ? 0.43510 0.47819 0.26873 -0.08108 -0.03235 0.13166  328 GLU A CB  
2533 C CG  . GLU A 335 ? 0.53483 0.55773 0.35511 -0.07822 -0.02802 0.10816  328 GLU A CG  
2534 C CD  . GLU A 335 ? 0.48600 0.47285 0.30990 -0.07029 -0.02739 0.10166  328 GLU A CD  
2535 O OE1 . GLU A 335 ? 0.57186 0.54637 0.40774 -0.06711 -0.02983 0.11314  328 GLU A OE1 
2536 O OE2 . GLU A 335 ? 0.51734 0.48803 0.33201 -0.06816 -0.02484 0.08543  328 GLU A OE2 
2537 N N   . SER A 336 ? 0.52111 0.61620 0.37905 -0.09393 -0.04120 0.18143  329 SER A N   
2538 C CA  . SER A 336 ? 0.59957 0.70767 0.48102 -0.09392 -0.04609 0.20790  329 SER A CA  
2539 C C   . SER A 336 ? 0.62230 0.73442 0.51454 -0.09721 -0.04732 0.21727  329 SER A C   
2540 O O   . SER A 336 ? 0.65422 0.77047 0.57158 -0.09552 -0.05101 0.23654  329 SER A O   
2541 C CB  . SER A 336 ? 0.61976 0.76608 0.50581 -0.09931 -0.04876 0.21467  329 SER A CB  
2542 O OG  . SER A 336 ? 0.60513 0.77688 0.47248 -0.10907 -0.04673 0.20259  329 SER A OG  
2543 N N   . ARG A 337 ? 0.56772 0.67962 0.44457 -0.10168 -0.04400 0.20525  330 ARG A N   
2544 C CA  . ARG A 337 ? 0.50026 0.61874 0.38891 -0.10528 -0.04485 0.21524  330 ARG A CA  
2545 C C   . ARG A 337 ? 0.50642 0.58675 0.40843 -0.10104 -0.04845 0.22042  330 ARG A C   
2546 O O   . ARG A 337 ? 0.49133 0.53869 0.38744 -0.09436 -0.04702 0.20130  330 ARG A O   
2547 C CB  . ARG A 337 ? 0.52788 0.66228 0.39800 -0.11113 -0.03845 0.20170  330 ARG A CB  
2548 C CG  . ARG A 337 ? 0.53894 0.69655 0.38780 -0.11495 -0.03329 0.18624  330 ARG A CG  
2549 C CD  . ARG A 337 ? 0.58532 0.78172 0.43770 -0.12189 -0.03329 0.19528  330 ARG A CD  
2550 N NE  . ARG A 337 ? 0.81481 1.02917 0.65270 -0.12624 -0.03292 0.18527  330 ARG A NE  
2551 C CZ  . ARG A 337 ? 0.76481 0.97800 0.57912 -0.12868 -0.02638 0.16240  330 ARG A CZ  
2552 N NH1 . ARG A 337 ? 0.62935 0.82654 0.43227 -0.12641 -0.01863 0.14752  330 ARG A NH1 
2553 N NH2 . ARG A 337 ? 0.66424 0.89274 0.46817 -0.13422 -0.02790 0.15498  330 ARG A NH2 
2554 N N   . ASP A 338 ? 0.49392 0.57720 0.41920 -0.10264 -0.05231 0.23755  331 ASP A N   
2555 C CA  . ASP A 338 ? 0.52704 0.57435 0.46681 -0.10121 -0.05680 0.24205  331 ASP A CA  
2556 C C   . ASP A 338 ? 0.54539 0.60566 0.48924 -0.10829 -0.05728 0.24496  331 ASP A C   
2557 O O   . ASP A 338 ? 0.52718 0.61362 0.48820 -0.11188 -0.05840 0.25974  331 ASP A O   
2558 C CB  . ASP A 338 ? 0.66733 0.70367 0.63561 -0.09670 -0.06061 0.25896  331 ASP A CB  
2559 C CG  . ASP A 338 ? 0.77287 0.78257 0.74083 -0.08778 -0.05904 0.25551  331 ASP A CG  
