data_9HDL
# 
_entry.id   9HDL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9HDL         pdb_00009hdl 10.2210/pdb9hdl/pdb 
WWPDB D_1292143106 ?            ?                   
# 
_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       2025-02-26 
# 
_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                        9HDL 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              nico.fessner@pharmazie.uni-freiburg.de 
_pdbx_contact_author.name_first         'Nico D.' 
_pdbx_contact_author.name_last          Fessner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8247-1356 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Friedrich, F.' 1 0000-0001-5420-6184 
'Genz, F.'      2 0009-0002-4868-2752 
'Einsle, O.'    3 0000-0001-8722-2893 
'Mueller, M.'   4 0000-0002-2742-4992 
'Fessner, N.D.' 5 0000-0001-8247-1356 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acs Catalysis' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2155-5435 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Identification and Characterization of Pyrimidine Nucleoside 2'-Hydroxylase
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acscatal.4c07764 
_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 'Genz, F.'      1 ? 
primary 'Friedrich, F.' 2 ? 
primary 'Lonarz, C.'    3 ? 
primary 'Einsle, O.'    4 ? 
primary 'Jung, M.'      5 ? 
primary 'Muller, M.'    6 ? 
primary 'Fessner, N.D.' 7 ? 
# 
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 'Clavaminate synthase-like protein' 42508.672 1   ? ? ? ? 
2 non-polymer syn 'FE (III) ION'                      55.845    1   ? ? ? ? 
3 water       nat water                               18.015    192 ? ? ? ? 
# 
_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       
;MGSSHHHHHHSSGLVPRGSHMAPIAQAVTVSLNDLKNGTVSLEALEEAFGPDSLGILVVKDVPAEFAELRHRLLSYSSYL
GNLPKSELDRLENEKAKYLTGWSLGKETLKNGQVDNLKGSYYANCAFYVDPSLSCAKPTEEFNPDNFPEYLSPNLWPQES
TLPGFKPTFEDLCRLIIDVAVLVARACDRFAEKQIAGYPAGYLEGVVKTSTTTKARLLHYFPEEATATDASKESNKEEEG
DEDDWCATHLDHGCLTGLTSAMFVDEAATPPVVNPSVNGSLPPLGELPTSPDPKAGLYIKSRTGQTVQVKIPRDCIAFQT
GEALERITGGKFKAVPHFVRGARAEMSAGRIARNTLAVFTQPNLGDEVDMEQHITFGEFARGIVAKNTVS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSSGLVPRGSHMAPIAQAVTVSLNDLKNGTVSLEALEEAFGPDSLGILVVKDVPAEFAELRHRLLSYSSYL
GNLPKSELDRLENEKAKYLTGWSLGKETLKNGQVDNLKGSYYANCAFYVDPSLSCAKPTEEFNPDNFPEYLSPNLWPQES
TLPGFKPTFEDLCRLIIDVAVLVARACDRFAEKQIAGYPAGYLEGVVKTSTTTKARLLHYFPEEATATDASKESNKEEEG
DEDDWCATHLDHGCLTGLTSAMFVDEAATPPVVNPSVNGSLPPLGELPTSPDPKAGLYIKSRTGQTVQVKIPRDCIAFQT
GEALERITGGKFKAVPHFVRGARAEMSAGRIARNTLAVFTQPNLGDEVDMEQHITFGEFARGIVAKNTVS
;
_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 'FE (III) ION' FE  
3 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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  SER n 
1 13  GLY n 
1 14  LEU n 
1 15  VAL n 
1 16  PRO n 
1 17  ARG n 
1 18  GLY n 
1 19  SER n 
1 20  HIS n 
1 21  MET n 
1 22  ALA n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  GLN n 
1 27  ALA n 
1 28  VAL n 
1 29  THR n 
1 30  VAL n 
1 31  SER n 
1 32  LEU n 
1 33  ASN n 
1 34  ASP n 
1 35  LEU n 
1 36  LYS n 
1 37  ASN n 
1 38  GLY n 
1 39  THR n 
1 40  VAL n 
1 41  SER n 
1 42  LEU n 
1 43  GLU n 
1 44  ALA n 
1 45  LEU n 
1 46  GLU n 
1 47  GLU n 
1 48  ALA n 
1 49  PHE n 
1 50  GLY n 
1 51  PRO n 
1 52  ASP n 
1 53  SER n 
1 54  LEU n 
1 55  GLY n 
1 56  ILE n 
1 57  LEU n 
1 58  VAL n 
1 59  VAL n 
1 60  LYS n 
1 61  ASP n 
1 62  VAL n 
1 63  PRO n 
1 64  ALA n 
1 65  GLU n 
1 66  PHE n 
1 67  ALA n 
1 68  GLU n 
1 69  LEU n 
1 70  ARG n 
1 71  HIS n 
1 72  ARG n 
1 73  LEU n 
1 74  LEU n 
1 75  SER n 
1 76  TYR n 
1 77  SER n 
1 78  SER n 
1 79  TYR n 
1 80  LEU n 
1 81  GLY n 
1 82  ASN n 
1 83  LEU n 
1 84  PRO n 
1 85  LYS n 
1 86  SER n 
1 87  GLU n 
1 88  LEU n 
1 89  ASP n 
1 90  ARG n 
1 91  LEU n 
1 92  GLU n 
1 93  ASN n 
1 94  GLU n 
1 95  LYS n 
1 96  ALA n 
1 97  LYS n 
1 98  TYR n 
1 99  LEU n 
1 100 THR n 
1 101 GLY n 
1 102 TRP n 
1 103 SER n 
1 104 LEU n 
1 105 GLY n 
1 106 LYS n 
1 107 GLU n 
1 108 THR n 
1 109 LEU n 
1 110 LYS n 
1 111 ASN n 
1 112 GLY n 
1 113 GLN n 
1 114 VAL n 
1 115 ASP n 
1 116 ASN n 
1 117 LEU n 
1 118 LYS n 
1 119 GLY n 
1 120 SER n 
1 121 TYR n 
1 122 TYR n 
1 123 ALA n 
1 124 ASN n 
1 125 CYS n 
1 126 ALA n 
1 127 PHE n 
1 128 TYR n 
1 129 VAL n 
1 130 ASP n 
1 131 PRO n 
1 132 SER n 
1 133 LEU n 
1 134 SER n 
1 135 CYS n 
1 136 ALA n 
1 137 LYS n 
1 138 PRO n 
1 139 THR n 
1 140 GLU n 
1 141 GLU n 
1 142 PHE n 
1 143 ASN n 
1 144 PRO n 
1 145 ASP n 
1 146 ASN n 
1 147 PHE n 
1 148 PRO n 
1 149 GLU n 
1 150 TYR n 
1 151 LEU n 
1 152 SER n 
1 153 PRO n 
1 154 ASN n 
1 155 LEU n 
1 156 TRP n 
1 157 PRO n 
1 158 GLN n 
1 159 GLU n 
1 160 SER n 
1 161 THR n 
1 162 LEU n 
1 163 PRO n 
1 164 GLY n 
1 165 PHE n 
1 166 LYS n 
1 167 PRO n 
1 168 THR n 
1 169 PHE n 
1 170 GLU n 
1 171 ASP n 
1 172 LEU n 
1 173 CYS n 
1 174 ARG n 
1 175 LEU n 
1 176 ILE n 
1 177 ILE n 
1 178 ASP n 
1 179 VAL n 
1 180 ALA n 
1 181 VAL n 
1 182 LEU n 
1 183 VAL n 
1 184 ALA n 
1 185 ARG n 
1 186 ALA n 
1 187 CYS n 
1 188 ASP n 
1 189 ARG n 
1 190 PHE n 
1 191 ALA n 
1 192 GLU n 
1 193 LYS n 
1 194 GLN n 
1 195 ILE n 
1 196 ALA n 
1 197 GLY n 
1 198 TYR n 
1 199 PRO n 
1 200 ALA n 
1 201 GLY n 
1 202 TYR n 
1 203 LEU n 
1 204 GLU n 
1 205 GLY n 
1 206 VAL n 
1 207 VAL n 
1 208 LYS n 
1 209 THR n 
1 210 SER n 
1 211 THR n 
1 212 THR n 
1 213 THR n 
1 214 LYS n 
1 215 ALA n 
1 216 ARG n 
1 217 LEU n 
1 218 LEU n 
1 219 HIS n 
1 220 TYR n 
1 221 PHE n 
1 222 PRO n 
1 223 GLU n 
1 224 GLU n 
1 225 ALA n 
1 226 THR n 
1 227 ALA n 
1 228 THR n 
1 229 ASP n 
1 230 ALA n 
1 231 SER n 
1 232 LYS n 
1 233 GLU n 
1 234 SER n 
1 235 ASN n 
1 236 LYS n 
1 237 GLU n 
1 238 GLU n 
1 239 GLU n 
1 240 GLY n 
1 241 ASP n 
1 242 GLU n 
1 243 ASP n 
1 244 ASP n 
1 245 TRP n 
1 246 CYS n 
1 247 ALA n 
1 248 THR n 
1 249 HIS n 
1 250 LEU n 
1 251 ASP n 
1 252 HIS n 
1 253 GLY n 
1 254 CYS n 
1 255 LEU n 
1 256 THR n 
1 257 GLY n 
1 258 LEU n 
1 259 THR n 
1 260 SER n 
1 261 ALA n 
1 262 MET n 
1 263 PHE n 
1 264 VAL n 
1 265 ASP n 
1 266 GLU n 
1 267 ALA n 
1 268 ALA n 
1 269 THR n 
1 270 PRO n 
1 271 PRO n 
1 272 VAL n 
1 273 VAL n 
1 274 ASN n 
1 275 PRO n 
1 276 SER n 
1 277 VAL n 
1 278 ASN n 
1 279 GLY n 
1 280 SER n 
1 281 LEU n 
1 282 PRO n 
1 283 PRO n 
1 284 LEU n 
1 285 GLY n 
1 286 GLU n 
1 287 LEU n 
1 288 PRO n 
1 289 THR n 
1 290 SER n 
1 291 PRO n 
1 292 ASP n 
1 293 PRO n 
1 294 LYS n 
1 295 ALA n 
1 296 GLY n 
1 297 LEU n 
1 298 TYR n 
1 299 ILE n 
1 300 LYS n 
1 301 SER n 
1 302 ARG n 
1 303 THR n 
1 304 GLY n 
1 305 GLN n 
1 306 THR n 
1 307 VAL n 
1 308 GLN n 
1 309 VAL n 
1 310 LYS n 
1 311 ILE n 
1 312 PRO n 
1 313 ARG n 
1 314 ASP n 
1 315 CYS n 
1 316 ILE n 
1 317 ALA n 
1 318 PHE n 
1 319 GLN n 
1 320 THR n 
1 321 GLY n 
1 322 GLU n 
1 323 ALA n 
1 324 LEU n 
1 325 GLU n 
1 326 ARG n 
1 327 ILE n 
1 328 THR n 
1 329 GLY n 
1 330 GLY n 
1 331 LYS n 
1 332 PHE n 
1 333 LYS n 
1 334 ALA n 
1 335 VAL n 
1 336 PRO n 
1 337 HIS n 
1 338 PHE n 
1 339 VAL n 
1 340 ARG n 
1 341 GLY n 
1 342 ALA n 
1 343 ARG n 
1 344 ALA n 
1 345 GLU n 
1 346 MET n 
1 347 SER n 
1 348 ALA n 
1 349 GLY n 
1 350 ARG n 
1 351 ILE n 
1 352 ALA n 
1 353 ARG n 
1 354 ASN n 
1 355 THR n 
1 356 LEU n 
1 357 ALA n 
1 358 VAL n 
1 359 PHE n 
1 360 THR n 
1 361 GLN n 
1 362 PRO n 
1 363 ASN n 
1 364 LEU n 
1 365 GLY n 
1 366 ASP n 
1 367 GLU n 
1 368 VAL n 
1 369 ASP n 
1 370 MET n 
1 371 GLU n 
1 372 GLN n 
1 373 HIS n 
1 374 ILE n 
1 375 THR n 
1 376 PHE n 
1 377 GLY n 
1 378 GLU n 
1 379 PHE n 
1 380 ALA n 
1 381 ARG n 
1 382 GLY n 
1 383 ILE n 
1 384 VAL n 
1 385 ALA n 
1 386 LYS n 
1 387 ASN n 
1 388 THR n 
1 389 VAL n 
1 390 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                   390 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 NCU02560 
_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      'Neurospora crassa' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5141 
_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 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
FE  non-polymer         . 'FE (III) ION'  ? 'Fe 3'           55.845  
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -19 ?   ?   ?   A . n 
A 1 2   GLY 2   -18 ?   ?   ?   A . n 
A 1 3   SER 3   -17 ?   ?   ?   A . n 
A 1 4   SER 4   -16 ?   ?   ?   A . n 
A 1 5   HIS 5   -15 ?   ?   ?   A . n 
A 1 6   HIS 6   -14 ?   ?   ?   A . n 
A 1 7   HIS 7   -13 ?   ?   ?   A . n 
A 1 8   HIS 8   -12 ?   ?   ?   A . n 
A 1 9   HIS 9   -11 ?   ?   ?   A . n 
A 1 10  HIS 10  -10 ?   ?   ?   A . n 
A 1 11  SER 11  -9  ?   ?   ?   A . n 
A 1 12  SER 12  -8  ?   ?   ?   A . n 
A 1 13  GLY 13  -7  ?   ?   ?   A . n 
A 1 14  LEU 14  -6  ?   ?   ?   A . n 
A 1 15  VAL 15  -5  ?   ?   ?   A . n 
A 1 16  PRO 16  -4  ?   ?   ?   A . n 
A 1 17  ARG 17  -3  ?   ?   ?   A . n 
A 1 18  GLY 18  -2  -2  GLY GLY A . n 
A 1 19  SER 19  -1  -1  SER SER A . n 
A 1 20  HIS 20  0   0   HIS HIS A . n 
A 1 21  MET 21  1   1   MET MET A . n 
A 1 22  ALA 22  2   2   ALA ALA A . n 
A 1 23  PRO 23  3   3   PRO PRO A . n 
A 1 24  ILE 24  4   4   ILE ILE A . n 
A 1 25  ALA 25  5   5   ALA ALA A . n 
A 1 26  GLN 26  6   6   GLN GLN A . n 
A 1 27  ALA 27  7   7   ALA ALA A . n 
A 1 28  VAL 28  8   8   VAL VAL A . n 
A 1 29  THR 29  9   9   THR THR A . n 
A 1 30  VAL 30  10  10  VAL VAL A . n 
A 1 31  SER 31  11  11  SER SER A . n 
A 1 32  LEU 32  12  12  LEU LEU A . n 
A 1 33  ASN 33  13  13  ASN ASN A . n 
A 1 34  ASP 34  14  14  ASP ASP A . n 
A 1 35  LEU 35  15  15  LEU LEU A . n 
A 1 36  LYS 36  16  16  LYS LYS A . n 
A 1 37  ASN 37  17  17  ASN ASN A . n 
A 1 38  GLY 38  18  18  GLY GLY A . n 
A 1 39  THR 39  19  19  THR THR A . n 
A 1 40  VAL 40  20  20  VAL VAL A . n 
A 1 41  SER 41  21  21  SER SER A . n 
A 1 42  LEU 42  22  22  LEU LEU A . n 
A 1 43  GLU 43  23  23  GLU GLU A . n 
A 1 44  ALA 44  24  24  ALA ALA A . n 
A 1 45  LEU 45  25  25  LEU LEU A . n 
A 1 46  GLU 46  26  26  GLU GLU A . n 
A 1 47  GLU 47  27  27  GLU GLU A . n 
A 1 48  ALA 48  28  28  ALA ALA A . n 
A 1 49  PHE 49  29  29  PHE PHE A . n 
A 1 50  GLY 50  30  30  GLY GLY A . n 
A 1 51  PRO 51  31  31  PRO PRO A . n 
A 1 52  ASP 52  32  32  ASP ASP A . n 
A 1 53  SER 53  33  33  SER SER A . n 
A 1 54  LEU 54  34  34  LEU LEU A . n 
A 1 55  GLY 55  35  35  GLY GLY A . n 
A 1 56  ILE 56  36  36  ILE ILE A . n 
A 1 57  LEU 57  37  37  LEU LEU A . n 
A 1 58  VAL 58  38  38  VAL VAL A . n 
A 1 59  VAL 59  39  39  VAL VAL A . n 
A 1 60  LYS 60  40  40  LYS LYS A . n 
A 1 61  ASP 61  41  41  ASP ASP A . n 
A 1 62  VAL 62  42  42  VAL VAL A . n 
A 1 63  PRO 63  43  43  PRO PRO A . n 
A 1 64  ALA 64  44  44  ALA ALA A . n 
A 1 65  GLU 65  45  45  GLU GLU A . n 
A 1 66  PHE 66  46  46  PHE PHE A . n 
A 1 67  ALA 67  47  47  ALA ALA A . n 
A 1 68  GLU 68  48  48  GLU GLU A . n 
A 1 69  LEU 69  49  49  LEU LEU A . n 
A 1 70  ARG 70  50  50  ARG ARG A . n 
A 1 71  HIS 71  51  51  HIS HIS A . n 
A 1 72  ARG 72  52  52  ARG ARG A . n 
A 1 73  LEU 73  53  53  LEU LEU A . n 
A 1 74  LEU 74  54  54  LEU LEU A . n 
A 1 75  SER 75  55  55  SER SER A . n 
A 1 76  TYR 76  56  56  TYR TYR A . n 
A 1 77  SER 77  57  57  SER SER A . n 
A 1 78  SER 78  58  58  SER SER A . n 
A 1 79  TYR 79  59  59  TYR TYR A . n 
A 1 80  LEU 80  60  60  LEU LEU A . n 
A 1 81  GLY 81  61  61  GLY GLY A . n 
A 1 82  ASN 82  62  62  ASN ASN A . n 
A 1 83  LEU 83  63  63  LEU LEU A . n 
A 1 84  PRO 84  64  64  PRO PRO A . n 
A 1 85  LYS 85  65  65  LYS LYS A . n 
A 1 86  SER 86  66  66  SER SER A . n 
A 1 87  GLU 87  67  67  GLU GLU A . n 
A 1 88  LEU 88  68  68  LEU LEU A . n 
A 1 89  ASP 89  69  69  ASP ASP A . n 
A 1 90  ARG 90  70  70  ARG ARG A . n 
A 1 91  LEU 91  71  71  LEU LEU A . n 
A 1 92  GLU 92  72  72  GLU GLU A . n 
A 1 93  ASN 93  73  73  ASN ASN A . n 
A 1 94  GLU 94  74  74  GLU GLU A . n 
A 1 95  LYS 95  75  75  LYS LYS A . n 
A 1 96  ALA 96  76  76  ALA ALA A . n 
A 1 97  LYS 97  77  77  LYS LYS A . n 
A 1 98  TYR 98  78  78  TYR TYR A . n 
A 1 99  LEU 99  79  79  LEU LEU A . n 
A 1 100 THR 100 80  80  THR THR A . n 
A 1 101 GLY 101 81  81  GLY GLY A . n 
A 1 102 TRP 102 82  82  TRP TRP A . n 
A 1 103 SER 103 83  83  SER SER A . n 
A 1 104 LEU 104 84  84  LEU LEU A . n 
A 1 105 GLY 105 85  85  GLY GLY A . n 
A 1 106 LYS 106 86  86  LYS LYS A . n 
A 1 107 GLU 107 87  87  GLU GLU A . n 
A 1 108 THR 108 88  ?   ?   ?   A . n 
A 1 109 LEU 109 89  ?   ?   ?   A . n 
A 1 110 LYS 110 90  ?   ?   ?   A . n 
A 1 111 ASN 111 91  ?   ?   ?   A . n 
A 1 112 GLY 112 92  ?   ?   ?   A . n 
A 1 113 GLN 113 93  ?   ?   ?   A . n 
A 1 114 VAL 114 94  ?   ?   ?   A . n 
A 1 115 ASP 115 95  95  ASP ASP A . n 
A 1 116 ASN 116 96  96  ASN ASN A . n 
A 1 117 LEU 117 97  97  LEU LEU A . n 
A 1 118 LYS 118 98  98  LYS LYS A . n 
A 1 119 GLY 119 99  99  GLY GLY A . n 
A 1 120 SER 120 100 100 SER SER A . n 
A 1 121 TYR 121 101 101 TYR TYR A . n 
A 1 122 TYR 122 102 102 TYR TYR A . n 
A 1 123 ALA 123 103 103 ALA ALA A . n 
A 1 124 ASN 124 104 104 ASN ASN A . n 
A 1 125 CYS 125 105 105 CYS CYS A . n 
A 1 126 ALA 126 106 106 ALA ALA A . n 
A 1 127 PHE 127 107 107 PHE PHE A . n 
A 1 128 TYR 128 108 108 TYR TYR A . n 
A 1 129 VAL 129 109 109 VAL VAL A . n 
A 1 130 ASP 130 110 110 ASP ASP A . n 
A 1 131 PRO 131 111 111 PRO PRO A . n 
A 1 132 SER 132 112 112 SER SER A . n 
A 1 133 LEU 133 113 113 LEU LEU A . n 
A 1 134 SER 134 114 114 SER SER A . n 
A 1 135 CYS 135 115 115 CYS CYS A . n 
A 1 136 ALA 136 116 116 ALA ALA A . n 
A 1 137 LYS 137 117 117 LYS LYS A . n 
A 1 138 PRO 138 118 118 PRO PRO A . n 
A 1 139 THR 139 119 119 THR THR A . n 
A 1 140 GLU 140 120 120 GLU GLU A . n 
A 1 141 GLU 141 121 121 GLU GLU A . n 
A 1 142 PHE 142 122 122 PHE PHE A . n 
A 1 143 ASN 143 123 123 ASN ASN A . n 
A 1 144 PRO 144 124 124 PRO PRO A . n 
A 1 145 ASP 145 125 125 ASP ASP A . n 
A 1 146 ASN 146 126 126 ASN ASN A . n 
A 1 147 PHE 147 127 127 PHE PHE A . n 
A 1 148 PRO 148 128 128 PRO PRO A . n 
A 1 149 GLU 149 129 129 GLU GLU A . n 
A 1 150 TYR 150 130 130 TYR TYR A . n 
A 1 151 LEU 151 131 131 LEU LEU A . n 
A 1 152 SER 152 132 132 SER SER A . n 
A 1 153 PRO 153 133 133 PRO PRO A . n 
A 1 154 ASN 154 134 134 ASN ASN A . n 
A 1 155 LEU 155 135 135 LEU LEU A . n 
A 1 156 TRP 156 136 136 TRP TRP A . n 
A 1 157 PRO 157 137 137 PRO PRO A . n 
A 1 158 GLN 158 138 138 GLN GLN A . n 
A 1 159 GLU 159 139 139 GLU GLU A . n 
A 1 160 SER 160 140 140 SER SER A . n 
A 1 161 THR 161 141 141 THR THR A . n 
A 1 162 LEU 162 142 142 LEU LEU A . n 
A 1 163 PRO 163 143 143 PRO PRO A . n 
A 1 164 GLY 164 144 144 GLY GLY A . n 
A 1 165 PHE 165 145 145 PHE PHE A . n 
A 1 166 LYS 166 146 146 LYS LYS A . n 
A 1 167 PRO 167 147 147 PRO PRO A . n 
A 1 168 THR 168 148 148 THR THR A . n 
A 1 169 PHE 169 149 149 PHE PHE A . n 
A 1 170 GLU 170 150 150 GLU GLU A . n 
A 1 171 ASP 171 151 151 ASP ASP A . n 
A 1 172 LEU 172 152 152 LEU LEU A . n 
A 1 173 CYS 173 153 153 CYS CYS A . n 
A 1 174 ARG 174 154 154 ARG ARG A . n 
A 1 175 LEU 175 155 155 LEU LEU A . n 
A 1 176 ILE 176 156 156 ILE ILE A . n 
A 1 177 ILE 177 157 157 ILE ILE A . n 
A 1 178 ASP 178 158 158 ASP ASP A . n 
A 1 179 VAL 179 159 159 VAL VAL A . n 
A 1 180 ALA 180 160 160 ALA ALA A . n 
A 1 181 VAL 181 161 161 VAL VAL A . n 
A 1 182 LEU 182 162 162 LEU LEU A . n 
A 1 183 VAL 183 163 163 VAL VAL A . n 
A 1 184 ALA 184 164 164 ALA ALA A . n 
A 1 185 ARG 185 165 165 ARG ARG A . n 
A 1 186 ALA 186 166 166 ALA ALA A . n 
A 1 187 CYS 187 167 167 CYS CYS A . n 
A 1 188 ASP 188 168 168 ASP ASP A . n 
A 1 189 ARG 189 169 169 ARG ARG A . n 
A 1 190 PHE 190 170 170 PHE PHE A . n 
A 1 191 ALA 191 171 171 ALA ALA A . n 
A 1 192 GLU 192 172 172 GLU GLU A . n 
A 1 193 LYS 193 173 173 LYS LYS A . n 
A 1 194 GLN 194 174 174 GLN GLN A . n 
A 1 195 ILE 195 175 175 ILE ILE A . n 
A 1 196 ALA 196 176 176 ALA ALA A . n 
A 1 197 GLY 197 177 177 GLY GLY A . n 
A 1 198 TYR 198 178 178 TYR TYR A . n 
A 1 199 PRO 199 179 179 PRO PRO A . n 
A 1 200 ALA 200 180 180 ALA ALA A . n 
A 1 201 GLY 201 181 181 GLY GLY A . n 
A 1 202 TYR 202 182 182 TYR TYR A . n 
A 1 203 LEU 203 183 183 LEU LEU A . n 
A 1 204 GLU 204 184 184 GLU GLU A . n 
A 1 205 GLY 205 185 185 GLY GLY A . n 
A 1 206 VAL 206 186 186 VAL VAL A . n 
A 1 207 VAL 207 187 187 VAL VAL A . n 
A 1 208 LYS 208 188 188 LYS LYS A . n 
A 1 209 THR 209 189 189 THR THR A . n 
A 1 210 SER 210 190 190 SER SER A . n 
A 1 211 THR 211 191 191 THR THR A . n 
A 1 212 THR 212 192 192 THR THR A . n 
A 1 213 THR 213 193 193 THR THR A . n 
A 1 214 LYS 214 194 194 LYS LYS A . n 
A 1 215 ALA 215 195 195 ALA ALA A . n 
A 1 216 ARG 216 196 196 ARG ARG A . n 
A 1 217 LEU 217 197 197 LEU LEU A . n 
A 1 218 LEU 218 198 198 LEU LEU A . n 
A 1 219 HIS 219 199 199 HIS HIS A . n 
A 1 220 TYR 220 200 200 TYR TYR A . n 
A 1 221 PHE 221 201 201 PHE PHE A . n 
A 1 222 PRO 222 202 202 PRO PRO A . n 
A 1 223 GLU 223 203 203 GLU GLU A . n 
A 1 224 GLU 224 204 ?   ?   ?   A . n 
A 1 225 ALA 225 205 ?   ?   ?   A . n 
A 1 226 THR 226 206 ?   ?   ?   A . n 
A 1 227 ALA 227 207 ?   ?   ?   A . n 
A 1 228 THR 228 208 ?   ?   ?   A . n 
A 1 229 ASP 229 209 ?   ?   ?   A . n 
A 1 230 ALA 230 210 ?   ?   ?   A . n 
A 1 231 SER 231 211 ?   ?   ?   A . n 
A 1 232 LYS 232 212 ?   ?   ?   A . n 
A 1 233 GLU 233 213 ?   ?   ?   A . n 
A 1 234 SER 234 214 ?   ?   ?   A . n 
A 1 235 ASN 235 215 ?   ?   ?   A . n 
A 1 236 LYS 236 216 ?   ?   ?   A . n 
A 1 237 GLU 237 217 ?   ?   ?   A . n 
A 1 238 GLU 238 218 ?   ?   ?   A . n 
A 1 239 GLU 239 219 ?   ?   ?   A . n 
A 1 240 GLY 240 220 ?   ?   ?   A . n 
A 1 241 ASP 241 221 ?   ?   ?   A . n 
A 1 242 GLU 242 222 ?   ?   ?   A . n 
A 1 243 ASP 243 223 ?   ?   ?   A . n 
A 1 244 ASP 244 224 ?   ?   ?   A . n 
A 1 245 TRP 245 225 ?   ?   ?   A . n 
A 1 246 CYS 246 226 226 CYS CYS A . n 
A 1 247 ALA 247 227 227 ALA ALA A . n 
A 1 248 THR 248 228 228 THR THR A . n 
A 1 249 HIS 249 229 229 HIS HIS A . n 
A 1 250 LEU 250 230 230 LEU LEU A . n 
A 1 251 ASP 251 231 231 ASP ASP A . n 
A 1 252 HIS 252 232 232 HIS HIS A . n 
A 1 253 GLY 253 233 233 GLY GLY A . n 
A 1 254 CYS 254 234 234 CYS CYS A . n 
A 1 255 LEU 255 235 235 LEU LEU A . n 
A 1 256 THR 256 236 236 THR THR A . n 
A 1 257 GLY 257 237 237 GLY GLY A . n 
A 1 258 LEU 258 238 238 LEU LEU A . n 
A 1 259 THR 259 239 239 THR THR A . n 
A 1 260 SER 260 240 240 SER SER A . n 
A 1 261 ALA 261 241 241 ALA ALA A . n 
A 1 262 MET 262 242 242 MET MET A . n 
A 1 263 PHE 263 243 243 PHE PHE A . n 
A 1 264 VAL 264 244 244 VAL VAL A . n 
A 1 265 ASP 265 245 245 ASP ASP A . n 
A 1 266 GLU 266 246 246 GLU GLU A . n 
A 1 267 ALA 267 247 247 ALA ALA A . n 
A 1 268 ALA 268 248 248 ALA ALA A . n 
A 1 269 THR 269 249 249 THR THR A . n 
A 1 270 PRO 270 250 250 PRO PRO A . n 
A 1 271 PRO 271 251 251 PRO PRO A . n 
A 1 272 VAL 272 252 252 VAL VAL A . n 
A 1 273 VAL 273 253 253 VAL VAL A . n 
A 1 274 ASN 274 254 254 ASN ASN A . n 
A 1 275 PRO 275 255 255 PRO PRO A . n 
A 1 276 SER 276 256 256 SER SER A . n 
A 1 277 VAL 277 257 257 VAL VAL A . n 
A 1 278 ASN 278 258 258 ASN ASN A . n 
A 1 279 GLY 279 259 259 GLY GLY A . n 
A 1 280 SER 280 260 260 SER SER A . n 
A 1 281 LEU 281 261 261 LEU LEU A . n 
A 1 282 PRO 282 262 262 PRO PRO A . n 
A 1 283 PRO 283 263 263 PRO PRO A . n 
A 1 284 LEU 284 264 264 LEU LEU A . n 
A 1 285 GLY 285 265 265 GLY GLY A . n 
A 1 286 GLU 286 266 266 GLU GLU A . n 
A 1 287 LEU 287 267 267 LEU LEU A . n 
A 1 288 PRO 288 268 268 PRO PRO A . n 
A 1 289 THR 289 269 269 THR THR A . n 
A 1 290 SER 290 270 270 SER SER A . n 
A 1 291 PRO 291 271 271 PRO PRO A . n 
A 1 292 ASP 292 272 272 ASP ASP A . n 
A 1 293 PRO 293 273 273 PRO PRO A . n 
A 1 294 LYS 294 274 274 LYS LYS A . n 
A 1 295 ALA 295 275 275 ALA ALA A . n 
A 1 296 GLY 296 276 276 GLY GLY A . n 
A 1 297 LEU 297 277 277 LEU LEU A . n 
A 1 298 TYR 298 278 278 TYR TYR A . n 
A 1 299 ILE 299 279 279 ILE ILE A . n 
A 1 300 LYS 300 280 280 LYS LYS A . n 
A 1 301 SER 301 281 281 SER SER A . n 
A 1 302 ARG 302 282 282 ARG ARG A . n 
A 1 303 THR 303 283 283 THR THR A . n 
A 1 304 GLY 304 284 284 GLY GLY A . n 
A 1 305 GLN 305 285 285 GLN GLN A . n 
A 1 306 THR 306 286 286 THR THR A . n 
A 1 307 VAL 307 287 287 VAL VAL A . n 
A 1 308 GLN 308 288 288 GLN GLN A . n 
A 1 309 VAL 309 289 289 VAL VAL A . n 
A 1 310 LYS 310 290 290 LYS LYS A . n 
A 1 311 ILE 311 291 291 ILE ILE A . n 
A 1 312 PRO 312 292 292 PRO PRO A . n 
A 1 313 ARG 313 293 293 ARG ARG A . n 
A 1 314 ASP 314 294 294 ASP ASP A . n 
A 1 315 CYS 315 295 295 CYS CYS A . n 
A 1 316 ILE 316 296 296 ILE ILE A . n 
A 1 317 ALA 317 297 297 ALA ALA A . n 
A 1 318 PHE 318 298 298 PHE PHE A . n 
A 1 319 GLN 319 299 299 GLN GLN A . n 
A 1 320 THR 320 300 300 THR THR A . n 
A 1 321 GLY 321 301 301 GLY GLY A . n 
A 1 322 GLU 322 302 302 GLU GLU A . n 
A 1 323 ALA 323 303 303 ALA ALA A . n 
A 1 324 LEU 324 304 304 LEU LEU A . n 
A 1 325 GLU 325 305 305 GLU GLU A . n 
A 1 326 ARG 326 306 306 ARG ARG A . n 
A 1 327 ILE 327 307 307 ILE ILE A . n 
A 1 328 THR 328 308 308 THR THR A . n 
A 1 329 GLY 329 309 309 GLY GLY A . n 
A 1 330 GLY 330 310 310 GLY GLY A . n 
A 1 331 LYS 331 311 311 LYS LYS A . n 
A 1 332 PHE 332 312 312 PHE PHE A . n 
A 1 333 LYS 333 313 313 LYS LYS A . n 
A 1 334 ALA 334 314 314 ALA ALA A . n 
A 1 335 VAL 335 315 315 VAL VAL A . n 
A 1 336 PRO 336 316 316 PRO PRO A . n 
A 1 337 HIS 337 317 317 HIS HIS A . n 
A 1 338 PHE 338 318 318 PHE PHE A . n 
A 1 339 VAL 339 319 319 VAL VAL A . n 
A 1 340 ARG 340 320 320 ARG ARG A . n 
A 1 341 GLY 341 321 321 GLY GLY A . n 
A 1 342 ALA 342 322 322 ALA ALA A . n 
A 1 343 ARG 343 323 323 ARG ARG A . n 
A 1 344 ALA 344 324 324 ALA ALA A . n 
A 1 345 GLU 345 325 325 GLU GLU A . n 
A 1 346 MET 346 326 326 MET MET A . n 
A 1 347 SER 347 327 327 SER SER A . n 
A 1 348 ALA 348 328 328 ALA ALA A . n 
A 1 349 GLY 349 329 329 GLY GLY A . n 
A 1 350 ARG 350 330 330 ARG ARG A . n 
A 1 351 ILE 351 331 331 ILE ILE A . n 
A 1 352 ALA 352 332 332 ALA ALA A . n 
A 1 353 ARG 353 333 333 ARG ARG A . n 
A 1 354 ASN 354 334 334 ASN ASN A . n 
A 1 355 THR 355 335 335 THR THR A . n 
A 1 356 LEU 356 336 336 LEU LEU A . n 
A 1 357 ALA 357 337 337 ALA ALA A . n 
A 1 358 VAL 358 338 338 VAL VAL A . n 
A 1 359 PHE 359 339 339 PHE PHE A . n 
A 1 360 THR 360 340 340 THR THR A . n 
A 1 361 GLN 361 341 341 GLN GLN A . n 
A 1 362 PRO 362 342 342 PRO PRO A . n 
A 1 363 ASN 363 343 343 ASN ASN A . n 
A 1 364 LEU 364 344 344 LEU LEU A . n 
A 1 365 GLY 365 345 345 GLY GLY A . n 
A 1 366 ASP 366 346 346 ASP ASP A . n 
A 1 367 GLU 367 347 347 GLU GLU A . n 
A 1 368 VAL 368 348 348 VAL VAL A . n 
A 1 369 ASP 369 349 349 ASP ASP A . n 
A 1 370 MET 370 350 350 MET MET A . n 
A 1 371 GLU 371 351 351 GLU GLU A . n 
A 1 372 GLN 372 352 352 GLN GLN A . n 
A 1 373 HIS 373 353 353 HIS HIS A . n 
A 1 374 ILE 374 354 354 ILE ILE A . n 
A 1 375 THR 375 355 355 THR THR A . n 
A 1 376 PHE 376 356 356 PHE PHE A . n 
A 1 377 GLY 377 357 357 GLY GLY A . n 
A 1 378 GLU 378 358 358 GLU GLU A . n 
A 1 379 PHE 379 359 359 PHE PHE A . n 
A 1 380 ALA 380 360 360 ALA ALA A . n 
A 1 381 ARG 381 361 361 ARG ARG A . n 
A 1 382 GLY 382 362 362 GLY GLY A . n 
A 1 383 ILE 383 363 363 ILE ILE A . n 
A 1 384 VAL 384 364 364 VAL VAL A . n 
A 1 385 ALA 385 365 365 ALA ALA A . n 
A 1 386 LYS 386 366 366 LYS LYS A . n 
A 1 387 ASN 387 367 367 ASN ASN A . n 
A 1 388 THR 388 368 368 THR THR A . n 
A 1 389 VAL 389 369 369 VAL VAL A . n 
A 1 390 SER 390 370 370 SER SER A . n 
# 
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 FE  1   401 1   FE  FE  A . 
C 3 HOH 1   501 149 HOH HOH A . 
C 3 HOH 2   502 176 HOH HOH A . 
C 3 HOH 3   503 164 HOH HOH A . 
C 3 HOH 4   504 151 HOH HOH A . 
C 3 HOH 5   505 61  HOH HOH A . 
C 3 HOH 6   506 89  HOH HOH A . 
C 3 HOH 7   507 157 HOH HOH A . 
C 3 HOH 8   508 150 HOH HOH A . 
C 3 HOH 9   509 168 HOH HOH A . 
C 3 HOH 10  510 161 HOH HOH A . 
C 3 HOH 11  511 156 HOH HOH A . 
C 3 HOH 12  512 141 HOH HOH A . 
C 3 HOH 13  513 22  HOH HOH A . 
C 3 HOH 14  514 103 HOH HOH A . 
C 3 HOH 15  515 56  HOH HOH A . 
C 3 HOH 16  516 201 HOH HOH A . 
C 3 HOH 17  517 175 HOH HOH A . 
C 3 HOH 18  518 50  HOH HOH A . 
C 3 HOH 19  519 169 HOH HOH A . 
C 3 HOH 20  520 96  HOH HOH A . 
C 3 HOH 21  521 9   HOH HOH A . 
C 3 HOH 22  522 72  HOH HOH A . 
C 3 HOH 23  523 179 HOH HOH A . 
C 3 HOH 24  524 127 HOH HOH A . 
C 3 HOH 25  525 95  HOH HOH A . 
C 3 HOH 26  526 53  HOH HOH A . 
C 3 HOH 27  527 192 HOH HOH A . 
C 3 HOH 28  528 27  HOH HOH A . 
C 3 HOH 29  529 35  HOH HOH A . 
C 3 HOH 30  530 36  HOH HOH A . 
C 3 HOH 31  531 52  HOH HOH A . 
C 3 HOH 32  532 113 HOH HOH A . 
C 3 HOH 33  533 148 HOH HOH A . 
C 3 HOH 34  534 34  HOH HOH A . 
C 3 HOH 35  535 10  HOH HOH A . 
C 3 HOH 36  536 166 HOH HOH A . 
C 3 HOH 37  537 51  HOH HOH A . 
C 3 HOH 38  538 81  HOH HOH A . 
C 3 HOH 39  539 21  HOH HOH A . 
C 3 HOH 40  540 132 HOH HOH A . 
C 3 HOH 41  541 67  HOH HOH A . 
C 3 HOH 42  542 14  HOH HOH A . 
C 3 HOH 43  543 19  HOH HOH A . 
C 3 HOH 44  544 2   HOH HOH A . 
C 3 HOH 45  545 71  HOH HOH A . 
C 3 HOH 46  546 54  HOH HOH A . 
C 3 HOH 47  547 7   HOH HOH A . 
C 3 HOH 48  548 84  HOH HOH A . 
C 3 HOH 49  549 47  HOH HOH A . 
C 3 HOH 50  550 170 HOH HOH A . 
C 3 HOH 51  551 20  HOH HOH A . 
C 3 HOH 52  552 55  HOH HOH A . 
C 3 HOH 53  553 63  HOH HOH A . 
C 3 HOH 54  554 70  HOH HOH A . 
C 3 HOH 55  555 99  HOH HOH A . 
C 3 HOH 56  556 194 HOH HOH A . 
C 3 HOH 57  557 185 HOH HOH A . 
C 3 HOH 58  558 86  HOH HOH A . 
C 3 HOH 59  559 97  HOH HOH A . 
C 3 HOH 60  560 87  HOH HOH A . 
C 3 HOH 61  561 64  HOH HOH A . 
C 3 HOH 62  562 115 HOH HOH A . 
C 3 HOH 63  563 191 HOH HOH A . 
C 3 HOH 64  564 178 HOH HOH A . 
C 3 HOH 65  565 31  HOH HOH A . 
C 3 HOH 66  566 76  HOH HOH A . 
C 3 HOH 67  567 75  HOH HOH A . 
C 3 HOH 68  568 11  HOH HOH A . 
C 3 HOH 69  569 94  HOH HOH A . 
C 3 HOH 70  570 129 HOH HOH A . 
C 3 HOH 71  571 49  HOH HOH A . 
C 3 HOH 72  572 112 HOH HOH A . 
C 3 HOH 73  573 29  HOH HOH A . 
C 3 HOH 74  574 111 HOH HOH A . 
C 3 HOH 75  575 167 HOH HOH A . 
C 3 HOH 76  576 90  HOH HOH A . 
C 3 HOH 77  577 108 HOH HOH A . 
C 3 HOH 78  578 158 HOH HOH A . 
C 3 HOH 79  579 91  HOH HOH A . 
C 3 HOH 80  580 28  HOH HOH A . 
C 3 HOH 81  581 1   HOH HOH A . 
C 3 HOH 82  582 12  HOH HOH A . 
C 3 HOH 83  583 98  HOH HOH A . 
C 3 HOH 84  584 58  HOH HOH A . 
C 3 HOH 85  585 6   HOH HOH A . 
C 3 HOH 86  586 46  HOH HOH A . 
C 3 HOH 87  587 62  HOH HOH A . 
C 3 HOH 88  588 136 HOH HOH A . 
C 3 HOH 89  589 104 HOH HOH A . 
C 3 HOH 90  590 160 HOH HOH A . 
C 3 HOH 91  591 120 HOH HOH A . 
C 3 HOH 92  592 125 HOH HOH A . 
C 3 HOH 93  593 101 HOH HOH A . 
C 3 HOH 94  594 15  HOH HOH A . 
C 3 HOH 95  595 119 HOH HOH A . 
C 3 HOH 96  596 59  HOH HOH A . 
C 3 HOH 97  597 3   HOH HOH A . 
C 3 HOH 98  598 8   HOH HOH A . 
C 3 HOH 99  599 153 HOH HOH A . 
C 3 HOH 100 600 23  HOH HOH A . 
C 3 HOH 101 601 80  HOH HOH A . 
C 3 HOH 102 602 25  HOH HOH A . 
C 3 HOH 103 603 48  HOH HOH A . 
C 3 HOH 104 604 159 HOH HOH A . 
C 3 HOH 105 605 18  HOH HOH A . 
C 3 HOH 106 606 196 HOH HOH A . 
C 3 HOH 107 607 186 HOH HOH A . 
C 3 HOH 108 608 39  HOH HOH A . 
C 3 HOH 109 609 163 HOH HOH A . 
C 3 HOH 110 610 174 HOH HOH A . 
C 3 HOH 111 611 93  HOH HOH A . 
C 3 HOH 112 612 32  HOH HOH A . 
C 3 HOH 113 613 79  HOH HOH A . 
C 3 HOH 114 614 5   HOH HOH A . 
C 3 HOH 115 615 205 HOH HOH A . 
C 3 HOH 116 616 69  HOH HOH A . 
C 3 HOH 117 617 206 HOH HOH A . 
C 3 HOH 118 618 172 HOH HOH A . 
C 3 HOH 119 619 74  HOH HOH A . 
C 3 HOH 120 620 45  HOH HOH A . 
C 3 HOH 121 621 16  HOH HOH A . 
C 3 HOH 122 622 24  HOH HOH A . 
C 3 HOH 123 623 13  HOH HOH A . 
C 3 HOH 124 624 44  HOH HOH A . 
C 3 HOH 125 625 121 HOH HOH A . 
C 3 HOH 126 626 4   HOH HOH A . 
C 3 HOH 127 627 88  HOH HOH A . 
C 3 HOH 128 628 17  HOH HOH A . 
C 3 HOH 129 629 124 HOH HOH A . 
C 3 HOH 130 630 77  HOH HOH A . 
C 3 HOH 131 631 107 HOH HOH A . 
C 3 HOH 132 632 187 HOH HOH A . 
C 3 HOH 133 633 92  HOH HOH A . 
C 3 HOH 134 634 43  HOH HOH A . 
C 3 HOH 135 635 197 HOH HOH A . 
C 3 HOH 136 636 57  HOH HOH A . 
C 3 HOH 137 637 180 HOH HOH A . 
C 3 HOH 138 638 42  HOH HOH A . 
C 3 HOH 139 639 123 HOH HOH A . 
C 3 HOH 140 640 190 HOH HOH A . 
C 3 HOH 141 641 117 HOH HOH A . 
C 3 HOH 142 642 68  HOH HOH A . 
C 3 HOH 143 643 40  HOH HOH A . 
C 3 HOH 144 644 133 HOH HOH A . 
C 3 HOH 145 645 30  HOH HOH A . 
C 3 HOH 146 646 73  HOH HOH A . 
C 3 HOH 147 647 203 HOH HOH A . 
C 3 HOH 148 648 181 HOH HOH A . 
C 3 HOH 149 649 126 HOH HOH A . 
C 3 HOH 150 650 26  HOH HOH A . 
C 3 HOH 151 651 171 HOH HOH A . 
C 3 HOH 152 652 130 HOH HOH A . 
C 3 HOH 153 653 114 HOH HOH A . 
C 3 HOH 154 654 165 HOH HOH A . 
C 3 HOH 155 655 83  HOH HOH A . 
C 3 HOH 156 656 60  HOH HOH A . 
C 3 HOH 157 657 41  HOH HOH A . 
C 3 HOH 158 658 146 HOH HOH A . 
C 3 HOH 159 659 65  HOH HOH A . 
C 3 HOH 160 660 202 HOH HOH A . 
C 3 HOH 161 661 78  HOH HOH A . 
C 3 HOH 162 662 173 HOH HOH A . 
C 3 HOH 163 663 110 HOH HOH A . 
C 3 HOH 164 664 142 HOH HOH A . 
C 3 HOH 165 665 106 HOH HOH A . 
C 3 HOH 166 666 105 HOH HOH A . 
C 3 HOH 167 667 134 HOH HOH A . 
C 3 HOH 168 668 184 HOH HOH A . 
C 3 HOH 169 669 116 HOH HOH A . 
C 3 HOH 170 670 162 HOH HOH A . 
C 3 HOH 171 671 183 HOH HOH A . 
C 3 HOH 172 672 109 HOH HOH A . 
C 3 HOH 173 673 200 HOH HOH A . 
C 3 HOH 174 674 207 HOH HOH A . 
C 3 HOH 175 675 204 HOH HOH A . 
C 3 HOH 176 676 82  HOH HOH A . 
C 3 HOH 177 677 154 HOH HOH A . 
C 3 HOH 178 678 198 HOH HOH A . 
C 3 HOH 179 679 33  HOH HOH A . 
C 3 HOH 180 680 199 HOH HOH A . 
C 3 HOH 181 681 66  HOH HOH A . 
C 3 HOH 182 682 100 HOH HOH A . 
C 3 HOH 183 683 182 HOH HOH A . 
C 3 HOH 184 684 189 HOH HOH A . 
C 3 HOH 185 685 37  HOH HOH A . 
C 3 HOH 186 686 152 HOH HOH A . 
C 3 HOH 187 687 188 HOH HOH A . 
C 3 HOH 188 688 122 HOH HOH A . 
C 3 HOH 189 689 195 HOH HOH A . 
C 3 HOH 190 690 193 HOH HOH A . 
C 3 HOH 191 691 177 HOH HOH A . 
C 3 HOH 192 692 138 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9HDL 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.105 
_cell.length_a_esd                 ? 
_cell.length_b                     61.744 
_cell.length_b_esd                 ? 
_cell.length_c                     84.325 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9HDL 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_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                   9HDL 
_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             ? 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          ? 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;6.25 % (w/v) PEG 400, 6.25 % (w/v) PEG 500 MME, 6.25 % (w/v) PEG 600, 6.25 % (w/v) PEG 1000, 0.04 M CaCl2, 0.04 M sodium formate and 0.1 M Tris-HCl at pH 8.0
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-11-07 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.8731 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.8731 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9HDL 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               84.32 
_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                                     40809 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.162 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       538483 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.155 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.60 
_reflns_shell.d_res_low                                     1.63 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           22291 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2024 
_reflns_shell.percent_possible_obs                          100.0 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               11.0 
_reflns_shell.pdbx_chi_squared                              1.08 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.2 
_reflns_shell.pdbx_Rrim_I_all                               2.164 
_reflns_shell.pdbx_Rpim_I_all                               0.645 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.624 
_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                                  2.063 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9HDL 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             49.82 
_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                     40709 
_refine.ls_number_reflns_R_free                  2054 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.90 
_refine.ls_percent_reflns_R_free                 5.05 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1830 
_refine.ls_R_factor_R_free                       0.2132 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1814 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.96 
_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                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2634 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.number_atoms_solvent             192 
_refine_hist.number_atoms_total               2827 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        49.82 
# 
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' ? 0.006  ? 2716 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.809  ? 3697 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.722 ? 1004 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 416  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 486  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.60 1.64  . . 141 2529 100.00 . . . . 0.3106 . . . . . . . . . . . 0.3554 
'X-RAY DIFFRACTION' 1.64 1.68  . . 145 2525 100.00 . . . . 0.2676 . . . . . . . . . . . 0.3299 
'X-RAY DIFFRACTION' 1.68 1.72  . . 158 2524 100.00 . . . . 0.2498 . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 1.72 1.77  . . 119 2552 100.00 . . . . 0.2359 . . . . . . . . . . . 0.2792 
'X-RAY DIFFRACTION' 1.77 1.83  . . 141 2543 100.00 . . . . 0.2380 . . . . . . . . . . . 0.3091 
'X-RAY DIFFRACTION' 1.83 1.90  . . 155 2514 100.00 . . . . 0.2051 . . . . . . . . . . . 0.2201 
'X-RAY DIFFRACTION' 1.90 1.97  . . 138 2563 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2197 
'X-RAY DIFFRACTION' 1.97 2.06  . . 127 2560 100.00 . . . . 0.1732 . . . . . . . . . . . 0.2166 
'X-RAY DIFFRACTION' 2.06 2.17  . . 132 2569 100.00 . . . . 0.1720 . . . . . . . . . . . 0.2227 
'X-RAY DIFFRACTION' 2.17 2.31  . . 126 2575 100.00 . . . . 0.1702 . . . . . . . . . . . 0.1857 
'X-RAY DIFFRACTION' 2.31 2.49  . . 139 2583 100.00 . . . . 0.1690 . . . . . . . . . . . 0.2046 
'X-RAY DIFFRACTION' 2.49 2.74  . . 114 2601 100.00 . . . . 0.1766 . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 2.74 3.13  . . 139 2612 100.00 . . . . 0.1821 . . . . . . . . . . . 0.2306 
'X-RAY DIFFRACTION' 3.13 3.95  . . 149 2622 100.00 . . . . 0.1652 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 3.95 49.82 . . 131 2783 100.00 . . . . 0.1678 . . . . . . . . . . . 0.1942 
# 
_struct.entry_id                     9HDL 
_struct.title                        
;Crystal structure of Pyrimidine Nucleoside 2'-Hydroxylase (PDN2'H) from Neurospora crassa
;
_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        9HDL 
_struct_keywords.text            'alpha-ketoglutarate-dependent dioxygenase, nucleoside hydroxylase, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q7SHQ5_NEUCR 
_struct_ref.pdbx_db_accession          Q7SHQ5 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAPIAQAVTVSLNDLKNGTVSLEALEEAFGPDSLGILVVKDVPAEFAELRHRLLSYSSYLGNLPKSELDRLENEKAKYLT
GWSLGKETLKNGQVDNLKGSYYANCAFYVDPSLSCAKPTEEFNPDNFPEYLSPNLWPQESTLPGFKPTFEDLCRLIIDVA
VLVARACDRFAEKQIAGYPAGYLEGVVKTSTTTKARLLHYFPEEATATDASKESNKEEEGDEDDWCATHLDHGCLTGLTS
AMFVDEAATPPVVNPSVNGSLPPLGELPTSPDPKAGLYIKSRTGQTVQVKIPRDCIAFQTGEALERITGGKFKAVPHFVR
GARAEMSAGRIARNTLAVFTQPNLGDEVDMEQHITFGEFARGIVAKNTVS
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9HDL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 21 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 390 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q7SHQ5 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  370 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       370 
# 
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 9HDL MET A 1  ? UNP Q7SHQ5 ? ? 'initiating methionine' -19 1  
1 9HDL GLY A 2  ? UNP Q7SHQ5 ? ? 'expression tag'        -18 2  
1 9HDL SER A 3  ? UNP Q7SHQ5 ? ? 'expression tag'        -17 3  
1 9HDL SER A 4  ? UNP Q7SHQ5 ? ? 'expression tag'        -16 4  
1 9HDL HIS A 5  ? UNP Q7SHQ5 ? ? 'expression tag'        -15 5  
1 9HDL HIS A 6  ? UNP Q7SHQ5 ? ? 'expression tag'        -14 6  
1 9HDL HIS A 7  ? UNP Q7SHQ5 ? ? 'expression tag'        -13 7  
1 9HDL HIS A 8  ? UNP Q7SHQ5 ? ? 'expression tag'        -12 8  
1 9HDL HIS A 9  ? UNP Q7SHQ5 ? ? 'expression tag'        -11 9  
1 9HDL HIS A 10 ? UNP Q7SHQ5 ? ? 'expression tag'        -10 10 
1 9HDL SER A 11 ? UNP Q7SHQ5 ? ? 'expression tag'        -9  11 
1 9HDL SER A 12 ? UNP Q7SHQ5 ? ? 'expression tag'        -8  12 
1 9HDL GLY A 13 ? UNP Q7SHQ5 ? ? 'expression tag'        -7  13 
1 9HDL LEU A 14 ? UNP Q7SHQ5 ? ? 'expression tag'        -6  14 
1 9HDL VAL A 15 ? UNP Q7SHQ5 ? ? 'expression tag'        -5  15 
1 9HDL PRO A 16 ? UNP Q7SHQ5 ? ? 'expression tag'        -4  16 
1 9HDL ARG A 17 ? UNP Q7SHQ5 ? ? 'expression tag'        -3  17 
1 9HDL GLY A 18 ? UNP Q7SHQ5 ? ? 'expression tag'        -2  18 
1 9HDL SER A 19 ? UNP Q7SHQ5 ? ? 'expression tag'        -1  19 
1 9HDL HIS A 20 ? UNP Q7SHQ5 ? ? 'expression tag'        0   20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 140   ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  15440 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 32  ? ASN A 37  ? LEU A 12  ASN A 17  1 ? 6  
HELX_P HELX_P2  AA2 SER A 41  ? GLY A 50  ? SER A 21  GLY A 30  1 ? 10 
HELX_P HELX_P3  AA3 GLU A 65  ? ASN A 82  ? GLU A 45  ASN A 62  1 ? 18 
HELX_P HELX_P4  AA4 PRO A 84  ? ARG A 90  ? PRO A 64  ARG A 70  1 ? 7  
HELX_P HELX_P5  AA5 LEU A 91  ? GLU A 92  ? LEU A 71  GLU A 72  5 ? 2  
HELX_P HELX_P6  AA6 ASN A 93  ? LYS A 97  ? ASN A 73  LYS A 77  5 ? 5  
HELX_P HELX_P7  AA7 ALA A 126 ? VAL A 129 ? ALA A 106 VAL A 109 5 ? 4  
HELX_P HELX_P8  AA8 PHE A 147 ? SER A 152 ? PHE A 127 SER A 132 1 ? 6  
HELX_P HELX_P9  AA9 GLY A 164 ? ILE A 195 ? GLY A 144 ILE A 175 1 ? 32 
HELX_P HELX_P10 AB1 GLY A 201 ? THR A 209 ? GLY A 181 THR A 189 1 ? 9  
HELX_P HELX_P11 AB2 GLY A 321 ? THR A 328 ? GLY A 301 THR A 308 1 ? 8  
HELX_P HELX_P12 AB3 ARG A 343 ? SER A 347 ? ARG A 323 SER A 327 5 ? 5  
HELX_P HELX_P13 AB4 PHE A 376 ? ARG A 381 ? PHE A 356 ARG A 361 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 249 NE2 ? ? ? 1_555 B FE  . FE ? ? A HIS 229 A FE  401 1_555 ? ? ? ? ? ? ? 2.144 ? ? 
metalc2 metalc ? ? A ASP 251 OD1 ? ? ? 1_555 B FE  . FE ? ? A ASP 231 A FE  401 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc3 metalc ? ? A HIS 337 NE2 ? ? ? 1_555 B FE  . FE ? ? A HIS 317 A FE  401 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc4 metalc ? ? B FE  .   FE  ? ? ? 1_555 C HOH . O  ? ? A FE  401 A HOH 521 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc5 metalc ? ? B FE  .   FE  ? ? ? 1_555 C HOH . O  ? ? A FE  401 A HOH 657 1_555 ? ? ? ? ? ? ? 2.212 ? ? 
metalc6 metalc ? ? B FE  .   FE  ? ? ? 1_555 C HOH . O  ? ? A FE  401 A HOH 658 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 OD1 ? A ASP 251 ? A ASP 231 ? 1_555 94.5  ? 
2  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 NE2 ? A HIS 337 ? A HIS 317 ? 1_555 87.3  ? 
3  OD1 ? A ASP 251 ? A ASP 231 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 NE2 ? A HIS 337 ? A HIS 317 ? 1_555 88.5  ? 
4  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 521 ? 1_555 176.2 ? 
5  OD1 ? A ASP 251 ? A ASP 231 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 521 ? 1_555 88.0  ? 
6  NE2 ? A HIS 337 ? A HIS 317 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 521 ? 1_555 95.6  ? 
7  NE2 ? A HIS 249 ? A HIS 229 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 657 ? 1_555 92.1  ? 
8  OD1 ? A ASP 251 ? A ASP 231 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 657 ? 1_555 91.5  ? 
9  NE2 ? A HIS 337 ? A HIS 317 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 657 ? 1_555 179.3 ? 
10 O   ? C HOH .   ? A HOH 521 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 657 ? 1_555 85.1  ? 
11 NE2 ? A HIS 249 ? A HIS 229 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 658 ? 1_555 91.8  ? 
12 OD1 ? A ASP 251 ? A ASP 231 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 658 ? 1_555 173.7 ? 
13 NE2 ? A HIS 337 ? A HIS 317 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 658 ? 1_555 91.7  ? 
14 O   ? C HOH .   ? A HOH 521 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 658 ? 1_555 85.6  ? 
15 O   ? C HOH .   ? A HOH 657 ? 1_555 FE ? B FE . ? A FE 401 ? 1_555 O   ? C HOH .   ? A HOH 658 ? 1_555 88.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? 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 VAL A 28  ? SER A 31  ? VAL A 8   SER A 11  
AA1 2 ILE A 56  ? LYS A 60  ? ILE A 36  LYS A 40  
AA1 3 ILE A 316 ? THR A 320 ? ILE A 296 THR A 300 
AA1 4 LEU A 255 ? LEU A 258 ? LEU A 235 LEU A 238 
AA1 5 ILE A 351 ? THR A 360 ? ILE A 331 THR A 340 
AA1 6 LYS A 214 ? TYR A 220 ? LYS A 194 TYR A 200 
AA1 7 LEU A 117 ? ASN A 124 ? LEU A 97  ASN A 104 
AA1 8 GLY A 101 ? LYS A 106 ? GLY A 81  LYS A 86  
AA2 1 VAL A 28  ? SER A 31  ? VAL A 8   SER A 11  
AA2 2 ILE A 56  ? LYS A 60  ? ILE A 36  LYS A 40  
AA2 3 ILE A 316 ? THR A 320 ? ILE A 296 THR A 300 
AA2 4 LEU A 255 ? LEU A 258 ? LEU A 235 LEU A 238 
AA2 5 ILE A 351 ? THR A 360 ? ILE A 331 THR A 340 
AA2 6 MET A 262 ? ASP A 265 ? MET A 242 ASP A 245 
AA3 1 THR A 306 ? VAL A 309 ? THR A 286 VAL A 289 
AA3 2 GLY A 296 ? LYS A 300 ? GLY A 276 LYS A 280 
AA3 3 HIS A 337 ? ARG A 340 ? HIS A 317 ARG A 320 
AA4 1 GLU A 367 ? ASP A 369 ? GLU A 347 ASP A 349 
AA4 2 ILE A 374 ? THR A 375 ? ILE A 354 THR A 355 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 28  ? N VAL A 8   O VAL A 58  ? O VAL A 38  
AA1 2 3 N VAL A 59  ? N VAL A 39  O ILE A 316 ? O ILE A 296 
AA1 3 4 O GLN A 319 ? O GLN A 299 N THR A 256 ? N THR A 236 
AA1 4 5 N GLY A 257 ? N GLY A 237 O VAL A 358 ? O VAL A 338 
AA1 5 6 O ARG A 353 ? O ARG A 333 N TYR A 220 ? N TYR A 200 
AA1 6 7 O ALA A 215 ? O ALA A 195 N ALA A 123 ? N ALA A 103 
AA1 7 8 O LYS A 118 ? O LYS A 98  N GLY A 105 ? N GLY A 85  
AA2 1 2 N VAL A 28  ? N VAL A 8   O VAL A 58  ? O VAL A 38  
AA2 2 3 N VAL A 59  ? N VAL A 39  O ILE A 316 ? O ILE A 296 
AA2 3 4 O GLN A 319 ? O GLN A 299 N THR A 256 ? N THR A 236 
AA2 4 5 N GLY A 257 ? N GLY A 237 O VAL A 358 ? O VAL A 338 
AA2 5 6 O ASN A 354 ? O ASN A 334 N MET A 262 ? N MET A 242 
AA3 1 2 O VAL A 309 ? O VAL A 289 N LEU A 297 ? N LEU A 277 
AA3 2 3 N GLY A 296 ? N GLY A 276 O ARG A 340 ? O ARG A 320 
AA4 1 2 N VAL A 368 ? N VAL A 348 O ILE A 374 ? O ILE A 354 
# 
_pdbx_entry_details.entry_id                   9HDL 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    511 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    673 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
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 CYS A 234 ? ? -93.46  -69.42 
2 1 ARG A 330 ? ? -108.51 77.45  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -10.3843 
_pdbx_refine_tls.origin_y         2.0446 
_pdbx_refine_tls.origin_z         -11.5132 
_pdbx_refine_tls.T[1][1]          0.1410 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0054 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0195 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.1369 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0031 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2019 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.9004 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0002 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.4773 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.2156 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.3230 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.0885 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0724 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0611 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0213 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0347 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0483 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0539 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0673 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0188 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0047 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_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   all 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       692 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.95 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 -19 ? A MET 1   
2  1 Y 1 A GLY -18 ? A GLY 2   
3  1 Y 1 A SER -17 ? A SER 3   
4  1 Y 1 A SER -16 ? A SER 4   
5  1 Y 1 A HIS -15 ? A HIS 5   
6  1 Y 1 A HIS -14 ? A HIS 6   
7  1 Y 1 A HIS -13 ? A HIS 7   
8  1 Y 1 A HIS -12 ? A HIS 8   
9  1 Y 1 A HIS -11 ? A HIS 9   
10 1 Y 1 A HIS -10 ? A HIS 10  
11 1 Y 1 A SER -9  ? A SER 11  
12 1 Y 1 A SER -8  ? A SER 12  
13 1 Y 1 A GLY -7  ? A GLY 13  
14 1 Y 1 A LEU -6  ? A LEU 14  
15 1 Y 1 A VAL -5  ? A VAL 15  
16 1 Y 1 A PRO -4  ? A PRO 16  
17 1 Y 1 A ARG -3  ? A ARG 17  
18 1 Y 1 A THR 88  ? A THR 108 
19 1 Y 1 A LEU 89  ? A LEU 109 
20 1 Y 1 A LYS 90  ? A LYS 110 
21 1 Y 1 A ASN 91  ? A ASN 111 
22 1 Y 1 A GLY 92  ? A GLY 112 
23 1 Y 1 A GLN 93  ? A GLN 113 
24 1 Y 1 A VAL 94  ? A VAL 114 
25 1 Y 1 A GLU 204 ? A GLU 224 
26 1 Y 1 A ALA 205 ? A ALA 225 
27 1 Y 1 A THR 206 ? A THR 226 
28 1 Y 1 A ALA 207 ? A ALA 227 
29 1 Y 1 A THR 208 ? A THR 228 
30 1 Y 1 A ASP 209 ? A ASP 229 
31 1 Y 1 A ALA 210 ? A ALA 230 
32 1 Y 1 A SER 211 ? A SER 231 
33 1 Y 1 A LYS 212 ? A LYS 232 
34 1 Y 1 A GLU 213 ? A GLU 233 
35 1 Y 1 A SER 214 ? A SER 234 
36 1 Y 1 A ASN 215 ? A ASN 235 
37 1 Y 1 A LYS 216 ? A LYS 236 
38 1 Y 1 A GLU 217 ? A GLU 237 
39 1 Y 1 A GLU 218 ? A GLU 238 
40 1 Y 1 A GLU 219 ? A GLU 239 
41 1 Y 1 A GLY 220 ? A GLY 240 
42 1 Y 1 A ASP 221 ? A ASP 241 
43 1 Y 1 A GLU 222 ? A GLU 242 
44 1 Y 1 A ASP 223 ? A ASP 243 
45 1 Y 1 A ASP 224 ? A ASP 244 
46 1 Y 1 A TRP 225 ? A TRP 245 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
FE  FE   FE N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
PHE N    N  N N 251 
PHE CA   C  N S 252 
PHE C    C  N N 253 
PHE O    O  N N 254 
PHE CB   C  N N 255 
PHE CG   C  Y N 256 
PHE CD1  C  Y N 257 
PHE CD2  C  Y N 258 
PHE CE1  C  Y N 259 
PHE CE2  C  Y N 260 
PHE CZ   C  Y N 261 
PHE OXT  O  N N 262 
PHE H    H  N N 263 
PHE H2   H  N N 264 
PHE HA   H  N N 265 
PHE HB2  H  N N 266 
PHE HB3  H  N N 267 
PHE HD1  H  N N 268 
PHE HD2  H  N N 269 
PHE HE1  H  N N 270 
PHE HE2  H  N N 271 
PHE HZ   H  N N 272 
PHE HXT  H  N N 273 
PRO N    N  N N 274 
PRO CA   C  N S 275 
PRO C    C  N N 276 
PRO O    O  N N 277 
PRO CB   C  N N 278 
PRO CG   C  N N 279 
PRO CD   C  N N 280 
PRO OXT  O  N N 281 
PRO H    H  N N 282 
PRO HA   H  N N 283 
PRO HB2  H  N N 284 
PRO HB3  H  N N 285 
PRO HG2  H  N N 286 
PRO HG3  H  N N 287 
PRO HD2  H  N N 288 
PRO HD3  H  N N 289 
PRO HXT  H  N N 290 
SER N    N  N N 291 
SER CA   C  N S 292 
SER C    C  N N 293 
SER O    O  N N 294 
SER CB   C  N N 295 
SER OG   O  N N 296 
SER OXT  O  N N 297 
SER H    H  N N 298 
SER H2   H  N N 299 
SER HA   H  N N 300 
SER HB2  H  N N 301 
SER HB3  H  N N 302 
SER HG   H  N N 303 
SER HXT  H  N N 304 
THR N    N  N N 305 
THR CA   C  N S 306 
THR C    C  N N 307 
THR O    O  N N 308 
THR CB   C  N R 309 
THR OG1  O  N N 310 
THR CG2  C  N N 311 
THR OXT  O  N N 312 
THR H    H  N N 313 
THR H2   H  N N 314 
THR HA   H  N N 315 
THR HB   H  N N 316 
THR HG1  H  N N 317 
THR HG21 H  N N 318 
THR HG22 H  N N 319 
THR HG23 H  N N 320 
THR HXT  H  N N 321 
TRP N    N  N N 322 
TRP CA   C  N S 323 
TRP C    C  N N 324 
TRP O    O  N N 325 
TRP CB   C  N N 326 
TRP CG   C  Y N 327 
TRP CD1  C  Y N 328 
TRP CD2  C  Y N 329 
TRP NE1  N  Y N 330 
TRP CE2  C  Y N 331 
TRP CE3  C  Y N 332 
TRP CZ2  C  Y N 333 
TRP CZ3  C  Y N 334 
TRP CH2  C  Y N 335 
TRP OXT  O  N N 336 
TRP H    H  N N 337 
TRP H2   H  N N 338 
TRP HA   H  N N 339 
TRP HB2  H  N N 340 
TRP HB3  H  N N 341 
TRP HD1  H  N N 342 
TRP HE1  H  N N 343 
TRP HE3  H  N N 344 
TRP HZ2  H  N N 345 
TRP HZ3  H  N N 346 
TRP HH2  H  N N 347 
TRP HXT  H  N N 348 
TYR N    N  N N 349 
TYR CA   C  N S 350 
TYR C    C  N N 351 
TYR O    O  N N 352 
TYR CB   C  N N 353 
TYR CG   C  Y N 354 
TYR CD1  C  Y N 355 
TYR CD2  C  Y N 356 
TYR CE1  C  Y N 357 
TYR CE2  C  Y N 358 
TYR CZ   C  Y N 359 
TYR OH   O  N N 360 
TYR OXT  O  N N 361 
TYR H    H  N N 362 
TYR H2   H  N N 363 
TYR HA   H  N N 364 
TYR HB2  H  N N 365 
TYR HB3  H  N N 366 
TYR HD1  H  N N 367 
TYR HD2  H  N N 368 
TYR HE1  H  N N 369 
TYR HE2  H  N N 370 
TYR HH   H  N N 371 
TYR HXT  H  N N 372 
VAL N    N  N N 373 
VAL CA   C  N S 374 
VAL C    C  N N 375 
VAL O    O  N N 376 
VAL CB   C  N N 377 
VAL CG1  C  N N 378 
VAL CG2  C  N N 379 
VAL OXT  O  N N 380 
VAL H    H  N N 381 
VAL H2   H  N N 382 
VAL HA   H  N N 383 
VAL HB   H  N N 384 
VAL HG11 H  N N 385 
VAL HG12 H  N N 386 
VAL HG13 H  N N 387 
VAL HG21 H  N N 388 
VAL HG22 H  N N 389 
VAL HG23 H  N N 390 
VAL HXT  H  N N 391 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9HDL 
_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]   0.017210 
_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]   0.016196 
_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]   0.011859 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 18  ? -5.406  -22.636 3.959   1.00 49.17  ? -2  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 18  ? -5.099  -22.303 5.338   1.00 48.41  ? -2  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 18  ? -6.331  -22.069 6.192   1.00 49.09  ? -2  GLY A C   1 
ATOM   4    O  O   . GLY A 1 18  ? -7.270  -21.402 5.759   1.00 49.85  ? -2  GLY A O   1 
ATOM   5    N  N   . SER A 1 19  ? -6.327  -22.613 7.413   1.00 45.39  ? -1  SER A N   1 
ATOM   6    C  CA  . SER A 1 19  ? -7.478  -22.460 8.300   1.00 52.95  ? -1  SER A CA  1 
ATOM   7    C  C   . SER A 1 19  ? -7.656  -21.029 8.789   1.00 55.01  ? -1  SER A C   1 
ATOM   8    O  O   . SER A 1 19  ? -8.743  -20.680 9.260   1.00 51.71  ? -1  SER A O   1 
ATOM   9    C  CB  . SER A 1 19  ? -7.346  -23.395 9.503   1.00 52.01  ? -1  SER A CB  1 
ATOM   10   O  OG  . SER A 1 19  ? -6.358  -22.923 10.403  1.00 54.91  ? -1  SER A OG  1 
ATOM   11   N  N   . HIS A 1 20  ? -6.618  -20.201 8.702   1.00 44.02  ? 0   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 20  ? -6.677  -18.817 9.149   1.00 53.02  ? 0   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 20  ? -7.064  -17.851 8.036   1.00 56.56  ? 0   HIS A C   1 
ATOM   14   O  O   . HIS A 1 20  ? -7.056  -16.634 8.258   1.00 50.64  ? 0   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 20  ? -5.328  -18.399 9.748   1.00 51.33  ? 0   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 20  ? -4.180  -18.495 8.789   1.00 65.50  ? 0   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 20  ? -3.848  -19.664 8.136   1.00 64.91  ? 0   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 20  ? -3.276  -17.570 8.386   1.00 63.95  ? 0   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 20  ? -2.796  -19.451 7.365   1.00 66.35  ? 0   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 20  ? -2.426  -18.190 7.503   1.00 72.49  ? 0   HIS A NE2 1 
ATOM   21   N  N   . MET A 1 21  ? -7.397  -18.357 6.852   1.00 40.26  ? 1   MET A N   1 
ATOM   22   C  CA  . MET A 1 21  ? -7.734  -17.495 5.733   1.00 38.72  ? 1   MET A CA  1 
ATOM   23   C  C   . MET A 1 21  ? -9.172  -17.004 5.862   1.00 35.27  ? 1   MET A C   1 
ATOM   24   O  O   . MET A 1 21  ? -10.004 -17.612 6.536   1.00 40.76  ? 1   MET A O   1 
ATOM   25   C  CB  . MET A 1 21  ? -7.565  -18.234 4.402   1.00 42.54  ? 1   MET A CB  1 
ATOM   26   C  CG  . MET A 1 21  ? -6.174  -18.756 4.107   1.00 42.86  ? 1   MET A CG  1 
ATOM   27   S  SD  . MET A 1 21  ? -5.050  -17.453 3.585   1.00 49.87  ? 1   MET A SD  1 
ATOM   28   C  CE  . MET A 1 21  ? -4.159  -17.183 5.097   1.00 50.90  ? 1   MET A CE  1 
ATOM   29   N  N   . ALA A 1 22  ? -9.454  -15.880 5.213   1.00 32.00  ? 2   ALA A N   1 
ATOM   30   C  CA  . ALA A 1 22  ? -10.820 -15.412 5.108   1.00 30.56  ? 2   ALA A CA  1 
ATOM   31   C  C   . ALA A 1 22  ? -11.599 -16.328 4.166   1.00 29.22  ? 2   ALA A C   1 
ATOM   32   O  O   . ALA A 1 22  ? -11.017 -16.996 3.310   1.00 36.98  ? 2   ALA A O   1 
ATOM   33   C  CB  . ALA A 1 22  ? -10.861 -13.975 4.594   1.00 32.63  ? 2   ALA A CB  1 
ATOM   34   N  N   . PRO A 1 23  ? -12.918 -16.374 4.291   1.00 31.37  ? 3   PRO A N   1 
ATOM   35   C  CA  . PRO A 1 23  ? -13.691 -17.158 3.321   1.00 29.37  ? 3   PRO A CA  1 
ATOM   36   C  C   . PRO A 1 23  ? -13.540 -16.567 1.928   1.00 30.98  ? 3   PRO A C   1 
ATOM   37   O  O   . PRO A 1 23  ? -13.604 -15.352 1.742   1.00 29.70  ? 3   PRO A O   1 
ATOM   38   C  CB  . PRO A 1 23  ? -15.130 -17.067 3.847   1.00 32.81  ? 3   PRO A CB  1 
ATOM   39   C  CG  . PRO A 1 23  ? -15.139 -15.895 4.784   1.00 37.59  ? 3   PRO A CG  1 
ATOM   40   C  CD  . PRO A 1 23  ? -13.760 -15.798 5.354   1.00 37.22  ? 3   PRO A CD  1 
ATOM   41   N  N   . ILE A 1 24  ? -13.293 -17.430 0.950   1.00 27.80  ? 4   ILE A N   1 
ATOM   42   C  CA  . ILE A 1 24  ? -13.211 -17.005 -0.443  1.00 25.72  ? 4   ILE A CA  1 
ATOM   43   C  C   . ILE A 1 24  ? -14.608 -17.031 -1.045  1.00 26.66  ? 4   ILE A C   1 
ATOM   44   O  O   . ILE A 1 24  ? -15.351 -17.998 -0.861  1.00 30.63  ? 4   ILE A O   1 
ATOM   45   C  CB  . ILE A 1 24  ? -12.250 -17.903 -1.242  1.00 36.28  ? 4   ILE A CB  1 
ATOM   46   C  CG1 . ILE A 1 24  ? -10.812 -17.699 -0.769  1.00 45.35  ? 4   ILE A CG1 1 
ATOM   47   C  CG2 . ILE A 1 24  ? -12.350 -17.600 -2.728  1.00 37.59  ? 4   ILE A CG2 1 
ATOM   48   C  CD1 . ILE A 1 24  ? -9.789  -18.453 -1.585  1.00 51.18  ? 4   ILE A CD1 1 
ATOM   49   N  N   . ALA A 1 25  ? -14.971 -15.958 -1.741  1.00 27.42  ? 5   ALA A N   1 
ATOM   50   C  CA  . ALA A 1 25  ? -16.230 -15.867 -2.462  1.00 26.47  ? 5   ALA A CA  1 
ATOM   51   C  C   . ALA A 1 25  ? -15.957 -15.807 -3.957  1.00 29.98  ? 5   ALA A C   1 
ATOM   52   O  O   . ALA A 1 25  ? -14.894 -15.358 -4.393  1.00 34.11  ? 5   ALA A O   1 
ATOM   53   C  CB  . ALA A 1 25  ? -17.036 -14.637 -2.029  1.00 28.46  ? 5   ALA A CB  1 
ATOM   54   N  N   . GLN A 1 26  ? -16.921 -16.268 -4.743  1.00 29.54  ? 6   GLN A N   1 
ATOM   55   C  CA  . GLN A 1 26  ? -16.836 -16.206 -6.196  1.00 31.37  ? 6   GLN A CA  1 
ATOM   56   C  C   . GLN A 1 26  ? -17.627 -14.997 -6.683  1.00 25.87  ? 6   GLN A C   1 
ATOM   57   O  O   . GLN A 1 26  ? -18.827 -14.895 -6.405  1.00 29.81  ? 6   GLN A O   1 
ATOM   58   C  CB  . GLN A 1 26  ? -17.388 -17.488 -6.819  1.00 40.96  ? 6   GLN A CB  1 
ATOM   59   C  CG  . GLN A 1 26  ? -16.977 -17.704 -8.269  1.00 56.03  ? 6   GLN A CG  1 
ATOM   60   C  CD  . GLN A 1 26  ? -15.508 -18.069 -8.409  1.00 64.93  ? 6   GLN A CD  1 
ATOM   61   O  OE1 . GLN A 1 26  ? -14.859 -18.467 -7.438  1.00 60.92  ? 6   GLN A OE1 1 
ATOM   62   N  NE2 . GLN A 1 26  ? -14.976 -17.935 -9.621  1.00 65.05  ? 6   GLN A NE2 1 
ATOM   63   N  N   . ALA A 1 27  ? -16.965 -14.082 -7.400  1.00 24.94  ? 7   ALA A N   1 
ATOM   64   C  CA  . ALA A 1 27  ? -17.702 -12.971 -7.997  1.00 24.13  ? 7   ALA A CA  1 
ATOM   65   C  C   . ALA A 1 27  ? -18.541 -13.466 -9.170  1.00 22.79  ? 7   ALA A C   1 
ATOM   66   O  O   . ALA A 1 27  ? -18.147 -14.384 -9.900  1.00 24.59  ? 7   ALA A O   1 
ATOM   67   C  CB  . ALA A 1 27  ? -16.751 -11.869 -8.464  1.00 25.07  ? 7   ALA A CB  1 
ATOM   68   N  N   . VAL A 1 28  ? -19.725 -12.870 -9.332  1.00 20.19  ? 8   VAL A N   1 
ATOM   69   C  CA  . VAL A 1 28  ? -20.527 -13.138 -10.518 1.00 21.78  ? 8   VAL A CA  1 
ATOM   70   C  C   . VAL A 1 28  ? -19.711 -12.806 -11.752 1.00 23.86  ? 8   VAL A C   1 
ATOM   71   O  O   . VAL A 1 28  ? -19.076 -11.744 -11.825 1.00 21.37  ? 8   VAL A O   1 
ATOM   72   C  CB  . VAL A 1 28  ? -21.820 -12.311 -10.483 1.00 22.93  ? 8   VAL A CB  1 
ATOM   73   C  CG1 . VAL A 1 28  ? -22.618 -12.511 -11.772 1.00 24.68  ? 8   VAL A CG1 1 
ATOM   74   C  CG2 . VAL A 1 28  ? -22.643 -12.660 -9.265  1.00 22.06  ? 8   VAL A CG2 1 
ATOM   75   N  N   . THR A 1 29  ? -19.744 -13.695 -12.741 1.00 21.29  ? 9   THR A N   1 
ATOM   76   C  CA  . THR A 1 29  ? -18.904 -13.550 -13.924 1.00 21.85  ? 9   THR A CA  1 
ATOM   77   C  C   . THR A 1 29  ? -19.773 -13.649 -15.168 1.00 23.75  ? 9   THR A C   1 
ATOM   78   O  O   . THR A 1 29  ? -20.604 -14.550 -15.274 1.00 26.71  ? 9   THR A O   1 
ATOM   79   C  CB  . THR A 1 29  ? -17.806 -14.618 -13.947 1.00 25.08  ? 9   THR A CB  1 
ATOM   80   O  OG1 . THR A 1 29  ? -16.997 -14.486 -12.766 1.00 27.29  ? 9   THR A OG1 1 
ATOM   81   C  CG2 . THR A 1 29  ? -16.907 -14.457 -15.180 1.00 26.71  ? 9   THR A CG2 1 
ATOM   82   N  N   . VAL A 1 30  ? -19.583 -12.722 -16.104 1.00 22.60  ? 10  VAL A N   1 
ATOM   83   C  CA  . VAL A 1 30  ? -20.329 -12.724 -17.355 1.00 23.11  ? 10  VAL A CA  1 
ATOM   84   C  C   . VAL A 1 30  ? -19.339 -12.570 -18.500 1.00 21.98  ? 10  VAL A C   1 
ATOM   85   O  O   . VAL A 1 30  ? -18.225 -12.073 -18.330 1.00 22.97  ? 10  VAL A O   1 
ATOM   86   C  CB  . VAL A 1 30  ? -21.399 -11.609 -17.424 1.00 22.87  ? 10  VAL A CB  1 
ATOM   87   C  CG1 . VAL A 1 30  ? -22.516 -11.845 -16.394 1.00 26.34  ? 10  VAL A CG1 1 
ATOM   88   C  CG2 . VAL A 1 30  ? -20.761 -10.241 -17.249 1.00 24.13  ? 10  VAL A CG2 1 
ATOM   89   N  N   . SER A 1 31  ? -19.777 -12.974 -19.686 1.00 22.41  ? 11  SER A N   1 
ATOM   90   C  CA  . SER A 1 31  ? -18.948 -12.888 -20.880 1.00 22.19  ? 11  SER A CA  1 
ATOM   91   C  C   . SER A 1 31  ? -19.121 -11.542 -21.578 1.00 24.60  ? 11  SER A C   1 
ATOM   92   O  O   . SER A 1 31  ? -20.242 -11.046 -21.734 1.00 23.32  ? 11  SER A O   1 
ATOM   93   C  CB  . SER A 1 31  ? -19.298 -14.019 -21.848 1.00 21.41  ? 11  SER A CB  1 
ATOM   94   O  OG  . SER A 1 31  ? -18.700 -13.777 -23.110 1.00 26.41  ? 11  SER A OG  1 
ATOM   95   N  N   . LEU A 1 32  ? -17.997 -10.958 -22.014 1.00 20.26  ? 12  LEU A N   1 
ATOM   96   C  CA  . LEU A 1 32  ? -18.073 -9.759  -22.844 1.00 23.40  ? 12  LEU A CA  1 
ATOM   97   C  C   . LEU A 1 32  ? -18.939 -9.994  -24.075 1.00 24.25  ? 12  LEU A C   1 
ATOM   98   O  O   . LEU A 1 32  ? -19.606 -9.073  -24.550 1.00 24.25  ? 12  LEU A O   1 
ATOM   99   C  CB  . LEU A 1 32  ? -16.670 -9.316  -23.268 1.00 21.16  ? 12  LEU A CB  1 
ATOM   100  C  CG  . LEU A 1 32  ? -16.647 -8.056  -24.145 1.00 21.38  ? 12  LEU A CG  1 
ATOM   101  C  CD1 . LEU A 1 32  ? -17.258 -6.886  -23.417 1.00 24.90  ? 12  LEU A CD1 1 
ATOM   102  C  CD2 . LEU A 1 32  ? -15.216 -7.731  -24.564 1.00 28.18  ? 12  LEU A CD2 1 
ATOM   103  N  N   . ASN A 1 33  ? -18.949 -11.216 -24.602 1.00 23.74  ? 13  ASN A N   1 
ATOM   104  C  CA  . ASN A 1 33  ? -19.756 -11.487 -25.788 1.00 25.55  ? 13  ASN A CA  1 
ATOM   105  C  C   . ASN A 1 33  ? -21.230 -11.249 -25.504 1.00 27.53  ? 13  ASN A C   1 
ATOM   106  O  O   . ASN A 1 33  ? -21.957 -10.703 -26.347 1.00 28.67  ? 13  ASN A O   1 
ATOM   107  C  CB  . ASN A 1 33  ? -19.524 -12.914 -26.262 1.00 25.95  ? 13  ASN A CB  1 
ATOM   108  C  CG  . ASN A 1 33  ? -18.105 -13.126 -26.737 1.00 30.76  ? 13  ASN A CG  1 
ATOM   109  O  OD1 . ASN A 1 33  ? -17.481 -12.208 -27.273 1.00 32.04  ? 13  ASN A OD1 1 
ATOM   110  N  ND2 . ASN A 1 33  ? -17.585 -14.327 -26.543 1.00 33.13  ? 13  ASN A ND2 1 
ATOM   111  N  N   . ASP A 1 34  ? -21.675 -11.613 -24.302 1.00 23.41  ? 14  ASP A N   1 
ATOM   112  C  CA  . ASP A 1 34  ? -23.070 -11.403 -23.940 1.00 24.51  ? 14  ASP A CA  1 
ATOM   113  C  C   . ASP A 1 34  ? -23.353 -9.932  -23.676 1.00 25.31  ? 14  ASP A C   1 
ATOM   114  O  O   . ASP A 1 34  ? -24.436 -9.446  -24.008 1.00 23.75  ? 14  ASP A O   1 
ATOM   115  C  CB  . ASP A 1 34  ? -23.421 -12.268 -22.736 1.00 23.02  ? 14  ASP A CB  1 
ATOM   116  C  CG  . ASP A 1 34  ? -23.342 -13.752 -23.063 1.00 34.71  ? 14  ASP A CG  1 
ATOM   117  O  OD1 . ASP A 1 34  ? -23.679 -14.123 -24.210 1.00 42.47  ? 14  ASP A OD1 1 
ATOM   118  O  OD2 . ASP A 1 34  ? -22.944 -14.542 -22.190 1.00 30.98  ? 14  ASP A OD2 1 
ATOM   119  N  N   . LEU A 1 35  ? -22.394 -9.203  -23.088 1.00 20.63  ? 15  LEU A N   1 
ATOM   120  C  CA  . LEU A 1 35  ? -22.577 -7.762  -22.940 1.00 21.46  ? 15  LEU A CA  1 
ATOM   121  C  C   . LEU A 1 35  ? -22.694 -7.088  -24.302 1.00 26.44  ? 15  LEU A C   1 
ATOM   122  O  O   . LEU A 1 35  ? -23.505 -6.173  -24.485 1.00 27.25  ? 15  LEU A O   1 
ATOM   123  C  CB  . LEU A 1 35  ? -21.419 -7.156  -22.138 1.00 19.64  ? 15  LEU A CB  1 
ATOM   124  C  CG  . LEU A 1 35  ? -21.314 -7.602  -20.681 1.00 22.90  ? 15  LEU A CG  1 
ATOM   125  C  CD1 . LEU A 1 35  ? -19.961 -7.182  -20.104 1.00 25.31  ? 15  LEU A CD1 1 
ATOM   126  C  CD2 . LEU A 1 35  ? -22.461 -7.004  -19.861 1.00 26.42  ? 15  LEU A CD2 1 
ATOM   127  N  N   . LYS A 1 36  ? -21.908 -7.543  -25.276 1.00 24.11  ? 16  LYS A N   1 
ATOM   128  C  CA  . LYS A 1 36  ? -21.917 -6.914  -26.593 1.00 28.65  ? 16  LYS A CA  1 
ATOM   129  C  C   . LYS A 1 36  ? -23.201 -7.217  -27.347 1.00 31.07  ? 16  LYS A C   1 
ATOM   130  O  O   . LYS A 1 36  ? -23.714 -6.356  -28.070 1.00 33.46  ? 16  LYS A O   1 
ATOM   131  C  CB  . LYS A 1 36  ? -20.720 -7.378  -27.422 1.00 28.60  ? 16  LYS A CB  1 
ATOM   132  C  CG  . LYS A 1 36  ? -19.393 -6.803  -27.011 1.00 32.86  ? 16  LYS A CG  1 
ATOM   133  C  CD  . LYS A 1 36  ? -18.303 -7.205  -27.995 1.00 40.48  ? 16  LYS A CD  1 
ATOM   134  C  CE  . LYS A 1 36  ? -17.092 -6.287  -27.868 1.00 52.19  ? 16  LYS A CE  1 
ATOM   135  N  NZ  . LYS A 1 36  ? -16.088 -6.533  -28.939 1.00 54.53  ? 16  LYS A NZ  1 
ATOM   136  N  N   . ASN A 1 37  ? -23.720 -8.438  -27.219 1.00 26.46  ? 17  ASN A N   1 
ATOM   137  C  CA  . ASN A 1 37  ? -24.898 -8.833  -27.986 1.00 25.36  ? 17  ASN A CA  1 
ATOM   138  C  C   . ASN A 1 37  ? -26.214 -8.602  -27.250 1.00 30.12  ? 17  ASN A C   1 
ATOM   139  O  O   . ASN A 1 37  ? -27.274 -8.932  -27.795 1.00 34.36  ? 17  ASN A O   1 
ATOM   140  C  CB  . ASN A 1 37  ? -24.779 -10.302 -28.389 1.00 27.58  ? 17  ASN A CB  1 
ATOM   141  C  CG  . ASN A 1 37  ? -23.538 -10.571 -29.212 1.00 41.02  ? 17  ASN A CG  1 
ATOM   142  O  OD1 . ASN A 1 37  ? -23.162 -9.768  -30.069 1.00 42.57  ? 17  ASN A OD1 1 
ATOM   143  N  ND2 . ASN A 1 37  ? -22.886 -11.699 -28.949 1.00 45.51  ? 17  ASN A ND2 1 
ATOM   144  N  N   . GLY A 1 38  ? -26.183 -8.041  -26.042 1.00 29.68  ? 18  GLY A N   1 
ATOM   145  C  CA  . GLY A 1 38  ? -27.420 -7.795  -25.327 1.00 26.57  ? 18  GLY A CA  1 
ATOM   146  C  C   . GLY A 1 38  ? -28.082 -9.028  -24.764 1.00 29.73  ? 18  GLY A C   1 
ATOM   147  O  O   . GLY A 1 38  ? -29.276 -8.994  -24.464 1.00 34.88  ? 18  GLY A O   1 
ATOM   148  N  N   . THR A 1 39  ? -27.338 -10.120 -24.611 1.00 32.13  ? 19  THR A N   1 
ATOM   149  C  CA  . THR A 1 39  ? -27.876 -11.368 -24.092 1.00 28.98  ? 19  THR A CA  1 
ATOM   150  C  C   . THR A 1 39  ? -27.452 -11.631 -22.657 1.00 33.14  ? 19  THR A C   1 
ATOM   151  O  O   . THR A 1 39  ? -27.727 -12.714 -22.131 1.00 38.37  ? 19  THR A O   1 
ATOM   152  C  CB  . THR A 1 39  ? -27.452 -12.546 -24.975 1.00 31.00  ? 19  THR A CB  1 
ATOM   153  O  OG1 . THR A 1 39  ? -26.026 -12.539 -25.125 1.00 33.14  ? 19  THR A OG1 1 
ATOM   154  C  CG2 . THR A 1 39  ? -28.114 -12.458 -26.344 1.00 36.64  ? 19  THR A CG2 1 
ATOM   155  N  N   . VAL A 1 40  ? -26.778 -10.678 -22.014 1.00 25.02  ? 20  VAL A N   1 
ATOM   156  C  CA  . VAL A 1 40  ? -26.347 -10.892 -20.641 1.00 28.65  ? 20  VAL A CA  1 
ATOM   157  C  C   . VAL A 1 40  ? -27.565 -11.034 -19.736 1.00 29.86  ? 20  VAL A C   1 
ATOM   158  O  O   . VAL A 1 40  ? -28.578 -10.346 -19.910 1.00 28.87  ? 20  VAL A O   1 
ATOM   159  C  CB  . VAL A 1 40  ? -25.419 -9.751  -20.186 1.00 27.65  ? 20  VAL A CB  1 
ATOM   160  C  CG1 . VAL A 1 40  ? -26.176 -8.431  -20.096 1.00 33.31  ? 20  VAL A CG1 1 
ATOM   161  C  CG2 . VAL A 1 40  ? -24.767 -10.100 -18.862 1.00 30.23  ? 20  VAL A CG2 1 
ATOM   162  N  N   . SER A 1 41  ? -27.485 -11.965 -18.788 1.00 29.36  ? 21  SER A N   1 
ATOM   163  C  CA  . SER A 1 41  ? -28.573 -12.202 -17.850 1.00 29.07  ? 21  SER A CA  1 
ATOM   164  C  C   . SER A 1 41  ? -28.724 -11.026 -16.890 1.00 28.07  ? 21  SER A C   1 
ATOM   165  O  O   . SER A 1 41  ? -27.787 -10.688 -16.163 1.00 28.08  ? 21  SER A O   1 
ATOM   166  C  CB  . SER A 1 41  ? -28.309 -13.484 -17.066 1.00 33.10  ? 21  SER A CB  1 
ATOM   167  O  OG  . SER A 1 41  ? -29.183 -13.575 -15.955 1.00 32.91  ? 21  SER A OG  1 
ATOM   168  N  N   . LEU A 1 42  ? -29.914 -10.416 -16.863 1.00 27.79  ? 22  LEU A N   1 
ATOM   169  C  CA  . LEU A 1 42  ? -30.155 -9.360  -15.885 1.00 25.37  ? 22  LEU A CA  1 
ATOM   170  C  C   . LEU A 1 42  ? -30.311 -9.910  -14.470 1.00 31.17  ? 22  LEU A C   1 
ATOM   171  O  O   . LEU A 1 42  ? -30.058 -9.182  -13.505 1.00 26.58  ? 22  LEU A O   1 
ATOM   172  C  CB  . LEU A 1 42  ? -31.386 -8.540  -16.288 1.00 31.56  ? 22  LEU A CB  1 
ATOM   173  C  CG  . LEU A 1 42  ? -31.196 -7.705  -17.558 1.00 30.31  ? 22  LEU A CG  1 
ATOM   174  C  CD1 . LEU A 1 42  ? -32.429 -6.858  -17.844 1.00 32.92  ? 22  LEU A CD1 1 
ATOM   175  C  CD2 . LEU A 1 42  ? -29.954 -6.818  -17.457 1.00 29.47  ? 22  LEU A CD2 1 
ATOM   176  N  N   . GLU A 1 43  ? -30.717 -11.178 -14.320 1.00 27.19  ? 23  GLU A N   1 
ATOM   177  C  CA  . GLU A 1 43  ? -30.661 -11.800 -12.999 1.00 27.14  ? 23  GLU A CA  1 
ATOM   178  C  C   . GLU A 1 43  ? -29.218 -11.916 -12.508 1.00 27.96  ? 23  GLU A C   1 
ATOM   179  O  O   . GLU A 1 43  ? -28.923 -11.628 -11.343 1.00 28.98  ? 23  GLU A O   1 
ATOM   180  C  CB  . GLU A 1 43  ? -31.332 -13.175 -13.020 1.00 35.57  ? 23  GLU A CB  1 
ATOM   181  C  CG  . GLU A 1 43  ? -31.334 -13.865 -11.657 1.00 45.90  ? 23  GLU A CG  1 
ATOM   182  C  CD  . GLU A 1 43  ? -32.087 -15.186 -11.654 1.00 56.32  ? 23  GLU A CD  1 
ATOM   183  O  OE1 . GLU A 1 43  ? -32.613 -15.580 -12.716 1.00 55.96  ? 23  GLU A OE1 1 
ATOM   184  O  OE2 . GLU A 1 43  ? -32.156 -15.830 -10.585 1.00 61.49  ? 23  GLU A OE2 1 
ATOM   185  N  N   . ALA A 1 44  ? -28.303 -12.340 -13.380 1.00 25.86  ? 24  ALA A N   1 
ATOM   186  C  CA  . ALA A 1 44  ? -26.893 -12.361 -12.999 1.00 26.24  ? 24  ALA A CA  1 
ATOM   187  C  C   . ALA A 1 44  ? -26.411 -10.966 -12.621 1.00 24.03  ? 24  ALA A C   1 
ATOM   188  O  O   . ALA A 1 44  ? -25.690 -10.793 -11.633 1.00 26.41  ? 24  ALA A O   1 
ATOM   189  C  CB  . ALA A 1 44  ? -26.044 -12.936 -14.134 1.00 28.49  ? 24  ALA A CB  1 
ATOM   190  N  N   . LEU A 1 45  ? -26.819 -9.954  -13.387 1.00 23.29  ? 25  LEU A N   1 
ATOM   191  C  CA  . LEU A 1 45  ? -26.415 -8.586  -13.084 1.00 22.13  ? 25  LEU A CA  1 
ATOM   192  C  C   . LEU A 1 45  ? -26.902 -8.153  -11.706 1.00 22.85  ? 25  LEU A C   1 
ATOM   193  O  O   . LEU A 1 45  ? -26.151 -7.537  -10.939 1.00 22.21  ? 25  LEU A O   1 
ATOM   194  C  CB  . LEU A 1 45  ? -26.942 -7.643  -14.162 1.00 22.02  ? 25  LEU A CB  1 
ATOM   195  C  CG  . LEU A 1 45  ? -26.306 -6.261  -14.085 1.00 20.38  ? 25  LEU A CG  1 
ATOM   196  C  CD1 . LEU A 1 45  ? -24.850 -6.310  -14.512 1.00 22.59  ? 25  LEU A CD1 1 
ATOM   197  C  CD2 . LEU A 1 45  ? -27.099 -5.292  -14.942 1.00 25.24  ? 25  LEU A CD2 1 
ATOM   198  N  N   . GLU A 1 46  ? -28.156 -8.462  -11.373 1.00 22.68  ? 26  GLU A N   1 
ATOM   199  C  CA  . GLU A 1 46  ? -28.664 -8.108  -10.053 1.00 25.84  ? 26  GLU A CA  1 
ATOM   200  C  C   . GLU A 1 46  ? -27.996 -8.925  -8.952  1.00 24.82  ? 26  GLU A C   1 
ATOM   201  O  O   . GLU A 1 46  ? -27.865 -8.443  -7.821  1.00 28.07  ? 26  GLU A O   1 
ATOM   202  C  CB  . GLU A 1 46  ? -30.184 -8.292  -9.993  1.00 25.38  ? 26  GLU A CB  1 
ATOM   203  C  CG  . GLU A 1 46  ? -30.795 -7.732  -8.731  1.00 26.53  ? 26  GLU A CG  1 
ATOM   204  C  CD  . GLU A 1 46  ? -32.308 -7.749  -8.779  1.00 41.70  ? 26  GLU A CD  1 
ATOM   205  O  OE1 . GLU A 1 46  ? -32.862 -8.443  -9.660  1.00 45.53  ? 26  GLU A OE1 1 
ATOM   206  O  OE2 . GLU A 1 46  ? -32.938 -7.062  -7.947  1.00 38.12  ? 26  GLU A OE2 1 
ATOM   207  N  N   . GLU A 1 47  ? -27.593 -10.164 -9.247  1.00 24.28  ? 27  GLU A N   1 
ATOM   208  C  CA  . GLU A 1 47  ? -26.838 -10.928 -8.259  1.00 23.77  ? 27  GLU A CA  1 
ATOM   209  C  C   . GLU A 1 47  ? -25.448 -10.343 -8.056  1.00 19.74  ? 27  GLU A C   1 
ATOM   210  O  O   . GLU A 1 47  ? -24.826 -10.556 -7.003  1.00 23.26  ? 27  GLU A O   1 
ATOM   211  C  CB  . GLU A 1 47  ? -26.745 -12.397 -8.678  1.00 29.26  ? 27  GLU A CB  1 
ATOM   212  C  CG  . GLU A 1 47  ? -28.092 -13.120 -8.594  1.00 35.19  ? 27  GLU A CG  1 
