data_8R5E
# 
_entry.id   8R5E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8R5E         pdb_00008r5e 10.2210/pdb8r5e/pdb 
WWPDB D_1292134595 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        8R5E 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-16 
_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              remenyi.attila@ttk.hu 
_pdbx_contact_author.name_first         Attila 
_pdbx_contact_author.name_last          Remenyi 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8345-1311 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sok, P.'     1 0000-0001-8963-8163 
'Poti, A.'    2 0000-0001-8811-0586 
'Remenyi, A.' 3 0000-0002-8345-1311 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'The covalent coordination of cyclohexenone inhibitors in the MAP kinase docking groove' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Poti, A.'    1 ? 
primary 'Sok, P.'     2 ? 
primary 'Remenyi, A.' 3 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Mitogen-activated protein kinase 8' 42032.566 1   2.7.11.24 ? ? 
'The dephosphorylated inactive JNK1-beta-1 kinase with RU77 covalent inhibitor at the kinase docking groove' 
2 non-polymer syn 'MAGNESIUM ION' 24.305    1   ?         ? ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' 506.196   1   ?         ? ? ? 
4 non-polymer syn 
'~{O}3-~{tert}-butyl ~{O}1-methyl (1~{S},3~{R},5~{R})-6-methylidene-4-oxidanylidene-bicyclo[3.2.1]octane-1,3-dicarboxylate' 
294.343   1   ?         ? ? ? 
5 non-polymer syn GLYCEROL 92.094    1   ?         ? ? ? 
6 water       nat water 18.015    120 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'MAP kinase 8,MAPK 8,JNK-46,Stress-activated protein kinase 1c,SAPK1c,Stress-activated protein kinase JNK1,c-Jun N-terminal kinase 1' 
# 
_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       
;GSMSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMK
CVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV
VKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVI
EQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQH
PYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSMSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMK
CVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIV
VKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVI
EQLGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQH
PYINVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLE
;
_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 'MAGNESIUM ION'                                                                                                             MG  
3 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                                                                               ANP 
4 '~{O}3-~{tert}-butyl ~{O}1-methyl (1~{S},3~{R},5~{R})-6-methylidene-4-oxidanylidene-bicyclo[3.2.1]octane-1,3-dicarboxylate' Y6K 
5 GLYCEROL                                                                                                                    GOL 
6 water                                                                                                                       HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   MET n 
1 4   SER n 
1 5   ARG n 
1 6   SER n 
1 7   LYS n 
1 8   ARG n 
1 9   ASP n 
1 10  ASN n 
1 11  ASN n 
1 12  PHE n 
1 13  TYR n 
1 14  SER n 
1 15  VAL n 
1 16  GLU n 
1 17  ILE n 
1 18  GLY n 
1 19  ASP n 
1 20  SER n 
1 21  THR n 
1 22  PHE n 
1 23  THR n 
1 24  VAL n 
1 25  LEU n 
1 26  LYS n 
1 27  ARG n 
1 28  TYR n 
1 29  GLN n 
1 30  ASN n 
1 31  LEU n 
1 32  LYS n 
1 33  PRO n 
1 34  ILE n 
1 35  GLY n 
1 36  SER n 
1 37  GLY n 
1 38  ALA n 
1 39  GLN n 
1 40  GLY n 
1 41  ILE n 
1 42  VAL n 
1 43  CYS n 
1 44  ALA n 
1 45  ALA n 
1 46  TYR n 
1 47  ASP n 
1 48  ALA n 
1 49  ILE n 
1 50  LEU n 
1 51  GLU n 
1 52  ARG n 
1 53  ASN n 
1 54  VAL n 
1 55  ALA n 
1 56  ILE n 
1 57  LYS n 
1 58  LYS n 
1 59  LEU n 
1 60  SER n 
1 61  ARG n 
1 62  PRO n 
1 63  PHE n 
1 64  GLN n 
1 65  ASN n 
1 66  GLN n 
1 67  THR n 
1 68  HIS n 
1 69  ALA n 
1 70  LYS n 
1 71  ARG n 
1 72  ALA n 
1 73  TYR n 
1 74  ARG n 
1 75  GLU n 
1 76  LEU n 
1 77  VAL n 
1 78  LEU n 
1 79  MET n 
1 80  LYS n 
1 81  CYS n 
1 82  VAL n 
1 83  ASN n 
1 84  HIS n 
1 85  LYS n 
1 86  ASN n 
1 87  ILE n 
1 88  ILE n 
1 89  GLY n 
1 90  LEU n 
1 91  LEU n 
1 92  ASN n 
1 93  VAL n 
1 94  PHE n 
1 95  THR n 
1 96  PRO n 
1 97  GLN n 
1 98  LYS n 
1 99  SER n 
1 100 LEU n 
1 101 GLU n 
1 102 GLU n 
1 103 PHE n 
1 104 GLN n 
1 105 ASP n 
1 106 VAL n 
1 107 TYR n 
1 108 ILE n 
1 109 VAL n 
1 110 MET n 
1 111 GLU n 
1 112 LEU n 
1 113 MET n 
1 114 ASP n 
1 115 ALA n 
1 116 ASN n 
1 117 LEU n 
1 118 CYS n 
1 119 GLN n 
1 120 VAL n 
1 121 ILE n 
1 122 GLN n 
1 123 MET n 
1 124 GLU n 
1 125 LEU n 
1 126 ASP n 
1 127 HIS n 
1 128 GLU n 
1 129 ARG n 
1 130 MET n 
1 131 SER n 
1 132 TYR n 
1 133 LEU n 
1 134 LEU n 
1 135 TYR n 
1 136 GLN n 
1 137 MET n 
1 138 LEU n 
1 139 CYS n 
1 140 GLY n 
1 141 ILE n 
1 142 LYS n 
1 143 HIS n 
1 144 LEU n 
1 145 HIS n 
1 146 SER n 
1 147 ALA n 
1 148 GLY n 
1 149 ILE n 
1 150 ILE n 
1 151 HIS n 
1 152 ARG n 
1 153 ASP n 
1 154 LEU n 
1 155 LYS n 
1 156 PRO n 
1 157 SER n 
1 158 ASN n 
1 159 ILE n 
1 160 VAL n 
1 161 VAL n 
1 162 LYS n 
1 163 SER n 
1 164 ASP n 
1 165 CYS n 
1 166 THR n 
1 167 LEU n 
1 168 LYS n 
1 169 ILE n 
1 170 LEU n 
1 171 ASP n 
1 172 PHE n 
1 173 GLY n 
1 174 LEU n 
1 175 ALA n 
1 176 ARG n 
1 177 THR n 
1 178 ALA n 
1 179 GLY n 
1 180 THR n 
1 181 SER n 
1 182 PHE n 
1 183 MET n 
1 184 MET n 
1 185 THR n 
1 186 PRO n 
1 187 TYR n 
1 188 VAL n 
1 189 VAL n 
1 190 THR n 
1 191 ARG n 
1 192 TYR n 
1 193 TYR n 
1 194 ARG n 
1 195 ALA n 
1 196 PRO n 
1 197 GLU n 
1 198 VAL n 
1 199 ILE n 
1 200 LEU n 
1 201 GLY n 
1 202 MET n 
1 203 GLY n 
1 204 TYR n 
1 205 LYS n 
1 206 GLU n 
1 207 ASN n 
1 208 VAL n 
1 209 ASP n 
1 210 ILE n 
1 211 TRP n 
1 212 SER n 
1 213 VAL n 
1 214 GLY n 
1 215 CYS n 
1 216 ILE n 
1 217 MET n 
1 218 GLY n 
1 219 GLU n 
1 220 MET n 
1 221 ILE n 
1 222 LYS n 
1 223 GLY n 
1 224 GLY n 
1 225 VAL n 
1 226 LEU n 
1 227 PHE n 
1 228 PRO n 
1 229 GLY n 
1 230 THR n 
1 231 ASP n 
1 232 HIS n 
1 233 ILE n 
1 234 ASP n 
1 235 GLN n 
1 236 TRP n 
1 237 ASN n 
1 238 LYS n 
1 239 VAL n 
1 240 ILE n 
1 241 GLU n 
1 242 GLN n 
1 243 LEU n 
1 244 GLY n 
1 245 THR n 
1 246 PRO n 
1 247 CYS n 
1 248 PRO n 
1 249 GLU n 
1 250 PHE n 
1 251 MET n 
1 252 LYS n 
1 253 LYS n 
1 254 LEU n 
1 255 GLN n 
1 256 PRO n 
1 257 THR n 
1 258 VAL n 
1 259 ARG n 
1 260 THR n 
1 261 TYR n 
1 262 VAL n 
1 263 GLU n 
1 264 ASN n 
1 265 ARG n 
1 266 PRO n 
1 267 LYS n 
1 268 TYR n 
1 269 ALA n 
1 270 GLY n 
1 271 TYR n 
1 272 SER n 
1 273 PHE n 
1 274 GLU n 
1 275 LYS n 
1 276 LEU n 
1 277 PHE n 
1 278 PRO n 
1 279 ASP n 
1 280 VAL n 
1 281 LEU n 
1 282 PHE n 
1 283 PRO n 
1 284 ALA n 
1 285 ASP n 
1 286 SER n 
1 287 GLU n 
1 288 HIS n 
1 289 ASN n 
1 290 LYS n 
1 291 LEU n 
1 292 LYS n 
1 293 ALA n 
1 294 SER n 
1 295 GLN n 
1 296 ALA n 
1 297 ARG n 
1 298 ASP n 
1 299 LEU n 
1 300 LEU n 
1 301 SER n 
1 302 LYS n 
1 303 MET n 
1 304 LEU n 
1 305 VAL n 
1 306 ILE n 
1 307 ASP n 
1 308 ALA n 
1 309 SER n 
1 310 LYS n 
1 311 ARG n 
1 312 ILE n 
1 313 SER n 
1 314 VAL n 
1 315 ASP n 
1 316 GLU n 
1 317 ALA n 
1 318 LEU n 
1 319 GLN n 
1 320 HIS n 
1 321 PRO n 
1 322 TYR n 
1 323 ILE n 
1 324 ASN n 
1 325 VAL n 
1 326 TRP n 
1 327 TYR n 
1 328 ASP n 
1 329 PRO n 
1 330 SER n 
1 331 GLU n 
1 332 ALA n 
1 333 GLU n 
1 334 ALA n 
1 335 PRO n 
1 336 PRO n 
1 337 PRO n 
1 338 LYS n 
1 339 ILE n 
1 340 PRO n 
1 341 ASP n 
1 342 LYS n 
1 343 GLN n 
1 344 LEU n 
1 345 ASP n 
1 346 GLU n 
1 347 ARG n 
1 348 GLU n 
1 349 HIS n 
1 350 THR n 
1 351 ILE n 
1 352 GLU n 
1 353 GLU n 
1 354 TRP n 
1 355 LYS n 
1 356 GLU n 
1 357 LEU n 
1 358 ILE n 
1 359 TYR n 
1 360 LYS n 
1 361 GLU n 
1 362 VAL n 
1 363 MET n 
1 364 ASP n 
1 365 LEU n 
1 366 GLU 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                   366 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MAPK8, JNK1, PRKM8, SAPK1, SAPK1C' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?                               'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ?                               'C10 H17 N6 O12 P3' 
506.196 
ARG 'L-peptide linking' y ARGININE ?                               'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE ?                               'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE ?                               'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE ?                               'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE ?                               'C2 H5 N O2'        75.067  
GOL non-polymer         . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'          92.094  
HIS 'L-peptide linking' y HISTIDINE ?                               'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER ?                               'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?                               'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE ?                               'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE ?                               'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE ?                               'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?                               'Mg 2'              24.305  
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 
Y6K non-polymer         . 
'~{O}3-~{tert}-butyl ~{O}1-methyl (1~{S},3~{R},5~{R})-6-methylidene-4-oxidanylidene-bicyclo[3.2.1]octane-1,3-dicarboxylate' ? 
'C16 H22 O5'        294.343 
# 
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   GLY 1   -1  ?   ?   ?   A . n 
A 1 2   SER 2   0   ?   ?   ?   A . n 
A 1 3   MET 3   1   ?   ?   ?   A . n 
A 1 4   SER 4   2   ?   ?   ?   A . n 
A 1 5   ARG 5   3   ?   ?   ?   A . n 
A 1 6   SER 6   4   ?   ?   ?   A . n 
A 1 7   LYS 7   5   5   LYS LYS A . n 
A 1 8   ARG 8   6   6   ARG ARG A . n 
A 1 9   ASP 9   7   7   ASP ASP A . n 
A 1 10  ASN 10  8   8   ASN ASN A . n 
A 1 11  ASN 11  9   9   ASN ASN A . n 
A 1 12  PHE 12  10  10  PHE PHE A . n 
A 1 13  TYR 13  11  11  TYR TYR A . n 
A 1 14  SER 14  12  12  SER SER A . n 
A 1 15  VAL 15  13  13  VAL VAL A . n 
A 1 16  GLU 16  14  14  GLU GLU A . n 
A 1 17  ILE 17  15  15  ILE ILE A . n 
A 1 18  GLY 18  16  16  GLY GLY A . n 
A 1 19  ASP 19  17  17  ASP ASP A . n 
A 1 20  SER 20  18  18  SER SER A . n 
A 1 21  THR 21  19  19  THR THR A . n 
A 1 22  PHE 22  20  20  PHE PHE A . n 
A 1 23  THR 23  21  21  THR THR A . n 
A 1 24  VAL 24  22  22  VAL VAL A . n 
A 1 25  LEU 25  23  23  LEU LEU A . n 
A 1 26  LYS 26  24  24  LYS LYS A . n 
A 1 27  ARG 27  25  25  ARG ARG A . n 
A 1 28  TYR 28  26  26  TYR TYR A . n 
A 1 29  GLN 29  27  27  GLN GLN A . n 
A 1 30  ASN 30  28  28  ASN ASN A . n 
A 1 31  LEU 31  29  29  LEU LEU A . n 
A 1 32  LYS 32  30  30  LYS LYS A . n 
A 1 33  PRO 33  31  31  PRO PRO A . n 
A 1 34  ILE 34  32  32  ILE ILE A . n 
A 1 35  GLY 35  33  33  GLY GLY A . n 
A 1 36  SER 36  34  34  SER SER A . n 
A 1 37  GLY 37  35  35  GLY GLY A . n 
A 1 38  ALA 38  36  36  ALA ALA A . n 
A 1 39  GLN 39  37  37  GLN GLN A . n 
A 1 40  GLY 40  38  38  GLY GLY A . n 
A 1 41  ILE 41  39  39  ILE ILE A . n 
A 1 42  VAL 42  40  40  VAL VAL A . n 
A 1 43  CYS 43  41  41  CYS CYS A . n 
A 1 44  ALA 44  42  42  ALA ALA A . n 
A 1 45  ALA 45  43  43  ALA ALA A . n 
A 1 46  TYR 46  44  44  TYR TYR A . n 
A 1 47  ASP 47  45  45  ASP ASP A . n 
A 1 48  ALA 48  46  46  ALA ALA A . n 
A 1 49  ILE 49  47  47  ILE ILE A . n 
A 1 50  LEU 50  48  48  LEU LEU A . n 
A 1 51  GLU 51  49  49  GLU GLU A . n 
A 1 52  ARG 52  50  50  ARG ARG A . n 
A 1 53  ASN 53  51  51  ASN ASN A . n 
A 1 54  VAL 54  52  52  VAL VAL A . n 
A 1 55  ALA 55  53  53  ALA ALA A . n 
A 1 56  ILE 56  54  54  ILE ILE A . n 
A 1 57  LYS 57  55  55  LYS LYS A . n 
A 1 58  LYS 58  56  56  LYS LYS A . n 
A 1 59  LEU 59  57  57  LEU LEU A . n 
A 1 60  SER 60  58  58  SER SER A . n 
A 1 61  ARG 61  59  59  ARG ARG A . n 
A 1 62  PRO 62  60  60  PRO PRO A . n 
A 1 63  PHE 63  61  61  PHE PHE A . n 
A 1 64  GLN 64  62  62  GLN GLN A . n 
A 1 65  ASN 65  63  63  ASN ASN A . n 
A 1 66  GLN 66  64  64  GLN GLN A . n 
A 1 67  THR 67  65  65  THR THR A . n 
A 1 68  HIS 68  66  66  HIS HIS A . n 
A 1 69  ALA 69  67  67  ALA ALA A . n 
A 1 70  LYS 70  68  68  LYS LYS A . n 
A 1 71  ARG 71  69  69  ARG ARG A . n 
A 1 72  ALA 72  70  70  ALA ALA A . n 
A 1 73  TYR 73  71  71  TYR TYR A . n 
A 1 74  ARG 74  72  72  ARG ARG A . n 
A 1 75  GLU 75  73  73  GLU GLU A . n 
A 1 76  LEU 76  74  74  LEU LEU A . n 
A 1 77  VAL 77  75  75  VAL VAL A . n 
A 1 78  LEU 78  76  76  LEU LEU A . n 
A 1 79  MET 79  77  77  MET MET A . n 
A 1 80  LYS 80  78  78  LYS LYS A . n 
A 1 81  CYS 81  79  79  CYS CYS A . n 
A 1 82  VAL 82  80  80  VAL VAL A . n 
A 1 83  ASN 83  81  81  ASN ASN A . n 
A 1 84  HIS 84  82  82  HIS HIS A . n 
A 1 85  LYS 85  83  83  LYS LYS A . n 
A 1 86  ASN 86  84  84  ASN ASN A . n 
A 1 87  ILE 87  85  85  ILE ILE A . n 
A 1 88  ILE 88  86  86  ILE ILE A . n 
A 1 89  GLY 89  87  87  GLY GLY A . n 
A 1 90  LEU 90  88  88  LEU LEU A . n 
A 1 91  LEU 91  89  89  LEU LEU A . n 
A 1 92  ASN 92  90  90  ASN ASN A . n 
A 1 93  VAL 93  91  91  VAL VAL A . n 
A 1 94  PHE 94  92  92  PHE PHE A . n 
A 1 95  THR 95  93  93  THR THR A . n 
A 1 96  PRO 96  94  94  PRO PRO A . n 
A 1 97  GLN 97  95  95  GLN GLN A . n 
A 1 98  LYS 98  96  96  LYS LYS A . n 
A 1 99  SER 99  97  97  SER SER A . n 
A 1 100 LEU 100 98  98  LEU LEU A . n 
A 1 101 GLU 101 99  99  GLU GLU A . n 
A 1 102 GLU 102 100 100 GLU GLU A . n 
A 1 103 PHE 103 101 101 PHE PHE A . n 
A 1 104 GLN 104 102 102 GLN GLN A . n 
A 1 105 ASP 105 103 103 ASP ASP A . n 
A 1 106 VAL 106 104 104 VAL VAL A . n 
A 1 107 TYR 107 105 105 TYR TYR A . n 
A 1 108 ILE 108 106 106 ILE ILE A . n 
A 1 109 VAL 109 107 107 VAL VAL A . n 
A 1 110 MET 110 108 108 MET MET A . n 
A 1 111 GLU 111 109 109 GLU GLU A . n 
A 1 112 LEU 112 110 110 LEU LEU A . n 
A 1 113 MET 113 111 111 MET MET A . n 
A 1 114 ASP 114 112 112 ASP ASP A . n 
A 1 115 ALA 115 113 113 ALA ALA A . n 
A 1 116 ASN 116 114 114 ASN ASN A . n 
A 1 117 LEU 117 115 115 LEU LEU A . n 
A 1 118 CYS 118 116 116 CYS CYS A . n 
A 1 119 GLN 119 117 117 GLN GLN A . n 
A 1 120 VAL 120 118 118 VAL VAL A . n 
A 1 121 ILE 121 119 119 ILE ILE A . n 
A 1 122 GLN 122 120 120 GLN GLN A . n 
A 1 123 MET 123 121 121 MET MET A . n 
A 1 124 GLU 124 122 122 GLU GLU A . n 
A 1 125 LEU 125 123 123 LEU LEU A . n 
A 1 126 ASP 126 124 124 ASP ASP A . n 
A 1 127 HIS 127 125 125 HIS HIS A . n 
A 1 128 GLU 128 126 126 GLU GLU A . n 
A 1 129 ARG 129 127 127 ARG ARG A . n 
A 1 130 MET 130 128 128 MET MET A . n 
A 1 131 SER 131 129 129 SER SER A . n 
A 1 132 TYR 132 130 130 TYR TYR A . n 
A 1 133 LEU 133 131 131 LEU LEU A . n 
A 1 134 LEU 134 132 132 LEU LEU A . n 
A 1 135 TYR 135 133 133 TYR TYR A . n 
A 1 136 GLN 136 134 134 GLN GLN A . n 
A 1 137 MET 137 135 135 MET MET A . n 
A 1 138 LEU 138 136 136 LEU LEU A . n 
A 1 139 CYS 139 137 137 CYS CYS A . n 
A 1 140 GLY 140 138 138 GLY GLY A . n 
A 1 141 ILE 141 139 139 ILE ILE A . n 
A 1 142 LYS 142 140 140 LYS LYS A . n 
A 1 143 HIS 143 141 141 HIS HIS A . n 
A 1 144 LEU 144 142 142 LEU LEU A . n 
A 1 145 HIS 145 143 143 HIS HIS A . n 
A 1 146 SER 146 144 144 SER SER A . n 
A 1 147 ALA 147 145 145 ALA ALA A . n 
A 1 148 GLY 148 146 146 GLY GLY A . n 
A 1 149 ILE 149 147 147 ILE ILE A . n 
A 1 150 ILE 150 148 148 ILE ILE A . n 
A 1 151 HIS 151 149 149 HIS HIS A . n 
A 1 152 ARG 152 150 150 ARG ARG A . n 
A 1 153 ASP 153 151 151 ASP ASP A . n 
A 1 154 LEU 154 152 152 LEU LEU A . n 
A 1 155 LYS 155 153 153 LYS LYS A . n 
A 1 156 PRO 156 154 154 PRO PRO A . n 
A 1 157 SER 157 155 155 SER SER A . n 
A 1 158 ASN 158 156 156 ASN ASN A . n 
A 1 159 ILE 159 157 157 ILE ILE A . n 
A 1 160 VAL 160 158 158 VAL VAL A . n 
A 1 161 VAL 161 159 159 VAL VAL A . n 
A 1 162 LYS 162 160 160 LYS LYS A . n 
A 1 163 SER 163 161 161 SER SER A . n 
A 1 164 ASP 164 162 162 ASP ASP A . n 
A 1 165 CYS 165 163 163 CYS CYS A . n 
A 1 166 THR 166 164 164 THR THR A . n 
A 1 167 LEU 167 165 165 LEU LEU A . n 
A 1 168 LYS 168 166 166 LYS LYS A . n 
A 1 169 ILE 169 167 167 ILE ILE A . n 
A 1 170 LEU 170 168 168 LEU LEU A . n 
A 1 171 ASP 171 169 169 ASP ASP A . n 
A 1 172 PHE 172 170 170 PHE PHE A . n 
A 1 173 GLY 173 171 171 GLY GLY A . n 
A 1 174 LEU 174 172 172 LEU LEU A . n 
A 1 175 ALA 175 173 173 ALA ALA A . n 
A 1 176 ARG 176 174 174 ARG ARG A . n 
A 1 177 THR 177 175 175 THR THR A . n 
A 1 178 ALA 178 176 176 ALA ALA A . n 
A 1 179 GLY 179 177 177 GLY GLY A . n 
A 1 180 THR 180 178 178 THR THR A . n 
A 1 181 SER 181 179 179 SER SER A . n 
A 1 182 PHE 182 180 180 PHE PHE A . n 
A 1 183 MET 183 181 181 MET MET A . n 
A 1 184 MET 184 182 182 MET MET A . n 
A 1 185 THR 185 183 183 THR THR A . n 
A 1 186 PRO 186 184 184 PRO PRO A . n 
A 1 187 TYR 187 185 185 TYR TYR A . n 
A 1 188 VAL 188 186 186 VAL VAL A . n 
A 1 189 VAL 189 187 187 VAL VAL A . n 
A 1 190 THR 190 188 188 THR THR A . n 
A 1 191 ARG 191 189 189 ARG ARG A . n 
A 1 192 TYR 192 190 190 TYR TYR A . n 
A 1 193 TYR 193 191 191 TYR TYR A . n 
A 1 194 ARG 194 192 192 ARG ARG A . n 
A 1 195 ALA 195 193 193 ALA ALA A . n 
A 1 196 PRO 196 194 194 PRO PRO A . n 
A 1 197 GLU 197 195 195 GLU GLU A . n 
A 1 198 VAL 198 196 196 VAL VAL A . n 
A 1 199 ILE 199 197 197 ILE ILE A . n 
A 1 200 LEU 200 198 198 LEU LEU A . n 
A 1 201 GLY 201 199 199 GLY GLY A . n 
A 1 202 MET 202 200 200 MET MET A . n 
A 1 203 GLY 203 201 201 GLY GLY A . n 
A 1 204 TYR 204 202 202 TYR TYR A . n 
A 1 205 LYS 205 203 203 LYS LYS A . n 
A 1 206 GLU 206 204 204 GLU GLU A . n 
A 1 207 ASN 207 205 205 ASN ASN A . n 
A 1 208 VAL 208 206 206 VAL VAL A . n 
A 1 209 ASP 209 207 207 ASP ASP A . n 
A 1 210 ILE 210 208 208 ILE ILE A . n 
A 1 211 TRP 211 209 209 TRP TRP A . n 
A 1 212 SER 212 210 210 SER SER A . n 
A 1 213 VAL 213 211 211 VAL VAL A . n 
A 1 214 GLY 214 212 212 GLY GLY A . n 
A 1 215 CYS 215 213 213 CYS CYS A . n 
A 1 216 ILE 216 214 214 ILE ILE A . n 
A 1 217 MET 217 215 215 MET MET A . n 
A 1 218 GLY 218 216 216 GLY GLY A . n 
A 1 219 GLU 219 217 217 GLU GLU A . n 
A 1 220 MET 220 218 218 MET MET A . n 
A 1 221 ILE 221 219 219 ILE ILE A . n 
A 1 222 LYS 222 220 220 LYS LYS A . n 
A 1 223 GLY 223 221 221 GLY GLY A . n 
A 1 224 GLY 224 222 222 GLY GLY A . n 
A 1 225 VAL 225 223 223 VAL VAL A . n 
A 1 226 LEU 226 224 224 LEU LEU A . n 
A 1 227 PHE 227 225 225 PHE PHE A . n 
A 1 228 PRO 228 226 226 PRO PRO A . n 
A 1 229 GLY 229 227 227 GLY GLY A . n 
A 1 230 THR 230 228 228 THR THR A . n 
A 1 231 ASP 231 229 229 ASP ASP A . n 
A 1 232 HIS 232 230 230 HIS HIS A . n 
A 1 233 ILE 233 231 231 ILE ILE A . n 
A 1 234 ASP 234 232 232 ASP ASP A . n 
A 1 235 GLN 235 233 233 GLN GLN A . n 
A 1 236 TRP 236 234 234 TRP TRP A . n 
A 1 237 ASN 237 235 235 ASN ASN A . n 
A 1 238 LYS 238 236 236 LYS LYS A . n 
A 1 239 VAL 239 237 237 VAL VAL A . n 
A 1 240 ILE 240 238 238 ILE ILE A . n 
A 1 241 GLU 241 239 239 GLU GLU A . n 
A 1 242 GLN 242 240 240 GLN GLN A . n 
A 1 243 LEU 243 241 241 LEU LEU A . n 
A 1 244 GLY 244 242 242 GLY GLY A . n 
A 1 245 THR 245 243 243 THR THR A . n 
A 1 246 PRO 246 244 244 PRO PRO A . n 
A 1 247 CYS 247 245 245 CYS CYS A . n 
A 1 248 PRO 248 246 246 PRO PRO A . n 
A 1 249 GLU 249 247 247 GLU GLU A . n 
A 1 250 PHE 250 248 248 PHE PHE A . n 
A 1 251 MET 251 249 249 MET MET A . n 
A 1 252 LYS 252 250 250 LYS LYS A . n 
A 1 253 LYS 253 251 251 LYS LYS A . n 
A 1 254 LEU 254 252 252 LEU LEU A . n 
A 1 255 GLN 255 253 253 GLN GLN A . n 
A 1 256 PRO 256 254 254 PRO PRO A . n 
A 1 257 THR 257 255 255 THR THR A . n 
A 1 258 VAL 258 256 256 VAL VAL A . n 
A 1 259 ARG 259 257 257 ARG ARG A . n 
A 1 260 THR 260 258 258 THR THR A . n 
A 1 261 TYR 261 259 259 TYR TYR A . n 
A 1 262 VAL 262 260 260 VAL VAL A . n 
A 1 263 GLU 263 261 261 GLU GLU A . n 
A 1 264 ASN 264 262 262 ASN ASN A . n 
A 1 265 ARG 265 263 263 ARG ARG A . n 
A 1 266 PRO 266 264 264 PRO PRO A . n 
A 1 267 LYS 267 265 265 LYS LYS A . n 
A 1 268 TYR 268 266 266 TYR TYR A . n 
A 1 269 ALA 269 267 267 ALA ALA A . n 
A 1 270 GLY 270 268 268 GLY GLY A . n 
A 1 271 TYR 271 269 269 TYR TYR A . n 
A 1 272 SER 272 270 270 SER SER A . n 
A 1 273 PHE 273 271 271 PHE PHE A . n 
A 1 274 GLU 274 272 272 GLU GLU A . n 
A 1 275 LYS 275 273 273 LYS LYS A . n 
A 1 276 LEU 276 274 274 LEU LEU A . n 
A 1 277 PHE 277 275 275 PHE PHE A . n 
A 1 278 PRO 278 276 276 PRO PRO A . n 
A 1 279 ASP 279 277 277 ASP ASP A . n 
A 1 280 VAL 280 278 278 VAL VAL A . n 
A 1 281 LEU 281 279 279 LEU LEU A . n 
A 1 282 PHE 282 280 280 PHE PHE A . n 
A 1 283 PRO 283 281 281 PRO PRO A . n 
A 1 284 ALA 284 282 282 ALA ALA A . n 
A 1 285 ASP 285 283 283 ASP ASP A . n 
A 1 286 SER 286 284 284 SER SER A . n 
A 1 287 GLU 287 285 285 GLU GLU A . n 
A 1 288 HIS 288 286 286 HIS HIS A . n 
A 1 289 ASN 289 287 287 ASN ASN A . n 
A 1 290 LYS 290 288 288 LYS LYS A . n 
A 1 291 LEU 291 289 289 LEU LEU A . n 
A 1 292 LYS 292 290 290 LYS LYS A . n 
A 1 293 ALA 293 291 291 ALA ALA A . n 
A 1 294 SER 294 292 292 SER SER A . n 
A 1 295 GLN 295 293 293 GLN GLN A . n 
A 1 296 ALA 296 294 294 ALA ALA A . n 
A 1 297 ARG 297 295 295 ARG ARG A . n 
A 1 298 ASP 298 296 296 ASP ASP A . n 
A 1 299 LEU 299 297 297 LEU LEU A . n 
A 1 300 LEU 300 298 298 LEU LEU A . n 
A 1 301 SER 301 299 299 SER SER A . n 
A 1 302 LYS 302 300 300 LYS LYS A . n 
A 1 303 MET 303 301 301 MET MET A . n 
A 1 304 LEU 304 302 302 LEU LEU A . n 
A 1 305 VAL 305 303 303 VAL VAL A . n 
A 1 306 ILE 306 304 304 ILE ILE A . n 
A 1 307 ASP 307 305 305 ASP ASP A . n 
A 1 308 ALA 308 306 306 ALA ALA A . n 
A 1 309 SER 309 307 307 SER SER A . n 
A 1 310 LYS 310 308 308 LYS LYS A . n 
A 1 311 ARG 311 309 309 ARG ARG A . n 
A 1 312 ILE 312 310 310 ILE ILE A . n 
A 1 313 SER 313 311 311 SER SER A . n 
A 1 314 VAL 314 312 312 VAL VAL A . n 
A 1 315 ASP 315 313 313 ASP ASP A . n 
A 1 316 GLU 316 314 314 GLU GLU A . n 
A 1 317 ALA 317 315 315 ALA ALA A . n 
A 1 318 LEU 318 316 316 LEU LEU A . n 
A 1 319 GLN 319 317 317 GLN GLN A . n 
A 1 320 HIS 320 318 318 HIS HIS A . n 
A 1 321 PRO 321 319 319 PRO PRO A . n 
A 1 322 TYR 322 320 320 TYR TYR A . n 
A 1 323 ILE 323 321 321 ILE ILE A . n 
A 1 324 ASN 324 322 322 ASN ASN A . n 
A 1 325 VAL 325 323 323 VAL VAL A . n 
A 1 326 TRP 326 324 324 TRP TRP A . n 
A 1 327 TYR 327 325 325 TYR TYR A . n 
A 1 328 ASP 328 326 326 ASP ASP A . n 
A 1 329 PRO 329 327 327 PRO PRO A . n 
A 1 330 SER 330 328 328 SER SER A . n 
A 1 331 GLU 331 329 329 GLU GLU A . n 
A 1 332 ALA 332 330 330 ALA ALA A . n 
A 1 333 GLU 333 331 331 GLU GLU A . n 
A 1 334 ALA 334 332 332 ALA ALA A . n 
A 1 335 PRO 335 333 333 PRO PRO A . n 
A 1 336 PRO 336 334 334 PRO PRO A . n 
A 1 337 PRO 337 335 335 PRO PRO A . n 
A 1 338 LYS 338 336 336 LYS LYS A . n 
A 1 339 ILE 339 337 337 ILE ILE A . n 
A 1 340 PRO 340 338 338 PRO PRO A . n 
A 1 341 ASP 341 339 339 ASP ASP A . n 
A 1 342 LYS 342 340 340 LYS LYS A . n 
A 1 343 GLN 343 341 341 GLN GLN A . n 
A 1 344 LEU 344 342 342 LEU LEU A . n 
A 1 345 ASP 345 343 343 ASP ASP A . n 
A 1 346 GLU 346 344 344 GLU GLU A . n 
A 1 347 ARG 347 345 345 ARG ARG A . n 
A 1 348 GLU 348 346 346 GLU GLU A . n 
A 1 349 HIS 349 347 347 HIS HIS A . n 
A 1 350 THR 350 348 348 THR THR A . n 
A 1 351 ILE 351 349 349 ILE ILE A . n 
A 1 352 GLU 352 350 350 GLU GLU A . n 
A 1 353 GLU 353 351 351 GLU GLU A . n 
A 1 354 TRP 354 352 352 TRP TRP A . n 
A 1 355 LYS 355 353 353 LYS LYS A . n 
A 1 356 GLU 356 354 354 GLU GLU A . n 
A 1 357 LEU 357 355 355 LEU LEU A . n 
A 1 358 ILE 358 356 356 ILE ILE A . n 
A 1 359 TYR 359 357 357 TYR TYR A . n 
A 1 360 LYS 360 358 358 LYS LYS A . n 
A 1 361 GLU 361 359 359 GLU GLU A . n 
A 1 362 VAL 362 360 360 VAL VAL A . n 
A 1 363 MET 363 361 361 MET MET A . n 
A 1 364 ASP 364 362 362 ASP ASP A . n 
A 1 365 LEU 365 363 363 LEU LEU A . n 
A 1 366 GLU 366 364 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        Y6K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Y6K 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 MG  1   401 405 MG  MG  A . 
C 3 ANP 1   402 407 ANP ANP A . 
D 4 Y6K 1   403 408 Y6K R77 A . 
E 5 GOL 1   404 409 GOL GOL A . 
F 6 HOH 1   501 72  HOH HOH A . 
F 6 HOH 2   502 71  HOH HOH A . 
F 6 HOH 3   503 73  HOH HOH A . 
F 6 HOH 4   504 89  HOH HOH A . 
F 6 HOH 5   505 53  HOH HOH A . 
F 6 HOH 6   506 47  HOH HOH A . 
F 6 HOH 7   507 110 HOH HOH A . 
F 6 HOH 8   508 75  HOH HOH A . 
F 6 HOH 9   509 97  HOH HOH A . 
F 6 HOH 10  510 66  HOH HOH A . 
F 6 HOH 11  511 105 HOH HOH A . 
F 6 HOH 12  512 90  HOH HOH A . 
F 6 HOH 13  513 82  HOH HOH A . 
F 6 HOH 14  514 77  HOH HOH A . 
F 6 HOH 15  515 126 HOH HOH A . 
F 6 HOH 16  516 79  HOH HOH A . 
F 6 HOH 17  517 85  HOH HOH A . 
F 6 HOH 18  518 27  HOH HOH A . 
F 6 HOH 19  519 95  HOH HOH A . 
F 6 HOH 20  520 128 HOH HOH A . 
F 6 HOH 21  521 112 HOH HOH A . 
F 6 HOH 22  522 40  HOH HOH A . 
F 6 HOH 23  523 50  HOH HOH A . 
F 6 HOH 24  524 33  HOH HOH A . 
F 6 HOH 25  525 86  HOH HOH A . 
F 6 HOH 26  526 31  HOH HOH A . 
F 6 HOH 27  527 39  HOH HOH A . 
F 6 HOH 28  528 102 HOH HOH A . 
F 6 HOH 29  529 4   HOH HOH A . 
F 6 HOH 30  530 117 HOH HOH A . 
F 6 HOH 31  531 123 HOH HOH A . 
F 6 HOH 32  532 92  HOH HOH A . 
F 6 HOH 33  533 6   HOH HOH A . 
F 6 HOH 34  534 113 HOH HOH A . 
F 6 HOH 35  535 51  HOH HOH A . 
F 6 HOH 36  536 23  HOH HOH A . 
F 6 HOH 37  537 30  HOH HOH A . 
F 6 HOH 38  538 119 HOH HOH A . 
F 6 HOH 39  539 70  HOH HOH A . 
F 6 HOH 40  540 36  HOH HOH A . 
F 6 HOH 41  541 84  HOH HOH A . 
F 6 HOH 42  542 131 HOH HOH A . 
F 6 HOH 43  543 120 HOH HOH A . 
F 6 HOH 44  544 58  HOH HOH A . 
F 6 HOH 45  545 15  HOH HOH A . 
F 6 HOH 46  546 122 HOH HOH A . 
F 6 HOH 47  547 65  HOH HOH A . 
F 6 HOH 48  548 68  HOH HOH A . 
F 6 HOH 49  549 60  HOH HOH A . 
F 6 HOH 50  550 20  HOH HOH A . 
F 6 HOH 51  551 9   HOH HOH A . 
F 6 HOH 52  552 7   HOH HOH A . 
F 6 HOH 53  553 18  HOH HOH A . 
F 6 HOH 54  554 55  HOH HOH A . 
F 6 HOH 55  555 67  HOH HOH A . 
F 6 HOH 56  556 28  HOH HOH A . 
F 6 HOH 57  557 106 HOH HOH A . 
F 6 HOH 58  558 29  HOH HOH A . 
F 6 HOH 59  559 21  HOH HOH A . 
F 6 HOH 60  560 35  HOH HOH A . 
F 6 HOH 61  561 5   HOH HOH A . 
F 6 HOH 62  562 49  HOH HOH A . 
F 6 HOH 63  563 12  HOH HOH A . 
F 6 HOH 64  564 11  HOH HOH A . 
F 6 HOH 65  565 17  HOH HOH A . 
F 6 HOH 66  566 37  HOH HOH A . 
F 6 HOH 67  567 62  HOH HOH A . 
F 6 HOH 68  568 109 HOH HOH A . 
F 6 HOH 69  569 1   HOH HOH A . 
F 6 HOH 70  570 8   HOH HOH A . 
F 6 HOH 71  571 103 HOH HOH A . 
F 6 HOH 72  572 45  HOH HOH A . 
F 6 HOH 73  573 16  HOH HOH A . 
F 6 HOH 74  574 125 HOH HOH A . 
F 6 HOH 75  575 42  HOH HOH A . 
F 6 HOH 76  576 26  HOH HOH A . 
F 6 HOH 77  577 116 HOH HOH A . 
F 6 HOH 78  578 38  HOH HOH A . 
F 6 HOH 79  579 44  HOH HOH A . 
F 6 HOH 80  580 80  HOH HOH A . 
F 6 HOH 81  581 124 HOH HOH A . 
F 6 HOH 82  582 10  HOH HOH A . 
F 6 HOH 83  583 87  HOH HOH A . 
F 6 HOH 84  584 64  HOH HOH A . 
F 6 HOH 85  585 3   HOH HOH A . 
F 6 HOH 86  586 13  HOH HOH A . 
F 6 HOH 87  587 2   HOH HOH A . 
F 6 HOH 88  588 115 HOH HOH A . 
F 6 HOH 89  589 88  HOH HOH A . 
F 6 HOH 90  590 25  HOH HOH A . 
F 6 HOH 91  591 94  HOH HOH A . 
F 6 HOH 92  592 81  HOH HOH A . 
F 6 HOH 93  593 54  HOH HOH A . 
F 6 HOH 94  594 63  HOH HOH A . 
F 6 HOH 95  595 41  HOH HOH A . 
F 6 HOH 96  596 101 HOH HOH A . 
F 6 HOH 97  597 14  HOH HOH A . 
F 6 HOH 98  598 76  HOH HOH A . 
F 6 HOH 99  599 111 HOH HOH A . 
F 6 HOH 100 600 59  HOH HOH A . 
F 6 HOH 101 601 24  HOH HOH A . 
F 6 HOH 102 602 46  HOH HOH A . 
F 6 HOH 103 603 132 HOH HOH A . 
F 6 HOH 104 604 61  HOH HOH A . 
F 6 HOH 105 605 34  HOH HOH A . 
F 6 HOH 106 606 121 HOH HOH A . 
F 6 HOH 107 607 107 HOH HOH A . 
F 6 HOH 108 608 19  HOH HOH A . 
F 6 HOH 109 609 129 HOH HOH A . 
F 6 HOH 110 610 52  HOH HOH A . 
F 6 HOH 111 611 57  HOH HOH A . 
F 6 HOH 112 612 56  HOH HOH A . 
F 6 HOH 113 613 69  HOH HOH A . 
F 6 HOH 114 614 32  HOH HOH A . 
F 6 HOH 115 615 22  HOH HOH A . 
F 6 HOH 116 616 104 HOH HOH A . 
F 6 HOH 117 617 91  HOH HOH A . 
F 6 HOH 118 618 99  HOH HOH A . 
F 6 HOH 119 619 43  HOH HOH A . 
F 6 HOH 120 620 48  HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 5   ? CG  ? A LYS 7   CG  
2  1 Y 1 A LYS 5   ? CD  ? A LYS 7   CD  
3  1 Y 1 A LYS 5   ? CE  ? A LYS 7   CE  
4  1 Y 1 A LYS 5   ? NZ  ? A LYS 7   NZ  
5  1 Y 1 A ARG 6   ? CD  ? A ARG 8   CD  
6  1 Y 1 A ARG 6   ? NE  ? A ARG 8   NE  
7  1 Y 1 A ARG 6   ? CZ  ? A ARG 8   CZ  
8  1 Y 1 A ARG 6   ? NH1 ? A ARG 8   NH1 
9  1 Y 1 A ARG 6   ? NH2 ? A ARG 8   NH2 
10 1 Y 1 A ASN 8   ? CG  ? A ASN 10  CG  
11 1 Y 1 A ASN 8   ? OD1 ? A ASN 10  OD1 
12 1 Y 1 A ASN 8   ? ND2 ? A ASN 10  ND2 
13 1 Y 1 A ASP 17  ? CG  ? A ASP 19  CG  
14 1 Y 1 A ASP 17  ? OD1 ? A ASP 19  OD1 
15 1 Y 1 A ASP 17  ? OD2 ? A ASP 19  OD2 
16 1 Y 1 A LYS 30  ? CD  ? A LYS 32  CD  
17 1 Y 1 A LYS 30  ? CE  ? A LYS 32  CE  
18 1 Y 1 A LYS 30  ? NZ  ? A LYS 32  NZ  
19 1 Y 1 A GLN 37  ? CG  ? A GLN 39  CG  
20 1 Y 1 A GLN 37  ? CD  ? A GLN 39  CD  
21 1 Y 1 A GLN 37  ? OE1 ? A GLN 39  OE1 
22 1 Y 1 A GLN 37  ? NE2 ? A GLN 39  NE2 
23 1 Y 1 A LYS 96  ? CG  ? A LYS 98  CG  
24 1 Y 1 A LYS 96  ? CD  ? A LYS 98  CD  
25 1 Y 1 A LYS 96  ? CE  ? A LYS 98  CE  
26 1 Y 1 A LYS 96  ? NZ  ? A LYS 98  NZ  
27 1 Y 1 A GLU 122 ? CG  ? A GLU 124 CG  
28 1 Y 1 A GLU 122 ? CD  ? A GLU 124 CD  
29 1 Y 1 A GLU 122 ? OE1 ? A GLU 124 OE1 
30 1 Y 1 A GLU 122 ? OE2 ? A GLU 124 OE2 
31 1 Y 1 A ARG 174 ? NE  ? A ARG 176 NE  
32 1 Y 1 A ARG 174 ? CZ  ? A ARG 176 CZ  
33 1 Y 1 A ARG 174 ? NH1 ? A ARG 176 NH1 
34 1 Y 1 A ARG 174 ? NH2 ? A ARG 176 NH2 
35 1 Y 1 A HIS 230 ? CG  ? A HIS 232 CG  
36 1 Y 1 A HIS 230 ? ND1 ? A HIS 232 ND1 
37 1 Y 1 A HIS 230 ? CD2 ? A HIS 232 CD2 
38 1 Y 1 A HIS 230 ? CE1 ? A HIS 232 CE1 
39 1 Y 1 A HIS 230 ? NE2 ? A HIS 232 NE2 
40 1 Y 1 A ASP 283 ? CG  ? A ASP 285 CG  
41 1 Y 1 A ASP 283 ? OD1 ? A ASP 285 OD1 
42 1 Y 1 A ASP 283 ? OD2 ? A ASP 285 OD2 
43 1 Y 1 A LYS 288 ? CD  ? A LYS 290 CD  
44 1 Y 1 A LYS 288 ? CE  ? A LYS 290 CE  
45 1 Y 1 A LYS 288 ? NZ  ? A LYS 290 NZ  
46 1 Y 1 A ASP 362 ? CG  ? A ASP 364 CG  
47 1 Y 1 A ASP 362 ? OD1 ? A ASP 364 OD1 
48 1 Y 1 A ASP 362 ? OD2 ? A ASP 364 OD2 
49 1 Y 1 A LEU 363 ? CG  ? A LEU 365 CG  
50 1 Y 1 A LEU 363 ? CD1 ? A LEU 365 CD1 
51 1 Y 1 A LEU 363 ? CD2 ? A LEU 365 CD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC    ? ? ? 5.8.0419 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? .        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                     8R5E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     65.341 
_cell.length_a_esd                 ? 
_cell.length_b                     75.249 
_cell.length_b_esd                 ? 
_cell.length_c                     82.869 
_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                         8R5E 
_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                   8R5E 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.42 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.18 
_exptl_crystal.description                  'Long rods' 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '8% PEG 20000 , 0,1 M HEPES pH 7.5, 10% MPD,  and as reservoir 1.25 M NaCl was used' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976300 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8R5E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.697 
_reflns.d_resolution_low                               65.341 
_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                                     34746 
_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                           94.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          22.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.060 
_reflns.pdbx_Rpim_I_all                                0.026 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.053 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.697 1.848 ? 1.712 ? ? ? ? 1737 ? ? ? ? ? ? ? ? ? ? ? 8.1  ? ? ? ? ? ? 1 1 0.7611 ? ? 67.6  ? 1.353 ? ? ? ? ? ? ? ? ? 
1.848 1.912 ? 2.207 ? ? ? ? 1738 ? ? ? ? ? ? ? ? ? ? ? 9.75 ? ? ? ? ? ? 2 1 0.7920 ? ? 76.15 ? ?     ? ? ? ? ? ? ? ? ? 
1.912 1.961 ? 2.438 ? ? ? ? 1737 ? ? ? ? ? ? ? ? ? ? ? 9.87 ? ? ? ? ? ? 3 1 0.8246 ? ? 88.3  ? ?     ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.23 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            0.07 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -0.29 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               37.106 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8R5E 
_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                            1.70 
_refine.ls_d_res_low                             55.77 
_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                     32690 
_refine.ls_number_reflns_R_free                  2001 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    75.56 
_refine.ls_percent_reflns_R_free                 5.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17719 
_refine.ls_R_factor_R_free                       0.22161 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17449 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.236 
_refine.pdbx_overall_ESU_R_Free                  0.128 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             5.911 
_refine.overall_SU_ML                            0.092 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        55.77 
_refine_hist.number_atoms_solvent             120 
_refine_hist.number_atoms_total               3023 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2844 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         59 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
_refine_ls_restr.pdbx_refine_id            'X-RAY DIFFRACTION' 
_refine_ls_restr.criterion                 ? 
_refine_ls_restr.dev_ideal                 0.007 
_refine_ls_restr.dev_ideal_target          0.012 
_refine_ls_restr.number                    2993 
_refine_ls_restr.rejects                   ? 
_refine_ls_restr.type                      r_bond_refined_d 
_refine_ls_restr.weight                    ? 
_refine_ls_restr.pdbx_restraint_function   ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7 
_refine_ls_shell.d_res_low                        1.741 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             10 
_refine_ls_shell.number_reflns_R_work             161 
_refine_ls_shell.percent_reflns_obs               5.12 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.351 
_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                  0.552 
# 
_struct.entry_id                     8R5E 
_struct.title                        'JNK1 covalently bound to RU77 cyclohexenone based inhibitor' 
_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        8R5E 
_struct_keywords.text            
'MAPK, MAP kinase, Kinase, Inhibitor, Covalent Inhibitor, Signaling Protein, c-Jun N-terminal kinases' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MK08_HUMAN 
_struct_ref.pdbx_db_accession          P45983 
_struct_ref.pdbx_db_isoform            P45983-3 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRSKRDNNFYSVEIGDSTFTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCV
NHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVK
SDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDLWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQ
LGTPCPEFMKKLQPTVRTYVENRPKYAGYSFEKLFPDVLFPADSEHNKLKASQARDLLSKMLVIDASKRISVDEALQHPY
INVWYDPSEAEAPPPKIPDKQLDEREHTIEEWKELIYKEVMDLE
;
_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              8R5E 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 3 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 366 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P45983 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  364 
_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       364 
# 
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 8R5E GLY A 1   ? UNP P45983 ?   ?   'expression tag' -1  1 
1 8R5E SER A 2   ? UNP P45983 ?   ?   'expression tag' 0   2 
1 8R5E ILE A 210 ? UNP P45983 LEU 208 variant          208 3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1140  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  16770 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'isothermal titration calorimetry' 
_pdbx_struct_assembly_auth_evidence.details                'JNK 163CYS is covalently linked to RU77 C3 carbon atom' 
# 
_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 ASN A 65  ? VAL A 82  ? ASN A 63  VAL A 80  1 ? 18 
HELX_P HELX_P2  AA2 LEU A 117 ? MET A 123 ? LEU A 115 MET A 121 1 ? 7  
HELX_P HELX_P3  AA3 ASP A 126 ? ALA A 147 ? ASP A 124 ALA A 145 1 ? 22 
HELX_P HELX_P4  AA4 LYS A 155 ? SER A 157 ? LYS A 153 SER A 155 5 ? 3  
HELX_P HELX_P5  AA5 ALA A 195 ? LEU A 200 ? ALA A 193 LEU A 198 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 207 ? GLY A 223 ? ASN A 205 GLY A 221 1 ? 17 
HELX_P HELX_P7  AA7 ASP A 231 ? GLY A 244 ? ASP A 229 GLY A 242 1 ? 14 
HELX_P HELX_P8  AA8 CYS A 247 ? LYS A 252 ? CYS A 245 LYS A 250 1 ? 6  
HELX_P HELX_P9  AA9 GLN A 255 ? ASN A 264 ? GLN A 253 ASN A 262 1 ? 10 
HELX_P HELX_P10 AB1 SER A 272 ? PHE A 277 ? SER A 270 PHE A 275 1 ? 6  
HELX_P HELX_P11 AB2 PRO A 278 ? PHE A 282 ? PRO A 276 PHE A 280 5 ? 5  
HELX_P HELX_P12 AB3 SER A 286 ? LEU A 304 ? SER A 284 LEU A 302 1 ? 19 
HELX_P HELX_P13 AB4 ASP A 307 ? ARG A 311 ? ASP A 305 ARG A 309 5 ? 5  
HELX_P HELX_P14 AB5 SER A 313 ? HIS A 320 ? SER A 311 HIS A 318 1 ? 8  
HELX_P HELX_P15 AB6 ILE A 323 ? TYR A 327 ? ILE A 321 TYR A 325 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 328 ? GLU A 333 ? ASP A 326 GLU A 331 1 ? 6  
HELX_P HELX_P17 AB8 THR A 350 ? ASP A 364 ? THR A 348 ASP A 362 1 ? 15 
# 
_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 
covale1 covale none ? A CYS 165 SG  ? ? ? 1_555 D Y6K . C3  ? ? A CYS 163 A Y6K 403 1_555 ? ? ? ? ? ? ? 1.807 ? ? 
metalc1 metalc ?    ? A ASN 158 OD1 ? ? ? 1_555 B MG  . MG  ? ? A ASN 156 A MG  401 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
metalc2 metalc ?    ? B MG  .   MG  ? ? ? 1_555 C ANP . O2A ? ? A MG  401 A ANP 402 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc3 metalc ?    ? B MG  .   MG  ? ? ? 1_555 C ANP . O1G ? ? A MG  401 A ANP 402 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc4 metalc ?    ? B MG  .   MG  ? ? ? 1_555 F HOH . O   ? ? A MG  401 A HOH 539 1_555 ? ? ? ? ? ? ? 2.199 ? ? 
metalc5 metalc ?    ? B MG  .   MG  ? ? ? 1_555 F HOH . O   ? ? A MG  401 A HOH 599 1_555 ? ? ? ? ? ? ? 1.916 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASN 158 ? A ASN 156 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O2A ? C ANP . ? A ANP 402 ? 1_555 78.4  ? 
2  OD1 ? A ASN 158 ? A ASN 156 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O1G ? C ANP . ? A ANP 402 ? 1_555 86.2  ? 
3  O2A ? C ANP .   ? A ANP 402 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O1G ? C ANP . ? A ANP 402 ? 1_555 70.2  ? 
4  OD1 ? A ASN 158 ? A ASN 156 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 539 ? 1_555 88.5  ? 
5  O2A ? C ANP .   ? A ANP 402 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 539 ? 1_555 159.2 ? 
6  O1G ? C ANP .   ? A ANP 402 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 539 ? 1_555 93.1  ? 
7  OD1 ? A ASN 158 ? A ASN 156 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 599 ? 1_555 97.6  ? 
8  O2A ? C ANP .   ? A ANP 402 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 599 ? 1_555 100.7 ? 
9  O1G ? C ANP .   ? A ANP 402 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 599 ? 1_555 169.3 ? 
10 O   ? F HOH .   ? A HOH 539 ? 1_555 MG ? B MG . ? A MG 401 ? 1_555 O   ? F HOH . ? A HOH 599 ? 1_555 97.0  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      Y6K 
_pdbx_modification_feature.label_asym_id                      D 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      165 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       Y6K 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        403 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       163 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C3 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        Y6K 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 PHE A 12  ? ILE A 17  ? PHE A 10  ILE A 15  
AA1 2 SER A 20  ? LEU A 25  ? SER A 18  LEU A 23  
AA2 1 TYR A 28  ? GLY A 35  ? TYR A 26  GLY A 33  
AA2 2 ILE A 41  ? ASP A 47  ? ILE A 39  ASP A 45  
AA2 3 ARG A 52  ? SER A 60  ? ARG A 50  SER A 58  
AA2 4 ASP A 105 ? GLU A 111 ? ASP A 103 GLU A 109 
AA2 5 LEU A 90  ? PHE A 94  ? LEU A 88  PHE A 92  
AA3 1 ALA A 115 ? ASN A 116 ? ALA A 113 ASN A 114 
AA3 2 ILE A 159 ? VAL A 161 ? ILE A 157 VAL A 159 
AA3 3 LEU A 167 ? ILE A 169 ? LEU A 165 ILE A 167 
# 
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 15  ? N VAL A 13  O PHE A 22  ? O PHE A 20  
AA2 1 2 N LYS A 32  ? N LYS A 30  O ALA A 44  ? O ALA A 42  
AA2 2 3 N CYS A 43  ? N CYS A 41  O ILE A 56  ? O ILE A 54  
AA2 3 4 N LEU A 59  ? N LEU A 57  O VAL A 106 ? O VAL A 104 
AA2 4 5 O TYR A 107 ? O TYR A 105 N PHE A 94  ? N PHE A 92  
AA3 1 2 N ALA A 115 ? N ALA A 113 O VAL A 161 ? O VAL A 159 
AA3 2 3 N VAL A 160 ? N VAL A 158 O LYS A 168 ? O LYS A 166 
# 
_pdbx_entry_details.entry_id                   8R5E 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 ASN A 8   ? ? -58.50  -2.37   
2 1 GLN A 102 ? ? -128.38 -55.49  
3 1 ARG A 150 ? ? 76.05   -10.25  
4 1 CYS A 163 ? ? 86.96   5.95    
5 1 ALA A 173 ? ? 60.28   -130.18 
6 1 ALA A 282 ? ? -162.33 43.07   
# 
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 GLY -1  ? A GLY 1   
2 1 Y 1 A SER 0   ? A SER 2   
3 1 Y 1 A MET 1   ? A MET 3   
4 1 Y 1 A SER 2   ? A SER 4   
5 1 Y 1 A ARG 3   ? A ARG 5   
6 1 Y 1 A SER 4   ? A SER 6   
7 1 Y 1 A GLU 364 ? A GLU 366 
# 
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  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
GOL C1     C  N N 185 
GOL O1     O  N N 186 
GOL C2     C  N N 187 
GOL O2     O  N N 188 
GOL C3     C  N N 189 
GOL O3     O  N N 190 
GOL H11    H  N N 191 
GOL H12    H  N N 192 
GOL HO1    H  N N 193 
GOL H2     H  N N 194 
GOL HO2    H  N N 195 
GOL H31    H  N N 196 
GOL H32    H  N N 197 
GOL HO3    H  N N 198 
HIS N      N  N N 199 
HIS CA     C  N S 200 
HIS C      C  N N 201 
HIS O      O  N N 202 
HIS CB     C  N N 203 
HIS CG     C  Y N 204 
HIS ND1    N  Y N 205 
HIS CD2    C  Y N 206 
HIS CE1    C  Y N 207 
HIS NE2    N  Y N 208 
HIS OXT    O  N N 209 
HIS H      H  N N 210 
HIS H2     H  N N 211 
HIS HA     H  N N 212 
HIS HB2    H  N N 213 
HIS HB3    H  N N 214 
HIS HD1    H  N N 215 
HIS HD2    H  N N 216 
HIS HE1    H  N N 217 
HIS HE2    H  N N 218 
HIS HXT    H  N N 219 
HOH O      O  N N 220 
HOH H1     H  N N 221 
HOH H2     H  N N 222 
ILE N      N  N N 223 
ILE CA     C  N S 224 
ILE C      C  N N 225 
ILE O      O  N N 226 
ILE CB     C  N S 227 
ILE CG1    C  N N 228 
ILE CG2    C  N N 229 
ILE CD1    C  N N 230 
ILE OXT    O  N N 231 
ILE H      H  N N 232 
ILE H2     H  N N 233 
ILE HA     H  N N 234 
ILE HB     H  N N 235 
ILE HG12   H  N N 236 
ILE HG13   H  N N 237 
ILE HG21   H  N N 238 
ILE HG22   H  N N 239 
ILE HG23   H  N N 240 
ILE HD11   H  N N 241 
ILE HD12   H  N N 242 
ILE HD13   H  N N 243 
ILE HXT    H  N N 244 
LEU N      N  N N 245 
LEU CA     C  N S 246 
LEU C      C  N N 247 
LEU O      O  N N 248 
LEU CB     C  N N 249 
LEU CG     C  N N 250 
LEU CD1    C  N N 251 
LEU CD2    C  N N 252 
LEU OXT    O  N N 253 
LEU H      H  N N 254 
LEU H2     H  N N 255 
LEU HA     H  N N 256 
LEU HB2    H  N N 257 
LEU HB3    H  N N 258 
LEU HG     H  N N 259 
LEU HD11   H  N N 260 
LEU HD12   H  N N 261 
LEU HD13   H  N N 262 
LEU HD21   H  N N 263 
LEU HD22   H  N N 264 
LEU HD23   H  N N 265 
LEU HXT    H  N N 266 
LYS N      N  N N 267 
LYS CA     C  N S 268 
LYS C      C  N N 269 
LYS O      O  N N 270 
LYS CB     C  N N 271 
LYS CG     C  N N 272 
LYS CD     C  N N 273 
LYS CE     C  N N 274 
LYS NZ     N  N N 275 
LYS OXT    O  N N 276 
LYS H      H  N N 277 
LYS H2     H  N N 278 
LYS HA     H  N N 279 
LYS HB2    H  N N 280 
LYS HB3    H  N N 281 
LYS HG2    H  N N 282 
LYS HG3    H  N N 283 
LYS HD2    H  N N 284 
LYS HD3    H  N N 285 
LYS HE2    H  N N 286 
LYS HE3    H  N N 287 
LYS HZ1    H  N N 288 
LYS HZ2    H  N N 289 
LYS HZ3    H  N N 290 
LYS HXT    H  N N 291 
MET N      N  N N 292 
MET CA     C  N S 293 
MET C      C  N N 294 
MET O      O  N N 295 
MET CB     C  N N 296 
MET CG     C  N N 297 
MET SD     S  N N 298 
MET CE     C  N N 299 
MET OXT    O  N N 300 
MET H      H  N N 301 
MET H2     H  N N 302 
MET HA     H  N N 303 
MET HB2    H  N N 304 
MET HB3    H  N N 305 
MET HG2    H  N N 306 
MET HG3    H  N N 307 
MET HE1    H  N N 308 
MET HE2    H  N N 309 
MET HE3    H  N N 310 
MET HXT    H  N N 311 
MG  MG     MG N N 312 
PHE N      N  N N 313 
PHE CA     C  N S 314 
PHE C      C  N N 315 
PHE O      O  N N 316 
PHE CB     C  N N 317 
PHE CG     C  Y N 318 
PHE CD1    C  Y N 319 
PHE CD2    C  Y N 320 
PHE CE1    C  Y N 321 
PHE CE2    C  Y N 322 
PHE CZ     C  Y N 323 
PHE OXT    O  N N 324 
PHE H      H  N N 325 
PHE H2     H  N N 326 
PHE HA     H  N N 327 
PHE HB2    H  N N 328 
PHE HB3    H  N N 329 
PHE HD1    H  N N 330 
PHE HD2    H  N N 331 
PHE HE1    H  N N 332 
PHE HE2    H  N N 333 
PHE HZ     H  N N 334 
PHE HXT    H  N N 335 
PRO N      N  N N 336 
PRO CA     C  N S 337 
PRO C      C  N N 338 
PRO O      O  N N 339 
PRO CB     C  N N 340 
PRO CG     C  N N 341 
PRO CD     C  N N 342 
PRO OXT    O  N N 343 
PRO H      H  N N 344 
PRO HA     H  N N 345 
PRO HB2    H  N N 346 
PRO HB3    H  N N 347 
PRO HG2    H  N N 348 
PRO HG3    H  N N 349 
PRO HD2    H  N N 350 
PRO HD3    H  N N 351 
PRO HXT    H  N N 352 
SER N      N  N N 353 
SER CA     C  N S 354 
SER C      C  N N 355 
SER O      O  N N 356 
SER CB     C  N N 357 
SER OG     O  N N 358 
SER OXT    O  N N 359 
SER H      H  N N 360 
SER H2     H  N N 361 
SER HA     H  N N 362 
SER HB2    H  N N 363 
SER HB3    H  N N 364 
SER HG     H  N N 365 
SER HXT    H  N N 366 
THR N      N  N N 367 
THR CA     C  N S 368 
THR C      C  N N 369 
THR O      O  N N 370 
THR CB     C  N R 371 
THR OG1    O  N N 372 
THR CG2    C  N N 373 
THR OXT    O  N N 374 
THR H      H  N N 375 
THR H2     H  N N 376 
THR HA     H  N N 377 
THR HB     H  N N 378 
THR HG1    H  N N 379 
THR HG21   H  N N 380 
THR HG22   H  N N 381 
THR HG23   H  N N 382 
THR HXT    H  N N 383 
TRP N      N  N N 384 
TRP CA     C  N S 385 
TRP C      C  N N 386 
TRP O      O  N N 387 
TRP CB     C  N N 388 
TRP CG     C  Y N 389 
TRP CD1    C  Y N 390 
TRP CD2    C  Y N 391 
TRP NE1    N  Y N 392 
TRP CE2    C  Y N 393 
TRP CE3    C  Y N 394 
TRP CZ2    C  Y N 395 
TRP CZ3    C  Y N 396 
TRP CH2    C  Y N 397 
TRP OXT    O  N N 398 
TRP H      H  N N 399 
TRP H2     H  N N 400 
TRP HA     H  N N 401 
TRP HB2    H  N N 402 
TRP HB3    H  N N 403 
TRP HD1    H  N N 404 
TRP HE1    H  N N 405 
TRP HE3    H  N N 406 
TRP HZ2    H  N N 407 
TRP HZ3    H  N N 408 
TRP HH2    H  N N 409 
TRP HXT    H  N N 410 
TYR N      N  N N 411 
TYR CA     C  N S 412 
TYR C      C  N N 413 
TYR O      O  N N 414 
TYR CB     C  N N 415 
TYR CG     C  Y N 416 
TYR CD1    C  Y N 417 
TYR CD2    C  Y N 418 
TYR CE1    C  Y N 419 
TYR CE2    C  Y N 420 
TYR CZ     C  Y N 421 
TYR OH     O  N N 422 
TYR OXT    O  N N 423 
TYR H      H  N N 424 
TYR H2     H  N N 425 
TYR HA     H  N N 426 
TYR HB2    H  N N 427 
TYR HB3    H  N N 428 
TYR HD1    H  N N 429 
TYR HD2    H  N N 430 
TYR HE1    H  N N 431 
TYR HE2    H  N N 432 
TYR HH     H  N N 433 
TYR HXT    H  N N 434 
VAL N      N  N N 435 
VAL CA     C  N S 436 
VAL C      C  N N 437 
VAL O      O  N N 438 
VAL CB     C  N N 439 
VAL CG1    C  N N 440 
VAL CG2    C  N N 441 
VAL OXT    O  N N 442 
VAL H      H  N N 443 
VAL H2     H  N N 444 
VAL HA     H  N N 445 
VAL HB     H  N N 446 
VAL HG11   H  N N 447 
VAL HG12   H  N N 448 
VAL HG13   H  N N 449 
VAL HG21   H  N N 450 
VAL HG22   H  N N 451 
VAL HG23   H  N N 452 
VAL HXT    H  N N 453 
Y6K C1     C  N N 454 
Y6K C2     C  N R 455 
Y6K C3     C  N N 456 
Y6K C8     C  N N 457 
Y6K C14    C  N N 458 
Y6K C15    C  N N 459 
Y6K C16    C  N N 460 
Y6K C17    C  N N 461 
Y6K C19    C  N N 462 
Y6K C20    C  N N 463 
Y6K C18    C  N N 464 
Y6K C7     C  N N 465 
Y6K C5     C  N N 466 
Y6K C6     C  N R 467 
Y6K C9     C  N N 468 
Y6K C4     C  N S 469 
Y6K O4     O  N N 470 
Y6K O3     O  N N 471 
Y6K O2     O  N N 472 
Y6K O      O  N N 473 
Y6K O1     O  N N 474 
Y6K H1     H  N N 475 
Y6K H2     H  N N 476 
Y6K H3     H  N N 477 
Y6K H4     H  N N 478 
Y6K H5     H  N N 479 
Y6K H6     H  N N 480 
Y6K H7     H  N N 481 
Y6K H8     H  N N 482 
Y6K H9     H  N N 483 
Y6K H10    H  N N 484 
Y6K H11    H  N N 485 
Y6K H12    H  N N 486 
Y6K H13    H  N N 487 
Y6K H14    H  N N 488 
Y6K H15    H  N N 489 
Y6K H16    H  N N 490 
Y6K H17    H  N N 491 
Y6K H18    H  N N 492 
Y6K H19    H  N N 493 
Y6K H20    H  N N 494 
Y6K H21    H  N N 495 
Y6K H22    H  N N 496 
# 
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  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
GOL C1    O1     sing N N 179 
GOL C1    C2     sing N N 180 
GOL C1    H11    sing N N 181 
GOL C1    H12    sing N N 182 
GOL O1    HO1    sing N N 183 
GOL C2    O2     sing N N 184 
GOL C2    C3     sing N N 185 
GOL C2    H2     sing N N 186 
GOL O2    HO2    sing N N 187 
GOL C3    O3     sing N N 188 
GOL C3    H31    sing N N 189 
GOL C3    H32    sing N N 190 
GOL O3    HO3    sing N N 191 
HIS N     CA     sing N N 192 
HIS N     H      sing N N 193 
HIS N     H2     sing N N 194 
HIS CA    C      sing N N 195 
HIS CA    CB     sing N N 196 
HIS CA    HA     sing N N 197 
HIS C     O      doub N N 198 
HIS C     OXT    sing N N 199 
HIS CB    CG     sing N N 200 
HIS CB    HB2    sing N N 201 
HIS CB    HB3    sing N N 202 
HIS CG    ND1    sing Y N 203 
HIS CG    CD2    doub Y N 204 
HIS ND1   CE1    doub Y N 205 
HIS ND1   HD1    sing N N 206 
HIS CD2   NE2    sing Y N 207 
HIS CD2   HD2    sing N N 208 
HIS CE1   NE2    sing Y N 209 
HIS CE1   HE1    sing N N 210 
HIS NE2   HE2    sing N N 211 
HIS OXT   HXT    sing N N 212 
HOH O     H1     sing N N 213 
HOH O     H2     sing N N 214 
ILE N     CA     sing N N 215 
ILE N     H      sing N N 216 
ILE N     H2     sing N N 217 
ILE CA    C      sing N N 218 
ILE CA    CB     sing N N 219 
ILE CA    HA     sing N N 220 
ILE C     O      doub N N 221 
ILE C     OXT    sing N N 222 
ILE CB    CG1    sing N N 223 
ILE CB    CG2    sing N N 224 
ILE CB    HB     sing N N 225 
ILE CG1   CD1    sing N N 226 
ILE CG1   HG12   sing N N 227 
ILE CG1   HG13   sing N N 228 
ILE CG2   HG21   sing N N 229 
ILE CG2   HG22   sing N N 230 
ILE CG2   HG23   sing N N 231 
ILE CD1   HD11   sing N N 232 
ILE CD1   HD12   sing N N 233 
ILE CD1   HD13   sing N N 234 
ILE OXT   HXT    sing N N 235 
LEU N     CA     sing N N 236 
LEU N     H      sing N N 237 
LEU N     H2     sing N N 238 
LEU CA    C      sing N N 239 
LEU CA    CB     sing N N 240 
LEU CA    HA     sing N N 241 
LEU C     O      doub N N 242 
LEU C     OXT    sing N N 243 
LEU CB    CG     sing N N 244 
LEU CB    HB2    sing N N 245 
LEU CB    HB3    sing N N 246 
LEU CG    CD1    sing N N 247 
LEU CG    CD2    sing N N 248 
LEU CG    HG     sing N N 249 
LEU CD1   HD11   sing N N 250 
LEU CD1   HD12   sing N N 251 
LEU CD1   HD13   sing N N 252 
LEU CD2   HD21   sing N N 253 
LEU CD2   HD22   sing N N 254 
LEU CD2   HD23   sing N N 255 
LEU OXT   HXT    sing N N 256 
LYS N     CA     sing N N 257 
LYS N     H      sing N N 258 
LYS N     H2     sing N N 259 
LYS CA    C      sing N N 260 
LYS CA    CB     sing N N 261 
LYS CA    HA     sing N N 262 
LYS C     O      doub N N 263 
LYS C     OXT    sing N N 264 
LYS CB    CG     sing N N 265 
LYS CB    HB2    sing N N 266 
LYS CB    HB3    sing N N 267 
LYS CG    CD     sing N N 268 
LYS CG    HG2    sing N N 269 
LYS CG    HG3    sing N N 270 
LYS CD    CE     sing N N 271 
LYS CD    HD2    sing N N 272 
LYS CD    HD3    sing N N 273 
LYS CE    NZ     sing N N 274 
LYS CE    HE2    sing N N 275 
LYS CE    HE3    sing N N 276 
LYS NZ    HZ1    sing N N 277 
LYS NZ    HZ2    sing N N 278 
LYS NZ    HZ3    sing N N 279 
LYS OXT   HXT    sing N N 280 
MET N     CA     sing N N 281 
MET N     H      sing N N 282 
MET N     H2     sing N N 283 
MET CA    C      sing N N 284 
MET CA    CB     sing N N 285 
MET CA    HA     sing N N 286 
MET C     O      doub N N 287 
MET C     OXT    sing N N 288 
MET CB    CG     sing N N 289 
MET CB    HB2    sing N N 290 
MET CB    HB3    sing N N 291 
MET CG    SD     sing N N 292 
MET CG    HG2    sing N N 293 
MET CG    HG3    sing N N 294 
MET SD    CE     sing N N 295 
MET CE    HE1    sing N N 296 
MET CE    HE2    sing N N 297 
MET CE    HE3    sing N N 298 
MET OXT   HXT    sing N N 299 
PHE N     CA     sing N N 300 
PHE N     H      sing N N 301 
PHE N     H2     sing N N 302 
PHE CA    C      sing N N 303 
PHE CA    CB     sing N N 304 
PHE CA    HA     sing N N 305 
PHE C     O      doub N N 306 
PHE C     OXT    sing N N 307 
PHE CB    CG     sing N N 308 
PHE CB    HB2    sing N N 309 
PHE CB    HB3    sing N N 310 
PHE CG    CD1    doub Y N 311 
PHE CG    CD2    sing Y N 312 
PHE CD1   CE1    sing Y N 313 
PHE CD1   HD1    sing N N 314 
PHE CD2   CE2    doub Y N 315 
PHE CD2   HD2    sing N N 316 
PHE CE1   CZ     doub Y N 317 
PHE CE1   HE1    sing N N 318 
PHE CE2   CZ     sing Y N 319 
PHE CE2   HE2    sing N N 320 
PHE CZ    HZ     sing N N 321 
PHE OXT   HXT    sing N N 322 
PRO N     CA     sing N N 323 
PRO N     CD     sing N N 324 
PRO N     H      sing N N 325 
PRO CA    C      sing N N 326 
PRO CA    CB     sing N N 327 
PRO CA    HA     sing N N 328 
PRO C     O      doub N N 329 
PRO C     OXT    sing N N 330 
PRO CB    CG     sing N N 331 
PRO CB    HB2    sing N N 332 
PRO CB    HB3    sing N N 333 
PRO CG    CD     sing N N 334 
PRO CG    HG2    sing N N 335 
PRO CG    HG3    sing N N 336 
PRO CD    HD2    sing N N 337 
PRO CD    HD3    sing N N 338 
PRO OXT   HXT    sing N N 339 
SER N     CA     sing N N 340 
SER N     H      sing N N 341 
SER N     H2     sing N N 342 
SER CA    C      sing N N 343 
SER CA    CB     sing N N 344 
SER CA    HA     sing N N 345 
SER C     O      doub N N 346 
SER C     OXT    sing N N 347 
SER CB    OG     sing N N 348 
SER CB    HB2    sing N N 349 
SER CB    HB3    sing N N 350 
SER OG    HG     sing N N 351 
SER OXT   HXT    sing N N 352 
THR N     CA     sing N N 353 
THR N     H      sing N N 354 
THR N     H2     sing N N 355 
THR CA    C      sing N N 356 
THR CA    CB     sing N N 357 
THR CA    HA     sing N N 358 
THR C     O      doub N N 359 
THR C     OXT    sing N N 360 
THR CB    OG1    sing N N 361 
THR CB    CG2    sing N N 362 
THR CB    HB     sing N N 363 
THR OG1   HG1    sing N N 364 
THR CG2   HG21   sing N N 365 
THR CG2   HG22   sing N N 366 
THR CG2   HG23   sing N N 367 
THR OXT   HXT    sing N N 368 
TRP N     CA     sing N N 369 
TRP N     H      sing N N 370 
TRP N     H2     sing N N 371 
TRP CA    C      sing N N 372 
TRP CA    CB     sing N N 373 
TRP CA    HA     sing N N 374 
TRP C     O      doub N N 375 
TRP C     OXT    sing N N 376 
TRP CB    CG     sing N N 377 
TRP CB    HB2    sing N N 378 
TRP CB    HB3    sing N N 379 
TRP CG    CD1    doub Y N 380 
TRP CG    CD2    sing Y N 381 
TRP CD1   NE1    sing Y N 382 
TRP CD1   HD1    sing N N 383 
TRP CD2   CE2    doub Y N 384 
TRP CD2   CE3    sing Y N 385 
TRP NE1   CE2    sing Y N 386 
TRP NE1   HE1    sing N N 387 
TRP CE2   CZ2    sing Y N 388 
TRP CE3   CZ3    doub Y N 389 
TRP CE3   HE3    sing N N 390 
TRP CZ2   CH2    doub Y N 391 
TRP CZ2   HZ2    sing N N 392 
TRP CZ3   CH2    sing Y N 393 
TRP CZ3   HZ3    sing N N 394 
TRP CH2   HH2    sing N N 395 
TRP OXT   HXT    sing N N 396 
TYR N     CA     sing N N 397 
TYR N     H      sing N N 398 
TYR N     H2     sing N N 399 
TYR CA    C      sing N N 400 
TYR CA    CB     sing N N 401 
TYR CA    HA     sing N N 402 
TYR C     O      doub N N 403 
TYR C     OXT    sing N N 404 
TYR CB    CG     sing N N 405 
TYR CB    HB2    sing N N 406 
TYR CB    HB3    sing N N 407 
TYR CG    CD1    doub Y N 408 
TYR CG    CD2    sing Y N 409 
TYR CD1   CE1    sing Y N 410 
TYR CD1   HD1    sing N N 411 
TYR CD2   CE2    doub Y N 412 
TYR CD2   HD2    sing N N 413 
TYR CE1   CZ     doub Y N 414 
TYR CE1   HE1    sing N N 415 
TYR CE2   CZ     sing Y N 416 
TYR CE2   HE2    sing N N 417 
TYR CZ    OH     sing N N 418 
TYR OH    HH     sing N N 419 
TYR OXT   HXT    sing N N 420 
VAL N     CA     sing N N 421 
VAL N     H      sing N N 422 
VAL N     H2     sing N N 423 
VAL CA    C      sing N N 424 
VAL CA    CB     sing N N 425 
VAL CA    HA     sing N N 426 
VAL C     O      doub N N 427 
VAL C     OXT    sing N N 428 
VAL CB    CG1    sing N N 429 
VAL CB    CG2    sing N N 430 
VAL CB    HB     sing N N 431 
VAL CG1   HG11   sing N N 432 
VAL CG1   HG12   sing N N 433 
VAL CG1   HG13   sing N N 434 
VAL CG2   HG21   sing N N 435 
VAL CG2   HG22   sing N N 436 
VAL CG2   HG23   sing N N 437 
VAL OXT   HXT    sing N N 438 
Y6K C18   C17    sing N N 439 
Y6K C20   C17    sing N N 440 
Y6K C17   O3     sing N N 441 
Y6K C17   C19    sing N N 442 
Y6K O3    C16    sing N N 443 
Y6K C16   O2     doub N N 444 
Y6K C16   C2     sing N N 445 
Y6K C7    C8     sing N N 446 
Y6K C7    C4     sing N N 447 
Y6K C9    C8     doub N N 448 
Y6K C8    C6     sing N N 449 
Y6K O1    C14    doub N N 450 
Y6K C2    C3     sing N N 451 
Y6K C2    C1     sing N N 452 
Y6K C3    C4     sing N N 453 
Y6K C4    C14    sing N N 454 
Y6K C4    C5     sing N N 455 
Y6K O4    C1     doub N N 456 
Y6K C1    C6     sing N N 457 
Y6K C14   O      sing N N 458 
Y6K C6    C5     sing N N 459 
Y6K O     C15    sing N N 460 
Y6K C2    H1     sing N N 461 
Y6K C3    H2     sing N N 462 
Y6K C3    H3     sing N N 463 
Y6K C15   H4     sing N N 464 
Y6K C15   H5     sing N N 465 
Y6K C15   H6     sing N N 466 
Y6K C19   H7     sing N N 467 
Y6K C19   H8     sing N N 468 
Y6K C19   H9     sing N N 469 
Y6K C20   H10    sing N N 470 
Y6K C20   H11    sing N N 471 
Y6K C20   H12    sing N N 472 
Y6K C18   H13    sing N N 473 
Y6K C18   H14    sing N N 474 
Y6K C18   H15    sing N N 475 
Y6K C7    H16    sing N N 476 
Y6K C7    H17    sing N N 477 
Y6K C5    H18    sing N N 478 
Y6K C5    H19    sing N N 479 
Y6K C6    H20    sing N N 480 
Y6K C9    H21    sing N N 481 
Y6K C9    H22    sing N N 482 
# 
_pdbx_audit_support.funding_organization   'Hungarian National Research, Development and Innovation Office' 
_pdbx_audit_support.country                Hungary 
_pdbx_audit_support.grant_number           'KKP 126963' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3v6s 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8R5E 
_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]   0.015304 
_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]   0.013289 
_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]   0.012067 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . LYS A 1 7   ? 33.911  4.175   33.235  1.00 55.15  ? 5   LYS A N     1 
ATOM   2    C  CA    . LYS A 1 7   ? 34.910  3.165   32.795  1.00 58.50  ? 5   LYS A CA    1 
ATOM   3    C  C     . LYS A 1 7   ? 34.476  2.623   31.442  1.00 61.55  ? 5   LYS A C     1 
ATOM   4    O  O     . LYS A 1 7   ? 33.296  2.417   31.230  1.00 64.28  ? 5   LYS A O     1 
ATOM   5    C  CB    . LYS A 1 7   ? 35.027  1.998   33.786  1.00 56.90  ? 5   LYS A CB    1 
ATOM   6    N  N     . ARG A 1 8   ? 35.433  2.377   30.541  1.00 61.02  ? 6   ARG A N     1 
ATOM   7    C  CA    . ARG A 1 8   ? 35.133  1.694   29.293  1.00 65.10  ? 6   ARG A CA    1 
ATOM   8    C  C     . ARG A 1 8   ? 34.381  0.396   29.583  1.00 68.69  ? 6   ARG A C     1 
ATOM   9    O  O     . ARG A 1 8   ? 34.827  -0.405  30.406  1.00 73.70  ? 6   ARG A O     1 
ATOM   10   C  CB    . ARG A 1 8   ? 36.424  1.366   28.531  1.00 69.27  ? 6   ARG A CB    1 
ATOM   11   C  CG    . ARG A 1 8   ? 37.174  2.584   28.008  1.00 70.57  ? 6   ARG A CG    1 
ATOM   12   N  N     . ASP A 1 9   ? 33.249  0.200   28.890  1.00 65.62  ? 7   ASP A N     1 
ATOM   13   C  CA    . ASP A 1 9   ? 32.509  -1.049  28.930  1.00 61.75  ? 7   ASP A CA    1 
ATOM   14   C  C     . ASP A 1 9   ? 32.739  -1.777  27.606  1.00 64.57  ? 7   ASP A C     1 
ATOM   15   O  O     . ASP A 1 9   ? 32.144  -1.413  26.586  1.00 61.78  ? 7   ASP A O     1 
ATOM   16   C  CB    . ASP A 1 9   ? 31.026  -0.783  29.187  1.00 62.33  ? 7   ASP A CB    1 
ATOM   17   C  CG    . ASP A 1 9   ? 30.143  -2.016  29.301  1.00 61.76  ? 7   ASP A CG    1 
ATOM   18   O  OD1   . ASP A 1 9   ? 30.606  -3.127  28.941  1.00 63.98  ? 7   ASP A OD1   1 
ATOM   19   O  OD2   . ASP A 1 9   ? 28.989  -1.854  29.757  1.00 56.70  ? 7   ASP A OD2   1 
ATOM   20   N  N     . ASN A 1 10  ? 33.559  -2.836  27.658  1.00 61.45  ? 8   ASN A N     1 
ATOM   21   C  CA    . ASN A 1 10  ? 33.969  -3.599  26.485  1.00 61.73  ? 8   ASN A CA    1 
ATOM   22   C  C     . ASN A 1 10  ? 32.782  -4.193  25.721  1.00 61.66  ? 8   ASN A C     1 
ATOM   23   O  O     . ASN A 1 10  ? 33.010  -4.833  24.694  1.00 57.88  ? 8   ASN A O     1 
ATOM   24   C  CB    . ASN A 1 10  ? 34.921  -4.742  26.864  1.00 58.86  ? 8   ASN A CB    1 
ATOM   25   N  N     . ASN A 1 11  ? 31.543  -4.004  26.212  1.00 59.08  ? 9   ASN A N     1 
ATOM   26   C  CA    . ASN A 1 11  ? 30.376  -4.659  25.634  1.00 59.50  ? 9   ASN A CA    1 
ATOM   27   C  C     . ASN A 1 11  ? 29.814  -3.915  24.412  1.00 52.55  ? 9   ASN A C     1 
ATOM   28   O  O     . ASN A 1 11  ? 28.915  -4.436  23.753  1.00 49.73  ? 9   ASN A O     1 
ATOM   29   C  CB    . ASN A 1 11  ? 29.283  -4.888  26.687  1.00 64.45  ? 9   ASN A CB    1 
ATOM   30   C  CG    . ASN A 1 11  ? 29.619  -5.987  27.673  1.00 70.56  ? 9   ASN A CG    1 
ATOM   31   O  OD1   . ASN A 1 11  ? 29.563  -5.765  28.880  1.00 76.27  ? 9   ASN A OD1   1 
ATOM   32   N  ND2   . ASN A 1 11  ? 29.938  -7.175  27.180  1.00 71.83  ? 9   ASN A ND2   1 
ATOM   33   N  N     . PHE A 1 12  ? 30.350  -2.736  24.078  1.00 48.65  ? 10  PHE A N     1 
ATOM   34   C  CA    . PHE A 1 12  ? 29.834  -1.927  22.985  1.00 50.13  ? 10  PHE A CA    1 
ATOM   35   C  C     . PHE A 1 12  ? 30.867  -1.772  21.869  1.00 49.94  ? 10  PHE A C     1 
ATOM   36   O  O     . PHE A 1 12  ? 32.067  -1.875  22.094  1.00 52.06  ? 10  PHE A O     1 
ATOM   37   C  CB    . PHE A 1 12  ? 29.424  -0.532  23.482  1.00 51.97  ? 10  PHE A CB    1 
ATOM   38   C  CG    . PHE A 1 12  ? 28.213  -0.493  24.380  1.00 49.58  ? 10  PHE A CG    1 
ATOM   39   C  CD1   . PHE A 1 12  ? 28.324  -0.689  25.752  1.00 50.37  ? 10  PHE A CD1   1 
ATOM   40   C  CD2   . PHE A 1 12  ? 26.958  -0.253  23.848  1.00 42.34  ? 10  PHE A CD2   1 
ATOM   41   C  CE1   . PHE A 1 12  ? 27.201  -0.646  26.568  1.00 47.83  ? 10  PHE A CE1   1 
ATOM   42   C  CE2   . PHE A 1 12  ? 25.843  -0.232  24.663  1.00 42.66  ? 10  PHE A CE2   1 
ATOM   43   C  CZ    . PHE A 1 12  ? 25.962  -0.419  26.019  1.00 44.09  ? 10  PHE A CZ    1 
ATOM   44   N  N     . TYR A 1 13  ? 30.381  -1.485  20.655  1.00 50.15  ? 11  TYR A N     1 
ATOM   45   C  CA    . TYR A 1 13  ? 31.231  -1.111  19.535  1.00 50.40  ? 11  TYR A CA    1 
ATOM   46   C  C     . TYR A 1 13  ? 30.503  -0.038  18.720  1.00 52.35  ? 11  TYR A C     1 
ATOM   47   O  O     . TYR A 1 13  ? 29.309  0.201   18.920  1.00 54.98  ? 11  TYR A O     1 
ATOM   48   C  CB    . TYR A 1 13  ? 31.619  -2.349  18.705  1.00 52.83  ? 11  TYR A CB    1 
ATOM   49   C  CG    . TYR A 1 13  ? 30.541  -2.868  17.751  1.00 51.36  ? 11  TYR A CG    1 
ATOM   50   C  CD1   . TYR A 1 13  ? 29.428  -3.554  18.218  1.00 50.50  ? 11  TYR A CD1   1 
ATOM   51   C  CD2   . TYR A 1 13  ? 30.619  -2.637  16.381  1.00 52.58  ? 11  TYR A CD2   1 
ATOM   52   C  CE1   . TYR A 1 13  ? 28.434  -3.995  17.355  1.00 50.18  ? 11  TYR A CE1   1 
ATOM   53   C  CE2   . TYR A 1 13  ? 29.638  -3.083  15.507  1.00 50.04  ? 11  TYR A CE2   1 
ATOM   54   C  CZ    . TYR A 1 13  ? 28.540  -3.765  15.995  1.00 49.01  ? 11  TYR A CZ    1 
ATOM   55   O  OH    . TYR A 1 13  ? 27.549  -4.189  15.147  1.00 51.18  ? 11  TYR A OH    1 
ATOM   56   N  N     . SER A 1 14  ? 31.219  0.593   17.781  1.00 53.22  ? 12  SER A N     1 
ATOM   57   C  CA    . SER A 1 14  ? 30.682  1.697   16.996  1.00 55.88  ? 12  SER A CA    1 
ATOM   58   C  C     . SER A 1 14  ? 30.766  1.394   15.509  1.00 59.15  ? 12  SER A C     1 
ATOM   59   O  O     . SER A 1 14  ? 31.790  0.926   15.036  1.00 62.09  ? 12  SER A O     1 
ATOM   60   C  CB    . SER A 1 14  ? 31.415  2.972   17.286  1.00 58.97  ? 12  SER A CB    1 
ATOM   61   O  OG    . SER A 1 14  ? 31.264  3.339   18.645  1.00 63.00  ? 12  SER A OG    1 
ATOM   62   N  N     . VAL A 1 15  ? 29.698  1.723   14.778  1.00 64.62  ? 13  VAL A N     1 
ATOM   63   C  CA    . VAL A 1 15  ? 29.683  1.614   13.326  1.00 69.76  ? 13  VAL A CA    1 
ATOM   64   C  C     . VAL A 1 15  ? 29.013  2.863   12.758  1.00 74.09  ? 13  VAL A C     1 
ATOM   65   O  O     . VAL A 1 15  ? 28.033  3.354   13.318  1.00 77.35  ? 13  VAL A O     1 
ATOM   66   C  CB    . VAL A 1 15  ? 28.977  0.322   12.861  1.00 68.98  ? 13  VAL A CB    1 
ATOM   67   C  CG1   . VAL A 1 15  ? 27.666  0.092   13.600  1.00 67.74  ? 13  VAL A CG1   1 
ATOM   68   C  CG2   . VAL A 1 15  ? 28.767  0.289   11.351  1.00 66.45  ? 13  VAL A CG2   1 
ATOM   69   N  N     . GLU A 1 16  ? 29.550  3.371   11.645  1.00 76.29  ? 14  GLU A N     1 
ATOM   70   C  CA    . GLU A 1 16  ? 29.023  4.565   11.010  1.00 79.34  ? 14  GLU A CA    1 
ATOM   71   C  C     . GLU A 1 16  ? 27.950  4.169   9.999   1.00 87.58  ? 14  GLU A C     1 
ATOM   72   O  O     . GLU A 1 16  ? 28.211  3.376   9.094   1.00 96.71  ? 14  GLU A O     1 
ATOM   73   C  CB    . GLU A 1 16  ? 30.158  5.334   10.344  1.00 81.04  ? 14  GLU A CB    1 
ATOM   74   C  CG    . GLU A 1 16  ? 31.178  5.846   11.338  1.00 87.33  ? 14  GLU A CG    1 
ATOM   75   C  CD    . GLU A 1 16  ? 30.768  7.102   12.088  1.00 95.76  ? 14  GLU A CD    1 
ATOM   76   O  OE1   . GLU A 1 16  ? 29.756  7.733   11.694  1.00 99.62  ? 14  GLU A OE1   1 
ATOM   77   O  OE2   . GLU A 1 16  ? 31.455  7.436   13.078  1.00 100.82 ? 14  GLU A OE2   1 
ATOM   78   N  N     . ILE A 1 17  ? 26.744  4.719   10.182  1.00 87.25  ? 15  ILE A N     1 
ATOM   79   C  CA    . ILE A 1 17  ? 25.635  4.522   9.263   1.00 87.40  ? 15  ILE A CA    1 
ATOM   80   C  C     . ILE A 1 17  ? 25.304  5.872   8.636   1.00 88.57  ? 15  ILE A C     1 
ATOM   81   O  O     . ILE A 1 17  ? 24.755  6.756   9.293   1.00 89.04  ? 15  ILE A O     1 
ATOM   82   C  CB    . ILE A 1 17  ? 24.419  3.898   9.981   1.00 84.61  ? 15  ILE A CB    1 
ATOM   83   C  CG1   . ILE A 1 17  ? 24.650  2.415   10.285  1.00 82.63  ? 15  ILE A CG1   1 
ATOM   84   C  CG2   . ILE A 1 17  ? 23.143  4.089   9.174   1.00 85.36  ? 15  ILE A CG2   1 