2560 O OD1 . ASP A 338 ? 0.67185 0.64950 0.62530 -0.08278 -0.05649 0.23278  331 ASP A OD1 
2561 O OD2 . ASP A 338 ? 0.64074 0.66400 0.62643 -0.08328 -0.05863 0.26835  331 ASP A OD2 
2562 N N   . LEU A 339 ? 0.46473 0.50861 0.39634 -0.10895 -0.05593 0.22848  332 LEU A N   
2563 C CA  . LEU A 339 ? 0.55691 0.61531 0.49272 -0.11537 -0.05514 0.23186  332 LEU A CA  
2564 C C   . LEU A 339 ? 0.57179 0.59488 0.52004 -0.11656 -0.06259 0.22940  332 LEU A C   
2565 O O   . LEU A 339 ? 0.58972 0.57538 0.53778 -0.11242 -0.06706 0.22083  332 LEU A O   
2566 C CB  . LEU A 339 ? 0.50978 0.58525 0.42532 -0.11464 -0.04596 0.21276  332 LEU A CB  
2567 C CG  . LEU A 339 ? 0.52249 0.63081 0.42064 -0.11574 -0.03879 0.21085  332 LEU A CG  
2568 C CD1 . LEU A 339 ? 0.42928 0.54028 0.30735 -0.11331 -0.02964 0.18598  332 LEU A CD1 
2569 C CD2 . LEU A 339 ? 0.49713 0.64459 0.40435 -0.12170 -0.03661 0.22805  332 LEU A CD2 
2570 N N   . LEU A 340 ? 0.52037 0.55668 0.47900 -0.12304 -0.06363 0.23708  333 LEU A N   
2571 C CA  . LEU A 340 ? 0.64623 0.65387 0.61762 -0.12733 -0.07269 0.23716  333 LEU A CA  
2572 C C   . LEU A 340 ? 0.56800 0.56165 0.52593 -0.12511 -0.07158 0.21534  333 LEU A C   
2573 O O   . LEU A 340 ? 0.51812 0.52926 0.46200 -0.12068 -0.06237 0.20295  333 LEU A O   
2574 C CB  . LEU A 340 ? 0.45270 0.48369 0.44810 -0.13545 -0.07561 0.25820  333 LEU A CB  
2575 C CG  . LEU A 340 ? 0.68123 0.72883 0.69565 -0.13480 -0.07668 0.27442  333 LEU A CG  
2576 C CD1 . LEU A 340 ? 0.45909 0.53427 0.49718 -0.14095 -0.07828 0.29062  333 LEU A CD1 
2577 C CD2 . LEU A 340 ? 0.54338 0.55117 0.56745 -0.13267 -0.08464 0.27457  333 LEU A CD2 
2578 N N   . ILE A 341 ? 0.53110 0.49231 0.49403 -0.12923 -0.08170 0.21133  334 ILE A N   
2579 C CA  . ILE A 341 ? 0.63909 0.58438 0.58992 -0.12815 -0.08325 0.19301  334 ILE A CA  
2580 C C   . ILE A 341 ? 0.58127 0.55914 0.53807 -0.12861 -0.07646 0.19456  334 ILE A C   
2581 O O   . ILE A 341 ? 0.53746 0.51463 0.48282 -0.12364 -0.07152 0.17903  334 ILE A O   
2582 C CB  . ILE A 341 ? 0.65142 0.56056 0.60693 -0.13622 -0.09729 0.19203  334 ILE A CB  
2583 C CG1 . ILE A 341 ? 0.54509 0.43984 0.48683 -0.13640 -0.10049 0.17527  334 ILE A CG1 
2584 C CG2 . ILE A 341 ? 0.59103 0.51264 0.57298 -0.14724 -0.10516 0.21382  334 ILE A CG2 
2585 C CD1 . ILE A 341 ? 0.80258 0.65441 0.73441 -0.14288 -0.11283 0.16619  334 ILE A CD1 
2586 N N   . ASP A 342 ? 0.49890 0.50594 0.47551 -0.13403 -0.07495 0.21393  335 ASP A N   