ATOM   213  C  CD  . GLU A 1 47  ? -28.034 -14.581 -9.032  1.00 47.20  ? 27  GLU A CD  1 
ATOM   214  O  OE1 . GLU A 1 47  ? -27.106 -14.957 -9.781  1.00 43.54  ? 27  GLU A OE1 1 
ATOM   215  O  OE2 . GLU A 1 47  ? -28.933 -15.351 -8.631  1.00 50.73  ? 27  GLU A OE2 1 
ATOM   216  N  N   . ALA A 1 48  ? -24.930 -9.647  -9.067  1.00 19.02  ? 28  ALA A N   1 
ATOM   217  C  CA  . ALA A 1 48  ? -23.601 -9.043  -8.960  1.00 20.25  ? 28  ALA A CA  1 
ATOM   218  C  C   . ALA A 1 48  ? -23.631 -7.681  -8.271  1.00 21.11  ? 28  ALA A C   1 
ATOM   219  O  O   . ALA A 1 48  ? -22.687 -7.320  -7.552  1.00 19.22  ? 28  ALA A O   1 
ATOM   220  C  CB  . ALA A 1 48  ? -22.990 -8.901  -10.351 1.00 17.31  ? 28  ALA A CB  1 
ATOM   221  N  N   . PHE A 1 49  ? -24.696 -6.907  -8.497  1.00 20.19  ? 29  PHE A N   1 
ATOM   222  C  CA  . PHE A 1 49  ? -24.744 -5.496  -8.147  1.00 19.34  ? 29  PHE A CA  1 
ATOM   223  C  C   . PHE A 1 49  ? -25.907 -5.109  -7.235  1.00 20.74  ? 29  PHE A C   1 
ATOM   224  O  O   . PHE A 1 49  ? -25.964 -3.954  -6.793  1.00 23.20  ? 29  PHE A O   1 
ATOM   225  C  CB  . PHE A 1 49  ? -24.867 -4.639  -9.418  1.00 18.18  ? 29  PHE A CB  1 
ATOM   226  C  CG  . PHE A 1 49  ? -23.608 -4.508  -10.236 1.00 16.29  ? 29  PHE A CG  1 
ATOM   227  C  CD1 . PHE A 1 49  ? -22.350 -4.813  -9.720  1.00 17.87  ? 29  PHE A CD1 1 
ATOM   228  C  CD2 . PHE A 1 49  ? -23.702 -4.052  -11.541 1.00 19.38  ? 29  PHE A CD2 1 
ATOM   229  C  CE1 . PHE A 1 49  ? -21.210 -4.638  -10.503 1.00 16.13  ? 29  PHE A CE1 1 
ATOM   230  C  CE2 . PHE A 1 49  ? -22.588 -3.887  -12.330 1.00 19.87  ? 29  PHE A CE2 1 
ATOM   231  C  CZ  . PHE A 1 49  ? -21.320 -4.196  -11.810 1.00 17.60  ? 29  PHE A CZ  1 
ATOM   232  N  N   . GLY A 1 50  ? -26.831 -6.023  -6.953  1.00 19.53  ? 30  GLY A N   1 
ATOM   233  C  CA  . GLY A 1 50  ? -28.048 -5.700  -6.235  1.00 24.75  ? 30  GLY A CA  1 
ATOM   234  C  C   . GLY A 1 50  ? -27.886 -5.712  -4.727  1.00 23.50  ? 30  GLY A C   1 
ATOM   235  O  O   . GLY A 1 50  ? -26.781 -5.830  -4.187  1.00 26.88  ? 30  GLY A O   1 
ATOM   236  N  N   . PRO A 1 51  ? -29.009 -5.611  -4.016  1.00 30.12  ? 31  PRO A N   1 
ATOM   237  C  CA  . PRO A 1 51  ? -28.940 -5.348  -2.567  1.00 39.01  ? 31  PRO A CA  1 
ATOM   238  C  C   . PRO A 1 51  ? -28.275 -6.446  -1.745  1.00 38.77  ? 31  PRO A C   1 
ATOM   239  O  O   . PRO A 1 51  ? -27.729 -6.141  -0.679  1.00 40.64  ? 31  PRO A O   1 
ATOM   240  C  CB  . PRO A 1 51  ? -30.414 -5.176  -2.175  1.00 36.38  ? 31  PRO A CB  1 
ATOM   241  C  CG  . PRO A 1 51  ? -31.119 -4.832  -3.458  1.00 52.54  ? 31  PRO A CG  1 
ATOM   242  C  CD  . PRO A 1 51  ? -30.383 -5.559  -4.539  1.00 29.83  ? 31  PRO A CD  1 
ATOM   243  N  N   . ASP A 1 52  ? -28.310 -7.706  -2.187  1.00 28.09  ? 32  ASP A N   1 
ATOM   244  C  CA  . ASP A 1 52  ? -27.672 -8.805  -1.468  1.00 27.44  ? 32  ASP A CA  1 
ATOM   245  C  C   . ASP A 1 52  ? -26.294 -9.160  -2.015  1.00 33.21  ? 32  ASP A C   1 
ATOM   246  O  O   . ASP A 1 52  ? -25.747 -10.210 -1.652  1.00 28.55  ? 32  ASP A O   1 
ATOM   247  C  CB  . ASP A 1 52  ? -28.555 -10.049 -1.507  1.00 30.50  ? 32  ASP A CB  1 
ATOM   248  C  CG  . ASP A 1 52  ? -29.844 -9.863  -0.753  1.00 47.95  ? 32  ASP A CG  1 
ATOM   249  O  OD1 . ASP A 1 52  ? -29.777 -9.539  0.454   1.00 47.08  ? 32  ASP A OD1 1 
ATOM   250  O  OD2 . ASP A 1 52  ? -30.919 -10.028 -1.372  1.00 43.90  ? 32  ASP A OD2 1 
ATOM   251  N  N   . SER A 1 53  ? -25.714 -8.312  -2.859  1.00 26.71  ? 33  SER A N   1 
ATOM   252  C  CA  . SER A 1 53  ? -24.589 -8.694  -3.695  1.00 23.46  ? 33  SER A CA  1 
ATOM   253  C  C   . SER A 1 53  ? -23.256 -8.239  -3.099  1.00 25.62  ? 33  SER A C   1 
ATOM   254  O  O   . SER A 1 53  ? -23.193 -7.539  -2.084  1.00 24.53  ? 33  SER A O   1 
ATOM   255  C  CB  . SER A 1 53  ? -24.758 -8.092  -5.087  1.00 24.63  ? 33  SER A CB  1 
ATOM   256  O  OG  . SER A 1 53  ? -24.453 -6.699  -5.040  1.00 23.63  ? 33  SER A OG  1 
ATOM   257  N  N   . LEU A 1 54  ? -22.178 -8.620  -3.781  1.00 19.13  ? 34  LEU A N   1 
ATOM   258  C  CA  . LEU A 1 54  ? -20.828 -8.158  -3.471  1.00 18.55  ? 34  LEU A CA  1 
ATOM   259  C  C   . LEU A 1 54  ? -20.473 -6.852  -4.175  1.00 19.62  ? 34  LEU A C   1 
ATOM   260  O  O   . LEU A 1 54  ? -19.384 -6.321  -3.953  1.00 20.45  ? 34  LEU A O   1 
ATOM   261  C  CB  . LEU A 1 54  ? -19.820 -9.242  -3.847  1.00 18.47  ? 34  LEU A CB  1 
ATOM   262  C  CG  . LEU A 1 54  ? -19.958 -10.553 -3.068  1.00 21.31  ? 34  LEU A CG  1 
ATOM   263  C  CD1 . LEU A 1 54  ? -19.006 -11.588 -3.601  1.00 25.80  ? 34  LEU A CD1 1 
ATOM   264  C  CD2 . LEU A 1 54  ? -19.776 -10.366 -1.543  1.00 22.39  ? 34  LEU A CD2 1 
ATOM   265  N  N   . GLY A 1 55  ? -21.368 -6.318  -5.005  1.00 17.45  ? 35  GLY A N   1 
ATOM   266  C  CA  . GLY A 1 55  ? -21.095 -5.077  -5.707  1.00 18.45  ? 35  GLY A CA  1 
ATOM   267  C  C   . GLY A 1 55  ? -19.974 -5.174  -6.713  1.00 19.14  ? 35  GLY A C   1 
ATOM   268  O  O   . GLY A 1 55  ? -19.274 -4.183  -6.951  1.00 17.96  ? 35  GLY A O   1 
ATOM   269  N  N   . ILE A 1 56  ? -19.783 -6.342  -7.316  1.00 19.14  ? 36  ILE A N   1 
ATOM   270  C  CA  . ILE A 1 56  ? -18.662 -6.553  -8.227  1.00 19.56  ? 36  ILE A CA  1 
ATOM   271  C  C   . ILE A 1 56  ? -19.083 -7.561  -9.280  1.00 20.60  ? 36  ILE A C   1 
ATOM   272  O  O   . ILE A 1 56  ? -19.841 -8.493  -9.001  1.00 20.92  ? 36  ILE A O   1 
ATOM   273  C  CB  . ILE A 1 56  ? -17.386 -7.010  -7.478  1.00 17.88  ? 36  ILE A CB  1 
ATOM   274  C  CG1 . ILE A 1 56  ? -16.194 -7.017  -8.438  1.00 18.97  ? 36  ILE A CG1 1 
ATOM   275  C  CG2 . ILE A 1 56  ? -17.584 -8.380  -6.821  1.00 19.66  ? 36  ILE A CG2 1 
ATOM   276  C  CD1 . ILE A 1 56  ? -14.844 -7.192  -7.742  1.00 18.29  ? 36  ILE A CD1 1 
ATOM   277  N  N   . LEU A 1 57  ? -18.613 -7.337  -10.499 1.00 18.21  ? 37  LEU A N   1 
ATOM   278  C  CA  . LEU A 1 57  ? -18.922 -8.176  -11.650 1.00 17.54  ? 37  LEU A CA  1 
ATOM   279  C  C   . LEU A 1 57  ? -17.616 -8.430  -12.392 1.00 19.61  ? 37  LEU A C   1 
ATOM   280  O  O   . LEU A 1 57  ? -16.887 -7.486  -12.700 1.00 18.91  ? 37  LEU A O   1 
ATOM   281  C  CB  . LEU A 1 57  ? -19.946 -7.477  -12.568 1.00 19.84  ? 37  LEU A CB  1 
ATOM   282  C  CG  . LEU A 1 57  ? -20.256 -8.175  -13.887 1.00 20.00  ? 37  LEU A CG  1 
ATOM   283  C  CD1 . LEU A 1 57  ? -21.129 -9.416  -13.638 1.00 20.34  ? 37  LEU A CD1 1 
ATOM   284  C  CD2 . LEU A 1 57  ? -20.905 -7.206  -14.881 1.00 17.79  ? 37  LEU A CD2 1 
ATOM   285  N  N   . VAL A 1 58  ? -17.297 -9.688  -12.658 1.00 16.04  ? 38  VAL A N   1 
ATOM   286  C  CA  . VAL A 1 58  ? -16.106 -10.024 -13.429 1.00 17.70  ? 38  VAL A CA  1 
ATOM   287  C  C   . VAL A 1 58  ? -16.545 -10.230 -14.868 1.00 21.35  ? 38  VAL A C   1 
ATOM   288  O  O   . VAL A 1 58  ? -17.571 -10.864 -15.121 1.00 21.08  ? 38  VAL A O   1 
ATOM   289  C  CB  . VAL A 1 58  ? -15.417 -11.283 -12.860 1.00 21.82  ? 38  VAL A CB  1 
ATOM   290  C  CG1 . VAL A 1 58  ? -14.305 -11.770 -13.787 1.00 21.43  ? 38  VAL A CG1 1 
ATOM   291  C  CG2 . VAL A 1 58  ? -14.860 -10.996 -11.472 1.00 22.12  ? 38  VAL A CG2 1 
ATOM   292  N  N   . VAL A 1 59  ? -15.793 -9.671  -15.810 1.00 16.51  ? 39  VAL A N   1 
ATOM   293  C  CA  . VAL A 1 59  ? -16.060 -9.819  -17.236 1.00 17.78  ? 39  VAL A CA  1 
ATOM   294  C  C   . VAL A 1 59  ? -14.933 -10.635 -17.852 1.00 19.90  ? 39  VAL A C   1 
ATOM   295  O  O   . VAL A 1 59  ? -13.757 -10.243 -17.775 1.00 19.30  ? 39  VAL A O   1 
ATOM   296  C  CB  . VAL A 1 59  ? -16.184 -8.459  -17.938 1.00 17.57  ? 39  VAL A CB  1 
ATOM   297  C  CG1 . VAL A 1 59  ? -16.368 -8.667  -19.434 1.00 20.45  ? 39  VAL A CG1 1 
ATOM   298  C  CG2 . VAL A 1 59  ? -17.347 -7.642  -17.342 1.00 17.45  ? 39  VAL A CG2 1 
ATOM   299  N  N   . LYS A 1 60  ? -15.305 -11.772 -18.464 1.00 19.32  ? 40  LYS A N   1 
ATOM   300  C  CA  . LYS A 1 60  ? -14.381 -12.640 -19.175 1.00 19.39  ? 40  LYS A CA  1 
ATOM   301  C  C   . LYS A 1 60  ? -14.559 -12.458 -20.682 1.00 22.02  ? 40  LYS A C   1 
ATOM   302  O  O   . LYS A 1 60  ? -15.381 -11.666 -21.142 1.00 23.02  ? 40  LYS A O   1 
ATOM   303  C  CB  . LYS A 1 60  ? -14.600 -14.100 -18.765 1.00 22.52  ? 40  LYS A CB  1 
ATOM   304  C  CG  . LYS A 1 60  ? -15.955 -14.663 -19.161 1.00 23.82  ? 40  LYS A CG  1 
ATOM   305  C  CD  . LYS A 1 60  ? -16.022 -16.169 -18.827 1.00 30.15  ? 40  LYS A CD  1 
ATOM   306  C  CE  . LYS A 1 60  ? -17.323 -16.793 -19.290 1.00 38.14  ? 40  LYS A CE  1 
ATOM   307  N  NZ  . LYS A 1 60  ? -17.352 -18.248 -18.987 1.00 51.17  ? 40  LYS A NZ  1 
ATOM   308  N  N   . ASP A 1 61  ? -13.782 -13.220 -21.457 1.00 22.91  ? 41  ASP A N   1 
ATOM   309  C  CA  . ASP A 1 61  ? -13.755 -13.094 -22.919 1.00 22.16  ? 41  ASP A CA  1 
ATOM   310  C  C   . ASP A 1 61  ? -13.439 -11.660 -23.345 1.00 27.70  ? 41  ASP A C   1 
ATOM   311  O  O   . ASP A 1 61  ? -14.015 -11.128 -24.297 1.00 26.82  ? 41  ASP A O   1 
ATOM   312  C  CB  . ASP A 1 61  ? -15.071 -13.571 -23.555 1.00 27.81  ? 41  ASP A CB  1 
ATOM   313  C  CG  . ASP A 1 61  ? -15.425 -15.004 -23.183 1.00 38.31  ? 41  ASP A CG  1 
ATOM   314  O  OD1 . ASP A 1 61  ? -14.513 -15.854 -23.099 1.00 33.04  ? 41  ASP A OD1 1 
ATOM   315  O  OD2 . ASP A 1 61  ? -16.626 -15.281 -22.972 1.00 30.21  ? 41  ASP A OD2 1 
ATOM   316  N  N   . VAL A 1 62  ? -12.508 -11.023 -22.637 1.00 27.35  ? 42  VAL A N   1 
ATOM   317  C  CA  . VAL A 1 62  ? -12.189 -9.617  -22.889 1.00 29.02  ? 42  VAL A CA  1 
ATOM   318  C  C   . VAL A 1 62  ? -11.369 -9.522  -24.174 1.00 28.37  ? 42  VAL A C   1 
ATOM   319  O  O   . VAL A 1 62  ? -10.864 -10.546 -24.656 1.00 31.23  ? 42  VAL A O   1 
ATOM   320  C  CB  . VAL A 1 62  ? -11.452 -8.987  -21.690 1.00 29.88  ? 42  VAL A CB  1 
ATOM   321  C  CG1 . VAL A 1 62  ? -12.358 -8.975  -20.461 1.00 27.27  ? 42  VAL A CG1 1 
ATOM   322  C  CG2 . VAL A 1 62  ? -10.148 -9.717  -21.416 1.00 30.62  ? 42  VAL A CG2 1 
ATOM   323  N  N   . PRO A 1 63  ? -11.215 -8.332  -24.766 1.00 33.54  ? 43  PRO A N   1 
ATOM   324  C  CA  . PRO A 1 63  ? -10.499 -8.236  -26.042 1.00 37.86  ? 43  PRO A CA  1 
ATOM   325  C  C   . PRO A 1 63  ? -9.115  -8.868  -25.978 1.00 35.57  ? 43  PRO A C   1 
ATOM   326  O  O   . PRO A 1 63  ? -8.502  -8.980  -24.913 1.00 36.43  ? 43  PRO A O   1 
ATOM   327  C  CB  . PRO A 1 63  ? -10.423 -6.726  -26.288 1.00 32.65  ? 43  PRO A CB  1 
ATOM   328  C  CG  . PRO A 1 63  ? -11.633 -6.190  -25.597 1.00 40.00  ? 43  PRO A CG  1 
ATOM   329  C  CD  . PRO A 1 63  ? -11.779 -7.032  -24.360 1.00 33.62  ? 43  PRO A CD  1 
ATOM   330  N  N   . ALA A 1 64  ? -8.633  -9.293  -27.147 1.00 34.29  ? 44  ALA A N   1 
ATOM   331  C  CA  . ALA A 1 64  ? -7.401  -10.066 -27.216 1.00 36.98  ? 44  ALA A CA  1 
ATOM   332  C  C   . ALA A 1 64  ? -6.208  -9.286  -26.684 1.00 41.29  ? 44  ALA A C   1 
ATOM   333  O  O   . ALA A 1 64  ? -5.276  -9.879  -26.131 1.00 40.01  ? 44  ALA A O   1 
ATOM   334  C  CB  . ALA A 1 64  ? -7.138  -10.494 -28.658 1.00 50.37  ? 44  ALA A CB  1 
ATOM   335  N  N   . GLU A 1 65  ? -6.218  -7.964  -26.838 1.00 35.99  ? 45  GLU A N   1 
ATOM   336  C  CA  . GLU A 1 65  ? -5.073  -7.154  -26.454 1.00 34.43  ? 45  GLU A CA  1 
ATOM   337  C  C   . GLU A 1 65  ? -4.975  -6.915  -24.954 1.00 35.34  ? 45  GLU A C   1 
ATOM   338  O  O   . GLU A 1 65  ? -3.970  -6.351  -24.512 1.00 26.57  ? 45  GLU A O   1 
ATOM   339  C  CB  . GLU A 1 65  ? -5.128  -5.807  -27.182 1.00 32.39  ? 45  GLU A CB  1 
ATOM   340  C  CG  . GLU A 1 65  ? -4.898  -5.916  -28.684 1.00 56.22  ? 45  GLU A CG  1 
ATOM   341  C  CD  . GLU A 1 65  ? -5.246  -4.639  -29.431 1.00 84.35  ? 45  GLU A CD  1 
ATOM   342  O  OE1 . GLU A 1 65  ? -4.472  -3.659  -29.342 1.00 81.02  ? 45  GLU A OE1 1 
ATOM   343  O  OE2 . GLU A 1 65  ? -6.299  -4.616  -30.106 1.00 84.15  ? 45  GLU A OE2 1 
ATOM   344  N  N   . PHE A 1 66  ? -5.974  -7.322  -24.163 1.00 26.00  ? 46  PHE A N   1 
ATOM   345  C  CA  . PHE A 1 66  ? -6.000  -6.914  -22.761 1.00 22.50  ? 46  PHE A CA  1 
ATOM   346  C  C   . PHE A 1 66  ? -4.809  -7.451  -21.978 1.00 23.62  ? 46  PHE A C   1 
ATOM   347  O  O   . PHE A 1 66  ? -4.185  -6.713  -21.211 1.00 22.41  ? 46  PHE A O   1 
ATOM   348  C  CB  . PHE A 1 66  ? -7.285  -7.359  -22.076 1.00 21.88  ? 46  PHE A CB  1 
ATOM   349  C  CG  . PHE A 1 66  ? -7.242  -7.179  -20.581 1.00 19.01  ? 46  PHE A CG  1 
ATOM   350  C  CD1 . PHE A 1 66  ? -7.338  -5.918  -20.020 1.00 18.86  ? 46  PHE A CD1 1 
ATOM   351  C  CD2 . PHE A 1 66  ? -7.082  -8.276  -19.745 1.00 25.61  ? 46  PHE A CD2 1 
ATOM   352  C  CE1 . PHE A 1 66  ? -7.285  -5.745  -18.655 1.00 18.44  ? 46  PHE A CE1 1 
ATOM   353  C  CE2 . PHE A 1 66  ? -7.044  -8.115  -18.380 1.00 19.24  ? 46  PHE A CE2 1 
ATOM   354  C  CZ  . PHE A 1 66  ? -7.144  -6.860  -17.834 1.00 16.74  ? 46  PHE A CZ  1 
ATOM   355  N  N   . ALA A 1 67  ? -4.526  -8.752  -22.088 1.00 23.98  ? 47  ALA A N   1 
ATOM   356  C  CA  . ALA A 1 67  ? -3.521  -9.344  -21.210 1.00 25.66  ? 47  ALA A CA  1 
ATOM   357  C  C   . ALA A 1 67  ? -2.173  -8.653  -21.371 1.00 24.43  ? 47  ALA A C   1 
ATOM   358  O  O   . ALA A 1 67  ? -1.502  -8.329  -20.382 1.00 25.93  ? 47  ALA A O   1 
ATOM   359  C  CB  . ALA A 1 67  ? -3.386  -10.843 -21.494 1.00 27.91  ? 47  ALA A CB  1 
ATOM   360  N  N   . GLU A 1 68  ? -1.780  -8.386  -22.613 1.00 22.63  ? 48  GLU A N   1 
ATOM   361  C  CA  . GLU A 1 68  ? -0.493  -7.751  -22.854 1.00 25.28  ? 48  GLU A CA  1 
ATOM   362  C  C   . GLU A 1 68  ? -0.520  -6.279  -22.464 1.00 24.83  ? 48  GLU A C   1 
ATOM   363  O  O   . GLU A 1 68  ? 0.464   -5.762  -21.930 1.00 24.60  ? 48  GLU A O   1 
ATOM   364  C  CB  . GLU A 1 68  ? -0.085  -7.914  -24.315 1.00 32.76  ? 48  GLU A CB  1 
ATOM   365  C  CG  . GLU A 1 68  ? 1.350   -7.494  -24.554 1.00 39.69  ? 48  GLU A CG  1 
ATOM   366  C  CD  . GLU A 1 68  ? 1.851   -7.836  -25.939 1.00 53.14  ? 48  GLU A CD  1 
ATOM   367  O  OE1 . GLU A 1 68  ? 1.339   -8.804  -26.545 1.00 49.48  ? 48  GLU A OE1 1 
ATOM   368  O  OE2 . GLU A 1 68  ? 2.766   -7.132  -26.414 1.00 44.68  ? 48  GLU A OE2 1 
ATOM   369  N  N   . LEU A 1 69  ? -1.637  -5.586  -22.700 1.00 23.69  ? 49  LEU A N   1 
ATOM   370  C  CA  . LEU A 1 69  ? -1.704  -4.184  -22.283 1.00 18.84  ? 49  LEU A CA  1 
ATOM   371  C  C   . LEU A 1 69  ? -1.655  -4.062  -20.767 1.00 21.17  ? 49  LEU A C   1 
ATOM   372  O  O   . LEU A 1 69  ? -1.009  -3.153  -20.232 1.00 20.31  ? 49  LEU A O   1 
ATOM   373  C  CB  . LEU A 1 69  ? -2.970  -3.510  -22.820 1.00 19.16  ? 49  LEU A CB  1 
ATOM   374  C  CG  . LEU A 1 69  ? -2.987  -3.088  -24.280 1.00 23.78  ? 49  LEU A CG  1 
ATOM   375  C  CD1 . LEU A 1 69  ? -4.428  -2.716  -24.666 1.00 23.73  ? 49  LEU A CD1 1 
ATOM   376  C  CD2 . LEU A 1 69  ? -2.047  -1.911  -24.492 1.00 27.95  ? 49  LEU A CD2 1 
ATOM   377  N  N   . ARG A 1 70  ? -2.333  -4.963  -20.060 1.00 18.27  ? 50  ARG A N   1 
ATOM   378  C  CA  . ARG A 1 70  ? -2.267  -4.984  -18.603 1.00 17.94  ? 50  ARG A CA  1 
ATOM   379  C  C   . ARG A 1 70  ? -0.841  -5.229  -18.140 1.00 18.04  ? 50  ARG A C   1 
ATOM   380  O  O   . ARG A 1 70  ? -0.325  -4.507  -17.281 1.00 18.13  ? 50  ARG A O   1 
ATOM   381  C  CB  . ARG A 1 70  ? -3.176  -6.077  -18.041 1.00 18.55  ? 50  ARG A CB  1 
ATOM   382  C  CG  . ARG A 1 70  ? -2.978  -6.331  -16.536 1.00 18.22  ? 50  ARG A CG  1 
ATOM   383  C  CD  . ARG A 1 70  ? -3.622  -7.665  -16.096 1.00 18.12  ? 50  ARG A CD  1 
ATOM   384  N  NE  . ARG A 1 70  ? -3.212  -8.018  -14.744 1.00 19.70  ? 50  ARG A NE  1 
ATOM   385  C  CZ  . ARG A 1 70  ? -2.038  -8.573  -14.456 1.00 20.25  ? 50  ARG A CZ  1 
ATOM   386  N  NH1 . ARG A 1 70  ? -1.199  -8.955  -15.407 1.00 19.51  ? 50  ARG A NH1 1 
ATOM   387  N  NH2 . ARG A 1 70  ? -1.689  -8.730  -13.183 1.00 19.69  ? 50  ARG A NH2 1 
ATOM   388  N  N   . HIS A 1 71  ? -0.200  -6.266  -18.681 1.00 19.03  ? 51  HIS A N   1 
ATOM   389  C  CA  . HIS A 1 71  ? 1.168   -6.560  -18.270 1.00 21.41  ? 51  HIS A CA  1 
ATOM   390  C  C   . HIS A 1 71  ? 2.081   -5.363  -18.512 1.00 25.36  ? 51  HIS A C   1 
ATOM   391  O  O   . HIS A 1 71  ? 2.880   -4.986  -17.636 1.00 22.37  ? 51  HIS A O   1 
ATOM   392  C  CB  . HIS A 1 71  ? 1.662   -7.798  -19.018 1.00 25.79  ? 51  HIS A CB  1 
ATOM   393  C  CG  . HIS A 1 71  ? 2.951   -8.351  -18.500 1.00 30.23  ? 51  HIS A CG  1 
ATOM   394  N  ND1 . HIS A 1 71  ? 3.690   -9.282  -19.195 1.00 32.60  ? 51  HIS A ND1 1 
ATOM   395  C  CD2 . HIS A 1 71  ? 3.628   -8.112  -17.355 1.00 33.24  ? 51  HIS A CD2 1 
ATOM   396  C  CE1 . HIS A 1 71  ? 4.769   -9.589  -18.499 1.00 28.73  ? 51  HIS A CE1 1 
ATOM   397  N  NE2 . HIS A 1 71  ? 4.759   -8.889  -17.379 1.00 28.11  ? 51  HIS A NE2 1 
ATOM   398  N  N   . ARG A 1 72  ? 1.947   -4.725  -19.681 1.00 23.53  ? 52  ARG A N   1 
ATOM   399  C  CA  . ARG A 1 72  ? 2.797   -3.585  -20.011 1.00 21.73  ? 52  ARG A CA  1 
ATOM   400  C  C   . ARG A 1 72  ? 2.514   -2.386  -19.115 1.00 20.04  ? 52  ARG A C   1 
ATOM   401  O  O   . ARG A 1 72  ? 3.441   -1.774  -18.587 1.00 20.30  ? 52  ARG A O   1 
ATOM   402  C  CB  . ARG A 1 72  ? 2.640   -3.212  -21.485 1.00 23.30  ? 52  ARG A CB  1 
ATOM   403  C  CG  . ARG A 1 72  ? 3.332   -4.199  -22.398 1.00 31.22  ? 52  ARG A CG  1 
ATOM   404  C  CD  . ARG A 1 72  ? 3.163   -3.882  -23.869 1.00 42.69  ? 52  ARG A CD  1 
ATOM   405  N  NE  . ARG A 1 72  ? 3.715   -4.970  -24.671 1.00 44.77  ? 52  ARG A NE  1 
ATOM   406  C  CZ  . ARG A 1 72  ? 4.995   -5.083  -25.004 1.00 56.85  ? 52  ARG A CZ  1 
ATOM   407  N  NH1 . ARG A 1 72  ? 5.886   -4.168  -24.654 1.00 48.90  ? 52  ARG A NH1 1 
ATOM   408  N  NH2 . ARG A 1 72  ? 5.391   -6.143  -25.707 1.00 56.59  ? 52  ARG A NH2 1 
ATOM   409  N  N   . LEU A 1 73  ? 1.245   -2.024  -18.915 1.00 17.66  ? 53  LEU A N   1 
ATOM   410  C  CA  . LEU A 1 73  ? 0.987   -0.818  -18.134 1.00 17.04  ? 53  LEU A CA  1 
ATOM   411  C  C   . LEU A 1 73  ? 1.330   -1.021  -16.666 1.00 18.17  ? 53  LEU A C   1 
ATOM   412  O  O   . LEU A 1 73  ? 1.850   -0.104  -16.007 1.00 17.58  ? 53  LEU A O   1 
ATOM   413  C  CB  . LEU A 1 73  ? -0.473  -0.385  -18.264 1.00 17.34  ? 53  LEU A CB  1 
ATOM   414  C  CG  . LEU A 1 73  ? -0.690  1.044   -17.770 1.00 18.28  ? 53  LEU A CG  1 
ATOM   415  C  CD1 . LEU A 1 73  ? 0.010   2.034   -18.681 1.00 18.42  ? 53  LEU A CD1 1 
ATOM   416  C  CD2 . LEU A 1 73  ? -2.174  1.398   -17.691 1.00 17.67  ? 53  LEU A CD2 1 
ATOM   417  N  N   . LEU A 1 74  ? 1.053   -2.214  -16.126 1.00 17.89  ? 54  LEU A N   1 
ATOM   418  C  CA  . LEU A 1 74  ? 1.444   -2.450  -14.747 1.00 16.89  ? 54  LEU A CA  1 
ATOM   419  C  C   . LEU A 1 74  ? 2.959   -2.479  -14.619 1.00 19.26  ? 54  LEU A C   1 
ATOM   420  O  O   . LEU A 1 74  ? 3.486   -2.051  -13.590 1.00 18.78  ? 54  LEU A O   1 
ATOM   421  C  CB  . LEU A 1 74  ? 0.815   -3.736  -14.219 1.00 17.45  ? 54  LEU A CB  1 
ATOM   422  C  CG  . LEU A 1 74  ? -0.720  -3.631  -14.133 1.00 17.40  ? 54  LEU A CG  1 
ATOM   423  C  CD1 . LEU A 1 74  ? -1.296  -4.909  -13.547 1.00 19.58  ? 54  LEU A CD1 1 
ATOM   424  C  CD2 . LEU A 1 74  ? -1.128  -2.404  -13.303 1.00 17.36  ? 54  LEU A CD2 1 
ATOM   425  N  N   . SER A 1 75  ? 3.670   -2.942  -15.656 1.00 18.22  ? 55  SER A N   1 
ATOM   426  C  CA  . SER A 1 75  ? 5.125   -2.812  -15.648 1.00 19.71  ? 55  SER A CA  1 
ATOM   427  C  C   . SER A 1 75  ? 5.538   -1.347  -15.659 1.00 20.22  ? 55  SER A C   1 
ATOM   428  O  O   . SER A 1 75  ? 6.492   -0.956  -14.975 1.00 22.52  ? 55  SER A O   1 
ATOM   429  C  CB  . SER A 1 75  ? 5.734   -3.542  -16.848 1.00 21.51  ? 55  SER A CB  1 
ATOM   430  O  OG  . SER A 1 75  ? 5.486   -4.937  -16.783 1.00 24.01  ? 55  SER A OG  1 
ATOM   431  N  N   . TYR A 1 76  ? 4.850   -0.531  -16.461 1.00 21.49  ? 56  TYR A N   1 
ATOM   432  C  CA  . TYR A 1 76  ? 5.157   0.892   -16.499 1.00 22.00  ? 56  TYR A CA  1 
ATOM   433  C  C   . TYR A 1 76  ? 4.985   1.522   -15.132 1.00 20.30  ? 56  TYR A C   1 
ATOM   434  O  O   . TYR A 1 76  ? 5.650   2.511   -14.828 1.00 21.31  ? 56  TYR A O   1 
ATOM   435  C  CB  . TYR A 1 76  ? 4.274   1.630   -17.506 1.00 19.95  ? 56  TYR A CB  1 
ATOM   436  C  CG  . TYR A 1 76  ? 4.744   1.651   -18.942 1.00 19.91  ? 56  TYR A CG  1 
ATOM   437  C  CD1 . TYR A 1 76  ? 5.873   2.371   -19.329 1.00 26.93  ? 56  TYR A CD1 1 
ATOM   438  C  CD2 . TYR A 1 76  ? 4.029   0.983   -19.926 1.00 25.48  ? 56  TYR A CD2 1 
ATOM   439  C  CE1 . TYR A 1 76  ? 6.281   2.396   -20.657 1.00 26.98  ? 56  TYR A CE1 1 
ATOM   440  C  CE2 . TYR A 1 76  ? 4.418   1.007   -21.244 1.00 23.88  ? 56  TYR A CE2 1 
ATOM   441  C  CZ  . TYR A 1 76  ? 5.551   1.706   -21.611 1.00 24.86  ? 56  TYR A CZ  1 
ATOM   442  O  OH  . TYR A 1 76  ? 5.936   1.718   -22.933 1.00 30.55  ? 56  TYR A OH  1 
ATOM   443  N  N   . SER A 1 77  ? 4.063   1.011   -14.320 1.00 18.58  ? 57  SER A N   1 
ATOM   444  C  CA  . SER A 1 77  ? 3.935   1.538   -12.961 1.00 18.00  ? 57  SER A CA  1 
ATOM   445  C  C   . SER A 1 77  ? 5.255   1.384   -12.194 1.00 21.38  ? 57  SER A C   1 
ATOM   446  O  O   . SER A 1 77  ? 5.691   2.308   -11.494 1.00 18.78  ? 57  SER A O   1 
ATOM   447  C  CB  . SER A 1 77  ? 2.773   0.852   -12.225 1.00 16.71  ? 57  SER A CB  1 
ATOM   448  O  OG  . SER A 1 77  ? 2.541   1.482   -10.980 1.00 17.98  ? 57  SER A OG  1 
ATOM   449  N  N   . SER A 1 78  ? 5.927   0.239   -12.357 1.00 18.69  ? 58  SER A N   1 
ATOM   450  C  CA  . SER A 1 78  ? 7.230   0.018   -11.729 1.00 19.56  ? 58  SER A CA  1 
ATOM   451  C  C   . SER A 1 78  ? 8.309   0.897   -12.354 1.00 20.38  ? 58  SER A C   1 
ATOM   452  O  O   . SER A 1 78  ? 9.135   1.484   -11.644 1.00 21.33  ? 58  SER A O   1 
ATOM   453  C  CB  . SER A 1 78  ? 7.624   -1.457  -11.844 1.00 19.99  ? 58  SER A CB  1 
ATOM   454  O  OG  . SER A 1 78  ? 7.085   -2.220  -10.790 1.00 22.76  ? 58  SER A OG  1 
ATOM   455  N  N   . TYR A 1 79  ? 8.347   0.961   -13.687 1.00 21.33  ? 59  TYR A N   1 
ATOM   456  C  CA  . TYR A 1 79  ? 9.317   1.847   -14.335 1.00 22.82  ? 59  TYR A CA  1 
ATOM   457  C  C   . TYR A 1 79  ? 9.151   3.275   -13.839 1.00 21.33  ? 59  TYR A C   1 
ATOM   458  O  O   . TYR A 1 79  ? 10.130  3.955   -13.523 1.00 23.70  ? 59  TYR A O   1 
ATOM   459  C  CB  . TYR A 1 79  ? 9.161   1.816   -15.853 1.00 25.53  ? 59  TYR A CB  1 
ATOM   460  C  CG  . TYR A 1 79  ? 9.669   0.577   -16.547 1.00 22.39  ? 59  TYR A CG  1 
ATOM   461  C  CD1 . TYR A 1 79  ? 11.034  0.269   -16.575 1.00 26.62  ? 59  TYR A CD1 1 
ATOM   462  C  CD2 . TYR A 1 79  ? 8.794   -0.262  -17.215 1.00 24.17  ? 59  TYR A CD2 1 
ATOM   463  C  CE1 . TYR A 1 79  ? 11.491  -0.857  -17.231 1.00 30.08  ? 59  TYR A CE1 1 
ATOM   464  C  CE2 . TYR A 1 79  ? 9.246   -1.386  -17.872 1.00 23.98  ? 59  TYR A CE2 1 
ATOM   465  C  CZ  . TYR A 1 79  ? 10.589  -1.681  -17.873 1.00 25.14  ? 59  TYR A CZ  1 
ATOM   466  O  OH  . TYR A 1 79  ? 11.010  -2.802  -18.543 1.00 31.28  ? 59  TYR A OH  1 
ATOM   467  N  N   . LEU A 1 80  ? 7.905   3.739   -13.749 1.00 20.39  ? 60  LEU A N   1 
ATOM   468  C  CA  . LEU A 1 80  ? 7.636   5.109   -13.330 1.00 21.26  ? 60  LEU A CA  1 
ATOM   469  C  C   . LEU A 1 80  ? 8.058   5.322   -11.886 1.00 20.56  ? 60  LEU A C   1 
ATOM   470  O  O   . LEU A 1 80  ? 8.732   6.306   -11.565 1.00 24.05  ? 60  LEU A O   1 
ATOM   471  C  CB  . LEU A 1 80  ? 6.143   5.396   -13.516 1.00 20.16  ? 60  LEU A CB  1 
ATOM   472  C  CG  . LEU A 1 80  ? 5.616   6.760   -13.066 1.00 19.73  ? 60  LEU A CG  1 
ATOM   473  C  CD1 . LEU A 1 80  ? 6.246   7.870   -13.880 1.00 25.62  ? 60  LEU A CD1 1 
ATOM   474  C  CD2 . LEU A 1 80  ? 4.079   6.743   -13.195 1.00 21.82  ? 60  LEU A CD2 1 
ATOM   475  N  N   . GLY A 1 81  ? 7.683   4.395   -11.000 1.00 22.33  ? 61  GLY A N   1 
ATOM   476  C  CA  . GLY A 1 81  ? 8.012   4.528   -9.590  1.00 22.06  ? 61  GLY A CA  1 
ATOM   477  C  C   . GLY A 1 81  ? 9.502   4.511   -9.299  1.00 31.89  ? 61  GLY A C   1 
ATOM   478  O  O   . GLY A 1 81  ? 9.926   5.011   -8.251  1.00 27.51  ? 61  GLY A O   1 
ATOM   479  N  N   . ASN A 1 82  ? 10.308  3.951   -10.198 1.00 24.28  ? 62  ASN A N   1 
ATOM   480  C  CA  . ASN A 1 82  ? 11.743  3.830   -9.966  1.00 27.46  ? 62  ASN A CA  1 
ATOM   481  C  C   . ASN A 1 82  ? 12.575  4.898   -10.661 1.00 29.52  ? 62  ASN A C   1 
ATOM   482  O  O   . ASN A 1 82  ? 13.809  4.863   -10.558 1.00 29.89  ? 62  ASN A O   1 
ATOM   483  C  CB  . ASN A 1 82  ? 12.224  2.447   -10.393 1.00 27.10  ? 62  ASN A CB  1 
ATOM   484  C  CG  . ASN A 1 82  ? 12.022  1.429   -9.314  1.00 40.84  ? 62  ASN A CG  1 
ATOM   485  O  OD1 . ASN A 1 82  ? 12.923  1.171   -8.523  1.00 40.36  ? 62  ASN A OD1 1 
ATOM   486  N  ND2 . ASN A 1 82  ? 10.824  0.855   -9.254  1.00 33.64  ? 62  ASN A ND2 1 
ATOM   487  N  N   . LEU A 1 83  ? 11.939  5.838   -11.358 1.00 25.76  ? 63  LEU A N   1 
ATOM   488  C  CA  . LEU A 1 83  ? 12.667  6.949   -11.942 1.00 30.79  ? 63  LEU A CA  1 
ATOM   489  C  C   . LEU A 1 83  ? 13.334  7.769   -10.839 1.00 35.21  ? 63  LEU A C   1 
ATOM   490  O  O   . LEU A 1 83  ? 12.877  7.771   -9.692  1.00 30.71  ? 63  LEU A O   1 
ATOM   491  C  CB  . LEU A 1 83  ? 11.733  7.842   -12.756 1.00 29.82  ? 63  LEU A CB  1 
ATOM   492  C  CG  . LEU A 1 83  ? 11.134  7.273   -14.047 1.00 32.09  ? 63  LEU A CG  1 
ATOM   493  C  CD1 . LEU A 1 83  ? 10.065  8.200   -14.597 1.00 30.26  ? 63  LEU A CD1 1 
ATOM   494  C  CD2 . LEU A 1 83  ? 12.233  7.047   -15.082 1.00 29.59  ? 63  LEU A CD2 1 
ATOM   495  N  N   . PRO A 1 84  ? 14.427  8.461   -11.158 1.00 33.64  ? 64  PRO A N   1 
ATOM   496  C  CA  . PRO A 1 84  ? 15.058  9.334   -10.163 1.00 34.47  ? 64  PRO A CA  1 
ATOM   497  C  C   . PRO A 1 84  ? 14.063  10.362  -9.641  1.00 37.11  ? 64  PRO A C   1 
ATOM   498  O  O   . PRO A 1 84  ? 13.181  10.826  -10.367 1.00 35.30  ? 64  PRO A O   1 
ATOM   499  C  CB  . PRO A 1 84  ? 16.203  9.996   -10.942 1.00 38.44  ? 64  PRO A CB  1 
ATOM   500  C  CG  . PRO A 1 84  ? 16.462  9.065   -12.108 1.00 30.47  ? 64  PRO A CG  1 
ATOM   501  C  CD  . PRO A 1 84  ? 15.104  8.513   -12.464 1.00 30.48  ? 64  PRO A CD  1 
ATOM   502  N  N   . LYS A 1 85  ? 14.207  10.696  -8.353  1.00 41.83  ? 65  LYS A N   1 
ATOM   503  C  CA  . LYS A 1 85  ? 13.270  11.602  -7.695  1.00 43.60  ? 65  LYS A CA  1 
ATOM   504  C  C   . LYS A 1 85  ? 13.128  12.913  -8.453  1.00 39.22  ? 65  LYS A C   1 
ATOM   505  O  O   . LYS A 1 85  ? 12.040  13.497  -8.482  1.00 46.48  ? 65  LYS A O   1 
ATOM   506  C  CB  . LYS A 1 85  ? 13.724  11.866  -6.256  1.00 53.71  ? 65  LYS A CB  1 
ATOM   507  C  CG  . LYS A 1 85  ? 12.593  11.948  -5.236  1.00 65.44  ? 65  LYS A CG  1 
ATOM   508  C  CD  . LYS A 1 85  ? 12.141  13.381  -4.982  1.00 63.17  ? 65  LYS A CD  1 
ATOM   509  C  CE  . LYS A 1 85  ? 10.963  13.411  -4.012  1.00 68.38  ? 65  LYS A CE  1 
ATOM   510  N  NZ  . LYS A 1 85  ? 10.450  14.789  -3.780  1.00 76.04  ? 65  LYS A NZ  1 
ATOM   511  N  N   . SER A 1 86  ? 14.212  13.387  -9.076  1.00 39.25  ? 66  SER A N   1 
ATOM   512  C  CA  . SER A 1 86  ? 14.136  14.627  -9.846  1.00 49.48  ? 66  SER A CA  1 
ATOM   513  C  C   . SER A 1 86  ? 13.147  14.504  -11.001 1.00 45.86  ? 66  SER A C   1 
ATOM   514  O  O   . SER A 1 86  ? 12.418  15.454  -11.310 1.00 45.88  ? 66  SER A O   1 
ATOM   515  C  CB  . SER A 1 86  ? 15.527  15.016  -10.357 1.00 48.99  ? 66  SER A CB  1 
ATOM   516  O  OG  . SER A 1 86  ? 16.091  13.981  -11.149 1.00 57.44  ? 66  SER A OG  1 
ATOM   517  N  N   . GLU A 1 87  ? 13.098  13.338  -11.646 1.00 42.74  ? 67  GLU A N   1 
ATOM   518  C  CA  . GLU A 1 87  ? 12.152  13.140  -12.739 1.00 45.41  ? 67  GLU A CA  1 
ATOM   519  C  C   . GLU A 1 87  ? 10.716  13.105  -12.229 1.00 40.60  ? 67  GLU A C   1 
ATOM   520  O  O   . GLU A 1 87  ? 9.817   13.700  -12.835 1.00 35.46  ? 67  GLU A O   1 
ATOM   521  C  CB  . GLU A 1 87  ? 12.474  11.843  -13.483 1.00 49.47  ? 67  GLU A CB  1 
ATOM   522  C  CG  . GLU A 1 87  ? 13.765  11.869  -14.290 1.00 51.93  ? 67  GLU A CG  1 
ATOM   523  C  CD  . GLU A 1 87  ? 13.509  11.879  -15.787 1.00 55.94  ? 67  GLU A CD  1 
ATOM   524  O  OE1 . GLU A 1 87  ? 12.361  12.173  -16.200 1.00 53.09  ? 67  GLU A OE1 1 
ATOM   525  O  OE2 . GLU A 1 87  ? 14.458  11.587  -16.547 1.00 63.77  ? 67  GLU A OE2 1 
ATOM   526  N  N   . LEU A 1 88  ? 10.480  12.400  -11.121 1.00 32.71  ? 68  LEU A N   1 
ATOM   527  C  CA  . LEU A 1 88  ? 9.128   12.312  -10.581 1.00 36.42  ? 68  LEU A CA  1 
ATOM   528  C  C   . LEU A 1 88  ? 8.626   13.659  -10.079 1.00 32.80  ? 68  LEU A C   1 
ATOM   529  O  O   . LEU A 1 88  ? 7.435   13.953  -10.200 1.00 34.21  ? 68  LEU A O   1 
ATOM   530  C  CB  . LEU A 1 88  ? 9.087   11.270  -9.470  1.00 35.16  ? 68  LEU A CB  1 
ATOM   531  C  CG  . LEU A 1 88  ? 9.355   9.871   -10.016 1.00 29.41  ? 68  LEU A CG  1 
ATOM   532  C  CD1 . LEU A 1 88  ? 9.531   8.880   -8.883  1.00 31.58  ? 68  LEU A CD1 1 
ATOM   533  C  CD2 . LEU A 1 88  ? 8.242   9.459   -10.961 1.00 28.35  ? 68  LEU A CD2 1 
ATOM   534  N  N   . ASP A 1 89  ? 9.511   14.493  -9.526  1.00 37.46  ? 69  ASP A N   1 
ATOM   535  C  CA  . ASP A 1 89  ? 9.079   15.813  -9.078  1.00 39.65  ? 69  ASP A CA  1 
ATOM   536  C  C   . ASP A 1 89  ? 8.433   16.606  -10.204 1.00 36.45  ? 69  ASP A C   1 
ATOM   537  O  O   . ASP A 1 89  ? 7.529   17.412  -9.952  1.00 38.42  ? 69  ASP A O   1 
ATOM   538  C  CB  . ASP A 1 89  ? 10.255  16.590  -8.494  1.00 37.82  ? 69  ASP A CB  1 
ATOM   539  C  CG  . ASP A 1 89  ? 10.675  16.075  -7.131  1.00 48.63  ? 69  ASP A CG  1 
ATOM   540  O  OD1 . ASP A 1 89  ? 9.818   15.520  -6.410  1.00 53.82  ? 69  ASP A OD1 1 
ATOM   541  O  OD2 . ASP A 1 89  ? 11.864  16.232  -6.782  1.00 49.75  ? 69  ASP A OD2 1 
ATOM   542  N  N   . ARG A 1 90  ? 8.855   16.375  -11.452 1.00 39.71  ? 70  ARG A N   1 
ATOM   543  C  CA  . ARG A 1 90  ? 8.253   17.077  -12.584 1.00 37.94  ? 70  ARG A CA  1 
ATOM   544  C  C   . ARG A 1 90  ? 6.807   16.674  -12.831 1.00 40.70  ? 70  ARG A C   1 
ATOM   545  O  O   . ARG A 1 90  ? 6.096   17.378  -13.554 1.00 35.39  ? 70  ARG A O   1 
ATOM   546  C  CB  . ARG A 1 90  ? 9.067   16.838  -13.859 1.00 41.07  ? 70  ARG A CB  1 
ATOM   547  C  CG  . ARG A 1 90  ? 10.506  17.328  -13.791 1.00 55.09  ? 70  ARG A CG  1 
ATOM   548  C  CD  . ARG A 1 90  ? 11.153  17.367  -15.172 1.00 51.58  ? 70  ARG A CD  1 
ATOM   549  N  NE  . ARG A 1 90  ? 12.591  17.588  -15.081 1.00 57.92  ? 70  ARG A NE  1 
ATOM   550  C  CZ  . ARG A 1 90  ? 13.505  16.629  -15.159 1.00 57.75  ? 70  ARG A CZ  1 
ATOM   551  N  NH1 . ARG A 1 90  ? 13.169  15.368  -15.380 1.00 64.90  ? 70  ARG A NH1 1 
ATOM   552  N  NH2 . ARG A 1 90  ? 14.788  16.943  -15.008 1.00 60.40  ? 70  ARG A NH2 1 
ATOM   553  N  N   . LEU A 1 91  ? 6.351   15.564  -12.257 1.00 34.15  ? 71  LEU A N   1 
ATOM   554  C  CA  . LEU A 1 91  ? 5.009   15.065  -12.503 1.00 37.00  ? 71  LEU A CA  1 
ATOM   555  C  C   . LEU A 1 91  ? 4.048   15.369  -11.363 1.00 32.77  ? 71  LEU A C   1 
ATOM   556  O  O   . LEU A 1 91  ? 2.885   14.958  -11.426 1.00 31.17  ? 71  LEU A O   1 
ATOM   557  C  CB  . LEU A 1 91  ? 5.058   13.557  -12.766 1.00 36.09  ? 71  LEU A CB  1 
ATOM   558  C  CG  . LEU A 1 91  ? 5.924   13.161  -13.962 1.00 39.57  ? 71  LEU A CG  1 
ATOM   559  C  CD1 . LEU A 1 91  ? 6.012   11.644  -14.100 1.00 34.88  ? 71  LEU A CD1 1 
ATOM   560  C  CD2 . LEU A 1 91  ? 5.372   13.790  -15.238 1.00 39.46  ? 71  LEU A CD2 1 
ATOM   561  N  N   . GLU A 1 92  ? 4.493   16.105  -10.344 1.00 30.85  ? 72  GLU A N   1 
ATOM   562  C  CA  . GLU A 1 92  ? 3.632   16.426  -9.216  1.00 34.57  ? 72  GLU A CA  1 
ATOM   563  C  C   . GLU A 1 92  ? 2.769   17.637  -9.537  1.00 38.01  ? 72  GLU A C   1 
ATOM   564  O  O   . GLU A 1 92  ? 3.232   18.605  -10.152 1.00 40.43  ? 72  GLU A O   1 
ATOM   565  C  CB  . GLU A 1 92  ? 4.462   16.689  -7.960  1.00 34.34  ? 72  GLU A CB  1 
ATOM   566  C  CG  . GLU A 1 92  ? 5.088   15.425  -7.370  1.00 35.15  ? 72  GLU A CG  1 
ATOM   567  C  CD  . GLU A 1 92  ? 5.840   15.698  -6.077  1.00 41.35  ? 72  GLU A CD  1 
ATOM   568  O  OE1 . GLU A 1 92  ? 5.787   16.846  -5.587  1.00 50.93  ? 72  GLU A OE1 1 
ATOM   569  O  OE2 . GLU A 1 92  ? 6.488   14.768  -5.553  1.00 42.34  ? 72  GLU A OE2 1 
ATOM   570  N  N   . ASN A 1 93  ? 1.506   17.587  -9.099  1.00 31.65  ? 73  ASN A N   1 
ATOM   571  C  CA  . ASN A 1 93  ? 0.525   18.616  -9.439  1.00 31.43  ? 73  ASN A CA  1 
ATOM   572  C  C   . ASN A 1 93  ? -0.263  18.976  -8.174  1.00 28.33  ? 73  ASN A C   1 
ATOM   573  O  O   . ASN A 1 93  ? -1.362  18.473  -7.936  1.00 31.13  ? 73  ASN A O   1 
ATOM   574  C  CB  . ASN A 1 93  ? -0.383  18.128  -10.559 1.00 33.57  ? 73  ASN A CB  1 
ATOM   575  C  CG  . ASN A 1 93  ? -1.034  19.252  -11.310 1.00 40.98  ? 73  ASN A CG  1 
ATOM   576  O  OD1 . ASN A 1 93  ? -1.020  20.397  -10.865 1.00 44.39  ? 73  ASN A OD1 1 
ATOM   577  N  ND2 . ASN A 1 93  ? -1.618  18.933  -12.461 1.00 43.83  ? 73  ASN A ND2 1 
ATOM   578  N  N   . GLU A 1 94  ? 0.312   19.864  -7.357  1.00 31.89  ? 74  GLU A N   1 
ATOM   579  C  CA  . GLU A 1 94  ? -0.325  20.209  -6.087  1.00 40.30  ? 74  GLU A CA  1 
ATOM   580  C  C   . GLU A 1 94  ? -1.633  20.965  -6.299  1.00 40.10  ? 74  GLU A C   1 
ATOM   581  O  O   . GLU A 1 94  ? -2.608  20.740  -5.571  1.00 38.86  ? 74  GLU A O   1 
ATOM   582  C  CB  . GLU A 1 94  ? 0.626   21.027  -5.213  1.00 47.43  ? 74  GLU A CB  1 
ATOM   583  C  CG  . GLU A 1 94  ? -0.006  21.467  -3.896  1.00 44.42  ? 74  GLU A CG  1 
ATOM   584  C  CD  . GLU A 1 94  ? 0.985   22.123  -2.954  1.00 59.78  ? 74  GLU A CD  1 
ATOM   585  O  OE1 . GLU A 1 94  ? 2.020   22.635  -3.433  1.00 61.67  ? 74  GLU A OE1 1 
ATOM   586  O  OE2 . GLU A 1 94  ? 0.729   22.118  -1.731  1.00 65.57  ? 74  GLU A OE2 1 
ATOM   587  N  N   . LYS A 1 95  ? -1.685  21.855  -7.292  1.00 39.90  ? 75  LYS A N   1 
ATOM   588  C  CA  . LYS A 1 95  ? -2.928  22.576  -7.543  1.00 42.05  ? 75  LYS A CA  1 
ATOM   589  C  C   . LYS A 1 95  ? -4.064  21.642  -7.937  1.00 48.68  ? 75  LYS A C   1 
ATOM   590  O  O   . LYS A 1 95  ? -5.233  21.982  -7.724  1.00 43.08  ? 75  LYS A O   1 
ATOM   591  C  CB  . LYS A 1 95  ? -2.726  23.644  -8.622  1.00 54.10  ? 75  LYS A CB  1 
ATOM   592  C  CG  . LYS A 1 95  ? -1.991  23.175  -9.862  1.00 48.44  ? 75  LYS A CG  1 
ATOM   593  C  CD  . LYS A 1 95  ? -1.754  24.334  -10.820 1.00 72.67  ? 75  LYS A CD  1 
ATOM   594  C  CE  . LYS A 1 95  ? -0.752  23.970  -11.906 1.00 76.70  ? 75  LYS A CE  1 
ATOM   595  N  NZ  . LYS A 1 95  ? -0.409  25.150  -12.755 1.00 75.39  ? 75  LYS A NZ  1 
ATOM   596  N  N   . ALA A 1 96  ? -3.749  20.473  -8.488  1.00 32.04  ? 76  ALA A N   1 
ATOM   597  C  CA  . ALA A 1 96  ? -4.750  19.460  -8.790  1.00 39.28  ? 76  ALA A CA  1 
ATOM   598  C  C   . ALA A 1 96  ? -5.034  18.547  -7.601  1.00 36.27  ? 76  ALA A C   1 
ATOM   599  O  O   . ALA A 1 96  ? -5.660  17.493  -7.777  1.00 34.13  ? 76  ALA A O   1 
ATOM   600  C  CB  . ALA A 1 96  ? -4.309  18.627  -9.998  1.00 37.77  ? 76  ALA A CB  1 
ATOM   601  N  N   . LYS A 1 97  ? -4.600  18.936  -6.397  1.00 37.75  ? 77  LYS A N   1 
ATOM   602  C  CA  . LYS A 1 97  ? -4.690  18.087  -5.210  1.00 33.82  ? 77  LYS A CA  1 
ATOM   603  C  C   . LYS A 1 97  ? -4.020  16.738  -5.449  1.00 29.65  ? 77  LYS A C   1 
ATOM   604  O  O   . LYS A 1 97  ? -4.455  15.715  -4.918  1.00 31.23  ? 77  LYS A O   1 
ATOM   605  C  CB  . LYS A 1 97  ? -6.143  17.890  -4.764  1.00 39.23  ? 77  LYS A CB  1 
ATOM   606  C  CG  . LYS A 1 97  ? -6.909  19.189  -4.521  1.00 46.93  ? 77  LYS A CG  1 
ATOM   607  C  CD  . LYS A 1 97  ? -8.382  18.907  -4.249  1.00 57.46  ? 77  LYS A CD  1 
ATOM   608  C  CE  . LYS A 1 97  ? -9.206  20.188  -4.242  1.00 63.99  ? 77  LYS A CE  1 
ATOM   609  N  NZ  . LYS A 1 97  ? -10.667 19.913  -4.089  1.00 66.25  ? 77  LYS A NZ  1 
ATOM   610  N  N   . TYR A 1 98  ? -2.970  16.744  -6.273  1.00 34.03  ? 78  TYR A N   1 
ATOM   611  C  CA  . TYR A 1 98  ? -2.229  15.542  -6.663  1.00 33.39  ? 78  TYR A CA  1 
ATOM   612  C  C   . TYR A 1 98  ? -3.136  14.452  -7.234  1.00 38.29  ? 78  TYR A C   1 
ATOM   613  O  O   . TYR A 1 98  ? -2.777  13.266  -7.228  1.00 29.46  ? 78  TYR A O   1 
ATOM   614  C  CB  . TYR A 1 98  ? -1.408  15.001  -5.490  1.00 33.37  ? 78  TYR A CB  1 
ATOM   615  C  CG  . TYR A 1 98  ? -0.473  16.017  -4.887  1.00 32.36  ? 78  TYR A CG  1 
ATOM   616  C  CD1 . TYR A 1 98  ? 0.736   16.325  -5.495  1.00 32.53  ? 78  TYR A CD1 1 
ATOM   617  C  CD2 . TYR A 1 98  ? -0.790  16.662  -3.696  1.00 39.79  ? 78  TYR A CD2 1 
ATOM   618  C  CE1 . TYR A 1 98  ? 1.605   17.252  -4.936  1.00 35.41  ? 78  TYR A CE1 1 
ATOM   619  C  CE2 . TYR A 1 98  ? 0.065   17.580  -3.133  1.00 37.87  ? 78  TYR A CE2 1 
ATOM   620  C  CZ  . TYR A 1 98  ? 1.259   17.877  -3.756  1.00 40.67  ? 78  TYR A CZ  1 
ATOM   621  O  OH  . TYR A 1 98  ? 2.110   18.795  -3.194  1.00 43.15  ? 78  TYR A OH  1 
ATOM   622  N  N   . LEU A 1 99  ? -4.313  14.830  -7.739  1.00 30.81  ? 79  LEU A N   1 
ATOM   623  C  CA  . LEU A 1 99  ? -5.213  13.900  -8.407  1.00 30.52  ? 79  LEU A CA  1 
ATOM   624  C  C   . LEU A 1 99  ? -5.040  13.940  -9.917  1.00 23.98  ? 79  LEU A C   1 
ATOM   625  O  O   . LEU A 1 99  ? -5.870  13.395  -10.651 1.00 25.02  ? 79  LEU A O   1 
ATOM   626  C  CB  . LEU A 1 99  ? -6.662  14.183  -8.010  1.00 28.99  ? 79  LEU A CB  1 
ATOM   627  C  CG  . LEU A 1 99  ? -6.969  13.662  -6.600  1.00 42.52  ? 79  LEU A CG  1 
ATOM   628  C  CD1 . LEU A 1 99  ? -8.437  13.816  -6.262  1.00 40.05  ? 79  LEU A CD1 1 
ATOM   629  C  CD2 . LEU A 1 99  ? -6.552  12.198  -6.465  1.00 35.42  ? 79  LEU A CD2 1 
ATOM   630  N  N   . THR A 1 100 ? -3.972  14.583  -10.381 1.00 27.17  ? 80  THR A N   1 
ATOM   631  C  CA  . THR A 1 100 ? -3.435  14.435  -11.722 1.00 20.47  ? 80  THR A CA  1 
ATOM   632  C  C   . THR A 1 100 ? -1.924  14.322  -11.585 1.00 23.78  ? 80  THR A C   1 
ATOM   633  O  O   . THR A 1 100 ? -1.330  15.022  -10.765 1.00 25.61  ? 80  THR A O   1 
ATOM   634  C  CB  . THR A 1 100 ? -3.791  15.627  -12.612 1.00 39.64  ? 80  THR A CB  1 
ATOM   635  O  OG1 . THR A 1 100 ? -5.210  15.671  -12.821 1.00 36.73  ? 80  THR A OG1 1 
ATOM   636  C  CG2 . THR A 1 100 ? -3.087  15.508  -13.936 1.00 36.23  ? 80  THR A CG2 1 
ATOM   637  N  N   . GLY A 1 101 ? -1.306  13.433  -12.364 1.00 22.48  ? 81  GLY A N   1 
ATOM   638  C  CA  . GLY A 1 101 ? 0.130   13.263  -12.283 1.00 26.05  ? 81  GLY A CA  1 
ATOM   639  C  C   . GLY A 1 101 ? 0.527   12.331  -11.151 1.00 19.84  ? 81  GLY A C   1 
ATOM   640  O  O   . GLY A 1 101 ? -0.265  11.520  -10.664 1.00 19.46  ? 81  GLY A O   1 
ATOM   641  N  N   . TRP A 1 102 ? 1.773   12.484  -10.714 1.00 22.35  ? 82  TRP A N   1 
ATOM   642  C  CA  . TRP A 1 102 ? 2.406   11.574  -9.772  1.00 20.87  ? 82  TRP A CA  1 
ATOM   643  C  C   . TRP A 1 102 ? 2.375   12.128  -8.356  1.00 23.28  ? 82  TRP A C   1 
ATOM   644  O  O   . TRP A 1 102 ? 2.492   13.335  -8.140  1.00 25.21  ? 82  TRP A O   1 
ATOM   645  C  CB  . TRP A 1 102 ? 3.859   11.333  -10.178 1.00 24.01  ? 82  TRP A CB  1 
ATOM   646  C  CG  . TRP A 1 102 ? 4.674   10.655  -9.137  1.00 27.59  ? 82  TRP A CG  1 
ATOM   647  C  CD1 . TRP A 1 102 ? 5.443   11.248  -8.166  1.00 31.08  ? 82  TRP A CD1 1 
ATOM   648  C  CD2 . TRP A 1 102 ? 4.831   9.254   -8.973  1.00 28.44  ? 82  TRP A CD2 1 
ATOM   649  N  NE1 . TRP A 1 102 ? 6.059   10.289  -7.404  1.00 33.16  ? 82  TRP A NE1 1 
ATOM   650  C  CE2 . TRP A 1 102 ? 5.697   9.054   -7.879  1.00 33.87  ? 82  TRP A CE2 1 
ATOM   651  C  CE3 . TRP A 1 102 ? 4.324   8.142   -9.643  1.00 27.82  ? 82  TRP A CE3 1 
ATOM   652  C  CZ2 . TRP A 1 102 ? 6.068   7.789   -7.445  1.00 29.72  ? 82  TRP A CZ2 1 
ATOM   653  C  CZ3 . TRP A 1 102 ? 4.690   6.883   -9.201  1.00 31.58  ? 82  TRP A CZ3 1 
ATOM   654  C  CH2 . TRP A 1 102 ? 5.554   6.720   -8.120  1.00 37.37  ? 82  TRP A CH2 1 
ATOM   655  N  N   . SER A 1 103 ? 2.256   11.228  -7.386  1.00 25.15  ? 83  SER A N   1 
ATOM   656  C  CA  . SER A 1 103 ? 2.445   11.623  -5.997  1.00 27.32  ? 83  SER A CA  1 
ATOM   657  C  C   . SER A 1 103 ? 2.918   10.436  -5.176  1.00 28.65  ? 83  SER A C   1 
ATOM   658  O  O   . SER A 1 103 ? 2.642   9.278   -5.497  1.00 25.29  ? 83  SER A O   1 
ATOM   659  C  CB  . SER A 1 103 ? 1.160   12.197  -5.385  1.00 29.46  ? 83  SER A CB  1 
ATOM   660  O  OG  . SER A 1 103 ? 0.122   11.237  -5.392  1.00 27.28  ? 83  SER A OG  1 
ATOM   661  N  N   . LEU A 1 104 ? 3.647   10.744  -4.115  1.00 27.90  ? 84  LEU A N   1 
ATOM   662  C  CA  . LEU A 1 104 ? 4.024   9.762   -3.115  1.00 27.07  ? 84  LEU A CA  1 
ATOM   663  C  C   . LEU A 1 104 ? 3.020   9.829   -1.969  1.00 33.81  ? 84  LEU A C   1 
ATOM   664  O  O   . LEU A 1 104 ? 2.664   10.916  -1.506  1.00 31.31  ? 84  LEU A O   1 
ATOM   665  C  CB  . LEU A 1 104 ? 5.451   10.023  -2.627  1.00 24.40  ? 84  LEU A CB  1 
ATOM   666  C  CG  . LEU A 1 104 ? 6.179   8.854   -1.965  1.00 36.20  ? 84  LEU A CG  1 
ATOM   667  C  CD1 . LEU A 1 104 ? 6.235   7.633   -2.892  1.00 33.51  ? 84  LEU A CD1 1 
ATOM   668  C  CD2 . LEU A 1 104 ? 7.569   9.278   -1.527  1.00 33.34  ? 84  LEU A CD2 1 
ATOM   669  N  N   . GLY A 1 105 ? 2.538   8.667   -1.537  1.00 27.47  ? 85  GLY A N   1 
ATOM   670  C  CA  . GLY A 1 105 ? 1.578   8.594   -0.460  1.00 28.13  ? 85  GLY A CA  1 
ATOM   671  C  C   . GLY A 1 105 ? 1.945   7.466   0.480   1.00 31.87  ? 85  GLY A C   1 
ATOM   672  O  O   . GLY A 1 105 ? 2.854   6.673   0.209   1.00 28.61  ? 85  GLY A O   1 
ATOM   673  N  N   . LYS A 1 106 ? 1.236   7.411   1.599   1.00 32.85  ? 86  LYS A N   1 
ATOM   674  C  CA  . LYS A 1 106 ? 1.453   6.360   2.576   1.00 40.70  ? 86  LYS A CA  1 
ATOM   675  C  C   . LYS A 1 106 ? 0.114   5.798   3.027   1.00 50.78  ? 86  LYS A C   1 
ATOM   676  O  O   . LYS A 1 106 ? -0.917  6.474   2.966   1.00 48.66  ? 86  LYS A O   1 
ATOM   677  C  CB  . LYS A 1 106 ? 2.257   6.862   3.787   1.00 40.15  ? 86  LYS A CB  1 
ATOM   678  C  CG  . LYS A 1 106 ? 3.238   5.833   4.307   1.00 47.50  ? 86  LYS A CG  1 
ATOM   679  C  CD  . LYS A 1 106 ? 4.173   6.413   5.353   1.00 52.20  ? 86  LYS A CD  1 
ATOM   680  C  CE  . LYS A 1 106 ? 3.468   6.541   6.687   1.00 52.41  ? 86  LYS A CE  1 
ATOM   681  N  NZ  . LYS A 1 106 ? 4.375   7.047   7.756   1.00 51.54  ? 86  LYS A NZ  1 
ATOM   682  N  N   . GLU A 1 107 ? 0.149   4.538   3.448   1.00 41.63  ? 87  GLU A N   1 
ATOM   683  C  CA  . GLU A 1 107 ? -0.988  3.844   4.041   1.00 52.19  ? 87  GLU A CA  1 
ATOM   684  C  C   . GLU A 1 107 ? -0.560  3.282   5.396   1.00 54.20  ? 87  GLU A C   1 
ATOM   685  O  O   . GLU A 1 107 ? 0.584   2.832   5.558   1.00 51.70  ? 87  GLU A O   1 
ATOM   686  C  CB  . GLU A 1 107 ? -1.490  2.716   3.132   1.00 49.47  ? 87  GLU A CB  1 
ATOM   687  C  CG  . GLU A 1 107 ? -2.088  3.169   1.803   1.00 45.86  ? 87  GLU A CG  1 
ATOM   688  C  CD  . GLU A 1 107 ? -2.475  1.995   0.908   1.00 47.27  ? 87  GLU A CD  1 
ATOM   689  O  OE1 . GLU A 1 107 ? -2.254  0.833   1.312   1.00 49.44  ? 87  GLU A OE1 1 
ATOM   690  O  OE2 . GLU A 1 107 ? -2.995  2.229   -0.203  1.00 44.37  ? 87  GLU A OE2 1 
ATOM   691  N  N   . ASP A 1 115 ? 2.629   0.838   7.285   1.00 73.10  ? 95  ASP A N   1 
ATOM   692  C  CA  . ASP A 1 115 ? 3.780   1.403   6.591   1.00 83.08  ? 95  ASP A CA  1 
ATOM   693  C  C   . ASP A 1 115 ? 3.820   0.941   5.135   1.00 83.28  ? 95  ASP A C   1 
ATOM   694  O  O   . ASP A 1 115 ? 4.712   0.190   4.736   1.00 86.69  ? 95  ASP A O   1 
ATOM   695  C  CB  . ASP A 1 115 ? 5.076   1.018   7.312   1.00 93.51  ? 95  ASP A CB  1 
ATOM   696  C  CG  . ASP A 1 115 ? 6.296   1.739   6.759   1.00 103.91 ? 95  ASP A CG  1 
ATOM   697  O  OD1 . ASP A 1 115 ? 6.133   2.632   5.899   1.00 96.24  ? 95  ASP A OD1 1 
ATOM   698  O  OD2 . ASP A 1 115 ? 7.422   1.405   7.187   1.00 99.54  ? 95  ASP A OD2 1 
ATOM   699  N  N   . ASN A 1 116 ? 2.852   1.387   4.337   1.00 62.13  ? 96  ASN A N   1 
ATOM   700  C  CA  . ASN A 1 116 ? 2.815   1.075   2.908   1.00 58.08  ? 96  ASN A CA  1 
ATOM   701  C  C   . ASN A 1 116 ? 3.074   2.360   2.125   1.00 49.88  ? 96  ASN A C   1 
ATOM   702  O  O   . ASN A 1 116 ? 2.192   3.211   2.009   1.00 51.06  ? 96  ASN A O   1 
ATOM   703  C  CB  . ASN A 1 116 ? 1.480   0.448   2.517   1.00 59.64  ? 96  ASN A CB  1 
ATOM   704  C  CG  . ASN A 1 116 ? 1.462   -1.058  2.707   1.00 63.44  ? 96  ASN A CG  1 
ATOM   705  O  OD1 . ASN A 1 116 ? 2.399   -1.638  3.259   1.00 69.20  ? 96  ASN A OD1 1 
ATOM   706  N  ND2 . ASN A 1 116 ? 0.389   -1.700  2.251   1.00 66.55  ? 96  ASN A ND2 1 
ATOM   707  N  N   . LEU A 1 117 ? 4.279   2.493   1.583   1.00 41.34  ? 97  LEU A N   1 
ATOM   708  C  CA  . LEU A 1 117 ? 4.608   3.619   0.716   1.00 41.11  ? 97  LEU A CA  1 
ATOM   709  C  C   . LEU A 1 117 ? 4.161   3.334   -0.712  1.00 30.95  ? 97  LEU A C   1 
ATOM   710  O  O   . LEU A 1 117 ? 4.463   2.272   -1.264  1.00 30.27  ? 97  LEU A O   1 
ATOM   711  C  CB  . LEU A 1 117 ? 6.109   3.886   0.747   1.00 35.89  ? 97  LEU A CB  1 
ATOM   712  C  CG  . LEU A 1 117 ? 6.580   5.121   -0.009  1.00 37.44  ? 97  LEU A CG  1 
ATOM   713  C  CD1 . LEU A 1 117 ? 6.188   6.376   0.756   1.00 38.41  ? 97  LEU A CD1 1 
ATOM   714  C  CD2 . LEU A 1 117 ? 8.085   5.058   -0.216  1.00 40.59  ? 97  LEU A CD2 1 
ATOM   715  N  N   . LYS A 1 118 ? 3.456   4.279   -1.323  1.00 25.15  ? 98  LYS A N   1 
ATOM   716  C  CA  . LYS A 1 118 ? 2.880   4.013   -2.634  1.00 26.04  ? 98  LYS A CA  1 
ATOM   717  C  C   . LYS A 1 118 ? 2.994   5.233   -3.529  1.00 34.07  ? 98  LYS A C   1 
ATOM   718  O  O   . LYS A 1 118 ? 2.803   6.366   -3.091  1.00 30.35  ? 98  LYS A O   1 
ATOM   719  C  CB  . LYS A 1 118 ? 1.406   3.583   -2.534  1.00 33.47  ? 98  LYS A CB  1 
ATOM   720  C  CG  . LYS A 1 118 ? 0.487   4.633   -1.962  1.00 32.83  ? 98  LYS A CG  1 
ATOM   721  C  CD  . LYS A 1 118 ? -0.977  4.216   -2.046  1.00 44.22  ? 98  LYS A CD  1 
ATOM   722  C  CE  . LYS A 1 118 ? -1.877  5.326   -1.540  1.00 41.89  ? 98  LYS A CE  1 
ATOM   723  N  NZ  . LYS A 1 118 ? -3.279  4.857   -1.416  1.00 42.94  ? 98  LYS A NZ  1 
ATOM   724  N  N   . GLY A 1 119 ? 3.325   4.994   -4.795  1.00 23.76  ? 99  GLY A N   1 
ATOM   725  C  CA  . GLY A 1 119 ? 3.293   6.029   -5.801  1.00 26.24  ? 99  GLY A CA  1 
ATOM   726  C  C   . GLY A 1 119 ? 1.988   5.911   -6.566  1.00 22.28  ? 99  GLY A C   1 
ATOM   727  O  O   . GLY A 1 119 ? 1.585   4.820   -6.958  1.00 22.67  ? 99  GLY A O   1 
ATOM   728  N  N   . SER A 1 120 ? 1.318   7.038   -6.730  1.00 19.65  ? 100 SER A N   1 
ATOM   729  C  CA  . SER A 1 120 ? 0.073   7.095   -7.473  1.00 16.72  ? 100 SER A CA  1 
ATOM   730  C  C   . SER A 1 120 ? 0.298   7.920   -8.723  1.00 17.07  ? 100 SER A C   1 
ATOM   731  O  O   . SER A 1 120 ? 0.944   8.973   -8.668  1.00 21.84  ? 100 SER A O   1 
ATOM   732  C  CB  . SER A 1 120 ? -1.056  7.741   -6.653  1.00 25.72  ? 100 SER A CB  1 
ATOM   733  O  OG  . SER A 1 120 ? -1.272  7.080   -5.414  1.00 28.75  ? 100 SER A OG  1 
ATOM   734  N  N   . TYR A 1 121 ? -0.229  7.442   -9.844  1.00 17.44  ? 101 TYR A N   1 
ATOM   735  C  CA  . TYR A 1 121 ? -0.246  8.221   -11.075 1.00 18.06  ? 101 TYR A CA  1 
ATOM   736  C  C   . TYR A 1 121 ? -1.689  8.305   -11.537 1.00 16.06  ? 101 TYR A C   1 
ATOM   737  O  O   . TYR A 1 121 ? -2.307  7.276   -11.821 1.00 17.53  ? 101 TYR A O   1 
ATOM   738  C  CB  . TYR A 1 121 ? 0.632   7.607   -12.166 1.00 19.09  ? 101 TYR A CB  1 
ATOM   739  C  CG  . TYR A 1 121 ? 0.610   8.491   -13.380 1.00 16.88  ? 101 TYR A CG  1 
ATOM   740  C  CD1 . TYR A 1 121 ? 1.427   9.619   -13.452 1.00 19.53  ? 101 TYR A CD1 1 
ATOM   741  C  CD2 . TYR A 1 121 ? -0.260  8.235   -14.430 1.00 16.60  ? 101 TYR A CD2 1 
ATOM   742  C  CE1 . TYR A 1 121 ? 1.377   10.453  -14.545 1.00 21.05  ? 101 TYR A CE1 1 
ATOM   743  C  CE2 . TYR A 1 121 ? -0.315  9.066   -15.523 1.00 20.09  ? 101 TYR A CE2 1 
ATOM   744  C  CZ  . TYR A 1 121 ? 0.505   10.175  -15.575 1.00 23.14  ? 101 TYR A CZ  1 
ATOM   745  O  OH  . TYR A 1 121 ? 0.449   10.998  -16.673 1.00 25.82  ? 101 TYR A OH  1 
ATOM   746  N  N   . TYR A 1 122 ? -2.223  9.520   -11.592 1.00 16.29  ? 102 TYR A N   1 
ATOM   747  C  CA  . TYR A 1 122 ? -3.606  9.747   -11.980 1.00 18.57  ? 102 TYR A CA  1 
ATOM   748  C  C   . TYR A 1 122 ? -3.669  10.430  -13.332 1.00 17.05  ? 102 TYR A C   1 
ATOM   749  O  O   . TYR A 1 122 ? -2.891  11.349  -13.614 1.00 18.00  ? 102 TYR A O   1 
ATOM   750  C  CB  . TYR A 1 122 ? -4.334  10.631  -10.974 1.00 18.69  ? 102 TYR A CB  1 
ATOM   751  C  CG  . TYR A 1 122 ? -4.681  9.994   -9.658  1.00 19.78  ? 102 TYR A CG  1 
ATOM   752  C  CD1 . TYR A 1 122 ? -5.890  9.337   -9.478  1.00 25.21  ? 102 TYR A CD1 1 
ATOM   753  C  CD2 . TYR A 1 122 ? -3.827  10.107  -8.575  1.00 23.19  ? 102 TYR A CD2 1 
ATOM   754  C  CE1 . TYR A 1 122 ? -6.222  8.782   -8.257  1.00 24.87  ? 102 TYR A CE1 1 
ATOM   755  C  CE2 . TYR A 1 122 ? -4.146  9.553   -7.358  1.00 24.80  ? 102 TYR A CE2 1 
ATOM   756  C  CZ  . TYR A 1 122 ? -5.343  8.894   -7.207  1.00 21.99  ? 102 TYR A CZ  1 
ATOM   757  O  OH  . TYR A 1 122 ? -5.657  8.364   -5.976  1.00 29.02  ? 102 TYR A OH  1 
ATOM   758  N  N   . ALA A 1 123 ? -4.641  10.024  -14.139 1.00 16.62  ? 103 ALA A N   1 
ATOM   759  C  CA  . ALA A 1 123 ? -4.929  10.752  -15.367 1.00 15.83  ? 103 ALA A CA  1 
ATOM   760  C  C   . ALA A 1 123 ? -6.428  10.762  -15.595 1.00 18.38  ? 103 ALA A C   1 
ATOM   761  O  O   . ALA A 1 123 ? -7.083  9.737   -15.428 1.00 18.84  ? 103 ALA A O   1 
ATOM   762  C  CB  . ALA A 1 123 ? -4.228  10.118  -16.575 1.00 17.14  ? 103 ALA A CB  1 
ATOM   763  N  N   . ASN A 1 124 ? -6.963  11.908  -16.001 1.00 18.97  ? 104 ASN A N   1 
ATOM   764  C  CA  . ASN A 1 124 ? -8.350  11.872  -16.434 1.00 22.35  ? 104 ASN A CA  1 
ATOM   765  C  C   . ASN A 1 124 ? -8.429  11.189  -17.791 1.00 18.39  ? 104 ASN A C   1 
ATOM   766  O  O   . ASN A 1 124 ? -7.449  11.124  -18.542 1.00 18.07  ? 104 ASN A O   1 
ATOM   767  C  CB  . ASN A 1 124 ? -8.955  13.278  -16.486 1.00 25.08  ? 104 ASN A CB  1 
ATOM   768  C  CG  . ASN A 1 124 ? -8.433  14.115  -17.649 1.00 23.53  ? 104 ASN A CG  1 
ATOM   769  O  OD1 . ASN A 1 124 ? -8.802  13.895  -18.802 1.00 21.35  ? 104 ASN A OD1 1 
ATOM   770  N  ND2 . ASN A 1 124 ? -7.618  15.116  -17.340 1.00 24.08  ? 104 ASN A ND2 1 
ATOM   771  N  N   . CYS A 1 125 ? -9.612  10.646  -18.097 1.00 18.24  ? 105 CYS A N   1 
ATOM   772  C  CA  . CYS A 1 125 ? -9.808  9.915   -19.338 1.00 16.53  ? 105 CYS A CA  1 
ATOM   773  C  C   . CYS A 1 125 ? -10.704 10.673  -20.310 1.00 18.57  ? 105 CYS A C   1 
ATOM   774  O  O   . CYS A 1 125 ? -11.481 10.067  -21.058 1.00 18.62  ? 105 CYS A O   1 
ATOM   775  C  CB  . CYS A 1 125 ? -10.381 8.527   -19.058 1.00 17.23  ? 105 CYS A CB  1 
ATOM   776  S  SG  . CYS A 1 125 ? -9.238  7.491   -18.093 1.00 19.60  ? 105 CYS A SG  1 
ATOM   777  N  N   . ALA A 1 126 ? -10.592 12.004  -20.338 1.00 17.03  ? 106 ALA A N   1 
ATOM   778  C  CA  . ALA A 1 126 ? -11.363 12.761  -21.319 1.00 17.68  ? 106 ALA A CA  1 
ATOM   779  C  C   . ALA A 1 126 ? -10.988 12.359  -22.736 1.00 18.33  ? 106 ALA A C   1 
ATOM   780  O  O   . ALA A 1 126 ? -11.810 12.471  -23.650 1.00 18.31  ? 106 ALA A O   1 
ATOM   781  C  CB  . ALA A 1 126 ? -11.155 14.268  -21.119 1.00 20.32  ? 106 ALA A CB  1 
ATOM   782  N  N   . PHE A 1 127 ? -9.756  11.871  -22.930 1.00 17.86  ? 107 PHE A N   1 
ATOM   783  C  CA  . PHE A 1 127 ? -9.306  11.422  -24.238 1.00 17.98  ? 107 PHE A CA  1 
ATOM   784  C  C   . PHE A 1 127 ? -10.158 10.294  -24.781 1.00 17.76  ? 107 PHE A C   1 
ATOM   785  O  O   . PHE A 1 127 ? -10.145 10.057  -25.995 1.00 21.16  ? 107 PHE A O   1 
ATOM   786  C  CB  . PHE A 1 127 ? -7.833  10.968  -24.166 1.00 20.12  ? 107 PHE A CB  1 
ATOM   787  C  CG  . PHE A 1 127 ? -7.589  9.813   -23.195 1.00 20.37  ? 107 PHE A CG  1 
ATOM   788  C  CD1 . PHE A 1 127 ? -7.846  8.505   -23.567 1.00 23.45  ? 107 PHE A CD1 1 
ATOM   789  C  CD2 . PHE A 1 127 ? -7.098  10.052  -21.920 1.00 23.29  ? 107 PHE A CD2 1 
ATOM   790  C  CE1 . PHE A 1 127 ? -7.636  7.454   -22.680 1.00 20.65  ? 107 PHE A CE1 1 
ATOM   791  C  CE2 . PHE A 1 127 ? -6.860  9.014   -21.035 1.00 22.90  ? 107 PHE A CE2 1 
ATOM   792  C  CZ  . PHE A 1 127 ? -7.150  7.708   -21.409 1.00 21.64  ? 107 PHE A CZ  1 
ATOM   793  N  N   . TYR A 1 128 ? -10.884 9.591   -23.907 1.00 20.30  ? 108 TYR A N   1 
ATOM   794  C  CA  . TYR A 1 128 ? -11.822 8.571   -24.369 1.00 19.39  ? 108 TYR A CA  1 
ATOM   795  C  C   . TYR A 1 128 ? -12.919 9.187   -25.220 1.00 21.64  ? 108 TYR A C   1 
ATOM   796  O  O   . TYR A 1 128 ? -13.337 8.606   -26.233 1.00 23.79  ? 108 TYR A O   1 
ATOM   797  C  CB  . TYR A 1 128 ? -12.424 7.846   -23.170 1.00 17.17  ? 108 TYR A CB  1 
ATOM   798  C  CG  . TYR A 1 128 ? -13.380 6.760   -23.589 1.00 17.29  ? 108 TYR A CG  1 
ATOM   799  C  CD1 . TYR A 1 128 ? -12.911 5.511   -23.951 1.00 18.89  ? 108 TYR A CD1 1 
ATOM   800  C  CD2 . TYR A 1 128 ? -14.748 6.997   -23.645 1.00 18.14  ? 108 TYR A CD2 1 
ATOM   801  C  CE1 . TYR A 1 128 ? -13.784 4.504   -24.349 1.00 19.14  ? 108 TYR A CE1 1 
ATOM   802  C  CE2 . TYR A 1 128 ? -15.627 6.006   -24.044 1.00 21.06  ? 108 TYR A CE2 1 
ATOM   803  C  CZ  . TYR A 1 128 ? -15.139 4.766   -24.397 1.00 19.96  ? 108 TYR A CZ  1 
ATOM   804  O  OH  . TYR A 1 128 ? -16.007 3.766   -24.798 1.00 22.18  ? 108 TYR A OH  1 
ATOM   805  N  N   . VAL A 1 129 ? -13.417 10.358  -24.808 1.00 19.45  ? 109 VAL A N   1 
ATOM   806  C  CA  . VAL A 1 129 ? -14.503 11.016  -25.519 1.00 19.54  ? 109 VAL A CA  1 
ATOM   807  C  C   . VAL A 1 129 ? -13.988 11.675  -26.787 1.00 22.66  ? 109 VAL A C   1 
ATOM   808  O  O   . VAL A 1 129 ? -14.627 11.607  -27.842 1.00 26.24  ? 109 VAL A O   1 
ATOM   809  C  CB  . VAL A 1 129 ? -15.199 12.027  -24.592 1.00 23.85  ? 109 VAL A CB  1 
ATOM   810  C  CG1 . VAL A 1 129 ? -16.273 12.799  -25.343 1.00 26.79  ? 109 VAL A CG1 1 
ATOM   811  C  CG2 . VAL A 1 129 ? -15.803 11.295  -23.400 1.00 23.96  ? 109 VAL A CG2 1 
ATOM   812  N  N   . ASP A 1 130 ? -12.830 12.318  -26.705 1.00 23.57  ? 110 ASP A N   1 
ATOM   813  C  CA  . ASP A 1 130 ? -12.242 13.057  -27.813 1.00 26.09  ? 110 ASP A CA  1 
ATOM   814  C  C   . ASP A 1 130 ? -10.739 13.011  -27.601 1.00 23.45  ? 110 ASP A C   1 
ATOM   815  O  O   . ASP A 1 130 ? -10.260 13.495  -26.572 1.00 22.11  ? 110 ASP A O   1 
ATOM   816  C  CB  . ASP A 1 130 ? -12.770 14.499  -27.831 1.00 28.13  ? 110 ASP A CB  1 
ATOM   817  C  CG  . ASP A 1 130 ? -12.171 15.361  -28.942 1.00 36.79  ? 110 ASP A CG  1 
ATOM   818  O  OD1 . ASP A 1 130 ? -11.141 15.008  -29.566 1.00 32.20  ? 110 ASP A OD1 1 
ATOM   819  O  OD2 . ASP A 1 130 ? -12.753 16.436  -29.190 1.00 46.67  ? 110 ASP A OD2 1 
ATOM   820  N  N   . PRO A 1 131 ? -9.973  12.418  -28.523 1.00 26.13  ? 111 PRO A N   1 
ATOM   821  C  CA  . PRO A 1 131 ? -8.520  12.304  -28.317 1.00 28.85  ? 111 PRO A CA  1 
ATOM   822  C  C   . PRO A 1 131 ? -7.819  13.642  -28.140 1.00 24.31  ? 111 PRO A C   1 
ATOM   823  O  O   . PRO A 1 131 ? -6.669  13.648  -27.689 1.00 29.09  ? 111 PRO A O   1 
ATOM   824  C  CB  . PRO A 1 131 ? -8.036  11.600  -29.594 1.00 33.86  ? 111 PRO A CB  1 
ATOM   825  C  CG  . PRO A 1 131 ? -9.225  10.860  -30.085 1.00 42.40  ? 111 PRO A CG  1 
ATOM   826  C  CD  . PRO A 1 131 ? -10.413 11.723  -29.744 1.00 34.33  ? 111 PRO A CD  1 
ATOM   827  N  N   . SER A 1 132 ? -8.473  14.764  -28.461 1.00 27.33  ? 112 SER A N   1 
ATOM   828  C  CA  A SER A 1 132 ? -7.839  16.069  -28.323 0.39 24.07  ? 112 SER A CA  1 
ATOM   829  C  CA  B SER A 1 132 ? -7.841  16.072  -28.324 0.61 23.98  ? 112 SER A CA  1 
ATOM   830  C  C   . SER A 1 132 ? -7.943  16.640  -26.915 1.00 30.56  ? 112 SER A C   1 
ATOM   831  O  O   . SER A 1 132 ? -7.301  17.656  -26.629 1.00 29.40  ? 112 SER A O   1 
ATOM   832  C  CB  A SER A 1 132 ? -8.448  17.068  -29.309 0.39 26.81  ? 112 SER A CB  1 
ATOM   833  C  CB  B SER A 1 132 ? -8.451  17.082  -29.302 0.61 26.80  ? 112 SER A CB  1 
ATOM   834  O  OG  A SER A 1 132 ? -9.751  17.453  -28.898 0.39 27.81  ? 112 SER A OG  1 
ATOM   835  O  OG  B SER A 1 132 ? -8.343  16.653  -30.646 0.61 25.64  ? 112 SER A OG  1 
ATOM   836  N  N   . LEU A 1 133 ? -8.721  16.024  -26.031 1.00 24.41  ? 113 LEU A N   1 
ATOM   837  C  CA  . LEU A 1 133 ? -8.968  16.599  -24.717 1.00 26.97  ? 113 LEU A CA  1 
ATOM   838  C  C   . LEU A 1 133 ? -7.904  16.168  -23.718 1.00 27.60  ? 113 LEU A C   1 
ATOM   839  O  O   . LEU A 1 133 ? -7.642  14.973  -23.553 1.00 29.06  ? 113 LEU A O   1 
ATOM   840  C  CB  . LEU A 1 133 ? -10.347 16.196  -24.206 1.00 24.79  ? 113 LEU A CB  1 
ATOM   841  C  CG  . LEU A 1 133 ? -11.536 16.676  -25.038 1.00 24.58  ? 113 LEU A CG  1 
ATOM   842  C  CD1 . LEU A 1 133 ? -12.835 16.241  -24.381 1.00 31.45  ? 113 LEU A CD1 1 
ATOM   843  C  CD2 . LEU A 1 133 ? -11.481 18.199  -25.203 1.00 33.11  ? 113 LEU A CD2 1 
ATOM   844  N  N   . SER A 1 134 ? -7.313  17.150  -23.043 1.00 29.18  ? 114 SER A N   1 
ATOM   845  C  CA  . SER A 1 134 ? -6.423  16.920  -21.913 1.00 27.90  ? 114 SER A CA  1 
ATOM   846  C  C   . SER A 1 134 ? -7.166  16.877  -20.587 1.00 24.76  ? 114 SER A C   1 
ATOM   847  O  O   . SER A 1 134 ? -6.555  16.542  -19.564 1.00 24.73  ? 114 SER A O   1 
ATOM   848  C  CB  . SER A 1 134 ? -5.356  18.020  -21.848 1.00 34.89  ? 114 SER A CB  1 
ATOM   849  O  OG  . SER A 1 134 ? -5.946  19.260  -21.479 1.00 34.74  ? 114 SER A OG  1 
ATOM   850  N  N   . CYS A 1 135 ? -8.455  17.240  -20.586 1.00 25.40  ? 115 CYS A N   1 
ATOM   851  C  CA  . CYS A 1 135 ? -9.279  17.317  -19.384 1.00 28.62  ? 115 CYS A CA  1 
ATOM   852  C  C   . CYS A 1 135 ? -10.717 17.659  -19.760 1.00 30.14  ? 115 CYS A C   1 
ATOM   853  O  O   . CYS A 1 135 ? -11.005 17.843  -20.943 1.00 29.14  ? 115 CYS A O   1 
ATOM   854  C  CB  . CYS A 1 135 ? -8.714  18.367  -18.426 1.00 28.87  ? 115 CYS A CB  1 
ATOM   855  S  SG  . CYS A 1 135 ? -8.519  20.001  -19.176 1.00 31.64  ? 115 CYS A SG  1 
ATOM   856  N  N   . ALA A 1 136 ? -11.618 17.735  -18.782 1.00 27.62  ? 116 ALA A N   1 
ATOM   857  C  CA  . ALA A 1 136 ? -12.989 18.145  -19.049 1.00 31.11  ? 116 ALA A CA  1 
ATOM   858  C  C   . ALA A 1 136 ? -13.054 19.624  -19.417 1.00 47.00  ? 116 ALA A C   1 
ATOM   859  O  O   . ALA A 1 136 ? -12.063 20.358  -19.375 1.00 50.99  ? 116 ALA A O   1 
ATOM   860  C  CB  . ALA A 1 136 ? -13.878 17.891  -17.833 1.00 36.05  ? 116 ALA A CB  1 
ATOM   861  N  N   . LYS A 1 137 ? -14.256 20.061  -19.772 1.00 45.73  ? 117 LYS A N   1 
ATOM   862  C  CA  . LYS A 1 137 ? -14.478 21.467  -20.054 1.00 47.06  ? 117 LYS A CA  1 
ATOM   863  C  C   . LYS A 1 137 ? -15.339 22.092  -18.960 1.00 61.64  ? 117 LYS A C   1 
ATOM   864  O  O   . LYS A 1 137 ? -16.302 21.470  -18.494 1.00 60.45  ? 117 LYS A O   1 
ATOM   865  C  CB  . LYS A 1 137 ? -15.155 21.642  -21.414 1.00 41.02  ? 117 LYS A CB  1 
ATOM   866  C  CG  . LYS A 1 137 ? -14.557 20.759  -22.496 1.00 54.35  ? 117 LYS A CG  1 
ATOM   867  C  CD  . LYS A 1 137 ? -15.506 20.601  -23.668 1.00 43.00  ? 117 LYS A CD  1 
ATOM   868  C  CE  . LYS A 1 137 ? -15.028 19.527  -24.635 1.00 50.49  ? 117 LYS A CE  1 
ATOM   869  N  NZ  . LYS A 1 137 ? -15.947 19.397  -25.807 1.00 52.00  ? 117 LYS A NZ  1 
ATOM   870  N  N   . PRO A 1 138 ? -15.006 23.302  -18.523 1.00 67.70  ? 118 PRO A N   1 
ATOM   871  C  CA  . PRO A 1 138 ? -15.692 23.893  -17.368 1.00 75.71  ? 118 PRO A CA  1 
ATOM   872  C  C   . PRO A 1 138 ? -17.144 24.239  -17.663 1.00 71.67  ? 118 PRO A C   1 
ATOM   873  O  O   . PRO A 1 138 ? -17.609 24.254  -18.804 1.00 69.71  ? 118 PRO A O   1 
ATOM   874  C  CB  . PRO A 1 138 ? -14.873 25.154  -17.075 1.00 65.00  ? 118 PRO A CB  1 
ATOM   875  C  CG  . PRO A 1 138 ? -13.543 24.877  -17.662 1.00 68.54  ? 118 PRO A CG  1 
ATOM   876  C  CD  . PRO A 1 138 ? -13.807 24.066  -18.895 1.00 67.28  ? 118 PRO A CD  1 
ATOM   877  N  N   . THR A 1 139 ? -17.862 24.524  -16.577 1.00 78.37  ? 119 THR A N   1 
ATOM   878  C  CA  . THR A 1 139 ? -19.254 24.942  -16.607 1.00 83.74  ? 119 THR A CA  1 
ATOM   879  C  C   . THR A 1 139 ? -19.403 26.109  -15.637 1.00 90.47  ? 119 THR A C   1 
ATOM   880  O  O   . THR A 1 139 ? -18.465 26.454  -14.912 1.00 89.62  ? 119 THR A O   1 
ATOM   881  C  CB  . THR A 1 139 ? -20.186 23.776  -16.250 1.00 80.07  ? 119 THR A CB  1 
ATOM   882  O  OG1 . THR A 1 139 ? -19.699 22.580  -16.872 1.00 85.25  ? 119 THR A OG1 1 
ATOM   883  C  CG2 . THR A 1 139 ? -21.609 24.037  -16.738 1.00 83.48  ? 119 THR A CG2 1 
ATOM   884  N  N   . GLU A 1 140 ? -20.590 26.727  -15.634 1.00 95.60  ? 120 GLU A N   1 
ATOM   885  C  CA  . GLU A 1 140 ? -20.809 27.928  -14.829 1.00 99.01  ? 120 GLU A CA  1 
ATOM   886  C  C   . GLU A 1 140 ? -20.444 27.705  -13.368 1.00 101.82 ? 120 GLU A C   1 
ATOM   887  O  O   . GLU A 1 140 ? -19.786 28.549  -12.748 1.00 99.91  ? 120 GLU A O   1 
ATOM   888  C  CB  . GLU A 1 140 ? -22.265 28.385  -14.940 1.00 106.36 ? 120 GLU A CB  1 
ATOM   889  C  CG  . GLU A 1 140 ? -22.601 29.558  -14.024 1.00 95.83  ? 120 GLU A CG  1 
ATOM   890  C  CD  . GLU A 1 140 ? -24.090 29.793  -13.883 1.00 101.23 ? 120 GLU A CD  1 
ATOM   891  O  OE1 . GLU A 1 140 ? -24.861 29.271  -14.715 1.00 111.77 ? 120 GLU A OE1 1 
ATOM   892  O  OE2 . GLU A 1 140 ? -24.488 30.497  -12.932 1.00 100.20 ? 120 GLU A OE2 1 
ATOM   893  N  N   . GLU A 1 141 ? -20.859 26.576  -12.800 1.00 93.24  ? 121 GLU A N   1 
ATOM   894  C  CA  . GLU A 1 141 ? -20.549 26.260  -11.414 1.00 94.23  ? 121 GLU A CA  1 
ATOM   895  C  C   . GLU A 1 141 ? -19.277 25.441  -11.257 1.00 79.99  ? 121 GLU A C   1 
ATOM   896  O  O   . GLU A 1 141 ? -18.762 25.336  -10.139 1.00 72.16  ? 121 GLU A O   1 
ATOM   897  C  CB  . GLU A 1 141 ? -21.720 25.512  -10.769 1.00 87.59  ? 121 GLU A CB  1 
ATOM   898  C  CG  . GLU A 1 141 ? -22.923 26.390  -10.479 1.00 99.54  ? 121 GLU A CG  1 
ATOM   899  C  CD  . GLU A 1 141 ? -24.217 25.610  -10.475 1.00 100.44 ? 121 GLU A CD  1 
ATOM   900  O  OE1 . GLU A 1 141 ? -24.333 24.655  -11.273 1.00 95.22  ? 121 GLU A OE1 1 
ATOM   901  O  OE2 . GLU A 1 141 ? -25.114 25.948  -9.675  1.00 105.53 ? 121 GLU A OE2 1 
ATOM   902  N  N   . PHE A 1 142 ? -18.751 24.878  -12.343 1.00 74.70  ? 122 PHE A N   1 
ATOM   903  C  CA  . PHE A 1 142 ? -17.621 23.950  -12.299 1.00 69.82  ? 122 PHE A CA  1 
ATOM   904  C  C   . PHE A 1 142 ? -16.463 24.529  -13.105 1.00 66.87  ? 122 PHE A C   1 
ATOM   905  O  O   . PHE A 1 142 ? -16.287 24.207  -14.279 1.00 65.75  ? 122 PHE A O   1 
ATOM   906  C  CB  . PHE A 1 142 ? -18.045 22.579  -12.832 1.00 59.78  ? 122 PHE A CB  1 
ATOM   907  C  CG  . PHE A 1 142 ? -19.317 22.062  -12.230 1.00 50.17  ? 122 PHE A CG  1 
ATOM   908  C  CD1 . PHE A 1 142 ? -19.385 21.765  -10.880 1.00 49.80  ? 122 PHE A CD1 1 
ATOM   909  C  CD2 . PHE A 1 142 ? -20.441 21.862  -13.013 1.00 48.98  ? 122 PHE A CD2 1 
ATOM   910  C  CE1 . PHE A 1 142 ? -20.552 21.282  -10.313 1.00 50.21  ? 122 PHE A CE1 1 
ATOM   911  C  CE2 . PHE A 1 142 ? -21.613 21.382  -12.456 1.00 54.41  ? 122 PHE A CE2 1 
ATOM   912  C  CZ  . PHE A 1 142 ? -21.669 21.089  -11.102 1.00 49.43  ? 122 PHE A CZ  1 
ATOM   913  N  N   . ASN A 1 143 ? -15.674 25.386  -12.472 1.00 73.36  ? 123 ASN A N   1 
ATOM   914  C  CA  . ASN A 1 143 ? -14.454 25.866  -13.100 1.00 71.38  ? 123 ASN A CA  1 
ATOM   915  C  C   . ASN A 1 143 ? -13.253 25.110  -12.552 1.00 67.24  ? 123 ASN A C   1 
ATOM   916  O  O   . ASN A 1 143 ? -13.318 24.517  -11.473 1.00 66.71  ? 123 ASN A O   1 
ATOM   917  C  CB  . ASN A 1 143 ? -14.290 27.377  -12.880 1.00 70.22  ? 123 ASN A CB  1 
ATOM   918  C  CG  . ASN A 1 143 ? -14.483 27.788  -11.435 1.00 70.49  ? 123 ASN A CG  1 
ATOM   919  O  OD1 . ASN A 1 143 ? -13.525 27.871  -10.666 1.00 66.73  ? 123 ASN A OD1 1 
ATOM   920  N  ND2 . ASN A 1 143 ? -15.728 28.063  -11.061 1.00 62.49  ? 123 ASN A ND2 1 
ATOM   921  N  N   . PRO A 1 144 ? -12.134 25.072  -13.283 1.00 71.50  ? 124 PRO A N   1 
ATOM   922  C  CA  . PRO A 1 144 ? -10.987 24.275  -12.821 1.00 64.72  ? 124 PRO A CA  1 
ATOM   923  C  C   . PRO A 1 144 ? -10.341 24.797  -11.549 1.00 69.03  ? 124 PRO A C   1 
ATOM   924  O  O   . PRO A 1 144 ? -9.373  24.190  -11.075 1.00 58.34  ? 124 PRO A O   1 
ATOM   925  C  CB  . PRO A 1 144 ? -10.008 24.349  -14.004 1.00 75.28  ? 124 PRO A CB  1 
ATOM   926  C  CG  . PRO A 1 144 ? -10.843 24.757  -15.175 1.00 79.44  ? 124 PRO A CG  1 
ATOM   927  C  CD  . PRO A 1 144 ? -11.890 25.658  -14.610 1.00 77.03  ? 124 PRO A CD  1 
ATOM   928  N  N   . ASP A 1 145 ? -10.834 25.896  -10.980 1.00 58.50  ? 125 ASP A N   1 
ATOM   929  C  CA  . ASP A 1 145 ? -10.276 26.422  -9.743  1.00 57.20  ? 125 ASP A CA  1 
ATOM   930  C  C   . ASP A 1 145 ? -11.009 25.919  -8.506  1.00 50.77  ? 125 ASP A C   1 
ATOM   931  O  O   . ASP A 1 145 ? -10.400 25.834  -7.433  1.00 58.31  ? 125 ASP A O   1 
ATOM   932  C  CB  . ASP A 1 145 ? -10.285 27.953  -9.770  1.00 64.85  ? 125 ASP A CB  1 
ATOM   933  C  CG  . ASP A 1 145 ? -9.353  28.519  -10.827 1.00 67.42  ? 125 ASP A CG  1 
ATOM   934  O  OD1 . ASP A 1 145 ? -8.308  27.888  -11.096 1.00 73.21  ? 125 ASP A OD1 1 
ATOM   935  O  OD2 . ASP A 1 145 ? -9.664  29.589  -11.389 1.00 61.98  ? 125 ASP A OD2 1 
ATOM   936  N  N   . ASN A 1 146 ? -12.296 25.580  -8.619  1.00 53.00  ? 126 ASN A N   1 
ATOM   937  C  CA  . ASN A 1 146 ? -13.005 24.958  -7.507  1.00 51.19  ? 126 ASN A CA  1 
ATOM   938  C  C   . ASN A 1 146 ? -13.214 23.460  -7.696  1.00 55.64  ? 126 ASN A C   1 
ATOM   939  O  O   . ASN A 1 146 ? -13.588 22.777  -6.736  1.00 53.62  ? 126 ASN A O   1 
ATOM   940  C  CB  . ASN A 1 146 ? -14.354 25.656  -7.258  1.00 58.79  ? 126 ASN A CB  1 
ATOM   941  C  CG  . ASN A 1 146 ? -15.282 25.598  -8.452  1.00 67.17  ? 126 ASN A CG  1 
ATOM   942  O  OD1 . ASN A 1 146 ? -14.853 25.341  -9.570  1.00 66.01  ? 126 ASN A OD1 1 
ATOM   943  N  ND2 . ASN A 1 146 ? -16.567 25.853  -8.217  1.00 72.96  ? 126 ASN A ND2 1 
ATOM   944  N  N   . PHE A 1 147 ? -12.955 22.924  -8.893  1.00 43.55  ? 127 PHE A N   1 
ATOM   945  C  CA  . PHE A 1 147 ? -12.894 21.474  -9.094  1.00 35.32  ? 127 PHE A CA  1 
ATOM   946  C  C   . PHE A 1 147 ? -11.593 21.067  -9.789  1.00 40.72  ? 127 PHE A C   1 
ATOM   947  O  O   . PHE A 1 147 ? -11.608 20.355  -10.793 1.00 35.43  ? 127 PHE A O   1 
ATOM   948  C  CB  . PHE A 1 147 ? -14.106 20.986  -9.883  1.00 40.42  ? 127 PHE A CB  1 
ATOM   949  C  CG  . PHE A 1 147 ? -15.384 20.983  -9.089  1.00 37.45  ? 127 PHE A CG  1 
ATOM   950  C  CD1 . PHE A 1 147 ? -15.750 19.875  -8.347  1.00 40.21  ? 127 PHE A CD1 1 
ATOM   951  C  CD2 . PHE A 1 147 ? -16.212 22.093  -9.079  1.00 47.51  ? 127 PHE A CD2 1 
ATOM   952  C  CE1 . PHE A 1 147 ? -16.919 19.869  -7.613  1.00 48.86  ? 127 PHE A CE1 1 
ATOM   953  C  CE2 . PHE A 1 147 ? -17.383 22.093  -8.343  1.00 47.83  ? 127 PHE A CE2 1 
ATOM   954  C  CZ  . PHE A 1 147 ? -17.739 20.976  -7.614  1.00 47.37  ? 127 PHE A CZ  1 
ATOM   955  N  N   . PRO A 1 148 ? -10.436 21.480  -9.255  1.00 40.54  ? 128 PRO A N   1 
ATOM   956  C  CA  . PRO A 1 148 ? -9.174  21.109  -9.917  1.00 39.38  ? 128 PRO A CA  1 
ATOM   957  C  C   . PRO A 1 148 ? -8.904  19.616  -9.891  1.00 35.80  ? 128 PRO A C   1 
ATOM   958  O  O   . PRO A 1 148 ? -8.189  19.111  -10.763 1.00 43.93  ? 128 PRO A O   1 
ATOM   959  C  CB  . PRO A 1 148 ? -8.120  21.893  -9.123  1.00 44.57  ? 128 PRO A CB  1 
ATOM   960  C  CG  . PRO A 1 148 ? -8.705  22.013  -7.758  1.00 36.71  ? 128 PRO A CG  1 
ATOM   961  C  CD  . PRO A 1 148 ? -10.197 22.130  -7.951  1.00 43.78  ? 128 PRO A CD  1 
ATOM   962  N  N   . GLU A 1 149 ? -9.469  18.886  -8.930  1.00 38.34  ? 129 GLU A N   1 
ATOM   963  C  CA  . GLU A 1 149 ? -9.210  17.457  -8.837  1.00 36.35  ? 129 GLU A CA  1 
ATOM   964  C  C   . GLU A 1 149 ? -9.927  16.663  -9.918  1.00 43.96  ? 129 GLU A C   1 
ATOM   965  O  O   . GLU A 1 149 ? -9.610  15.484  -10.118 1.00 36.98  ? 129 GLU A O   1 
ATOM   966  C  CB  . GLU A 1 149 ? -9.625  16.934  -7.463  1.00 42.11  ? 129 GLU A CB  1 
ATOM   967  C  CG  . GLU A 1 149 ? -11.126 16.803  -7.265  1.00 46.53  ? 129 GLU A CG  1 
ATOM   968  C  CD  . GLU A 1 149 ? -11.783 18.104  -6.835  1.00 48.64  ? 129 GLU A CD  1 
ATOM   969  O  OE1 . GLU A 1 149 ? -11.127 19.168  -6.903  1.00 46.37  ? 129 GLU A OE1 1 
ATOM   970  O  OE2 . GLU A 1 149 ? -12.962 18.058  -6.422  1.00 58.61  ? 129 GLU A OE2 1 
ATOM   971  N  N   . TYR A 1 150 ? -10.903 17.267  -10.597 1.00 34.46  ? 130 TYR A N   1 
ATOM   972  C  CA  . TYR A 1 150 ? -11.572 16.627  -11.719 1.00 34.20  ? 130 TYR A CA  1 
ATOM   973  C  C   . TYR A 1 150 ? -11.199 17.220  -13.063 1.00 27.78  ? 130 TYR A C   1 
ATOM   974  O  O   . TYR A 1 150 ? -11.230 16.502  -14.066 1.00 34.17  ? 130 TYR A O   1 
ATOM   975  C  CB  . TYR A 1 150 ? -13.100 16.709  -11.565 1.00 28.28  ? 130 TYR A CB  1 
ATOM   976  C  CG  . TYR A 1 150 ? -13.647 15.926  -10.396 1.00 28.36  ? 130 TYR A CG  1 
ATOM   977  C  CD1 . TYR A 1 150 ? -13.782 14.544  -10.463 1.00 28.57  ? 130 TYR A CD1 1 