ATOM   85   C  CD1   . ILE A 1 17  ? 25.556  2.155   11.460  1.00 82.87  ? 15  ILE A CD1   1 
ATOM   86   N  N     . GLY A 1 18  ? 25.641  6.025   7.355   1.00 86.80  ? 16  GLY A N     1 
ATOM   87   C  CA    . GLY A 1 18  ? 25.515  7.315   6.705   1.00 86.72  ? 16  GLY A CA    1 
ATOM   88   C  C     . GLY A 1 18  ? 26.320  8.373   7.455   1.00 90.49  ? 16  GLY A C     1 
ATOM   89   O  O     . GLY A 1 18  ? 27.511  8.195   7.697   1.00 92.12  ? 16  GLY A O     1 
ATOM   90   N  N     . ASP A 1 19  ? 25.645  9.455   7.856   1.00 92.23  ? 17  ASP A N     1 
ATOM   91   C  CA    . ASP A 1 19  ? 26.294  10.567  8.529   1.00 92.81  ? 17  ASP A CA    1 
ATOM   92   C  C     . ASP A 1 19  ? 26.524  10.246  10.007  1.00 92.60  ? 17  ASP A C     1 
ATOM   93   O  O     . ASP A 1 19  ? 27.581  10.559  10.547  1.00 99.47  ? 17  ASP A O     1 
ATOM   94   C  CB    . ASP A 1 19  ? 25.467  11.848  8.382   1.00 90.75  ? 17  ASP A CB    1 
ATOM   95   N  N     A SER A 1 20  ? 25.534  9.613   10.645  0.51 90.53  ? 18  SER A N     1 
ATOM   96   N  N     B SER A 1 20  ? 25.532  9.618   10.647  0.49 90.54  ? 18  SER A N     1 
ATOM   97   C  CA    A SER A 1 20  ? 25.544  9.406   12.086  0.51 90.25  ? 18  SER A CA    1 
ATOM   98   C  CA    B SER A 1 20  ? 25.549  9.410   12.087  0.49 90.25  ? 18  SER A CA    1 
ATOM   99   C  C     A SER A 1 20  ? 26.218  8.083   12.445  0.51 86.46  ? 18  SER A C     1 
ATOM   100  C  C     B SER A 1 20  ? 26.234  8.092   12.440  0.49 86.57  ? 18  SER A C     1 
ATOM   101  O  O     A SER A 1 20  ? 26.292  7.170   11.624  0.51 87.54  ? 18  SER A O     1 
ATOM   102  O  O     B SER A 1 20  ? 26.338  7.194   11.606  0.49 87.90  ? 18  SER A O     1 
ATOM   103  C  CB    A SER A 1 20  ? 24.144  9.461   12.635  0.51 91.88  ? 18  SER A CB    1 
ATOM   104  C  CB    B SER A 1 20  ? 24.152  9.450   12.642  0.49 91.84  ? 18  SER A CB    1 
ATOM   105  O  OG    A SER A 1 20  ? 24.150  9.332   14.048  0.51 96.55  ? 18  SER A OG    1 
ATOM   106  O  OG    B SER A 1 20  ? 24.168  9.302   14.053  0.49 96.42  ? 18  SER A OG    1 
ATOM   107  N  N     . THR A 1 21  ? 26.685  7.996   13.697  1.00 79.83  ? 19  THR A N     1 
ATOM   108  C  CA    . THR A 1 21  ? 27.349  6.810   14.220  1.00 74.19  ? 19  THR A CA    1 
ATOM   109  C  C     . THR A 1 21  ? 26.401  6.049   15.143  1.00 68.12  ? 19  THR A C     1 
ATOM   110  O  O     . THR A 1 21  ? 25.767  6.660   15.995  1.00 68.59  ? 19  THR A O     1 
ATOM   111  C  CB    . THR A 1 21  ? 28.595  7.177   15.040  1.00 74.11  ? 19  THR A CB    1 
ATOM   112  O  OG1   . THR A 1 21  ? 29.291  8.268   14.436  1.00 76.15  ? 19  THR A OG1   1 
ATOM   113  C  CG2   . THR A 1 21  ? 29.543  6.011   15.191  1.00 73.79  ? 19  THR A CG2   1 
ATOM   114  N  N     . PHE A 1 22  ? 26.333  4.720   14.989  1.00 64.64  ? 20  PHE A N     1 
ATOM   115  C  CA    . PHE A 1 22  ? 25.638  3.866   15.940  1.00 61.45  ? 20  PHE A CA    1 
ATOM   116  C  C     . PHE A 1 22  ? 26.642  3.173   16.848  1.00 56.06  ? 20  PHE A C     1 
ATOM   117  O  O     . PHE A 1 22  ? 27.556  2.519   16.362  1.00 57.94  ? 20  PHE A O     1 
ATOM   118  C  CB    . PHE A 1 22  ? 24.812  2.773   15.256  1.00 62.32  ? 20  PHE A CB    1 
ATOM   119  C  CG    . PHE A 1 22  ? 23.414  3.185   14.889  1.00 61.79  ? 20  PHE A CG    1 
ATOM   120  C  CD1   . PHE A 1 22  ? 23.125  4.508   14.596  1.00 60.44  ? 20  PHE A CD1   1 
ATOM   121  C  CD2   . PHE A 1 22  ? 22.378  2.262   14.897  1.00 61.62  ? 20  PHE A CD2   1 
ATOM   122  C  CE1   . PHE A 1 22  ? 21.834  4.887   14.269  1.00 65.82  ? 20  PHE A CE1   1 
ATOM   123  C  CE2   . PHE A 1 22  ? 21.086  2.647   14.575  1.00 61.81  ? 20  PHE A CE2   1 
ATOM   124  C  CZ    . PHE A 1 22  ? 20.818  3.956   14.260  1.00 60.40  ? 20  PHE A CZ    1 
ATOM   125  N  N     . THR A 1 23  ? 26.410  3.293   18.157  1.00 53.03  ? 21  THR A N     1 
ATOM   126  C  CA    . THR A 1 23  ? 27.175  2.594   19.176  1.00 51.06  ? 21  THR A CA    1 
ATOM   127  C  C     . THR A 1 23  ? 26.240  1.634   19.904  1.00 49.66  ? 21  THR A C     1 
ATOM   128  O  O     . THR A 1 23  ? 25.348  2.067   20.636  1.00 51.71  ? 21  THR A O     1 
ATOM   129  C  CB    . THR A 1 23  ? 27.810  3.593   20.146  1.00 51.01  ? 21  THR A CB    1 
ATOM   130  O  OG1   . THR A 1 23  ? 28.577  4.451   19.309  1.00 51.08  ? 21  THR A OG1   1 
ATOM   131  C  CG2   . THR A 1 23  ? 28.678  2.944   21.204  1.00 54.45  ? 21  THR A CG2   1 
ATOM   132  N  N     . VAL A 1 24  ? 26.444  0.332   19.686  1.00 47.12  ? 22  VAL A N     1 
ATOM   133  C  CA    . VAL A 1 24  ? 25.469  -0.672  20.081  1.00 43.67  ? 22  VAL A CA    1 
ATOM   134  C  C     . VAL A 1 24  ? 26.175  -1.798  20.823  1.00 41.48  ? 22  VAL A C     1 
ATOM   135  O  O     . VAL A 1 24  ? 27.379  -1.990  20.673  1.00 41.42  ? 22  VAL A O     1 
ATOM   136  C  CB    . VAL A 1 24  ? 24.733  -1.218  18.845  1.00 42.64  ? 22  VAL A CB    1 
ATOM   137  C  CG1   . VAL A 1 24  ? 24.010  -0.117  18.095  1.00 44.58  ? 22  VAL A CG1   1 
ATOM   138  C  CG2   . VAL A 1 24  ? 25.686  -1.948  17.911  1.00 42.87  ? 22  VAL A CG2   1 
ATOM   139  N  N     . LEU A 1 25  ? 25.388  -2.583  21.565  1.00 40.01  ? 23  LEU A N     1 
ATOM   140  C  CA    . LEU A 1 25  ? 25.877  -3.798  22.201  1.00 37.57  ? 23  LEU A CA    1 
ATOM   141  C  C     . LEU A 1 25  ? 26.396  -4.770  21.135  1.00 39.02  ? 23  LEU A C     1 
ATOM   142  O  O     . LEU A 1 25  ? 25.899  -4.830  20.005  1.00 37.55  ? 23  LEU A O     1 
ATOM   143  C  CB    . LEU A 1 25  ? 24.750  -4.401  23.046  1.00 36.71  ? 23  LEU A CB    1 
ATOM   144  C  CG    . LEU A 1 25  ? 24.425  -3.650  24.340  1.00 37.46  ? 23  LEU A CG    1 
ATOM   145  C  CD1   . LEU A 1 25  ? 23.164  -4.177  24.998  1.00 36.90  ? 23  LEU A CD1   1 
ATOM   146  C  CD2   . LEU A 1 25  ? 25.583  -3.745  25.316  1.00 39.40  ? 23  LEU A CD2   1 
ATOM   147  N  N     . LYS A 1 26  ? 27.446  -5.509  21.494  1.00 39.19  ? 24  LYS A N     1 
ATOM   148  C  CA    . LYS A 1 26  ? 28.143  -6.366  20.544  1.00 40.13  ? 24  LYS A CA    1 
ATOM   149  C  C     . LYS A 1 26  ? 27.276  -7.517  20.040  1.00 39.76  ? 24  LYS A C     1 
ATOM   150  O  O     . LYS A 1 26  ? 27.588  -8.094  19.004  1.00 40.56  ? 24  LYS A O     1 
ATOM   151  C  CB    . LYS A 1 26  ? 29.423  -6.919  21.163  1.00 39.40  ? 24  LYS A CB    1 
ATOM   152  C  CG    . LYS A 1 26  ? 30.613  -5.977  21.092  1.00 41.04  ? 24  LYS A CG    1 
ATOM   153  C  CD    . LYS A 1 26  ? 31.765  -6.422  21.950  1.00 44.13  ? 24  LYS A CD    1 
ATOM   154  C  CE    . LYS A 1 26  ? 32.974  -5.538  21.747  1.00 46.84  ? 24  LYS A CE    1 
ATOM   155  N  NZ    . LYS A 1 26  ? 34.163  -6.138  22.374  1.00 49.40  ? 24  LYS A NZ    1 
ATOM   156  N  N     . ARG A 1 27  ? 26.220  -7.871  20.776  1.00 37.90  ? 25  ARG A N     1 
ATOM   157  C  CA    . ARG A 1 27  ? 25.254  -8.842  20.290  1.00 38.69  ? 25  ARG A CA    1 
ATOM   158  C  C     . ARG A 1 27  ? 24.638  -8.404  18.953  1.00 37.62  ? 25  ARG A C     1 
ATOM   159  O  O     . ARG A 1 27  ? 24.260  -9.246  18.164  1.00 37.13  ? 25  ARG A O     1 
ATOM   160  C  CB    . ARG A 1 27  ? 24.148  -9.035  21.332  1.00 39.64  ? 25  ARG A CB    1 
ATOM   161  C  CG    . ARG A 1 27  ? 23.282  -7.804  21.568  1.00 35.85  ? 25  ARG A CG    1 
ATOM   162  C  CD    . ARG A 1 27  ? 22.445  -7.949  22.817  1.00 34.07  ? 25  ARG A CD    1 
ATOM   163  N  NE    . ARG A 1 27  ? 21.360  -8.895  22.658  1.00 30.95  ? 25  ARG A NE    1 
ATOM   164  C  CZ    . ARG A 1 27  ? 20.434  -9.166  23.571  1.00 33.35  ? 25  ARG A CZ    1 
ATOM   165  N  NH1   . ARG A 1 27  ? 20.522  -8.667  24.790  1.00 32.04  ? 25  ARG A NH1   1 
ATOM   166  N  NH2   . ARG A 1 27  ? 19.426  -9.972  23.267  1.00 31.88  ? 25  ARG A NH2   1 
ATOM   167  N  N     . TYR A 1 28  ? 24.512  -7.099  18.697  1.00 35.74  ? 26  TYR A N     1 
ATOM   168  C  CA    . TYR A 1 28  ? 23.861  -6.625  17.480  1.00 36.00  ? 26  TYR A CA    1 
ATOM   169  C  C     . TYR A 1 28  ? 24.901  -6.479  16.370  1.00 42.28  ? 26  TYR A C     1 
ATOM   170  O  O     . TYR A 1 28  ? 25.818  -5.661  16.475  1.00 45.64  ? 26  TYR A O     1 
ATOM   171  C  CB    . TYR A 1 28  ? 23.115  -5.316  17.755  1.00 33.48  ? 26  TYR A CB    1 
ATOM   172  C  CG    . TYR A 1 28  ? 22.097  -5.429  18.885  1.00 32.65  ? 26  TYR A CG    1 
ATOM   173  C  CD1   . TYR A 1 28  ? 21.029  -6.315  18.794  1.00 31.92  ? 26  TYR A CD1   1 
ATOM   174  C  CD2   . TYR A 1 28  ? 22.206  -4.677  20.043  1.00 31.56  ? 26  TYR A CD2   1 
ATOM   175  C  CE1   . TYR A 1 28  ? 20.110  -6.454  19.809  1.00 29.29  ? 26  TYR A CE1   1 
ATOM   176  C  CE2   . TYR A 1 28  ? 21.282  -4.796  21.066  1.00 30.91  ? 26  TYR A CE2   1 
ATOM   177  C  CZ    . TYR A 1 28  ? 20.246  -5.702  20.957  1.00 30.65  ? 26  TYR A CZ    1 
ATOM   178  O  OH    . TYR A 1 28  ? 19.332  -5.870  21.942  1.00 31.21  ? 26  TYR A OH    1 
ATOM   179  N  N     . GLN A 1 29  ? 24.743  -7.279  15.309  1.00 41.95  ? 27  GLN A N     1 
ATOM   180  C  CA    . GLN A 1 29  ? 25.750  -7.445  14.269  1.00 42.94  ? 27  GLN A CA    1 
ATOM   181  C  C     . GLN A 1 29  ? 25.159  -7.026  12.924  1.00 43.49  ? 27  GLN A C     1 
ATOM   182  O  O     . GLN A 1 29  ? 23.936  -7.069  12.732  1.00 41.10  ? 27  GLN A O     1 
ATOM   183  C  CB    . GLN A 1 29  ? 26.182  -8.914  14.156  1.00 47.42  ? 27  GLN A CB    1 
ATOM   184  C  CG    . GLN A 1 29  ? 26.716  -9.528  15.449  1.00 53.85  ? 27  GLN A CG    1 
ATOM   185  C  CD    . GLN A 1 29  ? 27.069  -11.003 15.377  1.00 56.20  ? 27  GLN A CD    1 
ATOM   186  O  OE1   . GLN A 1 29  ? 26.662  -11.747 14.483  1.00 56.81  ? 27  GLN A OE1   1 
ATOM   187  N  NE2   . GLN A 1 29  ? 27.819  -11.459 16.365  1.00 58.05  ? 27  GLN A NE2   1 
ATOM   188  N  N     . ASN A 1 30  ? 26.036  -6.598  12.006  1.00 43.51  ? 28  ASN A N     1 
ATOM   189  C  CA    . ASN A 1 30  ? 25.685  -6.432  10.602  1.00 48.94  ? 28  ASN A CA    1 
ATOM   190  C  C     . ASN A 1 30  ? 24.597  -5.377  10.421  1.00 46.37  ? 28  ASN A C     1 
ATOM   191  O  O     . ASN A 1 30  ? 23.617  -5.613  9.722   1.00 45.97  ? 28  ASN A O     1 
ATOM   192  C  CB    . ASN A 1 30  ? 25.191  -7.740  9.971   1.00 55.12  ? 28  ASN A CB    1 
ATOM   193  C  CG    . ASN A 1 30  ? 26.213  -8.850  10.021  1.00 62.76  ? 28  ASN A CG    1 
ATOM   194  O  OD1   . ASN A 1 30  ? 27.418  -8.606  9.990   1.00 68.39  ? 28  ASN A OD1   1 
ATOM   195  N  ND2   . ASN A 1 30  ? 25.735  -10.082 10.059  1.00 70.59  ? 28  ASN A ND2   1 
ATOM   196  N  N     . LEU A 1 31  ? 24.787  -4.203  11.024  1.00 46.24  ? 29  LEU A N     1 
ATOM   197  C  CA    . LEU A 1 31  ? 23.762  -3.176  10.984  1.00 48.32  ? 29  LEU A CA    1 
ATOM   198  C  C     . LEU A 1 31  ? 23.618  -2.646  9.561   1.00 46.86  ? 29  LEU A C     1 
ATOM   199  O  O     . LEU A 1 31  ? 24.609  -2.397  8.898   1.00 47.77  ? 29  LEU A O     1 
ATOM   200  C  CB    . LEU A 1 31  ? 24.105  -2.061  11.981  1.00 50.04  ? 29  LEU A CB    1 
ATOM   201  C  CG    . LEU A 1 31  ? 23.514  -2.262  13.378  1.00 48.77  ? 29  LEU A CG    1 
ATOM   202  C  CD1   . LEU A 1 31  ? 24.217  -3.393  14.096  1.00 49.72  ? 29  LEU A CD1   1 
ATOM   203  C  CD2   . LEU A 1 31  ? 23.599  -0.997  14.207  1.00 51.12  ? 29  LEU A CD2   1 
ATOM   204  N  N     . LYS A 1 32  ? 22.370  -2.485  9.103   1.00 49.49  ? 30  LYS A N     1 
ATOM   205  C  CA    . LYS A 1 32  ? 22.086  -1.932  7.785   1.00 52.66  ? 30  LYS A CA    1 
ATOM   206  C  C     . LYS A 1 32  ? 20.986  -0.893  7.950   1.00 51.33  ? 30  LYS A C     1 
ATOM   207  O  O     . LYS A 1 32  ? 19.981  -1.165  8.595   1.00 50.89  ? 30  LYS A O     1 
ATOM   208  C  CB    . LYS A 1 32  ? 21.632  -3.019  6.802   1.00 53.70  ? 30  LYS A CB    1 
ATOM   209  C  CG    . LYS A 1 32  ? 22.602  -3.318  5.672   1.00 57.05  ? 30  LYS A CG    1 
ATOM   210  N  N     . PRO A 1 33  ? 21.118  0.318   7.375   1.00 55.23  ? 31  PRO A N     1 
ATOM   211  C  CA    . PRO A 1 33  ? 20.076  1.340   7.525   1.00 57.09  ? 31  PRO A CA    1 
ATOM   212  C  C     . PRO A 1 33  ? 18.815  0.954   6.755   1.00 56.35  ? 31  PRO A C     1 
ATOM   213  O  O     . PRO A 1 33  ? 18.908  0.555   5.599   1.00 56.17  ? 31  PRO A O     1 
ATOM   214  C  CB    . PRO A 1 33  ? 20.744  2.594   6.940   1.00 59.95  ? 31  PRO A CB    1 
ATOM   215  C  CG    . PRO A 1 33  ? 21.752  2.054   5.940   1.00 58.77  ? 31  PRO A CG    1 
ATOM   216  C  CD    . PRO A 1 33  ? 22.245  0.758   6.543   1.00 55.64  ? 31  PRO A CD    1 
ATOM   217  N  N     . ILE A 1 34  ? 17.645  1.024   7.407   1.00 56.87  ? 32  ILE A N     1 
ATOM   218  C  CA    . ILE A 1 34  ? 16.393  0.659   6.749   1.00 58.28  ? 32  ILE A CA    1 
ATOM   219  C  C     . ILE A 1 34  ? 15.409  1.821   6.772   1.00 62.09  ? 32  ILE A C     1 
ATOM   220  O  O     . ILE A 1 34  ? 14.371  1.754   6.116   1.00 58.68  ? 32  ILE A O     1 
ATOM   221  C  CB    . ILE A 1 34  ? 15.748  -0.599  7.365   1.00 56.61  ? 32  ILE A CB    1 
ATOM   222  C  CG1   . ILE A 1 34  ? 15.234  -0.343  8.788   1.00 54.12  ? 32  ILE A CG1   1 
ATOM   223  C  CG2   . ILE A 1 34  ? 16.715  -1.770  7.286   1.00 59.22  ? 32  ILE A CG2   1 
ATOM   224  C  CD1   . ILE A 1 34  ? 14.516  -1.517  9.427   1.00 53.04  ? 32  ILE A CD1   1 
ATOM   225  N  N     . GLY A 1 35  ? 15.722  2.869   7.535   1.00 66.55  ? 33  GLY A N     1 
ATOM   226  C  CA    . GLY A 1 35  ? 14.782  3.960   7.699   1.00 67.96  ? 33  GLY A CA    1 
ATOM   227  C  C     . GLY A 1 35  ? 15.419  5.179   8.348   1.00 68.38  ? 33  GLY A C     1 
ATOM   228  O  O     . GLY A 1 35  ? 16.422  5.085   9.057   1.00 67.64  ? 33  GLY A O     1 
ATOM   229  N  N     . SER A 1 36  ? 14.803  6.324   8.073   1.00 73.03  ? 34  SER A N     1 
ATOM   230  C  CA    . SER A 1 36  ? 15.216  7.588   8.641   1.00 78.08  ? 34  SER A CA    1 
ATOM   231  C  C     . SER A 1 36  ? 13.970  8.438   8.836   1.00 82.49  ? 34  SER A C     1 
ATOM   232  O  O     . SER A 1 36  ? 12.936  8.174   8.226   1.00 88.65  ? 34  SER A O     1 
ATOM   233  C  CB    . SER A 1 36  ? 16.202  8.273   7.746   1.00 81.54  ? 34  SER A CB    1 
ATOM   234  O  OG    . SER A 1 36  ? 15.604  8.541   6.487   1.00 83.56  ? 34  SER A OG    1 
ATOM   235  N  N     . GLY A 1 37  ? 14.080  9.443   9.701   1.00 80.58  ? 35  GLY A N     1 
ATOM   236  C  CA    . GLY A 1 37  ? 13.038  10.442  9.823   1.00 81.93  ? 35  GLY A CA    1 
ATOM   237  C  C     . GLY A 1 37  ? 13.275  11.328  11.036  1.00 80.21  ? 35  GLY A C     1 
ATOM   238  O  O     . GLY A 1 37  ? 14.343  11.283  11.647  1.00 78.21  ? 35  GLY A O     1 
ATOM   239  N  N     . ALA A 1 38  ? 12.235  12.086  11.394  1.00 82.65  ? 36  ALA A N     1 
ATOM   240  C  CA    . ALA A 1 38  ? 12.322  13.100  12.433  1.00 86.39  ? 36  ALA A CA    1 
ATOM   241  C  C     . ALA A 1 38  ? 12.729  12.504  13.780  1.00 89.52  ? 36  ALA A C     1 
ATOM   242  O  O     . ALA A 1 38  ? 13.323  13.213  14.590  1.00 92.40  ? 36  ALA A O     1 
ATOM   243  C  CB    . ALA A 1 38  ? 11.006  13.839  12.543  1.00 86.63  ? 36  ALA A CB    1 
ATOM   244  N  N     . GLN A 1 39  ? 12.389  11.231  14.026  1.00 91.47  ? 37  GLN A N     1 
ATOM   245  C  CA    . GLN A 1 39  ? 12.661  10.589  15.308  1.00 92.18  ? 37  GLN A CA    1 
ATOM   246  C  C     . GLN A 1 39  ? 14.132  10.169  15.390  1.00 90.17  ? 37  GLN A C     1 
ATOM   247  O  O     . GLN A 1 39  ? 14.823  10.479  16.363  1.00 89.33  ? 37  GLN A O     1 
ATOM   248  C  CB    . GLN A 1 39  ? 11.704  9.409   15.509  1.00 90.89  ? 37  GLN A CB    1 
ATOM   249  N  N     . GLY A 1 40  ? 14.609  9.450   14.370  1.00 79.46  ? 38  GLY A N     1 
ATOM   250  C  CA    . GLY A 1 40  ? 16.005  9.062   14.316  1.00 69.57  ? 38  GLY A CA    1 
ATOM   251  C  C     . GLY A 1 40  ? 16.258  8.072   13.191  1.00 66.65  ? 38  GLY A C     1 
ATOM   252  O  O     . GLY A 1 40  ? 15.427  7.897   12.304  1.00 69.68  ? 38  GLY A O     1 
ATOM   253  N  N     . ILE A 1 41  ? 17.410  7.409   13.263  1.00 62.73  ? 39  ILE A N     1 
ATOM   254  C  CA    . ILE A 1 41  ? 17.827  6.486   12.227  1.00 57.37  ? 39  ILE A CA    1 
ATOM   255  C  C     . ILE A 1 41  ? 17.443  5.089   12.694  1.00 48.71  ? 39  ILE A C     1 
ATOM   256  O  O     . ILE A 1 41  ? 17.585  4.806   13.875  1.00 44.13  ? 39  ILE A O     1 
ATOM   257  C  CB    . ILE A 1 41  ? 19.338  6.615   11.952  1.00 62.15  ? 39  ILE A CB    1 
ATOM   258  C  CG1   . ILE A 1 41  ? 19.797  8.079   11.925  1.00 71.41  ? 39  ILE A CG1   1 
ATOM   259  C  CG2   . ILE A 1 41  ? 19.697  5.885   10.665  1.00 61.93  ? 39  ILE A CG2   1 
ATOM   260  C  CD1   . ILE A 1 41  ? 20.191  8.660   13.282  1.00 74.28  ? 39  ILE A CD1   1 
ATOM   261  N  N     . VAL A 1 42  ? 16.929  4.259   11.776  1.00 46.42  ? 40  VAL A N     1 
ATOM   262  C  CA    . VAL A 1 42  ? 16.596  2.873   12.074  1.00 44.65  ? 40  VAL A CA    1 
ATOM   263  C  C     . VAL A 1 42  ? 17.506  1.955   11.259  1.00 47.50  ? 40  VAL A C     1 
ATOM   264  O  O     . VAL A 1 42  ? 17.630  2.120   10.042  1.00 47.13  ? 40  VAL A O     1 
ATOM   265  C  CB    . VAL A 1 42  ? 15.114  2.561   11.787  1.00 43.88  ? 40  VAL A CB    1 
ATOM   266  C  CG1   . VAL A 1 42  ? 14.763  1.120   12.143  1.00 38.82  ? 40  VAL A CG1   1 
ATOM   267  C  CG2   . VAL A 1 42  ? 14.185  3.546   12.484  1.00 45.39  ? 40  VAL A CG2   1 
ATOM   268  N  N     . CYS A 1 43  ? 18.110  0.972   11.950  1.00 42.77  ? 41  CYS A N     1 
ATOM   269  C  CA    . CYS A 1 43  ? 18.945  -0.033  11.314  1.00 44.85  ? 41  CYS A CA    1 
ATOM   270  C  C     . CYS A 1 43  ? 18.344  -1.415  11.521  1.00 42.70  ? 41  CYS A C     1 
ATOM   271  O  O     . CYS A 1 43  ? 17.822  -1.705  12.592  1.00 41.58  ? 41  CYS A O     1 
ATOM   272  C  CB    . CYS A 1 43  ? 20.360  -0.042  11.882  1.00 46.86  ? 41  CYS A CB    1 
ATOM   273  S  SG    . CYS A 1 43  ? 21.377  1.310   11.244  1.00 51.63  ? 41  CYS A SG    1 
ATOM   274  N  N     . ALA A 1 44  ? 18.444  -2.267  10.500  1.00 41.35  ? 42  ALA A N     1 
ATOM   275  C  CA    . ALA A 1 44  ? 18.236  -3.690  10.698  1.00 40.23  ? 42  ALA A CA    1 
ATOM   276  C  C     . ALA A 1 44  ? 19.549  -4.291  11.201  1.00 43.66  ? 42  ALA A C     1 
ATOM   277  O  O     . ALA A 1 44  ? 20.629  -3.788  10.869  1.00 42.79  ? 42  ALA A O     1 
ATOM   278  C  CB    . ALA A 1 44  ? 17.754  -4.345  9.431   1.00 40.70  ? 42  ALA A CB    1 
ATOM   279  N  N     . ALA A 1 45  ? 19.438  -5.329  12.044  1.00 37.26  ? 43  ALA A N     1 
ATOM   280  C  CA    . ALA A 1 45  ? 20.603  -5.969  12.626  1.00 37.93  ? 43  ALA A CA    1 
ATOM   281  C  C     . ALA A 1 45  ? 20.270  -7.418  12.968  1.00 36.70  ? 43  ALA A C     1 
ATOM   282  O  O     . ALA A 1 45  ? 19.107  -7.777  13.139  1.00 36.58  ? 43  ALA A O     1 
ATOM   283  C  CB    . ALA A 1 45  ? 21.061  -5.212  13.854  1.00 40.28  ? 43  ALA A CB    1 
ATOM   284  N  N     . TYR A 1 46  ? 21.313  -8.231  13.084  1.00 36.18  ? 44  TYR A N     1 
ATOM   285  C  CA    . TYR A 1 46  ? 21.192  -9.574  13.611  1.00 35.56  ? 44  TYR A CA    1 
ATOM   286  C  C     . TYR A 1 46  ? 21.574  -9.568  15.092  1.00 36.82  ? 44  TYR A C     1 
ATOM   287  O  O     . TYR A 1 46  ? 22.660  -9.124  15.451  1.00 39.33  ? 44  TYR A O     1 
ATOM   288  C  CB    . TYR A 1 46  ? 22.064  -10.523 12.794  1.00 36.54  ? 44  TYR A CB    1 
ATOM   289  C  CG    . TYR A 1 46  ? 22.017  -11.925 13.365  1.00 39.59  ? 44  TYR A CG    1 
ATOM   290  C  CD1   . TYR A 1 46  ? 20.858  -12.683 13.263  1.00 41.42  ? 44  TYR A CD1   1 
ATOM   291  C  CD2   . TYR A 1 46  ? 23.081  -12.444 14.094  1.00 42.16  ? 44  TYR A CD2   1 
ATOM   292  C  CE1   . TYR A 1 46  ? 20.787  -13.958 13.797  1.00 43.97  ? 44  TYR A CE1   1 
ATOM   293  C  CE2   . TYR A 1 46  ? 23.021  -13.723 14.639  1.00 43.88  ? 44  TYR A CE2   1 
ATOM   294  C  CZ    . TYR A 1 46  ? 21.861  -14.470 14.503  1.00 43.06  ? 44  TYR A CZ    1 
ATOM   295  O  OH    . TYR A 1 46  ? 21.730  -15.721 15.038  1.00 42.86  ? 44  TYR A OH    1 
ATOM   296  N  N     . ASP A 1 47  ? 20.651  -10.032 15.943  1.00 35.70  ? 45  ASP A N     1 
ATOM   297  C  CA    . ASP A 1 47  ? 20.882  -10.190 17.372  1.00 34.09  ? 45  ASP A CA    1 
ATOM   298  C  C     . ASP A 1 47  ? 21.412  -11.602 17.632  1.00 36.34  ? 45  ASP A C     1 
ATOM   299  O  O     . ASP A 1 47  ? 20.668  -12.578 17.542  1.00 35.77  ? 45  ASP A O     1 
ATOM   300  C  CB    . ASP A 1 47  ? 19.595  -9.897  18.161  1.00 32.22  ? 45  ASP A CB    1 
ATOM   301  C  CG    . ASP A 1 47  ? 19.739  -10.012 19.674  1.00 31.69  ? 45  ASP A CG    1 
ATOM   302  O  OD1   . ASP A 1 47  ? 20.786  -10.472 20.113  1.00 31.78  ? 45  ASP A OD1   1 
ATOM   303  O  OD2   . ASP A 1 47  ? 18.791  -9.626  20.409  1.00 31.69  ? 45  ASP A OD2   1 
ATOM   304  N  N     . ALA A 1 48  ? 22.702  -11.697 17.984  1.00 37.27  ? 46  ALA A N     1 
ATOM   305  C  CA    . ALA A 1 48  ? 23.386  -12.975 18.137  1.00 40.42  ? 46  ALA A CA    1 
ATOM   306  C  C     . ALA A 1 48  ? 22.891  -13.722 19.373  1.00 39.15  ? 46  ALA A C     1 
ATOM   307  O  O     . ALA A 1 48  ? 23.007  -14.936 19.416  1.00 38.34  ? 46  ALA A O     1 
ATOM   308  C  CB    . ALA A 1 48  ? 24.890  -12.768 18.184  1.00 42.67  ? 46  ALA A CB    1 
ATOM   309  N  N     . ILE A 1 49  ? 22.347  -13.005 20.370  1.00 37.58  ? 47  ILE A N     1 
ATOM   310  C  CA    . ILE A 1 49  ? 21.857  -13.625 21.592  1.00 36.82  ? 47  ILE A CA    1 
ATOM   311  C  C     . ILE A 1 49  ? 20.452  -14.214 21.394  1.00 38.90  ? 47  ILE A C     1 
ATOM   312  O  O     . ILE A 1 49  ? 20.220  -15.375 21.748  1.00 39.14  ? 47  ILE A O     1 
ATOM   313  C  CB    . ILE A 1 49  ? 21.953  -12.616 22.752  1.00 38.03  ? 47  ILE A CB    1 
ATOM   314  C  CG1   . ILE A 1 49  ? 23.415  -12.384 23.134  1.00 39.02  ? 47  ILE A CG1   1 
ATOM   315  C  CG2   . ILE A 1 49  ? 21.156  -13.059 23.965  1.00 38.68  ? 47  ILE A CG2   1 
ATOM   316  C  CD1   . ILE A 1 49  ? 23.598  -11.294 24.200  1.00 39.36  ? 47  ILE A CD1   1 
ATOM   317  N  N     . LEU A 1 50  ? 19.535  -13.453 20.791  1.00 35.59  ? 48  LEU A N     1 
ATOM   318  C  CA    . LEU A 1 50  ? 18.183  -13.905 20.480  1.00 37.12  ? 48  LEU A CA    1 
ATOM   319  C  C     . LEU A 1 50  ? 18.151  -14.818 19.250  1.00 42.48  ? 48  LEU A C     1 
ATOM   320  O  O     . LEU A 1 50  ? 17.171  -15.540 19.060  1.00 43.92  ? 48  LEU A O     1 
ATOM   321  C  CB    . LEU A 1 50  ? 17.238  -12.708 20.263  1.00 35.40  ? 48  LEU A CB    1 
ATOM   322  C  CG    . LEU A 1 50  ? 16.728  -12.019 21.531  1.00 35.59  ? 48  LEU A CG    1 
ATOM   323  C  CD1   . LEU A 1 50  ? 15.671  -10.955 21.243  1.00 36.36  ? 48  LEU A CD1   1 
ATOM   324  C  CD2   . LEU A 1 50  ? 16.219  -13.070 22.505  1.00 36.98  ? 48  LEU A CD2   1 
ATOM   325  N  N     . GLU A 1 51  ? 19.205  -14.773 18.418  1.00 43.06  ? 49  GLU A N     1 
ATOM   326  C  CA    . GLU A 1 51  ? 19.265  -15.477 17.145  1.00 42.09  ? 49  GLU A CA    1 
ATOM   327  C  C     . GLU A 1 51  ? 18.096  -15.087 16.252  1.00 41.67  ? 49  GLU A C     1 
ATOM   328  O  O     . GLU A 1 51  ? 17.394  -15.954 15.718  1.00 43.34  ? 49  GLU A O     1 
ATOM   329  C  CB    . GLU A 1 51  ? 19.296  -16.994 17.331  1.00 44.12  ? 49  GLU A CB    1 
ATOM   330  C  CG    . GLU A 1 51  ? 20.468  -17.426 18.178  1.00 48.07  ? 49  GLU A CG    1 
ATOM   331  C  CD    . GLU A 1 51  ? 20.722  -18.917 18.187  1.00 50.02  ? 49  GLU A CD    1 
ATOM   332  O  OE1   . GLU A 1 51  ? 19.883  -19.654 17.686  1.00 53.88  ? 49  GLU A OE1   1 
ATOM   333  O  OE2   . GLU A 1 51  ? 21.762  -19.305 18.680  1.00 54.61  ? 49  GLU A OE2   1 
ATOM   334  N  N     . ARG A 1 52  ? 17.911  -13.780 16.075  1.00 40.03  ? 50  ARG A N     1 
ATOM   335  C  CA    . ARG A 1 52  ? 16.908  -13.295 15.141  1.00 41.32  ? 50  ARG A CA    1 
ATOM   336  C  C     . ARG A 1 52  ? 17.260  -11.879 14.704  1.00 37.73  ? 50  ARG A C     1 
ATOM   337  O  O     . ARG A 1 52  ? 18.100  -11.213 15.319  1.00 37.26  ? 50  ARG A O     1 
ATOM   338  C  CB    . ARG A 1 52  ? 15.514  -13.319 15.773  1.00 41.21  ? 50  ARG A CB    1 
ATOM   339  C  CG    . ARG A 1 52  ? 15.425  -12.492 17.042  1.00 46.41  ? 50  ARG A CG    1 
ATOM   340  C  CD    . ARG A 1 52  ? 14.195  -12.794 17.870  1.00 49.15  ? 50  ARG A CD    1 
ATOM   341  N  NE    . ARG A 1 52  ? 13.019  -12.291 17.188  1.00 52.51  ? 50  ARG A NE    1 
ATOM   342  C  CZ    . ARG A 1 52  ? 11.830  -12.112 17.746  1.00 58.48  ? 50  ARG A CZ    1 
ATOM   343  N  NH1   . ARG A 1 52  ? 11.671  -12.234 19.055  1.00 61.37  ? 50  ARG A NH1   1 
ATOM   344  N  NH2   . ARG A 1 52  ? 10.807  -11.773 16.981  1.00 60.26  ? 50  ARG A NH2   1 
ATOM   345  N  N     . ASN A 1 53  ? 16.573  -11.423 13.655  1.00 34.95  ? 51  ASN A N     1 
ATOM   346  C  CA    . ASN A 1 53  ? 16.784  -10.075 13.168  1.00 36.79  ? 51  ASN A CA    1 
ATOM   347  C  C     . ASN A 1 53  ? 15.941  -9.096  13.972  1.00 34.28  ? 51  ASN A C     1 
ATOM   348  O  O     . ASN A 1 53  ? 14.834  -9.398  14.403  1.00 36.31  ? 51  ASN A O     1 
ATOM   349  C  CB    . ASN A 1 53  ? 16.478  -9.928  11.683  1.00 39.11  ? 51  ASN A CB    1 
ATOM   350  C  CG    . ASN A 1 53  ? 17.392  -10.776 10.831  1.00 42.44  ? 51  ASN A CG    1 
ATOM   351  O  OD1   . ASN A 1 53  ? 18.576  -10.933 11.138  1.00 43.26  ? 51  ASN A OD1   1 
ATOM   352  N  ND2   . ASN A 1 53  ? 16.836  -11.355 9.783   1.00 44.69  ? 51  ASN A ND2   1 
ATOM   353  N  N     . VAL A 1 54  ? 16.493  -7.900  14.137  1.00 31.36  ? 52  VAL A N     1 
ATOM   354  C  CA    . VAL A 1 54  ? 15.879  -6.854  14.927  1.00 31.89  ? 52  VAL A CA    1 
ATOM   355  C  C     . VAL A 1 54  ? 16.068  -5.524  14.215  1.00 30.05  ? 52  VAL A C     1 
ATOM   356  O  O     . VAL A 1 54  ? 16.883  -5.385  13.306  1.00 31.91  ? 52  VAL A O     1 
ATOM   357  C  CB    . VAL A 1 54  ? 16.477  -6.788  16.339  1.00 31.11  ? 52  VAL A CB    1 
ATOM   358  C  CG1   . VAL A 1 54  ? 16.278  -8.076  17.098  1.00 30.72  ? 52  VAL A CG1   1 
ATOM   359  C  CG2   . VAL A 1 54  ? 17.950  -6.397  16.296  1.00 31.89  ? 52  VAL A CG2   1 
ATOM   360  N  N     . ALA A 1 55  ? 15.290  -4.550  14.661  1.00 30.43  ? 53  ALA A N     1 
ATOM   361  C  CA    . ALA A 1 55  ? 15.419  -3.182  14.213  1.00 33.25  ? 53  ALA A CA    1 
ATOM   362  C  C     . ALA A 1 55  ? 15.871  -2.362  15.408  1.00 33.97  ? 53  ALA A C     1 
ATOM   363  O  O     . ALA A 1 55  ? 15.327  -2.512  16.505  1.00 31.07  ? 53  ALA A O     1 
ATOM   364  C  CB    . ALA A 1 55  ? 14.117  -2.670  13.637  1.00 33.93  ? 53  ALA A CB    1 
ATOM   365  N  N     . ILE A 1 56  ? 16.868  -1.508  15.163  1.00 34.66  ? 54  ILE A N     1 
ATOM   366  C  CA    . ILE A 1 56  ? 17.437  -0.657  16.186  1.00 33.80  ? 54  ILE A CA    1 
ATOM   367  C  C     . ILE A 1 56  ? 17.265  0.787   15.750  1.00 34.80  ? 54  ILE A C     1 
ATOM   368  O  O     . ILE A 1 56  ? 17.760  1.173   14.698  1.00 37.23  ? 54  ILE A O     1 
ATOM   369  C  CB    . ILE A 1 56  ? 18.924  -0.964  16.409  1.00 35.34  ? 54  ILE A CB    1 
ATOM   370  C  CG1   . ILE A 1 56  ? 19.148  -2.448  16.653  1.00 37.42  ? 54  ILE A CG1   1 
ATOM   371  C  CG2   . ILE A 1 56  ? 19.466  -0.146  17.565  1.00 35.32  ? 54  ILE A CG2   1 
ATOM   372  C  CD1   . ILE A 1 56  ? 20.594  -2.831  16.705  1.00 38.69  ? 54  ILE A CD1   1 
ATOM   373  N  N     . LYS A 1 57  ? 16.591  1.558   16.586  1.00 31.33  ? 55  LYS A N     1 
ATOM   374  C  CA    . LYS A 1 57  ? 16.342  2.962   16.321  1.00 35.91  ? 55  LYS A CA    1 
ATOM   375  C  C     . LYS A 1 57  ? 17.159  3.752   17.326  1.00 36.82  ? 55  LYS A C     1 
ATOM   376  O  O     . LYS A 1 57  ? 17.090  3.455   18.516  1.00 34.93  ? 55  LYS A O     1 
ATOM   377  C  CB    . LYS A 1 57  ? 14.853  3.291   16.472  1.00 39.10  ? 55  LYS A CB    1 
ATOM   378  C  CG    . LYS A 1 57  ? 14.510  4.772   16.404  1.00 43.52  ? 55  LYS A CG    1 
ATOM   379  C  CD    . LYS A 1 57  ? 13.049  5.070   16.654  1.00 50.20  ? 55  LYS A CD    1 
ATOM   380  C  CE    . LYS A 1 57  ? 12.244  5.142   15.379  1.00 55.74  ? 55  LYS A CE    1 
ATOM   381  N  NZ    . LYS A 1 57  ? 10.922  5.764   15.621  1.00 61.49  ? 55  LYS A NZ    1 
ATOM   382  N  N     . LYS A 1 58  ? 17.907  4.751   16.835  1.00 37.50  ? 56  LYS A N     1 
ATOM   383  C  CA    . LYS A 1 58  ? 18.682  5.628   17.697  1.00 39.79  ? 56  LYS A CA    1 
ATOM   384  C  C     . LYS A 1 58  ? 17.926  6.942   17.867  1.00 40.64  ? 56  LYS A C     1 
ATOM   385  O  O     . LYS A 1 58  ? 17.574  7.575   16.870  1.00 41.73  ? 56  LYS A O     1 
ATOM   386  C  CB    . LYS A 1 58  ? 20.056  5.912   17.086  1.00 43.43  ? 56  LYS A CB    1 
ATOM   387  C  CG    . LYS A 1 58  ? 20.959  6.808   17.918  1.00 47.37  ? 56  LYS A CG    1 
ATOM   388  C  CD    . LYS A 1 58  ? 22.153  7.296   17.144  1.00 52.40  ? 56  LYS A CD    1 
ATOM   389  C  CE    . LYS A 1 58  ? 23.130  8.079   17.992  1.00 52.76  ? 56  LYS A CE    1 
ATOM   390  N  NZ    . LYS A 1 58  ? 24.195  8.664   17.155  1.00 53.79  ? 56  LYS A NZ    1 
ATOM   391  N  N     . LEU A 1 59  ? 17.664  7.310   19.129  1.00 38.01  ? 57  LEU A N     1 
ATOM   392  C  CA    . LEU A 1 59  ? 17.167  8.631   19.482  1.00 40.67  ? 57  LEU A CA    1 
ATOM   393  C  C     . LEU A 1 59  ? 18.356  9.450   19.976  1.00 45.45  ? 57  LEU A C     1 
ATOM   394  O  O     . LEU A 1 59  ? 18.978  9.083   20.979  1.00 38.92  ? 57  LEU A O     1 
ATOM   395  C  CB    . LEU A 1 59  ? 16.117  8.522   20.589  1.00 40.81  ? 57  LEU A CB    1 
ATOM   396  C  CG    . LEU A 1 59  ? 14.975  7.529   20.368  1.00 46.10  ? 57  LEU A CG    1 
ATOM   397  C  CD1   . LEU A 1 59  ? 13.984  7.615   21.512  1.00 46.24  ? 57  LEU A CD1   1 
ATOM   398  C  CD2   . LEU A 1 59  ? 14.253  7.773   19.051  1.00 50.39  ? 57  LEU A CD2   1 
ATOM   399  N  N     . SER A 1 60  ? 18.653  10.549  19.262  1.00 47.71  ? 58  SER A N     1 
ATOM   400  C  CA    . SER A 1 60  ? 19.779  11.411  19.583  1.00 46.83  ? 58  SER A CA    1 
ATOM   401  C  C     . SER A 1 60  ? 19.309  12.558  20.472  1.00 43.96  ? 58  SER A C     1 
ATOM   402  O  O     . SER A 1 60  ? 18.516  13.386  20.034  1.00 43.38  ? 58  SER A O     1 
ATOM   403  C  CB    . SER A 1 60  ? 20.424  11.946  18.331  1.00 50.08  ? 58  SER A CB    1 
ATOM   404  O  OG    . SER A 1 60  ? 20.859  10.874  17.508  1.00 56.04  ? 58  SER A OG    1 
ATOM   405  N  N     . ARG A 1 61  ? 19.833  12.604  21.698  1.00 39.54  ? 59  ARG A N     1 
ATOM   406  C  CA    . ARG A 1 61  ? 19.566  13.665  22.658  1.00 43.11  ? 59  ARG A CA    1 
ATOM   407  C  C     . ARG A 1 61  ? 18.070  13.940  22.757  1.00 39.00  ? 59  ARG A C     1 
ATOM   408  O  O     . ARG A 1 61  ? 17.609  15.051  22.479  1.00 38.74  ? 59  ARG A O     1 
ATOM   409  C  CB    . ARG A 1 61  ? 20.357  14.920  22.278  1.00 47.04  ? 59  ARG A CB    1 
ATOM   410  C  CG    . ARG A 1 61  ? 21.864  14.700  22.224  1.00 52.33  ? 59  ARG A CG    1 
ATOM   411  C  CD    . ARG A 1 61  ? 22.646  15.914  21.743  1.00 54.89  ? 59  ARG A CD    1 
ATOM   412  N  NE    . ARG A 1 61  ? 22.210  17.113  22.440  1.00 59.47  ? 59  ARG A NE    1 
ATOM   413  C  CZ    . ARG A 1 61  ? 22.361  17.336  23.742  1.00 57.15  ? 59  ARG A CZ    1 
ATOM   414  N  NH1   . ARG A 1 61  ? 23.122  16.543  24.479  1.00 57.11  ? 59  ARG A NH1   1 
ATOM   415  N  NH2   . ARG A 1 61  ? 21.770  18.384  24.295  1.00 53.61  ? 59  ARG A NH2   1 
ATOM   416  N  N     . PRO A 1 62  ? 17.254  12.949  23.166  1.00 36.47  ? 60  PRO A N     1 
ATOM   417  C  CA    . PRO A 1 62  ? 15.798  13.113  23.134  1.00 35.70  ? 60  PRO A CA    1 
ATOM   418  C  C     . PRO A 1 62  ? 15.280  14.107  24.171  1.00 34.33  ? 60  PRO A C     1 
ATOM   419  O  O     . PRO A 1 62  ? 14.163  14.591  24.056  1.00 33.68  ? 60  PRO A O     1 
ATOM   420  C  CB    . PRO A 1 62  ? 15.227  11.720  23.413  1.00 35.84  ? 60  PRO A CB    1 
ATOM   421  C  CG    . PRO A 1 62  ? 16.369  10.872  23.819  1.00 36.18  ? 60  PRO A CG    1 
ATOM   422  C  CD    . PRO A 1 62  ? 17.665  11.612  23.604  1.00 36.81  ? 60  PRO A CD    1 
ATOM   423  N  N     . PHE A 1 63  ? 16.096  14.397  25.185  1.00 34.54  ? 61  PHE A N     1 
ATOM   424  C  CA    . PHE A 1 63  ? 15.753  15.368  26.213  1.00 34.83  ? 61  PHE A CA    1 
ATOM   425  C  C     . PHE A 1 63  ? 16.089  16.806  25.801  1.00 34.45  ? 61  PHE A C     1 
ATOM   426  O  O     . PHE A 1 63  ? 16.010  17.697  26.637  1.00 35.09  ? 61  PHE A O     1 
ATOM   427  C  CB    . PHE A 1 63  ? 16.539  15.032  27.478  1.00 37.43  ? 61  PHE A CB    1 
ATOM   428  C  CG    . PHE A 1 63  ? 18.021  14.869  27.233  1.00 38.69  ? 61  PHE A CG    1 
ATOM   429  C  CD1   . PHE A 1 63  ? 18.865  15.965  27.207  1.00 38.75  ? 61  PHE A CD1   1 
ATOM   430  C  CD2   . PHE A 1 63  ? 18.570  13.611  27.009  1.00 40.33  ? 61  PHE A CD2   1 
ATOM   431  C  CE1   . PHE A 1 63  ? 20.226  15.813  26.983  1.00 40.74  ? 61  PHE A CE1   1 
ATOM   432  C  CE2   . PHE A 1 63  ? 19.926  13.464  26.765  1.00 41.37  ? 61  PHE A CE2   1 
ATOM   433  C  CZ    . PHE A 1 63  ? 20.754  14.563  26.756  1.00 40.98  ? 61  PHE A CZ    1 
ATOM   434  N  N     . GLN A 1 64  ? 16.505  17.032  24.549  1.00 34.07  ? 62  GLN A N     1 
ATOM   435  C  CA    . GLN A 1 64  ? 17.101  18.304  24.150  1.00 35.62  ? 62  GLN A CA    1 
ATOM   436  C  C     . GLN A 1 64  ? 16.102  19.455  24.291  1.00 33.11  ? 62  GLN A C     1 
ATOM   437  O  O     . GLN A 1 64  ? 16.477  20.612  24.550  1.00 31.96  ? 62  GLN A O     1 
ATOM   438  C  CB    . GLN A 1 64  ? 17.651  18.201  22.723  1.00 37.35  ? 62  GLN A CB    1 
ATOM   439  C  CG    . GLN A 1 64  ? 16.601  17.897  21.659  1.00 37.38  ? 62  GLN A CG    1 
ATOM   440  C  CD    . GLN A 1 64  ? 17.274  17.716  20.323  1.00 39.82  ? 62  GLN A CD    1 
ATOM   441  O  OE1   . GLN A 1 64  ? 17.486  18.672  19.592  1.00 41.06  ? 62  GLN A OE1   1 
ATOM   442  N  NE2   . GLN A 1 64  ? 17.615  16.483  19.992  1.00 39.66  ? 62  GLN A NE2   1 
ATOM   443  N  N     . ASN A 1 65  ? 14.816  19.155  24.066  1.00 30.69  ? 63  ASN A N     1 
ATOM   444  C  CA    . ASN A 1 65  ? 13.749  20.105  24.344  1.00 28.55  ? 63  ASN A CA    1 
ATOM   445  C  C     . ASN A 1 65  ? 12.492  19.317  24.658  1.00 27.04  ? 63  ASN A C     1 
ATOM   446  O  O     . ASN A 1 65  ? 12.416  18.105  24.380  1.00 27.04  ? 63  ASN A O     1 
ATOM   447  C  CB    . ASN A 1 65  ? 13.529  21.118  23.210  1.00 30.34  ? 63  ASN A CB    1 
ATOM   448  C  CG    . ASN A 1 65  ? 13.153  20.479  21.886  1.00 32.36  ? 63  ASN A CG    1 
ATOM   449  O  OD1   . ASN A 1 65  ? 12.229  19.673  21.827  1.00 27.55  ? 63  ASN A OD1   1 
ATOM   450  N  ND2   . ASN A 1 65  ? 13.866  20.832  20.823  1.00 32.24  ? 63  ASN A ND2   1 
ATOM   451  N  N     . GLN A 1 66  ? 11.487  19.999  25.224  1.00 25.54  ? 64  GLN A N     1 
ATOM   452  C  CA    . GLN A 1 66  ? 10.275  19.285  25.620  1.00 26.17  ? 64  GLN A CA    1 
ATOM   453  C  C     . GLN A 1 66  ? 9.567   18.598  24.445  1.00 25.45  ? 64  GLN A C     1 
ATOM   454  O  O     . GLN A 1 66  ? 8.962   17.547  24.604  1.00 25.22  ? 64  GLN A O     1 
ATOM   455  C  CB    . GLN A 1 66  ? 9.290   20.243  26.276  1.00 26.89  ? 64  GLN A CB    1 
ATOM   456  C  CG    . GLN A 1 66  ? 9.768   20.785  27.602  1.00 27.51  ? 64  GLN A CG    1 
ATOM   457  C  CD    . GLN A 1 66  ? 8.598   20.868  28.546  1.00 27.05  ? 64  GLN A CD    1 
ATOM   458  O  OE1   . GLN A 1 66  ? 8.150   19.869  29.100  1.00 25.31  ? 64  GLN A OE1   1 
ATOM   459  N  NE2   . GLN A 1 66  ? 8.079   22.065  28.715  1.00 28.26  ? 64  GLN A NE2   1 
ATOM   460  N  N     . THR A 1 67  ? 9.576   19.202  23.261  1.00 26.87  ? 65  THR A N     1 
ATOM   461  C  CA    . THR A 1 67  ? 8.865   18.598  22.141  1.00 27.85  ? 65  THR A CA    1 
ATOM   462  C  C     . THR A 1 67  ? 9.445   17.208  21.854  1.00 26.36  ? 65  THR A C     1 
ATOM   463  O  O     . THR A 1 67  ? 8.720   16.203  21.770  1.00 26.01  ? 65  THR A O     1 
ATOM   464  C  CB    . THR A 1 67  ? 8.904   19.517  20.909  1.00 28.55  ? 65  THR A CB    1 
ATOM   465  O  OG1   . THR A 1 67  ? 8.214   20.736  21.204  1.00 28.19  ? 65  THR A OG1   1 
ATOM   466  C  CG2   . THR A 1 67  ? 8.305   18.866  19.676  1.00 30.13  ? 65  THR A CG2   1 
ATOM   467  N  N     . HIS A 1 68  ? 10.770  17.134  21.758  1.00 26.34  ? 66  HIS A N     1 
ATOM   468  C  CA    . HIS A 1 68  ? 11.447  15.866  21.559  1.00 30.59  ? 66  HIS A CA    1 
ATOM   469  C  C     . HIS A 1 68  ? 11.231  14.938  22.743  1.00 29.01  ? 66  HIS A C     1 
ATOM   470  O  O     . HIS A 1 68  ? 10.987  13.763  22.538  1.00 28.43  ? 66  HIS A O     1 
ATOM   471  C  CB    . HIS A 1 68  ? 12.957  16.010  21.335  1.00 31.68  ? 66  HIS A CB    1 
ATOM   472  C  CG    . HIS A 1 68  ? 13.321  16.500  19.976  1.00 37.03  ? 66  HIS A CG    1 
ATOM   473  N  ND1   . HIS A 1 68  ? 14.008  15.716  19.076  1.00 44.73  ? 66  HIS A ND1   1 
ATOM   474  C  CD2   . HIS A 1 68  ? 13.097  17.656  19.358  1.00 39.06  ? 66  HIS A CD2   1 
ATOM   475  C  CE1   . HIS A 1 68  ? 14.190  16.397  17.961  1.00 44.44  ? 66  HIS A CE1   1 
ATOM   476  N  NE2   . HIS A 1 68  ? 13.656  17.583  18.118  1.00 41.19  ? 66  HIS A NE2   1 
ATOM   477  N  N     . ALA A 1 69  ? 11.312  15.485  23.960  1.00 27.50  ? 67  ALA A N     1 
ATOM   478  C  CA    . ALA A 1 69  ? 11.362  14.691  25.169  1.00 26.91  ? 67  ALA A CA    1 
ATOM   479  C  C     . ALA A 1 69  ? 10.037  13.999  25.429  1.00 28.28  ? 67  ALA A C     1 
ATOM   480  O  O     . ALA A 1 69  ? 10.020  12.835  25.858  1.00 25.49  ? 67  ALA A O     1 
ATOM   481  C  CB    . ALA A 1 69  ? 11.747  15.571  26.334  1.00 27.06  ? 67  ALA A CB    1 
ATOM   482  N  N     . LYS A 1 70  ? 8.929   14.725  25.186  1.00 26.56  ? 68  LYS A N     1 
ATOM   483  C  CA    . LYS A 1 70  ? 7.614   14.179  25.466  1.00 26.97  ? 68  LYS A CA    1 
ATOM   484  C  C     . LYS A 1 70  ? 7.331   12.994  24.546  1.00 26.88  ? 68  LYS A C     1 
ATOM   485  O  O     . LYS A 1 70  ? 6.748   11.990  24.971  1.00 25.45  ? 68  LYS A O     1 
ATOM   486  C  CB    . LYS A 1 70  ? 6.535   15.250  25.314  1.00 24.40  ? 68  LYS A CB    1 
ATOM   487  C  CG    . LYS A 1 70  ? 6.517   16.288  26.425  1.00 25.04  ? 68  LYS A CG    1 
ATOM   488  C  CD    . LYS A 1 70  ? 5.653   17.496  26.123  1.00 25.80  ? 68  LYS A CD    1 
ATOM   489  C  CE    . LYS A 1 70  ? 5.522   18.414  27.324  1.00 26.58  ? 68  LYS A CE    1 
ATOM   490  N  NZ    . LYS A 1 70  ? 4.934   19.703  26.927  1.00 28.89  ? 68  LYS A NZ    1 
ATOM   491  N  N     . ARG A 1 71  ? 7.721   13.123  23.278  1.00 25.41  ? 69  ARG A N     1 
ATOM   492  C  CA    . ARG A 1 71  ? 7.504   12.048  22.323  1.00 30.16  ? 69  ARG A CA    1 
ATOM   493  C  C     . ARG A 1 71  ? 8.371   10.823  22.660  1.00 27.77  ? 69  ARG A C     1 
ATOM   494  O  O     . ARG A 1 71  ? 7.864   9.707   22.698  1.00 25.94  ? 69  ARG A O     1 
ATOM   495  C  CB    . ARG A 1 71  ? 7.735   12.524  20.883  1.00 31.87  ? 69  ARG A CB    1 
ATOM   496  C  CG    . ARG A 1 71  ? 7.684   11.372  19.888  1.00 39.54  ? 69  ARG A CG    1 
ATOM   497  C  CD    . ARG A 1 71  ? 7.506   11.766  18.431  1.00 47.68  ? 69  ARG A CD    1 
ATOM   498  N  NE    . ARG A 1 71  ? 7.052   10.601  17.671  1.00 57.75  ? 69  ARG A NE    1 
ATOM   499  C  CZ    . ARG A 1 71  ? 5.803   10.388  17.230  1.00 53.46  ? 69  ARG A CZ    1 
ATOM   500  N  NH1   . ARG A 1 71  ? 4.905   11.357  17.214  1.00 55.87  ? 69  ARG A NH1   1 
ATOM   501  N  NH2   . ARG A 1 71  ? 5.465   9.201   16.759  1.00 46.30  ? 69  ARG A NH2   1 
ATOM   502  N  N     . ALA A 1 72  ? 9.667   11.015  22.942  1.00 27.24  ? 70  ALA A N     1 
ATOM   503  C  CA    . ALA A 1 72  ? 10.554  9.906   23.296  1.00 27.32  ? 70  ALA A CA    1 
ATOM   504  C  C     . ALA A 1 72  ? 10.091  9.190   24.556  1.00 27.79  ? 70  ALA A C     1 
ATOM   505  O  O     . ALA A 1 72  ? 10.089  7.950   24.642  1.00 25.33  ? 70  ALA A O     1 
ATOM   506  C  CB    . ALA A 1 72  ? 11.960  10.404  23.508  1.00 27.64  ? 70  ALA A CB    1 
ATOM   507  N  N     . TYR A 1 73  ? 9.780   9.986   25.576  1.00 27.90  ? 71  TYR A N     1 
ATOM   508  C  CA    . TYR A 1 73  ? 9.378   9.442   26.863  1.00 27.68  ? 71  TYR A CA    1 
ATOM   509  C  C     . TYR A 1 73  ? 8.121   8.600   26.705  1.00 26.75  ? 71  TYR A C     1 
ATOM   510  O  O     . TYR A 1 73  ? 8.053   7.473   27.202  1.00 24.72  ? 71  TYR A O     1 
ATOM   511  C  CB    . TYR A 1 73  ? 9.149   10.581  27.860  1.00 27.52  ? 71  TYR A CB    1 
ATOM   512  C  CG    . TYR A 1 73  ? 8.741   10.109  29.236  1.00 28.21  ? 71  TYR A CG    1 
ATOM   513  C  CD1   . TYR A 1 73  ? 9.643   9.443   30.057  1.00 31.19  ? 71  TYR A CD1   1 
ATOM   514  C  CD2   . TYR A 1 73  ? 7.466   10.341  29.716  1.00 28.40  ? 71  TYR A CD2   1 
ATOM   515  C  CE1   . TYR A 1 73  ? 9.287   9.011   31.322  1.00 30.93  ? 71  TYR A CE1   1 
ATOM   516  C  CE2   . TYR A 1 73  ? 7.089   9.895   30.969  1.00 30.01  ? 71  TYR A CE2   1 
ATOM   517  C  CZ    . TYR A 1 73  ? 8.001   9.235   31.762  1.00 31.18  ? 71  TYR A CZ    1 
ATOM   518  O  OH    . TYR A 1 73  ? 7.634   8.810   32.982  1.00 36.57  ? 71  TYR A OH    1 
ATOM   519  N  N     . ARG A 1 74  ? 7.095   9.147   26.054  1.00 25.68  ? 72  ARG A N     1 
ATOM   520  C  CA    . ARG A 1 74  ? 5.854   8.397   26.004  1.00 28.13  ? 72  ARG A CA    1 
ATOM   521  C  C     . ARG A 1 74  ? 6.017   7.137   25.151  1.00 25.56  ? 72  ARG A C     1 
ATOM   522  O  O     . ARG A 1 74  ? 5.394   6.123   25.459  1.00 26.28  ? 72  ARG A O     1 
ATOM   523  C  CB    . ARG A 1 74  ? 4.692   9.262   25.526  1.00 28.08  ? 72  ARG A CB    1 
ATOM   524  C  CG    . ARG A 1 74  ? 4.678   9.554   24.040  1.00 30.57  ? 72  ARG A CG    1 
ATOM   525  C  CD    . ARG A 1 74  ? 3.740   10.713  23.749  1.00 35.38  ? 72  ARG A CD    1 
ATOM   526  N  NE    . ARG A 1 74  ? 2.374   10.443  24.185  1.00 36.74  ? 72  ARG A NE    1 
ATOM   527  C  CZ    . ARG A 1 74  ? 1.462   9.796   23.452  1.00 34.47  ? 72  ARG A CZ    1 
ATOM   528  N  NH1   . ARG A 1 74  ? 1.793   9.304   22.279  1.00 31.08  ? 72  ARG A NH1   1 
ATOM   529  N  NH2   . ARG A 1 74  ? 0.213   9.675   23.878  1.00 32.84  ? 72  ARG A NH2   1 
ATOM   530  N  N     . GLU A 1 75  ? 6.844   7.177   24.098  1.00 26.74  ? 73  GLU A N     1 
ATOM   531  C  CA    . GLU A 1 75  ? 7.033   5.979   23.274  1.00 27.83  ? 73  GLU A CA    1 
ATOM   532  C  C     . GLU A 1 75  ? 7.771   4.897   24.062  1.00 27.34  ? 73  GLU A C     1 
ATOM   533  O  O     . GLU A 1 75  ? 7.416   3.723   23.958  1.00 24.96  ? 73  GLU A O     1 
ATOM   534  C  CB    . GLU A 1 75  ? 7.673   6.334   21.934  1.00 30.40  ? 73  GLU A CB    1 
ATOM   535  C  CG    . GLU A 1 75  ? 6.741   7.286   21.153  1.00 39.13  ? 73  GLU A CG    1 
ATOM   536  C  CD    . GLU A 1 75  ? 6.609   7.145   19.639  1.00 45.85  ? 73  GLU A CD    1 
ATOM   537  O  OE1   . GLU A 1 75  ? 7.583   6.690   19.003  1.00 55.19  ? 73  GLU A OE1   1 
ATOM   538  O  OE2   . GLU A 1 75  ? 5.519   7.510   19.090  1.00 45.13  ? 73  GLU A OE2   1 
ATOM   539  N  N     . LEU A 1 76  ? 8.765   5.273   24.871  1.00 26.46  ? 74  LEU A N     1 
ATOM   540  C  CA    . LEU A 1 76  ? 9.406   4.332   25.781  1.00 28.86  ? 74  LEU A CA    1 
ATOM   541  C  C     . LEU A 1 76  ? 8.407   3.704   26.756  1.00 27.98  ? 74  LEU A C     1 
ATOM   542  O  O     . LEU A 1 76  ? 8.383   2.476   26.930  1.00 27.99  ? 74  LEU A O     1 
ATOM   543  C  CB    . LEU A 1 76  ? 10.512  5.053   26.556  1.00 32.85  ? 74  LEU A CB    1 
ATOM   544  C  CG    . LEU A 1 76  ? 11.822  5.255   25.796  1.00 38.46  ? 74  LEU A CG    1 
ATOM   545  C  CD1   . LEU A 1 76  ? 12.701  6.295   26.476  1.00 40.96  ? 74  LEU A CD1   1 
ATOM   546  C  CD2   . LEU A 1 76  ? 12.566  3.937   25.682  1.00 40.30  ? 74  LEU A CD2   1 
ATOM   547  N  N     . VAL A 1 77  ? 7.659   4.553   27.473  1.00 26.20  ? 75  VAL A N     1 
ATOM   548  C  CA    . VAL A 1 77  ? 6.752   4.063   28.492  1.00 26.01  ? 75  VAL A CA    1 
ATOM   549  C  C     . VAL A 1 77  ? 5.714   3.128   27.869  1.00 26.35  ? 75  VAL A C     1 
ATOM   550  O  O     . VAL A 1 77  ? 5.439   2.046   28.388  1.00 25.15  ? 75  VAL A O     1 
ATOM   551  C  CB    . VAL A 1 77  ? 6.092   5.222   29.252  1.00 26.47  ? 75  VAL A CB    1 
ATOM   552  C  CG1   . VAL A 1 77  ? 4.933   4.727   30.121  1.00 26.65  ? 75  VAL A CG1   1 
ATOM   553  C  CG2   . VAL A 1 77  ? 7.127   5.948   30.103  1.00 28.49  ? 75  VAL A CG2   1 
ATOM   554  N  N     . LEU A 1 78  ? 5.097   3.566   26.783  1.00 25.33  ? 76  LEU A N     1 
ATOM   555  C  CA    . LEU A 1 78  ? 4.037   2.797   26.146  1.00 24.33  ? 76  LEU A CA    1 
ATOM   556  C  C     . LEU A 1 78  ? 4.584   1.521   25.509  1.00 27.31  ? 76  LEU A C     1 
ATOM   557  O  O     . LEU A 1 78  ? 3.972   0.469   25.637  1.00 28.81  ? 76  LEU A O     1 
ATOM   558  C  CB    . LEU A 1 78  ? 3.332   3.659   25.107  1.00 23.22  ? 76  LEU A CB    1 
ATOM   559  C  CG    . LEU A 1 78  ? 2.510   4.798   25.704  1.00 26.24  ? 76  LEU A CG    1 
ATOM   560  C  CD1   . LEU A 1 78  ? 1.981   5.744   24.645  1.00 26.02  ? 76  LEU A CD1   1 
ATOM   561  C  CD2   . LEU A 1 78  ? 1.368   4.260   26.545  1.00 28.30  ? 76  LEU A CD2   1 
ATOM   562  N  N     . MET A 1 79  ? 5.720   1.595   24.812  1.00 24.60  ? 77  MET A N     1 
ATOM   563  C  CA    . MET A 1 79  ? 6.225   0.370   24.227  1.00 29.72  ? 77  MET A CA    1 
ATOM   564  C  C     . MET A 1 79  ? 6.511   -0.669  25.298  1.00 30.34  ? 77  MET A C     1 
ATOM   565  O  O     . MET A 1 79  ? 6.286   -1.860  25.052  1.00 29.86  ? 77  MET A O     1 
ATOM   566  C  CB    . MET A 1 79  ? 7.487   0.627   23.422  1.00 33.03  ? 77  MET A CB    1 
ATOM   567  C  CG    . MET A 1 79  ? 7.145   0.877   22.028  1.00 35.94  ? 77  MET A CG    1 
ATOM   568  S  SD    . MET A 1 79  ? 8.602   1.197   21.047  1.00 48.04  ? 77  MET A SD    1 
ATOM   569  C  CE    . MET A 1 79  ? 8.854   -0.499  20.582  1.00 30.43  ? 77  MET A CE    1 
ATOM   570  N  N     . LYS A 1 80  ? 6.948   -0.225  26.486  1.00 28.08  ? 78  LYS A N     1 
ATOM   571  C  CA    . LYS A 1 80  ? 7.255   -1.166  27.539  1.00 31.25  ? 78  LYS A CA    1 
ATOM   572  C  C     . LYS A 1 80  ? 6.007   -1.760  28.177  1.00 32.18  ? 78  LYS A C     1 
ATOM   573  O  O     . LYS A 1 80  ? 6.040   -2.915  28.594  1.00 32.48  ? 78  LYS A O     1 
ATOM   574  C  CB    . LYS A 1 80  ? 8.084   -0.522  28.645  1.00 31.93  ? 78  LYS A CB    1 
ATOM   575  C  CG    . LYS A 1 80  ? 9.537   -0.354  28.272  1.00 37.52  ? 78  LYS A CG    1 
ATOM   576  C  CD    . LYS A 1 80  ? 10.411  -0.236  29.453  1.00 43.92  ? 78  LYS A CD    1 
ATOM   577  C  CE    . LYS A 1 80  ? 10.417  1.151   30.013  1.00 46.66  ? 78  LYS A CE    1 
ATOM   578  N  NZ    . LYS A 1 80  ? 11.322  1.158   31.185  1.00 52.02  ? 78  LYS A NZ    1 
ATOM   579  N  N     . CYS A 1 81  ? 4.960   -0.962  28.387  1.00 29.24  ? 79  CYS A N     1 
ATOM   580  C  CA    . CYS A 1 81  ? 3.833   -1.475  29.148  1.00 30.13  ? 79  CYS A CA    1 
ATOM   581  C  C     . CYS A 1 81  ? 2.747   -2.064  28.241  1.00 30.50  ? 79  CYS A C     1 
ATOM   582  O  O     . CYS A 1 81  ? 1.836   -2.727  28.738  1.00 34.72  ? 79  CYS A O     1 
ATOM   583  C  CB    . CYS A 1 81  ? 3.235   -0.420  30.076  1.00 31.90  ? 79  CYS A CB    1 
ATOM   584  S  SG    . CYS A 1 81  ? 2.296   0.857   29.206  1.00 33.75  ? 79  CYS A SG    1 
ATOM   585  N  N     . VAL A 1 82  ? 2.806   -1.849  26.925  1.00 26.20  ? 80  VAL A N     1 
ATOM   586  C  CA    . VAL A 1 82  ? 1.821   -2.471  26.053  1.00 26.14  ? 80  VAL A CA    1 
ATOM   587  C  C     . VAL A 1 82  ? 2.339   -3.850  25.609  1.00 28.36  ? 80  VAL A C     1 
ATOM   588  O  O     . VAL A 1 82  ? 3.475   -3.987  25.168  1.00 28.77  ? 80  VAL A O     1 
ATOM   589  C  CB    . VAL A 1 82  ? 1.461   -1.583  24.852  1.00 25.50  ? 80  VAL A CB    1 
ATOM   590  C  CG1   . VAL A 1 82  ? 0.652   -2.355  23.813  1.00 24.77  ? 80  VAL A CG1   1 
ATOM   591  C  CG2   . VAL A 1 82  ? 0.739   -0.298  25.289  1.00 26.44  ? 80  VAL A CG2   1 
ATOM   592  N  N     . ASN A 1 83  ? 1.470   -4.862  25.672  1.00 29.07  ? 81  ASN A N     1 
ATOM   593  C  CA    . ASN A 1 83  ? 1.793   -6.175  25.129  1.00 29.41  ? 81  ASN A CA    1 
ATOM   594  C  C     . ASN A 1 83  ? 0.595   -6.646  24.312  1.00 26.91  ? 81  ASN A C     1 
ATOM   595  O  O     . ASN A 1 83  ? -0.353  -7.218  24.843  1.00 27.37  ? 81  ASN A O     1 
ATOM   596  C  CB    . ASN A 1 83  ? 2.177   -7.159  26.232  1.00 33.12  ? 81  ASN A CB    1 
ATOM   597  C  CG    . ASN A 1 83  ? 2.566   -8.509  25.668  1.00 40.28  ? 81  ASN A CG    1 
ATOM   598  O  OD1   . ASN A 1 83  ? 3.050   -8.595  24.541  1.00 39.42  ? 81  ASN A OD1   1 
ATOM   599  N  ND2   . ASN A 1 83  ? 2.408   -9.565  26.449  1.00 47.76  ? 81  ASN A ND2   1 
ATOM   600  N  N     . HIS A 1 84  ? 0.597   -6.329  23.026  1.00 23.54  ? 82  HIS A N     1 
ATOM   601  C  CA    . HIS A 1 84  ? -0.554  -6.645  22.204  1.00 23.34  ? 82  HIS A CA    1 
ATOM   602  C  C     . HIS A 1 84  ? -0.063  -7.047  20.820  1.00 23.92  ? 82  HIS A C     1 
ATOM   603  O  O     . HIS A 1 84  ? 0.866   -6.457  20.271  1.00 23.77  ? 82  HIS A O     1 
ATOM   604  C  CB    . HIS A 1 84  ? -1.506  -5.448  22.140  1.00 24.76  ? 82  HIS A CB    1 
ATOM   605  C  CG    . HIS A 1 84  ? -2.801  -5.714  21.468  1.00 23.32  ? 82  HIS A CG    1 
ATOM   606  N  ND1   . HIS A 1 84  ? -2.967  -5.746  20.098  1.00 24.83  ? 82  HIS A ND1   1 
ATOM   607  C  CD2   . HIS A 1 84  ? -4.001  -5.939  21.987  1.00 24.61  ? 82  HIS A CD2   1 
ATOM   608  C  CE1   . HIS A 1 84  ? -4.230  -6.018  19.805  1.00 25.59  ? 82  HIS A CE1   1 
ATOM   609  N  NE2   . HIS A 1 84  ? -4.879  -6.160  20.944  1.00 26.33  ? 82  HIS A NE2   1 
ATOM   610  N  N     . LYS A 1 85  ? -0.771  -8.014  20.237  1.00 21.91  ? 83  LYS A N     1 
ATOM   611  C  CA    . LYS A 1 85  ? -0.438  -8.541  18.919  1.00 25.78  ? 83  LYS A CA    1 
ATOM   612  C  C     . LYS A 1 85  ? -0.272  -7.435  17.868  1.00 23.88  ? 83  LYS A C     1 
ATOM   613  O  O     . LYS A 1 85  ? 0.546   -7.565  16.960  1.00 23.60  ? 83  LYS A O     1 
ATOM   614  C  CB    . LYS A 1 85  ? -1.538  -9.510  18.481  1.00 29.21  ? 83  LYS A CB    1 
ATOM   615  C  CG    . LYS A 1 85  ? -1.366  -10.082 17.088  1.00 34.17  ? 83  LYS A CG    1 
ATOM   616  C  CD    . LYS A 1 85  ? -2.489  -10.991 16.725  1.00 38.22  ? 83  LYS A CD    1 
ATOM   617  C  CE    . LYS A 1 85  ? -2.427  -11.382 15.265  1.00 45.08  ? 83  LYS A CE    1 
ATOM   618  N  NZ    . LYS A 1 85  ? -3.316  -12.531 15.010  1.00 47.27  ? 83  LYS A NZ    1 
ATOM   619  N  N     . ASN A 1 86  ? -1.038  -6.350  17.951  1.00 22.50  ? 84  ASN A N     1 
ATOM   620  C  CA    . ASN A 1 86  ? -1.039  -5.384  16.862  1.00 22.46  ? 84  ASN A CA    1 
ATOM   621  C  C     . ASN A 1 86  ? -0.336  -4.060  17.211  1.00 21.86  ? 84  ASN A C     1 
ATOM   622  O  O     . ASN A 1 86  ? -0.530  -3.068  16.514  1.00 21.61  ? 84  ASN A O     1 
ATOM   623  C  CB    . ASN A 1 86  ? -2.473  -5.154  16.398  1.00 22.46  ? 84  ASN A CB    1 
ATOM   624  C  CG    . ASN A 1 86  ? -3.190  -6.426  16.024  1.00 24.56  ? 84  ASN A CG    1 
ATOM   625  O  OD1   . ASN A 1 86  ? -4.158  -6.797  16.668  1.00 24.33  ? 84  ASN A OD1   1 
ATOM   626  N  ND2   . ASN A 1 86  ? -2.712  -7.113  15.003  1.00 24.93  ? 84  ASN A ND2   1 
ATOM   627  N  N     . ILE A 1 87  ? 0.528   -4.070  18.237  1.00 20.35  ? 85  ILE A N     1 
ATOM   628  C  CA    . ILE A 1 87  ? 1.352   -2.938  18.637  1.00 22.50  ? 85  ILE A CA    1 
ATOM   629  C  C     . ILE A 1 87  ? 2.791   -3.445  18.684  1.00 25.48  ? 85  ILE A C     1 
ATOM   630  O  O     . ILE A 1 87  ? 3.045   -4.496  19.271  1.00 25.04  ? 85  ILE A O     1 
ATOM   631  C  CB    . ILE A 1 87  ? 0.904   -2.345  19.989  1.00 21.89  ? 85  ILE A CB    1 
ATOM   632  C  CG1   . ILE A 1 87  ? -0.590  -1.968  20.008  1.00 20.31  ? 85  ILE A CG1   1 
ATOM   633  C  CG2   . ILE A 1 87  ? 1.861   -1.213  20.401  1.00 22.90  ? 85  ILE A CG2   1 
ATOM   634  C  CD1   . ILE A 1 87  ? -1.028  -0.904  19.005  1.00 21.45  ? 85  ILE A CD1   1 
ATOM   635  N  N     . ILE A 1 88  ? 3.714   -2.732  18.022  1.00 25.10  ? 86  ILE A N     1 
ATOM   636  C  CA    . ILE A 1 88  ? 5.117   -3.131  18.014  1.00 26.47  ? 86  ILE A CA    1 
ATOM   637  C  C     . ILE A 1 88  ? 5.619   -3.310  19.452  1.00 27.87  ? 86  ILE A C     1 
ATOM   638  O  O     . ILE A 1 88  ? 5.383   -2.470  20.327  1.00 28.30  ? 86  ILE A O     1 
ATOM   639  C  CB    . ILE A 1 88  ? 5.970   -2.125  17.216  1.00 25.49  ? 86  ILE A CB    1 
ATOM   640  C  CG1   . ILE A 1 88  ? 7.340   -2.713  16.880  1.00 28.23  ? 86  ILE A CG1   1 
ATOM   641  C  CG2   . ILE A 1 88  ? 6.050   -0.767  17.914  1.00 25.12  ? 86  ILE A CG2   1 
ATOM   642  C  CD1   . ILE A 1 88  ? 7.296   -3.911  15.974  1.00 27.74  ? 86  ILE A CD1   1 
ATOM   643  N  N     . GLY A 1 89  ? 6.291   -4.441  19.677  1.00 30.84  ? 87  GLY A N     1 
ATOM   644  C  CA    . GLY A 1 89  ? 6.898   -4.782  20.955  1.00 32.83  ? 87  GLY A CA    1 
ATOM   645  C  C     . GLY A 1 89  ? 8.324   -4.249  21.122  1.00 29.38  ? 87  GLY A C     1 
ATOM   646  O  O     . GLY A 1 89  ? 9.053   -4.065  20.165  1.00 30.58  ? 87  GLY A O     1 
ATOM   647  N  N     . LEU A 1 90  ? 8.713   -4.021  22.366  1.00 30.65  ? 88  LEU A N     1 
ATOM   648  C  CA    . LEU A 1 90  ? 10.081  -3.687  22.724  1.00 29.64  ? 88  LEU A CA    1 
ATOM   649  C  C     . LEU A 1 90  ? 10.872  -4.944  23.119  1.00 32.38  ? 88  LEU A C     1 
ATOM   650  O  O     . LEU A 1 90  ? 10.526  -5.611  24.091  1.00 32.88  ? 88  LEU A O     1 
ATOM   651  C  CB    . LEU A 1 90  ? 10.014  -2.698  23.892  1.00 28.79  ? 88  LEU A CB    1 
ATOM   652  C  CG    . LEU A 1 90  ? 11.323  -1.971  24.177  1.00 33.98  ? 88  LEU A CG    1 
ATOM   653  C  CD1   . LEU A 1 90  ? 11.833  -1.283  22.928  1.00 35.10  ? 88  LEU A CD1   1 
ATOM   654  C  CD2   . LEU A 1 90  ? 11.166  -0.957  25.291  1.00 37.20  ? 88  LEU A CD2   1 
ATOM   655  N  N     . LEU A 1 91  ? 11.952  -5.255  22.380  1.00 28.54  ? 89  LEU A N     1 
ATOM   656  C  CA    . LEU A 1 91  ? 12.823  -6.369  22.724  1.00 30.02  ? 89  LEU A CA    1 
ATOM   657  C  C     . LEU A 1 91  ? 13.920  -5.946  23.695  1.00 28.87  ? 89  LEU A C     1 
ATOM   658  O  O     . LEU A 1 91  ? 14.354  -6.759  24.495  1.00 30.69  ? 89  LEU A O     1 
ATOM   659  C  CB    . LEU A 1 91  ? 13.493  -6.945  21.474  1.00 30.64  ? 89  LEU A CB    1 
ATOM   660  C  CG    . LEU A 1 91  ? 12.576  -7.642  20.481  1.00 32.81  ? 89  LEU A CG    1 
ATOM   661  C  CD1   . LEU A 1 91  ? 13.399  -8.093  19.294  1.00 33.54  ? 89  LEU A CD1   1 
ATOM   662  C  CD2   . LEU A 1 91  ? 11.886  -8.843  21.125  1.00 37.54  ? 89  LEU A CD2   1 
ATOM   663  N  N     . ASN A 1 92  ? 14.410  -4.706  23.576  1.00 27.55  ? 90  ASN A N     1 
ATOM   664  C  CA    . ASN A 1 92  ? 15.489  -4.242  24.426  1.00 29.58  ? 90  ASN A CA    1 
ATOM   665  C  C     . ASN A 1 92  ? 15.551  -2.716  24.320  1.00 28.73  ? 90  ASN A C     1 
ATOM   666  O  O     . ASN A 1 92  ? 15.019  -2.121  23.389  1.00 26.94  ? 90  ASN A O     1 
ATOM   667  C  CB    . ASN A 1 92  ? 16.823  -4.914  24.067  1.00 29.45  ? 90  ASN A CB    1 
ATOM   668  C  CG    . ASN A 1 92  ? 17.869  -4.792  25.154  1.00 30.09  ? 90  ASN A CG    1 
ATOM   669  O  OD1   . ASN A 1 92  ? 17.545  -4.514  26.305  1.00 29.92  ? 90  ASN A OD1   1 
ATOM   670  N  ND2   . ASN A 1 92  ? 19.132  -4.957  24.791  1.00 29.49  ? 90  ASN A ND2   1 
ATOM   671  N  N     . VAL A 1 93  ? 16.235  -2.088  25.265  1.00 28.19  ? 91  VAL A N     1 
ATOM   672  C  CA    . VAL A 1 93  ? 16.524  -0.668  25.198  1.00 30.90  ? 91  VAL A CA    1 
ATOM   673  C  C     . VAL A 1 93  ? 17.823  -0.468  25.955  1.00 33.52  ? 91  VAL A C     1 
ATOM   674  O  O     . VAL A 1 93  ? 18.071  -1.177  26.931  1.00 36.05  ? 91  VAL A O     1 
ATOM   675  C  CB    . VAL A 1 93  ? 15.390  0.200   25.785  1.00 33.31  ? 91  VAL A CB    1 
ATOM   676  C  CG1   . VAL A 1 93  ? 15.032  -0.205  27.199  1.00 35.45  ? 91  VAL A CG1   1 
ATOM   677  C  CG2   . VAL A 1 93  ? 15.749  1.677   25.768  1.00 35.66  ? 91  VAL A CG2   1 
ATOM   678  N  N     . PHE A 1 94  ? 18.675  0.433   25.467  1.00 34.47  ? 92  PHE A N     1 
ATOM   679  C  CA    . PHE A 1 94  ? 19.923  0.712   26.160  1.00 36.45  ? 92  PHE A CA    1 
ATOM   680  C  C     . PHE A 1 94  ? 20.459  2.085   25.781  1.00 38.85  ? 92  PHE A C     1 
ATOM   681  O  O     . PHE A 1 94  ? 20.080  2.679   24.769  1.00 38.63  ? 92  PHE A O     1 
ATOM   682  C  CB    . PHE A 1 94  ? 20.954  -0.363  25.823  1.00 35.29  ? 92  PHE A CB    1 
ATOM   683  C  CG    . PHE A 1 94  ? 21.325  -0.452  24.365  1.00 36.36  ? 92  PHE A CG    1 
ATOM   684  C  CD1   . PHE A 1 94  ? 22.351  0.309   23.848  1.00 36.45  ? 92  PHE A CD1   1 
ATOM   685  C  CD2   . PHE A 1 94  ? 20.661  -1.320  23.515  1.00 36.66  ? 92  PHE A CD2   1 
ATOM   686  C  CE1   . PHE A 1 94  ? 22.714  0.215   22.516  1.00 36.11  ? 92  PHE A CE1   1 
ATOM   687  C  CE2   . PHE A 1 94  ? 21.025  -1.421  22.179  1.00 36.22  ? 92  PHE A CE2   1 
ATOM   688  C  CZ    . PHE A 1 94  ? 22.048  -0.647  21.683  1.00 35.65  ? 92  PHE A CZ    1 
ATOM   689  N  N     . THR A 1 95  ? 21.371  2.571   26.620  1.00 43.77  ? 93  THR A N     1 
ATOM   690  C  CA    . THR A 1 95  ? 22.200  3.714   26.287  1.00 45.35  ? 93  THR A CA    1 
ATOM   691  C  C     . THR A 1 95  ? 23.667  3.299   26.355  1.00 47.32  ? 93  THR A C     1 
ATOM   692  O  O     . THR A 1 95  ? 24.059  2.604   27.284  1.00 43.63  ? 93  THR A O     1 
ATOM   693  C  CB    . THR A 1 95  ? 21.944  4.886   27.233  1.00 47.11  ? 93  THR A CB    1 
ATOM   694  O  OG1   . THR A 1 95  ? 22.916  5.894   26.927  1.00 50.03  ? 93  THR A OG1   1 
ATOM   695  C  CG2   . THR A 1 95  ? 22.029  4.496   28.692  1.00 44.93  ? 93  THR A CG2   1 
ATOM   696  N  N     . PRO A 1 96  ? 24.517  3.711   25.385  1.00 50.77  ? 94  PRO A N     1 
ATOM   697  C  CA    . PRO A 1 96  ? 25.944  3.409   25.442  1.00 52.30  ? 94  PRO A CA    1 
ATOM   698  C  C     . PRO A 1 96  ? 26.654  4.235   26.508  1.00 57.18  ? 94  PRO A C     1 
ATOM   699  O  O     . PRO A 1 96  ? 27.665  3.791   27.032  1.00 61.86  ? 94  PRO A O     1 
ATOM   700  C  CB    . PRO A 1 96  ? 26.479  3.757   24.046  1.00 54.59  ? 94  PRO A CB    1 
ATOM   701  C  CG    . PRO A 1 96  ? 25.235  4.017   23.196  1.00 56.61  ? 94  PRO A CG    1 
ATOM   702  C  CD    . PRO A 1 96  ? 24.156  4.453   24.163  1.00 55.52  ? 94  PRO A CD    1 
ATOM   703  N  N     . GLN A 1 97  ? 26.125  5.425   26.832  1.00 54.40  ? 95  GLN A N     1 
ATOM   704  C  CA    . GLN A 1 97  ? 26.738  6.270   27.851  1.00 57.68  ? 95  GLN A CA    1 
ATOM   705  C  C     . GLN A 1 97  ? 26.477  5.680   29.238  1.00 56.28  ? 95  GLN A C     1 
ATOM   706  O  O     . GLN A 1 97  ? 25.463  5.029   29.452  1.00 56.64  ? 95  GLN A O     1 
ATOM   707  C  CB    . GLN A 1 97  ? 26.228  7.704   27.715  1.00 57.05  ? 95  GLN A CB    1 
ATOM   708  C  CG    . GLN A 1 97  ? 26.581  8.338   26.374  1.00 57.71  ? 95  GLN A CG    1 
ATOM   709  C  CD    . GLN A 1 97  ? 25.513  8.147   25.322  1.00 54.83  ? 95  GLN A CD    1 
ATOM   710  O  OE1   . GLN A 1 97  ? 24.319  8.156   25.606  1.00 57.05  ? 95  GLN A OE1   1 
ATOM   711  N  NE2   . GLN A 1 97  ? 25.934  7.966   24.083  1.00 52.89  ? 95  GLN A NE2   1 
ATOM   712  N  N     . LYS A 1 98  ? 27.407  5.899   30.175  1.00 61.62  ? 96  LYS A N     1 
ATOM   713  C  CA    . LYS A 1 98  ? 27.434  5.149   31.427  1.00 61.62  ? 96  LYS A CA    1 
ATOM   714  C  C     . LYS A 1 98  ? 26.892  5.956   32.607  1.00 64.24  ? 96  LYS A C     1 
ATOM   715  O  O     . LYS A 1 98  ? 26.668  5.384   33.679  1.00 60.58  ? 96  LYS A O     1 
ATOM   716  C  CB    . LYS A 1 98  ? 28.866  4.687   31.736  1.00 62.63  ? 96  LYS A CB    1 
ATOM   717  N  N     . SER A 1 99  ? 26.682  7.265   32.417  1.00 67.45  ? 97  SER A N     1 
ATOM   718  C  CA    . SER A 1 99  ? 26.229  8.146   33.486  1.00 65.11  ? 97  SER A CA    1 
ATOM   719  C  C     . SER A 1 99  ? 25.092  9.060   33.014  1.00 63.60  ? 97  SER A C     1 
ATOM   720  O  O     . SER A 1 99  ? 24.915  9.338   31.774  1.00 65.81  ? 97  SER A O     1 
ATOM   721  C  CB    . SER A 1 99  ? 27.377  8.966   34.038  1.00 65.95  ? 97  SER A CB    1 
ATOM   722  O  OG    . SER A 1 99  ? 27.922  9.808   33.031  1.00 65.59  ? 97  SER A OG    1 
ATOM   723  N  N     . LEU A 1 100 ? 24.330  9.558   34.011  1.00 61.19  ? 98  LEU A N     1 
ATOM   724  C  CA    . LEU A 1 100 ? 23.359  10.607  33.727  1.00 60.35  ? 98  LEU A CA    1 
ATOM   725  C  C     . LEU A 1 100 ? 24.072  11.804  33.100  1.00 58.55  ? 98  LEU A C     1 
ATOM   726  O  O     . LEU A 1 100 ? 23.593  12.341  32.110  1.00 61.72  ? 98  LEU A O     1 
ATOM   727  C  CB    . LEU A 1 100 ? 22.628  11.010  35.009  1.00 57.12  ? 98  LEU A CB    1 
ATOM   728  C  CG    . LEU A 1 100 ? 21.595  12.129  34.857  1.00 56.06  ? 98  LEU A CG    1 
ATOM   729  C  CD1   . LEU A 1 100 ? 20.588  11.856  33.740  1.00 54.79  ? 98  LEU A CD1   1 
ATOM   730  C  CD2   . LEU A 1 100 ? 20.854  12.341  36.165  1.00 56.98  ? 98  LEU A CD2   1 
ATOM   731  N  N     . GLU A 1 101 ? 25.242  12.176  33.632  1.00 63.14  ? 99  GLU A N     1 
ATOM   732  C  CA    . GLU A 1 101 ? 25.959  13.347  33.143  1.00 64.88  ? 99  GLU A CA    1 
ATOM   733  C  C     . GLU A 1 101 ? 26.320  13.168  31.667  1.00 64.84  ? 99  GLU A C     1 
ATOM   734  O  O     . GLU A 1 101 ? 26.182  14.110  30.887  1.00 69.84  ? 99  GLU A O     1 
ATOM   735  C  CB    . GLU A 1 101 ? 27.233  13.632  33.948  1.00 73.70  ? 99  GLU A CB    1 
ATOM   736  C  CG    . GLU A 1 101 ? 27.059  13.563  35.460  1.00 81.33  ? 99  GLU A CG    1 
ATOM   737  C  CD    . GLU A 1 101 ? 27.300  12.190  36.079  1.00 92.53  ? 99  GLU A CD    1 
ATOM   738  O  OE1   . GLU A 1 101 ? 28.495  11.831  36.315  1.00 91.65  ? 99  GLU A OE1   1 
ATOM   739  O  OE2   . GLU A 1 101 ? 26.292  11.472  36.317  1.00 96.92  ? 99  GLU A OE2   1 
ATOM   740  N  N     . GLU A 1 102 ? 26.789  11.963  31.293  1.00 64.38  ? 100 GLU A N     1 
ATOM   741  C  CA    . GLU A 1 102 ? 27.248  11.703  29.935  1.00 64.35  ? 100 GLU A CA    1 
ATOM   742  C  C     . GLU A 1 102 ? 26.114  11.286  28.998  1.00 56.18  ? 100 GLU A C     1 
ATOM   743  O  O     . GLU A 1 102 ? 26.325  11.220  27.786  1.00 54.29  ? 100 GLU A O     1 
ATOM   744  C  CB    . GLU A 1 102 ? 28.272  10.573  29.922  1.00 71.90  ? 100 GLU A CB    1 
ATOM   745  C  CG    . GLU A 1 102 ? 29.647  10.974  30.406  1.00 75.12  ? 100 GLU A CG    1 
ATOM   746  C  CD    . GLU A 1 102 ? 30.676  9.913   30.067  1.00 80.04  ? 100 GLU A CD    1 
ATOM   747  O  OE1   . GLU A 1 102 ? 30.543  8.757   30.585  1.00 82.82  ? 100 GLU A OE1   1 
ATOM   748  O  OE2   . GLU A 1 102 ? 31.583  10.222  29.264  1.00 83.28  ? 100 GLU A OE2   1 
ATOM   749  N  N     . PHE A 1 103 ? 24.933  10.983  29.547  1.00 54.12  ? 101 PHE A N     1 
ATOM   750  C  CA    . PHE A 1 103 ? 23.834  10.412  28.771  1.00 49.27  ? 101 PHE A CA    1 
ATOM   751  C  C     . PHE A 1 103 ? 23.504  11.292  27.564  1.00 46.83  ? 101 PHE A C     1 
ATOM   752  O  O     . PHE A 1 103 ? 23.327  12.500  27.709  1.00 49.11  ? 101 PHE A O     1 
ATOM   753  C  CB    . PHE A 1 103 ? 22.632  10.234  29.698  1.00 50.15  ? 101 PHE A CB    1 
ATOM   754  C  CG    . PHE A 1 103 ? 21.352  9.808   29.030  1.00 47.94  ? 101 PHE A CG    1 
ATOM   755  C  CD1   . PHE A 1 103 ? 21.304  8.676   28.241  1.00 47.42  ? 101 PHE A CD1   1 
ATOM   756  C  CD2   . PHE A 1 103 ? 20.177  10.513  29.233  1.00 43.88  ? 101 PHE A CD2   1 
ATOM   757  C  CE1   . PHE A 1 103 ? 20.116  8.275   27.655  1.00 44.54  ? 101 PHE A CE1   1 
ATOM   758  C  CE2   . PHE A 1 103 ? 18.997  10.116  28.623  1.00 45.50  ? 101 PHE A CE2   1 
ATOM   759  C  CZ    . PHE A 1 103 ? 18.973  8.991   27.843  1.00 44.43  ? 101 PHE A CZ    1 
ATOM   760  N  N     . GLN A 1 104 ? 23.463  10.689  26.376  1.00 46.74  ? 102 GLN A N     1 
ATOM   761  C  CA    . GLN A 1 104 ? 23.132  11.379  25.138  1.00 51.89  ? 102 GLN A CA    1 
ATOM   762  C  C     . GLN A 1 104 ? 22.026  10.644  24.382  1.00 51.41  ? 102 GLN A C     1 
ATOM   763  O  O     . GLN A 1 104 ? 21.004  11.241  24.046  1.00 48.31  ? 102 GLN A O     1 
ATOM   764  C  CB    . GLN A 1 104 ? 24.335  11.477  24.198  1.00 53.57  ? 102 GLN A CB    1 
ATOM   765  C  CG    . GLN A 1 104 ? 25.608  11.946  24.877  1.00 60.00  ? 102 GLN A CG    1 
ATOM   766  C  CD    . GLN A 1 104 ? 25.692  13.442  24.970  1.00 64.12  ? 102 GLN A CD    1 
ATOM   767  O  OE1   . GLN A 1 104 ? 25.119  14.169  24.160  1.00 64.60  ? 102 GLN A OE1   1 
ATOM   768  N  NE2   . GLN A 1 104 ? 26.434  13.911  25.958  1.00 72.24  ? 102 GLN A NE2   1 
ATOM   769  N  N     . ASP A 1 105 ? 22.249  9.350   24.095  1.00 49.73  ? 103 ASP A N     1 
ATOM   770  C  CA    . ASP A 1 105 ? 21.462  8.638   23.101  1.00 47.34  ? 103 ASP A CA    1 
ATOM   771  C  C     . ASP A 1 105 ? 20.766  7.415   23.706  1.00 43.60  ? 103 ASP A C     1 
ATOM   772  O  O     . ASP A 1 105 ? 21.282  6.763   24.609  1.00 43.67  ? 103 ASP A O     1 
ATOM   773  C  CB    . ASP A 1 105 ? 22.340  8.231   21.913  1.00 49.68  ? 103 ASP A CB    1 
ATOM   774  C  CG    . ASP A 1 105 ? 23.204  9.357   21.372  1.00 49.62  ? 103 ASP A CG    1 
ATOM   775  O  OD1   . ASP A 1 105 ? 22.628  10.323  20.854  1.00 50.41  ? 103 ASP A OD1   1 
ATOM   776  O  OD2   . ASP A 1 105 ? 24.440  9.263   21.486  1.00 49.98  ? 103 ASP A OD2   1 
ATOM   777  N  N     . VAL A 1 106 ? 19.580  7.125   23.166  1.00 39.50  ? 104 VAL A N     1 
ATOM   778  C  CA    . VAL A 1 106 ? 18.781  5.956   23.513  1.00 39.37  ? 104 VAL A CA    1 
ATOM   779  C  C     . VAL A 1 106 ? 18.642  5.091   22.267  1.00 37.23  ? 104 VAL A C     1 
ATOM   780  O  O     . VAL A 1 106 ? 18.327  5.610   21.194  1.00 38.47  ? 104 VAL A O     1 
ATOM   781  C  CB    . VAL A 1 106 ? 17.394  6.384   24.033  1.00 38.81  ? 104 VAL A CB    1 
ATOM   782  C  CG1   . VAL A 1 106 ? 16.500  5.211   24.384  1.00 39.54  ? 104 VAL A CG1   1 
ATOM   783  C  CG2   . VAL A 1 106 ? 17.536  7.292   25.235  1.00 39.91  ? 104 VAL A CG2   1 
ATOM   784  N  N     . TYR A 1 107 ? 18.809  3.770   22.438  1.00 35.98  ? 105 TYR A N     1 
ATOM   785  C  CA    . TYR A 1 107 ? 18.630  2.807   21.365  1.00 34.92  ? 105 TYR A CA    1 
ATOM   786  C  C     . TYR A 1 107 ? 17.462  1.892   21.717  1.00 35.67  ? 105 TYR A C     1 
ATOM   787  O  O     . TYR A 1 107 ? 17.463  1.267   22.779  1.00 37.18  ? 105 TYR A O     1 
ATOM   788  C  CB    . TYR A 1 107 ? 19.921  2.029   21.108  1.00 36.61  ? 105 TYR A CB    1 
ATOM   789  C  CG    . TYR A 1 107 ? 21.072  2.863   20.553  1.00 41.52  ? 105 TYR A CG    1 
ATOM   790  C  CD1   . TYR A 1 107 ? 21.808  3.722   21.367  1.00 48.57  ? 105 TYR A CD1   1 
ATOM   791  C  CD2   . TYR A 1 107 ? 21.444  2.783   19.218  1.00 45.07  ? 105 TYR A CD2   1 
ATOM   792  C  CE1   . TYR A 1 107 ? 22.869  4.477   20.875  1.00 46.55  ? 105 TYR A CE1   1 
ATOM   793  C  CE2   . TYR A 1 107 ? 22.505  3.527   18.715  1.00 46.83  ? 105 TYR A CE2   1 
ATOM   794  C  CZ    . TYR A 1 107 ? 23.218  4.382   19.540  1.00 49.35  ? 105 TYR A CZ    1 
ATOM   795  O  OH    . TYR A 1 107 ? 24.270  5.116   19.043  1.00 53.78  ? 105 TYR A OH    1 
ATOM   796  N  N     . ILE A 1 108 ? 16.474  1.862   20.811  1.00 33.33  ? 106 ILE A N     1 
ATOM   797  C  CA    . ILE A 1 108 ? 15.268  1.055   20.896  1.00 34.95  ? 106 ILE A CA    1 
ATOM   798  C  C     . ILE A 1 108 ? 15.461  -0.158  19.997  1.00 33.34  ? 106 ILE A C     1 
ATOM   799  O  O     . ILE A 1 108 ? 15.753  -0.011  18.821  1.00 33.90  ? 106 ILE A O     1 
ATOM   800  C  CB    . ILE A 1 108 ? 14.029  1.871   20.454  1.00 36.79  ? 106 ILE A CB    1 
ATOM   801  C  CG1   . ILE A 1 108 ? 13.821  3.083   21.352  1.00 43.28  ? 106 ILE A CG1   1 