2587 C CA  . ASP A 342 ? 0.57069 0.60921 0.55592 -0.13336 -0.06589 0.21595  335 ASP A CA  
2588 C C   . ASP A 342 ? 0.55300 0.61672 0.52207 -0.12554 -0.04958 0.20565  335 ASP A C   
2589 O O   . ASP A 342 ? 0.55282 0.62794 0.51967 -0.12094 -0.03991 0.19478  335 ASP A O   
2590 C CB  . ASP A 342 ? 0.56412 0.62755 0.57620 -0.14165 -0.06807 0.24082  335 ASP A CB  
2591 C CG  . ASP A 342 ? 0.66456 0.70850 0.69525 -0.15095 -0.08351 0.24903  335 ASP A CG  
2592 O OD1 . ASP A 342 ? 0.70494 0.73582 0.73296 -0.15032 -0.08715 0.23770  335 ASP A OD1 
2593 O OD2 . ASP A 342 ? 0.79545 0.83752 0.84400 -0.15997 -0.09289 0.26776  335 ASP A OD2 
2594 N N   . GLU A 343 ? 0.47285 0.54536 0.43166 -0.12464 -0.04664 0.20940  336 GLU A N   
2595 C CA  . GLU A 343 ? 0.45914 0.55406 0.39886 -0.11979 -0.03325 0.19848  336 GLU A CA  
2596 C C   . GLU A 343 ? 0.48333 0.55542 0.40432 -0.11268 -0.03123 0.17410  336 GLU A C   
2597 O O   . GLU A 343 ? 0.53565 0.61948 0.44740 -0.10874 -0.02002 0.15998  336 GLU A O   
2598 C CB  . GLU A 343 ? 0.51088 0.62164 0.44537 -0.12240 -0.03369 0.21140  336 GLU A CB  
2599 C CG  . GLU A 343 ? 0.47771 0.61044 0.43310 -0.13008 -0.03695 0.23877  336 GLU A CG  
2600 C CD  . GLU A 343 ? 0.55442 0.70139 0.51006 -0.13181 -0.03951 0.25278  336 GLU A CD  
2601 O OE1 . GLU A 343 ? 0.55787 0.74186 0.51340 -0.13347 -0.03237 0.25892  336 GLU A OE1 
2602 O OE2 . GLU A 343 ? 0.58263 0.70318 0.54171 -0.12944 -0.04829 0.25368  336 GLU A OE2 
2603 N N   . TRP A 344 ? 0.41196 0.45061 0.32789 -0.11094 -0.04108 0.16880  337 TRP A N   
2604 C CA  . TRP A 344 ? 0.49809 0.51451 0.39874 -0.10483 -0.04000 0.14789  337 TRP A CA  
2605 C C   . TRP A 344 ? 0.54544 0.55787 0.45317 -0.10414 -0.03905 0.14072  337 TRP A C   
2606 O O   . TRP A 344 ? 0.47675 0.48633 0.37532 -0.09895 -0.03268 0.12511  337 TRP A O   
2607 C CB  . TRP A 344 ? 0.45322 0.43430 0.34836 -0.10343 -0.04974 0.14475  337 TRP A CB  
2608 C CG  . TRP A 344 ? 0.53041 0.51299 0.42085 -0.10134 -0.04926 0.15028  337 TRP A CG  
2609 C CD1 . TRP A 344 ? 0.48161 0.44941 0.38186 -0.10284 -0.05620 0.16276  337 TRP A CD1 
2610 C CD2 . TRP A 344 ? 0.54228 0.54223 0.41980 -0.09780 -0.04185 0.14482  337 TRP A CD2 
2611 N NE1 . TRP A 344 ? 0.48008 0.45701 0.37708 -0.09931 -0.05312 0.16741  337 TRP A NE1 
2612 C CE2 . TRP A 344 ? 0.48702 0.48488 0.36915 -0.09705 -0.04526 0.15690  337 TRP A CE2 
2613 C CE3 . TRP A 344 ? 0.41007 0.42647 0.27396 -0.09589 -0.03298 0.13119  337 TRP A CE3 
2614 C CZ2 . TRP A 344 ? 0.45816 0.47328 0.33209 -0.09517 -0.04143 0.15775  337 TRP A CZ2 