ATOM   978  C  CD2 . TYR A 1 150 ? -14.033 16.569  -9.226  1.00 38.91  ? 130 TYR A CD2 1 
ATOM   979  C  CE1 . TYR A 1 150 ? -14.283 13.819  -9.392  1.00 29.10  ? 130 TYR A CE1 1 
ATOM   980  C  CE2 . TYR A 1 150 ? -14.537 15.856  -8.152  1.00 38.79  ? 130 TYR A CE2 1 
ATOM   981  C  CZ  . TYR A 1 150 ? -14.660 14.482  -8.241  1.00 36.57  ? 130 TYR A CZ  1 
ATOM   982  O  OH  . TYR A 1 150 ? -15.160 13.773  -7.173  1.00 43.45  ? 130 TYR A OH  1 
ATOM   983  N  N   . LEU A 1 151 ? -10.840 18.500  -13.103 1.00 27.32  ? 131 LEU A N   1 
ATOM   984  C  CA  . LEU A 1 151 ? -10.789 19.269  -14.340 1.00 33.61  ? 131 LEU A CA  1 
ATOM   985  C  C   . LEU A 1 151 ? -9.381  19.691  -14.742 1.00 32.92  ? 131 LEU A C   1 
ATOM   986  O  O   . LEU A 1 151 ? -9.225  20.401  -15.740 1.00 34.84  ? 131 LEU A O   1 
ATOM   987  C  CB  . LEU A 1 151 ? -11.669 20.520  -14.230 1.00 40.30  ? 131 LEU A CB  1 
ATOM   988  C  CG  . LEU A 1 151 ? -13.139 20.352  -13.835 1.00 38.85  ? 131 LEU A CG  1 
ATOM   989  C  CD1 . LEU A 1 151 ? -13.878 21.668  -14.025 1.00 44.11  ? 131 LEU A CD1 1 
ATOM   990  C  CD2 . LEU A 1 151 ? -13.803 19.250  -14.621 1.00 40.58  ? 131 LEU A CD2 1 
ATOM   991  N  N   . SER A 1 152 ? -8.353  19.265  -14.008 1.00 31.89  ? 132 SER A N   1 
ATOM   992  C  CA  . SER A 1 152 ? -6.999  19.697  -14.333 1.00 31.14  ? 132 SER A CA  1 
ATOM   993  C  C   . SER A 1 152 ? -6.427  18.879  -15.496 1.00 25.82  ? 132 SER A C   1 
ATOM   994  O  O   . SER A 1 152 ? -6.667  17.672  -15.586 1.00 26.51  ? 132 SER A O   1 
ATOM   995  C  CB  . SER A 1 152 ? -6.090  19.565  -13.120 1.00 36.68  ? 132 SER A CB  1 
ATOM   996  O  OG  . SER A 1 152 ? -6.551  20.379  -12.055 1.00 40.40  ? 132 SER A OG  1 
ATOM   997  N  N   . PRO A 1 153 ? -5.671  19.518  -16.391 1.00 27.28  ? 133 PRO A N   1 
ATOM   998  C  CA  . PRO A 1 153 ? -5.054  18.785  -17.508 1.00 26.28  ? 133 PRO A CA  1 
ATOM   999  C  C   . PRO A 1 153 ? -4.107  17.701  -17.017 1.00 26.30  ? 133 PRO A C   1 
ATOM   1000 O  O   . PRO A 1 153 ? -3.493  17.815  -15.955 1.00 24.80  ? 133 PRO A O   1 
ATOM   1001 C  CB  . PRO A 1 153 ? -4.288  19.876  -18.272 1.00 35.09  ? 133 PRO A CB  1 
ATOM   1002 C  CG  . PRO A 1 153 ? -4.949  21.162  -17.886 1.00 35.77  ? 133 PRO A CG  1 
ATOM   1003 C  CD  . PRO A 1 153 ? -5.452  20.972  -16.480 1.00 28.44  ? 133 PRO A CD  1 
ATOM   1004 N  N   . ASN A 1 154 ? -3.994  16.640  -17.813 1.00 20.32  ? 134 ASN A N   1 
ATOM   1005 C  CA  . ASN A 1 154 ? -3.092  15.546  -17.488 1.00 19.43  ? 134 ASN A CA  1 
ATOM   1006 C  C   . ASN A 1 154 ? -1.636  15.999  -17.571 1.00 24.63  ? 134 ASN A C   1 
ATOM   1007 O  O   . ASN A 1 154 ? -1.285  16.889  -18.345 1.00 26.43  ? 134 ASN A O   1 
ATOM   1008 C  CB  . ASN A 1 154 ? -3.323  14.371  -18.429 1.00 21.10  ? 134 ASN A CB  1 
ATOM   1009 C  CG  . ASN A 1 154 ? -4.553  13.576  -18.063 1.00 21.44  ? 134 ASN A CG  1 
ATOM   1010 O  OD1 . ASN A 1 154 ? -4.933  13.529  -16.900 1.00 20.63  ? 134 ASN A OD1 1 
ATOM   1011 N  ND2 . ASN A 1 154 ? -5.172  12.943  -19.050 1.00 21.23  ? 134 ASN A ND2 1 
ATOM   1012 N  N   . LEU A 1 155 ? -0.795  15.379  -16.750 1.00 22.78  ? 135 LEU A N   1 
ATOM   1013 C  CA  . LEU A 1 155 ? 0.637   15.650  -16.693 1.00 30.21  ? 135 LEU A CA  1 
ATOM   1014 C  C   . LEU A 1 155 ? 1.335   14.337  -17.035 1.00 28.98  ? 135 LEU A C   1 
ATOM   1015 O  O   . LEU A 1 155 ? 1.433   13.434  -16.197 1.00 28.52  ? 135 LEU A O   1 
ATOM   1016 C  CB  . LEU A 1 155 ? 1.026   16.183  -15.318 1.00 28.25  ? 135 LEU A CB  1 
ATOM   1017 C  CG  . LEU A 1 155 ? 2.471   16.562  -15.010 1.00 36.25  ? 135 LEU A CG  1 
ATOM   1018 C  CD1 . LEU A 1 155 ? 3.104   17.361  -16.146 1.00 45.19  ? 135 LEU A CD1 1 
ATOM   1019 C  CD2 . LEU A 1 155 ? 2.487   17.366  -13.719 1.00 39.74  ? 135 LEU A CD2 1 
ATOM   1020 N  N   . TRP A 1 156 ? 1.778   14.221  -18.280 1.00 23.09  ? 136 TRP A N   1 
ATOM   1021 C  CA  . TRP A 1 156 ? 2.358   12.998  -18.823 1.00 23.78  ? 136 TRP A CA  1 
ATOM   1022 C  C   . TRP A 1 156 ? 3.874   13.016  -18.686 1.00 25.96  ? 136 TRP A C   1 
ATOM   1023 O  O   . TRP A 1 156 ? 4.497   14.068  -18.851 1.00 28.46  ? 136 TRP A O   1 
ATOM   1024 C  CB  . TRP A 1 156 ? 2.012   12.844  -20.298 1.00 25.70  ? 136 TRP A CB  1 
ATOM   1025 C  CG  . TRP A 1 156 ? 0.571   12.652  -20.548 1.00 24.32  ? 136 TRP A CG  1 
ATOM   1026 C  CD1 . TRP A 1 156 ? -0.308  13.575  -21.033 1.00 28.52  ? 136 TRP A CD1 1 
ATOM   1027 C  CD2 . TRP A 1 156 ? -0.178  11.454  -20.333 1.00 23.42  ? 136 TRP A CD2 1 
ATOM   1028 N  NE1 . TRP A 1 156 ? -1.561  13.026  -21.135 1.00 26.01  ? 136 TRP A NE1 1 
ATOM   1029 C  CE2 . TRP A 1 156 ? -1.511  11.724  -20.706 1.00 25.48  ? 136 TRP A CE2 1 
ATOM   1030 C  CE3 . TRP A 1 156 ? 0.148   10.182  -19.856 1.00 22.96  ? 136 TRP A CE3 1 
ATOM   1031 C  CZ2 . TRP A 1 156 ? -2.520  10.763  -20.618 1.00 23.84  ? 136 TRP A CZ2 1 
ATOM   1032 C  CZ3 . TRP A 1 156 ? -0.847  9.232   -19.771 1.00 23.65  ? 136 TRP A CZ3 1 
ATOM   1033 C  CH2 . TRP A 1 156 ? -2.169  9.526   -20.154 1.00 23.39  ? 136 TRP A CH2 1 
ATOM   1034 N  N   . PRO A 1 157 ? 4.483   11.864  -18.411 1.00 21.93  ? 137 PRO A N   1 
ATOM   1035 C  CA  . PRO A 1 157 ? 5.948   11.788  -18.429 1.00 28.00  ? 137 PRO A CA  1 
ATOM   1036 C  C   . PRO A 1 157 ? 6.477   12.085  -19.821 1.00 29.82  ? 137 PRO A C   1 
ATOM   1037 O  O   . PRO A 1 157 ? 5.782   11.907  -20.825 1.00 28.29  ? 137 PRO A O   1 
ATOM   1038 C  CB  . PRO A 1 157 ? 6.241   10.337  -18.025 1.00 29.77  ? 137 PRO A CB  1 
ATOM   1039 C  CG  . PRO A 1 157 ? 4.941   9.797   -17.494 1.00 26.60  ? 137 PRO A CG  1 
ATOM   1040 C  CD  . PRO A 1 157 ? 3.857   10.551  -18.174 1.00 21.99  ? 137 PRO A CD  1 
ATOM   1041 N  N   . GLN A 1 158 ? 7.711   12.570  -19.871 1.00 28.96  ? 138 GLN A N   1 
ATOM   1042 C  CA  . GLN A 1 158 ? 8.376   12.776  -21.150 1.00 29.96  ? 138 GLN A CA  1 
ATOM   1043 C  C   . GLN A 1 158 ? 8.386   11.493  -21.957 1.00 30.95  ? 138 GLN A C   1 
ATOM   1044 O  O   . GLN A 1 158 ? 8.638   10.414  -21.422 1.00 33.87  ? 138 GLN A O   1 
ATOM   1045 C  CB  . GLN A 1 158 ? 9.817   13.224  -20.939 1.00 37.70  ? 138 GLN A CB  1 
ATOM   1046 C  CG  . GLN A 1 158 ? 10.001  14.689  -20.842 1.00 36.00  ? 138 GLN A CG  1 
ATOM   1047 C  CD  . GLN A 1 158 ? 11.465  15.040  -20.765 1.00 34.97  ? 138 GLN A CD  1 
ATOM   1048 O  OE1 . GLN A 1 158 ? 11.934  15.928  -21.460 1.00 35.75  ? 138 GLN A OE1 1 
ATOM   1049 N  NE2 . GLN A 1 158 ? 12.205  14.317  -19.929 1.00 41.63  ? 138 GLN A NE2 1 
ATOM   1050 N  N   . GLU A 1 159 ? 8.147   11.621  -23.263 1.00 35.96  ? 139 GLU A N   1 
ATOM   1051 C  CA  . GLU A 1 159 ? 8.165   10.441  -24.119 1.00 38.35  ? 139 GLU A CA  1 
ATOM   1052 C  C   . GLU A 1 159 ? 9.537   9.782   -24.117 1.00 44.67  ? 139 GLU A C   1 
ATOM   1053 O  O   . GLU A 1 159 ? 9.641   8.551   -24.136 1.00 44.93  ? 139 GLU A O   1 
ATOM   1054 C  CB  . GLU A 1 159 ? 7.745   10.809  -25.543 1.00 43.34  ? 139 GLU A CB  1 
ATOM   1055 C  CG  . GLU A 1 159 ? 7.650   9.616   -26.482 1.00 50.26  ? 139 GLU A CG  1 
ATOM   1056 C  CD  . GLU A 1 159 ? 6.670   8.555   -25.992 1.00 51.78  ? 139 GLU A CD  1 
ATOM   1057 O  OE1 . GLU A 1 159 ? 5.644   8.916   -25.373 1.00 58.39  ? 139 GLU A OE1 1 
ATOM   1058 O  OE2 . GLU A 1 159 ? 6.925   7.355   -26.224 1.00 49.85  ? 139 GLU A OE2 1 
ATOM   1059 N  N   . SER A 1 160 ? 10.607  10.582  -24.076 1.00 33.00  ? 140 SER A N   1 
ATOM   1060 C  CA  . SER A 1 160 ? 11.941  9.998   -24.036 1.00 41.07  ? 140 SER A CA  1 
ATOM   1061 C  C   . SER A 1 160 ? 12.244  9.330   -22.699 1.00 40.56  ? 140 SER A C   1 
ATOM   1062 O  O   . SER A 1 160 ? 13.085  8.428   -22.651 1.00 40.19  ? 140 SER A O   1 
ATOM   1063 C  CB  . SER A 1 160 ? 12.996  11.064  -24.344 1.00 38.95  ? 140 SER A CB  1 
ATOM   1064 O  OG  . SER A 1 160 ? 12.906  12.151  -23.441 1.00 41.62  ? 140 SER A OG  1 
ATOM   1065 N  N   . THR A 1 161 ? 11.574  9.741   -21.622 1.00 38.55  ? 141 THR A N   1 
ATOM   1066 C  CA  . THR A 1 161 ? 11.818  9.162   -20.303 1.00 36.29  ? 141 THR A CA  1 
ATOM   1067 C  C   . THR A 1 161 ? 11.131  7.806   -20.145 1.00 35.85  ? 141 THR A C   1 
ATOM   1068 O  O   . THR A 1 161 ? 11.725  6.855   -19.624 1.00 35.32  ? 141 THR A O   1 
ATOM   1069 C  CB  . THR A 1 161 ? 11.336  10.126  -19.215 1.00 38.79  ? 141 THR A CB  1 
ATOM   1070 O  OG1 . THR A 1 161 ? 12.017  11.380  -19.347 1.00 39.42  ? 141 THR A OG1 1 
ATOM   1071 C  CG2 . THR A 1 161 ? 11.592  9.545   -17.836 1.00 37.29  ? 141 THR A CG2 1 
ATOM   1072 N  N   . LEU A 1 162 ? 9.875   7.701   -20.567 1.00 33.55  ? 142 LEU A N   1 
ATOM   1073 C  CA  . LEU A 1 162 ? 9.129   6.444   -20.513 1.00 28.66  ? 142 LEU A CA  1 
ATOM   1074 C  C   . LEU A 1 162 ? 8.483   6.211   -21.868 1.00 33.82  ? 142 LEU A C   1 
ATOM   1075 O  O   . LEU A 1 162 ? 7.274   6.429   -22.037 1.00 32.45  ? 142 LEU A O   1 
ATOM   1076 C  CB  . LEU A 1 162 ? 8.068   6.459   -19.409 1.00 29.40  ? 142 LEU A CB  1 
ATOM   1077 C  CG  . LEU A 1 162 ? 8.468   6.288   -17.947 1.00 33.07  ? 142 LEU A CG  1 
ATOM   1078 C  CD1 . LEU A 1 162 ? 7.233   6.327   -17.073 1.00 28.04  ? 142 LEU A CD1 1 
ATOM   1079 C  CD2 . LEU A 1 162 ? 9.226   4.987   -17.739 1.00 39.63  ? 142 LEU A CD2 1 
ATOM   1080 N  N   . PRO A 1 163 ? 9.258   5.763   -22.858 1.00 32.16  ? 143 PRO A N   1 
ATOM   1081 C  CA  . PRO A 1 163 ? 8.705   5.610   -24.210 1.00 34.07  ? 143 PRO A CA  1 
ATOM   1082 C  C   . PRO A 1 163 ? 7.543   4.626   -24.228 1.00 32.26  ? 143 PRO A C   1 
ATOM   1083 O  O   . PRO A 1 163 ? 7.619   3.538   -23.657 1.00 28.94  ? 143 PRO A O   1 
ATOM   1084 C  CB  . PRO A 1 163 ? 9.898   5.104   -25.031 1.00 37.80  ? 143 PRO A CB  1 
ATOM   1085 C  CG  . PRO A 1 163 ? 10.913  4.629   -24.030 1.00 40.17  ? 143 PRO A CG  1 
ATOM   1086 C  CD  . PRO A 1 163 ? 10.696  5.438   -22.794 1.00 37.57  ? 143 PRO A CD  1 
ATOM   1087 N  N   . GLY A 1 164 ? 6.462   5.028   -24.891 1.00 28.66  ? 144 GLY A N   1 
ATOM   1088 C  CA  . GLY A 1 164 ? 5.259   4.221   -25.011 1.00 26.14  ? 144 GLY A CA  1 
ATOM   1089 C  C   . GLY A 1 164 ? 4.320   4.272   -23.829 1.00 26.10  ? 144 GLY A C   1 
ATOM   1090 O  O   . GLY A 1 164 ? 3.272   3.609   -23.864 1.00 25.85  ? 144 GLY A O   1 
ATOM   1091 N  N   . PHE A 1 165 ? 4.640   5.046   -22.788 1.00 25.70  ? 145 PHE A N   1 
ATOM   1092 C  CA  . PHE A 1 165 ? 3.771   5.090   -21.611 1.00 22.02  ? 145 PHE A CA  1 
ATOM   1093 C  C   . PHE A 1 165 ? 2.389   5.620   -21.959 1.00 22.02  ? 145 PHE A C   1 
ATOM   1094 O  O   . PHE A 1 165 ? 1.368   5.000   -21.624 1.00 20.29  ? 145 PHE A O   1 
ATOM   1095 C  CB  . PHE A 1 165 ? 4.405   5.952   -20.513 1.00 23.86  ? 145 PHE A CB  1 
ATOM   1096 C  CG  . PHE A 1 165 ? 3.541   6.099   -19.278 1.00 23.96  ? 145 PHE A CG  1 
ATOM   1097 C  CD1 . PHE A 1 165 ? 3.444   5.071   -18.363 1.00 33.50  ? 145 PHE A CD1 1 
ATOM   1098 C  CD2 . PHE A 1 165 ? 2.848   7.268   -19.028 1.00 24.49  ? 145 PHE A CD2 1 
ATOM   1099 C  CE1 . PHE A 1 165 ? 2.653   5.192   -17.233 1.00 26.89  ? 145 PHE A CE1 1 
ATOM   1100 C  CE2 . PHE A 1 165 ? 2.047   7.392   -17.897 1.00 20.85  ? 145 PHE A CE2 1 
ATOM   1101 C  CZ  . PHE A 1 165 ? 1.967   6.356   -16.992 1.00 25.01  ? 145 PHE A CZ  1 
ATOM   1102 N  N   . LYS A 1 166 ? 2.333   6.780   -22.601 1.00 22.81  ? 146 LYS A N   1 
ATOM   1103 C  CA  . LYS A 1 166 ? 1.049   7.433   -22.844 1.00 22.26  ? 146 LYS A CA  1 
ATOM   1104 C  C   . LYS A 1 166 ? 0.155   6.626   -23.775 1.00 22.34  ? 146 LYS A C   1 
ATOM   1105 O  O   . LYS A 1 166 ? -1.028  6.433   -23.438 1.00 20.81  ? 146 LYS A O   1 
ATOM   1106 C  CB  . LYS A 1 166 ? 1.290   8.861   -23.358 1.00 24.62  ? 146 LYS A CB  1 
ATOM   1107 C  CG  . LYS A 1 166 ? 0.016   9.642   -23.641 1.00 25.17  ? 146 LYS A CG  1 
ATOM   1108 C  CD  . LYS A 1 166 ? 0.338   11.099  -23.947 1.00 28.65  ? 146 LYS A CD  1 
ATOM   1109 C  CE  . LYS A 1 166 ? -0.928  11.870  -24.254 1.00 33.26  ? 146 LYS A CE  1 
ATOM   1110 N  NZ  . LYS A 1 166 ? -1.473  11.528  -25.599 1.00 39.64  ? 146 LYS A NZ  1 
ATOM   1111 N  N   . PRO A 1 167 ? 0.627   6.116   -24.921 1.00 23.39  ? 147 PRO A N   1 
ATOM   1112 C  CA  . PRO A 1 167 ? -0.269  5.290   -25.752 1.00 23.79  ? 147 PRO A CA  1 
ATOM   1113 C  C   . PRO A 1 167 ? -0.704  3.999   -25.082 1.00 23.17  ? 147 PRO A C   1 
ATOM   1114 O  O   . PRO A 1 167 ? -1.849  3.576   -25.274 1.00 20.88  ? 147 PRO A O   1 
ATOM   1115 C  CB  . PRO A 1 167 ? 0.560   5.025   -27.016 1.00 25.03  ? 147 PRO A CB  1 
ATOM   1116 C  CG  . PRO A 1 167 ? 1.974   5.315   -26.625 1.00 26.09  ? 147 PRO A CG  1 
ATOM   1117 C  CD  . PRO A 1 167 ? 1.902   6.398   -25.610 1.00 24.88  ? 147 PRO A CD  1 
ATOM   1118 N  N   . THR A 1 168 ? 0.167   3.357   -24.298 1.00 22.20  ? 148 THR A N   1 
ATOM   1119 C  CA  . THR A 1 168 ? -0.245  2.160   -23.564 1.00 19.85  ? 148 THR A CA  1 
ATOM   1120 C  C   . THR A 1 168 ? -1.333  2.491   -22.552 1.00 21.97  ? 148 THR A C   1 
ATOM   1121 O  O   . THR A 1 168 ? -2.342  1.780   -22.440 1.00 19.36  ? 148 THR A O   1 
ATOM   1122 C  CB  . THR A 1 168 ? 0.958   1.539   -22.852 1.00 19.59  ? 148 THR A CB  1 
ATOM   1123 O  OG1 . THR A 1 168 ? 1.992   1.270   -23.805 1.00 22.46  ? 148 THR A OG1 1 
ATOM   1124 C  CG2 . THR A 1 168 ? 0.545   0.230   -22.161 1.00 25.37  ? 148 THR A CG2 1 
ATOM   1125 N  N   . PHE A 1 169 ? -1.125  3.564   -21.791 1.00 17.33  ? 149 PHE A N   1 
ATOM   1126 C  CA  . PHE A 1 169 ? -2.100  4.016   -20.805 1.00 20.00  ? 149 PHE A CA  1 
ATOM   1127 C  C   . PHE A 1 169 ? -3.447  4.317   -21.461 1.00 18.73  ? 149 PHE A C   1 
ATOM   1128 O  O   . PHE A 1 169 ? -4.507  3.862   -20.997 1.00 18.80  ? 149 PHE A O   1 
ATOM   1129 C  CB  . PHE A 1 169 ? -1.529  5.257   -20.099 1.00 18.09  ? 149 PHE A CB  1 
ATOM   1130 C  CG  . PHE A 1 169 ? -2.255  5.637   -18.830 1.00 17.06  ? 149 PHE A CG  1 
ATOM   1131 C  CD1 . PHE A 1 169 ? -3.507  6.244   -18.886 1.00 17.62  ? 149 PHE A CD1 1 
ATOM   1132 C  CD2 . PHE A 1 169 ? -1.671  5.427   -17.593 1.00 20.91  ? 149 PHE A CD2 1 
ATOM   1133 C  CE1 . PHE A 1 169 ? -4.170  6.605   -17.724 1.00 19.36  ? 149 PHE A CE1 1 
ATOM   1134 C  CE2 . PHE A 1 169 ? -2.340  5.788   -16.423 1.00 19.77  ? 149 PHE A CE2 1 
ATOM   1135 C  CZ  . PHE A 1 169 ? -3.595  6.376   -16.500 1.00 17.16  ? 149 PHE A CZ  1 
ATOM   1136 N  N   . GLU A 1 170 ? -3.420  5.108   -22.538 1.00 21.02  ? 150 GLU A N   1 
ATOM   1137 C  CA  . GLU A 1 170 ? -4.648  5.450   -23.244 1.00 18.56  ? 150 GLU A CA  1 
ATOM   1138 C  C   . GLU A 1 170 ? -5.332  4.208   -23.795 1.00 20.49  ? 150 GLU A C   1 
ATOM   1139 O  O   . GLU A 1 170 ? -6.556  4.073   -23.692 1.00 17.41  ? 150 GLU A O   1 
ATOM   1140 C  CB  . GLU A 1 170 ? -4.343  6.419   -24.383 1.00 20.69  ? 150 GLU A CB  1 
ATOM   1141 C  CG  . GLU A 1 170 ? -3.979  7.798   -23.907 1.00 24.96  ? 150 GLU A CG  1 
ATOM   1142 C  CD  . GLU A 1 170 ? -3.539  8.687   -25.046 1.00 34.65  ? 150 GLU A CD  1 
ATOM   1143 O  OE1 . GLU A 1 170 ? -3.051  8.142   -26.059 1.00 43.09  ? 150 GLU A OE1 1 
ATOM   1144 O  OE2 . GLU A 1 170 ? -3.685  9.923   -24.928 1.00 43.21  ? 150 GLU A OE2 1 
ATOM   1145 N  N   . ASP A 1 171 ? -4.565  3.295   -24.397 1.00 17.24  ? 151 ASP A N   1 
ATOM   1146 C  CA  . ASP A 1 171 ? -5.181  2.131   -25.028 1.00 19.73  ? 151 ASP A CA  1 
ATOM   1147 C  C   . ASP A 1 171 ? -5.816  1.213   -23.999 1.00 21.19  ? 151 ASP A C   1 
ATOM   1148 O  O   . ASP A 1 171 ? -6.926  0.693   -24.218 1.00 18.31  ? 151 ASP A O   1 
ATOM   1149 C  CB  . ASP A 1 171 ? -4.147  1.373   -25.851 1.00 21.20  ? 151 ASP A CB  1 
ATOM   1150 C  CG  . ASP A 1 171 ? -3.801  2.077   -27.142 1.00 30.52  ? 151 ASP A CG  1 
ATOM   1151 O  OD1 . ASP A 1 171 ? -4.496  3.055   -27.499 1.00 36.49  ? 151 ASP A OD1 1 
ATOM   1152 O  OD2 . ASP A 1 171 ? -2.833  1.649   -27.799 1.00 37.47  ? 151 ASP A OD2 1 
ATOM   1153 N  N   . LEU A 1 172 ? -5.141  0.997   -22.865 1.00 17.59  ? 152 LEU A N   1 
ATOM   1154 C  CA  . LEU A 1 172 ? -5.730  0.131   -21.849 1.00 16.88  ? 152 LEU A CA  1 
ATOM   1155 C  C   . LEU A 1 172 ? -6.954  0.784   -21.221 1.00 17.04  ? 152 LEU A C   1 
ATOM   1156 O  O   . LEU A 1 172 ? -7.971  0.115   -21.002 1.00 16.30  ? 152 LEU A O   1 
ATOM   1157 C  CB  . LEU A 1 172 ? -4.701  -0.237  -20.775 1.00 18.23  ? 152 LEU A CB  1 
ATOM   1158 C  CG  . LEU A 1 172 ? -5.247  -1.218  -19.721 1.00 19.32  ? 152 LEU A CG  1 
ATOM   1159 C  CD1 . LEU A 1 172 ? -5.963  -2.413  -20.359 1.00 19.60  ? 152 LEU A CD1 1 
ATOM   1160 C  CD2 . LEU A 1 172 ? -4.110  -1.710  -18.842 1.00 21.18  ? 152 LEU A CD2 1 
ATOM   1161 N  N   . CYS A 1 173 ? -6.884  2.089   -20.933 1.00 16.59  ? 153 CYS A N   1 
ATOM   1162 C  CA  . CYS A 1 173 ? -8.056  2.760   -20.383 1.00 16.53  ? 153 CYS A CA  1 
ATOM   1163 C  C   . CYS A 1 173 ? -9.206  2.723   -21.363 1.00 16.02  ? 153 CYS A C   1 
ATOM   1164 O  O   . CYS A 1 173 ? -10.357 2.557   -20.957 1.00 16.75  ? 153 CYS A O   1 
ATOM   1165 C  CB  . CYS A 1 173 ? -7.726  4.209   -20.016 1.00 17.84  ? 153 CYS A CB  1 
ATOM   1166 S  SG  . CYS A 1 173 ? -6.714  4.300   -18.534 1.00 20.47  ? 153 CYS A SG  1 
ATOM   1167 N  N   . ARG A 1 174 ? -8.922  2.907   -22.652 1.00 15.78  ? 154 ARG A N   1 
ATOM   1168 C  CA  A ARG A 1 174 ? -9.991  2.879   -23.644 0.61 20.23  ? 154 ARG A CA  1 
ATOM   1169 C  CA  B ARG A 1 174 ? -9.978  2.874   -23.658 0.39 20.24  ? 154 ARG A CA  1 
ATOM   1170 C  C   . ARG A 1 174 ? -10.660 1.515   -23.677 1.00 19.79  ? 154 ARG A C   1 
ATOM   1171 O  O   . ARG A 1 174 ? -11.891 1.426   -23.760 1.00 18.35  ? 154 ARG A O   1 
ATOM   1172 C  CB  A ARG A 1 174 ? -9.445  3.246   -25.026 0.61 21.18  ? 154 ARG A CB  1 
ATOM   1173 C  CB  B ARG A 1 174 ? -9.386  3.217   -25.028 0.39 21.17  ? 154 ARG A CB  1 
ATOM   1174 C  CG  A ARG A 1 174 ? -10.526 3.315   -26.099 0.61 26.11  ? 154 ARG A CG  1 
ATOM   1175 C  CG  B ARG A 1 174 ? -10.356 3.144   -26.193 0.39 26.32  ? 154 ARG A CG  1 
ATOM   1176 C  CD  A ARG A 1 174 ? -9.993  3.907   -27.393 0.61 30.47  ? 154 ARG A CD  1 
ATOM   1177 C  CD  B ARG A 1 174 ? -9.730  3.736   -27.456 0.39 30.25  ? 154 ARG A CD  1 
ATOM   1178 N  NE  A ARG A 1 174 ? -9.491  5.266   -27.216 0.61 29.04  ? 154 ARG A NE  1 
ATOM   1179 N  NE  B ARG A 1 174 ? -9.569  5.184   -27.357 0.39 29.04  ? 154 ARG A NE  1 
ATOM   1180 C  CZ  A ARG A 1 174 ? -10.255 6.353   -27.206 0.61 23.65  ? 154 ARG A CZ  1 
ATOM   1181 C  CZ  B ARG A 1 174 ? -8.411  5.821   -27.239 0.39 31.35  ? 154 ARG A CZ  1 
ATOM   1182 N  NH1 A ARG A 1 174 ? -11.579 6.273   -27.296 0.61 24.68  ? 154 ARG A NH1 1 
ATOM   1183 N  NH1 B ARG A 1 174 ? -7.256  5.171   -27.225 0.39 29.56  ? 154 ARG A NH1 1 
ATOM   1184 N  NH2 A ARG A 1 174 ? -9.680  7.548   -27.105 0.61 26.52  ? 154 ARG A NH2 1 
ATOM   1185 N  NH2 B ARG A 1 174 ? -8.410  7.147   -27.139 0.39 29.33  ? 154 ARG A NH2 1 
ATOM   1186 N  N   . LEU A 1 175 ? -9.869  0.443   -23.578 1.00 16.35  ? 155 LEU A N   1 
ATOM   1187 C  CA  . LEU A 1 175 ? -10.423 -0.909  -23.574 1.00 16.42  ? 155 LEU A CA  1 
ATOM   1188 C  C   . LEU A 1 175 ? -11.311 -1.122  -22.355 1.00 18.78  ? 155 LEU A C   1 
ATOM   1189 O  O   . LEU A 1 175 ? -12.447 -1.628  -22.459 1.00 17.21  ? 155 LEU A O   1 
ATOM   1190 C  CB  . LEU A 1 175 ? -9.266  -1.915  -23.608 1.00 17.48  ? 155 LEU A CB  1 
ATOM   1191 C  CG  . LEU A 1 175 ? -9.532  -3.412  -23.679 1.00 16.71  ? 155 LEU A CG  1 
ATOM   1192 C  CD1 . LEU A 1 175 ? -8.277  -4.141  -24.199 1.00 21.92  ? 155 LEU A CD1 1 
ATOM   1193 C  CD2 . LEU A 1 175 ? -9.907  -3.936  -22.302 1.00 19.13  ? 155 LEU A CD2 1 
ATOM   1194 N  N   . ILE A 1 176 ? -10.812 -0.718  -21.185 1.00 14.26  ? 156 ILE A N   1 
ATOM   1195 C  CA  . ILE A 1 176 ? -11.569 -0.919  -19.956 1.00 15.36  ? 156 ILE A CA  1 
ATOM   1196 C  C   . ILE A 1 176 ? -12.845 -0.083  -19.962 1.00 18.90  ? 156 ILE A C   1 
ATOM   1197 O  O   . ILE A 1 176 ? -13.907 -0.555  -19.529 1.00 15.15  ? 156 ILE A O   1 
ATOM   1198 C  CB  . ILE A 1 176 ? -10.684 -0.618  -18.736 1.00 14.83  ? 156 ILE A CB  1 
ATOM   1199 C  CG1 . ILE A 1 176 ? -9.590  -1.688  -18.619 1.00 17.20  ? 156 ILE A CG1 1 
ATOM   1200 C  CG2 . ILE A 1 176 ? -11.512 -0.568  -17.472 1.00 16.88  ? 156 ILE A CG2 1 
ATOM   1201 C  CD1 . ILE A 1 176 ? -8.526  -1.348  -17.553 1.00 19.30  ? 156 ILE A CD1 1 
ATOM   1202 N  N   . ILE A 1 177 ? -12.780 1.152   -20.468 1.00 15.22  ? 157 ILE A N   1 
ATOM   1203 C  CA  . ILE A 1 177 ? -13.985 1.983   -20.507 1.00 16.46  ? 157 ILE A CA  1 
ATOM   1204 C  C   . ILE A 1 177 ? -14.975 1.462   -21.539 1.00 17.43  ? 157 ILE A C   1 
ATOM   1205 O  O   . ILE A 1 177 ? -16.188 1.524   -21.322 1.00 16.20  ? 157 ILE A O   1 
ATOM   1206 C  CB  . ILE A 1 177 ? -13.624 3.459   -20.766 1.00 13.86  ? 157 ILE A CB  1 
ATOM   1207 C  CG1 . ILE A 1 177 ? -12.796 4.009   -19.609 1.00 16.29  ? 157 ILE A CG1 1 
ATOM   1208 C  CG2 . ILE A 1 177 ? -14.906 4.323   -20.925 1.00 15.79  ? 157 ILE A CG2 1 
ATOM   1209 C  CD1 . ILE A 1 177 ? -12.048 5.333   -19.973 1.00 16.81  ? 157 ILE A CD1 1 
ATOM   1210 N  N   . ASP A 1 178 ? -14.494 0.968   -22.686 1.00 16.41  ? 158 ASP A N   1 
ATOM   1211 C  CA  . ASP A 1 178 ? -15.404 0.313   -23.635 1.00 17.21  ? 158 ASP A CA  1 
ATOM   1212 C  C   . ASP A 1 178 ? -16.225 -0.768  -22.932 1.00 16.89  ? 158 ASP A C   1 
ATOM   1213 O  O   . ASP A 1 178 ? -17.458 -0.872  -23.100 1.00 18.77  ? 158 ASP A O   1 
ATOM   1214 C  CB  . ASP A 1 178 ? -14.617 -0.318  -24.793 1.00 21.35  ? 158 ASP A CB  1 
ATOM   1215 C  CG  . ASP A 1 178 ? -14.118 0.701   -25.832 1.00 25.84  ? 158 ASP A CG  1 
ATOM   1216 O  OD1 . ASP A 1 178 ? -14.526 1.879   -25.813 1.00 26.62  ? 158 ASP A OD1 1 
ATOM   1217 O  OD2 . ASP A 1 178 ? -13.310 0.300   -26.695 1.00 28.06  ? 158 ASP A OD2 1 
ATOM   1218 N  N   . VAL A 1 179 ? -15.548 -1.588  -22.127 1.00 16.78  ? 159 VAL A N   1 
ATOM   1219 C  CA  . VAL A 1 179 ? -16.289 -2.638  -21.431 1.00 16.96  ? 159 VAL A CA  1 
ATOM   1220 C  C   . VAL A 1 179 ? -17.228 -2.036  -20.385 1.00 18.08  ? 159 VAL A C   1 
ATOM   1221 O  O   . VAL A 1 179 ? -18.365 -2.500  -20.215 1.00 17.36  ? 159 VAL A O   1 
ATOM   1222 C  CB  . VAL A 1 179 ? -15.321 -3.657  -20.806 1.00 15.94  ? 159 VAL A CB  1 
ATOM   1223 C  CG1 . VAL A 1 179 ? -16.097 -4.740  -20.064 1.00 17.61  ? 159 VAL A CG1 1 
ATOM   1224 C  CG2 . VAL A 1 179 ? -14.436 -4.279  -21.899 1.00 18.85  ? 159 VAL A CG2 1 
ATOM   1225 N  N   . ALA A 1 180 ? -16.754 -1.028  -19.643 1.00 16.30  ? 160 ALA A N   1 
ATOM   1226 C  CA  . ALA A 1 180 ? -17.601 -0.351  -18.655 1.00 17.27  ? 160 ALA A CA  1 
ATOM   1227 C  C   . ALA A 1 180 ? -18.873 0.187   -19.291 1.00 16.05  ? 160 ALA A C   1 
ATOM   1228 O  O   . ALA A 1 180 ? -19.956 0.133   -18.683 1.00 15.65  ? 160 ALA A O   1 
ATOM   1229 C  CB  . ALA A 1 180 ? -16.822 0.794   -17.990 1.00 16.07  ? 160 ALA A CB  1 
ATOM   1230 N  N   . VAL A 1 181 ? -18.768 0.714   -20.510 1.00 17.28  ? 161 VAL A N   1 
ATOM   1231 C  CA  . VAL A 1 181 ? -19.948 1.235   -21.205 1.00 18.11  ? 161 VAL A CA  1 
ATOM   1232 C  C   . VAL A 1 181 ? -20.950 0.114   -21.452 1.00 17.89  ? 161 VAL A C   1 
ATOM   1233 O  O   . VAL A 1 181 ? -22.167 0.303   -21.296 1.00 17.20  ? 161 VAL A O   1 
ATOM   1234 C  CB  . VAL A 1 181 ? -19.538 1.930   -22.521 1.00 15.91  ? 161 VAL A CB  1 
ATOM   1235 C  CG1 . VAL A 1 181 ? -20.774 2.233   -23.403 1.00 18.94  ? 161 VAL A CG1 1 
ATOM   1236 C  CG2 . VAL A 1 181 ? -18.785 3.228   -22.240 1.00 17.44  ? 161 VAL A CG2 1 
ATOM   1237 N  N   . LEU A 1 182 ? -20.456 -1.075  -21.815 1.00 17.03  ? 162 LEU A N   1 
ATOM   1238 C  CA  . LEU A 1 182 ? -21.375 -2.203  -22.015 1.00 16.31  ? 162 LEU A CA  1 
ATOM   1239 C  C   . LEU A 1 182 ? -21.976 -2.708  -20.697 1.00 18.94  ? 162 LEU A C   1 
ATOM   1240 O  O   . LEU A 1 182 ? -23.138 -3.150  -20.650 1.00 17.35  ? 162 LEU A O   1 
ATOM   1241 C  CB  . LEU A 1 182 ? -20.659 -3.332  -22.744 1.00 19.41  ? 162 LEU A CB  1 
ATOM   1242 C  CG  . LEU A 1 182 ? -20.279 -2.910  -24.161 1.00 20.87  ? 162 LEU A CG  1 
ATOM   1243 C  CD1 . LEU A 1 182 ? -19.474 -4.001  -24.811 1.00 26.67  ? 162 LEU A CD1 1 
ATOM   1244 C  CD2 . LEU A 1 182 ? -21.531 -2.600  -24.982 1.00 22.24  ? 162 LEU A CD2 1 
ATOM   1245 N  N   . VAL A 1 183 ? -21.193 -2.680  -19.616 1.00 15.31  ? 163 VAL A N   1 
ATOM   1246 C  CA  . VAL A 1 183 ? -21.750 -3.016  -18.306 1.00 15.66  ? 163 VAL A CA  1 
ATOM   1247 C  C   . VAL A 1 183 ? -22.826 -2.006  -17.916 1.00 16.45  ? 163 VAL A C   1 
ATOM   1248 O  O   . VAL A 1 183 ? -23.882 -2.365  -17.383 1.00 16.89  ? 163 VAL A O   1 
ATOM   1249 C  CB  . VAL A 1 183 ? -20.637 -3.075  -17.249 1.00 15.01  ? 163 VAL A CB  1 
ATOM   1250 C  CG1 . VAL A 1 183 ? -21.230 -3.299  -15.881 1.00 17.74  ? 163 VAL A CG1 1 
ATOM   1251 C  CG2 . VAL A 1 183 ? -19.630 -4.204  -17.586 1.00 16.15  ? 163 VAL A CG2 1 
ATOM   1252 N  N   . ALA A 1 184 ? -22.555 -0.725  -18.158 1.00 17.74  ? 164 ALA A N   1 
ATOM   1253 C  CA  . ALA A 1 184 ? -23.526 0.325   -17.880 1.00 16.60  ? 164 ALA A CA  1 
ATOM   1254 C  C   . ALA A 1 184 ? -24.790 0.136   -18.703 1.00 18.43  ? 164 ALA A C   1 
ATOM   1255 O  O   . ALA A 1 184 ? -25.895 0.431   -18.236 1.00 16.01  ? 164 ALA A O   1 
ATOM   1256 C  CB  . ALA A 1 184 ? -22.891 1.692   -18.184 1.00 15.75  ? 164 ALA A CB  1 
ATOM   1257 N  N   . ARG A 1 185 ? -24.640 -0.304  -19.949 1.00 16.68  ? 165 ARG A N   1 
ATOM   1258 C  CA  . ARG A 1 185 ? -25.805 -0.594  -20.781 1.00 17.68  ? 165 ARG A CA  1 
ATOM   1259 C  C   . ARG A 1 185 ? -26.661 -1.694  -20.166 1.00 21.89  ? 165 ARG A C   1 
ATOM   1260 O  O   . ARG A 1 185 ? -27.897 -1.591  -20.152 1.00 18.80  ? 165 ARG A O   1 
ATOM   1261 C  CB  . ARG A 1 185 ? -25.356 -0.984  -22.191 1.00 19.89  ? 165 ARG A CB  1 
ATOM   1262 C  CG  . ARG A 1 185 ? -26.518 -1.376  -23.111 1.00 19.20  ? 165 ARG A CG  1 
ATOM   1263 C  CD  . ARG A 1 185 ? -26.013 -1.797  -24.482 1.00 23.83  ? 165 ARG A CD  1 
ATOM   1264 N  NE  . ARG A 1 185 ? -25.353 -0.691  -25.161 1.00 24.66  ? 165 ARG A NE  1 
ATOM   1265 C  CZ  . ARG A 1 185 ? -24.604 -0.823  -26.247 1.00 34.90  ? 165 ARG A CZ  1 
ATOM   1266 N  NH1 . ARG A 1 185 ? -24.413 -2.006  -26.816 1.00 31.32  ? 165 ARG A NH1 1 
ATOM   1267 N  NH2 . ARG A 1 185 ? -24.022 0.253   -26.769 1.00 30.34  ? 165 ARG A NH2 1 
ATOM   1268 N  N   . ALA A 1 186 ? -26.024 -2.750  -19.646 1.00 17.93  ? 166 ALA A N   1 
ATOM   1269 C  CA  . ALA A 1 186 ? -26.804 -3.798  -18.982 1.00 18.13  ? 166 ALA A CA  1 
ATOM   1270 C  C   . ALA A 1 186 ? -27.498 -3.249  -17.739 1.00 20.78  ? 166 ALA A C   1 
ATOM   1271 O  O   . ALA A 1 186 ? -28.665 -3.583  -17.452 1.00 19.43  ? 166 ALA A O   1 
ATOM   1272 C  CB  . ALA A 1 186 ? -25.902 -4.983  -18.620 1.00 18.52  ? 166 ALA A CB  1 
ATOM   1273 N  N   . CYS A 1 187 ? -26.790 -2.388  -16.990 1.00 17.69  ? 167 CYS A N   1 
ATOM   1274 C  CA  . CYS A 1 187 ? -27.419 -1.733  -15.845 1.00 19.74  ? 167 CYS A CA  1 
ATOM   1275 C  C   . CYS A 1 187 ? -28.640 -0.933  -16.277 1.00 20.62  ? 167 CYS A C   1 
ATOM   1276 O  O   . CYS A 1 187 ? -29.669 -0.931  -15.588 1.00 20.95  ? 167 CYS A O   1 
ATOM   1277 C  CB  . CYS A 1 187 ? -26.419 -0.823  -15.143 1.00 16.30  ? 167 CYS A CB  1 
ATOM   1278 S  SG  . CYS A 1 187 ? -25.096 -1.714  -14.308 1.00 20.72  ? 167 CYS A SG  1 
ATOM   1279 N  N   . ASP A 1 188 ? -28.529 -0.222  -17.402 1.00 18.97  ? 168 ASP A N   1 
ATOM   1280 C  CA  . ASP A 1 188 ? -29.658 0.540   -17.926 1.00 21.32  ? 168 ASP A CA  1 
ATOM   1281 C  C   . ASP A 1 188 ? -30.821 -0.369  -18.271 1.00 20.11  ? 168 ASP A C   1 
ATOM   1282 O  O   . ASP A 1 188 ? -31.983 -0.018  -18.044 1.00 19.81  ? 168 ASP A O   1 
ATOM   1283 C  CB  . ASP A 1 188 ? -29.258 1.308   -19.178 1.00 19.39  ? 168 ASP A CB  1 
ATOM   1284 C  CG  . ASP A 1 188 ? -28.459 2.552   -18.885 1.00 20.75  ? 168 ASP A CG  1 
ATOM   1285 O  OD1 . ASP A 1 188 ? -28.613 3.148   -17.791 1.00 23.10  ? 168 ASP A OD1 1 
ATOM   1286 O  OD2 . ASP A 1 188 ? -27.706 2.945   -19.793 1.00 21.20  ? 168 ASP A OD2 1 
ATOM   1287 N  N   . ARG A 1 189 ? -30.541 -1.515  -18.890 1.00 20.27  ? 169 ARG A N   1 
ATOM   1288 C  CA  . ARG A 1 189 ? -31.638 -2.424  -19.228 1.00 19.57  ? 169 ARG A CA  1 
ATOM   1289 C  C   . ARG A 1 189 ? -32.413 -2.813  -17.975 1.00 24.78  ? 169 ARG A C   1 
ATOM   1290 O  O   . ARG A 1 189 ? -33.658 -2.774  -17.941 1.00 24.20  ? 169 ARG A O   1 
ATOM   1291 C  CB  . ARG A 1 189 ? -31.093 -3.667  -19.924 1.00 25.08  ? 169 ARG A CB  1 
ATOM   1292 C  CG  . ARG A 1 189 ? -30.581 -3.444  -21.322 1.00 29.61  ? 169 ARG A CG  1 
ATOM   1293 C  CD  . ARG A 1 189 ? -29.981 -4.748  -21.844 1.00 41.63  ? 169 ARG A CD  1 
ATOM   1294 N  NE  . ARG A 1 189 ? -30.873 -5.891  -21.679 1.00 43.03  ? 169 ARG A NE  1 
ATOM   1295 C  CZ  . ARG A 1 189 ? -30.472 -7.152  -21.574 1.00 38.98  ? 169 ARG A CZ  1 
ATOM   1296 N  NH1 . ARG A 1 189 ? -29.185 -7.474  -21.568 1.00 36.00  ? 169 ARG A NH1 1 
ATOM   1297 N  NH2 . ARG A 1 189 ? -31.384 -8.115  -21.464 1.00 44.22  ? 169 ARG A NH2 1 
ATOM   1298 N  N   . PHE A 1 190 ? -31.675 -3.157  -16.920 1.00 22.44  ? 170 PHE A N   1 
ATOM   1299 C  CA  . PHE A 1 190 ? -32.307 -3.447  -15.637 1.00 23.25  ? 170 PHE A CA  1 
ATOM   1300 C  C   . PHE A 1 190 ? -33.120 -2.256  -15.138 1.00 24.47  ? 170 PHE A C   1 
ATOM   1301 O  O   . PHE A 1 190 ? -34.299 -2.392  -14.791 1.00 24.22  ? 170 PHE A O   1 
ATOM   1302 C  CB  . PHE A 1 190 ? -31.243 -3.825  -14.611 1.00 24.28  ? 170 PHE A CB  1 
ATOM   1303 C  CG  . PHE A 1 190 ? -31.787 -4.082  -13.240 1.00 27.72  ? 170 PHE A CG  1 
ATOM   1304 C  CD1 . PHE A 1 190 ? -32.242 -5.344  -12.892 1.00 29.86  ? 170 PHE A CD1 1 
ATOM   1305 C  CD2 . PHE A 1 190 ? -31.832 -3.072  -12.297 1.00 29.20  ? 170 PHE A CD2 1 
ATOM   1306 C  CE1 . PHE A 1 190 ? -32.749 -5.594  -11.630 1.00 34.97  ? 170 PHE A CE1 1 
ATOM   1307 C  CE2 . PHE A 1 190 ? -32.352 -3.318  -11.026 1.00 34.04  ? 170 PHE A CE2 1 
ATOM   1308 C  CZ  . PHE A 1 190 ? -32.801 -4.578  -10.699 1.00 34.07  ? 170 PHE A CZ  1 
ATOM   1309 N  N   . ALA A 1 191 ? -32.490 -1.082  -15.066 1.00 19.91  ? 171 ALA A N   1 
ATOM   1310 C  CA  . ALA A 1 191 ? -33.168 0.088   -14.517 1.00 22.13  ? 171 ALA A CA  1 
ATOM   1311 C  C   . ALA A 1 191 ? -34.398 0.454   -15.338 1.00 26.29  ? 171 ALA A C   1 
ATOM   1312 O  O   . ALA A 1 191 ? -35.418 0.883   -14.787 1.00 24.67  ? 171 ALA A O   1 
ATOM   1313 C  CB  . ALA A 1 191 ? -32.204 1.272   -14.451 1.00 20.08  ? 171 ALA A CB  1 
ATOM   1314 N  N   . GLU A 1 192 ? -34.321 0.301   -16.658 1.00 20.92  ? 172 GLU A N   1 
ATOM   1315 C  CA  . GLU A 1 192 ? -35.437 0.654   -17.528 1.00 24.49  ? 172 GLU A CA  1 
ATOM   1316 C  C   . GLU A 1 192 ? -36.620 -0.259  -17.294 1.00 26.80  ? 172 GLU A C   1 
ATOM   1317 O  O   . GLU A 1 192 ? -37.771 0.183   -17.414 1.00 27.49  ? 172 GLU A O   1 
ATOM   1318 C  CB  . GLU A 1 192 ? -35.007 0.580   -18.996 1.00 25.31  ? 172 GLU A CB  1 
ATOM   1319 C  CG  . GLU A 1 192 ? -34.100 1.730   -19.464 1.00 23.36  ? 172 GLU A CG  1 
ATOM   1320 C  CD  . GLU A 1 192 ? -33.338 1.387   -20.735 1.00 31.07  ? 172 GLU A CD  1 
ATOM   1321 O  OE1 . GLU A 1 192 ? -33.751 0.453   -21.462 1.00 31.19  ? 172 GLU A OE1 1 
ATOM   1322 O  OE2 . GLU A 1 192 ? -32.303 2.035   -20.996 1.00 24.03  ? 172 GLU A OE2 1 
ATOM   1323 N  N   . LYS A 1 193 ? -36.359 -1.528  -16.962 1.00 23.52  ? 173 LYS A N   1 
ATOM   1324 C  CA  . LYS A 1 193 ? -37.464 -2.427  -16.635 1.00 27.49  ? 173 LYS A CA  1 
ATOM   1325 C  C   . LYS A 1 193 ? -37.997 -2.235  -15.221 1.00 26.14  ? 173 LYS A C   1 
ATOM   1326 O  O   . LYS A 1 193 ? -39.165 -2.566  -14.969 1.00 28.60  ? 173 LYS A O   1 
ATOM   1327 C  CB  . LYS A 1 193 ? -37.038 -3.890  -16.798 1.00 30.32  ? 173 LYS A CB  1 
ATOM   1328 C  CG  . LYS A 1 193 ? -36.626 -4.271  -18.209 1.00 37.89  ? 173 LYS A CG  1 
ATOM   1329 C  CD  . LYS A 1 193 ? -36.199 -5.732  -18.281 1.00 52.35  ? 173 LYS A CD  1 
ATOM   1330 C  CE  . LYS A 1 193 ? -35.474 -6.041  -19.587 1.00 58.95  ? 173 LYS A CE  1 
ATOM   1331 N  NZ  . LYS A 1 193 ? -36.285 -5.700  -20.791 1.00 54.23  ? 173 LYS A NZ  1 
ATOM   1332 N  N   . GLN A 1 194 ? -37.183 -1.715  -14.295 1.00 27.58  ? 174 GLN A N   1 
ATOM   1333 C  CA  . GLN A 1 194 ? -37.518 -1.764  -12.874 1.00 26.76  ? 174 GLN A CA  1 
ATOM   1334 C  C   . GLN A 1 194 ? -37.866 -0.425  -12.231 1.00 30.12  ? 174 GLN A C   1 
ATOM   1335 O  O   . GLN A 1 194 ? -38.494 -0.428  -11.166 1.00 33.36  ? 174 GLN A O   1 
ATOM   1336 C  CB  . GLN A 1 194 ? -36.354 -2.384  -12.083 1.00 28.48  ? 174 GLN A CB  1 
ATOM   1337 C  CG  . GLN A 1 194 ? -36.018 -3.809  -12.488 1.00 34.49  ? 174 GLN A CG  1 
ATOM   1338 C  CD  . GLN A 1 194 ? -37.072 -4.806  -12.037 1.00 41.06  ? 174 GLN A CD  1 
ATOM   1339 O  OE1 . GLN A 1 194 ? -37.732 -4.607  -11.017 1.00 42.03  ? 174 GLN A OE1 1 
ATOM   1340 N  NE2 . GLN A 1 194 ? -37.240 -5.883  -12.801 1.00 35.89  ? 174 GLN A NE2 1 
ATOM   1341 N  N   . ILE A 1 195 ? -37.485 0.702   -12.833 1.00 26.62  ? 175 ILE A N   1 
ATOM   1342 C  CA  . ILE A 1 195 ? -37.585 2.021   -12.209 1.00 28.26  ? 175 ILE A CA  1 
ATOM   1343 C  C   . ILE A 1 195 ? -38.502 2.903   -13.053 1.00 29.52  ? 175 ILE A C   1 
ATOM   1344 O  O   . ILE A 1 195 ? -38.183 3.218   -14.206 1.00 28.59  ? 175 ILE A O   1 
ATOM   1345 C  CB  . ILE A 1 195 ? -36.198 2.671   -12.052 1.00 25.21  ? 175 ILE A CB  1 
ATOM   1346 C  CG1 . ILE A 1 195 ? -35.298 1.798   -11.176 1.00 27.21  ? 175 ILE A CG1 1 
ATOM   1347 C  CG2 . ILE A 1 195 ? -36.322 4.081   -11.480 1.00 29.21  ? 175 ILE A CG2 1 
ATOM   1348 C  CD1 . ILE A 1 195 ? -33.925 2.383   -10.950 1.00 28.02  ? 175 ILE A CD1 1 
ATOM   1349 N  N   . ALA A 1 196 ? -39.634 3.316   -12.481 1.00 30.54  ? 176 ALA A N   1 
ATOM   1350 C  CA  . ALA A 1 196 ? -40.539 4.197   -13.205 1.00 27.12  ? 176 ALA A CA  1 
ATOM   1351 C  C   . ALA A 1 196 ? -39.917 5.580   -13.371 1.00 30.72  ? 176 ALA A C   1 
ATOM   1352 O  O   . ALA A 1 196 ? -39.430 6.176   -12.406 1.00 32.60  ? 176 ALA A O   1 
ATOM   1353 C  CB  . ALA A 1 196 ? -41.879 4.299   -12.474 1.00 32.26  ? 176 ALA A CB  1 
ATOM   1354 N  N   . GLY A 1 197 ? -39.930 6.089   -14.601 1.00 31.89  ? 177 GLY A N   1 
ATOM   1355 C  CA  . GLY A 1 197 ? -39.401 7.405   -14.897 1.00 30.48  ? 177 GLY A CA  1 
ATOM   1356 C  C   . GLY A 1 197 ? -37.920 7.432   -15.198 1.00 29.03  ? 177 GLY A C   1 
ATOM   1357 O  O   . GLY A 1 197 ? -37.374 8.512   -15.453 1.00 32.73  ? 177 GLY A O   1 
ATOM   1358 N  N   . TYR A 1 198 ? -37.260 6.277   -15.170 1.00 25.35  ? 178 TYR A N   1 
ATOM   1359 C  CA  . TYR A 1 198 ? -35.840 6.202   -15.467 1.00 27.53  ? 178 TYR A CA  1 
ATOM   1360 C  C   . TYR A 1 198 ? -35.571 6.669   -16.897 1.00 22.85  ? 178 TYR A C   1 
ATOM   1361 O  O   . TYR A 1 198 ? -36.324 6.321   -17.813 1.00 26.48  ? 178 TYR A O   1 
ATOM   1362 C  CB  . TYR A 1 198 ? -35.360 4.764   -15.273 1.00 26.34  ? 178 TYR A CB  1 
ATOM   1363 C  CG  . TYR A 1 198 ? -33.863 4.613   -15.353 1.00 20.80  ? 178 TYR A CG  1 
ATOM   1364 C  CD1 . TYR A 1 198 ? -33.065 4.897   -14.255 1.00 22.53  ? 178 TYR A CD1 1 
ATOM   1365 C  CD2 . TYR A 1 198 ? -33.252 4.183   -16.522 1.00 20.49  ? 178 TYR A CD2 1 
ATOM   1366 C  CE1 . TYR A 1 198 ? -31.672 4.773   -14.324 1.00 23.80  ? 178 TYR A CE1 1 
ATOM   1367 C  CE2 . TYR A 1 198 ? -31.863 4.043   -16.602 1.00 22.32  ? 178 TYR A CE2 1 
ATOM   1368 C  CZ  . TYR A 1 198 ? -31.086 4.339   -15.499 1.00 21.99  ? 178 TYR A CZ  1 
ATOM   1369 O  OH  . TYR A 1 198 ? -29.723 4.199   -15.554 1.00 23.57  ? 178 TYR A OH  1 
ATOM   1370 N  N   . PRO A 1 199 ? -34.523 7.467   -17.125 1.00 26.05  ? 179 PRO A N   1 
ATOM   1371 C  CA  . PRO A 1 199 ? -34.214 7.920   -18.490 1.00 26.15  ? 179 PRO A CA  1 
ATOM   1372 C  C   . PRO A 1 199 ? -33.533 6.800   -19.257 1.00 24.86  ? 179 PRO A C   1 
ATOM   1373 O  O   . PRO A 1 199 ? -32.504 6.283   -18.818 1.00 26.72  ? 179 PRO A O   1 
ATOM   1374 C  CB  . PRO A 1 199 ? -33.260 9.108   -18.271 1.00 29.81  ? 179 PRO A CB  1 
ATOM   1375 C  CG  . PRO A 1 199 ? -33.173 9.313   -16.781 1.00 34.27  ? 179 PRO A CG  1 
ATOM   1376 C  CD  . PRO A 1 199 ? -33.586 8.022   -16.140 1.00 29.22  ? 179 PRO A CD  1 
ATOM   1377 N  N   . ALA A 1 200 ? -34.091 6.443   -20.416 1.00 26.87  ? 180 ALA A N   1 
ATOM   1378 C  CA  . ALA A 1 200 ? -33.504 5.376   -21.228 1.00 26.62  ? 180 ALA A CA  1 
ATOM   1379 C  C   . ALA A 1 200 ? -32.021 5.627   -21.490 1.00 24.86  ? 180 ALA A C   1 
ATOM   1380 O  O   . ALA A 1 200 ? -31.629 6.718   -21.913 1.00 25.28  ? 180 ALA A O   1 
ATOM   1381 C  CB  . ALA A 1 200 ? -34.248 5.272   -22.558 1.00 33.90  ? 180 ALA A CB  1 
ATOM   1382 N  N   . GLY A 1 201 ? -31.200 4.606   -21.242 1.00 24.30  ? 181 GLY A N   1 
ATOM   1383 C  CA  . GLY A 1 201 ? -29.786 4.675   -21.582 1.00 18.64  ? 181 GLY A CA  1 
ATOM   1384 C  C   . GLY A 1 201 ? -28.956 5.611   -20.737 1.00 22.61  ? 181 GLY A C   1 
ATOM   1385 O  O   . GLY A 1 201 ? -27.851 5.970   -21.149 1.00 21.96  ? 181 GLY A O   1 
ATOM   1386 N  N   . TYR A 1 202 ? -29.441 5.998   -19.553 1.00 20.06  ? 182 TYR A N   1 
ATOM   1387 C  CA  . TYR A 1 202 ? -28.780 7.050   -18.784 1.00 21.24  ? 182 TYR A CA  1 
ATOM   1388 C  C   . TYR A 1 202 ? -27.348 6.678   -18.400 1.00 20.64  ? 182 TYR A C   1 
ATOM   1389 O  O   . TYR A 1 202 ? -26.420 7.462   -18.627 1.00 21.09  ? 182 TYR A O   1 
ATOM   1390 C  CB  . TYR A 1 202 ? -29.580 7.374   -17.529 1.00 22.18  ? 182 TYR A CB  1 
ATOM   1391 C  CG  . TYR A 1 202 ? -29.067 8.619   -16.864 1.00 21.56  ? 182 TYR A CG  1 
ATOM   1392 C  CD1 . TYR A 1 202 ? -29.190 9.856   -17.491 1.00 22.44  ? 182 TYR A CD1 1 
ATOM   1393 C  CD2 . TYR A 1 202 ? -28.468 8.573   -15.615 1.00 21.42  ? 182 TYR A CD2 1 
ATOM   1394 C  CE1 . TYR A 1 202 ? -28.721 11.020  -16.896 1.00 26.22  ? 182 TYR A CE1 1 
ATOM   1395 C  CE2 . TYR A 1 202 ? -27.983 9.742   -15.007 1.00 24.05  ? 182 TYR A CE2 1 
ATOM   1396 C  CZ  . TYR A 1 202 ? -28.119 10.958  -15.660 1.00 29.91  ? 182 TYR A CZ  1 
ATOM   1397 O  OH  . TYR A 1 202 ? -27.656 12.116  -15.086 1.00 25.04  ? 182 TYR A OH  1 
ATOM   1398 N  N   . LEU A 1 203 ? -27.150 5.516   -17.763 1.00 17.10  ? 183 LEU A N   1 
ATOM   1399 C  CA  . LEU A 1 203 ? -25.803 5.186   -17.281 1.00 17.94  ? 183 LEU A CA  1 
ATOM   1400 C  C   . LEU A 1 203 ? -24.838 4.978   -18.435 1.00 19.32  ? 183 LEU A C   1 
ATOM   1401 O  O   . LEU A 1 203 ? -23.673 5.393   -18.360 1.00 18.23  ? 183 LEU A O   1 
ATOM   1402 C  CB  . LEU A 1 203 ? -25.828 3.938   -16.395 1.00 18.93  ? 183 LEU A CB  1 
ATOM   1403 C  CG  . LEU A 1 203 ? -26.400 4.102   -14.985 1.00 23.64  ? 183 LEU A CG  1 
ATOM   1404 C  CD1 . LEU A 1 203 ? -26.621 2.738   -14.381 1.00 21.33  ? 183 LEU A CD1 1 
ATOM   1405 C  CD2 . LEU A 1 203 ? -25.460 4.905   -14.084 1.00 21.80  ? 183 LEU A CD2 1 
ATOM   1406 N  N   . GLU A 1 204 ? -25.299 4.331   -19.509 1.00 20.39  ? 184 GLU A N   1 
ATOM   1407 C  CA  . GLU A 1 204 ? -24.444 4.179   -20.679 1.00 18.16  ? 184 GLU A CA  1 
ATOM   1408 C  C   . GLU A 1 204 ? -23.979 5.534   -21.191 1.00 21.14  ? 184 GLU A C   1 
ATOM   1409 O  O   . GLU A 1 204 ? -22.789 5.736   -21.473 1.00 19.40  ? 184 GLU A O   1 
ATOM   1410 C  CB  . GLU A 1 204 ? -25.179 3.436   -21.787 1.00 20.59  ? 184 GLU A CB  1 
ATOM   1411 C  CG  . GLU A 1 204 ? -24.287 3.254   -23.000 1.00 22.88  ? 184 GLU A CG  1 
ATOM   1412 C  CD  . GLU A 1 204 ? -24.964 2.535   -24.136 1.00 27.36  ? 184 GLU A CD  1 
ATOM   1413 O  OE1 . GLU A 1 204 ? -26.059 1.960   -23.922 1.00 27.85  ? 184 GLU A OE1 1 
ATOM   1414 O  OE2 . GLU A 1 204 ? -24.401 2.552   -25.253 1.00 27.07  ? 184 GLU A OE2 1 
ATOM   1415 N  N   . GLY A 1 205 ? -24.914 6.470   -21.345 1.00 19.48  ? 185 GLY A N   1 
ATOM   1416 C  CA  . GLY A 1 205 ? -24.539 7.780   -21.842 1.00 21.61  ? 185 GLY A CA  1 
ATOM   1417 C  C   . GLY A 1 205 ? -23.609 8.508   -20.894 1.00 23.44  ? 185 GLY A C   1 
ATOM   1418 O  O   . GLY A 1 205 ? -22.655 9.156   -21.323 1.00 22.25  ? 185 GLY A O   1 
ATOM   1419 N  N   . VAL A 1 206 ? -23.874 8.410   -19.593 1.00 17.99  ? 186 VAL A N   1 
ATOM   1420 C  CA  . VAL A 1 206 ? -23.039 9.094   -18.608 1.00 17.49  ? 186 VAL A CA  1 
ATOM   1421 C  C   . VAL A 1 206 ? -21.594 8.605   -18.690 1.00 20.06  ? 186 VAL A C   1 
ATOM   1422 O  O   . VAL A 1 206 ? -20.652 9.408   -18.744 1.00 20.79  ? 186 VAL A O   1 
ATOM   1423 C  CB  . VAL A 1 206 ? -23.624 8.906   -17.199 1.00 22.96  ? 186 VAL A CB  1 
ATOM   1424 C  CG1 . VAL A 1 206 ? -22.575 9.187   -16.150 1.00 23.98  ? 186 VAL A CG1 1 
ATOM   1425 C  CG2 . VAL A 1 206 ? -24.851 9.818   -17.000 1.00 28.25  ? 186 VAL A CG2 1 
ATOM   1426 N  N   . VAL A 1 207 ? -21.402 7.281   -18.697 1.00 18.38  ? 187 VAL A N   1 
ATOM   1427 C  CA  . VAL A 1 207 ? -20.054 6.712   -18.732 1.00 15.72  ? 187 VAL A CA  1 
ATOM   1428 C  C   . VAL A 1 207 ? -19.381 7.000   -20.066 1.00 18.32  ? 187 VAL A C   1 
ATOM   1429 O  O   . VAL A 1 207 ? -18.190 7.345   -20.116 1.00 20.54  ? 187 VAL A O   1 
ATOM   1430 C  CB  . VAL A 1 207 ? -20.111 5.199   -18.447 1.00 17.07  ? 187 VAL A CB  1 
ATOM   1431 C  CG1 . VAL A 1 207 ? -18.731 4.563   -18.664 1.00 24.37  ? 187 VAL A CG1 1 
ATOM   1432 C  CG2 . VAL A 1 207 ? -20.603 4.950   -17.021 1.00 20.55  ? 187 VAL A CG2 1 
ATOM   1433 N  N   . LYS A 1 208 ? -20.124 6.849   -21.164 1.00 17.38  ? 188 LYS A N   1 
ATOM   1434 C  CA  . LYS A 1 208 ? -19.550 6.965   -22.501 1.00 18.77  ? 188 LYS A CA  1 
ATOM   1435 C  C   . LYS A 1 208 ? -19.139 8.394   -22.829 1.00 21.96  ? 188 LYS A C   1 
ATOM   1436 O  O   . LYS A 1 208 ? -18.227 8.596   -23.640 1.00 20.70  ? 188 LYS A O   1 
ATOM   1437 C  CB  . LYS A 1 208 ? -20.569 6.453   -23.522 1.00 24.45  ? 188 LYS A CB  1 
ATOM   1438 C  CG  . LYS A 1 208 ? -20.142 6.483   -24.971 1.00 33.55  ? 188 LYS A CG  1 
ATOM   1439 C  CD  . LYS A 1 208 ? -21.350 6.292   -25.888 1.00 32.50  ? 188 LYS A CD  1 
ATOM   1440 C  CE  . LYS A 1 208 ? -22.015 4.949   -25.645 1.00 38.59  ? 188 LYS A CE  1 
ATOM   1441 N  NZ  . LYS A 1 208 ? -23.116 4.685   -26.615 1.00 35.54  ? 188 LYS A NZ  1 
ATOM   1442 N  N   . THR A 1 209 ? -19.799 9.393   -22.230 1.00 18.49  ? 189 THR A N   1 
ATOM   1443 C  CA  . THR A 1 209 ? -19.508 10.800  -22.510 1.00 18.23  ? 189 THR A CA  1 
ATOM   1444 C  C   . THR A 1 209 ? -18.750 11.480  -21.381 1.00 19.33  ? 189 THR A C   1 
ATOM   1445 O  O   . THR A 1 209 ? -18.537 12.694  -21.440 1.00 21.19  ? 189 THR A O   1 
ATOM   1446 C  CB  . THR A 1 209 ? -20.790 11.611  -22.789 1.00 25.45  ? 189 THR A CB  1 
ATOM   1447 O  OG1 . THR A 1 209 ? -21.644 11.581  -21.636 1.00 21.87  ? 189 THR A OG1 1 
ATOM   1448 C  CG2 . THR A 1 209 ? -21.534 11.075  -23.998 1.00 25.51  ? 189 THR A CG2 1 
ATOM   1449 N  N   . SER A 1 210 ? -18.355 10.748  -20.350 1.00 18.37  ? 190 SER A N   1 
ATOM   1450 C  CA  . SER A 1 210 ? -17.710 11.391  -19.214 1.00 18.69  ? 190 SER A CA  1 
ATOM   1451 C  C   . SER A 1 210 ? -16.298 11.846  -19.556 1.00 19.44  ? 190 SER A C   1 
ATOM   1452 O  O   . SER A 1 210 ? -15.482 11.071  -20.064 1.00 20.09  ? 190 SER A O   1 
ATOM   1453 C  CB  . SER A 1 210 ? -17.651 10.450  -18.019 1.00 17.61  ? 190 SER A CB  1 
ATOM   1454 O  OG  . SER A 1 210 ? -16.868 11.082  -17.001 1.00 18.57  ? 190 SER A OG  1 
ATOM   1455 N  N   . THR A 1 211 ? -15.992 13.096  -19.222 1.00 19.31  ? 191 THR A N   1 
ATOM   1456 C  CA  . THR A 1 211 ? -14.623 13.579  -19.266 1.00 20.84  ? 191 THR A CA  1 
ATOM   1457 C  C   . THR A 1 211 ? -14.028 13.729  -17.873 1.00 19.25  ? 191 THR A C   1 
ATOM   1458 O  O   . THR A 1 211 ? -12.946 14.313  -17.730 1.00 24.67  ? 191 THR A O   1 
ATOM   1459 C  CB  . THR A 1 211 ? -14.556 14.903  -20.028 1.00 24.06  ? 191 THR A CB  1 
ATOM   1460 O  OG1 . THR A 1 211 ? -15.483 15.833  -19.462 1.00 26.46  ? 191 THR A OG1 1 
ATOM   1461 C  CG2 . THR A 1 211 ? -14.900 14.693  -21.500 1.00 25.03  ? 191 THR A CG2 1 
ATOM   1462 N  N   . THR A 1 212 ? -14.714 13.226  -16.847 1.00 19.17  ? 192 THR A N   1 
ATOM   1463 C  CA  . THR A 1 212 ? -14.225 13.247  -15.473 1.00 16.32  ? 192 THR A CA  1 
ATOM   1464 C  C   . THR A 1 212 ? -13.715 11.895  -15.004 1.00 16.94  ? 192 THR A C   1 
ATOM   1465 O  O   . THR A 1 212 ? -13.065 11.830  -13.957 1.00 21.27  ? 192 THR A O   1 
ATOM   1466 C  CB  . THR A 1 212 ? -15.324 13.694  -14.507 1.00 21.96  ? 192 THR A CB  1 
ATOM   1467 O  OG1 . THR A 1 212 ? -16.358 12.697  -14.479 1.00 25.73  ? 192 THR A OG1 1 
ATOM   1468 C  CG2 . THR A 1 212 ? -15.912 15.012  -14.954 1.00 20.73  ? 192 THR A CG2 1 
ATOM   1469 N  N   . THR A 1 213 ? -14.016 10.824  -15.738 1.00 15.44  ? 193 THR A N   1 
ATOM   1470 C  CA  . THR A 1 213 ? -13.494 9.505   -15.403 1.00 14.04  ? 193 THR A CA  1 
ATOM   1471 C  C   . THR A 1 213 ? -11.990 9.585   -15.196 1.00 19.12  ? 193 THR A C   1 
ATOM   1472 O  O   . THR A 1 213 ? -11.283 10.271  -15.943 1.00 18.26  ? 193 THR A O   1 
ATOM   1473 C  CB  . THR A 1 213 ? -13.832 8.532   -16.528 1.00 16.12  ? 193 THR A CB  1 
ATOM   1474 O  OG1 . THR A 1 213 ? -15.238 8.274   -16.505 1.00 16.83  ? 193 THR A OG1 1 
ATOM   1475 C  CG2 . THR A 1 213 ? -13.049 7.208   -16.418 1.00 15.02  ? 193 THR A CG2 1 
ATOM   1476 N  N   . LYS A 1 214 ? -11.510 8.920   -14.151 1.00 16.21  ? 194 LYS A N   1 
ATOM   1477 C  CA  . LYS A 1 214 ? -10.112 9.061   -13.772 1.00 19.69  ? 194 LYS A CA  1 
ATOM   1478 C  C   . LYS A 1 214 ? -9.488  7.692   -13.605 1.00 18.50  ? 194 LYS A C   1 
ATOM   1479 O  O   . LYS A 1 214 ? -10.045 6.844   -12.910 1.00 17.46  ? 194 LYS A O   1 
ATOM   1480 C  CB  . LYS A 1 214 ? -9.977  9.842   -12.470 1.00 22.99  ? 194 LYS A CB  1 
ATOM   1481 C  CG  . LYS A 1 214 ? -8.532  10.033  -12.021 1.00 27.05  ? 194 LYS A CG  1 
ATOM   1482 C  CD  . LYS A 1 214 ? -8.325  11.425  -11.452 1.00 29.47  ? 194 LYS A CD  1 
ATOM   1483 C  CE  . LYS A 1 214 ? -8.408  12.478  -12.533 1.00 36.78  ? 194 LYS A CE  1 
ATOM   1484 N  NZ  . LYS A 1 214 ? -8.381  13.855  -11.970 1.00 27.97  ? 194 LYS A NZ  1 
ATOM   1485 N  N   . ALA A 1 215 ? -8.313  7.494   -14.190 1.00 13.90  ? 195 ALA A N   1 
ATOM   1486 C  CA  . ALA A 1 215 ? -7.580  6.247   -14.037 1.00 14.91  ? 195 ALA A CA  1 
ATOM   1487 C  C   . ALA A 1 215 ? -6.443  6.471   -13.057 1.00 16.57  ? 195 ALA A C   1 
ATOM   1488 O  O   . ALA A 1 215 ? -5.837  7.547   -13.034 1.00 18.20  ? 195 ALA A O   1 
ATOM   1489 C  CB  . ALA A 1 215 ? -7.033  5.764   -15.378 1.00 18.07  ? 195 ALA A CB  1 
ATOM   1490 N  N   . ARG A 1 216 ? -6.176  5.449   -12.242 1.00 16.30  ? 196 ARG A N   1 
ATOM   1491 C  CA  . ARG A 1 216 ? -5.161  5.489   -11.197 1.00 16.21  ? 196 ARG A CA  1 
ATOM   1492 C  C   . ARG A 1 216 ? -4.260  4.279   -11.365 1.00 17.12  ? 196 ARG A C   1 
ATOM   1493 O  O   . ARG A 1 216 ? -4.734  3.138   -11.338 1.00 15.92  ? 196 ARG A O   1 
ATOM   1494 C  CB  . ARG A 1 216 ? -5.816  5.463   -9.818  1.00 16.66  ? 196 ARG A CB  1 
ATOM   1495 C  CG  . ARG A 1 216 ? -4.801  5.455   -8.692  1.00 19.02  ? 196 ARG A CG  1 
ATOM   1496 C  CD  . ARG A 1 216 ? -5.493  5.169   -7.360  1.00 26.00  ? 196 ARG A CD  1 
ATOM   1497 N  NE  . ARG A 1 216 ? -5.936  3.782   -7.292  1.00 24.61  ? 196 ARG A NE  1 
ATOM   1498 C  CZ  . ARG A 1 216 ? -6.735  3.289   -6.355  1.00 21.95  ? 196 ARG A CZ  1 
ATOM   1499 N  NH1 . ARG A 1 216 ? -7.234  4.054   -5.401  1.00 25.02  ? 196 ARG A NH1 1 
ATOM   1500 N  NH2 . ARG A 1 216 ? -7.006  1.988   -6.353  1.00 23.81  ? 196 ARG A NH2 1 
ATOM   1501 N  N   . LEU A 1 217 ? -2.967  4.528   -11.536 1.00 15.57  ? 197 LEU A N   1 
ATOM   1502 C  CA  . LEU A 1 217 ? -1.962  3.485   -11.611 1.00 18.17  ? 197 LEU A CA  1 
ATOM   1503 C  C   . LEU A 1 217 ? -1.184  3.573   -10.309 1.00 20.91  ? 197 LEU A C   1 
ATOM   1504 O  O   . LEU A 1 217 ? -0.628  4.628   -10.001 1.00 20.77  ? 197 LEU A O   1 
ATOM   1505 C  CB  . LEU A 1 217 ? -1.061  3.708   -12.831 1.00 18.31  ? 197 LEU A CB  1 
ATOM   1506 C  CG  . LEU A 1 217 ? -0.098  2.655   -13.328 1.00 25.07  ? 197 LEU A CG  1 
ATOM   1507 C  CD1 . LEU A 1 217 ? -0.841  1.397   -13.786 1.00 16.97  ? 197 LEU A CD1 1 
ATOM   1508 C  CD2 . LEU A 1 217 ? 0.743   3.240   -14.462 1.00 19.10  ? 197 LEU A CD2 1 
ATOM   1509 N  N   . LEU A 1 218 ? -1.203  2.507   -9.516  1.00 15.62  ? 198 LEU A N   1 
ATOM   1510 C  CA  . LEU A 1 218 ? -0.549  2.500   -8.218  1.00 15.42  ? 198 LEU A CA  1 
ATOM   1511 C  C   . LEU A 1 218 ? 0.699   1.632   -8.266  1.00 17.06  ? 198 LEU A C   1 
ATOM   1512 O  O   . LEU A 1 218 ? 0.716   0.584   -8.917  1.00 19.09  ? 198 LEU A O   1 
ATOM   1513 C  CB  . LEU A 1 218 ? -1.473  1.985   -7.113  1.00 18.91  ? 198 LEU A CB  1 
ATOM   1514 C  CG  . LEU A 1 218 ? -2.614  2.878   -6.661  1.00 27.34  ? 198 LEU A CG  1 
ATOM   1515 C  CD1 . LEU A 1 218 ? -3.323  2.280   -5.433  1.00 23.37  ? 198 LEU A CD1 1 
ATOM   1516 C  CD2 . LEU A 1 218 ? -2.078  4.270   -6.380  1.00 24.14  ? 198 LEU A CD2 1 
ATOM   1517 N  N   . HIS A 1 219 ? 1.735   2.083   -7.567  1.00 19.47  ? 199 HIS A N   1 
ATOM   1518 C  CA  . HIS A 1 219 ? 2.979   1.343   -7.406  1.00 18.36  ? 199 HIS A CA  1 
ATOM   1519 C  C   . HIS A 1 219 ? 3.281   1.268   -5.920  1.00 22.31  ? 199 HIS A C   1 
ATOM   1520 O  O   . HIS A 1 219 ? 3.643   2.275   -5.311  1.00 23.53  ? 199 HIS A O   1 
ATOM   1521 C  CB  . HIS A 1 219 ? 4.131   2.028   -8.141  1.00 17.99  ? 199 HIS A CB  1 
ATOM   1522 C  CG  . HIS A 1 219 ? 5.448   1.364   -7.916  1.00 18.89  ? 199 HIS A CG  1 
ATOM   1523 N  ND1 . HIS A 1 219 ? 5.726   0.096   -8.382  1.00 18.61  ? 199 HIS A ND1 1 
ATOM   1524 C  CD2 . HIS A 1 219 ? 6.546   1.770   -7.239  1.00 20.94  ? 199 HIS A CD2 1 
ATOM   1525 C  CE1 . HIS A 1 219 ? 6.958   -0.235  -8.027  1.00 19.48  ? 199 HIS A CE1 1 
ATOM   1526 N  NE2 . HIS A 1 219 ? 7.474   0.761   -7.328  1.00 20.99  ? 199 HIS A NE2 1 
ATOM   1527 N  N   . TYR A 1 220 ? 3.122   0.094   -5.332  1.00 19.46  ? 200 TYR A N   1 
ATOM   1528 C  CA  . TYR A 1 220 ? 3.519   -0.143  -3.960  1.00 20.75  ? 200 TYR A CA  1 
ATOM   1529 C  C   . TYR A 1 220 ? 4.986   -0.524  -3.955  1.00 22.99  ? 200 TYR A C   1 
ATOM   1530 O  O   . TYR A 1 220 ? 5.378   -1.537  -4.558  1.00 25.19  ? 200 TYR A O   1 
ATOM   1531 C  CB  . TYR A 1 220 ? 2.657   -1.234  -3.331  1.00 21.76  ? 200 TYR A CB  1 
ATOM   1532 C  CG  . TYR A 1 220 ? 1.260   -0.736  -3.090  1.00 24.59  ? 200 TYR A CG  1 
ATOM   1533 C  CD1 . TYR A 1 220 ? 0.940   -0.068  -1.917  1.00 30.65  ? 200 TYR A CD1 1 
ATOM   1534 C  CD2 . TYR A 1 220 ? 0.276   -0.888  -4.055  1.00 23.79  ? 200 TYR A CD2 1 
ATOM   1535 C  CE1 . TYR A 1 220 ? -0.348  0.407   -1.697  1.00 27.00  ? 200 TYR A CE1 1 
ATOM   1536 C  CE2 . TYR A 1 220 ? -1.024  -0.416  -3.845  1.00 28.23  ? 200 TYR A CE2 1 
ATOM   1537 C  CZ  . TYR A 1 220 ? -1.318  0.229   -2.663  1.00 24.84  ? 200 TYR A CZ  1 
ATOM   1538 O  OH  . TYR A 1 220 ? -2.586  0.703   -2.434  1.00 32.02  ? 200 TYR A OH  1 
ATOM   1539 N  N   . PHE A 1 221 ? 5.778   0.313   -3.295  1.00 21.10  ? 201 PHE A N   1 
ATOM   1540 C  CA  . PHE A 1 221 ? 7.215   0.146   -3.253  1.00 21.77  ? 201 PHE A CA  1 
ATOM   1541 C  C   . PHE A 1 221 ? 7.574   -1.045  -2.372  1.00 24.07  ? 201 PHE A C   1 
ATOM   1542 O  O   . PHE A 1 221 ? 6.914   -1.292  -1.359  1.00 32.07  ? 201 PHE A O   1 
ATOM   1543 C  CB  . PHE A 1 221 ? 7.881   1.407   -2.711  1.00 26.39  ? 201 PHE A CB  1 
ATOM   1544 C  CG  . PHE A 1 221 ? 7.891   2.550   -3.681  1.00 25.64  ? 201 PHE A CG  1 
ATOM   1545 C  CD1 . PHE A 1 221 ? 8.934   2.698   -4.581  1.00 21.82  ? 201 PHE A CD1 1 
ATOM   1546 C  CD2 . PHE A 1 221 ? 6.851   3.466   -3.702  1.00 24.56  ? 201 PHE A CD2 1 
ATOM   1547 C  CE1 . PHE A 1 221 ? 8.950   3.757   -5.481  1.00 25.62  ? 201 PHE A CE1 1 
ATOM   1548 C  CE2 . PHE A 1 221 ? 6.854   4.521   -4.600  1.00 25.92  ? 201 PHE A CE2 1 
ATOM   1549 C  CZ  . PHE A 1 221 ? 7.903   4.666   -5.490  1.00 22.38  ? 201 PHE A CZ  1 
ATOM   1550 N  N   . PRO A 1 222 ? 8.611   -1.791  -2.729  1.00 25.80  ? 202 PRO A N   1 
ATOM   1551 C  CA  . PRO A 1 222 ? 9.033   -2.912  -1.887  1.00 29.69  ? 202 PRO A CA  1 
ATOM   1552 C  C   . PRO A 1 222 ? 9.393   -2.451  -0.484  1.00 40.37  ? 202 PRO A C   1 
ATOM   1553 O  O   . PRO A 1 222 ? 9.827   -1.317  -0.264  1.00 32.14  ? 202 PRO A O   1 
ATOM   1554 C  CB  . PRO A 1 222 ? 10.255  -3.465  -2.624  1.00 34.87  ? 202 PRO A CB  1 
ATOM   1555 C  CG  . PRO A 1 222 ? 10.090  -3.006  -4.034  1.00 34.10  ? 202 PRO A CG  1 
ATOM   1556 C  CD  . PRO A 1 222 ? 9.427   -1.666  -3.946  1.00 29.08  ? 202 PRO A CD  1 
ATOM   1557 N  N   . GLU A 1 223 ? 9.217   -3.360  0.468   1.00 39.69  ? 203 GLU A N   1 
ATOM   1558 C  CA  . GLU A 1 223 ? 9.406   -3.054  1.878   1.00 51.30  ? 203 GLU A CA  1 
ATOM   1559 C  C   . GLU A 1 223 ? 10.288  -4.106  2.545   1.00 64.52  ? 203 GLU A C   1 
ATOM   1560 O  O   . GLU A 1 223 ? 11.424  -4.337  2.121   1.00 66.15  ? 203 GLU A O   1 
ATOM   1561 C  CB  . GLU A 1 223 ? 8.047   -2.962  2.577   1.00 66.39  ? 203 GLU A CB  1 
ATOM   1562 C  CG  . GLU A 1 223 ? 7.061   -4.026  2.110   1.00 67.77  ? 203 GLU A CG  1 
ATOM   1563 C  CD  . GLU A 1 223 ? 5.616   -3.689  2.431   1.00 74.21  ? 203 GLU A CD  1 
ATOM   1564 O  OE1 . GLU A 1 223 ? 5.346   -2.548  2.865   1.00 83.59  ? 203 GLU A OE1 1 
ATOM   1565 O  OE2 . GLU A 1 223 ? 4.749   -4.571  2.243   1.00 63.74  ? 203 GLU A OE2 1 
ATOM   1566 N  N   . CYS A 1 246 ? -7.666  -3.547  7.766   1.00 61.36  ? 226 CYS A N   1 
ATOM   1567 C  CA  . CYS A 1 246 ? -7.945  -2.302  7.058   1.00 54.04  ? 226 CYS A CA  1 
ATOM   1568 C  C   . CYS A 1 246 ? -9.428  -1.933  7.137   1.00 57.43  ? 226 CYS A C   1 
ATOM   1569 O  O   . CYS A 1 246 ? -10.285 -2.794  7.345   1.00 49.42  ? 226 CYS A O   1 
ATOM   1570 C  CB  . CYS A 1 246 ? -7.507  -2.413  5.593   1.00 54.01  ? 226 CYS A CB  1 
ATOM   1571 S  SG  . CYS A 1 246 ? -7.670  -0.878  4.634   1.00 55.30  ? 226 CYS A SG  1 
ATOM   1572 N  N   . ALA A 1 247 ? -9.727  -0.649  6.971   1.00 42.93  ? 227 ALA A N   1 
ATOM   1573 C  CA  . ALA A 1 247 ? -11.104 -0.181  6.994   1.00 48.05  ? 227 ALA A CA  1 
ATOM   1574 C  C   . ALA A 1 247 ? -11.706 -0.245  5.596   1.00 30.97  ? 227 ALA A C   1 
ATOM   1575 O  O   . ALA A 1 247 ? -11.005 -0.153  4.583   1.00 32.35  ? 227 ALA A O   1 
ATOM   1576 C  CB  . ALA A 1 247 ? -11.192 1.249   7.536   1.00 38.15  ? 227 ALA A CB  1 
ATOM   1577 N  N   . THR A 1 248 ? -13.021 -0.409  5.549   1.00 35.30  ? 228 THR A N   1 
ATOM   1578 C  CA  . THR A 1 248 ? -13.683 -0.453  4.262   1.00 27.32  ? 228 THR A CA  1 
ATOM   1579 C  C   . THR A 1 248 ? -13.965 0.956   3.752   1.00 28.35  ? 228 THR A C   1 
ATOM   1580 O  O   . THR A 1 248 ? -13.943 1.942   4.492   1.00 29.36  ? 228 THR A O   1 
ATOM   1581 C  CB  . THR A 1 248 ? -14.999 -1.229  4.349   1.00 24.64  ? 228 THR A CB  1 
ATOM   1582 O  OG1 . THR A 1 248 ? -15.846 -0.619  5.331   1.00 33.19  ? 228 THR A OG1 1 
ATOM   1583 C  CG2 . THR A 1 248 ? -14.750 -2.673  4.727   1.00 36.75  ? 228 THR A CG2 1 
ATOM   1584 N  N   . HIS A 1 249 ? -14.239 1.031   2.461   1.00 22.42  ? 229 HIS A N   1 
ATOM   1585 C  CA  . HIS A 1 249 ? -14.719 2.242   1.828   1.00 24.02  ? 229 HIS A CA  1 
ATOM   1586 C  C   . HIS A 1 249 ? -15.747 1.847   0.786   1.00 23.58  ? 229 HIS A C   1 
ATOM   1587 O  O   . HIS A 1 249 ? -15.895 0.670   0.441   1.00 20.08  ? 229 HIS A O   1 
ATOM   1588 C  CB  . HIS A 1 249 ? -13.586 3.016   1.161   1.00 21.86  ? 229 HIS A CB  1 
ATOM   1589 C  CG  . HIS A 1 249 ? -12.972 2.287   0.010   1.00 20.99  ? 229 HIS A CG  1 
ATOM   1590 N  ND1 . HIS A 1 249 ? -11.949 1.377   0.169   1.00 20.85  ? 229 HIS A ND1 1 
ATOM   1591 C  CD2 . HIS A 1 249 ? -13.239 2.325   -1.316  1.00 19.80  ? 229 HIS A CD2 1 
ATOM   1592 C  CE1 . HIS A 1 249 ? -11.609 0.888   -1.009  1.00 20.96  ? 229 HIS A CE1 1 
ATOM   1593 N  NE2 . HIS A 1 249 ? -12.369 1.455   -1.930  1.00 19.63  ? 229 HIS A NE2 1 
ATOM   1594 N  N   . LEU A 1 250 ? -16.445 2.857   0.279   1.00 20.43  ? 230 LEU A N   1 
ATOM   1595 C  CA  . LEU A 1 250 ? -17.274 2.746   -0.909  1.00 20.03  ? 230 LEU A CA  1 
ATOM   1596 C  C   . LEU A 1 250 ? -16.606 3.535   -2.020  1.00 19.36  ? 230 LEU A C   1 
ATOM   1597 O  O   . LEU A 1 250 ? -16.099 4.638   -1.780  1.00 23.64  ? 230 LEU A O   1 
ATOM   1598 C  CB  . LEU A 1 250 ? -18.674 3.313   -0.670  1.00 20.47  ? 230 LEU A CB  1 
ATOM   1599 C  CG  . LEU A 1 250 ? -19.483 2.699   0.453   1.00 21.51  ? 230 LEU A CG  1 
ATOM   1600 C  CD1 . LEU A 1 250 ? -20.764 3.527   0.703   1.00 25.29  ? 230 LEU A CD1 1 
ATOM   1601 C  CD2 . LEU A 1 250 ? -19.832 1.270   0.081   1.00 24.91  ? 230 LEU A CD2 1 
ATOM   1602 N  N   . ASP A 1 251 ? -16.633 3.001   -3.239  1.00 18.37  ? 231 ASP A N   1 
ATOM   1603 C  CA  . ASP A 1 251 ? -16.252 3.828   -4.377  1.00 17.50  ? 231 ASP A CA  1 
ATOM   1604 C  C   . ASP A 1 251 ? -17.327 4.887   -4.624  1.00 20.09  ? 231 ASP A C   1 
ATOM   1605 O  O   . ASP A 1 251 ? -18.517 4.678   -4.355  1.00 18.99  ? 231 ASP A O   1 
ATOM   1606 C  CB  . ASP A 1 251 ? -16.035 2.982   -5.633  1.00 16.24  ? 231 ASP A CB  1 
ATOM   1607 C  CG  . ASP A 1 251 ? -14.758 2.141   -5.562  1.00 20.03  ? 231 ASP A CG  1 
ATOM   1608 O  OD1 . ASP A 1 251 ? -14.231 1.958   -4.452  1.00 19.34  ? 231 ASP A OD1 1 
ATOM   1609 O  OD2 . ASP A 1 251 ? -14.285 1.688   -6.618  1.00 19.93  ? 231 ASP A OD2 1 
ATOM   1610 N  N   . HIS A 1 252 ? -16.895 6.032   -5.151  1.00 19.93  ? 232 HIS A N   1 
ATOM   1611 C  CA  A HIS A 1 252 ? -17.742 7.220   -5.248  0.48 19.42  ? 232 HIS A CA  1 
ATOM   1612 C  CA  B HIS A 1 252 ? -17.760 7.203   -5.233  0.52 19.35  ? 232 HIS A CA  1 
ATOM   1613 C  C   . HIS A 1 252 ? -18.545 7.292   -6.536  1.00 17.69  ? 232 HIS A C   1 
ATOM   1614 O  O   . HIS A 1 252 ? -19.647 7.867   -6.544  1.00 20.18  ? 232 HIS A O   1 
ATOM   1615 C  CB  A HIS A 1 252 ? -16.893 8.497   -5.174  0.48 24.00  ? 232 HIS A CB  1 
ATOM   1616 C  CB  B HIS A 1 252 ? -16.910 8.468   -5.064  0.52 23.99  ? 232 HIS A CB  1 
ATOM   1617 C  CG  A HIS A 1 252 ? -16.242 8.731   -3.849  0.48 27.49  ? 232 HIS A CG  1 
ATOM   1618 C  CG  B HIS A 1 252 ? -17.698 9.693   -4.731  0.52 25.53  ? 232 HIS A CG  1 
ATOM   1619 N  ND1 A HIS A 1 252 ? -14.987 8.255   -3.539  0.48 32.80  ? 232 HIS A ND1 1 
ATOM   1620 N  ND1 B HIS A 1 252 ? -17.807 10.765  -5.591  0.52 35.56  ? 232 HIS A ND1 1 
ATOM   1621 C  CD2 A HIS A 1 252 ? -16.658 9.424   -2.763  0.48 34.40  ? 232 HIS A CD2 1 
ATOM   1622 C  CD2 B HIS A 1 252 ? -18.405 10.024  -3.625  0.52 27.65  ? 232 HIS A CD2 1 
ATOM   1623 C  CE1 A HIS A 1 252 ? -14.667 8.626   -2.313  0.48 32.44  ? 232 HIS A CE1 1 
ATOM   1624 C  CE1 B HIS A 1 252 ? -18.552 11.701  -5.030  0.52 31.89  ? 232 HIS A CE1 1 
ATOM   1625 N  NE2 A HIS A 1 252 ? -15.667 9.331   -1.817  0.48 31.39  ? 232 HIS A NE2 1 
ATOM   1626 N  NE2 B HIS A 1 252 ? -18.927 11.277  -3.837  0.52 28.91  ? 232 HIS A NE2 1 
ATOM   1627 N  N   . GLY A 1 253 ? -18.005 6.768   -7.627  1.00 19.31  ? 233 GLY A N   1 
ATOM   1628 C  CA  . GLY A 1 253 ? -18.552 7.015   -8.946  1.00 18.12  ? 233 GLY A CA  1 
ATOM   1629 C  C   . GLY A 1 253 ? -19.531 5.993   -9.470  1.00 15.91  ? 233 GLY A C   1 
ATOM   1630 O  O   . GLY A 1 253 ? -20.395 5.524   -8.729  1.00 18.68  ? 233 GLY A O   1 
ATOM   1631 N  N   . CYS A 1 254 ? -19.438 5.674   -10.754 1.00 18.12  ? 234 CYS A N   1 
ATOM   1632 C  CA  . CYS A 1 254 ? -20.390 4.736   -11.360 1.00 14.88  ? 234 CYS A CA  1 
ATOM   1633 C  C   . CYS A 1 254 ? -19.838 3.319   -11.324 1.00 16.63  ? 234 CYS A C   1 
ATOM   1634 O  O   . CYS A 1 254 ? -20.328 2.470   -10.570 1.00 18.58  ? 234 CYS A O   1 
ATOM   1635 C  CB  . CYS A 1 254 ? -20.711 5.152   -12.792 1.00 17.81  ? 234 CYS A CB  1 
ATOM   1636 S  SG  . CYS A 1 254 ? -21.655 6.690   -12.837 1.00 23.23  ? 234 CYS A SG  1 
ATOM   1637 N  N   . LEU A 1 255 ? -18.795 3.068   -12.122 1.00 14.54  ? 235 LEU A N   1 
ATOM   1638 C  CA  . LEU A 1 255 ? -18.216 1.734   -12.249 1.00 13.39  ? 235 LEU A CA  1 
ATOM   1639 C  C   . LEU A 1 255 ? -16.706 1.855   -12.219 1.00 14.49  ? 235 LEU A C   1 
ATOM   1640 O  O   . LEU A 1 255 ? -16.123 2.587   -13.021 1.00 17.54  ? 235 LEU A O   1 
ATOM   1641 C  CB  . LEU A 1 255 ? -18.626 1.022   -13.547 1.00 13.12  ? 235 LEU A CB  1 
ATOM   1642 C  CG  . LEU A 1 255 ? -20.120 0.668   -13.646 1.00 15.97  ? 235 LEU A CG  1 
ATOM   1643 C  CD1 . LEU A 1 255 ? -20.505 0.434   -15.107 1.00 19.60  ? 235 LEU A CD1 1 
ATOM   1644 C  CD2 . LEU A 1 255 ? -20.521 -0.548  -12.782 1.00 16.86  ? 235 LEU A CD2 1 
ATOM   1645 N  N   . THR A 1 256 ? -16.089 1.142   -11.307 1.00 13.51  ? 236 THR A N   1 
ATOM   1646 C  CA  . THR A 1 256 ? -14.637 1.115   -11.208 1.00 16.00  ? 236 THR A CA  1 
ATOM   1647 C  C   . THR A 1 256 ? -14.149 -0.143  -11.905 1.00 16.67  ? 236 THR A C   1 
ATOM   1648 O  O   . THR A 1 256 ? -14.427 -1.254  -11.445 1.00 16.60  ? 236 THR A O   1 
ATOM   1649 C  CB  . THR A 1 256 ? -14.191 1.130   -9.758  1.00 15.01  ? 236 THR A CB  1 
ATOM   1650 O  OG1 . THR A 1 256 ? -14.797 2.246   -9.112  1.00 18.14  ? 236 THR A OG1 1 
ATOM   1651 C  CG2 . THR A 1 256 ? -12.653 1.226   -9.682  1.00 16.72  ? 236 THR A CG2 1 
ATOM   1652 N  N   . GLY A 1 257 ? -13.435 0.035   -13.016 1.00 15.62  ? 237 GLY A N   1 
ATOM   1653 C  CA  . GLY A 1 257 ? -12.820 -1.092  -13.689 1.00 14.35  ? 237 GLY A CA  1 
ATOM   1654 C  C   . GLY A 1 257 ? -11.494 -1.425  -13.024 1.00 18.48  ? 237 GLY A C   1 
ATOM   1655 O  O   . GLY A 1 257 ? -10.742 -0.545  -12.631 1.00 18.28  ? 237 GLY A O   1 
ATOM   1656 N  N   . LEU A 1 258 ? -11.235 -2.720  -12.868 1.00 14.80  ? 238 LEU A N   1 
ATOM   1657 C  CA  . LEU A 1 258 ? -10.097 -3.221  -12.097 1.00 17.00  ? 238 LEU A CA  1 
ATOM   1658 C  C   . LEU A 1 258 ? -9.381  -4.313  -12.872 1.00 19.60  ? 238 LEU A C   1 
ATOM   1659 O  O   . LEU A 1 258 ? -10.031 -5.186  -13.447 1.00 18.32  ? 238 LEU A O   1 
ATOM   1660 C  CB  . LEU A 1 258 ? -10.561 -3.815  -10.773 1.00 21.73  ? 238 LEU A CB  1 
ATOM   1661 C  CG  . LEU A 1 258 ? -11.435 -2.997  -9.833  1.00 25.03  ? 238 LEU A CG  1 
ATOM   1662 C  CD1 . LEU A 1 258 ? -11.940 -3.939  -8.773  1.00 29.45  ? 238 LEU A CD1 1 
ATOM   1663 C  CD2 . LEU A 1 258 ? -10.617 -1.880  -9.219  1.00 23.39  ? 238 LEU A CD2 1 
ATOM   1664 N  N   . THR A 1 259 ? -8.041  -4.265  -12.878 1.00 18.20  ? 239 THR A N   1 
ATOM   1665 C  CA  . THR A 1 259 ? -7.214  -5.421  -13.219 1.00 18.43  ? 239 THR A CA  1 
ATOM   1666 C  C   . THR A 1 259 ? -6.830  -6.181  -11.951 1.00 18.50  ? 239 THR A C   1 
ATOM   1667 O  O   . THR A 1 259 ? -6.821  -5.634  -10.847 1.00 19.62  ? 239 THR A O   1 
ATOM   1668 C  CB  . THR A 1 259 ? -5.921  -5.014  -13.953 1.00 24.91  ? 239 THR A CB  1 
ATOM   1669 O  OG1 . THR A 1 259 ? -5.155  -4.134  -13.122 1.00 24.79  ? 239 THR A OG1 1 
ATOM   1670 C  CG2 . THR A 1 259 ? -6.222  -4.309  -15.275 1.00 30.00  ? 239 THR A CG2 1 
ATOM   1671 N  N   . SER A 1 260 ? -6.478  -7.454  -12.116 1.00 17.25  ? 240 SER A N   1 
ATOM   1672 C  CA  . SER A 1 260 ? -5.805  -8.124  -11.017 1.00 17.96  ? 240 SER A CA  1 
ATOM   1673 C  C   . SER A 1 260 ? -4.440  -7.474  -10.797 1.00 19.51  ? 240 SER A C   1 
ATOM   1674 O  O   . SER A 1 260 ? -3.825  -6.939  -11.724 1.00 19.45  ? 240 SER A O   1 
ATOM   1675 C  CB  . SER A 1 260 ? -5.618  -9.616  -11.302 1.00 25.91  ? 240 SER A CB  1 
ATOM   1676 O  OG  . SER A 1 260 ? -4.617  -9.818  -12.283 1.00 27.37  ? 240 SER A OG  1 
ATOM   1677 N  N   . ALA A 1 261 ? -3.967  -7.525  -9.559  1.00 18.12  ? 241 ALA A N   1 
ATOM   1678 C  CA  . ALA A 1 261 ? -2.712  -6.858  -9.236  1.00 17.70  ? 241 ALA A CA  1 
ATOM   1679 C  C   . ALA A 1 261 ? -1.535  -7.610  -9.845  1.00 17.93  ? 241 ALA A C   1 
ATOM   1680 O  O   . ALA A 1 261 ? -1.581  -8.829  -10.034 1.00 19.56  ? 241 ALA A O   1 
ATOM   1681 C  CB  . ALA A 1 261 ? -2.534  -6.762  -7.723  1.00 21.49  ? 241 ALA A CB  1 
ATOM   1682 N  N   . MET A 1 262 ? -0.466  -6.869  -10.141 1.00 17.44  ? 242 MET A N   1 
ATOM   1683 C  CA  . MET A 1 262 ? 0.799   -7.455  -10.577 1.00 18.32  ? 242 MET A CA  1 
ATOM   1684 C  C   . MET A 1 262 ? 1.786   -7.409  -9.419  1.00 20.72  ? 242 MET A C   1 
ATOM   1685 O  O   . MET A 1 262 ? 2.044   -6.339  -8.868  1.00 21.65  ? 242 MET A O   1 
ATOM   1686 C  CB  . MET A 1 262 ? 1.384   -6.700  -11.769 1.00 18.74  ? 242 MET A CB  1 
ATOM   1687 C  CG  . MET A 1 262 ? 2.880   -6.973  -11.952 1.00 25.20  ? 242 MET A CG  1 
ATOM   1688 S  SD  . MET A 1 262 ? 3.442   -5.802  -13.186 1.00 25.06  ? 242 MET A SD  1 
ATOM   1689 C  CE  . MET A 1 262 ? 2.919   -6.658  -14.650 1.00 39.09  ? 242 MET A CE  1 
ATOM   1690 N  N   . PHE A 1 263 ? 2.330   -8.558  -9.047  1.00 20.36  ? 243 PHE A N   1 
ATOM   1691 C  CA  . PHE A 1 263 ? 3.468   -8.615  -8.137  1.00 19.41  ? 243 PHE A CA  1 
ATOM   1692 C  C   . PHE A 1 263 ? 4.733   -8.846  -8.955  1.00 21.08  ? 243 PHE A C   1 
ATOM   1693 O  O   . PHE A 1 263 ? 4.765   -9.729  -9.817  1.00 23.84  ? 243 PHE A O   1 
ATOM   1694 C  CB  . PHE A 1 263 ? 3.271   -9.725  -7.098  1.00 19.95  ? 243 PHE A CB  1 
ATOM   1695 C  CG  . PHE A 1 263 ? 2.155   -9.447  -6.144  1.00 21.32  ? 243 PHE A CG  1 
ATOM   1696 C  CD1 . PHE A 1 263 ? 2.377   -8.664  -5.026  1.00 22.85  ? 243 PHE A CD1 1 
ATOM   1697 C  CD2 . PHE A 1 263 ? 0.874   -9.950  -6.385  1.00 22.63  ? 243 PHE A CD2 1 
ATOM   1698 C  CE1 . PHE A 1 263 ? 1.347   -8.375  -4.148  1.00 19.85  ? 243 PHE A CE1 1 
ATOM   1699 C  CE2 . PHE A 1 263 ? -0.174  -9.668  -5.512  1.00 25.69  ? 243 PHE A CE2 1 
ATOM   1700 C  CZ  . PHE A 1 263 ? 0.066   -8.886  -4.385  1.00 26.52  ? 243 PHE A CZ  1 
ATOM   1701 N  N   . VAL A 1 264 ? 5.771   -8.054  -8.700  1.00 22.36  ? 244 VAL A N   1 
ATOM   1702 C  CA  . VAL A 1 264 ? 7.008   -8.183  -9.475  1.00 22.71  ? 244 VAL A CA  1 
ATOM   1703 C  C   . VAL A 1 264 ? 8.215   -8.137  -8.545  1.00 22.34  ? 244 VAL A C   1 
ATOM   1704 O  O   . VAL A 1 264 ? 8.275   -7.307  -7.636  1.00 24.60  ? 244 VAL A O   1 
ATOM   1705 C  CB  . VAL A 1 264 ? 7.110   -7.102  -10.572 1.00 26.59  ? 244 VAL A CB  1 
ATOM   1706 C  CG1 . VAL A 1 264 ? 6.861   -5.721  -10.000 1.00 28.17  ? 244 VAL A CG1 1 
ATOM   1707 C  CG2 . VAL A 1 264 ? 8.470   -7.162  -11.275 1.00 26.95  ? 244 VAL A CG2 1 
ATOM   1708 N  N   . ASP A 1 265 ? 9.164   -9.051  -8.747  1.00 25.13  ? 245 ASP A N   1 
ATOM   1709 C  CA  . ASP A 1 265 ? 10.432  -8.999  -8.025  1.00 24.33  ? 245 ASP A CA  1 
ATOM   1710 C  C   . ASP A 1 265 ? 11.336  -8.037  -8.783  1.00 29.59  ? 245 ASP A C   1 
ATOM   1711 O  O   . ASP A 1 265 ? 11.871  -8.370  -9.840  1.00 26.25  ? 245 ASP A O   1 
ATOM   1712 C  CB  . ASP A 1 265 ? 11.066  -10.380 -7.909  1.00 27.08  ? 245 ASP A CB  1 
ATOM   1713 C  CG  . ASP A 1 265 ? 12.339  -10.373 -7.077  1.00 37.66  ? 245 ASP A CG  1 
ATOM   1714 O  OD1 . ASP A 1 265 ? 12.809  -9.282  -6.661  1.00 32.75  ? 245 ASP A OD1 1 
ATOM   1715 O  OD2 . ASP A 1 265 ? 12.884  -11.474 -6.839  1.00 32.23  ? 245 ASP A OD2 1 
ATOM   1716 N  N   . GLU A 1 266 ? 11.485  -6.825  -8.254  1.00 25.89  ? 246 GLU A N   1 
ATOM   1717 C  CA  . GLU A 1 266 ? 12.263  -5.809  -8.947  1.00 24.60  ? 246 GLU A CA  1 
ATOM   1718 C  C   . GLU A 1 266 ? 13.760  -6.048  -8.859  1.00 27.78  ? 246 GLU A C   1 
ATOM   1719 O  O   . GLU A 1 266 ? 14.517  -5.377  -9.567  1.00 28.62  ? 246 GLU A O   1 
ATOM   1720 C  CB  . GLU A 1 266 ? 11.900  -4.432  -8.401  1.00 24.93  ? 246 GLU A CB  1 
ATOM   1721 C  CG  . GLU A 1 266 ? 10.458  -4.069  -8.740  1.00 23.47  ? 246 GLU A CG  1 
ATOM   1722 C  CD  . GLU A 1 266 ? 10.072  -2.660  -8.336  1.00 22.01  ? 246 GLU A CD  1 
ATOM   1723 O  OE1 . GLU A 1 266 ? 10.707  -2.096  -7.421  1.00 28.43  ? 246 GLU A OE1 1 
ATOM   1724 O  OE2 . GLU A 1 266 ? 9.121   -2.124  -8.951  1.00 25.30  ? 246 GLU A OE2 1 
ATOM   1725 N  N   . ALA A 1 267 ? 14.204  -6.973  -8.013  1.00 30.07  ? 247 ALA A N   1 
ATOM   1726 C  CA  . ALA A 1 267 ? 15.602  -7.396  -8.068  1.00 33.86  ? 247 ALA A CA  1 
ATOM   1727 C  C   . ALA A 1 267 ? 15.861  -8.350  -9.229  1.00 33.28  ? 247 ALA A C   1 
ATOM   1728 O  O   . ALA A 1 267 ? 16.940  -8.310  -9.832  1.00 38.10  ? 247 ALA A O   1 
ATOM   1729 C  CB  . ALA A 1 267 ? 16.013  -8.050  -6.746  1.00 41.86  ? 247 ALA A CB  1 
ATOM   1730 N  N   . ALA A 1 268 ? 14.887  -9.197  -9.568  1.00 31.91  ? 248 ALA A N   1 
ATOM   1731 C  CA  . ALA A 1 268 ? 15.066  -10.141 -10.665 1.00 38.05  ? 248 ALA A CA  1 
ATOM   1732 C  C   . ALA A 1 268 ? 14.915  -9.466  -12.021 1.00 35.48  ? 248 ALA A C   1 
ATOM   1733 O  O   . ALA A 1 268 ? 15.679  -9.759  -12.948 1.00 39.36  ? 248 ALA A O   1 
ATOM   1734 C  CB  . ALA A 1 268 ? 14.079  -11.302 -10.534 1.00 35.65  ? 248 ALA A CB  1 
ATOM   1735 N  N   . THR A 1 269 ? 13.956  -8.547  -12.156 1.00 32.79  ? 249 THR A N   1 
ATOM   1736 C  CA  . THR A 1 269 ? 13.746  -7.796  -13.394 1.00 35.79  ? 249 THR A CA  1 
ATOM   1737 C  C   . THR A 1 269 ? 13.757  -6.317  -13.022 1.00 30.31  ? 249 THR A C   1 
ATOM   1738 O  O   . THR A 1 269 ? 12.699  -5.724  -12.769 1.00 30.87  ? 249 THR A O   1 
ATOM   1739 C  CB  . THR A 1 269 ? 12.443  -8.196  -14.101 1.00 31.52  ? 249 THR A CB  1 
ATOM   1740 O  OG1 . THR A 1 269 ? 11.319  -7.985  -13.237 1.00 30.44  ? 249 THR A OG1 1 
ATOM   1741 C  CG2 . THR A 1 269 ? 12.468  -9.663  -14.519 1.00 31.47  ? 249 THR A CG2 1 