ATOM   802  C  CG2   . ILE A 1 108 ? 12.755  1.051   20.402  1.00 35.12  ? 106 ILE A CG2   1 
ATOM   803  C  CD1   . ILE A 1 108 ? 13.877  2.755   22.809  1.00 47.23  ? 106 ILE A CD1   1 
ATOM   804  N  N     . VAL A 1 109 ? 15.265  -1.354  20.557  1.00 33.28  ? 107 VAL A N     1 
ATOM   805  C  CA    . VAL A 1 109 ? 15.362  -2.579  19.781  1.00 31.67  ? 107 VAL A CA    1 
ATOM   806  C  C     . VAL A 1 109 ? 13.976  -3.193  19.665  1.00 32.06  ? 107 VAL A C     1 
ATOM   807  O  O     . VAL A 1 109 ? 13.323  -3.462  20.666  1.00 29.47  ? 107 VAL A O     1 
ATOM   808  C  CB    . VAL A 1 109 ? 16.356  -3.574  20.397  1.00 29.81  ? 107 VAL A CB    1 
ATOM   809  C  CG1   . VAL A 1 109 ? 16.604  -4.761  19.485  1.00 28.90  ? 107 VAL A CG1   1 
ATOM   810  C  CG2   . VAL A 1 109 ? 17.661  -2.898  20.768  1.00 30.13  ? 107 VAL A CG2   1 
ATOM   811  N  N     . MET A 1 110 ? 13.550  -3.421  18.422  1.00 30.71  ? 108 MET A N     1 
ATOM   812  C  CA    . MET A 1 110 ? 12.244  -3.987  18.151  1.00 30.71  ? 108 MET A CA    1 
ATOM   813  C  C     . MET A 1 110 ? 12.419  -5.217  17.273  1.00 30.33  ? 108 MET A C     1 
ATOM   814  O  O     . MET A 1 110 ? 13.467  -5.418  16.683  1.00 29.85  ? 108 MET A O     1 
ATOM   815  C  CB    . MET A 1 110 ? 11.375  -2.975  17.408  1.00 32.85  ? 108 MET A CB    1 
ATOM   816  C  CG    . MET A 1 110 ? 11.108  -1.705  18.164  1.00 32.81  ? 108 MET A CG    1 
ATOM   817  S  SD    . MET A 1 110 ? 10.696  -0.449  16.925  1.00 33.68  ? 108 MET A SD    1 
ATOM   818  C  CE    . MET A 1 110 ? 12.355  -0.106  16.331  1.00 35.56  ? 108 MET A CE    1 
ATOM   819  N  N     . GLU A 1 111 ? 11.370  -6.038  17.198  1.00 31.21  ? 109 GLU A N     1 
ATOM   820  C  CA    . GLU A 1 111 ? 11.268  -7.071  16.184  1.00 36.53  ? 109 GLU A CA    1 
ATOM   821  C  C     . GLU A 1 111 ? 11.378  -6.440  14.798  1.00 32.22  ? 109 GLU A C     1 
ATOM   822  O  O     . GLU A 1 111 ? 10.800  -5.388  14.558  1.00 32.59  ? 109 GLU A O     1 
ATOM   823  C  CB    . GLU A 1 111 ? 9.914   -7.765  16.324  1.00 39.23  ? 109 GLU A CB    1 
ATOM   824  C  CG    . GLU A 1 111 ? 9.724   -8.946  15.409  1.00 48.72  ? 109 GLU A CG    1 
ATOM   825  C  CD    . GLU A 1 111 ? 8.378   -9.624  15.620  1.00 54.79  ? 109 GLU A CD    1 
ATOM   826  O  OE1   . GLU A 1 111 ? 7.551   -9.091  16.421  1.00 53.53  ? 109 GLU A OE1   1 
ATOM   827  O  OE2   . GLU A 1 111 ? 8.162   -10.678 14.999  1.00 55.61  ? 109 GLU A OE2   1 
ATOM   828  N  N     . LEU A 1 112 ? 12.133  -7.085  13.910  1.00 32.08  ? 110 LEU A N     1 
ATOM   829  C  CA    . LEU A 1 112 ? 12.245  -6.634  12.536  1.00 31.63  ? 110 LEU A CA    1 
ATOM   830  C  C     . LEU A 1 112 ? 11.103  -7.245  11.731  1.00 33.04  ? 110 LEU A C     1 
ATOM   831  O  O     . LEU A 1 112 ? 11.062  -8.448  11.489  1.00 33.02  ? 110 LEU A O     1 
ATOM   832  C  CB    . LEU A 1 112 ? 13.599  -7.025  11.953  1.00 33.47  ? 110 LEU A CB    1 
ATOM   833  C  CG    . LEU A 1 112 ? 13.812  -6.552  10.517  1.00 36.31  ? 110 LEU A CG    1 
ATOM   834  C  CD1   . LEU A 1 112 ? 13.802  -5.042  10.496  1.00 37.54  ? 110 LEU A CD1   1 
ATOM   835  C  CD2   . LEU A 1 112 ? 15.118  -7.075  9.926   1.00 38.39  ? 110 LEU A CD2   1 
ATOM   836  N  N     . MET A 1 113 ? 10.156  -6.414  11.326  1.00 34.08  ? 111 MET A N     1 
ATOM   837  C  CA    . MET A 1 113 ? 9.029   -6.880  10.535  1.00 33.48  ? 111 MET A CA    1 
ATOM   838  C  C     . MET A 1 113 ? 9.454   -6.951  9.071   1.00 34.90  ? 111 MET A C     1 
ATOM   839  O  O     . MET A 1 113 ? 10.511  -6.451  8.715   1.00 36.43  ? 111 MET A O     1 
ATOM   840  C  CB    . MET A 1 113 ? 7.874   -5.913  10.770  1.00 31.82  ? 111 MET A CB    1 
ATOM   841  C  CG    . MET A 1 113 ? 7.526   -5.875  12.266  1.00 36.22  ? 111 MET A CG    1 
ATOM   842  S  SD    . MET A 1 113 ? 6.781   -7.411  12.836  1.00 41.65  ? 111 MET A SD    1 
ATOM   843  C  CE    . MET A 1 113 ? 5.142   -7.194  12.143  1.00 40.94  ? 111 MET A CE    1 
ATOM   844  N  N     . ASP A 1 114 ? 8.652   -7.596  8.220   1.00 35.63  ? 112 ASP A N     1 
ATOM   845  C  CA    . ASP A 1 114 ? 9.093   -7.881  6.863   1.00 35.76  ? 112 ASP A CA    1 
ATOM   846  C  C     . ASP A 1 114 ? 8.683   -6.779  5.873   1.00 35.57  ? 112 ASP A C     1 
ATOM   847  O  O     . ASP A 1 114 ? 9.248   -6.697  4.795   1.00 35.22  ? 112 ASP A O     1 
ATOM   848  C  CB    . ASP A 1 114 ? 8.591   -9.264  6.442   1.00 39.05  ? 112 ASP A CB    1 
ATOM   849  C  CG    . ASP A 1 114 ? 9.112   -10.353 7.373   1.00 43.53  ? 112 ASP A CG    1 
ATOM   850  O  OD1   . ASP A 1 114 ? 10.335  -10.463 7.484   1.00 45.55  ? 112 ASP A OD1   1 
ATOM   851  O  OD2   . ASP A 1 114 ? 8.295   -11.039 8.034   1.00 42.01  ? 112 ASP A OD2   1 
ATOM   852  N  N     . ALA A 1 115 ? 7.710   -5.933  6.193   1.00 32.44  ? 113 ALA A N     1 
ATOM   853  C  CA    . ALA A 1 115 ? 7.251   -4.947  5.223   1.00 33.57  ? 113 ALA A CA    1 
ATOM   854  C  C     . ALA A 1 115 ? 6.530   -3.838  5.964   1.00 32.75  ? 113 ALA A C     1 
ATOM   855  O  O     . ALA A 1 115 ? 6.059   -4.071  7.069   1.00 33.02  ? 113 ALA A O     1 
ATOM   856  C  CB    . ALA A 1 115 ? 6.341   -5.608  4.213   1.00 32.50  ? 113 ALA A CB    1 
ATOM   857  N  N     . ASN A 1 116 ? 6.458   -2.637  5.391   1.00 30.50  ? 114 ASN A N     1 
ATOM   858  C  CA    . ASN A 1 116 ? 5.500   -1.680  5.910   1.00 32.73  ? 114 ASN A CA    1 
ATOM   859  C  C     . ASN A 1 116 ? 4.236   -1.788  5.062   1.00 32.90  ? 114 ASN A C     1 
ATOM   860  O  O     . ASN A 1 116 ? 4.241   -2.437  4.019   1.00 31.89  ? 114 ASN A O     1 
ATOM   861  C  CB    . ASN A 1 116 ? 6.037   -0.251  6.018   1.00 32.89  ? 114 ASN A CB    1 
ATOM   862  C  CG    . ASN A 1 116 ? 6.346   0.390   4.694   1.00 37.51  ? 114 ASN A CG    1 
ATOM   863  O  OD1   . ASN A 1 116 ? 5.651   0.175   3.705   1.00 36.58  ? 114 ASN A OD1   1 
ATOM   864  N  ND2   . ASN A 1 116 ? 7.429   1.143   4.661   1.00 41.77  ? 114 ASN A ND2   1 
ATOM   865  N  N     . LEU A 1 117 ? 3.163   -1.141  5.525   1.00 32.06  ? 115 LEU A N     1 
ATOM   866  C  CA    . LEU A 1 117 ? 1.867   -1.276  4.889   1.00 31.20  ? 115 LEU A CA    1 
ATOM   867  C  C     . LEU A 1 117 ? 1.845   -0.605  3.522   1.00 31.95  ? 115 LEU A C     1 
ATOM   868  O  O     . LEU A 1 117 ? 1.067   -1.016  2.667   1.00 34.48  ? 115 LEU A O     1 
ATOM   869  C  CB    . LEU A 1 117 ? 0.798   -0.719  5.830   1.00 28.38  ? 115 LEU A CB    1 
ATOM   870  C  CG    . LEU A 1 117 ? -0.658  -0.963  5.447   1.00 27.86  ? 115 LEU A CG    1 
ATOM   871  C  CD1   . LEU A 1 117 ? -0.961  -2.462  5.348   1.00 28.44  ? 115 LEU A CD1   1 
ATOM   872  C  CD2   . LEU A 1 117 ? -1.544  -0.332  6.493   1.00 27.00  ? 115 LEU A CD2   1 
ATOM   873  N  N     . CYS A 1 118 ? 2.718   0.382   3.286   1.00 33.90  ? 116 CYS A N     1 
ATOM   874  C  CA    . CYS A 1 118 ? 2.830   0.987   1.967   1.00 36.96  ? 116 CYS A CA    1 
ATOM   875  C  C     . CYS A 1 118 ? 3.126   -0.112  0.942   1.00 35.13  ? 116 CYS A C     1 
ATOM   876  O  O     . CYS A 1 118 ? 2.485   -0.195  -0.103  1.00 34.57  ? 116 CYS A O     1 
ATOM   877  C  CB    . CYS A 1 118 ? 3.924   2.057   1.911   1.00 37.98  ? 116 CYS A CB    1 
ATOM   878  S  SG    . CYS A 1 118 ? 3.714   3.419   3.102   1.00 37.17  ? 116 CYS A SG    1 
ATOM   879  N  N     . GLN A 1 119 ? 4.098   -0.973  1.258   1.00 35.55  ? 117 GLN A N     1 
ATOM   880  C  CA    . GLN A 1 119 ? 4.485   -2.067  0.372   1.00 38.31  ? 117 GLN A CA    1 
ATOM   881  C  C     . GLN A 1 119 ? 3.342   -3.071  0.226   1.00 39.67  ? 117 GLN A C     1 
ATOM   882  O  O     . GLN A 1 119 ? 3.083   -3.542  -0.879  1.00 42.38  ? 117 GLN A O     1 
ATOM   883  C  CB    . GLN A 1 119 ? 5.738   -2.778  0.897   1.00 41.15  ? 117 GLN A CB    1 
ATOM   884  C  CG    . GLN A 1 119 ? 6.973   -1.883  1.019   1.00 42.55  ? 117 GLN A CG    1 
ATOM   885  C  CD    . GLN A 1 119 ? 8.081   -2.562  1.798   1.00 45.16  ? 117 GLN A CD    1 
ATOM   886  O  OE1   . GLN A 1 119 ? 8.076   -2.615  3.025   1.00 42.40  ? 117 GLN A OE1   1 
ATOM   887  N  NE2   . GLN A 1 119 ? 9.060   -3.089  1.085   1.00 48.85  ? 117 GLN A NE2   1 
ATOM   888  N  N     . VAL A 1 120 ? 2.663   -3.397  1.339   1.00 36.81  ? 118 VAL A N     1 
ATOM   889  C  CA    . VAL A 1 120 ? 1.559   -4.343  1.303   1.00 38.29  ? 118 VAL A CA    1 
ATOM   890  C  C     . VAL A 1 120 ? 0.421   -3.777  0.447   1.00 38.51  ? 118 VAL A C     1 
ATOM   891  O  O     . VAL A 1 120 ? -0.182  -4.521  -0.306  1.00 42.74  ? 118 VAL A O     1 
ATOM   892  C  CB    . VAL A 1 120 ? 1.105   -4.741  2.726   1.00 36.08  ? 118 VAL A CB    1 
ATOM   893  C  CG1   . VAL A 1 120 ? -0.151  -5.581  2.723   1.00 38.93  ? 118 VAL A CG1   1 
ATOM   894  C  CG2   . VAL A 1 120 ? 2.200   -5.468  3.481   1.00 35.74  ? 118 VAL A CG2   1 
ATOM   895  N  N     . ILE A 1 121 ? 0.130   -2.466  0.548   1.00 42.38  ? 119 ILE A N     1 
ATOM   896  C  CA    . ILE A 1 121 ? -0.864  -1.802  -0.298  1.00 40.15  ? 119 ILE A CA    1 
ATOM   897  C  C     . ILE A 1 121 ? -0.613  -2.038  -1.791  1.00 40.43  ? 119 ILE A C     1 
ATOM   898  O  O     . ILE A 1 121 ? -1.567  -2.084  -2.561  1.00 41.45  ? 119 ILE A O     1 
ATOM   899  C  CB    . ILE A 1 121 ? -0.961  -0.290  0.030   1.00 38.54  ? 119 ILE A CB    1 
ATOM   900  C  CG1   . ILE A 1 121 ? -1.874  -0.071  1.230   1.00 37.35  ? 119 ILE A CG1   1 
ATOM   901  C  CG2   . ILE A 1 121 ? -1.465  0.536   -1.146  1.00 43.66  ? 119 ILE A CG2   1 
ATOM   902  C  CD1   . ILE A 1 121 ? -1.785  1.300   1.842   1.00 39.73  ? 119 ILE A CD1   1 
ATOM   903  N  N     . GLN A 1 122 ? 0.650   -2.147  -2.226  1.00 40.31  ? 120 GLN A N     1 
ATOM   904  C  CA    . GLN A 1 122 ? 0.941   -2.258  -3.648  1.00 44.99  ? 120 GLN A CA    1 
ATOM   905  C  C     . GLN A 1 122 ? 0.429   -3.577  -4.236  1.00 47.78  ? 120 GLN A C     1 
ATOM   906  O  O     . GLN A 1 122 ? 0.149   -3.644  -5.425  1.00 49.76  ? 120 GLN A O     1 
ATOM   907  C  CB    . GLN A 1 122 ? 2.436   -2.089  -3.907  1.00 47.22  ? 120 GLN A CB    1 
ATOM   908  C  CG    . GLN A 1 122 ? 2.911   -0.674  -3.617  1.00 52.54  ? 120 GLN A CG    1 
ATOM   909  C  CD    . GLN A 1 122 ? 4.405   -0.524  -3.762  1.00 61.91  ? 120 GLN A CD    1 
ATOM   910  O  OE1   . GLN A 1 122 ? 5.093   -1.382  -4.315  1.00 64.69  ? 120 GLN A OE1   1 
ATOM   911  N  NE2   . GLN A 1 122 ? 4.919   0.586   -3.257  1.00 70.01  ? 120 GLN A NE2   1 
ATOM   912  N  N     . MET A 1 123 ? 0.258   -4.611  -3.410  1.00 48.60  ? 121 MET A N     1 
ATOM   913  C  CA    . MET A 1 123 ? -0.203  -5.902  -3.900  1.00 51.33  ? 121 MET A CA    1 
ATOM   914  C  C     . MET A 1 123 ? -1.705  -5.870  -4.175  1.00 49.17  ? 121 MET A C     1 
ATOM   915  O  O     . MET A 1 123 ? -2.434  -5.106  -3.561  1.00 45.81  ? 121 MET A O     1 
ATOM   916  C  CB    . MET A 1 123 ? 0.085   -6.999  -2.873  1.00 55.31  ? 121 MET A CB    1 
ATOM   917  C  CG    . MET A 1 123 ? 1.283   -6.711  -1.966  1.00 57.00  ? 121 MET A CG    1 
ATOM   918  S  SD    . MET A 1 123 ? 1.324   -7.800  -0.519  1.00 59.33  ? 121 MET A SD    1 
ATOM   919  C  CE    . MET A 1 123 ? 2.953   -7.455  0.148   1.00 42.74  ? 121 MET A CE    1 
ATOM   920  N  N     . GLU A 1 124 ? -2.174  -6.744  -5.077  1.00 54.18  ? 122 GLU A N     1 
ATOM   921  C  CA    . GLU A 1 124 ? -3.606  -6.947  -5.257  1.00 55.02  ? 122 GLU A CA    1 
ATOM   922  C  C     . GLU A 1 124 ? -4.086  -7.803  -4.084  1.00 56.30  ? 122 GLU A C     1 
ATOM   923  O  O     . GLU A 1 124 ? -3.600  -8.917  -3.888  1.00 65.85  ? 122 GLU A O     1 
ATOM   924  C  CB    . GLU A 1 124 ? -3.942  -7.549  -6.629  1.00 57.00  ? 122 GLU A CB    1 
ATOM   925  N  N     . LEU A 1 125 ? -5.000  -7.242  -3.282  1.00 48.82  ? 123 LEU A N     1 
ATOM   926  C  CA    . LEU A 1 125 ? -5.460  -7.847  -2.040  1.00 49.95  ? 123 LEU A CA    1 
ATOM   927  C  C     . LEU A 1 125 ? -6.934  -8.200  -2.203  1.00 47.51  ? 123 LEU A C     1 
ATOM   928  O  O     . LEU A 1 125 ? -7.751  -7.323  -2.500  1.00 44.71  ? 123 LEU A O     1 
ATOM   929  C  CB    . LEU A 1 125 ? -5.324  -6.861  -0.871  1.00 47.63  ? 123 LEU A CB    1 
ATOM   930  C  CG    . LEU A 1 125 ? -3.928  -6.378  -0.472  1.00 51.85  ? 123 LEU A CG    1 
ATOM   931  C  CD1   . LEU A 1 125 ? -4.013  -5.281  0.597   1.00 51.58  ? 123 LEU A CD1   1 
ATOM   932  C  CD2   . LEU A 1 125 ? -3.080  -7.524  0.046   1.00 52.21  ? 123 LEU A CD2   1 
ATOM   933  N  N     . ASP A 1 126 ? -7.274  -9.471  -1.974  1.00 43.39  ? 124 ASP A N     1 
ATOM   934  C  CA    . ASP A 1 126 ? -8.670  -9.873  -1.999  1.00 44.48  ? 124 ASP A CA    1 
ATOM   935  C  C     . ASP A 1 126 ? -9.362  -9.326  -0.743  1.00 38.59  ? 124 ASP A C     1 
ATOM   936  O  O     . ASP A 1 126 ? -8.748  -8.691  0.113   1.00 37.43  ? 124 ASP A O     1 
ATOM   937  C  CB    . ASP A 1 126 ? -8.777  -11.387 -2.223  1.00 43.94  ? 124 ASP A CB    1 
ATOM   938  C  CG    . ASP A 1 126 ? -8.308  -12.228 -1.049  1.00 43.48  ? 124 ASP A CG    1 
ATOM   939  O  OD1   . ASP A 1 126 ? -7.932  -11.656 -0.043  1.00 44.90  ? 124 ASP A OD1   1 
ATOM   940  O  OD2   . ASP A 1 126 ? -8.345  -13.456 -1.151  1.00 47.57  ? 124 ASP A OD2   1 
ATOM   941  N  N     . HIS A 1 127 ? -10.664 -9.579  -0.627  1.00 35.78  ? 125 HIS A N     1 
ATOM   942  C  CA    . HIS A 1 127 ? -11.449 -9.089  0.488   1.00 33.13  ? 125 HIS A CA    1 
ATOM   943  C  C     . HIS A 1 127 ? -10.992 -9.673  1.820   1.00 29.93  ? 125 HIS A C     1 
ATOM   944  O  O     . HIS A 1 127 ? -11.111 -9.026  2.847   1.00 28.28  ? 125 HIS A O     1 
ATOM   945  C  CB    . HIS A 1 127 ? -12.920 -9.405  0.267   1.00 35.99  ? 125 HIS A CB    1 
ATOM   946  C  CG    . HIS A 1 127 ? -13.524 -8.568  -0.819  1.00 38.78  ? 125 HIS A CG    1 
ATOM   947  N  ND1   . HIS A 1 127 ? -13.822 -7.233  -0.642  1.00 38.78  ? 125 HIS A ND1   1 
ATOM   948  C  CD2   . HIS A 1 127 ? -13.924 -8.891  -2.056  1.00 39.75  ? 125 HIS A CD2   1 
ATOM   949  C  CE1   . HIS A 1 127 ? -14.368 -6.771  -1.758  1.00 40.10  ? 125 HIS A CE1   1 
ATOM   950  N  NE2   . HIS A 1 127 ? -14.440 -7.760  -2.634  1.00 40.51  ? 125 HIS A NE2   1 
ATOM   951  N  N     . GLU A 1 128 ? -10.528 -10.914 1.821   1.00 31.51  ? 126 GLU A N     1 
ATOM   952  C  CA    . GLU A 1 128 ? -10.172 -11.552 3.075   1.00 31.25  ? 126 GLU A CA    1 
ATOM   953  C  C     . GLU A 1 128 ? -8.916  -10.891 3.637   1.00 29.45  ? 126 GLU A C     1 
ATOM   954  O  O     . GLU A 1 128 ? -8.849  -10.628 4.831   1.00 29.25  ? 126 GLU A O     1 
ATOM   955  C  CB    . GLU A 1 128 ? -10.005 -13.066 2.896   1.00 32.95  ? 126 GLU A CB    1 
ATOM   956  C  CG    . GLU A 1 128 ? -11.317 -13.827 2.825   1.00 36.78  ? 126 GLU A CG    1 
ATOM   957  C  CD    . GLU A 1 128 ? -12.176 -13.494 1.613   1.00 43.42  ? 126 GLU A CD    1 
ATOM   958  O  OE1   . GLU A 1 128 ? -11.654 -13.636 0.494   1.00 43.32  ? 126 GLU A OE1   1 
ATOM   959  O  OE2   . GLU A 1 128 ? -13.355 -13.074 1.796   1.00 48.70  ? 126 GLU A OE2   1 
ATOM   960  N  N     . ARG A 1 129 ? -7.947  -10.582 2.765   1.00 30.51  ? 127 ARG A N     1 
ATOM   961  C  CA    . ARG A 1 129 ? -6.718  -9.938  3.187   1.00 30.47  ? 127 ARG A CA    1 
ATOM   962  C  C     . ARG A 1 129 ? -6.957  -8.493  3.603   1.00 28.58  ? 127 ARG A C     1 
ATOM   963  O  O     . ARG A 1 129 ? -6.425  -8.063  4.630   1.00 25.37  ? 127 ARG A O     1 
ATOM   964  C  CB    . ARG A 1 129 ? -5.667  -10.083 2.087   1.00 34.83  ? 127 ARG A CB    1 
ATOM   965  C  CG    . ARG A 1 129 ? -5.129  -11.503 2.030   1.00 38.00  ? 127 ARG A CG    1 
ATOM   966  C  CD    . ARG A 1 129 ? -4.602  -11.929 0.682   1.00 42.46  ? 127 ARG A CD    1 
ATOM   967  N  NE    . ARG A 1 129 ? -4.009  -13.252 0.772   1.00 44.54  ? 127 ARG A NE    1 
ATOM   968  C  CZ    . ARG A 1 129 ? -4.667  -14.409 0.715   1.00 47.64  ? 127 ARG A CZ    1 
ATOM   969  N  NH1   . ARG A 1 129 ? -5.960  -14.455 0.432   1.00 47.66  ? 127 ARG A NH1   1 
ATOM   970  N  NH2   . ARG A 1 129 ? -4.001  -15.535 0.905   1.00 49.12  ? 127 ARG A NH2   1 
ATOM   971  N  N     . MET A 1 130 ? -7.746  -7.738  2.829   1.00 27.48  ? 128 MET A N     1 
ATOM   972  C  CA    . MET A 1 130 ? -8.045  -6.362  3.211   1.00 27.14  ? 128 MET A CA    1 
ATOM   973  C  C     . MET A 1 130 ? -8.778  -6.322  4.554   1.00 23.92  ? 128 MET A C     1 
ATOM   974  O  O     . MET A 1 130 ? -8.397  -5.567  5.457   1.00 22.97  ? 128 MET A O     1 
ATOM   975  C  CB    . MET A 1 130 ? -8.884  -5.658  2.135   1.00 30.95  ? 128 MET A CB    1 
ATOM   976  C  CG    . MET A 1 130 ? -8.126  -5.483  0.811   1.00 34.32  ? 128 MET A CG    1 
ATOM   977  S  SD    . MET A 1 130 ? -8.873  -4.318  -0.348  1.00 40.39  ? 128 MET A SD    1 
ATOM   978  C  CE    . MET A 1 130 ? -10.304 -5.256  -0.881  1.00 44.32  ? 128 MET A CE    1 
ATOM   979  N  N     . SER A 1 131 ? -9.848  -7.118  4.696   1.00 24.31  ? 129 SER A N     1 
ATOM   980  C  CA    . SER A 1 131 ? -10.602 -7.116  5.942   1.00 23.04  ? 129 SER A CA    1 
ATOM   981  C  C     . SER A 1 131 ? -9.742  -7.582  7.122   1.00 23.45  ? 129 SER A C     1 
ATOM   982  O  O     . SER A 1 131 ? -9.860  -7.014  8.186   1.00 20.12  ? 129 SER A O     1 
ATOM   983  C  CB    . SER A 1 131 ? -11.863 -7.910  5.855   1.00 24.93  ? 129 SER A CB    1 
ATOM   984  O  OG    . SER A 1 131 ? -11.617 -9.253  5.486   1.00 25.86  ? 129 SER A OG    1 
ATOM   985  N  N     . TYR A 1 132 ? -8.853  -8.569  6.937   1.00 23.68  ? 130 TYR A N     1 
ATOM   986  C  CA    . TYR A 1 132 ? -7.996  -9.002  8.035   1.00 23.83  ? 130 TYR A CA    1 
ATOM   987  C  C     . TYR A 1 132 ? -7.031  -7.900  8.452   1.00 23.58  ? 130 TYR A C     1 
ATOM   988  O  O     . TYR A 1 132 ? -6.795  -7.694  9.649   1.00 22.71  ? 130 TYR A O     1 
ATOM   989  C  CB    . TYR A 1 132 ? -7.213  -10.262 7.679   1.00 24.89  ? 130 TYR A CB    1 
ATOM   990  C  CG    . TYR A 1 132 ? -6.503  -10.867 8.883   1.00 26.19  ? 130 TYR A CG    1 
ATOM   991  C  CD1   . TYR A 1 132 ? -7.207  -11.198 10.042  1.00 28.19  ? 130 TYR A CD1   1 
ATOM   992  C  CD2   . TYR A 1 132 ? -5.133  -11.078 8.888   1.00 25.49  ? 130 TYR A CD2   1 
ATOM   993  C  CE1   . TYR A 1 132 ? -6.575  -11.736 11.146  1.00 28.84  ? 130 TYR A CE1   1 
ATOM   994  C  CE2   . TYR A 1 132 ? -4.494  -11.649 9.983   1.00 28.17  ? 130 TYR A CE2   1 
ATOM   995  C  CZ    . TYR A 1 132 ? -5.220  -11.977 11.116  1.00 30.43  ? 130 TYR A CZ    1 
ATOM   996  O  OH    . TYR A 1 132 ? -4.658  -12.515 12.252  1.00 32.46  ? 130 TYR A OH    1 
ATOM   997  N  N     . LEU A 1 133 ? -6.452  -7.190  7.478   1.00 23.03  ? 131 LEU A N     1 
ATOM   998  C  CA    . LEU A 1 133 ? -5.512  -6.145  7.833   1.00 22.75  ? 131 LEU A CA    1 
ATOM   999  C  C     . LEU A 1 133 ? -6.259  -5.003  8.506   1.00 22.22  ? 131 LEU A C     1 
ATOM   1000 O  O     . LEU A 1 133 ? -5.781  -4.456  9.497   1.00 21.84  ? 131 LEU A O     1 
ATOM   1001 C  CB    . LEU A 1 133 ? -4.720  -5.700  6.604   1.00 22.28  ? 131 LEU A CB    1 
ATOM   1002 C  CG    . LEU A 1 133 ? -3.800  -6.788  6.040   1.00 25.34  ? 131 LEU A CG    1 
ATOM   1003 C  CD1   . LEU A 1 133 ? -3.320  -6.390  4.672   1.00 29.72  ? 131 LEU A CD1   1 
ATOM   1004 C  CD2   . LEU A 1 133 ? -2.617  -7.067  6.978   1.00 24.59  ? 131 LEU A CD2   1 
ATOM   1005 N  N     . LEU A 1 134 ? -7.457  -4.675  8.027   1.00 23.78  ? 132 LEU A N     1 
ATOM   1006 C  CA    . LEU A 1 134 ? -8.207  -3.611  8.675   1.00 23.73  ? 132 LEU A CA    1 
ATOM   1007 C  C     . LEU A 1 134 ? -8.626  -4.021  10.087  1.00 23.40  ? 132 LEU A C     1 
ATOM   1008 O  O     . LEU A 1 134 ? -8.528  -3.217  11.010  1.00 19.90  ? 132 LEU A O     1 
ATOM   1009 C  CB    . LEU A 1 134 ? -9.388  -3.210  7.799   1.00 24.09  ? 132 LEU A CB    1 
ATOM   1010 C  CG    . LEU A 1 134 ? -8.967  -2.576  6.477   1.00 26.43  ? 132 LEU A CG    1 
ATOM   1011 C  CD1   . LEU A 1 134 ? -10.129 -2.635  5.507   1.00 27.81  ? 132 LEU A CD1   1 
ATOM   1012 C  CD2   . LEU A 1 134 ? -8.461  -1.136  6.648   1.00 26.58  ? 132 LEU A CD2   1 
ATOM   1013 N  N     . TYR A 1 135 ? -9.060  -5.279  10.247  1.00 20.99  ? 133 TYR A N     1 
ATOM   1014 C  CA    . TYR A 1 135 ? -9.466  -5.762  11.542  1.00 19.99  ? 133 TYR A CA    1 
ATOM   1015 C  C     . TYR A 1 135 ? -8.332  -5.598  12.555  1.00 20.77  ? 133 TYR A C     1 
ATOM   1016 O  O     . TYR A 1 135 ? -8.548  -5.147  13.672  1.00 22.50  ? 133 TYR A O     1 
ATOM   1017 C  CB    . TYR A 1 135 ? -9.831  -7.232  11.425  1.00 20.75  ? 133 TYR A CB    1 
ATOM   1018 C  CG    . TYR A 1 135 ? -9.894  -7.945  12.759  1.00 21.33  ? 133 TYR A CG    1 
ATOM   1019 C  CD1   . TYR A 1 135 ? -10.906 -7.670  13.684  1.00 22.88  ? 133 TYR A CD1   1 
ATOM   1020 C  CD2   . TYR A 1 135 ? -8.960  -8.923  13.074  1.00 22.54  ? 133 TYR A CD2   1 
ATOM   1021 C  CE1   . TYR A 1 135 ? -10.966 -8.343  14.898  1.00 23.56  ? 133 TYR A CE1   1 
ATOM   1022 C  CE2   . TYR A 1 135 ? -9.025  -9.619  14.275  1.00 23.07  ? 133 TYR A CE2   1 
ATOM   1023 C  CZ    . TYR A 1 135 ? -10.016 -9.312  15.194  1.00 23.90  ? 133 TYR A CZ    1 
ATOM   1024 O  OH    . TYR A 1 135 ? -10.059 -9.995  16.375  1.00 26.97  ? 133 TYR A OH    1 
ATOM   1025 N  N     . GLN A 1 136 ? -7.114  -5.935  12.137  1.00 21.49  ? 134 GLN A N     1 
ATOM   1026 C  CA    . GLN A 1 136 ? -5.967  -5.838  13.011  1.00 21.23  ? 134 GLN A CA    1 
ATOM   1027 C  C     . GLN A 1 136 ? -5.651  -4.377  13.351  1.00 19.85  ? 134 GLN A C     1 
ATOM   1028 O  O     . GLN A 1 136 ? -5.290  -4.071  14.491  1.00 19.71  ? 134 GLN A O     1 
ATOM   1029 C  CB    . GLN A 1 136 ? -4.766  -6.526  12.361  1.00 22.96  ? 134 GLN A CB    1 
ATOM   1030 C  CG    . GLN A 1 136 ? -4.841  -8.047  12.284  1.00 21.85  ? 134 GLN A CG    1 
ATOM   1031 C  CD    . GLN A 1 136 ? -3.508  -8.600  11.841  1.00 24.63  ? 134 GLN A CD    1 
ATOM   1032 O  OE1   . GLN A 1 136 ? -2.583  -8.763  12.638  1.00 23.95  ? 134 GLN A OE1   1 
ATOM   1033 N  NE2   . GLN A 1 136 ? -3.352  -8.787  10.543  1.00 22.95  ? 134 GLN A NE2   1 
ATOM   1034 N  N     . MET A 1 137 ? -5.793  -3.487  12.380  1.00 19.36  ? 135 MET A N     1 
ATOM   1035 C  CA    . MET A 1 137 ? -5.554  -2.077  12.628  1.00 21.85  ? 135 MET A CA    1 
ATOM   1036 C  C     . MET A 1 137 ? -6.548  -1.588  13.685  1.00 21.08  ? 135 MET A C     1 
ATOM   1037 O  O     . MET A 1 137 ? -6.170  -0.888  14.623  1.00 19.90  ? 135 MET A O     1 
ATOM   1038 C  CB    . MET A 1 137 ? -5.666  -1.240  11.355  1.00 21.19  ? 135 MET A CB    1 
ATOM   1039 C  CG    . MET A 1 137 ? -4.548  -1.500  10.314  1.00 24.98  ? 135 MET A CG    1 
ATOM   1040 S  SD    . MET A 1 137 ? -4.906  -0.637  8.757   1.00 29.46  ? 135 MET A SD    1 
ATOM   1041 C  CE    . MET A 1 137 ? -5.340  0.951   9.450   1.00 31.06  ? 135 MET A CE    1 
ATOM   1042 N  N     . LEU A 1 138 ? -7.814  -1.998  13.552  1.00 21.63  ? 136 LEU A N     1 
ATOM   1043 C  CA    . LEU A 1 138 ? -8.860  -1.624  14.489  1.00 21.03  ? 136 LEU A CA    1 
ATOM   1044 C  C     . LEU A 1 138 ? -8.596  -2.201  15.872  1.00 20.73  ? 136 LEU A C     1 
ATOM   1045 O  O     . LEU A 1 138 ? -8.841  -1.535  16.866  1.00 21.70  ? 136 LEU A O     1 
ATOM   1046 C  CB    . LEU A 1 138 ? -10.205 -2.077  13.938  1.00 20.87  ? 136 LEU A CB    1 
ATOM   1047 C  CG    . LEU A 1 138 ? -10.691 -1.213  12.776  1.00 21.65  ? 136 LEU A CG    1 
ATOM   1048 C  CD1   . LEU A 1 138 ? -11.874 -1.905  12.066  1.00 20.40  ? 136 LEU A CD1   1 
ATOM   1049 C  CD2   . LEU A 1 138 ? -11.007 0.229   13.248  1.00 19.62  ? 136 LEU A CD2   1 
ATOM   1050 N  N     . CYS A 1 139 ? -8.111  -3.438  15.947  1.00 20.03  ? 137 CYS A N     1 
ATOM   1051 C  CA    . CYS A 1 139 ? -7.769  -4.017  17.235  1.00 20.66  ? 137 CYS A CA    1 
ATOM   1052 C  C     . CYS A 1 139 ? -6.663  -3.208  17.922  1.00 22.00  ? 137 CYS A C     1 
ATOM   1053 O  O     . CYS A 1 139 ? -6.744  -2.956  19.124  1.00 20.53  ? 137 CYS A O     1 
ATOM   1054 C  CB    . CYS A 1 139 ? -7.349  -5.473  17.102  1.00 20.83  ? 137 CYS A CB    1 
ATOM   1055 S  SG    . CYS A 1 139 ? -8.685  -6.631  16.717  1.00 24.25  ? 137 CYS A SG    1 
ATOM   1056 N  N     . GLY A 1 140 ? -5.587  -2.875  17.194  1.00 20.46  ? 138 GLY A N     1 
ATOM   1057 C  CA    . GLY A 1 140 ? -4.513  -2.099  17.799  1.00 22.35  ? 138 GLY A CA    1 
ATOM   1058 C  C     . GLY A 1 140 ? -4.994  -0.725  18.272  1.00 21.30  ? 138 GLY A C     1 
ATOM   1059 O  O     . GLY A 1 140 ? -4.652  -0.294  19.364  1.00 21.30  ? 138 GLY A O     1 
ATOM   1060 N  N     . ILE A 1 141 ? -5.773  -0.031  17.431  1.00 19.66  ? 139 ILE A N     1 
ATOM   1061 C  CA    . ILE A 1 141 ? -6.309  1.268   17.792  1.00 21.94  ? 139 ILE A CA    1 
ATOM   1062 C  C     . ILE A 1 141 ? -7.229  1.145   19.004  1.00 20.48  ? 139 ILE A C     1 
ATOM   1063 O  O     . ILE A 1 141 ? -7.159  1.967   19.910  1.00 20.95  ? 139 ILE A O     1 
ATOM   1064 C  CB    . ILE A 1 141 ? -7.066  1.907   16.618  1.00 21.77  ? 139 ILE A CB    1 
ATOM   1065 C  CG1   . ILE A 1 141 ? -6.158  2.319   15.471  1.00 21.77  ? 139 ILE A CG1   1 
ATOM   1066 C  CG2   . ILE A 1 141 ? -7.831  3.093   17.095  1.00 22.87  ? 139 ILE A CG2   1 
ATOM   1067 C  CD1   . ILE A 1 141 ? -6.977  2.447   14.194  1.00 23.77  ? 139 ILE A CD1   1 
ATOM   1068 N  N     . LYS A 1 142 ? -8.109  0.140   19.013  1.00 21.73  ? 140 LYS A N     1 
ATOM   1069 C  CA    . LYS A 1 142 ? -9.001  -0.052  20.157  1.00 23.12  ? 140 LYS A CA    1 
ATOM   1070 C  C     . LYS A 1 142 ? -8.174  -0.233  21.431  1.00 23.74  ? 140 LYS A C     1 
ATOM   1071 O  O     . LYS A 1 142 ? -8.518  0.314   22.476  1.00 22.01  ? 140 LYS A O     1 
ATOM   1072 C  CB    . LYS A 1 142 ? -9.969  -1.227  19.989  1.00 24.43  ? 140 LYS A CB    1 
ATOM   1073 C  CG    . LYS A 1 142 ? -10.854 -1.524  21.224  1.00 26.54  ? 140 LYS A CG    1 
ATOM   1074 C  CD    . LYS A 1 142 ? -11.923 -2.604  21.007  1.00 31.63  ? 140 LYS A CD    1 
ATOM   1075 C  CE    . LYS A 1 142 ? -12.765 -2.975  22.236  1.00 35.53  ? 140 LYS A CE    1 
ATOM   1076 N  NZ    . LYS A 1 142 ? -13.424 -1.791  22.822  1.00 47.86  ? 140 LYS A NZ    1 
ATOM   1077 N  N     . HIS A 1 143 ? -7.080  -0.991  21.356  1.00 23.32  ? 141 HIS A N     1 
ATOM   1078 C  CA    . HIS A 1 143 ? -6.258  -1.226  22.532  1.00 21.98  ? 141 HIS A CA    1 
ATOM   1079 C  C     . HIS A 1 143 ? -5.659  0.085   23.053  1.00 21.80  ? 141 HIS A C     1 
ATOM   1080 O  O     . HIS A 1 143 ? -5.701  0.351   24.270  1.00 22.03  ? 141 HIS A O     1 
ATOM   1081 C  CB    . HIS A 1 143 ? -5.219  -2.312  22.229  1.00 23.37  ? 141 HIS A CB    1 
ATOM   1082 C  CG    . HIS A 1 143 ? -4.485  -2.828  23.408  1.00 22.65  ? 141 HIS A CG    1 
ATOM   1083 N  ND1   . HIS A 1 143 ? -5.131  -3.515  24.419  1.00 25.10  ? 141 HIS A ND1   1 
ATOM   1084 C  CD2   . HIS A 1 143 ? -3.195  -2.840  23.718  1.00 22.53  ? 141 HIS A CD2   1 
ATOM   1085 C  CE1   . HIS A 1 143 ? -4.239  -3.901  25.324  1.00 26.91  ? 141 HIS A CE1   1 
ATOM   1086 N  NE2   . HIS A 1 143 ? -3.054  -3.496  24.927  1.00 24.61  ? 141 HIS A NE2   1 
ATOM   1087 N  N     . LEU A 1 144 ? -5.118  0.916   22.157  1.00 21.92  ? 142 LEU A N     1 
ATOM   1088 C  CA    . LEU A 1 144 ? -4.615  2.238   22.551  1.00 23.83  ? 142 LEU A CA    1 
ATOM   1089 C  C     . LEU A 1 144 ? -5.691  3.085   23.210  1.00 23.38  ? 142 LEU A C     1 
ATOM   1090 O  O     . LEU A 1 144 ? -5.466  3.648   24.276  1.00 24.60  ? 142 LEU A O     1 
ATOM   1091 C  CB    . LEU A 1 144 ? -3.989  2.951   21.345  1.00 21.73  ? 142 LEU A CB    1 
ATOM   1092 C  CG    . LEU A 1 144 ? -2.787  2.204   20.764  1.00 22.49  ? 142 LEU A CG    1 
ATOM   1093 C  CD1   . LEU A 1 144 ? -2.179  2.977   19.614  1.00 24.06  ? 142 LEU A CD1   1 
ATOM   1094 C  CD2   . LEU A 1 144 ? -1.707  1.930   21.792  1.00 25.20  ? 142 LEU A CD2   1 
ATOM   1095 N  N     . HIS A 1 145 ? -6.862  3.153   22.590  1.00 21.26  ? 143 HIS A N     1 
ATOM   1096 C  CA    . HIS A 1 145 ? -7.985  3.932   23.068  1.00 21.39  ? 143 HIS A CA    1 
ATOM   1097 C  C     . HIS A 1 145 ? -8.411  3.502   24.463  1.00 23.24  ? 143 HIS A C     1 
ATOM   1098 O  O     . HIS A 1 145 ? -8.737  4.351   25.279  1.00 23.82  ? 143 HIS A O     1 
ATOM   1099 C  CB    . HIS A 1 145 ? -9.167  3.802   22.092  1.00 20.70  ? 143 HIS A CB    1 
ATOM   1100 C  CG    . HIS A 1 145 ? -8.989  4.512   20.795  1.00 20.72  ? 143 HIS A CG    1 
ATOM   1101 N  ND1   . HIS A 1 145 ? -9.995  4.558   19.849  1.00 21.33  ? 143 HIS A ND1   1 
ATOM   1102 C  CD2   . HIS A 1 145 ? -7.962  5.223   20.289  1.00 19.61  ? 143 HIS A CD2   1 
ATOM   1103 C  CE1   . HIS A 1 145 ? -9.576  5.278   18.821  1.00 23.28  ? 143 HIS A CE1   1 
ATOM   1104 N  NE2   . HIS A 1 145 ? -8.341  5.671   19.054  1.00 22.25  ? 143 HIS A NE2   1 
ATOM   1105 N  N     . SER A 1 146 ? -8.345  2.194   24.745  1.00 24.51  ? 144 SER A N     1 
ATOM   1106 C  CA    . SER A 1 146 ? -8.735  1.660   26.037  1.00 26.45  ? 144 SER A CA    1 
ATOM   1107 C  C     . SER A 1 146 ? -7.819  2.169   27.151  1.00 29.11  ? 144 SER A C     1 
ATOM   1108 O  O     . SER A 1 146 ? -8.224  2.147   28.308  1.00 30.92  ? 144 SER A O     1 
ATOM   1109 C  CB    . SER A 1 146 ? -8.771  0.144   26.047  1.00 25.43  ? 144 SER A CB    1 
ATOM   1110 O  OG    . SER A 1 146 ? -7.449  -0.416  26.060  1.00 26.06  ? 144 SER A OG    1 
ATOM   1111 N  N     . ALA A 1 147 ? -6.588  2.592   26.829  1.00 27.87  ? 145 ALA A N     1 
ATOM   1112 C  CA    . ALA A 1 147 ? -5.737  3.236   27.827  1.00 29.05  ? 145 ALA A CA    1 
ATOM   1113 C  C     . ALA A 1 147 ? -5.746  4.760   27.674  1.00 30.23  ? 145 ALA A C     1 
ATOM   1114 O  O     . ALA A 1 147 ? -4.906  5.423   28.260  1.00 30.67  ? 145 ALA A O     1 
ATOM   1115 C  CB    . ALA A 1 147 ? -4.338  2.711   27.720  1.00 31.84  ? 145 ALA A CB    1 
ATOM   1116 N  N     . GLY A 1 148 ? -6.702  5.322   26.928  1.00 28.87  ? 146 GLY A N     1 
ATOM   1117 C  CA    . GLY A 1 148 ? -6.805  6.766   26.766  1.00 26.25  ? 146 GLY A CA    1 
ATOM   1118 C  C     . GLY A 1 148 ? -5.790  7.352   25.778  1.00 27.37  ? 146 GLY A C     1 
ATOM   1119 O  O     . GLY A 1 148 ? -5.574  8.557   25.783  1.00 29.57  ? 146 GLY A O     1 
ATOM   1120 N  N     . ILE A 1 149 ? -5.179  6.518   24.922  1.00 24.53  ? 147 ILE A N     1 
ATOM   1121 C  CA    . ILE A 1 149 ? -4.188  6.962   23.949  1.00 24.49  ? 147 ILE A CA    1 
ATOM   1122 C  C     . ILE A 1 149 ? -4.903  7.079   22.602  1.00 23.71  ? 147 ILE A C     1 
ATOM   1123 O  O     . ILE A 1 149 ? -5.270  6.069   22.011  1.00 24.28  ? 147 ILE A O     1 
ATOM   1124 C  CB    . ILE A 1 149 ? -3.001  5.974   23.884  1.00 26.99  ? 147 ILE A CB    1 
ATOM   1125 C  CG1   . ILE A 1 149 ? -2.271  5.827   25.231  1.00 29.29  ? 147 ILE A CG1   1 
ATOM   1126 C  CG2   . ILE A 1 149 ? -2.012  6.329   22.774  1.00 26.20  ? 147 ILE A CG2   1 
ATOM   1127 C  CD1   . ILE A 1 149 ? -1.655  7.125   25.729  1.00 30.34  ? 147 ILE A CD1   1 
ATOM   1128 N  N     . ILE A 1 150 ? -5.109  8.311   22.139  1.00 22.71  ? 148 ILE A N     1 
ATOM   1129 C  CA    . ILE A 1 150 ? -5.697  8.591   20.829  1.00 23.97  ? 148 ILE A CA    1 
ATOM   1130 C  C     . ILE A 1 150 ? -4.537  8.984   19.902  1.00 25.90  ? 148 ILE A C     1 
ATOM   1131 O  O     . ILE A 1 150 ? -3.730  9.833   20.261  1.00 25.94  ? 148 ILE A O     1 
ATOM   1132 C  CB    . ILE A 1 150 ? -6.782  9.676   20.931  1.00 25.55  ? 148 ILE A CB    1 
ATOM   1133 C  CG1   . ILE A 1 150 ? -7.832  9.296   21.989  1.00 27.97  ? 148 ILE A CG1   1 
ATOM   1134 C  CG2   . ILE A 1 150 ? -7.387  9.947   19.543  1.00 25.73  ? 148 ILE A CG2   1 
ATOM   1135 C  CD1   . ILE A 1 150 ? -8.902  10.337  22.262  1.00 27.69  ? 148 ILE A CD1   1 
ATOM   1136 N  N     . HIS A 1 151 ? -4.409  8.315   18.753  1.00 22.51  ? 149 HIS A N     1 
ATOM   1137 C  CA    . HIS A 1 151 ? -3.182  8.371   17.958  1.00 22.74  ? 149 HIS A CA    1 
ATOM   1138 C  C     . HIS A 1 151 ? -3.105  9.688   17.185  1.00 23.03  ? 149 HIS A C     1 
ATOM   1139 O  O     . HIS A 1 151 ? -2.163  10.442  17.371  1.00 25.14  ? 149 HIS A O     1 
ATOM   1140 C  CB    . HIS A 1 151 ? -3.046  7.129   17.051  1.00 22.58  ? 149 HIS A CB    1 
ATOM   1141 C  CG    . HIS A 1 151 ? -1.690  6.920   16.435  1.00 21.02  ? 149 HIS A CG    1 
ATOM   1142 N  ND1   . HIS A 1 151 ? -1.130  7.807   15.538  1.00 23.19  ? 149 HIS A ND1   1 
ATOM   1143 C  CD2   . HIS A 1 151 ? -0.802  5.918   16.569  1.00 22.04  ? 149 HIS A CD2   1 
ATOM   1144 C  CE1   . HIS A 1 151 ? 0.056   7.339   15.148  1.00 23.88  ? 149 HIS A CE1   1 
ATOM   1145 N  NE2   . HIS A 1 151 ? 0.270   6.186   15.744  1.00 23.19  ? 149 HIS A NE2   1 
ATOM   1146 N  N     . ARG A 1 152 ? -4.090  9.946   16.316  1.00 22.65  ? 150 ARG A N     1 
ATOM   1147 C  CA    . ARG A 1 152 ? -4.256  11.140  15.494  1.00 25.80  ? 150 ARG A CA    1 
ATOM   1148 C  C     . ARG A 1 152 ? -3.317  11.183  14.288  1.00 26.24  ? 150 ARG A C     1 
ATOM   1149 O  O     . ARG A 1 152 ? -3.513  12.035  13.419  1.00 30.29  ? 150 ARG A O     1 
ATOM   1150 C  CB    . ARG A 1 152 ? -4.149  12.479  16.262  1.00 26.44  ? 150 ARG A CB    1 
ATOM   1151 C  CG    . ARG A 1 152 ? -5.413  12.849  17.022  1.00 30.75  ? 150 ARG A CG    1 
ATOM   1152 C  CD    . ARG A 1 152 ? -5.409  14.280  17.503  1.00 31.90  ? 150 ARG A CD    1 
ATOM   1153 N  NE    . ARG A 1 152 ? -4.332  14.519  18.442  1.00 33.69  ? 150 ARG A NE    1 
ATOM   1154 C  CZ    . ARG A 1 152 ? -3.841  15.723  18.749  1.00 40.12  ? 150 ARG A CZ    1 
ATOM   1155 N  NH1   . ARG A 1 152 ? -4.301  16.826  18.175  1.00 41.99  ? 150 ARG A NH1   1 
ATOM   1156 N  NH2   . ARG A 1 152 ? -2.867  15.817  19.638  1.00 42.01  ? 150 ARG A NH2   1 
ATOM   1157 N  N     . ASP A 1 153 ? -2.328  10.297  14.194  1.00 22.09  ? 151 ASP A N     1 
ATOM   1158 C  CA    . ASP A 1 153 ? -1.415  10.396  13.069  1.00 24.24  ? 151 ASP A CA    1 
ATOM   1159 C  C     . ASP A 1 153 ? -1.112  9.018   12.470  1.00 23.52  ? 151 ASP A C     1 
ATOM   1160 O  O     . ASP A 1 153 ? 0.011   8.756   12.075  1.00 25.05  ? 151 ASP A O     1 
ATOM   1161 C  CB    . ASP A 1 153 ? -0.110  11.093  13.454  1.00 27.01  ? 151 ASP A CB    1 
ATOM   1162 C  CG    . ASP A 1 153 ? 0.624   11.659  12.250  1.00 30.28  ? 151 ASP A CG    1 
ATOM   1163 O  OD1   . ASP A 1 153 ? -0.016  11.861  11.172  1.00 27.87  ? 151 ASP A OD1   1 
ATOM   1164 O  OD2   . ASP A 1 153 ? 1.806   11.907  12.383  1.00 35.73  ? 151 ASP A OD2   1 
ATOM   1165 N  N     . LEU A 1 154 ? -2.120  8.154   12.342  1.00 21.30  ? 152 LEU A N     1 
ATOM   1166 C  CA    . LEU A 1 154 ? -1.893  6.822   11.791  1.00 20.83  ? 152 LEU A CA    1 
ATOM   1167 C  C     . LEU A 1 154 ? -1.578  6.960   10.307  1.00 22.47  ? 152 LEU A C     1 
ATOM   1168 O  O     . LEU A 1 154 ? -2.198  7.766   9.603   1.00 22.65  ? 152 LEU A O     1 
ATOM   1169 C  CB    . LEU A 1 154 ? -3.126  5.941   11.937  1.00 20.52  ? 152 LEU A CB    1 
ATOM   1170 C  CG    . LEU A 1 154 ? -3.419  5.474   13.341  1.00 26.49  ? 152 LEU A CG    1 
ATOM   1171 C  CD1   . LEU A 1 154 ? -4.905  5.128   13.444  1.00 29.85  ? 152 LEU A CD1   1 
ATOM   1172 C  CD2   . LEU A 1 154 ? -2.508  4.295   13.739  1.00 25.37  ? 152 LEU A CD2   1 
ATOM   1173 N  N     . LYS A 1 155 ? -0.603  6.191   9.838   1.00 24.13  ? 153 LYS A N     1 
ATOM   1174 C  CA    . LYS A 1 155 ? -0.246  6.243   8.424   1.00 25.00  ? 153 LYS A CA    1 
ATOM   1175 C  C     . LYS A 1 155 ? 0.409   4.922   8.025   1.00 23.29  ? 153 LYS A C     1 
ATOM   1176 O  O     . LYS A 1 155 ? 1.033   4.249   8.845   1.00 22.89  ? 153 LYS A O     1 
ATOM   1177 C  CB    . LYS A 1 155 ? 0.665   7.435   8.109   1.00 27.47  ? 153 LYS A CB    1 
ATOM   1178 C  CG    . LYS A 1 155 ? 2.072   7.410   8.715   1.00 28.74  ? 153 LYS A CG    1 
ATOM   1179 C  CD    . LYS A 1 155 ? 2.798   8.799   8.641   1.00 34.61  ? 153 LYS A CD    1 
ATOM   1180 C  CE    . LYS A 1 155 ? 2.064   9.823   9.500   1.00 38.33  ? 153 LYS A CE    1 
ATOM   1181 N  NZ    . LYS A 1 155 ? 2.624   11.208  9.488   1.00 39.94  ? 153 LYS A NZ    1 
ATOM   1182 N  N     . PRO A 1 156 ? 0.276   4.501   6.755   1.00 24.04  ? 154 PRO A N     1 
ATOM   1183 C  CA    . PRO A 1 156 ? 0.814   3.197   6.340   1.00 24.69  ? 154 PRO A CA    1 
ATOM   1184 C  C     . PRO A 1 156 ? 2.319   3.004   6.528   1.00 25.18  ? 154 PRO A C     1 
ATOM   1185 O  O     . PRO A 1 156 ? 2.740   1.876   6.747   1.00 25.89  ? 154 PRO A O     1 
ATOM   1186 C  CB    . PRO A 1 156 ? 0.501   3.085   4.845   1.00 27.63  ? 154 PRO A CB    1 
ATOM   1187 C  CG    . PRO A 1 156 ? -0.449  4.192   4.533   1.00 28.52  ? 154 PRO A CG    1 
ATOM   1188 C  CD    . PRO A 1 156 ? -0.436  5.182   5.681   1.00 25.90  ? 154 PRO A CD    1 
ATOM   1189 N  N     . SER A 1 157 ? 3.122   4.071   6.427   1.00 26.75  ? 155 SER A N     1 
ATOM   1190 C  CA    . SER A 1 157 ? 4.556   3.960   6.672   1.00 30.92  ? 155 SER A CA    1 
ATOM   1191 C  C     . SER A 1 157 ? 4.877   3.601   8.129   1.00 31.53  ? 155 SER A C     1 
ATOM   1192 O  O     . SER A 1 157 ? 5.983   3.138   8.432   1.00 31.68  ? 155 SER A O     1 
ATOM   1193 C  CB    . SER A 1 157 ? 5.311   5.217   6.253   1.00 33.19  ? 155 SER A CB    1 
ATOM   1194 O  OG    . SER A 1 157 ? 4.924   6.343   7.043   1.00 31.61  ? 155 SER A OG    1 
ATOM   1195 N  N     . ASN A 1 158 ? 3.939   3.825   9.049   1.00 26.73  ? 156 ASN A N     1 
ATOM   1196 C  CA    . ASN A 1 158 ? 4.181   3.513   10.447  1.00 28.97  ? 156 ASN A CA    1 
ATOM   1197 C  C     . ASN A 1 158 ? 3.302   2.346   10.883  1.00 25.74  ? 156 ASN A C     1 
ATOM   1198 O  O     . ASN A 1 158 ? 2.908   2.251   12.030  1.00 22.67  ? 156 ASN A O     1 
ATOM   1199 C  CB    . ASN A 1 158 ? 4.018   4.750   11.338  1.00 33.05  ? 156 ASN A CB    1 
ATOM   1200 C  CG    . ASN A 1 158 ? 5.246   5.650   11.291  1.00 41.88  ? 156 ASN A CG    1 
ATOM   1201 O  OD1   . ASN A 1 158 ? 5.992   5.735   12.264  1.00 50.17  ? 156 ASN A OD1   1 
ATOM   1202 N  ND2   . ASN A 1 158 ? 5.491   6.308   10.171  1.00 42.70  ? 156 ASN A ND2   1 
ATOM   1203 N  N     . ILE A 1 159 ? 3.014   1.448   9.951   1.00 24.55  ? 157 ILE A N     1 
ATOM   1204 C  CA    . ILE A 1 159 ? 2.315   0.210   10.234  1.00 23.92  ? 157 ILE A CA    1 
ATOM   1205 C  C     . ILE A 1 159 ? 3.119   -0.828  9.476   1.00 26.71  ? 157 ILE A C     1 
ATOM   1206 O  O     . ILE A 1 159 ? 3.419   -0.605  8.311   1.00 26.25  ? 157 ILE A O     1 
ATOM   1207 C  CB    . ILE A 1 159 ? 0.841   0.237   9.763   1.00 23.92  ? 157 ILE A CB    1 
ATOM   1208 C  CG1   . ILE A 1 159 ? 0.003   1.244   10.550  1.00 24.31  ? 157 ILE A CG1   1 
ATOM   1209 C  CG2   . ILE A 1 159 ? 0.235   -1.179  9.815   1.00 23.59  ? 157 ILE A CG2   1 
ATOM   1210 C  CD1   . ILE A 1 159 ? -1.333  1.607   9.910   1.00 25.06  ? 157 ILE A CD1   1 
ATOM   1211 N  N     . VAL A 1 160 ? 3.474   -1.933  10.152  1.00 26.35  ? 158 VAL A N     1 
ATOM   1212 C  CA    . VAL A 1 160 ? 4.350   -2.916  9.560   1.00 27.07  ? 158 VAL A CA    1 
ATOM   1213 C  C     . VAL A 1 160 ? 3.647   -4.260  9.651   1.00 28.04  ? 158 VAL A C     1 
ATOM   1214 O  O     . VAL A 1 160 ? 2.727   -4.445  10.471  1.00 24.36  ? 158 VAL A O     1 
ATOM   1215 C  CB    . VAL A 1 160 ? 5.716   -2.950  10.273  1.00 28.94  ? 158 VAL A CB    1 
ATOM   1216 C  CG1   . VAL A 1 160 ? 6.554   -1.736  9.927   1.00 29.57  ? 158 VAL A CG1   1 
ATOM   1217 C  CG2   . VAL A 1 160 ? 5.545   -3.034  11.770  1.00 29.88  ? 158 VAL A CG2   1 
ATOM   1218 N  N     . VAL A 1 161 ? 4.117   -5.173  8.804   1.00 28.52  ? 159 VAL A N     1 
ATOM   1219 C  CA    . VAL A 1 161 ? 3.479   -6.459  8.608   1.00 28.01  ? 159 VAL A CA    1 
ATOM   1220 C  C     . VAL A 1 161 ? 4.555   -7.549  8.548   1.00 31.20  ? 159 VAL A C     1 
ATOM   1221 O  O     . VAL A 1 161 ? 5.645   -7.333  8.030   1.00 31.25  ? 159 VAL A O     1 
ATOM   1222 C  CB    . VAL A 1 161 ? 2.613   -6.452  7.335   1.00 29.68  ? 159 VAL A CB    1 
ATOM   1223 C  CG1   . VAL A 1 161 ? 1.865   -7.754  7.195   1.00 30.75  ? 159 VAL A CG1   1 
ATOM   1224 C  CG2   . VAL A 1 161 ? 1.632   -5.291  7.310   1.00 30.63  ? 159 VAL A CG2   1 
ATOM   1225 N  N     . LYS A 1 162 ? 4.217   -8.720  9.100   1.00 30.85  ? 160 LYS A N     1 
ATOM   1226 C  CA    . LYS A 1 162 ? 5.102   -9.873  9.147   1.00 34.04  ? 160 LYS A CA    1 
ATOM   1227 C  C     . LYS A 1 162 ? 4.627   -10.863 8.088   1.00 34.25  ? 160 LYS A C     1 
ATOM   1228 O  O     . LYS A 1 162 ? 3.472   -10.829 7.677   1.00 30.11  ? 160 LYS A O     1 
ATOM   1229 C  CB    . LYS A 1 162 ? 5.060   -10.482 10.552  1.00 39.16  ? 160 LYS A CB    1 
ATOM   1230 C  CG    . LYS A 1 162 ? 6.413   -10.931 11.066  1.00 47.50  ? 160 LYS A CG    1 
ATOM   1231 C  CD    . LYS A 1 162 ? 6.342   -11.961 12.158  1.00 54.00  ? 160 LYS A CD    1 
ATOM   1232 C  CE    . LYS A 1 162 ? 5.582   -11.485 13.374  1.00 56.20  ? 160 LYS A CE    1 
ATOM   1233 N  NZ    . LYS A 1 162 ? 5.741   -12.464 14.474  1.00 63.56  ? 160 LYS A NZ    1 
ATOM   1234 N  N     . SER A 1 163 ? 5.515   -11.753 7.655   1.00 36.71  ? 161 SER A N     1 
ATOM   1235 C  CA    . SER A 1 163 ? 5.190   -12.755 6.655   1.00 37.70  ? 161 SER A CA    1 
ATOM   1236 C  C     . SER A 1 163 ? 4.068   -13.690 7.110   1.00 35.74  ? 161 SER A C     1 
ATOM   1237 O  O     . SER A 1 163 ? 3.441   -14.324 6.268   1.00 36.03  ? 161 SER A O     1 
ATOM   1238 C  CB    . SER A 1 163 ? 6.412   -13.557 6.301   1.00 41.10  ? 161 SER A CB    1 
ATOM   1239 O  OG    . SER A 1 163 ? 6.856   -14.270 7.444   1.00 47.97  ? 161 SER A OG    1 
ATOM   1240 N  N     . ASP A 1 164 ? 3.799   -13.796 8.414   1.00 30.92  ? 162 ASP A N     1 
ATOM   1241 C  CA    . ASP A 1 164 ? 2.676   -14.600 8.877   1.00 33.25  ? 162 ASP A CA    1 
ATOM   1242 C  C     . ASP A 1 164 ? 1.374   -13.797 8.933   1.00 32.86  ? 162 ASP A C     1 
ATOM   1243 O  O     . ASP A 1 164 ? 0.373   -14.272 9.482   1.00 32.96  ? 162 ASP A O     1 
ATOM   1244 C  CB    . ASP A 1 164 ? 2.981   -15.221 10.243  1.00 34.81  ? 162 ASP A CB    1 
ATOM   1245 C  CG    . ASP A 1 164 ? 3.019   -14.268 11.430  1.00 34.65  ? 162 ASP A CG    1 
ATOM   1246 O  OD1   . ASP A 1 164 ? 2.851   -13.041 11.255  1.00 32.44  ? 162 ASP A OD1   1 
ATOM   1247 O  OD2   . ASP A 1 164 ? 3.193   -14.773 12.546  1.00 35.99  ? 162 ASP A OD2   1 
ATOM   1248 N  N     . CYS A 1 165 ? 1.421   -12.554 8.436   1.00 27.85  ? 163 CYS A N     1 
ATOM   1249 C  CA    . CYS A 1 165 ? 0.260   -11.707 8.222   1.00 28.54  ? 163 CYS A CA    1 
ATOM   1250 C  C     . CYS A 1 165 ? -0.118  -10.903 9.464   1.00 26.25  ? 163 CYS A C     1 
ATOM   1251 O  O     . CYS A 1 165 ? -1.128  -10.205 9.431   1.00 25.10  ? 163 CYS A O     1 
ATOM   1252 C  CB    . CYS A 1 165 ? -0.935  -12.486 7.673   1.00 30.07  ? 163 CYS A CB    1 
ATOM   1253 S  SG    . CYS A 1 165 ? -0.617  -13.421 6.184   1.00 30.20  ? 163 CYS A SG    1 
ATOM   1254 N  N     . THR A 1 166 ? 0.693   -10.961 10.530  1.00 25.91  ? 164 THR A N     1 
ATOM   1255 C  CA    . THR A 1 166 ? 0.484   -10.121 11.700  1.00 26.75  ? 164 THR A CA    1 
ATOM   1256 C  C     . THR A 1 166 ? 0.797   -8.657  11.354  1.00 26.17  ? 164 THR A C     1 
ATOM   1257 O  O     . THR A 1 166 ? 1.853   -8.366  10.793  1.00 25.29  ? 164 THR A O     1 
ATOM   1258 C  CB    . THR A 1 166 ? 1.355   -10.575 12.875  1.00 29.68  ? 164 THR A CB    1 
ATOM   1259 O  OG1   . THR A 1 166 ? 1.125   -11.963 13.119  1.00 33.89  ? 164 THR A OG1   1 
ATOM   1260 C  CG2   . THR A 1 166 ? 1.068   -9.801  14.146  1.00 30.83  ? 164 THR A CG2   1 
ATOM   1261 N  N     . LEU A 1 167 ? -0.132  -7.756  11.692  1.00 23.72  ? 165 LEU A N     1 
ATOM   1262 C  CA    . LEU A 1 167 ? 0.028   -6.330  11.455  1.00 22.19  ? 165 LEU A CA    1 
ATOM   1263 C  C     . LEU A 1 167 ? 0.301   -5.624  12.785  1.00 22.20  ? 165 LEU A C     1 
ATOM   1264 O  O     . LEU A 1 167 ? -0.344  -5.909  13.787  1.00 22.38  ? 165 LEU A O     1 
ATOM   1265 C  CB    . LEU A 1 167 ? -1.231  -5.789  10.765  1.00 21.82  ? 165 LEU A CB    1 
ATOM   1266 C  CG    . LEU A 1 167 ? -1.281  -4.270  10.557  1.00 22.40  ? 165 LEU A CG    1 
ATOM   1267 C  CD1   . LEU A 1 167 ? -2.075  -3.952  9.296   1.00 23.65  ? 165 LEU A CD1   1 
ATOM   1268 C  CD2   . LEU A 1 167 ? -1.911  -3.577  11.754  1.00 20.82  ? 165 LEU A CD2   1 
ATOM   1269 N  N     . LYS A 1 168 ? 1.266   -4.690  12.801  1.00 23.71  ? 166 LYS A N     1 
ATOM   1270 C  CA    . LYS A 1 168 ? 1.600   -3.988  14.039  1.00 21.58  ? 166 LYS A CA    1 
ATOM   1271 C  C     . LYS A 1 168 ? 1.695   -2.488  13.768  1.00 24.31  ? 166 LYS A C     1 
ATOM   1272 O  O     . LYS A 1 168 ? 2.310   -2.082  12.796  1.00 22.85  ? 166 LYS A O     1 
ATOM   1273 C  CB    . LYS A 1 168 ? 2.911   -4.472  14.656  1.00 24.31  ? 166 LYS A CB    1 
ATOM   1274 C  CG    . LYS A 1 168 ? 2.926   -5.949  15.061  1.00 27.21  ? 166 LYS A CG    1 
ATOM   1275 C  CD    . LYS A 1 168 ? 4.230   -6.439  15.644  1.00 29.33  ? 166 LYS A CD    1 
ATOM   1276 C  CE    . LYS A 1 168 ? 4.209   -7.949  15.829  1.00 33.55  ? 166 LYS A CE    1 
ATOM   1277 N  NZ    . LYS A 1 168 ? 3.156   -8.389  16.780  1.00 30.94  ? 166 LYS A NZ    1 
ATOM   1278 N  N     . ILE A 1 169 ? 1.098   -1.689  14.657  1.00 24.07  ? 167 ILE A N     1 
ATOM   1279 C  CA    . ILE A 1 169 ? 1.289   -0.248  14.628  1.00 21.85  ? 167 ILE A CA    1 
ATOM   1280 C  C     . ILE A 1 169 ? 2.638   0.079   15.257  1.00 22.34  ? 167 ILE A C     1 
ATOM   1281 O  O     . ILE A 1 169 ? 2.955   -0.413  16.333  1.00 20.44  ? 167 ILE A O     1 
ATOM   1282 C  CB    . ILE A 1 169 ? 0.118   0.448   15.341  1.00 24.57  ? 167 ILE A CB    1 
ATOM   1283 C  CG1   . ILE A 1 169 ? -1.203  0.069   14.664  1.00 25.00  ? 167 ILE A CG1   1 
ATOM   1284 C  CG2   . ILE A 1 169 ? 0.297   1.970   15.386  1.00 22.67  ? 167 ILE A CG2   1 
ATOM   1285 C  CD1   . ILE A 1 169 ? -2.399  0.461   15.461  1.00 24.64  ? 167 ILE A CD1   1 
ATOM   1286 N  N     . LEU A 1 170 ? 3.395   0.984   14.607  1.00 22.92  ? 168 LEU A N     1 
ATOM   1287 C  CA    . LEU A 1 170 ? 4.768   1.269   14.982  1.00 24.20  ? 168 LEU A CA    1 
ATOM   1288 C  C     . LEU A 1 170 ? 4.893   2.425   15.976  1.00 27.50  ? 168 LEU A C     1 
ATOM   1289 O  O     . LEU A 1 170 ? 5.889   2.488   16.692  1.00 26.38  ? 168 LEU A O     1 
ATOM   1290 C  CB    . LEU A 1 170 ? 5.585   1.653   13.754  1.00 26.63  ? 168 LEU A CB    1 
ATOM   1291 C  CG    . LEU A 1 170 ? 6.387   0.599   13.002  1.00 33.30  ? 168 LEU A CG    1 
ATOM   1292 C  CD1   . LEU A 1 170 ? 7.292   1.330   12.002  1.00 36.51  ? 168 LEU A CD1   1 
ATOM   1293 C  CD2   . LEU A 1 170 ? 7.228   -0.258  13.939  1.00 35.38  ? 168 LEU A CD2   1 
ATOM   1294 N  N     . ASP A 1 171 ? 3.940   3.358   15.983  1.00 27.84  ? 169 ASP A N     1 
ATOM   1295 C  CA    . ASP A 1 171 ? 4.109   4.566   16.778  1.00 29.46  ? 169 ASP A CA    1 
ATOM   1296 C  C     . ASP A 1 171 ? 2.833   4.860   17.567  1.00 27.63  ? 169 ASP A C     1 
ATOM   1297 O  O     . ASP A 1 171 ? 1.840   4.153   17.426  1.00 23.83  ? 169 ASP A O     1 
ATOM   1298 C  CB    . ASP A 1 171 ? 4.549   5.731   15.892  1.00 29.70  ? 169 ASP A CB    1 
ATOM   1299 C  CG    . ASP A 1 171 ? 3.555   6.175   14.822  1.00 34.36  ? 169 ASP A CG    1 
ATOM   1300 O  OD1   . ASP A 1 171 ? 2.578   5.450   14.518  1.00 30.69  ? 169 ASP A OD1   1 
ATOM   1301 O  OD2   . ASP A 1 171 ? 3.780   7.248   14.263  1.00 41.53  ? 169 ASP A OD2   1 
ATOM   1302 N  N     . PHE A 1 172 ? 2.868   5.929   18.373  1.00 25.03  ? 170 PHE A N     1 
ATOM   1303 C  CA    . PHE A 1 172 ? 1.825   6.211   19.333  1.00 26.88  ? 170 PHE A CA    1 
ATOM   1304 C  C     . PHE A 1 172 ? 1.212   7.602   19.147  1.00 25.59  ? 170 PHE A C     1 
ATOM   1305 O  O     . PHE A 1 172 ? 0.382   7.999   19.953  1.00 25.77  ? 170 PHE A O     1 
ATOM   1306 C  CB    . PHE A 1 172 ? 2.380   6.024   20.749  1.00 27.85  ? 170 PHE A CB    1 
ATOM   1307 C  CG    . PHE A 1 172 ? 2.765   4.596   21.043  1.00 27.14  ? 170 PHE A CG    1 
ATOM   1308 C  CD1   . PHE A 1 172 ? 1.809   3.666   21.443  1.00 28.30  ? 170 PHE A CD1   1 
ATOM   1309 C  CD2   . PHE A 1 172 ? 4.057   4.164   20.808  1.00 29.83  ? 170 PHE A CD2   1 
ATOM   1310 C  CE1   . PHE A 1 172 ? 2.176   2.345   21.681  1.00 28.62  ? 170 PHE A CE1   1 
ATOM   1311 C  CE2   . PHE A 1 172 ? 4.416   2.832   20.994  1.00 31.85  ? 170 PHE A CE2   1 
ATOM   1312 C  CZ    . PHE A 1 172 ? 3.477   1.930   21.438  1.00 30.31  ? 170 PHE A CZ    1 
ATOM   1313 N  N     . GLY A 1 173 ? 1.574   8.330   18.098  1.00 26.03  ? 171 GLY A N     1 
ATOM   1314 C  CA    . GLY A 1 173 ? 0.742   9.449   17.697  1.00 28.34  ? 171 GLY A CA    1 
ATOM   1315 C  C     . GLY A 1 173 ? 1.105   10.765  18.379  1.00 32.11  ? 171 GLY A C     1 
ATOM   1316 O  O     . GLY A 1 173 ? 2.206   10.936  18.926  1.00 29.61  ? 171 GLY A O     1 
ATOM   1317 N  N     . LEU A 1 174 ? 0.151   11.708  18.312  1.00 33.50  ? 172 LEU A N     1 
ATOM   1318 C  CA    . LEU A 1 174 ? 0.423   13.132  18.514  1.00 35.94  ? 172 LEU A CA    1 
ATOM   1319 C  C     . LEU A 1 174 ? 0.222   13.585  19.961  1.00 40.06  ? 172 LEU A C     1 
ATOM   1320 O  O     . LEU A 1 174 ? 0.428   14.785  20.253  1.00 43.45  ? 172 LEU A O     1 
ATOM   1321 C  CB    . LEU A 1 174 ? -0.496  13.960  17.612  1.00 36.91  ? 172 LEU A CB    1 
ATOM   1322 C  CG    . LEU A 1 174 ? -0.388  13.726  16.105  1.00 37.51  ? 172 LEU A CG    1 
ATOM   1323 C  CD1   . LEU A 1 174 ? -1.299  14.703  15.359  1.00 39.62  ? 172 LEU A CD1   1 
ATOM   1324 C  CD2   . LEU A 1 174 ? 1.047   13.854  15.613  1.00 40.32  ? 172 LEU A CD2   1 
ATOM   1325 N  N     . ALA A 1 175 ? -0.160  12.670  20.866  1.00 36.82  ? 173 ALA A N     1 
ATOM   1326 C  CA    . ALA A 1 175 ? -0.234  12.991  22.300  1.00 41.95  ? 173 ALA A CA    1 
ATOM   1327 C  C     . ALA A 1 175 ? -1.235  14.132  22.547  1.00 45.00  ? 173 ALA A C     1 
ATOM   1328 O  O     . ALA A 1 175 ? -2.370  14.061  22.081  1.00 43.02  ? 173 ALA A O     1 
ATOM   1329 C  CB    . ALA A 1 175 ? 1.146   13.315  22.859  1.00 40.74  ? 173 ALA A CB    1 
ATOM   1330 N  N     . ARG A 1 176 ? -0.848  15.179  23.296  1.00 46.53  ? 174 ARG A N     1 
ATOM   1331 C  CA    . ARG A 1 176 ? -1.764  16.283  23.548  1.00 50.05  ? 174 ARG A CA    1 
ATOM   1332 C  C     . ARG A 1 176 ? -1.302  17.554  22.826  1.00 50.35  ? 174 ARG A C     1 
ATOM   1333 O  O     . ARG A 1 176 ? -1.752  18.639  23.148  1.00 53.99  ? 174 ARG A O     1 
ATOM   1334 C  CB    . ARG A 1 176 ? -1.971  16.447  25.061  1.00 51.96  ? 174 ARG A CB    1 
ATOM   1335 C  CG    . ARG A 1 176 ? -2.846  15.364  25.689  1.00 56.45  ? 174 ARG A CG    1 
ATOM   1336 C  CD    . ARG A 1 176 ? -3.337  15.700  27.095  1.00 57.02  ? 174 ARG A CD    1 
ATOM   1337 N  N     . THR A 1 177 ? -0.480  17.420  21.779  1.00 56.40  ? 175 THR A N     1 
ATOM   1338 C  CA    . THR A 1 177 ? 0.028   18.569  21.038  1.00 57.95  ? 175 THR A CA    1 
ATOM   1339 C  C     . THR A 1 177 ? -1.048  19.100  20.084  1.00 61.15  ? 175 THR A C     1 
ATOM   1340 O  O     . THR A 1 177 ? -2.040  18.427  19.804  1.00 55.35  ? 175 THR A O     1 
ATOM   1341 C  CB    . THR A 1 177 ? 1.305   18.196  20.269  1.00 60.39  ? 175 THR A CB    1 
ATOM   1342 O  OG1   . THR A 1 177 ? 0.959   17.495  19.070  1.00 63.09  ? 175 THR A OG1   1 
ATOM   1343 C  CG2   . THR A 1 177 ? 2.258   17.343  21.080  1.00 56.98  ? 175 THR A CG2   1 
ATOM   1344 N  N     . ALA A 1 178 ? -0.851  20.316  19.562  1.00 66.14  ? 176 ALA A N     1 
ATOM   1345 C  CA    . ALA A 1 178 ? -1.761  20.847  18.554  1.00 71.09  ? 176 ALA A CA    1 
ATOM   1346 C  C     . ALA A 1 178 ? -1.313  20.370  17.170  1.00 79.15  ? 176 ALA A C     1 
ATOM   1347 O  O     . ALA A 1 178 ? -0.174  20.620  16.760  1.00 83.38  ? 176 ALA A O     1 
ATOM   1348 C  CB    . ALA A 1 178 ? -1.834  22.355  18.633  1.00 66.31  ? 176 ALA A CB    1 
ATOM   1349 N  N     . GLY A 1 179 ? -2.230  19.684  16.466  1.00 76.75  ? 177 GLY A N     1 
ATOM   1350 C  CA    . GLY A 1 179 ? -2.001  19.176  15.119  1.00 75.64  ? 177 GLY A CA    1 
ATOM   1351 C  C     . GLY A 1 179 ? -1.916  20.262  14.041  1.00 73.86  ? 177 GLY A C     1 
ATOM   1352 O  O     . GLY A 1 179 ? -1.715  19.929  12.877  1.00 75.40  ? 177 GLY A O     1 
ATOM   1353 N  N     . THR A 1 180 ? -2.115  21.540  14.411  1.00 75.79  ? 178 THR A N     1 
ATOM   1354 C  CA    . THR A 1 180 ? -1.812  22.667  13.534  1.00 77.76  ? 178 THR A CA    1 
ATOM   1355 C  C     . THR A 1 180 ? -1.031  23.737  14.298  1.00 80.08  ? 178 THR A C     1 
ATOM   1356 O  O     . THR A 1 180 ? -1.302  24.929  14.164  1.00 82.20  ? 178 THR A O     1 
ATOM   1357 C  CB    . THR A 1 180 ? -3.070  23.308  12.928  1.00 77.69  ? 178 THR A CB    1 
ATOM   1358 O  OG1   . THR A 1 180 ? -3.768  23.980  13.974  1.00 81.90  ? 178 THR A OG1   1 
ATOM   1359 C  CG2   . THR A 1 180 ? -3.985  22.319  12.241  1.00 78.14  ? 178 THR A CG2   1 
ATOM   1360 N  N     . SER A 1 181 ? -0.066  23.310  15.117  1.00 85.94  ? 179 SER A N     1 
ATOM   1361 C  CA    . SER A 1 181 ? 0.887   24.245  15.691  1.00 89.20  ? 179 SER A CA    1 
ATOM   1362 C  C     . SER A 1 181 ? 2.228   24.055  14.992  1.00 83.10  ? 179 SER A C     1 
ATOM   1363 O  O     . SER A 1 181 ? 2.515   22.981  14.462  1.00 74.35  ? 179 SER A O     1 
ATOM   1364 C  CB    . SER A 1 181 ? 1.003   24.101  17.195  1.00 93.77  ? 179 SER A CB    1 
ATOM   1365 O  OG    . SER A 1 181 ? 1.434   22.799  17.567  1.00 97.22  ? 179 SER A OG    1 
ATOM   1366 N  N     . PHE A 1 182 ? 3.034   25.117  14.977  1.00 81.56  ? 180 PHE A N     1 
ATOM   1367 C  CA    . PHE A 1 182 ? 4.346   25.059  14.359  1.00 88.77  ? 180 PHE A CA    1 
ATOM   1368 C  C     . PHE A 1 182 ? 5.162   23.929  14.984  1.00 89.04  ? 180 PHE A C     1 
ATOM   1369 O  O     . PHE A 1 182 ? 5.131   23.731  16.201  1.00 86.72  ? 180 PHE A O     1 
ATOM   1370 C  CB    . PHE A 1 182 ? 5.070   26.395  14.520  1.00 89.00  ? 180 PHE A CB    1 
ATOM   1371 C  CG    . PHE A 1 182 ? 6.485   26.397  14.002  1.00 90.73  ? 180 PHE A CG    1 
ATOM   1372 C  CD1   . PHE A 1 182 ? 6.747   26.194  12.652  1.00 91.02  ? 180 PHE A CD1   1 
ATOM   1373 C  CD2   . PHE A 1 182 ? 7.559   26.583  14.865  1.00 88.19  ? 180 PHE A CD2   1 
ATOM   1374 C  CE1   . PHE A 1 182 ? 8.051   26.195  12.174  1.00 87.92  ? 180 PHE A CE1   1 
ATOM   1375 C  CE2   . PHE A 1 182 ? 8.861   26.587  14.385  1.00 89.55  ? 180 PHE A CE2   1 
ATOM   1376 C  CZ    . PHE A 1 182 ? 9.105   26.393  13.040  1.00 88.51  ? 180 PHE A CZ    1 
ATOM   1377 N  N     . MET A 1 183 ? 5.878   23.186  14.132  1.00 85.12  ? 181 MET A N     1 
ATOM   1378 C  CA    . MET A 1 183 ? 6.820   22.181  14.592  1.00 78.23  ? 181 MET A CA    1 
ATOM   1379 C  C     . MET A 1 183 ? 8.174   22.441  13.930  1.00 75.85  ? 181 MET A C     1 
ATOM   1380 O  O     . MET A 1 183 ? 8.303   22.341  12.709  1.00 70.09  ? 181 MET A O     1 
ATOM   1381 C  CB    . MET A 1 183 ? 6.317   20.775  14.258  1.00 77.53  ? 181 MET A CB    1 
ATOM   1382 C  CG    . MET A 1 183 ? 7.313   19.699  14.601  1.00 81.38  ? 181 MET A CG    1 
ATOM   1383 S  SD    . MET A 1 183 ? 6.532   18.258  15.362  1.00 87.61  ? 181 MET A SD    1 
ATOM   1384 C  CE    . MET A 1 183 ? 7.975   17.444  16.059  1.00 75.95  ? 181 MET A CE    1 
ATOM   1385 N  N     . MET A 1 184 ? 9.167   22.819  14.746  1.00 72.26  ? 182 MET A N     1 
ATOM   1386 C  CA    . MET A 1 184 ? 10.531  22.951  14.263  1.00 74.09  ? 182 MET A CA    1 
ATOM   1387 C  C     . MET A 1 184 ? 11.027  21.560  13.886  1.00 70.32  ? 182 MET A C     1 
ATOM   1388 O  O     . MET A 1 184 ? 11.184  20.708  14.755  1.00 70.01  ? 182 MET A O     1 
ATOM   1389 C  CB    . MET A 1 184 ? 11.468  23.562  15.313  1.00 73.80  ? 182 MET A CB    1 
ATOM   1390 C  CG    . MET A 1 184 ? 11.874  24.977  14.997  1.00 82.25  ? 182 MET A CG    1 
ATOM   1391 S  SD    . MET A 1 184 ? 12.716  25.168  13.403  1.00 92.32  ? 182 MET A SD    1 
ATOM   1392 C  CE    . MET A 1 184 ? 14.274  24.340  13.721  1.00 92.90  ? 182 MET A CE    1 
ATOM   1393 N  N     . THR A 1 185 ? 11.224  21.332  12.583  1.00 66.15  ? 183 THR A N     1 
ATOM   1394 C  CA    . THR A 1 185 ? 11.750  20.069  12.089  1.00 56.91  ? 183 THR A CA    1 
ATOM   1395 C  C     . THR A 1 185 ? 12.177  20.245  10.635  1.00 50.01  ? 183 THR A C     1 
ATOM   1396 O  O     . THR A 1 185 ? 11.533  20.962  9.884   1.00 46.16  ? 183 THR A O     1 
ATOM   1397 C  CB    . THR A 1 185 ? 10.722  18.933  12.195  1.00 53.48  ? 183 THR A CB    1 
ATOM   1398 O  OG1   . THR A 1 185 ? 11.273  17.776  11.562  1.00 49.02  ? 183 THR A OG1   1 
ATOM   1399 C  CG2   . THR A 1 185 ? 9.398   19.291  11.563  1.00 53.61  ? 183 THR A CG2   1 
ATOM   1400 N  N     . PRO A 1 186 ? 13.274  19.605  10.195  1.00 50.66  ? 184 PRO A N     1 
ATOM   1401 C  CA    . PRO A 1 186 ? 13.670  19.668  8.790   1.00 47.82  ? 184 PRO A CA    1 
ATOM   1402 C  C     . PRO A 1 186 ? 12.931  18.686  7.880   1.00 39.66  ? 184 PRO A C     1 
ATOM   1403 O  O     . PRO A 1 186 ? 12.987  18.850  6.671   1.00 40.14  ? 184 PRO A O     1 
ATOM   1404 C  CB    . PRO A 1 186 ? 15.171  19.354  8.832   1.00 50.54  ? 184 PRO A CB    1 
ATOM   1405 C  CG    . PRO A 1 186 ? 15.359  18.497  10.069  1.00 55.10  ? 184 PRO A CG    1 
ATOM   1406 C  CD    . PRO A 1 186 ? 14.214  18.828  11.015  1.00 55.37  ? 184 PRO A CD    1 
ATOM   1407 N  N     . TYR A 1 187 ? 12.187  17.726  8.449   1.00 36.29  ? 185 TYR A N     1 
ATOM   1408 C  CA    . TYR A 1 187 ? 11.699  16.587  7.680   1.00 34.20  ? 185 TYR A CA    1 
ATOM   1409 C  C     . TYR A 1 187 ? 10.277  16.838  7.189   1.00 34.80  ? 185 TYR A C     1 
ATOM   1410 O  O     . TYR A 1 187 ? 9.487   17.543  7.826   1.00 33.40  ? 185 TYR A O     1 
ATOM   1411 C  CB    . TYR A 1 187 ? 11.795  15.271  8.466   1.00 36.98  ? 185 TYR A CB    1 
ATOM   1412 C  CG    . TYR A 1 187 ? 13.227  14.951  8.881   1.00 41.62  ? 185 TYR A CG    1 
ATOM   1413 C  CD1   . TYR A 1 187 ? 14.157  14.423  7.990   1.00 38.61  ? 185 TYR A CD1   1 
ATOM   1414 C  CD2   . TYR A 1 187 ? 13.675  15.263  10.161  1.00 46.80  ? 185 TYR A CD2   1 
ATOM   1415 C  CE1   . TYR A 1 187 ? 15.466  14.169  8.373   1.00 40.52  ? 185 TYR A CE1   1 
ATOM   1416 C  CE2   . TYR A 1 187 ? 14.984  15.021  10.553  1.00 47.48  ? 185 TYR A CE2   1 
ATOM   1417 C  CZ    . TYR A 1 187 ? 15.886  14.477  9.657   1.00 45.23  ? 185 TYR A CZ    1 
ATOM   1418 O  OH    . TYR A 1 187 ? 17.177  14.255  10.067  1.00 47.96  ? 185 TYR A OH    1 
ATOM   1419 N  N     . VAL A 1 188 ? 9.960   16.226  6.042   1.00 31.50  ? 186 VAL A N     1 
ATOM   1420 C  CA    . VAL A 1 188 ? 8.604   16.223  5.530   1.00 33.20  ? 186 VAL A CA    1 
ATOM   1421 C  C     . VAL A 1 188 ? 7.695   15.506  6.528   1.00 34.41  ? 186 VAL A C     1 
ATOM   1422 O  O     . VAL A 1 188 ? 8.077   14.509  7.118   1.00 36.53  ? 186 VAL A O     1 
ATOM   1423 C  CB    . VAL A 1 188 ? 8.550   15.547  4.149   1.00 35.68  ? 186 VAL A CB    1 
ATOM   1424 C  CG1   . VAL A 1 188 ? 7.116   15.317  3.691   1.00 38.65  ? 186 VAL A CG1   1 
ATOM   1425 C  CG2   . VAL A 1 188 ? 9.337   16.338  3.110   1.00 36.94  ? 186 VAL A CG2   1 
ATOM   1426 N  N     . VAL A 1 189 ? 6.467   15.998  6.677   1.00 35.84  ? 187 VAL A N     1 
ATOM   1427 C  CA    . VAL A 1 189 ? 5.471   15.373  7.539   1.00 36.38  ? 187 VAL A CA    1 
ATOM   1428 C  C     . VAL A 1 189 ? 4.291   15.010  6.650   1.00 34.99  ? 187 VAL A C     1 
ATOM   1429 O  O     . VAL A 1 189 ? 3.738   15.888  5.998   1.00 37.92  ? 187 VAL A O     1 
ATOM   1430 C  CB    . VAL A 1 189 ? 5.069   16.292  8.715   1.00 43.63  ? 187 VAL A CB    1 
ATOM   1431 C  CG1   . VAL A 1 189 ? 4.966   17.748  8.298   1.00 50.67  ? 187 VAL A CG1   1 
ATOM   1432 C  CG2   . VAL A 1 189 ? 3.784   15.837  9.394   1.00 43.22  ? 187 VAL A CG2   1 
ATOM   1433 N  N     . THR A 1 190 ? 3.972   13.716  6.562   1.00 31.31  ? 188 THR A N     1 
ATOM   1434 C  CA    . THR A 1 190 ? 2.895   13.234  5.712   1.00 33.67  ? 188 THR A CA    1 
ATOM   1435 C  C     . THR A 1 190 ? 1.555   13.559  6.368   1.00 32.98  ? 188 THR A C     1 
ATOM   1436 O  O     . THR A 1 190 ? 1.327   13.127  7.490   1.00 29.87  ? 188 THR A O     1 
ATOM   1437 C  CB    . THR A 1 190 ? 3.046   11.722  5.530   1.00 37.10  ? 188 THR A CB    1 
ATOM   1438 O  OG1   . THR A 1 190 ? 4.308   11.520  4.906   1.00 39.91  ? 188 THR A OG1   1 
ATOM   1439 C  CG2   . THR A 1 190 ? 1.973   11.076  4.680   1.00 37.62  ? 188 THR A CG2   1 
ATOM   1440 N  N     . ARG A 1 191 ? 0.662   14.278  5.666   1.00 31.51  ? 189 ARG A N     1 
ATOM   1441 C  CA    . ARG A 1 191 ? -0.602  14.702  6.253   1.00 28.94  ? 189 ARG A CA    1 
ATOM   1442 C  C     . ARG A 1 191 ? -1.820  14.068  5.577   1.00 26.65  ? 189 ARG A C     1 
ATOM   1443 O  O     . ARG A 1 191 ? -2.944  14.340  5.990   1.00 27.97  ? 189 ARG A O     1 
ATOM   1444 C  CB    . ARG A 1 191 ? -0.677  16.231  6.236   1.00 31.79  ? 189 ARG A CB    1 
ATOM   1445 C  CG    . ARG A 1 191 ? 0.364   16.854  7.161   1.00 37.10  ? 189 ARG A CG    1 
ATOM   1446 C  CD    . ARG A 1 191 ? 0.491   18.360  7.057   1.00 44.18  ? 189 ARG A CD    1 
ATOM   1447 N  NE    . ARG A 1 191 ? 1.704   18.845  7.750   1.00 52.88  ? 189 ARG A NE    1 
ATOM   1448 C  CZ    . ARG A 1 191 ? 1.733   19.568  8.871   1.00 57.71  ? 189 ARG A CZ    1 
ATOM   1449 N  NH1   . ARG A 1 191 ? 0.626   20.079  9.392   1.00 66.29  ? 189 ARG A NH1   1 
ATOM   1450 N  NH2   . ARG A 1 191 ? 2.891   19.807  9.464   1.00 57.50  ? 189 ARG A NH2   1 
ATOM   1451 N  N     . TYR A 1 192 ? -1.605  13.165  4.619   1.00 26.61  ? 190 TYR A N     1 
ATOM   1452 C  CA    . TYR A 1 192 ? -2.672  12.621  3.777   1.00 25.95  ? 190 TYR A CA    1 
ATOM   1453 C  C     . TYR A 1 192 ? -3.749  11.864  4.578   1.00 27.05  ? 190 TYR A C     1 
ATOM   1454 O  O     . TYR A 1 192 ? -4.866  11.706  4.072   1.00 24.46  ? 190 TYR A O     1 
ATOM   1455 C  CB    . TYR A 1 192 ? -2.085  11.671  2.732   1.00 24.19  ? 190 TYR A CB    1 
ATOM   1456 C  CG    . TYR A 1 192 ? -0.924  12.183  1.893   1.00 28.71  ? 190 TYR A CG    1 
ATOM   1457 C  CD1   . TYR A 1 192 ? -0.839  13.511  1.488   1.00 30.95  ? 190 TYR A CD1   1 
ATOM   1458 C  CD2   . TYR A 1 192 ? 0.068   11.306  1.466   1.00 29.16  ? 190 TYR A CD2   1 
ATOM   1459 C  CE1   . TYR A 1 192 ? 0.210   13.951  0.699   1.00 33.48  ? 190 TYR A CE1   1 
ATOM   1460 C  CE2   . TYR A 1 192 ? 1.125   11.735  0.691   1.00 32.53  ? 190 TYR A CE2   1 
ATOM   1461 C  CZ    . TYR A 1 192 ? 1.188   13.059  0.305   1.00 33.22  ? 190 TYR A CZ    1 
ATOM   1462 O  OH    . TYR A 1 192 ? 2.209   13.464  -0.475  1.00 41.17  ? 190 TYR A OH    1 
ATOM   1463 N  N     . TYR A 1 193 ? -3.413  11.351  5.780   1.00 22.71  ? 191 TYR A N     1 
ATOM   1464 C  CA    . TYR A 1 193 ? -4.302  10.461  6.535   1.00 21.91  ? 191 TYR A CA    1 
ATOM   1465 C  C     . TYR A 1 193 ? -4.929  11.132  7.767   1.00 22.57  ? 191 TYR A C     1 
ATOM   1466 O  O     . TYR A 1 193 ? -5.670  10.475  8.527   1.00 21.83  ? 191 TYR A O     1 
ATOM   1467 C  CB    . TYR A 1 193 ? -3.492  9.211   6.929   1.00 21.59  ? 191 TYR A CB    1 
ATOM   1468 C  CG    . TYR A 1 193 ? -2.807  8.545   5.737   1.00 21.93  ? 191 TYR A CG    1 
ATOM   1469 C  CD1   . TYR A 1 193 ? -3.469  7.628   4.919   1.00 23.38  ? 191 TYR A CD1   1 
ATOM   1470 C  CD2   . TYR A 1 193 ? -1.507  8.895   5.379   1.00 23.16  ? 191 TYR A CD2   1 
ATOM   1471 C  CE1   . TYR A 1 193 ? -2.871  7.087   3.784   1.00 22.81  ? 191 TYR A CE1   1 
ATOM   1472 C  CE2   . TYR A 1 193 ? -0.891  8.353   4.254   1.00 24.37  ? 191 TYR A CE2   1 
ATOM   1473 C  CZ    . TYR A 1 193 ? -1.578  7.437   3.458   1.00 22.55  ? 191 TYR A CZ    1 
ATOM   1474 O  OH    . TYR A 1 193 ? -0.994  6.915   2.337   1.00 24.69  ? 191 TYR A OH    1 
ATOM   1475 N  N     . ARG A 1 194 ? -4.598  12.405  8.002   1.00 22.73  ? 192 ARG A N     1 
ATOM   1476 C  CA    . ARG A 1 194 ? -5.065  13.138  9.178   1.00 24.90  ? 192 ARG A CA    1 
ATOM   1477 C  C     . ARG A 1 194 ? -6.527  13.541  8.997   1.00 22.68  ? 192 ARG A C     1 
ATOM   1478 O  O     . ARG A 1 194 ? -6.912  13.990  7.922   1.00 23.65  ? 192 ARG A O     1 
ATOM   1479 C  CB    . ARG A 1 194 ? -4.163  14.350  9.417   1.00 25.70  ? 192 ARG A CB    1 
ATOM   1480 C  CG    . ARG A 1 194 ? -2.802  13.914  9.924   1.00 27.51  ? 192 ARG A CG    1 
ATOM   1481 C  CD    . ARG A 1 194 ? -1.927  15.108  10.227  1.00 30.78  ? 192 ARG A CD    1 
ATOM   1482 N  NE    . ARG A 1 194 ? -0.635  14.654  10.680  1.00 28.98  ? 192 ARG A NE    1 
ATOM   1483 C  CZ    . ARG A 1 194 ? 0.290   15.433  11.209  1.00 32.74  ? 192 ARG A CZ    1 
ATOM   1484 N  NH1   . ARG A 1 194 ? 0.081   16.733  11.314  1.00 35.42  ? 192 ARG A NH1   1 
ATOM   1485 N  NH2   . ARG A 1 194 ? 1.415   14.898  11.655  1.00 30.47  ? 192 ARG A NH2   1 
ATOM   1486 N  N     . ALA A 1 195 ? -7.333  13.380  10.055  1.00 22.57  ? 193 ALA A N     1 
ATOM   1487 C  CA    . ALA A 1 195 ? -8.747  13.714  10.007  1.00 22.35  ? 193 ALA A CA    1 
ATOM   1488 C  C     . ALA A 1 195 ? -8.962  15.210  9.739   1.00 23.20  ? 193 ALA A C     1 
ATOM   1489 O  O     . ALA A 1 195 ? -8.139  16.050  10.115  1.00 23.27  ? 193 ALA A O     1 
ATOM   1490 C  CB    . ALA A 1 195 ? -9.383  13.342  11.326  1.00 22.98  ? 193 ALA A CB    1 
ATOM   1491 N  N     . PRO A 1 196 ? -10.115 15.611  9.157   1.00 21.98  ? 194 PRO A N     1 
ATOM   1492 C  CA    . PRO A 1 196 ? -10.463 17.029  9.059   1.00 22.51  ? 194 PRO A CA    1 
ATOM   1493 C  C     . PRO A 1 196 ? -10.274 17.803  10.357  1.00 25.08  ? 194 PRO A C     1 
ATOM   1494 O  O     . PRO A 1 196 ? -9.708  18.910  10.375  1.00 27.59  ? 194 PRO A O     1 
ATOM   1495 C  CB    . PRO A 1 196 ? -11.935 16.966  8.616   1.00 23.93  ? 194 PRO A CB    1 
ATOM   1496 C  CG    . PRO A 1 196 ? -12.019 15.705  7.806   1.00 23.49  ? 194 PRO A CG    1 
ATOM   1497 C  CD    . PRO A 1 196 ? -11.117 14.745  8.532   1.00 24.45  ? 194 PRO A CD    1 
ATOM   1498 N  N     . GLU A 1 197 ? -10.696 17.207  11.472  1.00 24.59  ? 195 GLU A N     1 
ATOM   1499 C  CA    . GLU A 1 197 ? -10.634 17.929  12.725  1.00 26.85  ? 195 GLU A CA    1 
ATOM   1500 C  C     . GLU A 1 197 ? -9.173  18.171  13.132  1.00 27.49  ? 195 GLU A C     1 
ATOM   1501 O  O     . GLU A 1 197 ? -8.868  19.148  13.801  1.00 29.23  ? 195 GLU A O     1 
ATOM   1502 C  CB    . GLU A 1 197 ? -11.444 17.210  13.819  1.00 28.11  ? 195 GLU A CB    1 
ATOM   1503 C  CG    . GLU A 1 197 ? -11.019 15.788  14.077  1.00 25.90  ? 195 GLU A CG    1 
ATOM   1504 C  CD    . GLU A 1 197 ? -11.871 14.772  13.317  1.00 25.91  ? 195 GLU A CD    1 
ATOM   1505 O  OE1   . GLU A 1 197 ? -12.333 15.075  12.170  1.00 24.55  ? 195 GLU A OE1   1 
ATOM   1506 O  OE2   . GLU A 1 197 ? -12.066 13.661  13.856  1.00 25.95  ? 195 GLU A OE2   1 
ATOM   1507 N  N     . VAL A 1 198 ? -8.246  17.332  12.691  1.00 26.52  ? 196 VAL A N     1 
ATOM   1508 C  CA    . VAL A 1 198 ? -6.844  17.584  12.960  1.00 28.07  ? 196 VAL A CA    1 
ATOM   1509 C  C     . VAL A 1 198 ? -6.334  18.708  12.053  1.00 30.25  ? 196 VAL A C     1 
ATOM   1510 O  O     . VAL A 1 198 ? -5.746  19.665  12.541  1.00 28.76  ? 196 VAL A O     1 
ATOM   1511 C  CB    . VAL A 1 198 ? -5.982  16.317  12.823  1.00 30.10  ? 196 VAL A CB    1 
ATOM   1512 C  CG1   . VAL A 1 198 ? -4.504  16.641  12.943  1.00 31.40  ? 196 VAL A CG1   1 
ATOM   1513 C  CG2   . VAL A 1 198 ? -6.375  15.246  13.837  1.00 27.86  ? 196 VAL A CG2   1 
ATOM   1514 N  N     . ILE A 1 199 ? -6.548  18.613  10.738  1.00 30.47  ? 197 ILE A N     1 
ATOM   1515 C  CA    . ILE A 1 199 ? -5.931  19.562  9.821   1.00 30.99  ? 197 ILE A CA    1 
ATOM   1516 C  C     . ILE A 1 199 ? -6.596  20.947  9.932   1.00 32.44  ? 197 ILE A C     1 
ATOM   1517 O  O     . ILE A 1 199 ? -5.940  21.936  9.648   1.00 36.20  ? 197 ILE A O     1 