2615 C CZ3 . TRP A 344 ? 0.45368 0.48465 0.30643 -0.09519 -0.02947 0.12968  337 TRP A CZ3 
2616 C CH2 . TRP A 344 ? 0.52897 0.56093 0.38692 -0.09517 -0.03433 0.14384  337 TRP A CH2 
2617 N N   . LYS A 345 ? 0.49661 0.50962 0.42341 -0.10984 -0.04596 0.15377  338 LYS A N   
2618 C CA  . LYS A 345 ? 0.48987 0.50210 0.42860 -0.11000 -0.04678 0.15150  338 LYS A CA  
2619 C C   . LYS A 345 ? 0.52864 0.57119 0.47434 -0.10531 -0.03069 0.14858  338 LYS A C   
2620 O O   . LYS A 345 ? 0.47012 0.50979 0.41835 -0.10045 -0.02570 0.13816  338 LYS A O   
2621 C CB  . LYS A 345 ? 0.54345 0.55202 0.50292 -0.11912 -0.05938 0.16884  338 LYS A CB  
2622 C CG  . LYS A 345 ? 0.55566 0.55881 0.52835 -0.12165 -0.06578 0.16950  338 LYS A CG  
2623 C CD  . LYS A 345 ? 0.55606 0.54364 0.54057 -0.13348 -0.08363 0.18296  338 LYS A CD  
2624 C CE  . LYS A 345 ? 0.61327 0.60394 0.61578 -0.13859 -0.09164 0.18941  338 LYS A CE  
2625 N NZ  . LYS A 345 ? 0.62374 0.59091 0.62893 -0.15233 -0.11216 0.19710  338 LYS A NZ  
2626 N N   . SER A 346 ? 0.46417 0.53581 0.41329 -0.10675 -0.02161 0.15782  339 SER A N   
2627 C CA  . SER A 346 ? 0.46233 0.56249 0.41623 -0.10256 -0.00386 0.15358  339 SER A CA  
2628 C C   . SER A 346 ? 0.46769 0.56560 0.39852 -0.09650 0.00732  0.13152  339 SER A C   
2629 O O   . SER A 346 ? 0.39346 0.49614 0.32812 -0.09086 0.01961  0.11960  339 SER A O   
2630 C CB  . SER A 346 ? 0.48420 0.61751 0.44492 -0.10718 0.00293  0.17020  339 SER A CB  
2631 O OG  . SER A 346 ? 0.49383 0.65449 0.45797 -0.10303 0.02234  0.16495  339 SER A OG  
2632 N N   . LEU A 347 ? 0.46236 0.55304 0.37172 -0.09783 0.00331  0.12672  340 LEU A N   
2633 C CA  . LEU A 347 ? 0.49371 0.58122 0.38173 -0.09401 0.01135  0.10669  340 LEU A CA  
2634 C C   . LEU A 347 ? 0.41264 0.47449 0.30245 -0.08826 0.00968  0.09238  340 LEU A C   
2635 O O   . LEU A 347 ? 0.42139 0.48462 0.30627 -0.08406 0.02091  0.07651  340 LEU A O   
2636 C CB  . LEU A 347 ? 0.42843 0.51257 0.29840 -0.09689 0.00444  0.10828  340 LEU A CB  
2637 C CG  . LEU A 347 ? 0.44968 0.56189 0.31731 -0.10329 0.00526  0.12461  340 LEU A CG  
2638 C CD1 . LEU A 347 ? 0.46620 0.57192 0.32385 -0.10519 -0.00412 0.13045  340 LEU A CD1 
2639 C CD2 . LEU A 347 ? 0.41095 0.55378 0.26605 -0.10536 0.02110  0.11687  340 LEU A CD2 
2640 N N   . THR A 348 ? 0.38339 0.42122 0.27973 -0.08878 -0.00423 0.09783  341 THR A N   
2641 C CA  . THR A 348 ? 0.40493 0.42121 0.30328 -0.08461 -0.00705 0.08761  341 THR A CA  