ATOM   1742 N  N   . PRO A 1 270 ? 14.940  -5.701  -12.968 1.00 32.14  ? 250 PRO A N   1 
ATOM   1743 C  CA  . PRO A 1 270 ? 15.057  -4.296  -12.534 1.00 29.10  ? 250 PRO A CA  1 
ATOM   1744 C  C   . PRO A 1 270 ? 14.184  -3.379  -13.366 1.00 30.17  ? 250 PRO A C   1 
ATOM   1745 O  O   . PRO A 1 270 ? 14.197  -3.445  -14.604 1.00 33.97  ? 250 PRO A O   1 
ATOM   1746 C  CB  . PRO A 1 270 ? 16.550  -3.989  -12.748 1.00 28.67  ? 250 PRO A CB  1 
ATOM   1747 C  CG  . PRO A 1 270 ? 17.195  -5.316  -12.567 1.00 31.34  ? 250 PRO A CG  1 
ATOM   1748 C  CD  . PRO A 1 270 ? 16.263  -6.294  -13.219 1.00 32.09  ? 250 PRO A CD  1 
ATOM   1749 N  N   . PRO A 1 271 ? 13.386  -2.531  -12.717 1.00 26.28  ? 251 PRO A N   1 
ATOM   1750 C  CA  . PRO A 1 271 ? 12.486  -1.587  -13.405 1.00 29.18  ? 251 PRO A CA  1 
ATOM   1751 C  C   . PRO A 1 271 ? 13.266  -0.354  -13.843 1.00 25.17  ? 251 PRO A C   1 
ATOM   1752 O  O   . PRO A 1 271 ? 13.084  0.767   -13.362 1.00 28.41  ? 251 PRO A O   1 
ATOM   1753 C  CB  . PRO A 1 271 ? 11.440  -1.297  -12.329 1.00 27.43  ? 251 PRO A CB  1 
ATOM   1754 C  CG  . PRO A 1 271 ? 12.220  -1.371  -11.065 1.00 36.33  ? 251 PRO A CG  1 
ATOM   1755 C  CD  . PRO A 1 271 ? 13.297  -2.402  -11.253 1.00 31.75  ? 251 PRO A CD  1 
ATOM   1756 N  N   . VAL A 1 272 ? 14.176  -0.583  -14.778 1.00 26.10  ? 252 VAL A N   1 
ATOM   1757 C  CA  . VAL A 1 272 ? 15.128  0.421   -15.232 1.00 27.13  ? 252 VAL A CA  1 
ATOM   1758 C  C   . VAL A 1 272 ? 14.950  0.595   -16.728 1.00 33.75  ? 252 VAL A C   1 
ATOM   1759 O  O   . VAL A 1 272 ? 14.940  -0.393  -17.473 1.00 33.93  ? 252 VAL A O   1 
ATOM   1760 C  CB  . VAL A 1 272 ? 16.572  0.012   -14.896 1.00 28.59  ? 252 VAL A CB  1 
ATOM   1761 C  CG1 . VAL A 1 272 ? 17.569  0.956   -15.566 1.00 29.86  ? 252 VAL A CG1 1 
ATOM   1762 C  CG2 . VAL A 1 272 ? 16.776  0.001   -13.388 1.00 32.56  ? 252 VAL A CG2 1 
ATOM   1763 N  N   . VAL A 1 273 ? 14.807  1.846   -17.163 1.00 31.28  ? 253 VAL A N   1 
ATOM   1764 C  CA  . VAL A 1 273 ? 14.733  2.181   -18.583 1.00 37.15  ? 253 VAL A CA  1 
ATOM   1765 C  C   . VAL A 1 273 ? 16.164  2.182   -19.110 1.00 42.49  ? 253 VAL A C   1 
ATOM   1766 O  O   . VAL A 1 273 ? 16.907  3.146   -18.910 1.00 38.22  ? 253 VAL A O   1 
ATOM   1767 C  CB  . VAL A 1 273 ? 14.050  3.529   -18.819 1.00 37.91  ? 253 VAL A CB  1 
ATOM   1768 C  CG1 . VAL A 1 273 ? 13.988  3.840   -20.310 1.00 41.16  ? 253 VAL A CG1 1 
ATOM   1769 C  CG2 . VAL A 1 273 ? 12.665  3.548   -18.197 1.00 33.55  ? 253 VAL A CG2 1 
ATOM   1770 N  N   . ASN A 1 274 ? 16.560  1.110   -19.774 1.00 34.93  ? 254 ASN A N   1 
ATOM   1771 C  CA  . ASN A 1 274 ? 17.932  1.023   -20.247 1.00 40.66  ? 254 ASN A CA  1 
ATOM   1772 C  C   . ASN A 1 274 ? 18.138  2.027   -21.374 1.00 43.56  ? 254 ASN A C   1 
ATOM   1773 O  O   . ASN A 1 274 ? 17.492  1.909   -22.424 1.00 45.00  ? 254 ASN A O   1 
ATOM   1774 C  CB  . ASN A 1 274 ? 18.260  -0.397  -20.707 1.00 41.53  ? 254 ASN A CB  1 
ATOM   1775 C  CG  . ASN A 1 274 ? 19.752  -0.613  -20.916 1.00 49.20  ? 254 ASN A CG  1 
ATOM   1776 O  OD1 . ASN A 1 274 ? 20.447  0.248   -21.454 1.00 47.00  ? 254 ASN A OD1 1 
ATOM   1777 N  ND2 . ASN A 1 274 ? 20.252  -1.766  -20.480 1.00 48.60  ? 254 ASN A ND2 1 
ATOM   1778 N  N   . PRO A 1 275 ? 19.017  3.023   -21.204 1.00 43.75  ? 255 PRO A N   1 
ATOM   1779 C  CA  . PRO A 1 275 ? 19.206  4.039   -22.252 1.00 42.22  ? 255 PRO A CA  1 
ATOM   1780 C  C   . PRO A 1 275 ? 19.873  3.507   -23.509 1.00 55.54  ? 255 PRO A C   1 
ATOM   1781 O  O   . PRO A 1 275 ? 19.897  4.222   -24.521 1.00 47.91  ? 255 PRO A O   1 
ATOM   1782 C  CB  . PRO A 1 275 ? 20.092  5.085   -21.561 1.00 42.18  ? 255 PRO A CB  1 
ATOM   1783 C  CG  . PRO A 1 275 ? 20.887  4.272   -20.554 1.00 42.37  ? 255 PRO A CG  1 
ATOM   1784 C  CD  . PRO A 1 275 ? 19.899  3.246   -20.045 1.00 40.65  ? 255 PRO A CD  1 
ATOM   1785 N  N   . SER A 1 276 ? 20.430  2.297   -23.471 1.00 50.14  ? 256 SER A N   1 
ATOM   1786 C  CA  . SER A 1 276 ? 21.038  1.664   -24.634 1.00 51.03  ? 256 SER A CA  1 
ATOM   1787 C  C   . SER A 1 276 ? 20.056  0.793   -25.409 1.00 62.09  ? 256 SER A C   1 
ATOM   1788 O  O   . SER A 1 276 ? 20.427  0.236   -26.447 1.00 69.15  ? 256 SER A O   1 
ATOM   1789 C  CB  . SER A 1 276 ? 22.241  0.818   -24.204 1.00 53.13  ? 256 SER A CB  1 
ATOM   1790 O  OG  . SER A 1 276 ? 23.305  1.633   -23.738 1.00 55.25  ? 256 SER A OG  1 
ATOM   1791 N  N   . VAL A 1 277 ? 18.822  0.668   -24.935 1.00 53.81  ? 257 VAL A N   1 
ATOM   1792 C  CA  . VAL A 1 277 ? 17.812  -0.195  -25.537 1.00 62.40  ? 257 VAL A CA  1 
ATOM   1793 C  C   . VAL A 1 277 ? 16.726  0.694   -26.127 1.00 65.36  ? 257 VAL A C   1 
ATOM   1794 O  O   . VAL A 1 277 ? 16.135  1.518   -25.418 1.00 66.57  ? 257 VAL A O   1 
ATOM   1795 C  CB  . VAL A 1 277 ? 17.228  -1.179  -24.511 1.00 60.55  ? 257 VAL A CB  1 
ATOM   1796 C  CG1 . VAL A 1 277 ? 16.083  -1.974  -25.122 1.00 68.72  ? 257 VAL A CG1 1 
ATOM   1797 C  CG2 . VAL A 1 277 ? 18.319  -2.109  -23.985 1.00 61.10  ? 257 VAL A CG2 1 
ATOM   1798 N  N   . ASN A 1 278 ? 16.467  0.531   -27.421 1.00 64.96  ? 258 ASN A N   1 
ATOM   1799 C  CA  . ASN A 1 278 ? 15.464  1.326   -28.114 1.00 67.32  ? 258 ASN A CA  1 
ATOM   1800 C  C   . ASN A 1 278 ? 14.129  0.587   -28.151 1.00 65.13  ? 258 ASN A C   1 
ATOM   1801 O  O   . ASN A 1 278 ? 14.048  -0.615  -27.891 1.00 63.44  ? 258 ASN A O   1 
ATOM   1802 C  CB  . ASN A 1 278 ? 15.930  1.657   -29.535 1.00 62.88  ? 258 ASN A CB  1 
ATOM   1803 C  CG  . ASN A 1 278 ? 17.301  2.317   -29.563 1.00 74.40  ? 258 ASN A CG  1 
ATOM   1804 O  OD1 . ASN A 1 278 ? 17.696  3.001   -28.616 1.00 71.47  ? 258 ASN A OD1 1 
ATOM   1805 N  ND2 . ASN A 1 278 ? 18.035  2.113   -30.652 1.00 71.38  ? 258 ASN A ND2 1 
ATOM   1806 N  N   . GLY A 1 279 ? 13.073  1.330   -28.475 1.00 67.53  ? 259 GLY A N   1 
ATOM   1807 C  CA  . GLY A 1 279 ? 11.737  0.778   -28.558 1.00 61.75  ? 259 GLY A CA  1 
ATOM   1808 C  C   . GLY A 1 279 ? 10.947  0.957   -27.273 1.00 63.10  ? 259 GLY A C   1 
ATOM   1809 O  O   . GLY A 1 279 ? 11.462  1.369   -26.232 1.00 60.33  ? 259 GLY A O   1 
ATOM   1810 N  N   . SER A 1 280 ? 9.653   0.644   -27.360 1.00 78.40  ? 260 SER A N   1 
ATOM   1811 C  CA  . SER A 1 280 ? 8.787   0.728   -26.191 1.00 66.39  ? 260 SER A CA  1 
ATOM   1812 C  C   . SER A 1 280 ? 9.304   -0.191  -25.090 1.00 57.61  ? 260 SER A C   1 
ATOM   1813 O  O   . SER A 1 280 ? 9.926   -1.224  -25.355 1.00 57.44  ? 260 SER A O   1 
ATOM   1814 C  CB  . SER A 1 280 ? 7.346   0.360   -26.556 1.00 62.27  ? 260 SER A CB  1 
ATOM   1815 O  OG  . SER A 1 280 ? 7.254   -0.984  -26.989 1.00 72.42  ? 260 SER A OG  1 
ATOM   1816 N  N   . LEU A 1 281 ? 9.055   0.202   -23.845 1.00 44.64  ? 261 LEU A N   1 
ATOM   1817 C  CA  . LEU A 1 281 ? 9.632   -0.520  -22.720 1.00 38.87  ? 261 LEU A CA  1 
ATOM   1818 C  C   . LEU A 1 281 ? 9.072   -1.936  -22.660 1.00 37.16  ? 261 LEU A C   1 
ATOM   1819 O  O   . LEU A 1 281 ? 7.847   -2.121  -22.733 1.00 45.38  ? 261 LEU A O   1 
ATOM   1820 C  CB  . LEU A 1 281 ? 9.361   0.198   -21.401 1.00 31.92  ? 261 LEU A CB  1 
ATOM   1821 C  CG  . LEU A 1 281 ? 10.066  1.529   -21.202 1.00 41.38  ? 261 LEU A CG  1 
ATOM   1822 C  CD1 . LEU A 1 281 ? 9.770   2.054   -19.817 1.00 39.14  ? 261 LEU A CD1 1 
ATOM   1823 C  CD2 . LEU A 1 281 ? 11.558  1.336   -21.409 1.00 32.30  ? 261 LEU A CD2 1 
ATOM   1824 N  N   . PRO A 1 282 ? 9.924   -2.951  -22.529 1.00 33.51  ? 262 PRO A N   1 
ATOM   1825 C  CA  . PRO A 1 282 ? 9.422   -4.316  -22.410 1.00 36.64  ? 262 PRO A CA  1 
ATOM   1826 C  C   . PRO A 1 282 ? 8.771   -4.530  -21.058 1.00 38.42  ? 262 PRO A C   1 
ATOM   1827 O  O   . PRO A 1 282 ? 9.134   -3.870  -20.068 1.00 32.43  ? 262 PRO A O   1 
ATOM   1828 C  CB  . PRO A 1 282 ? 10.694  -5.169  -22.551 1.00 44.08  ? 262 PRO A CB  1 
ATOM   1829 C  CG  . PRO A 1 282 ? 11.773  -4.266  -22.029 1.00 45.99  ? 262 PRO A CG  1 
ATOM   1830 C  CD  . PRO A 1 282 ? 11.395  -2.892  -22.501 1.00 35.51  ? 262 PRO A CD  1 
ATOM   1831 N  N   . PRO A 1 283 ? 7.818   -5.456  -20.957 1.00 37.45  ? 263 PRO A N   1 
ATOM   1832 C  CA  . PRO A 1 283 ? 7.227   -5.749  -19.651 1.00 28.88  ? 263 PRO A CA  1 
ATOM   1833 C  C   . PRO A 1 283 ? 8.263   -6.366  -18.723 1.00 27.11  ? 263 PRO A C   1 
ATOM   1834 O  O   . PRO A 1 283 ? 9.278   -6.927  -19.146 1.00 31.25  ? 263 PRO A O   1 
ATOM   1835 C  CB  . PRO A 1 283 ? 6.104   -6.742  -19.980 1.00 30.46  ? 263 PRO A CB  1 
ATOM   1836 C  CG  . PRO A 1 283 ? 6.630   -7.462  -21.205 1.00 34.18  ? 263 PRO A CG  1 
ATOM   1837 C  CD  . PRO A 1 283 ? 7.333   -6.380  -21.999 1.00 40.69  ? 263 PRO A CD  1 
ATOM   1838 N  N   . LEU A 1 284 ? 8.005   -6.216  -17.431 1.00 27.40  ? 264 LEU A N   1 
ATOM   1839 C  CA  . LEU A 1 284 ? 8.849   -6.827  -16.423 1.00 25.40  ? 264 LEU A CA  1 
ATOM   1840 C  C   . LEU A 1 284 ? 8.328   -8.231  -16.152 1.00 31.55  ? 264 LEU A C   1 
ATOM   1841 O  O   . LEU A 1 284 ? 7.330   -8.676  -16.730 1.00 32.16  ? 264 LEU A O   1 
ATOM   1842 C  CB  . LEU A 1 284 ? 8.861   -5.962  -15.162 1.00 22.65  ? 264 LEU A CB  1 
ATOM   1843 C  CG  . LEU A 1 284 ? 9.447   -4.570  -15.468 1.00 25.87  ? 264 LEU A CG  1 
ATOM   1844 C  CD1 . LEU A 1 284 ? 9.128   -3.559  -14.372 1.00 26.46  ? 264 LEU A CD1 1 
ATOM   1845 C  CD2 . LEU A 1 284 ? 10.962  -4.658  -15.685 1.00 27.51  ? 264 LEU A CD2 1 
ATOM   1846 N  N   . GLY A 1 285 ? 8.991   -8.940  -15.257 1.00 28.09  ? 265 GLY A N   1 
ATOM   1847 C  CA  . GLY A 1 285 ? 8.434   -10.186 -14.787 1.00 27.01  ? 265 GLY A CA  1 
ATOM   1848 C  C   . GLY A 1 285 ? 7.166   -9.954  -13.998 1.00 29.96  ? 265 GLY A C   1 
ATOM   1849 O  O   . GLY A 1 285 ? 6.887   -8.858  -13.511 1.00 36.15  ? 265 GLY A O   1 
ATOM   1850 N  N   . GLU A 1 286 ? 6.337   -10.984 -13.927 1.00 27.54  ? 266 GLU A N   1 
ATOM   1851 C  CA  . GLU A 1 286 ? 5.226   -10.982 -13.000 1.00 21.89  ? 266 GLU A CA  1 
ATOM   1852 C  C   . GLU A 1 286 ? 5.198   -12.326 -12.287 1.00 25.93  ? 266 GLU A C   1 
ATOM   1853 O  O   . GLU A 1 286 ? 5.205   -13.373 -12.942 1.00 27.47  ? 266 GLU A O   1 
ATOM   1854 C  CB  . GLU A 1 286 ? 3.893   -10.706 -13.724 1.00 27.40  ? 266 GLU A CB  1 
ATOM   1855 C  CG  . GLU A 1 286 ? 2.697   -11.067 -12.911 1.00 27.16  ? 266 GLU A CG  1 
ATOM   1856 C  CD  . GLU A 1 286 ? 1.427   -10.395 -13.379 1.00 22.40  ? 266 GLU A CD  1 
ATOM   1857 O  OE1 . GLU A 1 286 ? 1.310   -10.064 -14.576 1.00 24.46  ? 266 GLU A OE1 1 
ATOM   1858 O  OE2 . GLU A 1 286 ? 0.539   -10.217 -12.529 1.00 24.84  ? 266 GLU A OE2 1 
ATOM   1859 N  N   . LEU A 1 287 ? 5.178   -12.295 -10.953 1.00 22.46  ? 267 LEU A N   1 
ATOM   1860 C  CA  . LEU A 1 287 ? 5.095   -13.531 -10.183 1.00 25.19  ? 267 LEU A CA  1 
ATOM   1861 C  C   . LEU A 1 287 ? 3.829   -14.290 -10.571 1.00 23.68  ? 267 LEU A C   1 
ATOM   1862 O  O   . LEU A 1 287 ? 2.738   -13.690 -10.620 1.00 24.70  ? 267 LEU A O   1 
ATOM   1863 C  CB  . LEU A 1 287 ? 5.083   -13.246 -8.681  1.00 28.12  ? 267 LEU A CB  1 
ATOM   1864 C  CG  . LEU A 1 287 ? 6.342   -12.734 -7.987  1.00 29.67  ? 267 LEU A CG  1 
ATOM   1865 C  CD1 . LEU A 1 287 ? 6.128   -12.741 -6.485  1.00 32.81  ? 267 LEU A CD1 1 
ATOM   1866 C  CD2 . LEU A 1 287 ? 7.526   -13.596 -8.359  1.00 32.39  ? 267 LEU A CD2 1 
ATOM   1867 N  N   . PRO A 1 288 ? 3.921   -15.589 -10.854 1.00 26.78  ? 268 PRO A N   1 
ATOM   1868 C  CA  . PRO A 1 288 ? 2.710   -16.339 -11.229 1.00 30.74  ? 268 PRO A CA  1 
ATOM   1869 C  C   . PRO A 1 288 ? 1.661   -16.370 -10.134 1.00 30.86  ? 268 PRO A C   1 
ATOM   1870 O  O   . PRO A 1 288 ? 0.466   -16.484 -10.436 1.00 32.46  ? 268 PRO A O   1 
ATOM   1871 C  CB  . PRO A 1 288 ? 3.246   -17.748 -11.546 1.00 32.42  ? 268 PRO A CB  1 
ATOM   1872 C  CG  . PRO A 1 288 ? 4.619   -17.804 -10.987 1.00 37.00  ? 268 PRO A CG  1 
ATOM   1873 C  CD  . PRO A 1 288 ? 5.146   -16.401 -10.959 1.00 28.53  ? 268 PRO A CD  1 
ATOM   1874 N  N   . THR A 1 289 ? 2.070   -16.258 -8.871  1.00 37.60  ? 269 THR A N   1 
ATOM   1875 C  CA  . THR A 1 289 ? 1.176   -16.317 -7.722  1.00 43.41  ? 269 THR A CA  1 
ATOM   1876 C  C   . THR A 1 289 ? 1.579   -15.217 -6.750  1.00 44.49  ? 269 THR A C   1 
ATOM   1877 O  O   . THR A 1 289 ? 2.752   -14.840 -6.677  1.00 38.25  ? 269 THR A O   1 
ATOM   1878 C  CB  . THR A 1 289 ? 1.239   -17.700 -7.030  1.00 44.32  ? 269 THR A CB  1 
ATOM   1879 O  OG1 . THR A 1 289 ? 0.838   -18.726 -7.949  1.00 56.11  ? 269 THR A OG1 1 
ATOM   1880 C  CG2 . THR A 1 289 ? 0.339   -17.766 -5.803  1.00 55.20  ? 269 THR A CG2 1 
ATOM   1881 N  N   . SER A 1 290 ? 0.609   -14.703 -6.005  1.00 33.23  ? 270 SER A N   1 
ATOM   1882 C  CA  . SER A 1 290 ? 0.916   -13.702 -4.995  1.00 29.41  ? 270 SER A CA  1 
ATOM   1883 C  C   . SER A 1 290 ? 1.860   -14.280 -3.940  1.00 26.40  ? 270 SER A C   1 
ATOM   1884 O  O   . SER A 1 290 ? 1.751   -15.460 -3.583  1.00 29.67  ? 270 SER A O   1 
ATOM   1885 C  CB  . SER A 1 290 ? -0.362  -13.209 -4.316  1.00 28.90  ? 270 SER A CB  1 
ATOM   1886 O  OG  . SER A 1 290 ? -0.034  -12.438 -3.175  1.00 32.89  ? 270 SER A OG  1 
ATOM   1887 N  N   . PRO A 1 291 ? 2.805   -13.488 -3.426  1.00 28.28  ? 271 PRO A N   1 
ATOM   1888 C  CA  . PRO A 1 291 ? 3.645   -13.980 -2.328  1.00 28.48  ? 271 PRO A CA  1 
ATOM   1889 C  C   . PRO A 1 291 ? 2.899   -14.146 -1.018  1.00 31.92  ? 271 PRO A C   1 
ATOM   1890 O  O   . PRO A 1 291 ? 3.394   -14.842 -0.125  1.00 34.22  ? 271 PRO A O   1 
ATOM   1891 C  CB  . PRO A 1 291 ? 4.743   -12.910 -2.214  1.00 37.47  ? 271 PRO A CB  1 
ATOM   1892 C  CG  . PRO A 1 291 ? 4.145   -11.698 -2.783  1.00 34.15  ? 271 PRO A CG  1 
ATOM   1893 C  CD  . PRO A 1 291 ? 3.205   -12.138 -3.867  1.00 33.72  ? 271 PRO A CD  1 
ATOM   1894 N  N   . ASP A 1 292 ? 1.733   -13.532 -0.874  1.00 28.64  ? 272 ASP A N   1 
ATOM   1895 C  CA  . ASP A 1 292 ? 0.958   -13.579 0.363   1.00 29.62  ? 272 ASP A CA  1 
ATOM   1896 C  C   . ASP A 1 292 ? -0.456  -14.005 0.004   1.00 28.58  ? 272 ASP A C   1 
ATOM   1897 O  O   . ASP A 1 292 ? -1.173  -13.246 -0.680  1.00 30.51  ? 272 ASP A O   1 
ATOM   1898 C  CB  . ASP A 1 292 ? 0.976   -12.215 1.049   1.00 30.32  ? 272 ASP A CB  1 
ATOM   1899 C  CG  . ASP A 1 292 ? 0.218   -12.199 2.367   1.00 36.52  ? 272 ASP A CG  1 
ATOM   1900 O  OD1 . ASP A 1 292 ? -0.495  -13.178 2.678   1.00 30.76  ? 272 ASP A OD1 1 
ATOM   1901 O  OD2 . ASP A 1 292 ? 0.341   -11.196 3.105   1.00 31.96  ? 272 ASP A OD2 1 
ATOM   1902 N  N   . PRO A 1 293 ? -0.905  -15.188 0.428   1.00 30.33  ? 273 PRO A N   1 
ATOM   1903 C  CA  . PRO A 1 293 ? -2.265  -15.610 0.072   1.00 29.82  ? 273 PRO A CA  1 
ATOM   1904 C  C   . PRO A 1 293 ? -3.336  -14.669 0.588   1.00 36.63  ? 273 PRO A C   1 
ATOM   1905 O  O   . PRO A 1 293 ? -4.442  -14.674 0.045   1.00 30.75  ? 273 PRO A O   1 
ATOM   1906 C  CB  . PRO A 1 293 ? -2.382  -17.002 0.708   1.00 29.87  ? 273 PRO A CB  1 
ATOM   1907 C  CG  . PRO A 1 293 ? -1.378  -16.999 1.815   1.00 32.32  ? 273 PRO A CG  1 
ATOM   1908 C  CD  . PRO A 1 293 ? -0.235  -16.159 1.310   1.00 25.94  ? 273 PRO A CD  1 
ATOM   1909 N  N   . LYS A 1 294 ? -3.040  -13.851 1.598   1.00 29.40  ? 274 LYS A N   1 
ATOM   1910 C  CA  . LYS A 1 294 ? -4.034  -12.927 2.129   1.00 32.73  ? 274 LYS A CA  1 
ATOM   1911 C  C   . LYS A 1 294 ? -4.163  -11.651 1.309   1.00 30.59  ? 274 LYS A C   1 
ATOM   1912 O  O   . LYS A 1 294 ? -5.074  -10.863 1.568   1.00 29.07  ? 274 LYS A O   1 
ATOM   1913 C  CB  . LYS A 1 294 ? -3.698  -12.566 3.579   1.00 32.79  ? 274 LYS A CB  1 
ATOM   1914 C  CG  . LYS A 1 294 ? -3.783  -13.732 4.560   1.00 34.16  ? 274 LYS A CG  1 
ATOM   1915 C  CD  . LYS A 1 294 ? -3.388  -13.292 5.966   1.00 40.60  ? 274 LYS A CD  1 
ATOM   1916 C  CE  . LYS A 1 294 ? -3.875  -14.271 7.025   1.00 49.74  ? 274 LYS A CE  1 
ATOM   1917 N  NZ  . LYS A 1 294 ? -3.340  -13.942 8.376   1.00 65.60  ? 274 LYS A NZ  1 
ATOM   1918 N  N   . ALA A 1 295 ? -3.280  -11.411 0.345   1.00 26.45  ? 275 ALA A N   1 
ATOM   1919 C  CA  . ALA A 1 295 ? -3.420  -10.224 -0.484  1.00 23.85  ? 275 ALA A CA  1 
ATOM   1920 C  C   . ALA A 1 295 ? -4.655  -10.348 -1.368  1.00 25.84  ? 275 ALA A C   1 
ATOM   1921 O  O   . ALA A 1 295 ? -5.005  -11.440 -1.824  1.00 27.69  ? 275 ALA A O   1 
ATOM   1922 C  CB  . ALA A 1 295 ? -2.171  -10.015 -1.345  1.00 25.55  ? 275 ALA A CB  1 
ATOM   1923 N  N   . GLY A 1 296 ? -5.324  -9.227  -1.597  1.00 26.72  ? 276 GLY A N   1 
ATOM   1924 C  CA  . GLY A 1 296 ? -6.397  -9.186  -2.559  1.00 25.32  ? 276 GLY A CA  1 
ATOM   1925 C  C   . GLY A 1 296 ? -7.539  -8.319  -2.075  1.00 24.29  ? 276 GLY A C   1 
ATOM   1926 O  O   . GLY A 1 296 ? -7.402  -7.529  -1.143  1.00 21.69  ? 276 GLY A O   1 
ATOM   1927 N  N   . LEU A 1 297 ? -8.679  -8.495  -2.728  1.00 20.11  ? 277 LEU A N   1 
ATOM   1928 C  CA  . LEU A 1 297 ? -9.868  -7.688  -2.479  1.00 19.45  ? 277 LEU A CA  1 
ATOM   1929 C  C   . LEU A 1 297 ? -10.757 -8.356  -1.438  1.00 20.03  ? 277 LEU A C   1 
ATOM   1930 O  O   . LEU A 1 297 ? -11.000 -9.561  -1.505  1.00 25.30  ? 277 LEU A O   1 
ATOM   1931 C  CB  . LEU A 1 297 ? -10.627 -7.500  -3.784  1.00 21.69  ? 277 LEU A CB  1 
ATOM   1932 C  CG  . LEU A 1 297 ? -11.982 -6.800  -3.734  1.00 21.22  ? 277 LEU A CG  1 
ATOM   1933 C  CD1 . LEU A 1 297 ? -11.908 -5.376  -3.146  1.00 20.47  ? 277 LEU A CD1 1 
ATOM   1934 C  CD2 . LEU A 1 297 ? -12.532 -6.770  -5.140  1.00 25.42  ? 277 LEU A CD2 1 
ATOM   1935 N  N   . TYR A 1 298 ? -11.221 -7.579  -0.470  1.00 18.59  ? 278 TYR A N   1 
ATOM   1936 C  CA  . TYR A 1 298 ? -12.085 -8.060  0.596   1.00 19.77  ? 278 TYR A CA  1 
ATOM   1937 C  C   . TYR A 1 298 ? -13.376 -7.266  0.561   1.00 21.43  ? 278 TYR A C   1 
ATOM   1938 O  O   . TYR A 1 298 ? -13.353 -6.044  0.398   1.00 19.99  ? 278 TYR A O   1 
ATOM   1939 C  CB  . TYR A 1 298 ? -11.415 -7.918  1.961   1.00 19.67  ? 278 TYR A CB  1 
ATOM   1940 C  CG  . TYR A 1 298 ? -10.299 -8.920  2.154   1.00 20.31  ? 278 TYR A CG  1 
ATOM   1941 C  CD1 . TYR A 1 298 ? -9.044  -8.712  1.594   1.00 22.10  ? 278 TYR A CD1 1 
ATOM   1942 C  CD2 . TYR A 1 298 ? -10.507 -10.086 2.868   1.00 21.51  ? 278 TYR A CD2 1 
ATOM   1943 C  CE1 . TYR A 1 298 ? -8.025  -9.643  1.761   1.00 21.27  ? 278 TYR A CE1 1 
ATOM   1944 C  CE2 . TYR A 1 298 ? -9.491  -11.016 3.041   1.00 24.61  ? 278 TYR A CE2 1 
ATOM   1945 C  CZ  . TYR A 1 298 ? -8.263  -10.793 2.485   1.00 25.59  ? 278 TYR A CZ  1 
ATOM   1946 O  OH  . TYR A 1 298 ? -7.256  -11.722 2.652   1.00 29.36  ? 278 TYR A OH  1 
ATOM   1947 N  N   . ILE A 1 299 ? -14.499 -7.963  0.694   1.00 19.77  ? 279 ILE A N   1 
ATOM   1948 C  CA  . ILE A 1 299 ? -15.817 -7.360  0.529   1.00 20.67  ? 279 ILE A CA  1 
ATOM   1949 C  C   . ILE A 1 299 ? -16.690 -7.780  1.702   1.00 24.71  ? 279 ILE A C   1 
ATOM   1950 O  O   . ILE A 1 299 ? -16.672 -8.946  2.116   1.00 22.70  ? 279 ILE A O   1 
ATOM   1951 C  CB  . ILE A 1 299 ? -16.462 -7.767  -0.817  1.00 20.37  ? 279 ILE A CB  1 
ATOM   1952 C  CG1 . ILE A 1 299 ? -15.535 -7.399  -1.981  1.00 20.98  ? 279 ILE A CG1 1 
ATOM   1953 C  CG2 . ILE A 1 299 ? -17.844 -7.117  -0.994  1.00 22.05  ? 279 ILE A CG2 1 
ATOM   1954 C  CD1 . ILE A 1 299 ? -16.101 -7.711  -3.331  1.00 25.67  ? 279 ILE A CD1 1 
ATOM   1955 N  N   . LYS A 1 300 ? -17.449 -6.828  2.247   1.00 22.51  ? 280 LYS A N   1 
ATOM   1956 C  CA  . LYS A 1 300 ? -18.402 -7.140  3.299   1.00 27.98  ? 280 LYS A CA  1 
ATOM   1957 C  C   . LYS A 1 300 ? -19.625 -7.794  2.668   1.00 26.08  ? 280 LYS A C   1 
ATOM   1958 O  O   . LYS A 1 300 ? -20.316 -7.170  1.862   1.00 28.82  ? 280 LYS A O   1 
ATOM   1959 C  CB  . LYS A 1 300 ? -18.798 -5.876  4.059   1.00 35.10  ? 280 LYS A CB  1 
ATOM   1960 C  CG  . LYS A 1 300 ? -17.727 -5.340  4.997   1.00 41.35  ? 280 LYS A CG  1 
ATOM   1961 C  CD  . LYS A 1 300 ? -18.277 -4.173  5.816   1.00 67.03  ? 280 LYS A CD  1 
ATOM   1962 C  CE  . LYS A 1 300 ? -17.362 -3.800  6.974   1.00 72.16  ? 280 LYS A CE  1 
ATOM   1963 N  NZ  . LYS A 1 300 ? -17.821 -2.549  7.646   1.00 70.60  ? 280 LYS A NZ  1 
ATOM   1964 N  N   . SER A 1 301 ? -19.878 -9.049  3.013   1.00 28.22  ? 281 SER A N   1 
ATOM   1965 C  CA  . SER A 1 301 ? -20.964 -9.805  2.408   1.00 34.17  ? 281 SER A CA  1 
ATOM   1966 C  C   . SER A 1 301 ? -22.216 -9.750  3.272   1.00 29.72  ? 281 SER A C   1 
ATOM   1967 O  O   . SER A 1 301 ? -22.189 -9.347  4.436   1.00 27.84  ? 281 SER A O   1 
ATOM   1968 C  CB  . SER A 1 301 ? -20.546 -11.257 2.193   1.00 34.66  ? 281 SER A CB  1 
ATOM   1969 O  OG  . SER A 1 301 ? -20.521 -11.935 3.430   1.00 40.62  ? 281 SER A OG  1 
ATOM   1970 N  N   . ARG A 1 302 ? -23.324 -10.215 2.689   1.00 31.41  ? 282 ARG A N   1 
ATOM   1971 C  CA  . ARG A 1 302 ? -24.616 -10.156 3.367   1.00 35.15  ? 282 ARG A CA  1 
ATOM   1972 C  C   . ARG A 1 302 ? -24.663 -11.014 4.626   1.00 36.22  ? 282 ARG A C   1 
ATOM   1973 O  O   . ARG A 1 302 ? -25.526 -10.790 5.483   1.00 35.76  ? 282 ARG A O   1 
ATOM   1974 C  CB  . ARG A 1 302 ? -25.721 -10.586 2.398   1.00 37.15  ? 282 ARG A CB  1 
ATOM   1975 C  CG  . ARG A 1 302 ? -25.788 -12.088 2.166   1.00 40.35  ? 282 ARG A CG  1 
ATOM   1976 C  CD  . ARG A 1 302 ? -26.876 -12.446 1.165   1.00 40.81  ? 282 ARG A CD  1 
ATOM   1977 N  NE  . ARG A 1 302 ? -28.164 -11.852 1.511   1.00 48.14  ? 282 ARG A NE  1 
ATOM   1978 C  CZ  . ARG A 1 302 ? -29.140 -12.478 2.154   1.00 42.20  ? 282 ARG A CZ  1 
ATOM   1979 N  NH1 . ARG A 1 302 ? -29.014 -13.732 2.564   1.00 45.34  ? 282 ARG A NH1 1 
ATOM   1980 N  NH2 . ARG A 1 302 ? -30.280 -11.832 2.387   1.00 48.32  ? 282 ARG A NH2 1 
ATOM   1981 N  N   . THR A 1 303 ? -23.770 -11.995 4.756   1.00 32.16  ? 283 THR A N   1 
ATOM   1982 C  CA  . THR A 1 303 ? -23.720 -12.843 5.940   1.00 31.49  ? 283 THR A CA  1 
ATOM   1983 C  C   . THR A 1 303 ? -23.049 -12.174 7.125   1.00 39.64  ? 283 THR A C   1 
ATOM   1984 O  O   . THR A 1 303 ? -23.069 -12.741 8.220   1.00 44.42  ? 283 THR A O   1 
ATOM   1985 C  CB  . THR A 1 303 ? -22.954 -14.135 5.650   1.00 41.14  ? 283 THR A CB  1 
ATOM   1986 O  OG1 . THR A 1 303 ? -21.614 -13.804 5.267   1.00 34.59  ? 283 THR A OG1 1 
ATOM   1987 C  CG2 . THR A 1 303 ? -23.604 -14.918 4.535   1.00 39.04  ? 283 THR A CG2 1 
ATOM   1988 N  N   . GLY A 1 304 ? -22.430 -11.011 6.932   1.00 34.34  ? 284 GLY A N   1 
ATOM   1989 C  CA  . GLY A 1 304 ? -21.549 -10.455 7.930   1.00 39.30  ? 284 GLY A CA  1 
ATOM   1990 C  C   . GLY A 1 304 ? -20.116 -10.929 7.824   1.00 40.44  ? 284 GLY A C   1 
ATOM   1991 O  O   . GLY A 1 304 ? -19.244 -10.374 8.508   1.00 39.49  ? 284 GLY A O   1 
ATOM   1992 N  N   . GLN A 1 305 ? -19.847 -11.951 7.012   1.00 32.22  ? 285 GLN A N   1 
ATOM   1993 C  CA  . GLN A 1 305 ? -18.470 -12.339 6.728   1.00 35.84  ? 285 GLN A CA  1 
ATOM   1994 C  C   . GLN A 1 305 ? -17.797 -11.306 5.843   1.00 26.28  ? 285 GLN A C   1 
ATOM   1995 O  O   . GLN A 1 305 ? -18.409 -10.745 4.929   1.00 27.79  ? 285 GLN A O   1 
ATOM   1996 C  CB  . GLN A 1 305 ? -18.403 -13.681 6.004   1.00 32.93  ? 285 GLN A CB  1 
ATOM   1997 C  CG  . GLN A 1 305 ? -19.002 -14.871 6.693   1.00 30.43  ? 285 GLN A CG  1 
ATOM   1998 C  CD  . GLN A 1 305 ? -19.180 -16.023 5.718   1.00 35.87  ? 285 GLN A CD  1 
ATOM   1999 O  OE1 . GLN A 1 305 ? -18.454 -17.018 5.768   1.00 37.28  ? 285 GLN A OE1 1 
ATOM   2000 N  NE2 . GLN A 1 305 ? -20.147 -15.883 4.812   1.00 35.00  ? 285 GLN A NE2 1 
ATOM   2001 N  N   . THR A 1 306 ? -16.520 -11.080 6.090   1.00 26.77  ? 286 THR A N   1 
ATOM   2002 C  CA  . THR A 1 306 ? -15.684 -10.351 5.149   1.00 25.98  ? 286 THR A CA  1 
ATOM   2003 C  C   . THR A 1 306 ? -14.983 -11.369 4.255   1.00 26.49  ? 286 THR A C   1 
ATOM   2004 O  O   . THR A 1 306 ? -14.202 -12.191 4.739   1.00 34.83  ? 286 THR A O   1 
ATOM   2005 C  CB  . THR A 1 306 ? -14.681 -9.477  5.894   1.00 31.38  ? 286 THR A CB  1 
ATOM   2006 O  OG1 . THR A 1 306 ? -15.404 -8.577  6.749   1.00 36.68  ? 286 THR A OG1 1 
ATOM   2007 C  CG2 . THR A 1 306 ? -13.850 -8.683  4.912   1.00 26.49  ? 286 THR A CG2 1 
ATOM   2008 N  N   . VAL A 1 307 ? -15.287 -11.330 2.961   1.00 22.51  ? 287 VAL A N   1 
ATOM   2009 C  CA  . VAL A 1 307 ? -14.914 -12.393 2.039   1.00 25.79  ? 287 VAL A CA  1 
ATOM   2010 C  C   . VAL A 1 307 ? -13.820 -11.905 1.100   1.00 23.06  ? 287 VAL A C   1 
ATOM   2011 O  O   . VAL A 1 307 ? -13.767 -10.733 0.721   1.00 23.98  ? 287 VAL A O   1 
ATOM   2012 C  CB  . VAL A 1 307 ? -16.149 -12.902 1.259   1.00 23.47  ? 287 VAL A CB  1 
ATOM   2013 C  CG1 . VAL A 1 307 ? -17.220 -13.410 2.242   1.00 23.66  ? 287 VAL A CG1 1 
ATOM   2014 C  CG2 . VAL A 1 307 ? -16.740 -11.808 0.373   1.00 23.97  ? 287 VAL A CG2 1 
ATOM   2015 N  N   . GLN A 1 308 ? -12.940 -12.821 0.719   1.00 22.38  ? 288 GLN A N   1 
ATOM   2016 C  CA  . GLN A 1 308 ? -11.873 -12.524 -0.224  1.00 20.88  ? 288 GLN A CA  1 
ATOM   2017 C  C   . GLN A 1 308 ? -12.342 -12.868 -1.627  1.00 24.40  ? 288 GLN A C   1 
ATOM   2018 O  O   . GLN A 1 308 ? -12.889 -13.947 -1.856  1.00 28.32  ? 288 GLN A O   1 
ATOM   2019 C  CB  . GLN A 1 308 ? -10.610 -13.317 0.125   1.00 22.26  ? 288 GLN A CB  1 
ATOM   2020 C  CG  . GLN A 1 308 ? -9.391  -12.936 -0.698  1.00 23.05  ? 288 GLN A CG  1 
ATOM   2021 C  CD  . GLN A 1 308 ? -8.173  -13.738 -0.307  1.00 30.68  ? 288 GLN A CD  1 
ATOM   2022 O  OE1 . GLN A 1 308 ? -8.286  -14.793 0.311   1.00 34.26  ? 288 GLN A OE1 1 
ATOM   2023 N  NE2 . GLN A 1 308 ? -6.997  -13.236 -0.656  1.00 30.94  ? 288 GLN A NE2 1 
ATOM   2024 N  N   . VAL A 1 309 ? -12.117 -11.962 -2.565  1.00 21.34  ? 289 VAL A N   1 
ATOM   2025 C  CA  . VAL A 1 309 ? -12.536 -12.133 -3.948  1.00 24.38  ? 289 VAL A CA  1 
ATOM   2026 C  C   . VAL A 1 309 ? -11.316 -11.966 -4.843  1.00 27.79  ? 289 VAL A C   1 
ATOM   2027 O  O   . VAL A 1 309 ? -10.548 -11.008 -4.692  1.00 28.87  ? 289 VAL A O   1 
ATOM   2028 C  CB  . VAL A 1 309 ? -13.648 -11.138 -4.320  1.00 27.00  ? 289 VAL A CB  1 
ATOM   2029 C  CG1 . VAL A 1 309 ? -14.037 -11.295 -5.779  1.00 30.13  ? 289 VAL A CG1 1 
ATOM   2030 C  CG2 . VAL A 1 309 ? -14.840 -11.355 -3.406  1.00 26.48  ? 289 VAL A CG2 1 
ATOM   2031 N  N   . LYS A 1 310 ? -11.122 -12.909 -5.756  1.00 26.65  ? 290 LYS A N   1 
ATOM   2032 C  CA  . LYS A 1 310 ? -9.967  -12.898 -6.643  1.00 25.53  ? 290 LYS A CA  1 
ATOM   2033 C  C   . LYS A 1 310 ? -10.411 -12.589 -8.066  1.00 31.83  ? 290 LYS A C   1 
ATOM   2034 O  O   . LYS A 1 310 ? -11.422 -13.115 -8.535  1.00 38.32  ? 290 LYS A O   1 
ATOM   2035 C  CB  . LYS A 1 310 ? -9.226  -14.232 -6.562  1.00 33.96  ? 290 LYS A CB  1 
ATOM   2036 C  CG  . LYS A 1 310 ? -8.638  -14.445 -5.179  1.00 44.08  ? 290 LYS A CG  1 
ATOM   2037 C  CD  . LYS A 1 310 ? -7.949  -15.781 -5.024  1.00 53.68  ? 290 LYS A CD  1 
ATOM   2038 C  CE  . LYS A 1 310 ? -7.406  -15.922 -3.614  1.00 51.65  ? 290 LYS A CE  1 
ATOM   2039 N  NZ  . LYS A 1 310 ? -6.790  -17.255 -3.386  1.00 61.57  ? 290 LYS A NZ  1 
ATOM   2040 N  N   . ILE A 1 311 ? -9.682  -11.703 -8.729  1.00 25.55  ? 291 ILE A N   1 
ATOM   2041 C  CA  . ILE A 1 311 ? -9.932  -11.361 -10.126 1.00 26.18  ? 291 ILE A CA  1 
ATOM   2042 C  C   . ILE A 1 311 ? -9.006  -12.219 -10.979 1.00 25.84  ? 291 ILE A C   1 
ATOM   2043 O  O   . ILE A 1 311 ? -7.782  -12.099 -10.840 1.00 26.39  ? 291 ILE A O   1 
ATOM   2044 C  CB  . ILE A 1 311 ? -9.679  -9.873  -10.399 1.00 24.94  ? 291 ILE A CB  1 
ATOM   2045 C  CG1 . ILE A 1 311 ? -10.484 -8.990  -9.444  1.00 27.80  ? 291 ILE A CG1 1 
ATOM   2046 C  CG2 . ILE A 1 311 ? -9.990  -9.544  -11.859 1.00 22.17  ? 291 ILE A CG2 1 
ATOM   2047 C  CD1 . ILE A 1 311 ? -10.169 -7.508  -9.599  1.00 28.05  ? 291 ILE A CD1 1 
ATOM   2048 N  N   . PRO A 1 312 ? -9.530  -13.072 -11.860 1.00 24.08  ? 292 PRO A N   1 
ATOM   2049 C  CA  . PRO A 1 312 ? -8.660  -13.785 -12.798 1.00 28.47  ? 292 PRO A CA  1 
ATOM   2050 C  C   . PRO A 1 312 ? -7.796  -12.803 -13.575 1.00 25.48  ? 292 PRO A C   1 
ATOM   2051 O  O   . PRO A 1 312 ? -8.256  -11.736 -13.998 1.00 22.36  ? 292 PRO A O   1 
ATOM   2052 C  CB  . PRO A 1 312 ? -9.648  -14.513 -13.714 1.00 28.45  ? 292 PRO A CB  1 
ATOM   2053 C  CG  . PRO A 1 312 ? -10.898 -14.602 -12.928 1.00 28.04  ? 292 PRO A CG  1 
ATOM   2054 C  CD  . PRO A 1 312 ? -10.954 -13.320 -12.140 1.00 27.98  ? 292 PRO A CD  1 
ATOM   2055 N  N   . ARG A 1 313 ? -6.527  -13.167 -13.758 1.00 24.47  ? 293 ARG A N   1 
ATOM   2056 C  CA  . ARG A 1 313 ? -5.584  -12.228 -14.352 1.00 22.66  ? 293 ARG A CA  1 
ATOM   2057 C  C   . ARG A 1 313 ? -6.008  -11.810 -15.753 1.00 20.44  ? 293 ARG A C   1 
ATOM   2058 O  O   . ARG A 1 313 ? -5.727  -10.681 -16.170 1.00 22.65  ? 293 ARG A O   1 
ATOM   2059 C  CB  . ARG A 1 313 ? -4.178  -12.845 -14.377 1.00 23.51  ? 293 ARG A CB  1 
ATOM   2060 C  CG  . ARG A 1 313 ? -3.122  -11.904 -14.888 1.00 22.65  ? 293 ARG A CG  1 
ATOM   2061 C  CD  . ARG A 1 313 ? -1.734  -12.540 -14.827 1.00 27.01  ? 293 ARG A CD  1 
ATOM   2062 N  NE  . ARG A 1 313 ? -1.332  -12.824 -13.455 1.00 30.34  ? 293 ARG A NE  1 
ATOM   2063 C  CZ  . ARG A 1 313 ? -0.175  -13.377 -13.114 1.00 31.68  ? 293 ARG A CZ  1 
ATOM   2064 N  NH1 . ARG A 1 313 ? 0.710   -13.740 -14.026 1.00 29.99  ? 293 ARG A NH1 1 
ATOM   2065 N  NH2 . ARG A 1 313 ? 0.096   -13.572 -11.828 1.00 29.65  ? 293 ARG A NH2 1 
ATOM   2066 N  N   . ASP A 1 314 ? -6.687  -12.687 -16.496 1.00 23.25  ? 294 ASP A N   1 
ATOM   2067 C  CA  . ASP A 1 314 ? -7.068  -12.345 -17.859 1.00 25.16  ? 294 ASP A CA  1 
ATOM   2068 C  C   . ASP A 1 314 ? -8.452  -11.719 -17.947 1.00 22.68  ? 294 ASP A C   1 
ATOM   2069 O  O   . ASP A 1 314 ? -8.971  -11.561 -19.053 1.00 24.37  ? 294 ASP A O   1 
ATOM   2070 C  CB  . ASP A 1 314 ? -6.997  -13.574 -18.771 1.00 27.45  ? 294 ASP A CB  1 
ATOM   2071 C  CG  . ASP A 1 314 ? -7.636  -14.795 -18.168 1.00 33.15  ? 294 ASP A CG  1 
ATOM   2072 O  OD1 . ASP A 1 314 ? -8.525  -14.661 -17.299 1.00 32.12  ? 294 ASP A OD1 1 
ATOM   2073 O  OD2 . ASP A 1 314 ? -7.250  -15.908 -18.576 1.00 36.10  ? 294 ASP A OD2 1 
ATOM   2074 N  N   . CYS A 1 315 ? -9.042  -11.342 -16.822 1.00 20.51  ? 295 CYS A N   1 
ATOM   2075 C  CA  . CYS A 1 315 ? -10.375 -10.754 -16.803 1.00 19.50  ? 295 CYS A CA  1 
ATOM   2076 C  C   . CYS A 1 315 ? -10.335 -9.323  -16.290 1.00 20.01  ? 295 CYS A C   1 
ATOM   2077 O  O   . CYS A 1 315 ? -9.326  -8.864  -15.745 1.00 19.96  ? 295 CYS A O   1 
ATOM   2078 C  CB  . CYS A 1 315 ? -11.323 -11.568 -15.921 1.00 22.50  ? 295 CYS A CB  1 
ATOM   2079 S  SG  . CYS A 1 315 ? -11.706 -13.188 -16.585 1.00 24.81  ? 295 CYS A SG  1 
ATOM   2080 N  N   . ILE A 1 316 ? -11.460 -8.607  -16.466 1.00 17.61  ? 296 ILE A N   1 
ATOM   2081 C  CA  . ILE A 1 316 ? -11.622 -7.257  -15.918 1.00 17.43  ? 296 ILE A CA  1 
ATOM   2082 C  C   . ILE A 1 316 ? -12.769 -7.286  -14.925 1.00 22.00  ? 296 ILE A C   1 
ATOM   2083 O  O   . ILE A 1 316 ? -13.810 -7.879  -15.209 1.00 23.50  ? 296 ILE A O   1 
ATOM   2084 C  CB  . ILE A 1 316 ? -11.913 -6.204  -17.010 1.00 18.89  ? 296 ILE A CB  1 
ATOM   2085 C  CG1 . ILE A 1 316 ? -10.832 -6.218  -18.084 1.00 21.80  ? 296 ILE A CG1 1 
ATOM   2086 C  CG2 . ILE A 1 316 ? -12.013 -4.775  -16.413 1.00 21.20  ? 296 ILE A CG2 1 
ATOM   2087 C  CD1 . ILE A 1 316 ? -11.261 -5.549  -19.365 1.00 22.83  ? 296 ILE A CD1 1 
ATOM   2088 N  N   . ALA A 1 317 ? -12.614 -6.637  -13.779 1.00 15.44  ? 297 ALA A N   1 
ATOM   2089 C  CA  . ALA A 1 317 ? -13.724 -6.579  -12.831 1.00 14.67  ? 297 ALA A CA  1 
ATOM   2090 C  C   . ALA A 1 317 ? -14.275 -5.163  -12.768 1.00 17.67  ? 297 ALA A C   1 
ATOM   2091 O  O   . ALA A 1 317 ? -13.588 -4.197  -13.093 1.00 16.52  ? 297 ALA A O   1 
ATOM   2092 C  CB  . ALA A 1 317 ? -13.304 -7.021  -11.428 1.00 20.44  ? 297 ALA A CB  1 
ATOM   2093 N  N   . PHE A 1 318 ? -15.531 -5.046  -12.349 1.00 15.17  ? 298 PHE A N   1 
ATOM   2094 C  CA  . PHE A 1 318 ? -16.174 -3.745  -12.202 1.00 14.53  ? 298 PHE A CA  1 
ATOM   2095 C  C   . PHE A 1 318 ? -16.888 -3.697  -10.869 1.00 16.06  ? 298 PHE A C   1 
ATOM   2096 O  O   . PHE A 1 318 ? -17.693 -4.578  -10.563 1.00 18.78  ? 298 PHE A O   1 
ATOM   2097 C  CB  . PHE A 1 318 ? -17.150 -3.460  -13.353 1.00 15.20  ? 298 PHE A CB  1 
ATOM   2098 C  CG  . PHE A 1 318 ? -16.469 -3.326  -14.665 1.00 14.94  ? 298 PHE A CG  1 
ATOM   2099 C  CD1 . PHE A 1 318 ? -16.239 -4.448  -15.452 1.00 16.34  ? 298 PHE A CD1 1 
ATOM   2100 C  CD2 . PHE A 1 318 ? -15.955 -2.094  -15.064 1.00 19.01  ? 298 PHE A CD2 1 
ATOM   2101 C  CE1 . PHE A 1 318 ? -15.562 -4.330  -16.650 1.00 21.37  ? 298 PHE A CE1 1 
ATOM   2102 C  CE2 . PHE A 1 318 ? -15.263 -1.959  -16.264 1.00 15.82  ? 298 PHE A CE2 1 
ATOM   2103 C  CZ  . PHE A 1 318 ? -15.073 -3.073  -17.065 1.00 18.42  ? 298 PHE A CZ  1 
ATOM   2104 N  N   . GLN A 1 319 ? -16.589 -2.671  -10.084 1.00 13.49  ? 299 GLN A N   1 
ATOM   2105 C  CA  . GLN A 1 319 ? -17.264 -2.453  -8.815  1.00 15.38  ? 299 GLN A CA  1 
ATOM   2106 C  C   . GLN A 1 319 ? -18.195 -1.266  -8.938  1.00 15.00  ? 299 GLN A C   1 
ATOM   2107 O  O   . GLN A 1 319 ? -17.845 -0.252  -9.546  1.00 17.16  ? 299 GLN A O   1 
ATOM   2108 C  CB  . GLN A 1 319 ? -16.280 -2.212  -7.673  1.00 18.21  ? 299 GLN A CB  1 
ATOM   2109 C  CG  . GLN A 1 319 ? -15.617 -3.484  -7.189  1.00 18.83  ? 299 GLN A CG  1 
ATOM   2110 C  CD  . GLN A 1 319 ? -14.678 -3.203  -6.051  1.00 21.43  ? 299 GLN A CD  1 
ATOM   2111 O  OE1 . GLN A 1 319 ? -13.619 -2.607  -6.252  1.00 20.65  ? 299 GLN A OE1 1 
ATOM   2112 N  NE2 . GLN A 1 319 ? -15.073 -3.589  -4.840  1.00 19.04  ? 299 GLN A NE2 1 
ATOM   2113 N  N   . THR A 1 320 ? -19.373 -1.391  -8.336  1.00 15.80  ? 300 THR A N   1 
ATOM   2114 C  CA  . THR A 1 320 ? -20.314 -0.286  -8.330  1.00 17.36  ? 300 THR A CA  1 
ATOM   2115 C  C   . THR A 1 320 ? -19.869 0.788   -7.347  1.00 17.45  ? 300 THR A C   1 
ATOM   2116 O  O   . THR A 1 320 ? -19.282 0.499   -6.307  1.00 21.30  ? 300 THR A O   1 
ATOM   2117 C  CB  . THR A 1 320 ? -21.698 -0.785  -7.932  1.00 22.60  ? 300 THR A CB  1 
ATOM   2118 O  OG1 . THR A 1 320 ? -21.549 -1.695  -6.836  1.00 21.48  ? 300 THR A OG1 1 
ATOM   2119 C  CG2 . THR A 1 320 ? -22.363 -1.497  -9.098  1.00 23.05  ? 300 THR A CG2 1 
ATOM   2120 N  N   . GLY A 1 321 ? -20.176 2.042   -7.676  1.00 16.39  ? 301 GLY A N   1 
ATOM   2121 C  CA  . GLY A 1 321 ? -19.940 3.155   -6.786  1.00 19.48  ? 301 GLY A CA  1 
ATOM   2122 C  C   . GLY A 1 321 ? -21.228 3.851   -6.373  1.00 18.00  ? 301 GLY A C   1 
ATOM   2123 O  O   . GLY A 1 321 ? -22.327 3.541   -6.853  1.00 19.85  ? 301 GLY A O   1 
ATOM   2124 N  N   . GLU A 1 322 ? -21.062 4.832   -5.483  1.00 17.24  ? 302 GLU A N   1 
ATOM   2125 C  CA  . GLU A 1 322 ? -22.219 5.494   -4.870  1.00 17.26  ? 302 GLU A CA  1 
ATOM   2126 C  C   . GLU A 1 322 ? -23.064 6.257   -5.877  1.00 19.36  ? 302 GLU A C   1 
ATOM   2127 O  O   . GLU A 1 322 ? -24.291 6.338   -5.717  1.00 21.58  ? 302 GLU A O   1 
ATOM   2128 C  CB  . GLU A 1 322 ? -21.750 6.435   -3.767  1.00 22.25  ? 302 GLU A CB  1 
ATOM   2129 C  CG  . GLU A 1 322 ? -21.211 5.715   -2.550  1.00 26.90  ? 302 GLU A CG  1 
ATOM   2130 C  CD  . GLU A 1 322 ? -20.855 6.673   -1.438  1.00 32.27  ? 302 GLU A CD  1 
ATOM   2131 O  OE1 . GLU A 1 322 ? -19.797 7.320   -1.533  1.00 39.36  ? 302 GLU A OE1 1 
ATOM   2132 O  OE2 . GLU A 1 322 ? -21.647 6.788   -0.482  1.00 38.78  ? 302 GLU A OE2 1 
ATOM   2133 N  N   . ALA A 1 323 ? -22.440 6.834   -6.910  1.00 18.74  ? 303 ALA A N   1 
ATOM   2134 C  CA  . ALA A 1 323 ? -23.219 7.574   -7.900  1.00 19.91  ? 303 ALA A CA  1 
ATOM   2135 C  C   . ALA A 1 323 ? -24.155 6.647   -8.666  1.00 21.77  ? 303 ALA A C   1 
ATOM   2136 O  O   . ALA A 1 323 ? -25.309 7.006   -8.947  1.00 20.14  ? 303 ALA A O   1 
ATOM   2137 C  CB  . ALA A 1 323 ? -22.281 8.312   -8.859  1.00 21.15  ? 303 ALA A CB  1 
ATOM   2138 N  N   . LEU A 1 324 ? -23.681 5.446   -9.004  1.00 20.91  ? 304 LEU A N   1 
ATOM   2139 C  CA  . LEU A 1 324 ? -24.552 4.475   -9.660  1.00 19.68  ? 304 LEU A CA  1 
ATOM   2140 C  C   . LEU A 1 324 ? -25.658 4.013   -8.721  1.00 22.68  ? 304 LEU A C   1 
ATOM   2141 O  O   . LEU A 1 324 ? -26.804 3.826   -9.148  1.00 21.02  ? 304 LEU A O   1 
ATOM   2142 C  CB  . LEU A 1 324 ? -23.727 3.287   -10.160 1.00 18.88  ? 304 LEU A CB  1 
ATOM   2143 C  CG  . LEU A 1 324 ? -24.470 2.236   -10.997 1.00 22.26  ? 304 LEU A CG  1 
ATOM   2144 C  CD1 . LEU A 1 324 ? -23.545 1.600   -12.025 1.00 23.95  ? 304 LEU A CD1 1 
ATOM   2145 C  CD2 . LEU A 1 324 ? -25.082 1.165   -10.120 1.00 28.01  ? 304 LEU A CD2 1 
ATOM   2146 N  N   . GLU A 1 325 ? -25.340 3.806   -7.442  1.00 18.39  ? 305 GLU A N   1 
ATOM   2147 C  CA  . GLU A 1 325 ? -26.383 3.447   -6.487  1.00 22.34  ? 305 GLU A CA  1 
ATOM   2148 C  C   . GLU A 1 325 ? -27.472 4.513   -6.460  1.00 22.94  ? 305 GLU A C   1 
ATOM   2149 O  O   . GLU A 1 325 ? -28.669 4.200   -6.503  1.00 23.50  ? 305 GLU A O   1 
ATOM   2150 C  CB  . GLU A 1 325 ? -25.791 3.253   -5.086  1.00 22.59  ? 305 GLU A CB  1 
ATOM   2151 C  CG  . GLU A 1 325 ? -26.856 2.990   -4.024  1.00 24.72  ? 305 GLU A CG  1 
ATOM   2152 C  CD  . GLU A 1 325 ? -26.305 2.653   -2.644  1.00 31.11  ? 305 GLU A CD  1 
ATOM   2153 O  OE1 . GLU A 1 325 ? -25.163 2.177   -2.539  1.00 28.06  ? 305 GLU A OE1 1 
ATOM   2154 O  OE2 . GLU A 1 325 ? -27.041 2.834   -1.650  1.00 36.14  ? 305 GLU A OE2 1 
ATOM   2155 N  N   . ARG A 1 326 ? -27.069 5.782   -6.401  1.00 21.31  ? 306 ARG A N   1 
ATOM   2156 C  CA  . ARG A 1 326 ? -28.051 6.855   -6.339  1.00 24.46  ? 306 ARG A CA  1 
ATOM   2157 C  C   . ARG A 1 326 ? -28.854 6.950   -7.632  1.00 24.20  ? 306 ARG A C   1 
ATOM   2158 O  O   . ARG A 1 326 ? -30.075 7.141   -7.597  1.00 21.37  ? 306 ARG A O   1 
ATOM   2159 C  CB  . ARG A 1 326 ? -27.361 8.177   -6.023  1.00 20.33  ? 306 ARG A CB  1 
ATOM   2160 C  CG  . ARG A 1 326 ? -28.355 9.352   -5.902  1.00 25.17  ? 306 ARG A CG  1 
ATOM   2161 C  CD  . ARG A 1 326 ? -29.370 9.144   -4.777  1.00 36.48  ? 306 ARG A CD  1 
ATOM   2162 N  NE  . ARG A 1 326 ? -28.715 9.113   -3.476  1.00 47.33  ? 306 ARG A NE  1 
ATOM   2163 C  CZ  . ARG A 1 326 ? -28.626 10.148  -2.652  1.00 49.47  ? 306 ARG A CZ  1 
ATOM   2164 N  NH1 . ARG A 1 326 ? -29.201 11.308  -2.931  1.00 43.97  ? 306 ARG A NH1 1 
ATOM   2165 N  NH2 . ARG A 1 326 ? -27.948 10.014  -1.516  1.00 47.01  ? 306 ARG A NH2 1 
ATOM   2166 N  N   . ILE A 1 327 ? -28.189 6.801   -8.779  1.00 22.09  ? 307 ILE A N   1 
ATOM   2167 C  CA  . ILE A 1 327 ? -28.880 6.872   -10.064 1.00 19.93  ? 307 ILE A CA  1 
ATOM   2168 C  C   . ILE A 1 327 ? -29.939 5.784   -10.168 1.00 22.67  ? 307 ILE A C   1 
ATOM   2169 O  O   . ILE A 1 327 ? -31.018 6.001   -10.736 1.00 25.90  ? 307 ILE A O   1 
ATOM   2170 C  CB  . ILE A 1 327 ? -27.859 6.788   -11.213 1.00 19.57  ? 307 ILE A CB  1 
ATOM   2171 C  CG1 . ILE A 1 327 ? -27.171 8.142   -11.383 1.00 20.03  ? 307 ILE A CG1 1 
ATOM   2172 C  CG2 . ILE A 1 327 ? -28.521 6.354   -12.517 1.00 22.31  ? 307 ILE A CG2 1 
ATOM   2173 C  CD1 . ILE A 1 327 ? -25.901 8.071   -12.205 1.00 18.24  ? 307 ILE A CD1 1 
ATOM   2174 N  N   . THR A 1 328 ? -29.660 4.605   -9.615  1.00 24.39  ? 308 THR A N   1 
ATOM   2175 C  CA  . THR A 1 328 ? -30.612 3.505   -9.662  1.00 21.97  ? 308 THR A CA  1 
ATOM   2176 C  C   . THR A 1 328 ? -31.512 3.462   -8.438  1.00 24.07  ? 308 THR A C   1 
ATOM   2177 O  O   . THR A 1 328 ? -32.214 2.465   -8.235  1.00 26.75  ? 308 THR A O   1 
ATOM   2178 C  CB  . THR A 1 328 ? -29.886 2.158   -9.831  1.00 21.23  ? 308 THR A CB  1 
ATOM   2179 O  OG1 . THR A 1 328 ? -29.104 1.850   -8.666  1.00 24.78  ? 308 THR A OG1 1 
ATOM   2180 C  CG2 . THR A 1 328 ? -28.966 2.178   -11.051 1.00 24.03  ? 308 THR A CG2 1 
ATOM   2181 N  N   . GLY A 1 329 ? -31.520 4.515   -7.626  1.00 23.10  ? 309 GLY A N   1 
ATOM   2182 C  CA  . GLY A 1 329 ? -32.422 4.569   -6.486  1.00 26.42  ? 309 GLY A CA  1 
ATOM   2183 C  C   . GLY A 1 329 ? -32.178 3.479   -5.467  1.00 32.24  ? 309 GLY A C   1 
ATOM   2184 O  O   . GLY A 1 329 ? -33.111 3.066   -4.764  1.00 30.00  ? 309 GLY A O   1 
ATOM   2185 N  N   . GLY A 1 330 ? -30.946 2.991   -5.372  1.00 24.49  ? 310 GLY A N   1 
ATOM   2186 C  CA  . GLY A 1 330 ? -30.646 1.922   -4.453  1.00 26.66  ? 310 GLY A CA  1 
ATOM   2187 C  C   . GLY A 1 330 ? -30.971 0.531   -4.952  1.00 32.80  ? 310 GLY A C   1 
ATOM   2188 O  O   . GLY A 1 330 ? -30.758 -0.436  -4.209  1.00 32.02  ? 310 GLY A O   1 
ATOM   2189 N  N   . LYS A 1 331 ? -31.481 0.389   -6.178  1.00 24.39  ? 311 LYS A N   1 
ATOM   2190 C  CA  . LYS A 1 331 ? -31.717 -0.950  -6.706  1.00 24.62  ? 311 LYS A CA  1 
ATOM   2191 C  C   . LYS A 1 331 ? -30.396 -1.688  -6.908  1.00 23.46  ? 311 LYS A C   1 
ATOM   2192 O  O   . LYS A 1 331 ? -30.325 -2.901  -6.704  1.00 25.96  ? 311 LYS A O   1 
ATOM   2193 C  CB  . LYS A 1 331 ? -32.499 -0.889  -8.014  1.00 27.74  ? 311 LYS A CB  1 
ATOM   2194 C  CG  . LYS A 1 331 ? -33.897 -0.314  -7.888  1.00 31.80  ? 311 LYS A CG  1 
ATOM   2195 C  CD  . LYS A 1 331 ? -34.931 -1.392  -8.100  1.00 36.44  ? 311 LYS A CD  1 
ATOM   2196 C  CE  . LYS A 1 331 ? -36.311 -0.801  -8.351  1.00 45.31  ? 311 LYS A CE  1 
ATOM   2197 N  NZ  . LYS A 1 331 ? -36.682 0.198   -7.315  1.00 49.78  ? 311 LYS A NZ  1 
ATOM   2198 N  N   . PHE A 1 332 ? -29.351 -0.979  -7.322  1.00 22.56  ? 312 PHE A N   1 
ATOM   2199 C  CA  . PHE A 1 332 ? -27.986 -1.478  -7.251  1.00 21.60  ? 312 PHE A CA  1 
ATOM   2200 C  C   . PHE A 1 332 ? -27.264 -0.736  -6.139  1.00 25.87  ? 312 PHE A C   1 
ATOM   2201 O  O   . PHE A 1 332 ? -27.610 0.398   -5.804  1.00 25.95  ? 312 PHE A O   1 
ATOM   2202 C  CB  . PHE A 1 332 ? -27.248 -1.311  -8.582  1.00 20.25  ? 312 PHE A CB  1 
ATOM   2203 C  CG  . PHE A 1 332 ? -27.697 -2.277  -9.647  1.00 22.46  ? 312 PHE A CG  1 
ATOM   2204 C  CD1 . PHE A 1 332 ? -28.582 -3.299  -9.348  1.00 24.13  ? 312 PHE A CD1 1 
ATOM   2205 C  CD2 . PHE A 1 332 ? -27.218 -2.172  -10.943 1.00 29.70  ? 312 PHE A CD2 1 
ATOM   2206 C  CE1 . PHE A 1 332 ? -29.003 -4.180  -10.327 1.00 28.59  ? 312 PHE A CE1 1 
ATOM   2207 C  CE2 . PHE A 1 332 ? -27.625 -3.065  -11.923 1.00 33.97  ? 312 PHE A CE2 1 
ATOM   2208 C  CZ  . PHE A 1 332 ? -28.518 -4.066  -11.614 1.00 30.80  ? 312 PHE A CZ  1 
ATOM   2209 N  N   . LYS A 1 333 ? -26.261 -1.389  -5.564  1.00 22.36  ? 313 LYS A N   1 
ATOM   2210 C  CA  . LYS A 1 333 ? -25.654 -0.945  -4.321  1.00 23.30  ? 313 LYS A CA  1 
ATOM   2211 C  C   . LYS A 1 333 ? -24.150 -0.852  -4.485  1.00 21.17  ? 313 LYS A C   1 
ATOM   2212 O  O   . LYS A 1 333 ? -23.528 -1.724  -5.102  1.00 21.55  ? 313 LYS A O   1 
ATOM   2213 C  CB  . LYS A 1 333 ? -25.941 -1.918  -3.172  1.00 27.54  ? 313 LYS A CB  1 
ATOM   2214 C  CG  . LYS A 1 333 ? -26.560 -1.281  -1.944  1.00 49.78  ? 313 LYS A CG  1 
ATOM   2215 C  CD  . LYS A 1 333 ? -27.966 -0.804  -2.246  1.00 39.08  ? 313 LYS A CD  1 
ATOM   2216 C  CE  . LYS A 1 333 ? -28.696 -0.360  -0.993  1.00 54.92  ? 313 LYS A CE  1 
ATOM   2217 N  NZ  . LYS A 1 333 ? -30.136 -0.103  -1.274  1.00 60.73  ? 313 LYS A NZ  1 
ATOM   2218 N  N   . ALA A 1 334 ? -23.575 0.193   -3.902  1.00 21.12  ? 314 ALA A N   1 
ATOM   2219 C  CA  . ALA A 1 334 ? -22.144 0.215   -3.620  1.00 23.61  ? 314 ALA A CA  1 
ATOM   2220 C  C   . ALA A 1 334 ? -21.887 -0.559  -2.330  1.00 20.48  ? 314 ALA A C   1 
ATOM   2221 O  O   . ALA A 1 334 ? -22.552 -0.328  -1.316  1.00 25.69  ? 314 ALA A O   1 
ATOM   2222 C  CB  . ALA A 1 334 ? -21.653 1.658   -3.495  1.00 21.48  ? 314 ALA A CB  1 
ATOM   2223 N  N   . VAL A 1 335 ? -20.949 -1.494  -2.362  1.00 20.25  ? 315 VAL A N   1 
ATOM   2224 C  CA  . VAL A 1 335 ? -20.755 -2.442  -1.265  1.00 19.63  ? 315 VAL A CA  1 
ATOM   2225 C  C   . VAL A 1 335 ? -19.399 -2.167  -0.630  1.00 20.01  ? 315 VAL A C   1 
ATOM   2226 O  O   . VAL A 1 335 ? -18.409 -2.043  -1.353  1.00 21.29  ? 315 VAL A O   1 
ATOM   2227 C  CB  . VAL A 1 335 ? -20.851 -3.899  -1.752  1.00 21.74  ? 315 VAL A CB  1 
ATOM   2228 C  CG1 . VAL A 1 335 ? -20.599 -4.865  -0.605  1.00 21.65  ? 315 VAL A CG1 1 
ATOM   2229 C  CG2 . VAL A 1 335 ? -22.258 -4.154  -2.364  1.00 19.92  ? 315 VAL A CG2 1 
ATOM   2230 N  N   . PRO A 1 336 ? -19.310 -2.066  0.700   1.00 19.63  ? 316 PRO A N   1 
ATOM   2231 C  CA  . PRO A 1 336 ? -18.019 -1.745  1.333   1.00 22.99  ? 316 PRO A CA  1 
ATOM   2232 C  C   . PRO A 1 336 ? -16.969 -2.815  1.068   1.00 23.60  ? 316 PRO A C   1 
ATOM   2233 O  O   . PRO A 1 336 ? -17.256 -4.018  1.050   1.00 19.83  ? 316 PRO A O   1 
ATOM   2234 C  CB  . PRO A 1 336 ? -18.358 -1.663  2.824   1.00 25.93  ? 316 PRO A CB  1 
ATOM   2235 C  CG  . PRO A 1 336 ? -19.834 -1.539  2.899   1.00 31.03  ? 316 PRO A CG  1 
ATOM   2236 C  CD  . PRO A 1 336 ? -20.388 -2.219  1.686   1.00 21.75  ? 316 PRO A CD  1 
ATOM   2237 N  N   . HIS A 1 337 ? -15.728 -2.367  0.904   1.00 19.88  ? 317 HIS A N   1 
ATOM   2238 C  CA  . HIS A 1 337 ? -14.647 -3.272  0.550   1.00 20.33  ? 317 HIS A CA  1 
ATOM   2239 C  C   . HIS A 1 337 ? -13.315 -2.621  0.899   1.00 24.29  ? 317 HIS A C   1 
ATOM   2240 O  O   . HIS A 1 337 ? -13.231 -1.420  1.167   1.00 19.51  ? 317 HIS A O   1 
ATOM   2241 C  CB  . HIS A 1 337 ? -14.689 -3.628  -0.937  1.00 18.87  ? 317 HIS A CB  1 
ATOM   2242 C  CG  . HIS A 1 337 ? -14.574 -2.439  -1.835  1.00 17.35  ? 317 HIS A CG  1 
ATOM   2243 N  ND1 . HIS A 1 337 ? -15.658 -1.649  -2.159  1.00 18.66  ? 317 HIS A ND1 1 
ATOM   2244 C  CD2 . HIS A 1 337 ? -13.501 -1.880  -2.445  1.00 20.07  ? 317 HIS A CD2 1 
ATOM   2245 C  CE1 . HIS A 1 337 ? -15.258 -0.668  -2.951  1.00 17.26  ? 317 HIS A CE1 1 
ATOM   2246 N  NE2 . HIS A 1 337 ? -13.955 -0.783  -3.135  1.00 15.80  ? 317 HIS A NE2 1 
ATOM   2247 N  N   . PHE A 1 338 ? -12.263 -3.434  0.872   1.00 19.96  ? 318 PHE A N   1 
ATOM   2248 C  CA  . PHE A 1 338 ? -10.912 -2.893  0.971   1.00 19.61  ? 318 PHE A CA  1 
ATOM   2249 C  C   . PHE A 1 338 ? -9.954  -3.809  0.229   1.00 26.37  ? 318 PHE A C   1 
ATOM   2250 O  O   . PHE A 1 338 ? -10.286 -4.942  -0.115  1.00 20.11  ? 318 PHE A O   1 
ATOM   2251 C  CB  . PHE A 1 338 ? -10.463 -2.693  2.431   1.00 20.33  ? 318 PHE A CB  1 
ATOM   2252 C  CG  . PHE A 1 338 ? -10.399 -3.953  3.257   1.00 22.92  ? 318 PHE A CG  1 
ATOM   2253 C  CD1 . PHE A 1 338 ? -9.241  -4.725  3.293   1.00 25.36  ? 318 PHE A CD1 1 
ATOM   2254 C  CD2 . PHE A 1 338 ? -11.476 -4.338  4.035   1.00 27.11  ? 318 PHE A CD2 1 
ATOM   2255 C  CE1 . PHE A 1 338 ? -9.177  -5.871  4.074   1.00 26.94  ? 318 PHE A CE1 1 
ATOM   2256 C  CE2 . PHE A 1 338 ? -11.414 -5.484  4.815   1.00 31.04  ? 318 PHE A CE2 1 
ATOM   2257 C  CZ  . PHE A 1 338 ? -10.266 -6.248  4.832   1.00 27.85  ? 318 PHE A CZ  1 
ATOM   2258 N  N   . VAL A 1 339 ? -8.758  -3.297  -0.046  1.00 20.40  ? 319 VAL A N   1 
ATOM   2259 C  CA  . VAL A 1 339 ? -7.737  -4.057  -0.754  1.00 20.37  ? 319 VAL A CA  1 
ATOM   2260 C  C   . VAL A 1 339 ? -6.560  -4.251  0.181   1.00 25.10  ? 319 VAL A C   1 
ATOM   2261 O  O   . VAL A 1 339 ? -6.071  -3.292  0.785   1.00 23.59  ? 319 VAL A O   1 
ATOM   2262 C  CB  . VAL A 1 339 ? -7.285  -3.366  -2.053  1.00 21.64  ? 319 VAL A CB  1 
ATOM   2263 C  CG1 . VAL A 1 339 ? -6.165  -4.165  -2.708  1.00 27.12  ? 319 VAL A CG1 1 
ATOM   2264 C  CG2 . VAL A 1 339 ? -8.446  -3.207  -3.007  1.00 24.53  ? 319 VAL A CG2 1 
ATOM   2265 N  N   . ARG A 1 340 ? -6.097  -5.485  0.287   1.00 24.06  ? 320 ARG A N   1 
ATOM   2266 C  CA  . ARG A 1 340 ? -4.962  -5.835  1.119   1.00 31.22  ? 320 ARG A CA  1 
ATOM   2267 C  C   . ARG A 1 340 ? -3.772  -6.157  0.230   1.00 26.71  ? 320 ARG A C   1 
ATOM   2268 O  O   . ARG A 1 340 ? -3.907  -6.891  -0.752  1.00 26.85  ? 320 ARG A O   1 
ATOM   2269 C  CB  . ARG A 1 340 ? -5.314  -7.027  2.005   1.00 32.85  ? 320 ARG A CB  1 
ATOM   2270 C  CG  . ARG A 1 340 ? -4.244  -7.409  2.973   1.00 37.45  ? 320 ARG A CG  1 
ATOM   2271 C  CD  . ARG A 1 340 ? -4.801  -8.368  3.995   1.00 41.06  ? 320 ARG A CD  1 
ATOM   2272 N  NE  . ARG A 1 340 ? -3.748  -8.835  4.881   1.00 42.21  ? 320 ARG A NE  1 
ATOM   2273 C  CZ  . ARG A 1 340 ? -3.956  -9.546  5.979   1.00 52.00  ? 320 ARG A CZ  1 
ATOM   2274 N  NH1 . ARG A 1 340 ? -5.177  -9.885  6.361   1.00 40.72  ? 320 ARG A NH1 1 
ATOM   2275 N  NH2 . ARG A 1 340 ? -2.912  -9.925  6.710   1.00 49.47  ? 320 ARG A NH2 1 
ATOM   2276 N  N   . GLY A 1 341 ? -2.620  -5.590  0.566   1.00 22.61  ? 321 GLY A N   1 
ATOM   2277 C  CA  . GLY A 1 341 ? -1.379  -5.908  -0.106  1.00 26.57  ? 321 GLY A CA  1 
ATOM   2278 C  C   . GLY A 1 341 ? -0.722  -7.125  0.508   1.00 30.58  ? 321 GLY A C   1 
ATOM   2279 O  O   . GLY A 1 341 ? -1.287  -7.821  1.353   1.00 32.06  ? 321 GLY A O   1 
ATOM   2280 N  N   . ALA A 1 342 ? 0.496   -7.387  0.067   1.00 25.77  ? 322 ALA A N   1 
ATOM   2281 C  CA  . ALA A 1 342 ? 1.250   -8.520  0.579   1.00 27.26  ? 322 ALA A CA  1 
ATOM   2282 C  C   . ALA A 1 342 ? 2.069   -8.083  1.785   1.00 25.18  ? 322 ALA A C   1 
ATOM   2283 O  O   . ALA A 1 342 ? 2.667   -7.005  1.779   1.00 31.16  ? 322 ALA A O   1 
ATOM   2284 C  CB  . ALA A 1 342 ? 2.161   -9.095  -0.507  1.00 31.77  ? 322 ALA A CB  1 
ATOM   2285 N  N   . ARG A 1 343 ? 2.067   -8.910  2.826   1.00 25.00  ? 323 ARG A N   1 
ATOM   2286 C  CA  . ARG A 1 343 ? 2.864   -8.625  4.006   1.00 29.71  ? 323 ARG A CA  1 
ATOM   2287 C  C   . ARG A 1 343 ? 4.343   -8.695  3.655   1.00 34.47  ? 323 ARG A C   1 
ATOM   2288 O  O   . ARG A 1 343 ? 4.775   -9.588  2.921   1.00 33.93  ? 323 ARG A O   1 
ATOM   2289 C  CB  . ARG A 1 343 ? 2.542   -9.622  5.118   1.00 27.73  ? 323 ARG A CB  1 
ATOM   2290 C  CG  . ARG A 1 343 ? 1.233   -9.350  5.840   1.00 33.79  ? 323 ARG A CG  1 
ATOM   2291 C  CD  . ARG A 1 343 ? 0.835   -10.552 6.674   1.00 34.44  ? 323 ARG A CD  1 
ATOM   2292 N  NE  . ARG A 1 343 ? 0.376   -11.638 5.820   1.00 32.37  ? 323 ARG A NE  1 
ATOM   2293 C  CZ  . ARG A 1 343 ? 0.196   -12.889 6.227   1.00 40.89  ? 323 ARG A CZ  1 
ATOM   2294 N  NH1 . ARG A 1 343 ? 0.463   -13.258 7.470   1.00 43.13  ? 323 ARG A NH1 1 
ATOM   2295 N  NH2 . ARG A 1 343 ? -0.261  -13.791 5.365   1.00 35.90  ? 323 ARG A NH2 1 
ATOM   2296 N  N   . ALA A 1 344 ? 5.120   -7.743  4.184   1.00 29.28  ? 324 ALA A N   1 
ATOM   2297 C  CA  . ALA A 1 344 ? 6.552   -7.710  3.898   1.00 37.81  ? 324 ALA A CA  1 
ATOM   2298 C  C   . ALA A 1 344 ? 7.228   -9.026  4.266   1.00 35.46  ? 324 ALA A C   1 
ATOM   2299 O  O   . ALA A 1 344 ? 8.094   -9.514  3.529   1.00 36.46  ? 324 ALA A O   1 
ATOM   2300 C  CB  . ALA A 1 344 ? 7.213   -6.549  4.643   1.00 45.69  ? 324 ALA A CB  1 
ATOM   2301 N  N   . GLU A 1 345 ? 6.846   -9.621  5.401   1.00 34.30  ? 325 GLU A N   1 
ATOM   2302 C  CA  . GLU A 1 345 ? 7.525   -10.829 5.859   1.00 35.18  ? 325 GLU A CA  1 
ATOM   2303 C  C   . GLU A 1 345 ? 7.207   -12.044 4.993   1.00 34.82  ? 325 GLU A C   1 
ATOM   2304 O  O   . GLU A 1 345 ? 7.929   -13.044 5.063   1.00 39.61  ? 325 GLU A O   1 
ATOM   2305 C  CB  . GLU A 1 345 ? 7.173   -11.107 7.325   1.00 44.42  ? 325 GLU A CB  1 
ATOM   2306 C  CG  . GLU A 1 345 ? 5.689   -11.355 7.604   1.00 44.17  ? 325 GLU A CG  1 
ATOM   2307 C  CD  . GLU A 1 345 ? 4.880   -10.075 7.816   1.00 52.43  ? 325 GLU A CD  1 
ATOM   2308 O  OE1 . GLU A 1 345 ? 5.382   -8.973  7.499   1.00 48.47  ? 325 GLU A OE1 1 
ATOM   2309 O  OE2 . GLU A 1 345 ? 3.731   -10.175 8.301   1.00 55.97  ? 325 GLU A OE2 1 
ATOM   2310 N  N   . MET A 1 346 ? 6.152   -11.979 4.180   1.00 34.44  ? 326 MET A N   1 
ATOM   2311 C  CA  . MET A 1 346 ? 5.800   -13.037 3.242   1.00 39.14  ? 326 MET A CA  1 
ATOM   2312 C  C   . MET A 1 346 ? 6.413   -12.839 1.861   1.00 49.75  ? 326 MET A C   1 
ATOM   2313 O  O   . MET A 1 346 ? 6.253   -13.714 1.001   1.00 49.32  ? 326 MET A O   1 
ATOM   2314 C  CB  . MET A 1 346 ? 4.271   -13.118 3.089   1.00 38.64  ? 326 MET A CB  1 
ATOM   2315 C  CG  . MET A 1 346 ? 3.532   -13.497 4.353   1.00 49.65  ? 326 MET A CG  1 
ATOM   2316 S  SD  . MET A 1 346 ? 3.709   -15.248 4.721   1.00 72.14  ? 326 MET A SD  1 
ATOM   2317 C  CE  . MET A 1 346 ? 2.941   -15.323 6.335   1.00 66.44  ? 326 MET A CE  1 
ATOM   2318 N  N   . SER A 1 347 ? 7.097   -11.719 1.624   1.00 33.15  ? 327 SER A N   1 
ATOM   2319 C  CA  . SER A 1 347 ? 7.517   -11.307 0.285   1.00 28.37  ? 327 SER A CA  1 
ATOM   2320 C  C   . SER A 1 347 ? 9.022   -11.488 0.172   1.00 40.75  ? 327 SER A C   1 
ATOM   2321 O  O   . SER A 1 347 ? 9.794   -10.667 0.674   1.00 49.48  ? 327 SER A O   1 
ATOM   2322 C  CB  . SER A 1 347 ? 7.133   -9.861  0.005   1.00 29.95  ? 327 SER A CB  1 
ATOM   2323 O  OG  . SER A 1 347 ? 5.731   -9.706  0.054   1.00 37.98  ? 327 SER A OG  1 
ATOM   2324 N  N   . ALA A 1 348 ? 9.430   -12.547 -0.515  1.00 31.75  ? 328 ALA A N   1 
ATOM   2325 C  CA  . ALA A 1 348 ? 10.846  -12.828 -0.699  1.00 34.22  ? 328 ALA A CA  1 
ATOM   2326 C  C   . ALA A 1 348 ? 11.396  -11.994 -1.848  1.00 36.22  ? 328 ALA A C   1 
ATOM   2327 O  O   . ALA A 1 348 ? 10.808  -11.951 -2.932  1.00 36.10  ? 328 ALA A O   1 
ATOM   2328 C  CB  . ALA A 1 348 ? 11.054  -14.314 -0.966  1.00 37.19  ? 328 ALA A CB  1 
ATOM   2329 N  N   . GLY A 1 349 ? 12.524  -11.339 -1.613  1.00 39.48  ? 329 GLY A N   1 
ATOM   2330 C  CA  . GLY A 1 349 ? 13.081  -10.442 -2.601  1.00 38.55  ? 329 GLY A CA  1 
ATOM   2331 C  C   . GLY A 1 349 ? 12.529  -9.036  -2.459  1.00 37.91  ? 329 GLY A C   1 
ATOM   2332 O  O   . GLY A 1 349 ? 12.076  -8.604  -1.396  1.00 41.48  ? 329 GLY A O   1 
ATOM   2333 N  N   . ARG A 1 350 ? 12.568  -8.313  -3.571  1.00 31.69  ? 330 ARG A N   1 
ATOM   2334 C  CA  . ARG A 1 350 ? 12.145  -6.916  -3.622  1.00 26.50  ? 330 ARG A CA  1 
ATOM   2335 C  C   . ARG A 1 350 ? 10.830  -6.874  -4.395  1.00 27.68  ? 330 ARG A C   1 
ATOM   2336 O  O   . ARG A 1 350 ? 10.784  -6.521  -5.569  1.00 30.61  ? 330 ARG A O   1 
ATOM   2337 C  CB  . ARG A 1 350 ? 13.239  -6.051  -4.276  1.00 35.35  ? 330 ARG A CB  1 
ATOM   2338 C  CG  . ARG A 1 350 ? 13.304  -4.622  -3.776  1.00 47.42  ? 330 ARG A CG  1 
ATOM   2339 C  CD  . ARG A 1 350 ? 14.504  -3.871  -4.347  1.00 51.19  ? 330 ARG A CD  1 
ATOM   2340 N  NE  . ARG A 1 350 ? 14.565  -2.501  -3.852  1.00 64.57  ? 330 ARG A NE  1 
ATOM   2341 C  CZ  . ARG A 1 350 ? 15.605  -1.693  -4.007  1.00 86.21  ? 330 ARG A CZ  1 
ATOM   2342 N  NH1 . ARG A 1 350 ? 16.697  -2.085  -4.643  1.00 88.69  ? 330 ARG A NH1 1 
ATOM   2343 N  NH2 . ARG A 1 350 ? 15.550  -0.461  -3.508  1.00 82.88  ? 330 ARG A NH2 1 
ATOM   2344 N  N   . ILE A 1 351 ? 9.751   -7.257  -3.726  1.00 24.97  ? 331 ILE A N   1 
ATOM   2345 C  CA  . ILE A 1 351 ? 8.462   -7.420  -4.386  1.00 22.71  ? 331 ILE A CA  1 
ATOM   2346 C  C   . ILE A 1 351 ? 7.705   -6.099  -4.357  1.00 23.18  ? 331 ILE A C   1 
ATOM   2347 O  O   . ILE A 1 351 ? 7.424   -5.557  -3.284  1.00 27.09  ? 331 ILE A O   1 
ATOM   2348 C  CB  . ILE A 1 351 ? 7.635   -8.525  -3.723  1.00 25.34  ? 331 ILE A CB  1 
ATOM   2349 C  CG1 . ILE A 1 351 ? 8.407   -9.842  -3.734  1.00 27.20  ? 331 ILE A CG1 1 
ATOM   2350 C  CG2 . ILE A 1 351 ? 6.317   -8.659  -4.446  1.00 29.61  ? 331 ILE A CG2 1 
ATOM   2351 C  CD1 . ILE A 1 351 ? 8.756   -10.313 -5.111  1.00 30.51  ? 331 ILE A CD1 1 
ATOM   2352 N  N   . ALA A 1 352 ? 7.371   -5.592  -5.535  1.00 22.83  ? 332 ALA A N   1 
ATOM   2353 C  CA  . ALA A 1 352 ? 6.478   -4.455  -5.704  1.00 22.63  ? 332 ALA A CA  1 
ATOM   2354 C  C   . ALA A 1 352 ? 5.111   -4.937  -6.147  1.00 21.39  ? 332 ALA A C   1 
ATOM   2355 O  O   . ALA A 1 352 ? 4.981   -5.997  -6.766  1.00 21.16  ? 332 ALA A O   1 
ATOM   2356 C  CB  . ALA A 1 352 ? 7.019   -3.483  -6.748  1.00 20.93  ? 332 ALA A CB  1 
ATOM   2357 N  N   . ARG A 1 353 ? 4.091   -4.127  -5.857  1.00 18.87  ? 333 ARG A N   1 
ATOM   2358 C  CA  . ARG A 1 353 ? 2.737   -4.424  -6.330  1.00 18.70  ? 333 ARG A CA  1 
ATOM   2359 C  C   . ARG A 1 353 ? 2.235   -3.275  -7.188  1.00 19.77  ? 333 ARG A C   1 
ATOM   2360 O  O   . ARG A 1 353 ? 2.236   -2.129  -6.748  1.00 21.75  ? 333 ARG A O   1 
ATOM   2361 C  CB  . ARG A 1 353 ? 1.773   -4.681  -5.165  1.00 17.98  ? 333 ARG A CB  1 
ATOM   2362 C  CG  . ARG A 1 353 ? 0.296   -4.949  -5.607  1.00 20.03  ? 333 ARG A CG  1 
ATOM   2363 C  CD  . ARG A 1 353 ? -0.594  -5.334  -4.432  1.00 23.48  ? 333 ARG A CD  1 
ATOM   2364 N  NE  . ARG A 1 353 ? -0.426  -4.475  -3.265  1.00 24.24  ? 333 ARG A NE  1 
ATOM   2365 C  CZ  . ARG A 1 353 ? -1.374  -3.709  -2.732  1.00 26.27  ? 333 ARG A CZ  1 
ATOM   2366 N  NH1 . ARG A 1 353 ? -2.597  -3.656  -3.241  1.00 26.92  ? 333 ARG A NH1 1 
ATOM   2367 N  NH2 . ARG A 1 353 ? -1.095  -3.001  -1.639  1.00 27.37  ? 333 ARG A NH2 1 
ATOM   2368 N  N   . ASN A 1 354 ? 1.805   -3.567  -8.409  1.00 16.84  ? 334 ASN A N   1 
ATOM   2369 C  CA  . ASN A 1 354 ? 1.244   -2.538  -9.275  1.00 16.90  ? 334 ASN A CA  1 
ATOM   2370 C  C   . ASN A 1 354 ? -0.215  -2.826  -9.560  1.00 17.75  ? 334 ASN A C   1 
ATOM   2371 O  O   . ASN A 1 354 ? -0.593  -3.977  -9.796  1.00 17.62  ? 334 ASN A O   1 
ATOM   2372 C  CB  . ASN A 1 354 ? 1.990   -2.457  -10.583 1.00 16.57  ? 334 ASN A CB  1 
ATOM   2373 C  CG  . ASN A 1 354 ? 3.445   -2.152  -10.367 1.00 21.35  ? 334 ASN A CG  1 
ATOM   2374 O  OD1 . ASN A 1 354 ? 3.774   -1.165  -9.718  1.00 20.43  ? 334 ASN A OD1 1 
ATOM   2375 N  ND2 . ASN A 1 354 ? 4.318   -3.016  -10.861 1.00 19.74  ? 334 ASN A ND2 1 
ATOM   2376 N  N   . THR A 1 355 ? -1.031  -1.772  -9.546  1.00 15.77  ? 335 THR A N   1 
ATOM   2377 C  CA  . THR A 1 355 ? -2.460  -1.950  -9.805  1.00 16.49  ? 335 THR A CA  1 
ATOM   2378 C  C   . THR A 1 355 ? -2.987  -0.838  -10.707 1.00 15.90  ? 335 THR A C   1 
ATOM   2379 O  O   . THR A 1 355 ? -2.414  0.245   -10.788 1.00 16.14  ? 335 THR A O   1 
ATOM   2380 C  CB  . THR A 1 355 ? -3.304  -1.964  -8.511  1.00 18.53  ? 335 THR A CB  1 
ATOM   2381 O  OG1 . THR A 1 355 ? -3.332  -0.653  -7.939  1.00 22.18  ? 335 THR A OG1 1 
ATOM   2382 C  CG2 . THR A 1 355 ? -2.741  -2.936  -7.483  1.00 24.56  ? 335 THR A CG2 1 
ATOM   2383 N  N   . LEU A 1 356 ? -4.115  -1.121  -11.368 1.00 15.59  ? 336 LEU A N   1 
ATOM   2384 C  CA  . LEU A 1 356 ? -4.802  -0.138  -12.199 1.00 13.59  ? 336 LEU A CA  1 
ATOM   2385 C  C   . LEU A 1 356 ? -6.259  -0.151  -11.804 1.00 16.22  ? 336 LEU A C   1 
ATOM   2386 O  O   . LEU A 1 356 ? -6.846  -1.226  -11.674 1.00 17.55  ? 336 LEU A O   1 
ATOM   2387 C  CB  . LEU A 1 356 ? -4.674  -0.460  -13.691 1.00 18.02  ? 336 LEU A CB  1 
ATOM   2388 C  CG  . LEU A 1 356 ? -5.501  0.440   -14.616 1.00 18.41  ? 336 LEU A CG  1 
ATOM   2389 C  CD1 . LEU A 1 356 ? -5.028  1.898   -14.598 1.00 18.12  ? 336 LEU A CD1 1 
ATOM   2390 C  CD2 . LEU A 1 356 ? -5.473  -0.091  -16.031 1.00 19.33  ? 336 LEU A CD2 1 
ATOM   2391 N  N   . ALA A 1 357 ? -6.824  1.031   -11.602 1.00 15.33  ? 337 ALA A N   1 
ATOM   2392 C  CA  . ALA A 1 357 ? -8.263  1.181   -11.443 1.00 13.26  ? 337 ALA A CA  1 
ATOM   2393 C  C   . ALA A 1 357 ? -8.723  2.299   -12.360 1.00 16.58  ? 337 ALA A C   1 
ATOM   2394 O  O   . ALA A 1 357 ? -8.055  3.324   -12.476 1.00 16.00  ? 337 ALA A O   1 
ATOM   2395 C  CB  . ALA A 1 357 ? -8.650  1.492   -9.994  1.00 15.34  ? 337 ALA A CB  1 
ATOM   2396 N  N   . VAL A 1 358 ? -9.860  2.104   -13.024 1.00 13.29  ? 338 VAL A N   1 
ATOM   2397 C  CA  . VAL A 1 358 ? -10.434 3.133   -13.885 1.00 14.37  ? 338 VAL A CA  1 
ATOM   2398 C  C   . VAL A 1 358 ? -11.762 3.523   -13.258 1.00 14.01  ? 338 VAL A C   1 
ATOM   2399 O  O   . VAL A 1 358 ? -12.731 2.748   -13.299 1.00 15.04  ? 338 VAL A O   1 
ATOM   2400 C  CB  . VAL A 1 358 ? -10.609 2.649   -15.332 1.00 14.17  ? 338 VAL A CB  1 
ATOM   2401 C  CG1 . VAL A 1 358 ? -11.239 3.727   -16.184 1.00 15.25  ? 338 VAL A CG1 1 
ATOM   2402 C  CG2 . VAL A 1 358 ? -9.261  2.219   -15.913 1.00 14.57  ? 338 VAL A CG2 1 
ATOM   2403 N  N   . PHE A 1 359 ? -11.803 4.696   -12.632 1.00 14.04  ? 339 PHE A N   1 
ATOM   2404 C  CA  . PHE A 1 359 ? -12.981 5.177   -11.909 1.00 16.98  ? 339 PHE A CA  1 
ATOM   2405 C  C   . PHE A 1 359 ? -13.888 5.901   -12.893 1.00 16.52  ? 339 PHE A C   1 
ATOM   2406 O  O   . PHE A 1 359 ? -13.751 7.113   -13.102 1.00 16.01  ? 339 PHE A O   1 
ATOM   2407 C  CB  . PHE A 1 359 ? -12.537 6.106   -10.780 1.00 17.63  ? 339 PHE A CB  1 
ATOM   2408 C  CG  . PHE A 1 359 ? -11.699 5.424   -9.725  1.00 15.84  ? 339 PHE A CG  1 
ATOM   2409 C  CD1 . PHE A 1 359 ? -12.310 4.668   -8.745  1.00 18.23  ? 339 PHE A CD1 1 
ATOM   2410 C  CD2 . PHE A 1 359 ? -10.304 5.564   -9.700  1.00 18.42  ? 339 PHE A CD2 1 
ATOM   2411 C  CE1 . PHE A 1 359 ? -11.563 4.021   -7.766  1.00 17.70  ? 339 PHE A CE1 1 
ATOM   2412 C  CE2 . PHE A 1 359 ? -9.551  4.924   -8.722  1.00 20.06  ? 339 PHE A CE2 1 
ATOM   2413 C  CZ  . PHE A 1 359 ? -10.175 4.150   -7.758  1.00 22.60  ? 339 PHE A CZ  1 
ATOM   2414 N  N   . THR A 1 360 ? -14.814 5.171   -13.531 1.00 15.12  ? 340 THR A N   1 
ATOM   2415 C  CA  . THR A 1 360 ? -15.789 5.870   -14.353 1.00 15.06  ? 340 THR A CA  1 
ATOM   2416 C  C   . THR A 1 360 ? -16.790 6.544   -13.432 1.00 17.73  ? 340 THR A C   1 
ATOM   2417 O  O   . THR A 1 360 ? -17.231 5.967   -12.427 1.00 18.52  ? 340 THR A O   1 
ATOM   2418 C  CB  . THR A 1 360 ? -16.506 4.945   -15.359 1.00 16.20  ? 340 THR A CB  1 
ATOM   2419 O  OG1 . THR A 1 360 ? -17.456 4.096   -14.699 1.00 17.18  ? 340 THR A OG1 1 
ATOM   2420 C  CG2 . THR A 1 360 ? -15.517 4.068   -16.166 1.00 14.15  ? 340 THR A CG2 1 
ATOM   2421 N  N   . GLN A 1 361 ? -17.107 7.788   -13.769 1.00 19.27  ? 341 GLN A N   1 
ATOM   2422 C  CA  . GLN A 1 361 ? -17.967 8.632   -12.953 1.00 19.64  ? 341 GLN A CA  1 
ATOM   2423 C  C   . GLN A 1 361 ? -18.594 9.685   -13.856 1.00 18.16  ? 341 GLN A C   1 
ATOM   2424 O  O   . GLN A 1 361 ? -18.113 9.921   -14.971 1.00 17.80  ? 341 GLN A O   1 
ATOM   2425 C  CB  . GLN A 1 361 ? -17.173 9.287   -11.813 1.00 21.70  ? 341 GLN A CB  1 
ATOM   2426 C  CG  . GLN A 1 361 ? -15.853 9.910   -12.252 1.00 20.61  ? 341 GLN A CG  1 
ATOM   2427 C  CD  . GLN A 1 361 ? -14.956 10.192  -11.076 1.00 28.52  ? 341 GLN A CD  1 
ATOM   2428 O  OE1 . GLN A 1 361 ? -15.279 9.838   -9.941  1.00 29.39  ? 341 GLN A OE1 1 
ATOM   2429 N  NE2 . GLN A 1 361 ? -13.817 10.825  -11.334 1.00 26.75  ? 341 GLN A NE2 1 
ATOM   2430 N  N   . PRO A 1 362 ? -19.674 10.322  -13.412 1.00 17.18  ? 342 PRO A N   1 
ATOM   2431 C  CA  . PRO A 1 362 ? -20.373 11.286  -14.266 1.00 18.62  ? 342 PRO A CA  1 
ATOM   2432 C  C   . PRO A 1 362 ? -19.595 12.573  -14.457 1.00 18.44  ? 342 PRO A C   1 
ATOM   2433 O  O   . PRO A 1 362 ? -18.735 12.952  -13.658 1.00 20.19  ? 342 PRO A O   1 
ATOM   2434 C  CB  . PRO A 1 362 ? -21.667 11.568  -13.498 1.00 18.62  ? 342 PRO A CB  1 
ATOM   2435 C  CG  . PRO A 1 362 ? -21.791 10.460  -12.492 1.00 17.35  ? 342 PRO A CG  1 
ATOM   2436 C  CD  . PRO A 1 362 ? -20.400 10.060  -12.157 1.00 20.78  ? 342 PRO A CD  1 
ATOM   2437 N  N   . ASN A 1 363 ? -19.944 13.269  -15.528 1.00 19.46  ? 343 ASN A N   1 
ATOM   2438 C  CA  . ASN A 1 363 ? -19.540 14.663  -15.616 1.00 19.05  ? 343 ASN A CA  1 
ATOM   2439 C  C   . ASN A 1 363 ? -20.142 15.433  -14.448 1.00 22.54  ? 343 ASN A C   1 
ATOM   2440 O  O   . ASN A 1 363 ? -21.174 15.043  -13.881 1.00 20.25  ? 343 ASN A O   1 
ATOM   2441 C  CB  . ASN A 1 363 ? -19.970 15.256  -16.950 1.00 21.11  ? 343 ASN A CB  1 
ATOM   2442 C  CG  . ASN A 1 363 ? -19.070 14.810  -18.083 1.00 20.58  ? 343 ASN A CG  1 
ATOM   2443 O  OD1 . ASN A 1 363 ? -17.855 14.692  -17.909 1.00 25.31  ? 343 ASN A OD1 1 
ATOM   2444 N  ND2 . ASN A 1 363 ? -19.657 14.545  -19.245 1.00 27.21  ? 343 ASN A ND2 1 
ATOM   2445 N  N   . LEU A 1 364 ? -19.480 16.536  -14.084 1.00 22.88  ? 344 LEU A N   1 
ATOM   2446 C  CA  . LEU A 1 364 ? -19.864 17.247  -12.871 1.00 24.20  ? 344 LEU A CA  1 
ATOM   2447 C  C   . LEU A 1 364 ? -21.301 17.736  -12.938 1.00 26.24  ? 344 LEU A C   1 
ATOM   2448 O  O   . LEU A 1 364 ? -21.989 17.766  -11.912 1.00 26.56  ? 344 LEU A O   1 
ATOM   2449 C  CB  . LEU A 1 364 ? -18.909 18.417  -12.616 1.00 25.15  ? 344 LEU A CB  1 
ATOM   2450 C  CG  . LEU A 1 364 ? -17.438 18.014  -12.374 1.00 28.21  ? 344 LEU A CG  1 
ATOM   2451 C  CD1 . LEU A 1 364 ? -16.586 19.271  -12.264 1.00 30.23  ? 344 LEU A CD1 1 
ATOM   2452 C  CD2 . LEU A 1 364 ? -17.278 17.164  -11.135 1.00 27.97  ? 344 LEU A CD2 1 
ATOM   2453 N  N   . GLY A 1 365 ? -21.780 18.103  -14.128 1.00 22.45  ? 345 GLY A N   1 
ATOM   2454 C  CA  . GLY A 1 365 ? -23.149 18.566  -14.265 1.00 22.24  ? 345 GLY A CA  1 
ATOM   2455 C  C   . GLY A 1 365 ? -24.203 17.501  -14.440 1.00 26.00  ? 345 GLY A C   1 
ATOM   2456 O  O   . GLY A 1 365 ? -25.395 17.833  -14.486 1.00 26.14  ? 345 GLY A O   1 
ATOM   2457 N  N   . ASP A 1 366 ? -23.808 16.231  -14.534 1.00 22.51  ? 346 ASP A N   1 
ATOM   2458 C  CA  . ASP A 1 366 ? -24.782 15.160  -14.685 1.00 21.20  ? 346 ASP A CA  1 
ATOM   2459 C  C   . ASP A 1 366 ? -25.526 14.917  -13.383 1.00 23.44  ? 346 ASP A C   1 
ATOM   2460 O  O   . ASP A 1 366 ? -24.920 14.808  -12.315 1.00 22.46  ? 346 ASP A O   1 
ATOM   2461 C  CB  . ASP A 1 366 ? -24.103 13.855  -15.097 1.00 22.15  ? 346 ASP A CB  1 
ATOM   2462 C  CG  . ASP A 1 366 ? -23.544 13.899  -16.497 1.00 29.08  ? 346 ASP A CG  1 
ATOM   2463 O  OD1 . ASP A 1 366 ? -24.023 14.718  -17.310 1.00 32.59  ? 346 ASP A OD1 1 
ATOM   2464 O  OD2 . ASP A 1 366 ? -22.627 13.098  -16.773 1.00 30.62  ? 346 ASP A OD2 1 
ATOM   2465 N  N   . GLU A 1 367 ? -26.839 14.757  -13.483 1.00 21.95  ? 347 GLU A N   1 
ATOM   2466 C  CA  . GLU A 1 367 ? -27.623 14.445  -12.298 1.00 23.05  ? 347 GLU A CA  1 
ATOM   2467 C  C   . GLU A 1 367 ? -27.313 13.044  -11.790 1.00 24.72  ? 347 GLU A C   1 
ATOM   2468 O  O   . GLU A 1 367 ? -27.178 12.087  -12.562 1.00 23.73  ? 347 GLU A O   1 
ATOM   2469 C  CB  . GLU A 1 367 ? -29.115 14.580  -12.590 1.00 28.24  ? 347 GLU A CB  1 
ATOM   2470 C  CG  . GLU A 1 367 ? -29.547 16.016  -12.730 1.00 28.17  ? 347 GLU A CG  1 
ATOM   2471 C  CD  . GLU A 1 367 ? -31.055 16.179  -12.725 1.00 31.05  ? 347 GLU A CD  1 
ATOM   2472 O  OE1 . GLU A 1 367 ? -31.761 15.168  -12.914 1.00 38.58  ? 347 GLU A OE1 1 
ATOM   2473 O  OE2 . GLU A 1 367 ? -31.507 17.316  -12.526 1.00 42.09  ? 347 GLU A OE2 1 
ATOM   2474 N  N   . VAL A 1 368 ? -27.187 12.932  -10.473 1.00 20.58  ? 348 VAL A N   1 
ATOM   2475 C  CA  . VAL A 1 368 ? -27.027 11.656  -9.808  1.00 20.51  ? 348 VAL A CA  1 
ATOM   2476 C  C   . VAL A 1 368 ? -28.257 11.293  -8.986  1.00 22.90  ? 348 VAL A C   1 
ATOM   2477 O  O   . VAL A 1 368 ? -28.695 10.142  -8.992  1.00 26.77  ? 348 VAL A O   1 
ATOM   2478 C  CB  . VAL A 1 368 ? -25.758 11.679  -8.935  1.00 25.62  ? 348 VAL A CB  1 
ATOM   2479 C  CG1 . VAL A 1 368 ? -25.736 10.520  -7.981  1.00 37.88  ? 348 VAL A CG1 1 
ATOM   2480 C  CG2 . VAL A 1 368 ? -24.540 11.652  -9.837  1.00 22.43  ? 348 VAL A CG2 1 
ATOM   2481 N  N   . ASP A 1 369 ? -28.835 12.259  -8.280  1.00 25.17  ? 349 ASP A N   1 
ATOM   2482 C  CA  . ASP A 1 369 ? -30.132 12.074  -7.641  1.00 30.02  ? 349 ASP A CA  1 
ATOM   2483 C  C   . ASP A 1 369 ? -31.177 12.670  -8.570  1.00 34.19  ? 349 ASP A C   1 
ATOM   2484 O  O   . ASP A 1 369 ? -31.293 13.893  -8.670  1.00 30.76  ? 349 ASP A O   1 
ATOM   2485 C  CB  . ASP A 1 369 ? -30.167 12.732  -6.263  1.00 35.49  ? 349 ASP A CB  1 
ATOM   2486 C  CG  . ASP A 1 369 ? -31.426 12.398  -5.488  1.00 40.91  ? 349 ASP A CG  1 
ATOM   2487 O  OD1 . ASP A 1 369 ? -32.523 12.383  -6.088  1.00 36.35  ? 349 ASP A OD1 1 
ATOM   2488 O  OD2 . ASP A 1 369 ? -31.315 12.153  -4.268  1.00 50.09  ? 349 ASP A OD2 1 
ATOM   2489 N  N   . MET A 1 370 ? -31.918 11.807  -9.267  1.00 28.60  ? 350 MET A N   1 
ATOM   2490 C  CA  . MET A 1 370 ? -32.893 12.279  -10.241 1.00 38.69  ? 350 MET A CA  1 
ATOM   2491 C  C   . MET A 1 370 ? -34.123 12.886  -9.583  1.00 42.16  ? 350 MET A C   1 
ATOM   2492 O  O   . MET A 1 370 ? -34.873 13.610  -10.247 1.00 41.13  ? 350 MET A O   1 
ATOM   2493 C  CB  . MET A 1 370 ? -33.316 11.130  -11.159 1.00 39.04  ? 350 MET A CB  1 
ATOM   2494 C  CG  . MET A 1 370 ? -32.237 10.096  -11.415 1.00 55.27  ? 350 MET A CG  1 
ATOM   2495 S  SD  . MET A 1 370 ? -30.872 10.738  -12.399 1.00 59.04  ? 350 MET A SD  1 
ATOM   2496 C  CE  . MET A 1 370 ? -31.698 10.983  -13.968 1.00 40.99  ? 350 MET A CE  1 
ATOM   2497 N  N   . GLU A 1 371 ? -34.349 12.605  -8.299  1.00 43.51  ? 351 GLU A N   1 
ATOM   2498 C  CA  . GLU A 1 371 ? -35.526 13.130  -7.615  1.00 38.49  ? 351 GLU A CA  1 
ATOM   2499 C  C   . GLU A 1 371 ? -35.288 14.551  -7.119  1.00 41.79  ? 351 GLU A C   1 
ATOM   2500 O  O   . GLU A 1 371 ? -36.130 15.437  -7.315  1.00 39.81  ? 351 GLU A O   1 
ATOM   2501 C  CB  . GLU A 1 371 ? -35.909 12.217  -6.445  1.00 48.43  ? 351 GLU A CB  1 
ATOM   2502 C  CG  . GLU A 1 371 ? -35.883 10.726  -6.766  1.00 65.72  ? 351 GLU A CG  1 
ATOM   2503 C  CD  . GLU A 1 371 ? -36.953 10.314  -7.762  1.00 76.84  ? 351 GLU A CD  1 
ATOM   2504 O  OE1 . GLU A 1 371 ? -38.058 10.898  -7.731  1.00 76.69  ? 351 GLU A OE1 1 
ATOM   2505 O  OE2 . GLU A 1 371 ? -36.684 9.404   -8.578  1.00 77.15  ? 351 GLU A OE2 1 
ATOM   2506 N  N   . GLN A 1 372 ? -34.152 14.779  -6.464  1.00 38.07  ? 352 GLN A N   1 