ATOM   1518 C  CB    . ILE A 1 199 ? -5.894  19.050  8.368   1.00 31.66  ? 197 ILE A CB    1 
ATOM   1519 C  CG1   . ILE A 1 199 ? -7.307  18.939  7.790   1.00 31.52  ? 197 ILE A CG1   1 
ATOM   1520 C  CG2   . ILE A 1 199 ? -5.061  17.761  8.230   1.00 32.11  ? 197 ILE A CG2   1 
ATOM   1521 C  CD1   . ILE A 1 199 ? -7.375  18.576  6.303   1.00 35.70  ? 197 ILE A CD1   1 
ATOM   1522 N  N     . LEU A 1 200 ? -7.851  21.039  10.417  1.00 30.73  ? 198 LEU A N     1 
ATOM   1523 C  CA    . LEU A 1 200 ? -8.542  22.310  10.628  1.00 31.72  ? 198 LEU A CA    1 
ATOM   1524 C  C     . LEU A 1 200 ? -8.410  22.819  12.065  1.00 32.96  ? 198 LEU A C     1 
ATOM   1525 O  O     . LEU A 1 200 ? -8.952  23.873  12.396  1.00 36.97  ? 198 LEU A O     1 
ATOM   1526 C  CB    . LEU A 1 200 ? -10.018 22.157  10.256  1.00 31.27  ? 198 LEU A CB    1 
ATOM   1527 C  CG    . LEU A 1 200 ? -10.320 21.863  8.788   1.00 34.31  ? 198 LEU A CG    1 
ATOM   1528 C  CD1   . LEU A 1 200 ? -11.793 22.036  8.504   1.00 36.14  ? 198 LEU A CD1   1 
ATOM   1529 C  CD2   . LEU A 1 200 ? -9.515  22.758  7.861   1.00 37.41  ? 198 LEU A CD2   1 
ATOM   1530 N  N     . GLY A 1 201 ? -7.693  22.095  12.926  1.00 33.38  ? 199 GLY A N     1 
ATOM   1531 C  CA    . GLY A 1 201 ? -7.416  22.562  14.280  1.00 34.45  ? 199 GLY A CA    1 
ATOM   1532 C  C     . GLY A 1 201 ? -8.654  22.606  15.180  1.00 32.87  ? 199 GLY A C     1 
ATOM   1533 O  O     . GLY A 1 201 ? -8.854  23.571  15.912  1.00 33.62  ? 199 GLY A O     1 
ATOM   1534 N  N     . MET A 1 202 ? -9.442  21.524  15.167  1.00 31.00  ? 200 MET A N     1 
ATOM   1535 C  CA    . MET A 1 202 ? -10.713 21.442  15.876  1.00 32.54  ? 200 MET A CA    1 
ATOM   1536 C  C     . MET A 1 202 ? -10.540 20.491  17.052  1.00 33.87  ? 200 MET A C     1 
ATOM   1537 O  O     . MET A 1 202 ? -9.501  19.866  17.155  1.00 34.28  ? 200 MET A O     1 
ATOM   1538 C  CB    . MET A 1 202 ? -11.798 20.872  14.963  1.00 32.48  ? 200 MET A CB    1 
ATOM   1539 C  CG    . MET A 1 202 ? -11.961 21.631  13.655  1.00 34.38  ? 200 MET A CG    1 
ATOM   1540 S  SD    . MET A 1 202 ? -13.178 20.821  12.608  1.00 35.95  ? 200 MET A SD    1 
ATOM   1541 C  CE    . MET A 1 202 ? -14.629 21.205  13.591  1.00 39.49  ? 200 MET A CE    1 
ATOM   1542 N  N     . GLY A 1 203 ? -11.571 20.372  17.898  1.00 34.55  ? 201 GLY A N     1 
ATOM   1543 C  CA    . GLY A 1 203 ? -11.583 19.356  18.933  1.00 33.74  ? 201 GLY A CA    1 
ATOM   1544 C  C     . GLY A 1 203 ? -11.713 17.973  18.299  1.00 31.81  ? 201 GLY A C     1 
ATOM   1545 O  O     . GLY A 1 203 ? -12.150 17.825  17.154  1.00 31.74  ? 201 GLY A O     1 
ATOM   1546 N  N     . TYR A 1 204 ? -11.351 16.945  19.054  1.00 31.39  ? 202 TYR A N     1 
ATOM   1547 C  CA    . TYR A 1 204 ? -11.431 15.596  18.522  1.00 29.76  ? 202 TYR A CA    1 
ATOM   1548 C  C     . TYR A 1 204 ? -11.796 14.617  19.629  1.00 29.34  ? 202 TYR A C     1 
ATOM   1549 O  O     . TYR A 1 204 ? -11.721 14.938  20.802  1.00 29.90  ? 202 TYR A O     1 
ATOM   1550 C  CB    . TYR A 1 204 ? -10.117 15.180  17.853  1.00 25.96  ? 202 TYR A CB    1 
ATOM   1551 C  CG    . TYR A 1 204 ? -8.951  15.109  18.821  1.00 27.21  ? 202 TYR A CG    1 
ATOM   1552 C  CD1   . TYR A 1 204 ? -8.263  16.254  19.217  1.00 31.37  ? 202 TYR A CD1   1 
ATOM   1553 C  CD2   . TYR A 1 204 ? -8.598  13.910  19.425  1.00 27.16  ? 202 TYR A CD2   1 
ATOM   1554 C  CE1   . TYR A 1 204 ? -7.216  16.191  20.125  1.00 33.66  ? 202 TYR A CE1   1 
ATOM   1555 C  CE2   . TYR A 1 204 ? -7.567  13.835  20.342  1.00 30.86  ? 202 TYR A CE2   1 
ATOM   1556 C  CZ    . TYR A 1 204 ? -6.875  14.976  20.695  1.00 35.12  ? 202 TYR A CZ    1 
ATOM   1557 O  OH    . TYR A 1 204 ? -5.831  14.862  21.566  1.00 35.41  ? 202 TYR A OH    1 
ATOM   1558 N  N     . LYS A 1 205 ? -12.144 13.405  19.205  1.00 27.80  ? 203 LYS A N     1 
ATOM   1559 C  CA    . LYS A 1 205 ? -12.443 12.300  20.097  1.00 28.40  ? 203 LYS A CA    1 
ATOM   1560 C  C     . LYS A 1 205 ? -11.853 11.037  19.474  1.00 27.43  ? 203 LYS A C     1 
ATOM   1561 O  O     . LYS A 1 205 ? -11.136 11.113  18.492  1.00 25.35  ? 203 LYS A O     1 
ATOM   1562 C  CB    . LYS A 1 205 ? -13.950 12.192  20.310  1.00 29.16  ? 203 LYS A CB    1 
ATOM   1563 C  CG    . LYS A 1 205 ? -14.762 11.769  19.091  1.00 32.63  ? 203 LYS A CG    1 
ATOM   1564 C  CD    . LYS A 1 205 ? -16.250 11.671  19.401  1.00 34.50  ? 203 LYS A CD    1 
ATOM   1565 C  CE    . LYS A 1 205 ? -17.046 11.243  18.192  1.00 35.45  ? 203 LYS A CE    1 
ATOM   1566 N  NZ    . LYS A 1 205 ? -18.484 11.214  18.518  1.00 41.89  ? 203 LYS A NZ    1 
ATOM   1567 N  N     . GLU A 1 206 ? -12.155 9.875   20.051  1.00 27.43  ? 204 GLU A N     1 
ATOM   1568 C  CA    . GLU A 1 206 ? -11.516 8.629   19.644  1.00 25.89  ? 204 GLU A CA    1 
ATOM   1569 C  C     . GLU A 1 206 ? -11.613 8.380   18.139  1.00 22.34  ? 204 GLU A C     1 
ATOM   1570 O  O     . GLU A 1 206 ? -10.662 7.885   17.536  1.00 22.68  ? 204 GLU A O     1 
ATOM   1571 C  CB    . GLU A 1 206 ? -12.115 7.438   20.421  1.00 26.19  ? 204 GLU A CB    1 
ATOM   1572 C  CG    . GLU A 1 206 ? -11.567 7.294   21.824  1.00 30.42  ? 204 GLU A CG    1 
ATOM   1573 C  CD    . GLU A 1 206 ? -12.094 8.283   22.836  1.00 36.09  ? 204 GLU A CD    1 
ATOM   1574 O  OE1   . GLU A 1 206 ? -12.891 9.180   22.467  1.00 38.41  ? 204 GLU A OE1   1 
ATOM   1575 O  OE2   . GLU A 1 206 ? -11.704 8.142   23.995  1.00 45.40  ? 204 GLU A OE2   1 
ATOM   1576 N  N     . ASN A 1 207 ? -12.753 8.668   17.501  1.00 22.66  ? 205 ASN A N     1 
ATOM   1577 C  CA    . ASN A 1 207 ? -12.933 8.265   16.117  1.00 22.95  ? 205 ASN A CA    1 
ATOM   1578 C  C     . ASN A 1 207 ? -12.162 9.172   15.145  1.00 23.61  ? 205 ASN A C     1 
ATOM   1579 O  O     . ASN A 1 207 ? -12.280 8.993   13.936  1.00 21.63  ? 205 ASN A O     1 
ATOM   1580 C  CB    . ASN A 1 207 ? -14.416 8.192   15.721  1.00 22.51  ? 205 ASN A CB    1 
ATOM   1581 C  CG    . ASN A 1 207 ? -15.138 9.521   15.696  1.00 24.33  ? 205 ASN A CG    1 
ATOM   1582 O  OD1   . ASN A 1 207 ? -14.582 10.560  16.032  1.00 25.87  ? 205 ASN A OD1   1 
ATOM   1583 N  ND2   . ASN A 1 207 ? -16.388 9.509   15.283  1.00 25.00  ? 205 ASN A ND2   1 
ATOM   1584 N  N     . VAL A 1 208 ? -11.371 10.133  15.650  1.00 23.15  ? 206 VAL A N     1 
ATOM   1585 C  CA    . VAL A 1 208 ? -10.380 10.788  14.812  1.00 22.32  ? 206 VAL A CA    1 
ATOM   1586 C  C     . VAL A 1 208 ? -9.559  9.718   14.069  1.00 22.91  ? 206 VAL A C     1 
ATOM   1587 O  O     . VAL A 1 208 ? -9.180  9.884   12.904  1.00 22.95  ? 206 VAL A O     1 
ATOM   1588 C  CB    . VAL A 1 208 ? -9.504  11.745  15.643  1.00 21.74  ? 206 VAL A CB    1 
ATOM   1589 C  CG1   . VAL A 1 208 ? -8.551  10.951  16.526  1.00 23.42  ? 206 VAL A CG1   1 
ATOM   1590 C  CG2   . VAL A 1 208 ? -8.747  12.742  14.785  1.00 22.08  ? 206 VAL A CG2   1 
ATOM   1591 N  N     . ASP A 1 209 ? -9.299  8.569   14.725  1.00 20.03  ? 207 ASP A N     1 
ATOM   1592 C  CA    . ASP A 1 209 ? -8.432  7.548   14.150  1.00 18.69  ? 207 ASP A CA    1 
ATOM   1593 C  C     . ASP A 1 209 ? -9.164  6.742   13.086  1.00 20.36  ? 207 ASP A C     1 
ATOM   1594 O  O     . ASP A 1 209 ? -8.528  6.131   12.233  1.00 19.28  ? 207 ASP A O     1 
ATOM   1595 C  CB    . ASP A 1 209 ? -7.870  6.631   15.242  1.00 19.88  ? 207 ASP A CB    1 
ATOM   1596 C  CG    . ASP A 1 209 ? -6.816  7.322   16.089  1.00 21.21  ? 207 ASP A CG    1 
ATOM   1597 O  OD1   . ASP A 1 209 ? -6.073  8.153   15.514  1.00 20.30  ? 207 ASP A OD1   1 
ATOM   1598 O  OD2   . ASP A 1 209 ? -6.699  6.993   17.289  1.00 22.05  ? 207 ASP A OD2   1 
ATOM   1599 N  N     . ILE A 1 210 ? -10.496 6.747   13.127  1.00 18.52  ? 208 ILE A N     1 
ATOM   1600 C  CA    . ILE A 1 210 ? -11.294 6.059   12.126  1.00 20.22  ? 208 ILE A CA    1 
ATOM   1601 C  C     . ILE A 1 210 ? -11.122 6.704   10.754  1.00 22.05  ? 208 ILE A C     1 
ATOM   1602 O  O     . ILE A 1 210 ? -11.121 5.988   9.750   1.00 21.39  ? 208 ILE A O     1 
ATOM   1603 C  CB    . ILE A 1 210 ? -12.776 5.959   12.555  1.00 20.93  ? 208 ILE A CB    1 
ATOM   1604 C  CG1   . ILE A 1 210 ? -12.973 4.859   13.603  1.00 21.61  ? 208 ILE A CG1   1 
ATOM   1605 C  CG2   . ILE A 1 210 ? -13.686 5.743   11.351  1.00 19.99  ? 208 ILE A CG2   1 
ATOM   1606 C  CD1   . ILE A 1 210 ? -12.864 3.464   13.033  1.00 23.80  ? 208 ILE A CD1   1 
ATOM   1607 N  N     . TRP A 1 211 ? -11.015 8.042   10.697  1.00 18.59  ? 209 TRP A N     1 
ATOM   1608 C  CA    . TRP A 1 211 ? -10.782 8.707   9.431   1.00 18.82  ? 209 TRP A CA    1 
ATOM   1609 C  C     . TRP A 1 211 ? -9.554  8.120   8.745   1.00 20.25  ? 209 TRP A C     1 
ATOM   1610 O  O     . TRP A 1 211 ? -9.602  7.805   7.551   1.00 19.05  ? 209 TRP A O     1 
ATOM   1611 C  CB    . TRP A 1 211 ? -10.599 10.221  9.601   1.00 20.27  ? 209 TRP A CB    1 
ATOM   1612 C  CG    . TRP A 1 211 ? -10.270 10.937  8.322   1.00 22.12  ? 209 TRP A CG    1 
ATOM   1613 C  CD1   . TRP A 1 211 ? -9.037  11.151  7.786   1.00 22.48  ? 209 TRP A CD1   1 
ATOM   1614 C  CD2   . TRP A 1 211 ? -11.215 11.477  7.377   1.00 23.59  ? 209 TRP A CD2   1 
ATOM   1615 N  NE1   . TRP A 1 211 ? -9.143  11.823  6.595   1.00 23.27  ? 209 TRP A NE1   1 
ATOM   1616 C  CE2   . TRP A 1 211 ? -10.463 12.032  6.315   1.00 24.45  ? 209 TRP A CE2   1 
ATOM   1617 C  CE3   . TRP A 1 211 ? -12.611 11.571  7.335   1.00 24.02  ? 209 TRP A CE3   1 
ATOM   1618 C  CZ2   . TRP A 1 211 ? -11.059 12.668  5.234   1.00 25.74  ? 209 TRP A CZ2   1 
ATOM   1619 C  CZ3   . TRP A 1 211 ? -13.194 12.195  6.253   1.00 26.98  ? 209 TRP A CZ3   1 
ATOM   1620 C  CH2   . TRP A 1 211 ? -12.428 12.730  5.227   1.00 25.53  ? 209 TRP A CH2   1 
ATOM   1621 N  N     . SER A 1 212 ? -8.464  7.986   9.503   1.00 18.89  ? 210 SER A N     1 
ATOM   1622 C  CA    . SER A 1 212 ? -7.193  7.474   9.001   1.00 18.94  ? 210 SER A CA    1 
ATOM   1623 C  C     . SER A 1 212 ? -7.329  6.032   8.483   1.00 18.96  ? 210 SER A C     1 
ATOM   1624 O  O     . SER A 1 212 ? -6.803  5.675   7.440   1.00 19.01  ? 210 SER A O     1 
ATOM   1625 C  CB    . SER A 1 212 ? -6.124  7.584   10.086  1.00 18.40  ? 210 SER A CB    1 
ATOM   1626 O  OG    . SER A 1 212 ? -5.985  8.898   10.591  1.00 21.24  ? 210 SER A OG    1 
ATOM   1627 N  N     . VAL A 1 213 ? -8.085  5.195   9.181   1.00 19.49  ? 211 VAL A N     1 
ATOM   1628 C  CA    . VAL A 1 213 ? -8.356  3.826   8.746   1.00 20.01  ? 211 VAL A CA    1 
ATOM   1629 C  C     . VAL A 1 213 ? -9.096  3.868   7.408   1.00 19.32  ? 211 VAL A C     1 
ATOM   1630 O  O     . VAL A 1 213 ? -8.805  3.080   6.514   1.00 20.94  ? 211 VAL A O     1 
ATOM   1631 C  CB    . VAL A 1 213 ? -9.154  3.042   9.820   1.00 20.95  ? 211 VAL A CB    1 
ATOM   1632 C  CG1   . VAL A 1 213 ? -9.575  1.648   9.295   1.00 24.20  ? 211 VAL A CG1   1 
ATOM   1633 C  CG2   . VAL A 1 213 ? -8.373  2.898   11.145  1.00 19.61  ? 211 VAL A CG2   1 
ATOM   1634 N  N     . GLY A 1 214 ? -10.078 4.763   7.285   1.00 20.80  ? 212 GLY A N     1 
ATOM   1635 C  CA    . GLY A 1 214 ? -10.827 4.906   6.047   1.00 20.50  ? 212 GLY A CA    1 
ATOM   1636 C  C     . GLY A 1 214 ? -9.913  5.304   4.895   1.00 20.19  ? 212 GLY A C     1 
ATOM   1637 O  O     . GLY A 1 214 ? -10.024 4.774   3.789   1.00 21.80  ? 212 GLY A O     1 
ATOM   1638 N  N     . CYS A 1 215 ? -8.987  6.229   5.149   1.00 20.55  ? 213 CYS A N     1 
ATOM   1639 C  CA    . CYS A 1 215 ? -8.042  6.641   4.127   1.00 20.46  ? 213 CYS A CA    1 
ATOM   1640 C  C     . CYS A 1 215 ? -7.166  5.474   3.685   1.00 22.56  ? 213 CYS A C     1 
ATOM   1641 O  O     . CYS A 1 215 ? -6.880  5.321   2.491   1.00 23.18  ? 213 CYS A O     1 
ATOM   1642 C  CB    . CYS A 1 215 ? -7.138  7.767   4.614   1.00 20.75  ? 213 CYS A CB    1 
ATOM   1643 S  SG    . CYS A 1 215 ? -7.986  9.345   4.838   1.00 22.04  ? 213 CYS A SG    1 
ATOM   1644 N  N     . ILE A 1 216 ? -6.752  4.629   4.639   1.00 20.50  ? 214 ILE A N     1 
ATOM   1645 C  CA    . ILE A 1 216 ? -5.900  3.499   4.317   1.00 21.24  ? 214 ILE A CA    1 
ATOM   1646 C  C     . ILE A 1 216 ? -6.689  2.444   3.543   1.00 23.30  ? 214 ILE A C     1 
ATOM   1647 O  O     . ILE A 1 216 ? -6.188  1.899   2.552   1.00 22.78  ? 214 ILE A O     1 
ATOM   1648 C  CB    . ILE A 1 216 ? -5.229  2.953   5.585   1.00 21.53  ? 214 ILE A CB    1 
ATOM   1649 C  CG1   . ILE A 1 216 ? -4.204  3.965   6.098   1.00 21.91  ? 214 ILE A CG1   1 
ATOM   1650 C  CG2   . ILE A 1 216 ? -4.636  1.573   5.350   1.00 22.17  ? 214 ILE A CG2   1 
ATOM   1651 C  CD1   . ILE A 1 216 ? -3.683  3.659   7.476   1.00 22.82  ? 214 ILE A CD1   1 
ATOM   1652 N  N     . MET A 1 217 ? -7.928  2.196   3.982   1.00 22.29  ? 215 MET A N     1 
ATOM   1653 C  CA    . MET A 1 217 ? -8.782  1.240   3.305   1.00 23.36  ? 215 MET A CA    1 
ATOM   1654 C  C     . MET A 1 217 ? -9.029  1.685   1.863   1.00 23.81  ? 215 MET A C     1 
ATOM   1655 O  O     . MET A 1 217 ? -8.937  0.874   0.953   1.00 23.42  ? 215 MET A O     1 
ATOM   1656 C  CB    . MET A 1 217 ? -10.114 1.102   4.032   1.00 21.71  ? 215 MET A CB    1 
ATOM   1657 C  CG    . MET A 1 217 ? -11.079 0.158   3.367   1.00 24.10  ? 215 MET A CG    1 
ATOM   1658 S  SD    . MET A 1 217 ? -12.604 -0.005  4.379   1.00 24.19  ? 215 MET A SD    1 
ATOM   1659 C  CE    . MET A 1 217 ? -13.469 -1.284  3.465   1.00 25.67  ? 215 MET A CE    1 
ATOM   1660 N  N     . GLY A 1 218 ? -9.343  2.978   1.661   1.00 21.60  ? 216 GLY A N     1 
ATOM   1661 C  CA    . GLY A 1 218 ? -9.626  3.454   0.325   1.00 24.13  ? 216 GLY A CA    1 
ATOM   1662 C  C     . GLY A 1 218 ? -8.409  3.309   -0.573  1.00 24.65  ? 216 GLY A C     1 
ATOM   1663 O  O     . GLY A 1 218 ? -8.523  2.934   -1.737  1.00 27.58  ? 216 GLY A O     1 
ATOM   1664 N  N     . GLU A 1 219 ? -7.233  3.569   -0.012  1.00 23.26  ? 217 GLU A N     1 
ATOM   1665 C  CA    . GLU A 1 219 ? -5.988  3.423   -0.755  1.00 24.93  ? 217 GLU A CA    1 
ATOM   1666 C  C     . GLU A 1 219 ? -5.714  1.956   -1.119  1.00 25.28  ? 217 GLU A C     1 
ATOM   1667 O  O     . GLU A 1 219 ? -5.249  1.665   -2.216  1.00 26.36  ? 217 GLU A O     1 
ATOM   1668 C  CB    . GLU A 1 219 ? -4.853  4.021   0.080   1.00 25.84  ? 217 GLU A CB    1 
ATOM   1669 C  CG    . GLU A 1 219 ? -3.505  3.993   -0.596  1.00 29.71  ? 217 GLU A CG    1 
ATOM   1670 C  CD    . GLU A 1 219 ? -2.458  4.802   0.133   1.00 31.32  ? 217 GLU A CD    1 
ATOM   1671 O  OE1   . GLU A 1 219 ? -2.843  5.585   1.039   1.00 28.31  ? 217 GLU A OE1   1 
ATOM   1672 O  OE2   . GLU A 1 219 ? -1.279  4.670   -0.220  1.00 28.66  ? 217 GLU A OE2   1 
ATOM   1673 N  N     . MET A 1 220 ? -5.981  1.039   -0.185  1.00 24.70  ? 218 MET A N     1 
ATOM   1674 C  CA    . MET A 1 220 ? -5.831  -0.395  -0.427  1.00 27.70  ? 218 MET A CA    1 
ATOM   1675 C  C     . MET A 1 220 ? -6.619  -0.831  -1.661  1.00 27.97  ? 218 MET A C     1 
ATOM   1676 O  O     . MET A 1 220 ? -6.139  -1.636  -2.449  1.00 29.57  ? 218 MET A O     1 
ATOM   1677 C  CB    . MET A 1 220 ? -6.363  -1.227  0.746   1.00 28.34  ? 218 MET A CB    1 
ATOM   1678 C  CG    . MET A 1 220 ? -5.516  -1.257  1.946   1.00 33.72  ? 218 MET A CG    1 
ATOM   1679 S  SD    . MET A 1 220 ? -6.341  -2.332  3.178   1.00 38.25  ? 218 MET A SD    1 
ATOM   1680 C  CE    . MET A 1 220 ? -4.916  -2.600  4.227   1.00 43.52  ? 218 MET A CE    1 
ATOM   1681 N  N     . ILE A 1 221 ? -7.834  -0.295  -1.803  1.00 29.57  ? 219 ILE A N     1 
ATOM   1682 C  CA    . ILE A 1 221 ? -8.727  -0.601  -2.907  1.00 30.85  ? 219 ILE A CA    1 
ATOM   1683 C  C     . ILE A 1 221 ? -8.259  0.073   -4.202  1.00 32.53  ? 219 ILE A C     1 
ATOM   1684 O  O     . ILE A 1 221 ? -8.109  -0.581  -5.236  1.00 32.09  ? 219 ILE A O     1 
ATOM   1685 C  CB    . ILE A 1 221 ? -10.164 -0.194  -2.520  1.00 30.40  ? 219 ILE A CB    1 
ATOM   1686 C  CG1   . ILE A 1 221 ? -10.687 -1.070  -1.368  1.00 30.71  ? 219 ILE A CG1   1 
ATOM   1687 C  CG2   . ILE A 1 221 ? -11.099 -0.246  -3.726  1.00 31.60  ? 219 ILE A CG2   1 
ATOM   1688 C  CD1   . ILE A 1 221 ? -11.858 -0.477  -0.611  1.00 28.20  ? 219 ILE A CD1   1 
ATOM   1689 N  N     . LYS A 1 222 ? -8.049  1.386   -4.151  1.00 32.46  ? 220 LYS A N     1 
ATOM   1690 C  CA    . LYS A 1 222 ? -7.780  2.161   -5.347  1.00 34.24  ? 220 LYS A CA    1 
ATOM   1691 C  C     . LYS A 1 222 ? -6.343  2.008   -5.831  1.00 35.35  ? 220 LYS A C     1 
ATOM   1692 O  O     . LYS A 1 222 ? -6.101  2.120   -7.023  1.00 36.96  ? 220 LYS A O     1 
ATOM   1693 C  CB    . LYS A 1 222 ? -8.113  3.627   -5.087  1.00 37.35  ? 220 LYS A CB    1 
ATOM   1694 C  CG    . LYS A 1 222 ? -9.585  3.841   -4.785  1.00 42.57  ? 220 LYS A CG    1 
ATOM   1695 C  CD    . LYS A 1 222 ? -10.077 5.269   -4.925  1.00 43.83  ? 220 LYS A CD    1 
ATOM   1696 C  CE    . LYS A 1 222 ? -10.364 5.627   -6.363  1.00 42.29  ? 220 LYS A CE    1 
ATOM   1697 N  NZ    . LYS A 1 222 ? -11.226 6.834   -6.485  1.00 43.95  ? 220 LYS A NZ    1 
ATOM   1698 N  N     . GLY A 1 223 ? -5.382  1.784   -4.926  1.00 36.30  ? 221 GLY A N     1 
ATOM   1699 C  CA    . GLY A 1 223 ? -3.987  1.682   -5.323  1.00 36.54  ? 221 GLY A CA    1 
ATOM   1700 C  C     . GLY A 1 223 ? -3.248  3.021   -5.340  1.00 40.90  ? 221 GLY A C     1 
ATOM   1701 O  O     . GLY A 1 223 ? -2.129  3.087   -5.813  1.00 47.84  ? 221 GLY A O     1 
ATOM   1702 N  N     . GLY A 1 224 ? -3.867  4.099   -4.859  1.00 37.03  ? 222 GLY A N     1 
ATOM   1703 C  CA    . GLY A 1 224 ? -3.172  5.369   -4.714  1.00 35.97  ? 222 GLY A CA    1 
ATOM   1704 C  C     . GLY A 1 224 ? -3.738  6.130   -3.527  1.00 34.44  ? 222 GLY A C     1 
ATOM   1705 O  O     . GLY A 1 224 ? -4.803  5.762   -3.033  1.00 31.62  ? 222 GLY A O     1 
ATOM   1706 N  N     . VAL A 1 225 ? -2.998  7.141   -3.051  1.00 31.95  ? 223 VAL A N     1 
ATOM   1707 C  CA    . VAL A 1 225 ? -3.418  7.935   -1.909  1.00 30.09  ? 223 VAL A CA    1 
ATOM   1708 C  C     . VAL A 1 225 ? -4.738  8.611   -2.239  1.00 28.69  ? 223 VAL A C     1 
ATOM   1709 O  O     . VAL A 1 225 ? -4.868  9.185   -3.312  1.00 29.64  ? 223 VAL A O     1 
ATOM   1710 C  CB    . VAL A 1 225 ? -2.341  8.977   -1.567  1.00 29.75  ? 223 VAL A CB    1 
ATOM   1711 C  CG1   . VAL A 1 225 ? -2.829  9.977   -0.528  1.00 27.55  ? 223 VAL A CG1   1 
ATOM   1712 C  CG2   . VAL A 1 225 ? -1.039  8.326   -1.133  1.00 30.37  ? 223 VAL A CG2   1 
ATOM   1713 N  N     . LEU A 1 226 ? -5.696  8.605   -1.312  1.00 25.02  ? 224 LEU A N     1 
ATOM   1714 C  CA    . LEU A 1 226 ? -7.012  9.184   -1.612  1.00 27.62  ? 224 LEU A CA    1 
ATOM   1715 C  C     . LEU A 1 226 ? -6.971  10.710  -1.676  1.00 28.21  ? 224 LEU A C     1 
ATOM   1716 O  O     . LEU A 1 226 ? -7.605  11.311  -2.541  1.00 30.78  ? 224 LEU A O     1 
ATOM   1717 C  CB    . LEU A 1 226 ? -8.029  8.856   -0.513  1.00 26.87  ? 224 LEU A CB    1 
ATOM   1718 C  CG    . LEU A 1 226 ? -8.633  7.469   -0.414  1.00 29.61  ? 224 LEU A CG    1 
ATOM   1719 C  CD1   . LEU A 1 226 ? -9.837  7.591   0.509   1.00 30.35  ? 224 LEU A CD1   1 
ATOM   1720 C  CD2   . LEU A 1 226 ? -8.998  6.873   -1.785  1.00 32.57  ? 224 LEU A CD2   1 
ATOM   1721 N  N     . PHE A 1 227 ? -6.282  11.336  -0.718  1.00 27.66  ? 225 PHE A N     1 
ATOM   1722 C  CA    . PHE A 1 227 ? -6.288  12.790  -0.569  1.00 28.77  ? 225 PHE A CA    1 
ATOM   1723 C  C     . PHE A 1 227 ? -4.844  13.292  -0.530  1.00 32.03  ? 225 PHE A C     1 
ATOM   1724 O  O     . PHE A 1 227 ? -4.312  13.660  0.512   1.00 33.61  ? 225 PHE A O     1 
ATOM   1725 C  CB    . PHE A 1 227 ? -7.075  13.197  0.675   1.00 28.87  ? 225 PHE A CB    1 
ATOM   1726 C  CG    . PHE A 1 227 ? -8.456  12.601  0.789   1.00 27.91  ? 225 PHE A CG    1 
ATOM   1727 C  CD1   . PHE A 1 227 ? -9.443  12.901  -0.136  1.00 31.01  ? 225 PHE A CD1   1 
ATOM   1728 C  CD2   . PHE A 1 227 ? -8.772  11.741  1.829   1.00 30.10  ? 225 PHE A CD2   1 
ATOM   1729 C  CE1   . PHE A 1 227 ? -10.715 12.354  -0.026  1.00 30.43  ? 225 PHE A CE1   1 
ATOM   1730 C  CE2   . PHE A 1 227 ? -10.044 11.192  1.945   1.00 30.33  ? 225 PHE A CE2   1 
ATOM   1731 C  CZ    . PHE A 1 227 ? -11.014 11.504  1.016   1.00 30.61  ? 225 PHE A CZ    1 
ATOM   1732 N  N     . PRO A 1 228 ? -4.142  13.251  -1.676  1.00 33.11  ? 226 PRO A N     1 
ATOM   1733 C  CA    . PRO A 1 228 ? -2.718  13.560  -1.725  1.00 36.51  ? 226 PRO A CA    1 
ATOM   1734 C  C     . PRO A 1 228 ? -2.429  15.051  -1.847  1.00 38.50  ? 226 PRO A C     1 
ATOM   1735 O  O     . PRO A 1 228 ? -1.928  15.498  -2.869  1.00 45.29  ? 226 PRO A O     1 
ATOM   1736 C  CB    . PRO A 1 228 ? -2.281  12.820  -2.992  1.00 36.43  ? 226 PRO A CB    1 
ATOM   1737 C  CG    . PRO A 1 228 ? -3.487  12.968  -3.907  1.00 40.36  ? 226 PRO A CG    1 
ATOM   1738 C  CD    . PRO A 1 228 ? -4.682  12.839  -2.975  1.00 35.27  ? 226 PRO A CD    1 
ATOM   1739 N  N     . GLY A 1 229 ? -2.728  15.816  -0.803  1.00 39.95  ? 227 GLY A N     1 
ATOM   1740 C  CA    . GLY A 1 229 ? -2.613  17.259  -0.898  1.00 43.16  ? 227 GLY A CA    1 
ATOM   1741 C  C     . GLY A 1 229 ? -1.152  17.688  -0.936  1.00 44.82  ? 227 GLY A C     1 
ATOM   1742 O  O     . GLY A 1 229 ? -0.365  17.227  -0.121  1.00 41.92  ? 227 GLY A O     1 
ATOM   1743 N  N     . THR A 1 230 ? -0.802  18.583  -1.868  1.00 49.69  ? 228 THR A N     1 
ATOM   1744 C  CA    . THR A 1 230 ? 0.577   19.041  -1.985  1.00 52.06  ? 228 THR A CA    1 
ATOM   1745 C  C     . THR A 1 230 ? 0.909   20.025  -0.866  1.00 55.97  ? 228 THR A C     1 
ATOM   1746 O  O     . THR A 1 230 ? 2.075   20.350  -0.673  1.00 63.00  ? 228 THR A O     1 
ATOM   1747 C  CB    . THR A 1 230 ? 0.867   19.672  -3.355  1.00 56.49  ? 228 THR A CB    1 
ATOM   1748 O  OG1   . THR A 1 230 ? -0.069  20.724  -3.600  1.00 55.12  ? 228 THR A OG1   1 
ATOM   1749 C  CG2   . THR A 1 230 ? 0.802   18.661  -4.478  1.00 59.35  ? 228 THR A CG2   1 
ATOM   1750 N  N     . ASP A 1 231 ? -0.114  20.496  -0.146  1.00 51.88  ? 229 ASP A N     1 
ATOM   1751 C  CA    . ASP A 1 231 ? 0.059   21.368  1.002   1.00 55.20  ? 229 ASP A CA    1 
ATOM   1752 C  C     . ASP A 1 231 ? -1.270  21.405  1.751   1.00 52.65  ? 229 ASP A C     1 
ATOM   1753 O  O     . ASP A 1 231 ? -2.192  20.676  1.405   1.00 48.44  ? 229 ASP A O     1 
ATOM   1754 C  CB    . ASP A 1 231 ? 0.554   22.748  0.549   1.00 59.04  ? 229 ASP A CB    1 
ATOM   1755 C  CG    . ASP A 1 231 ? -0.374  23.460  -0.420  1.00 62.39  ? 229 ASP A CG    1 
ATOM   1756 O  OD1   . ASP A 1 231 ? -1.058  22.775  -1.217  1.00 63.93  ? 229 ASP A OD1   1 
ATOM   1757 O  OD2   . ASP A 1 231 ? -0.366  24.692  -0.407  1.00 67.81  ? 229 ASP A OD2   1 
ATOM   1758 N  N     . HIS A 1 232 ? -1.377  22.239  2.784   1.00 55.13  ? 230 HIS A N     1 
ATOM   1759 C  CA    . HIS A 1 232 ? -2.551  22.189  3.642   1.00 55.25  ? 230 HIS A CA    1 
ATOM   1760 C  C     . HIS A 1 232 ? -3.773  22.600  2.824   1.00 59.74  ? 230 HIS A C     1 
ATOM   1761 O  O     . HIS A 1 232 ? -4.846  22.025  2.976   1.00 63.37  ? 230 HIS A O     1 
ATOM   1762 C  CB    . HIS A 1 232 ? -2.360  23.069  4.881   1.00 57.28  ? 230 HIS A CB    1 
ATOM   1763 N  N     . ILE A 1 233 ? -3.585  23.592  1.945   1.00 63.15  ? 231 ILE A N     1 
ATOM   1764 C  CA    . ILE A 1 233 ? -4.650  24.092  1.088   1.00 61.64  ? 231 ILE A CA    1 
ATOM   1765 C  C     . ILE A 1 233 ? -5.228  22.937  0.275   1.00 54.63  ? 231 ILE A C     1 
ATOM   1766 O  O     . ILE A 1 233 ? -6.430  22.675  0.315   1.00 50.91  ? 231 ILE A O     1 
ATOM   1767 C  CB    . ILE A 1 233 ? -4.112  25.239  0.199   1.00 64.48  ? 231 ILE A CB    1 
ATOM   1768 C  CG1   . ILE A 1 233 ? -3.694  26.436  1.062   1.00 70.98  ? 231 ILE A CG1   1 
ATOM   1769 C  CG2   . ILE A 1 233 ? -5.095  25.644  -0.897  1.00 61.51  ? 231 ILE A CG2   1 
ATOM   1770 C  CD1   . ILE A 1 233 ? -4.622  26.704  2.239   1.00 73.55  ? 231 ILE A CD1   1 
ATOM   1771 N  N     . ASP A 1 234 ? -4.341  22.251  -0.445  1.00 49.41  ? 232 ASP A N     1 
ATOM   1772 C  CA    . ASP A 1 234 ? -4.725  21.255  -1.422  1.00 48.52  ? 232 ASP A CA    1 
ATOM   1773 C  C     . ASP A 1 234 ? -5.440  20.104  -0.708  1.00 44.15  ? 232 ASP A C     1 
ATOM   1774 O  O     . ASP A 1 234 ? -6.428  19.595  -1.215  1.00 41.30  ? 232 ASP A O     1 
ATOM   1775 C  CB    . ASP A 1 234 ? -3.489  20.797  -2.196  1.00 50.70  ? 232 ASP A CB    1 
ATOM   1776 C  CG    . ASP A 1 234 ? -3.801  20.087  -3.495  1.00 57.19  ? 232 ASP A CG    1 
ATOM   1777 O  OD1   . ASP A 1 234 ? -4.867  20.386  -4.081  1.00 59.21  ? 232 ASP A OD1   1 
ATOM   1778 O  OD2   . ASP A 1 234 ? -2.983  19.217  -3.893  1.00 66.33  ? 232 ASP A OD2   1 
ATOM   1779 N  N     . GLN A 1 235 ? -4.950  19.735  0.485   1.00 41.96  ? 233 GLN A N     1 
ATOM   1780 C  CA    . GLN A 1 235 ? -5.456  18.602  1.249   1.00 41.17  ? 233 GLN A CA    1 
ATOM   1781 C  C     . GLN A 1 235 ? -6.962  18.747  1.462   1.00 40.89  ? 233 GLN A C     1 
ATOM   1782 O  O     . GLN A 1 235 ? -7.730  17.854  1.121   1.00 36.40  ? 233 GLN A O     1 
ATOM   1783 C  CB    . GLN A 1 235 ? -4.729  18.535  2.600   1.00 42.45  ? 233 GLN A CB    1 
ATOM   1784 C  CG    . GLN A 1 235 ? -5.053  17.321  3.460   1.00 42.84  ? 233 GLN A CG    1 
ATOM   1785 C  CD    . GLN A 1 235 ? -4.516  16.062  2.835   1.00 42.42  ? 233 GLN A CD    1 
ATOM   1786 O  OE1   . GLN A 1 235 ? -3.466  16.064  2.192   1.00 45.81  ? 233 GLN A OE1   1 
ATOM   1787 N  NE2   . GLN A 1 235 ? -5.270  14.988  2.961   1.00 43.05  ? 233 GLN A NE2   1 
ATOM   1788 N  N     . TRP A 1 236 ? -7.376  19.898  2.002   1.00 36.39  ? 234 TRP A N     1 
ATOM   1789 C  CA    . TRP A 1 236 ? -8.784  20.172  2.226   1.00 35.71  ? 234 TRP A CA    1 
ATOM   1790 C  C     . TRP A 1 236 ? -9.555  20.150  0.905   1.00 36.21  ? 234 TRP A C     1 
ATOM   1791 O  O     . TRP A 1 236 ? -10.606 19.522  0.817   1.00 37.13  ? 234 TRP A O     1 
ATOM   1792 C  CB    . TRP A 1 236 ? -8.960  21.519  2.934   1.00 34.51  ? 234 TRP A CB    1 
ATOM   1793 C  CG    . TRP A 1 236 ? -10.405 21.829  3.193   1.00 33.79  ? 234 TRP A CG    1 
ATOM   1794 C  CD1   . TRP A 1 236 ? -11.115 22.862  2.657   1.00 34.59  ? 234 TRP A CD1   1 
ATOM   1795 C  CD2   . TRP A 1 236 ? -11.330 21.080  4.008   1.00 32.50  ? 234 TRP A CD2   1 
ATOM   1796 N  NE1   . TRP A 1 236 ? -12.411 22.826  3.102   1.00 35.46  ? 234 TRP A NE1   1 
ATOM   1797 C  CE2   . TRP A 1 236 ? -12.574 21.752  3.928   1.00 33.05  ? 234 TRP A CE2   1 
ATOM   1798 C  CE3   . TRP A 1 236 ? -11.233 19.931  4.806   1.00 32.58  ? 234 TRP A CE3   1 
ATOM   1799 C  CZ2   . TRP A 1 236 ? -13.714 21.294  4.587   1.00 32.16  ? 234 TRP A CZ2   1 
ATOM   1800 C  CZ3   . TRP A 1 236 ? -12.357 19.496  5.482   1.00 33.86  ? 234 TRP A CZ3   1 
ATOM   1801 C  CH2   . TRP A 1 236 ? -13.583 20.164  5.356   1.00 32.71  ? 234 TRP A CH2   1 
ATOM   1802 N  N     . ASN A 1 237 ? -9.033  20.826  -0.121  1.00 37.70  ? 235 ASN A N     1 
ATOM   1803 C  CA    . ASN A 1 237 ? -9.680  20.837  -1.428  1.00 39.67  ? 235 ASN A CA    1 
ATOM   1804 C  C     . ASN A 1 237 ? -9.951  19.416  -1.918  1.00 39.62  ? 235 ASN A C     1 
ATOM   1805 O  O     . ASN A 1 237 ? -11.025 19.145  -2.444  1.00 34.69  ? 235 ASN A O     1 
ATOM   1806 C  CB    . ASN A 1 237 ? -8.848  21.544  -2.494  1.00 41.73  ? 235 ASN A CB    1 
ATOM   1807 C  CG    . ASN A 1 237 ? -8.981  23.039  -2.441  1.00 47.14  ? 235 ASN A CG    1 
ATOM   1808 O  OD1   . ASN A 1 237 ? -9.806  23.557  -1.696  1.00 51.78  ? 235 ASN A OD1   1 
ATOM   1809 N  ND2   . ASN A 1 237 ? -8.150  23.725  -3.214  1.00 52.52  ? 235 ASN A ND2   1 
ATOM   1810 N  N     . LYS A 1 238 ? -8.991  18.502  -1.740  1.00 37.96  ? 236 LYS A N     1 
ATOM   1811 C  CA    . LYS A 1 238 ? -9.142  17.155  -2.272  1.00 35.91  ? 236 LYS A CA    1 
ATOM   1812 C  C     . LYS A 1 238 ? -10.215 16.391  -1.500  1.00 33.35  ? 236 LYS A C     1 
ATOM   1813 O  O     . LYS A 1 238 ? -10.943 15.586  -2.074  1.00 32.67  ? 236 LYS A O     1 
ATOM   1814 C  CB    . LYS A 1 238 ? -7.795  16.434  -2.282  1.00 36.22  ? 236 LYS A CB    1 
ATOM   1815 C  CG    . LYS A 1 238 ? -6.860  16.933  -3.378  1.00 40.98  ? 236 LYS A CG    1 
ATOM   1816 C  CD    . LYS A 1 238 ? -5.559  16.186  -3.424  1.00 44.92  ? 236 LYS A CD    1 
ATOM   1817 C  CE    . LYS A 1 238 ? -4.838  16.285  -4.756  1.00 46.45  ? 236 LYS A CE    1 
ATOM   1818 N  NZ    . LYS A 1 238 ? -5.093  17.575  -5.441  1.00 51.45  ? 236 LYS A NZ    1 
ATOM   1819 N  N     . VAL A 1 239 ? -10.356 16.686  -0.213  1.00 29.69  ? 237 VAL A N     1 
ATOM   1820 C  CA    . VAL A 1 239 ? -11.370 16.017  0.590   1.00 29.82  ? 237 VAL A CA    1 
ATOM   1821 C  C     . VAL A 1 239 ? -12.774 16.450  0.132   1.00 30.27  ? 237 VAL A C     1 
ATOM   1822 O  O     . VAL A 1 239 ? -13.625 15.608  -0.168  1.00 27.97  ? 237 VAL A O     1 
ATOM   1823 C  CB    . VAL A 1 239 ? -11.102 16.223  2.093   1.00 26.95  ? 237 VAL A CB    1 
ATOM   1824 C  CG1   . VAL A 1 239 ? -12.232 15.697  2.961   1.00 29.70  ? 237 VAL A CG1   1 
ATOM   1825 C  CG2   . VAL A 1 239 ? -9.803  15.544  2.514   1.00 25.00  ? 237 VAL A CG2   1 
ATOM   1826 N  N     . ILE A 1 240 ? -13.000 17.764  0.011   1.00 29.23  ? 238 ILE A N     1 
ATOM   1827 C  CA    . ILE A 1 240 ? -14.322 18.285  -0.296  1.00 29.39  ? 238 ILE A CA    1 
ATOM   1828 C  C     . ILE A 1 240 ? -14.723 17.955  -1.732  1.00 31.45  ? 238 ILE A C     1 
ATOM   1829 O  O     . ILE A 1 240 ? -15.907 17.768  -2.013  1.00 33.61  ? 238 ILE A O     1 
ATOM   1830 C  CB    . ILE A 1 240 ? -14.409 19.798  0.002   1.00 30.48  ? 238 ILE A CB    1 
ATOM   1831 C  CG1   . ILE A 1 240 ? -13.421 20.604  -0.846  1.00 34.71  ? 238 ILE A CG1   1 
ATOM   1832 C  CG2   . ILE A 1 240 ? -14.254 20.028  1.506   1.00 30.67  ? 238 ILE A CG2   1 
ATOM   1833 C  CD1   . ILE A 1 240 ? -13.588 22.111  -0.789  1.00 34.83  ? 238 ILE A CD1   1 
ATOM   1834 N  N     . GLU A 1 241 ? -13.750 17.896  -2.648  1.00 31.80  ? 239 GLU A N     1 
ATOM   1835 C  CA    . GLU A 1 241 ? -14.033 17.630  -4.048  1.00 34.05  ? 239 GLU A CA    1 
ATOM   1836 C  C     . GLU A 1 241 ? -14.672 16.250  -4.168  1.00 31.18  ? 239 GLU A C     1 
ATOM   1837 O  O     . GLU A 1 241 ? -15.518 16.031  -5.026  1.00 31.10  ? 239 GLU A O     1 
ATOM   1838 C  CB    . GLU A 1 241 ? -12.749 17.708  -4.897  1.00 37.99  ? 239 GLU A CB    1 
ATOM   1839 C  CG    . GLU A 1 241 ? -12.266 19.141  -5.143  1.00 45.95  ? 239 GLU A CG    1 
ATOM   1840 C  CD    . GLU A 1 241 ? -10.903 19.310  -5.795  1.00 49.92  ? 239 GLU A CD    1 
ATOM   1841 O  OE1   . GLU A 1 241 ? -10.350 18.303  -6.252  1.00 56.62  ? 239 GLU A OE1   1 
ATOM   1842 O  OE2   . GLU A 1 241 ? -10.397 20.452  -5.828  1.00 51.80  ? 239 GLU A OE2   1 
ATOM   1843 N  N     . GLN A 1 242 ? -14.234 15.312  -3.320  1.00 30.62  ? 240 GLN A N     1 
ATOM   1844 C  CA    . GLN A 1 242 ? -14.647 13.927  -3.472  1.00 31.36  ? 240 GLN A CA    1 
ATOM   1845 C  C     . GLN A 1 242 ? -15.866 13.610  -2.610  1.00 31.55  ? 240 GLN A C     1 
ATOM   1846 O  O     . GLN A 1 242 ? -16.786 12.951  -3.092  1.00 32.32  ? 240 GLN A O     1 
ATOM   1847 C  CB    . GLN A 1 242 ? -13.473 13.016  -3.159  1.00 33.49  ? 240 GLN A CB    1 
ATOM   1848 C  CG    . GLN A 1 242 ? -12.450 12.980  -4.282  1.00 36.75  ? 240 GLN A CG    1 
ATOM   1849 C  CD    . GLN A 1 242 ? -11.353 12.011  -3.918  1.00 42.35  ? 240 GLN A CD    1 
ATOM   1850 O  OE1   . GLN A 1 242 ? -10.218 12.394  -3.638  1.00 43.07  ? 240 GLN A OE1   1 
ATOM   1851 N  NE2   . GLN A 1 242 ? -11.713 10.740  -3.832  1.00 45.57  ? 240 GLN A NE2   1 
ATOM   1852 N  N     . LEU A 1 243 ? -15.893 14.132  -1.377  1.00 28.47  ? 241 LEU A N     1 
ATOM   1853 C  CA    . LEU A 1 243 ? -16.877 13.720  -0.387  1.00 29.98  ? 241 LEU A CA    1 
ATOM   1854 C  C     . LEU A 1 243 ? -18.003 14.728  -0.229  1.00 28.75  ? 241 LEU A C     1 
ATOM   1855 O  O     . LEU A 1 243 ? -19.004 14.397  0.386   1.00 29.80  ? 241 LEU A O     1 
ATOM   1856 C  CB    . LEU A 1 243 ? -16.193 13.512  0.969   1.00 29.52  ? 241 LEU A CB    1 
ATOM   1857 C  CG    . LEU A 1 243 ? -15.118 12.423  1.005   1.00 29.79  ? 241 LEU A CG    1 
ATOM   1858 C  CD1   . LEU A 1 243 ? -14.638 12.216  2.425   1.00 29.15  ? 241 LEU A CD1   1 
ATOM   1859 C  CD2   . LEU A 1 243 ? -15.632 11.114  0.424   1.00 31.11  ? 241 LEU A CD2   1 
ATOM   1860 N  N     . GLY A 1 244 ? -17.822 15.944  -0.746  1.00 27.44  ? 242 GLY A N     1 
ATOM   1861 C  CA    . GLY A 1 244 ? -18.791 17.019  -0.610  1.00 29.61  ? 242 GLY A CA    1 
ATOM   1862 C  C     . GLY A 1 244 ? -18.433 18.008  0.501   1.00 30.52  ? 242 GLY A C     1 
ATOM   1863 O  O     . GLY A 1 244 ? -17.716 17.692  1.453   1.00 31.47  ? 242 GLY A O     1 
ATOM   1864 N  N     . THR A 1 245 ? -18.926 19.236  0.352   1.00 30.78  ? 243 THR A N     1 
ATOM   1865 C  CA    . THR A 1 245 ? -18.824 20.250  1.377   1.00 30.86  ? 243 THR A CA    1 
ATOM   1866 C  C     . THR A 1 245 ? -19.600 19.803  2.606   1.00 31.49  ? 243 THR A C     1 
ATOM   1867 O  O     . THR A 1 245 ? -20.732 19.347  2.474   1.00 31.92  ? 243 THR A O     1 
ATOM   1868 C  CB    . THR A 1 245 ? -19.418 21.569  0.873   1.00 31.36  ? 243 THR A CB    1 
ATOM   1869 O  OG1   . THR A 1 245 ? -18.728 21.905  -0.329  1.00 33.38  ? 243 THR A OG1   1 
ATOM   1870 C  CG2   . THR A 1 245 ? -19.291 22.691  1.882   1.00 33.14  ? 243 THR A CG2   1 
ATOM   1871 N  N     . PRO A 1 246 ? -19.046 19.909  3.832   1.00 29.52  ? 244 PRO A N     1 
ATOM   1872 C  CA    . PRO A 1 246 ? -19.786 19.494  5.020   1.00 30.93  ? 244 PRO A CA    1 
ATOM   1873 C  C     . PRO A 1 246 ? -20.866 20.496  5.407   1.00 32.96  ? 244 PRO A C     1 
ATOM   1874 O  O     . PRO A 1 246 ? -20.951 21.578  4.826   1.00 35.94  ? 244 PRO A O     1 
ATOM   1875 C  CB    . PRO A 1 246 ? -18.690 19.401  6.080   1.00 29.96  ? 244 PRO A CB    1 
ATOM   1876 C  CG    . PRO A 1 246 ? -17.707 20.468  5.665   1.00 31.24  ? 244 PRO A CG    1 
ATOM   1877 C  CD    . PRO A 1 246 ? -17.694 20.397  4.152   1.00 30.23  ? 244 PRO A CD    1 
ATOM   1878 N  N     . CYS A 1 247 ? -21.713 20.094  6.360   1.00 32.39  ? 245 CYS A N     1 
ATOM   1879 C  CA    . CYS A 1 247 ? -22.935 20.805  6.671   1.00 36.57  ? 245 CYS A CA    1 
ATOM   1880 C  C     . CYS A 1 247 ? -22.595 22.113  7.368   1.00 37.34  ? 245 CYS A C     1 
ATOM   1881 O  O     . CYS A 1 247 ? -21.504 22.279  7.927   1.00 35.22  ? 245 CYS A O     1 
ATOM   1882 C  CB    . CYS A 1 247 ? -23.876 19.998  7.561   1.00 40.29  ? 245 CYS A CB    1 
ATOM   1883 S  SG    . CYS A 1 247 ? -23.163 19.571  9.170   1.00 52.05  ? 245 CYS A SG    1 
ATOM   1884 N  N     . PRO A 1 248 ? -23.533 23.077  7.371   1.00 39.87  ? 246 PRO A N     1 
ATOM   1885 C  CA    . PRO A 1 248 ? -23.287 24.338  8.068   1.00 41.53  ? 246 PRO A CA    1 
ATOM   1886 C  C     . PRO A 1 248 ? -22.989 24.152  9.559   1.00 45.06  ? 246 PRO A C     1 
ATOM   1887 O  O     . PRO A 1 248 ? -22.161 24.877  10.127  1.00 44.10  ? 246 PRO A O     1 
ATOM   1888 C  CB    . PRO A 1 248 ? -24.581 25.119  7.790   1.00 44.47  ? 246 PRO A CB    1 
ATOM   1889 C  CG    . PRO A 1 248 ? -25.094 24.523  6.495   1.00 41.92  ? 246 PRO A CG    1 
ATOM   1890 C  CD    . PRO A 1 248 ? -24.833 23.045  6.672   1.00 39.98  ? 246 PRO A CD    1 
ATOM   1891 N  N     . GLU A 1 249 ? -23.623 23.152  10.187  1.00 47.01  ? 247 GLU A N     1 
ATOM   1892 C  CA    . GLU A 1 249 ? -23.463 22.926  11.620  1.00 48.03  ? 247 GLU A CA    1 
ATOM   1893 C  C     . GLU A 1 249 ? -21.997 22.657  11.925  1.00 44.51  ? 247 GLU A C     1 
ATOM   1894 O  O     . GLU A 1 249 ? -21.497 23.076  12.965  1.00 46.57  ? 247 GLU A O     1 
ATOM   1895 C  CB    . GLU A 1 249 ? -24.305 21.756  12.151  1.00 51.59  ? 247 GLU A CB    1 
ATOM   1896 C  CG    . GLU A 1 249 ? -25.706 21.668  11.551  1.00 58.19  ? 247 GLU A CG    1 
ATOM   1897 C  CD    . GLU A 1 249 ? -26.506 22.958  11.620  1.00 66.59  ? 247 GLU A CD    1 
ATOM   1898 O  OE1   . GLU A 1 249 ? -26.221 23.788  12.525  1.00 67.20  ? 247 GLU A OE1   1 
ATOM   1899 O  OE2   . GLU A 1 249 ? -27.391 23.146  10.746  1.00 74.80  ? 247 GLU A OE2   1 
ATOM   1900 N  N     . PHE A 1 250 ? -21.320 21.940  11.020  1.00 35.56  ? 248 PHE A N     1 
ATOM   1901 C  CA    . PHE A 1 250 ? -19.912 21.647  11.182  1.00 32.78  ? 248 PHE A CA    1 
ATOM   1902 C  C     . PHE A 1 250 ? -19.085 22.926  11.017  1.00 35.22  ? 248 PHE A C     1 
ATOM   1903 O  O     . PHE A 1 250 ? -18.145 23.195  11.768  1.00 34.70  ? 248 PHE A O     1 
ATOM   1904 C  CB    . PHE A 1 250 ? -19.503 20.561  10.181  1.00 31.72  ? 248 PHE A CB    1 
ATOM   1905 C  CG    . PHE A 1 250 ? -18.023 20.324  10.050  1.00 32.34  ? 248 PHE A CG    1 
ATOM   1906 C  CD1   . PHE A 1 250 ? -17.366 19.458  10.920  1.00 35.02  ? 248 PHE A CD1   1 
ATOM   1907 C  CD2   . PHE A 1 250 ? -17.283 20.990  9.086   1.00 30.43  ? 248 PHE A CD2   1 
ATOM   1908 C  CE1   . PHE A 1 250 ? -16.005 19.230  10.799  1.00 32.43  ? 248 PHE A CE1   1 
ATOM   1909 C  CE2   . PHE A 1 250 ? -15.918 20.782  8.978   1.00 32.84  ? 248 PHE A CE2   1 
ATOM   1910 C  CZ    . PHE A 1 250 ? -15.286 19.876  9.826   1.00 31.50  ? 248 PHE A CZ    1 
ATOM   1911 N  N     . MET A 1 251 ? -19.436 23.722  10.015  1.00 34.54  ? 249 MET A N     1 
ATOM   1912 C  CA    . MET A 1 251 ? -18.786 25.001  9.763   1.00 34.60  ? 249 MET A CA    1 
ATOM   1913 C  C     . MET A 1 251 ? -18.743 25.903  11.006  1.00 32.34  ? 249 MET A C     1 
ATOM   1914 O  O     . MET A 1 251 ? -17.778 26.641  11.193  1.00 30.27  ? 249 MET A O     1 
ATOM   1915 C  CB    . MET A 1 251 ? -19.573 25.760  8.696   1.00 38.37  ? 249 MET A CB    1 
ATOM   1916 C  CG    . MET A 1 251 ? -19.761 25.022  7.413   1.00 45.66  ? 249 MET A CG    1 
ATOM   1917 S  SD    . MET A 1 251 ? -18.190 24.746  6.627   1.00 49.94  ? 249 MET A SD    1 
ATOM   1918 C  CE    . MET A 1 251 ? -18.732 25.015  4.941   1.00 44.46  ? 249 MET A CE    1 
ATOM   1919 N  N     . LYS A 1 252 ? -19.817 25.896  11.819  1.00 32.03  ? 250 LYS A N     1 
ATOM   1920 C  CA    . LYS A 1 252 ? -19.977 26.821  12.928  1.00 31.87  ? 250 LYS A CA    1 
ATOM   1921 C  C     . LYS A 1 252 ? -18.942 26.554  14.023  1.00 32.09  ? 250 LYS A C     1 
ATOM   1922 O  O     . LYS A 1 252 ? -18.759 27.364  14.930  1.00 31.35  ? 250 LYS A O     1 
ATOM   1923 C  CB    . LYS A 1 252 ? -21.400 26.724  13.480  1.00 37.48  ? 250 LYS A CB    1 
ATOM   1924 C  CG    . LYS A 1 252 ? -22.466 27.185  12.491  1.00 42.82  ? 250 LYS A CG    1 
ATOM   1925 C  CD    . LYS A 1 252 ? -23.765 27.603  13.121  1.00 53.53  ? 250 LYS A CD    1 
ATOM   1926 C  CE    . LYS A 1 252 ? -24.732 26.459  13.334  1.00 62.02  ? 250 LYS A CE    1 
ATOM   1927 N  NZ    . LYS A 1 252 ? -26.053 26.941  13.818  1.00 64.33  ? 250 LYS A NZ    1 
ATOM   1928 N  N     . LYS A 1 253 ? -18.275 25.412  13.927  1.00 29.96  ? 251 LYS A N     1 
ATOM   1929 C  CA    . LYS A 1 253 ? -17.258 25.012  14.880  1.00 32.69  ? 251 LYS A CA    1 
ATOM   1930 C  C     . LYS A 1 253 ? -15.908 25.661  14.557  1.00 34.48  ? 251 LYS A C     1 
ATOM   1931 O  O     . LYS A 1 253 ? -14.995 25.589  15.371  1.00 37.54  ? 251 LYS A O     1 
ATOM   1932 C  CB    . LYS A 1 253 ? -17.192 23.481  14.890  1.00 33.70  ? 251 LYS A CB    1 
ATOM   1933 C  CG    . LYS A 1 253 ? -18.437 22.817  15.450  1.00 35.61  ? 251 LYS A CG    1 
ATOM   1934 C  CD    . LYS A 1 253 ? -18.353 21.313  15.544  1.00 37.44  ? 251 LYS A CD    1 
ATOM   1935 C  CE    . LYS A 1 253 ? -19.682 20.704  15.927  1.00 39.85  ? 251 LYS A CE    1 
ATOM   1936 N  NZ    . LYS A 1 253 ? -19.566 19.234  16.012  1.00 46.14  ? 251 LYS A NZ    1 
ATOM   1937 N  N     . LEU A 1 254 ? -15.751 26.304  13.393  1.00 32.19  ? 252 LEU A N     1 
ATOM   1938 C  CA    . LEU A 1 254 ? -14.403 26.645  12.951  1.00 33.88  ? 252 LEU A CA    1 
ATOM   1939 C  C     . LEU A 1 254 ? -14.003 28.052  13.416  1.00 35.14  ? 252 LEU A C     1 
ATOM   1940 O  O     . LEU A 1 254 ? -14.854 28.930  13.562  1.00 35.28  ? 252 LEU A O     1 
ATOM   1941 C  CB    . LEU A 1 254 ? -14.327 26.522  11.429  1.00 33.17  ? 252 LEU A CB    1 
ATOM   1942 C  CG    . LEU A 1 254 ? -14.571 25.128  10.839  1.00 34.05  ? 252 LEU A CG    1 
ATOM   1943 C  CD1   . LEU A 1 254 ? -14.735 25.214  9.338   1.00 34.64  ? 252 LEU A CD1   1 
ATOM   1944 C  CD2   . LEU A 1 254 ? -13.423 24.205  11.152  1.00 34.52  ? 252 LEU A CD2   1 
ATOM   1945 N  N     A GLN A 1 255 ? -12.697 28.241  13.651  0.52 35.81  ? 253 GLN A N     1 
ATOM   1946 N  N     B GLN A 1 255 ? -12.695 28.255  13.646  0.48 35.28  ? 253 GLN A N     1 
ATOM   1947 C  CA    A GLN A 1 255 ? -12.144 29.536  14.020  0.52 36.54  ? 253 GLN A CA    1 
ATOM   1948 C  CA    B GLN A 1 255 ? -12.171 29.554  14.049  0.48 36.67  ? 253 GLN A CA    1 
ATOM   1949 C  C     A GLN A 1 255 ? -12.363 30.504  12.863  0.52 36.16  ? 253 GLN A C     1 
ATOM   1950 C  C     B GLN A 1 255 ? -12.322 30.508  12.870  0.48 36.43  ? 253 GLN A C     1 
ATOM   1951 O  O     A GLN A 1 255 ? -12.414 30.072  11.716  0.52 34.01  ? 253 GLN A O     1 
ATOM   1952 O  O     B GLN A 1 255 ? -12.300 30.066  11.726  0.48 33.90  ? 253 GLN A O     1 
ATOM   1953 C  CB    A GLN A 1 255 ? -10.646 29.432  14.332  0.52 38.25  ? 253 GLN A CB    1 
ATOM   1954 C  CB    B GLN A 1 255 ? -10.713 29.453  14.526  0.48 38.79  ? 253 GLN A CB    1 
ATOM   1955 C  CG    A GLN A 1 255 ? -10.303 28.524  15.505  0.52 38.65  ? 253 GLN A CG    1 
ATOM   1956 C  CG    B GLN A 1 255 ? -9.672  29.357  13.415  0.48 40.17  ? 253 GLN A CG    1 
ATOM   1957 C  CD    A GLN A 1 255 ? -8.939  28.853  16.062  0.52 41.14  ? 253 GLN A CD    1 
ATOM   1958 C  CD    B GLN A 1 255 ? -9.010  30.674  13.073  0.48 43.24  ? 253 GLN A CD    1 
ATOM   1959 O  OE1   A GLN A 1 255 ? -7.920  28.733  15.380  0.52 42.07  ? 253 GLN A OE1   1 
ATOM   1960 O  OE1   B GLN A 1 255 ? -9.129  31.677  13.782  0.48 46.80  ? 253 GLN A OE1   1 
ATOM   1961 N  NE2   A GLN A 1 255 ? -8.915  29.351  17.290  0.52 39.66  ? 253 GLN A NE2   1 
ATOM   1962 N  NE2   B GLN A 1 255 ? -8.250  30.677  11.991  0.48 43.57  ? 253 GLN A NE2   1 
ATOM   1963 N  N     . PRO A 1 256 ? -12.498 31.827  13.107  1.00 37.65  ? 254 PRO A N     1 
ATOM   1964 C  CA    . PRO A 1 256 ? -12.842 32.760  12.031  1.00 40.46  ? 254 PRO A CA    1 
ATOM   1965 C  C     . PRO A 1 256 ? -12.034 32.674  10.729  1.00 40.03  ? 254 PRO A C     1 
ATOM   1966 O  O     . PRO A 1 256 ? -12.635 32.645  9.665   1.00 39.09  ? 254 PRO A O     1 
ATOM   1967 C  CB    . PRO A 1 256 ? -12.705 34.127  12.714  1.00 41.24  ? 254 PRO A CB    1 
ATOM   1968 C  CG    . PRO A 1 256 ? -13.054 33.832  14.148  1.00 40.53  ? 254 PRO A CG    1 
ATOM   1969 C  CD    . PRO A 1 256 ? -12.403 32.490  14.414  1.00 40.06  ? 254 PRO A CD    1 
ATOM   1970 N  N     . THR A 1 257 ? -10.697 32.607  10.770  1.00 42.44  ? 255 THR A N     1 
ATOM   1971 C  CA    . THR A 1 257 ? -9.961  32.667  9.511   1.00 44.23  ? 255 THR A CA    1 
ATOM   1972 C  C     . THR A 1 257 ? -10.197 31.393  8.697   1.00 41.57  ? 255 THR A C     1 
ATOM   1973 O  O     . THR A 1 257 ? -10.480 31.485  7.504   1.00 42.96  ? 255 THR A O     1 
ATOM   1974 C  CB    . THR A 1 257 ? -8.469  32.954  9.697   1.00 47.46  ? 255 THR A CB    1 
ATOM   1975 O  OG1   . THR A 1 257 ? -8.364  34.180  10.421  1.00 54.64  ? 255 THR A OG1   1 
ATOM   1976 C  CG2   . THR A 1 257 ? -7.739  33.093  8.375   1.00 47.24  ? 255 THR A CG2   1 
ATOM   1977 N  N     . VAL A 1 258 ? -10.116 30.231  9.356   1.00 39.47  ? 256 VAL A N     1 
ATOM   1978 C  CA    . VAL A 1 258 ? -10.378 28.932  8.744   1.00 39.26  ? 256 VAL A CA    1 
ATOM   1979 C  C     . VAL A 1 258 ? -11.820 28.894  8.232   1.00 36.56  ? 256 VAL A C     1 
ATOM   1980 O  O     . VAL A 1 258 ? -12.101 28.380  7.155   1.00 32.88  ? 256 VAL A O     1 
ATOM   1981 C  CB    . VAL A 1 258 ? -10.131 27.772  9.733   1.00 38.95  ? 256 VAL A CB    1 
ATOM   1982 C  CG1   . VAL A 1 258 ? -10.458 26.434  9.120   1.00 36.51  ? 256 VAL A CG1   1 
ATOM   1983 C  CG2   . VAL A 1 258 ? -8.706  27.722  10.252  1.00 42.29  ? 256 VAL A CG2   1 
ATOM   1984 N  N     . ARG A 1 259 ? -12.755 29.409  9.034   1.00 37.84  ? 257 ARG A N     1 
ATOM   1985 C  CA    . ARG A 1 259 ? -14.168 29.326  8.695   1.00 36.88  ? 257 ARG A CA    1 
ATOM   1986 C  C     . ARG A 1 259 ? -14.458 30.100  7.414   1.00 37.39  ? 257 ARG A C     1 
ATOM   1987 O  O     . ARG A 1 259 ? -15.177 29.604  6.549   1.00 38.51  ? 257 ARG A O     1 
ATOM   1988 C  CB    . ARG A 1 259 ? -15.063 29.817  9.833   1.00 36.44  ? 257 ARG A CB    1 
ATOM   1989 C  CG    . ARG A 1 259 ? -16.553 29.575  9.609   1.00 37.95  ? 257 ARG A CG    1 
ATOM   1990 C  CD    . ARG A 1 259 ? -17.326 30.109  10.806  1.00 42.91  ? 257 ARG A CD    1 
ATOM   1991 N  NE    . ARG A 1 259 ? -18.726 30.375  10.544  1.00 47.33  ? 257 ARG A NE    1 
ATOM   1992 C  CZ    . ARG A 1 259 ? -19.584 30.863  11.443  1.00 56.61  ? 257 ARG A CZ    1 
ATOM   1993 N  NH1   . ARG A 1 259 ? -19.217 31.018  12.709  1.00 62.02  ? 257 ARG A NH1   1 
ATOM   1994 N  NH2   . ARG A 1 259 ? -20.813 31.191  11.072  1.00 53.49  ? 257 ARG A NH2   1 
ATOM   1995 N  N     . THR A 1 260 ? -13.925 31.316  7.297   1.00 38.24  ? 258 THR A N     1 
ATOM   1996 C  CA    . THR A 1 260 ? -14.179 32.129  6.115   1.00 41.16  ? 258 THR A CA    1 
ATOM   1997 C  C     . THR A 1 260 ? -13.620 31.424  4.873   1.00 40.80  ? 258 THR A C     1 
ATOM   1998 O  O     . THR A 1 260 ? -14.292 31.371  3.845   1.00 42.97  ? 258 THR A O     1 
ATOM   1999 C  CB    . THR A 1 260 ? -13.694 33.580  6.304   1.00 45.19  ? 258 THR A CB    1 
ATOM   2000 O  OG1   . THR A 1 260 ? -12.307 33.601  6.628   1.00 53.78  ? 258 THR A OG1   1 
ATOM   2001 C  CG2   . THR A 1 260 ? -14.429 34.291  7.417   1.00 43.67  ? 258 THR A CG2   1 
ATOM   2002 N  N     . TYR A 1 261 ? -12.415 30.855  4.983   1.00 40.08  ? 259 TYR A N     1 
ATOM   2003 C  CA    . TYR A 1 261 ? -11.805 30.121  3.888   1.00 38.75  ? 259 TYR A CA    1 
ATOM   2004 C  C     . TYR A 1 261 ? -12.711 28.954  3.492   1.00 38.44  ? 259 TYR A C     1 
ATOM   2005 O  O     . TYR A 1 261 ? -13.172 28.862  2.355   1.00 42.78  ? 259 TYR A O     1 
ATOM   2006 C  CB    . TYR A 1 261 ? -10.406 29.636  4.284   1.00 39.86  ? 259 TYR A CB    1 
ATOM   2007 C  CG    . TYR A 1 261 ? -9.742  28.892  3.135   1.00 43.08  ? 259 TYR A CG    1 
ATOM   2008 C  CD1   . TYR A 1 261 ? -9.152  29.588  2.080   1.00 43.40  ? 259 TYR A CD1   1 
ATOM   2009 C  CD2   . TYR A 1 261 ? -9.797  27.504  3.057   1.00 42.65  ? 259 TYR A CD2   1 
ATOM   2010 C  CE1   . TYR A 1 261 ? -8.600  28.923  0.998   1.00 42.35  ? 259 TYR A CE1   1 
ATOM   2011 C  CE2   . TYR A 1 261 ? -9.245  26.827  1.981   1.00 43.91  ? 259 TYR A CE2   1 
ATOM   2012 C  CZ    . TYR A 1 261 ? -8.637  27.540  0.961   1.00 44.70  ? 259 TYR A CZ    1 
ATOM   2013 O  OH    . TYR A 1 261 ? -8.105  26.886  -0.096  1.00 40.81  ? 259 TYR A OH    1 
ATOM   2014 N  N     . VAL A 1 262 ? -12.999 28.073  4.449   1.00 37.11  ? 260 VAL A N     1 
ATOM   2015 C  CA    . VAL A 1 262 ? -13.790 26.876  4.178   1.00 35.04  ? 260 VAL A CA    1 
ATOM   2016 C  C     . VAL A 1 262 ? -15.162 27.254  3.610   1.00 36.81  ? 260 VAL A C     1 
ATOM   2017 O  O     . VAL A 1 262 ? -15.679 26.575  2.728   1.00 34.94  ? 260 VAL A O     1 
ATOM   2018 C  CB    . VAL A 1 262 ? -13.904 25.994  5.434   1.00 35.14  ? 260 VAL A CB    1 
ATOM   2019 C  CG1   . VAL A 1 262 ? -14.960 24.905  5.292   1.00 36.68  ? 260 VAL A CG1   1 
ATOM   2020 C  CG2   . VAL A 1 262 ? -12.567 25.373  5.772   1.00 36.27  ? 260 VAL A CG2   1 
ATOM   2021 N  N     . GLU A 1 263 ? -15.763 28.334  4.112   1.00 37.95  ? 261 GLU A N     1 
ATOM   2022 C  CA    . GLU A 1 263 ? -17.100 28.713  3.687   1.00 40.93  ? 261 GLU A CA    1 
ATOM   2023 C  C     . GLU A 1 263 ? -17.066 29.301  2.278   1.00 41.91  ? 261 GLU A C     1 
ATOM   2024 O  O     . GLU A 1 263 ? -18.049 29.187  1.564   1.00 44.15  ? 261 GLU A O     1 
ATOM   2025 C  CB    . GLU A 1 263 ? -17.760 29.672  4.680   1.00 41.09  ? 261 GLU A CB    1 
ATOM   2026 C  CG    . GLU A 1 263 ? -18.356 28.951  5.866   1.00 44.71  ? 261 GLU A CG    1 
ATOM   2027 C  CD    . GLU A 1 263 ? -19.121 29.784  6.878   1.00 51.07  ? 261 GLU A CD    1 
ATOM   2028 O  OE1   . GLU A 1 263 ? -19.143 31.030  6.753   1.00 54.72  ? 261 GLU A OE1   1 
ATOM   2029 O  OE2   . GLU A 1 263 ? -19.687 29.176  7.813   1.00 54.11  ? 261 GLU A OE2   1 
ATOM   2030 N  N     . ASN A 1 264 ? -15.936 29.871  1.851   1.00 41.43  ? 262 ASN A N     1 
ATOM   2031 C  CA    . ASN A 1 264 ? -15.868 30.542  0.556   1.00 44.33  ? 262 ASN A CA    1 
ATOM   2032 C  C     . ASN A 1 264 ? -15.269 29.648  -0.536  1.00 45.09  ? 262 ASN A C     1 
ATOM   2033 O  O     . ASN A 1 264 ? -15.010 30.117  -1.644  1.00 46.71  ? 262 ASN A O     1 
ATOM   2034 C  CB    . ASN A 1 264 ? -15.043 31.823  0.655   1.00 46.47  ? 262 ASN A CB    1 
ATOM   2035 C  CG    . ASN A 1 264 ? -15.793 32.929  1.355   1.00 52.37  ? 262 ASN A CG    1 
ATOM   2036 O  OD1   . ASN A 1 264 ? -17.017 33.000  1.269   1.00 55.15  ? 262 ASN A OD1   1 
ATOM   2037 N  ND2   . ASN A 1 264 ? -15.066 33.816  2.014   1.00 54.96  ? 262 ASN A ND2   1 
ATOM   2038 N  N     . ARG A 1 265 ? -14.997 28.378  -0.222  1.00 40.46  ? 263 ARG A N     1 
ATOM   2039 C  CA    . ARG A 1 265 ? -14.688 27.399  -1.249  1.00 38.89  ? 263 ARG A CA    1 
ATOM   2040 C  C     . ARG A 1 265 ? -15.940 27.136  -2.087  1.00 39.75  ? 263 ARG A C     1 
ATOM   2041 O  O     . ARG A 1 265 ? -17.057 27.298  -1.604  1.00 40.16  ? 263 ARG A O     1 
ATOM   2042 C  CB    . ARG A 1 265 ? -14.232 26.070  -0.641  1.00 38.88  ? 263 ARG A CB    1 
ATOM   2043 C  CG    . ARG A 1 265 ? -12.934 26.122  0.150   1.00 44.23  ? 263 ARG A CG    1 
ATOM   2044 C  CD    . ARG A 1 265 ? -11.729 26.024  -0.753  1.00 45.99  ? 263 ARG A CD    1 
ATOM   2045 N  NE    . ARG A 1 265 ? -11.500 27.270  -1.441  1.00 49.45  ? 263 ARG A NE    1 
ATOM   2046 C  CZ    . ARG A 1 265 ? -10.900 27.380  -2.622  1.00 53.48  ? 263 ARG A CZ    1 
ATOM   2047 N  NH1   . ARG A 1 265 ? -10.469 26.303  -3.257  1.00 54.19  ? 263 ARG A NH1   1 
ATOM   2048 N  NH2   . ARG A 1 265 ? -10.744 28.579  -3.162  1.00 51.09  ? 263 ARG A NH2   1 
ATOM   2049 N  N     . PRO A 1 266 ? -15.808 26.693  -3.357  1.00 44.32  ? 264 PRO A N     1 
ATOM   2050 C  CA    . PRO A 1 266 ? -16.978 26.302  -4.150  1.00 42.07  ? 264 PRO A CA    1 
ATOM   2051 C  C     . PRO A 1 266 ? -17.708 25.169  -3.425  1.00 39.60  ? 264 PRO A C     1 
ATOM   2052 O  O     . PRO A 1 266 ? -17.095 24.444  -2.648  1.00 34.46  ? 264 PRO A O     1 
ATOM   2053 C  CB    . PRO A 1 266 ? -16.385 25.833  -5.487  1.00 47.80  ? 264 PRO A CB    1 
ATOM   2054 C  CG    . PRO A 1 266 ? -14.994 26.444  -5.528  1.00 50.20  ? 264 PRO A CG    1 
ATOM   2055 C  CD    . PRO A 1 266 ? -14.546 26.489  -4.080  1.00 47.46  ? 264 PRO A CD    1 
ATOM   2056 N  N     . LYS A 1 267 ? -19.021 25.054  -3.651  1.00 39.03  ? 265 LYS A N     1 
ATOM   2057 C  CA    . LYS A 1 267 ? -19.832 24.087  -2.930  1.00 38.75  ? 265 LYS A CA    1 
ATOM   2058 C  C     . LYS A 1 267 ? -19.903 22.792  -3.733  1.00 36.98  ? 265 LYS A C     1 
ATOM   2059 O  O     . LYS A 1 267 ? -20.458 22.755  -4.832  1.00 36.12  ? 265 LYS A O     1 
ATOM   2060 C  CB    . LYS A 1 267 ? -21.242 24.609  -2.674  1.00 40.33  ? 265 LYS A CB    1 
ATOM   2061 C  CG    . LYS A 1 267 ? -21.297 25.976  -2.021  1.00 43.95  ? 265 LYS A CG    1 
ATOM   2062 C  CD    . LYS A 1 267 ? -20.877 25.932  -0.577  1.00 47.01  ? 265 LYS A CD    1 
ATOM   2063 C  CE    . LYS A 1 267 ? -21.175 27.237  0.144   1.00 53.30  ? 265 LYS A CE    1 
ATOM   2064 N  NZ    . LYS A 1 267 ? -20.904 27.119  1.596   1.00 54.49  ? 265 LYS A NZ    1 
ATOM   2065 N  N     . TYR A 1 268 ? -19.356 21.741  -3.142  1.00 34.35  ? 266 TYR A N     1 
ATOM   2066 C  CA    . TYR A 1 268 ? -19.265 20.435  -3.778  1.00 36.39  ? 266 TYR A CA    1 
ATOM   2067 C  C     . TYR A 1 268 ? -20.320 19.484  -3.228  1.00 34.91  ? 266 TYR A C     1 
ATOM   2068 O  O     . TYR A 1 268 ? -20.533 19.409  -2.020  1.00 33.67  ? 266 TYR A O     1 
ATOM   2069 C  CB    . TYR A 1 268 ? -17.891 19.819  -3.543  1.00 37.03  ? 266 TYR A CB    1 
ATOM   2070 C  CG    . TYR A 1 268 ? -16.757 20.543  -4.246  1.00 39.93  ? 266 TYR A CG    1 
ATOM   2071 C  CD1   . TYR A 1 268 ? -16.611 20.469  -5.625  1.00 41.42  ? 266 TYR A CD1   1 
ATOM   2072 C  CD2   . TYR A 1 268 ? -15.840 21.300  -3.528  1.00 42.30  ? 266 TYR A CD2   1 
ATOM   2073 C  CE1   . TYR A 1 268 ? -15.583 21.135  -6.272  1.00 45.28  ? 266 TYR A CE1   1 
ATOM   2074 C  CE2   . TYR A 1 268 ? -14.805 21.967  -4.165  1.00 41.94  ? 266 TYR A CE2   1 
ATOM   2075 C  CZ    . TYR A 1 268 ? -14.677 21.881  -5.535  1.00 43.17  ? 266 TYR A CZ    1 
ATOM   2076 O  OH    . TYR A 1 268 ? -13.661 22.535  -6.158  1.00 44.65  ? 266 TYR A OH    1 
ATOM   2077 N  N     . ALA A 1 269 ? -20.971 18.772  -4.152  1.00 35.10  ? 267 ALA A N     1 
ATOM   2078 C  CA    . ALA A 1 269 ? -21.946 17.752  -3.818  1.00 34.83  ? 267 ALA A CA    1 
ATOM   2079 C  C     . ALA A 1 269 ? -21.227 16.490  -3.368  1.00 34.61  ? 267 ALA A C     1 
ATOM   2080 O  O     . ALA A 1 269 ? -21.792 15.734  -2.599  1.00 35.57  ? 267 ALA A O     1 
ATOM   2081 C  CB    . ALA A 1 269 ? -22.836 17.457  -5.005  1.00 37.38  ? 267 ALA A CB    1 
ATOM   2082 N  N     . GLY A 1 270 ? -19.993 16.267  -3.834  1.00 32.69  ? 268 GLY A N     1 
ATOM   2083 C  CA    . GLY A 1 270 ? -19.341 15.007  -3.555  1.00 37.65  ? 268 GLY A CA    1 
ATOM   2084 C  C     . GLY A 1 270 ? -19.851 13.940  -4.513  1.00 34.18  ? 268 GLY A C     1 
ATOM   2085 O  O     . GLY A 1 270 ? -20.806 14.163  -5.224  1.00 35.89  ? 268 GLY A O     1 
ATOM   2086 N  N     . TYR A 1 271 ? -19.169 12.808  -4.546  1.00 33.93  ? 269 TYR A N     1 
ATOM   2087 C  CA    . TYR A 1 271 ? -19.573 11.698  -5.376  1.00 33.80  ? 269 TYR A CA    1 
ATOM   2088 C  C     . TYR A 1 271 ? -20.001 10.549  -4.476  1.00 35.54  ? 269 TYR A C     1 
ATOM   2089 O  O     . TYR A 1 271 ? -19.512 10.395  -3.355  1.00 34.62  ? 269 TYR A O     1 
ATOM   2090 C  CB    . TYR A 1 271 ? -18.417 11.284  -6.286  1.00 39.29  ? 269 TYR A CB    1 
ATOM   2091 C  CG    . TYR A 1 271 ? -17.960 12.385  -7.224  1.00 42.39  ? 269 TYR A CG    1 
ATOM   2092 C  CD1   . TYR A 1 271 ? -16.974 13.289  -6.849  1.00 44.01  ? 269 TYR A CD1   1 
ATOM   2093 C  CD2   . TYR A 1 271 ? -18.549 12.538  -8.467  1.00 43.15  ? 269 TYR A CD2   1 
ATOM   2094 C  CE1   . TYR A 1 271 ? -16.567 14.298  -7.709  1.00 46.11  ? 269 TYR A CE1   1 
ATOM   2095 C  CE2   . TYR A 1 271 ? -18.158 13.542  -9.332  1.00 43.97  ? 269 TYR A CE2   1 
ATOM   2096 C  CZ    . TYR A 1 271 ? -17.155 14.414  -8.955  1.00 47.62  ? 269 TYR A CZ    1 
ATOM   2097 O  OH    . TYR A 1 271 ? -16.787 15.395  -9.828  1.00 53.99  ? 269 TYR A OH    1 
ATOM   2098 N  N     . SER A 1 272 ? -20.866 9.708   -5.030  1.00 34.15  ? 270 SER A N     1 
ATOM   2099 C  CA    . SER A 1 272 ? -21.307 8.507   -4.353  1.00 37.29  ? 270 SER A CA    1 
ATOM   2100 C  C     . SER A 1 272 ? -20.113 7.578   -4.127  1.00 35.33  ? 270 SER A C     1 
ATOM   2101 O  O     . SER A 1 272 ? -19.137 7.585   -4.876  1.00 35.64  ? 270 SER A O     1 
ATOM   2102 C  CB    . SER A 1 272 ? -22.391 7.813   -5.146  1.00 37.78  ? 270 SER A CB    1 
ATOM   2103 O  OG    . SER A 1 272 ? -21.830 7.162   -6.262  1.00 37.97  ? 270 SER A OG    1 
ATOM   2104 N  N     . PHE A 1 273 ? -20.208 6.738   -3.104  1.00 32.68  ? 271 PHE A N     1 
ATOM   2105 C  CA    . PHE A 1 273 ? -19.154 5.774   -2.849  1.00 33.86  ? 271 PHE A CA    1 
ATOM   2106 C  C     . PHE A 1 273 ? -19.090 4.728   -3.963  1.00 37.53  ? 271 PHE A C     1 
ATOM   2107 O  O     . PHE A 1 273 ? -18.030 4.131   -4.168  1.00 37.43  ? 271 PHE A O     1 
ATOM   2108 C  CB    . PHE A 1 273 ? -19.280 5.201   -1.432  1.00 32.62  ? 271 PHE A CB    1 
ATOM   2109 C  CG    . PHE A 1 273 ? -18.732 6.153   -0.406  1.00 31.95  ? 271 PHE A CG    1 
ATOM   2110 C  CD1   . PHE A 1 273 ? -19.489 7.242   0.018   1.00 31.66  ? 271 PHE A CD1   1 
ATOM   2111 C  CD2   . PHE A 1 273 ? -17.430 6.027   0.062   1.00 31.55  ? 271 PHE A CD2   1 
ATOM   2112 C  CE1   . PHE A 1 273 ? -18.974 8.152   0.938   1.00 29.75  ? 271 PHE A CE1   1 
ATOM   2113 C  CE2   . PHE A 1 273 ? -16.909 6.946   0.969   1.00 30.61  ? 271 PHE A CE2   1 
ATOM   2114 C  CZ    . PHE A 1 273 ? -17.679 8.019   1.395   1.00 28.79  ? 271 PHE A CZ    1 
ATOM   2115 N  N     . GLU A 1 274 ? -20.186 4.548   -4.715  1.00 36.32  ? 272 GLU A N     1 
ATOM   2116 C  CA    . GLU A 1 274 ? -20.162 3.688   -5.879  1.00 38.02  ? 272 GLU A CA    1 
ATOM   2117 C  C     . GLU A 1 274 ? -19.303 4.299   -6.978  1.00 39.22  ? 272 GLU A C     1 
ATOM   2118 O  O     . GLU A 1 274 ? -18.619 3.567   -7.690  1.00 37.66  ? 272 GLU A O     1 
ATOM   2119 C  CB    . GLU A 1 274 ? -21.570 3.392   -6.403  1.00 42.74  ? 272 GLU A CB    1 
ATOM   2120 C  CG    . GLU A 1 274 ? -22.405 2.556   -5.441  1.00 47.28  ? 272 GLU A CG    1 
ATOM   2121 C  CD    . GLU A 1 274 ? -22.903 3.290   -4.202  1.00 49.07  ? 272 GLU A CD    1 
ATOM   2122 O  OE1   . GLU A 1 274 ? -22.968 4.537   -4.217  1.00 48.27  ? 272 GLU A OE1   1 
ATOM   2123 O  OE2   . GLU A 1 274 ? -23.187 2.616   -3.205  1.00 55.73  ? 272 GLU A OE2   1 
ATOM   2124 N  N     . LYS A 1 275 ? -19.343 5.631   -7.136  1.00 38.50  ? 273 LYS A N     1 
ATOM   2125 C  CA    . LYS A 1 275 ? -18.524 6.263   -8.151  1.00 38.92  ? 273 LYS A CA    1 
ATOM   2126 C  C     . LYS A 1 275 ? -17.070 6.362   -7.673  1.00 38.56  ? 273 LYS A C     1 
ATOM   2127 O  O     . LYS A 1 275 ? -16.143 6.229   -8.465  1.00 39.57  ? 273 LYS A O     1 
ATOM   2128 C  CB    . LYS A 1 275 ? -19.108 7.622   -8.525  1.00 43.44  ? 273 LYS A CB    1 
ATOM   2129 C  CG    . LYS A 1 275 ? -18.174 8.468   -9.369  1.00 51.57  ? 273 LYS A CG    1 
ATOM   2130 C  CD    . LYS A 1 275 ? -18.831 9.290   -10.449 1.00 61.40  ? 273 LYS A CD    1 
ATOM   2131 C  CE    . LYS A 1 275 ? -17.803 9.902   -11.387 1.00 67.92  ? 273 LYS A CE    1 
ATOM   2132 N  NZ    . LYS A 1 275 ? -16.574 10.350  -10.670 1.00 72.24  ? 273 LYS A NZ    1 
ATOM   2133 N  N     . LEU A 1 276 ? -16.865 6.562   -6.372  1.00 35.77  ? 274 LEU A N     1 
ATOM   2134 C  CA    . LEU A 1 276 ? -15.520 6.708   -5.831  1.00 35.69  ? 274 LEU A CA    1 
ATOM   2135 C  C     . LEU A 1 276 ? -14.806 5.365   -5.819  1.00 36.39  ? 274 LEU A C     1 
ATOM   2136 O  O     . LEU A 1 276 ? -13.600 5.309   -6.040  1.00 38.43  ? 274 LEU A O     1 
ATOM   2137 C  CB    . LEU A 1 276 ? -15.580 7.282   -4.416  1.00 34.61  ? 274 LEU A CB    1 
ATOM   2138 C  CG    . LEU A 1 276 ? -16.084 8.725   -4.321  1.00 35.84  ? 274 LEU A CG    1 
ATOM   2139 C  CD1   . LEU A 1 276 ? -16.143 9.174   -2.867  1.00 37.09  ? 274 LEU A CD1   1 
ATOM   2140 C  CD2   . LEU A 1 276 ? -15.199 9.652   -5.141  1.00 38.74  ? 274 LEU A CD2   1 
ATOM   2141 N  N     . PHE A 1 277 ? -15.558 4.300   -5.523  1.00 33.35  ? 275 PHE A N     1 
ATOM   2142 C  CA    . PHE A 1 277 ? -14.979 2.976   -5.369  1.00 36.32  ? 275 PHE A CA    1 
ATOM   2143 C  C     . PHE A 1 277 ? -15.766 1.984   -6.227  1.00 36.68  ? 275 PHE A C     1 
ATOM   2144 O  O     . PHE A 1 277 ? -16.515 1.164   -5.703  1.00 37.11  ? 275 PHE A O     1 
ATOM   2145 C  CB    . PHE A 1 277 ? -14.941 2.591   -3.888  1.00 35.61  ? 275 PHE A CB    1 
ATOM   2146 C  CG    . PHE A 1 277 ? -14.144 3.541   -3.047  1.00 32.15  ? 275 PHE A CG    1 
ATOM   2147 C  CD1   . PHE A 1 277 ? -12.770 3.417   -2.950  1.00 32.00  ? 275 PHE A CD1   1 
ATOM   2148 C  CD2   . PHE A 1 277 ? -14.760 4.581   -2.382  1.00 34.04  ? 275 PHE A CD2   1 
ATOM   2149 C  CE1   . PHE A 1 277 ? -12.035 4.307   -2.185  1.00 31.43  ? 275 PHE A CE1   1 
ATOM   2150 C  CE2   . PHE A 1 277 ? -14.018 5.458   -1.604  1.00 32.82  ? 275 PHE A CE2   1 
ATOM   2151 C  CZ    . PHE A 1 277 ? -12.659 5.346   -1.541  1.00 28.39  ? 275 PHE A CZ    1 
ATOM   2152 N  N     . PRO A 1 278 ? -15.634 2.058   -7.567  1.00 39.18  ? 276 PRO A N     1 
ATOM   2153 C  CA    . PRO A 1 278 ? -16.369 1.167   -8.470  1.00 40.58  ? 276 PRO A CA    1 
ATOM   2154 C  C     . PRO A 1 278 ? -15.946 -0.298  -8.379  1.00 45.37  ? 276 PRO A C     1 
ATOM   2155 O  O     . PRO A 1 278 ? -14.826 -0.607  -7.967  1.00 43.88  ? 276 PRO A O     1 
ATOM   2156 C  CB    . PRO A 1 278 ? -16.057 1.684   -9.885  1.00 44.50  ? 276 PRO A CB    1 
ATOM   2157 C  CG    . PRO A 1 278 ? -15.359 3.010   -9.697  1.00 42.79  ? 276 PRO A CG    1 
ATOM   2158 C  CD    . PRO A 1 278 ? -14.804 3.031   -8.290  1.00 39.06  ? 276 PRO A CD    1 
ATOM   2159 N  N     . ASP A 1 279 ? -16.843 -1.184  -8.835  1.00 46.94  ? 277 ASP A N     1 
ATOM   2160 C  CA    . ASP A 1 279 ? -16.668 -2.628  -8.741  1.00 52.80  ? 277 ASP A CA    1 
ATOM   2161 C  C     . ASP A 1 279 ? -15.398 -3.088  -9.460  1.00 51.21  ? 277 ASP A C     1 
ATOM   2162 O  O     . ASP A 1 279 ? -14.756 -4.058  -9.050  1.00 47.99  ? 277 ASP A O     1 
ATOM   2163 C  CB    . ASP A 1 279 ? -17.891 -3.359  -9.297  1.00 59.72  ? 277 ASP A CB    1 
ATOM   2164 C  CG    . ASP A 1 279 ? -19.114 -3.224  -8.410  1.00 67.03  ? 277 ASP A CG    1 
ATOM   2165 O  OD1   . ASP A 1 279 ? -19.037 -3.673  -7.241  1.00 64.17  ? 277 ASP A OD1   1 
ATOM   2166 O  OD2   . ASP A 1 279 ? -20.128 -2.661  -8.893  1.00 76.36  ? 277 ASP A OD2   1 
ATOM   2167 N  N     . VAL A 1 280 ? -15.029 -2.374  -10.524 1.00 50.43  ? 278 VAL A N     1 
ATOM   2168 C  CA    . VAL A 1 280 ? -13.836 -2.685  -11.296 1.00 49.26  ? 278 VAL A CA    1 
ATOM   2169 C  C     . VAL A 1 280 ? -12.594 -2.747  -10.399 1.00 49.16  ? 278 VAL A C     1 
ATOM   2170 O  O     . VAL A 1 280 ? -11.675 -3.502  -10.704 1.00 46.98  ? 278 VAL A O     1 
ATOM   2171 C  CB    . VAL A 1 280 ? -13.652 -1.669  -12.443 1.00 52.19  ? 278 VAL A CB    1 
ATOM   2172 C  CG1   . VAL A 1 280 ? -13.123 -0.322  -11.956 1.00 54.42  ? 278 VAL A CG1   1 
ATOM   2173 C  CG2   . VAL A 1 280 ? -12.759 -2.224  -13.531 1.00 55.40  ? 278 VAL A CG2   1 
ATOM   2174 N  N     . LEU A 1 281 ? -12.542 -1.938  -9.325  1.00 49.62  ? 279 LEU A N     1 
ATOM   2175 C  CA    . LEU A 1 281 ? -11.375 -1.887  -8.452  1.00 46.86  ? 279 LEU A CA    1 
ATOM   2176 C  C     . LEU A 1 281 ? -11.339 -3.046  -7.468  1.00 47.02  ? 279 LEU A C     1 
ATOM   2177 O  O     . LEU A 1 281 ? -10.316 -3.216  -6.811  1.00 46.28  ? 279 LEU A O     1 
ATOM   2178 C  CB    . LEU A 1 281 ? -11.364 -0.582  -7.652  1.00 44.16  ? 279 LEU A CB    1 
ATOM   2179 C  CG    . LEU A 1 281 ? -11.098 0.672   -8.468  1.00 47.35  ? 279 LEU A CG    1 
ATOM   2180 C  CD1   . LEU A 1 281 ? -11.315 1.906   -7.599  1.00 47.65  ? 279 LEU A CD1   1 
ATOM   2181 C  CD2   . LEU A 1 281 ? -9.687  0.632   -9.051  1.00 52.86  ? 279 LEU A CD2   1 
ATOM   2182 N  N     . PHE A 1 282 ? -12.453 -3.778  -7.329  1.00 45.17  ? 280 PHE A N     1 
ATOM   2183 C  CA    . PHE A 1 282 ? -12.597 -4.815  -6.316  1.00 48.13  ? 280 PHE A CA    1 
ATOM   2184 C  C     . PHE A 1 282 ? -12.482 -6.217  -6.915  1.00 50.50  ? 280 PHE A C     1 
ATOM   2185 O  O     . PHE A 1 282 ? -12.707 -6.422  -8.103  1.00 52.89  ? 280 PHE A O     1 
ATOM   2186 C  CB    . PHE A 1 282 ? -13.968 -4.713  -5.645  1.00 45.53  ? 280 PHE A CB    1 
ATOM   2187 C  CG    . PHE A 1 282 ? -14.118 -3.607  -4.634  1.00 43.84  ? 280 PHE A CG    1 
ATOM   2188 C  CD1   . PHE A 1 282 ? -13.533 -3.703  -3.380  1.00 41.84  ? 280 PHE A CD1   1 
ATOM   2189 C  CD2   . PHE A 1 282 ? -14.871 -2.481  -4.928  1.00 43.16  ? 280 PHE A CD2   1 
ATOM   2190 C  CE1   . PHE A 1 282 ? -13.706 -2.698  -2.438  1.00 40.02  ? 280 PHE A CE1   1 
ATOM   2191 C  CE2   . PHE A 1 282 ? -15.045 -1.484  -3.987  1.00 40.90  ? 280 PHE A CE2   1 
ATOM   2192 C  CZ    . PHE A 1 282 ? -14.464 -1.592  -2.747  1.00 42.63  ? 280 PHE A CZ    1 
ATOM   2193 N  N     . PRO A 1 283 ? -12.185 -7.261  -6.112  1.00 52.87  ? 281 PRO A N     1 
ATOM   2194 C  CA    . PRO A 1 283 ? -12.539 -8.619  -6.517  1.00 58.00  ? 281 PRO A CA    1 
ATOM   2195 C  C     . PRO A 1 283 ? -14.067 -8.639  -6.620  1.00 65.95  ? 281 PRO A C     1 
ATOM   2196 O  O     . PRO A 1 283 ? -14.771 -8.143  -5.733  1.00 67.63  ? 281 PRO A O     1 
ATOM   2197 C  CB    . PRO A 1 283 ? -11.981 -9.516  -5.401  1.00 53.77  ? 281 PRO A CB    1 
ATOM   2198 C  CG    . PRO A 1 283 ? -11.025 -8.625  -4.613  1.00 53.30  ? 281 PRO A CG    1 
ATOM   2199 C  CD    . PRO A 1 283 ? -11.545 -7.212  -4.790  1.00 52.63  ? 281 PRO A CD    1 
ATOM   2200 N  N     . ALA A 1 284 ? -14.589 -9.154  -7.729  1.00 70.81  ? 282 ALA A N     1 
ATOM   2201 C  CA    . ALA A 1 284 ? -16.027 -9.095  -7.965  1.00 78.49  ? 282 ALA A CA    1 
ATOM   2202 C  C     . ALA A 1 284 ? -16.429 -10.103 -9.042  1.00 78.46  ? 282 ALA A C     1 
ATOM   2203 O  O     . ALA A 1 284 ? -17.271 -9.813  -9.883  1.00 80.97  ? 282 ALA A O     1 
ATOM   2204 C  CB    . ALA A 1 284 ? -16.439 -7.677  -8.325  1.00 77.81  ? 282 ALA A CB    1 
ATOM   2205 N  N     . ASP A 1 285 ? -15.866 -11.312 -8.957  1.00 79.21  ? 283 ASP A N     1 
ATOM   2206 C  CA    . ASP A 1 285 ? -16.093 -12.342 -9.953  1.00 83.81  ? 283 ASP A CA    1 
ATOM   2207 C  C     . ASP A 1 285 ? -17.141 -13.346 -9.477  1.00 84.65  ? 283 ASP A C     1 
ATOM   2208 O  O     . ASP A 1 285 ? -17.387 -14.326 -10.170 1.00 98.08  ? 283 ASP A O     1 
ATOM   2209 C  CB    . ASP A 1 285 ? -14.789 -13.078 -10.281 1.00 86.56  ? 283 ASP A CB    1 
ATOM   2210 N  N     . SER A 1 286 ? -17.767 -13.101 -8.320  1.00 79.08  ? 284 SER A N     1 
ATOM   2211 C  CA    . SER A 1 286 ? -18.659 -14.079 -7.714  1.00 74.12  ? 284 SER A CA    1 
ATOM   2212 C  C     . SER A 1 286 ? -19.684 -13.373 -6.832  1.00 79.68  ? 284 SER A C     1 
ATOM   2213 O  O     . SER A 1 286 ? -19.581 -12.163 -6.585  1.00 79.35  ? 284 SER A O     1 
ATOM   2214 C  CB    . SER A 1 286 ? -17.886 -15.117 -6.923  1.00 71.99  ? 284 SER A CB    1 
ATOM   2215 O  OG    . SER A 1 286 ? -17.184 -14.524 -5.833  1.00 65.55  ? 284 SER A OG    1 
ATOM   2216 N  N     . GLU A 1 287 ? -20.658 -14.170 -6.364  1.00 78.87  ? 285 GLU A N     1 
ATOM   2217 C  CA    . GLU A 1 287 ? -21.717 -13.706 -5.477  1.00 83.06  ? 285 GLU A CA    1 
ATOM   2218 C  C     . GLU A 1 287 ? -21.115 -13.154 -4.181  1.00 78.39  ? 285 GLU A C     1 
ATOM   2219 O  O     . GLU A 1 287 ? -21.416 -12.025 -3.793  1.00 86.62  ? 285 GLU A O     1 
ATOM   2220 C  CB    . GLU A 1 287 ? -22.753 -14.810 -5.207  1.00 83.39  ? 285 GLU A CB    1 
ATOM   2221 C  CG    . GLU A 1 287 ? -22.182 -16.208 -4.974  1.00 87.39  ? 285 GLU A CG    1 
ATOM   2222 C  CD    . GLU A 1 287 ? -22.020 -17.074 -6.218  1.00 90.34  ? 285 GLU A CD    1 
ATOM   2223 O  OE1   . GLU A 1 287 ? -21.338 -16.625 -7.167  1.00 93.24  ? 285 GLU A OE1   1 
ATOM   2224 O  OE2   . GLU A 1 287 ? -22.556 -18.209 -6.234  1.00 82.60  ? 285 GLU A OE2   1 
ATOM   2225 N  N     . HIS A 1 288 ? -20.249 -13.944 -3.532  1.00 65.34  ? 286 HIS A N     1 
ATOM   2226 C  CA    . HIS A 1 288 ? -19.593 -13.540 -2.294  1.00 68.07  ? 286 HIS A CA    1 
ATOM   2227 C  C     . HIS A 1 288 ? -18.852 -12.208 -2.484  1.00 66.56  ? 286 HIS A C     1 
ATOM   2228 O  O     . HIS A 1 288 ? -18.968 -11.298 -1.650  1.00 62.56  ? 286 HIS A O     1 
ATOM   2229 C  CB    . HIS A 1 288 ? -18.711 -14.689 -1.780  1.00 68.81  ? 286 HIS A CB    1 
ATOM   2230 C  CG    . HIS A 1 288 ? -17.778 -14.290 -0.688  1.00 70.06  ? 286 HIS A CG    1 
ATOM   2231 N  ND1   . HIS A 1 288 ? -16.477 -13.943 -0.983  1.00 71.10  ? 286 HIS A ND1   1 
ATOM   2232 C  CD2   . HIS A 1 288 ? -17.918 -14.108 0.634   1.00 71.16  ? 286 HIS A CD2   1 
ATOM   2233 C  CE1   . HIS A 1 288 ? -15.856 -13.583 0.123   1.00 67.94  ? 286 HIS A CE1   1 
ATOM   2234 N  NE2   . HIS A 1 288 ? -16.709 -13.685 1.121   1.00 67.36  ? 286 HIS A NE2   1 