2642 C C   . THR A 348 ? 0.49941 0.52653 0.41979 -0.08151 0.00101  0.08852  341 THR A C   
2643 O O   . THR A 348 ? 0.44829 0.46945 0.37062 -0.07609 0.00796  0.07645  341 THR A O   
2644 C CB  . THR A 348 ? 0.43921 0.42961 0.33696 -0.08778 -0.02356 0.09382  341 THR A CB  
2645 O OG1 . THR A 348 ? 0.43694 0.41572 0.31720 -0.08848 -0.02830 0.09217  341 THR A OG1 
2646 C CG2 . THR A 348 ? 0.37924 0.35080 0.27739 -0.08482 -0.02710 0.08542  341 THR A CG2 
2647 N N   . TYR A 349 ? 0.49897 0.54246 0.43957 -0.08468 0.00043  0.10439  342 TYR A N   
2648 C CA  . TYR A 349 ? 0.51825 0.57648 0.48479 -0.08069 0.01020  0.10790  342 TYR A CA  
2649 C C   . TYR A 349 ? 0.44075 0.51397 0.40272 -0.07420 0.03158  0.09275  342 TYR A C   
2650 O O   . TYR A 349 ? 0.41875 0.49021 0.39520 -0.06748 0.04136  0.08512  342 TYR A O   
2651 C CB  . TYR A 349 ? 0.48937 0.56727 0.47888 -0.08584 0.00709  0.12931  342 TYR A CB  
2652 C CG  . TYR A 349 ? 0.49108 0.58486 0.51383 -0.08169 0.01529  0.13748  342 TYR A CG  
2653 C CD1 . TYR A 349 ? 0.54773 0.62912 0.58913 -0.08226 0.00386  0.14415  342 TYR A CD1 
2654 C CD2 . TYR A 349 ? 0.50557 0.62840 0.54180 -0.07732 0.03501  0.13962  342 TYR A CD2 
2655 C CE1 . TYR A 349 ? 0.52843 0.62680 0.60540 -0.07808 0.01099  0.15486  342 TYR A CE1 
2656 C CE2 . TYR A 349 ? 0.51974 0.65804 0.59084 -0.07192 0.04454  0.14831  342 TYR A CE2 
2657 C CZ  . TYR A 349 ? 0.54444 0.67086 0.63803 -0.07206 0.03204  0.15699  342 TYR A CZ  
2658 O OH  . TYR A 349 ? 0.44073 0.58491 0.57399 -0.06633 0.04112  0.16877  342 TYR A OH  
2659 N N   . ASP A 350 ? 0.44959 0.53722 0.39153 -0.07679 0.03896  0.08835  343 ASP A N   
2660 C CA  . ASP A 350 ? 0.40999 0.50967 0.34033 -0.07310 0.05858  0.07074  343 ASP A CA  
2661 C C   . ASP A 350 ? 0.48895 0.56583 0.40894 -0.06876 0.06023  0.05076  343 ASP A C   
2662 O O   . ASP A 350 ? 0.53698 0.61469 0.46248 -0.06320 0.07612  0.03644  343 ASP A O   
2663 C CB  . ASP A 350 ? 0.42948 0.54768 0.33458 -0.07960 0.06158  0.07063  343 ASP A CB  
2664 C CG  . ASP A 350 ? 0.49109 0.63902 0.40739 -0.08305 0.06725  0.08817  343 ASP A CG  
2665 O OD1 . ASP A 350 ? 0.48470 0.64184 0.42819 -0.07908 0.07414  0.09629  343 ASP A OD1 
2666 O OD2 . ASP A 350 ? 0.52961 0.69366 0.42966 -0.08989 0.06472  0.09586  343 ASP A OD2 
2667 N N   . GLU A 351 ? 0.49111 0.54693 0.39748 -0.07104 0.04494  0.04970  344 GLU A N   
2668 C CA  . GLU A 351 ? 0.47921 0.51505 0.37620 -0.06779 0.04571  0.03297  344 GLU A CA  
2669 C C   . GLU A 351 ? 0.47706 0.49960 0.39860 -0.06160 0.04597  0.03337  344 GLU A C   