ATOM   2507 C  CA  . GLN A 1 372 ? -33.789 16.092  -5.951  1.00 39.22  ? 352 GLN A CA  1 
ATOM   2508 C  C   . GLN A 1 372 ? -32.953 16.906  -6.925  1.00 35.83  ? 352 GLN A C   1 
ATOM   2509 O  O   . GLN A 1 372 ? -32.696 18.083  -6.654  1.00 39.16  ? 352 GLN A O   1 
ATOM   2510 C  CB  . GLN A 1 372 ? -33.020 15.955  -4.633  1.00 44.55  ? 352 GLN A CB  1 
ATOM   2511 C  CG  . GLN A 1 372 ? -33.844 15.442  -3.469  1.00 58.33  ? 352 GLN A CG  1 
ATOM   2512 C  CD  . GLN A 1 372 ? -33.230 15.808  -2.132  1.00 66.03  ? 352 GLN A CD  1 
ATOM   2513 O  OE1 . GLN A 1 372 ? -32.940 16.978  -1.866  1.00 63.50  ? 352 GLN A OE1 1 
ATOM   2514 N  NE2 . GLN A 1 372 ? -33.021 14.808  -1.283  1.00 67.88  ? 352 GLN A NE2 1 
ATOM   2515 N  N   . HIS A 1 373 ? -32.503 16.302  -8.030  1.00 32.35  ? 353 HIS A N   1 
ATOM   2516 C  CA  . HIS A 1 373 ? -31.748 16.998  -9.077  1.00 31.88  ? 353 HIS A CA  1 
ATOM   2517 C  C   . HIS A 1 373 ? -30.365 17.418  -8.590  1.00 33.80  ? 353 HIS A C   1 
ATOM   2518 O  O   . HIS A 1 373 ? -29.857 18.478  -8.952  1.00 40.22  ? 353 HIS A O   1 
ATOM   2519 C  CB  . HIS A 1 373 ? -32.527 18.193  -9.630  1.00 33.94  ? 353 HIS A CB  1 
ATOM   2520 C  CG  . HIS A 1 373 ? -33.886 17.823  -10.122 1.00 40.98  ? 353 HIS A CG  1 
ATOM   2521 N  ND1 . HIS A 1 373 ? -34.080 16.988  -11.201 1.00 42.24  ? 353 HIS A ND1 1 
ATOM   2522 C  CD2 . HIS A 1 373 ? -35.118 18.125  -9.652  1.00 39.16  ? 353 HIS A CD2 1 
ATOM   2523 C  CE1 . HIS A 1 373 ? -35.376 16.814  -11.391 1.00 44.22  ? 353 HIS A CE1 1 
ATOM   2524 N  NE2 . HIS A 1 373 ? -36.027 17.496  -10.467 1.00 43.57  ? 353 HIS A NE2 1 
ATOM   2525 N  N   . ILE A 1 374 ? -29.742 16.562  -7.793  1.00 28.77  ? 354 ILE A N   1 
ATOM   2526 C  CA  . ILE A 1 374 ? -28.390 16.789  -7.308  1.00 27.51  ? 354 ILE A CA  1 
ATOM   2527 C  C   . ILE A 1 374 ? -27.416 16.241  -8.339  1.00 26.58  ? 354 ILE A C   1 
ATOM   2528 O  O   . ILE A 1 374 ? -27.491 15.065  -8.713  1.00 26.10  ? 354 ILE A O   1 
ATOM   2529 C  CB  . ILE A 1 374 ? -28.184 16.120  -5.941  1.00 26.90  ? 354 ILE A CB  1 
ATOM   2530 C  CG1 . ILE A 1 374 ? -29.169 16.705  -4.923  1.00 32.93  ? 354 ILE A CG1 1 
ATOM   2531 C  CG2 . ILE A 1 374 ? -26.752 16.292  -5.472  1.00 27.41  ? 354 ILE A CG2 1 
ATOM   2532 C  CD1 . ILE A 1 374 ? -29.126 16.014  -3.585  1.00 36.58  ? 354 ILE A CD1 1 
ATOM   2533 N  N   . THR A 1 375 ? -26.501 17.091  -8.789  1.00 26.97  ? 355 THR A N   1 
ATOM   2534 C  CA  . THR A 1 375 ? -25.515 16.715  -9.789  1.00 24.43  ? 355 THR A CA  1 
ATOM   2535 C  C   . THR A 1 375 ? -24.308 16.037  -9.141  1.00 26.21  ? 355 THR A C   1 
ATOM   2536 O  O   . THR A 1 375 ? -24.102 16.085  -7.925  1.00 28.88  ? 355 THR A O   1 
ATOM   2537 C  CB  . THR A 1 375 ? -25.038 17.939  -10.562 1.00 30.74  ? 355 THR A CB  1 
ATOM   2538 O  OG1 . THR A 1 375 ? -24.394 18.839  -9.652  1.00 32.45  ? 355 THR A OG1 1 
ATOM   2539 C  CG2 . THR A 1 375 ? -26.194 18.643  -11.224 1.00 32.42  ? 355 THR A CG2 1 
ATOM   2540 N  N   . PHE A 1 376 ? -23.479 15.414  -9.980  1.00 21.30  ? 356 PHE A N   1 
ATOM   2541 C  CA  . PHE A 1 376 ? -22.308 14.730  -9.451  1.00 21.16  ? 356 PHE A CA  1 
ATOM   2542 C  C   . PHE A 1 376 ? -21.356 15.704  -8.761  1.00 21.84  ? 356 PHE A C   1 
ATOM   2543 O  O   . PHE A 1 376 ? -20.794 15.384  -7.713  1.00 24.38  ? 356 PHE A O   1 
ATOM   2544 C  CB  . PHE A 1 376 ? -21.589 13.962  -10.564 1.00 20.17  ? 356 PHE A CB  1 
ATOM   2545 C  CG  . PHE A 1 376 ? -20.404 13.162  -10.079 1.00 18.58  ? 356 PHE A CG  1 
ATOM   2546 C  CD1 . PHE A 1 376 ? -20.579 12.132  -9.168  1.00 24.04  ? 356 PHE A CD1 1 
ATOM   2547 C  CD2 . PHE A 1 376 ? -19.134 13.440  -10.532 1.00 25.48  ? 356 PHE A CD2 1 
ATOM   2548 C  CE1 . PHE A 1 376 ? -19.501 11.401  -8.717  1.00 24.66  ? 356 PHE A CE1 1 
ATOM   2549 C  CE2 . PHE A 1 376 ? -18.048 12.705  -10.089 1.00 26.17  ? 356 PHE A CE2 1 
ATOM   2550 C  CZ  . PHE A 1 376 ? -18.236 11.688  -9.182  1.00 23.90  ? 356 PHE A CZ  1 
ATOM   2551 N  N   . GLY A 1 377 ? -21.147 16.886  -9.337  1.00 26.75  ? 357 GLY A N   1 
ATOM   2552 C  CA  . GLY A 1 377 ? -20.295 17.873  -8.683  1.00 28.57  ? 357 GLY A CA  1 
ATOM   2553 C  C   . GLY A 1 377 ? -20.813 18.285  -7.317  1.00 29.69  ? 357 GLY A C   1 
ATOM   2554 O  O   . GLY A 1 377 ? -20.046 18.410  -6.351  1.00 29.72  ? 357 GLY A O   1 
ATOM   2555 N  N   . GLU A 1 378 ? -22.124 18.499  -7.212  1.00 24.53  ? 358 GLU A N   1 
ATOM   2556 C  CA  . GLU A 1 378 ? -22.709 18.780  -5.908  1.00 29.55  ? 358 GLU A CA  1 
ATOM   2557 C  C   . GLU A 1 378 ? -22.504 17.597  -4.971  1.00 30.50  ? 358 GLU A C   1 
ATOM   2558 O  O   . GLU A 1 378 ? -22.010 17.753  -3.846  1.00 32.35  ? 358 GLU A O   1 
ATOM   2559 C  CB  . GLU A 1 378 ? -24.196 19.118  -6.074  1.00 26.19  ? 358 GLU A CB  1 
ATOM   2560 C  CG  . GLU A 1 378 ? -24.417 20.416  -6.845  1.00 29.66  ? 358 GLU A CG  1 
ATOM   2561 C  CD  . GLU A 1 378 ? -25.798 20.554  -7.464  1.00 38.25  ? 358 GLU A CD  1 
ATOM   2562 O  OE1 . GLU A 1 378 ? -26.619 19.614  -7.380  1.00 31.59  ? 358 GLU A OE1 1 
ATOM   2563 O  OE2 . GLU A 1 378 ? -26.065 21.624  -8.044  1.00 40.38  ? 358 GLU A OE2 1 
ATOM   2564 N  N   . PHE A 1 379 ? -22.862 16.398  -5.445  1.00 26.84  ? 359 PHE A N   1 
ATOM   2565 C  CA  . PHE A 1 379 ? -22.691 15.152  -4.703  1.00 29.74  ? 359 PHE A CA  1 
ATOM   2566 C  C   . PHE A 1 379 ? -21.271 15.017  -4.166  1.00 38.70  ? 359 PHE A C   1 
ATOM   2567 O  O   . PHE A 1 379 ? -21.064 14.585  -3.027  1.00 35.26  ? 359 PHE A O   1 
ATOM   2568 C  CB  . PHE A 1 379 ? -23.062 13.999  -5.647  1.00 30.76  ? 359 PHE A CB  1 
ATOM   2569 C  CG  . PHE A 1 379 ? -22.959 12.610  -5.054  1.00 38.02  ? 359 PHE A CG  1 
ATOM   2570 C  CD1 . PHE A 1 379 ? -23.968 12.108  -4.239  1.00 44.61  ? 359 PHE A CD1 1 
ATOM   2571 C  CD2 . PHE A 1 379 ? -21.906 11.773  -5.400  1.00 36.78  ? 359 PHE A CD2 1 
ATOM   2572 C  CE1 . PHE A 1 379 ? -23.896 10.816  -3.727  1.00 46.99  ? 359 PHE A CE1 1 
ATOM   2573 C  CE2 . PHE A 1 379 ? -21.824 10.476  -4.891  1.00 33.64  ? 359 PHE A CE2 1 
ATOM   2574 C  CZ  . PHE A 1 379 ? -22.824 10.001  -4.054  1.00 35.99  ? 359 PHE A CZ  1 
ATOM   2575 N  N   . ALA A 1 380 ? -20.286 15.431  -4.962  1.00 29.60  ? 360 ALA A N   1 
ATOM   2576 C  CA  . ALA A 1 380 ? -18.882 15.304  -4.600  1.00 32.70  ? 360 ALA A CA  1 
ATOM   2577 C  C   . ALA A 1 380 ? -18.453 16.370  -3.610  1.00 42.24  ? 360 ALA A C   1 
ATOM   2578 O  O   . ALA A 1 380 ? -17.510 16.148  -2.843  1.00 41.59  ? 360 ALA A O   1 
ATOM   2579 C  CB  . ALA A 1 380 ? -18.011 15.376  -5.857  1.00 31.91  ? 360 ALA A CB  1 
ATOM   2580 N  N   . ARG A 1 381 ? -19.118 17.526  -3.606  1.00 37.34  ? 361 ARG A N   1 
ATOM   2581 C  CA  . ARG A 1 381 ? -18.856 18.526  -2.581  1.00 31.89  ? 361 ARG A CA  1 
ATOM   2582 C  C   . ARG A 1 381 ? -19.662 18.300  -1.306  1.00 37.07  ? 361 ARG A C   1 
ATOM   2583 O  O   . ARG A 1 381 ? -19.674 19.168  -0.433  1.00 40.35  ? 361 ARG A O   1 
ATOM   2584 C  CB  . ARG A 1 381 ? -19.119 19.927  -3.127  1.00 39.65  ? 361 ARG A CB  1 
ATOM   2585 C  CG  . ARG A 1 381 ? -18.011 20.411  -4.037  1.00 44.96  ? 361 ARG A CG  1 
ATOM   2586 C  CD  . ARG A 1 381 ? -16.656 20.280  -3.349  1.00 52.57  ? 361 ARG A CD  1 
ATOM   2587 N  NE  . ARG A 1 381 ? -15.578 20.767  -4.199  1.00 56.26  ? 361 ARG A NE  1 
ATOM   2588 C  CZ  . ARG A 1 381 ? -14.735 19.987  -4.861  1.00 48.62  ? 361 ARG A CZ  1 
ATOM   2589 N  NH1 . ARG A 1 381 ? -14.770 18.669  -4.741  1.00 52.87  ? 361 ARG A NH1 1 
ATOM   2590 N  NH2 . ARG A 1 381 ? -13.829 20.545  -5.660  1.00 52.54  ? 361 ARG A NH2 1 
ATOM   2591 N  N   . GLY A 1 382 ? -20.323 17.155  -1.169  1.00 37.36  ? 362 GLY A N   1 
ATOM   2592 C  CA  . GLY A 1 382 ? -21.072 16.884  0.038   1.00 42.65  ? 362 GLY A CA  1 
ATOM   2593 C  C   . GLY A 1 382 ? -22.407 17.578  0.125   1.00 40.43  ? 362 GLY A C   1 
ATOM   2594 O  O   . GLY A 1 382 ? -22.969 17.675  1.224   1.00 43.24  ? 362 GLY A O   1 
ATOM   2595 N  N   . ILE A 1 383 ? -22.927 18.079  -0.991  1.00 38.07  ? 363 ILE A N   1 
ATOM   2596 C  CA  . ILE A 1 383 ? -24.267 18.648  -1.022  1.00 38.52  ? 363 ILE A CA  1 
ATOM   2597 C  C   . ILE A 1 383 ? -25.270 17.505  -1.052  1.00 39.09  ? 363 ILE A C   1 
ATOM   2598 O  O   . ILE A 1 383 ? -25.139 16.568  -1.847  1.00 44.55  ? 363 ILE A O   1 
ATOM   2599 C  CB  . ILE A 1 383 ? -24.428 19.572  -2.238  1.00 32.30  ? 363 ILE A CB  1 
ATOM   2600 C  CG1 . ILE A 1 383 ? -23.532 20.805  -2.077  1.00 40.93  ? 363 ILE A CG1 1 
ATOM   2601 C  CG2 . ILE A 1 383 ? -25.878 19.953  -2.432  1.00 40.74  ? 363 ILE A CG2 1 
ATOM   2602 C  CD1 . ILE A 1 383 ? -23.499 21.710  -3.291  1.00 44.26  ? 363 ILE A CD1 1 
ATOM   2603 N  N   . VAL A 1 384 ? -26.266 17.560  -0.173  1.00 41.70  ? 364 VAL A N   1 
ATOM   2604 C  CA  . VAL A 1 384 ? -27.220 16.469  -0.032  1.00 48.72  ? 364 VAL A CA  1 
ATOM   2605 C  C   . VAL A 1 384 ? -28.654 16.929  -0.203  1.00 45.79  ? 364 VAL A C   1 
ATOM   2606 O  O   . VAL A 1 384 ? -29.567 16.097  -0.176  1.00 53.51  ? 364 VAL A O   1 
ATOM   2607 C  CB  . VAL A 1 384 ? -27.048 15.740  1.316   1.00 44.15  ? 364 VAL A CB  1 
ATOM   2608 C  CG1 . VAL A 1 384 ? -25.686 15.067  1.382   1.00 48.74  ? 364 VAL A CG1 1 
ATOM   2609 C  CG2 . VAL A 1 384 ? -27.231 16.711  2.469   1.00 37.29  ? 364 VAL A CG2 1 
ATOM   2610 N  N   . ALA A 1 385 ? -28.880 18.227  -0.386  1.00 39.56  ? 365 ALA A N   1 
ATOM   2611 C  CA  . ALA A 1 385 ? -30.202 18.769  -0.647  1.00 46.19  ? 365 ALA A CA  1 
ATOM   2612 C  C   . ALA A 1 385 ? -30.062 19.907  -1.643  1.00 46.16  ? 365 ALA A C   1 
ATOM   2613 O  O   . ALA A 1 385 ? -29.049 20.609  -1.666  1.00 45.98  ? 365 ALA A O   1 
ATOM   2614 C  CB  . ALA A 1 385 ? -30.877 19.274  0.636   1.00 45.33  ? 365 ALA A CB  1 
ATOM   2615 N  N   . LYS A 1 386 ? -31.083 20.087  -2.472  1.00 49.20  ? 366 LYS A N   1 
ATOM   2616 C  CA  . LYS A 1 386 ? -31.008 21.100  -3.511  1.00 48.06  ? 366 LYS A CA  1 
ATOM   2617 C  C   . LYS A 1 386 ? -32.309 21.875  -3.597  1.00 55.26  ? 366 LYS A C   1 
ATOM   2618 O  O   . LYS A 1 386 ? -33.391 21.283  -3.617  1.00 59.77  ? 366 LYS A O   1 
ATOM   2619 C  CB  . LYS A 1 386 ? -30.691 20.489  -4.870  1.00 47.74  ? 366 LYS A CB  1 
ATOM   2620 C  CG  . LYS A 1 386 ? -30.609 21.515  -5.971  1.00 50.13  ? 366 LYS A CG  1 
ATOM   2621 C  CD  . LYS A 1 386 ? -29.385 21.275  -6.813  1.00 49.35  ? 366 LYS A CD  1 
ATOM   2622 C  CE  . LYS A 1 386 ? -29.628 21.722  -8.227  1.00 51.51  ? 366 LYS A CE  1 
ATOM   2623 N  NZ  . LYS A 1 386 ? -28.695 21.023  -9.123  1.00 33.36  ? 366 LYS A NZ  1 
ATOM   2624 N  N   . ASN A 1 387 ? -32.178 23.204  -3.655  1.00 49.63  ? 367 ASN A N   1 
ATOM   2625 C  CA  . ASN A 1 387 ? -33.304 24.128  -3.798  1.00 63.20  ? 367 ASN A CA  1 
ATOM   2626 C  C   . ASN A 1 387 ? -34.407 23.841  -2.789  1.00 64.45  ? 367 ASN A C   1 
ATOM   2627 O  O   . ASN A 1 387 ? -35.591 24.051  -3.067  1.00 64.56  ? 367 ASN A O   1 
ATOM   2628 C  CB  . ASN A 1 387 ? -33.852 24.122  -5.227  1.00 64.96  ? 367 ASN A CB  1 
ATOM   2629 C  CG  . ASN A 1 387 ? -33.011 24.966  -6.177  1.00 75.52  ? 367 ASN A CG  1 
ATOM   2630 O  OD1 . ASN A 1 387 ? -32.491 26.020  -5.801  1.00 67.00  ? 367 ASN A OD1 1 
ATOM   2631 N  ND2 . ASN A 1 387 ? -32.872 24.502  -7.414  1.00 80.43  ? 367 ASN A ND2 1 
ATOM   2632 N  N   . THR A 1 388 ? -34.020 23.341  -1.616  1.00 63.08  ? 368 THR A N   1 
ATOM   2633 C  CA  . THR A 1 388 ? -34.924 23.344  -0.479  1.00 66.26  ? 368 THR A CA  1 
ATOM   2634 C  C   . THR A 1 388 ? -35.372 24.774  -0.218  1.00 69.22  ? 368 THR A C   1 
ATOM   2635 O  O   . THR A 1 388 ? -34.546 25.688  -0.153  1.00 70.42  ? 368 THR A O   1 
ATOM   2636 C  CB  . THR A 1 388 ? -34.232 22.763  0.756   1.00 64.05  ? 368 THR A CB  1 
ATOM   2637 O  OG1 . THR A 1 388 ? -34.013 21.360  0.566   1.00 60.56  ? 368 THR A OG1 1 
ATOM   2638 C  CG2 . THR A 1 388 ? -35.084 22.973  1.997   1.00 69.84  ? 368 THR A CG2 1 
ATOM   2639 N  N   . VAL A 1 389 ? -36.687 24.975  -0.107  1.00 73.94  ? 369 VAL A N   1 
ATOM   2640 C  CA  . VAL A 1 389 ? -37.199 26.330  0.035   1.00 61.24  ? 369 VAL A CA  1 
ATOM   2641 C  C   . VAL A 1 389 ? -36.638 26.954  1.304   1.00 66.07  ? 369 VAL A C   1 
ATOM   2642 O  O   . VAL A 1 389 ? -36.428 26.277  2.319   1.00 60.43  ? 369 VAL A O   1 
ATOM   2643 C  CB  . VAL A 1 389 ? -38.738 26.342  0.034   1.00 66.82  ? 369 VAL A CB  1 
ATOM   2644 C  CG1 . VAL A 1 389 ? -39.272 25.563  -1.160  1.00 69.55  ? 369 VAL A CG1 1 
ATOM   2645 C  CG2 . VAL A 1 389 ? -39.295 25.792  1.347   1.00 59.31  ? 369 VAL A CG2 1 
ATOM   2646 N  N   . SER A 1 390 ? -36.353 28.247  1.235   1.00 58.22  ? 370 SER A N   1 
ATOM   2647 C  CA  . SER A 1 390 ? -35.930 28.989  2.411   1.00 53.59  ? 370 SER A CA  1 
ATOM   2648 C  C   . SER A 1 390 ? -37.165 29.577  3.069   1.00 55.08  ? 370 SER A C   1 
ATOM   2649 O  O   . SER A 1 390 ? -37.717 28.990  3.997   1.00 58.73  ? 370 SER A O   1 
ATOM   2650 C  CB  . SER A 1 390 ? -34.930 30.089  2.043   1.00 59.50  ? 370 SER A CB  1 
ATOM   2651 O  OG  . SER A 1 390 ? -34.648 30.923  3.155   1.00 56.55  ? 370 SER A OG  1 
ATOM   2652 O  OXT . SER A 1 390 ? -37.639 30.634  2.670   1.00 56.66  ? 370 SER A OXT 1 
HETATM 2653 FE FE  . FE  B 2 .   ? -12.535 0.695   -3.928  1.00 18.37  ? 401 FE  A FE  1 
HETATM 2654 O  O   . HOH C 3 .   ? -10.617 1.032   2.768   1.00 32.14  ? 501 HOH A O   1 
HETATM 2655 O  O   . HOH C 3 .   ? -25.013 30.048  -10.763 1.00 44.42  ? 502 HOH A O   1 
HETATM 2656 O  O   . HOH C 3 .   ? 11.502  -9.076  0.765   1.00 42.89  ? 503 HOH A O   1 
HETATM 2657 O  O   . HOH C 3 .   ? -17.515 7.113   -1.377  1.00 37.83  ? 504 HOH A O   1 
HETATM 2658 O  O   . HOH C 3 .   ? 4.695   8.277   -23.375 1.00 30.82  ? 505 HOH A O   1 
HETATM 2659 O  O   . HOH C 3 .   ? -8.289  -10.550 -4.745  1.00 33.87  ? 506 HOH A O   1 
HETATM 2660 O  O   . HOH C 3 .   ? -15.386 10.668  -29.816 1.00 30.55  ? 507 HOH A O   1 
HETATM 2661 O  O   . HOH C 3 .   ? -22.811 13.450  -20.894 1.00 28.01  ? 508 HOH A O   1 
HETATM 2662 O  O   . HOH C 3 .   ? 14.905  -4.809  -16.406 1.00 42.87  ? 509 HOH A O   1 
HETATM 2663 O  O   . HOH C 3 .   ? -4.309  12.016  -23.987 1.00 34.17  ? 510 HOH A O   1 
HETATM 2664 O  O   . HOH C 3 .   ? -30.852 1.328   -22.818 1.00 34.88  ? 511 HOH A O   1 
HETATM 2665 O  O   . HOH C 3 .   ? -4.765  5.203   -3.323  1.00 40.97  ? 512 HOH A O   1 
HETATM 2666 O  O   . HOH C 3 .   ? -22.436 -14.166 -19.815 1.00 29.48  ? 513 HOH A O   1 
HETATM 2667 O  O   . HOH C 3 .   ? -4.587  -3.972  -10.736 1.00 29.70  ? 514 HOH A O   1 
HETATM 2668 O  O   . HOH C 3 .   ? 11.005  18.201  -21.643 1.00 41.69  ? 515 HOH A O   1 
HETATM 2669 O  O   . HOH C 3 .   ? -22.812 14.288  -1.273  1.00 47.66  ? 516 HOH A O   1 
HETATM 2670 O  O   . HOH C 3 .   ? -22.623 15.061  -19.350 1.00 39.89  ? 517 HOH A O   1 
HETATM 2671 O  O   . HOH C 3 .   ? -18.733 14.714  -22.919 1.00 34.67  ? 518 HOH A O   1 
HETATM 2672 O  O   . HOH C 3 .   ? 8.450   13.353  -6.309  1.00 50.18  ? 519 HOH A O   1 
HETATM 2673 O  O   . HOH C 3 .   ? -2.201  17.521  -20.624 1.00 41.58  ? 520 HOH A O   1 
HETATM 2674 O  O   . HOH C 3 .   ? -12.560 -0.031  -5.896  1.00 20.30  ? 521 HOH A O   1 
HETATM 2675 O  O   . HOH C 3 .   ? -6.923  -2.733  -9.615  1.00 32.99  ? 522 HOH A O   1 
HETATM 2676 O  O   . HOH C 3 .   ? 13.120  -1.601  -6.696  1.00 40.88  ? 523 HOH A O   1 
HETATM 2677 O  O   . HOH C 3 .   ? 15.427  -11.709 -6.568  1.00 43.68  ? 524 HOH A O   1 
HETATM 2678 O  O   . HOH C 3 .   ? 9.764   -7.781  -0.615  1.00 45.12  ? 525 HOH A O   1 
HETATM 2679 O  O   . HOH C 3 .   ? -21.518 12.221  -18.929 1.00 32.99  ? 526 HOH A O   1 
HETATM 2680 O  O   . HOH C 3 .   ? -4.930  11.866  -27.003 1.00 43.51  ? 527 HOH A O   1 
HETATM 2681 O  O   . HOH C 3 .   ? 10.049  0.241   -6.533  1.00 25.91  ? 528 HOH A O   1 
HETATM 2682 O  O   . HOH C 3 .   ? 0.194   8.218   -3.606  1.00 35.27  ? 529 HOH A O   1 
HETATM 2683 O  O   . HOH C 3 .   ? -12.833 -15.247 -5.963  1.00 33.31  ? 530 HOH A O   1 
HETATM 2684 O  O   . HOH C 3 .   ? 3.365   -14.821 -14.066 1.00 34.45  ? 531 HOH A O   1 
HETATM 2685 O  O   . HOH C 3 .   ? -2.835  20.070  -14.458 1.00 42.61  ? 532 HOH A O   1 
HETATM 2686 O  O   . HOH C 3 .   ? -38.085 2.803   -16.773 1.00 27.13  ? 533 HOH A O   1 
HETATM 2687 O  O   . HOH C 3 .   ? -24.116 1.551   -0.236  1.00 37.21  ? 534 HOH A O   1 
HETATM 2688 O  O   . HOH C 3 .   ? -0.767  11.447  -7.838  1.00 27.82  ? 535 HOH A O   1 
HETATM 2689 O  O   . HOH C 3 .   ? -8.907  -16.967 1.620   1.00 45.16  ? 536 HOH A O   1 
HETATM 2690 O  O   . HOH C 3 .   ? -1.517  -9.371  3.631   1.00 32.17  ? 537 HOH A O   1 
HETATM 2691 O  O   . HOH C 3 .   ? -2.845  -11.501 -11.349 1.00 33.87  ? 538 HOH A O   1 
HETATM 2692 O  O   . HOH C 3 .   ? -28.067 1.973   -22.237 1.00 22.70  ? 539 HOH A O   1 
HETATM 2693 O  O   . HOH C 3 .   ? -40.810 -4.009  -16.424 1.00 45.56  ? 540 HOH A O   1 
HETATM 2694 O  O   . HOH C 3 .   ? 4.946   -0.218  0.012   1.00 40.52  ? 541 HOH A O   1 
HETATM 2695 O  O   . HOH C 3 .   ? -15.718 7.120   -18.817 1.00 18.84  ? 542 HOH A O   1 
HETATM 2696 O  O   . HOH C 3 .   ? -1.706  -9.747  -18.175 1.00 24.22  ? 543 HOH A O   1 
HETATM 2697 O  O   . HOH C 3 .   ? -13.981 8.907   -20.093 1.00 21.26  ? 544 HOH A O   1 
HETATM 2698 O  O   . HOH C 3 .   ? -32.622 -4.619  -6.984  1.00 32.49  ? 545 HOH A O   1 
HETATM 2699 O  O   . HOH C 3 .   ? -14.429 -15.051 -12.472 1.00 33.22  ? 546 HOH A O   1 
HETATM 2700 O  O   . HOH C 3 .   ? 1.400   -11.061 -10.173 1.00 26.56  ? 547 HOH A O   1 
HETATM 2701 O  O   . HOH C 3 .   ? -26.434 20.265  -14.627 1.00 37.10  ? 548 HOH A O   1 
HETATM 2702 O  O   . HOH C 3 .   ? -11.211 16.044  -16.719 1.00 31.26  ? 549 HOH A O   1 
HETATM 2703 O  O   . HOH C 3 .   ? 11.927  6.514   -7.359  1.00 40.39  ? 550 HOH A O   1 
HETATM 2704 O  O   . HOH C 3 .   ? -20.303 -10.667 -7.534  1.00 21.52  ? 551 HOH A O   1 
HETATM 2705 O  O   . HOH C 3 .   ? -0.433  0.637   -27.186 1.00 45.30  ? 552 HOH A O   1 
HETATM 2706 O  O   . HOH C 3 .   ? -38.900 6.767   -18.387 1.00 42.06  ? 553 HOH A O   1 
HETATM 2707 O  O   . HOH C 3 .   ? -33.502 6.902   -10.291 1.00 33.86  ? 554 HOH A O   1 
HETATM 2708 O  O   . HOH C 3 .   ? -3.750  7.307   -4.414  1.00 35.18  ? 555 HOH A O   1 
HETATM 2709 O  O   . HOH C 3 .   ? -36.860 11.001  -14.593 1.00 52.73  ? 556 HOH A O   1 
HETATM 2710 O  O   . HOH C 3 .   ? 5.451   -16.560 -0.263  1.00 42.01  ? 557 HOH A O   1 
HETATM 2711 O  O   . HOH C 3 .   ? -2.272  -3.828  2.561   1.00 35.94  ? 558 HOH A O   1 
HETATM 2712 O  O   . HOH C 3 .   ? 9.400   12.691  -17.782 1.00 39.30  ? 559 HOH A O   1 
HETATM 2713 O  O   . HOH C 3 .   ? -3.694  -13.484 -2.984  1.00 39.52  ? 560 HOH A O   1 
HETATM 2714 O  O   . HOH C 3 .   ? -4.081  -5.002  -5.045  1.00 42.53  ? 561 HOH A O   1 
HETATM 2715 O  O   . HOH C 3 .   ? -28.589 -8.670  -4.698  1.00 36.35  ? 562 HOH A O   1 
HETATM 2716 O  O   . HOH C 3 .   ? 7.807   15.761  -3.410  1.00 51.37  ? 563 HOH A O   1 
HETATM 2717 O  O   . HOH C 3 .   ? -5.621  13.812  -25.200 1.00 39.07  ? 564 HOH A O   1 
HETATM 2718 O  O   . HOH C 3 .   ? 0.361   15.023  -8.650  1.00 26.43  ? 565 HOH A O   1 
HETATM 2719 O  O   . HOH C 3 .   ? 4.973   13.278  -3.842  1.00 32.83  ? 566 HOH A O   1 
HETATM 2720 O  O   . HOH C 3 .   ? -11.030 13.610  -13.572 1.00 27.91  ? 567 HOH A O   1 
HETATM 2721 O  O   . HOH C 3 .   ? -7.610  13.347  -21.357 1.00 20.61  ? 568 HOH A O   1 
HETATM 2722 O  O   . HOH C 3 .   ? 12.316  -5.766  -0.031  1.00 58.49  ? 569 HOH A O   1 
HETATM 2723 O  O   . HOH C 3 .   ? 8.749   -11.081 -10.542 1.00 37.69  ? 570 HOH A O   1 
HETATM 2724 O  O   . HOH C 3 .   ? -7.866  0.337   -26.775 1.00 30.77  ? 571 HOH A O   1 
HETATM 2725 O  O   . HOH C 3 .   ? -23.304 -10.527 -0.041  1.00 35.73  ? 572 HOH A O   1 
HETATM 2726 O  O   . HOH C 3 .   ? 14.939  4.101   -15.598 1.00 31.08  ? 573 HOH A O   1 
HETATM 2727 O  O   . HOH C 3 .   ? -27.249 5.977   -23.833 1.00 39.87  ? 574 HOH A O   1 
HETATM 2728 O  O   . HOH C 3 .   ? 7.769   -5.926  -0.580  1.00 39.96  ? 575 HOH A O   1 
HETATM 2729 O  O   . HOH C 3 .   ? -4.037  -10.881 -18.334 1.00 31.77  ? 576 HOH A O   1 
HETATM 2730 O  O   . HOH C 3 .   ? -37.666 8.137   -11.607 1.00 43.04  ? 577 HOH A O   1 
HETATM 2731 O  O   . HOH C 3 .   ? -34.383 14.362  -13.195 1.00 46.18  ? 578 HOH A O   1 
HETATM 2732 O  O   . HOH C 3 .   ? 2.056   -11.541 -16.783 1.00 37.89  ? 579 HOH A O   1 
HETATM 2733 O  O   . HOH C 3 .   ? -24.693 -4.926  -22.330 1.00 25.52  ? 580 HOH A O   1 
HETATM 2734 O  O   . HOH C 3 .   ? -13.646 5.863   -2.111  1.00 34.37  ? 581 HOH A O   1 
HETATM 2735 O  O   . HOH C 3 .   ? -22.409 -10.688 -5.670  1.00 22.61  ? 582 HOH A O   1 
HETATM 2736 O  O   . HOH C 3 .   ? -16.889 -17.126 8.046   1.00 43.31  ? 583 HOH A O   1 
HETATM 2737 O  O   . HOH C 3 .   ? -17.921 9.132   -26.343 1.00 41.52  ? 584 HOH A O   1 
HETATM 2738 O  O   . HOH C 3 .   ? -6.777  -8.454  -14.734 1.00 20.16  ? 585 HOH A O   1 
HETATM 2739 O  O   . HOH C 3 .   ? -31.894 9.171   -8.407  1.00 32.44  ? 586 HOH A O   1 
HETATM 2740 O  O   . HOH C 3 .   ? 0.118   19.216  -18.903 1.00 42.08  ? 587 HOH A O   1 
HETATM 2741 O  O   . HOH C 3 .   ? -2.763  -10.765 -8.437  1.00 37.84  ? 588 HOH A O   1 
HETATM 2742 O  O   . HOH C 3 .   ? -29.420 -10.158 -29.056 1.00 38.13  ? 589 HOH A O   1 
HETATM 2743 O  O   . HOH C 3 .   ? -2.752  -9.723  -24.986 1.00 37.36  ? 590 HOH A O   1 
HETATM 2744 O  O   . HOH C 3 .   ? -5.657  -13.386 -9.591  1.00 50.66  ? 591 HOH A O   1 
HETATM 2745 O  O   . HOH C 3 .   ? 7.824   -13.832 -2.398  1.00 42.11  ? 592 HOH A O   1 
HETATM 2746 O  O   . HOH C 3 .   ? -15.653 8.094   -27.708 1.00 48.88  ? 593 HOH A O   1 
HETATM 2747 O  O   . HOH C 3 .   ? 12.899  3.492   -13.947 1.00 26.26  ? 594 HOH A O   1 
HETATM 2748 O  O   . HOH C 3 .   ? -16.182 18.046  -21.021 1.00 34.99  ? 595 HOH A O   1 
HETATM 2749 O  O   . HOH C 3 .   ? -7.489  -14.210 4.108   1.00 35.33  ? 596 HOH A O   1 
HETATM 2750 O  O   . HOH C 3 .   ? -18.200 0.523   -3.717  1.00 19.28  ? 597 HOH A O   1 
HETATM 2751 O  O   . HOH C 3 .   ? -17.573 -4.195  -3.648  1.00 21.00  ? 598 HOH A O   1 
HETATM 2752 O  O   . HOH C 3 .   ? -8.475  15.974  -14.249 1.00 35.59  ? 599 HOH A O   1 
HETATM 2753 O  O   . HOH C 3 .   ? -1.834  12.820  -15.769 1.00 22.97  ? 600 HOH A O   1 
HETATM 2754 O  O   . HOH C 3 .   ? -16.250 5.271   1.722   1.00 32.05  ? 601 HOH A O   1 
HETATM 2755 O  O   . HOH C 3 .   ? -4.394  13.679  -21.659 1.00 37.77  ? 602 HOH A O   1 
HETATM 2756 O  O   . HOH C 3 .   ? -28.221 14.718  -16.026 1.00 29.82  ? 603 HOH A O   1 
HETATM 2757 O  O   . HOH C 3 .   ? -24.597 -13.383 -27.418 1.00 40.41  ? 604 HOH A O   1 
HETATM 2758 O  O   . HOH C 3 .   ? -15.859 4.832   -10.226 1.00 20.51  ? 605 HOH A O   1 
HETATM 2759 O  O   . HOH C 3 .   ? 14.273  6.777   -18.380 1.00 41.14  ? 606 HOH A O   1 
HETATM 2760 O  O   . HOH C 3 .   ? 3.705   -5.750  5.625   1.00 48.96  ? 607 HOH A O   1 
HETATM 2761 O  O   . HOH C 3 .   ? -10.961 -2.721  -5.263  1.00 27.36  ? 608 HOH A O   1 
HETATM 2762 O  O   . HOH C 3 .   ? -15.244 10.890  -7.295  1.00 41.67  ? 609 HOH A O   1 
HETATM 2763 O  O   . HOH C 3 .   ? -8.480  -0.471  0.185   1.00 28.46  ? 610 HOH A O   1 
HETATM 2764 O  O   . HOH C 3 .   ? -5.266  -1.142  -5.904  1.00 34.60  ? 611 HOH A O   1 
HETATM 2765 O  O   . HOH C 3 .   ? -3.605  -6.938  -3.600  1.00 35.32  ? 612 HOH A O   1 
HETATM 2766 O  O   . HOH C 3 .   ? -14.076 6.210   -5.632  1.00 29.30  ? 613 HOH A O   1 
HETATM 2767 O  O   . HOH C 3 .   ? -4.904  1.637   -8.889  1.00 18.88  ? 614 HOH A O   1 
HETATM 2768 O  O   . HOH C 3 .   ? -1.889  -4.228  -28.229 1.00 49.51  ? 615 HOH A O   1 
HETATM 2769 O  O   . HOH C 3 .   ? -15.112 -12.975 7.734   1.00 39.17  ? 616 HOH A O   1 
HETATM 2770 O  O   . HOH C 3 .   ? -7.970  -6.256  -28.376 1.00 44.76  ? 617 HOH A O   1 
HETATM 2771 O  O   . HOH C 3 .   ? -40.524 2.153   -9.989  1.00 42.16  ? 618 HOH A O   1 
HETATM 2772 O  O   . HOH C 3 .   ? 2.328   4.355   -10.706 1.00 25.34  ? 619 HOH A O   1 
HETATM 2773 O  O   . HOH C 3 .   ? -14.201 -14.317 -8.233  1.00 35.75  ? 620 HOH A O   1 
HETATM 2774 O  O   . HOH C 3 .   ? 1.849   -5.419  -1.738  1.00 26.79  ? 621 HOH A O   1 
HETATM 2775 O  O   . HOH C 3 .   ? -7.952  19.950  -23.481 1.00 29.37  ? 622 HOH A O   1 
HETATM 2776 O  O   . HOH C 3 .   ? -5.579  -8.812  -7.512  1.00 40.33  ? 623 HOH A O   1 
HETATM 2777 O  O   . HOH C 3 .   ? -15.156 6.587   -8.205  1.00 24.84  ? 624 HOH A O   1 
HETATM 2778 O  O   . HOH C 3 .   ? -26.990 9.866   -20.176 1.00 39.75  ? 625 HOH A O   1 
HETATM 2779 O  O   . HOH C 3 .   ? -19.286 -2.026  -4.847  1.00 19.49  ? 626 HOH A O   1 
HETATM 2780 O  O   . HOH C 3 .   ? -13.591 3.927   -27.677 1.00 38.99  ? 627 HOH A O   1 
HETATM 2781 O  O   . HOH C 3 .   ? -20.571 18.974  -16.648 1.00 33.47  ? 628 HOH A O   1 
HETATM 2782 O  O   . HOH C 3 .   ? 23.109  -2.351  -20.964 1.00 42.74  ? 629 HOH A O   1 
HETATM 2783 O  O   . HOH C 3 .   ? 1.789   16.556  -20.093 1.00 36.19  ? 630 HOH A O   1 
HETATM 2784 O  O   . HOH C 3 .   ? -5.390  -15.660 -12.634 1.00 40.25  ? 631 HOH A O   1 
HETATM 2785 O  O   . HOH C 3 .   ? -11.067 18.027  -31.489 1.00 43.90  ? 632 HOH A O   1 
HETATM 2786 O  O   . HOH C 3 .   ? -40.195 4.534   -17.109 1.00 36.98  ? 633 HOH A O   1 
HETATM 2787 O  O   . HOH C 3 .   ? -20.926 -16.377 -12.294 1.00 31.64  ? 634 HOH A O   1 
HETATM 2788 O  O   . HOH C 3 .   ? -23.117 -3.552  -28.999 1.00 45.22  ? 635 HOH A O   1 
HETATM 2789 O  O   . HOH C 3 .   ? -28.670 13.151  -0.659  1.00 52.29  ? 636 HOH A O   1 
HETATM 2790 O  O   . HOH C 3 .   ? -6.417  -10.637 -23.397 1.00 36.56  ? 637 HOH A O   1 
HETATM 2791 O  O   . HOH C 3 .   ? -25.419 6.206   -2.961  1.00 35.79  ? 638 HOH A O   1 
HETATM 2792 O  O   . HOH C 3 .   ? -3.005  5.692   -27.778 1.00 47.51  ? 639 HOH A O   1 
HETATM 2793 O  O   . HOH C 3 .   ? -0.530  8.763   -27.561 1.00 45.69  ? 640 HOH A O   1 
HETATM 2794 O  O   . HOH C 3 .   ? -25.612 -4.701  -26.226 1.00 35.63  ? 641 HOH A O   1 
HETATM 2795 O  O   . HOH C 3 .   ? -32.295 -11.180 -18.538 1.00 36.36  ? 642 HOH A O   1 
HETATM 2796 O  O   . HOH C 3 .   ? -17.395 17.508  -16.026 1.00 32.69  ? 643 HOH A O   1 
HETATM 2797 O  O   . HOH C 3 .   ? -26.305 -14.985 -20.757 1.00 43.18  ? 644 HOH A O   1 
HETATM 2798 O  O   . HOH C 3 .   ? -25.101 -13.823 -18.736 1.00 29.07  ? 645 HOH A O   1 
HETATM 2799 O  O   . HOH C 3 .   ? 4.895   -3.559  -1.241  1.00 43.86  ? 646 HOH A O   1 
HETATM 2800 O  O   . HOH C 3 .   ? -3.602  -1.871  -0.321  1.00 41.39  ? 647 HOH A O   1 
HETATM 2801 O  O   . HOH C 3 .   ? -36.428 7.977   -21.636 1.00 42.73  ? 648 HOH A O   1 
HETATM 2802 O  O   . HOH C 3 .   ? 6.005   -2.209  -20.185 1.00 37.44  ? 649 HOH A O   1 
HETATM 2803 O  O   . HOH C 3 .   ? -7.143  -10.662 -7.374  1.00 37.02  ? 650 HOH A O   1 
HETATM 2804 O  O   . HOH C 3 .   ? 4.945   14.484  -22.253 1.00 42.99  ? 651 HOH A O   1 
HETATM 2805 O  O   . HOH C 3 .   ? -18.381 0.199   -25.820 1.00 34.87  ? 652 HOH A O   1 
HETATM 2806 O  O   . HOH C 3 .   ? -4.506  17.834  -25.354 1.00 38.83  ? 653 HOH A O   1 
HETATM 2807 O  O   . HOH C 3 .   ? -11.847 10.831  -8.959  1.00 39.17  ? 654 HOH A O   1 
HETATM 2808 O  O   . HOH C 3 .   ? -27.121 -5.341  -22.522 1.00 33.04  ? 655 HOH A O   1 
HETATM 2809 O  O   . HOH C 3 .   ? -19.587 -16.571 -3.137  1.00 38.22  ? 656 HOH A O   1 
HETATM 2810 O  O   . HOH C 3 .   ? -11.104 2.193   -4.702  1.00 24.32  ? 657 HOH A O   1 
HETATM 2811 O  O   . HOH C 3 .   ? -10.801 -0.702  -3.617  1.00 18.61  ? 658 HOH A O   1 
HETATM 2812 O  O   . HOH C 3 .   ? -17.617 1.851   4.405   1.00 39.55  ? 659 HOH A O   1 
HETATM 2813 O  O   . HOH C 3 .   ? -12.473 -20.078 2.549   1.00 46.42  ? 660 HOH A O   1 
HETATM 2814 O  O   . HOH C 3 .   ? -21.177 -14.490 1.585   1.00 41.23  ? 661 HOH A O   1 
HETATM 2815 O  O   . HOH C 3 .   ? -9.871  0.539   -6.658  1.00 32.37  ? 662 HOH A O   1 
HETATM 2816 O  O   . HOH C 3 .   ? -2.859  15.549  -22.691 1.00 49.08  ? 663 HOH A O   1 
HETATM 2817 O  O   . HOH C 3 .   ? -19.815 -16.283 -25.213 1.00 44.59  ? 664 HOH A O   1 
HETATM 2818 O  O   . HOH C 3 .   ? -24.670 22.000  -13.122 1.00 47.11  ? 665 HOH A O   1 
HETATM 2819 O  O   . HOH C 3 .   ? 4.305   -5.893  -2.214  1.00 41.24  ? 666 HOH A O   1 
HETATM 2820 O  O   . HOH C 3 .   ? -24.429 4.983   -0.435  1.00 49.34  ? 667 HOH A O   1 
HETATM 2821 O  O   . HOH C 3 .   ? -9.347  -19.330 1.586   1.00 49.35  ? 668 HOH A O   1 
HETATM 2822 O  O   . HOH C 3 .   ? -0.864  -12.066 -8.938  1.00 41.81  ? 669 HOH A O   1 
HETATM 2823 O  O   . HOH C 3 .   ? -30.950 14.529  -16.157 1.00 47.12  ? 670 HOH A O   1 
HETATM 2824 O  O   . HOH C 3 .   ? 11.985  0.697   -5.200  1.00 42.37  ? 671 HOH A O   1 
HETATM 2825 O  O   . HOH C 3 .   ? 1.239   -11.023 -21.108 1.00 42.78  ? 672 HOH A O   1 
HETATM 2826 O  O   . HOH C 3 .   ? -29.858 -0.574  -22.975 1.00 43.20  ? 673 HOH A O   1 
HETATM 2827 O  O   . HOH C 3 .   ? -26.572 -9.466  -31.276 1.00 50.47  ? 674 HOH A O   1 
HETATM 2828 O  O   . HOH C 3 .   ? -33.906 -10.484 -12.820 1.00 48.64  ? 675 HOH A O   1 
HETATM 2829 O  O   . HOH C 3 .   ? -34.986 6.214   -8.439  1.00 47.07  ? 676 HOH A O   1 
HETATM 2830 O  O   . HOH C 3 .   ? -11.981 4.868   -4.224  1.00 30.42  ? 677 HOH A O   1 
HETATM 2831 O  O   . HOH C 3 .   ? -15.246 -4.059  -26.282 1.00 43.58  ? 678 HOH A O   1 
HETATM 2832 O  O   . HOH C 3 .   ? -3.870  -9.409  -5.063  1.00 32.33  ? 679 HOH A O   1 
HETATM 2833 O  O   . HOH C 3 .   ? -3.443  -13.376 -18.450 1.00 38.83  ? 680 HOH A O   1 
HETATM 2834 O  O   . HOH C 3 .   ? 0.169   -11.492 -18.852 1.00 33.73  ? 681 HOH A O   1 
HETATM 2835 O  O   . HOH C 3 .   ? -35.152 7.867   -12.282 1.00 40.98  ? 682 HOH A O   1 
HETATM 2836 O  O   . HOH C 3 .   ? -2.752  -15.960 -3.543  1.00 44.00  ? 683 HOH A O   1 
HETATM 2837 O  O   . HOH C 3 .   ? -6.203  -12.316 -5.732  1.00 51.33  ? 684 HOH A O   1 
HETATM 2838 O  O   . HOH C 3 .   ? -22.659 -13.110 -4.473  1.00 31.50  ? 685 HOH A O   1 
HETATM 2839 O  O   . HOH C 3 .   ? -28.341 -4.357  -24.702 1.00 33.33  ? 686 HOH A O   1 
HETATM 2840 O  O   . HOH C 3 .   ? -13.596 -16.870 8.714   1.00 54.78  ? 687 HOH A O   1 
HETATM 2841 O  O   . HOH C 3 .   ? -19.736 -18.613 -14.304 1.00 54.52  ? 688 HOH A O   1 
HETATM 2842 O  O   . HOH C 3 .   ? 0.817   17.039  -22.478 1.00 46.87  ? 689 HOH A O   1 
HETATM 2843 O  O   . HOH C 3 .   ? -33.126 13.723  -17.108 1.00 57.61  ? 690 HOH A O   1 
HETATM 2844 O  O   . HOH C 3 .   ? -10.185 -8.590  8.109   1.00 50.74  ? 691 HOH A O   1 
HETATM 2845 O  O   . HOH C 3 .   ? -18.917 6.904   -31.690 1.00 51.85  ? 692 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   . GLY A 18  ? 0.5394 0.5297 0.7992 0.0136  -0.0558 0.2183  -2  GLY A N   
2    C  CA  . GLY A 18  ? 0.5290 0.5364 0.7740 0.0126  -0.0588 0.2326  -2  GLY A CA  
3    C  C   . GLY A 18  ? 0.5387 0.5593 0.7670 0.0058  -0.0548 0.2450  -2  GLY A C   
4    O  O   . GLY A 18  ? 0.5508 0.5734 0.7698 0.0036  -0.0478 0.2397  -2  GLY A O   
5    N  N   . SER A 19  ? 0.4896 0.5207 0.7144 0.0026  -0.0588 0.2615  -1  SER A N   
6    C  CA  . SER A 19  ? 0.5854 0.6318 0.7948 -0.0036 -0.0542 0.2738  -1  SER A CA  
7    C  C   . SER A 19  ? 0.6155 0.6786 0.7960 -0.0022 -0.0490 0.2711  -1  SER A C   
8    O  O   . SER A 19  ? 0.5742 0.6501 0.7406 -0.0062 -0.0425 0.2765  -1  SER A O   
9    C  CB  . SER A 19  ? 0.5697 0.6242 0.7821 -0.0071 -0.0600 0.2921  -1  SER A CB  
10   O  OG  . SER A 19  ? 0.6077 0.6732 0.8056 -0.0037 -0.0646 0.2963  -1  SER A OG  
11   N  N   . HIS A 20  ? 0.4788 0.5430 0.6509 0.0036  -0.0517 0.2627  0   HIS A N   
12   C  CA  . HIS A 20  ? 0.5970 0.6760 0.7416 0.0055  -0.0483 0.2588  0   HIS A CA  
13   C  C   . HIS A 20  ? 0.6449 0.7178 0.7864 0.0078  -0.0418 0.2439  0   HIS A C   
14   O  O   . HIS A 20  ? 0.5738 0.6571 0.6931 0.0097  -0.0386 0.2348  0   HIS A O   
15   C  CB  . HIS A 20  ? 0.5762 0.6614 0.7129 0.0099  -0.0564 0.2583  0   HIS A CB  
16   C  CG  . HIS A 20  ? 0.7535 0.8249 0.9103 0.0153  -0.0614 0.2474  0   HIS A CG  
17   N  ND1 . HIS A 20  ? 0.7421 0.7978 0.9263 0.0159  -0.0640 0.2469  0   HIS A ND1 
18   C  CD2 . HIS A 20  ? 0.7346 0.8070 0.8884 0.0204  -0.0640 0.2360  0   HIS A CD2 
19   C  CE1 . HIS A 20  ? 0.7587 0.8070 0.9552 0.0216  -0.0668 0.2352  0   HIS A CE1 
20   N  NE2 . HIS A 20  ? 0.8387 0.8973 1.0183 0.0241  -0.0670 0.2290  0   HIS A NE2 
21   N  N   . MET A 21  ? 0.4372 0.4934 0.5989 0.0073  -0.0394 0.2366  1   MET A N   
22   C  CA  . MET A 21  ? 0.4207 0.4710 0.5794 0.0087  -0.0327 0.2175  1   MET A CA  
23   C  C   . MET A 21  ? 0.3786 0.4383 0.5233 0.0043  -0.0237 0.2177  1   MET A C   
24   O  O   . MET A 21  ? 0.4456 0.5123 0.5910 -0.0003 -0.0225 0.2349  1   MET A O   
25   C  CB  . MET A 21  ? 0.4675 0.4972 0.6516 0.0099  -0.0337 0.2087  1   MET A CB  
26   C  CG  . MET A 21  ? 0.4689 0.4890 0.6704 0.0155  -0.0413 0.2064  1   MET A CG  
27   S  SD  . MET A 21  ? 0.5598 0.5844 0.7508 0.0211  -0.0399 0.1853  1   MET A SD  
28   C  CE  . MET A 21  ? 0.5715 0.6126 0.7500 0.0225  -0.0477 0.1984  1   MET A CE  
29   N  N   . ALA A 22  ? 0.3407 0.4013 0.4738 0.0058  -0.0174 0.1992  2   ALA A N   
30   C  CA  . ALA A 22  ? 0.3230 0.3908 0.4472 0.0027  -0.0088 0.1972  2   ALA A CA  
31   C  C   . ALA A 22  ? 0.3030 0.3579 0.4492 -0.0015 -0.0077 0.1992  2   ALA A C   
32   O  O   . ALA A 22  ? 0.4008 0.4387 0.5655 -0.0005 -0.0123 0.1943  2   ALA A O   
33   C  CB  . ALA A 22  ? 0.3537 0.4239 0.4620 0.0059  -0.0035 0.1769  2   ALA A CB  
34   N  N   . PRO A 23  ? 0.3280 0.3908 0.4731 -0.0061 -0.0018 0.2056  3   PRO A N   
35   C  CA  . PRO A 23  ? 0.2999 0.3500 0.4659 -0.0108 -0.0017 0.2057  3   PRO A CA  
36   C  C   . PRO A 23  ? 0.3238 0.3615 0.4918 -0.0081 -0.0002 0.1836  3   PRO A C   
37   O  O   . PRO A 23  ? 0.3109 0.3553 0.4625 -0.0051 0.0046  0.1706  3   PRO A O   
38   C  CB  . PRO A 23  ? 0.3395 0.4059 0.5011 -0.0160 0.0051  0.2165  3   PRO A CB  
39   C  CG  . PRO A 23  ? 0.4023 0.4886 0.5372 -0.0119 0.0108  0.2141  3   PRO A CG  
40   C  CD  . PRO A 23  ? 0.4012 0.4858 0.5274 -0.0074 0.0047  0.2139  3   PRO A CD  
41   N  N   . ILE A 24  ? 0.2831 0.3021 0.4709 -0.0090 -0.0049 0.1793  4   ILE A N   
42   C  CA  . ILE A 24  ? 0.2599 0.2674 0.4499 -0.0071 -0.0035 0.1594  4   ILE A CA  
43   C  C   . ILE A 24  ? 0.2702 0.2780 0.4648 -0.0127 0.0000  0.1581  4   ILE A C   
44   O  O   . ILE A 24  ? 0.3164 0.3220 0.5256 -0.0186 -0.0023 0.1710  4   ILE A O   
45   C  CB  . ILE A 24  ? 0.3943 0.3824 0.6019 -0.0044 -0.0098 0.1533  4   ILE A CB  
46   C  CG1 . ILE A 24  ? 0.5098 0.4998 0.7135 0.0019  -0.0128 0.1523  4   ILE A CG1 
47   C  CG2 . ILE A 24  ? 0.4138 0.3911 0.6234 -0.0035 -0.0079 0.1340  4   ILE A CG2 
48   C  CD1 . ILE A 24  ? 0.5834 0.5568 0.8045 0.0062  -0.0177 0.1444  4   ILE A CD1 
49   N  N   . ALA A 25  ? 0.2824 0.2937 0.4657 -0.0112 0.0048  0.1437  5   ALA A N   
50   C  CA  . ALA A 25  ? 0.2686 0.2805 0.4566 -0.0158 0.0074  0.1404  5   ALA A CA  
51   C  C   . ALA A 25  ? 0.3168 0.3133 0.5090 -0.0147 0.0054  0.1229  5   ALA A C   
52   O  O   . ALA A 25  ? 0.3730 0.3641 0.5587 -0.0094 0.0051  0.1113  5   ALA A O   
53   C  CB  . ALA A 25  ? 0.2932 0.3234 0.4648 -0.0149 0.0148  0.1393  5   ALA A CB  
54   N  N   . GLN A 26  ? 0.3095 0.3001 0.5127 -0.0200 0.0039  0.1212  6   GLN A N   
55   C  CA  . GLN A 26  ? 0.3363 0.3141 0.5415 -0.0196 0.0019  0.1046  6   GLN A CA  
56   C  C   . GLN A 26  ? 0.2673 0.2553 0.4603 -0.0197 0.0067  0.0968  6   GLN A C   
57   O  O   . GLN A 26  ? 0.3127 0.3111 0.5087 -0.0241 0.0086  0.1045  6   GLN A O   
58   C  CB  . GLN A 26  ? 0.4560 0.4194 0.6809 -0.0255 -0.0045 0.1064  6   GLN A CB  
59   C  CG  . GLN A 26  ? 0.6516 0.5987 0.8785 -0.0239 -0.0078 0.0884  6   GLN A CG  
60   C  CD  . GLN A 26  ? 0.7676 0.7037 0.9958 -0.0171 -0.0094 0.0815  6   GLN A CD  
61   O  OE1 . GLN A 26  ? 0.7149 0.6522 0.9477 -0.0148 -0.0104 0.0920  6   GLN A OE1 
62   N  NE2 . GLN A 26  ? 0.7734 0.7003 0.9979 -0.0137 -0.0096 0.0643  6   GLN A NE2 
63   N  N   . ALA A 27  ? 0.2604 0.2462 0.4410 -0.0150 0.0086  0.0827  7   ALA A N   
64   C  CA  . ALA A 27  ? 0.2510 0.2441 0.4218 -0.0152 0.0119  0.0753  7   ALA A CA  
65   C  C   . ALA A 27  ? 0.2336 0.2189 0.4136 -0.0203 0.0081  0.0699  7   ALA A C   
66   O  O   . ALA A 27  ? 0.2584 0.2291 0.4469 -0.0216 0.0033  0.0643  7   ALA A O   
67   C  CB  . ALA A 27  ? 0.2680 0.2604 0.4241 -0.0097 0.0143  0.0631  7   ALA A CB  
68   N  N   . VAL A 28  ? 0.1976 0.1929 0.3764 -0.0230 0.0098  0.0714  8   VAL A N   
69   C  CA  . VAL A 28  ? 0.2175 0.2071 0.4028 -0.0278 0.0054  0.0652  8   VAL A CA  
70   C  C   . VAL A 28  ? 0.2507 0.2295 0.4263 -0.0249 0.0039  0.0494  8   VAL A C   
71   O  O   . VAL A 28  ? 0.2226 0.2053 0.3843 -0.0199 0.0079  0.0437  8   VAL A O   
72   C  CB  . VAL A 28  ? 0.2273 0.2320 0.4118 -0.0297 0.0080  0.0689  8   VAL A CB  
73   C  CG1 . VAL A 28  ? 0.2493 0.2488 0.4396 -0.0348 0.0022  0.0621  8   VAL A CG1 
74   C  CG2 . VAL A 28  ? 0.2086 0.2268 0.4030 -0.0325 0.0107  0.0849  8   VAL A CG2 
75   N  N   . THR A 29  ? 0.2201 0.1858 0.4029 -0.0282 -0.0019 0.0422  9   THR A N   
76   C  CA  . THR A 29  ? 0.2336 0.1896 0.4071 -0.0251 -0.0028 0.0271  9   THR A CA  
77   C  C   . THR A 29  ? 0.2588 0.2111 0.4323 -0.0300 -0.0079 0.0193  9   THR A C   
78   O  O   . THR A 29  ? 0.2935 0.2410 0.4803 -0.0360 -0.0137 0.0225  9   THR A O   
79   C  CB  . THR A 29  ? 0.2768 0.2189 0.4571 -0.0224 -0.0048 0.0230  9   THR A CB  
80   O  OG1 . THR A 29  ? 0.3032 0.2502 0.4835 -0.0181 -0.0009 0.0312  9   THR A OG1 
81   C  CG2 . THR A 29  ? 0.3032 0.2380 0.4736 -0.0185 -0.0043 0.0069  9   THR A CG2 
82   N  N   . VAL A 30  ? 0.2483 0.2031 0.4072 -0.0279 -0.0064 0.0098  10  VAL A N   
83   C  CA  . VAL A 30  ? 0.2566 0.2089 0.4125 -0.0322 -0.0117 0.0020  10  VAL A CA  
84   C  C   . VAL A 30  ? 0.2492 0.1948 0.3913 -0.0287 -0.0109 -0.0124 10  VAL A C   
85   O  O   . VAL A 30  ? 0.2638 0.2110 0.3978 -0.0231 -0.0051 -0.0147 10  VAL A O   
86   C  CB  . VAL A 30  ? 0.2503 0.2165 0.4021 -0.0341 -0.0112 0.0071  10  VAL A CB  
87   C  CG1 . VAL A 30  ? 0.2862 0.2615 0.4532 -0.0379 -0.0116 0.0209  10  VAL A CG1 
88   C  CG2 . VAL A 30  ? 0.2684 0.2424 0.4059 -0.0283 -0.0046 0.0067  10  VAL A CG2 
89   N  N   . SER A 31  ? 0.2576 0.1970 0.3968 -0.0323 -0.0168 -0.0219 11  SER A N   
90   C  CA  . SER A 31  ? 0.2613 0.1959 0.3860 -0.0293 -0.0160 -0.0360 11  SER A CA  
91   C  C   . SER A 31  ? 0.2937 0.2392 0.4019 -0.0292 -0.0139 -0.0369 11  SER A C   
92   O  O   . SER A 31  ? 0.2751 0.2274 0.3837 -0.0335 -0.0177 -0.0318 11  SER A O   
93   C  CB  . SER A 31  ? 0.2547 0.1766 0.3821 -0.0330 -0.0239 -0.0474 11  SER A CB  
94   O  OG  . SER A 31  ? 0.3243 0.2450 0.4342 -0.0305 -0.0229 -0.0612 11  SER A OG  
95   N  N   . LEU A 32  ? 0.2423 0.1901 0.3374 -0.0243 -0.0080 -0.0427 12  LEU A N   
96   C  CA  . LEU A 32  ? 0.2844 0.2411 0.3636 -0.0248 -0.0067 -0.0437 12  LEU A CA  
97   C  C   . LEU A 32  ? 0.2980 0.2531 0.3701 -0.0298 -0.0141 -0.0505 12  LEU A C   
98   O  O   . LEU A 32  ? 0.2980 0.2611 0.3623 -0.0323 -0.0164 -0.0467 12  LEU A O   
99   C  CB  . LEU A 32  ? 0.2592 0.2181 0.3268 -0.0198 0.0004  -0.0496 12  LEU A CB  
100  C  CG  . LEU A 32  ? 0.2643 0.2325 0.3155 -0.0207 0.0019  -0.0490 12  LEU A CG  
101  C  CD1 . LEU A 32  ? 0.3056 0.2810 0.3594 -0.0216 0.0020  -0.0369 12  LEU A CD1 
102  C  CD2 . LEU A 32  ? 0.3523 0.3241 0.3943 -0.0165 0.0094  -0.0540 12  LEU A CD2 
103  N  N   . ASN A 33  ? 0.2943 0.2386 0.3690 -0.0312 -0.0188 -0.0608 13  ASN A N   
104  C  CA  . ASN A 33  ? 0.3205 0.2629 0.3873 -0.0363 -0.0272 -0.0686 13  ASN A CA  
105  C  C   . ASN A 33  ? 0.3405 0.2881 0.4173 -0.0426 -0.0344 -0.0585 13  ASN A C   
106  O  O   . ASN A 33  ? 0.3560 0.3098 0.4236 -0.0464 -0.0397 -0.0588 13  ASN A O   
107  C  CB  . ASN A 33  ? 0.3293 0.2570 0.3995 -0.0365 -0.0317 -0.0822 13  ASN A CB  
108  C  CG  . ASN A 33  ? 0.3949 0.3195 0.4544 -0.0294 -0.0244 -0.0940 13  ASN A CG  
109  O  OD1 . ASN A 33  ? 0.4131 0.3477 0.4566 -0.0267 -0.0182 -0.0950 13  ASN A OD1 
110  N  ND2 . ASN A 33  ? 0.4259 0.3372 0.4955 -0.0264 -0.0250 -0.1022 13  ASN A ND2 
111  N  N   . ASP A 34  ? 0.2823 0.2292 0.3781 -0.0437 -0.0343 -0.0485 14  ASP A N   
112  C  CA  . ASP A 34  ? 0.2896 0.2441 0.3975 -0.0492 -0.0398 -0.0380 14  ASP A CA  
113  C  C   . ASP A 34  ? 0.2968 0.2656 0.3994 -0.0469 -0.0355 -0.0284 14  ASP A C   
114  O  O   . ASP A 34  ? 0.2735 0.2506 0.3784 -0.0506 -0.0409 -0.0236 14  ASP A O   
115  C  CB  . ASP A 34  ? 0.2647 0.2158 0.3943 -0.0511 -0.0402 -0.0295 14  ASP A CB  
116  C  CG  . ASP A 34  ? 0.4152 0.3504 0.5532 -0.0546 -0.0469 -0.0383 14  ASP A CG  
117  O  OD1 . ASP A 34  ? 0.5176 0.4471 0.6489 -0.0584 -0.0548 -0.0490 14  ASP A OD1 
118  O  OD2 . ASP A 34  ? 0.3662 0.2939 0.5171 -0.0534 -0.0450 -0.0346 14  ASP A OD2 
119  N  N   . LEU A 35  ? 0.2386 0.2101 0.3352 -0.0407 -0.0265 -0.0257 15  LEU A N   
120  C  CA  . LEU A 35  ? 0.2475 0.2299 0.3380 -0.0382 -0.0231 -0.0185 15  LEU A CA  
121  C  C   . LEU A 35  ? 0.3149 0.3003 0.3896 -0.0398 -0.0270 -0.0231 15  LEU A C   
122  O  O   . LEU A 35  ? 0.3224 0.3163 0.3969 -0.0408 -0.0299 -0.0166 15  LEU A O   
123  C  CB  . LEU A 35  ? 0.2256 0.2086 0.3121 -0.0320 -0.0140 -0.0163 15  LEU A CB  
124  C  CG  . LEU A 35  ? 0.2625 0.2451 0.3625 -0.0298 -0.0099 -0.0096 15  LEU A CG  
125  C  CD1 . LEU A 35  ? 0.2955 0.2769 0.3894 -0.0243 -0.0025 -0.0103 15  LEU A CD1 
126  C  CD2 . LEU A 35  ? 0.3003 0.2934 0.4102 -0.0302 -0.0100 0.0012  15  LEU A CD2 
127  N  N   . LYS A 36  ? 0.2919 0.2710 0.3533 -0.0399 -0.0273 -0.0342 16  LYS A N   
128  C  CA  . LYS A 36  ? 0.3539 0.3371 0.3974 -0.0416 -0.0304 -0.0382 16  LYS A CA  
129  C  C   . LYS A 36  ? 0.3835 0.3686 0.4285 -0.0478 -0.0415 -0.0390 16  LYS A C   
130  O  O   . LYS A 36  ? 0.4141 0.4069 0.4504 -0.0497 -0.0456 -0.0353 16  LYS A O   
131  C  CB  . LYS A 36  ? 0.3602 0.3382 0.3884 -0.0395 -0.0267 -0.0506 16  LYS A CB  
132  C  CG  . LYS A 36  ? 0.4150 0.3949 0.4386 -0.0340 -0.0164 -0.0493 16  LYS A CG  
133  C  CD  . LYS A 36  ? 0.5171 0.4955 0.5255 -0.0319 -0.0125 -0.0613 16  LYS A CD  
134  C  CE  . LYS A 36  ? 0.6654 0.6504 0.6673 -0.0279 -0.0032 -0.0576 16  LYS A CE  
135  N  NZ  . LYS A 36  ? 0.6993 0.6869 0.6855 -0.0260 0.0016  -0.0681 16  LYS A NZ  
136  N  N   . ASN A 37  ? 0.3237 0.3016 0.3802 -0.0516 -0.0472 -0.0435 17  ASN A N   
137  C  CA  . ASN A 37  ? 0.3086 0.2877 0.3673 -0.0585 -0.0591 -0.0454 17  ASN A CA  
138  C  C   . ASN A 37  ? 0.3592 0.3469 0.4384 -0.0617 -0.0634 -0.0326 17  ASN A C   
139  O  O   . ASN A 37  ? 0.4101 0.4005 0.4950 -0.0680 -0.0740 -0.0326 17  ASN A O   
140  C  CB  . ASN A 37  ? 0.3406 0.3064 0.4010 -0.0617 -0.0646 -0.0584 17  ASN A CB  
141  C  CG  . ASN A 37  ? 0.5198 0.4787 0.5599 -0.0577 -0.0602 -0.0726 17  ASN A CG  
142  O  OD1 . ASN A 37  ? 0.5439 0.5096 0.5641 -0.0563 -0.0583 -0.0747 17  ASN A OD1 
143  N  ND2 . ASN A 37  ? 0.5791 0.5251 0.6250 -0.0557 -0.0584 -0.0819 17  ASN A ND2 
144  N  N   . GLY A 38  ? 0.3479 0.3412 0.4385 -0.0574 -0.0557 -0.0220 18  GLY A N   
145  C  CA  . GLY A 38  ? 0.2985 0.3023 0.4086 -0.0594 -0.0583 -0.0102 18  GLY A CA  
146  C  C   . GLY A 38  ? 0.3328 0.3336 0.4631 -0.0648 -0.0625 -0.0082 18  GLY A C   
147  O  O   . GLY A 38  ? 0.3890 0.4001 0.5362 -0.0685 -0.0670 0.0007  18  GLY A O   
148  N  N   . THR A 39  ? 0.3676 0.3549 0.4982 -0.0653 -0.0614 -0.0157 19  THR A N   
149  C  CA  . THR A 39  ? 0.3228 0.3047 0.4735 -0.0710 -0.0661 -0.0134 19  THR A CA  
150  C  C   . THR A 39  ? 0.3716 0.3533 0.5344 -0.0675 -0.0571 -0.0049 19  THR A C   
151  O  O   . THR A 39  ? 0.4341 0.4102 0.6136 -0.0719 -0.0601 -0.0018 19  THR A O   
152  C  CB  . THR A 39  ? 0.3560 0.3209 0.5010 -0.0747 -0.0734 -0.0280 19  THR A CB  
153  O  OG1 . THR A 39  ? 0.3917 0.3473 0.5203 -0.0678 -0.0658 -0.0375 19  THR A OG1 
154  C  CG2 . THR A 39  ? 0.4304 0.3966 0.5654 -0.0801 -0.0845 -0.0357 19  THR A CG2 
155  N  N   . VAL A 40  ? 0.2696 0.2570 0.4242 -0.0599 -0.0470 -0.0009 20  VAL A N   
156  C  CA  . VAL A 40  ? 0.3123 0.3005 0.4759 -0.0564 -0.0390 0.0069  20  VAL A CA  
157  C  C   . VAL A 40  ? 0.3165 0.3172 0.5009 -0.0602 -0.0395 0.0206  20  VAL A C   
158  O  O   . VAL A 40  ? 0.2979 0.3119 0.4871 -0.0615 -0.0417 0.0259  20  VAL A O   
159  C  CB  . VAL A 40  ? 0.3029 0.2951 0.4527 -0.0481 -0.0293 0.0076  20  VAL A CB  
160  C  CG1 . VAL A 40  ? 0.3702 0.3769 0.5187 -0.0458 -0.0276 0.0142  20  VAL A CG1 
161  C  CG2 . VAL A 40  ? 0.3339 0.3248 0.4898 -0.0445 -0.0221 0.0134  20  VAL A CG2 
162  N  N   . SER A 41  ? 0.3067 0.3042 0.5047 -0.0621 -0.0378 0.0271  21  SER A N   
163  C  CA  . SER A 41  ? 0.2917 0.3027 0.5102 -0.0660 -0.0371 0.0415  21  SER A CA  
164  C  C   . SER A 41  ? 0.2743 0.3023 0.4899 -0.0590 -0.0272 0.0500  21  SER A C   
165  O  O   . SER A 41  ? 0.2783 0.3044 0.4841 -0.0526 -0.0194 0.0500  21  SER A O   
166  C  CB  . SER A 41  ? 0.3409 0.3435 0.5731 -0.0697 -0.0375 0.0473  21  SER A CB  
167  O  OG  . SER A 41  ? 0.3275 0.3461 0.5769 -0.0722 -0.0338 0.0633  21  SER A OG  
168  N  N   . LEU A 42  ? 0.2620 0.3069 0.4871 -0.0601 -0.0278 0.0569  22  LEU A N   
169  C  CA  . LEU A 42  ? 0.2262 0.2873 0.4505 -0.0528 -0.0182 0.0643  22  LEU A CA  
170  C  C   . LEU A 42  ? 0.2927 0.3628 0.5288 -0.0531 -0.0115 0.0763  22  LEU A C   
171  O  O   . LEU A 42  ? 0.2338 0.3128 0.4634 -0.0458 -0.0023 0.0798  22  LEU A O   
172  C  CB  . LEU A 42  ? 0.2964 0.3737 0.5290 -0.0527 -0.0207 0.0679  22  LEU A CB  
173  C  CG  . LEU A 42  ? 0.2876 0.3586 0.5056 -0.0507 -0.0261 0.0580  22  LEU A CG  
174  C  CD1 . LEU A 42  ? 0.3115 0.3995 0.5397 -0.0497 -0.0286 0.0632  22  LEU A CD1 
175  C  CD2 . LEU A 42  ? 0.2869 0.3493 0.4834 -0.0425 -0.0196 0.0509  22  LEU A CD2 
176  N  N   . GLU A 43  ? 0.2374 0.3053 0.4905 -0.0616 -0.0162 0.0830  23  GLU A N   
177  C  CA  . GLU A 43  ? 0.2316 0.3058 0.4938 -0.0624 -0.0101 0.0952  23  GLU A CA  
178  C  C   . GLU A 43  ? 0.2519 0.3123 0.4982 -0.0570 -0.0057 0.0906  23  GLU A C   
179  O  O   . GLU A 43  ? 0.2632 0.3325 0.5052 -0.0520 0.0027  0.0975  23  GLU A O   
180  C  CB  . GLU A 43  ? 0.3316 0.4036 0.6164 -0.0736 -0.0174 0.1038  23  GLU A CB  
181  C  CG  . GLU A 43  ? 0.4574 0.5363 0.7504 -0.0745 -0.0116 0.1182  23  GLU A CG  
182  C  CD  . GLU A 43  ? 0.5861 0.6607 0.8930 -0.0821 -0.0193 0.1248  23  GLU A CD  
183  O  OE1 . GLU A 43  ? 0.5819 0.6487 0.8955 -0.0879 -0.0292 0.1186  23  GLU A OE1 
184  O  OE2 . GLU A 43  ? 0.6486 0.7280 0.9598 -0.0824 -0.0157 0.1365  23  GLU A OE2 
185  N  N   . ALA A 44  ? 0.2351 0.2748 0.4725 -0.0576 -0.0114 0.0788  24  ALA A N   
186  C  CA  . ALA A 44  ? 0.2485 0.2766 0.4719 -0.0517 -0.0074 0.0738  24  ALA A CA  
187  C  C   . ALA A 44  ? 0.2236 0.2598 0.4297 -0.0426 0.0005  0.0705  24  ALA A C   
188  O  O   . ALA A 44  ? 0.2554 0.2935 0.4546 -0.0377 0.0066  0.0739  24  ALA A O   
189  C  CB  . ALA A 44  ? 0.2862 0.2932 0.5032 -0.0529 -0.0141 0.0602  24  ALA A CB  
190  N  N   . LEU A 45  ? 0.2150 0.2558 0.4143 -0.0404 -0.0002 0.0643  25  LEU A N   
191  C  CA  . LEU A 45  ? 0.2033 0.2498 0.3877 -0.0321 0.0061  0.0609  25  LEU A CA  
192  C  C   . LEU A 45  ? 0.2056 0.2691 0.3935 -0.0281 0.0141  0.0710  25  LEU A C   
193  O  O   . LEU A 45  ? 0.2012 0.2655 0.3771 -0.0217 0.0199  0.0697  25  LEU A O   
194  C  CB  . LEU A 45  ? 0.2026 0.2513 0.3826 -0.0313 0.0027  0.0548  25  LEU A CB  
195  C  CG  . LEU A 45  ? 0.1871 0.2361 0.3511 -0.0233 0.0074  0.0495  25  LEU A CG  
196  C  CD1 . LEU A 45  ? 0.2249 0.2588 0.3746 -0.0218 0.0071  0.0406  25  LEU A CD1 
197  C  CD2 . LEU A 45  ? 0.2469 0.3015 0.4107 -0.0224 0.0042  0.0474  25  LEU A CD2 
198  N  N   . GLU A 46  ? 0.1930 0.2712 0.3974 -0.0318 0.0144  0.0809  26  GLU A N   
199  C  CA  . GLU A 46  ? 0.2259 0.3227 0.4334 -0.0277 0.0230  0.0906  26  GLU A CA  
200  C  C   . GLU A 46  ? 0.2138 0.3092 0.4201 -0.0286 0.0265  0.0980  26  GLU A C   
201  O  O   . GLU A 46  ? 0.2538 0.3603 0.4527 -0.0229 0.0342  0.1021  26  GLU A O   
202  C  CB  . GLU A 46  ? 0.2071 0.3226 0.4347 -0.0319 0.0230  0.1004  26  GLU A CB  
203  C  CG  . GLU A 46  ? 0.2135 0.3514 0.4432 -0.0260 0.0333  0.1089  26  GLU A CG  
204  C  CD  . GLU A 46  ? 0.3916 0.5504 0.6424 -0.0290 0.0339  0.1178  26  GLU A CD  
205  O  OE1 . GLU A 46  ? 0.4363 0.5915 0.7020 -0.0377 0.0253  0.1196  26  GLU A OE1 
206  O  OE2 . GLU A 46  ? 0.3387 0.5180 0.5916 -0.0225 0.0427  0.1223  26  GLU A OE2 
207  N  N   . GLU A 47  ? 0.2090 0.2910 0.4226 -0.0354 0.0205  0.0999  27  GLU A N   
208  C  CA  . GLU A 47  ? 0.2040 0.2826 0.4164 -0.0358 0.0227  0.1071  27  GLU A CA  
209  C  C   . GLU A 47  ? 0.1629 0.2316 0.3556 -0.0285 0.0249  0.0981  27  GLU A C   
210  O  O   . GLU A 47  ? 0.2085 0.2795 0.3959 -0.0262 0.0284  0.1041  27  GLU A O   
211  C  CB  . GLU A 47  ? 0.2733 0.3378 0.5005 -0.0444 0.0147  0.1108  27  GLU A CB  
212  C  CG  . GLU A 47  ? 0.3373 0.4131 0.5868 -0.0530 0.0124  0.1233  27  GLU A CG  
213  C  CD  . GLU A 47  ? 0.4895 0.5489 0.7552 -0.0621 0.0031  0.1263  27  GLU A CD  
214  O  OE1 . GLU A 47  ? 0.4522 0.4904 0.7119 -0.0614 -0.0026 0.1148  27  GLU A OE1 
215  O  OE2 . GLU A 47  ? 0.5271 0.5939 0.8065 -0.0675 0.0009  0.1374  27  GLU A OE2 
216  N  N   . ALA A 48  ? 0.1607 0.2188 0.3430 -0.0255 0.0223  0.0847  28  ALA A N   
217  C  CA  . ALA A 48  ? 0.1848 0.2343 0.3503 -0.0194 0.0241  0.0763  28  ALA A CA  
218  C  C   . ALA A 48  ? 0.1961 0.2569 0.3490 -0.0121 0.0304  0.0745  28  ALA A C   
219  O  O   . ALA A 48  ? 0.1766 0.2359 0.3177 -0.0075 0.0330  0.0728  28  ALA A O   
220  C  CB  . ALA A 48  ? 0.1544 0.1888 0.3145 -0.0199 0.0190  0.0635  28  ALA A CB  
221  N  N   . PHE A 49  ? 0.1800 0.2514 0.3357 -0.0106 0.0322  0.0742  29  PHE A N   
222  C  CA  . PHE A 49  ? 0.1708 0.2490 0.3152 -0.0030 0.0368  0.0691  29  PHE A CA  
223  C  C   . PHE A 49  ? 0.1800 0.2785 0.3297 0.0003  0.0432  0.0764  29  PHE A C   
224  O  O   . PHE A 49  ? 0.2123 0.3165 0.3528 0.0078  0.0475  0.0716  29  PHE A O   
225  C  CB  . PHE A 49  ? 0.1593 0.2305 0.3009 -0.0021 0.0328  0.0599  29  PHE A CB  
226  C  CG  . PHE A 49  ? 0.1445 0.1989 0.2756 -0.0025 0.0289  0.0507  29  PHE A CG  
227  C  CD1 . PHE A 49  ? 0.1696 0.2166 0.2929 -0.0014 0.0297  0.0492  29  PHE A CD1 
228  C  CD2 . PHE A 49  ? 0.1864 0.2341 0.3159 -0.0039 0.0244  0.0443  29  PHE A CD2 
229  C  CE1 . PHE A 49  ? 0.1545 0.1887 0.2699 -0.0014 0.0269  0.0411  29  PHE A CE1 
230  C  CE2 . PHE A 49  ? 0.2000 0.2351 0.3200 -0.0043 0.0218  0.0366  29  PHE A CE2 
231  C  CZ  . PHE A 49  ? 0.1755 0.2041 0.2891 -0.0030 0.0234  0.0348  29  PHE A CZ  
232  N  N   . GLY A 50  ? 0.1557 0.2655 0.3209 -0.0050 0.0441  0.0875  30  GLY A N   
233  C  CA  . GLY A 50  ? 0.2117 0.3436 0.3851 -0.0023 0.0507  0.0950  30  GLY A CA  
234  C  C   . GLY A 50  ? 0.1941 0.3391 0.3595 0.0019  0.0587  0.1016  30  GLY A C   
235  O  O   . GLY A 50  ? 0.2443 0.3808 0.3963 0.0033  0.0586  0.0997  30  GLY A O   
236  N  N   . PRO A 51  ? 0.2676 0.4353 0.4415 0.0037  0.0658  0.1099  31  PRO A N   
237  C  CA  . PRO A 51  ? 0.3788 0.5621 0.5412 0.0097  0.0749  0.1142  31  PRO A CA  
238  C  C   . PRO A 51  ? 0.3772 0.5596 0.5362 0.0046  0.0748  0.1249  31  PRO A C   
239  O  O   . PRO A 51  ? 0.4047 0.5925 0.5471 0.0098  0.0795  0.1247  31  PRO A O   
240  C  CB  . PRO A 51  ? 0.3319 0.5418 0.5085 0.0116  0.0825  0.1222  31  PRO A CB  
241  C  CG  . PRO A 51  ? 0.5331 0.7388 0.7243 0.0101  0.0771  0.1172  31  PRO A CG  
242  C  CD  . PRO A 51  ? 0.2529 0.4345 0.4460 0.0017  0.0662  0.1143  31  PRO A CD  
243  N  N   . ASP A 52  ? 0.2392 0.4145 0.4134 -0.0054 0.0689  0.1341  32  ASP A N   
244  C  CA  . ASP A 52  ? 0.2322 0.4046 0.4059 -0.0105 0.0676  0.1454  32  ASP A CA  
245  C  C   . ASP A 52  ? 0.3163 0.4628 0.4827 -0.0119 0.0593  0.1377  32  ASP A C   
246  O  O   . ASP A 52  ? 0.2581 0.3984 0.4284 -0.0168 0.0560  0.1468  32  ASP A O   
247  C  CB  . ASP A 52  ? 0.2606 0.4407 0.4577 -0.0207 0.0660  0.1618  32  ASP A CB  
248  C  CG  . ASP A 52  ? 0.4728 0.6765 0.6728 -0.0186 0.0725  0.1688  32  ASP A CG  
249  O  OD1 . ASP A 52  ? 0.4618 0.6797 0.6474 -0.0130 0.0798  0.1723  32  ASP A OD1 
250  O  OD2 . ASP A 52  ? 0.4148 0.6227 0.6306 -0.0222 0.0700  0.1701  32  ASP A OD2 
251  N  N   . SER A 53  ? 0.2418 0.3742 0.3989 -0.0076 0.0561  0.1219  33  SER A N   
252  C  CA  . SER A 53  ? 0.2090 0.3182 0.3640 -0.0097 0.0482  0.1140  33  SER A CA  
253  C  C   . SER A 53  ? 0.2447 0.3473 0.3814 -0.0042 0.0485  0.1082  33  SER A C   
254  O  O   . SER A 53  ? 0.2315 0.3456 0.3549 0.0015  0.0539  0.1085  33  SER A O   
255  C  CB  . SER A 53  ? 0.2267 0.3256 0.3836 -0.0095 0.0442  0.1015  33  SER A CB  
256  O  OG  . SER A 53  ? 0.2188 0.3186 0.3603 -0.0016 0.0472  0.0908  33  SER A OG  
257  N  N   . LEU A 54  ? 0.1689 0.2529 0.3050 -0.0056 0.0423  0.1020  34  LEU A N   
258  C  CA  . LEU A 54  ? 0.1691 0.2452 0.2905 -0.0010 0.0410  0.0950  34  LEU A CA  
259  C  C   . LEU A 54  ? 0.1883 0.2583 0.2990 0.0037  0.0408  0.0804  34  LEU A C   
260  O  O   . LEU A 54  ? 0.2044 0.2688 0.3037 0.0072  0.0396  0.0741  34  LEU A O   
261  C  CB  . LEU A 54  ? 0.1707 0.2316 0.2993 -0.0044 0.0349  0.0962  34  LEU A CB  
262  C  CG  . LEU A 54  ? 0.2021 0.2662 0.3415 -0.0089 0.0336  0.1118  34  LEU A CG  
263  C  CD1 . LEU A 54  ? 0.2616 0.3083 0.4104 -0.0112 0.0270  0.1110  34  LEU A CD1 
264  C  CD2 . LEU A 54  ? 0.2148 0.2934 0.3426 -0.0059 0.0376  0.1212  34  LEU A CD2 
265  N  N   . GLY A 55  ? 0.1587 0.2302 0.2740 0.0035  0.0414  0.0757  35  GLY A N   
266  C  CA  . GLY A 55  ? 0.1763 0.2417 0.2828 0.0074  0.0407  0.0636  35  GLY A CA  
267  C  C   . GLY A 55  ? 0.1911 0.2403 0.2957 0.0057  0.0357  0.0558  35  GLY A C   
268  O  O   . GLY A 55  ? 0.1813 0.2252 0.2759 0.0090  0.0351  0.0474  35  GLY A O   
269  N  N   . ILE A 56  ? 0.1904 0.2317 0.3050 0.0007  0.0321  0.0580  36  ILE A N   
270  C  CA  . ILE A 56  ? 0.2008 0.2284 0.3140 -0.0001 0.0283  0.0504  36  ILE A CA  
271  C  C   . ILE A 56  ? 0.2126 0.2328 0.3374 -0.0054 0.0245  0.0498  36  ILE A C   
272  O  O   . ILE A 56  ? 0.2119 0.2349 0.3481 -0.0093 0.0235  0.0578  36  ILE A O   
273  C  CB  . ILE A 56  ? 0.1816 0.2058 0.2921 0.0016  0.0276  0.0524  36  ILE A CB  
274  C  CG1 . ILE A 56  ? 0.1996 0.2124 0.3087 0.0020  0.0250  0.0434  36  ILE A CG1 
275  C  CG2 . ILE A 56  ? 0.2001 0.2252 0.3215 -0.0015 0.0264  0.0633  36  ILE A CG2 
276  C  CD1 . ILE A 56  ? 0.1924 0.2036 0.2990 0.0046  0.0240  0.0443  36  ILE A CD1 
277  N  N   . LEU A 57  ? 0.1864 0.1976 0.3080 -0.0058 0.0221  0.0403  37  LEU A N   
278  C  CA  . LEU A 57  ? 0.1781 0.1812 0.3073 -0.0103 0.0179  0.0366  37  LEU A CA  
279  C  C   . LEU A 57  ? 0.2092 0.2016 0.3344 -0.0089 0.0167  0.0278  37  LEU A C   
280  O  O   . LEU A 57  ? 0.2036 0.1962 0.3186 -0.0060 0.0185  0.0221  37  LEU A O   
281  C  CB  . LEU A 57  ? 0.2065 0.2131 0.3341 -0.0122 0.0165  0.0333  37  LEU A CB  
282  C  CG  . LEU A 57  ? 0.2098 0.2083 0.3417 -0.0168 0.0112  0.0274  37  LEU A CG  
283  C  CD1 . LEU A 57  ? 0.2091 0.2071 0.3566 -0.0222 0.0077  0.0342  37  LEU A CD1 
284  C  CD2 . LEU A 57  ? 0.1828 0.1847 0.3085 -0.0175 0.0095  0.0231  37  LEU A CD2 
285  N  N   . VAL A 58  ? 0.1640 0.1474 0.2982 -0.0107 0.0137  0.0268  38  VAL A N   
286  C  CA  . VAL A 58  ? 0.1887 0.1630 0.3207 -0.0085 0.0131  0.0175  38  VAL A CA  
287  C  C   . VAL A 58  ? 0.2375 0.2059 0.3679 -0.0115 0.0101  0.0084  38  VAL A C   
288  O  O   . VAL A 58  ? 0.2322 0.1983 0.3703 -0.0160 0.0061  0.0101  38  VAL A O   
289  C  CB  . VAL A 58  ? 0.2396 0.2066 0.3830 -0.0074 0.0114  0.0208  38  VAL A CB  
290  C  CG1 . VAL A 58  ? 0.2375 0.1953 0.3813 -0.0045 0.0110  0.0098  38  VAL A CG1 
291  C  CG2 . VAL A 58  ? 0.2414 0.2154 0.3838 -0.0044 0.0138  0.0296  38  VAL A CG2 
292  N  N   . VAL A 59  ? 0.1799 0.1472 0.3002 -0.0094 0.0118  -0.0008 39  VAL A N   
293  C  CA  . VAL A 59  ? 0.1992 0.1620 0.3143 -0.0117 0.0093  -0.0104 39  VAL A CA  
294  C  C   . VAL A 59  ? 0.2285 0.1831 0.3445 -0.0087 0.0099  -0.0200 39  VAL A C   
295  O  O   . VAL A 59  ? 0.2212 0.1786 0.3333 -0.0044 0.0144  -0.0221 39  VAL A O   
296  C  CB  . VAL A 59  ? 0.1988 0.1687 0.3003 -0.0119 0.0110  -0.0126 39  VAL A CB  
297  C  CG1 . VAL A 59  ? 0.2389 0.2052 0.3330 -0.0143 0.0082  -0.0222 39  VAL A CG1 
298  C  CG2 . VAL A 59  ? 0.1944 0.1722 0.2967 -0.0136 0.0103  -0.0040 39  VAL A CG2 
299  N  N   . LYS A 60  ? 0.2224 0.1671 0.3446 -0.0108 0.0053  -0.0260 40  LYS A N   
300  C  CA  . LYS A 60  ? 0.2258 0.1615 0.3493 -0.0073 0.0055  -0.0375 40  LYS A CA  
301  C  C   . LYS A 60  ? 0.2638 0.1988 0.3740 -0.0087 0.0045  -0.0496 40  LYS A C   
302  O  O   . LYS A 60  ? 0.2775 0.2187 0.3785 -0.0127 0.0029  -0.0478 40  LYS A O   
303  C  CB  . LYS A 60  ? 0.2642 0.1871 0.4045 -0.0081 0.0002  -0.0368 40  LYS A CB  
304  C  CG  . LYS A 60  ? 0.2810 0.1978 0.4261 -0.0151 -0.0072 -0.0370 40  LYS A CG  
305  C  CD  . LYS A 60  ? 0.3602 0.2620 0.5235 -0.0161 -0.0130 -0.0369 40  LYS A CD  
306  C  CE  . LYS A 60  ? 0.4615 0.3563 0.6314 -0.0240 -0.0216 -0.0379 40  LYS A CE  
307  N  NZ  . LYS A 60  ? 0.6256 0.5040 0.8146 -0.0254 -0.0280 -0.0376 40  LYS A NZ  
308  N  N   . ASP A 61  ? 0.2778 0.2056 0.3870 -0.0050 0.0052  -0.0621 41  ASP A N   
309  C  CA  . ASP A 61  ? 0.2731 0.2016 0.3671 -0.0053 0.0053  -0.0750 41  ASP A CA  
310  C  C   . ASP A 61  ? 0.3438 0.2866 0.4219 -0.0053 0.0108  -0.0723 41  ASP A C   
311  O  O   . ASP A 61  ? 0.3359 0.2828 0.4003 -0.0089 0.0089  -0.0753 41  ASP A O   
312  C  CB  . ASP A 61  ? 0.3474 0.2691 0.4401 -0.0118 -0.0035 -0.0788 41  ASP A CB  
313  C  CG  . ASP A 61  ? 0.4798 0.3859 0.5899 -0.0130 -0.0102 -0.0811 41  ASP A CG  
314  O  OD1 . ASP A 61  ? 0.4136 0.3108 0.5311 -0.0073 -0.0084 -0.0880 41  ASP A OD1 
315  O  OD2 . ASP A 61  ? 0.3758 0.2787 0.4935 -0.0197 -0.0174 -0.0755 41  ASP A OD2 
316  N  N   . VAL A 62  ? 0.3363 0.2864 0.4166 -0.0016 0.0170  -0.0659 42  VAL A N   
317  C  CA  . VAL A 62  ? 0.3572 0.3198 0.4254 -0.0023 0.0216  -0.0614 42  VAL A CA  
318  C  C   . VAL A 62  ? 0.3517 0.3193 0.4071 0.0000  0.0264  -0.0719 42  VAL A C   
319  O  O   . VAL A 62  ? 0.3889 0.3511 0.4466 0.0039  0.0275  -0.0831 42  VAL A O   
320  C  CB  . VAL A 62  ? 0.3640 0.3321 0.4394 0.0002  0.0255  -0.0517 42  VAL A CB  
321  C  CG1 . VAL A 62  ? 0.3287 0.2941 0.4133 -0.0021 0.0214  -0.0412 42  VAL A CG1 
322  C  CG2 . VAL A 62  ? 0.3706 0.3375 0.4554 0.0062  0.0296  -0.0560 42  VAL A CG2 
323  N  N   . PRO A 63  ? 0.4179 0.3963 0.4602 -0.0021 0.0294  -0.0687 43  PRO A N   
324  C  CA  . PRO A 63  ? 0.4747 0.4603 0.5034 -0.0005 0.0345  -0.0776 43  PRO A CA  
325  C  C   . PRO A 63  ? 0.4425 0.4305 0.4786 0.0064  0.0416  -0.0844 43  PRO A C   
326  O  O   . PRO A 63  ? 0.4488 0.4360 0.4994 0.0094  0.0433  -0.0791 43  PRO A O   
327  C  CB  . PRO A 63  ? 0.4083 0.4055 0.4268 -0.0041 0.0368  -0.0680 43  PRO A CB  
328  C  CG  . PRO A 63  ? 0.5016 0.4945 0.5238 -0.0084 0.0301  -0.0583 43  PRO A CG  
329  C  CD  . PRO A 63  ? 0.4181 0.4022 0.4571 -0.0060 0.0279  -0.0569 43  PRO A CD  
330  N  N   . ALA A 64  ? 0.4285 0.4202 0.4543 0.0092  0.0457  -0.0966 44  ALA A N   
331  C  CA  . ALA A 64  ? 0.4591 0.4529 0.4930 0.0170  0.0525  -0.1056 44  ALA A CA  
332  C  C   . ALA A 64  ? 0.5068 0.5139 0.5482 0.0192  0.0599  -0.0969 44  ALA A C   
333  O  O   . ALA A 64  ? 0.4855 0.4928 0.5420 0.0254  0.0633  -0.0990 44  ALA A O   
334  C  CB  . ALA A 64  ? 0.6324 0.6306 0.6506 0.0198  0.0566  -0.1206 44  ALA A CB  
335  N  N   . GLU A 65  ? 0.4390 0.4569 0.4714 0.0139  0.0615  -0.0869 45  GLU A N   
336  C  CA  . GLU A 65  ? 0.4126 0.4437 0.4518 0.0147  0.0678  -0.0788 45  GLU A CA  
337  C  C   . GLU A 65  ? 0.4204 0.4468 0.4756 0.0144  0.0641  -0.0685 45  GLU A C   
338  O  O   . GLU A 65  ? 0.3033 0.3394 0.3666 0.0152  0.0680  -0.0625 45  GLU A O   
339  C  CB  . GLU A 65  ? 0.3877 0.4307 0.4122 0.0085  0.0699  -0.0711 45  GLU A CB  
340  C  CG  . GLU A 65  ? 0.6917 0.7451 0.6992 0.0090  0.0758  -0.0797 45  GLU A CG  
341  C  CD  . GLU A 65  ? 1.0503 1.1128 1.0416 0.0017  0.0755  -0.0704 45  GLU A CD  
342  O  OE1 . GLU A 65  ? 1.0031 1.0776 0.9977 -0.0009 0.0800  -0.0603 45  GLU A OE1 
343  O  OE2 . GLU A 65  ? 1.0543 1.1121 1.0308 -0.0019 0.0702  -0.0725 45  GLU A OE2 
344  N  N   . PHE A 66  ? 0.3051 0.3179 0.3649 0.0131  0.0565  -0.0662 46  PHE A N   
345  C  CA  . PHE A 66  ? 0.2580 0.2681 0.3288 0.0120  0.0530  -0.0556 46  PHE A CA  
346  C  C   . PHE A 66  ? 0.2658 0.2787 0.3529 0.0177  0.0557  -0.0552 46  PHE A C   
347  O  O   . PHE A 66  ? 0.2464 0.2657 0.3395 0.0168  0.0561  -0.0471 46  PHE A O   
348  C  CB  . PHE A 66  ? 0.2536 0.2510 0.3268 0.0099  0.0456  -0.0529 46  PHE A CB  
349  C  CG  . PHE A 66  ? 0.2143 0.2096 0.2984 0.0102  0.0428  -0.0434 46  PHE A CG  
350  C  CD1 . PHE A 66  ? 0.2119 0.2120 0.2925 0.0070  0.0419  -0.0347 46  PHE A CD1 
351  C  CD2 . PHE A 66  ? 0.2957 0.2840 0.3933 0.0139  0.0406  -0.0434 46  PHE A CD2 
352  C  CE1 . PHE A 66  ? 0.2045 0.2033 0.2927 0.0076  0.0393  -0.0274 46  PHE A CE1 
353  C  CE2 . PHE A 66  ? 0.2125 0.2004 0.3180 0.0140  0.0379  -0.0343 46  PHE A CE2 
354  C  CZ  . PHE A 66  ? 0.1809 0.1744 0.2807 0.0110  0.0374  -0.0269 46  PHE A CZ  
355  N  N   . ALA A 67  ? 0.2694 0.2764 0.3653 0.0235  0.0564  -0.0637 47  ALA A N   
356  C  CA  . ALA A 67  ? 0.2843 0.2924 0.3981 0.0292  0.0572  -0.0619 47  ALA A CA  
357  C  C   . ALA A 67  ? 0.2618 0.2866 0.3797 0.0309  0.0639  -0.0598 47  ALA A C   
358  O  O   . ALA A 67  ? 0.2756 0.3052 0.4046 0.0314  0.0626  -0.0518 47  ALA A O   
359  C  CB  . ALA A 67  ? 0.3130 0.3115 0.4360 0.0359  0.0570  -0.0726 47  ALA A CB  
360  N  N   . GLU A 68  ? 0.2387 0.2737 0.3474 0.0313  0.0708  -0.0663 48  GLU A N   
361  C  CA  . GLU A 68  ? 0.2644 0.3176 0.3785 0.0324  0.0779  -0.0636 48  GLU A CA  
362  C  C   . GLU A 68  ? 0.2582 0.3178 0.3675 0.0246  0.0759  -0.0514 48  GLU A C   
363  O  O   . GLU A 68  ? 0.2480 0.3181 0.3686 0.0243  0.0773  -0.0449 48  GLU A O   
364  C  CB  . GLU A 68  ? 0.3586 0.4226 0.4633 0.0351  0.0866  -0.0737 48  GLU A CB  
365  C  CG  . GLU A 68  ? 0.4362 0.5212 0.5506 0.0375  0.0953  -0.0713 48  GLU A CG  
366  C  CD  . GLU A 68  ? 0.6050 0.7028 0.7114 0.0421  0.1054  -0.0823 48  GLU A CD  
367  O  OE1 . GLU A 68  ? 0.5643 0.6523 0.6633 0.0467  0.1055  -0.0953 48  GLU A OE1 
368  O  OE2 . GLU A 68  ? 0.4906 0.6087 0.5984 0.0408  0.1133  -0.0779 48  GLU A OE2 
369  N  N   . LEU A 69  ? 0.2510 0.3041 0.3451 0.0182  0.0720  -0.0482 49  LEU A N   
370  C  CA  . LEU A 69  ? 0.1894 0.2460 0.2803 0.0115  0.0692  -0.0372 49  LEU A CA  
371  C  C   . LEU A 69  ? 0.2172 0.2678 0.3193 0.0115  0.0630  -0.0305 49  LEU A C   
372  O  O   . LEU A 69  ? 0.2024 0.2595 0.3098 0.0085  0.0620  -0.0233 49  LEU A O   
373  C  CB  . LEU A 69  ? 0.2013 0.2514 0.2753 0.0057  0.0657  -0.0353 49  LEU A CB  
374  C  CG  . LEU A 69  ? 0.2616 0.3207 0.3214 0.0029  0.0706  -0.0374 49  LEU A CG  
375  C  CD1 . LEU A 69  ? 0.2689 0.3185 0.3140 -0.0015 0.0648  -0.0361 49  LEU A CD1 
376  C  CD2 . LEU A 69  ? 0.3091 0.3822 0.3708 -0.0014 0.0744  -0.0287 49  LEU A CD2 
377  N  N   . ARG A 70  ? 0.1834 0.2218 0.2888 0.0144  0.0584  -0.0325 50  ARG A N   
378  C  CA  . ARG A 70  ? 0.1776 0.2117 0.2924 0.0151  0.0529  -0.0261 50  ARG A CA  
379  C  C   . ARG A 70  ? 0.1704 0.2142 0.3008 0.0189  0.0548  -0.0247 50  ARG A C   
380  O  O   . ARG A 70  ? 0.1684 0.2166 0.3038 0.0167  0.0517  -0.0178 50  ARG A O   
381  C  CB  . ARG A 70  ? 0.1889 0.2101 0.3057 0.0176  0.0486  -0.0278 50  ARG A CB  
382  C  CG  . ARG A 70  ? 0.1823 0.2008 0.3092 0.0192  0.0436  -0.0210 50  ARG A CG  
383  C  CD  . ARG A 70  ? 0.1827 0.1901 0.3156 0.0223  0.0404  -0.0219 50  ARG A CD  
384  N  NE  . ARG A 70  ? 0.1994 0.2066 0.3427 0.0244  0.0362  -0.0147 50  ARG A NE  
385  C  CZ  . ARG A 70  ? 0.1999 0.2120 0.3573 0.0292  0.0366  -0.0143 50  ARG A CZ  
386  N  NH1 . ARG A 70  ? 0.1866 0.2038 0.3507 0.0333  0.0418  -0.0217 50  ARG A NH1 
387  N  NH2 . ARG A 70  ? 0.1900 0.2032 0.3548 0.0303  0.0317  -0.0063 50  ARG A NH2 
388  N  N   . HIS A 71  ? 0.1789 0.2261 0.3181 0.0250  0.0595  -0.0316 51  HIS A N   
389  C  CA  . HIS A 71  ? 0.1996 0.2575 0.3564 0.0295  0.0613  -0.0301 51  HIS A CA  
390  C  C   . HIS A 71  ? 0.2438 0.3175 0.4023 0.0252  0.0645  -0.0250 51  HIS A C   
391  O  O   . HIS A 71  ? 0.1998 0.2802 0.3699 0.0244  0.0612  -0.0185 51  HIS A O   
392  C  CB  . HIS A 71  ? 0.2517 0.3112 0.4171 0.0376  0.0670  -0.0400 51  HIS A CB  
393  C  CG  . HIS A 71  ? 0.2976 0.3664 0.4845 0.0441  0.0680  -0.0388 51  HIS A CG  
394  N  ND1 . HIS A 71  ? 0.3221 0.3965 0.5200 0.0526  0.0744  -0.0477 51  HIS A ND1 
395  C  CD2 . HIS A 71  ? 0.3298 0.4036 0.5295 0.0439  0.0630  -0.0299 51  HIS A CD2 
396  C  CE1 . HIS A 71  ? 0.2635 0.3464 0.4818 0.0574  0.0734  -0.0436 51  HIS A CE1 
397  N  NE2 . HIS A 71  ? 0.2552 0.3381 0.4747 0.0518  0.0661  -0.0325 51  HIS A NE2 
398  N  N   . ARG A 72  ? 0.2224 0.3023 0.3694 0.0216  0.0700  -0.0271 52  ARG A N   
399  C  CA  . ARG A 72  ? 0.1936 0.2889 0.3431 0.0165  0.0732  -0.0210 52  ARG A CA  
400  C  C   . ARG A 72  ? 0.1748 0.2652 0.3213 0.0092  0.0654  -0.0119 52  ARG A C   
401  O  O   . ARG A 72  ? 0.1713 0.2709 0.3292 0.0066  0.0636  -0.0058 52  ARG A O   
402  C  CB  . ARG A 72  ? 0.2154 0.3183 0.3517 0.0139  0.0807  -0.0241 52  ARG A CB  
403  C  CG  . ARG A 72  ? 0.3104 0.4241 0.4516 0.0214  0.0901  -0.0334 52  ARG A CG  
404  C  CD  . ARG A 72  ? 0.4580 0.5806 0.5834 0.0192  0.0977  -0.0369 52  ARG A CD  
405  N  NE  . ARG A 72  ? 0.4805 0.6115 0.6092 0.0279  0.1065  -0.0485 52  ARG A NE  
406  C  CZ  . ARG A 72  ? 0.6222 0.7734 0.7643 0.0320  0.1152  -0.0492 52  ARG A CZ  
407  N  NH1 . ARG A 72  ? 0.5126 0.6787 0.6668 0.0271  0.1160  -0.0379 52  ARG A NH1 
408  N  NH2 . ARG A 72  ? 0.6163 0.7732 0.7606 0.0414  0.1230  -0.0617 52  ARG A NH2 
409  N  N   . LEU A 73  ? 0.1542 0.2303 0.2865 0.0060  0.0605  -0.0112 53  LEU A N   
410  C  CA  . LEU A 73  ? 0.1489 0.2204 0.2781 0.0000  0.0536  -0.0041 53  LEU A CA  
411  C  C   . LEU A 73  ? 0.1611 0.2295 0.2999 0.0019  0.0470  -0.0014 53  LEU A C   
412  O  O   . LEU A 73  ? 0.1512 0.2225 0.2944 -0.0022 0.0423  0.0039  53  LEU A O   
413  C  CB  . LEU A 73  ? 0.1625 0.2208 0.2755 -0.0027 0.0503  -0.0044 53  LEU A CB  
414  C  CG  . LEU A 73  ? 0.1771 0.2313 0.2862 -0.0087 0.0445  0.0019  53  LEU A CG  
415  C  CD1 . LEU A 73  ? 0.1751 0.2394 0.2852 -0.0145 0.0476  0.0066  53  LEU A CD1 
416  C  CD2 . LEU A 73  ? 0.1781 0.2193 0.2740 -0.0097 0.0407  0.0016  53  LEU A CD2 
417  N  N   . LEU A 74  ? 0.1583 0.2208 0.3007 0.0079  0.0458  -0.0045 54  LEU A N   
418  C  CA  . LEU A 74  ? 0.1431 0.2045 0.2942 0.0097  0.0395  -0.0007 54  LEU A CA  
419  C  C   . LEU A 74  ? 0.1625 0.2385 0.3309 0.0108  0.0403  0.0017  54  LEU A C   
420  O  O   . LEU A 74  ? 0.1535 0.2321 0.3278 0.0090  0.0338  0.0066  54  LEU A O   
421  C  CB  . LEU A 74  ? 0.1529 0.2050 0.3050 0.0152  0.0378  -0.0026 54  LEU A CB  
422  C  CG  . LEU A 74  ? 0.1617 0.2010 0.2986 0.0133  0.0358  -0.0033 54  LEU A CG  
423  C  CD1 . LEU A 74  ? 0.1909 0.2220 0.3311 0.0176  0.0337  -0.0033 54  LEU A CD1 
424  C  CD2 . LEU A 74  ? 0.1650 0.2016 0.2931 0.0087  0.0304  0.0011  54  LEU A CD2 
425  N  N   . SER A 75  ? 0.1429 0.2296 0.3196 0.0138  0.0482  -0.0018 55  SER A N   
426  C  CA  . SER A 75  ? 0.1501 0.2539 0.3448 0.0143  0.0500  0.0013  55  SER A CA  
427  C  C   . SER A 75  ? 0.1546 0.2653 0.3485 0.0055  0.0476  0.0074  55  SER A C   
428  O  O   . SER A 75  ? 0.1762 0.2959 0.3835 0.0033  0.0430  0.0125  55  SER A O   
429  C  CB  . SER A 75  ? 0.1664 0.2819 0.3689 0.0197  0.0604  -0.0045 55  SER A CB  
430  O  OG  . SER A 75  ? 0.1992 0.3072 0.4057 0.0283  0.0615  -0.0107 55  SER A OG  
431  N  N   . TYR A 76  ? 0.1768 0.2835 0.3563 0.0002  0.0501  0.0073  56  TYR A N   
432  C  CA  . TYR A 76  ? 0.1821 0.2925 0.3613 -0.0086 0.0470  0.0137  56  TYR A CA  
433  C  C   . TYR A 76  ? 0.1642 0.2648 0.3423 -0.0117 0.0359  0.0168  56  TYR A C   
434  O  O   . TYR A 76  ? 0.1730 0.2785 0.3582 -0.0180 0.0311  0.0219  56  TYR A O   
435  C  CB  . TYR A 76  ? 0.1635 0.2682 0.3263 -0.0133 0.0501  0.0139  56  TYR A CB  
436  C  CG  . TYR A 76  ? 0.1579 0.2773 0.3213 -0.0144 0.0602  0.0143  56  TYR A CG  
437  C  CD1 . TYR A 76  ? 0.2370 0.3734 0.4127 -0.0199 0.0630  0.0212  56  TYR A CD1 
438  C  CD2 . TYR A 76  ? 0.2335 0.3503 0.3842 -0.0106 0.0668  0.0081  56  TYR A CD2 
439  C  CE1 . TYR A 76  ? 0.2327 0.3847 0.4075 -0.0210 0.0733  0.0223  56  TYR A CE1 
440  C  CE2 . TYR A 76  ? 0.2093 0.3404 0.3574 -0.0114 0.0762  0.0078  56  TYR A CE2 
441  C  CZ  . TYR A 76  ? 0.2118 0.3612 0.3716 -0.0164 0.0801  0.0152  56  TYR A CZ  
442  O  OH  . TYR A 76  ? 0.2797 0.4455 0.4358 -0.0171 0.0905  0.0156  56  TYR A OH  
443  N  N   . SER A 77  ? 0.1501 0.2370 0.3188 -0.0078 0.0315  0.0137  57  SER A N   
444  C  CA  . SER A 77  ? 0.1461 0.2255 0.3124 -0.0097 0.0214  0.0157  57  SER A CA  
445  C  C   . SER A 77  ? 0.1792 0.2704 0.3629 -0.0096 0.0167  0.0192  57  SER A C   