ATOM   2235 N  N     . ASN A 1 289 ? -18.124 -12.089 -3.604  1.00 66.50  ? 287 ASN A N     1 
ATOM   2236 C  CA    . ASN A 1 289 ? -17.233 -10.963 -3.864  1.00 59.44  ? 287 ASN A CA    1 
ATOM   2237 C  C     . ASN A 1 289 ? -17.979 -9.674  -4.233  1.00 66.11  ? 287 ASN A C     1 
ATOM   2238 O  O     . ASN A 1 289 ? -17.441 -8.576  -4.002  1.00 60.20  ? 287 ASN A O     1 
ATOM   2239 C  CB    . ASN A 1 289 ? -16.214 -11.312 -4.953  1.00 60.56  ? 287 ASN A CB    1 
ATOM   2240 C  CG    . ASN A 1 289 ? -14.982 -12.014 -4.419  1.00 65.66  ? 287 ASN A CG    1 
ATOM   2241 O  OD1   . ASN A 1 289 ? -14.791 -12.121 -3.208  1.00 61.23  ? 287 ASN A OD1   1 
ATOM   2242 N  ND2   . ASN A 1 289 ? -14.122 -12.469 -5.317  1.00 69.49  ? 287 ASN A ND2   1 
ATOM   2243 N  N     . LYS A 1 290 ? -19.180 -9.791  -4.834  1.00 68.76  ? 288 LYS A N     1 
ATOM   2244 C  CA    . LYS A 1 290 ? -19.990 -8.624  -5.180  1.00 69.17  ? 288 LYS A CA    1 
ATOM   2245 C  C     . LYS A 1 290 ? -20.640 -8.034  -3.921  1.00 60.27  ? 288 LYS A C     1 
ATOM   2246 O  O     . LYS A 1 290 ? -20.580 -6.820  -3.703  1.00 56.51  ? 288 LYS A O     1 
ATOM   2247 C  CB    . LYS A 1 290 ? -21.053 -8.975  -6.232  1.00 72.12  ? 288 LYS A CB    1 
ATOM   2248 C  CG    . LYS A 1 290 ? -20.537 -9.309  -7.630  1.00 77.87  ? 288 LYS A CG    1 
ATOM   2249 N  N     . LEU A 1 291 ? -21.276 -8.893  -3.105  1.00 57.30  ? 289 LEU A N     1 
ATOM   2250 C  CA    . LEU A 1 291 ? -21.764 -8.515  -1.780  1.00 51.74  ? 289 LEU A CA    1 
ATOM   2251 C  C     . LEU A 1 291 ? -20.647 -7.885  -0.938  1.00 48.00  ? 289 LEU A C     1 
ATOM   2252 O  O     . LEU A 1 291 ? -20.880 -6.899  -0.237  1.00 43.71  ? 289 LEU A O     1 
ATOM   2253 C  CB    . LEU A 1 291 ? -22.326 -9.749  -1.054  1.00 54.46  ? 289 LEU A CB    1 
ATOM   2254 C  CG    . LEU A 1 291 ? -22.508 -9.583  0.459   1.00 56.63  ? 289 LEU A CG    1 
ATOM   2255 C  CD1   . LEU A 1 291 ? -23.616 -8.575  0.772   1.00 56.53  ? 289 LEU A CD1   1 
ATOM   2256 C  CD2   . LEU A 1 291 ? -22.757 -10.911 1.165   1.00 60.77  ? 289 LEU A CD2   1 
ATOM   2257 N  N     . LYS A 1 292 ? -19.446 -8.484  -0.969  1.00 45.70  ? 290 LYS A N     1 
ATOM   2258 C  CA    . LYS A 1 292 ? -18.332 -7.986  -0.180  1.00 43.99  ? 290 LYS A CA    1 
ATOM   2259 C  C     . LYS A 1 292 ? -17.959 -6.570  -0.622  1.00 40.47  ? 290 LYS A C     1 
ATOM   2260 O  O     . LYS A 1 292 ? -17.666 -5.740  0.238   1.00 37.89  ? 290 LYS A O     1 
ATOM   2261 C  CB    . LYS A 1 292 ? -17.162 -8.976  -0.212  1.00 45.99  ? 290 LYS A CB    1 
ATOM   2262 C  CG    . LYS A 1 292 ? -17.295 -10.148 0.757   1.00 47.32  ? 290 LYS A CG    1 
ATOM   2263 C  CD    . LYS A 1 292 ? -17.379 -9.725  2.216   1.00 50.23  ? 290 LYS A CD    1 
ATOM   2264 C  CE    . LYS A 1 292 ? -17.841 -10.818 3.163   1.00 51.70  ? 290 LYS A CE    1 
ATOM   2265 N  NZ    . LYS A 1 292 ? -17.954 -10.310 4.560   1.00 43.12  ? 290 LYS A NZ    1 
ATOM   2266 N  N     . ALA A 1 293 ? -18.032 -6.284  -1.933  1.00 41.38  ? 291 ALA A N     1 
ATOM   2267 C  CA    . ALA A 1 293 ? -17.749 -4.946  -2.449  1.00 40.47  ? 291 ALA A CA    1 
ATOM   2268 C  C     . ALA A 1 293 ? -18.750 -3.920  -1.902  1.00 39.66  ? 291 ALA A C     1 
ATOM   2269 O  O     . ALA A 1 293 ? -18.355 -2.836  -1.500  1.00 36.15  ? 291 ALA A O     1 
ATOM   2270 C  CB    . ALA A 1 293 ? -17.719 -4.933  -3.961  1.00 40.35  ? 291 ALA A CB    1 
ATOM   2271 N  N     A SER A 1 294 ? -20.041 -4.283  -1.888  0.47 39.39  ? 292 SER A N     1 
ATOM   2272 N  N     B SER A 1 294 ? -20.042 -4.267  -1.889  0.53 39.10  ? 292 SER A N     1 
ATOM   2273 C  CA    A SER A 1 294 ? -21.074 -3.431  -1.319  0.47 38.55  ? 292 SER A CA    1 
ATOM   2274 C  CA    B SER A 1 294 ? -21.045 -3.387  -1.312  0.53 37.98  ? 292 SER A CA    1 
ATOM   2275 C  C     A SER A 1 294 ? -20.817 -3.195  0.170   0.47 36.15  ? 292 SER A C     1 
ATOM   2276 C  C     B SER A 1 294 ? -20.786 -3.179  0.179   0.53 35.82  ? 292 SER A C     1 
ATOM   2277 O  O     A SER A 1 294 ? -20.974 -2.080  0.655   0.47 34.70  ? 292 SER A O     1 
ATOM   2278 O  O     B SER A 1 294 ? -20.912 -2.064  0.675   0.53 34.43  ? 292 SER A O     1 
ATOM   2279 C  CB    A SER A 1 294 ? -22.466 -3.987  -1.569  0.47 40.45  ? 292 SER A CB    1 
ATOM   2280 C  CB    B SER A 1 294 ? -22.445 -3.884  -1.566  0.53 38.80  ? 292 SER A CB    1 
ATOM   2281 O  OG    A SER A 1 294 ? -22.680 -5.211  -0.872  0.47 39.88  ? 292 SER A OG    1 
ATOM   2282 O  OG    B SER A 1 294 ? -22.766 -3.771  -2.939  0.53 37.83  ? 292 SER A OG    1 
ATOM   2283 N  N     . GLN A 1 295 ? -20.411 -4.239  0.895   1.00 35.90  ? 293 GLN A N     1 
ATOM   2284 C  CA    . GLN A 1 295 ? -20.129 -4.119  2.316   1.00 33.96  ? 293 GLN A CA    1 
ATOM   2285 C  C     . GLN A 1 295 ? -18.922 -3.212  2.532   1.00 32.22  ? 293 GLN A C     1 
ATOM   2286 O  O     . GLN A 1 295 ? -18.905 -2.426  3.476   1.00 30.33  ? 293 GLN A O     1 
ATOM   2287 C  CB    . GLN A 1 295 ? -19.861 -5.480  2.970   1.00 34.74  ? 293 GLN A CB    1 
ATOM   2288 C  CG    . GLN A 1 295 ? -21.040 -6.429  2.972   1.00 38.39  ? 293 GLN A CG    1 
ATOM   2289 C  CD    . GLN A 1 295 ? -20.750 -7.726  3.690   1.00 40.66  ? 293 GLN A CD    1 
ATOM   2290 O  OE1   . GLN A 1 295 ? -19.603 -8.084  3.931   1.00 42.14  ? 293 GLN A OE1   1 
ATOM   2291 N  NE2   . GLN A 1 295 ? -21.788 -8.462  4.037   1.00 41.03  ? 293 GLN A NE2   1 
ATOM   2292 N  N     . ALA A 1 296 ? -17.901 -3.337  1.668   1.00 32.54  ? 294 ALA A N     1 
ATOM   2293 C  CA    . ALA A 1 296 ? -16.714 -2.504  1.773   1.00 31.93  ? 294 ALA A CA    1 
ATOM   2294 C  C     . ALA A 1 296 ? -17.077 -1.033  1.584   1.00 29.90  ? 294 ALA A C     1 
ATOM   2295 O  O     . ALA A 1 296 ? -16.549 -0.199  2.305   1.00 28.66  ? 294 ALA A O     1 
ATOM   2296 C  CB    . ALA A 1 296 ? -15.661 -2.924  0.766   1.00 32.85  ? 294 ALA A CB    1 
ATOM   2297 N  N     . ARG A 1 297 ? -17.923 -0.726  0.582   1.00 29.78  ? 295 ARG A N     1 
ATOM   2298 C  CA    . ARG A 1 297 ? -18.308 0.654   0.287   1.00 31.51  ? 295 ARG A CA    1 
ATOM   2299 C  C     . ARG A 1 297 ? -19.148 1.200   1.444   1.00 29.91  ? 295 ARG A C     1 
ATOM   2300 O  O     . ARG A 1 297 ? -19.033 2.370   1.819   1.00 28.90  ? 295 ARG A O     1 
ATOM   2301 C  CB    . ARG A 1 297 ? -19.083 0.786   -1.035  1.00 34.34  ? 295 ARG A CB    1 
ATOM   2302 C  CG    . ARG A 1 297 ? -18.247 0.836   -2.313  1.00 37.38  ? 295 ARG A CG    1 
ATOM   2303 C  CD    . ARG A 1 297 ? -19.094 1.058   -3.589  1.00 38.51  ? 295 ARG A CD    1 
ATOM   2304 N  NE    . ARG A 1 297 ? -19.888 -0.106  -3.934  1.00 43.14  ? 295 ARG A NE    1 
ATOM   2305 C  CZ    . ARG A 1 297 ? -19.558 -1.037  -4.835  1.00 45.30  ? 295 ARG A CZ    1 
ATOM   2306 N  NH1   . ARG A 1 297 ? -18.488 -0.910  -5.608  1.00 43.44  ? 295 ARG A NH1   1 
ATOM   2307 N  NH2   . ARG A 1 297 ? -20.320 -2.108  -4.962  1.00 50.51  ? 295 ARG A NH2   1 
ATOM   2308 N  N     . ASP A 1 298 ? -19.986 0.333   2.024   1.00 30.19  ? 296 ASP A N     1 
ATOM   2309 C  CA    . ASP A 1 298 ? -20.777 0.706   3.183   1.00 30.35  ? 296 ASP A CA    1 
ATOM   2310 C  C     . ASP A 1 298 ? -19.852 1.096   4.337   1.00 27.54  ? 296 ASP A C     1 
ATOM   2311 O  O     . ASP A 1 298 ? -20.045 2.158   4.918   1.00 27.40  ? 296 ASP A O     1 
ATOM   2312 C  CB    . ASP A 1 298 ? -21.757 -0.404  3.577   1.00 33.58  ? 296 ASP A CB    1 
ATOM   2313 C  CG    . ASP A 1 298 ? -22.657 -0.001  4.721   1.00 33.15  ? 296 ASP A CG    1 
ATOM   2314 O  OD1   . ASP A 1 298 ? -23.571 0.764   4.463   1.00 36.84  ? 296 ASP A OD1   1 
ATOM   2315 O  OD2   . ASP A 1 298 ? -22.379 -0.387  5.860   1.00 33.29  ? 296 ASP A OD2   1 
ATOM   2316 N  N     . LEU A 1 299 ? -18.813 0.305   4.622   1.00 26.29  ? 297 LEU A N     1 
ATOM   2317 C  CA    . LEU A 1 299 ? -17.880 0.646   5.686   1.00 25.03  ? 297 LEU A CA    1 
ATOM   2318 C  C     . LEU A 1 299 ? -17.138 1.938   5.361   1.00 25.39  ? 297 LEU A C     1 
ATOM   2319 O  O     . LEU A 1 299 ? -17.028 2.793   6.225   1.00 23.05  ? 297 LEU A O     1 
ATOM   2320 C  CB    . LEU A 1 299 ? -16.872 -0.482  5.959   1.00 24.58  ? 297 LEU A CB    1 
ATOM   2321 C  CG    . LEU A 1 299 ? -15.910 -0.269  7.133   1.00 22.48  ? 297 LEU A CG    1 
ATOM   2322 C  CD1   . LEU A 1 299 ? -16.603 0.108   8.470   1.00 22.99  ? 297 LEU A CD1   1 
ATOM   2323 C  CD2   . LEU A 1 299 ? -15.051 -1.505  7.285   1.00 22.47  ? 297 LEU A CD2   1 
ATOM   2324 N  N     . LEU A 1 300 ? -16.624 2.078   4.126   1.00 27.04  ? 298 LEU A N     1 
ATOM   2325 C  CA    . LEU A 1 300 ? -15.951 3.312   3.752   1.00 26.82  ? 298 LEU A CA    1 
ATOM   2326 C  C     . LEU A 1 300 ? -16.871 4.502   3.961   1.00 27.93  ? 298 LEU A C     1 
ATOM   2327 O  O     . LEU A 1 300 ? -16.422 5.533   4.445   1.00 27.53  ? 298 LEU A O     1 
ATOM   2328 C  CB    . LEU A 1 300 ? -15.506 3.255   2.292   1.00 26.17  ? 298 LEU A CB    1 
ATOM   2329 C  CG    . LEU A 1 300 ? -14.234 2.479   2.048   1.00 29.15  ? 298 LEU A CG    1 
ATOM   2330 C  CD1   . LEU A 1 300 ? -14.113 2.111   0.577   1.00 32.94  ? 298 LEU A CD1   1 
ATOM   2331 C  CD2   . LEU A 1 300 ? -13.055 3.330   2.518   1.00 28.82  ? 298 LEU A CD2   1 
ATOM   2332 N  N     . SER A 1 301 ? -18.137 4.374   3.560   1.00 27.02  ? 299 SER A N     1 
ATOM   2333 C  CA    . SER A 1 301 ? -19.051 5.496   3.621   1.00 27.70  ? 299 SER A CA    1 
ATOM   2334 C  C     . SER A 1 301 ? -19.339 5.912   5.061   1.00 28.51  ? 299 SER A C     1 
ATOM   2335 O  O     . SER A 1 301 ? -19.903 6.985   5.261   1.00 29.05  ? 299 SER A O     1 
ATOM   2336 C  CB    . SER A 1 301 ? -20.341 5.166   2.913   1.00 29.71  ? 299 SER A CB    1 
ATOM   2337 O  OG    . SER A 1 301 ? -21.137 4.318   3.743   1.00 27.60  ? 299 SER A OG    1 
ATOM   2338 N  N     . LYS A 1 302 ? -18.993 5.069   6.046   1.00 26.39  ? 300 LYS A N     1 
ATOM   2339 C  CA    . LYS A 1 302 ? -19.193 5.378   7.457   1.00 27.19  ? 300 LYS A CA    1 
ATOM   2340 C  C     . LYS A 1 302 ? -17.903 5.871   8.115   1.00 26.52  ? 300 LYS A C     1 
ATOM   2341 O  O     . LYS A 1 302 ? -17.939 6.470   9.187   1.00 26.86  ? 300 LYS A O     1 
ATOM   2342 C  CB    . LYS A 1 302 ? -19.775 4.176   8.224   1.00 26.70  ? 300 LYS A CB    1 
ATOM   2343 C  CG    . LYS A 1 302 ? -21.250 3.902   7.932   1.00 27.89  ? 300 LYS A CG    1 
ATOM   2344 C  CD    . LYS A 1 302 ? -21.745 2.524   8.333   1.00 28.24  ? 300 LYS A CD    1 
ATOM   2345 C  CE    . LYS A 1 302 ? -23.230 2.373   8.050   1.00 30.03  ? 300 LYS A CE    1 
ATOM   2346 N  NZ    . LYS A 1 302 ? -23.577 0.953   7.879   1.00 34.69  ? 300 LYS A NZ    1 
ATOM   2347 N  N     . MET A 1 303 ? -16.749 5.638   7.489   1.00 23.80  ? 301 MET A N     1 
ATOM   2348 C  CA    . MET A 1 303 ? -15.500 6.040   8.117   1.00 22.50  ? 301 MET A CA    1 
ATOM   2349 C  C     . MET A 1 303 ? -15.028 7.356   7.496   1.00 22.26  ? 301 MET A C     1 
ATOM   2350 O  O     . MET A 1 303 ? -14.492 8.200   8.191   1.00 23.23  ? 301 MET A O     1 
ATOM   2351 C  CB    . MET A 1 303 ? -14.437 4.948   7.961   1.00 23.36  ? 301 MET A CB    1 
ATOM   2352 C  CG    . MET A 1 303 ? -14.821 3.656   8.705   1.00 25.67  ? 301 MET A CG    1 
ATOM   2353 S  SD    . MET A 1 303 ? -13.405 2.521   8.867   1.00 33.10  ? 301 MET A SD    1 
ATOM   2354 C  CE    . MET A 1 303 ? -12.951 2.370   7.187   1.00 22.34  ? 301 MET A CE    1 
ATOM   2355 N  N     . LEU A 1 304 ? -15.242 7.510   6.193   1.00 23.20  ? 302 LEU A N     1 
ATOM   2356 C  CA    . LEU A 1 304 ? -14.826 8.695   5.461   1.00 24.29  ? 302 LEU A CA    1 
ATOM   2357 C  C     . LEU A 1 304 ? -15.973 9.700   5.485   1.00 24.99  ? 302 LEU A C     1 
ATOM   2358 O  O     . LEU A 1 304 ? -16.641 9.990   4.474   1.00 24.77  ? 302 LEU A O     1 
ATOM   2359 C  CB    . LEU A 1 304 ? -14.412 8.275   4.063   1.00 23.69  ? 302 LEU A CB    1 
ATOM   2360 C  CG    . LEU A 1 304 ? -13.094 7.528   3.945   1.00 25.18  ? 302 LEU A CG    1 
ATOM   2361 C  CD1   . LEU A 1 304 ? -12.797 7.243   2.487   1.00 26.09  ? 302 LEU A CD1   1 
ATOM   2362 C  CD2   . LEU A 1 304 ? -11.928 8.270   4.606   1.00 27.46  ? 302 LEU A CD2   1 
ATOM   2363 N  N     . VAL A 1 305 ? -16.176 10.206  6.703   1.00 24.43  ? 303 VAL A N     1 
ATOM   2364 C  CA    . VAL A 1 305 ? -17.230 11.154  7.032   1.00 25.75  ? 303 VAL A CA    1 
ATOM   2365 C  C     . VAL A 1 305 ? -16.566 12.377  7.648   1.00 25.38  ? 303 VAL A C     1 
ATOM   2366 O  O     . VAL A 1 305 ? -15.934 12.269  8.698   1.00 24.08  ? 303 VAL A O     1 
ATOM   2367 C  CB    . VAL A 1 305 ? -18.236 10.539  8.015   1.00 26.12  ? 303 VAL A CB    1 
ATOM   2368 C  CG1   . VAL A 1 305 ? -19.295 11.545  8.409   1.00 28.24  ? 303 VAL A CG1   1 
ATOM   2369 C  CG2   . VAL A 1 305 ? -18.897 9.286   7.449   1.00 26.56  ? 303 VAL A CG2   1 
ATOM   2370 N  N     . ILE A 1 306 ? -16.709 13.541  7.004   1.00 24.61  ? 304 ILE A N     1 
ATOM   2371 C  CA    . ILE A 1 306 ? -15.943 14.711  7.421   1.00 24.74  ? 304 ILE A CA    1 
ATOM   2372 C  C     . ILE A 1 306 ? -16.291 15.080  8.860   1.00 23.76  ? 304 ILE A C     1 
ATOM   2373 O  O     . ILE A 1 306 ? -15.405 15.398  9.643   1.00 27.14  ? 304 ILE A O     1 
ATOM   2374 C  CB    . ILE A 1 306 ? -16.167 15.882  6.439   1.00 25.41  ? 304 ILE A CB    1 
ATOM   2375 C  CG1   . ILE A 1 306 ? -15.494 15.579  5.090   1.00 26.96  ? 304 ILE A CG1   1 
ATOM   2376 C  CG2   . ILE A 1 306 ? -15.704 17.200  7.061   1.00 27.78  ? 304 ILE A CG2   1 
ATOM   2377 C  CD1   . ILE A 1 306 ? -15.722 16.606  4.011   1.00 26.66  ? 304 ILE A CD1   1 
ATOM   2378 N  N     . ASP A 1 307 ? -17.591 15.172  9.157   1.00 26.56  ? 305 ASP A N     1 
ATOM   2379 C  CA    . ASP A 1 307 ? -18.099 15.545  10.468  1.00 27.49  ? 305 ASP A CA    1 
ATOM   2380 C  C     . ASP A 1 307 ? -17.987 14.349  11.424  1.00 27.13  ? 305 ASP A C     1 
ATOM   2381 O  O     . ASP A 1 307 ? -18.739 13.390  11.338  1.00 25.43  ? 305 ASP A O     1 
ATOM   2382 C  CB    . ASP A 1 307 ? -19.550 16.015  10.342  1.00 29.86  ? 305 ASP A CB    1 
ATOM   2383 C  CG    . ASP A 1 307 ? -20.180 16.506  11.635  1.00 32.73  ? 305 ASP A CG    1 
ATOM   2384 O  OD1   . ASP A 1 307 ? -19.603 16.288  12.724  1.00 32.20  ? 305 ASP A OD1   1 
ATOM   2385 O  OD2   . ASP A 1 307 ? -21.243 17.112  11.541  1.00 39.89  ? 305 ASP A OD2   1 
ATOM   2386 N  N     . ALA A 1 308 ? -17.066 14.413  12.376  1.00 26.23  ? 306 ALA A N     1 
ATOM   2387 C  CA    . ALA A 1 308 ? -16.808 13.270  13.240  1.00 25.64  ? 306 ALA A CA    1 
ATOM   2388 C  C     . ALA A 1 308 ? -18.021 12.882  14.075  1.00 27.46  ? 306 ALA A C     1 
ATOM   2389 O  O     . ALA A 1 308 ? -18.082 11.742  14.550  1.00 27.53  ? 306 ALA A O     1 
ATOM   2390 C  CB    . ALA A 1 308 ? -15.640 13.569  14.153  1.00 24.19  ? 306 ALA A CB    1 
ATOM   2391 N  N     . SER A 1 309 ? -18.951 13.813  14.308  1.00 27.49  ? 307 SER A N     1 
ATOM   2392 C  CA    . SER A 1 309 ? -20.146 13.489  15.073  1.00 30.24  ? 307 SER A CA    1 
ATOM   2393 C  C     . SER A 1 309 ? -21.045 12.512  14.308  1.00 31.60  ? 307 SER A C     1 
ATOM   2394 O  O     . SER A 1 309 ? -21.894 11.866  14.906  1.00 33.52  ? 307 SER A O     1 
ATOM   2395 C  CB    . SER A 1 309 ? -20.904 14.743  15.461  1.00 31.44  ? 307 SER A CB    1 
ATOM   2396 O  OG    . SER A 1 309 ? -21.457 15.364  14.314  1.00 33.62  ? 307 SER A OG    1 
ATOM   2397 N  N     . LYS A 1 310 ? -20.857 12.380  12.992  1.00 30.74  ? 308 LYS A N     1 
ATOM   2398 C  CA    . LYS A 1 310 ? -21.618 11.408  12.214  1.00 31.65  ? 308 LYS A CA    1 
ATOM   2399 C  C     . LYS A 1 310 ? -20.727 10.253  11.734  1.00 29.31  ? 308 LYS A C     1 
ATOM   2400 O  O     . LYS A 1 310 ? -21.143 9.461   10.911  1.00 30.42  ? 308 LYS A O     1 
ATOM   2401 C  CB    . LYS A 1 310 ? -22.268 12.120  11.026  1.00 34.14  ? 308 LYS A CB    1 
ATOM   2402 C  CG    . LYS A 1 310 ? -23.177 13.314  11.353  1.00 41.84  ? 308 LYS A CG    1 
ATOM   2403 C  CD    . LYS A 1 310 ? -23.265 14.278  10.153  1.00 51.31  ? 308 LYS A CD    1 
ATOM   2404 C  CE    . LYS A 1 310 ? -24.468 15.199  10.117  1.00 58.88  ? 308 LYS A CE    1 
ATOM   2405 N  NZ    . LYS A 1 310 ? -24.416 16.204  11.202  1.00 67.10  ? 308 LYS A NZ    1 
ATOM   2406 N  N     . ARG A 1 311 ? -19.505 10.139  12.244  1.00 24.73  ? 309 ARG A N     1 
ATOM   2407 C  CA    . ARG A 1 311 ? -18.555 9.129   11.791  1.00 26.08  ? 309 ARG A CA    1 
ATOM   2408 C  C     . ARG A 1 311 ? -18.604 7.931   12.729  1.00 25.96  ? 309 ARG A C     1 
ATOM   2409 O  O     . ARG A 1 311 ? -18.715 8.081   13.936  1.00 26.64  ? 309 ARG A O     1 
ATOM   2410 C  CB    . ARG A 1 311 ? -17.136 9.707   11.748  1.00 24.12  ? 309 ARG A CB    1 
ATOM   2411 C  CG    . ARG A 1 311 ? -16.065 8.789   11.186  1.00 22.64  ? 309 ARG A CG    1 
ATOM   2412 C  CD    . ARG A 1 311 ? -14.690 9.400   11.390  1.00 24.87  ? 309 ARG A CD    1 
ATOM   2413 N  NE    . ARG A 1 311 ? -14.590 10.772  10.858  1.00 23.22  ? 309 ARG A NE    1 
ATOM   2414 C  CZ    . ARG A 1 311 ? -13.873 11.756  11.380  1.00 21.44  ? 309 ARG A CZ    1 
ATOM   2415 N  NH1   . ARG A 1 311 ? -13.068 11.531  12.403  1.00 20.54  ? 309 ARG A NH1   1 
ATOM   2416 N  NH2   . ARG A 1 311 ? -13.948 12.961  10.836  1.00 22.81  ? 309 ARG A NH2   1 
ATOM   2417 N  N     . ILE A 1 312 ? -18.473 6.725   12.168  1.00 28.25  ? 310 ILE A N     1 
ATOM   2418 C  CA    . ILE A 1 312 ? -18.578 5.512   12.962  1.00 27.69  ? 310 ILE A CA    1 
ATOM   2419 C  C     . ILE A 1 312 ? -17.448 5.403   13.994  1.00 26.33  ? 310 ILE A C     1 
ATOM   2420 O  O     . ILE A 1 312 ? -16.354 5.928   13.815  1.00 24.91  ? 310 ILE A O     1 
ATOM   2421 C  CB    . ILE A 1 312 ? -18.577 4.326   11.987  1.00 27.75  ? 310 ILE A CB    1 
ATOM   2422 C  CG1   . ILE A 1 312 ? -18.997 3.023   12.642  1.00 31.71  ? 310 ILE A CG1   1 
ATOM   2423 C  CG2   . ILE A 1 312 ? -17.219 4.151   11.332  1.00 25.51  ? 310 ILE A CG2   1 
ATOM   2424 C  CD1   . ILE A 1 312 ? -19.101 1.916   11.619  1.00 34.62  ? 310 ILE A CD1   1 
ATOM   2425 N  N     . SER A 1 313 ? -17.712 4.667   15.078  1.00 25.55  ? 311 SER A N     1 
ATOM   2426 C  CA    . SER A 1 313 ? -16.733 4.433   16.122  1.00 25.71  ? 311 SER A CA    1 
ATOM   2427 C  C     . SER A 1 313 ? -15.881 3.191   15.824  1.00 26.87  ? 311 SER A C     1 
ATOM   2428 O  O     . SER A 1 313 ? -16.199 2.389   14.954  1.00 24.33  ? 311 SER A O     1 
ATOM   2429 C  CB    . SER A 1 313 ? -17.412 4.255   17.423  1.00 29.53  ? 311 SER A CB    1 
ATOM   2430 O  OG    . SER A 1 313 ? -18.008 2.978   17.485  1.00 28.23  ? 311 SER A OG    1 
ATOM   2431 N  N     . VAL A 1 314 ? -14.796 3.018   16.584  1.00 24.16  ? 312 VAL A N     1 
ATOM   2432 C  CA    . VAL A 1 314 ? -13.945 1.853   16.416  1.00 24.45  ? 312 VAL A CA    1 
ATOM   2433 C  C     . VAL A 1 314 ? -14.730 0.588   16.724  1.00 25.72  ? 312 VAL A C     1 
ATOM   2434 O  O     . VAL A 1 314 ? -14.560 -0.402  16.020  1.00 24.99  ? 312 VAL A O     1 
ATOM   2435 C  CB    . VAL A 1 314 ? -12.687 1.962   17.289  1.00 25.70  ? 312 VAL A CB    1 
ATOM   2436 C  CG1   . VAL A 1 314 ? -11.938 0.634   17.410  1.00 27.43  ? 312 VAL A CG1   1 
ATOM   2437 C  CG2   . VAL A 1 314 ? -11.794 3.080   16.754  1.00 24.08  ? 312 VAL A CG2   1 
ATOM   2438 N  N     . ASP A 1 315 ? -15.552 0.606   17.784  1.00 23.80  ? 313 ASP A N     1 
ATOM   2439 C  CA    . ASP A 1 315 ? -16.284 -0.586  18.192  1.00 26.84  ? 313 ASP A CA    1 
ATOM   2440 C  C     . ASP A 1 315 ? -17.317 -0.958  17.135  1.00 26.82  ? 313 ASP A C     1 
ATOM   2441 O  O     . ASP A 1 315 ? -17.542 -2.138  16.845  1.00 28.94  ? 313 ASP A O     1 
ATOM   2442 C  CB    . ASP A 1 315 ? -16.977 -0.383  19.545  1.00 28.07  ? 313 ASP A CB    1 
ATOM   2443 C  CG    . ASP A 1 315 ? -16.029 -0.431  20.741  1.00 32.57  ? 313 ASP A CG    1 
ATOM   2444 O  OD1   . ASP A 1 315 ? -14.846 -0.719  20.569  1.00 34.31  ? 313 ASP A OD1   1 
ATOM   2445 O  OD2   . ASP A 1 315 ? -16.476 -0.145  21.840  1.00 41.09  ? 313 ASP A OD2   1 
ATOM   2446 N  N     . GLU A 1 316 ? -17.986 0.049   16.589  1.00 27.36  ? 314 GLU A N     1 
ATOM   2447 C  CA    . GLU A 1 316 ? -18.972 -0.158  15.533  1.00 27.26  ? 314 GLU A CA    1 
ATOM   2448 C  C     . GLU A 1 316 ? -18.289 -0.714  14.272  1.00 27.96  ? 314 GLU A C     1 
ATOM   2449 O  O     . GLU A 1 316 ? -18.820 -1.619  13.618  1.00 30.36  ? 314 GLU A O     1 
ATOM   2450 C  CB    . GLU A 1 316 ? -19.716 1.150   15.267  1.00 28.84  ? 314 GLU A CB    1 
ATOM   2451 C  CG    . GLU A 1 316 ? -20.847 1.461   16.253  1.00 32.11  ? 314 GLU A CG    1 
ATOM   2452 C  CD    . GLU A 1 316 ? -21.239 2.934   16.298  1.00 37.62  ? 314 GLU A CD    1 
ATOM   2453 O  OE1   . GLU A 1 316 ? -20.639 3.752   15.569  1.00 40.54  ? 314 GLU A OE1   1 
ATOM   2454 O  OE2   . GLU A 1 316 ? -22.120 3.273   17.078  1.00 46.44  ? 314 GLU A OE2   1 
ATOM   2455 N  N     . ALA A 1 317 ? -17.090 -0.223  13.950  1.00 23.49  ? 315 ALA A N     1 
ATOM   2456 C  CA    . ALA A 1 317 ? -16.368 -0.747  12.802  1.00 25.58  ? 315 ALA A CA    1 
ATOM   2457 C  C     . ALA A 1 317 ? -16.014 -2.230  12.993  1.00 26.51  ? 315 ALA A C     1 
ATOM   2458 O  O     . ALA A 1 317 ? -16.104 -3.007  12.043  1.00 26.32  ? 315 ALA A O     1 
ATOM   2459 C  CB    . ALA A 1 317 ? -15.133 0.045   12.548  1.00 25.26  ? 315 ALA A CB    1 
ATOM   2460 N  N     . LEU A 1 318 ? -15.576 -2.604  14.211  1.00 27.33  ? 316 LEU A N     1 
ATOM   2461 C  CA    . LEU A 1 318 ? -15.240 -3.989  14.512  1.00 25.42  ? 316 LEU A CA    1 
ATOM   2462 C  C     . LEU A 1 318 ? -16.443 -4.914  14.357  1.00 28.11  ? 316 LEU A C     1 
ATOM   2463 O  O     . LEU A 1 318 ? -16.250 -6.091  14.058  1.00 31.31  ? 316 LEU A O     1 
ATOM   2464 C  CB    . LEU A 1 318 ? -14.643 -4.089  15.924  1.00 23.13  ? 316 LEU A CB    1 
ATOM   2465 C  CG    . LEU A 1 318 ? -13.189 -3.646  15.993  1.00 23.15  ? 316 LEU A CG    1 
ATOM   2466 C  CD1   . LEU A 1 318 ? -12.742 -3.345  17.404  1.00 22.51  ? 316 LEU A CD1   1 
ATOM   2467 C  CD2   . LEU A 1 318 ? -12.256 -4.663  15.384  1.00 24.42  ? 316 LEU A CD2   1 
ATOM   2468 N  N     . GLN A 1 319 ? -17.657 -4.384  14.549  1.00 29.57  ? 317 GLN A N     1 
ATOM   2469 C  CA    . GLN A 1 319 ? -18.903 -5.125  14.429  1.00 32.51  ? 317 GLN A CA    1 
ATOM   2470 C  C     . GLN A 1 319 ? -19.476 -5.101  13.010  1.00 30.43  ? 317 GLN A C     1 
ATOM   2471 O  O     . GLN A 1 319 ? -20.444 -5.805  12.736  1.00 31.08  ? 317 GLN A O     1 
ATOM   2472 C  CB    . GLN A 1 319 ? -19.937 -4.544  15.403  1.00 35.99  ? 317 GLN A CB    1 
ATOM   2473 C  CG    . GLN A 1 319 ? -19.607 -4.803  16.874  1.00 41.18  ? 317 GLN A CG    1 
ATOM   2474 C  CD    . GLN A 1 319 ? -19.432 -6.278  17.176  1.00 50.90  ? 317 GLN A CD    1 
ATOM   2475 O  OE1   . GLN A 1 319 ? -20.147 -7.137  16.658  1.00 57.11  ? 317 GLN A OE1   1 
ATOM   2476 N  NE2   . GLN A 1 319 ? -18.448 -6.599  18.005  1.00 53.36  ? 317 GLN A NE2   1 
ATOM   2477 N  N     . HIS A 1 320 ? -18.896 -4.310  12.111  1.00 28.35  ? 318 HIS A N     1 
ATOM   2478 C  CA    . HIS A 1 320 ? -19.401 -4.199  10.746  1.00 28.42  ? 318 HIS A CA    1 
ATOM   2479 C  C     . HIS A 1 320 ? -19.249 -5.542  10.037  1.00 29.10  ? 318 HIS A C     1 
ATOM   2480 O  O     . HIS A 1 320 ? -18.236 -6.214  10.225  1.00 29.94  ? 318 HIS A O     1 
ATOM   2481 C  CB    . HIS A 1 320 ? -18.632 -3.123  9.967   1.00 27.47  ? 318 HIS A CB    1 
ATOM   2482 C  CG    . HIS A 1 320 ? -19.249 -2.797  8.664   1.00 28.03  ? 318 HIS A CG    1 
ATOM   2483 N  ND1   . HIS A 1 320 ? -19.054 -3.567  7.539   1.00 29.42  ? 318 HIS A ND1   1 
ATOM   2484 C  CD2   . HIS A 1 320 ? -20.060 -1.769  8.281   1.00 31.14  ? 318 HIS A CD2   1 
ATOM   2485 C  CE1   . HIS A 1 320 ? -19.772 -3.047  6.534   1.00 30.45  ? 318 HIS A CE1   1 
ATOM   2486 N  NE2   . HIS A 1 320 ? -20.380 -1.951  6.957   1.00 29.44  ? 318 HIS A NE2   1 
ATOM   2487 N  N     . PRO A 1 321 ? -20.220 -5.977  9.204   1.00 30.70  ? 319 PRO A N     1 
ATOM   2488 C  CA    . PRO A 1 321 ? -20.117 -7.283  8.544   1.00 32.95  ? 319 PRO A CA    1 
ATOM   2489 C  C     . PRO A 1 321 ? -18.839 -7.508  7.729   1.00 32.80  ? 319 PRO A C     1 
ATOM   2490 O  O     . PRO A 1 321 ? -18.451 -8.647  7.522   1.00 30.46  ? 319 PRO A O     1 
ATOM   2491 C  CB    . PRO A 1 321 ? -21.332 -7.351  7.617   1.00 35.01  ? 319 PRO A CB    1 
ATOM   2492 C  CG    . PRO A 1 321 ? -22.308 -6.321  8.153   1.00 35.27  ? 319 PRO A CG    1 
ATOM   2493 C  CD    . PRO A 1 321 ? -21.487 -5.293  8.898   1.00 33.00  ? 319 PRO A CD    1 
ATOM   2494 N  N     . TYR A 1 322 ? -18.171 -6.434  7.276   1.00 31.40  ? 320 TYR A N     1 
ATOM   2495 C  CA    . TYR A 1 322 ? -16.966 -6.593  6.476   1.00 27.45  ? 320 TYR A CA    1 
ATOM   2496 C  C     . TYR A 1 322 ? -15.815 -7.046  7.362   1.00 27.53  ? 320 TYR A C     1 
ATOM   2497 O  O     . TYR A 1 322 ? -14.931 -7.769  6.909   1.00 28.58  ? 320 TYR A O     1 
ATOM   2498 C  CB    . TYR A 1 322 ? -16.542 -5.278  5.821   1.00 27.96  ? 320 TYR A CB    1 
ATOM   2499 C  CG    . TYR A 1 322 ? -15.528 -5.427  4.695   1.00 28.29  ? 320 TYR A CG    1 
ATOM   2500 C  CD1   . TYR A 1 322 ? -15.867 -6.046  3.496   1.00 31.27  ? 320 TYR A CD1   1 
ATOM   2501 C  CD2   . TYR A 1 322 ? -14.229 -4.967  4.834   1.00 27.41  ? 320 TYR A CD2   1 
ATOM   2502 C  CE1   . TYR A 1 322 ? -14.952 -6.173  2.459   1.00 33.28  ? 320 TYR A CE1   1 
ATOM   2503 C  CE2   . TYR A 1 322 ? -13.304 -5.069  3.802   1.00 29.44  ? 320 TYR A CE2   1 
ATOM   2504 C  CZ    . TYR A 1 322 ? -13.664 -5.685  2.612   1.00 31.43  ? 320 TYR A CZ    1 
ATOM   2505 O  OH    . TYR A 1 322 ? -12.789 -5.805  1.564   1.00 31.73  ? 320 TYR A OH    1 
ATOM   2506 N  N     . ILE A 1 323 ? -15.846 -6.609  8.619   1.00 24.98  ? 321 ILE A N     1 
ATOM   2507 C  CA    . ILE A 1 323 ? -14.749 -6.778  9.560   1.00 24.95  ? 321 ILE A CA    1 
ATOM   2508 C  C     . ILE A 1 323 ? -14.979 -7.977  10.475  1.00 26.75  ? 321 ILE A C     1 
ATOM   2509 O  O     . ILE A 1 323 ? -14.020 -8.664  10.841  1.00 26.17  ? 321 ILE A O     1 
ATOM   2510 C  CB    . ILE A 1 323 ? -14.568 -5.488  10.378  1.00 25.43  ? 321 ILE A CB    1 
ATOM   2511 C  CG1   . ILE A 1 323 ? -14.263 -4.312  9.449   1.00 24.97  ? 321 ILE A CG1   1 
ATOM   2512 C  CG2   . ILE A 1 323 ? -13.485 -5.662  11.441  1.00 24.47  ? 321 ILE A CG2   1 
ATOM   2513 C  CD1   . ILE A 1 323 ? -12.906 -4.421  8.745   1.00 26.97  ? 321 ILE A CD1   1 
ATOM   2514 N  N     . ASN A 1 324 ? -16.243 -8.199  10.876  1.00 26.76  ? 322 ASN A N     1 
ATOM   2515 C  CA    . ASN A 1 324 ? -16.557 -8.981  12.066  1.00 29.04  ? 322 ASN A CA    1 
ATOM   2516 C  C     . ASN A 1 324 ? -16.377 -10.477 11.803  1.00 28.42  ? 322 ASN A C     1 
ATOM   2517 O  O     . ASN A 1 324 ? -16.425 -11.271 12.733  1.00 26.74  ? 322 ASN A O     1 
ATOM   2518 C  CB    . ASN A 1 324 ? -17.961 -8.676  12.617  1.00 28.75  ? 322 ASN A CB    1 
ATOM   2519 C  CG    . ASN A 1 324 ? -19.087 -9.252  11.777  1.00 32.63  ? 322 ASN A CG    1 
ATOM   2520 O  OD1   . ASN A 1 324 ? -18.970 -10.319 11.178  1.00 34.94  ? 322 ASN A OD1   1 
ATOM   2521 N  ND2   . ASN A 1 324 ? -20.216 -8.572  11.750  1.00 32.16  ? 322 ASN A ND2   1 
ATOM   2522 N  N     . VAL A 1 325 ? -16.141 -10.866 10.540  1.00 29.53  ? 323 VAL A N     1 
ATOM   2523 C  CA    . VAL A 1 325 ? -15.841 -12.248 10.198  1.00 28.97  ? 323 VAL A CA    1 
ATOM   2524 C  C     . VAL A 1 325 ? -14.531 -12.698 10.867  1.00 27.92  ? 323 VAL A C     1 
ATOM   2525 O  O     . VAL A 1 325 ? -14.264 -13.904 10.944  1.00 25.63  ? 323 VAL A O     1 
ATOM   2526 C  CB    . VAL A 1 325 ? -15.771 -12.431 8.667   1.00 30.01  ? 323 VAL A CB    1 
ATOM   2527 C  CG1   . VAL A 1 325 ? -17.104 -12.077 8.002   1.00 29.98  ? 323 VAL A CG1   1 
ATOM   2528 C  CG2   . VAL A 1 325 ? -14.598 -11.651 8.075   1.00 31.23  ? 323 VAL A CG2   1 
ATOM   2529 N  N     . TRP A 1 326 ? -13.730 -11.728 11.348  1.00 26.17  ? 324 TRP A N     1 
ATOM   2530 C  CA    . TRP A 1 326 ? -12.438 -12.010 11.965  1.00 27.46  ? 324 TRP A CA    1 
ATOM   2531 C  C     . TRP A 1 326 ? -12.455 -11.837 13.476  1.00 24.19  ? 324 TRP A C     1 
ATOM   2532 O  O     . TRP A 1 326 ? -11.420 -12.019 14.127  1.00 23.66  ? 324 TRP A O     1 
ATOM   2533 C  CB    . TRP A 1 326 ? -11.361 -11.080 11.402  1.00 27.54  ? 324 TRP A CB    1 
ATOM   2534 C  CG    . TRP A 1 326 ? -11.101 -11.274 9.934   1.00 26.54  ? 324 TRP A CG    1 
ATOM   2535 C  CD1   . TRP A 1 326 ? -11.359 -10.391 8.929   1.00 27.00  ? 324 TRP A CD1   1 
ATOM   2536 C  CD2   . TRP A 1 326 ? -10.432 -12.392 9.343   1.00 25.80  ? 324 TRP A CD2   1 
ATOM   2537 N  NE1   . TRP A 1 326 ? -10.926 -10.905 7.738   1.00 27.72  ? 324 TRP A NE1   1 
ATOM   2538 C  CE2   . TRP A 1 326 ? -10.349 -12.126 7.959   1.00 27.74  ? 324 TRP A CE2   1 
ATOM   2539 C  CE3   . TRP A 1 326 ? -9.883  -13.578 9.847   1.00 26.17  ? 324 TRP A CE3   1 
ATOM   2540 C  CZ2   . TRP A 1 326 ? -9.761  -13.010 7.064   1.00 28.61  ? 324 TRP A CZ2   1 
ATOM   2541 C  CZ3   . TRP A 1 326 ? -9.292  -14.444 8.951   1.00 27.88  ? 324 TRP A CZ3   1 
ATOM   2542 C  CH2   . TRP A 1 326 ? -9.229  -14.160 7.587   1.00 30.06  ? 324 TRP A CH2   1 
ATOM   2543 N  N     . TYR A 1 327 ? -13.612 -11.474 14.029  1.00 25.10  ? 325 TYR A N     1 
ATOM   2544 C  CA    . TYR A 1 327 ? -13.651 -11.003 15.405  1.00 26.24  ? 325 TYR A CA    1 
ATOM   2545 C  C     . TYR A 1 327 ? -13.286 -12.107 16.400  1.00 28.04  ? 325 TYR A C     1 
ATOM   2546 O  O     . TYR A 1 327 ? -13.901 -13.169 16.456  1.00 26.62  ? 325 TYR A O     1 
ATOM   2547 C  CB    . TYR A 1 327 ? -15.026 -10.421 15.693  1.00 26.04  ? 325 TYR A CB    1 
ATOM   2548 C  CG    . TYR A 1 327 ? -15.083 -9.626  16.985  1.00 27.98  ? 325 TYR A CG    1 
ATOM   2549 C  CD1   . TYR A 1 327 ? -15.296 -10.254 18.197  1.00 29.74  ? 325 TYR A CD1   1 
ATOM   2550 C  CD2   . TYR A 1 327 ? -14.987 -8.240  16.978  1.00 31.33  ? 325 TYR A CD2   1 
ATOM   2551 C  CE1   . TYR A 1 327 ? -15.347 -9.552  19.390  1.00 33.07  ? 325 TYR A CE1   1 
ATOM   2552 C  CE2   . TYR A 1 327 ? -15.046 -7.514  18.165  1.00 32.12  ? 325 TYR A CE2   1 
ATOM   2553 C  CZ    . TYR A 1 327 ? -15.229 -8.172  19.371  1.00 34.12  ? 325 TYR A CZ    1 
ATOM   2554 O  OH    . TYR A 1 327 ? -15.311 -7.497  20.548  1.00 34.90  ? 325 TYR A OH    1 
ATOM   2555 N  N     . ASP A 1 328 ? -12.306 -11.789 17.255  1.00 26.08  ? 326 ASP A N     1 
ATOM   2556 C  CA    . ASP A 1 328 ? -11.912 -12.658 18.339  1.00 27.16  ? 326 ASP A CA    1 
ATOM   2557 C  C     . ASP A 1 328 ? -11.695 -11.769 19.557  1.00 28.79  ? 326 ASP A C     1 
ATOM   2558 O  O     . ASP A 1 328 ? -10.805 -10.916 19.531  1.00 25.20  ? 326 ASP A O     1 
ATOM   2559 C  CB    . ASP A 1 328 ? -10.646 -13.442 17.979  1.00 27.04  ? 326 ASP A CB    1 
ATOM   2560 C  CG    . ASP A 1 328 ? -10.298 -14.525 19.009  1.00 28.34  ? 326 ASP A CG    1 
ATOM   2561 O  OD1   . ASP A 1 328 ? -10.758 -14.422 20.176  1.00 27.87  ? 326 ASP A OD1   1 
ATOM   2562 O  OD2   . ASP A 1 328 ? -9.615  -15.500 18.627  1.00 28.21  ? 326 ASP A OD2   1 
ATOM   2563 N  N     . PRO A 1 329 ? -12.480 -11.956 20.641  1.00 28.88  ? 327 PRO A N     1 
ATOM   2564 C  CA    . PRO A 1 329 ? -12.326 -11.145 21.841  1.00 32.45  ? 327 PRO A CA    1 
ATOM   2565 C  C     . PRO A 1 329 ? -10.929 -11.214 22.477  1.00 32.68  ? 327 PRO A C     1 
ATOM   2566 O  O     . PRO A 1 329 ? -10.534 -10.291 23.175  1.00 33.31  ? 327 PRO A O     1 
ATOM   2567 C  CB    . PRO A 1 329 ? -13.370 -11.687 22.843  1.00 33.24  ? 327 PRO A CB    1 
ATOM   2568 C  CG    . PRO A 1 329 ? -14.132 -12.768 22.128  1.00 33.99  ? 327 PRO A CG    1 
ATOM   2569 C  CD    . PRO A 1 329 ? -13.436 -13.056 20.816  1.00 32.21  ? 327 PRO A CD    1 
ATOM   2570 N  N     . SER A 1 330 ? -10.169 -12.295 22.259  1.00 34.83  ? 328 SER A N     1 
ATOM   2571 C  CA    . SER A 1 330 ? -8.796  -12.318 22.752  1.00 40.14  ? 328 SER A CA    1 
ATOM   2572 C  C     . SER A 1 330 ? -7.984  -11.129 22.208  1.00 40.85  ? 328 SER A C     1 
ATOM   2573 O  O     . SER A 1 330 ? -7.149  -10.589 22.924  1.00 44.72  ? 328 SER A O     1 
ATOM   2574 C  CB    . SER A 1 330 ? -8.143  -13.643 22.487  1.00 44.82  ? 328 SER A CB    1 
ATOM   2575 O  OG    . SER A 1 330 ? -8.700  -14.649 23.355  1.00 49.12  ? 328 SER A OG    1 
ATOM   2576 N  N     . GLU A 1 331 ? -8.266  -10.666 20.983  1.00 34.74  ? 329 GLU A N     1 
ATOM   2577 C  CA    . GLU A 1 331 ? -7.548  -9.527  20.418  1.00 31.73  ? 329 GLU A CA    1 
ATOM   2578 C  C     . GLU A 1 331 ? -8.387  -8.247  20.503  1.00 34.56  ? 329 GLU A C     1 
ATOM   2579 O  O     . GLU A 1 331 ? -7.871  -7.137  20.628  1.00 33.60  ? 329 GLU A O     1 
ATOM   2580 C  CB    . GLU A 1 331 ? -7.142  -9.883  18.984  1.00 37.29  ? 329 GLU A CB    1 
ATOM   2581 C  CG    . GLU A 1 331 ? -6.883  -11.383 18.819  1.00 40.11  ? 329 GLU A CG    1 
ATOM   2582 C  CD    . GLU A 1 331 ? -6.937  -11.955 17.414  1.00 42.13  ? 329 GLU A CD    1 
ATOM   2583 O  OE1   . GLU A 1 331 ? -7.890  -11.636 16.593  1.00 33.21  ? 329 GLU A OE1   1 
ATOM   2584 O  OE2   . GLU A 1 331 ? -6.043  -12.743 17.143  1.00 49.22  ? 329 GLU A OE2   1 
ATOM   2585 N  N     . ALA A 1 332 ? -9.705  -8.380  20.431  1.00 31.29  ? 330 ALA A N     1 
ATOM   2586 C  CA    . ALA A 1 332 ? -10.556 -7.221  20.303  1.00 31.95  ? 330 ALA A CA    1 
ATOM   2587 C  C     . ALA A 1 332 ? -11.031 -6.705  21.669  1.00 36.25  ? 330 ALA A C     1 
ATOM   2588 O  O     . ALA A 1 332 ? -11.566 -5.594  21.738  1.00 35.08  ? 330 ALA A O     1 
ATOM   2589 C  CB    . ALA A 1 332 ? -11.702 -7.588  19.408  1.00 32.48  ? 330 ALA A CB    1 
ATOM   2590 N  N     . GLU A 1 333 ? -10.864 -7.511  22.739  1.00 33.40  ? 331 GLU A N     1 
ATOM   2591 C  CA    . GLU A 1 333 ? -11.330 -7.167  24.074  1.00 36.17  ? 331 GLU A CA    1 
ATOM   2592 C  C     . GLU A 1 333 ? -10.250 -7.462  25.107  1.00 37.78  ? 331 GLU A C     1 
ATOM   2593 O  O     . GLU A 1 333 ? -10.544 -7.980  26.187  1.00 38.07  ? 331 GLU A O     1 
ATOM   2594 C  CB    . GLU A 1 333 ? -12.597 -7.949  24.428  1.00 35.20  ? 331 GLU A CB    1 
ATOM   2595 C  CG    . GLU A 1 333 ? -13.729 -7.660  23.462  1.00 36.93  ? 331 GLU A CG    1 
ATOM   2596 C  CD    . GLU A 1 333 ? -14.976 -8.496  23.628  1.00 38.40  ? 331 GLU A CD    1 
ATOM   2597 O  OE1   . GLU A 1 333 ? -15.187 -9.022  24.730  1.00 39.94  ? 331 GLU A OE1   1 
ATOM   2598 O  OE2   . GLU A 1 333 ? -15.694 -8.659  22.634  1.00 37.71  ? 331 GLU A OE2   1 
ATOM   2599 N  N     . ALA A 1 334 ? -8.999  -7.138  24.771  1.00 36.96  ? 332 ALA A N     1 
ATOM   2600 C  CA    . ALA A 1 334 ? -7.886  -7.380  25.670  1.00 38.53  ? 332 ALA A CA    1 
ATOM   2601 C  C     . ALA A 1 334 ? -7.960  -6.397  26.835  1.00 36.38  ? 332 ALA A C     1 
ATOM   2602 O  O     . ALA A 1 334 ? -8.487  -5.296  26.684  1.00 34.64  ? 332 ALA A O     1 
ATOM   2603 C  CB    . ALA A 1 334 ? -6.572  -7.254  24.930  1.00 42.97  ? 332 ALA A CB    1 
ATOM   2604 N  N     . PRO A 1 335 ? -7.431  -6.753  28.022  1.00 36.22  ? 333 PRO A N     1 
ATOM   2605 C  CA    . PRO A 1 335 ? -7.348  -5.808  29.134  1.00 37.39  ? 333 PRO A CA    1 
ATOM   2606 C  C     . PRO A 1 335 ? -6.509  -4.601  28.723  1.00 35.08  ? 333 PRO A C     1 
ATOM   2607 O  O     . PRO A 1 335 ? -5.474  -4.750  28.083  1.00 34.06  ? 333 PRO A O     1 
ATOM   2608 C  CB    . PRO A 1 335 ? -6.691  -6.578  30.285  1.00 39.01  ? 333 PRO A CB    1 
ATOM   2609 C  CG    . PRO A 1 335 ? -6.840  -8.037  29.887  1.00 41.45  ? 333 PRO A CG    1 
ATOM   2610 C  CD    . PRO A 1 335 ? -6.893  -8.068  28.374  1.00 40.84  ? 333 PRO A CD    1 
ATOM   2611 N  N     . PRO A 1 336 ? -6.921  -3.373  29.104  1.00 34.61  ? 334 PRO A N     1 
ATOM   2612 C  CA    . PRO A 1 336 ? -6.195  -2.181  28.709  1.00 34.61  ? 334 PRO A CA    1 
ATOM   2613 C  C     . PRO A 1 336 ? -4.768  -2.218  29.224  1.00 35.28  ? 334 PRO A C     1 
ATOM   2614 O  O     . PRO A 1 336 ? -4.490  -2.762  30.278  1.00 34.93  ? 334 PRO A O     1 
ATOM   2615 C  CB    . PRO A 1 336 ? -6.964  -1.044  29.389  1.00 38.97  ? 334 PRO A CB    1 
ATOM   2616 C  CG    . PRO A 1 336 ? -8.344  -1.629  29.564  1.00 41.26  ? 334 PRO A CG    1 
ATOM   2617 C  CD    . PRO A 1 336 ? -8.069  -3.057  29.970  1.00 38.13  ? 334 PRO A CD    1 
ATOM   2618 N  N     . PRO A 1 337 ? -3.828  -1.577  28.518  1.00 38.53  ? 335 PRO A N     1 
ATOM   2619 C  CA    . PRO A 1 337 ? -2.518  -1.304  29.097  1.00 39.20  ? 335 PRO A CA    1 
ATOM   2620 C  C     . PRO A 1 337 ? -2.676  -0.628  30.462  1.00 41.23  ? 335 PRO A C     1 
ATOM   2621 O  O     . PRO A 1 337 ? -3.605  0.152   30.677  1.00 38.38  ? 335 PRO A O     1 
ATOM   2622 C  CB    . PRO A 1 337 ? -1.880  -0.345  28.084  1.00 37.87  ? 335 PRO A CB    1 
ATOM   2623 C  CG    . PRO A 1 337 ? -2.622  -0.599  26.788  1.00 40.18  ? 335 PRO A CG    1 
ATOM   2624 C  CD    . PRO A 1 337 ? -4.030  -0.967  27.195  1.00 36.63  ? 335 PRO A CD    1 
ATOM   2625 N  N     . LYS A 1 338 ? -1.792  -0.983  31.397  1.00 39.03  ? 336 LYS A N     1 
ATOM   2626 C  CA    . LYS A 1 338 ? -1.682  -0.280  32.654  1.00 42.33  ? 336 LYS A CA    1 
ATOM   2627 C  C     . LYS A 1 338 ? -0.448  0.599   32.556  1.00 40.28  ? 336 LYS A C     1 
ATOM   2628 O  O     . LYS A 1 338 ? 0.677   0.113   32.631  1.00 42.44  ? 336 LYS A O     1 
ATOM   2629 C  CB    . LYS A 1 338 ? -1.596  -1.233  33.844  1.00 45.18  ? 336 LYS A CB    1 
ATOM   2630 C  CG    . LYS A 1 338 ? -2.833  -2.097  34.041  1.00 54.17  ? 336 LYS A CG    1 
ATOM   2631 C  CD    . LYS A 1 338 ? -2.635  -3.208  35.053  1.00 60.43  ? 336 LYS A CD    1 
ATOM   2632 C  CE    . LYS A 1 338 ? -3.890  -4.020  35.327  1.00 68.60  ? 336 LYS A CE    1 
ATOM   2633 N  NZ    . LYS A 1 338 ? -4.999  -3.188  35.854  1.00 70.52  ? 336 LYS A NZ    1 
ATOM   2634 N  N     . ILE A 1 339 ? -0.690  1.892   32.340  1.00 40.22  ? 337 ILE A N     1 
ATOM   2635 C  CA    . ILE A 1 339 ? 0.392   2.840   32.201  1.00 37.49  ? 337 ILE A CA    1 
ATOM   2636 C  C     . ILE A 1 339 ? 0.877   3.200   33.600  1.00 39.46  ? 337 ILE A C     1 
ATOM   2637 O  O     . ILE A 1 339 ? 0.102   3.719   34.402  1.00 42.08  ? 337 ILE A O     1 
ATOM   2638 C  CB    . ILE A 1 339 ? -0.062  4.070   31.400  1.00 34.86  ? 337 ILE A CB    1 
ATOM   2639 C  CG1   . ILE A 1 339 ? -0.668  3.653   30.053  1.00 33.85  ? 337 ILE A CG1   1 
ATOM   2640 C  CG2   . ILE A 1 339 ? 1.102   5.027   31.237  1.00 37.88  ? 337 ILE A CG2   1 
ATOM   2641 C  CD1   . ILE A 1 339 ? -1.187  4.814   29.244  1.00 35.39  ? 337 ILE A CD1   1 
ATOM   2642 N  N     . PRO A 1 340 ? 2.147   2.917   33.960  1.00 43.15  ? 338 PRO A N     1 
ATOM   2643 C  CA    . PRO A 1 340 ? 2.604   3.182   35.331  1.00 44.18  ? 338 PRO A CA    1 
ATOM   2644 C  C     . PRO A 1 340 ? 2.704   4.669   35.669  1.00 44.65  ? 338 PRO A C     1 
ATOM   2645 O  O     . PRO A 1 340 ? 2.515   5.066   36.819  1.00 47.45  ? 338 PRO A O     1 
ATOM   2646 C  CB    . PRO A 1 340 ? 3.974   2.489   35.419  1.00 43.21  ? 338 PRO A CB    1 
ATOM   2647 C  CG    . PRO A 1 340 ? 4.432   2.332   33.983  1.00 44.74  ? 338 PRO A CG    1 
ATOM   2648 C  CD    . PRO A 1 340 ? 3.189   2.322   33.104  1.00 43.16  ? 338 PRO A CD    1 
ATOM   2649 N  N     . ASP A 1 341 ? 3.015   5.499   34.668  1.00 42.99  ? 339 ASP A N     1 
ATOM   2650 C  CA    . ASP A 1 341 ? 3.146   6.931   34.882  1.00 44.02  ? 339 ASP A CA    1 
ATOM   2651 C  C     . ASP A 1 341 ? 1.761   7.552   34.761  1.00 44.64  ? 339 ASP A C     1 
ATOM   2652 O  O     . ASP A 1 341 ? 1.247   7.697   33.651  1.00 41.73  ? 339 ASP A O     1 
ATOM   2653 C  CB    . ASP A 1 341 ? 4.114   7.566   33.881  1.00 40.44  ? 339 ASP A CB    1 
ATOM   2654 C  CG    . ASP A 1 341 ? 4.275   9.049   34.106  1.00 41.98  ? 339 ASP A CG    1 
ATOM   2655 O  OD1   . ASP A 1 341 ? 3.619   9.561   35.041  1.00 42.54  ? 339 ASP A OD1   1 
ATOM   2656 O  OD2   . ASP A 1 341 ? 5.051   9.672   33.358  1.00 39.13  ? 339 ASP A OD2   1 
ATOM   2657 N  N     . LYS A 1 342 ? 1.178   7.910   35.909  1.00 45.54  ? 340 LYS A N     1 
ATOM   2658 C  CA    . LYS A 1 342 ? -0.177  8.434   35.952  1.00 50.15  ? 340 LYS A CA    1 
ATOM   2659 C  C     . LYS A 1 342 ? -0.247  9.858   35.400  1.00 48.86  ? 340 LYS A C     1 
ATOM   2660 O  O     . LYS A 1 342 ? -1.343  10.334  35.112  1.00 44.89  ? 340 LYS A O     1 
ATOM   2661 C  CB    . LYS A 1 342 ? -0.716  8.367   37.386  1.00 55.19  ? 340 LYS A CB    1 
ATOM   2662 C  CG    . LYS A 1 342 ? -0.733  6.966   37.992  1.00 60.57  ? 340 LYS A CG    1 
ATOM   2663 C  CD    . LYS A 1 342 ? -1.357  5.915   37.084  1.00 63.81  ? 340 LYS A CD    1 
ATOM   2664 C  CE    . LYS A 1 342 ? -1.097  4.492   37.534  1.00 65.91  ? 340 LYS A CE    1 
ATOM   2665 N  NZ    . LYS A 1 342 ? -1.559  3.510   36.519  1.00 66.48  ? 340 LYS A NZ    1 
ATOM   2666 N  N     . GLN A 1 343 ? 0.909   10.526  35.232  1.00 46.51  ? 341 GLN A N     1 
ATOM   2667 C  CA    . GLN A 1 343 ? 0.937   11.868  34.667  1.00 44.64  ? 341 GLN A CA    1 
ATOM   2668 C  C     . GLN A 1 343 ? 1.448   11.859  33.226  1.00 40.72  ? 341 GLN A C     1 
ATOM   2669 O  O     . GLN A 1 343 ? 1.883   12.903  32.722  1.00 41.06  ? 341 GLN A O     1 
ATOM   2670 C  CB    . GLN A 1 343 ? 1.817   12.781  35.523  1.00 46.43  ? 341 GLN A CB    1 
ATOM   2671 C  CG    . GLN A 1 343 ? 1.259   13.011  36.911  1.00 48.28  ? 341 GLN A CG    1 
ATOM   2672 C  CD    . GLN A 1 343 ? 2.157   13.934  37.686  1.00 57.44  ? 341 GLN A CD    1 
ATOM   2673 O  OE1   . GLN A 1 343 ? 1.946   15.147  37.709  1.00 63.22  ? 341 GLN A OE1   1 
ATOM   2674 N  NE2   . GLN A 1 343 ? 3.195   13.373  38.290  1.00 61.78  ? 341 GLN A NE2   1 
ATOM   2675 N  N     . LEU A 1 344 ? 1.416   10.697  32.565  1.00 36.49  ? 342 LEU A N     1 
ATOM   2676 C  CA    . LEU A 1 344 ? 1.869   10.624  31.187  1.00 36.96  ? 342 LEU A CA    1 
ATOM   2677 C  C     . LEU A 1 344 ? 1.089   11.656  30.373  1.00 38.25  ? 342 LEU A C     1 
ATOM   2678 O  O     . LEU A 1 344 ? -0.135  11.707  30.465  1.00 44.40  ? 342 LEU A O     1 
ATOM   2679 C  CB    . LEU A 1 344 ? 1.651   9.220   30.619  1.00 35.72  ? 342 LEU A CB    1 
ATOM   2680 C  CG    . LEU A 1 344 ? 2.202   9.016   29.210  1.00 38.00  ? 342 LEU A CG    1 
ATOM   2681 C  CD1   . LEU A 1 344 ? 3.717   9.100   29.192  1.00 39.38  ? 342 LEU A CD1   1 
ATOM   2682 C  CD2   . LEU A 1 344 ? 1.751   7.705   28.574  1.00 40.54  ? 342 LEU A CD2   1 
ATOM   2683 N  N     . ASP A 1 345 ? 1.813   12.478  29.602  1.00 40.11  ? 343 ASP A N     1 
ATOM   2684 C  CA    . ASP A 1 345 ? 1.258   13.491  28.702  1.00 40.01  ? 343 ASP A CA    1 
ATOM   2685 C  C     . ASP A 1 345 ? 0.639   14.678  29.447  1.00 38.49  ? 343 ASP A C     1 
ATOM   2686 O  O     . ASP A 1 345 ? -0.047  15.496  28.839  1.00 38.78  ? 343 ASP A O     1 
ATOM   2687 C  CB    . ASP A 1 345 ? 0.211   12.917  27.748  1.00 42.65  ? 343 ASP A CB    1 
ATOM   2688 C  CG    . ASP A 1 345 ? 0.768   11.892  26.778  1.00 42.51  ? 343 ASP A CG    1 
ATOM   2689 O  OD1   . ASP A 1 345 ? 1.916   12.070  26.323  1.00 40.14  ? 343 ASP A OD1   1 
ATOM   2690 O  OD2   . ASP A 1 345 ? 0.026   10.945  26.463  1.00 45.04  ? 343 ASP A OD2   1 
ATOM   2691 N  N     . GLU A 1 346 ? 0.858   14.764  30.758  1.00 37.77  ? 344 GLU A N     1 
ATOM   2692 C  CA    . GLU A 1 346 ? 0.320   15.867  31.540  1.00 43.72  ? 344 GLU A CA    1 
ATOM   2693 C  C     . GLU A 1 346 ? 1.450   16.575  32.280  1.00 39.17  ? 344 GLU A C     1 
ATOM   2694 O  O     . GLU A 1 346 ? 1.228   17.169  33.329  1.00 41.54  ? 344 GLU A O     1 
ATOM   2695 C  CB    . GLU A 1 346 ? -0.734  15.364  32.536  1.00 48.30  ? 344 GLU A CB    1 
ATOM   2696 C  CG    . GLU A 1 346 ? -1.890  14.613  31.891  1.00 56.43  ? 344 GLU A CG    1 
ATOM   2697 C  CD    . GLU A 1 346 ? -2.818  13.902  32.863  1.00 64.81  ? 344 GLU A CD    1 
ATOM   2698 O  OE1   . GLU A 1 346 ? -2.630  14.059  34.090  1.00 70.99  ? 344 GLU A OE1   1 
ATOM   2699 O  OE2   . GLU A 1 346 ? -3.725  13.186  32.393  1.00 72.32  ? 344 GLU A OE2   1 
ATOM   2700 N  N     . ARG A 1 347 ? 2.675   16.507  31.761  1.00 36.99  ? 345 ARG A N     1 
ATOM   2701 C  CA    . ARG A 1 347 ? 3.790   17.030  32.537  1.00 39.70  ? 345 ARG A CA    1 
ATOM   2702 C  C     . ARG A 1 347 ? 4.582   18.045  31.714  1.00 36.66  ? 345 ARG A C     1 
ATOM   2703 O  O     . ARG A 1 347 ? 4.701   17.940  30.493  1.00 32.03  ? 345 ARG A O     1 
ATOM   2704 C  CB    . ARG A 1 347 ? 4.610   15.880  33.141  1.00 44.13  ? 345 ARG A CB    1 
ATOM   2705 C  CG    . ARG A 1 347 ? 4.864   14.683  32.242  1.00 46.33  ? 345 ARG A CG    1 
ATOM   2706 C  CD    . ARG A 1 347 ? 5.822   13.654  32.851  1.00 46.78  ? 345 ARG A CD    1 
ATOM   2707 N  NE    . ARG A 1 347 ? 5.292   12.818  33.923  1.00 44.40  ? 345 ARG A NE    1 
ATOM   2708 C  CZ    . ARG A 1 347 ? 5.833   12.662  35.129  1.00 47.40  ? 345 ARG A CZ    1 
ATOM   2709 N  NH1   . ARG A 1 347 ? 6.910   13.332  35.498  1.00 50.76  ? 345 ARG A NH1   1 
ATOM   2710 N  NH2   . ARG A 1 347 ? 5.277   11.849  36.007  1.00 45.68  ? 345 ARG A NH2   1 
ATOM   2711 N  N     . GLU A 1 348 ? 5.030   19.102  32.389  1.00 33.45  ? 346 GLU A N     1 
ATOM   2712 C  CA    . GLU A 1 348 ? 5.993   20.024  31.815  1.00 29.95  ? 346 GLU A CA    1 
ATOM   2713 C  C     . GLU A 1 348 ? 7.262   19.887  32.634  1.00 29.04  ? 346 GLU A C     1 
ATOM   2714 O  O     . GLU A 1 348 ? 7.199   19.896  33.858  1.00 29.65  ? 346 GLU A O     1 
ATOM   2715 C  CB    . GLU A 1 348 ? 5.498   21.477  31.846  1.00 30.54  ? 346 GLU A CB    1 
ATOM   2716 C  CG    . GLU A 1 348 ? 4.119   21.687  31.255  1.00 33.12  ? 346 GLU A CG    1 
ATOM   2717 C  CD    . GLU A 1 348 ? 4.063   21.623  29.745  1.00 32.54  ? 346 GLU A CD    1 
ATOM   2718 O  OE1   . GLU A 1 348 ? 5.136   21.587  29.114  1.00 29.79  ? 346 GLU A OE1   1 
ATOM   2719 O  OE2   . GLU A 1 348 ? 2.961   21.615  29.219  1.00 37.16  ? 346 GLU A OE2   1 
ATOM   2720 N  N     . HIS A 1 349 ? 8.406   19.758  31.962  1.00 27.95  ? 347 HIS A N     1 
ATOM   2721 C  CA    . HIS A 1 349 ? 9.656   19.558  32.672  1.00 28.55  ? 347 HIS A CA    1 
ATOM   2722 C  C     . HIS A 1 349 ? 10.758  20.371  32.012  1.00 28.76  ? 347 HIS A C     1 
ATOM   2723 O  O     . HIS A 1 349 ? 10.705  20.638  30.812  1.00 27.84  ? 347 HIS A O     1 
ATOM   2724 C  CB    . HIS A 1 349 ? 10.063  18.074  32.734  1.00 29.64  ? 347 HIS A CB    1 
ATOM   2725 C  CG    . HIS A 1 349 ? 9.209   17.229  33.622  1.00 31.32  ? 347 HIS A CG    1 
ATOM   2726 N  ND1   . HIS A 1 349 ? 9.226   17.322  34.995  1.00 34.23  ? 347 HIS A ND1   1 
ATOM   2727 C  CD2   . HIS A 1 349 ? 8.347   16.250  33.327  1.00 34.56  ? 347 HIS A CD2   1 
ATOM   2728 C  CE1   . HIS A 1 349 ? 8.383   16.425  35.503  1.00 36.78  ? 347 HIS A CE1   1 
ATOM   2729 N  NE2   . HIS A 1 349 ? 7.824   15.771  34.501  1.00 34.24  ? 347 HIS A NE2   1 
ATOM   2730 N  N     . THR A 1 350 ? 11.737  20.746  32.844  1.00 28.69  ? 348 THR A N     1 
ATOM   2731 C  CA    . THR A 1 350 ? 12.994  21.306  32.392  1.00 29.20  ? 348 THR A CA    1 
ATOM   2732 C  C     . THR A 1 350 ? 13.784  20.264  31.612  1.00 30.89  ? 348 THR A C     1 
ATOM   2733 O  O     . THR A 1 350 ? 13.536  19.060  31.719  1.00 30.10  ? 348 THR A O     1 
ATOM   2734 C  CB    . THR A 1 350 ? 13.876  21.763  33.560  1.00 29.30  ? 348 THR A CB    1 
ATOM   2735 O  OG1   . THR A 1 350 ? 14.314  20.639  34.330  1.00 30.07  ? 348 THR A OG1   1 
ATOM   2736 C  CG2   . THR A 1 350 ? 13.194  22.740  34.491  1.00 31.17  ? 348 THR A CG2   1 
ATOM   2737 N  N     . ILE A 1 351 ? 14.779  20.761  30.877  1.00 29.84  ? 349 ILE A N     1 
ATOM   2738 C  CA    . ILE A 1 351 ? 15.640  19.926  30.061  1.00 30.74  ? 349 ILE A CA    1 
ATOM   2739 C  C     . ILE A 1 351 ? 16.326  18.882  30.947  1.00 33.39  ? 349 ILE A C     1 
ATOM   2740 O  O     . ILE A 1 351 ? 16.339  17.699  30.602  1.00 33.59  ? 349 ILE A O     1 
ATOM   2741 C  CB    . ILE A 1 351 ? 16.611  20.804  29.243  1.00 30.79  ? 349 ILE A CB    1 
ATOM   2742 C  CG1   . ILE A 1 351 ? 15.902  21.451  28.051  1.00 30.74  ? 349 ILE A CG1   1 
ATOM   2743 C  CG2   . ILE A 1 351 ? 17.806  20.006  28.742  1.00 33.74  ? 349 ILE A CG2   1 
ATOM   2744 C  CD1   . ILE A 1 351 ? 16.693  22.581  27.436  1.00 33.95  ? 349 ILE A CD1   1 
ATOM   2745 N  N     . GLU A 1 352 ? 16.844  19.298  32.115  1.00 33.47  ? 350 GLU A N     1 
ATOM   2746 C  CA    . GLU A 1 352 ? 17.503  18.368  33.011  1.00 37.72  ? 350 GLU A CA    1 
ATOM   2747 C  C     . GLU A 1 352 ? 16.514  17.380  33.634  1.00 33.30  ? 350 GLU A C     1 
ATOM   2748 O  O     . GLU A 1 352 ? 16.858  16.231  33.871  1.00 35.21  ? 350 GLU A O     1 
ATOM   2749 C  CB    . GLU A 1 352 ? 18.313  19.119  34.072  1.00 41.18  ? 350 GLU A CB    1 
ATOM   2750 C  CG    . GLU A 1 352 ? 19.593  19.750  33.524  1.00 45.89  ? 350 GLU A CG    1 
ATOM   2751 C  CD    . GLU A 1 352 ? 20.668  18.791  33.027  1.00 49.60  ? 350 GLU A CD    1 
ATOM   2752 O  OE1   . GLU A 1 352 ? 21.006  17.853  33.756  1.00 51.90  ? 350 GLU A OE1   1 
ATOM   2753 O  OE2   . GLU A 1 352 ? 21.202  19.016  31.931  1.00 55.27  ? 350 GLU A OE2   1 
ATOM   2754 N  N     . GLU A 1 353 ? 15.297  17.809  33.940  1.00 33.72  ? 351 GLU A N     1 
ATOM   2755 C  CA    . GLU A 1 353 ? 14.293  16.898  34.462  1.00 33.34  ? 351 GLU A CA    1 
ATOM   2756 C  C     . GLU A 1 353 ? 13.940  15.850  33.399  1.00 33.01  ? 351 GLU A C     1 
ATOM   2757 O  O     . GLU A 1 353 ? 13.882  14.668  33.721  1.00 32.65  ? 351 GLU A O     1 
ATOM   2758 C  CB    . GLU A 1 353 ? 13.056  17.675  34.913  1.00 33.33  ? 351 GLU A CB    1 
ATOM   2759 C  CG    . GLU A 1 353 ? 13.250  18.449  36.206  1.00 37.16  ? 351 GLU A CG    1 
ATOM   2760 C  CD    . GLU A 1 353 ? 12.082  19.370  36.513  1.00 35.61  ? 351 GLU A CD    1 
ATOM   2761 O  OE1   . GLU A 1 353 ? 11.195  19.495  35.635  1.00 32.83  ? 351 GLU A OE1   1 
ATOM   2762 O  OE2   . GLU A 1 353 ? 12.026  19.921  37.637  1.00 39.56  ? 351 GLU A OE2   1 
ATOM   2763 N  N     . TRP A 1 354 ? 13.710  16.261  32.137  1.00 30.41  ? 352 TRP A N     1 
ATOM   2764 C  CA    . TRP A 1 354 ? 13.419  15.298  31.074  1.00 30.93  ? 352 TRP A CA    1 
ATOM   2765 C  C     . TRP A 1 354 ? 14.578  14.334  30.834  1.00 33.75  ? 352 TRP A C     1 
ATOM   2766 O  O     . TRP A 1 354 ? 14.368  13.135  30.571  1.00 29.60  ? 352 TRP A O     1 
ATOM   2767 C  CB    . TRP A 1 354 ? 13.080  16.013  29.759  1.00 29.97  ? 352 TRP A CB    1 
ATOM   2768 C  CG    . TRP A 1 354 ? 11.646  16.445  29.612  1.00 29.78  ? 352 TRP A CG    1 
ATOM   2769 C  CD1   . TRP A 1 354 ? 11.189  17.716  29.388  1.00 27.72  ? 352 TRP A CD1   1 
ATOM   2770 C  CD2   . TRP A 1 354 ? 10.488  15.597  29.643  1.00 30.09  ? 352 TRP A CD2   1 
ATOM   2771 N  NE1   . TRP A 1 354 ? 9.822   17.703  29.282  1.00 28.71  ? 352 TRP A NE1   1 
ATOM   2772 C  CE2   . TRP A 1 354 ? 9.364   16.423  29.437  1.00 28.79  ? 352 TRP A CE2   1 
ATOM   2773 C  CE3   . TRP A 1 354 ? 10.285  14.231  29.852  1.00 31.68  ? 352 TRP A CE3   1 
ATOM   2774 C  CZ2   . TRP A 1 354 ? 8.065   15.925  29.433  1.00 30.96  ? 352 TRP A CZ2   1 
ATOM   2775 C  CZ3   . TRP A 1 354 ? 8.996   13.738  29.824  1.00 32.39  ? 352 TRP A CZ3   1 
ATOM   2776 C  CH2   . TRP A 1 354 ? 7.903   14.576  29.646  1.00 30.48  ? 352 TRP A CH2   1 
ATOM   2777 N  N     . LYS A 1 355 ? 15.812  14.851  30.956  1.00 36.35  ? 353 LYS A N     1 
ATOM   2778 C  CA    . LYS A 1 355 ? 16.984  14.012  30.769  1.00 38.67  ? 353 LYS A CA    1 
ATOM   2779 C  C     . LYS A 1 355 ? 17.007  12.910  31.827  1.00 41.71  ? 353 LYS A C     1 
ATOM   2780 O  O     . LYS A 1 355 ? 17.286  11.749  31.502  1.00 41.68  ? 353 LYS A O     1 
ATOM   2781 C  CB    . LYS A 1 355 ? 18.253  14.861  30.774  1.00 41.38  ? 353 LYS A CB    1 
ATOM   2782 C  CG    . LYS A 1 355 ? 19.557  14.073  30.835  1.00 43.95  ? 353 LYS A CG    1 
ATOM   2783 C  CD    . LYS A 1 355 ? 20.806  14.950  30.955  1.00 46.67  ? 353 LYS A CD    1 
ATOM   2784 C  CE    . LYS A 1 355 ? 22.029  14.324  30.302  1.00 51.03  ? 353 LYS A CE    1 
ATOM   2785 N  NZ    . LYS A 1 355 ? 23.304  15.040  30.578  1.00 54.77  ? 353 LYS A NZ    1 
ATOM   2786 N  N     . GLU A 1 356 ? 16.677  13.256  33.081  1.00 40.69  ? 354 GLU A N     1 
ATOM   2787 C  CA    . GLU A 1 356 ? 16.669  12.258  34.139  1.00 41.40  ? 354 GLU A CA    1 
ATOM   2788 C  C     . GLU A 1 356 ? 15.489  11.287  34.006  1.00 40.66  ? 354 GLU A C     1 
ATOM   2789 O  O     . GLU A 1 356 ? 15.674  10.085  34.192  1.00 40.60  ? 354 GLU A O     1 
ATOM   2790 C  CB    . GLU A 1 356 ? 16.651  12.921  35.511  1.00 45.73  ? 354 GLU A CB    1 
ATOM   2791 C  CG    . GLU A 1 356 ? 16.542  11.902  36.637  1.00 51.40  ? 354 GLU A CG    1 
ATOM   2792 C  CD    . GLU A 1 356 ? 16.846  12.459  38.013  1.00 56.10  ? 354 GLU A CD    1 
ATOM   2793 O  OE1   . GLU A 1 356 ? 17.009  13.682  38.123  1.00 59.17  ? 354 GLU A OE1   1 
ATOM   2794 O  OE2   . GLU A 1 356 ? 16.932  11.660  38.957  1.00 61.61  ? 354 GLU A OE2   1 
ATOM   2795 N  N     . LEU A 1 357 ? 14.280  11.786  33.708  1.00 36.49  ? 355 LEU A N     1 
ATOM   2796 C  CA    . LEU A 1 357 ? 13.142  10.907  33.453  1.00 38.57  ? 355 LEU A CA    1 
ATOM   2797 C  C     . LEU A 1 357 ? 13.460  9.893   32.350  1.00 36.84  ? 355 LEU A C     1 
ATOM   2798 O  O     . LEU A 1 357 ? 13.248  8.701   32.536  1.00 37.09  ? 355 LEU A O     1 
ATOM   2799 C  CB    . LEU A 1 357 ? 11.908  11.719  33.073  1.00 38.39  ? 355 LEU A CB    1 
ATOM   2800 C  CG    . LEU A 1 357 ? 11.113  12.342  34.214  1.00 41.95  ? 355 LEU A CG    1 
ATOM   2801 C  CD1   . LEU A 1 357 ? 10.074  13.318  33.660  1.00 43.10  ? 355 LEU A CD1   1 
ATOM   2802 C  CD2   . LEU A 1 357 ? 10.454  11.270  35.086  1.00 43.03  ? 355 LEU A CD2   1 
ATOM   2803 N  N     . ILE A 1 358 ? 13.986  10.341  31.204  1.00 33.69  ? 356 ILE A N     1 
ATOM   2804 C  CA    . ILE A 1 358 ? 14.272  9.413   30.115  1.00 34.22  ? 356 ILE A CA    1 
ATOM   2805 C  C     . ILE A 1 358 ? 15.417  8.460   30.476  1.00 37.51  ? 356 ILE A C     1 
ATOM   2806 O  O     . ILE A 1 358 ? 15.395  7.275   30.120  1.00 33.92  ? 356 ILE A O     1 
ATOM   2807 C  CB    . ILE A 1 358 ? 14.525  10.195  28.813  1.00 33.36  ? 356 ILE A CB    1 
ATOM   2808 C  CG1   . ILE A 1 358 ? 13.230  10.872  28.352  1.00 31.60  ? 356 ILE A CG1   1 
ATOM   2809 C  CG2   . ILE A 1 358 ? 15.096  9.285   27.727  1.00 33.68  ? 356 ILE A CG2   1 
ATOM   2810 C  CD1   . ILE A 1 358 ? 13.389  11.930  27.272  1.00 29.57  ? 356 ILE A CD1   1 
ATOM   2811 N  N     . TYR A 1 359 ? 16.441  8.963   31.176  1.00 38.46  ? 357 TYR A N     1 
ATOM   2812 C  CA    . TYR A 1 359 ? 17.541  8.113   31.624  1.00 41.99  ? 357 TYR A CA    1 
ATOM   2813 C  C     . TYR A 1 359 ? 17.029  6.980   32.513  1.00 41.86  ? 357 TYR A C     1 
ATOM   2814 O  O     . TYR A 1 359 ? 17.430  5.823   32.359  1.00 41.91  ? 357 TYR A O     1 
ATOM   2815 C  CB    . TYR A 1 359 ? 18.573  8.919   32.408  1.00 44.62  ? 357 TYR A CB    1 
ATOM   2816 C  CG    . TYR A 1 359 ? 19.800  8.113   32.803  1.00 46.41  ? 357 TYR A CG    1 
ATOM   2817 C  CD1   . TYR A 1 359 ? 20.670  7.616   31.838  1.00 49.69  ? 357 TYR A CD1   1 
ATOM   2818 C  CD2   . TYR A 1 359 ? 20.072  7.830   34.133  1.00 49.53  ? 357 TYR A CD2   1 
ATOM   2819 C  CE1   . TYR A 1 359 ? 21.799  6.888   32.192  1.00 53.66  ? 357 TYR A CE1   1 
ATOM   2820 C  CE2   . TYR A 1 359 ? 21.204  7.117   34.503  1.00 55.18  ? 357 TYR A CE2   1 
ATOM   2821 C  CZ    . TYR A 1 359 ? 22.065  6.641   33.528  1.00 56.17  ? 357 TYR A CZ    1 
ATOM   2822 O  OH    . TYR A 1 359 ? 23.178  5.930   33.861  1.00 63.65  ? 357 TYR A OH    1 
ATOM   2823 N  N     . LYS A 1 360 ? 16.159  7.319   33.469  1.00 44.25  ? 358 LYS A N     1 
ATOM   2824 C  CA    . LYS A 1 360 ? 15.633  6.319   34.383  1.00 47.22  ? 358 LYS A CA    1 
ATOM   2825 C  C     . LYS A 1 360 ? 14.777  5.329   33.615  1.00 48.23  ? 358 LYS A C     1 
ATOM   2826 O  O     . LYS A 1 360 ? 14.791  4.140   33.890  1.00 47.79  ? 358 LYS A O     1 
ATOM   2827 C  CB    . LYS A 1 360 ? 14.781  6.951   35.484  1.00 51.53  ? 358 LYS A CB    1 
ATOM   2828 C  CG    . LYS A 1 360 ? 15.556  7.613   36.614  1.00 54.98  ? 358 LYS A CG    1 
ATOM   2829 C  CD    . LYS A 1 360 ? 14.621  8.178   37.642  1.00 56.91  ? 358 LYS A CD    1 
ATOM   2830 C  CE    . LYS A 1 360 ? 15.317  8.687   38.876  1.00 62.12  ? 358 LYS A CE    1 
ATOM   2831 N  NZ    . LYS A 1 360 ? 14.309  9.140   39.862  1.00 68.83  ? 358 LYS A NZ    1 
ATOM   2832 N  N     . GLU A 1 361 ? 14.010  5.818   32.648  1.00 49.15  ? 359 GLU A N     1 
ATOM   2833 C  CA    . GLU A 1 361 ? 13.147  4.926   31.901  1.00 49.58  ? 359 GLU A CA    1 
ATOM   2834 C  C     . GLU A 1 361 ? 13.993  3.835   31.254  1.00 50.46  ? 359 GLU A C     1 
ATOM   2835 O  O     . GLU A 1 361 ? 13.597  2.670   31.202  1.00 58.23  ? 359 GLU A O     1 
ATOM   2836 C  CB    . GLU A 1 361 ? 12.332  5.714   30.880  1.00 46.70  ? 359 GLU A CB    1 
ATOM   2837 C  CG    . GLU A 1 361 ? 11.011  5.073   30.589  1.00 45.47  ? 359 GLU A CG    1 
ATOM   2838 C  CD    . GLU A 1 361 ? 10.259  4.607   31.819  1.00 45.61  ? 359 GLU A CD    1 
ATOM   2839 O  OE1   . GLU A 1 361 ? 10.218  5.356   32.798  1.00 47.41  ? 359 GLU A OE1   1 
ATOM   2840 O  OE2   . GLU A 1 361 ? 9.716   3.484   31.781  1.00 51.20  ? 359 GLU A OE2   1 
ATOM   2841 N  N     . VAL A 1 362 ? 15.183  4.210   30.798  1.00 45.03  ? 360 VAL A N     1 
ATOM   2842 C  CA    . VAL A 1 362 ? 16.060  3.266   30.146  1.00 47.94  ? 360 VAL A CA    1 
ATOM   2843 C  C     . VAL A 1 362 ? 16.574  2.274   31.196  1.00 58.60  ? 360 VAL A C     1 
ATOM   2844 O  O     . VAL A 1 362 ? 16.637  1.064   30.933  1.00 63.90  ? 360 VAL A O     1 
ATOM   2845 C  CB    . VAL A 1 362 ? 17.162  4.043   29.406  1.00 50.29  ? 360 VAL A CB    1 
ATOM   2846 C  CG1   . VAL A 1 362 ? 18.260  3.154   28.868  1.00 55.12  ? 360 VAL A CG1   1 
ATOM   2847 C  CG2   . VAL A 1 362 ? 16.556  4.876   28.280  1.00 54.38  ? 360 VAL A CG2   1 
ATOM   2848 N  N     . MET A 1 363 ? 16.830  2.778   32.418  1.00 61.86  ? 361 MET A N     1 
ATOM   2849 C  CA    . MET A 1 363 ? 17.436  2.003   33.500  1.00 68.09  ? 361 MET A CA    1 
ATOM   2850 C  C     . MET A 1 363 ? 16.400  1.280   34.383  1.00 70.58  ? 361 MET A C     1 
ATOM   2851 O  O     . MET A 1 363 ? 16.780  0.461   35.225  1.00 75.96  ? 361 MET A O     1 
ATOM   2852 C  CB    . MET A 1 363 ? 18.290  2.941   34.372  1.00 65.70  ? 361 MET A CB    1 
ATOM   2853 C  CG    . MET A 1 363 ? 19.467  3.571   33.636  1.00 60.69  ? 361 MET A CG    1 
ATOM   2854 S  SD    . MET A 1 363 ? 20.694  2.386   33.065  1.00 78.39  ? 361 MET A SD    1 
ATOM   2855 C  CE    . MET A 1 363 ? 20.159  2.071   31.385  1.00 82.94  ? 361 MET A CE    1 
ATOM   2856 N  N     . ASP A 1 364 ? 15.098  1.559   34.198  1.00 71.58  ? 362 ASP A N     1 
ATOM   2857 C  CA    . ASP A 1 364 ? 14.042  1.150   35.122  1.00 74.47  ? 362 ASP A CA    1 
ATOM   2858 C  C     . ASP A 1 364 ? 14.438  1.470   36.572  1.00 79.19  ? 362 ASP A C     1 
ATOM   2859 O  O     . ASP A 1 364 ? 14.400  0.587   37.435  1.00 77.54  ? 362 ASP A O     1 
ATOM   2860 C  CB    . ASP A 1 364 ? 13.664  -0.317  34.902  1.00 73.74  ? 362 ASP A CB    1 
ATOM   2861 N  N     . LEU A 1 365 ? 14.805  2.745   36.819  1.00 76.39  ? 363 LEU A N     1 
ATOM   2862 C  CA    . LEU A 1 365 ? 15.128  3.273   38.142  1.00 75.87  ? 363 LEU A CA    1 
ATOM   2863 C  C     . LEU A 1 365 ? 14.078  4.323   38.533  1.00 72.94  ? 363 LEU A C     1 
ATOM   2864 O  O     . LEU A 1 365 ? 13.143  3.956   39.271  1.00 75.23  ? 363 LEU A O     1 
ATOM   2865 C  CB    . LEU A 1 365 ? 16.523  3.917   38.135  1.00 70.09  ? 363 LEU A CB    1 
HETATM 2866 MG MG    . MG  B 2 .   ? 7.663   6.671   13.112  1.00 62.43  ? 401 MG  A MG    1 
HETATM 2867 P  PG    . ANP C 3 .   ? 8.842   8.744   11.052  1.00 91.91  ? 402 ANP A PG    1 
HETATM 2868 O  O1G   . ANP C 3 .   ? 7.796   7.706   11.375  1.00 83.07  ? 402 ANP A O1G   1 
HETATM 2869 O  O2G   . ANP C 3 .   ? 8.247   10.115  11.186  1.00 92.30  ? 402 ANP A O2G   1 
HETATM 2870 O  O3G   . ANP C 3 .   ? 9.241   8.483   9.618   1.00 82.32  ? 402 ANP A O3G   1 
HETATM 2871 P  PB    . ANP C 3 .   ? 11.326  7.629   11.922  1.00 102.80 ? 402 ANP A PB    1 
HETATM 2872 O  O1B   . ANP C 3 .   ? 11.584  7.366   10.465  1.00 110.58 ? 402 ANP A O1B   1 
HETATM 2873 O  O2B   . ANP C 3 .   ? 12.502  7.939   12.810  1.00 107.77 ? 402 ANP A O2B   1 
HETATM 2874 N  N3B   . ANP C 3 .   ? 10.089  8.674   12.110  1.00 93.39  ? 402 ANP A N3B   1 
HETATM 2875 P  PA    . ANP C 3 .   ? 10.079  4.940   11.797  1.00 79.10  ? 402 ANP A PA    1 
HETATM 2876 O  O1A   . ANP C 3 .   ? 10.270  3.817   12.767  1.00 87.59  ? 402 ANP A O1A   1 
HETATM 2877 O  O2A   . ANP C 3 .   ? 8.673   5.312   11.438  1.00 78.66  ? 402 ANP A O2A   1 
HETATM 2878 O  O3A   . ANP C 3 .   ? 10.765  6.237   12.463  1.00 90.31  ? 402 ANP A O3A   1 
HETATM 2879 O  "O5'" . ANP C 3 .   ? 10.926  4.638   10.450  1.00 70.74  ? 402 ANP A "O5'" 1 
HETATM 2880 C  "C5'" . ANP C 3 .   ? 10.293  4.616   9.126   1.00 63.53  ? 402 ANP A "C5'" 1 
HETATM 2881 C  "C4'" . ANP C 3 .   ? 10.437  3.264   8.467   1.00 59.75  ? 402 ANP A "C4'" 1 
HETATM 2882 O  "O4'" . ANP C 3 .   ? 11.363  2.419   9.203   1.00 56.87  ? 402 ANP A "O4'" 1 
HETATM 2883 C  "C3'" . ANP C 3 .   ? 9.154   2.430   8.385   1.00 57.63  ? 402 ANP A "C3'" 1 
HETATM 2884 O  "O3'" . ANP C 3 .   ? 8.352   2.753   7.252   1.00 52.68  ? 402 ANP A "O3'" 1 
HETATM 2885 C  "C2'" . ANP C 3 .   ? 9.704   1.009   8.244   1.00 54.49  ? 402 ANP A "C2'" 1 
HETATM 2886 O  "O2'" . ANP C 3 .   ? 9.913   0.683   6.890   1.00 55.19  ? 402 ANP A "O2'" 1 
HETATM 2887 C  "C1'" . ANP C 3 .   ? 11.013  1.058   9.034   1.00 53.31  ? 402 ANP A "C1'" 1 
HETATM 2888 N  N9    . ANP C 3 .   ? 10.894  0.404   10.362  1.00 50.77  ? 402 ANP A N9    1 
HETATM 2889 C  C8    . ANP C 3 .   ? 10.898  1.008   11.590  1.00 45.13  ? 402 ANP A C8    1 
HETATM 2890 N  N7    . ANP C 3 .   ? 10.753  0.161   12.584  1.00 41.59  ? 402 ANP A N7    1 
HETATM 2891 C  C5    . ANP C 3 .   ? 10.646  -1.079  11.976  1.00 43.38  ? 402 ANP A C5    1 
HETATM 2892 C  C6    . ANP C 3 .   ? 10.484  -2.380  12.495  1.00 40.33  ? 402 ANP A C6    1 
HETATM 2893 N  N6    . ANP C 3 .   ? 10.407  -2.637  13.793  1.00 36.87  ? 402 ANP A N6    1 
HETATM 2894 N  N1    . ANP C 3 .   ? 10.409  -3.410  11.612  1.00 41.01  ? 402 ANP A N1    1 
HETATM 2895 C  C2    . ANP C 3 .   ? 10.507  -3.122  10.301  1.00 44.90  ? 402 ANP A C2    1 
HETATM 2896 N  N3    . ANP C 3 .   ? 10.658  -1.938  9.700   1.00 42.94  ? 402 ANP A N3    1 
HETATM 2897 C  C4    . ANP C 3 .   ? 10.726  -0.943  10.602  1.00 47.08  ? 402 ANP A C4    1 
HETATM 2898 C  C1    . Y6K D 4 .   ? -4.145  -11.833 5.612   1.00 27.36  ? 403 Y6K A C1    1 
HETATM 2899 C  C2    . Y6K D 4 .   ? -2.689  -12.059 5.231   1.00 27.27  ? 403 Y6K A C2    1 
HETATM 2900 C  C3    . Y6K D 4 .   ? -2.176  -13.482 5.273   1.00 26.61  ? 403 Y6K A C3    1 
HETATM 2901 C  C8    . Y6K D 4 .   ? -5.399  -13.812 4.924   1.00 30.46  ? 403 Y6K A C8    1 
HETATM 2902 C  C14   . Y6K D 4 .   ? -2.391  -15.867 5.743   1.00 32.53  ? 403 Y6K A C14   1 
HETATM 2903 C  C15   . Y6K D 4 .   ? -1.742  -17.477 7.295   1.00 47.48  ? 403 Y6K A C15   1 
HETATM 2904 C  C16   . Y6K D 4 .   ? -2.136  -10.960 4.366   1.00 29.29  ? 403 Y6K A C16   1 
HETATM 2905 C  C17   . Y6K D 4 .   ? -0.018  -10.396 3.140   1.00 34.34  ? 403 Y6K A C17   1 
HETATM 2906 C  C19   . Y6K D 4 .   ? 0.445   -9.363  4.132   1.00 33.52  ? 403 Y6K A C19   1 
HETATM 2907 C  C20   . Y6K D 4 .   ? 1.175   -11.210 2.687   1.00 34.82  ? 403 Y6K A C20   1 
HETATM 2908 C  C18   . Y6K D 4 .   ? -0.757  -9.752  1.972   1.00 35.00  ? 403 Y6K A C18   1 
HETATM 2909 C  C7    . Y6K D 4 .   ? -4.269  -14.684 4.418   1.00 33.58  ? 403 Y6K A C7    1 
HETATM 2910 C  C5    . Y6K D 4 .   ? -3.920  -14.047 6.740   1.00 29.10  ? 403 Y6K A C5    1 
HETATM 2911 C  C6    . Y6K D 4 .   ? -4.906  -13.043 6.130   1.00 29.05  ? 403 Y6K A C6    1 
HETATM 2912 C  C9    . Y6K D 4 .   ? -6.618  -13.727 4.432   1.00 30.52  ? 403 Y6K A C9    1 
HETATM 2913 C  C4    . Y6K D 4 .   ? -3.164  -14.585 5.492   1.00 30.01  ? 403 Y6K A C4    1 
HETATM 2914 O  O4    . Y6K D 4 .   ? -4.642  -10.715 5.591   1.00 29.44  ? 403 Y6K A O4    1 
HETATM 2915 O  O3    . Y6K D 4 .   ? -0.964  -11.323 3.827   1.00 33.71  ? 403 Y6K A O3    1 
HETATM 2916 O  O2    . Y6K D 4 .   ? -2.616  -9.863  4.398   1.00 31.60  ? 403 Y6K A O2    1 
HETATM 2917 O  O     . Y6K D 4 .   ? -2.498  -16.279 6.991   1.00 37.86  ? 403 Y6K A O     1 
HETATM 2918 O  O1    . Y6K D 4 .   ? -1.675  -16.395 4.947   1.00 33.14  ? 403 Y6K A O1    1 
HETATM 2919 C  C1    . GOL E 5 .   ? 4.754   16.625  37.060  1.00 62.92  ? 404 GOL A C1    1 
HETATM 2920 O  O1    . GOL E 5 .   ? 5.345   16.397  38.337  1.00 69.74  ? 404 GOL A O1    1 
HETATM 2921 C  C2    . GOL E 5 .   ? 5.260   17.921  36.458  1.00 65.13  ? 404 GOL A C2    1 
HETATM 2922 O  O2    . GOL E 5 .   ? 4.597   18.193  35.228  1.00 56.61  ? 404 GOL A O2    1 
HETATM 2923 C  C3    . GOL E 5 .   ? 5.097   19.091  37.407  1.00 68.12  ? 404 GOL A C3    1 
HETATM 2924 O  O3    . GOL E 5 .   ? 6.356   19.644  37.780  1.00 72.39  ? 404 GOL A O3    1 
HETATM 2925 O  O     . HOH F 6 .   ? 24.275  4.407   31.325  1.00 47.44  ? 501 HOH A O     1 
HETATM 2926 O  O     . HOH F 6 .   ? 16.509  11.563  17.538  1.00 53.04  ? 502 HOH A O     1 
HETATM 2927 O  O     . HOH F 6 .   ? 24.552  8.415   36.062  1.00 53.32  ? 503 HOH A O     1 
HETATM 2928 O  O     . HOH F 6 .   ? -0.702  17.108  2.324   1.00 40.96  ? 504 HOH A O     1 
HETATM 2929 O  O     . HOH F 6 .   ? -16.015 -14.197 17.304  1.00 33.54  ? 505 HOH A O     1 
HETATM 2930 O  O     . HOH F 6 .   ? 4.102   -17.088 12.838  1.00 42.38  ? 506 HOH A O     1 
HETATM 2931 O  O     . HOH F 6 .   ? -3.611  9.730   -5.418  1.00 45.84  ? 507 HOH A O     1 
HETATM 2932 O  O     . HOH F 6 .   ? 17.531  -7.644  21.704  1.00 26.94  ? 508 HOH A O     1 
HETATM 2933 O  O     . HOH F 6 .   ? -22.735 -0.446  -0.202  1.00 38.01  ? 509 HOH A O     1 
HETATM 2934 O  O     . HOH F 6 .   ? -13.322 23.983  16.441  1.00 40.22  ? 510 HOH A O     1 
HETATM 2935 O  O     . HOH F 6 .   ? -0.167  -2.915  30.995  1.00 46.35  ? 511 HOH A O     1 
HETATM 2936 O  O     . HOH F 6 .   ? -17.897 17.683  14.845  1.00 48.52  ? 512 HOH A O     1 
HETATM 2937 O  O     . HOH F 6 .   ? 8.401   20.587  36.550  1.00 46.74  ? 513 HOH A O     1 
HETATM 2938 O  O     . HOH F 6 .   ? -3.524  -6.405  27.847  1.00 43.64  ? 514 HOH A O     1 
HETATM 2939 O  O     . HOH F 6 .   ? 0.658   21.144  30.289  1.00 46.81  ? 515 HOH A O     1 
HETATM 2940 O  O     . HOH F 6 .   ? 6.838   -4.341  24.574  1.00 34.19  ? 516 HOH A O     1 
HETATM 2941 O  O     . HOH F 6 .   ? -5.464  -11.086 14.873  1.00 31.46  ? 517 HOH A O     1 
HETATM 2942 O  O     . HOH F 6 .   ? -19.525 11.942  1.048   1.00 33.05  ? 518 HOH A O     1 
HETATM 2943 O  O     . HOH F 6 .   ? 7.953   19.644  7.977   1.00 39.93  ? 519 HOH A O     1 
HETATM 2944 O  O     . HOH F 6 .   ? 5.285   12.391  27.090  1.00 41.68  ? 520 HOH A O     1 
HETATM 2945 O  O     . HOH F 6 .   ? 33.390  -0.472  24.488  1.00 48.42  ? 521 HOH A O     1 
HETATM 2946 O  O     . HOH F 6 .   ? -1.278  9.829   21.179  1.00 31.63  ? 522 HOH A O     1 
HETATM 2947 O  O     . HOH F 6 .   ? -10.843 -15.936 22.315  1.00 37.61  ? 523 HOH A O     1 
HETATM 2948 O  O     . HOH F 6 .   ? -21.290 -1.947  12.782  1.00 38.63  ? 524 HOH A O     1 
HETATM 2949 O  O     . HOH F 6 .   ? 2.489   7.598   11.970  1.00 40.11  ? 525 HOH A O     1 
HETATM 2950 O  O     . HOH F 6 .   ? -20.696 10.873  -1.023  1.00 32.96  ? 526 HOH A O     1 