2670 O O   . GLU A 351 ? 0.49410 0.50660 0.41731 -0.05725 0.05406  0.01917  344 GLU A O   
2671 C CB  . GLU A 351 ? 0.42202 0.44176 0.29964 -0.07129 0.03076  0.03378  344 GLU A CB  
2672 C CG  . GLU A 351 ? 0.43024 0.46344 0.28563 -0.07693 0.03065  0.03341  344 GLU A CG  
2673 C CD  . GLU A 351 ? 0.52382 0.56642 0.36331 -0.07838 0.04351  0.01550  344 GLU A CD  
2674 O OE1 . GLU A 351 ? 0.44404 0.47160 0.28310 -0.07528 0.04725  0.00098  344 GLU A OE1 
2675 O OE2 . GLU A 351 ? 0.53444 0.59957 0.36125 -0.08373 0.04942  0.01624  344 GLU A OE2 
2676 N N   . VAL A 352 ? 0.45003 0.47276 0.39206 -0.06213 0.03634  0.05066  345 VAL A N   
2677 C CA  . VAL A 352 ? 0.50839 0.52355 0.47694 -0.05731 0.03555  0.05508  345 VAL A CA  
2678 C C   . VAL A 352 ? 0.56602 0.59608 0.55815 -0.04999 0.05609  0.05049  345 VAL A C   
2679 O O   . VAL A 352 ? 0.56825 0.58912 0.57587 -0.04355 0.06345  0.04335  345 VAL A O   
2680 C CB  . VAL A 352 ? 0.46084 0.47515 0.44449 -0.06221 0.01858  0.07585  345 VAL A CB  
2681 C CG1 . VAL A 352 ? 0.37316 0.38321 0.38513 -0.05865 0.01578  0.08355  345 VAL A CG1 
2682 C CG2 . VAL A 352 ? 0.44975 0.44563 0.40815 -0.06894 0.00093  0.07713  345 VAL A CG2 
2683 N N   . ILE A 353 ? 0.49224 0.54541 0.48852 -0.05052 0.06686  0.05479  346 ILE A N   
2684 C CA  . ILE A 353 ? 0.50376 0.57222 0.52329 -0.04270 0.08915  0.05052  346 ILE A CA  
2685 C C   . ILE A 353 ? 0.52028 0.58067 0.52252 -0.03896 0.10652  0.02416  346 ILE A C   
2686 O O   . ILE A 353 ? 0.64307 0.70092 0.66671 -0.03047 0.12346  0.01529  346 ILE A O   
2687 C CB  . ILE A 353 ? 0.63192 0.72930 0.65743 -0.04499 0.09695  0.06248  346 ILE A CB  
2688 C CG1 . ILE A 353 ? 0.52130 0.62321 0.55805 -0.05208 0.07607  0.08753  346 ILE A CG1 
2689 C CG2 . ILE A 353 ? 0.61312 0.72726 0.67013 -0.03544 0.12040  0.06214  346 ILE A CG2 
2690 C CD1 . ILE A 353 ? 0.58542 0.69547 0.66503 -0.04868 0.07385  0.10660  346 ILE A CD1 
2691 N N   . SER A 354 ? 0.57560 0.63149 0.54088 -0.04566 0.10252  0.01175  347 SER A N   
2692 C CA  . SER A 354 ? 0.50181 0.55173 0.44663 -0.04547 0.11717  -0.01356 347 SER A CA  
2693 C C   . SER A 354 ? 0.52844 0.55122 0.47422 -0.04306 0.11249  -0.02512 347 SER A C   
2694 O O   . SER A 354 ? 0.54855 0.56296 0.47871 -0.04415 0.12288  -0.04662 347 SER A O   
2695 C CB  . SER A 354 ? 0.44630 0.50733 0.35267 -0.05542 0.11358  -0.01914 347 SER A CB  
2696 O OG  . SER A 354 ? 0.45996 0.51129 0.35359 -0.06070 0.09180  -0.00901 347 SER A OG  