446  O  O   . SER A 77  ? 0.1453 0.2368 0.3314 -0.0150 0.0088  0.0221  57  SER A O   
447  C  CB  . SER A 77  ? 0.1382 0.2044 0.2925 -0.0049 0.0191  0.0128  57  SER A CB  
448  O  OG  . SER A 77  ? 0.1584 0.2180 0.3066 -0.0068 0.0103  0.0140  57  SER A OG  
449  N  N   . SER A 78  ? 0.1374 0.2384 0.3343 -0.0036 0.0210  0.0188  58  SER A N   
450  C  CA  . SER A 78  ? 0.1374 0.2520 0.3538 -0.0028 0.0168  0.0228  58  SER A CA  
451  C  C   . SER A 78  ? 0.1382 0.2682 0.3681 -0.0091 0.0187  0.0268  58  SER A C   
452  O  O   . SER A 78  ? 0.1443 0.2812 0.3850 -0.0137 0.0108  0.0313  58  SER A O   
453  C  CB  . SER A 78  ? 0.1367 0.2573 0.3656 0.0064  0.0215  0.0212  58  SER A CB  
454  O  OG  . SER A 78  ? 0.1768 0.2870 0.4008 0.0108  0.0155  0.0215  58  SER A OG  
455  N  N   . TYR A 79  ? 0.1478 0.2849 0.3779 -0.0097 0.0290  0.0257  59  TYR A N   
456  C  CA  . TYR A 79  ? 0.1571 0.3102 0.3997 -0.0168 0.0316  0.0312  59  TYR A CA  
457  C  C   . TYR A 79  ? 0.1430 0.2877 0.3799 -0.0268 0.0221  0.0354  59  TYR A C   
458  O  O   . TYR A 79  ? 0.1646 0.3195 0.4166 -0.0330 0.0167  0.0410  59  TYR A O   
459  C  CB  . TYR A 79  ? 0.1906 0.3509 0.4285 -0.0166 0.0440  0.0298  59  TYR A CB  
460  C  CG  . TYR A 79  ? 0.1430 0.3167 0.3909 -0.0075 0.0546  0.0253  59  TYR A CG  
461  C  CD1 . TYR A 79  ? 0.1812 0.3769 0.4535 -0.0052 0.0578  0.0285  59  TYR A CD1 
462  C  CD2 . TYR A 79  ? 0.1731 0.3380 0.4071 -0.0010 0.0613  0.0175  59  TYR A CD2 
463  C  CE1 . TYR A 79  ? 0.2178 0.4255 0.4997 0.0044  0.0679  0.0231  59  TYR A CE1 
464  C  CE2 . TYR A 79  ? 0.1645 0.3398 0.4070 0.0079  0.0706  0.0116  59  TYR A CE2 
465  C  CZ  . TYR A 79  ? 0.1641 0.3605 0.4304 0.0111  0.0742  0.0141  59  TYR A CZ  
466  O  OH  . TYR A 79  ? 0.2358 0.4420 0.5108 0.0212  0.0839  0.0069  59  TYR A OH  
467  N  N   . LEU A 80  ? 0.1443 0.2698 0.3606 -0.0281 0.0194  0.0323  60  LEU A N   
468  C  CA  . LEU A 80  ? 0.1610 0.2757 0.3710 -0.0365 0.0105  0.0347  60  LEU A CA  
469  C  C   . LEU A 80  ? 0.1516 0.2631 0.3663 -0.0377 -0.0018 0.0346  60  LEU A C   
470  O  O   . LEU A 80  ? 0.1921 0.3059 0.4157 -0.0455 -0.0095 0.0384  60  LEU A O   
471  C  CB  . LEU A 80  ? 0.1609 0.2565 0.3487 -0.0354 0.0109  0.0306  60  LEU A CB  
472  C  CG  . LEU A 80  ? 0.1633 0.2438 0.3424 -0.0418 0.0019  0.0311  60  LEU A CG  
473  C  CD1 . LEU A 80  ? 0.2327 0.3194 0.4212 -0.0513 0.0020  0.0383  60  LEU A CD1 
474  C  CD2 . LEU A 80  ? 0.2020 0.2660 0.3610 -0.0380 0.0036  0.0264  60  LEU A CD2 
475  N  N   . GLY A 81  ? 0.1777 0.2839 0.3866 -0.0303 -0.0043 0.0307  61  GLY A N   
476  C  CA  . GLY A 81  ? 0.1749 0.2785 0.3849 -0.0309 -0.0161 0.0306  61  GLY A CA  
477  C  C   . GLY A 81  ? 0.2858 0.4072 0.5188 -0.0339 -0.0208 0.0358  61  GLY A C   
478  O  O   . GLY A 81  ? 0.2300 0.3502 0.4651 -0.0376 -0.0326 0.0363  61  GLY A O   
479  N  N   . ASN A 82  ? 0.1776 0.3166 0.4283 -0.0321 -0.0119 0.0392  62  ASN A N   
480  C  CA  . ASN A 82  ? 0.2029 0.3618 0.4787 -0.0340 -0.0153 0.0448  62  ASN A CA  
481  C  C   . ASN A 82  ? 0.2199 0.3911 0.5106 -0.0440 -0.0148 0.0507  62  ASN A C   
482  O  O   . ASN A 82  ? 0.2103 0.4007 0.5247 -0.0464 -0.0172 0.0562  62  ASN A O   
483  C  CB  . ASN A 82  ? 0.1890 0.3621 0.4786 -0.0244 -0.0062 0.0449  62  ASN A CB  
484  C  CG  . ASN A 82  ? 0.3658 0.5332 0.6526 -0.0166 -0.0120 0.0433  62  ASN A CG  
485  O  OD1 . ASN A 82  ? 0.3511 0.5291 0.6535 -0.0159 -0.0198 0.0473  62  ASN A OD1 
486  N  ND2 . ASN A 82  ? 0.2866 0.4376 0.5539 -0.0111 -0.0089 0.0384  62  ASN A ND2 
487  N  N   . LEU A 83  ? 0.1795 0.3407 0.4585 -0.0501 -0.0122 0.0507  63  LEU A N   
488  C  CA  . LEU A 83  ? 0.2356 0.4062 0.5282 -0.0610 -0.0132 0.0579  63  LEU A CA  
489  C  C   . LEU A 83  ? 0.2888 0.4578 0.5913 -0.0690 -0.0291 0.0601  63  LEU A C   
490  O  O   . LEU A 83  ? 0.2408 0.3951 0.5308 -0.0668 -0.0395 0.0544  63  LEU A O   
491  C  CB  . LEU A 83  ? 0.2334 0.3898 0.5098 -0.0660 -0.0098 0.0581  63  LEU A CB  
492  C  CG  . LEU A 83  ? 0.2644 0.4240 0.5311 -0.0608 0.0052  0.0571  63  LEU A CG  
493  C  CD1 . LEU A 83  ? 0.2530 0.3952 0.5015 -0.0654 0.0051  0.0572  63  LEU A CD1 
494  C  CD2 . LEU A 83  ? 0.2170 0.4037 0.5037 -0.0625 0.0159  0.0640  63  LEU A CD2 
495  N  N   . PRO A 84  ? 0.2561 0.4410 0.5810 -0.0784 -0.0315 0.0683  64  PRO A N   
496  C  CA  . PRO A 84  ? 0.2642 0.4464 0.5990 -0.0875 -0.0481 0.0701  64  PRO A CA  
497  C  C   . PRO A 84  ? 0.3144 0.4682 0.6274 -0.0918 -0.0581 0.0640  64  PRO A C   
498  O  O   . PRO A 84  ? 0.3006 0.4414 0.5995 -0.0926 -0.0522 0.0631  64  PRO A O   
499  C  CB  . PRO A 84  ? 0.3027 0.5015 0.6564 -0.0959 -0.0450 0.0794  64  PRO A CB  
500  C  CG  . PRO A 84  ? 0.1931 0.4117 0.5530 -0.0888 -0.0270 0.0823  64  PRO A CG  
501  C  CD  . PRO A 84  ? 0.2033 0.4098 0.5450 -0.0818 -0.0192 0.0766  64  PRO A CD  
502  N  N   . LYS A 85  ? 0.3784 0.5228 0.6883 -0.0939 -0.0735 0.0593  65  LYS A N   
503  C  CA  . LYS A 85  ? 0.4170 0.5343 0.7054 -0.0960 -0.0834 0.0511  65  LYS A CA  
504  C  C   . LYS A 85  ? 0.3638 0.4711 0.6555 -0.1063 -0.0849 0.0550  65  LYS A C   
505  O  O   . LYS A 85  ? 0.4696 0.5546 0.7419 -0.1051 -0.0857 0.0493  65  LYS A O   
506  C  CB  . LYS A 85  ? 0.5466 0.6595 0.8347 -0.0985 -0.1008 0.0461  65  LYS A CB  
507  C  CG  . LYS A 85  ? 0.7125 0.8026 0.9713 -0.0922 -0.1070 0.0342  65  LYS A CG  
508  C  CD  . LYS A 85  ? 0.6944 0.7617 0.9440 -0.0994 -0.1176 0.0281  65  LYS A CD  
509  C  CE  . LYS A 85  ? 0.7771 0.8239 0.9970 -0.0914 -0.1215 0.0155  65  LYS A CE  
510  N  NZ  . LYS A 85  ? 0.8852 0.9083 1.0959 -0.0965 -0.1312 0.0079  65  LYS A NZ  
511  N  N   . SER A 86  ? 0.3514 0.4741 0.6658 -0.1154 -0.0844 0.0651  66  SER A N   
512  C  CA  . SER A 86  ? 0.4851 0.5968 0.7979 -0.1233 -0.0840 0.0698  66  SER A CA  
513  C  C   . SER A 86  ? 0.4437 0.5519 0.7468 -0.1207 -0.0709 0.0724  66  SER A C   
514  O  O   . SER A 86  ? 0.4540 0.5426 0.7467 -0.1243 -0.0736 0.0720  66  SER A O   
515  C  CB  . SER A 86  ? 0.4666 0.5962 0.7985 -0.1299 -0.0822 0.0799  66  SER A CB  
516  O  OG  . SER A 86  ? 0.5612 0.7171 0.9042 -0.1250 -0.0677 0.0859  66  SER A OG  
517  N  N   . GLU A 87  ? 0.3973 0.5236 0.7032 -0.1139 -0.0570 0.0747  67  GLU A N   
518  C  CA  . GLU A 87  ? 0.4375 0.5595 0.7285 -0.1095 -0.0439 0.0755  67  GLU A CA  
519  C  C   . GLU A 87  ? 0.3943 0.4905 0.6580 -0.1016 -0.0464 0.0644  67  GLU A C   
520  O  O   . GLU A 87  ? 0.3379 0.4199 0.5895 -0.1026 -0.0441 0.0649  67  GLU A O   
521  C  CB  . GLU A 87  ? 0.4797 0.6249 0.7752 -0.1015 -0.0283 0.0774  67  GLU A CB  
522  C  CG  . GLU A 87  ? 0.4950 0.6663 0.8117 -0.1065 -0.0212 0.0876  67  GLU A CG  
523  C  CD  . GLU A 87  ? 0.5452 0.7247 0.8555 -0.1066 -0.0066 0.0933  67  GLU A CD  
524  O  OE1 . GLU A 87  ? 0.5194 0.6838 0.8141 -0.1068 -0.0050 0.0923  67  GLU A OE1 
525  O  OE2 . GLU A 87  ? 0.6335 0.8352 0.9541 -0.1062 0.0030  0.0986  67  GLU A OE2 
526  N  N   . LEU A 88  ? 0.2990 0.3903 0.5535 -0.0935 -0.0508 0.0553  68  LEU A N   
527  C  CA  . LEU A 88  ? 0.3615 0.4312 0.5910 -0.0857 -0.0522 0.0453  68  LEU A CA  
528  C  C   . LEU A 88  ? 0.3258 0.3726 0.5480 -0.0912 -0.0643 0.0412  68  LEU A C   
529  O  O   . LEU A 88  ? 0.3551 0.3847 0.5600 -0.0871 -0.0627 0.0364  68  LEU A O   
530  C  CB  . LEU A 88  ? 0.3471 0.4191 0.5698 -0.0769 -0.0545 0.0383  68  LEU A CB  
531  C  CG  . LEU A 88  ? 0.2663 0.3566 0.4946 -0.0696 -0.0421 0.0410  68  LEU A CG  
532  C  CD1 . LEU A 88  ? 0.2932 0.3872 0.5195 -0.0624 -0.0461 0.0368  68  LEU A CD1 
533  C  CD2 . LEU A 88  ? 0.2597 0.3440 0.4732 -0.0640 -0.0301 0.0394  68  LEU A CD2 
534  N  N   . ASP A 89  ? 0.3805 0.4263 0.6164 -0.1003 -0.0769 0.0428  69  ASP A N   
535  C  CA  . ASP A 89  ? 0.4181 0.4402 0.6484 -0.1055 -0.0892 0.0379  69  ASP A CA  
536  C  C   . ASP A 89  ? 0.3814 0.3932 0.6102 -0.1092 -0.0845 0.0438  69  ASP A C   
537  O  O   . ASP A 89  ? 0.4181 0.4068 0.6348 -0.1079 -0.0905 0.0374  69  ASP A O   
538  C  CB  . ASP A 89  ? 0.3879 0.4122 0.6370 -0.1165 -0.1037 0.0401  69  ASP A CB  
539  C  CG  . ASP A 89  ? 0.5249 0.5525 0.7704 -0.1128 -0.1129 0.0319  69  ASP A CG  
540  O  OD1 . ASP A 89  ? 0.6006 0.6199 0.8245 -0.1024 -0.1116 0.0220  69  ASP A OD1 
541  O  OD2 . ASP A 89  ? 0.5287 0.5684 0.7933 -0.1207 -0.1216 0.0361  69  ASP A OD2 
542  N  N   . ARG A 90  ? 0.4132 0.4422 0.6535 -0.1132 -0.0737 0.0557  70  ARG A N   
543  C  CA  . ARG A 90  ? 0.3941 0.4153 0.6320 -0.1170 -0.0691 0.0630  70  ARG A CA  
544  C  C   . ARG A 90  ? 0.4406 0.4500 0.6557 -0.1063 -0.0618 0.0565  70  ARG A C   
545  O  O   . ARG A 90  ? 0.3790 0.3767 0.5892 -0.1083 -0.0610 0.0606  70  ARG A O   
546  C  CB  . ARG A 90  ? 0.4204 0.4662 0.6739 -0.1232 -0.0582 0.0774  70  ARG A CB  
547  C  CG  . ARG A 90  ? 0.5881 0.6466 0.8585 -0.1304 -0.0624 0.0839  70  ARG A CG  
548  C  CD  . ARG A 90  ? 0.5343 0.6130 0.8124 -0.1343 -0.0506 0.0969  70  ARG A CD  
549  N  NE  . ARG A 90  ? 0.6032 0.6982 0.8991 -0.1400 -0.0529 0.1029  70  ARG A NE  
550  C  CZ  . ARG A 90  ? 0.5888 0.7092 0.8962 -0.1374 -0.0453 0.1047  70  ARG A CZ  
551  N  NH1 . ARG A 90  ? 0.6766 0.8095 0.9799 -0.1291 -0.0343 0.1011  70  ARG A NH1 
552  N  NH2 . ARG A 90  ? 0.6124 0.7459 0.9368 -0.1430 -0.0489 0.1102  70  ARG A NH2 
553  N  N   . LEU A 91  ? 0.3610 0.3734 0.5631 -0.0955 -0.0569 0.0476  71  LEU A N   
554  C  CA  . LEU A 91  ? 0.4064 0.4104 0.5890 -0.0859 -0.0495 0.0423  71  LEU A CA  
555  C  C   . LEU A 91  ? 0.3648 0.3481 0.5320 -0.0793 -0.0573 0.0301  71  LEU A C   
556  O  O   . LEU A 91  ? 0.3518 0.3287 0.5038 -0.0710 -0.0519 0.0253  71  LEU A O   
557  C  CB  . LEU A 91  ? 0.3901 0.4119 0.5693 -0.0783 -0.0376 0.0415  71  LEU A CB  
558  C  CG  . LEU A 91  ? 0.4225 0.4662 0.6148 -0.0827 -0.0278 0.0517  71  LEU A CG  
559  C  CD1 . LEU A 91  ? 0.3588 0.4177 0.5487 -0.0741 -0.0173 0.0487  71  LEU A CD1 
560  C  CD2 . LEU A 91  ? 0.4235 0.4639 0.6117 -0.0868 -0.0228 0.0592  71  LEU A CD2 
561  N  N   . GLU A 92  ? 0.3426 0.3161 0.5136 -0.0829 -0.0700 0.0249  72  GLU A N   
562  C  CA  . GLU A 92  ? 0.4009 0.3562 0.5564 -0.0761 -0.0772 0.0122  72  GLU A CA  
563  C  C   . GLU A 92  ? 0.4530 0.3866 0.6046 -0.0771 -0.0817 0.0106  72  GLU A C   
564  O  O   . GLU A 92  ? 0.4810 0.4092 0.6459 -0.0865 -0.0868 0.0182  72  GLU A O   
565  C  CB  . GLU A 92  ? 0.3974 0.3509 0.5563 -0.0791 -0.0896 0.0057  72  GLU A CB  
566  C  CG  . GLU A 92  ? 0.4012 0.3737 0.5605 -0.0753 -0.0864 0.0054  72  GLU A CG  
567  C  CD  . GLU A 92  ? 0.4799 0.4508 0.6405 -0.0780 -0.1000 -0.0012 72  GLU A CD  
568  O  OE1 . GLU A 92  ? 0.6076 0.5610 0.7666 -0.0820 -0.1117 -0.0076 72  GLU A OE1 
569  O  OE2 . GLU A 92  ? 0.4863 0.4728 0.6497 -0.0761 -0.0996 -0.0001 72  GLU A OE2 
570  N  N   . ASN A 93  ? 0.3821 0.3037 0.5169 -0.0672 -0.0801 0.0014  73  ASN A N   
571  C  CA  . ASN A 93  ? 0.3871 0.2890 0.5183 -0.0656 -0.0830 -0.0003 73  ASN A CA  
572  C  C   . ASN A 93  ? 0.3577 0.2438 0.4748 -0.0569 -0.0893 -0.0157 73  ASN A C   
573  O  O   . ASN A 93  ? 0.3980 0.2837 0.5012 -0.0468 -0.0828 -0.0214 73  ASN A O   
574  C  CB  . ASN A 93  ? 0.4139 0.3212 0.5404 -0.0617 -0.0715 0.0064  73  ASN A CB  
575  C  CG  . ASN A 93  ? 0.5119 0.4033 0.6418 -0.0638 -0.0749 0.0108  73  ASN A CG  
576  O  OD1 . ASN A 93  ? 0.5599 0.4328 0.6941 -0.0661 -0.0858 0.0065  73  ASN A OD1 
577  N  ND2 . ASN A 93  ? 0.5465 0.4442 0.6746 -0.0630 -0.0663 0.0194  73  ASN A ND2 
578  N  N   . GLU A 94  ? 0.4057 0.2793 0.5265 -0.0611 -0.1023 -0.0228 74  GLU A N   
579  C  CA  . GLU A 94  ? 0.5218 0.3817 0.6277 -0.0526 -0.1084 -0.0391 74  GLU A CA  
580  C  C   . GLU A 94  ? 0.5273 0.3690 0.6272 -0.0451 -0.1078 -0.0444 74  GLU A C   
581  O  O   . GLU A 94  ? 0.5178 0.3566 0.6022 -0.0339 -0.1045 -0.0552 74  GLU A O   
582  C  CB  . GLU A 94  ? 0.6138 0.4634 0.7248 -0.0592 -0.1237 -0.0464 74  GLU A CB  
583  C  CG  . GLU A 94  ? 0.5865 0.4212 0.6802 -0.0502 -0.1306 -0.0649 74  GLU A CG  
584  C  CD  . GLU A 94  ? 0.7829 0.6093 0.8793 -0.0568 -0.1463 -0.0735 74  GLU A CD  
585  O  OE1 . GLU A 94  ? 0.8008 0.6261 0.9164 -0.0693 -0.1542 -0.0652 74  GLU A OE1 
586  O  OE2 . GLU A 94  ? 0.8634 0.6855 0.9425 -0.0498 -0.1510 -0.0885 74  GLU A OE2 
587  N  N   . LYS A 95  ? 0.5242 0.3547 0.6371 -0.0510 -0.1107 -0.0361 75  LYS A N   
588  C  CA  . LYS A 95  ? 0.5582 0.3717 0.6678 -0.0436 -0.1106 -0.0400 75  LYS A CA  
589  C  C   . LYS A 95  ? 0.6417 0.4672 0.7408 -0.0340 -0.0971 -0.0378 75  LYS A C   
590  O  O   . LYS A 95  ? 0.5764 0.3917 0.6687 -0.0242 -0.0959 -0.0452 75  LYS A O   
591  C  CB  . LYS A 95  ? 0.7095 0.5101 0.8361 -0.0525 -0.1165 -0.0285 75  LYS A CB  
592  C  CG  . LYS A 95  ? 0.6281 0.4464 0.7661 -0.0630 -0.1102 -0.0099 75  LYS A CG  
593  C  CD  . LYS A 95  ? 0.9332 0.7432 1.0846 -0.0708 -0.1149 0.0024  75  LYS A CD  
594  C  CE  . LYS A 95  ? 0.9740 0.8033 1.1368 -0.0825 -0.1098 0.0200  75  LYS A CE  
595  N  NZ  . LYS A 95  ? 0.9554 0.7803 1.1290 -0.0894 -0.1139 0.0321  75  LYS A NZ  
596  N  N   . ALA A 96  ? 0.4239 0.2707 0.5226 -0.0365 -0.0872 -0.0284 76  ALA A N   
597  C  CA  . ALA A 96  ? 0.5148 0.3737 0.6038 -0.0283 -0.0752 -0.0269 76  ALA A CA  
598  C  C   . ALA A 96  ? 0.4785 0.3463 0.5532 -0.0200 -0.0712 -0.0371 76  ALA A C   
599  O  O   . ALA A 96  ? 0.4493 0.3301 0.5175 -0.0149 -0.0613 -0.0346 76  ALA A O   
600  C  CB  . ALA A 96  ? 0.4879 0.3641 0.5830 -0.0346 -0.0668 -0.0129 76  ALA A CB  
601  N  N   . LYS A 97  ? 0.5013 0.3623 0.5708 -0.0189 -0.0793 -0.0480 77  LYS A N   
602  C  CA  . LYS A 97  ? 0.4528 0.3239 0.5082 -0.0124 -0.0766 -0.0562 77  LYS A CA  
603  C  C   . LYS A 97  ? 0.3924 0.2843 0.4497 -0.0160 -0.0697 -0.0470 77  LYS A C   
604  O  O   . LYS A 97  ? 0.4120 0.3154 0.4591 -0.0098 -0.0629 -0.0485 77  LYS A O   
605  C  CB  . LYS A 97  ? 0.5258 0.3963 0.5683 -0.0001 -0.0698 -0.0635 77  LYS A CB  
606  C  CG  . LYS A 97  ? 0.6304 0.4808 0.6718 0.0057  -0.0756 -0.0736 77  LYS A CG  
607  C  CD  . LYS A 97  ? 0.7658 0.6197 0.7976 0.0180  -0.0670 -0.0787 77  LYS A CD  
608  C  CE  . LYS A 97  ? 0.8540 0.6886 0.8886 0.0246  -0.0717 -0.0872 77  LYS A CE  
609  N  NZ  . LYS A 97  ? 0.8826 0.7233 0.9112 0.0367  -0.0625 -0.0906 77  LYS A NZ  
610  N  N   . TYR A 98  ? 0.4416 0.3385 0.5131 -0.0258 -0.0712 -0.0371 78  TYR A N   
611  C  CA  . TYR A 98  ? 0.4252 0.3414 0.5019 -0.0293 -0.0647 -0.0283 78  TYR A CA  
612  C  C   . TYR A 98  ? 0.4858 0.4120 0.5571 -0.0233 -0.0525 -0.0241 78  TYR A C   
613  O  O   . TYR A 98  ? 0.3690 0.3098 0.4406 -0.0227 -0.0468 -0.0202 78  TYR A O   
614  C  CB  . TYR A 98  ? 0.4235 0.3479 0.4964 -0.0292 -0.0693 -0.0326 78  TYR A CB  
615  C  CG  . TYR A 98  ? 0.4119 0.3273 0.4904 -0.0358 -0.0826 -0.0373 78  TYR A CG  
616  C  CD1 . TYR A 98  ? 0.4067 0.3264 0.5029 -0.0464 -0.0870 -0.0291 78  TYR A CD1 
617  C  CD2 . TYR A 98  ? 0.5143 0.4174 0.5803 -0.0315 -0.0909 -0.0504 78  TYR A CD2 
618  C  CE1 . TYR A 98  ? 0.4436 0.3551 0.5467 -0.0535 -0.1003 -0.0330 78  TYR A CE1 
619  C  CE2 . TYR A 98  ? 0.4914 0.3851 0.5622 -0.0378 -0.1043 -0.0558 78  TYR A CE2 
620  C  CZ  . TYR A 98  ? 0.5192 0.4166 0.6093 -0.0493 -0.1095 -0.0468 78  TYR A CZ  
621  O  OH  . TYR A 98  ? 0.5516 0.4395 0.6483 -0.0566 -0.1240 -0.0518 78  TYR A OH  
622  N  N   . LEU A 99  ? 0.3950 0.3131 0.4625 -0.0189 -0.0491 -0.0247 79  LEU A N   
623  C  CA  . LEU A 99  ? 0.3896 0.3163 0.4537 -0.0146 -0.0389 -0.0204 79  LEU A CA  
624  C  C   . LEU A 99  ? 0.3027 0.2325 0.3758 -0.0206 -0.0352 -0.0102 79  LEU A C   
625  O  O   . LEU A 99  ? 0.3154 0.2495 0.3858 -0.0178 -0.0284 -0.0068 79  LEU A O   
626  C  CB  . LEU A 99  ? 0.3758 0.2950 0.4306 -0.0056 -0.0372 -0.0268 79  LEU A CB  
627  C  CG  . LEU A 99  ? 0.5498 0.4732 0.5927 0.0014  -0.0365 -0.0351 79  LEU A CG  
628  C  CD1 . LEU A 99  ? 0.5221 0.4424 0.5572 0.0107  -0.0326 -0.0404 79  LEU A CD1 
629  C  CD2 . LEU A 99  ? 0.4548 0.3943 0.4968 0.0009  -0.0306 -0.0301 79  LEU A CD2 
630  N  N   . THR A 100 ? 0.3400 0.2685 0.4236 -0.0292 -0.0400 -0.0051 80  THR A N   
631  C  CA  . THR A 100 ? 0.2495 0.1866 0.3417 -0.0360 -0.0356 0.0056  80  THR A CA  
632  C  C   . THR A 100 ? 0.2847 0.2313 0.3876 -0.0432 -0.0381 0.0090  80  THR A C   
633  O  O   . THR A 100 ? 0.3089 0.2485 0.4157 -0.0461 -0.0471 0.0052  80  THR A O   
634  C  CB  . THR A 100 ? 0.4945 0.4203 0.5913 -0.0403 -0.0393 0.0113  80  THR A CB  
635  O  OG1 . THR A 100 ? 0.4626 0.3818 0.5514 -0.0332 -0.0368 0.0091  80  THR A OG1 
636  C  CG2 . THR A 100 ? 0.4449 0.3821 0.5496 -0.0483 -0.0348 0.0231  80  THR A CG2 
637  N  N   . GLY A 101 ? 0.2610 0.2239 0.3690 -0.0457 -0.0305 0.0155  81  GLY A N   
638  C  CA  . GLY A 101 ? 0.2982 0.2730 0.4187 -0.0518 -0.0319 0.0194  81  GLY A CA  
639  C  C   . GLY A 101 ? 0.2178 0.1995 0.3364 -0.0471 -0.0326 0.0135  81  GLY A C   
640  O  O   . GLY A 101 ? 0.2167 0.1980 0.3246 -0.0393 -0.0290 0.0084  81  GLY A O   
641  N  N   . TRP A 102 ? 0.2435 0.2321 0.3738 -0.0524 -0.0381 0.0153  82  TRP A N   
642  C  CA  . TRP A 102 ? 0.2208 0.2193 0.3528 -0.0493 -0.0393 0.0124  82  TRP A CA  
643  C  C   . TRP A 102 ? 0.2571 0.2449 0.3824 -0.0482 -0.0505 0.0044  82  TRP A C   
644  O  O   . TRP A 102 ? 0.2849 0.2607 0.4122 -0.0533 -0.0594 0.0023  82  TRP A O   
645  C  CB  . TRP A 102 ? 0.2486 0.2643 0.3993 -0.0555 -0.0386 0.0197  82  TRP A CB  
646  C  CG  . TRP A 102 ? 0.2892 0.3142 0.4450 -0.0536 -0.0431 0.0178  82  TRP A CG  
647  C  CD1 . TRP A 102 ? 0.3319 0.3555 0.4936 -0.0582 -0.0550 0.0158  82  TRP A CD1 
648  C  CD2 . TRP A 102 ? 0.2956 0.3329 0.4523 -0.0470 -0.0369 0.0180  82  TRP A CD2 
649  N  NE1 . TRP A 102 ? 0.3530 0.3884 0.5184 -0.0546 -0.0564 0.0156  82  TRP A NE1 
650  C  CE2 . TRP A 102 ? 0.3601 0.4036 0.5231 -0.0476 -0.0453 0.0173  82  TRP A CE2 
651  C  CE3 . TRP A 102 ? 0.2870 0.3298 0.4402 -0.0407 -0.0258 0.0188  82  TRP A CE3 
652  C  CZ2 . TRP A 102 ? 0.3024 0.3575 0.4692 -0.0418 -0.0428 0.0184  82  TRP A CZ2 
653  C  CZ3 . TRP A 102 ? 0.3299 0.3828 0.4871 -0.0350 -0.0234 0.0189  82  TRP A CZ3 
654  C  CH2 . TRP A 102 ? 0.3988 0.4578 0.5632 -0.0354 -0.0317 0.0193  82  TRP A CH2 
655  N  N   . SER A 103 ? 0.2819 0.2742 0.3994 -0.0419 -0.0505 0.0001  83  SER A N   
656  C  CA  . SER A 103 ? 0.3136 0.3000 0.4243 -0.0412 -0.0612 -0.0070 83  SER A CA  
657  C  C   . SER A 103 ? 0.3264 0.3259 0.4363 -0.0372 -0.0611 -0.0063 83  SER A C   
658  O  O   . SER A 103 ? 0.2811 0.2892 0.3906 -0.0322 -0.0521 -0.0027 83  SER A O   
659  C  CB  . SER A 103 ? 0.3522 0.3225 0.4446 -0.0354 -0.0630 -0.0162 83  SER A CB  
660  O  OG  . SER A 103 ? 0.3272 0.3006 0.4088 -0.0272 -0.0537 -0.0166 83  SER A OG  
661  N  N   . LEU A 104 ? 0.3165 0.3168 0.4266 -0.0397 -0.0720 -0.0095 84  LEU A N   
662  C  CA  . LEU A 104 ? 0.3037 0.3145 0.4104 -0.0357 -0.0745 -0.0090 84  LEU A CA  
663  C  C   . LEU A 104 ? 0.3997 0.4016 0.4834 -0.0292 -0.0771 -0.0175 84  LEU A C   
664  O  O   . LEU A 104 ? 0.3757 0.3644 0.4496 -0.0301 -0.0839 -0.0260 84  LEU A O   
665  C  CB  . LEU A 104 ? 0.2623 0.2817 0.3830 -0.0425 -0.0856 -0.0068 84  LEU A CB  
666  C  CG  . LEU A 104 ? 0.4047 0.4401 0.5306 -0.0397 -0.0873 -0.0019 84  LEU A CG  
667  C  CD1 . LEU A 104 ? 0.3629 0.4101 0.5003 -0.0357 -0.0748 0.0061  84  LEU A CD1 
668  C  CD2 . LEU A 104 ? 0.3605 0.4044 0.5019 -0.0472 -0.0997 0.0003  84  LEU A CD2 
669  N  N   . GLY A 105 ? 0.3197 0.3288 0.3951 -0.0224 -0.0714 -0.0151 85  GLY A N   
670  C  CA  . GLY A 105 ? 0.3368 0.3413 0.3906 -0.0160 -0.0720 -0.0213 85  GLY A CA  
671  C  C   . GLY A 105 ? 0.3811 0.3983 0.4314 -0.0129 -0.0739 -0.0164 85  GLY A C   
672  O  O   . GLY A 105 ? 0.3310 0.3594 0.3969 -0.0147 -0.0739 -0.0083 85  GLY A O   
673  N  N   . LYS A 106 ? 0.4008 0.4168 0.4307 -0.0078 -0.0756 -0.0210 86  LYS A N   
674  C  CA  . LYS A 106 ? 0.4983 0.5261 0.5221 -0.0047 -0.0776 -0.0152 86  LYS A CA  
675  C  C   . LYS A 106 ? 0.6315 0.6597 0.6382 0.0023  -0.0693 -0.0150 86  LYS A C   
676  O  O   . LYS A 106 ? 0.6114 0.6309 0.6067 0.0053  -0.0650 -0.0225 86  LYS A O   
677  C  CB  . LYS A 106 ? 0.4935 0.5238 0.5084 -0.0073 -0.0916 -0.0198 86  LYS A CB  
678  C  CG  . LYS A 106 ? 0.5787 0.6238 0.6022 -0.0081 -0.0969 -0.0097 86  LYS A CG  
679  C  CD  . LYS A 106 ? 0.6391 0.6873 0.6569 -0.0121 -0.1124 -0.0140 86  LYS A CD  
680  C  CE  . LYS A 106 ? 0.6518 0.6996 0.6401 -0.0076 -0.1160 -0.0202 86  LYS A CE  
681  N  NZ  . LYS A 106 ? 0.6423 0.6936 0.6225 -0.0114 -0.1322 -0.0249 86  LYS A NZ  
682  N  N   . GLU A 107 ? 0.5119 0.5509 0.5192 0.0049  -0.0669 -0.0053 87  GLU A N   
683  C  CA  . GLU A 107 ? 0.6492 0.6921 0.6418 0.0106  -0.0601 -0.0021 87  GLU A CA  
684  C  C   . GLU A 107 ? 0.6748 0.7285 0.6560 0.0117  -0.0673 0.0031  87  GLU A C   
685  O  O   . GLU A 107 ? 0.6372 0.6976 0.6298 0.0089  -0.0747 0.0093  87  GLU A O   
686  C  CB  . GLU A 107 ? 0.6097 0.6543 0.6156 0.0122  -0.0496 0.0070  87  GLU A CB  
687  C  CG  . GLU A 107 ? 0.5644 0.5997 0.5785 0.0116  -0.0419 0.0028  87  GLU A CG  
688  C  CD  . GLU A 107 ? 0.5773 0.6144 0.6043 0.0127  -0.0332 0.0109  87  GLU A CD  
689  O  OE1 . GLU A 107 ? 0.6010 0.6453 0.6324 0.0140  -0.0333 0.0198  87  GLU A OE1 
690  O  OE2 . GLU A 107 ? 0.5407 0.5715 0.5737 0.0121  -0.0270 0.0083  87  GLU A OE2 
691  N  N   . ASP A 115 ? 0.8957 0.9830 0.8988 0.0079  -0.0932 0.0334  95  ASP A N   
692  C  CA  . ASP A 115 ? 1.0160 1.1019 1.0389 0.0032  -0.0991 0.0297  95  ASP A CA  
693  C  C   . ASP A 115 ? 1.0116 1.0940 1.0585 0.0034  -0.0890 0.0327  95  ASP A C   
694  O  O   . ASP A 115 ? 1.0452 1.1345 1.1140 0.0033  -0.0903 0.0405  95  ASP A O   
695  C  CB  . ASP A 115 ? 1.1412 1.2390 1.1729 0.0010  -0.1122 0.0371  95  ASP A CB  
696  C  CG  . ASP A 115 ? 1.2659 1.3646 1.3175 -0.0047 -0.1196 0.0331  95  ASP A CG  
697  O  OD1 . ASP A 115 ? 1.1705 1.2599 1.2264 -0.0076 -0.1153 0.0243  95  ASP A OD1 
698  O  OD2 . ASP A 115 ? 1.2027 1.3125 1.2668 -0.0066 -0.1300 0.0397  95  ASP A OD2 
699  N  N   . ASN A 116 ? 0.7486 0.8207 0.7912 0.0042  -0.0792 0.0261  96  ASN A N   
700  C  CA  . ASN A 116 ? 0.6923 0.7607 0.7540 0.0041  -0.0697 0.0273  96  ASN A CA  
701  C  C   . ASN A 116 ? 0.5893 0.6505 0.6554 -0.0006 -0.0704 0.0181  96  ASN A C   
702  O  O   . ASN A 116 ? 0.6120 0.6635 0.6647 -0.0006 -0.0674 0.0101  96  ASN A O   
703  C  CB  . ASN A 116 ? 0.7158 0.7791 0.7712 0.0082  -0.0583 0.0291  96  ASN A CB  
704  C  CG  . ASN A 116 ? 0.7591 0.8284 0.8228 0.0117  -0.0559 0.0407  96  ASN A CG  
705  O  OD1 . ASN A 116 ? 0.8266 0.9041 0.8988 0.0118  -0.0631 0.0478  96  ASN A OD1 
706  N  ND2 . ASN A 116 ? 0.8004 0.8653 0.8630 0.0143  -0.0466 0.0430  96  ASN A ND2 
707  N  N   . LEU A 117 ? 0.4727 0.5392 0.5589 -0.0046 -0.0742 0.0200  97  LEU A N   
708  C  CA  . LEU A 117 ? 0.4689 0.5301 0.5630 -0.0100 -0.0743 0.0140  97  LEU A CA  
709  C  C   . LEU A 117 ? 0.3380 0.3959 0.4420 -0.0090 -0.0619 0.0151  97  LEU A C   
710  O  O   . LEU A 117 ? 0.3225 0.3873 0.4405 -0.0063 -0.0562 0.0212  97  LEU A O   
711  C  CB  . LEU A 117 ? 0.3933 0.4642 0.5062 -0.0154 -0.0834 0.0169  97  LEU A CB  
712  C  CG  . LEU A 117 ? 0.4112 0.4778 0.5335 -0.0227 -0.0855 0.0124  97  LEU A CG  
713  C  CD1 . LEU A 117 ? 0.4336 0.4881 0.5375 -0.0257 -0.0944 0.0027  97  LEU A CD1 
714  C  CD2 . LEU A 117 ? 0.4381 0.5188 0.5853 -0.0275 -0.0914 0.0182  97  LEU A CD2 
715  N  N   . LYS A 118 ? 0.2705 0.3177 0.3674 -0.0109 -0.0582 0.0088  98  LYS A N   
716  C  CA  . LYS A 118 ? 0.2810 0.3250 0.3835 -0.0098 -0.0469 0.0097  98  LYS A CA  
717  C  C   . LYS A 118 ? 0.3833 0.4211 0.4900 -0.0155 -0.0467 0.0061  98  LYS A C   
718  O  O   . LYS A 118 ? 0.3421 0.3711 0.4398 -0.0183 -0.0531 0.0004  98  LYS A O   
719  C  CB  . LYS A 118 ? 0.3827 0.4196 0.4696 -0.0045 -0.0400 0.0081  98  LYS A CB  
720  C  CG  . LYS A 118 ? 0.3841 0.4108 0.4527 -0.0040 -0.0426 0.0007  98  LYS A CG  
721  C  CD  . LYS A 118 ? 0.5336 0.5558 0.5907 0.0010  -0.0344 0.0001  98  LYS A CD  
722  C  CE  . LYS A 118 ? 0.5126 0.5256 0.5535 0.0025  -0.0362 -0.0081 98  LYS A CE  
723  N  NZ  . LYS A 118 ? 0.5295 0.5417 0.5602 0.0079  -0.0287 -0.0077 98  LYS A NZ  
724  N  N   . GLY A 119 ? 0.2466 0.2890 0.3672 -0.0171 -0.0394 0.0096  99  GLY A N   
725  C  CA  . GLY A 119 ? 0.2787 0.3158 0.4027 -0.0224 -0.0374 0.0083  99  GLY A CA  
726  C  C   . GLY A 119 ? 0.2346 0.2635 0.3484 -0.0191 -0.0287 0.0065  99  GLY A C   
727  O  O   . GLY A 119 ? 0.2384 0.2707 0.3525 -0.0145 -0.0212 0.0084  99  GLY A O   
728  N  N   . SER A 120 ? 0.2080 0.2252 0.3134 -0.0213 -0.0306 0.0027  100 SER A N   
729  C  CA  . SER A 120 ? 0.1763 0.1858 0.2731 -0.0187 -0.0236 0.0014  100 SER A CA  
730  C  C   . SER A 120 ? 0.1789 0.1867 0.2830 -0.0245 -0.0217 0.0042  100 SER A C   
731  O  O   . SER A 120 ? 0.2384 0.2432 0.3483 -0.0305 -0.0283 0.0046  100 SER A O   
732  C  CB  . SER A 120 ? 0.2996 0.2971 0.3806 -0.0152 -0.0270 -0.0049 100 SER A CB  
733  O  OG  . SER A 120 ? 0.3399 0.3402 0.4122 -0.0103 -0.0290 -0.0068 100 SER A OG  
734  N  N   . TYR A 121 ? 0.1830 0.1929 0.2869 -0.0233 -0.0132 0.0066  101 TYR A N   
735  C  CA  . TYR A 121 ? 0.1903 0.1984 0.2976 -0.0284 -0.0108 0.0100  101 TYR A CA  
736  C  C   . TYR A 121 ? 0.1719 0.1709 0.2675 -0.0250 -0.0072 0.0082  101 TYR A C   
737  O  O   . TYR A 121 ? 0.1908 0.1930 0.2823 -0.0204 -0.0011 0.0075  101 TYR A O   
738  C  CB  . TYR A 121 ? 0.1949 0.2172 0.3133 -0.0309 -0.0038 0.0152  101 TYR A CB  
739  C  CG  . TYR A 121 ? 0.1666 0.1882 0.2866 -0.0368 -0.0016 0.0200  101 TYR A CG  
740  C  CD1 . TYR A 121 ? 0.1970 0.2186 0.3264 -0.0446 -0.0072 0.0245  101 TYR A CD1 
741  C  CD2 . TYR A 121 ? 0.1660 0.1865 0.2782 -0.0352 0.0049  0.0208  101 TYR A CD2 
742  C  CE1 . TYR A 121 ? 0.2160 0.2367 0.3470 -0.0505 -0.0057 0.0308  101 TYR A CE1 
743  C  CE2 . TYR A 121 ? 0.2103 0.2305 0.3226 -0.0407 0.0062  0.0264  101 TYR A CE2 
744  C  CZ  . TYR A 121 ? 0.2457 0.2661 0.3675 -0.0484 0.0011  0.0320  101 TYR A CZ  
745  O  OH  . TYR A 121 ? 0.2794 0.2998 0.4018 -0.0545 0.0022  0.0394  101 TYR A OH  
746  N  N   . TYR A 122 ? 0.1799 0.1674 0.2717 -0.0270 -0.0118 0.0074  102 TYR A N   
747  C  CA  . TYR A 122 ? 0.2147 0.1937 0.2974 -0.0236 -0.0097 0.0060  102 TYR A CA  
748  C  C   . TYR A 122 ? 0.1948 0.1726 0.2804 -0.0287 -0.0082 0.0121  102 TYR A C   
749  O  O   . TYR A 122 ? 0.2048 0.1810 0.2980 -0.0353 -0.0123 0.0162  102 TYR A O   
750  C  CB  . TYR A 122 ? 0.2227 0.1888 0.2986 -0.0203 -0.0161 0.0000  102 TYR A CB  
751  C  CG  . TYR A 122 ? 0.2387 0.2059 0.3069 -0.0139 -0.0166 -0.0059 102 TYR A CG  
752  C  CD1 . TYR A 122 ? 0.3098 0.2777 0.3703 -0.0076 -0.0117 -0.0077 102 TYR A CD1 
753  C  CD2 . TYR A 122 ? 0.2814 0.2496 0.3503 -0.0147 -0.0226 -0.0090 102 TYR A CD2 
754  C  CE1 . TYR A 122 ? 0.3070 0.2774 0.3604 -0.0023 -0.0118 -0.0116 102 TYR A CE1 
755  C  CE2 . TYR A 122 ? 0.3040 0.2743 0.3642 -0.0092 -0.0232 -0.0134 102 TYR A CE2 
756  C  CZ  . TYR A 122 ? 0.2705 0.2422 0.3228 -0.0030 -0.0174 -0.0143 102 TYR A CZ  
757  O  OH  . TYR A 122 ? 0.3613 0.3366 0.4048 0.0021  -0.0176 -0.0173 102 TYR A OH  
758  N  N   . ALA A 123 ? 0.1911 0.1694 0.2709 -0.0262 -0.0031 0.0132  103 ALA A N   
759  C  CA  . ALA A 123 ? 0.1819 0.1579 0.2617 -0.0305 -0.0027 0.0193  103 ALA A CA  
760  C  C   . ALA A 123 ? 0.2190 0.1884 0.2908 -0.0257 -0.0022 0.0177  103 ALA A C   
761  O  O   . ALA A 123 ? 0.2252 0.1984 0.2921 -0.0208 0.0019  0.0142  103 ALA A O   
762  C  CB  . ALA A 123 ? 0.1930 0.1827 0.2754 -0.0345 0.0041  0.0246  103 ALA A CB  
763  N  N   . ASN A 124 ? 0.2297 0.1895 0.3016 -0.0274 -0.0067 0.0211  104 ASN A N   
764  C  CA  . ASN A 124 ? 0.2754 0.2319 0.3417 -0.0232 -0.0059 0.0212  104 ASN A CA  
765  C  C   . ASN A 124 ? 0.2232 0.1897 0.2859 -0.0262 -0.0005 0.0264  104 ASN A C   
766  O  O   . ASN A 124 ? 0.2158 0.1902 0.2805 -0.0319 0.0021  0.0312  104 ASN A O   
767  C  CB  . ASN A 124 ? 0.3138 0.2567 0.3825 -0.0232 -0.0129 0.0235  104 ASN A CB  
768  C  CG  . ASN A 124 ? 0.2931 0.2351 0.3658 -0.0312 -0.0153 0.0338  104 ASN A CG  
769  O  OD1 . ASN A 124 ? 0.2648 0.2128 0.3338 -0.0333 -0.0125 0.0400  104 ASN A OD1 
770  N  ND2 . ASN A 124 ? 0.3001 0.2343 0.3803 -0.0359 -0.0211 0.0359  104 ASN A ND2 
771  N  N   . CYS A 125 ? 0.2228 0.1902 0.2801 -0.0221 0.0012  0.0249  105 CYS A N   
772  C  CA  . CYS A 125 ? 0.1999 0.1762 0.2519 -0.0243 0.0055  0.0279  105 CYS A CA  
773  C  C   . CYS A 125 ? 0.2279 0.2008 0.2769 -0.0260 0.0019  0.0343  105 CYS A C   
774  O  O   . CYS A 125 ? 0.2289 0.2065 0.2722 -0.0253 0.0033  0.0346  105 CYS A O   
775  C  CB  . CYS A 125 ? 0.2081 0.1894 0.2571 -0.0197 0.0096  0.0217  105 CYS A CB  
776  S  SG  . CYS A 125 ? 0.2351 0.2217 0.2881 -0.0181 0.0137  0.0161  105 CYS A SG  
777  N  N   . ALA A 126 ? 0.2098 0.1741 0.2632 -0.0285 -0.0037 0.0398  106 ALA A N   
778  C  CA  . ALA A 126 ? 0.2197 0.1808 0.2713 -0.0304 -0.0079 0.0478  106 ALA A CA  
779  C  C   . ALA A 126 ? 0.2265 0.1994 0.2706 -0.0363 -0.0043 0.0543  106 ALA A C   
780  O  O   . ALA A 126 ? 0.2275 0.2019 0.2661 -0.0371 -0.0065 0.0593  106 ALA A O   
781  C  CB  . ALA A 126 ? 0.2547 0.2034 0.3141 -0.0326 -0.0151 0.0534  106 ALA A CB  
782  N  N   . PHE A 127 ? 0.2178 0.1999 0.2611 -0.0403 0.0013  0.0539  107 PHE A N   
783  C  CA  . PHE A 127 ? 0.2176 0.2129 0.2526 -0.0451 0.0063  0.0585  107 PHE A CA  
784  C  C   . PHE A 127 ? 0.2162 0.2172 0.2413 -0.0418 0.0090  0.0529  107 PHE A C   
785  O  O   . PHE A 127 ? 0.2595 0.2697 0.2747 -0.0452 0.0113  0.0565  107 PHE A O   
786  C  CB  . PHE A 127 ? 0.2401 0.2457 0.2785 -0.0480 0.0130  0.0571  107 PHE A CB  
787  C  CG  . PHE A 127 ? 0.2418 0.2489 0.2832 -0.0422 0.0169  0.0457  107 PHE A CG  
788  C  CD1 . PHE A 127 ? 0.2808 0.2949 0.3153 -0.0388 0.0221  0.0387  107 PHE A CD1 
789  C  CD2 . PHE A 127 ? 0.2777 0.2786 0.3288 -0.0405 0.0146  0.0424  107 PHE A CD2 
790  C  CE1 . PHE A 127 ? 0.2439 0.2582 0.2825 -0.0338 0.0249  0.0299  107 PHE A CE1 
791  C  CE2 . PHE A 127 ? 0.2712 0.2740 0.3248 -0.0356 0.0176  0.0338  107 PHE A CE2 
792  C  CZ  . PHE A 127 ? 0.2550 0.2642 0.3030 -0.0322 0.0227  0.0281  107 PHE A CZ  
793  N  N   . TYR A 128 ? 0.2493 0.2455 0.2766 -0.0355 0.0086  0.0442  108 TYR A N   
794  C  CA  . TYR A 128 ? 0.2389 0.2388 0.2591 -0.0330 0.0094  0.0393  108 TYR A CA  
795  C  C   . TYR A 128 ? 0.2695 0.2679 0.2849 -0.0345 0.0034  0.0461  108 TYR A C   
796  O  O   . TYR A 128 ? 0.2978 0.3029 0.3033 -0.0362 0.0037  0.0458  108 TYR A O   
797  C  CB  . TYR A 128 ? 0.2103 0.2054 0.2364 -0.0269 0.0094  0.0312  108 TYR A CB  
798  C  CG  . TYR A 128 ? 0.2125 0.2109 0.2338 -0.0252 0.0095  0.0266  108 TYR A CG  
799  C  CD1 . TYR A 128 ? 0.2321 0.2364 0.2491 -0.0254 0.0144  0.0201  108 TYR A CD1 
800  C  CD2 . TYR A 128 ? 0.2237 0.2192 0.2462 -0.0234 0.0042  0.0286  108 TYR A CD2 
801  C  CE1 . TYR A 128 ? 0.2360 0.2418 0.2494 -0.0246 0.0133  0.0153  108 TYR A CE1 
802  C  CE2 . TYR A 128 ? 0.2605 0.2594 0.2802 -0.0229 0.0033  0.0248  108 TYR A CE2 
803  C  CZ  . TYR A 128 ? 0.2468 0.2500 0.2616 -0.0239 0.0075  0.0180  108 TYR A CZ  
804  O  OH  . TYR A 128 ? 0.2751 0.2800 0.2877 -0.0240 0.0054  0.0136  108 TYR A OH  
805  N  N   . VAL A 129 ? 0.2425 0.2316 0.2648 -0.0334 -0.0026 0.0517  109 VAL A N   
806  C  CA  . VAL A 129 ? 0.2449 0.2319 0.2656 -0.0339 -0.0093 0.0591  109 VAL A CA  
807  C  C   . VAL A 129 ? 0.2853 0.2772 0.2984 -0.0410 -0.0106 0.0700  109 VAL A C   
808  O  O   . VAL A 129 ? 0.3317 0.3291 0.3361 -0.0432 -0.0136 0.0748  109 VAL A O   
809  C  CB  . VAL A 129 ? 0.2996 0.2745 0.3320 -0.0290 -0.0151 0.0604  109 VAL A CB  
810  C  CG1 . VAL A 129 ? 0.3373 0.3099 0.3705 -0.0290 -0.0228 0.0692  109 VAL A CG1 
811  C  CG2 . VAL A 129 ? 0.2997 0.2731 0.3376 -0.0220 -0.0130 0.0503  109 VAL A CG2 
812  N  N   . ASP A 130 ? 0.2960 0.2871 0.3125 -0.0451 -0.0086 0.0748  110 ASP A N   
813  C  CA  . ASP A 130 ? 0.3278 0.3244 0.3391 -0.0527 -0.0094 0.0873  110 ASP A CA  
814  C  C   . ASP A 130 ? 0.2914 0.2937 0.3059 -0.0566 -0.0028 0.0871  110 ASP A C   
815  O  O   . ASP A 130 ? 0.2734 0.2669 0.2998 -0.0556 -0.0042 0.0852  110 ASP A O   
816  C  CB  . ASP A 130 ? 0.3549 0.3396 0.3745 -0.0538 -0.0187 0.0986  110 ASP A CB  
817  C  CG  . ASP A 130 ? 0.4642 0.4538 0.4799 -0.0625 -0.0204 0.1143  110 ASP A CG  
818  O  OD1 . ASP A 130 ? 0.4041 0.4069 0.4125 -0.0681 -0.0134 0.1169  110 ASP A OD1 
819  O  OD2 . ASP A 130 ? 0.5906 0.5710 0.6116 -0.0636 -0.0289 0.1250  110 ASP A OD2 
820  N  N   . PRO A 131 ? 0.3237 0.3412 0.3281 -0.0607 0.0043  0.0883  111 PRO A N   
821  C  CA  . PRO A 131 ? 0.3536 0.3793 0.3633 -0.0639 0.0113  0.0880  111 PRO A CA  
822  C  C   . PRO A 131 ? 0.2940 0.3145 0.3152 -0.0701 0.0074  0.1000  111 PRO A C   
823  O  O   . PRO A 131 ? 0.3501 0.3752 0.3801 -0.0725 0.0114  0.0994  111 PRO A O   
824  C  CB  . PRO A 131 ? 0.4156 0.4600 0.4108 -0.0670 0.0193  0.0890  111 PRO A CB  
825  C  CG  . PRO A 131 ? 0.5282 0.5721 0.5107 -0.0631 0.0171  0.0827  111 PRO A CG  
826  C  CD  . PRO A 131 ? 0.4292 0.4583 0.4170 -0.0618 0.0066  0.0881  111 PRO A CD  
827  N  N   . SER A 132 ? 0.3348 0.3457 0.3579 -0.0729 -0.0010 0.1111  112 SER A N   
828  C  CA  A SER A 132 ? 0.2918 0.2956 0.3273 -0.0795 -0.0061 0.1231  112 SER A CA  
829  C  CA  B SER A 132 ? 0.2907 0.2944 0.3261 -0.0795 -0.0061 0.1231  112 SER A CA  
830  C  C   . SER A 132 ? 0.3753 0.3603 0.4256 -0.0755 -0.0126 0.1166  112 SER A C   
831  O  O   . SER A 132 ? 0.3591 0.3364 0.4215 -0.0809 -0.0174 0.1240  112 SER A O   
832  C  CB  A SER A 132 ? 0.3287 0.3292 0.3608 -0.0844 -0.0131 0.1390  112 SER A CB  
833  C  CB  B SER A 132 ? 0.3285 0.3288 0.3608 -0.0844 -0.0133 0.1390  112 SER A CB  
834  O  OG  A SER A 132 ? 0.3456 0.3301 0.3808 -0.0781 -0.0219 0.1364  112 SER A OG  
835  O  OG  B SER A 132 ? 0.3130 0.3316 0.3295 -0.0888 -0.0078 0.1460  112 SER A OG  
836  N  N   . LEU A 133 ? 0.3001 0.2778 0.3497 -0.0666 -0.0131 0.1032  113 LEU A N   
837  C  CA  . LEU A 133 ? 0.3345 0.2949 0.3954 -0.0618 -0.0193 0.0965  113 LEU A CA  
838  C  C   . LEU A 133 ? 0.3396 0.3023 0.4066 -0.0616 -0.0155 0.0879  113 LEU A C   
839  O  O   . LEU A 133 ? 0.3563 0.3300 0.4180 -0.0586 -0.0082 0.0796  113 LEU A O   
840  C  CB  . LEU A 133 ? 0.3102 0.2638 0.3679 -0.0523 -0.0214 0.0873  113 LEU A CB  
841  C  CG  . LEU A 133 ? 0.3097 0.2600 0.3642 -0.0513 -0.0270 0.0951  113 LEU A CG  
842  C  CD1 . LEU A 133 ? 0.3983 0.3438 0.4530 -0.0416 -0.0284 0.0854  113 LEU A CD1 
843  C  CD2 . LEU A 133 ? 0.4189 0.3556 0.4835 -0.0552 -0.0359 0.1068  113 LEU A CD2 
844  N  N   . SER A 134 ? 0.3594 0.3109 0.4383 -0.0647 -0.0216 0.0899  114 SER A N   
845  C  CA  . SER A 134 ? 0.3411 0.2918 0.4270 -0.0640 -0.0209 0.0813  114 SER A CA  
846  C  C   . SER A 134 ? 0.3056 0.2430 0.3919 -0.0549 -0.0248 0.0684  114 SER A C   
847  O  O   . SER A 134 ? 0.3042 0.2417 0.3936 -0.0532 -0.0243 0.0601  114 SER A O   
848  C  CB  . SER A 134 ? 0.4270 0.3727 0.5258 -0.0730 -0.0265 0.0898  114 SER A CB  
849  O  OG  . SER A 134 ? 0.4299 0.3546 0.5355 -0.0724 -0.0370 0.0915  114 SER A OG  
850  N  N   . CYS A 135 ? 0.3181 0.2452 0.4017 -0.0490 -0.0287 0.0671  115 CYS A N   
851  C  CA  . CYS A 135 ? 0.3626 0.2782 0.4467 -0.0397 -0.0318 0.0555  115 CYS A CA  
852  C  C   . CYS A 135 ? 0.3845 0.2938 0.4669 -0.0340 -0.0348 0.0573  115 CYS A C   
853  O  O   . CYS A 135 ? 0.3712 0.2843 0.4517 -0.0379 -0.0353 0.0678  115 CYS A O   
854  C  CB  . CYS A 135 ? 0.3677 0.2680 0.4610 -0.0408 -0.0396 0.0519  115 CYS A CB  
855  S  SG  . CYS A 135 ? 0.4041 0.2896 0.5086 -0.0485 -0.0495 0.0651  115 CYS A SG  
856  N  N   . ALA A 136 ? 0.3550 0.2562 0.4382 -0.0246 -0.0365 0.0475  116 ALA A N   
857  C  CA  . ALA A 136 ? 0.4006 0.2963 0.4854 -0.0184 -0.0398 0.0490  116 ALA A CA  
858  C  C   . ALA A 136 ? 0.6039 0.4835 0.6982 -0.0206 -0.0492 0.0568  116 ALA A C   
859  O  O   . ALA A 136 ? 0.6553 0.5269 0.7554 -0.0272 -0.0536 0.0605  116 ALA A O   
860  C  CB  . ALA A 136 ? 0.4641 0.3570 0.5486 -0.0074 -0.0384 0.0364  116 ALA A CB  
861  N  N   . LYS A 137 ? 0.5883 0.4632 0.6861 -0.0150 -0.0529 0.0599  117 LYS A N   
862  C  CA  . LYS A 137 ? 0.6073 0.4651 0.7159 -0.0153 -0.0627 0.0670  117 LYS A CA  
863  C  C   . LYS A 137 ? 0.7941 0.6378 0.9100 -0.0034 -0.0666 0.0554  117 LYS A C   
864  O  O   . LYS A 137 ? 0.7775 0.6287 0.8906 0.0056  -0.0619 0.0475  117 LYS A O   
865  C  CB  . LYS A 137 ? 0.5291 0.3917 0.6377 -0.0181 -0.0654 0.0814  117 LYS A CB  
866  C  CG  . LYS A 137 ? 0.6955 0.5765 0.7929 -0.0275 -0.0594 0.0901  117 LYS A CG  
867  C  CD  . LYS A 137 ? 0.5505 0.4398 0.6436 -0.0277 -0.0610 0.1002  117 LYS A CD  
868  C  CE  . LYS A 137 ? 0.6436 0.5524 0.7225 -0.0350 -0.0538 0.1046  117 LYS A CE  
869  N  NZ  . LYS A 137 ? 0.6619 0.5789 0.7351 -0.0357 -0.0566 0.1142  117 LYS A NZ  
870  N  N   . PRO A 138 ? 0.8743 0.6981 1.0000 -0.0032 -0.0749 0.0538  118 PRO A N   
871  C  CA  . PRO A 138 ? 0.9784 0.7884 1.1098 0.0089  -0.0781 0.0398  118 PRO A CA  
872  C  C   . PRO A 138 ? 0.9255 0.7335 1.0640 0.0189  -0.0803 0.0416  118 PRO A C   
873  O  O   . PRO A 138 ? 0.8981 0.7117 1.0390 0.0157  -0.0821 0.0552  118 PRO A O   
874  C  CB  . PRO A 138 ? 0.8469 0.6350 0.9878 0.0046  -0.0880 0.0394  118 PRO A CB  
875  C  CG  . PRO A 138 ? 0.8905 0.6852 1.0285 -0.0097 -0.0872 0.0495  118 PRO A CG  
876  C  CD  . PRO A 138 ? 0.8703 0.6845 1.0017 -0.0145 -0.0810 0.0626  118 PRO A CD  
877  N  N   . THR A 139 ? 1.0115 0.8127 1.1535 0.0316  -0.0800 0.0273  119 THR A N   
878  C  CA  . THR A 139 ? 1.0770 0.8762 1.2285 0.0435  -0.0818 0.0262  119 THR A CA  
879  C  C   . THR A 139 ? 1.1657 0.9505 1.3211 0.0514  -0.0852 0.0130  119 THR A C   
880  O  O   . THR A 139 ? 1.1596 0.9348 1.3109 0.0481  -0.0871 0.0047  119 THR A O   
881  C  CB  . THR A 139 ? 1.0255 0.8462 1.1708 0.0509  -0.0716 0.0203  119 THR A CB  
882  O  OG1 . THR A 139 ? 1.0889 0.9275 1.2227 0.0408  -0.0654 0.0275  119 THR A OG1 
883  C  CG2 . THR A 139 ? 1.0634 0.8881 1.2203 0.0597  -0.0736 0.0254  119 THR A CG2 
884  N  N   . GLU A 140 ? 1.2283 1.0120 1.3922 0.0616  -0.0864 0.0113  120 GLU A N   
885  C  CA  . GLU A 140 ? 1.2747 1.0439 1.4433 0.0695  -0.0901 -0.0002 120 GLU A CA  
886  C  C   . GLU A 140 ? 1.3142 1.0813 1.4732 0.0753  -0.0854 -0.0191 120 GLU A C   
887  O  O   . GLU A 140 ? 1.2952 1.0478 1.4530 0.0739  -0.0903 -0.0273 120 GLU A O   
888  C  CB  . GLU A 140 ? 1.3633 1.1355 1.5422 0.0816  -0.0897 -0.0005 120 GLU A CB  
889  C  CG  . GLU A 140 ? 1.2333 0.9912 1.4167 0.0916  -0.0921 -0.0141 120 GLU A CG  
890  C  CD  . GLU A 140 ? 1.2964 1.0609 1.4889 0.1058  -0.0889 -0.0174 120 GLU A CD  
891  O  OE1 . GLU A 140 ? 1.4234 1.2015 1.6217 0.1063  -0.0875 -0.0060 120 GLU A OE1 
892  O  OE2 . GLU A 140 ? 1.2854 1.0423 1.4795 0.1165  -0.0877 -0.0313 120 GLU A OE2 
893  N  N   . GLU A 141 ? 1.2027 0.9852 1.3548 0.0814  -0.0764 -0.0258 121 GLU A N   
894  C  CA  . GLU A 141 ? 1.2186 1.0022 1.3596 0.0870  -0.0714 -0.0429 121 GLU A CA  
895  C  C   . GLU A 141 ? 1.0410 0.8265 1.1718 0.0766  -0.0708 -0.0427 121 GLU A C   
896  O  O   . GLU A 141 ? 0.9457 0.7294 1.0665 0.0788  -0.0692 -0.0561 121 GLU A O   
897  C  CB  . GLU A 141 ? 1.1291 0.9305 1.2684 0.0999  -0.0613 -0.0506 121 GLU A CB  
898  C  CG  . GLU A 141 ? 1.2783 1.0780 1.4259 0.1126  -0.0604 -0.0560 121 GLU A CG  
899  C  CD  . GLU A 141 ? 1.2808 1.1020 1.4333 0.1222  -0.0516 -0.0545 121 GLU A CD  
900  O  OE1 . GLU A 141 ? 1.2095 1.0434 1.3649 0.1169  -0.0500 -0.0431 121 GLU A OE1 
901  O  OE2 . GLU A 141 ? 1.3432 1.1694 1.4972 0.1347  -0.0462 -0.0646 121 GLU A OE2 
902  N  N   . PHE A 142 ? 0.9720 0.7616 1.1049 0.0655  -0.0721 -0.0278 122 PHE A N   
903  C  CA  . PHE A 142 ? 0.9107 0.7097 1.0324 0.0546  -0.0685 -0.0255 122 PHE A CA  
904  C  C   . PHE A 142 ? 0.8757 0.6626 1.0024 0.0410  -0.0768 -0.0145 122 PHE A C   
905  O  O   . PHE A 142 ? 0.8583 0.6533 0.9865 0.0321  -0.0762 0.0008  122 PHE A O   
906  C  CB  . PHE A 142 ? 0.7774 0.6012 0.8927 0.0521  -0.0588 -0.0175 122 PHE A CB  
907  C  CG  . PHE A 142 ? 0.6517 0.4886 0.7660 0.0644  -0.0512 -0.0247 122 PHE A CG  
908  C  CD1 . PHE A 142 ? 0.6483 0.4897 0.7541 0.0721  -0.0458 -0.0390 122 PHE A CD1 
909  C  CD2 . PHE A 142 ? 0.6308 0.4773 0.7529 0.0678  -0.0494 -0.0162 122 PHE A CD2 
910  C  CE1 . PHE A 142 ? 0.6487 0.5047 0.7543 0.0830  -0.0379 -0.0444 122 PHE A CE1 
911  C  CE2 . PHE A 142 ? 0.6944 0.5551 0.8179 0.0786  -0.0423 -0.0218 122 PHE A CE2 
912  C  CZ  . PHE A 142 ? 0.6323 0.4982 0.7478 0.0861  -0.0360 -0.0356 122 PHE A CZ  
913  N  N   . ASN A 143 ? 0.9628 0.7343 1.0902 0.0386  -0.0836 -0.0219 123 ASN A N   
914  C  CA  . ASN A 143 ? 0.9384 0.7037 1.0698 0.0244  -0.0899 -0.0115 123 ASN A CA  
915  C  C   . ASN A 143 ? 0.8869 0.6568 1.0110 0.0171  -0.0884 -0.0156 123 ASN A C   
916  O  O   . ASN A 143 ? 0.8815 0.6580 0.9952 0.0236  -0.0835 -0.0289 123 ASN A O   
917  C  CB  . ASN A 143 ? 0.9270 0.6754 1.0656 0.0243  -0.0989 -0.0147 123 ASN A CB  
918  C  CG  . ASN A 143 ? 0.9350 0.6752 1.0680 0.0344  -0.0998 -0.0347 123 ASN A CG  
919  O  OD1 . ASN A 143 ? 0.8905 0.6264 1.0186 0.0302  -0.1029 -0.0428 123 ASN A OD1 
920  N  ND2 . ASN A 143 ? 0.8337 0.5730 0.9675 0.0478  -0.0969 -0.0427 123 ASN A ND2 
921  N  N   . PRO A 144 ? 0.9390 0.7113 1.0665 0.0033  -0.0907 -0.0034 124 PRO A N   
922  C  CA  . PRO A 144 ? 0.8516 0.6357 0.9716 -0.0038 -0.0872 -0.0060 124 PRO A CA  
923  C  C   . PRO A 144 ? 0.9110 0.6819 1.0298 -0.0026 -0.0942 -0.0206 124 PRO A C   
924  O  O   . PRO A 144 ? 0.7743 0.5549 0.8877 -0.0082 -0.0925 -0.0231 124 PRO A O   
925  C  CB  . PRO A 144 ? 0.9813 0.7703 1.1087 -0.0184 -0.0888 0.0116  124 PRO A CB  
926  C  CG  . PRO A 144 ? 1.0329 0.8194 1.1662 -0.0180 -0.0896 0.0243  124 PRO A CG  
927  C  CD  . PRO A 144 ? 1.0062 0.7785 1.1422 -0.0063 -0.0941 0.0145  124 PRO A CD  
928  N  N   . ASP A 145 ? 0.7819 0.5385 0.9025 0.0046  -0.0998 -0.0300 125 ASP A N   
929  C  CA  . ASP A 145 ? 0.7698 0.5176 0.8859 0.0062  -0.1056 -0.0448 125 ASP A CA  
930  C  C   . ASP A 145 ? 0.6921 0.4424 0.7948 0.0196  -0.1008 -0.0626 125 ASP A C   
931  O  O   . ASP A 145 ? 0.7907 0.5399 0.8848 0.0199  -0.1034 -0.0745 125 ASP A O   
932  C  CB  . ASP A 145 ? 0.8692 0.6004 0.9943 0.0058  -0.1147 -0.0456 125 ASP A CB  
933  C  CG  . ASP A 145 ? 0.8981 0.6277 1.0358 -0.0083 -0.1204 -0.0287 125 ASP A CG  
934  O  OD1 . ASP A 145 ? 0.9679 0.7078 1.1061 -0.0189 -0.1192 -0.0212 125 ASP A OD1 
935  O  OD2 . ASP A 145 ? 0.8293 0.5487 0.9769 -0.0088 -0.1257 -0.0225 125 ASP A OD2 
936  N  N   . ASN A 146 ? 0.7192 0.4747 0.8198 0.0307  -0.0937 -0.0642 126 ASN A N   
937  C  CA  . ASN A 146 ? 0.6981 0.4611 0.7859 0.0433  -0.0870 -0.0792 126 ASN A CA  
938  C  C   . ASN A 146 ? 0.7488 0.5367 0.8284 0.0428  -0.0752 -0.0725 126 ASN A C   
939  O  O   . ASN A 146 ? 0.7233 0.5234 0.7905 0.0504  -0.0683 -0.0819 126 ASN A O   
940  C  CB  . ASN A 146 ? 0.7950 0.5543 0.8844 0.0567  -0.0845 -0.0861 126 ASN A CB  
941  C  CG  . ASN A 146 ? 0.8961 0.6596 0.9966 0.0583  -0.0813 -0.0728 126 ASN A CG  
942  O  OD1 . ASN A 146 ? 0.8785 0.6438 0.9859 0.0482  -0.0828 -0.0575 126 ASN A OD1 
943  N  ND2 . ASN A 146 ? 0.9680 0.7342 1.0700 0.0710  -0.0769 -0.0782 126 ASN A ND2 
944  N  N   . PHE A 147 ? 0.5905 0.3883 0.6758 0.0335  -0.0722 -0.0560 127 PHE A N   
945  C  CA  . PHE A 147 ? 0.4810 0.3024 0.5584 0.0307  -0.0618 -0.0494 127 PHE A CA  
946  C  C   . PHE A 147 ? 0.5465 0.3738 0.6267 0.0168  -0.0630 -0.0383 127 PHE A C   
947  O  O   . PHE A 147 ? 0.4749 0.3147 0.5567 0.0118  -0.0575 -0.0264 127 PHE A O   
948  C  CB  . PHE A 147 ? 0.5411 0.3734 0.6213 0.0355  -0.0547 -0.0417 127 PHE A CB  
949  C  CG  . PHE A 147 ? 0.5036 0.3389 0.5803 0.0494  -0.0500 -0.0520 127 PHE A CG  
950  C  CD1 . PHE A 147 ? 0.5361 0.3895 0.6023 0.0541  -0.0408 -0.0563 127 PHE A CD1 
951  C  CD2 . PHE A 147 ? 0.6330 0.4539 0.7182 0.0580  -0.0547 -0.0569 127 PHE A CD2 
952  C  CE1 . PHE A 147 ? 0.6445 0.5035 0.7083 0.0667  -0.0355 -0.0647 127 PHE A CE1 
953  C  CE2 . PHE A 147 ? 0.6360 0.4621 0.7192 0.0717  -0.0494 -0.0666 127 PHE A CE2 
954  C  CZ  . PHE A 147 ? 0.6272 0.4734 0.6995 0.0758  -0.0394 -0.0703 127 PHE A CZ  
955  N  N   . PRO A 148 ? 0.5467 0.3662 0.6276 0.0106  -0.0701 -0.0424 128 PRO A N   
956  C  CA  . PRO A 148 ? 0.5277 0.3550 0.6135 -0.0023 -0.0707 -0.0313 128 PRO A CA  
957  C  C   . PRO A 148 ? 0.4776 0.3272 0.5556 -0.0034 -0.0608 -0.0282 128 PRO A C   
958  O  O   . PRO A 148 ? 0.5755 0.4356 0.6579 -0.0119 -0.0579 -0.0173 128 PRO A O   
959  C  CB  . PRO A 148 ? 0.5968 0.4111 0.6855 -0.0073 -0.0812 -0.0386 128 PRO A CB  
960  C  CG  . PRO A 148 ? 0.5029 0.3115 0.5803 0.0040  -0.0823 -0.0558 128 PRO A CG  
961  C  CD  . PRO A 148 ? 0.5936 0.4003 0.6694 0.0152  -0.0770 -0.0580 128 PRO A CD  
962  N  N   . GLU A 149 ? 0.5108 0.3684 0.5776 0.0052  -0.0555 -0.0372 129 GLU A N   
963  C  CA  . GLU A 149 ? 0.4811 0.3582 0.5418 0.0043  -0.0471 -0.0340 129 GLU A CA  
964  C  C   . GLU A 149 ? 0.5734 0.4616 0.6354 0.0045  -0.0389 -0.0246 129 GLU A C   
965  O  O   . GLU A 149 ? 0.4809 0.3837 0.5405 0.0022  -0.0326 -0.0204 129 GLU A O   
966  C  CB  . GLU A 149 ? 0.5563 0.4388 0.6048 0.0129  -0.0443 -0.0448 129 GLU A CB  
967  C  CG  . GLU A 149 ? 0.6131 0.4980 0.6569 0.0234  -0.0383 -0.0486 129 GLU A CG  
968  C  CD  . GLU A 149 ? 0.6451 0.5134 0.6896 0.0307  -0.0439 -0.0583 129 GLU A CD  
969  O  OE1 . GLU A 149 ? 0.6198 0.4720 0.6701 0.0264  -0.0533 -0.0607 129 GLU A OE1 
970  O  OE2 . GLU A 149 ? 0.7716 0.6432 0.8122 0.0407  -0.0390 -0.0636 129 GLU A OE2 
971  N  N   . TYR A 150 ? 0.4539 0.3353 0.5200 0.0077  -0.0394 -0.0218 130 TYR A N   
972  C  CA  . TYR A 150 ? 0.4469 0.3381 0.5144 0.0069  -0.0334 -0.0127 130 TYR A CA  
973  C  C   . TYR A 150 ? 0.3645 0.2513 0.4397 -0.0013 -0.0368 -0.0015 130 TYR A C   
974  O  O   . TYR A 150 ? 0.4420 0.3399 0.5165 -0.0052 -0.0319 0.0067  130 TYR A O   
975  C  CB  . TYR A 150 ? 0.3724 0.2632 0.4389 0.0168  -0.0309 -0.0161 130 TYR A CB  
976  C  CG  . TYR A 150 ? 0.3729 0.2730 0.4315 0.0247  -0.0251 -0.0245 130 TYR A CG  
977  C  CD1 . TYR A 150 ? 0.3717 0.2877 0.4262 0.0239  -0.0177 -0.0211 130 TYR A CD1 
978  C  CD2 . TYR A 150 ? 0.5102 0.4031 0.5652 0.0330  -0.0273 -0.0357 130 TYR A CD2 
979  C  CE1 . TYR A 150 ? 0.3775 0.3026 0.4254 0.0303  -0.0125 -0.0267 130 TYR A CE1 
980  C  CE2 . TYR A 150 ? 0.5080 0.4115 0.5545 0.0400  -0.0213 -0.0422 130 TYR A CE2 
981  C  CZ  . TYR A 150 ? 0.4754 0.3953 0.5189 0.0382  -0.0140 -0.0367 130 TYR A CZ  
982  O  OH  . TYR A 150 ? 0.5614 0.4924 0.5972 0.0443  -0.0082 -0.0412 130 TYR A OH  
983  N  N   . LEU A 151 ? 0.3615 0.2327 0.4438 -0.0042 -0.0453 -0.0008 131 LEU A N   
984  C  CA  . LEU A 151 ? 0.4405 0.3056 0.5309 -0.0106 -0.0495 0.0110  131 LEU A CA  
985  C  C   . LEU A 151 ? 0.4302 0.2937 0.5270 -0.0222 -0.0536 0.0183  131 LEU A C   
986  O  O   . LEU A 151 ? 0.4537 0.3124 0.5576 -0.0287 -0.0574 0.0296  131 LEU A O   
987  C  CB  . LEU A 151 ? 0.5292 0.3760 0.6260 -0.0046 -0.0569 0.0086  131 LEU A CB  
988  C  CG  . LEU A 151 ? 0.5114 0.3593 0.6053 0.0077  -0.0536 0.0018  131 LEU A CG  
989  C  CD1 . LEU A 151 ? 0.5808 0.4108 0.6846 0.0125  -0.0616 0.0024  131 LEU A CD1 
990  C  CD2 . LEU A 151 ? 0.5290 0.3945 0.6185 0.0079  -0.0457 0.0085  131 LEU A CD2 
991  N  N   . SER A 152 ? 0.4158 0.2845 0.5113 -0.0252 -0.0531 0.0133  132 SER A N   
992  C  CA  . SER A 152 ? 0.4034 0.2721 0.5076 -0.0364 -0.0573 0.0204  132 SER A CA  
993  C  C   . SER A 152 ? 0.3297 0.2173 0.4340 -0.0434 -0.0494 0.0320  132 SER A C   
994  O  O   . SER A 152 ? 0.3363 0.2381 0.4327 -0.0397 -0.0408 0.0300  132 SER A O   
995  C  CB  . SER A 152 ? 0.4738 0.3422 0.5778 -0.0371 -0.0606 0.0110  132 SER A CB  
996  O  OG  . SER A 152 ? 0.5273 0.3781 0.6297 -0.0308 -0.0682 -0.0009 132 SER A OG  
997  N  N   . PRO A 153 ? 0.3450 0.2330 0.4584 -0.0536 -0.0522 0.0441  133 PRO A N   
998  C  CA  . PRO A 153 ? 0.3262 0.2337 0.4388 -0.0600 -0.0440 0.0546  133 PRO A CA  
999  C  C   . PRO A 153 ? 0.3214 0.2446 0.4333 -0.0604 -0.0380 0.0497  133 PRO A C   
1000 O  O   . PRO A 153 ? 0.3023 0.2216 0.4183 -0.0604 -0.0426 0.0427  133 PRO A O   
1001 C  CB  . PRO A 153 ? 0.4349 0.3388 0.5595 -0.0714 -0.0495 0.0682  133 PRO A CB  
1002 C  CG  . PRO A 153 ? 0.4499 0.3296 0.5798 -0.0694 -0.0605 0.0665  133 PRO A CG  
1003 C  CD  . PRO A 153 ? 0.3620 0.2321 0.4866 -0.0593 -0.0629 0.0493  133 PRO A CD  
1004 N  N   . ASN A 154 ? 0.2415 0.1825 0.3481 -0.0605 -0.0283 0.0533  134 ASN A N   
1005 C  CA  . ASN A 154 ? 0.2247 0.1813 0.3322 -0.0603 -0.0221 0.0496  134 ASN A CA  
1006 C  C   . ASN A 154 ? 0.2837 0.2475 0.4048 -0.0698 -0.0243 0.0565  134 ASN A C   
1007 O  O   . ASN A 154 ? 0.3044 0.2672 0.4325 -0.0780 -0.0269 0.0674  134 ASN A O   
1008 C  CB  . ASN A 154 ? 0.2433 0.2156 0.3428 -0.0580 -0.0116 0.0513  134 ASN A CB  
1009 C  CG  . ASN A 154 ? 0.2524 0.2211 0.3410 -0.0485 -0.0091 0.0427  134 ASN A CG  
1010 O  OD1 . ASN A 154 ? 0.2454 0.2058 0.3326 -0.0430 -0.0125 0.0344  134 ASN A OD1 
1011 N  ND2 . ASN A 154 ? 0.2501 0.2259 0.3308 -0.0471 -0.0032 0.0449  134 ASN A ND2 
1012 N  N   . LEU A 155 ? 0.2561 0.2277 0.3818 -0.0689 -0.0237 0.0509  135 LEU A N   
1013 C  CA  . LEU A 155 ? 0.3420 0.3233 0.4825 -0.0773 -0.0257 0.0565  135 LEU A CA  
1014 C  C   . LEU A 155 ? 0.3186 0.3221 0.4605 -0.0753 -0.0153 0.0567  135 LEU A C   
1015 O  O   . LEU A 155 ? 0.3123 0.3194 0.4521 -0.0690 -0.0140 0.0484  135 LEU A O   
1016 C  CB  . LEU A 155 ? 0.3191 0.2889 0.4652 -0.0777 -0.0365 0.0492  135 LEU A CB  
1017 C  CG  . LEU A 155 ? 0.4122 0.3897 0.5754 -0.0867 -0.0418 0.0537  135 LEU A CG  
1018 C  CD1 . LEU A 155 ? 0.5191 0.5027 0.6950 -0.0979 -0.0414 0.0683  135 LEU A CD1 
1019 C  CD2 . LEU A 155 ? 0.4620 0.4213 0.6266 -0.0869 -0.0550 0.0450  135 LEU A CD2 
1020 N  N   . TRP A 156 ? 0.2379 0.2565 0.3829 -0.0801 -0.0076 0.0662  136 TRP A N   
1021 C  CA  . TRP A 156 ? 0.2394 0.2792 0.3849 -0.0773 0.0035  0.0659  136 TRP A CA  
1022 C  C   . TRP A 156 ? 0.2554 0.3117 0.4193 -0.0833 0.0041  0.0710  136 TRP A C   
1023 O  O   . TRP A 156 ? 0.2830 0.3395 0.4588 -0.0929 -0.0010 0.0801  136 TRP A O   
1024 C  CB  . TRP A 156 ? 0.2633 0.3126 0.4006 -0.0787 0.0123  0.0726  136 TRP A CB  
1025 C  CG  . TRP A 156 ? 0.2555 0.2924 0.3760 -0.0727 0.0124  0.0680  136 TRP A CG  
1026 C  CD1 . TRP A 156 ? 0.3149 0.3395 0.4292 -0.0753 0.0077  0.0734  136 TRP A CD1 
1027 C  CD2 . TRP A 156 ? 0.2480 0.2842 0.3577 -0.0633 0.0168  0.0577  136 TRP A CD2 
1028 N  NE1 . TRP A 156 ? 0.2901 0.3077 0.3904 -0.0680 0.0091  0.0670  136 TRP A NE1 
1029 C  CE2 . TRP A 156 ? 0.2821 0.3065 0.3795 -0.0609 0.0146  0.0573  136 TRP A CE2 
1030 C  CE3 . TRP A 156 ? 0.2391 0.2834 0.3498 -0.0569 0.0218  0.0495  136 TRP A CE3 
1031 C  CZ2 . TRP A 156 ? 0.2661 0.2873 0.3525 -0.0531 0.0174  0.0491  136 TRP A CZ2 
1032 C  CZ3 . TRP A 156 ? 0.2532 0.2927 0.3527 -0.0492 0.0243  0.0416  136 TRP A CZ3 
1033 C  CH2 . TRP A 156 ? 0.2576 0.2861 0.3452 -0.0477 0.0222  0.0414  136 TRP A CH2 
1034 N  N   . PRO A 157 ? 0.1981 0.2687 0.3664 -0.0780 0.0101  0.0660  137 PRO A N   
1035 C  CA  . PRO A 157 ? 0.2620 0.3524 0.4496 -0.0830 0.0121  0.0716  137 PRO A CA  
1036 C  C   . PRO A 157 ? 0.2774 0.3855 0.4701 -0.0897 0.0208  0.0830  137 PRO A C   
1037 O  O   . PRO A 157 ? 0.2624 0.3715 0.4412 -0.0878 0.0278  0.0843  137 PRO A O   
1038 C  CB  . PRO A 157 ? 0.2805 0.3816 0.4692 -0.0735 0.0181  0.0633  137 PRO A CB  
1039 C  CG  . PRO A 157 ? 0.2522 0.3356 0.4229 -0.0649 0.0163  0.0533  137 PRO A CG  
1040 C  CD  . PRO A 157 ? 0.2026 0.2730 0.3598 -0.0672 0.0155  0.0559  137 PRO A CD  
1041 N  N   . GLN A 158 ? 0.2549 0.3780 0.4675 -0.0980 0.0199  0.0920  138 GLN A N   
1042 C  CA  . GLN A 158 ? 0.2580 0.4029 0.4774 -0.1045 0.0295  0.1039  138 GLN A CA  
1043 C  C   . GLN A 158 ? 0.2673 0.4301 0.4785 -0.0956 0.0442  0.0988  138 GLN A C   
1044 O  O   . GLN A 158 ? 0.3017 0.4696 0.5157 -0.0869 0.0472  0.0892  138 GLN A O   
1045 C  CB  . GLN A 158 ? 0.3431 0.5038 0.5856 -0.1120 0.0272  0.1115  138 GLN A CB  
1046 C  CG  . GLN A 158 ? 0.3251 0.4716 0.5710 -0.1216 0.0161  0.1191  138 GLN A CG  
1047 C  CD  . GLN A 158 ? 0.3008 0.4628 0.5651 -0.1269 0.0148  0.1248  138 GLN A CD  
1048 O  OE1 . GLN A 158 ? 0.3085 0.4740 0.5760 -0.1341 0.0146  0.1350  138 GLN A OE1 
1049 N  NE2 . GLN A 158 ? 0.3775 0.5497 0.6546 -0.1232 0.0138  0.1190  138 GLN A NE2 
1050 N  N   . GLU A 159 ? 0.3308 0.5033 0.5320 -0.0980 0.0531  0.1054  139 GLU A N   
1051 C  CA  . GLU A 159 ? 0.3586 0.5480 0.5505 -0.0897 0.0670  0.0994  139 GLU A CA  
1052 C  C   . GLU A 159 ? 0.4231 0.6393 0.6349 -0.0877 0.0754  0.0997  139 GLU A C   
1053 O  O   . GLU A 159 ? 0.4244 0.6484 0.6343 -0.0771 0.0829  0.0890  139 GLU A O   
1054 C  CB  . GLU A 159 ? 0.4243 0.6213 0.6012 -0.0939 0.0744  0.1075  139 GLU A CB  
1055 C  CG  . GLU A 159 ? 0.5112 0.7237 0.6746 -0.0850 0.0881  0.0993  139 GLU A CG  
1056 C  CD  . GLU A 159 ? 0.5410 0.7359 0.6904 -0.0735 0.0862  0.0829  139 GLU A CD  
1057 O  OE1 . GLU A 159 ? 0.6358 0.8062 0.7768 -0.0734 0.0758  0.0803  139 GLU A OE1 
1058 O  OE2 . GLU A 159 ? 0.5134 0.7192 0.6614 -0.0644 0.0951  0.0727  139 GLU A OE2 
1059 N  N   . SER A 160 ? 0.2670 0.4922 0.4946 -0.0957 0.0724  0.1087  140 SER A N   
1060 C  CA  . SER A 160 ? 0.3563 0.6034 0.6008 -0.0923 0.0786  0.1070  140 SER A CA  
1061 C  C   . SER A 160 ? 0.3458 0.5901 0.6053 -0.0867 0.0723  0.0994  140 SER A C   
1062 O  O   . SER A 160 ? 0.3314 0.5931 0.6024 -0.0798 0.0789  0.0946  140 SER A O   
1063 C  CB  . SER A 160 ? 0.3226 0.5784 0.5789 -0.1022 0.0761  0.1184  140 SER A CB  
1064 O  OG  . SER A 160 ? 0.3606 0.5972 0.6236 -0.1104 0.0606  0.1233  140 SER A OG  
1065 N  N   . THR A 161 ? 0.3276 0.5502 0.5869 -0.0892 0.0594  0.0980  141 THR A N   
1066 C  CA  . THR A 161 ? 0.2972 0.5146 0.5672 -0.0838 0.0517  0.0906  141 THR A CA  
1067 C  C   . THR A 161 ? 0.2987 0.5090 0.5545 -0.0700 0.0567  0.0770  141 THR A C   
1068 O  O   . THR A 161 ? 0.2850 0.5046 0.5525 -0.0625 0.0583  0.0718  141 THR A O   
1069 C  CB  . THR A 161 ? 0.3381 0.5302 0.6053 -0.0898 0.0352  0.0904  141 THR A CB  
1070 O  OG1 . THR A 161 ? 0.3418 0.5360 0.6200 -0.1017 0.0290  0.1010  141 THR A OG1 
1071 C  CG2 . THR A 161 ? 0.3188 0.5052 0.5927 -0.0841 0.0266  0.0824  141 THR A CG2 
1072 N  N   . LEU A 162 ? 0.2831 0.4766 0.5152 -0.0667 0.0582  0.0718  142 LEU A N   
1073 C  CA  . LEU A 162 ? 0.2283 0.4140 0.4468 -0.0549 0.0625  0.0597  142 LEU A CA  
1074 C  C   . LEU A 162 ? 0.2983 0.4872 0.4993 -0.0531 0.0729  0.0583  142 LEU A C   
1075 O  O   . LEU A 162 ? 0.2935 0.4642 0.4751 -0.0530 0.0698  0.0557  142 LEU A O   
1076 C  CB  . LEU A 162 ? 0.2507 0.4097 0.4569 -0.0521 0.0515  0.0532  142 LEU A CB  
1077 C  CG  . LEU A 162 ? 0.2953 0.4488 0.5124 -0.0502 0.0415  0.0506  142 LEU A CG  
1078 C  CD1 . LEU A 162 ? 0.2454 0.3742 0.4457 -0.0472 0.0331  0.0443  142 LEU A CD1 
1079 C  CD2 . LEU A 162 ? 0.3693 0.5372 0.5993 -0.0415 0.0468  0.0462  142 LEU A CD2 
1080 N  N   . PRO A 163 ? 0.2674 0.4803 0.4744 -0.0512 0.0854  0.0596  143 PRO A N   
1081 C  CA  . PRO A 163 ? 0.2961 0.5140 0.4845 -0.0502 0.0951  0.0585  143 PRO A CA  
1082 C  C   . PRO A 163 ? 0.2853 0.4860 0.4546 -0.0410 0.0952  0.0454  143 PRO A C   
1083 O  O   . PRO A 163 ? 0.2425 0.4401 0.4169 -0.0319 0.0955  0.0357  143 PRO A O   
1084 C  CB  . PRO A 163 ? 0.3288 0.5776 0.5298 -0.0475 0.1089  0.0597  143 PRO A CB  
1085 C  CG  . PRO A 163 ? 0.3478 0.6048 0.5739 -0.0436 0.1064  0.0580  143 PRO A CG  
1086 C  CD  . PRO A 163 ? 0.3192 0.5573 0.5508 -0.0501 0.0910  0.0627  143 PRO A CD  
1087 N  N   . GLY A 164 ? 0.2504 0.4398 0.3988 -0.0438 0.0941  0.0461  144 GLY A N   
1088 C  CA  . GLY A 164 ? 0.2299 0.4033 0.3600 -0.0369 0.0932  0.0352  144 GLY A CA  
1089 C  C   . GLY A 164 ? 0.2386 0.3873 0.3657 -0.0356 0.0816  0.0318  144 GLY A C   
1090 O  O   . GLY A 164 ? 0.2443 0.3798 0.3580 -0.0305 0.0803  0.0237  144 GLY A O   
1091 N  N   . PHE A 165 ? 0.2317 0.3742 0.3706 -0.0402 0.0730  0.0377  145 PHE A N   
1092 C  CA  . PHE A 165 ? 0.1935 0.3144 0.3286 -0.0382 0.0627  0.0339  145 PHE A CA  
1093 C  C   . PHE A 165 ? 0.2049 0.3099 0.3219 -0.0402 0.0587  0.0343  145 PHE A C   
1094 O  O   . PHE A 165 ? 0.1905 0.2825 0.2980 -0.0348 0.0563  0.0271  145 PHE A O   
1095 C  CB  . PHE A 165 ? 0.2130 0.3311 0.3623 -0.0434 0.0538  0.0396  145 PHE A CB  
1096 C  CG  . PHE A 165 ? 0.2231 0.3205 0.3668 -0.0413 0.0437  0.0355  145 PHE A CG  
1097 C  CD1 . PHE A 165 ? 0.3447 0.4380 0.4903 -0.0338 0.0421  0.0284  145 PHE A CD1 
1098 C  CD2 . PHE A 165 ? 0.2368 0.3196 0.3740 -0.0465 0.0358  0.0391  145 PHE A CD2 
1099 C  CE1 . PHE A 165 ? 0.2684 0.3453 0.4079 -0.0319 0.0339  0.0252  145 PHE A CE1 
1100 C  CE2 . PHE A 165 ? 0.1984 0.2640 0.3298 -0.0436 0.0277  0.0344  145 PHE A CE2 
1101 C  CZ  . PHE A 165 ? 0.2515 0.3153 0.3835 -0.0365 0.0271  0.0277  145 PHE A CZ  
1102 N  N   . LYS A 166 ? 0.2156 0.3216 0.3294 -0.0482 0.0573  0.0436  146 LYS A N   
1103 C  CA  . LYS A 166 ? 0.2185 0.3090 0.3181 -0.0502 0.0519  0.0454  146 LYS A CA  
1104 C  C   . LYS A 166 ? 0.2251 0.3157 0.3082 -0.0458 0.0570  0.0397  146 LYS A C   
1105 O  O   . LYS A 166 ? 0.2135 0.2893 0.2877 -0.0424 0.0522  0.0349  146 LYS A O   
1106 C  CB  . LYS A 166 ? 0.2472 0.3389 0.3492 -0.0600 0.0487  0.0582  146 LYS A CB  
1107 C  CG  . LYS A 166 ? 0.2636 0.3395 0.3532 -0.0620 0.0424  0.0615  146 LYS A CG  
1108 C  CD  . LYS A 166 ? 0.3061 0.3804 0.4020 -0.0718 0.0374  0.0749  146 LYS A CD  
1109 C  CE  . LYS A 166 ? 0.3733 0.4318 0.4586 -0.0729 0.0307  0.0786  146 LYS A CE  
1110 N  NZ  . LYS A 166 ? 0.4564 0.5235 0.5262 -0.0729 0.0365  0.0814  146 LYS A NZ  
1111 N  N   . PRO A 167 ? 0.2344 0.3415 0.3129 -0.0454 0.0665  0.0391  147 PRO A N   
1112 C  CA  . PRO A 167 ? 0.2456 0.3510 0.3072 -0.0410 0.0699  0.0316  147 PRO A CA  
1113 C  C   . PRO A 167 ? 0.2405 0.3373 0.3027 -0.0324 0.0694  0.0192  147 PRO A C   
1114 O  O   . PRO A 167 ? 0.2188 0.3052 0.2693 -0.0300 0.0666  0.0140  147 PRO A O   
1115 C  CB  . PRO A 167 ? 0.2554 0.3825 0.3131 -0.0419 0.0808  0.0328  147 PRO A CB  
1116 C  CG  . PRO A 167 ? 0.2579 0.3990 0.3346 -0.0442 0.0844  0.0383  147 PRO A CG  
1117 C  CD  . PRO A 167 ? 0.2434 0.3717 0.3301 -0.0498 0.0741  0.0462  147 PRO A CD  
1118 N  N   . THR A 168 ? 0.2220 0.3229 0.2986 -0.0281 0.0713  0.0151  148 THR A N   
1119 C  CA  . THR A 168 ? 0.1947 0.2860 0.2735 -0.0205 0.0697  0.0053  148 THR A CA  
1120 C  C   . THR A 168 ? 0.2285 0.3016 0.3047 -0.0209 0.0603  0.0062  148 THR A C   
1121 O  O   . THR A 168 ? 0.2011 0.2641 0.2704 -0.0172 0.0581  0.0003  148 THR A O   
1122 C  CB  . THR A 168 ? 0.1827 0.2824 0.2792 -0.0162 0.0723  0.0031  148 THR A CB  
1123 O  OG1 . THR A 168 ? 0.2113 0.3303 0.3119 -0.0152 0.0821  0.0023  148 THR A OG1 
1124 C  CG2 . THR A 168 ? 0.2583 0.3480 0.3576 -0.0084 0.0706  -0.0059 148 THR A CG2 
1125 N  N   . PHE A 169 ? 0.1689 0.2383 0.2513 -0.0252 0.0546  0.0132  149 PHE A N   
1126 C  CA  . PHE A 169 ? 0.2089 0.2624 0.2885 -0.0250 0.0463  0.0137  149 PHE A CA  
1127 C  C   . PHE A 169 ? 0.2001 0.2455 0.2660 -0.0262 0.0441  0.0141  149 PHE A C   
1128 O  O   . PHE A 169 ? 0.2058 0.2413 0.2674 -0.0226 0.0410  0.0101  149 PHE A O   
1129 C  CB  . PHE A 169 ? 0.1826 0.2343 0.2703 -0.0301 0.0407  0.0205  149 PHE A CB  
1130 C  CG  . PHE A 169 ? 0.1746 0.2119 0.2616 -0.0284 0.0327  0.0191  149 PHE A CG  
1131 C  CD1 . PHE A 169 ? 0.1887 0.2144 0.2663 -0.0287 0.0286  0.0197  149 PHE A CD1 
1132 C  CD2 . PHE A 169 ? 0.2208 0.2574 0.3163 -0.0263 0.0293  0.0172  149 PHE A CD2 
1133 C  CE1 . PHE A 169 ? 0.2149 0.2292 0.2916 -0.0262 0.0224  0.0176  149 PHE A CE1 
1134 C  CE2 . PHE A 169 ? 0.2113 0.2360 0.3038 -0.0244 0.0226  0.0152  149 PHE A CE2 
1135 C  CZ  . PHE A 169 ? 0.1850 0.1989 0.2681 -0.0240 0.0197  0.0150  149 PHE A CZ  
1136 N  N   . GLU A 170 ? 0.2295 0.2799 0.2893 -0.0314 0.0455  0.0202  150 GLU A N   
1137 C  CA  . GLU A 170 ? 0.2046 0.2486 0.2520 -0.0328 0.0427  0.0219  150 GLU A CA  
1138 C  C   . GLU A 170 ? 0.2318 0.2762 0.2704 -0.0285 0.0456  0.0135  150 GLU A C   
1139 O  O   . GLU A 170 ? 0.1978 0.2330 0.2308 -0.0270 0.0412  0.0116  150 GLU A O   
1140 C  CB  . GLU A 170 ? 0.2307 0.2824 0.2731 -0.0395 0.0440  0.0311  150 GLU A CB  
1141 C  CG  . GLU A 170 ? 0.2836 0.3305 0.3343 -0.0449 0.0386  0.0403  150 GLU A CG  
1142 C  CD  . GLU A 170 ? 0.4043 0.4603 0.4520 -0.0524 0.0403  0.0513  150 GLU A CD  
1143 O  OE1 . GLU A 170 ? 0.5082 0.5792 0.5498 -0.0531 0.0482  0.0512  150 GLU A OE1 
1144 O  OE2 . GLU A 170 ? 0.5140 0.5622 0.5655 -0.0573 0.0339  0.0601  150 GLU A OE2 
1145 N  N   . ASP A 171 ? 0.1871 0.2423 0.2254 -0.0264 0.0529  0.0082  151 ASP A N   
1146 C  CA  . ASP A 171 ? 0.2220 0.2764 0.2514 -0.0226 0.0550  -0.0008 151 ASP A CA  
1147 C  C   . ASP A 171 ? 0.2423 0.2854 0.2776 -0.0176 0.0513  -0.0071 151 ASP A C   
1148 O  O   . ASP A 171 ? 0.2104 0.2464 0.2391 -0.0166 0.0481  -0.0111 151 ASP A O   
1149 C  CB  . ASP A 171 ? 0.2363 0.3044 0.2649 -0.0203 0.0639  -0.0065 151 ASP A CB  
1150 C  CG  . ASP A 171 ? 0.3536 0.4347 0.3714 -0.0253 0.0683  -0.0010 151 ASP A CG  
1151 O  OD1 . ASP A 171 ? 0.4330 0.5107 0.4429 -0.0306 0.0634  0.0072  151 ASP A OD1 
1152 O  OD2 . ASP A 171 ? 0.4368 0.5322 0.4546 -0.0236 0.0768  -0.0043 151 ASP A OD2 
1153 N  N   . LEU A 172 ? 0.1928 0.2347 0.2410 -0.0149 0.0512  -0.0072 152 LEU A N   
1154 C  CA  . LEU A 172 ? 0.1852 0.2175 0.2388 -0.0106 0.0478  -0.0113 152 LEU A CA  
1155 C  C   . LEU A 172 ? 0.1915 0.2140 0.2420 -0.0122 0.0413  -0.0072 152 LEU A C   
1156 O  O   . LEU A 172 ? 0.1848 0.2006 0.2338 -0.0103 0.0387  -0.0101 152 LEU A O   
1157 C  CB  . LEU A 172 ? 0.1970 0.2314 0.2642 -0.0075 0.0487  -0.0113 152 LEU A CB  
1158 C  CG  . LEU A 172 ? 0.2119 0.2375 0.2847 -0.0032 0.0454  -0.0140 152 LEU A CG  
1159 C  CD1 . LEU A 172 ? 0.2182 0.2391 0.2873 -0.0008 0.0462  -0.0211 152 LEU A CD1 
1160 C  CD2 . LEU A 172 ? 0.2297 0.2593 0.3156 0.0002  0.0463  -0.0138 152 LEU A CD2 
1161 N  N   . CYS A 173 ? 0.1861 0.2078 0.2367 -0.0154 0.0384  -0.0005 153 CYS A N   
1162 C  CA  . CYS A 173 ? 0.1891 0.2019 0.2372 -0.0157 0.0327  0.0025  153 CYS A CA  
1163 C  C   . CYS A 173 ? 0.1861 0.1973 0.2251 -0.0170 0.0311  0.0023  153 CYS A C   
1164 O  O   . CYS A 173 ? 0.1973 0.2029 0.2361 -0.0154 0.0276  0.0018  153 CYS A O   
1165 C  CB  . CYS A 173 ? 0.2057 0.2164 0.2558 -0.0187 0.0294  0.0087  153 CYS A CB  
1166 S  SG  . CYS A 173 ? 0.2357 0.2459 0.2961 -0.0169 0.0281  0.0082  153 CYS A SG  
1167 N  N   . ARG A 174 ? 0.1835 0.2010 0.2149 -0.0203 0.0335  0.0033  154 ARG A N   
1168 C  CA  A ARG A 174 ? 0.2435 0.2603 0.2650 -0.0220 0.0309  0.0034  154 ARG A CA  
1169 C  CA  B ARG A 174 ? 0.2435 0.2605 0.2649 -0.0220 0.0310  0.0034  154 ARG A CA  
1170 C  C   . ARG A 174 ? 0.2389 0.2532 0.2597 -0.0192 0.0308  -0.0045 154 ARG A C   
1171 O  O   . ARG A 174 ? 0.2228 0.2329 0.2416 -0.0194 0.0260  -0.0042 154 ARG A O   
1172 C  CB  A ARG A 174 ? 0.2558 0.2818 0.2674 -0.0260 0.0340  0.0060  154 ARG A CB  
1173 C  CB  B ARG A 174 ? 0.2554 0.2817 0.2671 -0.0260 0.0344  0.0058  154 ARG A CB  
1174 C  CG  A ARG A 174 ? 0.3220 0.3483 0.3217 -0.0284 0.0302  0.0070  154 ARG A CG  
1175 C  CG  B ARG A 174 ? 0.3244 0.3521 0.3235 -0.0282 0.0315  0.0058  154 ARG A CG  
1176 C  CD  A ARG A 174 ? 0.3776 0.4138 0.3661 -0.0330 0.0328  0.0122  154 ARG A CD  
1177 C  CD  B ARG A 174 ? 0.3743 0.4125 0.3626 -0.0328 0.0346  0.0109  154 ARG A CD  
1178 N  NE  A ARG A 174 ? 0.3578 0.3945 0.3510 -0.0367 0.0317  0.0232  154 ARG A NE  
1179 N  NE  B ARG A 174 ? 0.3582 0.3955 0.3497 -0.0368 0.0318  0.0227  154 ARG A NE  
1180 C  CZ  A ARG A 174 ? 0.2915 0.3220 0.2850 -0.0390 0.0250  0.0318  154 ARG A CZ  
1181 C  CZ  B ARG A 174 ? 0.3838 0.4264 0.3808 -0.0393 0.0355  0.0282  154 ARG A CZ  
1182 N  NH1 A ARG A 174 ? 0.3074 0.3322 0.2980 -0.0377 0.0189  0.0312  154 ARG A NH1 
1183 N  NH1 B ARG A 174 ? 0.3570 0.4086 0.3575 -0.0379 0.0430  0.0234  154 ARG A NH1 
1184 N  NH2 A ARG A 174 ? 0.3264 0.3563 0.3250 -0.0428 0.0238  0.0414  154 ARG A NH2 
1185 N  NH2 B ARG A 174 ? 0.3582 0.3972 0.3591 -0.0434 0.0311  0.0390  154 ARG A NH2 
1186 N  N   . LEU A 175 ? 0.1934 0.2098 0.2179 -0.0164 0.0353  -0.0112 155 LEU A N   
1187 C  CA  . LEU A 175 ? 0.1954 0.2074 0.2213 -0.0139 0.0344  -0.0189 155 LEU A CA  
1188 C  C   . LEU A 175 ? 0.2249 0.2294 0.2595 -0.0123 0.0302  -0.0166 155 LEU A C   
1189 O  O   . LEU A 175 ? 0.2063 0.2068 0.2406 -0.0129 0.0262  -0.0180 155 LEU A O   
1190 C  CB  . LEU A 175 ? 0.2062 0.2212 0.2369 -0.0103 0.0401  -0.0259 155 LEU A CB  
1191 C  CG  . LEU A 175 ? 0.1973 0.2065 0.2312 -0.0072 0.0396  -0.0350 155 LEU A CG  
1192 C  CD1 . LEU A 175 ? 0.2609 0.2756 0.2963 -0.0034 0.0463  -0.0428 155 LEU A CD1 
1193 C  CD2 . LEU A 175 ? 0.2262 0.2278 0.2727 -0.0051 0.0365  -0.0325 155 LEU A CD2 
1194 N  N   . ILE A 176 ? 0.1652 0.1690 0.2076 -0.0105 0.0308  -0.0127 156 ILE A N   
1195 C  CA  . ILE A 176 ? 0.1784 0.1773 0.2279 -0.0085 0.0279  -0.0103 156 ILE A CA  
1196 C  C   . ILE A 176 ? 0.2248 0.2221 0.2713 -0.0100 0.0237  -0.0058 156 ILE A C   
1197 O  O   . ILE A 176 ? 0.1766 0.1718 0.2270 -0.0093 0.0213  -0.0052 156 ILE A O   
1198 C  CB  . ILE A 176 ? 0.1694 0.1688 0.2254 -0.0063 0.0291  -0.0077 156 ILE A CB  
1199 C  CG1 . ILE A 176 ? 0.1967 0.1979 0.2590 -0.0039 0.0324  -0.0117 156 ILE A CG1 
1200 C  CG2 . ILE A 176 ? 0.1950 0.1913 0.2550 -0.0043 0.0265  -0.0044 156 ILE A CG2 
1201 C  CD1 . ILE A 176 ? 0.2203 0.2239 0.2891 -0.0022 0.0329  -0.0088 156 ILE A CD1 
1202 N  N   . ILE A 177 ? 0.1796 0.1783 0.2206 -0.0120 0.0227  -0.0021 157 ILE A N   
1203 C  CA  . ILE A 177 ? 0.1961 0.1931 0.2361 -0.0125 0.0183  0.0023  157 ILE A CA  
1204 C  C   . ILE A 177 ? 0.2093 0.2076 0.2451 -0.0147 0.0154  0.0010  157 ILE A C   
1205 O  O   . ILE A 177 ? 0.1928 0.1906 0.2322 -0.0141 0.0118  0.0032  157 ILE A O   
1206 C  CB  . ILE A 177 ? 0.1644 0.1608 0.2013 -0.0141 0.0169  0.0074  157 ILE A CB  
1207 C  CG1 . ILE A 177 ? 0.1943 0.1882 0.2363 -0.0121 0.0180  0.0081  157 ILE A CG1 
1208 C  CG2 . ILE A 177 ? 0.1896 0.1839 0.2266 -0.0137 0.0118  0.0120  157 ILE A CG2 
1209 C  CD1 . ILE A 177 ? 0.2017 0.1946 0.2423 -0.0151 0.0167  0.0127  157 ILE A CD1 
1210 N  N   . ASP A 178 ? 0.1982 0.1991 0.2262 -0.0172 0.0168  -0.0029 158 ASP A N   
1211 C  CA  . ASP A 178 ? 0.2097 0.2113 0.2327 -0.0195 0.0131  -0.0059 158 ASP A CA  
1212 C  C   . ASP A 178 ? 0.2037 0.2020 0.2362 -0.0182 0.0111  -0.0086 158 ASP A C   
1213 O  O   . ASP A 178 ? 0.2266 0.2253 0.2615 -0.0197 0.0060  -0.0068 158 ASP A O   
1214 C  CB  . ASP A 178 ? 0.2645 0.2693 0.2774 -0.0211 0.0160  -0.0125 158 ASP A CB  
1215 C  CG  . ASP A 178 ? 0.3232 0.3341 0.3245 -0.0240 0.0170  -0.0083 158 ASP A CG  
1216 O  OD1 . ASP A 178 ? 0.3331 0.3441 0.3342 -0.0255 0.0138  0.0001  158 ASP A OD1 
1217 O  OD2 . ASP A 178 ? 0.3526 0.3684 0.3451 -0.0248 0.0212  -0.0132 158 ASP A OD2 
1218 N  N   . VAL A 179 ? 0.2009 0.1966 0.2400 -0.0157 0.0147  -0.0118 159 VAL A N   
1219 C  CA  . VAL A 179 ? 0.2009 0.1934 0.2500 -0.0152 0.0128  -0.0126 159 VAL A CA  
1220 C  C   . VAL A 179 ? 0.2119 0.2063 0.2685 -0.0139 0.0113  -0.0053 159 VAL A C   
1221 O  O   . VAL A 179 ? 0.2003 0.1957 0.2637 -0.0151 0.0079  -0.0033 159 VAL A O   
1222 C  CB  . VAL A 179 ? 0.1871 0.1761 0.2423 -0.0126 0.0164  -0.0164 159 VAL A CB  
1223 C  CG1 . VAL A 179 ? 0.2057 0.1911 0.2722 -0.0129 0.0139  -0.0152 159 VAL A CG1 
1224 C  CG2 . VAL A 179 ? 0.2265 0.2145 0.2751 -0.0127 0.0185  -0.0250 159 VAL A CG2 
1225 N  N   . ALA A 180 ? 0.1891 0.1847 0.2454 -0.0112 0.0138  -0.0016 160 ALA A N   
1226 C  CA  . ALA A 180 ? 0.1988 0.1966 0.2607 -0.0087 0.0131  0.0037  160 ALA A CA  
1227 C  C   . ALA A 180 ? 0.1823 0.1831 0.2447 -0.0100 0.0086  0.0067  160 ALA A C   
1228 O  O   . ALA A 180 ? 0.1732 0.1779 0.2438 -0.0086 0.0076  0.0102  160 ALA A O   
1229 C  CB  . ALA A 180 ? 0.1849 0.1818 0.2440 -0.0058 0.0152  0.0053  160 ALA A CB  
1230 N  N   . VAL A 181 ? 0.2006 0.2011 0.2549 -0.0126 0.0060  0.0063  161 VAL A N   
1231 C  CA  . VAL A 181 ? 0.2098 0.2136 0.2647 -0.0140 0.0006  0.0099  161 VAL A CA  
1232 C  C   . VAL A 181 ? 0.2041 0.2105 0.2651 -0.0168 -0.0029 0.0087  161 VAL A C   
1233 O  O   . VAL A 181 ? 0.1909 0.2022 0.2603 -0.0164 -0.0063 0.0130  161 VAL A O   
1234 C  CB  . VAL A 181 ? 0.1859 0.1894 0.2292 -0.0171 -0.0018 0.0106  161 VAL A CB  
1235 C  CG1 . VAL A 181 ? 0.2229 0.2304 0.2662 -0.0193 -0.0088 0.0144  161 VAL A CG1 
1236 C  CG2 . VAL A 181 ? 0.2070 0.2079 0.2478 -0.0151 0.0001  0.0142  161 VAL A CG2 
1237 N  N   . LEU A 182 ? 0.1952 0.1983 0.2536 -0.0194 -0.0023 0.0027  162 LEU A N   
1238 C  CA  . LEU A 182 ? 0.1834 0.1871 0.2491 -0.0227 -0.0067 0.0012  162 LEU A CA  
1239 C  C   . LEU A 182 ? 0.2110 0.2171 0.2915 -0.0211 -0.0049 0.0056  162 LEU A C   
1240 O  O   . LEU A 182 ? 0.1861 0.1965 0.2768 -0.0237 -0.0090 0.0087  162 LEU A O   
1241 C  CB  . LEU A 182 ? 0.2268 0.2245 0.2863 -0.0253 -0.0070 -0.0076 162 LEU A CB  
1242 C  CG  . LEU A 182 ? 0.2503 0.2487 0.2941 -0.0274 -0.0089 -0.0117 162 LEU A CG  
1243 C  CD1 . LEU A 182 ? 0.3278 0.3209 0.3648 -0.0284 -0.0077 -0.0220 162 LEU A CD1 
1244 C  CD2 . LEU A 182 ? 0.2665 0.2695 0.3090 -0.0312 -0.0170 -0.0088 162 LEU A CD2 
1245 N  N   . VAL A 183 ? 0.1652 0.1696 0.2471 -0.0174 0.0010  0.0064  163 VAL A N   