HETATM 2951 O  O     . HOH F 6 .   ? 4.210   -2.479  22.714  1.00 29.86  ? 527 HOH A O     1 
HETATM 2952 O  O     . HOH F 6 .   ? -7.617  -14.918 16.969  1.00 37.39  ? 528 HOH A O     1 
HETATM 2953 O  O     . HOH F 6 .   ? -2.084  10.425  9.758   1.00 24.07  ? 529 HOH A O     1 
HETATM 2954 O  O     . HOH F 6 .   ? 11.848  12.428  20.394  1.00 37.97  ? 530 HOH A O     1 
HETATM 2955 O  O     . HOH F 6 .   ? 15.812  21.539  36.347  1.00 43.87  ? 531 HOH A O     1 
HETATM 2956 O  O     . HOH F 6 .   ? 3.055   9.444   15.599  1.00 34.60  ? 532 HOH A O     1 
HETATM 2957 O  O     . HOH F 6 .   ? -20.789 9.223   4.101   1.00 28.27  ? 533 HOH A O     1 
HETATM 2958 O  O     . HOH F 6 .   ? 14.646  20.757  5.780   1.00 39.16  ? 534 HOH A O     1 
HETATM 2959 O  O     . HOH F 6 .   ? -14.564 -12.137 4.003   1.00 49.65  ? 535 HOH A O     1 
HETATM 2960 O  O     . HOH F 6 .   ? -14.623 16.475  12.067  1.00 30.01  ? 536 HOH A O     1 
HETATM 2961 O  O     . HOH F 6 .   ? -14.913 24.084  2.070   1.00 28.93  ? 537 HOH A O     1 
HETATM 2962 O  O     . HOH F 6 .   ? -19.234 2.719   19.864  1.00 44.62  ? 538 HOH A O     1 
HETATM 2963 O  O     . HOH F 6 .   ? 6.305   8.142   14.022  1.00 40.75  ? 539 HOH A O     1 
HETATM 2964 O  O     . HOH F 6 .   ? -7.072  12.959  4.981   1.00 23.99  ? 540 HOH A O     1 
HETATM 2965 O  O     . HOH F 6 .   ? -14.580 17.791  15.984  1.00 51.55  ? 541 HOH A O     1 
HETATM 2966 O  O     . HOH F 6 .   ? -23.408 6.416   -8.323  1.00 40.78  ? 542 HOH A O     1 
HETATM 2967 O  O     . HOH F 6 .   ? -1.991  18.578  10.550  1.00 42.74  ? 543 HOH A O     1 
HETATM 2968 O  O     . HOH F 6 .   ? 1.689   6.586   2.216   1.00 33.85  ? 544 HOH A O     1 
HETATM 2969 O  O     . HOH F 6 .   ? -18.910 11.205  3.631   1.00 25.58  ? 545 HOH A O     1 
HETATM 2970 O  O     . HOH F 6 .   ? 23.122  16.180  33.451  1.00 49.63  ? 546 HOH A O     1 
HETATM 2971 O  O     . HOH F 6 .   ? -8.456  -4.296  20.754  1.00 31.90  ? 547 HOH A O     1 
HETATM 2972 O  O     . HOH F 6 .   ? 5.990   1.360   30.960  1.00 35.34  ? 548 HOH A O     1 
HETATM 2973 O  O     . HOH F 6 .   ? -3.046  12.450  19.987  1.00 34.98  ? 549 HOH A O     1 
HETATM 2974 O  O     . HOH F 6 .   ? -12.897 13.010  16.363  1.00 23.72  ? 550 HOH A O     1 
HETATM 2975 O  O     . HOH F 6 .   ? -4.831  8.801   13.062  1.00 22.31  ? 551 HOH A O     1 
HETATM 2976 O  O     . HOH F 6 .   ? 3.080   -4.913  21.971  1.00 23.27  ? 552 HOH A O     1 
HETATM 2977 O  O     . HOH F 6 .   ? -16.855 23.895  0.027   1.00 30.72  ? 553 HOH A O     1 
HETATM 2978 O  O     . HOH F 6 .   ? 5.981   16.151  21.595  1.00 30.02  ? 554 HOH A O     1 
HETATM 2979 O  O     . HOH F 6 .   ? -11.071 26.042  13.378  1.00 40.79  ? 555 HOH A O     1 
HETATM 2980 O  O     . HOH F 6 .   ? 2.431   22.285  26.606  1.00 45.40  ? 556 HOH A O     1 
HETATM 2981 O  O     . HOH F 6 .   ? -22.624 6.776   -1.790  1.00 41.62  ? 557 HOH A O     1 
HETATM 2982 O  O     . HOH F 6 .   ? -8.930  -13.211 14.129  1.00 29.51  ? 558 HOH A O     1 
HETATM 2983 O  O     . HOH F 6 .   ? -12.673 4.110   20.396  1.00 26.09  ? 559 HOH A O     1 
HETATM 2984 O  O     . HOH F 6 .   ? -17.892 26.126  1.120   1.00 34.75  ? 560 HOH A O     1 
HETATM 2985 O  O     . HOH F 6 .   ? -12.334 -15.384 12.306  1.00 26.17  ? 561 HOH A O     1 
HETATM 2986 O  O     . HOH F 6 .   ? -0.744  7.771   -4.598  1.00 37.04  ? 562 HOH A O     1 
HETATM 2987 O  O     . HOH F 6 .   ? -12.421 -15.181 15.173  1.00 25.20  ? 563 HOH A O     1 
HETATM 2988 O  O     . HOH F 6 .   ? -1.045  11.621  7.383   1.00 21.03  ? 564 HOH A O     1 
HETATM 2989 O  O     . HOH F 6 .   ? -6.084  -8.568  15.602  1.00 25.85  ? 565 HOH A O     1 
HETATM 2990 O  O     . HOH F 6 .   ? 3.642   -7.253  19.430  1.00 32.44  ? 566 HOH A O     1 
HETATM 2991 O  O     . HOH F 6 .   ? -11.557 -7.816  28.821  1.00 46.26  ? 567 HOH A O     1 
HETATM 2992 O  O     . HOH F 6 .   ? -11.928 29.704  -0.045  1.00 45.79  ? 568 HOH A O     1 
HETATM 2993 O  O     . HOH F 6 .   ? -18.538 13.750  4.844   1.00 26.33  ? 569 HOH A O     1 
HETATM 2994 O  O     . HOH F 6 .   ? -1.102  -4.398  26.792  1.00 29.37  ? 570 HOH A O     1 
HETATM 2995 O  O     . HOH F 6 .   ? 5.181   11.920  8.461   1.00 38.64  ? 571 HOH A O     1 
HETATM 2996 O  O     . HOH F 6 .   ? 14.033  -9.598  24.448  1.00 33.91  ? 572 HOH A O     1 
HETATM 2997 O  O     . HOH F 6 .   ? -5.173  7.261   1.236   1.00 26.43  ? 573 HOH A O     1 
HETATM 2998 O  O     . HOH F 6 .   ? -21.927 18.869  13.711  1.00 46.41  ? 574 HOH A O     1 
HETATM 2999 O  O     . HOH F 6 .   ? 17.195  22.116  32.581  1.00 33.69  ? 575 HOH A O     1 
HETATM 3000 O  O     . HOH F 6 .   ? 5.959   20.626  24.400  1.00 33.21  ? 576 HOH A O     1 
HETATM 3001 O  O     . HOH F 6 .   ? 10.675  23.637  10.554  1.00 54.05  ? 577 HOH A O     1 
HETATM 3002 O  O     . HOH F 6 .   ? 6.371   -6.929  18.193  1.00 39.21  ? 578 HOH A O     1 
HETATM 3003 O  O     . HOH F 6 .   ? -13.992 21.940  17.592  1.00 37.39  ? 579 HOH A O     1 
HETATM 3004 O  O     . HOH F 6 .   ? 22.629  -7.452  26.372  1.00 38.93  ? 580 HOH A O     1 
HETATM 3005 O  O     . HOH F 6 .   ? 4.718   -6.931  22.847  1.00 38.84  ? 581 HOH A O     1 
HETATM 3006 O  O     . HOH F 6 .   ? -5.487  10.047  1.770   1.00 24.65  ? 582 HOH A O     1 
HETATM 3007 O  O     . HOH F 6 .   ? 13.181  14.317  36.525  1.00 42.44  ? 583 HOH A O     1 
HETATM 3008 O  O     . HOH F 6 .   ? -15.022 -9.642  4.680   1.00 42.16  ? 584 HOH A O     1 
HETATM 3009 O  O     . HOH F 6 .   ? 2.406   6.546   5.068   1.00 27.26  ? 585 HOH A O     1 
HETATM 3010 O  O     . HOH F 6 .   ? -6.179  11.828  12.242  1.00 24.81  ? 586 HOH A O     1 
HETATM 3011 O  O     . HOH F 6 .   ? -14.054 5.263   18.300  1.00 26.40  ? 587 HOH A O     1 
HETATM 3012 O  O     . HOH F 6 .   ? 22.873  17.815  29.763  1.00 57.05  ? 588 HOH A O     1 
HETATM 3013 O  O     . HOH F 6 .   ? -3.816  10.467  23.635  1.00 37.64  ? 589 HOH A O     1 
HETATM 3014 O  O     . HOH F 6 .   ? -19.729 14.899  7.172   1.00 28.96  ? 590 HOH A O     1 
HETATM 3015 O  O     . HOH F 6 .   ? 3.299   -11.320 16.718  1.00 40.48  ? 591 HOH A O     1 
HETATM 3016 O  O     . HOH F 6 .   ? 26.244  -7.801  23.729  1.00 38.02  ? 592 HOH A O     1 
HETATM 3017 O  O     . HOH F 6 .   ? 16.532  -8.692  23.946  1.00 34.27  ? 593 HOH A O     1 
HETATM 3018 O  O     . HOH F 6 .   ? 6.343   18.805  5.715   1.00 41.67  ? 594 HOH A O     1 
HETATM 3019 O  O     . HOH F 6 .   ? -19.218 15.877  3.275   1.00 30.22  ? 595 HOH A O     1 
HETATM 3020 O  O     . HOH F 6 .   ? 1.021   4.747   12.064  1.00 34.79  ? 596 HOH A O     1 
HETATM 3021 O  O     . HOH F 6 .   ? -2.885  -9.619  21.668  1.00 33.44  ? 597 HOH A O     1 
HETATM 3022 O  O     . HOH F 6 .   ? -2.272  20.134  8.553   1.00 42.86  ? 598 HOH A O     1 
HETATM 3023 O  O     . HOH F 6 .   ? 7.837   5.535   14.645  1.00 52.77  ? 599 HOH A O     1 
HETATM 3024 O  O     . HOH F 6 .   ? 14.685  12.822  19.633  1.00 47.92  ? 600 HOH A O     1 
HETATM 3025 O  O     . HOH F 6 .   ? -15.412 2.725   19.966  1.00 28.39  ? 601 HOH A O     1 
HETATM 3026 O  O     . HOH F 6 .   ? -1.677  -13.040 11.887  1.00 38.02  ? 602 HOH A O     1 
HETATM 3027 O  O     . HOH F 6 .   ? -21.618 10.408  -7.916  1.00 38.65  ? 603 HOH A O     1 
HETATM 3028 O  O     . HOH F 6 .   ? -21.314 17.099  6.969   1.00 37.52  ? 604 HOH A O     1 
HETATM 3029 O  O     . HOH F 6 .   ? -10.494 17.788  21.899  1.00 40.97  ? 605 HOH A O     1 
HETATM 3030 O  O     . HOH F 6 .   ? 16.243  22.799  21.322  1.00 37.69  ? 606 HOH A O     1 
HETATM 3031 O  O     . HOH F 6 .   ? -23.031 -9.312  10.593  1.00 44.97  ? 607 HOH A O     1 
HETATM 3032 O  O     . HOH F 6 .   ? -16.682 -4.206  19.085  1.00 39.01  ? 608 HOH A O     1 
HETATM 3033 O  O     . HOH F 6 .   ? -22.570 3.130   -0.126  1.00 48.03  ? 609 HOH A O     1 
HETATM 3034 O  O     . HOH F 6 .   ? -21.624 15.861  1.475   1.00 49.26  ? 610 HOH A O     1 
HETATM 3035 O  O     . HOH F 6 .   ? -6.683  18.339  16.515  1.00 43.48  ? 611 HOH A O     1 
HETATM 3036 O  O     . HOH F 6 .   ? -22.272 0.001   10.738  1.00 39.61  ? 612 HOH A O     1 
HETATM 3037 O  O     . HOH F 6 .   ? -14.748 -4.389  24.437  1.00 45.29  ? 613 HOH A O     1 
HETATM 3038 O  O     . HOH F 6 .   ? 1.716   18.832  26.769  1.00 46.81  ? 614 HOH A O     1 
HETATM 3039 O  O     . HOH F 6 .   ? -15.639 7.642   18.878  1.00 33.73  ? 615 HOH A O     1 
HETATM 3040 O  O     . HOH F 6 .   ? -3.844  1.900   34.622  1.00 51.20  ? 616 HOH A O     1 
HETATM 3041 O  O     . HOH F 6 .   ? -22.542 7.340   7.383   1.00 40.34  ? 617 HOH A O     1 
HETATM 3042 O  O     . HOH F 6 .   ? -18.176 7.490   17.572  1.00 47.36  ? 618 HOH A O     1 
HETATM 3043 O  O     . HOH F 6 .   ? -14.915 15.046  17.416  1.00 34.64  ? 619 HOH A O     1 
HETATM 3044 O  O     . HOH F 6 .   ? -22.806 8.436   2.107   1.00 40.97  ? 620 HOH A O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . LYS A 7   ? 0.2861 0.7819 1.0274 0.0187  -0.1490 -0.4111 5   LYS A N     
2    C  CA    . LYS A 7   ? 0.3709 0.8216 1.0300 0.0525  0.0136  -0.3510 5   LYS A CA    
3    C  C     . LYS A 7   ? 0.3737 0.8848 1.0798 0.0368  -0.0756 -0.2923 5   LYS A C     
4    O  O     . LYS A 7   ? 0.4003 0.9803 1.0616 0.0523  -0.1819 -0.1745 5   LYS A O     
5    C  CB    . LYS A 7   ? 0.3977 0.6985 1.0657 0.2102  0.1494  -0.3338 5   LYS A CB    
6    N  N     . ARG A 8   ? 0.4993 0.7553 1.0637 0.0056  0.0086  -0.2662 6   ARG A N     
7    C  CA    . ARG A 8   ? 0.5539 0.8469 1.0725 -0.0246 -0.0416 -0.2506 6   ARG A CA    
8    C  C     . ARG A 8   ? 0.6178 0.8696 1.1223 0.0313  -0.0361 -0.1980 6   ARG A C     
9    O  O     . ARG A 8   ? 0.7804 0.8630 1.1569 0.0627  -0.0367 -0.1110 6   ARG A O     
10   C  CB    . ARG A 8   ? 0.5799 0.9254 1.1263 -0.0766 -0.0109 -0.2763 6   ARG A CB    
11   C  CG    . ARG A 8   ? 0.6351 0.9362 1.1099 -0.1747 -0.0138 -0.3350 6   ARG A CG    
12   N  N     . ASP A 9   ? 0.6237 0.7609 1.1085 0.0581  -0.0257 -0.2264 7   ASP A N     
13   C  CA    . ASP A 9   ? 0.6237 0.6957 1.0265 0.0507  -0.0480 -0.1839 7   ASP A CA    
14   C  C     . ASP A 9   ? 0.6400 0.7788 1.0345 0.0402  -0.0446 -0.1458 7   ASP A C     
15   O  O     . ASP A 9   ? 0.5672 0.8267 0.9532 -0.0449 -0.1285 -0.0966 7   ASP A O     
16   C  CB    . ASP A 9   ? 0.6701 0.6563 1.0416 0.1263  -0.0549 -0.1124 7   ASP A CB    
17   C  CG    . ASP A 9   ? 0.6878 0.6528 1.0058 0.1467  -0.0637 -0.0525 7   ASP A CG    
18   O  OD1   . ASP A 9   ? 0.7104 0.7362 0.9841 0.2248  -0.0226 0.0993  7   ASP A OD1   
19   O  OD2   . ASP A 9   ? 0.7033 0.4587 0.9924 0.1918  -0.0867 -0.1412 7   ASP A OD2   
20   N  N     . ASN A 10  ? 0.5556 0.7932 0.9858 0.0839  -0.0506 -0.2360 8   ASN A N     
21   C  CA    . ASN A 10  ? 0.4752 0.9047 0.9656 0.1241  -0.0766 -0.2506 8   ASN A CA    
22   C  C     . ASN A 10  ? 0.4842 0.9125 0.9458 0.1422  -0.1222 -0.2740 8   ASN A C     
23   O  O     . ASN A 10  ? 0.3579 0.9125 0.9287 0.1631  -0.1890 -0.2499 8   ASN A O     
24   C  CB    . ASN A 10  ? 0.5402 0.8511 0.8451 0.1241  -0.1033 -0.2478 8   ASN A CB    
25   N  N     . ASN A 11  ? 0.4312 0.8566 0.9567 0.1678  -0.1432 -0.2385 9   ASN A N     
26   C  CA    . ASN A 11  ? 0.4898 0.7909 0.9797 0.1385  -0.1185 -0.2227 9   ASN A CA    
27   C  C     . ASN A 11  ? 0.3681 0.6508 0.9775 0.1043  -0.0856 -0.1905 9   ASN A C     
28   O  O     . ASN A 11  ? 0.4050 0.6239 0.8603 0.1055  -0.1156 -0.1496 9   ASN A O     
29   C  CB    . ASN A 11  ? 0.6226 0.8759 0.9501 0.1987  -0.1132 -0.2210 9   ASN A CB    
30   C  CG    . ASN A 11  ? 0.7675 0.9931 0.9201 0.2019  -0.1638 -0.2344 9   ASN A CG    
31   O  OD1   . ASN A 11  ? 0.7562 1.1308 1.0109 0.1692  -0.1746 -0.3383 9   ASN A OD1   
32   N  ND2   . ASN A 11  ? 0.7921 1.0275 0.9095 0.2387  -0.1469 -0.2470 9   ASN A ND2   
33   N  N     . PHE A 12  ? 0.2461 0.5913 1.0109 0.0970  -0.0829 -0.2014 10  PHE A N     
34   C  CA    . PHE A 12  ? 0.3223 0.5905 0.9917 0.0651  -0.0542 -0.1837 10  PHE A CA    
35   C  C     . PHE A 12  ? 0.2500 0.6162 1.0311 0.0879  -0.0435 -0.1745 10  PHE A C     
36   O  O     . PHE A 12  ? 0.2224 0.6705 1.0849 -0.0199 -0.0304 -0.1734 10  PHE A O     
37   C  CB    . PHE A 12  ? 0.3586 0.5801 1.0356 0.0595  -0.0257 -0.1559 10  PHE A CB    
38   C  CG    . PHE A 12  ? 0.3658 0.5315 0.9864 0.0631  -0.0372 -0.1423 10  PHE A CG    
39   C  CD1   . PHE A 12  ? 0.3583 0.5912 0.9642 0.0284  -0.0544 -0.1767 10  PHE A CD1   
40   C  CD2   . PHE A 12  ? 0.3198 0.3534 0.9353 0.0661  -0.0410 -0.1398 10  PHE A CD2   
41   C  CE1   . PHE A 12  ? 0.3479 0.5118 0.9576 0.0549  -0.0501 -0.2017 10  PHE A CE1   
42   C  CE2   . PHE A 12  ? 0.3310 0.3582 0.9314 0.0634  -0.0416 -0.1266 10  PHE A CE2   
43   C  CZ    . PHE A 12  ? 0.3375 0.4110 0.9264 0.0672  -0.0540 -0.1310 10  PHE A CZ    
44   N  N     . TYR A 13  ? 0.2805 0.6131 1.0116 0.0367  0.0191  -0.1460 11  TYR A N     
45   C  CA    . TYR A 13  ? 0.3162 0.5916 1.0071 0.0301  0.0811  -0.1332 11  TYR A CA    
46   C  C     . TYR A 13  ? 0.3550 0.5809 1.0529 0.0280  0.1618  -0.1274 11  TYR A C     
47   O  O     . TYR A 13  ? 0.3751 0.5243 1.1894 0.0562  0.1252  -0.0927 11  TYR A O     
48   C  CB    . TYR A 13  ? 0.3819 0.6196 1.0059 0.0506  0.0544  -0.1100 11  TYR A CB    
49   C  CG    . TYR A 13  ? 0.3678 0.6350 0.9484 0.0072  0.0433  -0.0768 11  TYR A CG    
50   C  CD1   . TYR A 13  ? 0.4037 0.5885 0.9265 0.0237  0.0573  -0.0732 11  TYR A CD1   
51   C  CD2   . TYR A 13  ? 0.3847 0.6846 0.9284 0.0179  0.0409  -0.0783 11  TYR A CD2   
52   C  CE1   . TYR A 13  ? 0.4173 0.5957 0.8934 0.0217  0.0354  -0.0552 11  TYR A CE1   
53   C  CE2   . TYR A 13  ? 0.3524 0.6371 0.9117 0.0554  0.0261  -0.0277 11  TYR A CE2   
54   C  CZ    . TYR A 13  ? 0.4252 0.5647 0.8722 0.0304  0.0457  -0.0078 11  TYR A CZ    
55   O  OH    . TYR A 13  ? 0.5373 0.4945 0.9127 0.0676  0.1002  -0.0427 11  TYR A OH    
56   N  N     . SER A 14  ? 0.2908 0.6146 1.1164 0.0273  0.1777  -0.1045 12  SER A N     
57   C  CA    . SER A 14  ? 0.3920 0.6465 1.0846 -0.0147 0.2109  -0.0457 12  SER A CA    
58   C  C     . SER A 14  ? 0.4207 0.7207 1.1057 0.0267  0.2396  0.0120  12  SER A C     
59   O  O     . SER A 14  ? 0.4475 0.7460 1.1657 0.0683  0.2634  0.0656  12  SER A O     
60   C  CB    . SER A 14  ? 0.4509 0.6973 1.0921 -0.0581 0.2183  -0.0294 12  SER A CB    
61   O  OG    . SER A 14  ? 0.6328 0.6902 1.0707 -0.0906 0.2176  -0.0468 12  SER A OG    
62   N  N     . VAL A 15  ? 0.4862 0.7816 1.1873 0.0554  0.2685  0.0382  13  VAL A N     
63   C  CA    . VAL A 15  ? 0.5871 0.8382 1.2253 0.0415  0.2859  0.0388  13  VAL A CA    
64   C  C     . VAL A 15  ? 0.6474 0.8829 1.2844 0.0369  0.2978  0.0555  13  VAL A C     
65   O  O     . VAL A 15  ? 0.6805 0.8160 1.4424 -0.0397 0.3091  0.0372  13  VAL A O     
66   C  CB    . VAL A 15  ? 0.5591 0.8404 1.2213 0.0601  0.2531  0.0631  13  VAL A CB    
67   C  CG1   . VAL A 15  ? 0.5431 0.8054 1.2252 0.0708  0.2530  0.0665  13  VAL A CG1   
68   C  CG2   . VAL A 15  ? 0.5607 0.8240 1.1400 0.0799  0.2229  0.0820  13  VAL A CG2   
69   N  N     . GLU A 16  ? 0.6654 0.9711 1.2622 0.0959  0.3441  0.0363  14  GLU A N     
70   C  CA    . GLU A 16  ? 0.8031 0.9757 1.2356 0.0445  0.3415  0.0439  14  GLU A CA    
71   C  C     . GLU A 16  ? 0.9377 1.1389 1.2507 0.0558  0.3232  0.0456  14  GLU A C     
72   O  O     . GLU A 16  ? 1.1325 1.2550 1.2867 0.0752  0.2792  0.0011  14  GLU A O     
73   C  CB    . GLU A 16  ? 0.7924 0.9906 1.2962 -0.0096 0.3471  0.0299  14  GLU A CB    
74   C  CG    . GLU A 16  ? 0.8825 1.0568 1.3788 0.0124  0.3269  0.0523  14  GLU A CG    
75   C  CD    . GLU A 16  ? 0.9859 1.1079 1.5447 -0.0580 0.3334  -0.0116 14  GLU A CD    
76   O  OE1   . GLU A 16  ? 0.7905 1.3183 1.6763 -0.1831 0.3550  0.0284  14  GLU A OE1   
77   O  OE2   . GLU A 16  ? 1.0977 1.0516 1.6812 -0.0887 0.1888  -0.1196 14  GLU A OE2   
78   N  N     . ILE A 17  ? 0.8311 1.2012 1.2827 -0.0174 0.3430  0.1395  15  ILE A N     
79   C  CA    . ILE A 17  ? 0.9138 1.1612 1.2457 -0.0113 0.3362  0.2052  15  ILE A CA    
80   C  C     . ILE A 17  ? 0.9656 1.1620 1.2377 0.0088  0.3567  0.1803  15  ILE A C     
81   O  O     . ILE A 17  ? 0.8999 1.1407 1.3423 0.1117  0.3335  0.2263  15  ILE A O     
82   C  CB    . ILE A 17  ? 0.8613 1.1308 1.2227 0.0424  0.3381  0.2545  15  ILE A CB    
83   C  CG1   . ILE A 17  ? 0.8658 1.1509 1.1228 0.0086  0.3492  0.3180  15  ILE A CG1   
84   C  CG2   . ILE A 17  ? 0.8899 1.1238 1.2294 0.0946  0.3285  0.2480  15  ILE A CG2   
85   C  CD1   . ILE A 17  ? 0.8451 1.1682 1.1354 -0.0062 0.3605  0.2966  15  ILE A CD1   
86   N  N     . GLY A 18  ? 0.8906 1.1397 1.2673 -0.0786 0.3457  0.1576  16  GLY A N     
87   C  CA    . GLY A 18  ? 0.8883 1.1008 1.3057 -0.0844 0.2832  0.1412  16  GLY A CA    
88   C  C     . GLY A 18  ? 0.8635 1.1713 1.4032 -0.1297 0.2423  0.1118  16  GLY A C     
89   O  O     . GLY A 18  ? 0.8706 1.1658 1.4637 -0.1807 0.2514  0.0827  16  GLY A O     
90   N  N     . ASP A 19  ? 0.9001 1.1435 1.4607 -0.1917 0.1598  0.0877  17  ASP A N     
91   C  CA    . ASP A 19  ? 0.9918 1.0776 1.4567 -0.2169 0.1179  0.1369  17  ASP A CA    
92   C  C     . ASP A 19  ? 1.0613 1.0670 1.3898 -0.2153 0.1848  0.1769  17  ASP A C     
93   O  O     . ASP A 19  ? 1.2026 1.1560 1.4205 -0.3145 0.1553  0.1694  17  ASP A O     
94   C  CB    . ASP A 19  ? 0.9912 1.0101 1.4465 -0.2100 0.0514  0.1612  17  ASP A CB    
95   N  N     A SER A 20  ? 1.0662 1.0217 1.3517 -0.1375 0.2111  0.1912  18  SER A N     
96   N  N     B SER A 20  ? 1.0635 1.0225 1.3540 -0.1367 0.2105  0.1893  18  SER A N     
97   C  CA    A SER A 20  ? 1.1277 0.9775 1.3237 -0.0703 0.2283  0.1878  18  SER A CA    
98   C  CA    B SER A 20  ? 1.1231 0.9788 1.3271 -0.0672 0.2265  0.1846  18  SER A CA    
99   C  C     A SER A 20  ? 1.0389 0.9630 1.2830 -0.0868 0.2697  0.1713  18  SER A C     
100  C  C     B SER A 20  ? 1.0358 0.9653 1.2879 -0.0828 0.2667  0.1686  18  SER A C     
101  O  O     A SER A 20  ? 1.0721 0.9184 1.3357 -0.0953 0.2275  0.1546  18  SER A O     
102  O  O     B SER A 20  ? 1.0673 0.9291 1.3434 -0.0807 0.2244  0.1477  18  SER A O     
103  C  CB    A SER A 20  ? 1.2103 1.0013 1.2794 -0.0538 0.2215  0.2108  18  SER A CB    
104  C  CB    B SER A 20  ? 1.2033 1.0014 1.2846 -0.0495 0.2202  0.2064  18  SER A CB    
105  O  OG    A SER A 20  ? 1.3545 1.0177 1.2962 -0.0176 0.1798  0.2200  18  SER A OG    
106  O  OG    B SER A 20  ? 1.3438 1.0180 1.3013 -0.0108 0.1787  0.2133  18  SER A OG    
107  N  N     . THR A 21  ? 0.8892 0.8908 1.2532 -0.0905 0.3131  0.1432  19  THR A N     
108  C  CA    . THR A 21  ? 0.8178 0.6904 1.3104 -0.1147 0.3195  0.0698  19  THR A CA    
109  C  C     . THR A 21  ? 0.7559 0.6011 1.2311 -0.0396 0.3363  0.0351  19  THR A C     
110  O  O     . THR A 21  ? 0.7812 0.5610 1.2637 -0.0933 0.3945  0.0247  19  THR A O     
111  C  CB    . THR A 21  ? 0.8025 0.6565 1.3569 -0.0773 0.2857  0.0965  19  THR A CB    
112  O  OG1   . THR A 21  ? 0.7705 0.6879 1.4347 -0.1709 0.2829  0.0392  19  THR A OG1   
113  C  CG2   . THR A 21  ? 0.7973 0.6491 1.3571 -0.0617 0.2074  0.1363  19  THR A CG2   
114  N  N     . PHE A 22  ? 0.6900 0.5777 1.1883 -0.0499 0.3068  0.0446  20  PHE A N     
115  C  CA    . PHE A 22  ? 0.5928 0.5712 1.1706 0.0022  0.2631  0.0608  20  PHE A CA    
116  C  C     . PHE A 22  ? 0.4484 0.5471 1.1344 -0.0305 0.2275  0.0250  20  PHE A C     
117  O  O     . PHE A 22  ? 0.5095 0.4846 1.2073 0.0251  0.2416  0.0342  20  PHE A O     
118  C  CB    . PHE A 22  ? 0.5797 0.5865 1.2015 0.0204  0.2444  0.0868  20  PHE A CB    
119  C  CG    . PHE A 22  ? 0.5546 0.5831 1.2098 0.0657  0.2753  0.0994  20  PHE A CG    
120  C  CD1   . PHE A 22  ? 0.4874 0.5860 1.2229 0.0492  0.3288  0.1574  20  PHE A CD1   
121  C  CD2   . PHE A 22  ? 0.5211 0.5778 1.2422 0.0959  0.2544  0.1076  20  PHE A CD2   
122  C  CE1   . PHE A 22  ? 0.5240 0.6823 1.2943 0.0771  0.2410  0.1506  20  PHE A CE1   
123  C  CE2   . PHE A 22  ? 0.5234 0.6032 1.2218 0.0896  0.3147  0.1212  20  PHE A CE2   
124  C  CZ    . PHE A 22  ? 0.4805 0.5709 1.2435 0.0793  0.2998  0.1377  20  PHE A CZ    
125  N  N     . THR A 23  ? 0.4622 0.4627 1.0899 -0.0425 0.1584  0.0086  21  THR A N     
126  C  CA    . THR A 23  ? 0.3923 0.4612 1.0864 -0.0386 0.1110  -0.0238 21  THR A CA    
127  C  C     . THR A 23  ? 0.4422 0.4433 1.0011 -0.0056 0.0998  -0.0189 21  THR A C     
128  O  O     . THR A 23  ? 0.4964 0.4184 1.0499 0.0054  0.0631  -0.1006 21  THR A O     
129  C  CB    . THR A 23  ? 0.3731 0.4414 1.1236 -0.0375 0.1103  -0.0103 21  THR A CB    
130  O  OG1   . THR A 23  ? 0.4498 0.3032 1.1877 -0.0674 0.0648  0.0284  21  THR A OG1   
131  C  CG2   . THR A 23  ? 0.4385 0.5050 1.1250 -0.0472 0.0984  -0.0281 21  THR A CG2   
132  N  N     . VAL A 24  ? 0.3845 0.4558 0.9498 0.0313  0.1202  -0.0613 22  VAL A N     
133  C  CA    . VAL A 24  ? 0.3554 0.4138 0.8898 0.0450  0.1002  -0.0407 22  VAL A CA    
134  C  C     . VAL A 24  ? 0.2967 0.4514 0.8277 0.0609  0.0644  -0.0557 22  VAL A C     
135  O  O     . VAL A 24  ? 0.2903 0.4028 0.8805 0.0438  0.0722  -0.0766 22  VAL A O     
136  C  CB    . VAL A 24  ? 0.3168 0.4116 0.8915 0.0361  0.0597  0.0065  22  VAL A CB    
137  C  CG1   . VAL A 24  ? 0.2905 0.4590 0.9443 0.0281  0.0573  0.0482  22  VAL A CG1   
138  C  CG2   . VAL A 24  ? 0.3239 0.4620 0.8426 0.0220  0.0562  -0.0023 22  VAL A CG2   
139  N  N     . LEU A 25  ? 0.2965 0.4307 0.7930 0.0889  0.0639  -0.0888 23  LEU A N     
140  C  CA    . LEU A 25  ? 0.2957 0.4080 0.7234 0.0823  0.0257  -0.1067 23  LEU A CA    
141  C  C     . LEU A 25  ? 0.3197 0.3943 0.7685 0.0886  0.0005  -0.0941 23  LEU A C     
142  O  O     . LEU A 25  ? 0.3125 0.4290 0.6850 0.0721  0.0314  -0.1005 23  LEU A O     
143  C  CB    . LEU A 25  ? 0.3232 0.3634 0.7080 0.0721  0.0034  -0.1010 23  LEU A CB    
144  C  CG    . LEU A 25  ? 0.3290 0.3818 0.7123 0.0779  -0.0133 -0.1011 23  LEU A CG    
145  C  CD1   . LEU A 25  ? 0.3428 0.3531 0.7058 0.0775  -0.0125 -0.0765 23  LEU A CD1   
146  C  CD2   . LEU A 25  ? 0.3812 0.4112 0.7044 0.0761  -0.0410 -0.1284 23  LEU A CD2   
147  N  N     . LYS A 26  ? 0.3442 0.4105 0.7342 0.1168  -0.0173 -0.1141 24  LYS A N     
148  C  CA    . LYS A 26  ? 0.3428 0.4568 0.7251 0.1086  -0.0023 -0.0944 24  LYS A CA    
149  C  C     . LYS A 26  ? 0.3870 0.4262 0.6971 0.1233  -0.0079 -0.1013 24  LYS A C     
150  O  O     . LYS A 26  ? 0.4192 0.4335 0.6881 0.1024  -0.0151 -0.1166 24  LYS A O     
151  C  CB    . LYS A 26  ? 0.3279 0.4348 0.7342 0.1527  -0.0024 -0.1305 24  LYS A CB    
152  C  CG    . LYS A 26  ? 0.2974 0.4769 0.7848 0.1724  -0.0159 -0.1540 24  LYS A CG    
153  C  CD    . LYS A 26  ? 0.3285 0.6070 0.7411 0.1390  -0.0452 -0.1708 24  LYS A CD    
154  C  CE    . LYS A 26  ? 0.3477 0.6471 0.7846 0.1197  -0.0564 -0.1824 24  LYS A CE    
155  N  NZ    . LYS A 26  ? 0.3510 0.7060 0.8198 0.1023  -0.0751 -0.1959 24  LYS A NZ    
156  N  N     . ARG A 27  ? 0.3440 0.4374 0.6586 0.1419  -0.0118 -0.0982 25  ARG A N     
157  C  CA    . ARG A 27  ? 0.3853 0.4474 0.6370 0.1445  -0.0153 -0.0557 25  ARG A CA    
158  C  C     . ARG A 27  ? 0.4096 0.4401 0.5795 0.1497  -0.0250 -0.0503 25  ARG A C     
159  O  O     . ARG A 27  ? 0.4296 0.4068 0.5743 0.1232  -0.0763 -0.0394 25  ARG A O     
160  C  CB    . ARG A 27  ? 0.4355 0.4370 0.6334 0.1322  -0.0055 -0.0370 25  ARG A CB    
161  C  CG    . ARG A 27  ? 0.4109 0.3617 0.5895 0.1199  -0.0224 -0.0454 25  ARG A CG    
162  C  CD    . ARG A 27  ? 0.4038 0.3336 0.5570 0.1117  -0.0370 -0.0659 25  ARG A CD    
163  N  NE    . ARG A 27  ? 0.3939 0.2955 0.4863 0.0897  -0.0537 -0.0579 25  ARG A NE    
164  C  CZ    . ARG A 27  ? 0.4158 0.3308 0.5203 0.0822  -0.0627 -0.0527 25  ARG A CZ    
165  N  NH1   . ARG A 27  ? 0.3743 0.3158 0.5270 0.0748  -0.0656 -0.0686 25  ARG A NH1   
166  N  NH2   . ARG A 27  ? 0.3968 0.3138 0.5006 0.0934  -0.0717 -0.0082 25  ARG A NH2   
167  N  N     . TYR A 28  ? 0.3499 0.4175 0.5904 0.1407  0.0228  -0.0270 26  TYR A N     
168  C  CA    . TYR A 28  ? 0.3015 0.4403 0.6260 0.1133  0.0152  -0.0193 26  TYR A CA    
169  C  C     . TYR A 28  ? 0.4003 0.5307 0.6754 0.0977  0.0450  -0.0034 26  TYR A C     
170  O  O     . TYR A 28  ? 0.4174 0.5850 0.7314 0.0702  0.0151  0.0291  26  TYR A O     
171  C  CB    . TYR A 28  ? 0.3015 0.3714 0.5990 0.0876  0.0052  -0.0015 26  TYR A CB    
172  C  CG    . TYR A 28  ? 0.3000 0.3491 0.5915 0.0888  0.0052  -0.0181 26  TYR A CG    
173  C  CD1   . TYR A 28  ? 0.2905 0.3735 0.5487 0.0897  0.0072  -0.0112 26  TYR A CD1   
174  C  CD2   . TYR A 28  ? 0.2778 0.3407 0.5806 0.0646  0.0048  -0.0420 26  TYR A CD2   
175  C  CE1   . TYR A 28  ? 0.2567 0.3282 0.5280 0.1050  -0.0107 -0.0138 26  TYR A CE1   
176  C  CE2   . TYR A 28  ? 0.2993 0.3338 0.5411 0.0754  -0.0138 -0.0287 26  TYR A CE2   
177  C  CZ    . TYR A 28  ? 0.2889 0.3154 0.5602 0.1086  0.0075  -0.0077 26  TYR A CZ    
178  O  OH    . TYR A 28  ? 0.3408 0.3167 0.5282 0.1051  0.0207  0.0289  26  TYR A OH    
179  N  N     . GLN A 29  ? 0.4125 0.5177 0.6636 0.0914  0.0466  -0.0241 27  GLN A N     
180  C  CA    . GLN A 29  ? 0.3273 0.5875 0.7168 0.1530  0.0671  0.0013  27  GLN A CA    
181  C  C     . GLN A 29  ? 0.3567 0.5958 0.6998 0.1538  0.0967  -0.0107 27  GLN A C     
182  O  O     . GLN A 29  ? 0.3308 0.5376 0.6928 0.1166  0.0784  -0.0013 27  GLN A O     
183  C  CB    . GLN A 29  ? 0.3961 0.6581 0.7474 0.1901  0.0914  0.0123  27  GLN A CB    
184  C  CG    . GLN A 29  ? 0.5159 0.7547 0.7753 0.2068  0.0667  0.0122  27  GLN A CG    
185  C  CD    . GLN A 29  ? 0.5363 0.7872 0.8116 0.2455  0.0286  0.0042  27  GLN A CD    
186  O  OE1   . GLN A 29  ? 0.5530 0.6850 0.9205 0.2310  0.0865  -0.0278 27  GLN A OE1   
187  N  NE2   . GLN A 29  ? 0.5338 0.7894 0.8822 0.2533  0.0180  0.0726  27  GLN A NE2   
188  N  N     . ASN A 30  ? 0.2888 0.6483 0.7159 0.1649  0.0952  -0.0100 28  ASN A N     
189  C  CA    . ASN A 30  ? 0.4458 0.7069 0.7068 0.1115  0.1232  0.0177  28  ASN A CA    
190  C  C     . ASN A 30  ? 0.3864 0.7070 0.6681 0.1001  0.1383  0.0565  28  ASN A C     
191  O  O     . ASN A 30  ? 0.3576 0.7454 0.6435 0.0704  0.1891  0.0782  28  ASN A O     
192  C  CB    . ASN A 30  ? 0.5670 0.7220 0.8051 0.0551  0.0841  -0.0002 28  ASN A CB    
193  C  CG    . ASN A 30  ? 0.6872 0.7732 0.9241 0.0459  0.0631  -0.0573 28  ASN A CG    
194  O  OD1   . ASN A 30  ? 0.7850 0.8636 0.9497 -0.0664 0.0526  -0.1066 28  ASN A OD1   
195  N  ND2   . ASN A 30  ? 0.7705 0.8565 1.0548 -0.0136 0.0509  -0.0947 28  ASN A ND2   
196  N  N     . LEU A 31  ? 0.3931 0.6743 0.6893 0.1095  0.1473  0.0841  29  LEU A N     
197  C  CA    . LEU A 31  ? 0.4548 0.6616 0.7196 0.0812  0.1872  0.0990  29  LEU A CA    
198  C  C     . LEU A 31  ? 0.4282 0.6495 0.7025 0.0506  0.2521  0.0957  29  LEU A C     
199  O  O     . LEU A 31  ? 0.4335 0.6404 0.7408 0.0367  0.2853  0.1574  29  LEU A O     
200  C  CB    . LEU A 31  ? 0.5109 0.6422 0.7481 0.0905  0.1624  0.0844  29  LEU A CB    
201  C  CG    . LEU A 31  ? 0.4948 0.6081 0.7501 0.1060  0.1460  0.0963  29  LEU A CG    
202  C  CD1   . LEU A 31  ? 0.4299 0.6675 0.7914 0.1162  0.0842  0.0817  29  LEU A CD1   
203  C  CD2   . LEU A 31  ? 0.5142 0.6465 0.7815 0.1239  0.1535  0.0874  29  LEU A CD2   
204  N  N     . LYS A 32  ? 0.4948 0.6639 0.7215 0.0388  0.2085  0.1444  30  LYS A N     
205  C  CA    . LYS A 32  ? 0.5444 0.7251 0.7310 0.0468  0.2356  0.1737  30  LYS A CA    
206  C  C     . LYS A 32  ? 0.4997 0.7172 0.7330 0.0568  0.2156  0.2373  30  LYS A C     
207  O  O     . LYS A 32  ? 0.5798 0.7420 0.6117 0.0922  0.2733  0.2483  30  LYS A O     
208  C  CB    . LYS A 32  ? 0.5615 0.7874 0.6912 0.0351  0.2616  0.1841  30  LYS A CB    
209  C  CG    . LYS A 32  ? 0.6139 0.8413 0.7122 0.0434  0.2680  0.1271  30  LYS A CG    
210  N  N     . PRO A 33  ? 0.5510 0.7548 0.7927 0.0710  0.2414  0.2487  31  PRO A N     
211  C  CA    . PRO A 33  ? 0.5870 0.7651 0.8169 0.0860  0.1989  0.3180  31  PRO A CA    
212  C  C     . PRO A 33  ? 0.5951 0.7998 0.7458 0.1091  0.2006  0.3352  31  PRO A C     
213  O  O     . PRO A 33  ? 0.5697 0.8353 0.7291 0.1852  0.2439  0.3394  31  PRO A O     
214  C  CB    . PRO A 33  ? 0.6161 0.8141 0.8476 0.0988  0.2503  0.3024  31  PRO A CB    
215  C  CG    . PRO A 33  ? 0.5022 0.8213 0.9093 0.0982  0.2366  0.2890  31  PRO A CG    
216  C  CD    . PRO A 33  ? 0.5226 0.7399 0.8513 0.0597  0.2380  0.2864  31  PRO A CD    
217  N  N     . ILE A 34  ? 0.6409 0.8085 0.7114 0.1357  0.1892  0.3212  32  ILE A N     
218  C  CA    . ILE A 34  ? 0.6760 0.8236 0.7147 0.1605  0.1935  0.2890  32  ILE A CA    
219  C  C     . ILE A 34  ? 0.6802 0.8754 0.8035 0.1788  0.1785  0.2730  32  ILE A C     
220  O  O     . ILE A 34  ? 0.6379 0.8652 0.7263 0.1397  0.1977  0.3767  32  ILE A O     
221  C  CB    . ILE A 34  ? 0.6637 0.8301 0.6571 0.1187  0.1916  0.2408  32  ILE A CB    
222  C  CG1   . ILE A 34  ? 0.6265 0.8166 0.6130 0.0971  0.1946  0.1962  32  ILE A CG1   
223  C  CG2   . ILE A 34  ? 0.7536 0.8055 0.6911 0.1442  0.1743  0.2111  32  ILE A CG2   
224  C  CD1   . ILE A 34  ? 0.5626 0.8172 0.6354 0.0891  0.1347  0.1790  32  ILE A CD1   
225  N  N     . GLY A 35  ? 0.7627 0.8394 0.9266 0.1609  0.1721  0.2659  33  GLY A N     
226  C  CA    . GLY A 35  ? 0.8000 0.8652 0.9169 0.1525  0.1623  0.2970  33  GLY A CA    
227  C  C     . GLY A 35  ? 0.8513 0.7833 0.9635 0.1511  0.1401  0.3117  33  GLY A C     
228  O  O     . GLY A 35  ? 0.8869 0.7404 0.9425 0.1624  0.0851  0.2552  33  GLY A O     
229  N  N     . SER A 36  ? 0.8745 0.8291 1.0711 0.1820  0.0892  0.3270  34  SER A N     
230  C  CA    . SER A 36  ? 0.9750 0.8523 1.1393 0.1373  0.0584  0.4065  34  SER A CA    
231  C  C     . SER A 36  ? 0.9606 0.9309 1.2425 0.1572  0.0372  0.3544  34  SER A C     
232  O  O     . SER A 36  ? 1.0946 1.0961 1.1774 0.2018  0.0030  0.5154  34  SER A O     
233  C  CB    . SER A 36  ? 1.0545 0.8949 1.1488 0.1081  0.0855  0.4615  34  SER A CB    
234  O  OG    . SER A 36  ? 1.1738 0.8008 1.2001 -0.0209 0.0646  0.5877  34  SER A OG    
235  N  N     . GLY A 37  ? 0.8393 0.8776 1.3444 0.1356  0.0312  0.2732  35  GLY A N     
236  C  CA    . GLY A 37  ? 0.8807 0.8555 1.3765 0.1138  0.0998  0.2185  35  GLY A CA    
237  C  C     . GLY A 37  ? 0.8884 0.7171 1.4418 0.0343  0.1458  0.2536  35  GLY A C     
238  O  O     . GLY A 37  ? 0.8395 0.7047 1.4273 0.0745  0.1935  0.2495  35  GLY A O     
239  N  N     . ALA A 38  ? 0.9886 0.6796 1.4721 0.0603  0.1641  0.2918  36  ALA A N     
240  C  CA    . ALA A 38  ? 1.0426 0.8180 1.4217 0.0718  0.1186  0.3501  36  ALA A CA    
241  C  C     . ALA A 38  ? 1.0268 0.9401 1.4343 0.2067  -0.0094 0.3449  36  ALA A C     
242  O  O     . ALA A 38  ? 0.9477 1.1079 1.4551 0.1879  -0.0565 0.3576  36  ALA A O     
243  C  CB    . ALA A 38  ? 0.9963 0.8762 1.4189 0.0426  0.1785  0.3234  36  ALA A CB    
244  N  N     . GLN A 39  ? 1.1523 0.8718 1.4511 0.2911  -0.0455 0.2964  37  GLN A N     
245  C  CA    . GLN A 39  ? 1.2118 0.8805 1.4098 0.3441  -0.0514 0.2550  37  GLN A CA    
246  C  C     . GLN A 39  ? 1.2150 0.9128 1.2980 0.2972  0.0153  0.1359  37  GLN A C     
247  O  O     . GLN A 39  ? 1.4070 0.7465 1.2405 0.2962  0.0083  0.0643  37  GLN A O     
248  C  CB    . GLN A 39  ? 1.1558 0.8249 1.4725 0.3435  -0.0495 0.2943  37  GLN A CB    
249  N  N     . GLY A 40  ? 1.0037 0.8481 1.1671 0.2511  0.0399  0.1224  38  GLY A N     
250  C  CA    . GLY A 40  ? 0.8979 0.7214 1.0240 0.1998  0.0871  0.1507  38  GLY A CA    
251  C  C     . GLY A 40  ? 0.8088 0.7556 0.9677 0.1698  0.1533  0.1727  38  GLY A C     
252  O  O     . GLY A 40  ? 0.7758 0.7670 1.1046 0.1420  0.1895  0.2159  38  GLY A O     
253  N  N     . ILE A 41  ? 0.8032 0.7213 0.8588 0.1008  0.1926  0.1407  39  ILE A N     
254  C  CA    . ILE A 41  ? 0.7470 0.5513 0.8813 0.0748  0.2041  0.1336  39  ILE A CA    
255  C  C     . ILE A 41  ? 0.6410 0.4902 0.7194 0.0924  0.1979  0.1262  39  ILE A C     
256  O  O     . ILE A 41  ? 0.5064 0.4192 0.7508 0.1398  0.1652  0.0622  39  ILE A O     
257  C  CB    . ILE A 41  ? 0.7741 0.6266 0.9605 0.0721  0.2086  0.1047  39  ILE A CB    
258  C  CG1   . ILE A 41  ? 0.9100 0.7047 1.0984 0.0003  0.1622  0.0730  39  ILE A CG1   
259  C  CG2   . ILE A 41  ? 0.7283 0.6900 0.9345 0.0856  0.2727  0.0807  39  ILE A CG2   
260  C  CD1   . ILE A 41  ? 0.9624 0.7471 1.1126 0.0031  0.1396  0.0771  39  ILE A CD1   
261  N  N     . VAL A 42  ? 0.5945 0.4868 0.6822 0.0658  0.2046  0.1405  40  VAL A N     
262  C  CA    . VAL A 42  ? 0.5689 0.4821 0.6453 0.0861  0.1774  0.1134  40  VAL A CA    
263  C  C     . VAL A 42  ? 0.5832 0.5634 0.6578 0.0901  0.1861  0.1197  40  VAL A C     
264  O  O     . VAL A 42  ? 0.6063 0.5680 0.6161 0.0792  0.1892  0.1431  40  VAL A O     
265  C  CB    . VAL A 42  ? 0.5723 0.5131 0.5818 0.0668  0.2215  0.0928  40  VAL A CB    
266  C  CG1   . VAL A 42  ? 0.4809 0.4795 0.5144 0.0816  0.2570  0.0810  40  VAL A CG1   
267  C  CG2   . VAL A 42  ? 0.6082 0.4956 0.6207 0.0679  0.1959  0.0745  40  VAL A CG2   
268  N  N     . CYS A 43  ? 0.5238 0.4705 0.6307 0.0892  0.1782  0.1202  41  CYS A N     
269  C  CA    . CYS A 43  ? 0.5363 0.5264 0.6411 0.0504  0.1552  0.0768  41  CYS A CA    
270  C  C     . CYS A 43  ? 0.5327 0.4831 0.6064 0.0680  0.1396  0.0776  41  CYS A C     
271  O  O     . CYS A 43  ? 0.4693 0.5032 0.6073 0.0864  0.1311  0.0030  41  CYS A O     
272  C  CB    . CYS A 43  ? 0.4994 0.5898 0.6912 0.0361  0.1587  0.0992  41  CYS A CB    
273  S  SG    . CYS A 43  ? 0.5126 0.6673 0.7818 0.0196  0.1622  0.1187  41  CYS A SG    
274  N  N     . ALA A 44  ? 0.5250 0.4881 0.5580 0.0791  0.1661  0.0708  42  ALA A N     
275  C  CA    . ALA A 44  ? 0.4710 0.4759 0.5815 0.1199  0.1249  0.0408  42  ALA A CA    
276  C  C     . ALA A 44  ? 0.4923 0.5148 0.6515 0.0941  0.1197  0.0395  42  ALA A C     
277  O  O     . ALA A 44  ? 0.4546 0.4875 0.6837 0.0773  0.1416  0.0883  42  ALA A O     
278  C  CB    . ALA A 44  ? 0.4576 0.4998 0.5889 0.1387  0.1330  0.0461  42  ALA A CB    
279  N  N     . ALA A 45  ? 0.4419 0.3954 0.5782 0.0624  0.0823  0.0130  43  ALA A N     
280  C  CA    . ALA A 45  ? 0.4364 0.4369 0.5677 0.0731  0.0739  -0.0221 43  ALA A CA    
281  C  C     . ALA A 45  ? 0.4210 0.4312 0.5422 0.0899  0.0465  -0.0164 43  ALA A C     
282  O  O     . ALA A 45  ? 0.4634 0.3752 0.5510 0.0410  0.0313  -0.0077 43  ALA A O     
283  C  CB    . ALA A 45  ? 0.4092 0.4969 0.6240 0.0992  0.0566  -0.0376 43  ALA A CB    
284  N  N     . TYR A 46  ? 0.4008 0.4276 0.5460 0.0962  0.0534  -0.0307 44  TYR A N     
285  C  CA    . TYR A 46  ? 0.3904 0.3938 0.5667 0.0796  0.0000  -0.0491 44  TYR A CA    
286  C  C     . TYR A 46  ? 0.4191 0.3631 0.6165 0.1037  -0.0259 -0.0366 44  TYR A C     
287  O  O     . TYR A 46  ? 0.4164 0.4096 0.6681 0.1354  -0.0331 -0.0633 44  TYR A O     
288  C  CB    . TYR A 46  ? 0.4147 0.4177 0.5557 0.1038  -0.0191 -0.0319 44  TYR A CB    
289  C  CG    . TYR A 46  ? 0.5055 0.3892 0.6095 0.1125  -0.0281 -0.0593 44  TYR A CG    
290  C  CD1   . TYR A 46  ? 0.5366 0.4327 0.6043 0.1311  -0.0334 -0.0258 44  TYR A CD1   
291  C  CD2   . TYR A 46  ? 0.5774 0.3665 0.6576 0.1412  -0.0304 -0.0446 44  TYR A CD2   
292  C  CE1   . TYR A 46  ? 0.5671 0.4655 0.6379 0.1112  -0.0174 -0.0145 44  TYR A CE1   
293  C  CE2   . TYR A 46  ? 0.6192 0.3702 0.6776 0.1028  -0.0391 -0.0327 44  TYR A CE2   
294  C  CZ    . TYR A 46  ? 0.5655 0.3853 0.6852 0.1547  -0.0253 -0.0402 44  TYR A CZ    
295  O  OH    . TYR A 46  ? 0.5901 0.3642 0.6741 0.1535  -0.0401 -0.0885 44  TYR A OH    
296  N  N     . ASP A 47  ? 0.4550 0.3277 0.5735 0.0933  -0.0431 -0.0378 45  ASP A N     
297  C  CA    . ASP A 47  ? 0.4466 0.3120 0.5365 0.0919  -0.0807 -0.0735 45  ASP A CA    
298  C  C     . ASP A 47  ? 0.4675 0.3474 0.5658 0.1088  -0.0986 -0.0607 45  ASP A C     
299  O  O     . ASP A 47  ? 0.4518 0.3691 0.5380 0.1101  -0.1034 -0.0844 45  ASP A O     
300  C  CB    . ASP A 47  ? 0.4316 0.2954 0.4971 0.0750  -0.0975 -0.0535 45  ASP A CB    
301  C  CG    . ASP A 47  ? 0.4165 0.2924 0.4952 0.0785  -0.0875 -0.0349 45  ASP A CG    
302  O  OD1   . ASP A 47  ? 0.3960 0.3304 0.4808 0.0963  -0.0655 -0.0448 45  ASP A OD1   
303  O  OD2   . ASP A 47  ? 0.4136 0.2906 0.4996 0.0759  -0.0827 -0.0164 45  ASP A OD2   
304  N  N     . ALA A 48  ? 0.4861 0.3441 0.5857 0.1237  -0.0995 -0.0667 46  ALA A N     
305  C  CA    . ALA A 48  ? 0.4918 0.4047 0.6393 0.1504  -0.1284 -0.0454 46  ALA A CA    
306  C  C     . ALA A 48  ? 0.5140 0.3019 0.6717 0.1422  -0.1221 -0.0309 46  ALA A C     
307  O  O     . ALA A 48  ? 0.5491 0.2801 0.6274 0.1663  -0.1423 -0.0876 46  ALA A O     
308  C  CB    . ALA A 48  ? 0.4979 0.4323 0.6909 0.1768  -0.1137 -0.0412 46  ALA A CB    
309  N  N     . ILE A 49  ? 0.5069 0.2858 0.6349 0.1004  -0.1423 -0.0485 47  ILE A N     
310  C  CA    . ILE A 49  ? 0.4992 0.3224 0.5772 0.0897  -0.1866 -0.0314 47  ILE A CA    
311  C  C     . ILE A 49  ? 0.5338 0.3272 0.6169 0.0908  -0.1497 0.0120  47  ILE A C     
312  O  O     . ILE A 49  ? 0.5356 0.2823 0.6692 0.1066  -0.2179 0.0022  47  ILE A O     
313  C  CB    . ILE A 49  ? 0.4815 0.3437 0.6196 0.0842  -0.1932 -0.0340 47  ILE A CB    
314  C  CG1   . ILE A 49  ? 0.4653 0.3722 0.6449 0.0897  -0.1798 -0.0593 47  ILE A CG1   
315  C  CG2   . ILE A 49  ? 0.4609 0.3838 0.6247 0.0916  -0.1999 -0.0178 47  ILE A CG2   
316  C  CD1   . ILE A 49  ? 0.4374 0.4049 0.6531 0.0871  -0.1667 -0.0781 47  ILE A CD1   
317  N  N     . LEU A 50  ? 0.5119 0.2986 0.5417 0.0891  -0.1179 0.0112  48  LEU A N     
318  C  CA    . LEU A 50  ? 0.5368 0.3241 0.5492 0.0416  -0.1116 0.0048  48  LEU A CA    
319  C  C     . LEU A 50  ? 0.5774 0.4003 0.6362 0.0773  -0.1062 -0.0367 48  LEU A C     
320  O  O     . LEU A 50  ? 0.5632 0.4064 0.6989 0.0738  -0.1535 -0.0220 48  LEU A O     
321  C  CB    . LEU A 50  ? 0.5134 0.3432 0.4882 0.0464  -0.1319 0.0164  48  LEU A CB    
322  C  CG    . LEU A 50  ? 0.4765 0.3712 0.5043 0.0474  -0.1297 0.0129  48  LEU A CG    
323  C  CD1   . LEU A 50  ? 0.4957 0.3681 0.5176 0.0460  -0.1298 0.0218  48  LEU A CD1   
324  C  CD2   . LEU A 50  ? 0.4997 0.4281 0.4770 0.0175  -0.1254 0.0119  48  LEU A CD2   
325  N  N     . GLU A 51  ? 0.5821 0.3879 0.6659 0.0945  -0.0907 -0.0198 49  GLU A N     
326  C  CA    . GLU A 51  ? 0.5801 0.3854 0.6335 0.0737  -0.1338 -0.0306 49  GLU A CA    
327  C  C     . GLU A 51  ? 0.5594 0.4147 0.6090 0.0895  -0.1083 -0.0253 49  GLU A C     
328  O  O     . GLU A 51  ? 0.6327 0.4544 0.5593 0.1093  -0.1403 -0.1548 49  GLU A O     
329  C  CB    . GLU A 51  ? 0.6306 0.3629 0.6825 0.1051  -0.1741 -0.0412 49  GLU A CB    
330  C  CG    . GLU A 51  ? 0.6977 0.3499 0.7789 0.1266  -0.1949 -0.0592 49  GLU A CG    
331  C  CD    . GLU A 51  ? 0.7221 0.3340 0.8443 0.1422  -0.2362 -0.0786 49  GLU A CD    
332  O  OE1   . GLU A 51  ? 0.8445 0.3499 0.8528 0.0994  -0.2280 -0.1080 49  GLU A OE1   
333  O  OE2   . GLU A 51  ? 0.7787 0.3760 0.9202 0.1911  -0.2405 -0.0850 49  GLU A OE2   
334  N  N     . ARG A 52  ? 0.5665 0.3970 0.5573 0.0520  -0.1053 -0.0640 50  ARG A N     
335  C  CA    . ARG A 52  ? 0.5650 0.4207 0.5842 0.0805  -0.0775 -0.0127 50  ARG A CA    
336  C  C     . ARG A 52  ? 0.4995 0.4044 0.5297 0.1076  -0.0476 -0.0220 50  ARG A C     
337  O  O     . ARG A 52  ? 0.4771 0.3935 0.5448 0.1302  -0.0798 0.0197  50  ARG A O     
338  C  CB    . ARG A 52  ? 0.5685 0.4277 0.5696 0.0761  -0.0755 -0.0237 50  ARG A CB    
339  C  CG    . ARG A 52  ? 0.6211 0.5790 0.5632 0.0300  -0.1084 -0.0507 50  ARG A CG    
340  C  CD    . ARG A 52  ? 0.6103 0.6805 0.5766 0.0071  -0.1250 -0.0623 50  ARG A CD    
341  N  NE    . ARG A 52  ? 0.6738 0.6938 0.6275 0.0568  -0.0665 -0.0469 50  ARG A NE    
342  C  CZ    . ARG A 52  ? 0.7113 0.8022 0.7084 0.0338  -0.0361 -0.0116 50  ARG A CZ    
343  N  NH1   . ARG A 52  ? 0.7933 0.7736 0.7645 -0.0023 0.0039  -0.0027 50  ARG A NH1   
344  N  NH2   . ARG A 52  ? 0.7024 0.8957 0.6913 0.0398  -0.0337 0.0147  50  ARG A NH2   
345  N  N     . ASN A 53  ? 0.4726 0.4000 0.4551 0.0970  -0.0282 -0.0374 51  ASN A N     
346  C  CA    . ASN A 53  ? 0.4890 0.4183 0.4905 0.1010  -0.0375 -0.0406 51  ASN A CA    
347  C  C     . ASN A 53  ? 0.4444 0.3926 0.4653 0.0733  -0.0276 -0.0203 51  ASN A C     
348  O  O     . ASN A 53  ? 0.4996 0.3818 0.4980 0.0248  -0.0165 -0.0067 51  ASN A O     
349  C  CB    . ASN A 53  ? 0.5475 0.4503 0.4880 0.1007  -0.0133 -0.0793 51  ASN A CB    
350  C  CG    . ASN A 53  ? 0.5938 0.4797 0.5390 0.1161  0.0018  -0.1087 51  ASN A CG    
351  O  OD1   . ASN A 53  ? 0.6102 0.4449 0.5887 0.1118  0.0497  -0.1295 51  ASN A OD1   
352  N  ND2   . ASN A 53  ? 0.6500 0.5201 0.5276 0.1094  0.0359  -0.1973 51  ASN A ND2   
353  N  N     . VAL A 54  ? 0.3939 0.3787 0.4189 0.0788  -0.0149 0.0072  52  VAL A N     
354  C  CA    . VAL A 54  ? 0.3892 0.3749 0.4476 0.0668  -0.0229 -0.0084 52  VAL A CA    
355  C  C     . VAL A 54  ? 0.3440 0.3717 0.4259 0.0478  -0.0387 -0.0259 52  VAL A C     
356  O  O     . VAL A 54  ? 0.4018 0.3557 0.4546 0.0753  -0.0154 -0.0295 52  VAL A O     
357  C  CB    . VAL A 54  ? 0.3819 0.3357 0.4643 0.0786  -0.0331 -0.0103 52  VAL A CB    
358  C  CG1   . VAL A 54  ? 0.3837 0.3376 0.4458 0.0651  -0.0307 0.0039  52  VAL A CG1   
359  C  CG2   . VAL A 54  ? 0.3971 0.3381 0.4765 0.0762  -0.0201 -0.0048 52  VAL A CG2   
360  N  N     . ALA A 55  ? 0.3489 0.3642 0.4428 0.0532  0.0158  0.0041  53  ALA A N     
361  C  CA    . ALA A 55  ? 0.3974 0.3920 0.4737 0.0475  0.0440  0.0262  53  ALA A CA    
362  C  C     . ALA A 55  ? 0.4021 0.3901 0.4982 0.0527  0.0279  0.0290  53  ALA A C     
363  O  O     . ALA A 55  ? 0.3647 0.3573 0.4583 0.0288  0.0248  0.0518  53  ALA A O     
364  C  CB    . ALA A 55  ? 0.4108 0.3909 0.4874 0.0424  0.0322  0.0366  53  ALA A CB    
365  N  N     . ILE A 56  ? 0.4027 0.3917 0.5223 0.0345  0.0624  0.0530  54  ILE A N     
366  C  CA    . ILE A 56  ? 0.4088 0.3425 0.5328 0.0361  0.0505  0.0353  54  ILE A CA    
367  C  C     . ILE A 56  ? 0.4105 0.3571 0.5545 0.0398  0.0544  0.0576  54  ILE A C     
368  O  O     . ILE A 56  ? 0.4681 0.3348 0.6116 0.0337  0.0787  0.0814  54  ILE A O     
369  C  CB    . ILE A 56  ? 0.3911 0.3803 0.5712 0.0463  0.0506  0.0076  54  ILE A CB    
370  C  CG1   . ILE A 56  ? 0.4045 0.4030 0.6142 0.0436  0.0304  -0.0089 54  ILE A CG1   
371  C  CG2   . ILE A 56  ? 0.3861 0.3620 0.5937 0.0372  0.0382  -0.0095 54  ILE A CG2   
372  C  CD1   . ILE A 56  ? 0.3810 0.4963 0.5925 0.0612  0.0249  0.0008  54  ILE A CD1   
373  N  N     . LYS A 57  ? 0.3599 0.2783 0.5521 0.0549  0.0653  0.0594  55  LYS A N     
374  C  CA    . LYS A 57  ? 0.4439 0.3114 0.6089 -0.0019 0.0604  0.0915  55  LYS A CA    
375  C  C     . LYS A 57  ? 0.4482 0.3335 0.6173 -0.0043 0.0474  0.0627  55  LYS A C     
376  O  O     . LYS A 57  ? 0.4191 0.2948 0.6131 -0.0380 0.0191  0.0701  55  LYS A O     
377  C  CB    . LYS A 57  ? 0.4740 0.3564 0.6549 0.0530  0.0283  0.0916  55  LYS A CB    
378  C  CG    . LYS A 57  ? 0.5369 0.4388 0.6777 0.0893  0.0366  0.0563  55  LYS A CG    
379  C  CD    . LYS A 57  ? 0.5212 0.6234 0.7627 0.1008  0.0317  0.0815  55  LYS A CD    
380  C  CE    . LYS A 57  ? 0.5301 0.7894 0.7982 0.1398  0.0582  0.0566  55  LYS A CE    
381  N  NZ    . LYS A 57  ? 0.5664 0.8248 0.9450 0.2052  0.1084  0.0326  55  LYS A NZ    
382  N  N     . LYS A 58  ? 0.4325 0.3550 0.6370 -0.0099 0.0726  0.0711  56  LYS A N     
383  C  CA    . LYS A 58  ? 0.4762 0.3476 0.6880 0.0045  0.0962  0.0442  56  LYS A CA    
384  C  C     . LYS A 58  ? 0.4924 0.3406 0.7108 0.0242  0.0653  0.0389  56  LYS A C     
385  O  O     . LYS A 58  ? 0.5604 0.3083 0.7168 0.0022  0.0757  0.0494  56  LYS A O     
386  C  CB    . LYS A 58  ? 0.4522 0.4270 0.7709 0.0072  0.0913  -0.0002 56  LYS A CB    
387  C  CG    . LYS A 58  ? 0.4810 0.5197 0.7990 -0.0069 0.1140  -0.0128 56  LYS A CG    
388  C  CD    . LYS A 58  ? 0.4901 0.5909 0.9098 -0.0189 0.1034  0.0015  56  LYS A CD    
389  C  CE    . LYS A 58  ? 0.4717 0.5835 0.9491 -0.0345 0.1165  0.0158  56  LYS A CE    
390  N  NZ    . LYS A 58  ? 0.3997 0.6437 1.0001 -0.0202 0.0984  0.0609  56  LYS A NZ    
391  N  N     . LEU A 59  ? 0.4977 0.2625 0.6839 -0.0005 0.0263  0.0260  57  LEU A N     
392  C  CA    . LEU A 59  ? 0.4858 0.3256 0.7337 0.0442  0.0065  0.0414  57  LEU A CA    
393  C  C     . LEU A 59  ? 0.5417 0.3601 0.8249 0.0169  0.0100  0.0154  57  LEU A C     
394  O  O     . LEU A 59  ? 0.4180 0.2655 0.7951 0.0243  -0.0076 0.0065  57  LEU A O     
395  C  CB    . LEU A 59  ? 0.4730 0.3741 0.7032 0.0492  0.0106  0.0698  57  LEU A CB    
396  C  CG    . LEU A 59  ? 0.5278 0.5063 0.7173 -0.0066 0.0087  0.0518  57  LEU A CG    
397  C  CD1   . LEU A 59  ? 0.5098 0.5181 0.7289 -0.0280 0.0074  0.0274  57  LEU A CD1   
398  C  CD2   . LEU A 59  ? 0.5690 0.5702 0.7753 -0.0010 0.0161  0.0782  57  LEU A CD2   
399  N  N     . SER A 60  ? 0.5661 0.3818 0.8648 0.0271  0.0569  0.0242  58  SER A N     
400  C  CA    . SER A 60  ? 0.4527 0.4400 0.8864 0.0386  0.0463  0.0036  58  SER A CA    
401  C  C     . SER A 60  ? 0.4115 0.3803 0.8784 0.0250  0.0107  0.0282  58  SER A C     
402  O  O     . SER A 60  ? 0.3383 0.4041 0.9058 0.0846  0.0248  0.0146  58  SER A O     
403  C  CB    . SER A 60  ? 0.4616 0.5712 0.8699 0.0724  0.0396  -0.0037 58  SER A CB    
404  O  OG    . SER A 60  ? 0.5518 0.6335 0.9437 0.0380  0.0236  -0.0212 58  SER A OG    
405  N  N     . ARG A 61  ? 0.3839 0.3172 0.8010 -0.0139 0.0231  0.0483  59  ARG A N     
406  C  CA    . ARG A 61  ? 0.3998 0.3497 0.8882 0.0002  -0.0059 0.0133  59  ARG A CA    
407  C  C     . ARG A 61  ? 0.3744 0.3241 0.7831 -0.0195 -0.0054 0.0035  59  ARG A C     
408  O  O     . ARG A 61  ? 0.4009 0.3051 0.7658 -0.0220 0.0092  -0.0331 59  ARG A O     
409  C  CB    . ARG A 61  ? 0.4535 0.3818 0.9518 -0.0122 0.0277  0.0528  59  ARG A CB    
410  C  CG    . ARG A 61  ? 0.4978 0.4316 1.0586 -0.0326 0.0265  0.0246  59  ARG A CG    
411  C  CD    . ARG A 61  ? 0.5426 0.4606 1.0822 -0.0603 0.0411  0.0173  59  ARG A CD    
412  N  NE    . ARG A 61  ? 0.6083 0.5414 1.1096 -0.0568 0.0524  -0.0302 59  ARG A NE    
413  C  CZ    . ARG A 61  ? 0.5874 0.4459 1.1379 0.0240  0.0742  -0.0753 59  ARG A CZ    
414  N  NH1   . ARG A 61  ? 0.4885 0.5171 1.1643 0.0619  0.1088  -0.0365 59  ARG A NH1   
415  N  NH2   . ARG A 61  ? 0.5760 0.2728 1.1881 -0.0023 0.0827  -0.0618 59  ARG A NH2   
416  N  N     . PRO A 62  ? 0.3830 0.2908 0.7118 0.0176  -0.0176 0.0144  60  PRO A N     
417  C  CA    . PRO A 62  ? 0.3867 0.2829 0.6867 -0.0141 -0.0063 0.0215  60  PRO A CA    
418  C  C     . PRO A 62  ? 0.3539 0.3287 0.6214 0.0019  -0.0237 0.0015  60  PRO A C     
419  O  O     . PRO A 62  ? 0.3780 0.3315 0.5699 0.0150  -0.0464 0.0008  60  PRO A O     
420  C  CB    . PRO A 62  ? 0.3739 0.2875 0.7003 -0.0359 -0.0304 -0.0249 60  PRO A CB    
421  C  CG    . PRO A 62  ? 0.3991 0.2710 0.7043 -0.0111 -0.0287 -0.0224 60  PRO A CG    
422  C  CD    . PRO A 62  ? 0.3875 0.2858 0.7251 -0.0221 -0.0512 0.0000  60  PRO A CD    
423  N  N     . PHE A 63  ? 0.3062 0.3421 0.6639 0.0008  -0.0380 -0.0279 61  PHE A N     
424  C  CA    . PHE A 63  ? 0.3333 0.3023 0.6878 -0.0028 -0.0679 -0.0176 61  PHE A CA    
425  C  C     . PHE A 63  ? 0.3706 0.2740 0.6643 0.0318  -0.0557 -0.0078 61  PHE A C     
426  O  O     . PHE A 63  ? 0.4028 0.2692 0.6612 -0.0022 -0.0792 -0.0312 61  PHE A O     
427  C  CB    . PHE A 63  ? 0.3490 0.3473 0.7256 0.0313  -0.0880 0.0110  61  PHE A CB    
428  C  CG    . PHE A 63  ? 0.3381 0.3296 0.8022 0.0295  -0.0929 -0.0144 61  PHE A CG    
429  C  CD1   . PHE A 63  ? 0.3418 0.3004 0.8301 0.0400  -0.0815 0.0064  61  PHE A CD1   
430  C  CD2   . PHE A 63  ? 0.3462 0.3218 0.8640 0.0228  -0.0844 -0.0223 61  PHE A CD2   
431  C  CE1   . PHE A 63  ? 0.3402 0.3182 0.8893 0.0531  -0.0862 0.0018  61  PHE A CE1   
432  C  CE2   . PHE A 63  ? 0.3633 0.3009 0.9074 0.0233  -0.0859 -0.0136 61  PHE A CE2   
433  C  CZ    . PHE A 63  ? 0.3761 0.2838 0.8969 0.0052  -0.0875 -0.0210 61  PHE A CZ    
434  N  N     . GLN A 64  ? 0.3561 0.2587 0.6794 0.0396  -0.0855 0.0012  62  GLN A N     
435  C  CA    . GLN A 64  ? 0.3601 0.3165 0.6765 -0.0205 -0.0466 0.0021  62  GLN A CA    
436  C  C     . GLN A 64  ? 0.3434 0.2869 0.6274 -0.0322 -0.0383 -0.0237 62  GLN A C     
437  O  O     . GLN A 64  ? 0.2726 0.2735 0.6680 -0.0203 -0.0638 -0.0001 62  GLN A O     
438  C  CB    . GLN A 64  ? 0.4096 0.3103 0.6991 0.0000  -0.0071 -0.0415 62  GLN A CB    
439  C  CG    . GLN A 64  ? 0.4471 0.2893 0.6837 0.0055  0.0422  -0.0367 62  GLN A CG    
440  C  CD    . GLN A 64  ? 0.5075 0.3203 0.6850 -0.0045 0.0633  0.0176  62  GLN A CD    
441  O  OE1   . GLN A 64  ? 0.5008 0.3346 0.7246 -0.0749 0.0954  0.0244  62  GLN A OE1   
442  N  NE2   . GLN A 64  ? 0.4909 0.3360 0.6798 -0.0180 0.1330  -0.0544 62  GLN A NE2   
443  N  N     . ASN A 65  ? 0.3588 0.2391 0.5681 -0.0221 -0.0516 -0.0235 63  ASN A N     
444  C  CA    . ASN A 65  ? 0.3535 0.2279 0.5031 0.0072  -0.0617 -0.0148 63  ASN A CA    
445  C  C     . ASN A 65  ? 0.3240 0.2598 0.4433 0.0144  -0.0737 0.0123  63  ASN A C     
446  O  O     . ASN A 65  ? 0.3100 0.2590 0.4581 0.0373  -0.0556 -0.0013 63  ASN A O     
447  C  CB    . ASN A 65  ? 0.3876 0.2835 0.4815 -0.0140 -0.0371 0.0041  63  ASN A CB    
448  C  CG    . ASN A 65  ? 0.4151 0.3005 0.5140 -0.0257 -0.0253 0.0271  63  ASN A CG    
449  O  OD1   . ASN A 65  ? 0.3447 0.2678 0.4342 0.0063  -0.0476 0.0300  63  ASN A OD1   
450  N  ND2   . ASN A 65  ? 0.4270 0.2981 0.4998 -0.0307 0.0469  0.0085  63  ASN A ND2   
451  N  N     . GLN A 66  ? 0.3367 0.2327 0.4008 0.0025  -0.0800 -0.0035 64  GLN A N     
452  C  CA    . GLN A 66  ? 0.3215 0.2653 0.4074 0.0163  -0.0809 -0.0066 64  GLN A CA    
453  C  C     . GLN A 66  ? 0.3343 0.2345 0.3980 0.0353  -0.0643 0.0055  64  GLN A C     
454  O  O     . GLN A 66  ? 0.3235 0.2625 0.3722 0.0165  -0.0698 -0.0185 64  GLN A O     
455  C  CB    . GLN A 66  ? 0.3243 0.2779 0.4195 0.0395  -0.1023 -0.0136 64  GLN A CB    
456  C  CG    . GLN A 66  ? 0.3478 0.2902 0.4070 0.0227  -0.0980 -0.0168 64  GLN A CG    
457  C  CD    . GLN A 66  ? 0.3348 0.2809 0.4120 0.0295  -0.1047 -0.0263 64  GLN A CD    
458  O  OE1   . GLN A 66  ? 0.3690 0.2314 0.3613 0.0347  -0.1297 -0.0169 64  GLN A OE1   
459  N  NE2   . GLN A 66  ? 0.3627 0.2641 0.4466 0.0128  -0.0878 -0.0097 64  GLN A NE2   
460  N  N     . THR A 67  ? 0.3678 0.2493 0.4037 0.0390  -0.0675 0.0056  65  THR A N     
461  C  CA    . THR A 67  ? 0.3624 0.2705 0.4250 0.0034  -0.0643 0.0014  65  THR A CA    
462  C  C     . THR A 67  ? 0.3424 0.2621 0.3968 -0.0147 -0.0357 0.0162  65  THR A C     
463  O  O     . THR A 67  ? 0.3516 0.2571 0.3793 0.0136  -0.0417 -0.0063 65  THR A O     
464  C  CB    . THR A 67  ? 0.3846 0.2698 0.4303 0.0051  -0.0542 -0.0040 65  THR A CB    
465  O  OG1   . THR A 67  ? 0.3819 0.2610 0.4278 0.0444  -0.0907 0.0166  65  THR A OG1   
466  C  CG2   . THR A 67  ? 0.3995 0.3152 0.4300 -0.0098 -0.0558 0.0268  65  THR A CG2   
467  N  N     . HIS A 68  ? 0.3388 0.2562 0.4057 -0.0151 -0.0147 0.0078  66  HIS A N     
468  C  CA    . HIS A 68  ? 0.4119 0.3039 0.4463 -0.0197 -0.0051 0.0085  66  HIS A CA    
469  C  C     . HIS A 68  ? 0.3800 0.2722 0.4498 -0.0051 -0.0243 0.0152  66  HIS A C     
470  O  O     . HIS A 68  ? 0.3688 0.2707 0.4405 0.0127  0.0338  -0.0165 66  HIS A O     
471  C  CB    . HIS A 68  ? 0.4001 0.3046 0.4989 -0.0294 -0.0154 -0.0008 66  HIS A CB    
472  C  CG    . HIS A 68  ? 0.5223 0.3680 0.5165 0.0031  0.0320  -0.0164 66  HIS A CG    
473  N  ND1   . HIS A 68  ? 0.6132 0.4781 0.6083 0.0253  0.0880  0.0504  66  HIS A ND1   
474  C  CD2   . HIS A 68  ? 0.6033 0.3583 0.5223 -0.0201 0.0534  -0.0286 66  HIS A CD2   
475  C  CE1   . HIS A 68  ? 0.6095 0.4939 0.5851 0.0456  0.1292  0.0558  66  HIS A CE1   
476  N  NE2   . HIS A 68  ? 0.6278 0.3671 0.5700 -0.0409 0.1004  0.0281  66  HIS A NE2   
477  N  N     . ALA A 69  ? 0.3491 0.2736 0.4222 0.0155  -0.0516 0.0167  67  ALA A N     
478  C  CA    . ALA A 69  ? 0.3417 0.2599 0.4207 0.0230  -0.0664 0.0069  67  ALA A CA    
479  C  C     . ALA A 69  ? 0.3691 0.2874 0.4179 0.0133  -0.0869 0.0084  67  ALA A C     
480  O  O     . ALA A 69  ? 0.3462 0.2291 0.3932 0.0075  -0.0907 -0.0078 67  ALA A O     
481  C  CB    . ALA A 69  ? 0.3474 0.2679 0.4128 0.0020  -0.0782 0.0196  67  ALA A CB    
482  N  N     . LYS A 70  ? 0.3741 0.2433 0.3915 0.0099  -0.0733 -0.0029 68  LYS A N     
483  C  CA    . LYS A 70  ? 0.3636 0.2911 0.3700 0.0159  -0.0577 0.0109  68  LYS A CA    
484  C  C     . LYS A 70  ? 0.3796 0.2843 0.3572 0.0090  -0.0506 0.0046  68  LYS A C     
485  O  O     . LYS A 70  ? 0.3563 0.2672 0.3434 0.0245  -0.0457 0.0175  68  LYS A O     
486  C  CB    . LYS A 70  ? 0.3695 0.2458 0.3118 0.0118  -0.0555 0.0095  68  LYS A CB    
487  C  CG    . LYS A 70  ? 0.3661 0.2943 0.2908 0.0268  -0.0864 0.0074  68  LYS A CG    
488  C  CD    . LYS A 70  ? 0.3696 0.2897 0.3210 0.0286  -0.0669 -0.0181 68  LYS A CD    
489  C  CE    . LYS A 70  ? 0.3634 0.3213 0.3251 0.0239  -0.0713 -0.0125 68  LYS A CE    
490  N  NZ    . LYS A 70  ? 0.3842 0.3492 0.3642 0.0413  -0.0734 -0.0260 68  LYS A NZ    
491  N  N     . ARG A 71  ? 0.3624 0.2556 0.3475 0.0220  -0.0445 0.0357  69  ARG A N     
492  C  CA    . ARG A 71  ? 0.4132 0.3367 0.3959 0.0072  -0.0607 0.0089  69  ARG A CA    
493  C  C     . ARG A 71  ? 0.3639 0.3212 0.3701 0.0123  -0.0307 -0.0067 69  ARG A C     
494  O  O     . ARG A 71  ? 0.3561 0.2853 0.3442 0.0035  -0.0314 -0.0010 69  ARG A O     
495  C  CB    . ARG A 71  ? 0.4134 0.3967 0.4009 0.0311  -0.0665 0.0029  69  ARG A CB    
496  C  CG    . ARG A 71  ? 0.5251 0.4528 0.5244 0.0493  -0.0925 -0.0437 69  ARG A CG    
497  C  CD    . ARG A 71  ? 0.6127 0.5888 0.6098 0.0530  -0.1079 -0.0597 69  ARG A CD    
498  N  NE    . ARG A 71  ? 0.7179 0.7220 0.7541 0.0249  -0.1455 -0.1181 69  ARG A NE    
499  C  CZ    . ARG A 71  ? 0.6338 0.6844 0.7127 0.0591  -0.1157 -0.0907 69  ARG A CZ    
500  N  NH1   . ARG A 71  ? 0.6238 0.7585 0.7402 0.0735  -0.0661 -0.0950 69  ARG A NH1   
501  N  NH2   . ARG A 71  ? 0.4978 0.5766 0.6848 0.0187  -0.1466 -0.0331 69  ARG A NH2   
502  N  N     . ALA A 72  ? 0.3508 0.3018 0.3824 0.0168  -0.0207 -0.0291 70  ALA A N     
503  C  CA    . ALA A 72  ? 0.3576 0.3047 0.3757 0.0086  -0.0408 -0.0071 70  ALA A CA    
504  C  C     . ALA A 72  ? 0.3625 0.3015 0.3916 0.0147  -0.0490 -0.0080 70  ALA A C     
505  O  O     . ALA A 72  ? 0.3089 0.2776 0.3760 0.0161  -0.0722 -0.0168 70  ALA A O     
506  C  CB    . ALA A 72  ? 0.3397 0.3176 0.3929 0.0341  -0.0284 -0.0067 70  ALA A CB    
507  N  N     . TYR A 73  ? 0.4018 0.2679 0.3903 -0.0007 -0.0495 -0.0156 71  TYR A N     
508  C  CA    . TYR A 73  ? 0.3911 0.2816 0.3789 0.0152  -0.0797 -0.0001 71  TYR A CA    
509  C  C     . TYR A 73  ? 0.3759 0.2993 0.3409 0.0152  -0.0755 0.0166  71  TYR A C     
510  O  O     . TYR A 73  ? 0.3334 0.2568 0.3490 0.0310  -0.0887 0.0077  71  TYR A O     
511  C  CB    . TYR A 73  ? 0.3839 0.2914 0.3703 0.0283  -0.0794 -0.0179 71  TYR A CB    
512  C  CG    . TYR A 73  ? 0.4037 0.2669 0.4013 -0.0038 -0.1024 -0.0034 71  TYR A CG    
513  C  CD1   . TYR A 73  ? 0.4322 0.3245 0.4281 0.0103  -0.1088 0.0076  71  TYR A CD1   
514  C  CD2   . TYR A 73  ? 0.4073 0.2894 0.3820 -0.0203 -0.1106 -0.0117 71  TYR A CD2   
515  C  CE1   . TYR A 73  ? 0.4568 0.3503 0.3678 0.0037  -0.1161 -0.0300 71  TYR A CE1   
516  C  CE2   . TYR A 73  ? 0.4414 0.3470 0.3517 -0.0155 -0.1121 -0.0420 71  TYR A CE2   
517  C  CZ    . TYR A 73  ? 0.4761 0.3437 0.3646 0.0153  -0.1127 -0.0217 71  TYR A CZ    
518  O  OH    . TYR A 73  ? 0.5944 0.3980 0.3970 -0.0125 -0.1097 -0.0417 71  TYR A OH    
519  N  N     . ARG A 74  ? 0.3640 0.2656 0.3460 0.0265  -0.0589 0.0098  72  ARG A N     
520  C  CA    . ARG A 74  ? 0.3786 0.3171 0.3730 0.0205  -0.0732 -0.0110 72  ARG A CA    
521  C  C     . ARG A 74  ? 0.3466 0.2791 0.3454 0.0421  -0.0674 0.0068  72  ARG A C     
522  O  O     . ARG A 74  ? 0.3368 0.3128 0.3487 0.0255  -0.0714 0.0316  72  ARG A O     
523  C  CB    . ARG A 74  ? 0.4235 0.2580 0.3852 0.0346  -0.0654 -0.0248 72  ARG A CB    
524  C  CG    . ARG A 74  ? 0.4558 0.3102 0.3955 0.0375  -0.0320 -0.0232 72  ARG A CG    
525  C  CD    . ARG A 74  ? 0.4519 0.3954 0.4967 0.0406  -0.0463 -0.0121 72  ARG A CD    
526  N  NE    . ARG A 74  ? 0.4551 0.4233 0.5172 0.0083  -0.0627 0.0156  72  ARG A NE    
527  C  CZ    . ARG A 74  ? 0.4826 0.3919 0.4349 0.0246  -0.0589 0.0139  72  ARG A CZ    
528  N  NH1   . ARG A 74  ? 0.4689 0.3514 0.3607 0.0224  -0.0661 0.0028  72  ARG A NH1   
529  N  NH2   . ARG A 74  ? 0.4481 0.3687 0.4308 -0.0122 -0.0748 0.0505  72  ARG A NH2   
530  N  N     . GLU A 75  ? 0.3780 0.2841 0.3537 0.0379  -0.0725 0.0279  73  GLU A N     
531  C  CA    . GLU A 75  ? 0.3937 0.3056 0.3580 0.0386  -0.0828 0.0024  73  GLU A CA    
532  C  C     . GLU A 75  ? 0.4043 0.2893 0.3451 0.0204  -0.0605 0.0023  73  GLU A C     
533  O  O     . GLU A 75  ? 0.3567 0.2638 0.3276 0.0031  -0.0452 0.0069  73  GLU A O     
534  C  CB    . GLU A 75  ? 0.4221 0.3617 0.3710 0.0527  -0.0782 0.0076  73  GLU A CB    
535  C  CG    . GLU A 75  ? 0.5623 0.4702 0.4541 0.0588  -0.0993 0.0242  73  GLU A CG    
536  C  CD    . GLU A 75  ? 0.6541 0.5990 0.4888 0.1067  -0.0559 -0.0072 73  GLU A CD    
537  O  OE1   . GLU A 75  ? 0.7262 0.7246 0.6459 0.1400  0.0711  0.0234  73  GLU A OE1   
538  O  OE2   . GLU A 75  ? 0.5481 0.6401 0.5263 0.0694  -0.0338 -0.0683 73  GLU A OE2   
539  N  N     . LEU A 76  ? 0.3628 0.2658 0.3767 0.0187  -0.0594 0.0126  74  LEU A N     
540  C  CA    . LEU A 76  ? 0.3935 0.3236 0.3794 0.0463  -0.0734 0.0237  74  LEU A CA    
541  C  C     . LEU A 76  ? 0.3599 0.3296 0.3733 0.0240  -0.0928 0.0149  74  LEU A C     
542  O  O     . LEU A 76  ? 0.3755 0.3366 0.3515 0.0344  -0.1154 0.0166  74  LEU A O     
543  C  CB    . LEU A 76  ? 0.4173 0.3618 0.4688 0.0219  -0.0534 0.0023  74  LEU A CB    
544  C  CG    . LEU A 76  ? 0.4488 0.4402 0.5723 0.0500  -0.0604 -0.0126 74  LEU A CG    
545  C  CD1   . LEU A 76  ? 0.4622 0.4747 0.6194 0.0404  -0.0645 -0.0304 74  LEU A CD1   
546  C  CD2   . LEU A 76  ? 0.4806 0.4262 0.6241 0.0547  -0.0720 -0.0209 74  LEU A CD2   
547  N  N     . VAL A 77  ? 0.3428 0.3275 0.3252 0.0311  -0.0944 0.0259  75  VAL A N     
548  C  CA    . VAL A 77  ? 0.3757 0.3261 0.2864 0.0125  -0.0863 0.0170  75  VAL A CA    
549  C  C     . VAL A 77  ? 0.3989 0.3230 0.2792 0.0085  -0.0777 0.0101  75  VAL A C     
550  O  O     . VAL A 77  ? 0.4084 0.3032 0.2437 0.0034  -0.0958 0.0075  75  VAL A O     
551  C  CB    . VAL A 77  ? 0.3896 0.3355 0.2804 -0.0007 -0.0839 0.0062  75  VAL A CB    
552  C  CG1   . VAL A 77  ? 0.4177 0.3235 0.2712 -0.0192 -0.1001 -0.0274 75  VAL A CG1   
553  C  CG2   . VAL A 77  ? 0.4142 0.3340 0.3341 -0.0043 -0.0713 -0.0234 75  VAL A CG2   
554  N  N     . LEU A 78  ? 0.3848 0.2924 0.2850 0.0116  -0.0666 0.0227  76  LEU A N     
555  C  CA    . LEU A 78  ? 0.3524 0.2908 0.2812 0.0038  -0.0493 0.0196  76  LEU A CA    
556  C  C     . LEU A 78  ? 0.4000 0.3078 0.3297 0.0075  -0.0613 0.0284  76  LEU A C     
557  O  O     . LEU A 78  ? 0.4033 0.3137 0.3774 -0.0114 -0.0782 0.0400  76  LEU A O     
558  C  CB    . LEU A 78  ? 0.3364 0.2990 0.2467 -0.0120 -0.0677 0.0124  76  LEU A CB    
559  C  CG    . LEU A 78  ? 0.3624 0.3446 0.2898 0.0217  -0.0684 0.0293  76  LEU A CG    
560  C  CD1   . LEU A 78  ? 0.3877 0.3062 0.2945 0.0288  -0.0559 0.0359  76  LEU A CD1   
561  C  CD2   . LEU A 78  ? 0.3634 0.3702 0.3413 0.0215  -0.0923 0.0604  76  LEU A CD2   
562  N  N     . MET A 79  ? 0.3710 0.2649 0.2984 0.0401  -0.0569 0.0270  77  MET A N     
563  C  CA    . MET A 79  ? 0.4290 0.3324 0.3675 0.0276  -0.0641 0.0001  77  MET A CA    
564  C  C     . MET A 79  ? 0.4606 0.3325 0.3597 0.0311  -0.0810 0.0024  77  MET A C     
565  O  O     . MET A 79  ? 0.4518 0.3018 0.3808 0.0192  -0.0976 0.0363  77  MET A O     
566  C  CB    . MET A 79  ? 0.4460 0.4122 0.3968 0.0379  -0.0480 0.0246  77  MET A CB    
567  C  CG    . MET A 79  ? 0.4209 0.5272 0.4171 0.0477  -0.0877 0.0666  77  MET A CG    
568  S  SD    . MET A 79  ? 0.5329 0.6479 0.6442 0.0223  -0.0456 0.0693  77  MET A SD    
569  C  CE    . MET A 79  ? 0.3686 0.4006 0.3869 0.0158  -0.0723 0.1174  77  MET A CE    
570  N  N     . LYS A 80  ? 0.4271 0.2733 0.3661 0.0149  -0.0870 0.0026  78  LYS A N     
571  C  CA    . LYS A 80  ? 0.4827 0.3399 0.3648 0.0314  -0.0895 0.0113  78  LYS A CA    
572  C  C     . LYS A 80  ? 0.4871 0.3347 0.4006 -0.0037 -0.1004 0.0039  78  LYS A C     
573  O  O     . LYS A 80  ? 0.5309 0.2905 0.4126 0.0106  -0.1049 0.0246  78  LYS A O     
574  C  CB    . LYS A 80  ? 0.4996 0.3137 0.3999 0.0513  -0.1002 -0.0145 78  LYS A CB    
575  C  CG    . LYS A 80  ? 0.5414 0.4177 0.4665 0.0778  -0.1199 -0.0111 78  LYS A CG    
576  C  CD    . LYS A 80  ? 0.6477 0.5330 0.4878 0.0654  -0.1456 -0.0181 78  LYS A CD    
577  C  CE    . LYS A 80  ? 0.6939 0.5414 0.5374 0.0348  -0.1892 -0.0349 78  LYS A CE    
578  N  NZ    . LYS A 80  ? 0.7125 0.6474 0.6164 0.0580  -0.2425 0.0333  78  LYS A NZ    
579  N  N     . CYS A 81  ? 0.4453 0.3204 0.3449 -0.0010 -0.0944 0.0189  79  CYS A N     
580  C  CA    . CYS A 81  ? 0.4835 0.3500 0.3110 -0.0248 -0.0667 0.0272  79  CYS A CA    
581  C  C     . CYS A 81  ? 0.4848 0.3778 0.2962 -0.0390 -0.0510 0.0248  79  CYS A C     
582  O  O     . CYS A 81  ? 0.5310 0.4065 0.3816 -0.0853 -0.0226 -0.0082 79  CYS A O     
583  C  CB    . CYS A 81  ? 0.5283 0.3787 0.3050 -0.0197 -0.0553 0.0372  79  CYS A CB    
584  S  SG    . CYS A 81  ? 0.5502 0.4064 0.3257 -0.0081 -0.0379 0.0294  79  CYS A SG    
585  N  N     . VAL A 82  ? 0.4052 0.3084 0.2817 -0.0400 -0.0445 0.0275  80  VAL A N     
586  C  CA    . VAL A 82  ? 0.3964 0.3076 0.2891 -0.0267 -0.0522 0.0183  80  VAL A CA    
587  C  C     . VAL A 82  ? 0.4320 0.3303 0.3151 -0.0140 -0.0525 0.0147  80  VAL A C     
588  O  O     . VAL A 82  ? 0.4523 0.3070 0.3336 0.0151  -0.0684 -0.0112 80  VAL A O     
589  C  CB    . VAL A 82  ? 0.3623 0.3186 0.2877 -0.0150 -0.0310 0.0080  80  VAL A CB    
590  C  CG1   . VAL A 82  ? 0.3320 0.3490 0.2599 0.0015  -0.0271 0.0282  80  VAL A CG1   
591  C  CG2   . VAL A 82  ? 0.3571 0.3253 0.3222 -0.0184 -0.0331 0.0153  80  VAL A CG2   
592  N  N     . ASN A 83  ? 0.5009 0.2911 0.3124 -0.0013 -0.0685 0.0392  81  ASN A N     
593  C  CA    . ASN A 83  ? 0.4732 0.3229 0.3214 -0.0099 -0.0693 0.0365  81  ASN A CA    
594  C  C     . ASN A 83  ? 0.4523 0.2814 0.2887 -0.0318 -0.0416 0.0344  81  ASN A C     
595  O  O     . ASN A 83  ? 0.4252 0.3108 0.3038 -0.0347 -0.0635 0.0386  81  ASN A O     
596  C  CB    . ASN A 83  ? 0.5367 0.3534 0.3680 0.0036  -0.0749 0.0764  81  ASN A CB    
597  C  CG    . ASN A 83  ? 0.6491 0.4482 0.4331 0.0467  -0.0494 0.0819  81  ASN A CG    
598  O  OD1   . ASN A 83  ? 0.6570 0.4196 0.4210 0.0570  -0.1072 0.0833  81  ASN A OD1   
599  N  ND2   . ASN A 83  ? 0.7477 0.5206 0.5461 0.0003  -0.0040 0.1301  81  ASN A ND2   
600  N  N     . HIS A 84  ? 0.3858 0.2508 0.2575 -0.0296 -0.0615 0.0252  82  HIS A N     
601  C  CA    . HIS A 84  ? 0.3594 0.2564 0.2710 -0.0338 -0.0471 0.0139  82  HIS A CA    
602  C  C     . HIS A 84  ? 0.3670 0.2898 0.2519 -0.0446 -0.0697 0.0166  82  HIS A C     
603  O  O     . HIS A 84  ? 0.3612 0.2742 0.2675 -0.0317 -0.0588 0.0148  82  HIS A O     
604  C  CB    . HIS A 84  ? 0.3712 0.2722 0.2972 -0.0395 -0.0423 0.0286  82  HIS A CB    
605  C  CG    . HIS A 84  ? 0.3453 0.2609 0.2797 -0.0367 -0.0441 0.0198  82  HIS A CG    
606  N  ND1   . HIS A 84  ? 0.3511 0.2837 0.3084 -0.0294 -0.0390 0.0298  82  HIS A ND1   
607  C  CD2   . HIS A 84  ? 0.3612 0.2867 0.2870 -0.0237 -0.0309 0.0262  82  HIS A CD2   
608  C  CE1   . HIS A 84  ? 0.3630 0.2935 0.3157 -0.0126 -0.0512 0.0267  82  HIS A CE1   
609  N  NE2   . HIS A 84  ? 0.3657 0.3110 0.3237 -0.0083 -0.0387 0.0181  82  HIS A NE2   
610  N  N     . LYS A 85  ? 0.3801 0.2131 0.2391 -0.0319 -0.0559 0.0337  83  LYS A N     
611  C  CA    . LYS A 85  ? 0.4178 0.2902 0.2714 -0.0357 -0.0524 0.0124  83  LYS A CA    
612  C  C     . LYS A 85  ? 0.3874 0.2540 0.2657 -0.0176 -0.0635 0.0000  83  LYS A C     
613  O  O     . LYS A 85  ? 0.3640 0.2634 0.2691 -0.0145 -0.0551 0.0173  83  LYS A O     
614  C  CB    . LYS A 85  ? 0.4727 0.3334 0.3036 -0.0415 -0.0637 -0.0092 83  LYS A CB    
615  C  CG    . LYS A 85  ? 0.5584 0.4054 0.3345 -0.0464 -0.0825 -0.0017 83  LYS A CG    
616  C  CD    . LYS A 85  ? 0.5883 0.4530 0.4107 -0.0844 -0.1157 -0.0433 83  LYS A CD    
617  C  CE    . LYS A 85  ? 0.6557 0.5538 0.5032 -0.0780 -0.0821 -0.0869 83  LYS A CE    
618  N  NZ    . LYS A 85  ? 0.6009 0.6132 0.5820 -0.1161 -0.1295 -0.1463 83  LYS A NZ    
619  N  N     . ASN A 86  ? 0.3257 0.2751 0.2539 -0.0008 -0.0709 0.0138  84  ASN A N     
620  C  CA    . ASN A 86  ? 0.3466 0.2644 0.2423 0.0040  -0.0696 0.0038  84  ASN A CA    
621  C  C     . ASN A 86  ? 0.3218 0.2758 0.2327 0.0049  -0.0624 0.0032  84  ASN A C     
622  O  O     . ASN A 86  ? 0.3067 0.2943 0.2198 0.0177  -0.0491 -0.0063 84  ASN A O     
623  C  CB    . ASN A 86  ? 0.3323 0.2601 0.2610 -0.0037 -0.0616 -0.0019 84  ASN A CB    
624  C  CG    . ASN A 86  ? 0.3843 0.2632 0.2854 0.0046  -0.0525 -0.0125 84  ASN A CG    
625  O  OD1   . ASN A 86  ? 0.3415 0.2730 0.3098 -0.0044 -0.0485 -0.0056 84  ASN A OD1   
626  N  ND2   . ASN A 86  ? 0.4114 0.2560 0.2797 -0.0203 -0.0469 -0.0383 84  ASN A ND2   
627  N  N     . ILE A 87  ? 0.3152 0.2520 0.2060 0.0157  -0.0542 0.0286  85  ILE A N     
628  C  CA    . ILE A 87  ? 0.3192 0.2969 0.2386 0.0038  -0.0607 0.0337  85  ILE A CA    
629  C  C     . ILE A 87  ? 0.3588 0.3137 0.2955 0.0213  -0.0520 0.0502  85  ILE A C     
630  O  O     . ILE A 87  ? 0.3477 0.3081 0.2952 0.0034  -0.0616 0.0644  85  ILE A O     
631  C  CB    . ILE A 87  ? 0.3064 0.2652 0.2601 0.0020  -0.0596 0.0145  85  ILE A CB    
632  C  CG1   . ILE A 87  ? 0.2950 0.2572 0.2192 -0.0252 -0.0592 0.0134  85  ILE A CG1   
633  C  CG2   . ILE A 87  ? 0.3196 0.2862 0.2643 0.0000  -0.0587 -0.0044 85  ILE A CG2   
634  C  CD1   . ILE A 87  ? 0.2800 0.2872 0.2479 -0.0141 -0.0685 0.0138  85  ILE A CD1   
635  N  N     . ILE A 88  ? 0.3500 0.2868 0.3169 0.0146  -0.0428 0.0461  86  ILE A N     
636  C  CA    . ILE A 88  ? 0.3653 0.3410 0.2992 0.0255  -0.0446 0.0490  86  ILE A CA    
637  C  C     . ILE A 88  ? 0.3751 0.3716 0.3119 0.0173  -0.0716 0.0244  86  ILE A C     
638  O  O     . ILE A 88  ? 0.3868 0.3829 0.3053 -0.0041 -0.0742 0.0699  86  ILE A O     
639  C  CB    . ILE A 88  ? 0.3415 0.3218 0.3051 0.0286  -0.0459 0.0501  86  ILE A CB    
640  C  CG1   . ILE A 88  ? 0.3636 0.3730 0.3357 0.0109  -0.0382 0.0594  86  ILE A CG1   
641  C  CG2   . ILE A 88  ? 0.3516 0.3189 0.2836 0.0083  -0.0475 0.0506  86  ILE A CG2   
642  C  CD1   . ILE A 88  ? 0.3371 0.3818 0.3350 0.0320  -0.0370 0.0553  86  ILE A CD1   
643  N  N     . GLY A 89  ? 0.4037 0.4044 0.3635 0.0015  -0.0940 0.0347  87  GLY A N     
644  C  CA    . GLY A 89  ? 0.4492 0.4551 0.3431 -0.0102 -0.0415 0.0654  87  GLY A CA    
645  C  C     . GLY A 89  ? 0.3968 0.3798 0.3393 0.0141  -0.0743 0.0514  87  GLY A C     
646  O  O     . GLY A 89  ? 0.3675 0.4074 0.3867 -0.0052 -0.0817 0.0467  87  GLY A O     
647  N  N     . LEU A 90  ? 0.4336 0.3435 0.3875 0.0181  -0.0810 0.0501  88  LEU A N     
648  C  CA    . LEU A 90  ? 0.4016 0.3221 0.4023 0.0228  -0.0953 0.0451  88  LEU A CA    
649  C  C     . LEU A 90  ? 0.4391 0.3588 0.4321 0.0306  -0.0864 0.0275  88  LEU A C     
650  O  O     . LEU A 90  ? 0.4421 0.3899 0.4173 0.0597  -0.0856 0.0477  88  LEU A O     