2697 N N   . PHE A 355 ? 0.52881 0.53827 0.49150 -0.04102 0.09701  -0.01132 348 PHE A N   
2698 C CA  . PHE A 355 ? 0.52444 0.51047 0.48741 -0.03954 0.09153  -0.01933 348 PHE A CA  
2699 C C   . PHE A 355 ? 0.44424 0.42184 0.43198 -0.03134 0.10976  -0.03161 348 PHE A C   
2700 O O   . PHE A 355 ? 0.55091 0.53738 0.57016 -0.02397 0.12092  -0.02428 348 PHE A O   
2701 C CB  . PHE A 355 ? 0.44457 0.42099 0.41896 -0.03992 0.07170  -0.00048 348 PHE A CB  
2702 C CG  . PHE A 355 ? 0.48484 0.44008 0.46126 -0.03846 0.06607  -0.00531 348 PHE A CG  
2703 C CD1 . PHE A 355 ? 0.43176 0.37602 0.37977 -0.04353 0.05848  -0.01432 348 PHE A CD1 
2704 C CD2 . PHE A 355 ? 0.42617 0.37464 0.43575 -0.03206 0.06845  0.00156  348 PHE A CD2 
2705 C CE1 . PHE A 355 ? 0.46379 0.39069 0.41485 -0.04252 0.05381  -0.01707 348 PHE A CE1 
2706 C CE2 . PHE A 355 ? 0.45002 0.38079 0.46269 -0.03131 0.06307  -0.00051 348 PHE A CE2 
2707 C CZ  . PHE A 355 ? 0.41835 0.33832 0.40092 -0.03668 0.05597  -0.01019 348 PHE A CZ  
2708 N N   . VAL A 356 ? 0.56493 0.52513 0.54100 -0.03260 0.11308  -0.04956 349 VAL A N   
2709 C CA  . VAL A 356 ? 0.58718 0.53282 0.58729 -0.02543 0.12897  -0.06243 349 VAL A CA  
2710 C C   . VAL A 356 ? 0.51027 0.43537 0.51854 -0.02542 0.11588  -0.05804 349 VAL A C   
2711 O O   . VAL A 356 ? 0.55545 0.47177 0.53692 -0.03258 0.10662  -0.06594 349 VAL A O   
2712 C CB  . VAL A 356 ? 0.62432 0.56653 0.60283 -0.02865 0.14726  -0.09089 349 VAL A CB  
2713 C CG1 . VAL A 356 ? 0.50904 0.43197 0.51610 -0.02058 0.16513  -0.10513 349 VAL A CG1 
2714 C CG2 . VAL A 356 ? 0.61273 0.57863 0.57753 -0.03015 0.15981  -0.09420 349 VAL A CG2 
2715 N N   . PRO A 357 ? 0.54905 0.46834 0.59491 -0.01798 0.11442  -0.04351 350 PRO A N   
2716 C CA  . PRO A 357 ? 0.62983 0.53227 0.68267 -0.01877 0.10183  -0.03711 350 PRO A CA  
2717 C C   . PRO A 357 ? 0.61502 0.49842 0.66337 -0.01974 0.11188  -0.05906 350 PRO A C   
2718 O O   . PRO A 357 ? 0.63222 0.51149 0.68669 -0.01661 0.13189  -0.07798 350 PRO A O   
2719 C CB  . PRO A 357 ? 0.57602 0.48080 0.67492 -0.01049 0.10151  -0.01617 350 PRO A CB  
2720 C CG  . PRO A 357 ? 0.57653 0.49307 0.69842 -0.00278 0.12196  -0.02012 350 PRO A CG  
2721 C CD  . PRO A 357 ? 0.51488 0.44577 0.60047 -0.00895 0.12372  -0.02951 350 PRO A CD  
2722 N N   . PRO A 358 ? 0.64562 0.51655 0.68280 -0.02472 0.09909  -0.05789 351 PRO A N   
2723 C CA  . PRO A 358 ? 0.81920 0.67093 0.85802 -0.02654 0.10702  -0.07608 351 PRO A CA  
2724 C C   . PRO A 358 ? 0.82693 0.66558 0.91218 -0.01712 0.11812  -0.07241 351 PRO A C   