1246 C  CA  . VAL A 183 ? 0.1641 0.1729 0.2579 -0.0155 0.0034  0.0119  163 VAL A CA  
1247 C  C   . VAL A 183 ? 0.1695 0.1870 0.2684 -0.0129 0.0031  0.0178  163 VAL A C   
1248 O  O   . VAL A 183 ? 0.1687 0.1937 0.2794 -0.0134 0.0027  0.0229  163 VAL A O   
1249 C  CB  . VAL A 183 ? 0.1574 0.1634 0.2493 -0.0119 0.0090  0.0117  163 VAL A CB  
1250 C  CG1 . VAL A 183 ? 0.1868 0.1992 0.2881 -0.0098 0.0118  0.0182  163 VAL A CG1 
1251 C  CG2 . VAL A 183 ? 0.1751 0.1733 0.2655 -0.0136 0.0092  0.0062  163 VAL A CG2 
1252 N  N   . ALA A 184 ? 0.1886 0.2055 0.2800 -0.0098 0.0035  0.0175  164 ALA A N   
1253 C  CA  . ALA A 184 ? 0.1701 0.1937 0.2668 -0.0061 0.0028  0.0220  164 ALA A CA  
1254 C  C   . ALA A 184 ? 0.1887 0.2185 0.2930 -0.0095 -0.0033 0.0250  164 ALA A C   
1255 O  O   . ALA A 184 ? 0.1511 0.1903 0.2669 -0.0070 -0.0035 0.0298  164 ALA A O   
1256 C  CB  . ALA A 184 ? 0.1640 0.1827 0.2516 -0.0031 0.0026  0.0209  164 ALA A CB  
1257 N  N   . ARG A 185 ? 0.1700 0.1958 0.2680 -0.0149 -0.0085 0.0218  165 ARG A N   
1258 C  CA  . ARG A 185 ? 0.1786 0.2101 0.2831 -0.0191 -0.0159 0.0241  165 ARG A CA  
1259 C  C   . ARG A 185 ? 0.2248 0.2623 0.3446 -0.0218 -0.0163 0.0269  165 ARG A C   
1260 O  O   . ARG A 185 ? 0.1780 0.2257 0.3107 -0.0224 -0.0198 0.0323  165 ARG A O   
1261 C  CB  . ARG A 185 ? 0.2128 0.2383 0.3046 -0.0245 -0.0212 0.0186  165 ARG A CB  
1262 C  CG  . ARG A 185 ? 0.2006 0.2315 0.2974 -0.0299 -0.0304 0.0199  165 ARG A CG  
1263 C  CD  . ARG A 185 ? 0.2664 0.2915 0.3475 -0.0349 -0.0354 0.0128  165 ARG A CD  
1264 N  NE  . ARG A 185 ? 0.2823 0.3061 0.3486 -0.0331 -0.0347 0.0136  165 ARG A NE  
1265 C  CZ  . ARG A 185 ? 0.4189 0.4390 0.4680 -0.0360 -0.0359 0.0080  165 ARG A CZ  
1266 N  NH1 . ARG A 185 ? 0.3767 0.3928 0.4203 -0.0400 -0.0382 -0.0007 165 ARG A NH1 
1267 N  NH2 . ARG A 185 ? 0.3650 0.3853 0.4024 -0.0347 -0.0347 0.0111  165 ARG A NH2 
1268 N  N   . ALA A 186 ? 0.1764 0.2084 0.2967 -0.0235 -0.0131 0.0241  166 ALA A N   
1269 C  CA  . ALA A 186 ? 0.1718 0.2092 0.3080 -0.0266 -0.0134 0.0286  166 ALA A CA  
1270 C  C   . ALA A 186 ? 0.1976 0.2473 0.3447 -0.0216 -0.0077 0.0365  166 ALA A C   
1271 O  O   . ALA A 186 ? 0.1713 0.2325 0.3344 -0.0237 -0.0092 0.0430  166 ALA A O   
1272 C  CB  . ALA A 186 ? 0.1803 0.2081 0.3153 -0.0288 -0.0113 0.0251  166 ALA A CB  
1273 N  N   . CYS A 187 ? 0.1616 0.2101 0.3006 -0.0148 -0.0012 0.0357  167 CYS A N   
1274 C  CA  . CYS A 187 ? 0.1811 0.2414 0.3277 -0.0087 0.0046  0.0411  167 CYS A CA  
1275 C  C   . CYS A 187 ? 0.1856 0.2563 0.3415 -0.0067 0.0013  0.0446  167 CYS A C   
1276 O  O   . CYS A 187 ? 0.1803 0.2654 0.3505 -0.0045 0.0041  0.0507  167 CYS A O   
1277 C  CB  . CYS A 187 ? 0.1434 0.1984 0.2777 -0.0019 0.0102  0.0375  167 CYS A CB  
1278 S  SG  . CYS A 187 ? 0.2044 0.2515 0.3313 -0.0028 0.0147  0.0355  167 CYS A SG  
1279 N  N   . ASP A 188 ? 0.1690 0.2339 0.3177 -0.0071 -0.0045 0.0416  168 ASP A N   
1280 C  CA  . ASP A 188 ? 0.1927 0.2667 0.3507 -0.0053 -0.0092 0.0456  168 ASP A CA  
1281 C  C   . ASP A 188 ? 0.1685 0.2531 0.3426 -0.0116 -0.0145 0.0505  168 ASP A C   
1282 O  O   . ASP A 188 ? 0.1546 0.2536 0.3445 -0.0090 -0.0150 0.0565  168 ASP A O   
1283 C  CB  . ASP A 188 ? 0.1751 0.2402 0.3212 -0.0063 -0.0156 0.0427  168 ASP A CB  
1284 C  CG  . ASP A 188 ? 0.1983 0.2559 0.3342 0.0004  -0.0119 0.0404  168 ASP A CG  
1285 O  OD1 . ASP A 188 ? 0.2251 0.2867 0.3660 0.0077  -0.0059 0.0410  168 ASP A OD1 
1286 O  OD2 . ASP A 188 ? 0.2115 0.2595 0.3344 -0.0020 -0.0154 0.0379  168 ASP A OD2 
1287 N  N   . ARG A 189 ? 0.1737 0.2514 0.3449 -0.0199 -0.0193 0.0478  169 ARG A N   
1288 C  CA  . ARG A 189 ? 0.1566 0.2430 0.3441 -0.0270 -0.0257 0.0522  169 ARG A CA  
1289 C  C   . ARG A 189 ? 0.2115 0.3125 0.4177 -0.0256 -0.0195 0.0602  169 ARG A C   
1290 O  O   . ARG A 189 ? 0.1927 0.3096 0.4174 -0.0266 -0.0220 0.0673  169 ARG A O   
1291 C  CB  . ARG A 189 ? 0.2327 0.3067 0.4137 -0.0355 -0.0312 0.0463  169 ARG A CB  
1292 C  CG  . ARG A 189 ? 0.2991 0.3627 0.4631 -0.0381 -0.0384 0.0389  169 ARG A CG  
1293 C  CD  . ARG A 189 ? 0.4576 0.5087 0.6155 -0.0449 -0.0422 0.0312  169 ARG A CD  
1294 N  NE  . ARG A 189 ? 0.4679 0.5230 0.6440 -0.0520 -0.0474 0.0346  169 ARG A NE  
1295 C  CZ  . ARG A 189 ? 0.4192 0.4641 0.5976 -0.0568 -0.0486 0.0306  169 ARG A CZ  
1296 N  NH1 . ARG A 189 ? 0.3908 0.4219 0.5550 -0.0546 -0.0443 0.0228  169 ARG A NH1 
1297 N  NH2 . ARG A 189 ? 0.4780 0.5268 0.6752 -0.0641 -0.0546 0.0349  169 ARG A NH2 
1298 N  N   . PHE A 190 ? 0.1845 0.2820 0.3862 -0.0232 -0.0112 0.0600  170 PHE A N   
1299 C  CA  . PHE A 190 ? 0.1848 0.2975 0.4011 -0.0212 -0.0037 0.0683  170 PHE A CA  
1300 C  C   . PHE A 190 ? 0.1924 0.3211 0.4163 -0.0123 0.0012  0.0719  170 PHE A C   
1301 O  O   . PHE A 190 ? 0.1766 0.3238 0.4200 -0.0127 0.0023  0.0799  170 PHE A O   
1302 C  CB  . PHE A 190 ? 0.2036 0.3091 0.4096 -0.0190 0.0040  0.0670  170 PHE A CB  
1303 C  CG  . PHE A 190 ? 0.2380 0.3599 0.4554 -0.0166 0.0124  0.0760  170 PHE A CG  
1304 C  CD1 . PHE A 190 ? 0.2584 0.3859 0.4904 -0.0244 0.0116  0.0842  170 PHE A CD1 
1305 C  CD2 . PHE A 190 ? 0.2550 0.3864 0.4682 -0.0068 0.0211  0.0761  170 PHE A CD2 
1306 C  CE1 . PHE A 190 ? 0.3140 0.4586 0.5560 -0.0228 0.0198  0.0941  170 PHE A CE1 
1307 C  CE2 . PHE A 190 ? 0.3077 0.4563 0.5295 -0.0044 0.0296  0.0843  170 PHE A CE2 
1308 C  CZ  . PHE A 190 ? 0.3008 0.4569 0.5368 -0.0125 0.0293  0.0940  170 PHE A CZ  
1309 N  N   . ALA A 191 ? 0.1416 0.2634 0.3514 -0.0041 0.0043  0.0661  171 ALA A N   
1310 C  CA  . ALA A 191 ? 0.1633 0.2977 0.3797 0.0058  0.0092  0.0678  171 ALA A CA  
1311 C  C   . ALA A 191 ? 0.2067 0.3525 0.4395 0.0053  0.0022  0.0722  171 ALA A C   
1312 O  O   . ALA A 191 ? 0.1747 0.3388 0.4237 0.0112  0.0063  0.0773  171 ALA A O   
1313 C  CB  . ALA A 191 ? 0.1477 0.2688 0.3463 0.0136  0.0113  0.0600  171 ALA A CB  
1314 N  N   . GLU A 192 ? 0.1432 0.2797 0.3721 -0.0014 -0.0083 0.0703  172 GLU A N   
1315 C  CA  . GLU A 192 ? 0.1802 0.3269 0.4234 -0.0025 -0.0168 0.0748  172 GLU A CA  
1316 C  C   . GLU A 192 ? 0.1953 0.3607 0.4622 -0.0082 -0.0181 0.0832  172 GLU A C   
1317 O  O   . GLU A 192 ? 0.1921 0.3746 0.4779 -0.0054 -0.0205 0.0892  172 GLU A O   
1318 C  CB  . GLU A 192 ? 0.1996 0.3321 0.4299 -0.0094 -0.0281 0.0708  172 GLU A CB  
1319 C  CG  . GLU A 192 ? 0.1861 0.3041 0.3974 -0.0040 -0.0286 0.0654  172 GLU A CG  
1320 C  CD  . GLU A 192 ? 0.2946 0.3980 0.4880 -0.0118 -0.0367 0.0605  172 GLU A CD  
1321 O  OE1 . GLU A 192 ? 0.2943 0.3996 0.4913 -0.0205 -0.0444 0.0609  172 GLU A OE1 
1322 O  OE2 . GLU A 192 ? 0.2156 0.3060 0.3914 -0.0093 -0.0352 0.0560  172 GLU A OE2 
1323 N  N   . LYS A 193 ? 0.1543 0.3171 0.4221 -0.0162 -0.0170 0.0844  173 LYS A N   
1324 C  CA  . LYS A 193 ? 0.1905 0.3715 0.4827 -0.0225 -0.0179 0.0938  173 LYS A CA  
1325 C  C   . LYS A 193 ? 0.1623 0.3634 0.4676 -0.0155 -0.0052 0.1009  173 LYS A C   
1326 O  O   . LYS A 193 ? 0.1781 0.4008 0.5077 -0.0180 -0.0050 0.1104  173 LYS A O   
1327 C  CB  . LYS A 193 ? 0.2304 0.4004 0.5212 -0.0342 -0.0222 0.0934  173 LYS A CB  
1328 C  CG  . LYS A 193 ? 0.3361 0.4884 0.6152 -0.0419 -0.0348 0.0857  173 LYS A CG  
1329 C  CD  . LYS A 193 ? 0.5232 0.6635 0.8022 -0.0520 -0.0386 0.0840  173 LYS A CD  
1330 C  CE  . LYS A 193 ? 0.6197 0.7395 0.8805 -0.0572 -0.0485 0.0729  173 LYS A CE  
1331 N  NZ  . LYS A 193 ? 0.5570 0.6820 0.8216 -0.0609 -0.0604 0.0724  173 LYS A NZ  
1332 N  N   . GLN A 194 ? 0.1874 0.3832 0.4774 -0.0069 0.0052  0.0966  174 GLN A N   
1333 C  CA  . GLN A 194 ? 0.1684 0.3821 0.4662 -0.0015 0.0177  0.1025  174 GLN A CA  
1334 C  C   . GLN A 194 ? 0.2069 0.4322 0.5052 0.0128  0.0262  0.1001  174 GLN A C   
1335 O  O   . GLN A 194 ? 0.2372 0.4837 0.5467 0.0178  0.0363  0.1060  174 GLN A O   
1336 C  CB  . GLN A 194 ? 0.2002 0.4013 0.4806 -0.0030 0.0236  0.1001  174 GLN A CB  
1337 C  CG  . GLN A 194 ? 0.2793 0.4695 0.5616 -0.0160 0.0169  0.1029  174 GLN A CG  
1338 C  CD  . GLN A 194 ? 0.3477 0.5576 0.6548 -0.0235 0.0178  0.1160  174 GLN A CD  
1339 O  OE1 . GLN A 194 ? 0.3516 0.5802 0.6652 -0.0183 0.0271  0.1225  174 GLN A OE1 
1340 N  NE2 . GLN A 194 ? 0.2817 0.4839 0.5981 -0.0356 0.0075  0.1183  174 GLN A NE2 
1341 N  N   . ILE A 195 ? 0.1706 0.3831 0.4577 0.0196  0.0224  0.0919  175 ILE A N   
1342 C  CA  . ILE A 195 ? 0.1907 0.4080 0.4751 0.0339  0.0296  0.0871  175 ILE A CA  
1343 C  C   . ILE A 195 ? 0.1993 0.4234 0.4989 0.0385  0.0228  0.0884  175 ILE A C   
1344 O  O   . ILE A 195 ? 0.1950 0.4035 0.4877 0.0350  0.0122  0.0856  175 ILE A O   
1345 C  CB  . ILE A 195 ? 0.1687 0.3626 0.4266 0.0384  0.0310  0.0765  175 ILE A CB  
1346 C  CG1 . ILE A 195 ? 0.2003 0.3890 0.4445 0.0343  0.0372  0.0759  175 ILE A CG1 
1347 C  CG2 . ILE A 195 ? 0.2193 0.4153 0.4752 0.0529  0.0367  0.0703  175 ILE A CG2 
1348 C  CD1 . ILE A 195 ? 0.2256 0.3934 0.4456 0.0381  0.0384  0.0661  175 ILE A CD1 
1349 N  N   . ALA A 196 ? 0.1973 0.4454 0.5175 0.0467  0.0290  0.0931  176 ALA A N   
1350 C  CA  . ALA A 196 ? 0.1477 0.4012 0.4817 0.0521  0.0224  0.0941  176 ALA A CA  
1351 C  C   . ALA A 196 ? 0.2023 0.4398 0.5250 0.0633  0.0214  0.0855  176 ALA A C   
1352 O  O   . ALA A 196 ? 0.2311 0.4648 0.5428 0.0730  0.0307  0.0782  176 ALA A O   
1353 C  CB  . ALA A 196 ? 0.2010 0.4760 0.5489 0.0572  0.0293  0.0973  176 ALA A CB  
1354 N  N   . GLY A 197 ? 0.2210 0.4470 0.5438 0.0611  0.0091  0.0858  177 GLY A N   
1355 C  CA  . GLY A 197 ? 0.2126 0.4208 0.5247 0.0699  0.0060  0.0790  177 GLY A CA  
1356 C  C   . GLY A 197 ? 0.2128 0.3935 0.4965 0.0646  0.0034  0.0720  177 GLY A C   
1357 O  O   . GLY A 197 ? 0.2684 0.4327 0.5426 0.0704  0.0004  0.0671  177 GLY A O   
1358 N  N   . TYR A 198 ? 0.1719 0.3476 0.4436 0.0537  0.0043  0.0720  178 TYR A N   
1359 C  CA  . TYR A 198 ? 0.2157 0.3678 0.4623 0.0484  0.0023  0.0657  178 TYR A CA  
1360 C  C   . TYR A 198 ? 0.1632 0.3015 0.4033 0.0438  -0.0098 0.0666  178 TYR A C   
1361 O  O   . TYR A 198 ? 0.2031 0.3491 0.4539 0.0380  -0.0183 0.0727  178 TYR A O   
1362 C  CB  . TYR A 198 ? 0.2031 0.3548 0.4428 0.0378  0.0045  0.0667  178 TYR A CB  
1363 C  CG  . TYR A 198 ? 0.1481 0.2783 0.3638 0.0338  0.0046  0.0599  178 TYR A CG  
1364 C  CD1 . TYR A 198 ? 0.1758 0.3005 0.3798 0.0396  0.0132  0.0543  178 TYR A CD1 
1365 C  CD2 . TYR A 198 ? 0.1522 0.2693 0.3571 0.0244  -0.0038 0.0591  178 TYR A CD2 
1366 C  CE1 . TYR A 198 ? 0.2046 0.3110 0.3887 0.0359  0.0130  0.0486  178 TYR A CE1 
1367 C  CE2 . TYR A 198 ? 0.1879 0.2875 0.3726 0.0213  -0.0029 0.0531  178 TYR A CE2 
1368 C  CZ  . TYR A 198 ? 0.1884 0.2831 0.3640 0.0269  0.0053  0.0484  178 TYR A CZ  
1369 O  OH  . TYR A 198 ? 0.2194 0.2986 0.3775 0.0238  0.0059  0.0432  178 TYR A OH  
1370 N  N   . PRO A 199 ? 0.2161 0.3348 0.4390 0.0458  -0.0113 0.0613  179 PRO A N   
1371 C  CA  . PRO A 199 ? 0.2238 0.3305 0.4391 0.0409  -0.0222 0.0635  179 PRO A CA  
1372 C  C   . PRO A 199 ? 0.2144 0.3145 0.4155 0.0283  -0.0260 0.0629  179 PRO A C   
1373 O  O   . PRO A 199 ? 0.2457 0.3369 0.4327 0.0253  -0.0206 0.0576  179 PRO A O   
1374 C  CB  . PRO A 199 ? 0.2802 0.3692 0.4831 0.0472  -0.0207 0.0583  179 PRO A CB  
1375 C  CG  . PRO A 199 ? 0.3352 0.4272 0.5398 0.0563  -0.0098 0.0521  179 PRO A CG  
1376 C  CD  . PRO A 199 ? 0.2641 0.3718 0.4742 0.0524  -0.0034 0.0535  179 PRO A CD  
1377 N  N   . ALA A 200 ? 0.2372 0.3418 0.4420 0.0212  -0.0358 0.0678  180 ALA A N   
1378 C  CA  . ALA A 200 ? 0.2408 0.3390 0.4318 0.0098  -0.0401 0.0658  180 ALA A CA  
1379 C  C   . ALA A 200 ? 0.2322 0.3122 0.4001 0.0079  -0.0382 0.0601  180 ALA A C   
1380 O  O   . ALA A 200 ? 0.2425 0.3142 0.4037 0.0111  -0.0409 0.0613  180 ALA A O   
1381 C  CB  . ALA A 200 ? 0.3299 0.4335 0.5246 0.0036  -0.0526 0.0710  180 ALA A CB  
1382 N  N   . GLY A 201 ? 0.2304 0.3048 0.3879 0.0027  -0.0337 0.0548  181 GLY A N   
1383 C  CA  . GLY A 201 ? 0.1705 0.2302 0.3077 0.0000  -0.0320 0.0496  181 GLY A CA  
1384 C  C   . GLY A 201 ? 0.2253 0.2767 0.3573 0.0070  -0.0253 0.0470  181 GLY A C   
1385 O  O   . GLY A 201 ? 0.2255 0.2657 0.3430 0.0050  -0.0252 0.0446  181 GLY A O   
1386 N  N   . TYR A 202 ? 0.1873 0.2444 0.3306 0.0149  -0.0196 0.0471  182 TYR A N   
1387 C  CA  . TYR A 202 ? 0.2066 0.2551 0.3453 0.0222  -0.0150 0.0437  182 TYR A CA  
1388 C  C   . TYR A 202 ? 0.2076 0.2455 0.3311 0.0192  -0.0102 0.0381  182 TYR A C   
1389 O  O   . TYR A 202 ? 0.2203 0.2469 0.3342 0.0195  -0.0111 0.0364  182 TYR A O   
1390 C  CB  . TYR A 202 ? 0.2108 0.2691 0.3628 0.0314  -0.0090 0.0432  182 TYR A CB  
1391 C  CG  . TYR A 202 ? 0.2075 0.2559 0.3557 0.0397  -0.0064 0.0388  182 TYR A CG  
1392 C  CD1 . TYR A 202 ? 0.2205 0.2611 0.3711 0.0432  -0.0127 0.0409  182 TYR A CD1 
1393 C  CD2 . TYR A 202 ? 0.2083 0.2547 0.3507 0.0438  0.0013  0.0327  182 TYR A CD2 
1394 C  CE1 . TYR A 202 ? 0.2728 0.3022 0.4212 0.0505  -0.0115 0.0363  182 TYR A CE1 
1395 C  CE2 . TYR A 202 ? 0.2465 0.2825 0.3848 0.0512  0.0025  0.0273  182 TYR A CE2 
1396 C  CZ  . TYR A 202 ? 0.3225 0.3493 0.4645 0.0544  -0.0041 0.0288  182 TYR A CZ  
1397 O  OH  . TYR A 202 ? 0.2657 0.2803 0.4052 0.0613  -0.0041 0.0231  182 TYR A OH  
1398 N  N   . LEU A 203 ? 0.1615 0.2035 0.2845 0.0166  -0.0051 0.0358  183 LEU A N   
1399 C  CA  . LEU A 203 ? 0.1791 0.2124 0.2900 0.0150  -0.0006 0.0309  183 LEU A CA  
1400 C  C   . LEU A 203 ? 0.2036 0.2280 0.3024 0.0081  -0.0043 0.0296  183 LEU A C   
1401 O  O   . LEU A 203 ? 0.1959 0.2115 0.2851 0.0080  -0.0026 0.0267  183 LEU A O   
1402 C  CB  . LEU A 203 ? 0.1885 0.2281 0.3026 0.0136  0.0047  0.0303  183 LEU A CB  
1403 C  CG  . LEU A 203 ? 0.2426 0.2913 0.3642 0.0207  0.0111  0.0309  183 LEU A CG  
1404 C  CD1 . LEU A 203 ? 0.2089 0.2657 0.3357 0.0171  0.0147  0.0335  183 LEU A CD1 
1405 C  CD2 . LEU A 203 ? 0.2250 0.2661 0.3370 0.0262  0.0150  0.0257  183 LEU A CD2 
1406 N  N   . GLU A 204 ? 0.2160 0.2436 0.3150 0.0023  -0.0093 0.0314  184 GLU A N   
1407 C  CA  . GLU A 204 ? 0.1943 0.2154 0.2804 -0.0036 -0.0123 0.0297  184 GLU A CA  
1408 C  C   . GLU A 204 ? 0.2363 0.2512 0.3159 -0.0023 -0.0148 0.0323  184 GLU A C   
1409 O  O   . GLU A 204 ? 0.2199 0.2283 0.2890 -0.0045 -0.0130 0.0304  184 GLU A O   
1410 C  CB  . GLU A 204 ? 0.2232 0.2492 0.3097 -0.0095 -0.0187 0.0308  184 GLU A CB  
1411 C  CG  . GLU A 204 ? 0.2593 0.2800 0.3300 -0.0150 -0.0210 0.0280  184 GLU A CG  
1412 C  CD  . GLU A 204 ? 0.3155 0.3404 0.3838 -0.0208 -0.0281 0.0274  184 GLU A CD  
1413 O  OE1 . GLU A 204 ? 0.3155 0.3467 0.3960 -0.0217 -0.0313 0.0289  184 GLU A OE1 
1414 O  OE2 . GLU A 204 ? 0.3173 0.3399 0.3712 -0.0248 -0.0305 0.0256  184 GLU A OE2 
1415 N  N   . GLY A 205 ? 0.2117 0.2292 0.2992 0.0013  -0.0193 0.0374  185 GLY A N   
1416 C  CA  . GLY A 205 ? 0.2423 0.2528 0.3259 0.0023  -0.0228 0.0413  185 GLY A CA  
1417 C  C   . GLY A 205 ? 0.2691 0.2707 0.3509 0.0064  -0.0181 0.0381  185 GLY A C   
1418 O  O   . GLY A 205 ? 0.2591 0.2531 0.3332 0.0038  -0.0191 0.0395  185 GLY A O   
1419 N  N   . VAL A 206 ? 0.1971 0.2006 0.2861 0.0124  -0.0132 0.0341  186 VAL A N   
1420 C  CA  . VAL A 206 ? 0.1942 0.1895 0.2809 0.0165  -0.0097 0.0300  186 VAL A CA  
1421 C  C   . VAL A 206 ? 0.2321 0.2225 0.3077 0.0109  -0.0068 0.0270  186 VAL A C   
1422 O  O   . VAL A 206 ? 0.2457 0.2276 0.3168 0.0099  -0.0078 0.0270  186 VAL A O   
1423 C  CB  . VAL A 206 ? 0.2593 0.2601 0.3532 0.0238  -0.0044 0.0258  186 VAL A CB  
1424 C  CG1 . VAL A 206 ? 0.2766 0.2703 0.3643 0.0261  -0.0005 0.0200  186 VAL A CG1 
1425 C  CG2 . VAL A 206 ? 0.3211 0.3251 0.4271 0.0316  -0.0068 0.0277  186 VAL A CG2 
1426 N  N   . VAL A 207 ? 0.2098 0.2058 0.2825 0.0074  -0.0035 0.0248  187 VAL A N   
1427 C  CA  . VAL A 207 ? 0.1801 0.1729 0.2444 0.0032  -0.0003 0.0216  187 VAL A CA  
1428 C  C   . VAL A 207 ? 0.2165 0.2068 0.2728 -0.0026 -0.0030 0.0244  187 VAL A C   
1429 O  O   . VAL A 207 ? 0.2476 0.2337 0.2990 -0.0048 -0.0015 0.0239  187 VAL A O   
1430 C  CB  . VAL A 207 ? 0.1949 0.1934 0.2602 0.0016  0.0032  0.0187  187 VAL A CB  
1431 C  CG1 . VAL A 207 ? 0.2907 0.2864 0.3487 -0.0022 0.0061  0.0154  187 VAL A CG1 
1432 C  CG2 . VAL A 207 ? 0.2355 0.2377 0.3076 0.0068  0.0069  0.0174  187 VAL A CG2 
1433 N  N   . LYS A 208 ? 0.2038 0.1981 0.2587 -0.0055 -0.0071 0.0278  188 LYS A N   
1434 C  CA  . LYS A 208 ? 0.2247 0.2192 0.2694 -0.0114 -0.0092 0.0306  188 LYS A CA  
1435 C  C   . LYS A 208 ? 0.2674 0.2562 0.3109 -0.0120 -0.0123 0.0368  188 LYS A C   
1436 O  O   . LYS A 208 ? 0.2542 0.2431 0.2893 -0.0169 -0.0117 0.0394  188 LYS A O   
1437 C  CB  . LYS A 208 ? 0.2951 0.2958 0.3380 -0.0142 -0.0141 0.0325  188 LYS A CB  
1438 C  CG  . LYS A 208 ? 0.4140 0.4170 0.4439 -0.0202 -0.0166 0.0351  188 LYS A CG  
1439 C  CD  . LYS A 208 ? 0.3990 0.4076 0.4281 -0.0223 -0.0239 0.0382  188 LYS A CD  
1440 C  CE  . LYS A 208 ? 0.4735 0.4859 0.5070 -0.0226 -0.0238 0.0318  188 LYS A CE  
1441 N  NZ  . LYS A 208 ? 0.4332 0.4516 0.4655 -0.0259 -0.0319 0.0341  188 LYS A NZ  
1442 N  N   . THR A 209 ? 0.2219 0.2060 0.2745 -0.0070 -0.0155 0.0394  189 THR A N   
1443 C  CA  . THR A 209 ? 0.2208 0.1972 0.2748 -0.0073 -0.0198 0.0458  189 THR A CA  
1444 C  C   . THR A 209 ? 0.2363 0.2037 0.2944 -0.0041 -0.0178 0.0422  189 THR A C   
1445 O  O   . THR A 209 ? 0.2616 0.2202 0.3232 -0.0040 -0.0221 0.0466  189 THR A O   
1446 C  CB  . THR A 209 ? 0.3098 0.2852 0.3721 -0.0035 -0.0266 0.0517  189 THR A CB  
1447 O  OG1 . THR A 209 ? 0.2607 0.2366 0.3337 0.0045  -0.0251 0.0466  189 THR A OG1 
1448 C  CG2 . THR A 209 ? 0.3091 0.2933 0.3669 -0.0075 -0.0307 0.0563  189 THR A CG2 
1449 N  N   . SER A 210 ? 0.2236 0.1925 0.2818 -0.0018 -0.0123 0.0345  190 SER A N   
1450 C  CA  . SER A 210 ? 0.2293 0.1902 0.2905 0.0014  -0.0114 0.0303  190 SER A CA  
1451 C  C   . SER A 210 ? 0.2416 0.1980 0.2990 -0.0047 -0.0117 0.0327  190 SER A C   
1452 O  O   . SER A 210 ? 0.2497 0.2124 0.3013 -0.0098 -0.0080 0.0329  190 SER A O   
1453 C  CB  . SER A 210 ? 0.2142 0.1795 0.2754 0.0051  -0.0059 0.0227  190 SER A CB  
1454 O  OG  . SER A 210 ? 0.2287 0.1866 0.2905 0.0072  -0.0059 0.0184  190 SER A OG  
1455 N  N   . THR A 211 ? 0.2420 0.1876 0.3041 -0.0040 -0.0161 0.0342  191 THR A N   
1456 C  CA  . THR A 211 ? 0.2631 0.2043 0.3246 -0.0097 -0.0167 0.0361  191 THR A CA  
1457 C  C   . THR A 211 ? 0.2439 0.1795 0.3079 -0.0065 -0.0162 0.0279  191 THR A C   
1458 O  O   . THR A 211 ? 0.3137 0.2440 0.3797 -0.0109 -0.0184 0.0290  191 THR A O   
1459 C  CB  . THR A 211 ? 0.3054 0.2378 0.3711 -0.0135 -0.0235 0.0452  191 THR A CB  
1460 O  OG1 . THR A 211 ? 0.3369 0.2583 0.4100 -0.0065 -0.0289 0.0433  191 THR A OG1 
1461 C  CG2 . THR A 211 ? 0.3167 0.2570 0.3772 -0.0183 -0.0240 0.0546  191 THR A CG2 
1462 N  N   . THR A 212 ? 0.2423 0.1799 0.3060 0.0007  -0.0136 0.0203  192 THR A N   
1463 C  CA  . THR A 212 ? 0.2076 0.1418 0.2708 0.0042  -0.0129 0.0121  192 THR A CA  
1464 C  C   . THR A 212 ? 0.2133 0.1581 0.2721 0.0035  -0.0069 0.0089  192 THR A C   
1465 O  O   . THR A 212 ? 0.2690 0.2126 0.3264 0.0048  -0.0068 0.0036  192 THR A O   
1466 C  CB  . THR A 212 ? 0.2797 0.2097 0.3450 0.0136  -0.0138 0.0058  192 THR A CB  
1467 O  OG1 . THR A 212 ? 0.3239 0.2652 0.3885 0.0175  -0.0088 0.0057  192 THR A OG1 
1468 C  CG2 . THR A 212 ? 0.2657 0.1844 0.3376 0.0158  -0.0202 0.0087  192 THR A CG2 
1469 N  N   . THR A 213 ? 0.1919 0.1462 0.2486 0.0016  -0.0028 0.0118  193 THR A N   
1470 C  CA  . THR A 213 ? 0.1722 0.1350 0.2263 0.0007  0.0022  0.0093  193 THR A CA  
1471 C  C   . THR A 213 ? 0.2366 0.1989 0.2911 -0.0035 0.0020  0.0089  193 THR A C   
1472 O  O   . THR A 213 ? 0.2259 0.1857 0.2820 -0.0088 -0.0002 0.0131  193 THR A O   
1473 C  CB  . THR A 213 ? 0.1966 0.1669 0.2489 -0.0022 0.0051  0.0125  193 THR A CB  
1474 O  OG1 . THR A 213 ? 0.2043 0.1769 0.2580 0.0017  0.0050  0.0125  193 THR A OG1 
1475 C  CG2 . THR A 213 ? 0.1808 0.1579 0.2319 -0.0039 0.0097  0.0102  193 THR A CG2 
1476 N  N   . LYS A 214 ? 0.1989 0.1643 0.2527 -0.0014 0.0039  0.0047  194 LYS A N   
1477 C  CA  . LYS A 214 ? 0.2423 0.2078 0.2981 -0.0048 0.0026  0.0041  194 LYS A CA  
1478 C  C   . LYS A 214 ? 0.2239 0.1986 0.2804 -0.0051 0.0070  0.0035  194 LYS A C   
1479 O  O   . LYS A 214 ? 0.2103 0.1881 0.2651 -0.0010 0.0092  0.0014  194 LYS A O   
1480 C  CB  . LYS A 214 ? 0.2866 0.2452 0.3415 -0.0017 -0.0020 -0.0010 194 LYS A CB  
1481 C  CG  . LYS A 214 ? 0.3369 0.2958 0.3949 -0.0059 -0.0050 -0.0016 194 LYS A CG  
1482 C  CD  . LYS A 214 ? 0.3711 0.3185 0.4300 -0.0063 -0.0123 -0.0049 194 LYS A CD  
1483 C  CE  . LYS A 214 ? 0.4647 0.4045 0.5283 -0.0107 -0.0154 0.0003  194 LYS A CE  
1484 N  NZ  . LYS A 214 ? 0.3572 0.2826 0.4228 -0.0103 -0.0234 -0.0036 194 LYS A NZ  
1485 N  N   . ALA A 215 ? 0.1627 0.1422 0.2230 -0.0098 0.0082  0.0059  195 ALA A N   
1486 C  CA  . ALA A 215 ? 0.1719 0.1596 0.2351 -0.0093 0.0120  0.0051  195 ALA A CA  
1487 C  C   . ALA A 215 ? 0.1910 0.1799 0.2585 -0.0101 0.0088  0.0041  195 ALA A C   
1488 O  O   . ALA A 215 ? 0.2120 0.1975 0.2822 -0.0138 0.0046  0.0052  195 ALA A O   
1489 C  CB  . ALA A 215 ? 0.2089 0.2035 0.2741 -0.0128 0.0164  0.0075  195 ALA A CB  
1490 N  N   . ARG A 216 ? 0.1857 0.1792 0.2546 -0.0070 0.0100  0.0027  196 ARG A N   
1491 C  CA  . ARG A 216 ? 0.1825 0.1784 0.2549 -0.0072 0.0062  0.0020  196 ARG A CA  
1492 C  C   . ARG A 216 ? 0.1883 0.1935 0.2687 -0.0068 0.0095  0.0036  196 ARG A C   
1493 O  O   . ARG A 216 ? 0.1726 0.1797 0.2526 -0.0033 0.0130  0.0035  196 ARG A O   
1494 C  CB  . ARG A 216 ? 0.1916 0.1843 0.2569 -0.0026 0.0033  -0.0009 196 ARG A CB  
1495 C  CG  . ARG A 216 ? 0.2200 0.2158 0.2870 -0.0028 -0.0016 -0.0016 196 ARG A CG  
1496 C  CD  . ARG A 216 ? 0.3115 0.3069 0.3693 0.0022  -0.0030 -0.0037 196 ARG A CD  
1497 N  NE  . ARG A 216 ? 0.2917 0.2927 0.3505 0.0052  0.0018  -0.0003 196 ARG A NE  
1498 C  CZ  . ARG A 216 ? 0.2597 0.2625 0.3116 0.0092  0.0027  0.0004  196 ARG A CZ  
1499 N  NH1 . ARG A 216 ? 0.3029 0.3034 0.3445 0.0117  0.0002  -0.0033 196 ARG A NH1 
1500 N  NH2 . ARG A 216 ? 0.2806 0.2879 0.3362 0.0106  0.0063  0.0049  196 ARG A NH2 
1501 N  N   . LEU A 217 ? 0.1638 0.1749 0.2529 -0.0103 0.0082  0.0054  197 LEU A N   
1502 C  CA  . LEU A 217 ? 0.1900 0.2110 0.2892 -0.0091 0.0109  0.0068  197 LEU A CA  
1503 C  C   . LEU A 217 ? 0.2226 0.2461 0.3257 -0.0088 0.0044  0.0073  197 LEU A C   
1504 O  O   . LEU A 217 ? 0.2207 0.2431 0.3254 -0.0130 -0.0010 0.0075  197 LEU A O   
1505 C  CB  . LEU A 217 ? 0.1863 0.2155 0.2939 -0.0131 0.0150  0.0090  197 LEU A CB  
1506 C  CG  . LEU A 217 ? 0.2643 0.3051 0.3831 -0.0111 0.0202  0.0094  197 LEU A CG  
1507 C  CD1 . LEU A 217 ? 0.1636 0.2024 0.2789 -0.0060 0.0256  0.0061  197 LEU A CD1 
1508 C  CD2 . LEU A 217 ? 0.1833 0.2336 0.3087 -0.0160 0.0242  0.0122  197 LEU A CD2 
1509 N  N   . LEU A 218 ? 0.1546 0.1804 0.2585 -0.0044 0.0041  0.0078  198 LEU A N   
1510 C  CA  . LEU A 218 ? 0.1504 0.1793 0.2560 -0.0038 -0.0027 0.0090  198 LEU A CA  
1511 C  C   . LEU A 218 ? 0.1624 0.2022 0.2834 -0.0028 -0.0024 0.0123  198 LEU A C   
1512 O  O   . LEU A 218 ? 0.1850 0.2279 0.3126 0.0003  0.0035  0.0129  198 LEU A O   
1513 C  CB  . LEU A 218 ? 0.1995 0.2245 0.2943 0.0005  -0.0044 0.0089  198 LEU A CB  
1514 C  CG  . LEU A 218 ? 0.3141 0.3305 0.3942 0.0010  -0.0058 0.0053  198 LEU A CG  
1515 C  CD1 . LEU A 218 ? 0.2668 0.2838 0.3374 0.0053  -0.0069 0.0064  198 LEU A CD1 
1516 C  CD2 . LEU A 218 ? 0.2754 0.2884 0.3536 -0.0029 -0.0124 0.0020  198 LEU A CD2 
1517 N  N   . HIS A 219 ? 0.1889 0.2343 0.3163 -0.0054 -0.0093 0.0138  199 HIS A N   
1518 C  CA  . HIS A 219 ? 0.1655 0.2228 0.3094 -0.0041 -0.0107 0.0176  199 HIS A CA  
1519 C  C   . HIS A 219 ? 0.2160 0.2747 0.3568 -0.0032 -0.0200 0.0196  199 HIS A C   
1520 O  O   . HIS A 219 ? 0.2329 0.2909 0.3703 -0.0075 -0.0277 0.0182  199 HIS A O   
1521 C  CB  . HIS A 219 ? 0.1530 0.2196 0.3110 -0.0093 -0.0105 0.0190  199 HIS A CB  
1522 C  CG  . HIS A 219 ? 0.1533 0.2340 0.3303 -0.0078 -0.0124 0.0230  199 HIS A CG  
1523 N  ND1 . HIS A 219 ? 0.1439 0.2312 0.3320 -0.0017 -0.0060 0.0240  199 HIS A ND1 
1524 C  CD2 . HIS A 219 ? 0.1727 0.2623 0.3607 -0.0111 -0.0206 0.0260  199 HIS A CD2 
1525 C  CE1 . HIS A 219 ? 0.1446 0.2450 0.3507 -0.0009 -0.0096 0.0280  199 HIS A CE1 
1526 N  NE2 . HIS A 219 ? 0.1627 0.2654 0.3692 -0.0069 -0.0187 0.0296  199 HIS A NE2 
1527 N  N   . TYR A 220 ? 0.1791 0.2394 0.3207 0.0020  -0.0200 0.0229  200 TYR A N   
1528 C  CA  . TYR A 220 ? 0.1948 0.2591 0.3344 0.0031  -0.0289 0.0265  200 TYR A CA  
1529 C  C   . TYR A 220 ? 0.2119 0.2890 0.3723 0.0030  -0.0326 0.0309  200 TYR A C   
1530 O  O   . TYR A 220 ? 0.2332 0.3155 0.4086 0.0070  -0.0274 0.0335  200 TYR A O   
1531 C  CB  . TYR A 220 ? 0.2114 0.2722 0.3432 0.0082  -0.0274 0.0302  200 TYR A CB  
1532 C  CG  . TYR A 220 ? 0.2572 0.3083 0.3689 0.0081  -0.0250 0.0265  200 TYR A CG  
1533 C  CD1 . TYR A 220 ? 0.3397 0.3895 0.4354 0.0073  -0.0313 0.0250  200 TYR A CD1 
1534 C  CD2 . TYR A 220 ? 0.2502 0.2945 0.3591 0.0089  -0.0166 0.0238  200 TYR A CD2 
1535 C  CE1 . TYR A 220 ? 0.3017 0.3442 0.3801 0.0083  -0.0283 0.0211  200 TYR A CE1 
1536 C  CE2 . TYR A 220 ? 0.3142 0.3513 0.4070 0.0092  -0.0144 0.0208  200 TYR A CE2 
1537 C  CZ  . TYR A 220 ? 0.2764 0.3130 0.3546 0.0092  -0.0198 0.0195  200 TYR A CZ  
1538 O  OH  . TYR A 220 ? 0.3739 0.4050 0.4375 0.0105  -0.0169 0.0161  200 TYR A OH  
1539 N  N   . PHE A 221 ? 0.1859 0.2679 0.3479 -0.0016 -0.0419 0.0311  201 PHE A N   
1540 C  CA  . PHE A 221 ? 0.1827 0.2787 0.3659 -0.0027 -0.0467 0.0355  201 PHE A CA  
1541 C  C   . PHE A 221 ? 0.2076 0.3100 0.3972 0.0027  -0.0514 0.0422  201 PHE A C   
1542 O  O   . PHE A 221 ? 0.3160 0.4131 0.4895 0.0045  -0.0558 0.0438  201 PHE A O   
1543 C  CB  . PHE A 221 ? 0.2405 0.3390 0.4231 -0.0101 -0.0572 0.0337  201 PHE A CB  
1544 C  CG  . PHE A 221 ? 0.2316 0.3266 0.4161 -0.0163 -0.0537 0.0297  201 PHE A CG  
1545 C  CD1 . PHE A 221 ? 0.1718 0.2790 0.3782 -0.0196 -0.0507 0.0328  201 PHE A CD1 
1546 C  CD2 . PHE A 221 ? 0.2292 0.3095 0.3944 -0.0186 -0.0532 0.0236  201 PHE A CD2 
1547 C  CE1 . PHE A 221 ? 0.2201 0.3249 0.4284 -0.0261 -0.0476 0.0310  201 PHE A CE1 
1548 C  CE2 . PHE A 221 ? 0.2470 0.3232 0.4148 -0.0245 -0.0508 0.0213  201 PHE A CE2 
1549 C  CZ  . PHE A 221 ? 0.1910 0.2793 0.3799 -0.0287 -0.0481 0.0256  201 PHE A CZ  
1550 N  N   . PRO A 222 ? 0.2175 0.3319 0.4307 0.0057  -0.0505 0.0469  202 PRO A N   
1551 C  CA  . PRO A 222 ? 0.2619 0.3823 0.4838 0.0111  -0.0562 0.0545  202 PRO A CA  
1552 C  C   . PRO A 222 ? 0.3988 0.5231 0.6120 0.0077  -0.0702 0.0579  202 PRO A C   
1553 O  O   . PRO A 222 ? 0.2946 0.4215 0.5049 0.0011  -0.0767 0.0546  202 PRO A O   
1554 C  CB  . PRO A 222 ? 0.3129 0.4475 0.5646 0.0142  -0.0532 0.0573  202 PRO A CB  
1555 C  CG  . PRO A 222 ? 0.3027 0.4359 0.5570 0.0125  -0.0416 0.0507  202 PRO A CG  
1556 C  CD  . PRO A 222 ? 0.2491 0.3732 0.4827 0.0048  -0.0436 0.0457  202 PRO A CD  
1557 N  N   . GLU A 223 ? 0.3915 0.5161 0.6005 0.0120  -0.0753 0.0649  203 GLU A N   
1558 C  CA  . GLU A 223 ? 0.5415 0.6698 0.7377 0.0095  -0.0884 0.0686  203 GLU A CA  
1559 C  C   . GLU A 223 ? 0.6995 0.8393 0.9127 0.0137  -0.0964 0.0798  203 GLU A C   
1560 O  O   . GLU A 223 ? 0.7074 0.8589 0.9471 0.0148  -0.0981 0.0827  203 GLU A O   
1561 C  CB  . GLU A 223 ? 0.7465 0.8634 0.9128 0.0099  -0.0872 0.0668  203 GLU A CB  
1562 C  CG  . GLU A 223 ? 0.7669 0.8757 0.9323 0.0153  -0.0765 0.0697  203 GLU A CG  
1563 C  CD  . GLU A 223 ? 0.8610 0.9591 0.9995 0.0147  -0.0720 0.0658  203 GLU A CD  
1564 O  OE1 . GLU A 223 ? 0.9865 1.0822 1.1071 0.0108  -0.0755 0.0588  203 GLU A OE1 
1565 O  OE2 . GLU A 223 ? 0.7310 0.8234 0.8677 0.0183  -0.0650 0.0695  203 GLU A OE2 
1566 N  N   . CYS A 246 ? 0.7577 0.8619 0.7118 0.0289  -0.0133 0.0760  226 CYS A N   
1567 C  CA  . CYS A 246 ? 0.6689 0.7641 0.6204 0.0304  -0.0105 0.0594  226 CYS A CA  
1568 C  C   . CYS A 246 ? 0.7132 0.8133 0.6557 0.0336  -0.0004 0.0563  226 CYS A C   
1569 O  O   . CYS A 246 ? 0.6080 0.7165 0.5533 0.0333  0.0059  0.0680  226 CYS A O   
1570 C  CB  . CYS A 246 ? 0.6654 0.7473 0.6394 0.0278  -0.0106 0.0561  226 CYS A CB  
1571 S  SG  . CYS A 246 ? 0.6860 0.7560 0.6591 0.0287  -0.0090 0.0379  226 CYS A SG  
1572 N  N   . ALA A 247 ? 0.5342 0.6292 0.4675 0.0366  0.0009  0.0411  227 ALA A N   
1573 C  CA  . ALA A 247 ? 0.5998 0.6995 0.5265 0.0408  0.0104  0.0367  227 ALA A CA  
1574 C  C   . ALA A 247 ? 0.3801 0.4704 0.3261 0.0393  0.0154  0.0357  227 ALA A C   
1575 O  O   . ALA A 247 ? 0.3972 0.4751 0.3566 0.0362  0.0114  0.0324  227 ALA A O   
1576 C  CB  . ALA A 247 ? 0.4813 0.5793 0.3891 0.0458  0.0090  0.0203  227 ALA A CB  
1577 N  N   . THR A 248 ? 0.4320 0.5300 0.3793 0.0415  0.0244  0.0390  228 THR A N   
1578 C  CA  . THR A 248 ? 0.3276 0.4181 0.2921 0.0400  0.0285  0.0381  228 THR A CA  
1579 C  C   . THR A 248 ? 0.3447 0.4266 0.3058 0.0438  0.0289  0.0228  228 THR A C   
1580 O  O   . THR A 248 ? 0.3624 0.4455 0.3077 0.0486  0.0279  0.0129  228 THR A O   
1581 C  CB  . THR A 248 ? 0.2876 0.3903 0.2584 0.0400  0.0370  0.0487  228 THR A CB  
1582 O  OG1 . THR A 248 ? 0.3966 0.5130 0.3516 0.0459  0.0431  0.0455  228 THR A OG1 
1583 C  CG2 . THR A 248 ? 0.4367 0.5455 0.4143 0.0353  0.0359  0.0652  228 THR A CG2 
1584 N  N   . HIS A 249 ? 0.2678 0.3402 0.2439 0.0417  0.0299  0.0212  229 HIS A N   
1585 C  CA  . HIS A 249 ? 0.2905 0.3550 0.2670 0.0449  0.0308  0.0098  229 HIS A CA  
1586 C  C   . HIS A 249 ? 0.2798 0.3447 0.2714 0.0435  0.0359  0.0145  229 HIS A C   
1587 O  O   . HIS A 249 ? 0.2308 0.2990 0.2332 0.0391  0.0373  0.0249  229 HIS A O   
1588 C  CB  . HIS A 249 ? 0.2676 0.3168 0.2463 0.0424  0.0231  0.0015  229 HIS A CB  
1589 C  CG  . HIS A 249 ? 0.2537 0.2959 0.2478 0.0362  0.0210  0.0071  229 HIS A CG  
1590 N  ND1 . HIS A 249 ? 0.2503 0.2935 0.2482 0.0324  0.0172  0.0137  229 HIS A ND1 
1591 C  CD2 . HIS A 249 ? 0.2369 0.2720 0.2432 0.0337  0.0221  0.0068  229 HIS A CD2 
1592 C  CE1 . HIS A 249 ? 0.2492 0.2859 0.2611 0.0284  0.0168  0.0161  229 HIS A CE1 
1593 N  NE2 . HIS A 249 ? 0.2327 0.2645 0.2488 0.0288  0.0196  0.0119  229 HIS A NE2 
1594 N  N   . LEU A 250 ? 0.2408 0.3016 0.2339 0.0472  0.0376  0.0065  230 LEU A N   
1595 C  CA  . LEU A 250 ? 0.2317 0.2900 0.2392 0.0455  0.0400  0.0088  230 LEU A CA  
1596 C  C   . LEU A 250 ? 0.2271 0.2694 0.2389 0.0432  0.0343  0.0019  230 LEU A C   
1597 O  O   . LEU A 250 ? 0.2865 0.3211 0.2906 0.0458  0.0306  -0.0072 230 LEU A O   
1598 C  CB  . LEU A 250 ? 0.2341 0.3017 0.2419 0.0519  0.0463  0.0065  230 LEU A CB  
1599 C  CG  . LEU A 250 ? 0.2423 0.3290 0.2458 0.0549  0.0535  0.0134  230 LEU A CG  
1600 C  CD1 . LEU A 250 ? 0.2870 0.3833 0.2906 0.0631  0.0600  0.0083  230 LEU A CD1 
1601 C  CD2 . LEU A 250 ? 0.2789 0.3721 0.2956 0.0482  0.0554  0.0272  230 LEU A CD2 
1602 N  N   . ASP A 251 ? 0.2121 0.2497 0.2361 0.0381  0.0335  0.0061  231 ASP A N   
1603 C  CA  . ASP A 251 ? 0.2040 0.2291 0.2319 0.0362  0.0295  0.0008  231 ASP A CA  
1604 C  C   . ASP A 251 ? 0.2367 0.2610 0.2658 0.0413  0.0310  -0.0040 231 ASP A C   
1605 O  O   . ASP A 251 ? 0.2182 0.2527 0.2505 0.0448  0.0360  -0.0012 231 ASP A O   
1606 C  CB  . ASP A 251 ? 0.1857 0.2072 0.2241 0.0300  0.0286  0.0058  231 ASP A CB  
1607 C  CG  . ASP A 251 ? 0.2342 0.2536 0.2732 0.0258  0.0261  0.0085  231 ASP A CG  
1608 O  OD1 . ASP A 251 ? 0.2263 0.2497 0.2589 0.0273  0.0254  0.0093  231 ASP A OD1 
1609 O  OD2 . ASP A 251 ? 0.2323 0.2469 0.2782 0.0216  0.0248  0.0096  231 ASP A OD2 
1610 N  N   . HIS A 252 ? 0.2388 0.2512 0.2671 0.0415  0.0264  -0.0104 232 HIS A N   
1611 C  CA  A HIS A 252 ? 0.2332 0.2422 0.2624 0.0474  0.0263  -0.0160 232 HIS A CA  
1612 C  CA  B HIS A 252 ? 0.2323 0.2415 0.2615 0.0475  0.0264  -0.0159 232 HIS A CA  
1613 C  C   . HIS A 252 ? 0.2081 0.2156 0.2485 0.0458  0.0262  -0.0121 232 HIS A C   
1614 O  O   . HIS A 252 ? 0.2371 0.2478 0.2819 0.0515  0.0281  -0.0136 232 HIS A O   
1615 C  CB  A HIS A 252 ? 0.2976 0.2925 0.3217 0.0482  0.0200  -0.0243 232 HIS A CB  
1616 C  CB  B HIS A 252 ? 0.2975 0.2931 0.3209 0.0486  0.0203  -0.0245 232 HIS A CB  
1617 C  CG  A HIS A 252 ? 0.3458 0.3409 0.3576 0.0511  0.0186  -0.0308 232 HIS A CG  
1618 C  CG  B HIS A 252 ? 0.3187 0.3102 0.3410 0.0568  0.0201  -0.0324 232 HIS A CG  
1619 N  ND1 A HIS A 252 ? 0.4149 0.4090 0.4224 0.0459  0.0152  -0.0294 232 HIS A ND1 
1620 N  ND1 B HIS A 252 ? 0.4477 0.4267 0.4766 0.0570  0.0154  -0.0348 232 HIS A ND1 
1621 C  CD2 A HIS A 252 ? 0.4359 0.4326 0.4386 0.0589  0.0196  -0.0392 232 HIS A CD2 
1622 C  CD2 B HIS A 252 ? 0.3455 0.3438 0.3612 0.0654  0.0240  -0.0386 232 HIS A CD2 
1623 C  CE1 A HIS A 252 ? 0.4140 0.4090 0.4096 0.0497  0.0135  -0.0361 232 HIS A CE1 
1624 C  CE1 B HIS A 252 ? 0.4023 0.3792 0.4300 0.0660  0.0159  -0.0425 232 HIS A CE1 
1625 N  NE2 A HIS A 252 ? 0.4015 0.3980 0.3930 0.0577  0.0164  -0.0426 232 HIS A NE2 
1626 N  NE2 B HIS A 252 ? 0.3634 0.3524 0.3828 0.0715  0.0216  -0.0457 232 HIS A NE2 
1627 N  N   . GLY A 253 ? 0.2285 0.2318 0.2735 0.0385  0.0238  -0.0075 233 GLY A N   
1628 C  CA  . GLY A 253 ? 0.2118 0.2119 0.2647 0.0362  0.0219  -0.0046 233 GLY A CA  
1629 C  C   . GLY A 253 ? 0.1781 0.1878 0.2388 0.0342  0.0247  0.0018  233 GLY A C   
1630 O  O   . GLY A 253 ? 0.2086 0.2293 0.2719 0.0376  0.0291  0.0038  233 GLY A O   
1631 N  N   . CYS A 254 ? 0.2059 0.2123 0.2704 0.0284  0.0221  0.0050  234 CYS A N   
1632 C  CA  . CYS A 254 ? 0.1596 0.1739 0.2320 0.0258  0.0231  0.0101  234 CYS A CA  
1633 C  C   . CYS A 254 ? 0.1811 0.1975 0.2535 0.0207  0.0246  0.0126  234 CYS A C   
1634 O  O   . CYS A 254 ? 0.2018 0.2266 0.2778 0.0213  0.0278  0.0160  234 CYS A O   
1635 C  CB  . CYS A 254 ? 0.1970 0.2070 0.2725 0.0226  0.0186  0.0117  234 CYS A CB  
1636 S  SG  . CYS A 254 ? 0.2648 0.2733 0.3447 0.0294  0.0163  0.0108  234 CYS A SG  
1637 N  N   . LEU A 255 ? 0.1580 0.1672 0.2271 0.0159  0.0223  0.0113  235 LEU A N   
1638 C  CA  . LEU A 255 ? 0.1429 0.1524 0.2134 0.0118  0.0231  0.0127  235 LEU A CA  
1639 C  C   . LEU A 255 ? 0.1607 0.1642 0.2257 0.0106  0.0226  0.0097  235 LEU A C   
1640 O  O   . LEU A 255 ? 0.2021 0.2005 0.2640 0.0089  0.0206  0.0076  235 LEU A O   
1641 C  CB  . LEU A 255 ? 0.1384 0.1472 0.2129 0.0070  0.0210  0.0136  235 LEU A CB  
1642 C  CG  . LEU A 255 ? 0.1694 0.1853 0.2522 0.0068  0.0205  0.0174  235 LEU A CG  
1643 C  CD1 . LEU A 255 ? 0.2157 0.2294 0.2995 0.0021  0.0163  0.0168  235 LEU A CD1 
1644 C  CD2 . LEU A 255 ? 0.1763 0.1982 0.2661 0.0060  0.0229  0.0216  235 LEU A CD2 
1645 N  N   . THR A 256 ? 0.1476 0.1530 0.2126 0.0112  0.0241  0.0106  236 THR A N   
1646 C  CA  . THR A 256 ? 0.1813 0.1830 0.2436 0.0101  0.0234  0.0085  236 THR A CA  
1647 C  C   . THR A 256 ? 0.1885 0.1892 0.2558 0.0070  0.0238  0.0089  236 THR A C   
1648 O  O   . THR A 256 ? 0.1852 0.1882 0.2574 0.0070  0.0247  0.0120  236 THR A O   
1649 C  CB  . THR A 256 ? 0.1688 0.1734 0.2280 0.0132  0.0238  0.0092  236 THR A CB  
1650 O  OG1 . THR A 256 ? 0.2099 0.2152 0.2639 0.0170  0.0236  0.0071  236 THR A OG1 
1651 C  CG2 . THR A 256 ? 0.1919 0.1936 0.2500 0.0118  0.0218  0.0072  236 THR A CG2 
1652 N  N   . GLY A 257 ? 0.1766 0.1741 0.2428 0.0045  0.0233  0.0060  237 GLY A N   
1653 C  CA  . GLY A 257 ? 0.1596 0.1560 0.2298 0.0027  0.0242  0.0044  237 GLY A CA  
1654 C  C   . GLY A 257 ? 0.2106 0.2079 0.2836 0.0040  0.0247  0.0043  237 GLY A C   
1655 O  O   . GLY A 257 ? 0.2087 0.2068 0.2790 0.0044  0.0240  0.0040  237 GLY A O   
1656 N  N   . LEU A 258 ? 0.1619 0.1587 0.2416 0.0046  0.0252  0.0049  238 LEU A N   
1657 C  CA  . LEU A 258 ? 0.1876 0.1859 0.2723 0.0065  0.0250  0.0063  238 LEU A CA  
1658 C  C   . LEU A 258 ? 0.2188 0.2151 0.3109 0.0070  0.0262  0.0031  238 LEU A C   
1659 O  O   . LEU A 258 ? 0.2029 0.1952 0.2980 0.0063  0.0263  0.0015  238 LEU A O   
1660 C  CB  . LEU A 258 ? 0.2462 0.2461 0.3332 0.0082  0.0238  0.0123  238 LEU A CB  
1661 C  CG  . LEU A 258 ? 0.2893 0.2926 0.3691 0.0090  0.0235  0.0153  238 LEU A CG  
1662 C  CD1 . LEU A 258 ? 0.3431 0.3495 0.4264 0.0099  0.0235  0.0222  238 LEU A CD1 
1663 C  CD2 . LEU A 258 ? 0.2700 0.2750 0.3435 0.0103  0.0220  0.0136  238 LEU A CD2 
1664 N  N   . THR A 259 ? 0.1988 0.1980 0.2947 0.0083  0.0269  0.0017  239 THR A N   
1665 C  CA  . THR A 259 ? 0.1986 0.1971 0.3046 0.0108  0.0281  -0.0008 239 THR A CA  
1666 C  C   . THR A 259 ? 0.1966 0.1953 0.3109 0.0134  0.0253  0.0051  239 THR A C   
1667 O  O   . THR A 259 ? 0.2109 0.2128 0.3216 0.0133  0.0230  0.0102  239 THR A O   
1668 C  CB  . THR A 259 ? 0.2780 0.2823 0.3862 0.0114  0.0309  -0.0048 239 THR A CB  
1669 O  OG1 . THR A 259 ? 0.2746 0.2844 0.3831 0.0109  0.0291  -0.0009 239 THR A OG1 
1670 C  CG2 . THR A 259 ? 0.3450 0.3503 0.4444 0.0085  0.0338  -0.0093 239 THR A CG2 
1671 N  N   . SER A 260 ? 0.1784 0.1734 0.3035 0.0160  0.0252  0.0041  240 SER A N   
1672 C  CA  . SER A 260 ? 0.1838 0.1801 0.3185 0.0189  0.0222  0.0104  240 SER A CA  
1673 C  C   . SER A 260 ? 0.1997 0.2044 0.3370 0.0204  0.0221  0.0102  240 SER A C   
1674 O  O   . SER A 260 ? 0.1979 0.2065 0.3347 0.0202  0.0255  0.0044  240 SER A O   
1675 C  CB  . SER A 260 ? 0.2823 0.2715 0.4305 0.0221  0.0215  0.0092  240 SER A CB  
1676 O  OG  . SER A 260 ? 0.2982 0.2891 0.4528 0.0254  0.0247  0.0010  240 SER A OG  
1677 N  N   . ALA A 261 ? 0.1798 0.1883 0.3202 0.0216  0.0180  0.0173  241 ALA A N   
1678 C  CA  . ALA A 261 ? 0.1706 0.1878 0.3142 0.0221  0.0165  0.0178  241 ALA A CA  
1679 C  C   . ALA A 261 ? 0.1670 0.1875 0.3266 0.0262  0.0183  0.0149  241 ALA A C   
1680 O  O   . ALA A 261 ? 0.1862 0.2011 0.3558 0.0299  0.0186  0.0145  241 ALA A O   
1681 C  CB  . ALA A 261 ? 0.2180 0.2389 0.3596 0.0222  0.0106  0.0259  241 ALA A CB  
1682 N  N   . MET A 262 ? 0.1565 0.1862 0.3198 0.0258  0.0194  0.0128  242 MET A N   
1683 C  CA  . MET A 262 ? 0.1597 0.1966 0.3400 0.0303  0.0214  0.0109  242 MET A CA  
1684 C  C   . MET A 262 ? 0.1842 0.2291 0.3739 0.0314  0.0150  0.0181  242 MET A C   
1685 O  O   . MET A 262 ? 0.1963 0.2466 0.3796 0.0272  0.0115  0.0207  242 MET A O   
1686 C  CB  . MET A 262 ? 0.1623 0.2072 0.3424 0.0287  0.0275  0.0047  242 MET A CB  
1687 C  CG  . MET A 262 ? 0.2337 0.2914 0.4324 0.0327  0.0292  0.0046  242 MET A CG  
1688 S  SD  . MET A 262 ? 0.2290 0.2986 0.4247 0.0284  0.0363  0.0004  242 MET A SD  
1689 C  CE  . MET A 262 ? 0.4096 0.4742 0.6015 0.0325  0.0450  -0.0096 242 MET A CE  
1690 N  N   . PHE A 263 ? 0.1744 0.2195 0.3797 0.0370  0.0127  0.0214  243 PHE A N   
1691 C  CA  . PHE A 263 ? 0.1548 0.2098 0.3727 0.0389  0.0066  0.0281  243 PHE A CA  
1692 C  C   . PHE A 263 ? 0.1661 0.2319 0.4030 0.0434  0.0110  0.0240  243 PHE A C   
1693 O  O   . PHE A 263 ? 0.1993 0.2615 0.4452 0.0488  0.0165  0.0181  243 PHE A O   
1694 C  CB  . PHE A 263 ? 0.1616 0.2109 0.3856 0.0423  0.0003  0.0366  243 PHE A CB  
1695 C  CG  . PHE A 263 ? 0.1871 0.2301 0.3930 0.0380  -0.0037 0.0423  243 PHE A CG  
1696 C  CD1 . PHE A 263 ? 0.2072 0.2569 0.4041 0.0347  -0.0101 0.0479  243 PHE A CD1 
1697 C  CD2 . PHE A 263 ? 0.2102 0.2416 0.4081 0.0371  -0.0009 0.0415  243 PHE A CD2 
1698 C  CE1 . PHE A 263 ? 0.1764 0.2222 0.3556 0.0314  -0.0127 0.0522  243 PHE A CE1 
1699 C  CE2 . PHE A 263 ? 0.2552 0.2835 0.4374 0.0333  -0.0034 0.0471  243 PHE A CE2 
1700 C  CZ  . PHE A 263 ? 0.2665 0.3024 0.4388 0.0310  -0.0088 0.0522  243 PHE A CZ  
1701 N  N   . VAL A 264 ? 0.1754 0.2550 0.4191 0.0412  0.0085  0.0265  244 VAL A N   
1702 C  CA  . VAL A 264 ? 0.1688 0.2623 0.4320 0.0451  0.0135  0.0234  244 VAL A CA  
1703 C  C   . VAL A 264 ? 0.1539 0.2608 0.4342 0.0461  0.0058  0.0312  244 VAL A C   
1704 O  O   . VAL A 264 ? 0.1843 0.2937 0.4567 0.0402  -0.0020 0.0365  244 VAL A O   
1705 C  CB  . VAL A 264 ? 0.2178 0.3184 0.4742 0.0400  0.0210  0.0177  244 VAL A CB  
1706 C  CG1 . VAL A 264 ? 0.2426 0.3433 0.4846 0.0310  0.0155  0.0213  244 VAL A CG1 
1707 C  CG2 . VAL A 264 ? 0.2091 0.3282 0.4867 0.0436  0.0265  0.0161  244 VAL A CG2 
1708 N  N   . ASP A 265 ? 0.1786 0.2937 0.4824 0.0541  0.0072  0.0316  245 ASP A N   
1709 C  CA  . ASP A 265 ? 0.1566 0.2876 0.4804 0.0554  0.0003  0.0389  245 ASP A CA  
1710 C  C   . ASP A 265 ? 0.2144 0.3632 0.5465 0.0517  0.0056  0.0362  245 ASP A C   
1711 O  O   . ASP A 265 ? 0.1646 0.3226 0.5102 0.0569  0.0153  0.0306  245 ASP A O   
1712 C  CB  . ASP A 265 ? 0.1827 0.3157 0.5307 0.0661  -0.0007 0.0411  245 ASP A CB  
1713 C  CG  . ASP A 265 ? 0.3038 0.4536 0.6734 0.0678  -0.0094 0.0501  245 ASP A CG  
1714 O  OD1 . ASP A 265 ? 0.2388 0.3998 0.6055 0.0601  -0.0144 0.0538  245 ASP A OD1 
1715 O  OD2 . ASP A 265 ? 0.2319 0.3796 0.6131 0.0748  -0.0117 0.0523  245 ASP A OD2 
1716 N  N   . GLU A 266 ? 0.1687 0.3225 0.4926 0.0426  -0.0005 0.0401  246 GLU A N   
1717 C  CA  . GLU A 266 ? 0.1446 0.3142 0.4760 0.0371  0.0037  0.0392  246 GLU A CA  
1718 C  C   . GLU A 266 ? 0.1673 0.3592 0.5292 0.0407  0.0021  0.0439  246 GLU A C   
1719 O  O   . GLU A 266 ? 0.1687 0.3770 0.5417 0.0371  0.0074  0.0437  246 GLU A O   
1720 C  CB  . GLU A 266 ? 0.1561 0.3213 0.4699 0.0260  -0.0035 0.0413  246 GLU A CB  
1721 C  CG  . GLU A 266 ? 0.1531 0.2993 0.4393 0.0229  0.0003  0.0359  246 GLU A CG  
1722 C  CD  . GLU A 266 ? 0.1419 0.2828 0.4117 0.0130  -0.0057 0.0365  246 GLU A CD  
1723 O  OE1 . GLU A 266 ? 0.2196 0.3664 0.4942 0.0086  -0.0159 0.0410  246 GLU A OE1 
1724 O  OE2 . GLU A 266 ? 0.1929 0.3231 0.4452 0.0097  -0.0007 0.0321  246 GLU A OE2 
1725 N  N   . ALA A 267 ? 0.1907 0.3844 0.5672 0.0473  -0.0053 0.0492  247 ALA A N   
1726 C  CA  . ALA A 267 ? 0.2252 0.4362 0.6253 0.0520  -0.0054 0.0519  247 ALA A CA  
1727 C  C   . ALA A 267 ? 0.2153 0.4273 0.6219 0.0614  0.0076  0.0438  247 ALA A C   
1728 O  O   . ALA A 267 ? 0.2661 0.4951 0.6864 0.0633  0.0132  0.0425  247 ALA A O   
1729 C  CB  . ALA A 267 ? 0.3249 0.5342 0.7315 0.0549  -0.0185 0.0601  247 ALA A CB  
1730 N  N   . ALA A 268 ? 0.2070 0.4016 0.6038 0.0674  0.0123  0.0378  248 ALA A N   
1731 C  CA  . ALA A 268 ? 0.2839 0.4773 0.6847 0.0765  0.0234  0.0285  248 ALA A CA  
1732 C  C   . ALA A 268 ? 0.2513 0.4524 0.6444 0.0738  0.0363  0.0205  248 ALA A C   
1733 O  O   . ALA A 268 ? 0.2936 0.5073 0.6947 0.0790  0.0455  0.0149  248 ALA A O   
1734 C  CB  . ALA A 268 ? 0.2637 0.4342 0.6566 0.0828  0.0224  0.0248  248 ALA A CB  
1735 N  N   . THR A 269 ? 0.2245 0.4194 0.6020 0.0657  0.0373  0.0202  249 THR A N   
1736 C  CA  . THR A 269 ? 0.2631 0.4651 0.6315 0.0615  0.0487  0.0145  249 THR A CA  
1737 C  C   . THR A 269 ? 0.1930 0.4017 0.5568 0.0490  0.0436  0.0220  249 THR A C   
1738 O  O   . THR A 269 ? 0.2138 0.4055 0.5535 0.0419  0.0395  0.0219  249 THR A O   
1739 C  CB  . THR A 269 ? 0.2213 0.4053 0.5712 0.0637  0.0551  0.0054  249 THR A CB  
1740 O  OG1 . THR A 269 ? 0.2213 0.3843 0.5509 0.0579  0.0456  0.0087  249 THR A OG1 
1741 C  CG2 . THR A 269 ? 0.2225 0.3977 0.5757 0.0753  0.0588  -0.0031 249 THR A CG2 
1742 N  N   . PRO A 270 ? 0.2044 0.4333 0.5836 0.0450  0.0424  0.0278  250 PRO A N   
1743 C  CA  . PRO A 270 ? 0.1646 0.3990 0.5422 0.0324  0.0354  0.0352  250 PRO A CA  
1744 C  C   . PRO A 270 ? 0.1890 0.4144 0.5427 0.0246  0.0413  0.0320  250 PRO A C   
1745 O  O   . PRO A 270 ? 0.2351 0.4683 0.5874 0.0265  0.0539  0.0274  250 PRO A O   
1746 C  CB  . PRO A 270 ? 0.1452 0.4027 0.5413 0.0306  0.0365  0.0397  250 PRO A CB  
1747 C  CG  . PRO A 270 ? 0.1737 0.4343 0.5827 0.0426  0.0371  0.0372  250 PRO A CG  
1748 C  CD  . PRO A 270 ? 0.1921 0.4378 0.5893 0.0515  0.0455  0.0277  250 PRO A CD  
1749 N  N   . PRO A 271 ? 0.1517 0.3608 0.4858 0.0161  0.0323  0.0341  251 PRO A N   
1750 C  CA  . PRO A 271 ? 0.1994 0.3981 0.5111 0.0085  0.0359  0.0320  251 PRO A CA  
1751 C  C   . PRO A 271 ? 0.1403 0.3548 0.4614 -0.0015 0.0366  0.0384  251 PRO A C   
1752 O  O   . PRO A 271 ? 0.1860 0.3935 0.4998 -0.0111 0.0280  0.0423  251 PRO A O   
1753 C  CB  . PRO A 271 ? 0.1914 0.3677 0.4830 0.0055  0.0249  0.0318  251 PRO A CB  
1754 C  CG  . PRO A 271 ? 0.2975 0.4797 0.6033 0.0053  0.0133  0.0373  251 PRO A CG  
1755 C  CD  . PRO A 271 ? 0.2249 0.4248 0.5565 0.0137  0.0177  0.0385  251 PRO A CD  
1756 N  N   . VAL A 272 ? 0.1388 0.3755 0.4774 0.0011  0.0472  0.0393  252 VAL A N   
1757 C  CA  . VAL A 272 ? 0.1399 0.3971 0.4936 -0.0079 0.0492  0.0472  252 VAL A CA  
1758 C  C   . VAL A 272 ? 0.2235 0.4894 0.5695 -0.0086 0.0638  0.0455  252 VAL A C   
1759 O  O   . VAL A 272 ? 0.2238 0.4956 0.5699 0.0013  0.0750  0.0385  252 VAL A O   
1760 C  CB  . VAL A 272 ? 0.1432 0.4209 0.5221 -0.0046 0.0475  0.0508  252 VAL A CB  
1761 C  CG1 . VAL A 272 ? 0.1503 0.4465 0.5375 -0.0135 0.0509  0.0572  252 VAL A CG1 
1762 C  CG2 . VAL A 272 ? 0.1932 0.4643 0.5798 -0.0058 0.0315  0.0543  252 VAL A CG2 
1763 N  N   . VAL A 273 ? 0.1947 0.4606 0.5334 -0.0202 0.0631  0.0516  253 VAL A N   
1764 C  CA  . VAL A 273 ? 0.2678 0.5446 0.5991 -0.0228 0.0761  0.0528  253 VAL A CA  
1765 C  C   . VAL A 273 ? 0.3221 0.6236 0.6689 -0.0231 0.0819  0.0559  253 VAL A C   
1766 O  O   . VAL A 273 ? 0.2624 0.5711 0.6187 -0.0330 0.0761  0.0644  253 VAL A O   
1767 C  CB  . VAL A 273 ? 0.2871 0.5512 0.6022 -0.0352 0.0713  0.0588  253 VAL A CB  
1768 C  CG1 . VAL A 273 ? 0.3269 0.6036 0.6335 -0.0380 0.0846  0.0615  253 VAL A CG1 
1769 C  CG2 . VAL A 273 ? 0.2505 0.4833 0.5409 -0.0340 0.0626  0.0524  253 VAL A CG2 
1770 N  N   . ASN A 274 ? 0.2211 0.5351 0.5710 -0.0122 0.0931  0.0484  254 ASN A N   
1771 C  CA  . ASN A 274 ? 0.2798 0.6189 0.6462 -0.0113 0.0992  0.0503  254 ASN A CA  
1772 C  C   . ASN A 274 ? 0.3150 0.6656 0.6746 -0.0212 0.1069  0.0566  254 ASN A C   
1773 O  O   . ASN A 274 ? 0.3392 0.6893 0.6813 -0.0195 0.1172  0.0523  254 ASN A O   
1774 C  CB  . ASN A 274 ? 0.2862 0.6349 0.6570 0.0037  0.1091  0.0392  254 ASN A CB  
1775 C  CG  . ASN A 274 ? 0.3673 0.7420 0.7600 0.0062  0.1135  0.0406  254 ASN A CG  
1776 O  OD1 . ASN A 274 ? 0.3324 0.7229 0.7306 -0.0027 0.1172  0.0477  254 ASN A OD1 
1777 N  ND2 . ASN A 274 ? 0.3540 0.7325 0.7599 0.0184  0.1129  0.0343  254 ASN A ND2 
1778 N  N   . PRO A 275 ? 0.3098 0.6702 0.6822 -0.0318 0.1018  0.0669  255 PRO A N   
1779 C  CA  . PRO A 275 ? 0.2896 0.6589 0.6558 -0.0420 0.1082  0.0746  255 PRO A CA  
1780 C  C   . PRO A 275 ? 0.4499 0.8425 0.8179 -0.0365 0.1248  0.0707  255 PRO A C   
1781 O  O   . PRO A 275 ? 0.3540 0.7534 0.7131 -0.0436 0.1319  0.0766  255 PRO A O   
1782 C  CB  . PRO A 275 ? 0.2822 0.6550 0.6656 -0.0533 0.0969  0.0859  255 PRO A CB  
1783 C  CG  . PRO A 275 ? 0.2754 0.6552 0.6792 -0.0458 0.0911  0.0822  255 PRO A CG  
1784 C  CD  . PRO A 275 ? 0.2627 0.6261 0.6559 -0.0349 0.0895  0.0722  255 PRO A CD  
1785 N  N   . SER A 276 ? 0.3738 0.7783 0.7530 -0.0239 0.1307  0.0611  256 SER A N   
1786 C  CA  . SER A 276 ? 0.3772 0.8031 0.7584 -0.0168 0.1469  0.0545  256 SER A CA  
1787 C  C   . SER A 276 ? 0.5273 0.9449 0.8869 -0.0072 0.1566  0.0416  256 SER A C   
1788 O  O   . SER A 276 ? 0.6125 1.0448 0.9702 -0.0008 0.1706  0.0340  256 SER A O   
1789 C  CB  . SER A 276 ? 0.3893 0.8334 0.7962 -0.0077 0.1478  0.0502  256 SER A CB  
1790 O  OG  . SER A 276 ? 0.4050 0.8617 0.8326 -0.0170 0.1414  0.0621  256 SER A OG  
1791 N  N   . VAL A 277 ? 0.4357 0.8296 0.7793 -0.0060 0.1495  0.0386  257 VAL A N   
1792 C  CA  . VAL A 277 ? 0.5546 0.9380 0.8781 0.0032  0.1566  0.0261  257 VAL A CA  
1793 C  C   . VAL A 277 ? 0.6047 0.9752 0.9036 -0.0061 0.1569  0.0317  257 VAL A C   
1794 O  O   . VAL A 277 ? 0.6262 0.9815 0.9216 -0.0147 0.1456  0.0405  257 VAL A O   
1795 C  CB  . VAL A 277 ? 0.5364 0.9024 0.8618 0.0135  0.1481  0.0184  257 VAL A CB  
1796 C  CG1 . VAL A 277 ? 0.6518 1.0043 0.9550 0.0218  0.1538  0.0062  257 VAL A CG1 
1797 C  CG2 . VAL A 277 ? 0.5314 0.9100 0.8802 0.0237  0.1471  0.0138  257 VAL A CG2 
1798 N  N   . ASN A 278 ? 0.6036 0.9793 0.8852 -0.0041 0.1694  0.0267  258 ASN A N   
1799 C  CA  . ASN A 278 ? 0.6454 1.0107 0.9018 -0.0122 0.1699  0.0326  258 ASN A CA  
1800 C  C   . ASN A 278 ? 0.6307 0.9771 0.8668 -0.0047 0.1693  0.0218  258 ASN A C   
1801 O  O   . ASN A 278 ? 0.6093 0.9516 0.8495 0.0075  0.1713  0.0085  258 ASN A O   
1802 C  CB  . ASN A 278 ? 0.5870 0.9688 0.8333 -0.0149 0.1827  0.0358  258 ASN A CB  
1803 C  CG  . ASN A 278 ? 0.7189 1.1215 0.9866 -0.0217 0.1844  0.0464  258 ASN A CG  
1804 O  OD1 . ASN A 278 ? 0.6766 1.0777 0.9611 -0.0292 0.1735  0.0557  258 ASN A OD1 
1805 N  ND2 . ASN A 278 ? 0.6744 1.0964 0.9414 -0.0189 0.1982  0.0449  258 ASN A ND2 
1806 N  N   . GLY A 279 ? 0.6722 1.0066 0.8870 -0.0123 0.1657  0.0278  259 GLY A N   
1807 C  CA  . GLY A 279 ? 0.6116 0.9292 0.8056 -0.0070 0.1642  0.0188  259 GLY A CA  
1808 C  C   . GLY A 279 ? 0.6353 0.9299 0.8323 -0.0092 0.1499  0.0209  259 GLY A C   
1809 O  O   . GLY A 279 ? 0.5941 0.8872 0.8107 -0.0131 0.1418  0.0282  259 GLY A O   
1810 N  N   . SER A 280 ? 0.8448 1.1153 1.0187 -0.0073 0.1447  0.0128  260 SER A N   
1811 C  CA  . SER A 280 ? 0.7028 0.9451 0.8746 -0.0087 0.1304  0.0122  260 SER A CA  
1812 C  C   . SER A 280 ? 0.5862 0.8248 0.7780 -0.0003 0.1268  0.0063  260 SER A C   
1813 O  O   . SER A 280 ? 0.5769 0.8271 0.7785 0.0097  0.1349  -0.0024 260 SER A O   
1814 C  CB  . SER A 280 ? 0.6665 0.8872 0.8125 -0.0067 0.1271  0.0037  260 SER A CB  
1815 O  OG  . SER A 280 ? 0.7964 1.0170 0.9382 0.0045  0.1335  -0.0112 260 SER A OG  
1816 N  N   . LEU A 281 ? 0.4251 0.6478 0.6232 -0.0040 0.1143  0.0111  261 LEU A N   
1817 C  CA  . LEU A 281 ? 0.3459 0.5670 0.5638 0.0024  0.1094  0.0085  261 LEU A CA  
1818 C  C   . LEU A 281 ? 0.3303 0.5386 0.5430 0.0138  0.1106  -0.0047 261 LEU A C   
1819 O  O   . LEU A 281 ? 0.4475 0.6358 0.6408 0.0138  0.1068  -0.0097 261 LEU A O   
1820 C  CB  . LEU A 281 ? 0.2619 0.4677 0.4831 -0.0041 0.0954  0.0155  261 LEU A CB  
1821 C  CG  . LEU A 281 ? 0.3747 0.5911 0.6065 -0.0151 0.0915  0.0281  261 LEU A CG  
1822 C  CD1 . LEU A 281 ? 0.3514 0.5506 0.5851 -0.0194 0.0771  0.0315  261 LEU A CD1 
1823 C  CD2 . LEU A 281 ? 0.2418 0.4863 0.4990 -0.0134 0.0986  0.0320  261 LEU A CD2 
1824 N  N   . PRO A 282 ? 0.2745 0.4933 0.5056 0.0236  0.1152  -0.0103 262 PRO A N   
1825 C  CA  . PRO A 282 ? 0.3197 0.5240 0.5484 0.0344  0.1150  -0.0224 262 PRO A CA  
1826 C  C   . PRO A 282 ? 0.3494 0.5316 0.5787 0.0338  0.1018  -0.0201 262 PRO A C   
1827 O  O   . PRO A 282 ? 0.2700 0.4533 0.5089 0.0285  0.0939  -0.0106 262 PRO A O   
1828 C  CB  . PRO A 282 ? 0.3994 0.6234 0.6523 0.0446  0.1229  -0.0267 262 PRO A CB  
1829 C  CG  . PRO A 282 ? 0.4107 0.6536 0.6832 0.0382  0.1209  -0.0139 262 PRO A CG  
1830 C  CD  . PRO A 282 ? 0.2825 0.5274 0.5392 0.0254  0.1207  -0.0053 262 PRO A CD  
1831 N  N   . PRO A 283 ? 0.3470 0.5096 0.5664 0.0391  0.0990  -0.0284 263 PRO A N   
1832 C  CA  . PRO A 283 ? 0.2442 0.3881 0.4651 0.0390  0.0874  -0.0252 263 PRO A CA  
1833 C  C   . PRO A 283 ? 0.2111 0.3622 0.4569 0.0451  0.0842  -0.0222 263 PRO A C   
1834 O  O   . PRO A 283 ? 0.2526 0.4193 0.5155 0.0524  0.0912  -0.0257 263 PRO A O   
1835 C  CB  . PRO A 283 ? 0.2747 0.3997 0.4827 0.0437  0.0871  -0.0350 263 PRO A CB  
1836 C  CG  . PRO A 283 ? 0.3173 0.4532 0.5281 0.0514  0.0982  -0.0459 263 PRO A CG  
1837 C  CD  . PRO A 283 ? 0.3932 0.5510 0.6019 0.0459  0.1061  -0.0413 263 PRO A CD  
1838 N  N   . LEU A 284 ? 0.2175 0.3583 0.4653 0.0422  0.0732  -0.0152 264 LEU A N   
1839 C  CA  . LEU A 284 ? 0.1834 0.3288 0.4529 0.0476  0.0678  -0.0110 264 LEU A CA  
1840 C  C   . LEU A 284 ? 0.2657 0.3952 0.5377 0.0563  0.0656  -0.0167 264 LEU A C   
1841 O  O   . LEU A 284 ? 0.2831 0.3985 0.5404 0.0573  0.0680  -0.0240 264 LEU A O   
1842 C  CB  . LEU A 284 ? 0.1497 0.2927 0.4183 0.0400  0.0567  -0.0007 264 LEU A CB  
1843 C  CG  . LEU A 284 ? 0.1854 0.3431 0.4544 0.0310  0.0580  0.0048  264 LEU A CG  
1844 C  CD1 . LEU A 284 ? 0.1981 0.3480 0.4591 0.0224  0.0467  0.0121  264 LEU A CD1 
1845 C  CD2 . LEU A 284 ? 0.1895 0.3715 0.4842 0.0340  0.0624  0.0075  264 LEU A CD2 
1846 N  N   . GLY A 285 ? 0.2149 0.3462 0.5063 0.0621  0.0601  -0.0126 265 GLY A N   
1847 C  CA  . GLY A 285 ? 0.2060 0.3200 0.5004 0.0686  0.0556  -0.0148 265 GLY A CA  
1848 C  C   . GLY A 285 ? 0.2556 0.3514 0.5312 0.0619  0.0474  -0.0100 265 GLY A C   
1849 O  O   . GLY A 285 ? 0.3376 0.4346 0.6012 0.0535  0.0434  -0.0039 265 GLY A O   
1850 N  N   . GLU A 286 ? 0.2317 0.3102 0.5045 0.0657  0.0454  -0.0133 266 GLU A N   
1851 C  CA  . GLU A 286 ? 0.1695 0.2328 0.4294 0.0607  0.0374  -0.0070 266 GLU A CA  
1852 C  C   . GLU A 286 ? 0.2194 0.2721 0.4936 0.0673  0.0315  -0.0035 266 GLU A C   
1853 O  O   . GLU A 286 ? 0.2383 0.2836 0.5216 0.0742  0.0348  -0.0114 266 GLU A O   
1854 C  CB  . GLU A 286 ? 0.2504 0.3019 0.4886 0.0557  0.0405  -0.0129 266 GLU A CB  
1855 C  CG  . GLU A 286 ? 0.2556 0.2915 0.4850 0.0527  0.0337  -0.0077 266 GLU A CG  
1856 C  CD  . GLU A 286 ? 0.2048 0.2335 0.4128 0.0460  0.0352  -0.0104 266 GLU A CD  
1857 O  OE1 . GLU A 286 ? 0.2327 0.2638 0.4330 0.0451  0.0416  -0.0187 266 GLU A OE1 
1858 O  OE2 . GLU A 286 ? 0.2410 0.2626 0.4402 0.0418  0.0300  -0.0038 266 GLU A OE2 
1859 N  N   . LEU A 287 ? 0.1753 0.2269 0.4512 0.0650  0.0226  0.0081  267 LEU A N   
1860 C  CA  . LEU A 287 ? 0.2090 0.2504 0.4978 0.0700  0.0160  0.0142  267 LEU A CA  
1861 C  C   . LEU A 287 ? 0.1989 0.2213 0.4795 0.0695  0.0167  0.0099  267 LEU A C   
1862 O  O   . LEU A 287 ? 0.2203 0.2372 0.4810 0.0623  0.0173  0.0097  267 LEU A O   
1863 C  CB  . LEU A 287 ? 0.2463 0.2901 0.5321 0.0660  0.0064  0.0282  267 LEU A CB  
1864 C  CG  . LEU A 287 ? 0.2564 0.3173 0.5535 0.0666  0.0018  0.0349  267 LEU A CG  
1865 C  CD1 . LEU A 287 ? 0.2983 0.3581 0.5902 0.0634  -0.0088 0.0481  267 LEU A CD1 
1866 C  CD2 . LEU A 287 ? 0.2794 0.3474 0.6039 0.0763  0.0032  0.0328  267 LEU A CD2 
1867 N  N   . PRO A 288 ? 0.2364 0.2481 0.5328 0.0768  0.0161  0.0063  268 PRO A N   
1868 C  CA  . PRO A 288 ? 0.2951 0.2878 0.5853 0.0754  0.0155  0.0022  268 PRO A CA  
1869 C  C   . PRO A 288 ? 0.3023 0.2869 0.5831 0.0684  0.0084  0.0149  268 PRO A C   
1870 O  O   . PRO A 288 ? 0.3302 0.3037 0.5996 0.0636  0.0087  0.0126  268 PRO A O   
1871 C  CB  . PRO A 288 ? 0.3136 0.2970 0.6214 0.0835  0.0142  -0.0028 268 PRO A CB  
1872 C  CG  . PRO A 288 ? 0.3624 0.3592 0.6841 0.0882  0.0121  0.0030  268 PRO A CG  
1873 C  CD  . PRO A 288 ? 0.2499 0.2663 0.5679 0.0858  0.0161  0.0044  268 PRO A CD  
1874 N  N   . THR A 289 ? 0.3841 0.3753 0.6691 0.0677  0.0019  0.0285  269 THR A N   
1875 C  CA  . THR A 289 ? 0.4622 0.4488 0.7383 0.0618  -0.0044 0.0418  269 THR A CA  
1876 C  C   . THR A 289 ? 0.4744 0.4761 0.7400 0.0580  -0.0072 0.0499  269 THR A C   
1877 O  O   . THR A 289 ? 0.3885 0.4024 0.6624 0.0611  -0.0076 0.0494  269 THR A O   
1878 C  CB  . THR A 289 ? 0.4710 0.4471 0.7659 0.0658  -0.0118 0.0521  269 THR A CB  
1879 O  OG1 . THR A 289 ? 0.6229 0.5830 0.9263 0.0685  -0.0101 0.0429  269 THR A OG1 
1880 C  CG2 . THR A 289 ? 0.6126 0.5867 0.8980 0.0593  -0.0177 0.0677  269 THR A CG2 
1881 N  N   . SER A 290 ? 0.3377 0.3392 0.5855 0.0513  -0.0091 0.0569  270 SER A N   
1882 C  CA  . SER A 290 ? 0.2891 0.3032 0.5251 0.0479  -0.0127 0.0637  270 SER A CA  
1883 C  C   . SER A 290 ? 0.2444 0.2644 0.4942 0.0515  -0.0209 0.0754  270 SER A C   
1884 O  O   . SER A 290 ? 0.2842 0.2962 0.5468 0.0544  -0.0250 0.0836  270 SER A O   
1885 C  CB  . SER A 290 ? 0.2900 0.3025 0.5054 0.0414  -0.0131 0.0690  270 SER A CB  
1886 O  OG  . SER A 290 ? 0.3405 0.3641 0.5452 0.0392  -0.0178 0.0759  270 SER A OG  
1887 N  N   . PRO A 291 ? 0.2641 0.2976 0.5127 0.0512  -0.0243 0.0772  271 PRO A N   
1888 C  CA  . PRO A 291 ? 0.2605 0.3010 0.5204 0.0540  -0.0335 0.0896  271 PRO A CA  
1889 C  C   . PRO A 291 ? 0.3090 0.3488 0.5551 0.0501  -0.0396 0.1031  271 PRO A C   
1890 O  O   . PRO A 291 ? 0.3339 0.3767 0.5898 0.0525  -0.0477 0.1157  271 PRO A O   
1891 C  CB  . PRO A 291 ? 0.3694 0.4251 0.6292 0.0531  -0.0355 0.0863  271 PRO A CB  
1892 C  CG  . PRO A 291 ? 0.3338 0.3896 0.5743 0.0475  -0.0291 0.0761  271 PRO A CG  
1893 C  CD  . PRO A 291 ? 0.3330 0.3761 0.5719 0.0481  -0.0207 0.0683  271 PRO A CD  
1894 N  N   . ASP A 292 ? 0.2756 0.3128 0.4997 0.0445  -0.0360 0.1015  272 ASP A N   
1895 C  CA  . ASP A 292 ? 0.2924 0.3319 0.5009 0.0408  -0.0401 0.1137  272 ASP A CA  
1896 C  C   . ASP A 292 ? 0.2848 0.3136 0.4876 0.0380  -0.0344 0.1138  272 ASP A C   
1897 O  O   . ASP A 292 ? 0.3140 0.3406 0.5048 0.0352  -0.0275 0.1033  272 ASP A O   
1898 C  CB  . ASP A 292 ? 0.3051 0.3556 0.4912 0.0368  -0.0416 0.1110  272 ASP A CB  
1899 C  CG  . ASP A 292 ? 0.3882 0.4437 0.5557 0.0337  -0.0450 0.1225  272 ASP A CG  
1900 O  OD1 . ASP A 292 ? 0.3157 0.3663 0.4866 0.0334  -0.0450 0.1332  272 ASP A OD1 
1901 O  OD2 . ASP A 292 ? 0.3335 0.3981 0.4828 0.0315  -0.0479 0.1208  272 ASP A OD2 
1902 N  N   . PRO A 293 ? 0.3061 0.3284 0.5181 0.0382  -0.0374 0.1261  273 PRO A N   
1903 C  CA  . PRO A 293 ? 0.3038 0.3167 0.5127 0.0346  -0.0325 0.1269  273 PRO A CA  
1904 C  C   . PRO A 293 ? 0.3957 0.4161 0.5801 0.0294  -0.0285 0.1273  273 PRO A C   
1905 O  O   . PRO A 293 ? 0.3243 0.3390 0.5049 0.0264  -0.0230 0.1236  273 PRO A O   
1906 C  CB  . PRO A 293 ? 0.3015 0.3081 0.5255 0.0351  -0.0386 0.1435  273 PRO A CB  
1907 C  CG  . PRO A 293 ? 0.3286 0.3462 0.5531 0.0373  -0.0466 0.1545  273 PRO A CG  
1908 C  CD  . PRO A 293 ? 0.2452 0.2691 0.4712 0.0410  -0.0462 0.1414  273 PRO A CD  
1909 N  N   . LYS A 294 ? 0.3053 0.3385 0.4732 0.0286  -0.0313 0.1308  274 LYS A N   
1910 C  CA  . LYS A 294 ? 0.3528 0.3935 0.4972 0.0249  -0.0272 0.1298  274 LYS A CA  
1911 C  C   . LYS A 294 ? 0.3293 0.3696 0.4632 0.0245  -0.0216 0.1129  274 LYS A C   
1912 O  O   . LYS A 294 ? 0.3145 0.3591 0.4310 0.0223  -0.0174 0.1100  274 LYS A O   
1913 C  CB  . LYS A 294 ? 0.3543 0.4085 0.4832 0.0245  -0.0329 0.1393  274 LYS A CB  
1914 C  CG  . LYS A 294 ? 0.3688 0.4258 0.5034 0.0239  -0.0382 0.1590  274 LYS A CG  
1915 C  CD  . LYS A 294 ? 0.4514 0.5233 0.5677 0.0236  -0.0442 0.1674  274 LYS A CD  
1916 C  CE  . LYS A 294 ? 0.5658 0.6434 0.6808 0.0215  -0.0473 0.1884  274 LYS A CE  
1917 N  NZ  . LYS A 294 ? 0.7675 0.8600 0.8648 0.0216  -0.0544 0.1971  274 LYS A NZ  
1918 N  N   . ALA A 295 ? 0.2749 0.3110 0.4193 0.0267  -0.0213 0.1023  275 ALA A N   
1919 C  CA  . ALA A 295 ? 0.2452 0.2805 0.3806 0.0256  -0.0163 0.0880  275 ALA A CA  
1920 C  C   . ALA A 295 ? 0.2733 0.3007 0.4078 0.0237  -0.0094 0.0833  275 ALA A C   
1921 O  O   . ALA A 295 ? 0.2950 0.3145 0.4427 0.0239  -0.0087 0.0867  275 ALA A O   
1922 C  CB  . ALA A 295 ? 0.2627 0.2973 0.4109 0.0279  -0.0170 0.0795  275 ALA A CB  
1923 N  N   . GLY A 296 ? 0.2887 0.3179 0.4085 0.0218  -0.0053 0.0756  276 GLY A N   
1924 C  CA  . GLY A 296 ? 0.2733 0.2961 0.3928 0.0200  0.0005  0.0700  276 GLY A CA  
1925 C  C   . GLY A 296 ? 0.2640 0.2920 0.3668 0.0183  0.0038  0.0696  276 GLY A C   
1926 O  O   . GLY A 296 ? 0.2331 0.2686 0.3224 0.0189  0.0022  0.0701  276 GLY A O   
1927 N  N   . LEU A 297 ? 0.2120 0.2359 0.3162 0.0164  0.0081  0.0681  277 LEU A N   
1928 C  CA  . LEU A 297 ? 0.2060 0.2351 0.2977 0.0155  0.0121  0.0668  277 LEU A CA  
1929 C  C   . LEU A 297 ? 0.2116 0.2480 0.3016 0.0143  0.0131  0.0793  277 LEU A C   
1930 O  O   . LEU A 297 ? 0.2752 0.3082 0.3779 0.0124  0.0121  0.0877  277 LEU A O   
1931 C  CB  . LEU A 297 ? 0.2353 0.2579 0.3309 0.0138  0.0157  0.0593  277 LEU A CB  
1932 C  CG  . LEU A 297 ? 0.2305 0.2580 0.3178 0.0131  0.0199  0.0582  277 LEU A CG  
1933 C  CD1 . LEU A 297 ? 0.2243 0.2574 0.2960 0.0158  0.0207  0.0525  277 LEU A CD1 
1934 C  CD2 . LEU A 297 ? 0.2841 0.3044 0.3775 0.0112  0.0216  0.0515  277 LEU A CD2 
1935 N  N   . TYR A 298 ? 0.1950 0.2417 0.2697 0.0156  0.0151  0.0806  278 TYR A N   
1936 C  CA  . TYR A 298 ? 0.2078 0.2652 0.2782 0.0148  0.0173  0.0927  278 TYR A CA  
1937 C  C   . TYR A 298 ? 0.2292 0.2934 0.2916 0.0154  0.0237  0.0887  278 TYR A C   
1938 O  O   . TYR A 298 ? 0.2145 0.2785 0.2663 0.0182  0.0250  0.0775  278 TYR A O   
1939 C  CB  . TYR A 298 ? 0.2076 0.2745 0.2652 0.0167  0.0140  0.0984  278 TYR A CB  
1940 C  CG  . TYR A 298 ? 0.2136 0.2762 0.2821 0.0161  0.0073  0.1064  278 TYR A CG  
1941 C  CD1 . TYR A 298 ? 0.2369 0.2917 0.3111 0.0175  0.0026  0.0985  278 TYR A CD1 
1942 C  CD2 . TYR A 298 ? 0.2252 0.2920 0.3001 0.0142  0.0057  0.1226  278 TYR A CD2 
1943 C  CE1 . TYR A 298 ? 0.2233 0.2751 0.3098 0.0179  -0.0034 0.1058  278 TYR A CE1 
1944 C  CE2 . TYR A 298 ? 0.2621 0.3242 0.3489 0.0143  -0.0011 0.1305  278 TYR A CE2 
1945 C  CZ  . TYR A 298 ? 0.2748 0.3297 0.3677 0.0166  -0.0055 0.1216  278 TYR A CZ  
1946 O  OH  . TYR A 298 ? 0.3192 0.3703 0.4260 0.0177  -0.0122 0.1293  278 TYR A OH  
1947 N  N   . ILE A 299 ? 0.2039 0.2740 0.2731 0.0128  0.0274  0.0984  279 ILE A N   
1948 C  CA  . ILE A 299 ? 0.2137 0.2913 0.2803 0.0133  0.0337  0.0958  279 ILE A CA  
1949 C  C   . ILE A 299 ? 0.2605 0.3549 0.3234 0.0127  0.0382  0.1092  279 ILE A C   
1950 O  O   . ILE A 299 ? 0.2315 0.3278 0.3033 0.0089  0.0364  0.1231  279 ILE A O   
1951 C  CB  . ILE A 299 ? 0.2076 0.2761 0.2902 0.0097  0.0339  0.0931  279 ILE A CB  
1952 C  CG1 . ILE A 299 ? 0.2195 0.2732 0.3044 0.0103  0.0301  0.0806  279 ILE A CG1 
1953 C  CG2 . ILE A 299 ? 0.2261 0.3038 0.3079 0.0104  0.0397  0.0911  279 ILE A CG2 
1954 C  CD1 . ILE A 299 ? 0.2778 0.3229 0.3748 0.0071  0.0298  0.0764  279 ILE A CD1 
1955 N  N   . LYS A 300 ? 0.2326 0.3396 0.2829 0.0166  0.0442  0.1053  280 LYS A N   
1956 C  CA  . LYS A 300 ? 0.2967 0.4230 0.3432 0.0165  0.0504  0.1175  280 LYS A CA  
1957 C  C   . LYS A 300 ? 0.2653 0.3951 0.3307 0.0118  0.0539  0.1251  280 LYS A C   
1958 O  O   . LYS A 300 ? 0.2989 0.4270 0.3690 0.0131  0.0564  0.1164  280 LYS A O   
1959 C  CB  . LYS A 300 ? 0.3892 0.5282 0.4162 0.0236  0.0562  0.1089  280 LYS A CB  
1960 C  CG  . LYS A 300 ? 0.4751 0.6146 0.4816 0.0275  0.0525  0.1039  280 LYS A CG  
1961 C  CD  . LYS A 300 ? 0.8024 0.9552 0.7894 0.0348  0.0587  0.0951  280 LYS A CD  
1962 C  CE  . LYS A 300 ? 0.8734 1.0304 0.8381 0.0379  0.0550  0.0924  280 LYS A CE  
1963 N  NZ  . LYS A 300 ? 0.8571 1.0232 0.8021 0.0459  0.0601  0.0796  280 LYS A NZ  
1964 N  N   . SER A 301 ? 0.2870 0.4210 0.3641 0.0060  0.0531  0.1417  281 SER A N   
1965 C  CA  . SER A 301 ? 0.3549 0.4908 0.4526 0.0000  0.0546  0.1501  281 SER A CA  
1966 C  C   . SER A 301 ? 0.2906 0.4512 0.3875 -0.0001 0.0635  0.1611  281 SER A C   
1967 O  O   . SER A 301 ? 0.2672 0.4436 0.3471 0.0041  0.0685  0.1645  281 SER A O   
1968 C  CB  . SER A 301 ? 0.3594 0.4836 0.4741 -0.0070 0.0478  0.1620  281 SER A CB  
1969 O  OG  . SER A 301 ? 0.4315 0.5684 0.5433 -0.0091 0.0489  0.1794  281 SER A OG  
1970 N  N   . ARG A 302 ? 0.3042 0.4690 0.4203 -0.0053 0.0653  0.1672  282 ARG A N   
1971 C  CA  . ARG A 302 ? 0.3419 0.5322 0.4613 -0.0056 0.0744  0.1779  282 ARG A CA  
1972 C  C   . ARG A 302 ? 0.3516 0.5561 0.4685 -0.0089 0.0763  0.1966  282 ARG A C   
1973 O  O   . ARG A 302 ? 0.3410 0.5659 0.4518 -0.0062 0.0827  0.2003  282 ARG A O   
1974 C  CB  . ARG A 302 ? 0.3591 0.5496 0.5029 -0.0119 0.0738  0.1812  282 ARG A CB  
1975 C  CG  . ARG A 302 ? 0.3968 0.5767 0.5598 -0.0216 0.0658  0.1937  282 ARG A CG  
1976 C  CD  . ARG A 302 ? 0.3965 0.5736 0.5804 -0.0271 0.0625  0.1926  282 ARG A CD  
1977 N  NE  . ARG A 302 ? 0.4820 0.6808 0.6662 -0.0241 0.0697  0.1933  282 ARG A NE  
1978 C  CZ  . ARG A 302 ? 0.3993 0.6125 0.5915 -0.0273 0.0710  0.2052  282 ARG A CZ  
1979 N  NH1 . ARG A 302 ? 0.4376 0.6465 0.6384 -0.0339 0.0655  0.2181  282 ARG A NH1 
1980 N  NH2 . ARG A 302 ? 0.4701 0.7028 0.6631 -0.0237 0.0780  0.2044  282 ARG A NH2 
1981 N  N   . THR A 303 ? 0.3032 0.4945 0.4241 -0.0136 0.0686  0.2051  283 THR A N   
1982 C  CA  . THR A 303 ? 0.2928 0.4934 0.4104 -0.0159 0.0668  0.2197  283 THR A CA  
1983 C  C   . THR A 303 ? 0.4010 0.6136 0.4916 -0.0094 0.0706  0.2191  283 THR A C   
1984 O  O   . THR A 303 ? 0.4596 0.6835 0.5446 -0.0107 0.0701  0.2308  283 THR A O   
1985 C  CB  . THR A 303 ? 0.4165 0.5975 0.5492 -0.0223 0.0561  0.2281  283 THR A CB  
1986 O  OG1 . THR A 303 ? 0.3416 0.5062 0.4664 -0.0194 0.0521  0.2208  283 THR A OG1 
1987 C  CG2 . THR A 303 ? 0.3858 0.5536 0.5441 -0.0290 0.0510  0.2280  283 THR A CG2 
1988 N  N   . GLY A 304 ? 0.3403 0.5506 0.4139 -0.0026 0.0735  0.2054  284 GLY A N   
1989 C  CA  . GLY A 304 ? 0.4101 0.6253 0.4577 0.0033  0.0730  0.2016  284 GLY A CA  
1990 C  C   . GLY A 304 ? 0.4314 0.6269 0.4783 0.0020  0.0619  0.2011  284 GLY A C   
1991 O  O   . GLY A 304 ? 0.4258 0.6226 0.4519 0.0069  0.0594  0.1951  284 GLY A O   
1992 N  N   . GLN A 305 ? 0.3255 0.5035 0.3951 -0.0042 0.0548  0.2070  285 GLN A N   
1993 C  CA  . GLN A 305 ? 0.3773 0.5355 0.4492 -0.0041 0.0446  0.2038  285 GLN A CA  
1994 C  C   . GLN A 305 ? 0.2631 0.4065 0.3288 0.0012  0.0422  0.1808  285 GLN A C   
1995 O  O   . GLN A 305 ? 0.2820 0.4211 0.3530 0.0021  0.0455  0.1692  285 GLN A O   
1996 C  CB  . GLN A 305 ? 0.3368 0.4789 0.4356 -0.0111 0.0381  0.2138  285 GLN A CB  
1997 C  CG  . GLN A 305 ? 0.2980 0.4492 0.4090 -0.0177 0.0376  0.2354  285 GLN A CG  
1998 C  CD  . GLN A 305 ? 0.3639 0.4962 0.5029 -0.0237 0.0307  0.2372  285 GLN A CD  
1999 O  OE1 . GLN A 305 ? 0.3823 0.5019 0.5325 -0.0257 0.0222  0.2432  285 GLN A OE1 
2000 N  NE2 . GLN A 305 ? 0.3497 0.4799 0.5001 -0.0263 0.0338  0.2308  285 GLN A NE2 
2001 N  N   . THR A 306 ? 0.2751 0.4109 0.3310 0.0043  0.0358  0.1753  286 THR A N   
2002 C  CA  . THR A 306 ? 0.2707 0.3903 0.3261 0.0077  0.0319  0.1566  286 THR A CA  
2003 C  C   . THR A 306 ? 0.2763 0.3772 0.3529 0.0044  0.0247  0.1587  286 THR A C   
2004 O  O   . THR A 306 ? 0.3813 0.4794 0.4626 0.0033  0.0187  0.1692  286 THR A O   
2005 C  CB  . THR A 306 ? 0.3450 0.4678 0.3794 0.0127  0.0287  0.1487  286 THR A CB  
2006 O  OG1 . THR A 306 ? 0.4132 0.5530 0.4274 0.0164  0.0356  0.1458  286 THR A OG1 
2007 C  CG2 . THR A 306 ? 0.2879 0.3952 0.3233 0.0153  0.0250  0.1307  286 THR A CG2 
2008 N  N   . VAL A 307 ? 0.2259 0.3144 0.3151 0.0032  0.0253  0.1487  287 VAL A N   
2009 C  CA  . VAL A 307 ? 0.2660 0.3377 0.3763 -0.0001 0.0199  0.1502  287 VAL A CA  
2010 C  C   . VAL A 307 ? 0.2360 0.2938 0.3465 0.0034  0.0163  0.1341  287 VAL A C   
2011 O  O   . VAL A 307 ? 0.2511 0.3097 0.3503 0.0064  0.0190  0.1206  287 VAL A O   
2012 C  CB  . VAL A 307 ? 0.2324 0.3014 0.3580 -0.0051 0.0225  0.1525  287 VAL A CB  
2013 C  CG1 . VAL A 307 ? 0.2288 0.3141 0.3561 -0.0092 0.0265  0.1706  287 VAL A CG1 
2014 C  CG2 . VAL A 307 ? 0.2407 0.3095 0.3606 -0.0032 0.0270  0.1370  287 VAL A CG2 
2015 N  N   . GLN A 308 ? 0.2267 0.2721 0.3515 0.0031  0.0104  0.1360  288 GLN A N   
2016 C  CA  . GLN A 308 ? 0.2105 0.2443 0.3385 0.0063  0.0076  0.1220  288 GLN A CA  
2017 C  C   . GLN A 308 ? 0.2551 0.2764 0.3957 0.0042  0.0085  0.1134  288 GLN A C   
2018 O  O   . GLN A 308 ? 0.3019 0.3168 0.4573 0.0006  0.0068  0.1206  288 GLN A O   
2019 C  CB  . GLN A 308 ? 0.2266 0.2552 0.3640 0.0084  0.0010  0.1279  288 GLN A CB  
2020 C  CG  . GLN A 308 ? 0.2381 0.2589 0.3786 0.0123  -0.0011 0.1144  288 GLN A CG  
2021 C  CD  . GLN A 308 ? 0.3320 0.3496 0.4841 0.0150  -0.0077 0.1209  288 GLN A CD  
2022 O  OE1 . GLN A 308 ? 0.3745 0.3909 0.5363 0.0137  -0.0114 0.1351  288 GLN A OE1 
2023 N  NE2 . GLN A 308 ? 0.3354 0.3524 0.4878 0.0187  -0.0094 0.1116  288 GLN A NE2 
2024 N  N   . VAL A 309 ? 0.2194 0.2372 0.3542 0.0062  0.0106  0.0984  289 VAL A N   
2025 C  CA  . VAL A 309 ? 0.2587 0.2661 0.4016 0.0044  0.0114  0.0889  289 VAL A CA  
2026 C  C   . VAL A 309 ? 0.3039 0.3029 0.4491 0.0079  0.0099  0.0770  289 VAL A C   
2027 O  O   . VAL A 309 ? 0.3192 0.3231 0.4544 0.0107  0.0107  0.0714  289 VAL A O   
2028 C  CB  . VAL A 309 ? 0.2931 0.3066 0.4263 0.0030  0.0162  0.0834  289 VAL A CB  
2029 C  CG1 . VAL A 309 ? 0.3337 0.3373 0.4739 0.0010  0.0159  0.0736  289 VAL A CG1 
2030 C  CG2 . VAL A 309 ? 0.2829 0.3074 0.4158 0.0001  0.0186  0.0958  289 VAL A CG2 
2031 N  N   . LYS A 310 ? 0.2889 0.2759 0.4479 0.0076  0.0078  0.0730  290 LYS A N   
2032 C  CA  . LYS A 310 ? 0.2756 0.2561 0.4385 0.0114  0.0073  0.0619  290 LYS A CA  
2033 C  C   . LYS A 310 ? 0.3581 0.3329 0.5185 0.0101  0.0099  0.0492  290 LYS A C   
2034 O  O   . LYS A 310 ? 0.4405 0.4099 0.6056 0.0064  0.0091  0.0493  290 LYS A O   
2035 C  CB  . LYS A 310 ? 0.3796 0.3510 0.5599 0.0138  0.0028  0.0658  290 LYS A CB  
2036 C  CG  . LYS A 310 ? 0.5050 0.4832 0.6866 0.0154  -0.0005 0.0789  290 LYS A CG  
2037 C  CD  . LYS A 310 ? 0.6233 0.5923 0.8241 0.0181  -0.0058 0.0847  290 LYS A CD  
2038 C  CE  . LYS A 310 ? 0.5949 0.5723 0.7954 0.0193  -0.0098 0.0992  290 LYS A CE  
2039 N  NZ  . LYS A 310 ? 0.7168 0.6849 0.9377 0.0220  -0.0159 0.1072  290 LYS A NZ  
2040 N  N   . ILE A 311 ? 0.2802 0.2575 0.4332 0.0124  0.0124  0.0393  291 ILE A N   
2041 C  CA  . ILE A 311 ? 0.2908 0.2642 0.4399 0.0115  0.0148  0.0276  291 ILE A CA  
2042 C  C   . ILE A 311 ? 0.2856 0.2510 0.4450 0.0150  0.0143  0.0196  291 ILE A C   
2043 O  O   . ILE A 311 ? 0.2905 0.2593 0.4529 0.0191  0.0151  0.0181  291 ILE A O   
2044 C  CB  . ILE A 311 ? 0.2771 0.2583 0.4124 0.0116  0.0181  0.0224  291 ILE A CB  
2045 C  CG1 . ILE A 311 ? 0.3140 0.3027 0.4394 0.0099  0.0185  0.0290  291 ILE A CG1 