651  C  CB    . LEU A 90  ? 0.3774 0.3188 0.3975 0.0560  -0.0767 0.0382  88  LEU A CB    
652  C  CG    . LEU A 90  ? 0.4278 0.3992 0.4640 0.0350  -0.0795 0.0027  88  LEU A CG    
653  C  CD1   . LEU A 90  ? 0.4501 0.3922 0.4913 0.0343  -0.0908 0.0482  88  LEU A CD1   
654  C  CD2   . LEU A 90  ? 0.4617 0.3906 0.5609 0.0683  -0.0529 -0.0285 88  LEU A CD2   
655  N  N     . LEU A 91  ? 0.4117 0.3089 0.3637 0.0226  -0.0930 -0.0077 89  LEU A N     
656  C  CA    . LEU A 91  ? 0.4529 0.3067 0.3808 0.0179  -0.0871 -0.0106 89  LEU A CA    
657  C  C     . LEU A 91  ? 0.4125 0.3068 0.3776 0.0432  -0.0916 -0.0166 89  LEU A C     
658  O  O     . LEU A 91  ? 0.4505 0.3036 0.4119 0.0472  -0.0921 -0.0284 89  LEU A O     
659  C  CB    . LEU A 91  ? 0.4678 0.3057 0.3906 0.0134  -0.0647 0.0107  89  LEU A CB    
660  C  CG    . LEU A 91  ? 0.5210 0.3265 0.3990 0.0100  -0.0712 -0.0002 89  LEU A CG    
661  C  CD1   . LEU A 91  ? 0.4917 0.3360 0.4465 0.0497  -0.0523 0.0041  89  LEU A CD1   
662  C  CD2   . LEU A 91  ? 0.5716 0.3846 0.4702 -0.0010 -0.0534 -0.0249 89  LEU A CD2   
663  N  N     . ASN A 92  ? 0.3972 0.2736 0.3758 0.0482  -0.1080 -0.0180 90  ASN A N     
664  C  CA    . ASN A 92  ? 0.3999 0.2734 0.4507 0.0527  -0.1109 -0.0104 90  ASN A CA    
665  C  C     . ASN A 92  ? 0.3872 0.2731 0.4311 0.0562  -0.1175 -0.0005 90  ASN A C     
666  O  O     . ASN A 92  ? 0.3201 0.2732 0.4303 0.0653  -0.0980 0.0120  90  ASN A O     
667  C  CB    . ASN A 92  ? 0.3743 0.2828 0.4616 0.0509  -0.1308 -0.0212 90  ASN A CB    
668  C  CG    . ASN A 92  ? 0.3872 0.3052 0.4508 0.0786  -0.1515 -0.0031 90  ASN A CG    
669  O  OD1   . ASN A 92  ? 0.3690 0.3330 0.4346 0.0645  -0.1725 -0.0261 90  ASN A OD1   
670  N  ND2   . ASN A 92  ? 0.3741 0.3222 0.4242 0.1020  -0.1912 0.0043  90  ASN A ND2   
671  N  N     . VAL A 93  ? 0.3758 0.2704 0.4248 0.0858  -0.1405 0.0031  91  VAL A N     
672  C  CA    . VAL A 93  ? 0.4038 0.2898 0.4804 0.0502  -0.1261 0.0094  91  VAL A CA    
673  C  C     . VAL A 93  ? 0.4186 0.3033 0.5515 0.0603  -0.1451 -0.0269 91  VAL A C     
674  O  O     . VAL A 93  ? 0.4702 0.3714 0.5280 0.0484  -0.1857 -0.0417 91  VAL A O     
675  C  CB    . VAL A 93  ? 0.4591 0.2987 0.5078 0.0512  -0.1143 0.0023  91  VAL A CB    
676  C  CG1   . VAL A 93  ? 0.4630 0.3252 0.5585 0.0337  -0.1153 0.0078  91  VAL A CG1   
677  C  CG2   . VAL A 93  ? 0.4767 0.3402 0.5381 0.0283  -0.1074 -0.0256 91  VAL A CG2   
678  N  N     . PHE A 94  ? 0.3896 0.3098 0.6100 0.0682  -0.1439 -0.0309 92  PHE A N     
679  C  CA    . PHE A 94  ? 0.4033 0.3453 0.6362 0.0637  -0.1866 -0.0586 92  PHE A CA    
680  C  C     . PHE A 94  ? 0.4166 0.3483 0.7110 0.0574  -0.1964 -0.0931 92  PHE A C     
681  O  O     . PHE A 94  ? 0.4477 0.3541 0.6658 0.0730  -0.1506 -0.1259 92  PHE A O     
682  C  CB    . PHE A 94  ? 0.3886 0.3581 0.5940 0.0420  -0.1739 -0.0942 92  PHE A CB    
683  C  CG    . PHE A 94  ? 0.3846 0.3475 0.6491 0.0438  -0.1365 -0.0908 92  PHE A CG    
684  C  CD1   . PHE A 94  ? 0.3795 0.3481 0.6573 0.0322  -0.1225 -0.1215 92  PHE A CD1   
685  C  CD2   . PHE A 94  ? 0.3872 0.3628 0.6427 0.0539  -0.1322 -0.0886 92  PHE A CD2   
686  C  CE1   . PHE A 94  ? 0.3389 0.3681 0.6649 0.0605  -0.1246 -0.0950 92  PHE A CE1   
687  C  CE2   . PHE A 94  ? 0.3840 0.3416 0.6504 0.0596  -0.0984 -0.0538 92  PHE A CE2   
688  C  CZ    . PHE A 94  ? 0.3485 0.3532 0.6528 0.0674  -0.0637 -0.1020 92  PHE A CZ    
689  N  N     . THR A 95  ? 0.4359 0.3688 0.8581 0.0834  -0.2451 -0.1176 93  THR A N     
690  C  CA    . THR A 95  ? 0.4424 0.3522 0.9282 0.0678  -0.2576 -0.1645 93  THR A CA    
691  C  C     . THR A 95  ? 0.4870 0.3520 0.9586 0.1170  -0.3016 -0.1415 93  THR A C     
692  O  O     . THR A 95  ? 0.4305 0.3144 0.9127 0.1872  -0.3939 -0.1810 93  THR A O     
693  C  CB    . THR A 95  ? 0.4815 0.3177 0.9903 0.0601  -0.2591 -0.1802 93  THR A CB    
694  O  OG1   . THR A 95  ? 0.3981 0.4049 1.0979 0.0033  -0.2524 -0.2062 93  THR A OG1   
695  C  CG2   . THR A 95  ? 0.5079 0.2589 0.9403 0.0585  -0.2957 -0.1448 93  THR A CG2   
696  N  N     . PRO A 96  ? 0.5060 0.3813 1.0415 0.1227  -0.2506 -0.1745 94  PRO A N     
697  C  CA    . PRO A 96  ? 0.4975 0.3969 1.0927 0.0708  -0.2889 -0.1710 94  PRO A CA    
698  C  C     . PRO A 96  ? 0.5481 0.4230 1.2012 0.0861  -0.3042 -0.2086 94  PRO A C     
699  O  O     . PRO A 96  ? 0.5702 0.4299 1.3501 0.1772  -0.2495 -0.2117 94  PRO A O     
700  C  CB    . PRO A 96  ? 0.4908 0.4610 1.1222 0.0691  -0.2396 -0.1541 94  PRO A CB    
701  C  CG    . PRO A 96  ? 0.5308 0.5087 1.1113 0.0777  -0.2242 -0.1260 94  PRO A CG    
702  C  CD    . PRO A 96  ? 0.5434 0.4915 1.0747 0.1030  -0.2273 -0.1336 94  PRO A CD    
703  N  N     . GLN A 97  ? 0.4483 0.3718 1.2467 0.1318  -0.2937 -0.1894 95  GLN A N     
704  C  CA    . GLN A 97  ? 0.4787 0.4179 1.2948 0.1054  -0.3120 -0.1837 95  GLN A CA    
705  C  C     . GLN A 97  ? 0.5032 0.4452 1.1898 0.1465  -0.3944 -0.1620 95  GLN A C     
706  O  O     . GLN A 97  ? 0.4180 0.5414 1.1925 0.1449  -0.4189 -0.1177 95  GLN A O     
707  C  CB    . GLN A 97  ? 0.4918 0.3584 1.3174 0.0475  -0.2990 -0.1631 95  GLN A CB    
708  C  CG    . GLN A 97  ? 0.4970 0.3976 1.2981 0.1060  -0.2975 -0.1519 95  GLN A CG    
709  C  CD    . GLN A 97  ? 0.5274 0.2803 1.2753 0.0235  -0.2376 -0.1742 95  GLN A CD    
710  O  OE1   . GLN A 97  ? 0.5163 0.3327 1.3185 0.1195  -0.2610 -0.1520 95  GLN A OE1   
711  N  NE2   . GLN A 97  ? 0.5250 0.2438 1.2408 0.0449  -0.1789 -0.1437 95  GLN A NE2   
712  N  N     . LYS A 98  ? 0.6250 0.4756 1.2405 0.1864  -0.4488 -0.1849 96  LYS A N     
713  C  CA    . LYS A 98  ? 0.6735 0.4235 1.2442 0.1906  -0.5318 -0.2026 96  LYS A CA    
714  C  C     . LYS A 98  ? 0.6992 0.5329 1.2085 0.1926  -0.5265 -0.1857 96  LYS A C     
715  O  O     . LYS A 98  ? 0.5584 0.4815 1.2615 -0.0632 -0.5629 -0.1617 96  LYS A O     
716  C  CB    . LYS A 98  ? 0.6496 0.6378 1.0922 0.1266  -0.6603 -0.2189 96  LYS A CB    
717  N  N     . SER A 99  ? 0.7817 0.5094 1.2716 0.2441  -0.5216 -0.2189 97  SER A N     
718  C  CA    . SER A 99  ? 0.6263 0.5654 1.2820 0.3193  -0.5811 -0.1863 97  SER A CA    
719  C  C     . SER A 99  ? 0.6093 0.4715 1.3356 0.3840  -0.4578 -0.2085 97  SER A C     
720  O  O     . SER A 99  ? 0.6283 0.6331 1.2388 0.3033  -0.3071 -0.2599 97  SER A O     
721  C  CB    . SER A 99  ? 0.5819 0.4583 1.4656 0.2241  -0.6226 -0.1511 97  SER A CB    
722  O  OG    . SER A 99  ? 0.5770 0.3592 1.5558 0.3366  -0.6218 -0.1594 97  SER A OG    
723  N  N     . LEU A 100 ? 0.5982 0.4999 1.2269 0.3426  -0.5389 -0.1230 98  LEU A N     
724  C  CA    . LEU A 100 ? 0.6373 0.4347 1.2211 0.3321  -0.4479 -0.1491 98  LEU A CA    
725  C  C     . LEU A 100 ? 0.6966 0.2498 1.2782 0.2438  -0.4466 -0.2685 98  LEU A C     
726  O  O     . LEU A 100 ? 0.7995 0.2930 1.2526 0.1306  -0.3866 -0.2999 98  LEU A O     
727  C  CB    . LEU A 100 ? 0.6340 0.4037 1.1323 0.2130  -0.4653 -0.1922 98  LEU A CB    
728  C  CG    . LEU A 100 ? 0.6961 0.3123 1.1214 0.1644  -0.4714 -0.1516 98  LEU A CG    
729  C  CD1   . LEU A 100 ? 0.7135 0.2583 1.1097 0.0907  -0.4481 -0.1425 98  LEU A CD1   
730  C  CD2   . LEU A 100 ? 0.6990 0.3820 1.0838 0.1556  -0.4929 -0.1444 98  LEU A CD2   
731  N  N     . GLU A 101 ? 0.7161 0.4561 1.2266 0.2209  -0.5060 -0.2500 99  GLU A N     
732  C  CA    . GLU A 101 ? 0.7219 0.4572 1.2858 0.2192  -0.4766 -0.2616 99  GLU A CA    
733  C  C     . GLU A 101 ? 0.5903 0.5392 1.3341 0.1256  -0.4357 -0.2485 99  GLU A C     
734  O  O     . GLU A 101 ? 0.7875 0.5003 1.3656 0.1132  -0.3311 -0.2288 99  GLU A O     
735  C  CB    . GLU A 101 ? 0.8189 0.6480 1.3333 0.3068  -0.5282 -0.1298 99  GLU A CB    
736  C  CG    . GLU A 101 ? 0.9593 0.8002 1.3306 0.3433  -0.5173 -0.1230 99  GLU A CG    
737  C  CD    . GLU A 101 ? 1.1521 0.9751 1.3885 0.3433  -0.4873 -0.0631 99  GLU A CD    
738  O  OE1   . GLU A 101 ? 1.0341 1.0565 1.3916 0.1517  -0.5651 -0.1119 99  GLU A OE1   
739  O  OE2   . GLU A 101 ? 1.1852 1.0598 1.4372 0.3305  -0.4197 -0.0079 99  GLU A OE2   
740  N  N     . GLU A 102 ? 0.5261 0.5470 1.3730 0.0890  -0.3868 -0.2507 100 GLU A N     
741  C  CA    . GLU A 102 ? 0.5578 0.5871 1.2998 0.0415  -0.4063 -0.2567 100 GLU A CA    
742  C  C     . GLU A 102 ? 0.4750 0.3552 1.3044 0.0227  -0.3724 -0.2353 100 GLU A C     
743  O  O     . GLU A 102 ? 0.4171 0.4338 1.2117 0.0371  -0.4526 -0.2437 100 GLU A O     
744  C  CB    . GLU A 102 ? 0.6455 0.7544 1.3318 0.0571  -0.3229 -0.2390 100 GLU A CB    
745  C  CG    . GLU A 102 ? 0.6679 0.8616 1.3244 0.0363  -0.3080 -0.1811 100 GLU A CG    
746  C  CD    . GLU A 102 ? 0.6896 0.9411 1.4103 0.1181  -0.3174 -0.1756 100 GLU A CD    
747  O  OE1   . GLU A 102 ? 0.7206 1.0883 1.3376 0.2596  -0.4420 -0.2120 100 GLU A OE1   
748  O  OE2   . GLU A 102 ? 0.7436 0.9689 1.4517 0.1562  -0.2416 -0.1299 100 GLU A OE2   
749  N  N     . PHE A 103 ? 0.4179 0.3678 1.2703 0.0245  -0.3797 -0.2018 101 PHE A N     
750  C  CA    . PHE A 103 ? 0.3994 0.2908 1.1819 0.0580  -0.3602 -0.1603 101 PHE A CA    
751  C  C     . PHE A 103 ? 0.2472 0.3586 1.1735 0.0860  -0.3637 -0.1582 101 PHE A C     
752  O  O     . PHE A 103 ? 0.3926 0.2935 1.1796 0.0768  -0.4126 -0.1437 101 PHE A O     
753  C  CB    . PHE A 103 ? 0.4056 0.3465 1.1532 0.0637  -0.3921 -0.1475 101 PHE A CB    
754  C  CG    . PHE A 103 ? 0.5015 0.2420 1.0780 0.0347  -0.3696 -0.1955 101 PHE A CG    
755  C  CD1   . PHE A 103 ? 0.5404 0.2204 1.0407 0.1022  -0.3571 -0.2436 101 PHE A CD1   
756  C  CD2   . PHE A 103 ? 0.5212 0.1354 1.0106 0.0501  -0.3553 -0.1789 101 PHE A CD2   
757  C  CE1   . PHE A 103 ? 0.4736 0.2491 0.9696 0.1145  -0.3141 -0.2002 101 PHE A CE1   
758  C  CE2   . PHE A 103 ? 0.4972 0.2249 1.0066 0.0683  -0.3219 -0.1567 101 PHE A CE2   
759  C  CZ    . PHE A 103 ? 0.4617 0.3017 0.9245 0.0720  -0.3243 -0.1894 101 PHE A CZ    
760  N  N     . GLN A 104 ? 0.3301 0.2804 1.1653 0.0968  -0.2960 -0.1446 102 GLN A N     
761  C  CA    . GLN A 104 ? 0.4395 0.3309 1.2010 0.0976  -0.2247 -0.1885 102 GLN A CA    
762  C  C     . GLN A 104 ? 0.4292 0.3482 1.1757 0.0772  -0.2222 -0.1283 102 GLN A C     
763  O  O     . GLN A 104 ? 0.3871 0.3512 1.0969 0.0610  -0.1841 -0.1880 102 GLN A O     
764  C  CB    . GLN A 104 ? 0.3427 0.4454 1.2473 0.1165  -0.2343 -0.1387 102 GLN A CB    
765  C  CG    . GLN A 104 ? 0.4680 0.5431 1.2683 0.0621  -0.2524 -0.1828 102 GLN A CG    
766  C  CD    . GLN A 104 ? 0.4999 0.5876 1.3488 -0.0456 -0.2654 -0.1464 102 GLN A CD    
767  O  OE1   . GLN A 104 ? 0.4654 0.6334 1.3557 -0.1632 -0.2417 -0.0880 102 GLN A OE1   
768  N  NE2   . GLN A 104 ? 0.6544 0.7311 1.3590 -0.0042 -0.2942 -0.1422 102 GLN A NE2   
769  N  N     . ASP A 105 ? 0.3637 0.3925 1.1330 0.1301  -0.1660 -0.1755 103 ASP A N     
770  C  CA    . ASP A 105 ? 0.3975 0.3201 1.0811 0.0398  -0.1325 -0.1215 103 ASP A CA    
771  C  C     . ASP A 105 ? 0.3568 0.3438 0.9558 0.0591  -0.1594 -0.1045 103 ASP A C     
772  O  O     . ASP A 105 ? 0.4365 0.2647 0.9580 0.0753  -0.1843 -0.1534 103 ASP A O     
773  C  CB    . ASP A 105 ? 0.4182 0.3605 1.1088 0.0204  -0.0988 -0.0885 103 ASP A CB    
774  C  CG    . ASP A 105 ? 0.3998 0.3937 1.0916 -0.0079 -0.1142 -0.0829 103 ASP A CG    
775  O  OD1   . ASP A 105 ? 0.4248 0.4020 1.0884 -0.0895 -0.0957 -0.0194 103 ASP A OD1   
776  O  OD2   . ASP A 105 ? 0.4143 0.4757 1.0089 -0.0038 -0.1878 -0.1225 103 ASP A OD2   
777  N  N     . VAL A 106 ? 0.3847 0.2728 0.8432 -0.0167 -0.1691 -0.1022 104 VAL A N     
778  C  CA    . VAL A 106 ? 0.3752 0.2906 0.8300 0.0331  -0.1643 -0.0692 104 VAL A CA    
779  C  C     . VAL A 106 ? 0.3291 0.3033 0.7822 0.0396  -0.1646 -0.0416 104 VAL A C     
780  O  O     . VAL A 106 ? 0.3542 0.2938 0.8135 -0.0241 -0.1586 -0.0354 104 VAL A O     
781  C  CB    . VAL A 106 ? 0.3528 0.2976 0.8241 0.0759  -0.1544 -0.0737 104 VAL A CB    
782  C  CG1   . VAL A 106 ? 0.3574 0.3065 0.8384 0.0974  -0.1322 -0.0944 104 VAL A CG1   
783  C  CG2   . VAL A 106 ? 0.3717 0.2982 0.8462 0.1074  -0.1711 -0.0363 104 VAL A CG2   
784  N  N     . TYR A 107 ? 0.3211 0.3025 0.7432 0.0663  -0.1725 -0.0493 105 TYR A N     
785  C  CA    . TYR A 107 ? 0.2926 0.3229 0.7113 0.0636  -0.1640 -0.0369 105 TYR A CA    
786  C  C     . TYR A 107 ? 0.3470 0.3224 0.6858 0.0740  -0.1682 -0.0333 105 TYR A C     
787  O  O     . TYR A 107 ? 0.3880 0.3683 0.6563 0.0589  -0.1686 -0.0372 105 TYR A O     
788  C  CB    . TYR A 107 ? 0.3090 0.3073 0.7746 0.0689  -0.1556 -0.0645 105 TYR A CB    
789  C  CG    . TYR A 107 ? 0.3205 0.4045 0.8523 0.0421  -0.1266 -0.0685 105 TYR A CG    
790  C  CD1   . TYR A 107 ? 0.3928 0.4853 0.9673 0.0321  -0.1247 -0.0922 105 TYR A CD1   
791  C  CD2   . TYR A 107 ? 0.3698 0.4539 0.8885 0.0204  -0.1299 -0.0395 105 TYR A CD2   
792  C  CE1   . TYR A 107 ? 0.3340 0.4685 0.9661 0.0288  -0.1032 -0.0728 105 TYR A CE1   
793  C  CE2   . TYR A 107 ? 0.3448 0.5039 0.9305 0.0356  -0.0917 -0.0451 105 TYR A CE2   
794  C  CZ    . TYR A 107 ? 0.3678 0.5209 0.9864 0.0414  -0.1071 -0.0735 105 TYR A CZ    
795  O  OH    . TYR A 107 ? 0.4887 0.4756 1.0790 0.0018  -0.1052 -0.1246 105 TYR A OH    
796  N  N     . ILE A 108 ? 0.3422 0.3129 0.6112 0.0536  -0.1536 -0.0364 106 ILE A N     
797  C  CA    . ILE A 108 ? 0.3882 0.3329 0.6066 0.0408  -0.1201 0.0016  106 ILE A CA    
798  C  C     . ILE A 108 ? 0.3643 0.3133 0.5891 0.0324  -0.1251 -0.0257 106 ILE A C     
799  O  O     . ILE A 108 ? 0.3824 0.3123 0.5933 0.0188  -0.0937 0.0386  106 ILE A O     
800  C  CB    . ILE A 108 ? 0.3826 0.3804 0.6349 0.0291  -0.1209 0.0124  106 ILE A CB    
801  C  CG1   . ILE A 108 ? 0.4555 0.5053 0.6834 0.0094  -0.1099 0.0062  106 ILE A CG1   
802  C  CG2   . ILE A 108 ? 0.3914 0.3740 0.5689 0.0419  -0.1371 0.0378  106 ILE A CG2   
803  C  CD1   . ILE A 108 ? 0.5253 0.5498 0.7193 -0.0105 -0.0920 0.0462  106 ILE A CD1   
804  N  N     . VAL A 109 ? 0.3798 0.3313 0.5533 0.0574  -0.1225 -0.0066 107 VAL A N     
805  C  CA    . VAL A 109 ? 0.3404 0.3403 0.5226 0.0524  -0.1137 -0.0254 107 VAL A CA    
806  C  C     . VAL A 109 ? 0.3499 0.3560 0.5123 0.0556  -0.1329 -0.0261 107 VAL A C     
807  O  O     . VAL A 109 ? 0.3596 0.2567 0.5032 0.0338  -0.1296 -0.0260 107 VAL A O     
808  C  CB    . VAL A 109 ? 0.2813 0.3278 0.5233 0.0503  -0.1268 -0.0338 107 VAL A CB    
809  C  CG1   . VAL A 109 ? 0.2483 0.3089 0.5405 0.0589  -0.1133 -0.0258 107 VAL A CG1   
810  C  CG2   . VAL A 109 ? 0.3104 0.2797 0.5545 0.0346  -0.1398 -0.0433 107 VAL A CG2   
811  N  N     . MET A 110 ? 0.3516 0.3311 0.4841 0.0632  -0.1164 0.0214  108 MET A N     
812  C  CA    . MET A 110 ? 0.3297 0.3651 0.4718 0.0883  -0.1157 0.0266  108 MET A CA    
813  C  C     . MET A 110 ? 0.3101 0.3875 0.4546 0.0742  -0.1064 0.0177  108 MET A C     
814  O  O     . MET A 110 ? 0.3249 0.3523 0.4568 0.0790  -0.0896 0.0097  108 MET A O     
815  C  CB    . MET A 110 ? 0.3702 0.3982 0.4797 0.1044  -0.1066 0.0472  108 MET A CB    
816  C  CG    . MET A 110 ? 0.3694 0.3878 0.4895 0.0973  -0.1114 0.0319  108 MET A CG    
817  S  SD    . MET A 110 ? 0.3943 0.3536 0.5317 0.0792  -0.0546 0.0321  108 MET A SD    
818  C  CE    . MET A 110 ? 0.3382 0.3937 0.6190 0.0564  -0.0916 0.0344  108 MET A CE    
819  N  N     . GLU A 111 ? 0.3772 0.3881 0.4203 0.0487  -0.0948 0.0172  109 GLU A N     
820  C  CA    . GLU A 111 ? 0.4368 0.4544 0.4967 0.0544  -0.0746 0.0368  109 GLU A CA    
821  C  C     . GLU A 111 ? 0.3716 0.4201 0.4322 0.0769  -0.0557 0.0151  109 GLU A C     
822  O  O     . GLU A 111 ? 0.3811 0.4326 0.4244 0.0848  -0.0800 0.0161  109 GLU A O     
823  C  CB    . GLU A 111 ? 0.4983 0.4730 0.5190 -0.0378 -0.0616 0.0603  109 GLU A CB    
824  C  CG    . GLU A 111 ? 0.5859 0.5923 0.6728 -0.0213 -0.0483 0.0556  109 GLU A CG    
825  C  CD    . GLU A 111 ? 0.6103 0.6304 0.8409 -0.0755 -0.0533 0.0028  109 GLU A CD    
826  O  OE1   . GLU A 111 ? 0.4949 0.6365 0.9023 -0.0667 -0.0421 0.0740  109 GLU A OE1   
827  O  OE2   . GLU A 111 ? 0.6949 0.5813 0.8365 -0.0070 -0.0356 -0.0475 109 GLU A OE2   
828  N  N     . LEU A 112 ? 0.3811 0.3733 0.4642 0.1168  -0.0938 -0.0018 110 LEU A N     
829  C  CA    . LEU A 112 ? 0.3760 0.3551 0.4706 0.0929  -0.0099 -0.0251 110 LEU A CA    
830  C  C     . LEU A 112 ? 0.4204 0.4193 0.4153 0.1105  -0.0157 -0.0473 110 LEU A C     
831  O  O     . LEU A 112 ? 0.4111 0.3882 0.4550 0.0810  -0.0308 -0.0703 110 LEU A O     
832  C  CB    . LEU A 112 ? 0.3686 0.3932 0.5098 0.0996  -0.0234 0.0096  110 LEU A CB    
833  C  CG    . LEU A 112 ? 0.3887 0.4794 0.5114 0.1027  -0.0044 0.0009  110 LEU A CG    
834  C  CD1   . LEU A 112 ? 0.4288 0.4959 0.5017 0.0756  0.0087  0.0250  110 LEU A CD1   
835  C  CD2   . LEU A 112 ? 0.4168 0.5156 0.5262 0.0967  -0.0278 -0.0056 110 LEU A CD2   
836  N  N     . MET A 113 ? 0.4230 0.4354 0.4365 0.0941  -0.0075 -0.0260 111 MET A N     
837  C  CA    . MET A 113 ? 0.3964 0.4806 0.3951 0.0746  0.0084  -0.0059 111 MET A CA    
838  C  C     . MET A 113 ? 0.3811 0.5285 0.4163 0.0649  0.0301  -0.0351 111 MET A C     
839  O  O     . MET A 113 ? 0.3822 0.5567 0.4453 0.0313  0.0127  0.0117  111 MET A O     
840  C  CB    . MET A 113 ? 0.3836 0.4722 0.3529 0.0754  0.0137  -0.0137 111 MET A CB    
841  C  CG    . MET A 113 ? 0.4724 0.4884 0.4152 0.0638  0.0085  -0.0328 111 MET A CG    
842  S  SD    . MET A 113 ? 0.5038 0.6320 0.4465 0.0495  0.0095  0.0350  111 MET A SD    
843  C  CE    . MET A 113 ? 0.4902 0.6425 0.4229 -0.0005 0.0250  0.0217  111 MET A CE    
844  N  N     . ASP A 114 ? 0.4267 0.5143 0.4127 0.0579  0.0615  -0.0218 112 ASP A N     
845  C  CA    . ASP A 114 ? 0.4449 0.5226 0.3912 0.0804  0.0627  -0.0004 112 ASP A CA    
846  C  C     . ASP A 114 ? 0.4337 0.5664 0.3512 0.0975  0.0639  -0.0010 112 ASP A C     
847  O  O     . ASP A 114 ? 0.4010 0.5898 0.3471 0.0367  0.0704  0.0326  112 ASP A O     
848  C  CB    . ASP A 114 ? 0.4588 0.5511 0.4738 0.1058  0.0815  -0.0004 112 ASP A CB    
849  C  CG    . ASP A 114 ? 0.4680 0.5997 0.5861 0.1242  0.0603  0.0148  112 ASP A CG    
850  O  OD1   . ASP A 114 ? 0.4714 0.6692 0.5901 0.1335  0.0969  -0.0027 112 ASP A OD1   
851  O  OD2   . ASP A 114 ? 0.4681 0.5432 0.5846 0.1481  0.0681  -0.0085 112 ASP A OD2   
852  N  N     . ALA A 115 ? 0.3583 0.5657 0.3082 0.0730  0.0688  0.0146  113 ALA A N     
853  C  CA    . ALA A 115 ? 0.3692 0.5666 0.3396 0.0443  0.0611  0.0215  113 ALA A CA    
854  C  C     . ALA A 115 ? 0.3490 0.5481 0.3472 0.0163  0.0528  0.0305  113 ALA A C     
855  O  O     . ALA A 115 ? 0.3710 0.5200 0.3636 0.0156  0.0861  0.0419  113 ALA A O     
856  C  CB    . ALA A 115 ? 0.3486 0.5591 0.3269 0.0533  0.0582  0.0412  113 ALA A CB    
857  N  N     . ASN A 116 ? 0.3020 0.5489 0.3076 0.0041  0.0556  0.0542  114 ASN A N     
858  C  CA    . ASN A 116 ? 0.3498 0.5261 0.3676 0.0123  0.0459  0.0477  114 ASN A CA    
859  C  C     . ASN A 116 ? 0.3947 0.5086 0.3466 0.0275  0.0400  0.0604  114 ASN A C     
860  O  O     . ASN A 116 ? 0.3873 0.5044 0.3198 0.0515  0.0370  0.0587  114 ASN A O     
861  C  CB    . ASN A 116 ? 0.3331 0.5451 0.3711 0.0054  0.0694  0.0461  114 ASN A CB    
862  C  CG    . ASN A 116 ? 0.3860 0.6010 0.4379 -0.0229 0.0488  0.1000  114 ASN A CG    
863  O  OD1   . ASN A 116 ? 0.3216 0.6170 0.4513 -0.0212 0.0421  0.1139  114 ASN A OD1   
864  N  ND2   . ASN A 116 ? 0.4278 0.6684 0.4908 -0.0715 0.0080  0.1236  114 ASN A ND2   
865  N  N     . LEU A 117 ? 0.3645 0.4863 0.3673 -0.0118 0.0661  0.0524  115 LEU A N     
866  C  CA    . LEU A 117 ? 0.3681 0.4865 0.3308 0.0097  0.0565  0.0461  115 LEU A CA    
867  C  C     . LEU A 117 ? 0.3814 0.4869 0.3456 0.0282  0.0630  0.0608  115 LEU A C     
868  O  O     . LEU A 117 ? 0.3630 0.5599 0.3869 0.0110  0.0757  0.0789  115 LEU A O     
869  C  CB    . LEU A 117 ? 0.3630 0.4093 0.3058 0.0069  0.0336  0.0274  115 LEU A CB    
870  C  CG    . LEU A 117 ? 0.3417 0.4225 0.2941 -0.0030 0.0336  0.0335  115 LEU A CG    
871  C  CD1   . LEU A 117 ? 0.3398 0.4420 0.2987 0.0134  0.0339  0.0333  115 LEU A CD1   
872  C  CD2   . LEU A 117 ? 0.3207 0.3978 0.3070 -0.0074 0.0171  0.0236  115 LEU A CD2   
873  N  N     . CYS A 118 ? 0.3743 0.5730 0.3405 0.0135  0.0726  0.0644  116 CYS A N     
874  C  CA    . CYS A 118 ? 0.4521 0.5961 0.3559 0.0169  0.0758  0.0732  116 CYS A CA    
875  C  C     . CYS A 118 ? 0.4176 0.5758 0.3411 0.0460  0.0962  0.0692  116 CYS A C     
876  O  O     . CYS A 118 ? 0.4094 0.5719 0.3320 0.1030  0.0899  0.1044  116 CYS A O     
877  C  CB    . CYS A 118 ? 0.4607 0.5778 0.4044 0.0201  0.0894  0.0541  116 CYS A CB    
878  S  SG    . CYS A 118 ? 0.4591 0.5617 0.3914 0.0407  0.0941  0.0930  116 CYS A SG    
879  N  N     . GLN A 119 ? 0.4162 0.6112 0.3231 0.0500  0.0805  0.0945  117 GLN A N     
880  C  CA    . GLN A 119 ? 0.4468 0.6450 0.3637 0.0711  0.0819  0.0657  117 GLN A CA    
881  C  C     . GLN A 119 ? 0.4968 0.6624 0.3478 0.0577  0.0779  0.0434  117 GLN A C     
882  O  O     . GLN A 119 ? 0.5992 0.6650 0.3460 0.0430  0.1231  0.0564  117 GLN A O     
883  C  CB    . GLN A 119 ? 0.4482 0.6880 0.4271 0.1060  0.0783  0.0356  117 GLN A CB    
884  C  CG    . GLN A 119 ? 0.4379 0.7298 0.4487 0.1118  0.0680  0.0565  117 GLN A CG    
885  C  CD    . GLN A 119 ? 0.4911 0.7968 0.4278 0.1314  0.0625  0.0486  117 GLN A CD    
886  O  OE1   . GLN A 119 ? 0.4398 0.7766 0.3944 0.0868  0.0626  0.0746  117 GLN A OE1   
887  N  NE2   . GLN A 119 ? 0.5383 0.8093 0.5083 0.1664  0.0598  0.0799  117 GLN A NE2   
888  N  N     . VAL A 120 ? 0.4640 0.5840 0.3504 0.0623  0.0653  0.0692  118 VAL A N     
889  C  CA    . VAL A 120 ? 0.4866 0.6024 0.3657 0.0446  0.0549  0.0408  118 VAL A CA    
890  C  C     . VAL A 120 ? 0.5266 0.6116 0.3248 0.0232  0.0463  0.0604  118 VAL A C     
891  O  O     . VAL A 120 ? 0.6150 0.6855 0.3232 -0.0364 0.0689  -0.0023 118 VAL A O     
892  C  CB    . VAL A 120 ? 0.4711 0.5406 0.3589 0.0184  0.0191  0.0606  118 VAL A CB    
893  C  CG1   . VAL A 120 ? 0.5189 0.5318 0.4283 -0.0057 -0.0003 0.0555  118 VAL A CG1   
894  C  CG2   . VAL A 120 ? 0.4655 0.5044 0.3879 0.0200  0.0463  0.0688  118 VAL A CG2   
895  N  N     . ILE A 121 ? 0.5490 0.6559 0.4051 0.0226  0.0644  0.0913  119 ILE A N     
896  C  CA    . ILE A 121 ? 0.5024 0.6197 0.4031 0.0452  0.0328  0.0506  119 ILE A CA    
897  C  C     . ILE A 121 ? 0.5401 0.5914 0.4046 0.0552  0.0462  0.0421  119 ILE A C     
898  O  O     . ILE A 121 ? 0.5819 0.5679 0.4252 0.0697  0.0775  0.0492  119 ILE A O     
899  C  CB    . ILE A 121 ? 0.4830 0.5995 0.3817 0.0038  0.0025  0.0549  119 ILE A CB    
900  C  CG1   . ILE A 121 ? 0.4268 0.5934 0.3989 0.0176  0.0076  0.0291  119 ILE A CG1   
901  C  CG2   . ILE A 121 ? 0.5207 0.6256 0.5123 -0.0171 -0.0404 0.0465  119 ILE A CG2   
902  C  CD1   . ILE A 121 ? 0.4617 0.6221 0.4257 0.0145  0.0211  0.0704  119 ILE A CD1   
903  N  N     . GLN A 122 ? 0.5526 0.6068 0.3721 0.0314  0.0805  0.0446  120 GLN A N     
904  C  CA    . GLN A 122 ? 0.6036 0.7023 0.4033 0.0272  0.0927  0.0415  120 GLN A CA    
905  C  C     . GLN A 122 ? 0.7295 0.6787 0.4071 0.1154  0.1307  0.0018  120 GLN A C     
906  O  O     . GLN A 122 ? 0.8471 0.6401 0.4033 0.0796  0.1472  -0.0411 120 GLN A O     
907  C  CB    . GLN A 122 ? 0.6207 0.7572 0.4162 0.0343  0.1374  0.0577  120 GLN A CB    
908  C  CG    . GLN A 122 ? 0.6560 0.8404 0.4999 -0.0324 0.1602  0.0443  120 GLN A CG    
909  C  CD    . GLN A 122 ? 0.7087 0.9113 0.7322 -0.0392 0.1347  0.0100  120 GLN A CD    
910  O  OE1   . GLN A 122 ? 0.6342 1.0141 0.8094 -0.0785 0.2017  -0.0835 120 GLN A OE1   
911  N  NE2   . GLN A 122 ? 0.7743 0.9385 0.9473 -0.0671 0.1340  0.0200  120 GLN A NE2   
912  N  N     . MET A 123 ? 0.7408 0.6568 0.4489 0.1255  0.1854  -0.0123 121 MET A N     
913  C  CA    . MET A 123 ? 0.7569 0.7644 0.4287 0.0859  0.1084  -0.0089 121 MET A CA    
914  C  C     . MET A 123 ? 0.7680 0.7083 0.3917 0.1372  0.1262  -0.0813 121 MET A C     
915  O  O     . MET A 123 ? 0.7469 0.6190 0.3746 0.1195  0.1445  -0.1006 121 MET A O     
916  C  CB    . MET A 123 ? 0.7792 0.7458 0.5763 0.1222  0.0659  0.0307  121 MET A CB    
917  C  CG    . MET A 123 ? 0.8494 0.7927 0.5234 0.0844  0.0478  -0.0102 121 MET A CG    
918  S  SD    . MET A 123 ? 0.8898 0.7392 0.6250 0.1188  0.0344  0.0191  121 MET A SD    
919  C  CE    . MET A 123 ? 0.6758 0.6226 0.3255 0.0872  0.0456  -0.0273 121 MET A CE    
920  N  N     . GLU A 124 ? 0.8277 0.7765 0.4542 0.1443  0.1840  -0.1685 122 GLU A N     
921  C  CA    . GLU A 124 ? 0.8240 0.7097 0.5567 0.1571  0.1404  -0.1564 122 GLU A CA    
922  C  C     . GLU A 124 ? 0.8145 0.6965 0.6281 0.1047  0.0898  -0.1203 122 GLU A C     
923  O  O     . GLU A 124 ? 0.8205 0.7251 0.9563 0.0741  0.0491  -0.1099 122 GLU A O     
924  C  CB    . GLU A 124 ? 0.8437 0.7748 0.5471 0.1187  0.1013  -0.1502 122 GLU A CB    
925  N  N     . LEU A 125 ? 0.7454 0.6545 0.4551 0.0952  0.0884  -0.0671 123 LEU A N     
926  C  CA    . LEU A 125 ? 0.6852 0.7176 0.4949 0.0850  0.0138  -0.0411 123 LEU A CA    
927  C  C     . LEU A 125 ? 0.6579 0.7179 0.4291 0.0840  -0.0445 -0.0641 123 LEU A C     
928  O  O     . LEU A 125 ? 0.6401 0.7556 0.3030 0.0921  -0.0810 -0.0494 123 LEU A O     
929  C  CB    . LEU A 125 ? 0.6606 0.8046 0.3443 0.0713  0.0241  0.0214  123 LEU A CB    
930  C  CG    . LEU A 125 ? 0.6608 0.8269 0.4824 0.0706  0.0388  0.0435  123 LEU A CG    
931  C  CD1   . LEU A 125 ? 0.6511 0.9169 0.3916 0.0582  0.0352  0.0529  123 LEU A CD1   
932  C  CD2   . LEU A 125 ? 0.6505 0.8323 0.5007 0.0985  0.0181  0.1407  123 LEU A CD2   
933  N  N     . ASP A 126 ? 0.5568 0.7218 0.3697 0.0563  -0.0927 -0.0938 124 ASP A N     
934  C  CA    . ASP A 126 ? 0.6118 0.6733 0.4046 0.0344  -0.1172 -0.1139 124 ASP A CA    
935  C  C     . ASP A 126 ? 0.5198 0.5742 0.3720 0.0189  -0.1294 -0.1055 124 ASP A C     
936  O  O     . ASP A 126 ? 0.5184 0.5392 0.3646 0.0096  -0.1123 -0.0842 124 ASP A O     
937  C  CB    . ASP A 126 ? 0.6398 0.6371 0.3927 0.0485  -0.1081 -0.1473 124 ASP A CB    
938  C  CG    . ASP A 126 ? 0.5987 0.6376 0.4157 0.0663  -0.1628 -0.1755 124 ASP A CG    
939  O  OD1   . ASP A 126 ? 0.6361 0.6720 0.3976 0.0723  -0.1449 -0.1741 124 ASP A OD1   
940  O  OD2   . ASP A 126 ? 0.6952 0.7081 0.4039 0.0719  -0.0847 -0.1891 124 ASP A OD2   
941  N  N     . HIS A 127 ? 0.5076 0.5288 0.3230 0.0596  -0.2220 -0.1189 125 HIS A N     
942  C  CA    . HIS A 127 ? 0.4584 0.4571 0.3431 0.0760  -0.1603 -0.0955 125 HIS A CA    
943  C  C     . HIS A 127 ? 0.3785 0.4214 0.3372 0.0260  -0.1192 -0.0891 125 HIS A C     
944  O  O     . HIS A 127 ? 0.3577 0.3937 0.3231 0.0237  -0.1175 -0.0614 125 HIS A O     
945  C  CB    . HIS A 127 ? 0.4879 0.4917 0.3876 0.0638  -0.1805 -0.1275 125 HIS A CB    
946  C  CG    . HIS A 127 ? 0.5255 0.5468 0.4011 0.0833  -0.1931 -0.1004 125 HIS A CG    
947  N  ND1   . HIS A 127 ? 0.5055 0.5265 0.4413 0.0575  -0.2400 -0.0774 125 HIS A ND1   
948  C  CD2   . HIS A 127 ? 0.5740 0.5631 0.3731 0.0939  -0.1394 -0.1211 125 HIS A CD2   
949  C  CE1   . HIS A 127 ? 0.5767 0.5231 0.4236 0.0844  -0.1801 -0.0652 125 HIS A CE1   
950  N  NE2   . HIS A 127 ? 0.5436 0.5853 0.4101 0.1004  -0.2117 -0.1190 125 HIS A NE2   
951  N  N     . GLU A 128 ? 0.3882 0.4274 0.3814 0.0081  -0.1084 -0.0856 126 GLU A N     
952  C  CA    . GLU A 128 ? 0.4021 0.4135 0.3717 0.0230  -0.1148 -0.1032 126 GLU A CA    
953  C  C     . GLU A 128 ? 0.4075 0.3754 0.3357 0.0137  -0.0950 -0.0960 126 GLU A C     
954  O  O     . GLU A 128 ? 0.4090 0.3691 0.3330 0.0090  -0.0650 -0.0554 126 GLU A O     
955  C  CB    . GLU A 128 ? 0.4432 0.4081 0.4006 0.0398  -0.1235 -0.1519 126 GLU A CB    
956  C  CG    . GLU A 128 ? 0.4921 0.4582 0.4469 0.0471  -0.1558 -0.1556 126 GLU A CG    
957  C  CD    . GLU A 128 ? 0.5978 0.5789 0.4727 0.0811  -0.1723 -0.1432 126 GLU A CD    
958  O  OE1   . GLU A 128 ? 0.6245 0.6116 0.4096 0.1231  -0.1791 -0.1749 126 GLU A OE1   
959  O  OE2   . GLU A 128 ? 0.5600 0.6638 0.6263 0.0874  -0.1852 -0.1039 126 GLU A OE2   
960  N  N     . ARG A 129 ? 0.4088 0.4582 0.2921 0.0371  -0.0858 -0.0801 127 ARG A N     
961  C  CA    . ARG A 129 ? 0.4130 0.4540 0.2908 0.0317  -0.0574 -0.0676 127 ARG A CA    
962  C  C     . ARG A 129 ? 0.3659 0.4523 0.2674 0.0458  -0.0433 -0.0444 127 ARG A C     
963  O  O     . ARG A 129 ? 0.3416 0.3668 0.2556 0.0467  -0.0497 -0.0368 127 ARG A O     
964  C  CB    . ARG A 129 ? 0.4596 0.5149 0.3488 0.0576  -0.0390 -0.0593 127 ARG A CB    
965  C  CG    . ARG A 129 ? 0.4988 0.5317 0.4133 0.0773  -0.0480 -0.0871 127 ARG A CG    
966  C  CD    . ARG A 129 ? 0.6018 0.5915 0.4199 0.0956  -0.0661 -0.0938 127 ARG A CD    
967  N  NE    . ARG A 129 ? 0.6250 0.5923 0.4750 0.1259  -0.0742 -0.1189 127 ARG A NE    
968  C  CZ    . ARG A 129 ? 0.6653 0.6233 0.5214 0.1177  -0.0833 -0.1612 127 ARG A CZ    
969  N  NH1   . ARG A 129 ? 0.7044 0.6468 0.4597 0.1264  -0.0420 -0.1995 127 ARG A NH1   
970  N  NH2   . ARG A 129 ? 0.6985 0.6507 0.5170 0.1556  -0.0573 -0.2016 127 ARG A NH2   
971  N  N     . MET A 130 ? 0.3918 0.4131 0.2389 0.0260  -0.0514 -0.0345 128 MET A N     
972  C  CA    . MET A 130 ? 0.3716 0.4149 0.2446 0.0209  -0.0583 -0.0218 128 MET A CA    
973  C  C     . MET A 130 ? 0.3342 0.3356 0.2388 0.0081  -0.0646 -0.0323 128 MET A C     
974  O  O     . MET A 130 ? 0.3110 0.3307 0.2310 0.0007  -0.0521 -0.0010 128 MET A O     
975  C  CB    . MET A 130 ? 0.3965 0.4706 0.3085 0.0336  -0.0728 0.0000  128 MET A CB    
976  C  CG    . MET A 130 ? 0.4342 0.5241 0.3455 0.0240  -0.0734 0.0189  128 MET A CG    
977  S  SD    . MET A 130 ? 0.5144 0.6424 0.3777 0.0240  -0.1045 0.0568  128 MET A SD    
978  C  CE    . MET A 130 ? 0.5537 0.6533 0.4768 0.0261  -0.1707 0.0809  128 MET A CE    
979  N  N     . SER A 131 ? 0.3357 0.3430 0.2447 0.0116  -0.0684 -0.0349 129 SER A N     
980  C  CA    . SER A 131 ? 0.3097 0.3042 0.2612 0.0079  -0.0709 -0.0440 129 SER A CA    
981  C  C     . SER A 131 ? 0.3363 0.3194 0.2352 0.0013  -0.0492 -0.0333 129 SER A C     
982  O  O     . SER A 131 ? 0.2814 0.2541 0.2287 -0.0265 -0.0459 -0.0210 129 SER A O     
983  C  CB    . SER A 131 ? 0.3316 0.3349 0.2806 0.0065  -0.0703 -0.0607 129 SER A CB    
984  O  OG    . SER A 131 ? 0.3662 0.3002 0.3160 -0.0169 -0.0874 -0.0515 129 SER A OG    
985  N  N     . TYR A 132 ? 0.3554 0.2877 0.2565 0.0061  -0.0766 -0.0181 130 TYR A N     
986  C  CA    . TYR A 132 ? 0.3363 0.2916 0.2774 -0.0089 -0.0439 -0.0274 130 TYR A CA    
987  C  C     . TYR A 132 ? 0.3262 0.3147 0.2550 -0.0137 -0.0282 -0.0252 130 TYR A C     
988  O  O     . TYR A 132 ? 0.3261 0.2701 0.2666 -0.0134 -0.0335 -0.0024 130 TYR A O     
989  C  CB    . TYR A 132 ? 0.3476 0.2885 0.3094 -0.0058 -0.0425 -0.0278 130 TYR A CB    
990  C  CG    . TYR A 132 ? 0.3833 0.2858 0.3258 -0.0058 -0.0415 -0.0212 130 TYR A CG    
991  C  CD1   . TYR A 132 ? 0.4164 0.2967 0.3579 0.0011  -0.0413 -0.0016 130 TYR A CD1   
992  C  CD2   . TYR A 132 ? 0.3804 0.2836 0.3045 -0.0004 -0.0412 -0.0280 130 TYR A CD2   
993  C  CE1   . TYR A 132 ? 0.4150 0.3173 0.3635 -0.0274 -0.0540 0.0032  130 TYR A CE1   
994  C  CE2   . TYR A 132 ? 0.4266 0.3339 0.3097 0.0055  -0.0670 -0.0114 130 TYR A CE2   
995  C  CZ    . TYR A 132 ? 0.4201 0.3564 0.3797 -0.0259 -0.0528 0.0232  130 TYR A CZ    
996  O  OH    . TYR A 132 ? 0.4878 0.3714 0.3741 -0.0420 -0.0815 0.0637  130 TYR A OH    
997  N  N     . LEU A 133 ? 0.3287 0.3077 0.2385 -0.0049 -0.0387 -0.0170 131 LEU A N     
998  C  CA    . LEU A 133 ? 0.3166 0.3134 0.2343 -0.0036 -0.0269 -0.0025 131 LEU A CA    
999  C  C     . LEU A 133 ? 0.3089 0.2919 0.2432 -0.0135 -0.0298 0.0031  131 LEU A C     
1000 O  O     . LEU A 133 ? 0.2967 0.2992 0.2338 -0.0312 -0.0161 0.0054  131 LEU A O     
1001 C  CB    . LEU A 133 ? 0.2967 0.3228 0.2269 -0.0028 -0.0283 -0.0004 131 LEU A CB    
1002 C  CG    . LEU A 133 ? 0.3385 0.3605 0.2638 0.0103  -0.0084 -0.0095 131 LEU A CG    
1003 C  CD1   . LEU A 133 ? 0.4188 0.4055 0.3048 0.0080  0.0168  -0.0322 131 LEU A CD1   
1004 C  CD2   . LEU A 133 ? 0.3022 0.3638 0.2682 0.0530  0.0155  0.0077  131 LEU A CD2   
1005 N  N     . LEU A 134 ? 0.3196 0.3063 0.2776 -0.0387 -0.0465 -0.0115 132 LEU A N     
1006 C  CA    . LEU A 134 ? 0.3177 0.3051 0.2789 -0.0306 -0.0201 0.0100  132 LEU A CA    
1007 C  C     . LEU A 134 ? 0.3272 0.2917 0.2700 -0.0366 -0.0234 0.0041  132 LEU A C     
1008 O  O     . LEU A 134 ? 0.2743 0.2461 0.2353 -0.0220 -0.0364 0.0355  132 LEU A O     
1009 C  CB    . LEU A 134 ? 0.3158 0.3062 0.2932 -0.0299 -0.0268 -0.0019 132 LEU A CB    
1010 C  CG    . LEU A 134 ? 0.3481 0.3552 0.3008 -0.0036 -0.0398 0.0025  132 LEU A CG    
1011 C  CD1   . LEU A 134 ? 0.3399 0.3938 0.3229 -0.0122 -0.0584 -0.0252 132 LEU A CD1   
1012 C  CD2   . LEU A 134 ? 0.3269 0.3731 0.3097 -0.0207 -0.0368 0.0028  132 LEU A CD2   
1013 N  N     . TYR A 135 ? 0.2758 0.2647 0.2568 -0.0258 -0.0262 0.0092  133 TYR A N     
1014 C  CA    . TYR A 135 ? 0.2616 0.2306 0.2671 -0.0409 -0.0248 0.0065  133 TYR A CA    
1015 C  C     . TYR A 135 ? 0.2980 0.2260 0.2649 -0.0405 -0.0201 0.0230  133 TYR A C     
1016 O  O     . TYR A 135 ? 0.3079 0.2641 0.2827 -0.0336 -0.0089 0.0268  133 TYR A O     
1017 C  CB    . TYR A 135 ? 0.2759 0.2223 0.2900 -0.0312 -0.0196 -0.0105 133 TYR A CB    
1018 C  CG    . TYR A 135 ? 0.2940 0.2330 0.2832 -0.0551 -0.0145 -0.0006 133 TYR A CG    
1019 C  CD1   . TYR A 135 ? 0.3258 0.2341 0.3094 -0.0517 -0.0047 -0.0076 133 TYR A CD1   
1020 C  CD2   . TYR A 135 ? 0.3093 0.2356 0.3114 -0.0557 -0.0042 0.0128  133 TYR A CD2   
1021 C  CE1   . TYR A 135 ? 0.3251 0.2532 0.3165 -0.0451 0.0118  0.0096  133 TYR A CE1   
1022 C  CE2   . TYR A 135 ? 0.3115 0.2574 0.3076 -0.0594 -0.0175 0.0236  133 TYR A CE2   
1023 C  CZ    . TYR A 135 ? 0.3524 0.2379 0.3175 -0.0581 -0.0124 0.0087  133 TYR A CZ    
1024 O  OH    . TYR A 135 ? 0.4119 0.2731 0.3395 -0.0790 0.0164  0.0191  133 TYR A OH    
1025 N  N     . GLN A 136 ? 0.3037 0.2408 0.2719 -0.0390 -0.0269 0.0231  134 GLN A N     
1026 C  CA    . GLN A 136 ? 0.3076 0.2555 0.2435 -0.0357 -0.0131 0.0205  134 GLN A CA    
1027 C  C     . GLN A 136 ? 0.2872 0.2458 0.2213 -0.0263 -0.0013 0.0144  134 GLN A C     
1028 O  O     . GLN A 136 ? 0.2541 0.2511 0.2434 -0.0315 -0.0142 0.0074  134 GLN A O     
1029 C  CB    . GLN A 136 ? 0.3321 0.2698 0.2703 -0.0305 -0.0190 0.0077  134 GLN A CB    
1030 C  CG    . GLN A 136 ? 0.3054 0.2626 0.2619 -0.0269 -0.0354 0.0135  134 GLN A CG    
1031 C  CD    . GLN A 136 ? 0.3537 0.3034 0.2786 -0.0012 -0.0238 -0.0043 134 GLN A CD    
1032 O  OE1   . GLN A 136 ? 0.3539 0.2898 0.2662 0.0041  -0.0292 0.0152  134 GLN A OE1   
1033 N  NE2   . GLN A 136 ? 0.3269 0.2782 0.2670 -0.0164 -0.0503 -0.0080 134 GLN A NE2   
1034 N  N     . MET A 137 ? 0.2963 0.2354 0.2039 -0.0309 -0.0185 0.0028  135 MET A N     
1035 C  CA    . MET A 137 ? 0.3091 0.2658 0.2552 -0.0271 -0.0193 0.0170  135 MET A CA    
1036 C  C     . MET A 137 ? 0.2889 0.2606 0.2511 -0.0389 -0.0062 0.0272  135 MET A C     
1037 O  O     . MET A 137 ? 0.2682 0.2590 0.2289 -0.0264 -0.0263 0.0278  135 MET A O     
1038 C  CB    . MET A 137 ? 0.2950 0.2749 0.2351 -0.0174 -0.0060 0.0303  135 MET A CB    
1039 C  CG    . MET A 137 ? 0.3180 0.3285 0.3024 -0.0091 0.0025  0.0439  135 MET A CG    
1040 S  SD    . MET A 137 ? 0.3756 0.4059 0.3378 0.0048  -0.0154 0.0473  135 MET A SD    
1041 C  CE    . MET A 137 ? 0.3789 0.3848 0.4163 0.0129  -0.0175 0.0628  135 MET A CE    
1042 N  N     . LEU A 138 ? 0.2949 0.2776 0.2491 -0.0405 -0.0100 0.0244  136 LEU A N     
1043 C  CA    . LEU A 138 ? 0.2814 0.2569 0.2604 -0.0436 -0.0043 0.0247  136 LEU A CA    
1044 C  C     . LEU A 138 ? 0.2851 0.2513 0.2509 -0.0465 0.0045  0.0258  136 LEU A C     
1045 O  O     . LEU A 138 ? 0.2987 0.2465 0.2791 -0.0309 0.0166  0.0167  136 LEU A O     
1046 C  CB    . LEU A 138 ? 0.2672 0.2631 0.2625 -0.0437 -0.0019 0.0287  136 LEU A CB    
1047 C  CG    . LEU A 138 ? 0.2532 0.2790 0.2901 -0.0442 -0.0081 0.0221  136 LEU A CG    
1048 C  CD1   . LEU A 138 ? 0.2401 0.2520 0.2829 -0.0216 -0.0122 0.0007  136 LEU A CD1   
1049 C  CD2   . LEU A 138 ? 0.2110 0.2483 0.2858 -0.0396 -0.0086 0.0242  136 LEU A CD2   
1050 N  N     . CYS A 139 ? 0.2870 0.2295 0.2446 -0.0413 0.0105  0.0293  137 CYS A N     
1051 C  CA    . CYS A 139 ? 0.2868 0.2597 0.2383 -0.0397 0.0040  0.0233  137 CYS A CA    
1052 C  C     . CYS A 139 ? 0.3156 0.2610 0.2592 -0.0441 0.0052  0.0234  137 CYS A C     
1053 O  O     . CYS A 139 ? 0.3068 0.2256 0.2474 -0.0359 0.0219  0.0482  137 CYS A O     
1054 C  CB    . CYS A 139 ? 0.2942 0.2561 0.2412 -0.0330 0.0023  0.0155  137 CYS A CB    
1055 S  SG    . CYS A 139 ? 0.3480 0.2789 0.2945 -0.0564 0.0127  0.0145  137 CYS A SG    
1056 N  N     . GLY A 140 ? 0.3157 0.2236 0.2379 -0.0476 -0.0129 0.0363  138 GLY A N     
1057 C  CA    . GLY A 140 ? 0.3226 0.2545 0.2719 -0.0323 -0.0026 0.0390  138 GLY A CA    
1058 C  C     . GLY A 140 ? 0.3067 0.2629 0.2395 -0.0266 -0.0074 0.0299  138 GLY A C     
1059 O  O     . GLY A 140 ? 0.2999 0.2689 0.2403 -0.0054 -0.0133 0.0175  138 GLY A O     
1060 N  N     . ILE A 141 ? 0.2917 0.2346 0.2205 -0.0417 -0.0031 0.0330  139 ILE A N     
1061 C  CA    . ILE A 141 ? 0.2922 0.2876 0.2536 -0.0176 -0.0037 0.0499  139 ILE A CA    
1062 C  C     . ILE A 141 ? 0.2839 0.2591 0.2350 -0.0094 -0.0001 0.0392  139 ILE A C     
1063 O  O     . ILE A 141 ? 0.2901 0.2622 0.2436 -0.0056 -0.0203 0.0278  139 ILE A O     
1064 C  CB    . ILE A 141 ? 0.2981 0.2684 0.2606 -0.0276 0.0082  0.0572  139 ILE A CB    
1065 C  CG1   . ILE A 141 ? 0.2828 0.2847 0.2594 -0.0193 -0.0097 0.0604  139 ILE A CG1   
1066 C  CG2   . ILE A 141 ? 0.2884 0.2865 0.2940 -0.0340 0.0339  0.0607  139 ILE A CG2   
1067 C  CD1   . ILE A 141 ? 0.3010 0.3177 0.2843 -0.0369 -0.0250 0.0402  139 ILE A CD1   
1068 N  N     . LYS A 142 ? 0.2971 0.2913 0.2372 -0.0143 0.0023  0.0222  140 LYS A N     
1069 C  CA    . LYS A 142 ? 0.3396 0.2898 0.2489 -0.0350 0.0096  0.0658  140 LYS A CA    
1070 C  C     . LYS A 142 ? 0.3469 0.3128 0.2422 -0.0250 0.0159  0.0317  140 LYS A C     
1071 O  O     . LYS A 142 ? 0.3327 0.2767 0.2266 -0.0190 0.0164  0.0568  140 LYS A O     
1072 C  CB    . LYS A 142 ? 0.3501 0.3174 0.2607 -0.0366 0.0057  0.0480  140 LYS A CB    
1073 C  CG    . LYS A 142 ? 0.3658 0.3512 0.2914 -0.0420 0.0411  0.0491  140 LYS A CG    
1074 C  CD    . LYS A 142 ? 0.4338 0.4087 0.3593 -0.0380 0.0807  0.0748  140 LYS A CD    
1075 C  CE    . LYS A 142 ? 0.4926 0.4810 0.3762 -0.0201 0.1227  0.0426  140 LYS A CE    
1076 N  NZ    . LYS A 142 ? 0.5935 0.6893 0.5355 0.0121  0.1604  0.0693  140 LYS A NZ    
1077 N  N     . HIS A 143 ? 0.3500 0.2976 0.2382 -0.0234 0.0142  0.0436  141 HIS A N     
1078 C  CA    . HIS A 143 ? 0.3431 0.2846 0.2073 -0.0196 0.0235  0.0322  141 HIS A CA    
1079 C  C     . HIS A 143 ? 0.3476 0.2681 0.2122 -0.0056 -0.0007 0.0312  141 HIS A C     
1080 O  O     . HIS A 143 ? 0.3500 0.2805 0.2065 -0.0126 0.0034  0.0234  141 HIS A O     
1081 C  CB    . HIS A 143 ? 0.3785 0.2792 0.2303 -0.0143 0.0184  0.0502  141 HIS A CB    
1082 C  CG    . HIS A 143 ? 0.3918 0.2727 0.1959 0.0037  0.0138  0.0392  141 HIS A CG    
1083 N  ND1   . HIS A 143 ? 0.4094 0.3052 0.2389 -0.0049 0.0152  0.0699  141 HIS A ND1   
1084 C  CD2   . HIS A 143 ? 0.3801 0.2698 0.2061 -0.0240 0.0177  0.0254  141 HIS A CD2   
1085 C  CE1   . HIS A 143 ? 0.4402 0.3489 0.2332 -0.0059 0.0267  0.0862  141 HIS A CE1   
1086 N  NE2   . HIS A 143 ? 0.4052 0.2859 0.2439 0.0030  -0.0110 0.0647  141 HIS A NE2   
1087 N  N     . LEU A 144 ? 0.3357 0.2854 0.2118 -0.0313 -0.0077 0.0124  142 LEU A N     
1088 C  CA    . LEU A 144 ? 0.3384 0.3059 0.2609 -0.0163 -0.0247 0.0222  142 LEU A CA    
1089 C  C     . LEU A 144 ? 0.3456 0.2991 0.2434 -0.0264 -0.0231 0.0049  142 LEU A C     
1090 O  O     . LEU A 144 ? 0.3709 0.3317 0.2321 -0.0259 -0.0197 0.0087  142 LEU A O     
1091 C  CB    . LEU A 144 ? 0.3144 0.2726 0.2384 -0.0194 -0.0404 0.0232  142 LEU A CB    
1092 C  CG    . LEU A 144 ? 0.3210 0.2972 0.2364 -0.0113 -0.0300 0.0285  142 LEU A CG    
1093 C  CD1   . LEU A 144 ? 0.3298 0.2829 0.3014 -0.0246 -0.0232 0.0347  142 LEU A CD1   
1094 C  CD2   . LEU A 144 ? 0.3258 0.3411 0.2905 -0.0077 -0.0236 0.0360  142 LEU A CD2   
1095 N  N     . HIS A 145 ? 0.3153 0.2770 0.2154 -0.0185 -0.0166 0.0174  143 HIS A N     
1096 C  CA    . HIS A 145 ? 0.3323 0.2382 0.2422 -0.0296 -0.0073 0.0141  143 HIS A CA    
1097 C  C     . HIS A 145 ? 0.3587 0.2927 0.2315 -0.0107 0.0072  -0.0031 143 HIS A C     
1098 O  O     . HIS A 145 ? 0.3629 0.2975 0.2444 0.0261  0.0404  0.0128  143 HIS A O     
1099 C  CB    . HIS A 145 ? 0.2869 0.2465 0.2529 -0.0175 -0.0125 0.0184  143 HIS A CB    
1100 C  CG    . HIS A 145 ? 0.2828 0.2430 0.2613 -0.0180 -0.0018 0.0080  143 HIS A CG    
1101 N  ND1   . HIS A 145 ? 0.2827 0.2541 0.2733 -0.0259 -0.0013 0.0086  143 HIS A ND1   
1102 C  CD2   . HIS A 145 ? 0.2512 0.2408 0.2531 0.0018  0.0003  0.0069  143 HIS A CD2   
1103 C  CE1   . HIS A 145 ? 0.3203 0.2793 0.2848 -0.0066 -0.0062 0.0062  143 HIS A CE1   
1104 N  NE2   . HIS A 145 ? 0.2941 0.2626 0.2883 -0.0174 -0.0093 0.0162  143 HIS A NE2   
1105 N  N     . SER A 146 ? 0.3755 0.3071 0.2486 -0.0226 0.0189  0.0128  144 SER A N     
1106 C  CA    . SER A 146 ? 0.4231 0.3298 0.2518 -0.0033 0.0315  0.0184  144 SER A CA    
1107 C  C     . SER A 146 ? 0.4586 0.3734 0.2739 -0.0100 0.0212  -0.0099 144 SER A C     
1108 O  O     . SER A 146 ? 0.5265 0.3817 0.2666 -0.0210 0.0506  0.0271  144 SER A O     
1109 C  CB    . SER A 146 ? 0.4099 0.3117 0.2447 -0.0251 0.0433  0.0259  144 SER A CB    
1110 O  OG    . SER A 146 ? 0.4252 0.2959 0.2691 -0.0311 0.0406  0.0705  144 SER A OG    
1111 N  N     . ALA A 147 ? 0.4509 0.3631 0.2446 -0.0278 0.0311  0.0276  145 ALA A N     
1112 C  CA    . ALA A 147 ? 0.4617 0.3658 0.2760 0.0014  0.0051  0.0173  145 ALA A CA    
1113 C  C     . ALA A 147 ? 0.4752 0.3898 0.2836 -0.0109 -0.0206 -0.0022 145 ALA A C     
1114 O  O     . ALA A 147 ? 0.4954 0.4164 0.2535 -0.0009 -0.0404 -0.0051 145 ALA A O     
1115 C  CB    . ALA A 147 ? 0.4804 0.3802 0.3489 -0.0037 -0.0398 0.0352  145 ALA A CB    
1116 N  N     . GLY A 148 ? 0.4381 0.3695 0.2891 0.0143  -0.0201 0.0108  146 GLY A N     
1117 C  CA    . GLY A 148 ? 0.3913 0.3519 0.2541 0.0088  -0.0371 -0.0205 146 GLY A CA    
1118 C  C     . GLY A 148 ? 0.4029 0.3257 0.3111 0.0144  -0.0435 -0.0042 146 GLY A C     
1119 O  O     . GLY A 148 ? 0.4409 0.3305 0.3521 -0.0024 -0.0483 -0.0691 146 GLY A O     
1120 N  N     . ILE A 149 ? 0.3578 0.3081 0.2661 -0.0093 -0.0477 -0.0092 147 ILE A N     
1121 C  CA    . ILE A 149 ? 0.3523 0.3066 0.2713 -0.0144 -0.0671 -0.0035 147 ILE A CA    
1122 C  C     . ILE A 149 ? 0.3255 0.3002 0.2750 -0.0040 -0.0500 0.0068  147 ILE A C     
1123 O  O     . ILE A 149 ? 0.3330 0.3005 0.2890 -0.0179 -0.0447 0.0291  147 ILE A O     
1124 C  CB    . ILE A 149 ? 0.3602 0.3615 0.3037 -0.0209 -0.0810 -0.0203 147 ILE A CB    
1125 C  CG1   . ILE A 149 ? 0.3979 0.3892 0.3256 -0.0277 -0.0680 -0.0314 147 ILE A CG1   
1126 C  CG2   . ILE A 149 ? 0.3516 0.3522 0.2917 -0.0399 -0.1203 -0.0294 147 ILE A CG2   
1127 C  CD1   . ILE A 149 ? 0.3546 0.4387 0.3594 -0.0334 -0.1032 -0.0607 147 ILE A CD1   
1128 N  N     . ILE A 150 ? 0.3046 0.2678 0.2905 -0.0021 -0.0514 -0.0001 148 ILE A N     
1129 C  CA    . ILE A 150 ? 0.3186 0.2918 0.3001 -0.0164 -0.0383 0.0115  148 ILE A CA    
1130 C  C     . ILE A 150 ? 0.3440 0.3090 0.3311 -0.0458 -0.0275 0.0186  148 ILE A C     
1131 O  O     . ILE A 150 ? 0.3383 0.3149 0.3324 -0.0431 -0.0466 0.0145  148 ILE A O     
1132 C  CB    . ILE A 150 ? 0.3068 0.3418 0.3220 -0.0128 -0.0552 0.0460  148 ILE A CB    
1133 C  CG1   . ILE A 150 ? 0.3435 0.3577 0.3616 0.0012  -0.0492 0.0207  148 ILE A CG1   
1134 C  CG2   . ILE A 150 ? 0.3005 0.3381 0.3390 -0.0043 -0.0711 0.0326  148 ILE A CG2   
1135 C  CD1   . ILE A 150 ? 0.3495 0.3490 0.3532 0.0044  -0.0408 0.0407  148 ILE A CD1   
1136 N  N     . HIS A 151 ? 0.2900 0.2672 0.2982 -0.0351 -0.0421 0.0047  149 HIS A N     
1137 C  CA    . HIS A 151 ? 0.2586 0.2714 0.3340 -0.0404 -0.0516 0.0117  149 HIS A CA    
1138 C  C     . HIS A 151 ? 0.2470 0.3000 0.3278 -0.0218 -0.0354 0.0121  149 HIS A C     
1139 O  O     . HIS A 151 ? 0.2877 0.3097 0.3575 -0.0562 -0.0629 0.0142  149 HIS A O     
1140 C  CB    . HIS A 151 ? 0.2652 0.2741 0.3184 -0.0224 -0.0360 0.0396  149 HIS A CB    
1141 C  CG    . HIS A 151 ? 0.2424 0.2665 0.2895 -0.0343 -0.0568 0.0343  149 HIS A CG    
1142 N  ND1   . HIS A 151 ? 0.2616 0.3150 0.3044 -0.0619 -0.0594 0.0396  149 HIS A ND1   
1143 C  CD2   . HIS A 151 ? 0.2634 0.2630 0.3107 -0.0304 -0.0590 0.0385  149 HIS A CD2   
1144 C  CE1   . HIS A 151 ? 0.2611 0.3232 0.3227 -0.0358 -0.0567 0.0462  149 HIS A CE1   
1145 N  NE2   . HIS A 151 ? 0.2667 0.2979 0.3163 -0.0457 -0.0528 0.0253  149 HIS A NE2   
1146 N  N     . ARG A 152 ? 0.2409 0.2724 0.3472 -0.0087 -0.0520 0.0164  150 ARG A N     
1147 C  CA    . ARG A 152 ? 0.2876 0.2892 0.4032 -0.0389 -0.0426 0.0338  150 ARG A CA    
1148 C  C     . ARG A 152 ? 0.2859 0.3178 0.3930 -0.0259 -0.0500 0.0419  150 ARG A C     
1149 O  O     . ARG A 152 ? 0.3715 0.3268 0.4523 -0.0138 -0.0197 0.0495  150 ARG A O     
1150 C  CB    . ARG A 152 ? 0.2964 0.2740 0.4338 -0.0192 -0.0626 0.0382  150 ARG A CB    
1151 C  CG    . ARG A 152 ? 0.3679 0.3232 0.4773 -0.0110 -0.0499 0.0306  150 ARG A CG    
1152 C  CD    . ARG A 152 ? 0.3489 0.3343 0.5288 -0.0105 -0.0512 -0.0093 150 ARG A CD    
1153 N  NE    . ARG A 152 ? 0.4106 0.3836 0.4858 -0.0072 -0.0873 -0.0069 150 ARG A NE    
1154 C  CZ    . ARG A 152 ? 0.4761 0.4216 0.6266 -0.0009 -0.1131 -0.0477 150 ARG A CZ    
1155 N  NH1   . ARG A 152 ? 0.5423 0.3853 0.6677 -0.0239 -0.1047 -0.0601 150 ARG A NH1   
1156 N  NH2   . ARG A 152 ? 0.5230 0.4127 0.6602 -0.0285 -0.1487 -0.1107 150 ARG A NH2   
1157 N  N     . ASP A 153 ? 0.2576 0.2536 0.3279 -0.0272 -0.0663 0.0690  151 ASP A N     
1158 C  CA    . ASP A 153 ? 0.2659 0.2860 0.3689 -0.0312 -0.0460 0.0757  151 ASP A CA    
1159 C  C     . ASP A 153 ? 0.2494 0.3055 0.3385 -0.0245 -0.0448 0.0817  151 ASP A C     
1160 O  O     . ASP A 153 ? 0.2427 0.3343 0.3746 -0.0361 -0.0366 0.0689  151 ASP A O     
1161 C  CB    . ASP A 153 ? 0.2895 0.3405 0.3960 -0.0305 -0.0454 0.0732  151 ASP A CB    
1162 C  CG    . ASP A 153 ? 0.2950 0.3901 0.4652 -0.0355 -0.0339 0.0860  151 ASP A CG    
1163 O  OD1   . ASP A 153 ? 0.2888 0.3402 0.4297 -0.0349 0.0109  0.1171  151 ASP A OD1   
1164 O  OD2   . ASP A 153 ? 0.2780 0.5594 0.5200 -0.0498 0.0109  0.0837  151 ASP A OD2   
1165 N  N     . LEU A 154 ? 0.2281 0.2771 0.3040 -0.0279 -0.0165 0.0806  152 LEU A N     
1166 C  CA    . LEU A 154 ? 0.2232 0.2726 0.2956 -0.0144 -0.0290 0.0867  152 LEU A CA    
1167 C  C     . LEU A 154 ? 0.2564 0.2985 0.2986 -0.0319 -0.0135 0.0934  152 LEU A C     
1168 O  O     . LEU A 154 ? 0.2737 0.3276 0.2590 -0.0055 -0.0275 0.0910  152 LEU A O     
1169 C  CB    . LEU A 154 ? 0.2047 0.2920 0.2828 -0.0062 -0.0323 0.0827  152 LEU A CB    
1170 C  CG    . LEU A 154 ? 0.2767 0.3598 0.3699 -0.0271 -0.0224 0.0861  152 LEU A CG    
1171 C  CD1   . LEU A 154 ? 0.2665 0.4396 0.4280 -0.0061 -0.0394 0.0781  152 LEU A CD1   
1172 C  CD2   . LEU A 154 ? 0.2477 0.3509 0.3654 -0.0316 -0.0280 0.0841  152 LEU A CD2   
1173 N  N     . LYS A 155 ? 0.2876 0.3019 0.3271 -0.0176 -0.0053 0.0876  153 LYS A N     
1174 C  CA    . LYS A 155 ? 0.3050 0.3202 0.3245 -0.0358 0.0328  0.1018  153 LYS A CA    
1175 C  C     . LYS A 155 ? 0.2817 0.3152 0.2878 -0.0089 0.0398  0.0856  153 LYS A C     
1176 O  O     . LYS A 155 ? 0.2612 0.3076 0.3009 -0.0133 0.0247  0.0874  153 LYS A O     
1177 C  CB    . LYS A 155 ? 0.3356 0.3497 0.3583 -0.0497 0.0684  0.1208  153 LYS A CB    
1178 C  CG    . LYS A 155 ? 0.3391 0.3721 0.3805 -0.0482 0.0304  0.1252  153 LYS A CG    
1179 C  CD    . LYS A 155 ? 0.4233 0.4039 0.4877 -0.0574 0.0746  0.1341  153 LYS A CD    
1180 C  CE    . LYS A 155 ? 0.4731 0.4292 0.5540 -0.0735 0.0748  0.1458  153 LYS A CE    
1181 N  NZ    . LYS A 155 ? 0.4366 0.5171 0.5636 -0.1322 0.0679  0.1038  153 LYS A NZ    
1182 N  N     . PRO A 156 ? 0.2866 0.3417 0.2849 0.0011  0.0258  0.0965  154 PRO A N     
1183 C  CA    . PRO A 156 ? 0.2952 0.3551 0.2878 0.0163  0.0386  0.0868  154 PRO A CA    
1184 C  C     . PRO A 156 ? 0.2859 0.3747 0.2958 0.0050  0.0213  0.0969  154 PRO A C     
1185 O  O     . PRO A 156 ? 0.2693 0.4008 0.3133 0.0289  0.0251  0.0812  154 PRO A O     
1186 C  CB    . PRO A 156 ? 0.3374 0.4019 0.3104 0.0296  0.0060  0.0720  154 PRO A CB    
1187 C  CG    . PRO A 156 ? 0.3368 0.4148 0.3319 0.0281  0.0163  0.0705  154 PRO A CG    
1188 C  CD    . PRO A 156 ? 0.3116 0.3752 0.2971 0.0027  0.0197  0.0854  154 PRO A CD    
1189 N  N     . SER A 157 ? 0.2823 0.4098 0.3241 -0.0116 0.0461  0.1072  155 SER A N     
1190 C  CA    . SER A 157 ? 0.3168 0.4358 0.4222 -0.0012 0.0368  0.1077  155 SER A CA    
1191 C  C     . SER A 157 ? 0.3063 0.4588 0.4327 -0.0094 0.0443  0.0966  155 SER A C     
1192 O  O     . SER A 157 ? 0.3009 0.4383 0.4643 0.0287  0.0287  0.1075  155 SER A O     
1193 C  CB    . SER A 157 ? 0.3398 0.4790 0.4421 -0.0328 0.0402  0.1178  155 SER A CB    
1194 O  OG    . SER A 157 ? 0.3287 0.4522 0.4201 -0.0187 0.0419  0.1070  155 SER A OG    
1195 N  N     . ASN A 158 ? 0.2508 0.3819 0.3827 0.0069  0.0194  0.0622  156 ASN A N     
1196 C  CA    . ASN A 158 ? 0.3019 0.3865 0.4123 -0.0161 -0.0045 0.0946  156 ASN A CA    
1197 C  C     . ASN A 158 ? 0.2759 0.3623 0.3395 -0.0083 -0.0075 0.0643  156 ASN A C     
1198 O  O     . ASN A 158 ? 0.2605 0.2995 0.3013 -0.0199 -0.0039 0.0675  156 ASN A O     
1199 C  CB    . ASN A 158 ? 0.3949 0.4269 0.4337 -0.0613 -0.0202 0.0725  156 ASN A CB    
1200 C  CG    . ASN A 158 ? 0.4952 0.5387 0.5573 -0.1379 -0.0465 0.0703  156 ASN A CG    
1201 O  OD1   . ASN A 158 ? 0.5399 0.6497 0.7163 -0.1355 -0.0914 0.0426  156 ASN A OD1   
1202 N  ND2   . ASN A 158 ? 0.5465 0.5645 0.5113 -0.1858 -0.0781 0.0376  156 ASN A ND2   
1203 N  N     . ILE A 159 ? 0.2636 0.3625 0.3064 -0.0010 -0.0098 0.0562  157 ILE A N     
1204 C  CA    . ILE A 159 ? 0.2753 0.3428 0.2908 0.0072  -0.0102 0.0590  157 ILE A CA    
1205 C  C     . ILE A 159 ? 0.3217 0.3781 0.3148 0.0145  -0.0034 0.0468  157 ILE A C     
1206 O  O     . ILE A 159 ? 0.3235 0.3451 0.3287 0.0230  0.0403  0.0575  157 ILE A O     
1207 C  CB    . ILE A 159 ? 0.2783 0.3281 0.3024 -0.0246 -0.0007 0.0584  157 ILE A CB    
1208 C  CG1   . ILE A 159 ? 0.2908 0.3102 0.3226 -0.0309 -0.0099 0.0673  157 ILE A CG1   
1209 C  CG2   . ILE A 159 ? 0.2841 0.3257 0.2862 -0.0127 -0.0073 0.0583  157 ILE A CG2   
1210 C  CD1   . ILE A 159 ? 0.2953 0.3040 0.3527 -0.0248 -0.0107 0.0729  157 ILE A CD1   
1211 N  N     . VAL A 160 ? 0.3211 0.3621 0.3177 0.0250  -0.0032 0.0345  158 VAL A N     
1212 C  CA    . VAL A 160 ? 0.2937 0.3934 0.3413 0.0248  0.0093  0.0390  158 VAL A CA    
1213 C  C     . VAL A 160 ? 0.3368 0.3903 0.3381 0.0264  0.0009  0.0351  158 VAL A C     
1214 O  O     . VAL A 160 ? 0.2974 0.3217 0.3065 0.0133  -0.0045 0.0385  158 VAL A O     
1215 C  CB    . VAL A 160 ? 0.3093 0.4415 0.3487 0.0144  -0.0020 0.0209  158 VAL A CB    
1216 C  CG1   . VAL A 160 ? 0.2867 0.4627 0.3738 0.0289  -0.0081 0.0404  158 VAL A CG1   
1217 C  CG2   . VAL A 160 ? 0.3095 0.4510 0.3748 0.0045  -0.0469 0.0680  158 VAL A CG2   
1218 N  N     . VAL A 161 ? 0.3543 0.4152 0.3139 0.0458  0.0203  0.0261  159 VAL A N     
1219 C  CA    . VAL A 161 ? 0.3612 0.3793 0.3237 0.0427  0.0047  0.0259  159 VAL A CA    
1220 C  C     . VAL A 161 ? 0.3630 0.4411 0.3813 0.0614  0.0012  0.0289  159 VAL A C     
1221 O  O     . VAL A 161 ? 0.3823 0.4575 0.3474 0.0844  0.0295  0.0448  159 VAL A O     
1222 C  CB    . VAL A 161 ? 0.3748 0.4106 0.3422 0.0498  -0.0086 0.0192  159 VAL A CB    
1223 C  CG1   . VAL A 161 ? 0.4013 0.4305 0.3363 0.0456  -0.0220 -0.0150 159 VAL A CG1   
1224 C  CG2   . VAL A 161 ? 0.4297 0.4149 0.3190 0.0583  -0.0007 0.0358  159 VAL A CG2   
1225 N  N     . LYS A 162 ? 0.3827 0.3796 0.4097 0.0635  -0.0233 -0.0012 160 LYS A N     
1226 C  CA    . LYS A 162 ? 0.4177 0.4086 0.4671 0.0827  -0.0035 -0.0174 160 LYS A CA    
1227 C  C     . LYS A 162 ? 0.3955 0.4111 0.4946 0.0781  -0.0089 -0.0273 160 LYS A C     
1228 O  O     . LYS A 162 ? 0.4166 0.3360 0.3913 0.0845  -0.0413 -0.0335 160 LYS A O     
1229 C  CB    . LYS A 162 ? 0.5020 0.4636 0.5221 0.1010  -0.0404 0.0013  160 LYS A CB    
1230 C  CG    . LYS A 162 ? 0.6102 0.5977 0.5968 0.0697  -0.0576 0.0264  160 LYS A CG    
1231 C  CD    . LYS A 162 ? 0.7603 0.6527 0.6384 0.0531  -0.0163 0.0609  160 LYS A CD    
1232 C  CE    . LYS A 162 ? 0.7847 0.7281 0.6224 0.0590  0.0042  0.1136  160 LYS A CE    
1233 N  NZ    . LYS A 162 ? 0.9189 0.8417 0.6542 0.0963  -0.0751 0.1361  160 LYS A NZ    
1234 N  N     . SER A 163 ? 0.4187 0.4440 0.5319 0.0850  0.0000  -0.0708 161 SER A N     
1235 C  CA    . SER A 163 ? 0.4123 0.5091 0.5109 0.0820  -0.0337 -0.0913 161 SER A CA    
1236 C  C     . SER A 163 ? 0.4907 0.4264 0.4408 0.0796  -0.0327 -0.0978 161 SER A C     
1237 O  O     . SER A 163 ? 0.5023 0.4192 0.4475 0.1005  -0.0637 -0.1001 161 SER A O     
1238 C  CB    . SER A 163 ? 0.4550 0.5178 0.5887 0.1113  -0.0283 -0.1199 161 SER A CB    
1239 O  OG    . SER A 163 ? 0.4887 0.6346 0.6993 0.0992  -0.0208 -0.0664 161 SER A OG    
1240 N  N     . ASP A 164 ? 0.4532 0.3366 0.3850 0.0734  -0.0577 -0.0547 162 ASP A N     
1241 C  CA    . ASP A 164 ? 0.4806 0.3519 0.4308 0.0564  -0.0558 -0.0533 162 ASP A CA    
1242 C  C     . ASP A 164 ? 0.4698 0.3626 0.4158 0.0251  -0.0768 -0.0346 162 ASP A C     
1243 O  O     . ASP A 164 ? 0.5158 0.2870 0.4495 -0.0200 -0.0725 -0.0181 162 ASP A O     
1244 C  CB    . ASP A 164 ? 0.4896 0.3967 0.4362 0.0454  -0.0543 -0.0261 162 ASP A CB    
1245 C  CG    . ASP A 164 ? 0.4998 0.3683 0.4482 0.0526  -0.0628 -0.0171 162 ASP A CG    
1246 O  OD1   . ASP A 164 ? 0.4374 0.3397 0.4554 0.0599  -0.0728 -0.0554 162 ASP A OD1   
1247 O  OD2   . ASP A 164 ? 0.5426 0.3543 0.4703 0.0643  -0.1127 -0.0076 162 ASP A OD2   
1248 N  N     . CYS A 165 ? 0.4097 0.3150 0.3333 0.0233  -0.0539 -0.0273 163 CYS A N     
1249 C  CA    . CYS A 165 ? 0.4028 0.3452 0.3361 0.0092  -0.0444 -0.0272 163 CYS A CA    
1250 C  C     . CYS A 165 ? 0.3782 0.3127 0.3062 0.0170  -0.0295 -0.0083 163 CYS A C     
1251 O  O     . CYS A 165 ? 0.3776 0.3019 0.2738 -0.0053 -0.0172 -0.0163 163 CYS A O     
1252 C  CB    . CYS A 165 ? 0.4246 0.3567 0.3611 0.0052  -0.0441 -0.0418 163 CYS A CB    
1253 S  SG    . CYS A 165 ? 0.4217 0.3802 0.3453 0.0587  -0.0322 -0.0585 163 CYS A SG    
1254 N  N     . THR A 166 ? 0.3795 0.2839 0.3211 0.0301  -0.0405 -0.0063 164 THR A N     
1255 C  CA    . THR A 166 ? 0.3961 0.2885 0.3315 0.0246  -0.0407 -0.0028 164 THR A CA    
1256 C  C     . THR A 166 ? 0.3504 0.3161 0.3277 0.0250  -0.0374 0.0084  164 THR A C     
1257 O  O     . THR A 166 ? 0.3681 0.2877 0.3048 0.0134  -0.0451 0.0108  164 THR A O     
1258 C  CB    . THR A 166 ? 0.4670 0.3129 0.3477 0.0478  -0.0546 -0.0029 164 THR A CB    
1259 O  OG1   . THR A 166 ? 0.5594 0.3414 0.3868 0.0357  -0.0349 0.0228  164 THR A OG1   
1260 C  CG2   . THR A 166 ? 0.4808 0.3354 0.3549 0.0530  -0.0629 -0.0118 164 THR A CG2   
1261 N  N     . LEU A 167 ? 0.2994 0.3348 0.2667 0.0286  -0.0309 -0.0013 165 LEU A N     
1262 C  CA    . LEU A 167 ? 0.2783 0.3384 0.2263 0.0217  -0.0407 0.0182  165 LEU A CA    
1263 C  C     . LEU A 167 ? 0.2579 0.3582 0.2272 0.0401  -0.0401 0.0124  165 LEU A C     
1264 O  O     . LEU A 167 ? 0.2786 0.3418 0.2298 0.0271  -0.0413 0.0072  165 LEU A O     
1265 C  CB    . LEU A 167 ? 0.2665 0.3391 0.2232 0.0215  -0.0373 0.0171  165 LEU A CB    
1266 C  CG    . LEU A 167 ? 0.2734 0.3532 0.2244 0.0118  -0.0502 0.0273  165 LEU A CG    
1267 C  CD1   . LEU A 167 ? 0.2925 0.3611 0.2448 0.0110  -0.0587 0.0402  165 LEU A CD1   
1268 C  CD2   . LEU A 167 ? 0.2269 0.3457 0.2185 0.0064  -0.0474 0.0408  165 LEU A CD2   
1269 N  N     . LYS A 168 ? 0.2753 0.3943 0.2310 0.0359  -0.0425 0.0261  166 LYS A N     
1270 C  CA    . LYS A 168 ? 0.2579 0.3346 0.2272 0.0304  -0.0335 0.0345  166 LYS A CA    
1271 C  C     . LYS A 168 ? 0.2883 0.3936 0.2416 0.0317  -0.0365 0.0368  166 LYS A C     
1272 O  O     . LYS A 168 ? 0.2857 0.3685 0.2138 0.0264  -0.0180 0.0467  166 LYS A O     
1273 C  CB    . LYS A 168 ? 0.2691 0.3714 0.2829 0.0530  -0.0303 0.0346  166 LYS A CB    
1274 C  CG    . LYS A 168 ? 0.3090 0.3916 0.3331 0.0756  -0.0276 0.0224  166 LYS A CG    
1275 C  CD    . LYS A 168 ? 0.3198 0.4325 0.3618 0.1083  -0.0386 0.0210  166 LYS A CD    
1276 C  CE    . LYS A 168 ? 0.3681 0.4771 0.4292 0.1088  -0.0347 0.0283  166 LYS A CE    
1277 N  NZ    . LYS A 168 ? 0.3307 0.4149 0.4298 0.1146  -0.0466 0.0195  166 LYS A NZ    
1278 N  N     . ILE A 169 ? 0.2821 0.3733 0.2589 0.0288  -0.0590 0.0439  167 ILE A N     
1279 C  CA    . ILE A 169 ? 0.2457 0.3449 0.2395 0.0241  -0.0575 0.0492  167 ILE A CA    
1280 C  C     . ILE A 169 ? 0.2476 0.3771 0.2239 0.0368  -0.0571 0.0463  167 ILE A C     
1281 O  O     . ILE A 169 ? 0.2100 0.3652 0.2011 0.0268  -0.0551 0.0326  167 ILE A O     
1282 C  CB    . ILE A 169 ? 0.2817 0.3536 0.2981 0.0098  -0.0591 0.0432  167 ILE A CB    
1283 C  CG1   . ILE A 169 ? 0.2757 0.3488 0.3254 0.0089  -0.0754 0.0518  167 ILE A CG1   
1284 C  CG2   . ILE A 169 ? 0.2600 0.3314 0.2697 -0.0077 -0.0505 0.0196  167 ILE A CG2   
1285 C  CD1   . ILE A 169 ? 0.2781 0.3216 0.3362 0.0015  -0.0873 0.0451  167 ILE A CD1   
1286 N  N     . LEU A 170 ? 0.2457 0.4117 0.2132 0.0373  -0.0352 0.0302  168 LEU A N     
1287 C  CA    . LEU A 170 ? 0.2551 0.4275 0.2366 0.0338  -0.0477 0.0336  168 LEU A CA    
1288 C  C     . LEU A 170 ? 0.2788 0.4817 0.2843 0.0077  -0.0717 0.0191  168 LEU A C     
1289 O  O     . LEU A 170 ? 0.2208 0.4790 0.3022 -0.0148 -0.0513 -0.0302 168 LEU A O     
1290 C  CB    . LEU A 170 ? 0.2946 0.4654 0.2518 0.0353  -0.0123 0.0570  168 LEU A CB    
1291 C  CG    . LEU A 170 ? 0.3634 0.5839 0.3180 0.0680  0.0098  0.0669  168 LEU A CG    
1292 C  CD1   . LEU A 170 ? 0.3987 0.6398 0.3484 0.0773  0.0403  0.0704  168 LEU A CD1   
1293 C  CD2   . LEU A 170 ? 0.3634 0.6159 0.3650 0.1018  -0.0021 0.0854  168 LEU A CD2   
1294 N  N     . ASP A 171 ? 0.2842 0.4640 0.3093 0.0000  -0.0684 -0.0043 169 ASP A N     
1295 C  CA    . ASP A 171 ? 0.3124 0.4787 0.3280 0.0061  -0.0569 -0.0123 169 ASP A CA    
1296 C  C     . ASP A 171 ? 0.2898 0.4565 0.3034 -0.0447 -0.0343 0.0034  169 ASP A C     
1297 O  O     . ASP A 171 ? 0.2562 0.4074 0.2417 0.0082  -0.0396 -0.0011 169 ASP A O     
1298 C  CB    . ASP A 171 ? 0.3182 0.4800 0.3302 -0.0502 -0.0166 -0.0095 169 ASP A CB    
1299 C  CG    . ASP A 171 ? 0.3782 0.5163 0.4111 -0.0368 -0.0137 0.0348  169 ASP A CG    
1300 O  OD1   . ASP A 171 ? 0.3015 0.5254 0.3389 -0.0202 -0.0277 0.0859  169 ASP A OD1   
1301 O  OD2   . ASP A 171 ? 0.4970 0.5844 0.4963 -0.0171 -0.0274 0.1221  169 ASP A OD2   
1302 N  N     . PHE A 172 ? 0.2399 0.3866 0.3245 -0.0401 -0.0430 0.0042  170 PHE A N     
1303 C  CA    . PHE A 172 ? 0.2993 0.3762 0.3456 -0.0087 -0.0566 -0.0102 170 PHE A CA    
1304 C  C     . PHE A 172 ? 0.2955 0.3583 0.3182 0.0049  -0.0638 0.0026  170 PHE A C     
1305 O  O     . PHE A 172 ? 0.3130 0.3215 0.3446 0.0015  -0.0644 -0.0161 170 PHE A O     
1306 C  CB    . PHE A 172 ? 0.2978 0.4024 0.3578 0.0108  -0.0724 -0.0059 170 PHE A CB    
1307 C  CG    . PHE A 172 ? 0.2942 0.3943 0.3427 0.0064  -0.0604 -0.0382 170 PHE A CG    
1308 C  CD1   . PHE A 172 ? 0.3040 0.4240 0.3472 0.0329  -0.0568 -0.0316 170 PHE A CD1   
1309 C  CD2   . PHE A 172 ? 0.2637 0.4314 0.4382 -0.0422 -0.0749 -0.0093 170 PHE A CD2   
1310 C  CE1   . PHE A 172 ? 0.3089 0.4081 0.3705 -0.0113 -0.0784 -0.0374 170 PHE A CE1   
1311 C  CE2   . PHE A 172 ? 0.2913 0.4818 0.4369 -0.0129 -0.0580 0.0048  170 PHE A CE2   
1312 C  CZ    . PHE A 172 ? 0.3054 0.4113 0.4348 -0.0140 -0.0698 -0.0188 170 PHE A CZ    
1313 N  N     . GLY A 173 ? 0.2887 0.3530 0.3471 -0.0201 -0.0410 0.0002  171 GLY A N     
1314 C  CA    . GLY A 173 ? 0.3230 0.3853 0.3685 -0.0257 -0.0677 0.0149  171 GLY A CA    
1315 C  C     . GLY A 173 ? 0.3700 0.4253 0.4244 -0.0365 -0.0705 -0.0063 171 GLY A C     
1316 O  O     . GLY A 173 ? 0.3084 0.4389 0.3776 -0.0501 -0.0627 -0.0197 171 GLY A O     
1317 N  N     . LEU A 174 ? 0.3805 0.3952 0.4970 -0.0290 -0.0891 -0.0428 172 LEU A N     
1318 C  CA    . LEU A 174 ? 0.4631 0.3584 0.5437 -0.0519 -0.0910 -0.0290 172 LEU A CA    
1319 C  C     . LEU A 174 ? 0.5474 0.3917 0.5829 -0.0206 -0.0907 -0.0772 172 LEU A C     
1320 O  O     . LEU A 174 ? 0.5756 0.3494 0.7257 0.0476  -0.1285 0.0317  172 LEU A O     
1321 C  CB    . LEU A 174 ? 0.4411 0.3985 0.5629 -0.0687 -0.1060 -0.0142 172 LEU A CB    
1322 C  CG    . LEU A 174 ? 0.4631 0.3789 0.5830 -0.0633 -0.1081 0.0059  172 LEU A CG    
1323 C  CD1   . LEU A 174 ? 0.5450 0.4055 0.5545 -0.0644 -0.1318 0.0395  172 LEU A CD1   
1324 C  CD2   . LEU A 174 ? 0.5213 0.4186 0.5920 -0.0512 -0.0820 0.0047  172 LEU A CD2   
1325 N  N     . ALA A 175 ? 0.5252 0.3177 0.5560 -0.0600 -0.0631 -0.1565 173 ALA A N     
1326 C  CA    . ALA A 175 ? 0.5317 0.4564 0.6056 -0.0138 -0.0416 -0.1157 173 ALA A CA    
1327 C  C     . ALA A 175 ? 0.5872 0.4657 0.6568 -0.0121 -0.0325 -0.1220 173 ALA A C     
1328 O  O     . ALA A 175 ? 0.5443 0.4701 0.6200 0.0317  0.0018  -0.0990 173 ALA A O     
1329 C  CB    . ALA A 175 ? 0.5050 0.4287 0.6142 -0.0256 -0.0721 -0.1208 173 ALA A CB    
1330 N  N     . ARG A 176 ? 0.6143 0.4585 0.6951 0.0003  -0.0537 -0.1517 174 ARG A N     
1331 C  CA    . ARG A 176 ? 0.6467 0.5329 0.7218 -0.0079 -0.0490 -0.2163 174 ARG A CA    
1332 C  C     . ARG A 176 ? 0.6775 0.4720 0.7636 0.0126  -0.0524 -0.2106 174 ARG A C     
1333 O  O     . ARG A 176 ? 0.7161 0.4862 0.8490 0.0494  -0.0456 -0.1476 174 ARG A O     
1334 C  CB    . ARG A 176 ? 0.6765 0.5357 0.7619 -0.0227 -0.0550 -0.2408 174 ARG A CB    
1335 C  CG    . ARG A 176 ? 0.6656 0.6758 0.8035 -0.0026 -0.0145 -0.1966 174 ARG A CG    
1336 C  CD    . ARG A 176 ? 0.6277 0.6958 0.8430 0.0108  -0.0167 -0.2265 174 ARG A CD    
1337 N  N     . THR A 177 ? 0.6493 0.5842 0.9092 0.0323  -0.0948 -0.0368 175 THR A N     
1338 C  CA    . THR A 177 ? 0.6632 0.5572 0.9814 0.0279  -0.1368 -0.0008 175 THR A CA    
1339 C  C     . THR A 177 ? 0.7428 0.5171 1.0633 0.0082  -0.1875 0.0641  175 THR A C     
1340 O  O     . THR A 177 ? 0.7412 0.3956 0.9661 0.0441  -0.2706 0.0422  175 THR A O     
1341 C  CB    . THR A 177 ? 0.6617 0.6084 1.0241 0.0753  -0.1266 0.0105  175 THR A CB    
1342 O  OG1   . THR A 177 ? 0.6803 0.6686 1.0480 0.1705  -0.0771 -0.0447 175 THR A OG1   
1343 C  CG2   . THR A 177 ? 0.6120 0.5758 0.9769 0.0749  -0.0876 0.0282  175 THR A CG2   
1344 N  N     . ALA A 178 ? 0.8793 0.5330 1.1005 -0.1064 -0.2671 0.0602  176 ALA A N     
1345 C  CA    . ALA A 178 ? 0.9216 0.6451 1.1341 -0.0575 -0.2737 0.0825  176 ALA A CA    
1346 C  C     . ALA A 178 ? 0.9773 0.8261 1.2038 -0.0851 -0.2700 0.1022  176 ALA A C     
1347 O  O     . ALA A 178 ? 0.8607 0.9761 1.3311 -0.1729 -0.2991 0.0510  176 ALA A O     
1348 C  CB    . ALA A 178 ? 0.8632 0.6014 1.0547 -0.0320 -0.3012 0.0299  176 ALA A CB    
1349 N  N     . GLY A 179 ? 0.8292 0.7842 1.3026 -0.1276 -0.2352 0.1660  177 GLY A N     
1350 C  CA    . GLY A 179 ? 0.8291 0.7217 1.3230 -0.1290 -0.1391 0.1314  177 GLY A CA    
1351 C  C     . GLY A 179 ? 0.8007 0.7402 1.2654 -0.1328 -0.0501 0.1424  177 GLY A C     
1352 O  O     . GLY A 179 ? 0.7493 0.7933 1.3221 -0.2055 0.1224  0.0872  177 GLY A O     
1353 N  N     . THR A 180 ? 0.8348 0.6947 1.3502 -0.0821 -0.0671 0.1657  178 THR A N     
1354 C  CA    . THR A 180 ? 0.9221 0.6376 1.3946 -0.1178 -0.0909 0.1751  178 THR A CA    
1355 C  C     . THR A 180 ? 0.9556 0.6573 1.4298 -0.0663 -0.2511 0.2469  178 THR A C     
1356 O  O     . THR A 180 ? 1.1713 0.4658 1.4858 -0.1947 -0.2415 0.3540  178 THR A O     
1357 C  CB    . THR A 180 ? 0.8469 0.6938 1.4109 -0.1252 -0.0607 0.1281  178 THR A CB    
1358 O  OG1   . THR A 180 ? 0.8674 0.7130 1.5313 -0.0435 -0.0322 0.0791  178 THR A OG1   
1359 C  CG2   . THR A 180 ? 0.9025 0.6917 1.3746 -0.1200 -0.0632 0.1301  178 THR A CG2   
1360 N  N     . SER A 181 ? 0.8435 0.9284 1.4934 -0.0598 -0.3080 0.2348  179 SER A N     
1361 C  CA    . SER A 181 ? 0.9050 1.0194 1.4647 -0.0538 -0.3544 0.2574  179 SER A CA    
1362 C  C     . SER A 181 ? 0.8184 0.9920 1.3468 -0.0330 -0.4011 0.2656  179 SER A C     
1363 O  O     . SER A 181 ? 0.7294 0.9213 1.1742 -0.0206 -0.5060 0.3250  179 SER A O     
1364 C  CB    . SER A 181 ? 0.9779 1.1043 1.4806 -0.0673 -0.3911 0.2325  179 SER A CB    
1365 O  OG    . SER A 181 ? 1.0498 1.1945 1.4495 -0.0454 -0.4437 0.3249  179 SER A OG    
1366 N  N     . PHE A 182 ? 0.8397 0.9135 1.3454 0.0218  -0.3471 0.1949  180 PHE A N     
1367 C  CA    . PHE A 182 ? 0.9353 1.0067 1.4307 -0.0215 -0.1833 0.1189  180 PHE A CA    
1368 C  C     . PHE A 182 ? 0.9686 0.9544 1.4601 -0.0148 -0.1373 0.0494  180 PHE A C     
1369 O  O     . PHE A 182 ? 1.0418 0.7985 1.4546 -0.0636 -0.2097 0.0850  180 PHE A O     
1370 C  CB    . PHE A 182 ? 0.8876 1.0284 1.4654 -0.0650 -0.0620 0.0870  180 PHE A CB    
1371 C  CG    . PHE A 182 ? 0.9929 0.9273 1.5268 -0.0582 0.0751  0.0105  180 PHE A CG    
1372 C  CD1   . PHE A 182 ? 1.0232 0.9312 1.5037 -0.0404 0.0867  -0.0183 180 PHE A CD1   
1373 C  CD2   . PHE A 182 ? 0.9809 0.8993 1.4705 -0.1083 0.1077  -0.0599 180 PHE A CD2   
1374 C  CE1   . PHE A 182 ? 1.0025 0.9084 1.4297 0.0096  0.1616  -0.0991 180 PHE A CE1   
1375 C  CE2   . PHE A 182 ? 0.9417 0.9483 1.5123 -0.0191 0.0925  -0.1190 180 PHE A CE2   
1376 C  CZ    . PHE A 182 ? 0.8687 0.9785 1.5155 0.0238  0.1880  -0.1130 180 PHE A CZ    
1377 N  N     . MET A 183 ? 0.9931 0.8458 1.3952 -0.0594 -0.1127 -0.0321 181 MET A N     
1378 C  CA    . MET A 183 ? 0.9947 0.6673 1.3101 -0.0774 -0.0984 -0.0707 181 MET A CA    
1379 C  C     . MET A 183 ? 0.9612 0.6806 1.2401 -0.0086 -0.1092 -0.0731 181 MET A C     
1380 O  O     . MET A 183 ? 0.7546 0.7377 1.1705 -0.0405 -0.2141 -0.0356 181 MET A O     
1381 C  CB    . MET A 183 ? 1.0271 0.6132 1.3053 -0.1359 -0.0758 -0.0374 181 MET A CB    
1382 C  CG    . MET A 183 ? 1.0962 0.6669 1.3288 -0.1171 -0.0587 -0.0642 181 MET A CG    
1383 S  SD    . MET A 183 ? 1.1605 0.8126 1.3553 -0.2157 -0.0398 -0.0868 181 MET A SD    
1384 C  CE    . MET A 183 ? 1.0752 0.6371 1.1731 -0.2238 0.0397  -0.2348 181 MET A CE    
1385 N  N     . MET A 184 ? 0.9388 0.6699 1.1368 0.0321  -0.1001 -0.0833 182 MET A N     
1386 C  CA    . MET A 184 ? 1.0143 0.7727 1.0278 0.0712  -0.0852 -0.1056 182 MET A CA    
1387 C  C     . MET A 184 ? 1.0638 0.7617 0.8462 0.0128  -0.0328 -0.1471 182 MET A C     
1388 O  O     . MET A 184 ? 1.2299 0.8655 0.5646 -0.0258 0.0207  -0.2282 182 MET A O     
1389 C  CB    . MET A 184 ? 0.9699 0.7573 1.0766 0.1235  -0.1262 -0.1231 182 MET A CB    
1390 C  CG    . MET A 184 ? 1.0421 0.8964 1.1866 0.0941  -0.1475 -0.1056 182 MET A CG    
1391 S  SD    . MET A 184 ? 1.1194 1.1389 1.2492 0.1814  -0.0978 -0.1292 182 MET A SD    
1392 C  CE    . MET A 184 ? 1.2401 1.0175 1.2720 0.1677  -0.2011 -0.0179 182 MET A CE    
1393 N  N     . THR A 185 ? 0.9317 0.7743 0.8072 -0.0560 0.0165  -0.1325 183 THR A N     
1394 C  CA    . THR A 185 ? 0.7479 0.6867 0.7276 -0.1485 0.0697  -0.0792 183 THR A CA    
1395 C  C     . THR A 185 ? 0.5737 0.6510 0.6752 -0.1374 0.0680  -0.1038 183 THR A C     
1396 O  O     . THR A 185 ? 0.5658 0.7121 0.4758 -0.1528 0.0978  -0.0569 183 THR A O     
1397 C  CB    . THR A 185 ? 0.7314 0.6096 0.6911 -0.1625 0.0322  -0.0691 183 THR A CB    
1398 O  OG1   . THR A 185 ? 0.6720 0.5446 0.6459 -0.1948 0.0481  -0.0956 183 THR A OG1   
1399 C  CG2   . THR A 185 ? 0.7395 0.5692 0.7280 -0.1873 0.0627  -0.0330 183 THR A CG2   