2725 O O   . PRO A 358 ? 0.67757 0.52241 0.79313 -0.01065 0.11280  -0.04956 351 PRO A O   
2726 C CB  . PRO A 358 ? 0.74962 0.59610 0.76917 -0.03361 0.08861  -0.06878 351 PRO A CB  
2727 C CG  . PRO A 358 ? 0.68038 0.53735 0.70334 -0.03180 0.07338  -0.04388 351 PRO A CG  
2728 C CD  . PRO A 358 ? 0.65385 0.52754 0.67580 -0.02935 0.07774  -0.04047 351 PRO A CD  
2729 N N   . PRO A 359 ? 0.91386 0.73409 1.00780 -0.01664 0.13335  -0.09368 352 PRO A N   
2730 C CA  . PRO A 359 ? 1.01578 0.82118 1.15910 -0.00646 0.14603  -0.09024 352 PRO A CA  
2731 C C   . PRO A 359 ? 1.06799 0.86477 1.23300 -0.00659 0.13083  -0.06957 352 PRO A C   
2732 O O   . PRO A 359 ? 1.07892 0.86769 1.22262 -0.01524 0.11983  -0.07323 352 PRO A O   
2733 C CB  . PRO A 359 ? 1.04704 0.83184 1.18479 -0.00869 0.16568  -0.12299 352 PRO A CB  
2734 C CG  . PRO A 359 ? 1.04610 0.83193 1.13402 -0.02319 0.15453  -0.13733 352 PRO A CG  
2735 C CD  . PRO A 359 ? 0.93548 0.74723 0.99534 -0.02632 0.13942  -0.12170 352 PRO A CD  
2736 N N   . LEU A 360 ? 0.94637 0.74737 1.15510 0.00262  0.13018  -0.04590 353 LEU A N   
2737 C CA  . LEU A 360 ? 1.03925 0.83465 1.27185 0.00242  0.11652  -0.02346 353 LEU A CA  
2738 C C   . LEU A 360 ? 1.09098 0.86004 1.34089 0.00186  0.12581  -0.03786 353 LEU A C   
2739 O O   . LEU A 360 ? 1.02890 0.78299 1.31087 0.00962  0.14594  -0.05037 353 LEU A O   
2740 C CB  . LEU A 360 ? 0.99542 0.80281 1.27541 0.01180  0.11492  0.00568  353 LEU A CB  
2741 C CG  . LEU A 360 ? 1.06623 0.87290 1.37170 0.01073  0.09926  0.03371  353 LEU A CG  
2742 C CD1 . LEU A 360 ? 0.94254 0.75349 1.20286 -0.00104 0.07838  0.03820  353 LEU A CD1 
2743 C CD2 . LEU A 360 ? 0.86335 0.68900 1.20865 0.01702  0.09329  0.06563  353 LEU A CD2 
2744 N N   . ASP A 361 ? 1.12698 0.88993 1.35688 -0.00735 0.11187  -0.03603 354 ASP A N   
2745 C CA  . ASP A 361 ? 1.03126 0.76982 1.27280 -0.01116 0.11718  -0.04906 354 ASP A CA  
2746 C C   . ASP A 361 ? 0.89251 0.61159 1.18947 -0.00095 0.13500  -0.05029 354 ASP A C   
2747 O O   . ASP A 361 ? 1.05417 0.78010 1.39348 0.00823  0.13390  -0.02439 354 ASP A O   
2748 C CB  . ASP A 361 ? 1.03753 0.77828 1.27456 -0.01799 0.09785  -0.02883 354 ASP A CB  
2749 C CG  . ASP A 361 ? 0.93551 0.69012 1.11941 -0.02789 0.08352  -0.03186 354 ASP A CG  
2750 O OD1 . ASP A 361 ? 0.86243 0.63459 1.02220 -0.02706 0.07918  -0.02910 354 ASP A OD1 
2751 O OD2 . ASP A 361 ? 1.00877 0.75686 1.17790 -0.03633 0.07692  -0.03589 354 ASP A OD2 
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