2046 C  CG2 . ILE A 311 ? 0.2447 0.2226 0.3751 0.0101  0.0202  0.0122  291 ILE A CG2 
2047 C  CD1 . ILE A 311 ? 0.3194 0.3136 0.4327 0.0103  0.0205  0.0242  291 ILE A CD1 
2048 N  N   . PRO A 312 ? 0.2648 0.2200 0.4302 0.0137  0.0130  0.0139  292 PRO A N   
2049 C  CA  . PRO A 312 ? 0.3203 0.2682 0.4934 0.0181  0.0135  0.0033  292 PRO A CA  
2050 C  C   . PRO A 312 ? 0.2828 0.2389 0.4464 0.0206  0.0187  -0.0056 292 PRO A C   
2051 O  O   . PRO A 312 ? 0.2458 0.2078 0.3960 0.0174  0.0211  -0.0077 292 PRO A O   
2052 C  CB  . PRO A 312 ? 0.3229 0.2598 0.4982 0.0149  0.0110  -0.0032 292 PRO A CB  
2053 C  CG  . PRO A 312 ? 0.3172 0.2544 0.4936 0.0090  0.0079  0.0081  292 PRO A CG  
2054 C  CD  . PRO A 312 ? 0.3158 0.2668 0.4804 0.0083  0.0111  0.0152  292 PRO A CD  
2055 N  N   . ARG A 313 ? 0.2668 0.2239 0.4389 0.0264  0.0203  -0.0100 293 ARG A N   
2056 C  CA  . ARG A 313 ? 0.2426 0.2103 0.4081 0.0284  0.0256  -0.0159 293 ARG A CA  
2057 C  C   . ARG A 313 ? 0.2185 0.1862 0.3720 0.0264  0.0292  -0.0265 293 ARG A C   
2058 O  O   . ARG A 313 ? 0.2467 0.2239 0.3898 0.0247  0.0329  -0.0278 293 ARG A O   
2059 C  CB  . ARG A 313 ? 0.2478 0.2178 0.4276 0.0356  0.0270  -0.0191 293 ARG A CB  
2060 C  CG  . ARG A 313 ? 0.2337 0.2173 0.4097 0.0372  0.0326  -0.0232 293 ARG A CG  
2061 C  CD  . ARG A 313 ? 0.2816 0.2698 0.4747 0.0447  0.0341  -0.0252 293 ARG A CD  
2062 N  NE  . ARG A 313 ? 0.3199 0.3089 0.5241 0.0461  0.0286  -0.0138 293 ARG A NE  
2063 C  CZ  . ARG A 313 ? 0.3295 0.3230 0.5509 0.0525  0.0278  -0.0123 293 ARG A CZ  
2064 N  NH1 . ARG A 313 ? 0.3037 0.3014 0.5344 0.0589  0.0331  -0.0220 293 ARG A NH1 
2065 N  NH2 . ARG A 313 ? 0.3008 0.2956 0.5302 0.0529  0.0217  -0.0006 293 ARG A NH2 
2066 N  N   . ASP A 314 ? 0.2573 0.2143 0.4119 0.0260  0.0275  -0.0337 294 ASP A N   
2067 C  CA  . ASP A 314 ? 0.2855 0.2431 0.4273 0.0241  0.0302  -0.0441 294 ASP A CA  
2068 C  C   . ASP A 314 ? 0.2582 0.2150 0.3886 0.0170  0.0273  -0.0402 294 ASP A C   
2069 O  O   . ASP A 314 ? 0.2833 0.2392 0.4034 0.0147  0.0277  -0.0478 294 ASP A O   
2070 C  CB  . ASP A 314 ? 0.3163 0.2632 0.4635 0.0277  0.0295  -0.0566 294 ASP A CB  
2071 C  CG  . ASP A 314 ? 0.3889 0.3210 0.5496 0.0271  0.0226  -0.0535 294 ASP A CG  
2072 O  OD1 . ASP A 314 ? 0.3759 0.3067 0.5379 0.0219  0.0185  -0.0422 294 ASP A OD1 
2073 O  OD2 . ASP A 314 ? 0.4263 0.3482 0.5972 0.0320  0.0214  -0.0623 294 ASP A OD2 
2074 N  N   . CYS A 315 ? 0.2296 0.1881 0.3615 0.0141  0.0247  -0.0288 295 CYS A N   
2075 C  CA  . CYS A 315 ? 0.2193 0.1786 0.3430 0.0084  0.0223  -0.0245 295 CYS A CA  
2076 C  C   . CYS A 315 ? 0.2253 0.1948 0.3401 0.0071  0.0245  -0.0181 295 CYS A C   
2077 O  O   . CYS A 315 ? 0.2224 0.1976 0.3383 0.0098  0.0268  -0.0156 295 CYS A O   
2078 C  CB  . CYS A 315 ? 0.2560 0.2091 0.3898 0.0058  0.0175  -0.0164 295 CYS A CB  
2079 S  SG  . CYS A 315 ? 0.2865 0.2245 0.4315 0.0052  0.0126  -0.0236 295 CYS A SG  
2080 N  N   . ILE A 316 ? 0.1969 0.1685 0.3038 0.0031  0.0232  -0.0157 296 ILE A N   
2081 C  CA  . ILE A 316 ? 0.1946 0.1737 0.2940 0.0023  0.0244  -0.0100 296 ILE A CA  
2082 C  C   . ILE A 316 ? 0.2512 0.2311 0.3537 0.0006  0.0221  -0.0019 296 ILE A C   
2083 O  O   . ILE A 316 ? 0.2700 0.2468 0.3761 -0.0023 0.0195  -0.0014 296 ILE A O   
2084 C  CB  . ILE A 316 ? 0.2158 0.1982 0.3036 -0.0001 0.0253  -0.0137 296 ILE A CB  
2085 C  CG1 . ILE A 316 ? 0.2535 0.2373 0.3374 0.0012  0.0286  -0.0212 296 ILE A CG1 
2086 C  CG2 . ILE A 316 ? 0.2452 0.2331 0.3272 -0.0004 0.0258  -0.0083 296 ILE A CG2 
2087 C  CD1 . ILE A 316 ? 0.2696 0.2558 0.3419 -0.0018 0.0287  -0.0249 296 ILE A CD1 
2088 N  N   . ALA A 317 ? 0.1668 0.1519 0.2678 0.0021  0.0229  0.0043  297 ALA A N   
2089 C  CA  . ALA A 317 ? 0.1553 0.1440 0.2579 0.0011  0.0221  0.0119  297 ALA A CA  
2090 C  C   . ALA A 317 ? 0.1946 0.1887 0.2881 0.0013  0.0231  0.0122  297 ALA A C   
2091 O  O   . ALA A 317 ? 0.1822 0.1768 0.2689 0.0022  0.0240  0.0087  297 ALA A O   
2092 C  CB  . ALA A 317 ? 0.2262 0.2173 0.3332 0.0031  0.0221  0.0191  297 ALA A CB  
2093 N  N   . PHE A 318 ? 0.1611 0.1593 0.2561 0.0004  0.0229  0.0170  298 PHE A N   
2094 C  CA  . PHE A 318 ? 0.1535 0.1567 0.2420 0.0017  0.0238  0.0173  298 PHE A CA  
2095 C  C   . PHE A 318 ? 0.1698 0.1806 0.2598 0.0038  0.0256  0.0239  298 PHE A C   
2096 O  O   . PHE A 318 ? 0.2004 0.2146 0.2984 0.0019  0.0257  0.0295  298 PHE A O   
2097 C  CB  . PHE A 318 ? 0.1620 0.1649 0.2507 -0.0008 0.0220  0.0151  298 PHE A CB  
2098 C  CG  . PHE A 318 ? 0.1622 0.1596 0.2459 -0.0026 0.0207  0.0088  298 PHE A CG  
2099 C  CD1 . PHE A 318 ? 0.1804 0.1730 0.2675 -0.0050 0.0193  0.0051  298 PHE A CD1 
2100 C  CD2 . PHE A 318 ? 0.2164 0.2137 0.2921 -0.0016 0.0212  0.0064  298 PHE A CD2 
2101 C  CE1 . PHE A 318 ? 0.2473 0.2367 0.3281 -0.0060 0.0193  -0.0014 298 PHE A CE1 
2102 C  CE2 . PHE A 318 ? 0.1786 0.1731 0.2492 -0.0035 0.0209  0.0018  298 PHE A CE2 
2103 C  CZ  . PHE A 318 ? 0.2121 0.2036 0.2843 -0.0055 0.0204  -0.0024 298 PHE A CZ  
2104 N  N   . GLN A 319 ? 0.1387 0.1526 0.2211 0.0075  0.0271  0.0232  299 GLN A N   
2105 C  CA  . GLN A 319 ? 0.1602 0.1829 0.2411 0.0105  0.0296  0.0279  299 GLN A CA  
2106 C  C   . GLN A 319 ? 0.1553 0.1817 0.2331 0.0133  0.0307  0.0255  299 GLN A C   
2107 O  O   . GLN A 319 ? 0.1860 0.2069 0.2590 0.0142  0.0291  0.0200  299 GLN A O   
2108 C  CB  . GLN A 319 ? 0.1982 0.2221 0.2716 0.0134  0.0300  0.0280  299 GLN A CB  
2109 C  CG  . GLN A 319 ? 0.2046 0.2281 0.2830 0.0117  0.0291  0.0335  299 GLN A CG  
2110 C  CD  . GLN A 319 ? 0.2391 0.2652 0.3098 0.0144  0.0283  0.0342  299 GLN A CD  
2111 O  OE1 . GLN A 319 ? 0.2322 0.2536 0.2989 0.0150  0.0261  0.0287  299 GLN A OE1 
2112 N  NE2 . GLN A 319 ? 0.2067 0.2415 0.2751 0.0157  0.0300  0.0413  299 GLN A NE2 
2113 N  N   . THR A 320 ? 0.1606 0.1970 0.2426 0.0148  0.0336  0.0304  300 THR A N   
2114 C  CA  . THR A 320 ? 0.1790 0.2204 0.2602 0.0189  0.0351  0.0283  300 THR A CA  
2115 C  C   . THR A 320 ? 0.1836 0.2255 0.2539 0.0249  0.0367  0.0236  300 THR A C   
2116 O  O   . THR A 320 ? 0.2336 0.2782 0.2977 0.0262  0.0381  0.0248  300 THR A O   
2117 C  CB  . THR A 320 ? 0.2378 0.2924 0.3285 0.0191  0.0385  0.0353  300 THR A CB  
2118 O  OG1 . THR A 320 ? 0.2212 0.2828 0.3120 0.0184  0.0414  0.0419  300 THR A OG1 
2119 C  CG2 . THR A 320 ? 0.2401 0.2934 0.3422 0.0133  0.0352  0.0380  300 THR A CG2 
2120 N  N   . GLY A 321 ? 0.1721 0.2109 0.2400 0.0287  0.0358  0.0180  301 GLY A N   
2121 C  CA  . GLY A 321 ? 0.2146 0.2525 0.2731 0.0350  0.0366  0.0121  301 GLY A CA  
2122 C  C   . GLY A 321 ? 0.1918 0.2389 0.2532 0.0417  0.0403  0.0109  301 GLY A C   
2123 O  O   . GLY A 321 ? 0.2092 0.2639 0.2813 0.0412  0.0419  0.0156  301 GLY A O   
2124 N  N   . GLU A 322 ? 0.1855 0.2316 0.2378 0.0484  0.0413  0.0040  302 GLU A N   
2125 C  CA  . GLU A 322 ? 0.1819 0.2381 0.2358 0.0568  0.0461  0.0014  302 GLU A CA  
2126 C  C   . GLU A 322 ? 0.2059 0.2589 0.2706 0.0590  0.0440  0.0003  302 GLU A C   
2127 O  O   . GLU A 322 ? 0.2270 0.2925 0.3003 0.0639  0.0483  0.0024  302 GLU A O   
2128 C  CB  . GLU A 322 ? 0.2507 0.3038 0.2909 0.0638  0.0464  -0.0082 302 GLU A CB  
2129 C  CG  . GLU A 322 ? 0.3106 0.3720 0.3395 0.0633  0.0494  -0.0063 302 GLU A CG  
2130 C  CD  . GLU A 322 ? 0.3843 0.4437 0.3982 0.0707  0.0493  -0.0170 302 GLU A CD  
2131 O  OE1 . GLU A 322 ? 0.4813 0.5257 0.4885 0.0691  0.0426  -0.0239 302 GLU A OE1 
2132 O  OE2 . GLU A 322 ? 0.4638 0.5371 0.4726 0.0779  0.0560  -0.0187 302 GLU A OE2 
2133 N  N   . ALA A 323 ? 0.2030 0.2408 0.2682 0.0555  0.0373  -0.0021 303 ALA A N   
2134 C  CA  . ALA A 323 ? 0.2157 0.2502 0.2907 0.0573  0.0343  -0.0018 303 ALA A CA  
2135 C  C   . ALA A 323 ? 0.2316 0.2766 0.3188 0.0529  0.0351  0.0069  303 ALA A C   
2136 O  O   . ALA A 323 ? 0.2050 0.2574 0.3030 0.0569  0.0357  0.0088  303 ALA A O   
2137 C  CB  . ALA A 323 ? 0.2381 0.2551 0.3103 0.0532  0.0270  -0.0042 303 ALA A CB  
2138 N  N   . LEU A 324 ? 0.2207 0.2663 0.3074 0.0447  0.0346  0.0118  304 LEU A N   
2139 C  CA  . LEU A 324 ? 0.1984 0.2530 0.2965 0.0398  0.0345  0.0192  304 LEU A CA  
2140 C  C   . LEU A 324 ? 0.2277 0.3005 0.3338 0.0436  0.0410  0.0238  304 LEU A C   
2141 O  O   . LEU A 324 ? 0.1988 0.2818 0.3181 0.0432  0.0411  0.0288  304 LEU A O   
2142 C  CB  . LEU A 324 ? 0.1909 0.2401 0.2865 0.0311  0.0324  0.0220  304 LEU A CB  
2143 C  CG  . LEU A 324 ? 0.2282 0.2827 0.3347 0.0246  0.0302  0.0280  304 LEU A CG  
2144 C  CD1 . LEU A 324 ? 0.2549 0.2981 0.3571 0.0174  0.0257  0.0266  304 LEU A CD1 
2145 C  CD2 . LEU A 324 ? 0.2942 0.3617 0.4082 0.0235  0.0348  0.0345  304 LEU A CD2 
2146 N  N   . GLU A 325 ? 0.1740 0.2525 0.2724 0.0468  0.0465  0.0230  305 GLU A N   
2147 C  CA  . GLU A 325 ? 0.2152 0.3134 0.3201 0.0507  0.0538  0.0280  305 GLU A CA  
2148 C  C   . GLU A 325 ? 0.2175 0.3238 0.3303 0.0596  0.0562  0.0249  305 GLU A C   
2149 O  O   . GLU A 325 ? 0.2143 0.3368 0.3416 0.0604  0.0594  0.0312  305 GLU A O   
2150 C  CB  . GLU A 325 ? 0.2211 0.3241 0.3130 0.0537  0.0591  0.0268  305 GLU A CB  
2151 C  CG  . GLU A 325 ? 0.2391 0.3647 0.3355 0.0586  0.0680  0.0321  305 GLU A CG  
2152 C  CD  . GLU A 325 ? 0.3225 0.4550 0.4046 0.0605  0.0730  0.0328  305 GLU A CD  
2153 O  OE1 . GLU A 325 ? 0.2906 0.4122 0.3632 0.0555  0.0691  0.0330  305 GLU A OE1 
2154 O  OE2 . GLU A 325 ? 0.3808 0.5313 0.4613 0.0672  0.0811  0.0338  305 GLU A OE2 
2155 N  N   . ARG A 326 ? 0.2032 0.2982 0.3081 0.0664  0.0542  0.0152  306 ARG A N   
2156 C  CA  . ARG A 326 ? 0.2385 0.3393 0.3515 0.0763  0.0561  0.0112  306 ARG A CA  
2157 C  C   . ARG A 326 ? 0.2297 0.3309 0.3590 0.0735  0.0508  0.0164  306 ARG A C   
2158 O  O   . ARG A 326 ? 0.1840 0.3003 0.3278 0.0789  0.0539  0.0194  306 ARG A O   
2159 C  CB  . ARG A 326 ? 0.1952 0.2804 0.2968 0.0835  0.0536  -0.0006 306 ARG A CB  
2160 C  CG  . ARG A 326 ? 0.2521 0.3414 0.3629 0.0954  0.0553  -0.0062 306 ARG A CG  
2161 C  CD  . ARG A 326 ? 0.3861 0.4991 0.5009 0.1038  0.0660  -0.0059 306 ARG A CD  
2162 N  NE  . ARG A 326 ? 0.5291 0.6437 0.6256 0.1073  0.0712  -0.0125 306 ARG A NE  
2163 C  CZ  . ARG A 326 ? 0.5606 0.6714 0.6477 0.1182  0.0735  -0.0249 306 ARG A CZ  
2164 N  NH1 . ARG A 326 ? 0.4898 0.5951 0.5857 0.1278  0.0717  -0.0323 306 ARG A NH1 
2165 N  NH2 . ARG A 326 ? 0.5352 0.6475 0.6035 0.1198  0.0769  -0.0305 306 ARG A NH2 
2166 N  N   . ILE A 327 ? 0.2087 0.2949 0.3357 0.0653  0.0428  0.0178  307 ILE A N   
2167 C  CA  . ILE A 327 ? 0.1772 0.2634 0.3169 0.0619  0.0366  0.0229  307 ILE A CA  
2168 C  C   . ILE A 327 ? 0.2009 0.3055 0.3552 0.0576  0.0387  0.0319  307 ILE A C   
2169 O  O   . ILE A 327 ? 0.2335 0.3474 0.4031 0.0591  0.0363  0.0360  307 ILE A O   
2170 C  CB  . ILE A 327 ? 0.1813 0.2498 0.3126 0.0532  0.0287  0.0226  307 ILE A CB  
2171 C  CG1 . ILE A 327 ? 0.1950 0.2473 0.3187 0.0577  0.0248  0.0160  307 ILE A CG1 
2172 C  CG2 . ILE A 327 ? 0.2115 0.2831 0.3530 0.0467  0.0225  0.0292  307 ILE A CG2 
2173 C  CD1 . ILE A 327 ? 0.1813 0.2177 0.2940 0.0496  0.0194  0.0154  307 ILE A CD1 
2174 N  N   . THR A 328 ? 0.2216 0.3320 0.3729 0.0519  0.0426  0.0357  308 THR A N   
2175 C  CA  . THR A 328 ? 0.1805 0.3074 0.3468 0.0465  0.0441  0.0451  308 THR A CA  
2176 C  C   . THR A 328 ? 0.1971 0.3459 0.3716 0.0532  0.0538  0.0486  308 THR A C   
2177 O  O   . THR A 328 ? 0.2217 0.3860 0.4085 0.0481  0.0564  0.0578  308 THR A O   
2178 C  CB  . THR A 328 ? 0.1748 0.2953 0.3364 0.0358  0.0420  0.0488  308 THR A CB  
2179 O  OG1 . THR A 328 ? 0.2239 0.3440 0.3736 0.0374  0.0479  0.0475  308 THR A OG1 
2180 C  CG2 . THR A 328 ? 0.2198 0.3206 0.3726 0.0299  0.0336  0.0445  308 THR A CG2 
2181 N  N   . GLY A 329 ? 0.1862 0.3372 0.3544 0.0644  0.0592  0.0416  309 GLY A N   
2182 C  CA  . GLY A 329 ? 0.2183 0.3923 0.3934 0.0723  0.0695  0.0438  309 GLY A CA  
2183 C  C   . GLY A 329 ? 0.2903 0.4751 0.4596 0.0679  0.0762  0.0501  309 GLY A C   
2184 O  O   . GLY A 329 ? 0.2505 0.4589 0.4306 0.0698  0.0842  0.0575  309 GLY A O   
2185 N  N   . GLY A 330 ? 0.2027 0.3718 0.3562 0.0619  0.0732  0.0484  310 GLY A N   
2186 C  CA  . GLY A 330 ? 0.2290 0.4066 0.3773 0.0573  0.0781  0.0556  310 GLY A CA  
2187 C  C   . GLY A 330 ? 0.3007 0.4826 0.4631 0.0454  0.0750  0.0677  310 GLY A C   
2188 O  O   . GLY A 330 ? 0.2892 0.4778 0.4496 0.0408  0.0784  0.0757  310 GLY A O   
2189 N  N   . LYS A 331 ? 0.1908 0.3687 0.3673 0.0402  0.0679  0.0697  311 LYS A N   
2190 C  CA  . LYS A 331 ? 0.1891 0.3679 0.3783 0.0284  0.0634  0.0794  311 LYS A CA  
2191 C  C   . LYS A 331 ? 0.1854 0.3439 0.3619 0.0217  0.0584  0.0774  311 LYS A C   
2192 O  O   . LYS A 331 ? 0.2148 0.3747 0.3970 0.0139  0.0577  0.0857  311 LYS A O   
2193 C  CB  . LYS A 331 ? 0.2238 0.4016 0.4286 0.0244  0.0556  0.0803  311 LYS A CB  
2194 C  CG  . LYS A 331 ? 0.2619 0.4619 0.4844 0.0302  0.0597  0.0842  311 LYS A CG  
2195 C  CD  . LYS A 331 ? 0.3078 0.5237 0.5531 0.0212  0.0580  0.0967  311 LYS A CD  
2196 C  CE  . LYS A 331 ? 0.4063 0.6427 0.6724 0.0258  0.0590  0.1002  311 LYS A CE  
2197 N  NZ  . LYS A 331 ? 0.4588 0.7105 0.7221 0.0393  0.0701  0.0970  311 LYS A NZ  
2198 N  N   . PHE A 332 ? 0.1854 0.3253 0.3464 0.0245  0.0547  0.0669  312 PHE A N   
2199 C  CA  . PHE A 332 ? 0.1831 0.3068 0.3307 0.0209  0.0520  0.0640  312 PHE A CA  
2200 C  C   . PHE A 332 ? 0.2428 0.3663 0.3737 0.0287  0.0573  0.0586  312 PHE A C   
2201 O  O   . PHE A 332 ? 0.2435 0.3720 0.3706 0.0371  0.0606  0.0529  312 PHE A O   
2202 C  CB  . PHE A 332 ? 0.1741 0.2782 0.3170 0.0172  0.0438  0.0567  312 PHE A CB  
2203 C  CG  . PHE A 332 ? 0.1989 0.3001 0.3542 0.0083  0.0375  0.0607  312 PHE A CG  
2204 C  CD1 . PHE A 332 ? 0.2109 0.3244 0.3817 0.0031  0.0384  0.0706  312 PHE A CD1 
2205 C  CD2 . PHE A 332 ? 0.2968 0.3834 0.4481 0.0049  0.0303  0.0544  312 PHE A CD2 
2206 C  CE1 . PHE A 332 ? 0.2647 0.3743 0.4473 -0.0055 0.0313  0.0732  312 PHE A CE1 
2207 C  CE2 . PHE A 332 ? 0.3487 0.4324 0.5096 -0.0031 0.0239  0.0564  312 PHE A CE2 
2208 C  CZ  . PHE A 332 ? 0.2997 0.3940 0.4764 -0.0083 0.0239  0.0653  312 PHE A CZ  
2209 N  N   . LYS A 333 ? 0.2035 0.3210 0.3251 0.0260  0.0573  0.0602  313 LYS A N   
2210 C  CA  . LYS A 333 ? 0.2194 0.3402 0.3257 0.0320  0.0619  0.0574  313 LYS A CA  
2211 C  C   . LYS A 333 ? 0.2028 0.3054 0.2962 0.0307  0.0568  0.0508  313 LYS A C   
2212 O  O   . LYS A 333 ? 0.2098 0.3022 0.3069 0.0240  0.0521  0.0532  313 LYS A O   
2213 C  CB  . LYS A 333 ? 0.2673 0.4037 0.3753 0.0301  0.0675  0.0688  313 LYS A CB  
2214 C  CG  . LYS A 333 ? 0.5450 0.7004 0.6461 0.0384  0.0764  0.0689  313 LYS A CG  
2215 C  CD  . LYS A 333 ? 0.3999 0.5698 0.5152 0.0421  0.0805  0.0699  313 LYS A CD  
2216 C  CE  . LYS A 333 ? 0.5945 0.7871 0.7053 0.0506  0.0910  0.0713  313 LYS A CE  
2217 N  NZ  . LYS A 333 ? 0.6560 0.8662 0.7851 0.0535  0.0955  0.0747  313 LYS A NZ  
2218 N  N   . ALA A 334 ? 0.2080 0.3072 0.2872 0.0373  0.0578  0.0422  314 ALA A N   
2219 C  CA  . ALA A 334 ? 0.2476 0.3350 0.3143 0.0364  0.0541  0.0380  314 ALA A CA  
2220 C  C   . ALA A 334 ? 0.2068 0.3043 0.2671 0.0361  0.0574  0.0453  314 ALA A C   
2221 O  O   . ALA A 334 ? 0.2693 0.3819 0.3248 0.0411  0.0636  0.0473  314 ALA A O   
2222 C  CB  . ALA A 334 ? 0.2274 0.3065 0.2824 0.0427  0.0525  0.0261  314 ALA A CB  
2223 N  N   . VAL A 335 ? 0.2060 0.2965 0.2667 0.0307  0.0536  0.0498  315 VAL A N   
2224 C  CA  . VAL A 335 ? 0.1960 0.2959 0.2539 0.0290  0.0556  0.0600  315 VAL A CA  
2225 C  C   . VAL A 335 ? 0.2079 0.3011 0.2513 0.0307  0.0519  0.0554  315 VAL A C   
2226 O  O   . VAL A 335 ? 0.2286 0.3074 0.2727 0.0287  0.0463  0.0497  315 VAL A O   
2227 C  CB  . VAL A 335 ? 0.2183 0.3159 0.2916 0.0212  0.0533  0.0708  315 VAL A CB  
2228 C  CG1 . VAL A 335 ? 0.2151 0.3214 0.2862 0.0193  0.0545  0.0829  315 VAL A CG1 
2229 C  CG2 . VAL A 335 ? 0.1876 0.2930 0.2762 0.0187  0.0560  0.0755  315 VAL A CG2 
2230 N  N   . PRO A 336 ? 0.2036 0.3081 0.2340 0.0342  0.0547  0.0580  316 PRO A N   
2231 C  CA  . PRO A 336 ? 0.2529 0.3516 0.2692 0.0357  0.0499  0.0532  316 PRO A CA  
2232 C  C   . PRO A 336 ? 0.2609 0.3512 0.2845 0.0299  0.0440  0.0600  316 PRO A C   
2233 O  O   . PRO A 336 ? 0.2084 0.3021 0.2430 0.0256  0.0446  0.0719  316 PRO A O   
2234 C  CB  . PRO A 336 ? 0.2895 0.4052 0.2908 0.0399  0.0546  0.0570  316 PRO A CB  
2235 C  CG  . PRO A 336 ? 0.3476 0.4774 0.3538 0.0427  0.0630  0.0598  316 PRO A CG  
2236 C  CD  . PRO A 336 ? 0.2249 0.3494 0.2523 0.0370  0.0624  0.0653  316 PRO A CD  
2237 N  N   . HIS A 337 ? 0.2191 0.2986 0.2377 0.0301  0.0380  0.0526  317 HIS A N   
2238 C  CA  . HIS A 337 ? 0.2246 0.2959 0.2518 0.0258  0.0324  0.0572  317 HIS A CA  
2239 C  C   . HIS A 337 ? 0.2797 0.3458 0.2974 0.0272  0.0265  0.0502  317 HIS A C   
2240 O  O   . HIS A 337 ? 0.2233 0.2885 0.2293 0.0305  0.0258  0.0403  317 HIS A O   
2241 C  CB  . HIS A 337 ? 0.2048 0.2648 0.2475 0.0223  0.0315  0.0550  317 HIS A CB  
2242 C  CG  . HIS A 337 ? 0.1890 0.2406 0.2295 0.0237  0.0308  0.0428  317 HIS A CG  
2243 N  ND1 . HIS A 337 ? 0.2053 0.2591 0.2444 0.0259  0.0345  0.0383  317 HIS A ND1 
2244 C  CD2 . HIS A 337 ? 0.2268 0.2687 0.2670 0.0230  0.0265  0.0353  317 HIS A CD2 
2245 C  CE1 . HIS A 337 ? 0.1912 0.2356 0.2290 0.0264  0.0321  0.0289  317 HIS A CE1 
2246 N  NE2 . HIS A 337 ? 0.1749 0.2124 0.2130 0.0243  0.0275  0.0271  317 HIS A NE2 
2247 N  N   . PHE A 338 ? 0.2239 0.2862 0.2485 0.0245  0.0215  0.0554  318 PHE A N   
2248 C  CA  . PHE A 338 ? 0.2224 0.2796 0.2430 0.0248  0.0151  0.0493  318 PHE A CA  
2249 C  C   . PHE A 338 ? 0.3050 0.3553 0.3416 0.0219  0.0115  0.0529  318 PHE A C   
2250 O  O   . PHE A 338 ? 0.2221 0.2713 0.2707 0.0201  0.0131  0.0607  318 PHE A O   
2251 C  CB  . PHE A 338 ? 0.2337 0.3000 0.2388 0.0268  0.0116  0.0516  318 PHE A CB  
2252 C  CG  . PHE A 338 ? 0.2630 0.3377 0.2701 0.0256  0.0106  0.0663  318 PHE A CG  
2253 C  CD1 . PHE A 338 ? 0.2917 0.3637 0.3081 0.0238  0.0042  0.0723  318 PHE A CD1 
2254 C  CD2 . PHE A 338 ? 0.3145 0.4008 0.3148 0.0265  0.0160  0.0747  318 PHE A CD2 
2255 C  CE1 . PHE A 338 ? 0.3085 0.3874 0.3276 0.0228  0.0024  0.0870  318 PHE A CE1 
2256 C  CE2 . PHE A 338 ? 0.3609 0.4551 0.3633 0.0247  0.0147  0.0900  318 PHE A CE2 
2257 C  CZ  . PHE A 338 ? 0.3189 0.4085 0.3307 0.0229  0.0075  0.0963  318 PHE A CZ  
2258 N  N   . VAL A 339 ? 0.2306 0.2761 0.2686 0.0216  0.0066  0.0468  319 VAL A N   
2259 C  CA  . VAL A 339 ? 0.2266 0.2673 0.2802 0.0200  0.0037  0.0488  319 VAL A CA  
2260 C  C   . VAL A 339 ? 0.2852 0.3309 0.3377 0.0205  -0.0031 0.0531  319 VAL A C   
2261 O  O   . VAL A 339 ? 0.2689 0.3172 0.3103 0.0209  -0.0071 0.0480  319 VAL A O   
2262 C  CB  . VAL A 339 ? 0.2431 0.2762 0.3029 0.0187  0.0044  0.0392  319 VAL A CB  
2263 C  CG1 . VAL A 339 ? 0.3080 0.3387 0.3836 0.0181  0.0024  0.0408  319 VAL A CG1 
2264 C  CG2 . VAL A 339 ? 0.2809 0.3095 0.3416 0.0180  0.0101  0.0358  319 VAL A CG2 
2265 N  N   . ARG A 340 ? 0.2677 0.3141 0.3325 0.0205  -0.0053 0.0622  320 ARG A N   
2266 C  CA  . ARG A 340 ? 0.3558 0.4076 0.4228 0.0212  -0.0125 0.0682  320 ARG A CA  
2267 C  C   . ARG A 340 ? 0.2940 0.3416 0.3792 0.0214  -0.0149 0.0656  320 ARG A C   
2268 O  O   . ARG A 340 ? 0.2933 0.3346 0.3923 0.0218  -0.0112 0.0653  320 ARG A O   
2269 C  CB  . ARG A 340 ? 0.3744 0.4309 0.4428 0.0216  -0.0138 0.0825  320 ARG A CB  
2270 C  CG  . ARG A 340 ? 0.4301 0.4933 0.4996 0.0224  -0.0221 0.0905  320 ARG A CG  
2271 C  CD  . ARG A 340 ? 0.4749 0.5444 0.5408 0.0222  -0.0230 0.1057  320 ARG A CD  
2272 N  NE  . ARG A 340 ? 0.4865 0.5623 0.5548 0.0230  -0.0319 0.1151  320 ARG A NE  
2273 C  CZ  . ARG A 340 ? 0.6098 0.6935 0.6726 0.0227  -0.0351 0.1298  320 ARG A CZ  
2274 N  NH1 . ARG A 340 ? 0.4684 0.5556 0.5233 0.0213  -0.0294 0.1373  320 ARG A NH1 
2275 N  NH2 . ARG A 340 ? 0.5747 0.6641 0.6408 0.0235  -0.0444 0.1382  320 ARG A NH2 
2276 N  N   . GLY A 341 ? 0.2405 0.2926 0.3259 0.0213  -0.0210 0.0631  321 GLY A N   
2277 C  CA  . GLY A 341 ? 0.2844 0.3365 0.3884 0.0219  -0.0234 0.0621  321 GLY A CA  
2278 C  C   . GLY A 341 ? 0.3298 0.3858 0.4463 0.0243  -0.0287 0.0734  321 GLY A C   
2279 O  O   . GLY A 341 ? 0.3498 0.4073 0.4611 0.0249  -0.0301 0.0831  321 GLY A O   
2280 N  N   . ALA A 342 ? 0.2622 0.3206 0.3964 0.0259  -0.0315 0.0728  322 ALA A N   
2281 C  CA  . ALA A 342 ? 0.2747 0.3368 0.4243 0.0290  -0.0373 0.0833  322 ALA A CA  
2282 C  C   . ALA A 342 ? 0.2469 0.3197 0.3903 0.0281  -0.0472 0.0885  322 ALA A C   
2283 O  O   . ALA A 342 ? 0.3225 0.3999 0.4614 0.0257  -0.0501 0.0814  322 ALA A O   
2284 C  CB  . ALA A 342 ? 0.3241 0.3849 0.4981 0.0324  -0.0350 0.0799  322 ALA A CB  
2285 N  N   . ARG A 343 ? 0.2435 0.3200 0.3862 0.0294  -0.0532 0.1012  323 ARG A N   
2286 C  CA  . ARG A 343 ? 0.3015 0.3890 0.4382 0.0286  -0.0639 0.1072  323 ARG A CA  
2287 C  C   . ARG A 343 ? 0.3523 0.4458 0.5115 0.0304  -0.0695 0.1066  323 ARG A C   
2288 O  O   . ARG A 343 ? 0.3387 0.4294 0.5211 0.0344  -0.0669 0.1087  323 ARG A O   
2289 C  CB  . ARG A 343 ? 0.2767 0.3675 0.4092 0.0297  -0.0688 0.1231  323 ARG A CB  
2290 C  CG  . ARG A 343 ? 0.3621 0.4532 0.4686 0.0274  -0.0651 0.1253  323 ARG A CG  
2291 C  CD  . ARG A 343 ? 0.3692 0.4627 0.4767 0.0281  -0.0678 0.1430  323 ARG A CD  
2292 N  NE  . ARG A 343 ? 0.3401 0.4227 0.4672 0.0298  -0.0620 0.1469  323 ARG A NE  
2293 C  CZ  . ARG A 343 ? 0.4451 0.5258 0.5828 0.0307  -0.0648 0.1626  323 ARG A CZ  
2294 N  NH1 . ARG A 343 ? 0.4725 0.5628 0.6034 0.0302  -0.0730 0.1775  323 ARG A NH1 
2295 N  NH2 . ARG A 343 ? 0.3800 0.4485 0.5356 0.0318  -0.0597 0.1635  323 ARG A NH2 
2296 N  N   . ALA A 344 ? 0.2857 0.3881 0.4388 0.0275  -0.0772 0.1034  324 ALA A N   
2297 C  CA  . ALA A 344 ? 0.3833 0.4942 0.5590 0.0284  -0.0830 0.1033  324 ALA A CA  
2298 C  C   . ALA A 344 ? 0.3450 0.4608 0.5416 0.0335  -0.0888 0.1166  324 ALA A C   
2299 O  O   . ALA A 344 ? 0.3479 0.4665 0.5711 0.0374  -0.0876 0.1164  324 ALA A O   
2300 C  CB  . ALA A 344 ? 0.4838 0.6037 0.6485 0.0236  -0.0929 0.0997  324 ALA A CB  
2301 N  N   . GLU A 345 ? 0.3335 0.4508 0.5189 0.0339  -0.0951 0.1288  325 GLU A N   
2302 C  CA  . GLU A 345 ? 0.3365 0.4583 0.5419 0.0385  -0.1026 0.1432  325 GLU A CA  
2303 C  C   . GLU A 345 ? 0.3286 0.4394 0.5548 0.0439  -0.0949 0.1459  325 GLU A C   
2304 O  O   . GLU A 345 ? 0.3808 0.4934 0.6308 0.0491  -0.1000 0.1553  325 GLU A O   
2305 C  CB  . GLU A 345 ? 0.4582 0.5854 0.6443 0.0368  -0.1115 0.1569  325 GLU A CB  
2306 C  CG  . GLU A 345 ? 0.4648 0.5839 0.6295 0.0351  -0.1043 0.1601  325 GLU A CG  
2307 C  CD  . GLU A 345 ? 0.5797 0.6987 0.7138 0.0304  -0.0998 0.1484  325 GLU A CD  
2308 O  OE1 . GLU A 345 ? 0.5298 0.6511 0.6609 0.0282  -0.1009 0.1357  325 GLU A OE1 
2309 O  OE2 . GLU A 345 ? 0.6317 0.7487 0.7460 0.0290  -0.0953 0.1522  325 GLU A OE2 
2310 N  N   . MET A 346 ? 0.3305 0.4294 0.5489 0.0430  -0.0835 0.1375  326 MET A N   
2311 C  CA  . MET A 346 ? 0.3879 0.4747 0.6245 0.0475  -0.0762 0.1370  326 MET A CA  
2312 C  C   . MET A 346 ? 0.5168 0.6023 0.7714 0.0506  -0.0689 0.1235  326 MET A C   
2313 O  O   . MET A 346 ? 0.5092 0.5850 0.7798 0.0552  -0.0631 0.1208  326 MET A O   
2314 C  CB  . MET A 346 ? 0.3913 0.4668 0.6101 0.0444  -0.0683 0.1355  326 MET A CB  
2315 C  CG  . MET A 346 ? 0.5355 0.6127 0.7383 0.0417  -0.0732 0.1501  326 MET A CG  
2316 S  SD  . MET A 346 ? 0.8144 0.8856 1.0409 0.0462  -0.0793 0.1683  326 MET A SD  
2317 C  CE  . MET A 346 ? 0.7479 0.8270 0.9494 0.0413  -0.0852 0.1859  326 MET A CE  
2318 N  N   . SER A 347 ? 0.3041 0.3993 0.5563 0.0480  -0.0691 0.1151  327 SER A N   
2319 C  CA  . SER A 347 ? 0.2394 0.3351 0.5033 0.0492  -0.0605 0.1022  327 SER A CA  
2320 C  C   . SER A 347 ? 0.3830 0.4920 0.6734 0.0534  -0.0651 0.1041  327 SER A C   
2321 O  O   . SER A 347 ? 0.4896 0.6112 0.7793 0.0499  -0.0720 0.1051  327 SER A O   
2322 C  CB  . SER A 347 ? 0.2660 0.3627 0.5093 0.0424  -0.0566 0.0919  327 SER A CB  
2323 O  OG  . SER A 347 ? 0.3788 0.4643 0.5999 0.0394  -0.0517 0.0898  327 SER A OG  
2324 N  N   . ALA A 348 ? 0.2617 0.3681 0.5766 0.0612  -0.0614 0.1039  328 ALA A N   
2325 C  CA  . ALA A 348 ? 0.2796 0.3990 0.6215 0.0664  -0.0641 0.1051  328 ALA A CA  
2326 C  C   . ALA A 348 ? 0.2990 0.4280 0.6491 0.0657  -0.0556 0.0933  328 ALA A C   
2327 O  O   . ALA A 348 ? 0.3020 0.4227 0.6469 0.0662  -0.0444 0.0829  328 ALA A O   
2328 C  CB  . ALA A 348 ? 0.3163 0.4250 0.6717 0.0734  -0.0615 0.1059  328 ALA A CB  
2329 N  N   . GLY A 349 ? 0.3317 0.4773 0.6910 0.0633  -0.0605 0.0945  329 GLY A N   
2330 C  CA  . GLY A 349 ? 0.3137 0.4706 0.6805 0.0609  -0.0531 0.0856  329 GLY A CA  
2331 C  C   . GLY A 349 ? 0.3146 0.4698 0.6561 0.0504  -0.0538 0.0815  329 GLY A C   
2332 O  O   . GLY A 349 ? 0.3676 0.5188 0.6897 0.0451  -0.0627 0.0860  329 GLY A O   
2333 N  N   . ARG A 350 ? 0.2349 0.3930 0.5759 0.0475  -0.0441 0.0723  330 ARG A N   
2334 C  CA  . ARG A 350 ? 0.1769 0.3329 0.4971 0.0377  -0.0440 0.0676  330 ARG A CA  
2335 C  C   . ARG A 350 ? 0.2042 0.3436 0.5040 0.0371  -0.0338 0.0598  330 ARG A C   
2336 O  O   . ARG A 350 ? 0.2405 0.3809 0.5415 0.0362  -0.0238 0.0527  330 ARG A O   
2337 C  CB  . ARG A 350 ? 0.2778 0.4510 0.6144 0.0336  -0.0419 0.0655  330 ARG A CB  
2338 C  CG  . ARG A 350 ? 0.4345 0.6094 0.7580 0.0229  -0.0496 0.0652  330 ARG A CG  
2339 C  CD  . ARG A 350 ? 0.4689 0.6626 0.8136 0.0183  -0.0489 0.0657  330 ARG A CD  
2340 N  NE  . ARG A 350 ? 0.6423 0.8354 0.9756 0.0075  -0.0577 0.0652  330 ARG A NE  
2341 C  CZ  . ARG A 350 ? 0.9055 1.1140 1.2560 0.0008  -0.0617 0.0675  330 ARG A CZ  
2342 N  NH1 . ARG A 350 ? 0.9203 1.1489 1.3005 0.0041  -0.0567 0.0710  330 ARG A NH1 
2343 N  NH2 . ARG A 350 ? 0.8688 1.0729 1.2074 -0.0092 -0.0708 0.0662  330 ARG A NH2 
2344 N  N   . ILE A 351 ? 0.1807 0.3059 0.4621 0.0374  -0.0365 0.0620  331 ILE A N   
2345 C  CA  . ILE A 351 ? 0.1626 0.2726 0.4278 0.0375  -0.0278 0.0560  331 ILE A CA  
2346 C  C   . ILE A 351 ? 0.1782 0.2828 0.4198 0.0295  -0.0275 0.0513  331 ILE A C   
2347 O  O   . ILE A 351 ? 0.2331 0.3360 0.4600 0.0257  -0.0355 0.0545  331 ILE A O   
2348 C  CB  . ILE A 351 ? 0.2016 0.3000 0.4613 0.0415  -0.0304 0.0616  331 ILE A CB  
2349 C  CG1 . ILE A 351 ? 0.2155 0.3174 0.5006 0.0499  -0.0318 0.0665  331 ILE A CG1 
2350 C  CG2 . ILE A 351 ? 0.2654 0.3494 0.5103 0.0409  -0.0219 0.0553  331 ILE A CG2 
2351 C  CD1 . ILE A 351 ? 0.2517 0.3545 0.5530 0.0553  -0.0215 0.0581  331 ILE A CD1 
2352 N  N   . ALA A 352 ? 0.1761 0.2779 0.4137 0.0275  -0.0184 0.0437  332 ALA A N   
2353 C  CA  . ALA A 352 ? 0.1832 0.2770 0.3995 0.0212  -0.0168 0.0390  332 ALA A CA  
2354 C  C   . ALA A 352 ? 0.1766 0.2567 0.3794 0.0230  -0.0103 0.0356  332 ALA A C   
2355 O  O   . ALA A 352 ? 0.1717 0.2489 0.3833 0.0282  -0.0049 0.0343  332 ALA A O   
2356 C  CB  . ALA A 352 ? 0.1577 0.2585 0.3792 0.0167  -0.0118 0.0345  332 ALA A CB  
2357 N  N   . ARG A 353 ? 0.1543 0.2260 0.3367 0.0188  -0.0112 0.0335  333 ARG A N   
2358 C  CA  . ARG A 353 ? 0.1601 0.2202 0.3302 0.0196  -0.0053 0.0304  333 ARG A CA  
2359 C  C   . ARG A 353 ? 0.1784 0.2350 0.3378 0.0150  -0.0009 0.0243  333 ARG A C   
2360 O  O   . ARG A 353 ? 0.2064 0.2630 0.3570 0.0107  -0.0052 0.0235  333 ARG A O   
2361 C  CB  . ARG A 353 ? 0.1576 0.2115 0.3139 0.0200  -0.0096 0.0349  333 ARG A CB  
2362 C  CG  . ARG A 353 ? 0.1909 0.2344 0.3359 0.0202  -0.0038 0.0325  333 ARG A CG  
2363 C  CD  . ARG A 353 ? 0.2391 0.2796 0.3734 0.0208  -0.0071 0.0386  333 ARG A CD  
2364 N  NE  . ARG A 353 ? 0.2512 0.2962 0.3736 0.0189  -0.0135 0.0404  333 ARG A NE  
2365 C  CZ  . ARG A 353 ? 0.2837 0.3261 0.3884 0.0173  -0.0135 0.0384  333 ARG A CZ  
2366 N  NH1 . ARG A 353 ? 0.2964 0.3326 0.3940 0.0171  -0.0075 0.0358  333 ARG A NH1 
2367 N  NH2 . ARG A 353 ? 0.2997 0.3463 0.3937 0.0162  -0.0199 0.0387  333 ARG A NH2 
2368 N  N   . ASN A 354 ? 0.1422 0.1954 0.3023 0.0159  0.0069  0.0198  334 ASN A N   
2369 C  CA  . ASN A 354 ? 0.1476 0.1973 0.2972 0.0116  0.0107  0.0154  334 ASN A CA  
2370 C  C   . ASN A 354 ? 0.1660 0.2051 0.3033 0.0123  0.0138  0.0132  334 ASN A C   
2371 O  O   . ASN A 354 ? 0.1642 0.1998 0.3055 0.0159  0.0165  0.0129  334 ASN A O   
2372 C  CB  . ASN A 354 ? 0.1378 0.1949 0.2970 0.0110  0.0170  0.0124  334 ASN A CB  
2373 C  CG  . ASN A 354 ? 0.1890 0.2591 0.3631 0.0099  0.0145  0.0153  334 ASN A CG  
2374 O  OD1 . ASN A 354 ? 0.1774 0.2493 0.3494 0.0053  0.0083  0.0177  334 ASN A OD1 
2375 N  ND2 . ASN A 354 ? 0.1602 0.2393 0.3505 0.0144  0.0186  0.0149  334 ASN A ND2 
2376 N  N   . THR A 355 ? 0.1470 0.1810 0.2710 0.0088  0.0131  0.0117  335 THR A N   
2377 C  CA  . THR A 355 ? 0.1624 0.1880 0.2760 0.0092  0.0157  0.0102  335 THR A CA  
2378 C  C   . THR A 355 ? 0.1588 0.1813 0.2641 0.0055  0.0179  0.0070  335 THR A C   
2379 O  O   . THR A 355 ? 0.1612 0.1859 0.2661 0.0022  0.0159  0.0068  335 THR A O   
2380 C  CB  . THR A 355 ? 0.1925 0.2146 0.2970 0.0103  0.0118  0.0133  335 THR A CB  
2381 O  OG1 . THR A 355 ? 0.2419 0.2634 0.3375 0.0080  0.0079  0.0120  335 THR A OG1 
2382 C  CG2 . THR A 355 ? 0.2652 0.2911 0.3767 0.0132  0.0083  0.0185  335 THR A CG2 
2383 N  N   . LEU A 356 ? 0.1586 0.1757 0.2580 0.0058  0.0211  0.0051  336 LEU A N   
2384 C  CA  . LEU A 356 ? 0.1371 0.1508 0.2283 0.0028  0.0224  0.0032  336 LEU A CA  
2385 C  C   . LEU A 356 ? 0.1752 0.1829 0.2583 0.0039  0.0217  0.0036  336 LEU A C   
2386 O  O   . LEU A 356 ? 0.1917 0.1981 0.2768 0.0060  0.0229  0.0042  336 LEU A O   
2387 C  CB  . LEU A 356 ? 0.1921 0.2079 0.2849 0.0017  0.0275  0.0005  336 LEU A CB  
2388 C  CG  . LEU A 356 ? 0.2011 0.2136 0.2849 -0.0015 0.0282  -0.0001 336 LEU A CG  
2389 C  CD1 . LEU A 356 ? 0.1978 0.2109 0.2800 -0.0054 0.0256  0.0023  336 LEU A CD1 
2390 C  CD2 . LEU A 356 ? 0.2121 0.2274 0.2949 -0.0021 0.0330  -0.0031 336 LEU A CD2 
2391 N  N   . ALA A 357 ? 0.1675 0.1719 0.2432 0.0026  0.0195  0.0033  337 ALA A N   
2392 C  CA  . ALA A 357 ? 0.1446 0.1452 0.2140 0.0039  0.0197  0.0033  337 ALA A CA  
2393 C  C   . ALA A 357 ? 0.1893 0.1863 0.2543 0.0016  0.0194  0.0022  337 ALA A C   
2394 O  O   . ALA A 357 ? 0.1824 0.1783 0.2473 -0.0007 0.0172  0.0020  337 ALA A O   
2395 C  CB  . ALA A 357 ? 0.1726 0.1731 0.2372 0.0067  0.0171  0.0041  337 ALA A CB  
2396 N  N   . VAL A 358 ? 0.1489 0.1444 0.2117 0.0017  0.0208  0.0023  338 VAL A N   
2397 C  CA  . VAL A 358 ? 0.1649 0.1572 0.2239 -0.0002 0.0198  0.0025  338 VAL A CA  
2398 C  C   . VAL A 358 ? 0.1619 0.1521 0.2184 0.0029  0.0185  0.0028  338 VAL A C   
2399 O  O   . VAL A 358 ? 0.1738 0.1662 0.2315 0.0041  0.0200  0.0037  338 VAL A O   
2400 C  CB  . VAL A 358 ? 0.1621 0.1560 0.2205 -0.0029 0.0219  0.0024  338 VAL A CB  
2401 C  CG1 . VAL A 358 ? 0.1780 0.1693 0.2322 -0.0050 0.0199  0.0043  338 VAL A CG1 
2402 C  CG2 . VAL A 358 ? 0.1647 0.1629 0.2260 -0.0049 0.0245  0.0014  338 VAL A CG2 
2403 N  N   . PHE A 359 ? 0.1643 0.1507 0.2183 0.0045  0.0158  0.0018  339 PHE A N   
2404 C  CA  . PHE A 359 ? 0.2026 0.1880 0.2545 0.0090  0.0152  0.0009  339 PHE A CA  
2405 C  C   . PHE A 359 ? 0.1976 0.1800 0.2502 0.0086  0.0138  0.0022  339 PHE A C   
2406 O  O   . PHE A 359 ? 0.1933 0.1694 0.2454 0.0083  0.0105  0.0018  339 PHE A O   
2407 C  CB  . PHE A 359 ? 0.2133 0.1949 0.2617 0.0116  0.0124  -0.0026 339 PHE A CB  
2408 C  CG  . PHE A 359 ? 0.1897 0.1754 0.2366 0.0122  0.0126  -0.0033 339 PHE A CG  
2409 C  CD1 . PHE A 359 ? 0.2188 0.2104 0.2634 0.0159  0.0152  -0.0025 339 PHE A CD1 
2410 C  CD2 . PHE A 359 ? 0.2222 0.2068 0.2707 0.0088  0.0100  -0.0037 339 PHE A CD2 
2411 C  CE1 . PHE A 359 ? 0.2112 0.2071 0.2541 0.0163  0.0147  -0.0016 339 PHE A CE1 
2412 C  CE2 . PHE A 359 ? 0.2417 0.2308 0.2897 0.0095  0.0093  -0.0036 339 PHE A CE2 
2413 C  CZ  . PHE A 359 ? 0.2733 0.2675 0.3178 0.0133  0.0114  -0.0024 339 PHE A CZ  
2414 N  N   . THR A 360 ? 0.1777 0.1643 0.2325 0.0081  0.0155  0.0044  340 THR A N   
2415 C  CA  . THR A 360 ? 0.1771 0.1620 0.2330 0.0083  0.0133  0.0064  340 THR A CA  
2416 C  C   . THR A 360 ? 0.2102 0.1953 0.2680 0.0145  0.0130  0.0051  340 THR A C   
2417 O  O   . THR A 360 ? 0.2180 0.2089 0.2766 0.0180  0.0160  0.0042  340 THR A O   
2418 C  CB  . THR A 360 ? 0.1894 0.1790 0.2472 0.0055  0.0138  0.0087  340 THR A CB  
2419 O  OG1 . THR A 360 ? 0.1984 0.1939 0.2606 0.0080  0.0158  0.0093  340 THR A OG1 
2420 C  CG2 . THR A 360 ? 0.1641 0.1543 0.2193 0.0007  0.0152  0.0079  340 THR A CG2 
2421 N  N   . GLN A 361 ? 0.2315 0.2106 0.2903 0.0161  0.0094  0.0053  341 GLN A N   
2422 C  CA  . GLN A 361 ? 0.2357 0.2136 0.2969 0.0232  0.0090  0.0026  341 GLN A CA  
2423 C  C   . GLN A 361 ? 0.2173 0.1897 0.2828 0.0239  0.0044  0.0054  341 GLN A C   
2424 O  O   . GLN A 361 ? 0.2144 0.1828 0.2790 0.0182  0.0013  0.0094  341 GLN A O   
2425 C  CB  . GLN A 361 ? 0.2654 0.2372 0.3219 0.0262  0.0082  -0.0033 341 GLN A CB  
2426 C  CG  . GLN A 361 ? 0.2554 0.2180 0.3099 0.0207  0.0040  -0.0033 341 GLN A CG  
2427 C  CD  . GLN A 361 ? 0.3583 0.3173 0.4082 0.0221  0.0029  -0.0090 341 GLN A CD  
2428 O  OE1 . GLN A 361 ? 0.3688 0.3328 0.4151 0.0271  0.0057  -0.0129 341 GLN A OE1 
2429 N  NE2 . GLN A 361 ? 0.3383 0.2896 0.3885 0.0172  -0.0014 -0.0089 341 GLN A NE2 
2430 N  N   . PRO A 362 ? 0.2029 0.1761 0.2737 0.0311  0.0041  0.0038  342 PRO A N   
2431 C  CA  . PRO A 362 ? 0.2207 0.1891 0.2978 0.0325  -0.0009 0.0075  342 PRO A CA  
2432 C  C   . PRO A 362 ? 0.2235 0.1773 0.2998 0.0316  -0.0065 0.0068  342 PRO A C   
2433 O  O   . PRO A 362 ? 0.2493 0.1961 0.3215 0.0322  -0.0067 0.0013  342 PRO A O   
2434 C  CB  . PRO A 362 ? 0.2162 0.1906 0.3007 0.0420  0.0013  0.0047  342 PRO A CB  
2435 C  CG  . PRO A 362 ? 0.1972 0.1831 0.2788 0.0435  0.0082  0.0021  342 PRO A CG  
2436 C  CD  . PRO A 362 ? 0.2456 0.2266 0.3175 0.0384  0.0089  -0.0003 342 PRO A CD  
2437 N  N   . ASN A 363 ? 0.2364 0.1855 0.3174 0.0298  -0.0118 0.0131  343 ASN A N   
2438 C  CA  . ASN A 363 ? 0.2352 0.1694 0.3192 0.0305  -0.0180 0.0133  343 ASN A CA  
2439 C  C   . ASN A 363 ? 0.2797 0.2083 0.3685 0.0411  -0.0182 0.0049  343 ASN A C   
2440 O  O   . ASN A 363 ? 0.2463 0.1848 0.3385 0.0484  -0.0138 0.0017  343 ASN A O   
2441 C  CB  . ASN A 363 ? 0.2606 0.1918 0.3496 0.0273  -0.0240 0.0232  343 ASN A CB  
2442 C  CG  . ASN A 363 ? 0.2554 0.1894 0.3372 0.0165  -0.0245 0.0305  343 ASN A CG  
2443 O  OD1 . ASN A 363 ? 0.3179 0.2493 0.3944 0.0114  -0.0229 0.0289  343 ASN A OD1 
2444 N  ND2 . ASN A 363 ? 0.3372 0.2778 0.4188 0.0132  -0.0265 0.0383  343 ASN A ND2 
2445 N  N   . LEU A 364 ? 0.2889 0.2021 0.3785 0.0419  -0.0232 0.0010  344 LEU A N   
2446 C  CA  . LEU A 364 ? 0.3071 0.2137 0.3986 0.0522  -0.0233 -0.0098 344 LEU A CA  
2447 C  C   . LEU A 364 ? 0.3286 0.2373 0.4309 0.0621  -0.0237 -0.0099 344 LEU A C   
2448 O  O   . LEU A 364 ? 0.3309 0.2444 0.4340 0.0722  -0.0193 -0.0186 344 LEU A O   
2449 C  CB  . LEU A 364 ? 0.3255 0.2126 0.4174 0.0505  -0.0306 -0.0139 344 LEU A CB  
2450 C  CG  . LEU A 364 ? 0.3676 0.2535 0.4508 0.0414  -0.0305 -0.0149 344 LEU A CG  
2451 C  CD1 . LEU A 364 ? 0.3985 0.2648 0.4853 0.0385  -0.0394 -0.0173 344 LEU A CD1 
2452 C  CD2 . LEU A 364 ? 0.3644 0.2602 0.4381 0.0450  -0.0241 -0.0238 344 LEU A CD2 
2453 N  N   . GLY A 365 ? 0.2786 0.1854 0.3891 0.0597  -0.0287 0.0002  345 GLY A N   
2454 C  CA  . GLY A 365 ? 0.2706 0.1806 0.3937 0.0691  -0.0299 0.0015  345 GLY A CA  
2455 C  C   . GLY A 365 ? 0.3103 0.2411 0.4365 0.0707  -0.0241 0.0052  345 GLY A C   
2456 O  O   . GLY A 365 ? 0.3062 0.2425 0.4446 0.0790  -0.0246 0.0063  345 GLY A O   
2457 N  N   . ASP A 366 ? 0.2652 0.2077 0.3822 0.0631  -0.0189 0.0073  346 ASP A N   
2458 C  CA  . ASP A 366 ? 0.2411 0.2025 0.3620 0.0634  -0.0142 0.0110  346 ASP A CA  
2459 C  C   . ASP A 366 ? 0.2647 0.2369 0.3889 0.0734  -0.0066 0.0031  346 ASP A C   
2460 O  O   . ASP A 366 ? 0.2558 0.2262 0.3712 0.0755  -0.0022 -0.0050 346 ASP A O   
2461 C  CB  . ASP A 366 ? 0.2541 0.2228 0.3648 0.0528  -0.0112 0.0144  346 ASP A CB  
2462 C  CG  . ASP A 366 ? 0.3449 0.3082 0.4517 0.0432  -0.0172 0.0227  346 ASP A CG  
2463 O  OD1 . ASP A 366 ? 0.3887 0.3473 0.5023 0.0439  -0.0237 0.0288  346 ASP A OD1 
2464 O  OD2 . ASP A 366 ? 0.3672 0.3319 0.4642 0.0352  -0.0150 0.0232  346 ASP A OD2 
2465 N  N   . GLU A 367 ? 0.2371 0.2230 0.3738 0.0790  -0.0050 0.0064  347 GLU A N   
2466 C  CA  . GLU A 367 ? 0.2448 0.2452 0.3857 0.0881  0.0035  0.0006  347 GLU A CA  
2467 C  C   . GLU A 367 ? 0.2648 0.2776 0.3968 0.0820  0.0105  0.0012  347 GLU A C   
2468 O  O   . GLU A 367 ? 0.2512 0.2687 0.3818 0.0723  0.0092  0.0083  347 GLU A O   
2469 C  CB  . GLU A 367 ? 0.2998 0.3142 0.4590 0.0949  0.0036  0.0054  347 GLU A CB  
2470 C  CG  . GLU A 367 ? 0.2989 0.3022 0.4691 0.1048  -0.0019 0.0028  347 GLU A CG  
2471 C  CD  . GLU A 367 ? 0.3233 0.3430 0.5135 0.1144  -0.0002 0.0057  347 GLU A CD  
2472 O  OE1 . GLU A 367 ? 0.4100 0.4495 0.6065 0.1107  0.0032  0.0123  347 GLU A OE1 
2473 O  OE2 . GLU A 367 ? 0.4620 0.4748 0.6627 0.1257  -0.0025 0.0012  347 GLU A OE2 
2474 N  N   . VAL A 368 ? 0.2130 0.2305 0.3386 0.0878  0.0176  -0.0065 348 VAL A N   
2475 C  CA  . VAL A 368 ? 0.2098 0.2406 0.3288 0.0836  0.0246  -0.0051 348 VAL A CA  
2476 C  C   . VAL A 368 ? 0.2299 0.2821 0.3580 0.0914  0.0330  -0.0045 348 VAL A C   
2477 O  O   . VAL A 368 ? 0.2725 0.3398 0.4049 0.0863  0.0368  0.0027  348 VAL A O   
2478 C  CB  . VAL A 368 ? 0.2834 0.3045 0.3856 0.0824  0.0259  -0.0125 348 VAL A CB  
2479 C  CG1 . VAL A 368 ? 0.4358 0.4717 0.5319 0.0809  0.0337  -0.0113 348 VAL A CG1 
2480 C  CG2 . VAL A 368 ? 0.2504 0.2561 0.3458 0.0722  0.0191  -0.0100 348 VAL A CG2 
2481 N  N   . ASP A 369 ? 0.2567 0.3108 0.3889 0.1037  0.0359  -0.0119 349 ASP A N   
2482 C  CA  . ASP A 369 ? 0.3066 0.3832 0.4508 0.1123  0.0441  -0.0108 349 ASP A CA  
2483 C  C   . ASP A 369 ? 0.3519 0.4312 0.5159 0.1164  0.0394  -0.0061 349 ASP A C   
2484 O  O   . ASP A 369 ? 0.3108 0.3785 0.4793 0.1250  0.0355  -0.0122 349 ASP A O   
2485 C  CB  . ASP A 369 ? 0.3776 0.4570 0.5138 0.1247  0.0512  -0.0228 349 ASP A CB  
2486 C  CG  . ASP A 369 ? 0.4337 0.5404 0.5804 0.1332  0.0620  -0.0211 349 ASP A CG  
2487 O  OD1 . ASP A 369 ? 0.3651 0.4842 0.5317 0.1353  0.0619  -0.0142 349 ASP A OD1 
2488 O  OD2 . ASP A 369 ? 0.5503 0.6674 0.6854 0.1377  0.0705  -0.0263 349 ASP A OD2 
2489 N  N   . MET A 370 ? 0.2721 0.3659 0.4487 0.1099  0.0388  0.0049  350 MET A N   
2490 C  CA  . MET A 370 ? 0.3923 0.4898 0.5880 0.1123  0.0328  0.0109  350 MET A CA  
2491 C  C   . MET A 370 ? 0.4250 0.5394 0.6376 0.1267  0.0390  0.0081  350 MET A C   
2492 O  O   . MET A 370 ? 0.4063 0.5210 0.6355 0.1322  0.0336  0.0108  350 MET A O   
2493 C  CB  . MET A 370 ? 0.3903 0.4989 0.5940 0.1005  0.0293  0.0227  350 MET A CB  
2494 C  CG  . MET A 370 ? 0.6042 0.7042 0.7917 0.0873  0.0278  0.0246  350 MET A CG  
2495 S  SD  . MET A 370 ? 0.6666 0.7383 0.8385 0.0809  0.0179  0.0219  350 MET A SD  
2496 C  CE  . MET A 370 ? 0.4328 0.5058 0.6190 0.0772  0.0074  0.0313  350 MET A CE  
2497 N  N   . GLU A 371 ? 0.4382 0.5677 0.6472 0.1333  0.0504  0.0031  351 GLU A N   
2498 C  CA  . GLU A 371 ? 0.3629 0.5118 0.5878 0.1479  0.0583  -0.0001 351 GLU A CA  
2499 C  C   . GLU A 371 ? 0.4115 0.5444 0.6319 0.1619  0.0578  -0.0143 351 GLU A C   
2500 O  O   . GLU A 371 ? 0.3806 0.5152 0.6169 0.1714  0.0554  -0.0170 351 GLU A O   
2501 C  CB  . GLU A 371 ? 0.4811 0.6555 0.7036 0.1491  0.0715  0.0013  351 GLU A CB  
2502 C  CG  . GLU A 371 ? 0.6962 0.8816 0.9194 0.1338  0.0715  0.0142  351 GLU A CG  
2503 C  CD  . GLU A 371 ? 0.8241 1.0237 1.0719 0.1290  0.0667  0.0264  351 GLU A CD  
2504 O  OE1 . GLU A 371 ? 0.8135 1.0243 1.0760 0.1363  0.0673  0.0252  351 GLU A OE1 
2505 O  OE2 . GLU A 371 ? 0.8296 1.0249 1.0768 0.1150  0.0601  0.0348  351 GLU A OE2 
2506 N  N   . GLN A 372 ? 0.3776 0.4936 0.5755 0.1613  0.0584  -0.0243 352 GLN A N   
2507 C  CA  . GLN A 372 ? 0.4003 0.4981 0.5918 0.1732  0.0567  -0.0392 352 GLN A CA  
2508 C  C   . GLN A 372 ? 0.3684 0.4355 0.5574 0.1680  0.0431  -0.0397 352 GLN A C   
2509 O  O   . GLN A 372 ? 0.4172 0.4661 0.6046 0.1773  0.0394  -0.0510 352 GLN A O   
2510 C  CB  . GLN A 372 ? 0.4759 0.5726 0.6441 0.1756  0.0638  -0.0505 352 GLN A CB  
2511 C  CG  . GLN A 372 ? 0.6420 0.7648 0.8095 0.1784  0.0768  -0.0516 352 GLN A CG  
2512 C  CD  . GLN A 372 ? 0.7492 0.8659 0.8938 0.1826  0.0820  -0.0654 352 GLN A CD  
2513 O  OE1 . GLN A 372 ? 0.7256 0.8223 0.8648 0.1893  0.0783  -0.0777 352 GLN A OE1 
2514 N  NE2 . GLN A 372 ? 0.7718 0.9050 0.9024 0.1781  0.0899  -0.0625 352 GLN A NE2 
2515 N  N   . HIS A 373 ? 0.3267 0.3877 0.5148 0.1534  0.0356  -0.0280 353 HIS A N   
2516 C  CA  . HIS A 373 ? 0.3299 0.3652 0.5163 0.1471  0.0232  -0.0256 353 HIS A CA  
2517 C  C   . HIS A 373 ? 0.3682 0.3814 0.5347 0.1441  0.0205  -0.0353 353 HIS A C   
2518 O  O   . HIS A 373 ? 0.4569 0.4475 0.6237 0.1454  0.0119  -0.0389 353 HIS A O   
2519 C  CB  . HIS A 373 ? 0.3519 0.3800 0.5577 0.1572  0.0167  -0.0255 353 HIS A CB  
2520 C  CG  . HIS A 373 ? 0.4263 0.4771 0.6536 0.1601  0.0183  -0.0157 353 HIS A CG  
2521 N  ND1 . HIS A 373 ? 0.4381 0.4969 0.6700 0.1478  0.0135  -0.0017 353 HIS A ND1 
2522 C  CD2 . HIS A 373 ? 0.3919 0.4605 0.6354 0.1732  0.0240  -0.0179 353 HIS A CD2 
2523 C  CE1 . HIS A 373 ? 0.4491 0.5292 0.7020 0.1531  0.0154  0.0046  353 HIS A CE1 
2524 N  NE2 . HIS A 373 ? 0.4363 0.5232 0.6959 0.1681  0.0219  -0.0047 353 HIS A NE2 
2525 N  N   . ILE A 374 ? 0.3076 0.3276 0.4578 0.1394  0.0270  -0.0382 354 ILE A N   
2526 C  CA  . ILE A 374 ? 0.3039 0.3061 0.4353 0.1351  0.0242  -0.0461 354 ILE A CA  
2527 C  C   . ILE A 374 ? 0.2972 0.2898 0.4230 0.1195  0.0174  -0.0365 354 ILE A C   
2528 O  O   . ILE A 374 ? 0.2868 0.2927 0.4121 0.1110  0.0203  -0.0273 354 ILE A O   
2529 C  CB  . ILE A 374 ? 0.2967 0.3121 0.4132 0.1377  0.0339  -0.0531 354 ILE A CB  
2530 C  CG1 . ILE A 374 ? 0.3678 0.3947 0.4888 0.1541  0.0417  -0.0635 354 ILE A CG1 
2531 C  CG2 . ILE A 374 ? 0.3152 0.3134 0.4129 0.1323  0.0298  -0.0604 354 ILE A CG2 
2532 C  CD1 . ILE A 374 ? 0.4131 0.4574 0.5192 0.1571  0.0523  -0.0686 354 ILE A CD1 
2533 N  N   . THR A 375 ? 0.3110 0.2807 0.4331 0.1158  0.0086  -0.0386 355 THR A N   
2534 C  CA  . THR A 375 ? 0.2835 0.2443 0.4004 0.1019  0.0026  -0.0300 355 THR A CA  
2535 C  C   . THR A 375 ? 0.3121 0.2717 0.4122 0.0949  0.0051  -0.0336 355 THR A C   
2536 O  O   . THR A 375 ? 0.3483 0.3096 0.4394 0.1005  0.0093  -0.0435 355 THR A O   
2537 C  CB  . THR A 375 ? 0.3693 0.3078 0.4910 0.1002  -0.0079 -0.0289 355 THR A CB  
2538 O  OG1 . THR A 375 ? 0.3983 0.3209 0.5136 0.1054  -0.0102 -0.0413 355 THR A OG1 
2539 C  CG2 . THR A 375 ? 0.3846 0.3233 0.5238 0.1073  -0.0117 -0.0242 355 THR A CG2 
2540 N  N   . PHE A 376 ? 0.2521 0.2092 0.3480 0.0826  0.0022  -0.0256 356 PHE A N   
2541 C  CA  . PHE A 376 ? 0.2549 0.2117 0.3374 0.0760  0.0040  -0.0278 356 PHE A CA  
2542 C  C   . PHE A 376 ? 0.2715 0.2116 0.3467 0.0778  -0.0006 -0.0376 356 PHE A C   
2543 O  O   . PHE A 376 ? 0.3065 0.2491 0.3708 0.0786  0.0022  -0.0443 356 PHE A O   
2544 C  CB  . PHE A 376 ? 0.2429 0.1998 0.3238 0.0636  0.0018  -0.0182 356 PHE A CB  
2545 C  CG  . PHE A 376 ? 0.2259 0.1842 0.2957 0.0572  0.0038  -0.0196 356 PHE A CG  
2546 C  CD1 . PHE A 376 ? 0.2923 0.2641 0.3570 0.0589  0.0107  -0.0210 356 PHE A CD1 
2547 C  CD2 . PHE A 376 ? 0.3183 0.2654 0.3842 0.0496  -0.0012 -0.0185 356 PHE A CD2 
2548 C  CE1 . PHE A 376 ? 0.3027 0.2756 0.3585 0.0535  0.0118  -0.0214 356 PHE A CE1 
2549 C  CE2 . PHE A 376 ? 0.3290 0.2785 0.3869 0.0443  0.0004  -0.0195 356 PHE A CE2 
2550 C  CZ  . PHE A 376 ? 0.2978 0.2596 0.3506 0.0466  0.0066  -0.0210 356 PHE A CZ  
2551 N  N   . GLY A 377 ? 0.3374 0.2601 0.4188 0.0777  -0.0086 -0.0380 357 GLY A N   
2552 C  CA  . GLY A 377 ? 0.3680 0.2733 0.4444 0.0791  -0.0144 -0.0477 357 GLY A CA  
2553 C  C   . GLY A 377 ? 0.3834 0.2897 0.4549 0.0915  -0.0109 -0.0617 357 GLY A C   
2554 O  O   . GLY A 377 ? 0.3892 0.2906 0.4493 0.0919  -0.0120 -0.0711 357 GLY A O   
2555 N  N   . GLU A 378 ? 0.3127 0.2267 0.3927 0.1022  -0.0068 -0.0635 358 GLU A N   
2556 C  CA  . GLU A 378 ? 0.3763 0.2956 0.4509 0.1150  -0.0013 -0.0769 358 GLU A CA  
2557 C  C   . GLU A 378 ? 0.3869 0.3247 0.4473 0.1134  0.0073  -0.0779 358 GLU A C   
2558 O  O   . GLU A 378 ? 0.4155 0.3513 0.4622 0.1169  0.0080  -0.0889 358 GLU A O   
2559 C  CB  . GLU A 378 ? 0.3260 0.2540 0.4151 0.1266  0.0026  -0.0766 358 GLU A CB  
2560 C  CG  . GLU A 378 ? 0.3719 0.2797 0.4753 0.1301  -0.0068 -0.0767 358 GLU A CG  
2561 C  CD  . GLU A 378 ? 0.4712 0.3892 0.5929 0.1376  -0.0048 -0.0702 358 GLU A CD  
2562 O  OE1 . GLU A 378 ? 0.3781 0.3196 0.5024 0.1392  0.0039  -0.0649 358 GLU A OE1 
2563 O  OE2 . GLU A 378 ? 0.4991 0.4012 0.6338 0.1418  -0.0126 -0.0697 358 GLU A OE2 
2564 N  N   . PHE A 379 ? 0.3336 0.2890 0.3971 0.1076  0.0129  -0.0659 359 PHE A N   
2565 C  CA  . PHE A 379 ? 0.3681 0.3411 0.4209 0.1046  0.0204  -0.0635 359 PHE A CA  
2566 C  C   . PHE A 379 ? 0.4894 0.4537 0.5275 0.0980  0.0164  -0.0675 359 PHE A C   
2567 O  O   . PHE A 379 ? 0.4471 0.4204 0.4724 0.1005  0.0208  -0.0725 359 PHE A O   
2568 C  CB  . PHE A 379 ? 0.3739 0.3597 0.4352 0.0965  0.0232  -0.0490 359 PHE A CB  
2569 C  CG  . PHE A 379 ? 0.4625 0.4655 0.5165 0.0923  0.0302  -0.0438 359 PHE A CG  
2570 C  CD1 . PHE A 379 ? 0.5391 0.5621 0.5939 0.0991  0.0393  -0.0434 359 PHE A CD1 
2571 C  CD2 . PHE A 379 ? 0.4495 0.4498 0.4983 0.0814  0.0277  -0.0379 359 PHE A CD2 
2572 C  CE1 . PHE A 379 ? 0.5658 0.6042 0.6155 0.0944  0.0450  -0.0365 359 PHE A CE1 
2573 C  CE2 . PHE A 379 ? 0.4065 0.4211 0.4506 0.0776  0.0332  -0.0321 359 PHE A CE2 
2574 C  CZ  . PHE A 379 ? 0.4300 0.4631 0.4745 0.0837  0.0415  -0.0309 359 PHE A CZ  
2575 N  N   . ALA A 380 ? 0.3789 0.3265 0.4193 0.0895  0.0078  -0.0650 360 ALA A N   
2576 C  CA  . ALA A 380 ? 0.4241 0.3642 0.4541 0.0821  0.0031  -0.0673 360 ALA A CA  
2577 C  C   . ALA A 380 ? 0.5522 0.4792 0.5735 0.0879  -0.0020 -0.0818 360 ALA A C   
2578 O  O   . ALA A 380 ? 0.5481 0.4746 0.5576 0.0846  -0.0042 -0.0862 360 ALA A O   
2579 C  CB  . ALA A 380 ? 0.4152 0.3447 0.4525 0.0708  -0.0035 -0.0586 360 ALA A CB  
2580 N  N   . ARG A 381 ? 0.4919 0.4078 0.5192 0.0967  -0.0047 -0.0899 361 ARG A N   
2581 C  CA  . ARG A 381 ? 0.4300 0.3332 0.4484 0.1039  -0.0092 -0.1061 361 ARG A CA  
2582 C  C   . ARG A 381 ? 0.4943 0.4129 0.5011 0.1159  -0.0003 -0.1161 361 ARG A C   
2583 O  O   . ARG A 381 ? 0.5417 0.4510 0.5404 0.1245  -0.0030 -0.1317 361 ARG A O   
2584 C  CB  . ARG A 381 ? 0.5314 0.4129 0.5621 0.1083  -0.0172 -0.1112 361 ARG A CB  
2585 C  CG  . ARG A 381 ? 0.6024 0.4657 0.6404 0.0961  -0.0280 -0.1047 361 ARG A CG  
2586 C  CD  . ARG A 381 ? 0.7043 0.5630 0.7300 0.0886  -0.0332 -0.1097 361 ARG A CD  
2587 N  NE  . ARG A 381 ? 0.7533 0.5965 0.7876 0.0767  -0.0431 -0.1028 361 ARG A NE  
2588 C  CZ  . ARG A 381 ? 0.6536 0.5043 0.6896 0.0647  -0.0427 -0.0904 361 ARG A CZ  
2589 N  NH1 . ARG A 381 ? 0.7028 0.5738 0.7322 0.0628  -0.0342 -0.0842 361 ARG A NH1 
2590 N  NH2 . ARG A 381 ? 0.7044 0.5421 0.7496 0.0546  -0.0511 -0.0838 361 ARG A NH2 
2591 N  N   . GLY A 382 ? 0.4907 0.4325 0.4963 0.1166  0.0100  -0.1076 362 GLY A N   
2592 C  CA  . GLY A 382 ? 0.5555 0.5150 0.5500 0.1271  0.0194  -0.1150 362 GLY A CA  
2593 C  C   . GLY A 382 ? 0.5231 0.4865 0.5267 0.1409  0.0248  -0.1217 362 GLY A C   
2594 O  O   . GLY A 382 ? 0.5581 0.5335 0.5513 0.1518  0.0320  -0.1319 362 GLY A O   
2595 N  N   . ILE A 383 ? 0.4896 0.4445 0.5122 0.1413  0.0215  -0.1163 363 ILE A N   
2596 C  CA  . ILE A 383 ? 0.4891 0.4501 0.5244 0.1545  0.0266  -0.1203 363 ILE A CA  
2597 C  C   . ILE A 383 ? 0.4848 0.4747 0.5260 0.1550  0.0382  -0.1086 363 ILE A C   
2598 O  O   . ILE A 383 ? 0.5497 0.5462 0.5968 0.1438  0.0381  -0.0937 363 ILE A O   
2599 C  CB  . ILE A 383 ? 0.4106 0.3520 0.4648 0.1538  0.0176  -0.1168 363 ILE A CB  
2600 C  CG1 . ILE A 383 ? 0.5309 0.4437 0.5804 0.1528  0.0063  -0.1279 363 ILE A CG1 
2601 C  CG2 . ILE A 383 ? 0.5087 0.4602 0.5790 0.1644  0.0232  -0.1154 363 ILE A CG2 
2602 C  CD1 . ILE A 383 ? 0.5742 0.4666 0.6409 0.1488  -0.0037 -0.1212 363 ILE A CD1 
2603 N  N   . VAL A 384 ? 0.5122 0.5200 0.5522 0.1678  0.0483  -0.1154 364 VAL A N   
2604 C  CA  . VAL A 384 ? 0.5893 0.6269 0.6351 0.1683  0.0598  -0.1043 364 VAL A CA  
2605 C  C   . VAL A 384 ? 0.5424 0.5908 0.6068 0.1764  0.0654  -0.1026 364 VAL A C   
2606 O  O   . VAL A 384 ? 0.6287 0.7022 0.7022 0.1765  0.0743  -0.0927 364 VAL A O   
2607 C  CB  . VAL A 384 ? 0.5320 0.5881 0.5574 0.1690  0.0687  -0.1069 364 VAL A CB  
2608 C  CG1 . VAL A 384 ? 0.5980 0.6455 0.6083 0.1562  0.0627  -0.1028 364 VAL A CG1 
2609 C  CG2 . VAL A 384 ? 0.4506 0.5024 0.4638 0.1772  0.0707  -0.1222 364 VAL A CG2 
2610 N  N   . ALA A 385 ? 0.4672 0.4972 0.5388 0.1824  0.0600  -0.1111 365 ALA A N   
2611 C  CA  . ALA A 385 ? 0.5420 0.5796 0.6334 0.1904  0.0641  -0.1092 365 ALA A CA  
2612 C  C   . ALA A 385 ? 0.5461 0.5574 0.6503 0.1912  0.0525  -0.1100 365 ALA A C   
2613 O  O   . ALA A 385 ? 0.5556 0.5417 0.6499 0.1883  0.0432  -0.1174 365 ALA A O   
2614 C  CB  . ALA A 385 ? 0.5302 0.5776 0.6147 0.2004  0.0733  -0.1205 365 ALA A CB  
2615 N  N   . LYS A 386 ? 0.5751 0.5926 0.7016 0.1946  0.0526  -0.1014 366 LYS A N   
2616 C  CA  . LYS A 386 ? 0.5643 0.5585 0.7031 0.1946  0.0412  -0.0989 366 LYS A CA  
2617 C  C   . LYS A 386 ? 0.6477 0.6471 0.8049 0.2055  0.0445  -0.0984 366 LYS A C   
2618 O  O   . LYS A 386 ? 0.6917 0.7164 0.8627 0.2090  0.0528  -0.0913 366 LYS A O   
2619 C  CB  . LYS A 386 ? 0.5578 0.5500 0.7060 0.1848  0.0332  -0.0848 366 LYS A CB  
2620 C  CG  . LYS A 386 ? 0.5919 0.5613 0.7517 0.1833  0.0210  -0.0801 366 LYS A CG  
2621 C  CD  . LYS A 386 ? 0.5893 0.5421 0.7438 0.1704  0.0106  -0.0746 366 LYS A CD  
2622 C  CE  . LYS A 386 ? 0.6146 0.5577 0.7850 0.1660  0.0005  -0.0620 366 LYS A CE  
2623 N  NZ  . LYS A 386 ? 0.3874 0.3256 0.5545 0.1519  -0.0056 -0.0524 366 LYS A NZ  
2624 N  N   . ASN A 387 ? 0.5839 0.5594 0.7424 0.2105  0.0375  -0.1057 367 ASN A N   
2625 C  CA  . ASN A 387 ? 0.7499 0.7254 0.9258 0.2217  0.0388  -0.1059 367 ASN A CA  
2626 C  C   . ASN A 387 ? 0.7556 0.7573 0.9358 0.2318  0.0538  -0.1107 367 ASN A C   
2627 O  O   . ASN A 387 ? 0.7461 0.7606 0.9463 0.2396  0.0579  -0.1050 367 ASN A O   
2628 C  CB  . ASN A 387 ? 0.7653 0.7419 0.9611 0.2193  0.0314  -0.0897 367 ASN A CB  
2629 C  CG  . ASN A 387 ? 0.9091 0.8556 1.1045 0.2125  0.0160  -0.0868 367 ASN A CG  
2630 O  OD1 . ASN A 387 ? 0.8111 0.7346 0.9999 0.2147  0.0110  -0.0971 367 ASN A OD1 
2631 N  ND2 . ASN A 387 ? 0.9687 0.9157 1.1716 0.2032  0.0082  -0.0724 367 ASN A ND2 
2632 N  N   . THR A 388 ? 0.7413 0.7524 0.9029 0.2311  0.0617  -0.1204 368 THR A N   
2633 C  CA  . THR A 388 ? 0.7749 0.8063 0.9365 0.2410  0.0751  -0.1284 368 THR A CA  
2634 C  C   . THR A 388 ? 0.8158 0.8309 0.9835 0.2533  0.0738  -0.1394 368 THR A C   
2635 O  O   . THR A 388 ? 0.8440 0.8309 1.0007 0.2532  0.0645  -0.1490 368 THR A O   
2636 C  CB  . THR A 388 ? 0.7532 0.7920 0.8883 0.2379  0.0811  -0.1380 368 THR A CB  
2637 O  OG1 . THR A 388 ? 0.7037 0.7618 0.8356 0.2278  0.0841  -0.1265 368 THR A OG1 
2638 C  CG2 . THR A 388 ? 0.8218 0.8783 0.9536 0.2488  0.0940  -0.1483 368 THR A CG2 
2639 N  N   . VAL A 389 ? 0.8633 0.8958 1.0501 0.2636  0.0825  -0.1376 369 VAL A N   
2640 C  CA  . VAL A 389 ? 0.7046 0.7220 0.9002 0.2764  0.0812  -0.1468 369 VAL A CA  
2641 C  C   . VAL A 389 ? 0.7776 0.7826 0.9503 0.2815  0.0835  -0.1670 369 VAL A C   
2642 O  O   . VAL A 389 ? 0.7068 0.7276 0.8617 0.2797  0.0920  -0.1734 369 VAL A O   
2643 C  CB  . VAL A 389 ? 0.7587 0.8006 0.9796 0.2872  0.0918  -0.1415 369 VAL A CB  
2644 C  CG1 . VAL A 389 ? 0.7809 0.8385 1.0233 0.2807  0.0891  -0.1210 369 VAL A CG1 
2645 C  CG2 . VAL A 389 ? 0.6566 0.7261 0.8708 0.2918  0.1077  -0.1499 369 VAL A CG2 
2646 N  N   . SER A 390 ? 0.6877 0.6642 0.8601 0.2872  0.0748  -0.1767 370 SER A N   
2647 C  CA  . SER A 390 ? 0.6397 0.6032 0.7930 0.2934  0.0760  -0.1970 370 SER A CA  
2648 C  C   . SER A 390 ? 0.6509 0.6265 0.8155 0.3098  0.0874  -0.2056 370 SER A C   
2649 O  O   . SER A 390 ? 0.6903 0.6922 0.8490 0.3142  0.1012  -0.2099 370 SER A O   
2650 C  CB  . SER A 390 ? 0.7291 0.6547 0.8769 0.2901  0.0599  -0.2038 370 SER A CB  
2651 O  OG  . SER A 390 ? 0.7013 0.6137 0.8337 0.2974  0.0603  -0.2243 370 SER A OG  
2652 O  OXT . SER A 390 ? 0.6707 0.6309 0.8510 0.3189  0.0831  -0.2078 370 SER A OXT 
2653 FE FE  . FE  B .   ? 0.2129 0.2372 0.2476 0.0235  0.0215  0.0150  401 FE  A FE  
2654 O  O   . HOH C .   ? 0.3966 0.4539 0.3705 0.0342  0.0090  0.0180  501 HOH A O   
2655 O  O   . HOH C .   ? 0.5801 0.3467 0.7609 0.1342  -0.0738 -0.0598 502 HOH A O   
2656 O  O   . HOH C .   ? 0.3944 0.5401 0.6951 0.0436  -0.0800 0.1011  503 HOH A O   
2657 O  O   . HOH C .   ? 0.4705 0.4998 0.4671 0.0600  0.0324  -0.0256 504 HOH A O   
2658 O  O   . HOH C .   ? 0.2972 0.4359 0.4378 -0.0637 0.0624  0.0645  505 HOH A O   
2659 O  O   . HOH C .   ? 0.3821 0.3863 0.5184 0.0163  0.0074  0.0641  506 HOH A O   
2660 O  O   . HOH C .   ? 0.3886 0.4020 0.3702 -0.0478 -0.0152 0.0767  507 HOH A O   
2661 O  O   . HOH C .   ? 0.3357 0.3015 0.4272 0.0165  -0.0315 0.0492  508 HOH A O   
2662 O  O   . HOH C .   ? 0.3388 0.5900 0.7001 0.0415  0.0749  0.0156  509 HOH A O   
2663 O  O   . HOH C .   ? 0.4044 0.4276 0.4661 -0.0620 0.0184  0.0697  510 HOH A O   
2664 O  O   . HOH C .   ? 0.3702 0.4404 0.5148 -0.0206 -0.0434 0.0469  511 HOH A O   
2665 O  O   . HOH C .   ? 0.5060 0.5084 0.5421 0.0084  -0.0171 -0.0089 512 HOH A O   
2666 O  O   . HOH C .   ? 0.3389 0.2771 0.5041 -0.0476 -0.0325 -0.0129 513 HOH A O   
2667 O  O   . HOH C .   ? 0.3345 0.3480 0.4461 0.0127  0.0220  0.0083  514 HOH A O   
2668 O  O   . HOH C .   ? 0.3987 0.5272 0.6583 -0.1454 -0.0026 0.1453  515 HOH A O   
2669 O  O   . HOH C .   ? 0.5962 0.6003 0.6142 0.1188  0.0371  -0.0805 516 HOH A O   
2670 O  O   . HOH C .   ? 0.4884 0.4369 0.5902 0.0276  -0.0321 0.0420  517 HOH A O   
2671 O  O   . HOH C .   ? 0.4347 0.3825 0.5003 -0.0083 -0.0342 0.0639  518 HOH A O   
2672 O  O   . HOH C .   ? 0.5610 0.5883 0.7574 -0.0812 -0.0917 0.0168  519 HOH A O   
2673 O  O   . HOH C .   ? 0.4978 0.4638 0.6183 -0.0836 -0.0226 0.0863  520 HOH A O   
2674 O  O   . HOH C .   ? 0.2348 0.2519 0.2847 0.0185  0.0225  0.0162  521 HOH A O   
2675 O  O   . HOH C .   ? 0.3850 0.3932 0.4754 0.0104  0.0196  0.0114  522 HOH A O   
2676 O  O   . HOH C .   ? 0.3539 0.5324 0.6672 0.0039  -0.0285 0.0509  523 HOH A O   
2677 O  O   . HOH C .   ? 0.3563 0.5329 0.7705 0.0796  -0.0162 0.0579  524 HOH A O   
2678 O  O   . HOH C .   ? 0.4400 0.5669 0.7073 0.0364  -0.0622 0.0823  525 HOH A O   
2679 O  O   . HOH C .   ? 0.4010 0.3679 0.4845 0.0180  -0.0184 0.0335  526 HOH A O   
2680 O  O   . HOH C .   ? 0.5244 0.5689 0.5599 -0.0684 0.0262  0.0833  527 HOH A O   
2681 O  O   . HOH C .   ? 0.2015 0.3344 0.4484 -0.0066 -0.0290 0.0392  528 HOH A O   
2682 O  O   . HOH C .   ? 0.4235 0.4227 0.4937 -0.0152 -0.0476 -0.0128 529 HOH A O   
2683 O  O   . HOH C .   ? 0.3689 0.3411 0.5557 -0.0010 0.0024  0.0869  530 HOH A O   
2684 O  O   . HOH C .   ? 0.3412 0.3549 0.6128 0.0760  0.0365  -0.0257 531 HOH A O   
2685 O  O   . HOH C .   ? 0.5339 0.4196 0.6655 -0.0662 -0.0650 0.0357  532 HOH A O   
2686 O  O   . HOH C .   ? 0.1845 0.3740 0.4722 0.0187  -0.0120 0.0867  533 HOH A O   
2687 O  O   . HOH C .   ? 0.4111 0.5446 0.4579 0.0577  0.0747  0.0363  534 HOH A O   
2688 O  O   . HOH C .   ? 0.3323 0.3029 0.4220 -0.0297 -0.0404 -0.0074 535 HOH A O   
2689 O  O   . HOH C .   ? 0.5065 0.5206 0.6886 0.0087  -0.0186 0.1683  536 HOH A O   
2690 O  O   . HOH C .   ? 0.3497 0.4179 0.4548 0.0259  -0.0395 0.1102  537 HOH A O   
2691 O  O   . HOH C .   ? 0.3707 0.3616 0.5544 0.0348  0.0206  0.0064  538 HOH A O   
2692 O  O   . HOH C .   ? 0.2339 0.2807 0.3478 -0.0153 -0.0299 0.0371  539 HOH A O   
2693 O  O   . HOH C .   ? 0.3811 0.6114 0.7384 -0.0377 -0.0255 0.1190  540 HOH A O   
2694 O  O   . HOH C .   ? 0.4443 0.5239 0.5713 0.0027  -0.0595 0.0365  541 HOH A O   
2695 O  O   . HOH C .   ? 0.2286 0.2103 0.2770 -0.0056 0.0056  0.0175  542 HOH A O   
2696 O  O   . HOH C .   ? 0.2518 0.2645 0.4040 0.0361  0.0517  -0.0434 543 HOH A O   
2697 O  O   . HOH C .   ? 0.2626 0.2387 0.3066 -0.0141 0.0024  0.0258  544 HOH A O   
2698 O  O   . HOH C .   ? 0.2727 0.4626 0.4994 -0.0003 0.0562  0.1089  545 HOH A O   
2699 O  O   . HOH C .   ? 0.3811 0.3180 0.5632 -0.0071 0.0010  0.0248  546 HOH A O   
2700 O  O   . HOH C .   ? 0.2555 0.2795 0.4742 0.0458  0.0176  0.0140  547 HOH A O   
2701 O  O   . HOH C .   ? 0.4443 0.3579 0.6075 0.0955  -0.0365 0.0049  548 HOH A O   
2702 O  O   . HOH C .   ? 0.4002 0.3119 0.4756 -0.0164 -0.0276 0.0271  549 HOH A O   
2703 O  O   . HOH C .   ? 0.3787 0.5140 0.6420 -0.0530 -0.0524 0.0432  550 HOH A O   
2704 O  O   . HOH C .   ? 0.2113 0.2379 0.3685 -0.0156 0.0220  0.0796  551 HOH A O   
2705 O  O   . HOH C .   ? 0.5202 0.6359 0.5650 -0.0156 0.0895  -0.0105 552 HOH A O   
2706 O  O   . HOH C .   ? 0.3735 0.5547 0.6700 0.0435  -0.0273 0.0867  553 HOH A O   
2707 O  O   . HOH C .   ? 0.3122 0.4593 0.5151 0.0744  0.0423  0.0409  554 HOH A O   
2708 O  O   . HOH C .   ? 0.4339 0.4232 0.4795 0.0001  -0.0249 -0.0149 555 HOH A O   
2709 O  O   . HOH C .   ? 0.5304 0.6745 0.7988 0.0937  0.0048  0.0540  556 HOH A O   
2710 O  O   . HOH C .   ? 0.4154 0.4598 0.7211 0.0658  -0.0562 0.1227  557 HOH A O   
2711 O  O   . HOH C .   ? 0.4166 0.4794 0.4697 0.0200  -0.0313 0.0586  558 HOH A O   
2712 O  O   . HOH C .   ? 0.3737 0.5014 0.6180 -0.1019 0.0042  0.0888  559 HOH A O   
2713 O  O   . HOH C .   ? 0.4370 0.4412 0.6236 0.0302  -0.0123 0.0860  560 HOH A O   
2714 O  O   . HOH C .   ? 0.4945 0.5196 0.6018 0.0180  0.0036  0.0342  561 HOH A O   
2715 O  O   . HOH C .   ? 0.3447 0.4920 0.5445 -0.0184 0.0523  0.1279  562 HOH A O   
2716 O  O   . HOH C .   ? 0.6022 0.5816 0.7679 -0.0845 -0.1287 -0.0117 563 HOH A O   
2717 O  O   . HOH C .   ? 0.4731 0.4832 0.5281 -0.0685 0.0082  0.0870  564 HOH A O   
2718 O  O   . HOH C .   ? 0.3166 0.2596 0.4281 -0.0493 -0.0611 -0.0041 565 HOH A O   
2719 O  O   . HOH C .   ? 0.3792 0.3633 0.5047 -0.0564 -0.0949 -0.0141 566 HOH A O   
2720 O  O   . HOH C .   ? 0.3568 0.2842 0.4196 -0.0031 -0.0168 0.0030  567 HOH A O   
2721 O  O   . HOH C .   ? 0.2491 0.2214 0.3127 -0.0462 -0.0035 0.0559  568 HOH A O   
2722 O  O   . HOH C .   ? 0.5913 0.7510 0.8799 0.0256  -0.0798 0.0830  569 HOH A O   
2723 O  O   . HOH C .   ? 0.3379 0.4397 0.6546 0.0689  0.0220  0.0163  570 HOH A O   
2724 O  O   . HOH C .   ? 0.3749 0.4181 0.3760 -0.0201 0.0495  -0.0169 571 HOH A O   
2725 O  O   . HOH C .   ? 0.3620 0.4914 0.5041 -0.0113 0.0537  0.1497  572 HOH A O   
2726 O  O   . HOH C .   ? 0.1965 0.4469 0.5376 -0.0419 0.0372  0.0642  573 HOH A O   
2727 O  O   . HOH C .   ? 0.4621 0.4962 0.5565 -0.0075 -0.0379 0.0478  574 HOH A O   
2728 O  O   . HOH C .   ? 0.3973 0.5065 0.6144 0.0255  -0.0568 0.0698  575 HOH A O   
2729 O  O   . HOH C .   ? 0.3591 0.3462 0.5019 0.0321  0.0437  -0.0474 576 HOH A O   
2730 O  O   . HOH C .   ? 0.3874 0.5847 0.6631 0.0901  0.0359  0.0574  577 HOH A O   
2731 O  O   . HOH C .   ? 0.4794 0.5625 0.7129 0.1171  0.0070  0.0251  578 HOH A O   
2732 O  O   . HOH C .   ? 0.3987 0.4308 0.6101 0.0571  0.0540  -0.0404 579 HOH A O   
2733 O  O   . HOH C .   ? 0.2874 0.2966 0.3857 -0.0356 -0.0240 0.0035  580 HOH A O   
2734 O  O   . HOH C .   ? 0.4314 0.4438 0.4307 0.0402  0.0167  -0.0177 581 HOH A O   
2735 O  O   . HOH C .   ? 0.2111 0.2707 0.3773 -0.0186 0.0302  0.1034  582 HOH A O   
2736 O  O   . HOH C .   ? 0.4623 0.5986 0.5848 -0.0209 0.0170  0.2593  583 HOH A O   
2737 O  O   . HOH C .   ? 0.5217 0.5186 0.5372 -0.0279 -0.0173 0.0518  584 HOH A O   
2738 O  O   . HOH C .   ? 0.2179 0.2046 0.3436 0.0165  0.0301  -0.0122 585 HOH A O   
2739 O  O   . HOH C .   ? 0.3135 0.4350 0.4841 0.0955  0.0501  0.0161  586 HOH A O   
2740 O  O   . HOH C .   ? 0.4968 0.4502 0.6518 -0.0987 -0.0407 0.0881  587 HOH A O   
2741 O  O   . HOH C .   ? 0.4196 0.4212 0.5971 0.0315  0.0107  0.0290  588 HOH A O   
2742 O  O   . HOH C .   ? 0.4528 0.4444 0.5518 -0.0839 -0.1000 -0.0369 589 HOH A O   
2743 O  O   . HOH C .   ? 0.4360 0.4621 0.5214 0.0349  0.0742  -0.0917 590 HOH A O   
2744 O  O   . HOH C .   ? 0.5896 0.5590 0.7764 0.0280  0.0101  0.0270  591 HOH A O   
2745 O  O   . HOH C .   ? 0.4022 0.4796 0.7182 0.0669  -0.0429 0.0901  592 HOH A O   
2746 O  O   . HOH C .   ? 0.6181 0.6276 0.6115 -0.0366 -0.0060 0.0476  593 HOH A O   
2747 O  O   . HOH C .   ? 0.1639 0.3669 0.4668 -0.0337 0.0227  0.0511  594 HOH A O   
2748 O  O   . HOH C .   ? 0.4468 0.3515 0.5311 -0.0098 -0.0435 0.0628  595 HOH A O   
2749 O  O   . HOH C .   ? 0.3878 0.4411 0.5136 0.0145  -0.0200 0.1660  596 HOH A O   
2750 O  O   . HOH C .   ? 0.2114 0.2652 0.2559 0.0319  0.0406  0.0255  597 HOH A O   
2751 O  O   . HOH C .   ? 0.2230 0.2793 0.2957 0.0160  0.0379  0.0557  598 HOH A O   
2752 O  O   . HOH C .   ? 0.4548 0.3641 0.5335 -0.0210 -0.0314 0.0127  599 HOH A O   
2753 O  O   . HOH C .   ? 0.2615 0.2429 0.3685 -0.0508 -0.0123 0.0335  600 HOH A O   
2754 O  O   . HOH C .   ? 0.3988 0.4541 0.3647 0.0592  0.0343  -0.0171 601 HOH A O   
2755 O  O   . HOH C .   ? 0.4541 0.4466 0.5344 -0.0611 0.0018  0.0664  602 HOH A O   
2756 O  O   . HOH C .   ? 0.3278 0.3224 0.4827 0.0714  -0.0177 0.0269  603 HOH A O   
2757 O  O   . HOH C .   ? 0.5025 0.4374 0.5954 -0.0656 -0.0707 -0.0707 604 HOH A O   
2758 O  O   . HOH C .   ? 0.2438 0.2398 0.2959 0.0199  0.0199  0.0015  605 HOH A O   
2759 O  O   . HOH C .   ? 0.3311 0.5833 0.6488 -0.0659 0.0507  0.0797  606 HOH A O   
2760 O  O   . HOH C .   ? 0.5537 0.6560 0.6506 0.0207  -0.0794 0.0927  607 HOH A O   
2761 O  O   . HOH C .   ? 0.3184 0.3385 0.3825 0.0159  0.0198  0.0284  608 HOH A O   
2762 O  O   . HOH C .   ? 0.5299 0.4899 0.5634 0.0388  0.0041  -0.0283 609 HOH A O   
2763 O  O   . HOH C .   ? 0.3415 0.3823 0.3576 0.0238  0.0029  0.0260  610 HOH A O   
2764 O  O   . HOH C .   ? 0.4060 0.4250 0.4837 0.0123  0.0060  0.0170  611 HOH A O   
2765 O  O   . HOH C .   ? 0.3979 0.4266 0.5175 0.0217  -0.0025 0.0496  612 HOH A O   
2766 O  O   . HOH C .   ? 0.3637 0.3603 0.3894 0.0316  0.0163  -0.0127 613 HOH A O   
2767 O  O   . HOH C .   ? 0.2096 0.2199 0.2878 0.0038  0.0093  0.0054  614 HOH A O   
2768 O  O   . HOH C .   ? 0.5872 0.6778 0.6161 0.0092  0.0928  -0.0614 615 HOH A O   
2769 O  O   . HOH C .   ? 0.4300 0.5691 0.4890 -0.0002 0.0235  0.2081  616 HOH A O   
2770 O  O   . HOH C .   ? 0.5596 0.5837 0.5575 0.0008  0.0550  -0.0787 617 HOH A O   
2771 O  O   . HOH C .   ? 0.3338 0.6124 0.6556 0.0473  0.0510  0.1002  618 HOH A O   
2772 O  O   . HOH C .   ? 0.2591 0.3073 0.3964 -0.0191 -0.0003 0.0146  619 HOH A O   
2773 O  O   . HOH C .   ? 0.4041 0.3715 0.5827 -0.0051 0.0059  0.0649  620 HOH A O   
2774 O  O   . HOH C .   ? 0.2711 0.3322 0.4144 0.0220  -0.0279 0.0532  621 HOH A O   
2775 O  O   . HOH C .   ? 0.3667 0.2872 0.4619 -0.0713 -0.0410 0.1094  622 HOH A O   
2776 O  O   . HOH C .   ? 0.4634 0.4665 0.6024 0.0209  0.0121  0.0339  623 HOH A O   
2777 O  O   . HOH C .   ? 0.3045 0.2942 0.3449 0.0274  0.0166  -0.0082 624 HOH A O   
2778 O  O   . HOH C .   ? 0.4582 0.4751 0.5770 0.0232  -0.0248 0.0460  625 HOH A O   
2779 O  O   . HOH C .   ? 0.2037 0.2621 0.2747 0.0211  0.0415  0.0424  626 HOH A O   
2780 O  O   . HOH C .   ? 0.4922 0.5143 0.4748 -0.0330 0.0144  0.0141  627 HOH A O   
2781 O  O   . HOH C .   ? 0.4227 0.3141 0.5349 0.0404  -0.0421 0.0228  628 HOH A O   
2782 O  O   . HOH C .   ? 0.2469 0.6787 0.6983 0.0263  0.1230  0.0351  629 HOH A O   
2783 O  O   . HOH C .   ? 0.4034 0.4148 0.5569 -0.0981 -0.0136 0.0916  630 HOH A O   
2784 O  O   . HOH C .   ? 0.4595 0.4015 0.6683 0.0358  0.0126  -0.0025 631 HOH A O   
2785 O  O   . HOH C .   ? 0.5527 0.5497 0.5655 -0.0853 -0.0293 0.1621  632 HOH A O   
2786 O  O   . HOH C .   ? 0.2869 0.5055 0.6125 0.0340  -0.0167 0.0956  633 HOH A O   
2787 O  O   . HOH C .   ? 0.3434 0.2942 0.5645 -0.0409 -0.0138 0.0577  634 HOH A O   
2788 O  O   . HOH C .   ? 0.5666 0.5743 0.5773 -0.0459 -0.0409 -0.0224 635 HOH A O   
2789 O  O   . HOH C .   ? 0.6082 0.7045 0.6742 0.1505  0.0772  -0.0635 636 HOH A O   
2790 O  O   . HOH C .   ? 0.4402 0.4229 0.5259 0.0231  0.0487  -0.0825 637 HOH A O   
2791 O  O   . HOH C .   ? 0.3992 0.4982 0.4625 0.0783  0.0648  0.0007  638 HOH A O   
2792 O  O   . HOH C .   ? 0.5641 0.6567 0.5845 -0.0445 0.0641  0.0336  639 HOH A O   
2793 O  O   . HOH C .   ? 0.5249 0.6349 0.5760 -0.0643 0.0628  0.0674  640 HOH A O   
2794 O  O   . HOH C .   ? 0.4251 0.4355 0.4934 -0.0471 -0.0457 -0.0085 641 HOH A O   
2795 O  O   . HOH C .   ? 0.3578 0.4123 0.6113 -0.0770 -0.0492 0.0594  642 HOH A O   
2796 O  O   . HOH C .   ? 0.4189 0.3154 0.5077 0.0218  -0.0339 0.0173  643 HOH A O   
2797 O  O   . HOH C .   ? 0.4980 0.4469 0.6958 -0.0712 -0.0567 -0.0023 644 HOH A O   
2798 O  O   . HOH C .   ? 0.3167 0.2793 0.5084 -0.0585 -0.0369 0.0124  645 HOH A O   
2799 O  O   . HOH C .   ? 0.4741 0.5573 0.6351 0.0155  -0.0442 0.0503  646 HOH A O   
2800 O  O   . HOH C .   ? 0.4916 0.5343 0.5469 0.0173  -0.0162 0.0346  647 HOH A O   
2801 O  O   . HOH C .   ? 0.4196 0.5448 0.6592 0.0293  -0.0527 0.0830  648 HOH A O   
2802 O  O   . HOH C .   ? 0.3655 0.5070 0.5498 0.0118  0.0818  -0.0076 649 HOH A O   
2803 O  O   . HOH C .   ? 0.4219 0.4136 0.5711 0.0192  0.0107  0.0423  650 HOH A O   
2804 O  O   . HOH C .   ? 0.4563 0.5479 0.6294 -0.1058 0.0191  0.1075  651 HOH A O   
2805 O  O   . HOH C .   ? 0.4354 0.4415 0.4479 -0.0270 -0.0033 -0.0038 652 HOH A O   
2806 O  O   . HOH C .   ? 0.4679 0.4532 0.5543 -0.0904 -0.0129 0.1220  653 HOH A O   
2807 O  O   . HOH C .   ? 0.4992 0.4490 0.5401 0.0175  -0.0054 -0.0194 654 HOH A O   
2808 O  O   . HOH C .   ? 0.3702 0.3928 0.4922 -0.0430 -0.0358 0.0124  655 HOH A O   
2809 O  O   . HOH C .   ? 0.4057 0.4279 0.6185 -0.0319 0.0099  0.1534  656 HOH A O   
2810 O  O   . HOH C .   ? 0.2927 0.3051 0.3264 0.0212  0.0152  0.0052  657 HOH A O   
2811 O  O   . HOH C .   ? 0.2132 0.2383 0.2554 0.0202  0.0170  0.0218  658 HOH A O   
2812 O  O   . HOH C .   ? 0.4792 0.5897 0.4339 0.0579  0.0518  0.0194  659 HOH A O   
2813 O  O   . HOH C .   ? 0.5117 0.5245 0.7277 -0.0126 -0.0196 0.2136  660 HOH A O   
2814 O  O   . HOH C .   ? 0.4312 0.5384 0.5969 -0.0256 0.0367  0.1929  661 HOH A O   
2815 O  O   . HOH C .   ? 0.3889 0.3981 0.4429 0.0145  0.0160  0.0104  662 HOH A O   
2816 O  O   . HOH C .   ? 0.5904 0.5877 0.6868 -0.0788 -0.0026 0.0891  663 HOH A O   
2817 O  O   . HOH C .   ? 0.5634 0.4538 0.6770 -0.0399 -0.0446 -0.0900 664 HOH A O   
2818 O  O   . HOH C .   ? 0.5875 0.4614 0.7411 0.0999  -0.0423 -0.0156 665 HOH A O   
2819 O  O   . HOH C .   ? 0.4369 0.5132 0.6168 0.0248  -0.0330 0.0558  666 HOH A O   
2820 O  O   . HOH C .   ? 0.5741 0.6911 0.6095 0.0780  0.0731  0.0045  667 HOH A O   
2821 O  O   . HOH C .   ? 0.5541 0.5488 0.7722 0.0041  -0.0266 0.1893  668 HOH A O   
2822 O  O   . HOH C .   ? 0.4595 0.4626 0.6664 0.0411  0.0103  0.0255  669 HOH A O   
2823 O  O   . HOH C .   ? 0.5257 0.5512 0.7135 0.0830  -0.0174 0.0345  670 HOH A O   
2824 O  O   . HOH C .   ? 0.3947 0.5485 0.6668 -0.0123 -0.0473 0.0472  671 HOH A O   
2825 O  O   . HOH C .   ? 0.4722 0.5128 0.6406 0.0554  0.0750  -0.0728 672 HOH A O   
2826 O  O   . HOH C .   ? 0.4830 0.5417 0.6168 -0.0295 -0.0421 0.0371  673 HOH A O   
2827 O  O   . HOH C .   ? 0.6355 0.6162 0.6659 -0.0736 -0.0887 -0.0640 674 HOH A O   
2828 O  O   . HOH C .   ? 0.4743 0.6026 0.7711 -0.0639 -0.0070 0.1136  675 HOH A O   
2829 O  O   . HOH C .   ? 0.4596 0.6487 0.6800 0.0828  0.0601  0.0473  676 HOH A O   
2830 O  O   . HOH C .   ? 0.3775 0.3811 0.3971 0.0274  0.0125  -0.0089 677 HOH A O   
2831 O  O   . HOH C .   ? 0.5507 0.5465 0.5587 -0.0218 0.0118  -0.0394 678 HOH A O   
2832 O  O   . HOH C .   ? 0.3552 0.3698 0.5033 0.0250  0.0016  0.0510  679 HOH A O   
2833 O  O   . HOH C .   ? 0.4457 0.4162 0.6136 0.0435  0.0417  -0.0587 680 HOH A O   
2834 O  O   . HOH C .   ? 0.3616 0.3798 0.5402 0.0514  0.0590  -0.0570 681 HOH A O   
2835 O  O   . HOH C .   ? 0.3902 0.5431 0.6237 0.0763  0.0277  0.0490  682 HOH A O   
2836 O  O   . HOH C .   ? 0.4859 0.4721 0.7137 0.0379  -0.0183 0.0908  683 HOH A O   
2837 O  O   . HOH C .   ? 0.5970 0.5884 0.7647 0.0229  0.0028  0.0598  684 HOH A O   
2838 O  O   . HOH C .   ? 0.3150 0.3752 0.5064 -0.0290 0.0262  0.1306  685 HOH A O   
2839 O  O   . HOH C .   ? 0.3747 0.4057 0.4861 -0.0483 -0.0513 0.0121  686 HOH A O   
2840 O  O   . HOH C .   ? 0.6184 0.7394 0.7235 -0.0110 0.0002  0.2569  687 HOH A O   
2841 O  O   . HOH C .   ? 0.6438 0.5497 0.8781 -0.0409 -0.0280 0.0313  688 HOH A O   
2842 O  O   . HOH C .   ? 0.5413 0.5594 0.6800 -0.1033 -0.0060 0.1102  689 HOH A O   
2843 O  O   . HOH C .   ? 0.6389 0.6959 0.8542 0.0826  -0.0219 0.0482  690 HOH A O   
2844 O  O   . HOH C .   ? 0.6030 0.7249 0.5999 0.0200  0.0012  0.1421  691 HOH A O   
2845 O  O   . HOH C .   ? 0.6612 0.6919 0.6169 -0.0461 -0.0276 0.0519  692 HOH A O   
# 