1400 N  N     . PRO A 186 ? 0.5107 0.7026 0.7115 -0.1649 0.0526  -0.1183 184 PRO A N     
1401 C  CA    . PRO A 186 ? 0.4428 0.6283 0.7458 -0.1925 0.0533  -0.0992 184 PRO A CA    
1402 C  C     . PRO A 186 ? 0.3611 0.4787 0.6670 -0.1501 0.0953  -0.1036 184 PRO A C     
1403 O  O     . PRO A 186 ? 0.3630 0.4638 0.6983 -0.1855 0.1218  -0.0571 184 PRO A O     
1404 C  CB    . PRO A 186 ? 0.4784 0.6582 0.7837 -0.1978 0.0692  -0.0967 184 PRO A CB    
1405 C  CG    . PRO A 186 ? 0.5493 0.7216 0.8224 -0.1752 0.0969  -0.0590 184 PRO A CG    
1406 C  CD    . PRO A 186 ? 0.5778 0.7397 0.7863 -0.1167 0.0726  -0.1059 184 PRO A CD    
1407 N  N     . TYR A 187 ? 0.3390 0.4783 0.5614 -0.1252 0.0726  -0.0498 185 TYR A N     
1408 C  CA    . TYR A 187 ? 0.2706 0.4682 0.5606 -0.1701 0.0823  -0.0192 185 TYR A CA    
1409 C  C     . TYR A 187 ? 0.3031 0.4572 0.5616 -0.1639 0.0810  0.0099  185 TYR A C     
1410 O  O     . TYR A 187 ? 0.3344 0.4573 0.4771 -0.1475 0.0344  -0.0362 185 TYR A O     
1411 C  CB    . TYR A 187 ? 0.3049 0.5266 0.5736 -0.1673 0.0672  -0.0306 185 TYR A CB    
1412 C  CG    . TYR A 187 ? 0.3624 0.5722 0.6467 -0.1428 0.0349  -0.0170 185 TYR A CG    
1413 C  CD1   . TYR A 187 ? 0.3432 0.5193 0.6043 -0.1398 0.0447  -0.0339 185 TYR A CD1   
1414 C  CD2   . TYR A 187 ? 0.4182 0.6658 0.6942 -0.1267 0.0159  -0.0281 185 TYR A CD2   
1415 C  CE1   . TYR A 187 ? 0.3316 0.5223 0.6857 -0.1691 0.0399  -0.0555 185 TYR A CE1   
1416 C  CE2   . TYR A 187 ? 0.3974 0.6815 0.7250 -0.0910 0.0051  -0.0223 185 TYR A CE2   
1417 C  CZ    . TYR A 187 ? 0.3649 0.6402 0.7133 -0.1214 0.0254  0.0200  185 TYR A CZ    
1418 O  OH    . TYR A 187 ? 0.3356 0.6049 0.8816 -0.1686 0.0233  0.0361  185 TYR A OH    
1419 N  N     . VAL A 188 ? 0.2507 0.4522 0.4941 -0.1465 0.1157  -0.0088 186 VAL A N     
1420 C  CA    . VAL A 188 ? 0.2735 0.4733 0.5147 -0.1573 0.0928  -0.0029 186 VAL A CA    
1421 C  C     . VAL A 188 ? 0.3007 0.4949 0.5115 -0.1450 0.0791  -0.0064 186 VAL A C     
1422 O  O     . VAL A 188 ? 0.3395 0.5269 0.5216 -0.1595 0.0458  0.0103  186 VAL A O     
1423 C  CB    . VAL A 188 ? 0.2807 0.5073 0.5674 -0.1556 0.1026  -0.0136 186 VAL A CB    
1424 C  CG1   . VAL A 188 ? 0.2924 0.5868 0.5894 -0.1324 0.0935  -0.0137 186 VAL A CG1   
1425 C  CG2   . VAL A 188 ? 0.3159 0.5345 0.5531 -0.1076 0.1451  -0.0149 186 VAL A CG2   
1426 N  N     . VAL A 189 ? 0.3240 0.5109 0.5269 -0.1569 0.0615  -0.0142 187 VAL A N     
1427 C  CA    . VAL A 189 ? 0.3408 0.5258 0.5155 -0.1354 0.0768  -0.0123 187 VAL A CA    
1428 C  C     . VAL A 189 ? 0.3027 0.4936 0.5331 -0.1010 0.0696  0.0314  187 VAL A C     
1429 O  O     . VAL A 189 ? 0.3696 0.4755 0.5955 -0.0950 0.0302  0.0795  187 VAL A O     
1430 C  CB    . VAL A 189 ? 0.4097 0.6037 0.6440 -0.0989 0.1535  -0.0006 187 VAL A CB    
1431 C  CG1   . VAL A 189 ? 0.5232 0.6754 0.7264 -0.0758 0.1711  -0.0092 187 VAL A CG1   
1432 C  CG2   . VAL A 189 ? 0.3655 0.6422 0.6344 -0.1135 0.1314  -0.0300 187 VAL A CG2   
1433 N  N     . THR A 190 ? 0.2836 0.4428 0.4631 -0.0793 0.0372  0.0413  188 THR A N     
1434 C  CA    . THR A 190 ? 0.3186 0.4823 0.4781 -0.1003 0.0325  0.0271  188 THR A CA    
1435 C  C     . THR A 190 ? 0.3296 0.4644 0.4589 -0.0748 0.0249  0.0344  188 THR A C     
1436 O  O     . THR A 190 ? 0.3079 0.4173 0.4095 -0.0811 0.0039  0.0142  188 THR A O     
1437 C  CB    . THR A 190 ? 0.3310 0.5392 0.5392 -0.0641 0.0171  -0.0164 188 THR A CB    
1438 O  OG1   . THR A 190 ? 0.3599 0.6465 0.5097 -0.0895 0.0117  0.0441  188 THR A OG1   
1439 C  CG2   . THR A 190 ? 0.3289 0.5821 0.5183 -0.0498 -0.0045 -0.0402 188 THR A CG2   
1440 N  N     . ARG A 191 ? 0.3655 0.4256 0.4059 -0.0912 0.0463  0.0690  189 ARG A N     
1441 C  CA    . ARG A 191 ? 0.3533 0.3317 0.4144 -0.0785 -0.0071 0.0395  189 ARG A CA    
1442 C  C     . ARG A 191 ? 0.3442 0.2965 0.3717 -0.0652 -0.0007 0.0798  189 ARG A C     
1443 O  O     . ARG A 191 ? 0.3274 0.2908 0.4444 -0.0647 -0.0089 0.0657  189 ARG A O     
1444 C  CB    . ARG A 191 ? 0.4089 0.3413 0.4573 -0.0960 -0.0075 0.0360  189 ARG A CB    
1445 C  CG    . ARG A 191 ? 0.4491 0.4009 0.5594 -0.1203 -0.0175 0.0116  189 ARG A CG    
1446 C  CD    . ARG A 191 ? 0.5401 0.4550 0.6833 -0.1247 0.0018  -0.0042 189 ARG A CD    
1447 N  NE    . ARG A 191 ? 0.6584 0.5605 0.7901 -0.0618 -0.0491 -0.0774 189 ARG A NE    
1448 C  CZ    . ARG A 191 ? 0.7271 0.6141 0.8512 -0.1204 -0.0490 -0.0440 189 ARG A CZ    
1449 N  NH1   . ARG A 191 ? 0.8406 0.7799 0.8982 -0.0705 0.0204  -0.0254 189 ARG A NH1   
1450 N  NH2   . ARG A 191 ? 0.6731 0.5910 0.9205 -0.1479 -0.0145 -0.0333 189 ARG A NH2   
1451 N  N     . TYR A 192 ? 0.3525 0.3157 0.3429 -0.0608 -0.0143 0.0726  190 TYR A N     
1452 C  CA    . TYR A 192 ? 0.3145 0.3214 0.3500 -0.0667 -0.0060 0.0703  190 TYR A CA    
1453 C  C     . TYR A 192 ? 0.3207 0.3711 0.3357 -0.0496 -0.0026 0.0556  190 TYR A C     
1454 O  O     . TYR A 192 ? 0.2937 0.3272 0.3084 -0.0151 -0.0247 0.0434  190 TYR A O     
1455 C  CB    . TYR A 192 ? 0.2771 0.3312 0.3104 -0.0748 -0.0108 0.0611  190 TYR A CB    
1456 C  CG    . TYR A 192 ? 0.3644 0.3703 0.3561 -0.0701 0.0198  0.0815  190 TYR A CG    
1457 C  CD1   . TYR A 192 ? 0.3820 0.4180 0.3757 -0.0758 0.0165  0.1121  190 TYR A CD1   
1458 C  CD2   . TYR A 192 ? 0.3465 0.4186 0.3428 -0.0644 0.0131  0.0871  190 TYR A CD2   
1459 C  CE1   . TYR A 192 ? 0.4199 0.4586 0.3933 -0.0648 0.0225  0.1141  190 TYR A CE1   
1460 C  CE2   . TYR A 192 ? 0.3956 0.4628 0.3775 -0.0687 0.0189  0.0928  190 TYR A CE2   
1461 C  CZ    . TYR A 192 ? 0.4009 0.4670 0.3944 -0.0764 0.0136  0.1049  190 TYR A CZ    
1462 O  OH    . TYR A 192 ? 0.4530 0.5846 0.5263 -0.0757 0.0359  0.1521  190 TYR A OH    
1463 N  N     . TYR A 193 ? 0.2742 0.3135 0.2749 -0.0405 -0.0111 0.0438  191 TYR A N     
1464 C  CA    . TYR A 193 ? 0.2609 0.2984 0.2729 -0.0386 -0.0220 0.0370  191 TYR A CA    
1465 C  C     . TYR A 193 ? 0.2626 0.3029 0.2918 -0.0247 -0.0232 0.0284  191 TYR A C     
1466 O  O     . TYR A 193 ? 0.2474 0.3025 0.2795 -0.0250 -0.0179 0.0003  191 TYR A O     
1467 C  CB    . TYR A 193 ? 0.2736 0.2926 0.2538 -0.0300 -0.0079 0.0417  191 TYR A CB    
1468 C  CG    . TYR A 193 ? 0.2629 0.3102 0.2600 -0.0233 -0.0028 0.0374  191 TYR A CG    
1469 C  CD1   . TYR A 193 ? 0.2812 0.3181 0.2888 -0.0177 0.0106  0.0301  191 TYR A CD1   
1470 C  CD2   . TYR A 193 ? 0.2937 0.3062 0.2799 -0.0117 -0.0107 0.0352  191 TYR A CD2   
1471 C  CE1   . TYR A 193 ? 0.2762 0.3126 0.2778 -0.0230 -0.0019 0.0341  191 TYR A CE1   
1472 C  CE2   . TYR A 193 ? 0.2853 0.3505 0.2902 0.0004  -0.0085 0.0350  191 TYR A CE2   
1473 C  CZ    . TYR A 193 ? 0.2761 0.3070 0.2734 -0.0091 0.0065  0.0432  191 TYR A CZ    
1474 O  OH    . TYR A 193 ? 0.3169 0.3378 0.2835 -0.0037 -0.0041 0.0276  191 TYR A OH    
1475 N  N     . ARG A 194 ? 0.2661 0.2998 0.2976 -0.0292 -0.0226 0.0268  192 ARG A N     
1476 C  CA    . ARG A 194 ? 0.2954 0.3014 0.3493 -0.0299 -0.0332 0.0036  192 ARG A CA    
1477 C  C     . ARG A 194 ? 0.3003 0.2416 0.3197 -0.0188 -0.0396 -0.0017 192 ARG A C     
1478 O  O     . ARG A 194 ? 0.3053 0.2824 0.3108 -0.0214 -0.0371 0.0256  192 ARG A O     
1479 C  CB    . ARG A 194 ? 0.2710 0.3456 0.3596 -0.0431 -0.0274 -0.0018 192 ARG A CB    
1480 C  CG    . ARG A 194 ? 0.3019 0.3544 0.3888 -0.0307 -0.0335 0.0119  192 ARG A CG    
1481 C  CD    . ARG A 194 ? 0.3191 0.4101 0.4400 -0.0428 -0.0442 -0.0128 192 ARG A CD    
1482 N  NE    . ARG A 194 ? 0.3008 0.3930 0.4072 -0.0461 -0.0437 -0.0176 192 ARG A NE    
1483 C  CZ    . ARG A 194 ? 0.3279 0.3968 0.5191 -0.0750 -0.0480 -0.0247 192 ARG A CZ    
1484 N  NH1   . ARG A 194 ? 0.3606 0.4082 0.5767 -0.0747 -0.0872 -0.0380 192 ARG A NH1   
1485 N  NH2   . ARG A 194 ? 0.3025 0.3711 0.4839 -0.0994 -0.0676 -0.0236 192 ARG A NH2   
1486 N  N     . ALA A 195 ? 0.3019 0.2554 0.2999 -0.0136 -0.0411 0.0077  193 ALA A N     
1487 C  CA    . ALA A 195 ? 0.2930 0.2427 0.3135 -0.0179 -0.0402 0.0079  193 ALA A CA    
1488 C  C     . ALA A 195 ? 0.2874 0.2596 0.3342 -0.0112 -0.0423 0.0122  193 ALA A C     
1489 O  O     . ALA A 195 ? 0.2896 0.2789 0.3153 -0.0234 -0.0302 -0.0011 193 ALA A O     
1490 C  CB    . ALA A 195 ? 0.2996 0.2511 0.3224 -0.0167 -0.0579 0.0148  193 ALA A CB    
1491 N  N     . PRO A 196 ? 0.3017 0.2352 0.2983 -0.0015 -0.0526 0.0244  194 PRO A N     
1492 C  CA    . PRO A 196 ? 0.3015 0.2251 0.3286 -0.0003 -0.0567 0.0264  194 PRO A CA    
1493 C  C     . PRO A 196 ? 0.3127 0.2785 0.3614 0.0107  -0.0589 0.0264  194 PRO A C     
1494 O  O     . PRO A 196 ? 0.3594 0.2872 0.4016 0.0202  -0.0575 -0.0035 194 PRO A O     
1495 C  CB    . PRO A 196 ? 0.3183 0.2374 0.3535 0.0042  -0.0713 0.0266  194 PRO A CB    
1496 C  CG    . PRO A 196 ? 0.3126 0.2636 0.3162 -0.0051 -0.0705 0.0171  194 PRO A CG    
1497 C  CD    . PRO A 196 ? 0.3103 0.2908 0.3276 -0.0056 -0.0546 0.0137  194 PRO A CD    
1498 N  N     . GLU A 197 ? 0.2876 0.2862 0.3602 0.0021  -0.0383 0.0009  195 GLU A N     
1499 C  CA    . GLU A 197 ? 0.3422 0.3060 0.3717 -0.0204 -0.0443 -0.0139 195 GLU A CA    
1500 C  C     . GLU A 197 ? 0.3599 0.2979 0.3866 -0.0282 -0.0380 -0.0080 195 GLU A C     
1501 O  O     . GLU A 197 ? 0.3746 0.3413 0.3948 -0.0465 -0.0639 -0.0535 195 GLU A O     
1502 C  CB    . GLU A 197 ? 0.3645 0.3109 0.3924 -0.0029 -0.0254 -0.0150 195 GLU A CB    
1503 C  CG    . GLU A 197 ? 0.3448 0.2953 0.3439 -0.0156 -0.0328 -0.0010 195 GLU A CG    
1504 C  CD    . GLU A 197 ? 0.3136 0.3230 0.3476 -0.0056 -0.0466 -0.0113 195 GLU A CD    
1505 O  OE1   . GLU A 197 ? 0.2818 0.2812 0.3696 0.0063  -0.0479 0.0016  195 GLU A OE1   
1506 O  OE2   . GLU A 197 ? 0.3352 0.3171 0.3335 0.0149  -0.0694 -0.0093 195 GLU A OE2   
1507 N  N     . VAL A 198 ? 0.3523 0.2724 0.3827 -0.0319 -0.0500 0.0049  196 VAL A N     
1508 C  CA    . VAL A 198 ? 0.3612 0.2887 0.4165 -0.0460 -0.0711 -0.0191 196 VAL A CA    
1509 C  C     . VAL A 198 ? 0.4018 0.3069 0.4406 -0.0549 -0.0689 -0.0227 196 VAL A C     
1510 O  O     . VAL A 198 ? 0.3696 0.3205 0.4024 -0.0541 -0.0909 -0.0441 196 VAL A O     
1511 C  CB    . VAL A 198 ? 0.3693 0.3345 0.4397 -0.0329 -0.0557 -0.0170 196 VAL A CB    
1512 C  CG1   . VAL A 198 ? 0.3767 0.3493 0.4669 -0.0132 -0.0682 -0.0146 196 VAL A CG1   
1513 C  CG2   . VAL A 198 ? 0.3587 0.3052 0.3946 0.0015  -0.0489 -0.0171 196 VAL A CG2   
1514 N  N     . ILE A 199 ? 0.3970 0.3044 0.4560 -0.0610 -0.0654 -0.0357 197 ILE A N     
1515 C  CA    . ILE A 199 ? 0.4226 0.3030 0.4520 -0.0455 -0.0566 -0.0027 197 ILE A CA    
1516 C  C     . ILE A 199 ? 0.4598 0.2979 0.4750 -0.0576 -0.0632 0.0404  197 ILE A C     
1517 O  O     . ILE A 199 ? 0.5129 0.3287 0.5336 -0.1022 -0.0332 0.0253  197 ILE A O     
1518 C  CB    . ILE A 199 ? 0.4374 0.2953 0.4702 -0.0485 -0.0483 0.0276  197 ILE A CB    
1519 C  CG1   . ILE A 199 ? 0.3975 0.3391 0.4607 -0.0181 -0.0530 0.0257  197 ILE A CG1   
1520 C  CG2   . ILE A 199 ? 0.4514 0.3318 0.4367 -0.0160 -0.0581 0.0549  197 ILE A CG2   
1521 C  CD1   . ILE A 199 ? 0.4420 0.4229 0.4913 -0.0053 -0.0225 0.0342  197 ILE A CD1   
1522 N  N     . LEU A 200 ? 0.4112 0.2676 0.4885 -0.0405 -0.1072 0.0262  198 LEU A N     
1523 C  CA    . LEU A 200 ? 0.4250 0.2760 0.5039 -0.0670 -0.0708 -0.0021 198 LEU A CA    
1524 C  C     . LEU A 200 ? 0.4260 0.3164 0.5098 -0.0370 -0.0322 -0.0052 198 LEU A C     
1525 O  O     . LEU A 200 ? 0.5380 0.3001 0.5663 -0.0080 -0.0831 -0.0080 198 LEU A O     
1526 C  CB    . LEU A 200 ? 0.4372 0.2685 0.4825 -0.0250 -0.0463 0.0096  198 LEU A CB    
1527 C  CG    . LEU A 200 ? 0.4868 0.3163 0.5002 -0.0504 -0.0582 -0.0017 198 LEU A CG    
1528 C  CD1   . LEU A 200 ? 0.4939 0.3820 0.4972 -0.0317 -0.0534 -0.0063 198 LEU A CD1   
1529 C  CD2   . LEU A 200 ? 0.5848 0.3037 0.5328 -0.0500 -0.0470 -0.0106 198 LEU A CD2   
1530 N  N     . GLY A 201 ? 0.3983 0.3366 0.5332 -0.0067 -0.0636 -0.0270 199 GLY A N     
1531 C  CA    . GLY A 201 ? 0.4134 0.3592 0.5361 -0.0199 -0.0950 -0.0605 199 GLY A CA    
1532 C  C     . GLY A 201 ? 0.4085 0.3547 0.4856 0.0096  -0.1259 -0.0712 199 GLY A C     
1533 O  O     . GLY A 201 ? 0.4422 0.3263 0.5089 0.0424  -0.1402 -0.0706 199 GLY A O     
1534 N  N     . MET A 202 ? 0.3873 0.3159 0.4746 0.0301  -0.1253 -0.0491 200 MET A N     
1535 C  CA    . MET A 202 ? 0.4287 0.3489 0.4586 0.0227  -0.1134 -0.0342 200 MET A CA    
1536 C  C     . MET A 202 ? 0.4420 0.3606 0.4844 0.0508  -0.1026 -0.0549 200 MET A C     
1537 O  O     . MET A 202 ? 0.4195 0.3848 0.4982 0.0365  -0.1487 -0.0273 200 MET A O     
1538 C  CB    . MET A 202 ? 0.4014 0.3598 0.4729 -0.0049 -0.1099 -0.0263 200 MET A CB    
1539 C  CG    . MET A 202 ? 0.4625 0.3254 0.5183 -0.0143 -0.1268 -0.0145 200 MET A CG    
1540 S  SD    . MET A 202 ? 0.4572 0.3946 0.5140 0.0468  -0.1270 -0.0432 200 MET A SD    
1541 C  CE    . MET A 202 ? 0.4844 0.4413 0.5745 0.0665  -0.1170 -0.0234 200 MET A CE    
1542 N  N     . GLY A 203 ? 0.4474 0.3651 0.5002 0.0360  -0.0924 -0.0586 201 GLY A N     
1543 C  CA    . GLY A 203 ? 0.4229 0.3893 0.4697 0.0448  -0.0703 -0.0809 201 GLY A CA    
1544 C  C     . GLY A 203 ? 0.3988 0.3807 0.4289 0.0567  -0.0804 -0.0880 201 GLY A C     
1545 O  O     . GLY A 203 ? 0.4404 0.3538 0.4116 0.0355  -0.0670 -0.0851 201 GLY A O     
1546 N  N     . TYR A 204 ? 0.4276 0.3984 0.3665 0.0554  -0.0625 -0.0896 202 TYR A N     
1547 C  CA    . TYR A 204 ? 0.3938 0.3930 0.3437 0.0336  -0.0570 -0.0669 202 TYR A CA    
1548 C  C     . TYR A 204 ? 0.3750 0.4056 0.3342 0.0344  -0.0181 -0.0719 202 TYR A C     
1549 O  O     . TYR A 204 ? 0.4121 0.4109 0.3129 0.0320  -0.0348 -0.0459 202 TYR A O     
1550 C  CB    . TYR A 204 ? 0.3383 0.3168 0.3310 0.0322  -0.0594 -0.0635 202 TYR A CB    
1551 C  CG    . TYR A 204 ? 0.3487 0.3346 0.3503 0.0166  -0.0717 -0.0766 202 TYR A CG    
1552 C  CD1   . TYR A 204 ? 0.4113 0.3748 0.4055 -0.0109 -0.0888 -0.0505 202 TYR A CD1   
1553 C  CD2   . TYR A 204 ? 0.3268 0.3283 0.3767 -0.0026 -0.0806 -0.0908 202 TYR A CD2   
1554 C  CE1   . TYR A 204 ? 0.4525 0.3752 0.4511 0.0243  -0.1128 -0.0734 202 TYR A CE1   
1555 C  CE2   . TYR A 204 ? 0.4146 0.3594 0.3984 0.0135  -0.1005 -0.0572 202 TYR A CE2   
1556 C  CZ    . TYR A 204 ? 0.4821 0.4058 0.4463 0.0153  -0.1324 -0.0866 202 TYR A CZ    
1557 O  OH    . TYR A 204 ? 0.5599 0.3640 0.4213 0.0361  -0.1560 -0.1116 202 TYR A OH    
1558 N  N     . LYS A 205 ? 0.3356 0.4022 0.3182 0.0338  0.0033  -0.0439 203 LYS A N     
1559 C  CA    . LYS A 205 ? 0.3602 0.3740 0.3448 0.0593  -0.0031 -0.0308 203 LYS A CA    
1560 C  C     . LYS A 205 ? 0.3589 0.3728 0.3102 0.0327  0.0038  -0.0203 203 LYS A C     
1561 O  O     . LYS A 205 ? 0.3276 0.3400 0.2954 0.0390  -0.0006 0.0007  203 LYS A O     
1562 C  CB    . LYS A 205 ? 0.3681 0.3648 0.3747 0.0362  -0.0188 -0.0151 203 LYS A CB    
1563 C  CG    . LYS A 205 ? 0.3974 0.4154 0.4268 0.0516  -0.0138 0.0008  203 LYS A CG    
1564 C  CD    . LYS A 205 ? 0.3889 0.4460 0.4759 0.0409  -0.0153 0.0069  203 LYS A CD    
1565 C  CE    . LYS A 205 ? 0.3705 0.4923 0.4840 0.0247  -0.0279 -0.0116 203 LYS A CE    
1566 N  NZ    . LYS A 205 ? 0.4431 0.5752 0.5732 0.0448  0.0173  0.0189  203 LYS A NZ    
1567 N  N     . GLU A 206 ? 0.3505 0.3783 0.3133 0.0278  -0.0003 0.0103  204 GLU A N     
1568 C  CA    . GLU A 206 ? 0.3340 0.3673 0.2821 0.0278  0.0044  0.0184  204 GLU A CA    
1569 C  C     . GLU A 206 ? 0.2680 0.3086 0.2720 0.0153  -0.0050 0.0277  204 GLU A C     
1570 O  O     . GLU A 206 ? 0.2512 0.3471 0.2633 0.0214  -0.0313 0.0393  204 GLU A O     
1571 C  CB    . GLU A 206 ? 0.3630 0.3543 0.2777 0.0340  0.0179  0.0309  204 GLU A CB    
1572 C  CG    . GLU A 206 ? 0.4021 0.4265 0.3271 0.0573  -0.0004 -0.0027 204 GLU A CG    
1573 C  CD    . GLU A 206 ? 0.4759 0.5529 0.3425 0.0632  0.0070  -0.0110 204 GLU A CD    
1574 O  OE1   . GLU A 206 ? 0.5068 0.5818 0.3708 0.0667  0.0397  0.0296  204 GLU A OE1   
1575 O  OE2   . GLU A 206 ? 0.6345 0.6994 0.3910 0.0782  -0.0081 0.0533  204 GLU A OE2   
1576 N  N     . ASN A 207 ? 0.2626 0.3211 0.2771 0.0312  0.0074  0.0182  205 ASN A N     
1577 C  CA    . ASN A 207 ? 0.2720 0.3195 0.2802 0.0091  -0.0179 0.0176  205 ASN A CA    
1578 C  C     . ASN A 207 ? 0.2726 0.3561 0.2682 -0.0145 -0.0027 -0.0050 205 ASN A C     
1579 O  O     . ASN A 207 ? 0.2756 0.2933 0.2530 -0.0146 -0.0340 0.0049  205 ASN A O     
1580 C  CB    . ASN A 207 ? 0.2583 0.3254 0.2716 0.0002  -0.0069 0.0131  205 ASN A CB    
1581 C  CG    . ASN A 207 ? 0.2706 0.3576 0.2961 0.0123  -0.0122 -0.0061 205 ASN A CG    
1582 O  OD1   . ASN A 207 ? 0.3003 0.3608 0.3217 0.0325  -0.0131 -0.0285 205 ASN A OD1   
1583 N  ND2   . ASN A 207 ? 0.2629 0.3470 0.3397 0.0261  -0.0036 -0.0055 205 ASN A ND2   
1584 N  N     . VAL A 208 ? 0.2782 0.3244 0.2767 -0.0065 -0.0086 -0.0121 206 VAL A N     
1585 C  CA    . VAL A 208 ? 0.2612 0.3227 0.2642 0.0049  -0.0271 0.0068  206 VAL A CA    
1586 C  C     . VAL A 208 ? 0.2850 0.3096 0.2759 0.0104  -0.0330 0.0186  206 VAL A C     
1587 O  O     . VAL A 208 ? 0.2869 0.2969 0.2882 -0.0097 -0.0426 0.0394  206 VAL A O     
1588 C  CB    . VAL A 208 ? 0.2465 0.3256 0.2540 0.0048  -0.0233 -0.0053 206 VAL A CB    
1589 C  CG1   . VAL A 208 ? 0.2659 0.3272 0.2966 0.0059  -0.0425 -0.0165 206 VAL A CG1   
1590 C  CG2   . VAL A 208 ? 0.2349 0.2961 0.3076 0.0115  -0.0294 -0.0011 206 VAL A CG2   
1591 N  N     . ASP A 209 ? 0.2399 0.2863 0.2347 0.0082  -0.0378 0.0148  207 ASP A N     
1592 C  CA    . ASP A 209 ? 0.2225 0.2710 0.2165 0.0026  -0.0344 0.0229  207 ASP A CA    
1593 C  C     . ASP A 209 ? 0.2359 0.2940 0.2435 0.0213  -0.0252 0.0150  207 ASP A C     
1594 O  O     . ASP A 209 ? 0.2281 0.2680 0.2365 0.0186  -0.0175 0.0155  207 ASP A O     
1595 C  CB    . ASP A 209 ? 0.2361 0.2895 0.2297 0.0157  -0.0454 0.0209  207 ASP A CB    
1596 C  CG    . ASP A 209 ? 0.2606 0.3095 0.2355 0.0128  -0.0365 0.0008  207 ASP A CG    
1597 O  OD1   . ASP A 209 ? 0.2416 0.3032 0.2264 0.0130  -0.0253 0.0028  207 ASP A OD1   
1598 O  OD2   . ASP A 209 ? 0.2712 0.3525 0.2138 0.0078  -0.0339 0.0052  207 ASP A OD2   
1599 N  N     . ILE A 210 ? 0.2043 0.2616 0.2376 0.0035  -0.0171 0.0074  208 ILE A N     
1600 C  CA    . ILE A 210 ? 0.2498 0.2734 0.2449 0.0141  -0.0226 0.0084  208 ILE A CA    
1601 C  C     . ILE A 210 ? 0.2702 0.2854 0.2821 -0.0094 -0.0067 0.0143  208 ILE A C     
1602 O  O     . ILE A 210 ? 0.2753 0.2791 0.2583 -0.0230 -0.0200 0.0020  208 ILE A O     
1603 C  CB    . ILE A 210 ? 0.2456 0.2806 0.2691 0.0035  -0.0304 0.0140  208 ILE A CB    
1604 C  CG1   . ILE A 210 ? 0.2498 0.2938 0.2772 -0.0011 -0.0120 0.0215  208 ILE A CG1   
1605 C  CG2   . ILE A 210 ? 0.2519 0.2481 0.2595 -0.0059 -0.0121 0.0012  208 ILE A CG2   
1606 C  CD1   . ILE A 210 ? 0.2828 0.3004 0.3211 -0.0010 -0.0239 0.0329  208 ILE A CD1   
1607 N  N     . TRP A 211 ? 0.2187 0.2416 0.2459 0.0085  -0.0230 0.0132  209 TRP A N     
1608 C  CA    . TRP A 211 ? 0.2283 0.2586 0.2281 0.0007  -0.0346 0.0152  209 TRP A CA    
1609 C  C     . TRP A 211 ? 0.2636 0.2606 0.2449 0.0049  -0.0334 0.0213  209 TRP A C     
1610 O  O     . TRP A 211 ? 0.2514 0.2478 0.2247 -0.0121 -0.0430 0.0372  209 TRP A O     
1611 C  CB    . TRP A 211 ? 0.2614 0.2583 0.2501 0.0125  -0.0353 0.0032  209 TRP A CB    
1612 C  CG    . TRP A 211 ? 0.2934 0.2659 0.2810 -0.0095 -0.0331 0.0244  209 TRP A CG    
1613 C  CD1   . TRP A 211 ? 0.2809 0.2706 0.3024 -0.0226 -0.0544 0.0228  209 TRP A CD1   
1614 C  CD2   . TRP A 211 ? 0.3077 0.2775 0.3107 -0.0041 -0.0513 0.0353  209 TRP A CD2   
1615 N  NE1   . TRP A 211 ? 0.2943 0.2866 0.3031 -0.0490 -0.0380 0.0468  209 TRP A NE1   
1616 C  CE2   . TRP A 211 ? 0.3182 0.3044 0.3063 0.0013  -0.0489 0.0439  209 TRP A CE2   
1617 C  CE3   . TRP A 211 ? 0.3238 0.2805 0.3082 -0.0040 -0.0624 0.0209  209 TRP A CE3   
1618 C  CZ2   . TRP A 211 ? 0.3614 0.3204 0.2961 0.0045  -0.0615 0.0600  209 TRP A CZ2   
1619 C  CZ3   . TRP A 211 ? 0.3726 0.3180 0.3342 0.0047  -0.0689 0.0358  209 TRP A CZ3   
1620 C  CH2   . TRP A 211 ? 0.3594 0.3159 0.2946 0.0037  -0.0674 0.0571  209 TRP A CH2   
1621 N  N     . SER A 212 ? 0.2308 0.2683 0.2184 -0.0111 -0.0240 0.0126  210 SER A N     
1622 C  CA    . SER A 212 ? 0.2320 0.2688 0.2185 -0.0120 -0.0237 0.0265  210 SER A CA    
1623 C  C     . SER A 212 ? 0.2300 0.2718 0.2184 -0.0012 -0.0154 0.0272  210 SER A C     
1624 O  O     . SER A 212 ? 0.2287 0.2595 0.2338 0.0021  -0.0181 0.0162  210 SER A O     
1625 C  CB    . SER A 212 ? 0.2035 0.2740 0.2214 -0.0131 -0.0087 0.0223  210 SER A CB    
1626 O  OG    . SER A 212 ? 0.2499 0.3127 0.2443 -0.0411 -0.0310 0.0123  210 SER A OG    
1627 N  N     . VAL A 213 ? 0.2361 0.2633 0.2409 -0.0048 -0.0151 0.0314  211 VAL A N     
1628 C  CA    . VAL A 213 ? 0.2381 0.2799 0.2421 -0.0082 -0.0356 0.0205  211 VAL A CA    
1629 C  C     . VAL A 213 ? 0.2462 0.2609 0.2269 -0.0156 -0.0170 0.0288  211 VAL A C     
1630 O  O     . VAL A 213 ? 0.2653 0.2779 0.2522 -0.0310 -0.0287 0.0263  211 VAL A O     
1631 C  CB    . VAL A 213 ? 0.2657 0.2831 0.2471 -0.0049 -0.0546 0.0332  211 VAL A CB    
1632 C  CG1   . VAL A 213 ? 0.3256 0.2985 0.2951 0.0039  -0.0702 0.0454  211 VAL A CG1   
1633 C  CG2   . VAL A 213 ? 0.2719 0.2765 0.1964 -0.0117 -0.0227 0.0322  211 VAL A CG2   
1634 N  N     . GLY A 214 ? 0.2537 0.2860 0.2506 -0.0154 -0.0218 0.0267  212 GLY A N     
1635 C  CA    . GLY A 214 ? 0.2783 0.2588 0.2418 -0.0001 -0.0252 0.0274  212 GLY A CA    
1636 C  C     . GLY A 214 ? 0.2680 0.2685 0.2307 -0.0087 -0.0278 0.0208  212 GLY A C     
1637 O  O     . GLY A 214 ? 0.2998 0.2694 0.2588 -0.0131 -0.0413 0.0114  212 GLY A O     
1638 N  N     . CYS A 215 ? 0.2703 0.2837 0.2265 -0.0101 -0.0331 0.0089  213 CYS A N     
1639 C  CA    . CYS A 215 ? 0.2723 0.2826 0.2224 -0.0218 -0.0355 0.0189  213 CYS A CA    
1640 C  C     . CYS A 215 ? 0.3031 0.3103 0.2436 -0.0004 -0.0267 0.0243  213 CYS A C     
1641 O  O     . CYS A 215 ? 0.3107 0.3243 0.2457 -0.0074 -0.0307 0.0273  213 CYS A O     
1642 C  CB    . CYS A 215 ? 0.2704 0.2833 0.2345 -0.0098 -0.0375 0.0189  213 CYS A CB    
1643 S  SG    . CYS A 215 ? 0.3026 0.2704 0.2641 -0.0199 -0.0283 0.0352  213 CYS A SG    
1644 N  N     . ILE A 216 ? 0.2518 0.3246 0.2022 -0.0090 -0.0236 0.0086  214 ILE A N     
1645 C  CA    . ILE A 216 ? 0.2594 0.3006 0.2468 -0.0223 -0.0143 0.0161  214 ILE A CA    
1646 C  C     . ILE A 216 ? 0.2940 0.3164 0.2747 -0.0095 -0.0303 0.0021  214 ILE A C     
1647 O  O     . ILE A 216 ? 0.2897 0.3222 0.2534 0.0210  -0.0325 0.0203  214 ILE A O     
1648 C  CB    . ILE A 216 ? 0.2483 0.3223 0.2473 -0.0225 0.0000  0.0297  214 ILE A CB    
1649 C  CG1   . ILE A 216 ? 0.2692 0.3271 0.2358 -0.0322 -0.0221 0.0296  214 ILE A CG1   
1650 C  CG2   . ILE A 216 ? 0.2646 0.3035 0.2742 -0.0190 -0.0071 0.0238  214 ILE A CG2   
1651 C  CD1   . ILE A 216 ? 0.2794 0.3442 0.2431 -0.0212 -0.0287 0.0239  214 ILE A CD1   
1652 N  N     . MET A 217 ? 0.2931 0.2885 0.2652 0.0069  -0.0370 0.0217  215 MET A N     
1653 C  CA    . MET A 217 ? 0.3097 0.2878 0.2902 0.0156  -0.0420 0.0123  215 MET A CA    
1654 C  C     . MET A 217 ? 0.3354 0.3016 0.2675 0.0143  -0.0354 0.0006  215 MET A C     
1655 O  O     . MET A 217 ? 0.3207 0.3096 0.2595 0.0200  -0.0363 0.0048  215 MET A O     
1656 C  CB    . MET A 217 ? 0.2789 0.2669 0.2788 0.0045  -0.0379 0.0021  215 MET A CB    
1657 C  CG    . MET A 217 ? 0.2811 0.3182 0.3163 0.0109  -0.0724 -0.0103 215 MET A CG    
1658 S  SD    . MET A 217 ? 0.3120 0.2941 0.3130 -0.0155 -0.0410 -0.0045 215 MET A SD    
1659 C  CE    . MET A 217 ? 0.3274 0.3256 0.3220 -0.0192 -0.0597 -0.0279 215 MET A CE    
1660 N  N     . GLY A 218 ? 0.3146 0.2727 0.2333 0.0156  -0.0260 0.0177  216 GLY A N     
1661 C  CA    . GLY A 218 ? 0.3498 0.3095 0.2574 0.0283  -0.0456 0.0167  216 GLY A CA    
1662 C  C     . GLY A 218 ? 0.3609 0.3049 0.2706 0.0102  -0.0275 0.0105  216 GLY A C     
1663 O  O     . GLY A 218 ? 0.4322 0.3473 0.2683 0.0103  -0.0512 0.0299  216 GLY A O     
1664 N  N     . GLU A 219 ? 0.3345 0.3144 0.2348 0.0153  -0.0295 0.0146  217 GLU A N     
1665 C  CA    . GLU A 219 ? 0.3648 0.3367 0.2457 0.0058  -0.0086 0.0151  217 GLU A CA    
1666 C  C     . GLU A 219 ? 0.3690 0.3446 0.2467 0.0064  -0.0113 -0.0054 217 GLU A C     
1667 O  O     . GLU A 219 ? 0.3913 0.3381 0.2719 0.0272  -0.0080 -0.0011 217 GLU A O     
1668 C  CB    . GLU A 219 ? 0.3600 0.3720 0.2497 0.0121  -0.0042 -0.0003 217 GLU A CB    
1669 C  CG    . GLU A 219 ? 0.3973 0.4149 0.3166 0.0000  0.0003  -0.0043 217 GLU A CG    
1670 C  CD    . GLU A 219 ? 0.3862 0.4761 0.3274 -0.0175 0.0187  -0.0161 217 GLU A CD    
1671 O  OE1   . GLU A 219 ? 0.3500 0.4721 0.2533 -0.0217 0.0434  0.0205  217 GLU A OE1   
1672 O  OE2   . GLU A 219 ? 0.3752 0.4301 0.2833 0.0080  0.0409  -0.0447 217 GLU A OE2   
1673 N  N     . MET A 220 ? 0.3684 0.3192 0.2507 0.0087  -0.0056 -0.0017 218 MET A N     
1674 C  CA    . MET A 220 ? 0.4030 0.3527 0.2968 0.0074  -0.0147 -0.0080 218 MET A CA    
1675 C  C     . MET A 220 ? 0.4145 0.3445 0.3036 0.0014  -0.0190 -0.0261 218 MET A C     
1676 O  O     . MET A 220 ? 0.4151 0.4284 0.2801 0.0204  -0.0084 -0.0401 218 MET A O     
1677 C  CB    . MET A 220 ? 0.4125 0.3734 0.2909 0.0048  -0.0046 -0.0048 218 MET A CB    
1678 C  CG    . MET A 220 ? 0.4670 0.4446 0.3694 0.0003  -0.0305 0.0408  218 MET A CG    
1679 S  SD    . MET A 220 ? 0.5135 0.5352 0.4044 -0.0141 -0.0077 0.0945  218 MET A SD    
1680 C  CE    . MET A 220 ? 0.5998 0.5817 0.4718 0.0011  -0.0444 0.1215  218 MET A CE    
1681 N  N     . ILE A 221 ? 0.3942 0.4014 0.3277 -0.0232 -0.0283 -0.0211 219 ILE A N     
1682 C  CA    . ILE A 221 ? 0.4514 0.4353 0.2855 -0.0230 -0.0388 -0.0345 219 ILE A CA    
1683 C  C     . ILE A 221 ? 0.4726 0.4639 0.2994 -0.0155 -0.0259 -0.0493 219 ILE A C     
1684 O  O     . ILE A 221 ? 0.4422 0.4863 0.2906 0.0126  -0.0101 -0.0705 219 ILE A O     
1685 C  CB    . ILE A 221 ? 0.4356 0.4308 0.2885 0.0181  -0.0694 -0.0311 219 ILE A CB    
1686 C  CG1   . ILE A 221 ? 0.4118 0.4437 0.3111 0.0021  -0.0651 -0.0329 219 ILE A CG1   
1687 C  CG2   . ILE A 221 ? 0.4910 0.4460 0.2635 0.0418  -0.0689 -0.0428 219 ILE A CG2   
1688 C  CD1   . ILE A 221 ? 0.3571 0.4034 0.3106 0.0115  -0.0760 -0.0155 219 ILE A CD1   
1689 N  N     . LYS A 222 ? 0.4724 0.4775 0.2833 0.0076  -0.0272 -0.0308 220 LYS A N     
1690 C  CA    . LYS A 222 ? 0.4865 0.4934 0.3211 0.0168  -0.0292 -0.0074 220 LYS A CA    
1691 C  C     . LYS A 222 ? 0.5132 0.5316 0.2983 -0.0157 -0.0168 -0.0065 220 LYS A C     
1692 O  O     . LYS A 222 ? 0.5385 0.5819 0.2839 -0.0020 -0.0417 0.0045  220 LYS A O     
1693 C  CB    . LYS A 222 ? 0.5306 0.4959 0.3928 0.0237  0.0047  -0.0183 220 LYS A CB    
1694 C  CG    . LYS A 222 ? 0.5796 0.5329 0.5051 0.0343  -0.0100 -0.0093 220 LYS A CG    
1695 C  CD    . LYS A 222 ? 0.6342 0.5009 0.5302 0.0310  -0.0219 0.0133  220 LYS A CD    
1696 C  CE    . LYS A 222 ? 0.6074 0.5068 0.4925 0.0318  0.0126  0.0128  220 LYS A CE    
1697 N  NZ    . LYS A 222 ? 0.6259 0.5232 0.5205 0.0281  0.0182  -0.0077 220 LYS A NZ    
1698 N  N     . GLY A 223 ? 0.4910 0.5415 0.3467 -0.0053 -0.0004 0.0167  221 GLY A N     
1699 C  CA    . GLY A 223 ? 0.5044 0.5204 0.3632 0.0187  0.0191  0.0098  221 GLY A CA    
1700 C  C     . GLY A 223 ? 0.5036 0.5568 0.4934 -0.0137 0.0883  -0.0011 221 GLY A C     
1701 O  O     . GLY A 223 ? 0.5239 0.6123 0.6814 0.0119  0.1206  -0.0190 221 GLY A O     
1702 N  N     . GLY A 224 ? 0.5055 0.5167 0.3848 -0.0601 0.0719  -0.0024 222 GLY A N     
1703 C  CA    . GLY A 224 ? 0.5135 0.5207 0.3323 -0.0395 0.0560  0.0377  222 GLY A CA    
1704 C  C     . GLY A 224 ? 0.4700 0.4829 0.3555 -0.0280 0.0372  0.0433  222 GLY A C     
1705 O  O     . GLY A 224 ? 0.4306 0.4705 0.3003 -0.0151 0.0044  0.0532  222 GLY A O     
1706 N  N     . VAL A 225 ? 0.4483 0.4599 0.3057 -0.0584 0.0616  0.0741  223 VAL A N     
1707 C  CA    . VAL A 225 ? 0.4466 0.4097 0.2869 -0.0397 0.0053  0.0719  223 VAL A CA    
1708 C  C     . VAL A 225 ? 0.4293 0.3906 0.2699 -0.0476 0.0201  0.0505  223 VAL A C     
1709 O  O     . VAL A 225 ? 0.4570 0.4486 0.2204 -0.0546 0.0332  0.0657  223 VAL A O     
1710 C  CB    . VAL A 225 ? 0.4236 0.4118 0.2948 -0.0435 0.0323  0.0814  223 VAL A CB    
1711 C  CG1   . VAL A 225 ? 0.3793 0.3767 0.2905 -0.0732 0.0189  0.0899  223 VAL A CG1   
1712 C  CG2   . VAL A 225 ? 0.4358 0.4277 0.2904 -0.0273 0.0350  0.0952  223 VAL A CG2   
1713 N  N     . LEU A 226 ? 0.3879 0.3313 0.2313 -0.0608 0.0125  0.0713  224 LEU A N     
1714 C  CA    . LEU A 226 ? 0.4074 0.3662 0.2757 -0.0320 -0.0036 0.0675  224 LEU A CA    
1715 C  C     . LEU A 226 ? 0.4171 0.3703 0.2842 -0.0079 -0.0069 0.0772  224 LEU A C     
1716 O  O     . LEU A 226 ? 0.4459 0.4152 0.3083 0.0069  -0.0341 0.0860  224 LEU A O     
1717 C  CB    . LEU A 226 ? 0.4106 0.3700 0.2400 -0.0174 -0.0252 0.0514  224 LEU A CB    
1718 C  CG    . LEU A 226 ? 0.4126 0.4377 0.2744 -0.0155 -0.0493 0.0256  224 LEU A CG    
1719 C  CD1   . LEU A 226 ? 0.4047 0.4502 0.2983 -0.0004 -0.0498 0.0214  224 LEU A CD1   
1720 C  CD2   . LEU A 226 ? 0.4460 0.4682 0.3231 -0.0225 -0.0523 -0.0050 224 LEU A CD2   
1721 N  N     . PHE A 227 ? 0.4101 0.3545 0.2862 -0.0136 -0.0107 0.0859  225 PHE A N     
1722 C  CA    . PHE A 227 ? 0.4229 0.3534 0.3167 -0.0115 -0.0178 0.0935  225 PHE A CA    
1723 C  C     . PHE A 227 ? 0.4860 0.3753 0.3556 -0.0339 -0.0110 0.0960  225 PHE A C     
1724 O  O     . PHE A 227 ? 0.5013 0.3941 0.3813 0.0042  -0.0289 0.0727  225 PHE A O     
1725 C  CB    . PHE A 227 ? 0.4387 0.3348 0.3232 -0.0101 -0.0354 0.0663  225 PHE A CB    
1726 C  CG    . PHE A 227 ? 0.4148 0.3289 0.3165 -0.0001 -0.0377 0.0334  225 PHE A CG    
1727 C  CD1   . PHE A 227 ? 0.4324 0.3741 0.3717 -0.0019 -0.0354 0.0526  225 PHE A CD1   
1728 C  CD2   . PHE A 227 ? 0.4196 0.3482 0.3755 -0.0137 -0.0523 0.0463  225 PHE A CD2   
1729 C  CE1   . PHE A 227 ? 0.4242 0.3722 0.3597 -0.0255 -0.0827 0.0540  225 PHE A CE1   
1730 C  CE2   . PHE A 227 ? 0.4103 0.3731 0.3689 0.0060  -0.0596 0.0418  225 PHE A CE2   
1731 C  CZ    . PHE A 227 ? 0.4073 0.3767 0.3789 -0.0226 -0.0845 0.0430  225 PHE A CZ    
1732 N  N     . PRO A 228 ? 0.4894 0.4248 0.3438 -0.0639 0.0279  0.1266  226 PRO A N     
1733 C  CA    . PRO A 228 ? 0.5330 0.4657 0.3884 -0.0634 0.0088  0.1343  226 PRO A CA    
1734 C  C     . PRO A 228 ? 0.5537 0.4610 0.4478 -0.0590 0.0236  0.1777  226 PRO A C     
1735 O  O     . PRO A 228 ? 0.6501 0.5097 0.5608 -0.1170 0.0485  0.2231  226 PRO A O     
1736 C  CB    . PRO A 228 ? 0.5491 0.4528 0.3820 -0.0459 0.0211  0.1284  226 PRO A CB    
1737 C  CG    . PRO A 228 ? 0.5390 0.5582 0.4361 -0.0542 0.0391  0.1223  226 PRO A CG    
1738 C  CD    . PRO A 228 ? 0.5234 0.4585 0.3580 -0.0584 0.0290  0.1220  226 PRO A CD    
1739 N  N     . GLY A 229 ? 0.5386 0.4655 0.5137 -0.0741 -0.0099 0.1578  227 GLY A N     
1740 C  CA    . GLY A 229 ? 0.5726 0.5026 0.5644 -0.1310 0.0020  0.1420  227 GLY A CA    
1741 C  C     . GLY A 229 ? 0.5695 0.5463 0.5871 -0.1365 0.0649  0.1662  227 GLY A C     
1742 O  O     . GLY A 229 ? 0.4507 0.5414 0.6004 -0.1490 0.0398  0.1020  227 GLY A O     
1743 N  N     . THR A 230 ? 0.7266 0.5481 0.6130 -0.1390 0.0832  0.1733  228 THR A N     
1744 C  CA    . THR A 230 ? 0.7230 0.5347 0.7200 -0.1510 0.0544  0.1522  228 THR A CA    
1745 C  C     . THR A 230 ? 0.7392 0.5856 0.8017 -0.1752 0.0159  0.1163  228 THR A C     
1746 O  O     . THR A 230 ? 0.8273 0.6010 0.9654 -0.2023 0.0308  0.0856  228 THR A O     
1747 C  CB    . THR A 230 ? 0.7870 0.6394 0.7198 -0.1208 0.1008  0.1522  228 THR A CB    
1748 O  OG1   . THR A 230 ? 0.7903 0.5814 0.7223 -0.0827 0.0879  0.2152  228 THR A OG1   
1749 C  CG2   . THR A 230 ? 0.8060 0.7132 0.7356 -0.0979 0.1354  0.1244  228 THR A CG2   
1750 N  N     . ASP A 231 ? 0.6918 0.4368 0.8426 -0.1793 -0.0100 0.0891  229 ASP A N     
1751 C  CA    . ASP A 231 ? 0.7351 0.5135 0.8486 -0.1400 -0.0774 0.0609  229 ASP A CA    
1752 C  C     . ASP A 231 ? 0.6489 0.5165 0.8348 -0.0686 -0.0836 0.0127  229 ASP A C     
1753 O  O     . ASP A 231 ? 0.5531 0.4007 0.8863 0.0367  -0.0663 -0.0059 229 ASP A O     
1754 C  CB    . ASP A 231 ? 0.8068 0.5450 0.8914 -0.1929 -0.1327 0.0131  229 ASP A CB    
1755 C  CG    . ASP A 231 ? 0.9611 0.4975 0.9119 -0.1339 -0.1243 0.0399  229 ASP A CG    
1756 O  OD1   . ASP A 231 ? 0.9192 0.6712 0.8384 -0.2488 -0.1901 0.1536  229 ASP A OD1   
1757 O  OD2   . ASP A 231 ? 0.9949 0.5219 1.0594 -0.2150 -0.0721 -0.0309 229 ASP A OD2   
1758 N  N     . HIS A 232 ? 0.6307 0.5840 0.8800 -0.0197 -0.1194 -0.0561 230 HIS A N     
1759 C  CA    . HIS A 232 ? 0.6907 0.5506 0.8579 -0.0214 -0.0887 -0.0165 230 HIS A CA    
1760 C  C     . HIS A 232 ? 0.7834 0.5563 0.9299 -0.0394 -0.0630 0.0086  230 HIS A C     
1761 O  O     . HIS A 232 ? 0.7699 0.5638 1.0740 -0.0136 -0.0382 -0.0926 230 HIS A O     
1762 C  CB    . HIS A 232 ? 0.7195 0.6699 0.7870 0.0391  -0.0677 -0.0307 230 HIS A CB    
1763 N  N     . ILE A 233 ? 0.9211 0.5757 0.9023 -0.0406 -0.1161 0.0485  231 ILE A N     
1764 C  CA    . ILE A 233 ? 0.8556 0.5421 0.9440 -0.0706 -0.0978 0.0336  231 ILE A CA    
1765 C  C     . ILE A 233 ? 0.7151 0.4882 0.8722 -0.1600 -0.0298 0.0982  231 ILE A C     
1766 O  O     . ILE A 233 ? 0.6837 0.4210 0.8295 -0.1812 -0.0455 0.0552  231 ILE A O     
1767 C  CB    . ILE A 233 ? 0.9457 0.4659 1.0383 -0.0033 -0.1302 0.0301  231 ILE A CB    
1768 C  CG1   . ILE A 233 ? 1.0501 0.5586 1.0880 0.0868  -0.1295 -0.0086 231 ILE A CG1   
1769 C  CG2   . ILE A 233 ? 0.8970 0.3821 1.0581 -0.0146 -0.1173 0.0476  231 ILE A CG2   
1770 C  CD1   . ILE A 233 ? 1.0991 0.5979 1.0974 0.1574  -0.0819 -0.0554 231 ILE A CD1   
1771 N  N     . ASP A 234 ? 0.6365 0.4316 0.8089 -0.2334 -0.0411 0.1632  232 ASP A N     
1772 C  CA    . ASP A 234 ? 0.6733 0.4160 0.7542 -0.2102 -0.0154 0.1929  232 ASP A CA    
1773 C  C     . ASP A 234 ? 0.6157 0.4093 0.6523 -0.1902 -0.0619 0.1998  232 ASP A C     
1774 O  O     . ASP A 234 ? 0.5585 0.4764 0.5343 -0.1362 -0.1061 0.1803  232 ASP A O     
1775 C  CB    . ASP A 234 ? 0.6982 0.4912 0.7370 -0.2062 0.0137  0.2065  232 ASP A CB    
1776 C  CG    . ASP A 234 ? 0.7931 0.6247 0.7549 -0.1634 0.0117  0.2209  232 ASP A CG    
1777 O  OD1   . ASP A 234 ? 0.8121 0.6121 0.8253 -0.0459 0.0610  0.3136  232 ASP A OD1   
1778 O  OD2   . ASP A 234 ? 0.8826 0.7871 0.8505 -0.0927 -0.0256 0.1816  232 ASP A OD2   
1779 N  N     . GLN A 235 ? 0.5603 0.4306 0.6032 -0.1505 -0.0829 0.1514  233 GLN A N     
1780 C  CA    . GLN A 235 ? 0.5366 0.4137 0.6137 -0.0815 -0.0393 0.1104  233 GLN A CA    
1781 C  C     . GLN A 235 ? 0.5322 0.3822 0.6390 -0.0575 -0.0833 0.0674  233 GLN A C     
1782 O  O     . GLN A 235 ? 0.5348 0.2695 0.5786 -0.0072 -0.0684 0.0721  233 GLN A O     
1783 C  CB    . GLN A 235 ? 0.5789 0.4312 0.6026 -0.0744 -0.0185 0.0968  233 GLN A CB    
1784 C  CG    . GLN A 235 ? 0.5745 0.4322 0.6207 -0.0664 0.0247  0.0752  233 GLN A CG    
1785 C  CD    . GLN A 235 ? 0.5591 0.4042 0.6484 -0.0315 0.0253  0.1227  233 GLN A CD    
1786 O  OE1   . GLN A 235 ? 0.5635 0.4475 0.7294 -0.0094 -0.0246 0.1097  233 GLN A OE1   
1787 N  NE2   . GLN A 235 ? 0.5360 0.4382 0.6613 -0.0183 0.0064  0.0985  233 GLN A NE2   
1788 N  N     . TRP A 236 ? 0.5119 0.3562 0.5146 -0.0383 -0.1145 0.0142  234 TRP A N     
1789 C  CA    . TRP A 236 ? 0.5236 0.3256 0.5075 -0.0198 -0.1166 0.0362  234 TRP A CA    
1790 C  C     . TRP A 236 ? 0.5163 0.3573 0.5021 -0.0143 -0.1123 0.0851  234 TRP A C     
1791 O  O     . TRP A 236 ? 0.5584 0.3403 0.5118 -0.0173 -0.1152 0.0787  234 TRP A O     
1792 C  CB    . TRP A 236 ? 0.5108 0.3126 0.4878 0.0084  -0.1395 0.0352  234 TRP A CB    
1793 C  CG    . TRP A 236 ? 0.5002 0.3072 0.4765 -0.0095 -0.1434 0.0387  234 TRP A CG    
1794 C  CD1   . TRP A 236 ? 0.5131 0.2956 0.5052 -0.0038 -0.1409 0.0678  234 TRP A CD1   
1795 C  CD2   . TRP A 236 ? 0.4746 0.3133 0.4466 -0.0092 -0.1319 0.0377  234 TRP A CD2   
1796 N  NE1   . TRP A 236 ? 0.5294 0.3278 0.4901 -0.0028 -0.1427 0.0635  234 TRP A NE1   
1797 C  CE2   . TRP A 236 ? 0.4819 0.3372 0.4367 -0.0010 -0.1348 0.0544  234 TRP A CE2   
1798 C  CE3   . TRP A 236 ? 0.4336 0.3629 0.4413 -0.0119 -0.1509 0.0438  234 TRP A CE3   
1799 C  CZ2   . TRP A 236 ? 0.4474 0.3509 0.4233 0.0288  -0.1180 0.0364  234 TRP A CZ2   
1800 C  CZ3   . TRP A 236 ? 0.4633 0.3623 0.4610 0.0072  -0.1347 0.0458  234 TRP A CZ3   
1801 C  CH2   . TRP A 236 ? 0.4492 0.3233 0.4701 0.0169  -0.0993 0.0165  234 TRP A CH2   
1802 N  N     . ASN A 237 ? 0.5248 0.4108 0.4966 -0.0256 -0.1030 0.0891  235 ASN A N     
1803 C  CA    . ASN A 237 ? 0.5536 0.4509 0.5026 -0.0410 -0.0881 0.1219  235 ASN A CA    
1804 C  C     . ASN A 237 ? 0.5753 0.4496 0.4802 -0.0279 -0.0821 0.1137  235 ASN A C     
1805 O  O     . ASN A 237 ? 0.5794 0.3524 0.3861 -0.0147 -0.1126 0.1198  235 ASN A O     
1806 C  CB    . ASN A 237 ? 0.5644 0.4453 0.5756 -0.0603 -0.1013 0.1504  235 ASN A CB    
1807 C  CG    . ASN A 237 ? 0.6560 0.4476 0.6874 -0.0289 -0.0670 0.1799  235 ASN A CG    
1808 O  OD1   . ASN A 237 ? 0.7136 0.4543 0.7992 -0.0448 0.0334  0.1990  235 ASN A OD1   
1809 N  ND2   . ASN A 237 ? 0.7899 0.4788 0.7268 -0.0042 -0.0752 0.2605  235 ASN A ND2   
1810 N  N     . LYS A 238 ? 0.5512 0.4422 0.4489 -0.0447 -0.0671 0.0976  236 LYS A N     
1811 C  CA    . LYS A 238 ? 0.5378 0.4323 0.3940 -0.0349 -0.0438 0.1211  236 LYS A CA    
1812 C  C     . LYS A 238 ? 0.5212 0.3891 0.3568 -0.0216 -0.0693 0.1129  236 LYS A C     
1813 O  O     . LYS A 238 ? 0.5252 0.3700 0.3462 -0.0446 -0.0457 0.1016  236 LYS A O     
1814 C  CB    . LYS A 238 ? 0.5860 0.4247 0.3653 -0.0244 -0.0132 0.1075  236 LYS A CB    
1815 C  CG    . LYS A 238 ? 0.5962 0.4979 0.4627 -0.0411 0.0271  0.1138  236 LYS A CG    
1816 C  CD    . LYS A 238 ? 0.6425 0.5660 0.4983 -0.0476 0.0532  0.1273  236 LYS A CD    
1817 C  CE    . LYS A 238 ? 0.6999 0.5944 0.4703 -0.0432 0.0759  0.1465  236 LYS A CE    
1818 N  NZ    . LYS A 238 ? 0.7465 0.6439 0.5642 -0.0239 0.0624  0.1201  236 LYS A NZ    
1819 N  N     . VAL A 239 ? 0.4349 0.3483 0.3448 -0.0177 -0.0778 0.0804  237 VAL A N     
1820 C  CA    . VAL A 239 ? 0.4581 0.3174 0.3574 -0.0118 -0.0926 0.0698  237 VAL A CA    
1821 C  C     . VAL A 239 ? 0.4555 0.3130 0.3816 -0.0037 -0.0902 0.0696  237 VAL A C     
1822 O  O     . VAL A 239 ? 0.4198 0.3023 0.3406 -0.0099 -0.1101 0.0555  237 VAL A O     
1823 C  CB    . VAL A 239 ? 0.3943 0.2925 0.3370 -0.0074 -0.0917 0.0490  237 VAL A CB    
1824 C  CG1   . VAL A 239 ? 0.4381 0.3409 0.3493 -0.0205 -0.0812 0.0385  237 VAL A CG1   
1825 C  CG2   . VAL A 239 ? 0.3773 0.2473 0.3251 -0.0122 -0.0853 0.0459  237 VAL A CG2   
1826 N  N     . ILE A 240 ? 0.4514 0.2785 0.3806 -0.0099 -0.1075 0.0757  238 ILE A N     
1827 C  CA    . ILE A 240 ? 0.4754 0.2874 0.3536 0.0231  -0.1131 0.0895  238 ILE A CA    
1828 C  C     . ILE A 240 ? 0.5149 0.2764 0.4034 0.0062  -0.1078 0.0923  238 ILE A C     
1829 O  O     . ILE A 240 ? 0.5407 0.3435 0.3928 0.0415  -0.1189 0.0726  238 ILE A O     
1830 C  CB    . ILE A 240 ? 0.5023 0.2850 0.3706 0.0056  -0.1376 0.1075  238 ILE A CB    
1831 C  CG1   . ILE A 240 ? 0.5026 0.3542 0.4619 -0.0167 -0.1478 0.0795  238 ILE A CG1   
1832 C  CG2   . ILE A 240 ? 0.4721 0.2898 0.4032 0.0275  -0.1556 0.0763  238 ILE A CG2   
1833 C  CD1   . ILE A 240 ? 0.5047 0.3456 0.4730 0.0143  -0.1917 0.0871  238 ILE A CD1   
1834 N  N     . GLU A 241 ? 0.5169 0.2797 0.4116 0.0041  -0.0967 0.0948  239 GLU A N     
1835 C  CA    . GLU A 241 ? 0.5645 0.3211 0.4080 0.0002  -0.0947 0.0956  239 GLU A CA    
1836 C  C     . GLU A 241 ? 0.5180 0.3198 0.3467 0.0028  -0.1218 0.1050  239 GLU A C     
1837 O  O     . GLU A 241 ? 0.4645 0.3249 0.3920 0.0552  -0.1635 0.0860  239 GLU A O     
1838 C  CB    . GLU A 241 ? 0.6057 0.3845 0.4531 -0.0243 -0.0740 0.1310  239 GLU A CB    
1839 C  CG    . GLU A 241 ? 0.6796 0.4824 0.5836 -0.0292 -0.0200 0.1519  239 GLU A CG    
1840 C  CD    . GLU A 241 ? 0.7114 0.5495 0.6358 -0.0048 0.0576  0.1362  239 GLU A CD    
1841 O  OE1   . GLU A 241 ? 0.7647 0.6902 0.6961 0.0042  0.0984  0.0274  239 GLU A OE1   
1842 O  OE2   . GLU A 241 ? 0.8195 0.6338 0.5149 -0.0455 0.0483  0.2023  239 GLU A OE2   
1843 N  N     . GLN A 242 ? 0.4790 0.3366 0.3478 0.0225  -0.1502 0.0759  240 GLN A N     
1844 C  CA    . GLN A 242 ? 0.4910 0.3488 0.3517 0.0199  -0.1376 0.0856  240 GLN A CA    
1845 C  C     . GLN A 242 ? 0.4882 0.3576 0.3527 0.0170  -0.1417 0.0808  240 GLN A C     
1846 O  O     . GLN A 242 ? 0.4965 0.3449 0.3865 0.0093  -0.1362 0.0424  240 GLN A O     
1847 C  CB    . GLN A 242 ? 0.5146 0.3668 0.3909 0.0169  -0.1148 0.0787  240 GLN A CB    
1848 C  CG    . GLN A 242 ? 0.5243 0.4428 0.4291 -0.0075 -0.0991 0.0980  240 GLN A CG    
1849 C  CD    . GLN A 242 ? 0.5762 0.4807 0.5522 -0.0005 -0.1042 0.1315  240 GLN A CD    
1850 O  OE1   . GLN A 242 ? 0.5754 0.5016 0.5592 -0.0205 -0.0419 0.1684  240 GLN A OE1   
1851 N  NE2   . GLN A 242 ? 0.5404 0.5439 0.6468 -0.0199 -0.1734 0.0570  240 GLN A NE2   
1852 N  N     . LEU A 243 ? 0.4165 0.3210 0.3443 0.0115  -0.1510 0.0563  241 LEU A N     
1853 C  CA    . LEU A 243 ? 0.4311 0.3359 0.3721 0.0196  -0.1528 0.0541  241 LEU A CA    
1854 C  C     . LEU A 243 ? 0.4093 0.3404 0.3426 0.0134  -0.1632 0.0465  241 LEU A C     
1855 O  O     . LEU A 243 ? 0.4080 0.3423 0.3819 0.0221  -0.1736 0.0564  241 LEU A O     
1856 C  CB    . LEU A 243 ? 0.4165 0.3285 0.3767 0.0080  -0.1451 0.0504  241 LEU A CB    
1857 C  CG    . LEU A 243 ? 0.4273 0.3113 0.3933 0.0117  -0.1171 0.0396  241 LEU A CG    
1858 C  CD1   . LEU A 243 ? 0.4138 0.2862 0.4075 0.0068  -0.0996 0.0703  241 LEU A CD1   
1859 C  CD2   . LEU A 243 ? 0.4248 0.3214 0.4356 -0.0119 -0.1019 0.0119  241 LEU A CD2   
1860 N  N     . GLY A 244 ? 0.3690 0.3295 0.3441 -0.0072 -0.1672 0.0514  242 GLY A N     
1861 C  CA    . GLY A 244 ? 0.3677 0.3801 0.3771 0.0075  -0.1597 0.0648  242 GLY A CA    
1862 C  C     . GLY A 244 ? 0.4104 0.3602 0.3889 0.0121  -0.1377 0.0756  242 GLY A C     
1863 O  O     . GLY A 244 ? 0.3998 0.3714 0.4244 0.0261  -0.1307 0.0476  242 GLY A O     
1864 N  N     . THR A 245 ? 0.3766 0.3921 0.4007 0.0312  -0.1474 0.0647  243 THR A N     
1865 C  CA    . THR A 245 ? 0.3900 0.3514 0.4311 -0.0045 -0.1467 0.0635  243 THR A CA    
1866 C  C     . THR A 245 ? 0.3803 0.3545 0.4614 0.0010  -0.1505 0.0531  243 THR A C     
1867 O  O     . THR A 245 ? 0.3282 0.4628 0.4216 0.0198  -0.2097 0.0575  243 THR A O     
1868 C  CB    . THR A 245 ? 0.4235 0.3299 0.4378 0.0025  -0.1653 0.0546  243 THR A CB    
1869 O  OG1   . THR A 245 ? 0.4688 0.3499 0.4493 0.0149  -0.1671 0.0877  243 THR A OG1   
1870 C  CG2   . THR A 245 ? 0.4345 0.3447 0.4797 -0.0016 -0.1679 0.0369  243 THR A CG2   
1871 N  N     . PRO A 246 ? 0.3516 0.3337 0.4361 0.0214  -0.1426 0.0580  244 PRO A N     
1872 C  CA    . PRO A 246 ? 0.3493 0.3704 0.4555 0.0181  -0.1203 0.0599  244 PRO A CA    
1873 C  C     . PRO A 246 ? 0.4000 0.3572 0.4950 0.0086  -0.1278 0.0493  244 PRO A C     
1874 O  O     . PRO A 246 ? 0.4180 0.3970 0.5504 0.0584  -0.1510 0.0333  244 PRO A O     
1875 C  CB    . PRO A 246 ? 0.3477 0.3593 0.4311 0.0305  -0.1117 0.0676  244 PRO A CB    
1876 C  CG    . PRO A 246 ? 0.3646 0.3789 0.4435 0.0267  -0.1221 0.0668  244 PRO A CG    
1877 C  CD    . PRO A 246 ? 0.3586 0.3494 0.4404 0.0106  -0.1081 0.0561  244 PRO A CD    
1878 N  N     . CYS A 247 ? 0.3915 0.3539 0.4851 -0.0021 -0.1285 0.0372  245 CYS A N     
1879 C  CA    . CYS A 247 ? 0.4061 0.3971 0.5863 -0.0034 -0.1231 0.0296  245 CYS A CA    
1880 C  C     . CYS A 247 ? 0.4258 0.4068 0.5862 0.0028  -0.0852 0.0502  245 CYS A C     
1881 O  O     . CYS A 247 ? 0.3932 0.3694 0.5753 0.0149  -0.0664 0.0487  245 CYS A O     
1882 C  CB    . CYS A 247 ? 0.4576 0.4233 0.6497 -0.0061 -0.0805 0.0536  245 CYS A CB    
1883 S  SG    . CYS A 247 ? 0.6809 0.5695 0.7272 -0.1733 -0.0340 -0.0058 245 CYS A SG    
1884 N  N     . PRO A 248 ? 0.3989 0.4678 0.6481 0.0383  -0.0914 0.0280  246 PRO A N     
1885 C  CA    . PRO A 248 ? 0.3876 0.4883 0.7020 -0.0255 -0.0954 0.0062  246 PRO A CA    
1886 C  C     . PRO A 248 ? 0.4552 0.5533 0.7034 -0.0319 -0.0389 0.0221  246 PRO A C     
1887 O  O     . PRO A 248 ? 0.4911 0.5499 0.6344 -0.0213 -0.0582 0.0126  246 PRO A O     
1888 C  CB    . PRO A 248 ? 0.4711 0.4867 0.7317 0.0078  -0.1160 -0.0085 246 PRO A CB    
1889 C  CG    . PRO A 248 ? 0.4222 0.4961 0.6744 0.0183  -0.1207 0.0081  246 PRO A CG    
1890 C  CD    . PRO A 248 ? 0.4136 0.4581 0.6472 0.0045  -0.1171 0.0039  246 PRO A CD    
1891 N  N     . GLU A 249 ? 0.5275 0.5208 0.7377 -0.0639 -0.0231 0.0153  247 GLU A N     
1892 C  CA    . GLU A 249 ? 0.5373 0.5490 0.7385 -0.0265 -0.0414 -0.0110 247 GLU A CA    
1893 C  C     . GLU A 249 ? 0.5496 0.4872 0.6544 -0.0166 -0.0263 -0.0028 247 GLU A C     
1894 O  O     . GLU A 249 ? 0.6440 0.4592 0.6662 -0.0435 0.0087  -0.0692 247 GLU A O     
1895 C  CB    . GLU A 249 ? 0.5675 0.5952 0.7974 -0.0264 -0.0067 0.0402  247 GLU A CB    
1896 C  CG    . GLU A 249 ? 0.5542 0.7014 0.9554 -0.0231 -0.0048 0.0691  247 GLU A CG    
1897 C  CD    . GLU A 249 ? 0.6104 0.8505 1.0691 0.0052  -0.0611 0.0674  247 GLU A CD    
1898 O  OE1   . GLU A 249 ? 0.5338 1.0244 0.9951 -0.0213 -0.0283 0.0132  247 GLU A OE1   
1899 O  OE2   . GLU A 249 ? 0.6861 1.0052 1.1507 -0.1261 -0.2300 0.0947  247 GLU A OE2   
1900 N  N     . PHE A 250 ? 0.4500 0.3673 0.5336 -0.0158 -0.0282 0.0431  248 PHE A N     
1901 C  CA    . PHE A 250 ? 0.3972 0.3646 0.4835 0.0042  -0.0607 0.0258  248 PHE A CA    
1902 C  C     . PHE A 250 ? 0.4391 0.3561 0.5428 0.0420  -0.0827 0.0094  248 PHE A C     
1903 O  O     . PHE A 250 ? 0.4422 0.3415 0.5348 0.0294  -0.1074 0.0198  248 PHE A O     
1904 C  CB    . PHE A 250 ? 0.3630 0.3480 0.4940 -0.0166 -0.1021 0.0007  248 PHE A CB    
1905 C  CG    . PHE A 250 ? 0.3831 0.3617 0.4837 0.0079  -0.0830 -0.0135 248 PHE A CG    
1906 C  CD1   . PHE A 250 ? 0.3699 0.4204 0.5401 0.0028  -0.0938 -0.0126 248 PHE A CD1   
1907 C  CD2   . PHE A 250 ? 0.3743 0.3193 0.4626 0.0341  -0.1056 -0.0347 248 PHE A CD2   
1908 C  CE1   . PHE A 250 ? 0.3652 0.3861 0.4806 0.0093  -0.0943 -0.0122 248 PHE A CE1   
1909 C  CE2   . PHE A 250 ? 0.3626 0.3968 0.4884 0.0046  -0.1128 -0.0225 248 PHE A CE2   
1910 C  CZ    . PHE A 250 ? 0.3559 0.3848 0.4560 -0.0003 -0.0826 0.0109  248 PHE A CZ    
1911 N  N     . MET A 251 ? 0.4422 0.3856 0.4844 0.0227  -0.0736 0.0149  249 MET A N     
1912 C  CA    . MET A 251 ? 0.4295 0.3586 0.5263 0.0186  -0.0608 -0.0027 249 MET A CA    
1913 C  C     . MET A 251 ? 0.3823 0.3773 0.4691 0.0192  -0.0752 0.0175  249 MET A C     
1914 O  O     . MET A 251 ? 0.3787 0.3385 0.4329 0.0464  -0.0876 -0.0026 249 MET A O     
1915 C  CB    . MET A 251 ? 0.4943 0.3987 0.5647 0.0095  -0.0826 0.0166  249 MET A CB    
1916 C  CG    . MET A 251 ? 0.5638 0.4923 0.6786 -0.0402 -0.0754 -0.0197 249 MET A CG    
1917 S  SD    . MET A 251 ? 0.6115 0.5753 0.7104 -0.0454 -0.0620 0.0401  249 MET A SD    
1918 C  CE    . MET A 251 ? 0.4981 0.5709 0.6200 -0.0346 -0.1744 0.2131  249 MET A CE    
1919 N  N     . LYS A 252 ? 0.3378 0.3742 0.5049 0.0508  -0.1039 -0.0177 250 LYS A N     
1920 C  CA    . LYS A 252 ? 0.3538 0.3641 0.4930 0.0741  -0.0868 -0.0247 250 LYS A CA    
1921 C  C     . LYS A 252 ? 0.3863 0.3609 0.4718 0.0805  -0.0634 -0.0091 250 LYS A C     
1922 O  O     . LYS A 252 ? 0.3735 0.3236 0.4940 0.0547  -0.0620 0.0100  250 LYS A O     
1923 C  CB    . LYS A 252 ? 0.4185 0.4271 0.5784 0.0755  -0.0887 -0.0595 250 LYS A CB    
1924 C  CG    . LYS A 252 ? 0.4169 0.5534 0.6564 0.1340  -0.1138 -0.0666 250 LYS A CG    
1925 C  CD    . LYS A 252 ? 0.5369 0.6689 0.8279 0.1005  -0.0373 -0.0827 250 LYS A CD    
1926 C  CE    . LYS A 252 ? 0.6165 0.7723 0.9675 0.0785  -0.0371 -0.0856 250 LYS A CE    
1927 N  NZ    . LYS A 252 ? 0.5687 0.8613 1.0142 0.1053  -0.0741 -0.0949 250 LYS A NZ    
1928 N  N     . LYS A 253 ? 0.3632 0.3396 0.4355 0.0612  -0.0358 -0.0017 251 LYS A N     
1929 C  CA    . LYS A 253 ? 0.3848 0.3898 0.4673 0.0749  -0.0248 -0.0021 251 LYS A CA    
1930 C  C     . LYS A 253 ? 0.4196 0.4010 0.4892 0.0561  -0.0323 0.0046  251 LYS A C     
1931 O  O     . LYS A 253 ? 0.4715 0.4570 0.4977 0.0812  -0.0411 0.0225  251 LYS A O     
1932 C  CB    . LYS A 253 ? 0.3917 0.4071 0.4816 0.0691  -0.0257 0.0113  251 LYS A CB    
1933 C  CG    . LYS A 253 ? 0.4146 0.4064 0.5320 0.0592  -0.0496 0.0029  251 LYS A CG    
1934 C  CD    . LYS A 253 ? 0.4553 0.4090 0.5582 0.0761  -0.0201 0.0093  251 LYS A CD    
1935 C  CE    . LYS A 253 ? 0.4882 0.4268 0.5992 0.0708  -0.0126 0.0050  251 LYS A CE    
1936 N  NZ    . LYS A 253 ? 0.5918 0.5122 0.6490 0.0364  0.0065  0.0534  251 LYS A NZ    
1937 N  N     . LEU A 254 ? 0.4075 0.3477 0.4676 0.0418  -0.0654 0.0324  252 LEU A N     
1938 C  CA    . LEU A 254 ? 0.4399 0.3594 0.4877 0.0246  -0.0645 0.0125  252 LEU A CA    
1939 C  C     . LEU A 254 ? 0.4684 0.3773 0.4894 0.0119  -0.0614 -0.0082 252 LEU A C     
1940 O  O     . LEU A 254 ? 0.4731 0.3926 0.4745 0.0140  -0.0546 0.0008  252 LEU A O     
1941 C  CB    . LEU A 254 ? 0.4408 0.3290 0.4903 0.0299  -0.0649 0.0013  252 LEU A CB    
1942 C  CG    . LEU A 254 ? 0.4484 0.3546 0.4905 0.0359  -0.0782 0.0088  252 LEU A CG    
1943 C  CD1   . LEU A 254 ? 0.4531 0.3625 0.5004 0.0303  -0.1109 0.0019  252 LEU A CD1   
1944 C  CD2   . LEU A 254 ? 0.4881 0.3293 0.4941 0.0778  -0.0569 0.0008  252 LEU A CD2   
1945 N  N     A GLN A 255 ? 0.4600 0.4124 0.4881 0.0097  -0.0693 -0.0121 253 GLN A N     
1946 N  N     B GLN A 255 ? 0.4584 0.3934 0.4885 0.0076  -0.0648 -0.0244 253 GLN A N     
1947 C  CA    A GLN A 255 ? 0.4528 0.4461 0.4893 -0.0140 -0.0851 0.0131  253 GLN A CA    
1948 C  CA    B GLN A 255 ? 0.4630 0.4268 0.5034 -0.0174 -0.0744 -0.0118 253 GLN A CA    
1949 C  C     A GLN A 255 ? 0.4625 0.4173 0.4942 -0.0317 -0.0856 0.0034  253 GLN A C     
1950 C  C     B GLN A 255 ? 0.4676 0.4137 0.5026 -0.0348 -0.0806 -0.0110 253 GLN A C     
1951 O  O     A GLN A 255 ? 0.4340 0.4044 0.4536 -0.0628 -0.0735 -0.0037 253 GLN A O     
1952 O  O     B GLN A 255 ? 0.4367 0.3942 0.4569 -0.0697 -0.0770 -0.0110 253 GLN A O     
1953 C  CB    A GLN A 255 ? 0.4552 0.4913 0.5069 0.0038  -0.0924 0.0178  253 GLN A CB    
1954 C  CB    B GLN A 255 ? 0.4657 0.4618 0.5460 -0.0065 -0.0742 -0.0340 253 GLN A CB    
1955 C  CG    A GLN A 255 ? 0.4281 0.5168 0.5234 0.0200  -0.0985 0.0364  253 GLN A CG    
1956 C  CG    B GLN A 255 ? 0.4603 0.4878 0.5779 0.0170  -0.0658 -0.0450 253 GLN A CG    
1957 C  CD    A GLN A 255 ? 0.4309 0.6083 0.5239 0.0837  -0.1266 0.0279  253 GLN A CD    
1958 C  CD    B GLN A 255 ? 0.4772 0.5219 0.6436 0.0255  -0.0500 -0.0560 253 GLN A CD    
1959 O  OE1   A GLN A 255 ? 0.3962 0.6445 0.5574 0.1553  -0.1342 -0.0189 253 GLN A OE1   
1960 O  OE1   B GLN A 255 ? 0.4904 0.6201 0.6677 0.1275  -0.0777 -0.0594 253 GLN A OE1   
1961 N  NE2   A GLN A 255 ? 0.3925 0.6294 0.4849 0.0984  -0.1338 0.0720  253 GLN A NE2   
1962 N  NE2   B GLN A 255 ? 0.4958 0.4955 0.6641 0.0062  -0.0306 -0.0830 253 GLN A NE2   
1963 N  N     . PRO A 256 ? 0.5099 0.4163 0.5041 -0.0232 -0.0813 -0.0097 254 PRO A N     
1964 C  CA    . PRO A 256 ? 0.5344 0.4149 0.5880 -0.0461 -0.0786 -0.0193 254 PRO A CA    
1965 C  C     . PRO A 256 ? 0.5558 0.3637 0.6013 -0.0530 -0.0764 -0.0219 254 PRO A C     
1966 O  O     . PRO A 256 ? 0.5684 0.3415 0.5752 -0.0485 -0.0620 0.0245  254 PRO A O     
1967 C  CB    . PRO A 256 ? 0.5638 0.4127 0.5903 -0.0294 -0.0826 -0.0361 254 PRO A CB    
1968 C  CG    . PRO A 256 ? 0.5537 0.4252 0.5608 -0.0162 -0.0971 -0.0208 254 PRO A CG    
1969 C  CD    . PRO A 256 ? 0.5711 0.3912 0.5596 -0.0378 -0.0992 -0.0272 254 PRO A CD    
1970 N  N     . THR A 257 ? 0.5505 0.4434 0.6185 -0.0920 -0.0748 -0.0903 255 THR A N     
1971 C  CA    . THR A 257 ? 0.5698 0.4701 0.6406 -0.0873 -0.0705 -0.0460 255 THR A CA    
1972 C  C     . THR A 257 ? 0.5559 0.4377 0.5858 -0.0849 -0.0824 -0.0178 255 THR A C     
1973 O  O     . THR A 257 ? 0.5682 0.4594 0.6046 -0.1338 -0.0505 0.0026  255 THR A O     
1974 C  CB    . THR A 257 ? 0.5733 0.5396 0.6901 -0.0727 -0.0678 -0.0633 255 THR A CB    
1975 O  OG1   . THR A 257 ? 0.6097 0.6112 0.8551 -0.0997 -0.0586 -0.1270 255 THR A OG1   
1976 C  CG2   . THR A 257 ? 0.5756 0.5108 0.7084 -0.0237 -0.1020 -0.0235 255 THR A CG2   
1977 N  N     . VAL A 258 ? 0.4824 0.4358 0.5812 -0.0684 -0.0849 0.0064  256 VAL A N     
1978 C  CA    . VAL A 258 ? 0.4810 0.4590 0.5516 -0.0306 -0.0774 -0.0131 256 VAL A CA    
1979 C  C     . VAL A 258 ? 0.4464 0.4043 0.5383 -0.0283 -0.0720 -0.0046 256 VAL A C     
1980 O  O     . VAL A 258 ? 0.4247 0.3745 0.4499 0.0067  -0.0715 0.0631  256 VAL A O     
1981 C  CB    . VAL A 258 ? 0.4552 0.4327 0.5920 -0.0182 -0.0892 -0.0089 256 VAL A CB    
1982 C  CG1   . VAL A 258 ? 0.4419 0.3883 0.5571 0.0158  -0.0714 0.0282  256 VAL A CG1   
1983 C  CG2   . VAL A 258 ? 0.5307 0.4761 0.5997 0.0091  -0.0975 -0.0157 256 VAL A CG2   
1984 N  N     . ARG A 259 ? 0.5065 0.3525 0.5787 -0.0252 -0.1181 -0.0346 257 ARG A N     
1985 C  CA    . ARG A 259 ? 0.4903 0.3386 0.5723 -0.0231 -0.1120 -0.0040 257 ARG A CA    
1986 C  C     . ARG A 259 ? 0.5199 0.3279 0.5725 -0.0380 -0.1079 0.0290  257 ARG A C     
1987 O  O     . ARG A 259 ? 0.5286 0.3924 0.5421 -0.0123 -0.1225 0.0553  257 ARG A O     
1988 C  CB    . ARG A 259 ? 0.5009 0.3187 0.5647 0.0106  -0.1031 0.0252  257 ARG A CB    
1989 C  CG    . ARG A 259 ? 0.4990 0.3645 0.5782 0.0246  -0.0871 0.0442  257 ARG A CG    
1990 C  CD    . ARG A 259 ? 0.5541 0.4534 0.6229 0.0271  -0.0758 0.0174  257 ARG A CD    
1991 N  NE    . ARG A 259 ? 0.6113 0.5426 0.6442 0.0697  -0.0902 0.0033  257 ARG A NE    
1992 C  CZ    . ARG A 259 ? 0.7354 0.7398 0.6756 0.0947  -0.0827 0.0080  257 ARG A CZ    
1993 N  NH1   . ARG A 259 ? 0.9228 0.7646 0.6688 0.1199  -0.1301 0.0129  257 ARG A NH1   
1994 N  NH2   . ARG A 259 ? 0.6379 0.7335 0.6610 0.1496  -0.0784 0.0460  257 ARG A NH2   
1995 N  N     . THR A 260 ? 0.5376 0.3409 0.5744 -0.0559 -0.1100 0.0433  258 THR A N     
1996 C  CA    . THR A 260 ? 0.5866 0.3813 0.5959 -0.0534 -0.1369 0.0567  258 THR A CA    
1997 C  C     . THR A 260 ? 0.5753 0.3913 0.5836 -0.0675 -0.0989 0.0868  258 THR A C     
1998 O  O     . THR A 260 ? 0.6987 0.4225 0.5111 -0.0880 -0.1103 0.1000  258 THR A O     
1999 C  CB    . THR A 260 ? 0.6218 0.4149 0.6800 -0.0653 -0.1083 0.0100  258 THR A CB    
2000 O  OG1   . THR A 260 ? 0.7228 0.5434 0.7770 -0.1390 -0.0912 0.0023  258 THR A OG1   
2001 C  CG2   . THR A 260 ? 0.6144 0.3927 0.6521 -0.0229 -0.1426 0.0351  258 THR A CG2   
2002 N  N     . TYR A 261 ? 0.5676 0.3727 0.5823 -0.0565 -0.0661 0.0985  259 TYR A N     
2003 C  CA    . TYR A 261 ? 0.5591 0.3817 0.5312 -0.0714 -0.0630 0.0975  259 TYR A CA    
2004 C  C     . TYR A 261 ? 0.5477 0.3946 0.5181 -0.0523 -0.0867 0.0878  259 TYR A C     
2005 O  O     . TYR A 261 ? 0.6339 0.4663 0.5250 -0.0721 -0.0375 0.0841  259 TYR A O     
2006 C  CB    . TYR A 261 ? 0.5269 0.4311 0.5561 -0.0624 -0.0350 0.0766  259 TYR A CB    
2007 C  CG    . TYR A 261 ? 0.6168 0.4278 0.5922 -0.0870 -0.0235 0.0918  259 TYR A CG    
2008 C  CD1   . TYR A 261 ? 0.5924 0.4126 0.6437 -0.1263 0.0308  0.1151  259 TYR A CD1   
2009 C  CD2   . TYR A 261 ? 0.5786 0.4075 0.6343 -0.0996 0.0105  0.1375  259 TYR A CD2   
2010 C  CE1   . TYR A 261 ? 0.6094 0.3592 0.6405 -0.1111 0.0655  0.1293  259 TYR A CE1   
2011 C  CE2   . TYR A 261 ? 0.6519 0.3607 0.6555 -0.0933 0.0344  0.1294  259 TYR A CE2   
2012 C  CZ    . TYR A 261 ? 0.6558 0.3971 0.6454 -0.0704 0.0922  0.1041  259 TYR A CZ    
2013 O  OH    . TYR A 261 ? 0.6744 0.2844 0.5917 -0.0303 0.1021  0.1060  259 TYR A OH    
2014 N  N     . VAL A 262 ? 0.5205 0.4448 0.4446 -0.0630 -0.1071 0.0588  260 VAL A N     
2015 C  CA    . VAL A 262 ? 0.5148 0.3951 0.4213 -0.0370 -0.0981 0.0474  260 VAL A CA    
2016 C  C     . VAL A 262 ? 0.5032 0.4085 0.4866 -0.0200 -0.1123 0.0401  260 VAL A C     
2017 O  O     . VAL A 262 ? 0.5150 0.3633 0.4492 0.0191  -0.1476 0.0745  260 VAL A O     
2018 C  CB    . VAL A 262 ? 0.5055 0.4429 0.3868 -0.0251 -0.0916 0.0365  260 VAL A CB    
2019 C  CG1   . VAL A 262 ? 0.5336 0.4931 0.3669 -0.0355 -0.1297 0.0358  260 VAL A CG1   
2020 C  CG2   . VAL A 262 ? 0.5214 0.5166 0.3401 -0.0223 -0.0771 0.0183  260 VAL A CG2   
2021 N  N     . GLU A 263 ? 0.5532 0.3596 0.5291 -0.0179 -0.1414 0.0669  261 GLU A N     
2022 C  CA    . GLU A 263 ? 0.5560 0.4049 0.5940 0.0090  -0.1403 0.0747  261 GLU A CA    
2023 C  C     . GLU A 263 ? 0.5710 0.4242 0.5969 0.0231  -0.1549 0.1105  261 GLU A C     
2024 O  O     . GLU A 263 ? 0.5439 0.4697 0.6636 0.0631  -0.1876 0.1205  261 GLU A O     
2025 C  CB    . GLU A 263 ? 0.5871 0.3411 0.6327 0.0109  -0.1516 0.0509  261 GLU A CB    
2026 C  CG    . GLU A 263 ? 0.6303 0.4008 0.6675 0.0337  -0.1527 0.0814  261 GLU A CG    
2027 C  CD    . GLU A 263 ? 0.6804 0.4915 0.7685 0.0487  -0.1305 0.1184  261 GLU A CD    
2028 O  OE1   . GLU A 263 ? 0.7465 0.5407 0.7916 0.1555  -0.2032 0.1429  261 GLU A OE1   
2029 O  OE2   . GLU A 263 ? 0.6707 0.5565 0.8283 0.0726  -0.1315 0.1400  261 GLU A OE2   
2030 N  N     . ASN A 264 ? 0.6401 0.3897 0.5443 -0.0211 -0.1274 0.1056  262 ASN A N     
2031 C  CA    . ASN A 264 ? 0.7025 0.4019 0.5799 0.0094  -0.1337 0.1155  262 ASN A CA    
2032 C  C     . ASN A 264 ? 0.7611 0.4133 0.5387 0.0042  -0.1499 0.1391  262 ASN A C     
2033 O  O     . ASN A 264 ? 0.7693 0.4464 0.5589 0.0440  -0.1974 0.1539  262 ASN A O     
2034 C  CB    . ASN A 264 ? 0.7279 0.3632 0.6744 0.0212  -0.1409 0.0993  262 ASN A CB    
2035 C  CG    . ASN A 264 ? 0.7454 0.4621 0.7823 -0.0046 -0.1191 0.0336  262 ASN A CG    
2036 O  OD1   . ASN A 264 ? 0.7678 0.5278 0.7997 0.0209  -0.1486 -0.0033 262 ASN A OD1   
2037 N  ND2   . ASN A 264 ? 0.7761 0.4630 0.8489 -0.0423 -0.1183 0.0087  262 ASN A ND2   
2038 N  N     . ARG A 265 ? 0.6775 0.4054 0.4543 0.0112  -0.1793 0.1424  263 ARG A N     
2039 C  CA    . ARG A 265 ? 0.6105 0.4430 0.4238 0.0183  -0.1247 0.1570  263 ARG A CA    
2040 C  C     . ARG A 265 ? 0.6106 0.4627 0.4371 -0.0315 -0.1565 0.1170  263 ARG A C     
2041 O  O     . ARG A 265 ? 0.5848 0.4560 0.4850 0.0134  -0.2380 0.0373  263 ARG A O     
2042 C  CB    . ARG A 265 ? 0.6166 0.4084 0.4522 0.0072  -0.0979 0.1424  263 ARG A CB    
2043 C  CG    . ARG A 265 ? 0.6156 0.5036 0.5614 0.0135  -0.0915 0.0975  263 ARG A CG    
2044 C  CD    . ARG A 265 ? 0.6249 0.5479 0.5743 -0.0064 -0.0667 0.1146  263 ARG A CD    
2045 N  NE    . ARG A 265 ? 0.6784 0.5851 0.6151 -0.0034 -0.0198 0.1480  263 ARG A NE    
2046 C  CZ    . ARG A 265 ? 0.6944 0.6482 0.6893 0.0175  0.0255  0.1586  263 ARG A CZ    
2047 N  NH1   . ARG A 265 ? 0.7195 0.6707 0.6686 0.0281  0.0368  0.0912  263 ARG A NH1   
2048 N  NH2   . ARG A 265 ? 0.5818 0.6706 0.6888 0.0672  0.0328  0.2848  263 ARG A NH2   
2049 N  N     . PRO A 266 ? 0.6452 0.5496 0.4891 -0.0404 -0.1657 0.1013  264 PRO A N     
2050 C  CA    . PRO A 266 ? 0.6687 0.4955 0.4342 -0.0645 -0.1689 0.1246  264 PRO A CA    
2051 C  C     . PRO A 266 ? 0.5878 0.4329 0.4839 -0.0203 -0.1954 0.1131  264 PRO A C     
2052 O  O     . PRO A 266 ? 0.5343 0.3663 0.4086 -0.0239 -0.1868 0.0885  264 PRO A O     
2053 C  CB    . PRO A 266 ? 0.7140 0.5792 0.5230 -0.0851 -0.1582 0.1027  264 PRO A CB    
2054 C  CG    . PRO A 266 ? 0.7255 0.6451 0.5367 -0.0502 -0.1844 0.0756  264 PRO A CG    
2055 C  CD    . PRO A 266 ? 0.6900 0.6076 0.5055 -0.0326 -0.1722 0.1118  264 PRO A CD    
2056 N  N     . LYS A 267 ? 0.5688 0.4506 0.4635 0.0222  -0.2193 0.1312  265 LYS A N     
2057 C  CA    . LYS A 267 ? 0.5448 0.3915 0.5358 0.0315  -0.2049 0.0724  265 LYS A CA    
2058 C  C     . LYS A 267 ? 0.5031 0.4223 0.4794 0.0240  -0.2338 0.0485  265 LYS A C     
2059 O  O     . LYS A 267 ? 0.4930 0.4239 0.4552 0.0786  -0.2125 0.0565  265 LYS A O     
2060 C  CB    . LYS A 267 ? 0.5426 0.4367 0.5531 0.0448  -0.1961 0.0560  265 LYS A CB    
2061 C  CG    . LYS A 267 ? 0.6294 0.4841 0.5562 0.0181  -0.1758 -0.0216 265 LYS A CG    
2062 C  CD    . LYS A 267 ? 0.7168 0.4949 0.5744 0.0546  -0.1751 -0.0251 265 LYS A CD    
2063 C  CE    . LYS A 267 ? 0.8332 0.5605 0.6314 0.0481  -0.1435 -0.1053 265 LYS A CE    
2064 N  NZ    . LYS A 267 ? 0.8741 0.5817 0.6144 0.0642  -0.1331 -0.1775 265 LYS A NZ    
2065 N  N     . TYR A 268 ? 0.4931 0.3876 0.4243 0.0087  -0.2520 0.0491  266 TYR A N     
2066 C  CA    . TYR A 268 ? 0.5428 0.3895 0.4501 0.0111  -0.2286 0.0578  266 TYR A CA    
2067 C  C     . TYR A 268 ? 0.5051 0.3885 0.4325 0.0285  -0.2429 0.0867  266 TYR A C     
2068 O  O     . TYR A 268 ? 0.4737 0.3629 0.4424 0.0292  -0.2395 0.0691  266 TYR A O     
2069 C  CB    . TYR A 268 ? 0.5407 0.3938 0.4722 0.0188  -0.2171 0.0846  266 TYR A CB    
2070 C  CG    . TYR A 268 ? 0.6235 0.4247 0.4688 -0.0115 -0.1784 0.0927  266 TYR A CG    
2071 C  CD1   . TYR A 268 ? 0.6662 0.4359 0.4713 -0.0185 -0.1760 0.0648  266 TYR A CD1   
2072 C  CD2   . TYR A 268 ? 0.5973 0.4859 0.5238 -0.0505 -0.1686 0.0757  266 TYR A CD2   
2073 C  CE1   . TYR A 268 ? 0.6519 0.5333 0.5352 -0.0274 -0.1525 0.0460  266 TYR A CE1   
2074 C  CE2   . TYR A 268 ? 0.6432 0.4831 0.4672 -0.0633 -0.1751 0.0727  266 TYR A CE2   
2075 C  CZ    . TYR A 268 ? 0.6339 0.5040 0.5022 -0.0312 -0.1632 0.0977  266 TYR A CZ    
2076 O  OH    . TYR A 268 ? 0.6154 0.5501 0.5308 -0.0281 -0.1803 0.1854  266 TYR A OH    
2077 N  N     . ALA A 269 ? 0.5160 0.3583 0.4591 0.0209  -0.2476 0.0717  267 ALA A N     
2078 C  CA    . ALA A 269 ? 0.4763 0.3886 0.4585 0.0292  -0.2570 0.0868  267 ALA A CA    
2079 C  C     . ALA A 269 ? 0.4859 0.3529 0.4760 -0.0021 -0.2425 0.0740  267 ALA A C     
2080 O  O     . ALA A 269 ? 0.4985 0.4002 0.4527 0.0165  -0.2420 0.0744  267 ALA A O     
2081 C  CB    . ALA A 269 ? 0.5200 0.4088 0.4915 0.0313  -0.2524 0.0173  267 ALA A CB    
2082 N  N     . GLY A 270 ? 0.4643 0.3572 0.4205 0.0366  -0.2371 0.0549  268 GLY A N     
2083 C  CA    . GLY A 270 ? 0.5124 0.4178 0.5003 0.0362  -0.2027 0.0063  268 GLY A CA    
2084 C  C     . GLY A 270 ? 0.4672 0.4067 0.4244 0.0087  -0.2437 0.0202  268 GLY A C     
2085 O  O     . GLY A 270 ? 0.5191 0.4193 0.4249 0.0334  -0.2483 0.0006  268 GLY A O     
2086 N  N     . TYR A 271 ? 0.4711 0.4175 0.4004 0.0063  -0.2365 0.0129  269 TYR A N     
2087 C  CA    . TYR A 271 ? 0.4891 0.3959 0.3990 0.0481  -0.2360 0.0249  269 TYR A CA    
2088 C  C     . TYR A 271 ? 0.4956 0.4428 0.4118 0.0249  -0.2294 0.0108  269 TYR A C     
2089 O  O     . TYR A 271 ? 0.5040 0.4093 0.4018 0.0050  -0.2188 0.0408  269 TYR A O     
2090 C  CB    . TYR A 271 ? 0.5926 0.4711 0.4291 -0.0004 -0.2041 0.0244  269 TYR A CB    
2091 C  CG    . TYR A 271 ? 0.6420 0.4983 0.4702 -0.0138 -0.1719 0.0314  269 TYR A CG    
2092 C  CD1   . TYR A 271 ? 0.6628 0.5211 0.4883 -0.0049 -0.1856 0.0114  269 TYR A CD1   
2093 C  CD2   . TYR A 271 ? 0.6539 0.5414 0.4440 -0.0126 -0.1474 0.0253  269 TYR A CD2   
2094 C  CE1   . TYR A 271 ? 0.7166 0.5458 0.4893 -0.0136 -0.1586 0.0365  269 TYR A CE1   
2095 C  CE2   . TYR A 271 ? 0.7304 0.4758 0.4641 0.0058  -0.1253 0.0069  269 TYR A CE2   
2096 C  CZ    . TYR A 271 ? 0.7597 0.5543 0.4952 0.0037  -0.1464 0.0236  269 TYR A CZ    
2097 O  OH    . TYR A 271 ? 0.8940 0.6389 0.5182 0.0055  -0.0676 0.0380  269 TYR A OH    
2098 N  N     . SER A 272 ? 0.4725 0.4315 0.3935 0.0289  -0.2830 0.0306  270 SER A N     
2099 C  CA    . SER A 272 ? 0.5087 0.4744 0.4335 -0.0099 -0.2571 0.0240  270 SER A CA    
2100 C  C     . SER A 272 ? 0.5045 0.4179 0.4199 -0.0082 -0.2410 0.0223  270 SER A C     
2101 O  O     . SER A 272 ? 0.5258 0.3948 0.4334 0.0192  -0.2319 0.0070  270 SER A O     
2102 C  CB    . SER A 272 ? 0.5347 0.4861 0.4145 -0.0159 -0.2660 0.0030  270 SER A CB    
2103 O  OG    . SER A 272 ? 0.5389 0.4648 0.4386 -0.0139 -0.2921 -0.0278 270 SER A OG    
2104 N  N     . PHE A 273 ? 0.4480 0.4174 0.3762 -0.0408 -0.2469 -0.0026 271 PHE A N     
2105 C  CA    . PHE A 273 ? 0.4600 0.4142 0.4121 -0.0106 -0.2090 -0.0078 271 PHE A CA    
2106 C  C     . PHE A 273 ? 0.5281 0.4695 0.4284 -0.0117 -0.2380 -0.0039 271 PHE A C     
2107 O  O     . PHE A 273 ? 0.5681 0.4848 0.3692 0.0011  -0.2107 -0.0165 271 PHE A O     
2108 C  CB    . PHE A 273 ? 0.4245 0.4019 0.4130 0.0066  -0.1701 -0.0210 271 PHE A CB    
2109 C  CG    . PHE A 273 ? 0.4148 0.3945 0.4043 -0.0254 -0.1522 -0.0051 271 PHE A CG    
2110 C  CD1   . PHE A 273 ? 0.4229 0.3696 0.4104 -0.0410 -0.1360 0.0126  271 PHE A CD1   
2111 C  CD2   . PHE A 273 ? 0.4208 0.3906 0.3874 -0.0279 -0.1393 -0.0053 271 PHE A CD2   
2112 C  CE1   . PHE A 273 ? 0.3798 0.3626 0.3876 -0.0351 -0.1295 0.0015  271 PHE A CE1   
2113 C  CE2   . PHE A 273 ? 0.3970 0.4054 0.3607 -0.0280 -0.1443 0.0105  271 PHE A CE2   
2114 C  CZ    . PHE A 273 ? 0.3907 0.3661 0.3368 -0.0312 -0.1577 0.0102  271 PHE A CZ    
2115 N  N     . GLU A 274 ? 0.5144 0.4177 0.4479 -0.0445 -0.2357 0.0293  272 GLU A N     
2116 C  CA    . GLU A 274 ? 0.5674 0.4087 0.4684 -0.0266 -0.2467 0.0131  272 GLU A CA    
2117 C  C     . GLU A 274 ? 0.6070 0.4213 0.4616 -0.0161 -0.2630 -0.0208 272 GLU A C     
2118 O  O     . GLU A 274 ? 0.6478 0.3894 0.3935 0.0063  -0.2657 -0.0625 272 GLU A O     
2119 C  CB    . GLU A 274 ? 0.5984 0.5102 0.5153 -0.0494 -0.2796 0.0156  272 GLU A CB    
2120 C  CG    . GLU A 274 ? 0.6626 0.5548 0.5789 -0.0339 -0.2734 0.0633  272 GLU A CG    
2121 C  CD    . GLU A 274 ? 0.6628 0.5716 0.6298 -0.0284 -0.2219 0.1017  272 GLU A CD    
2122 O  OE1   . GLU A 274 ? 0.5980 0.5562 0.6796 0.0087  -0.2312 0.1467  272 GLU A OE1   
2123 O  OE2   . GLU A 274 ? 0.7403 0.6036 0.7735 -0.0202 -0.1598 0.2515  272 GLU A OE2   
2124 N  N     . LYS A 275 ? 0.5967 0.4375 0.4283 -0.0083 -0.2773 -0.0437 273 LYS A N     
2125 C  CA    . LYS A 275 ? 0.6057 0.4763 0.3966 -0.0106 -0.2441 -0.0119 273 LYS A CA    
2126 C  C     . LYS A 275 ? 0.6260 0.4688 0.3703 -0.0126 -0.2064 -0.0124 273 LYS A C     
2127 O  O     . LYS A 275 ? 0.5907 0.5225 0.3902 -0.0087 -0.1930 0.0186  273 LYS A O     
2128 C  CB    . LYS A 275 ? 0.6903 0.4902 0.4698 -0.0399 -0.1946 -0.0597 273 LYS A CB    
2129 C  CG    . LYS A 275 ? 0.7777 0.6510 0.5305 -0.0662 -0.1647 -0.0186 273 LYS A CG    
2130 C  CD    . LYS A 275 ? 0.8715 0.7742 0.6869 -0.0638 -0.1782 0.0492  273 LYS A CD    
2131 C  CE    . LYS A 275 ? 0.9763 0.9055 0.6989 -0.1123 -0.1001 0.0914  273 LYS A CE    
2132 N  NZ    . LYS A 275 ? 0.9832 0.9864 0.7749 -0.1218 -0.0552 0.1517  273 LYS A NZ    
2133 N  N     . LEU A 276 ? 0.5704 0.4385 0.3501 -0.0116 -0.1948 0.0022  274 LEU A N     
2134 C  CA    . LEU A 276 ? 0.5615 0.4305 0.3637 -0.0071 -0.1492 0.0310  274 LEU A CA    
2135 C  C     . LEU A 276 ? 0.6076 0.4266 0.3484 0.0021  -0.1432 0.0222  274 LEU A C     
2136 O  O     . LEU A 276 ? 0.6338 0.4334 0.3929 0.0146  -0.1459 0.0370  274 LEU A O     
2137 C  CB    . LEU A 276 ? 0.5480 0.3917 0.3750 -0.0297 -0.1841 0.0153  274 LEU A CB    
2138 C  CG    . LEU A 276 ? 0.5964 0.3929 0.3724 -0.0318 -0.1876 0.0174  274 LEU A CG    
2139 C  CD1   . LEU A 276 ? 0.5765 0.4232 0.4093 -0.0400 -0.1873 0.0103  274 LEU A CD1   
2140 C  CD2   . LEU A 276 ? 0.6146 0.4121 0.4451 -0.0357 -0.1563 0.0054  274 LEU A CD2   
2141 N  N     . PHE A 277 ? 0.5872 0.3586 0.3211 -0.0102 -0.1811 -0.0372 275 PHE A N     
2142 C  CA    . PHE A 277 ? 0.6251 0.4191 0.3359 -0.0095 -0.1887 -0.0282 275 PHE A CA    
2143 C  C     . PHE A 277 ? 0.6303 0.4041 0.3591 -0.0101 -0.2368 -0.0449 275 PHE A C     
2144 O  O     . PHE A 277 ? 0.6097 0.3892 0.4107 -0.0231 -0.2618 -0.0792 275 PHE A O     
2145 C  CB    . PHE A 277 ? 0.5956 0.4444 0.3130 0.0044  -0.1972 -0.0297 275 PHE A CB    
2146 C  CG    . PHE A 277 ? 0.5472 0.4027 0.2716 0.0194  -0.1743 -0.0200 275 PHE A CG    
2147 C  CD1   . PHE A 277 ? 0.5476 0.4006 0.2674 0.0140  -0.1463 -0.0258 275 PHE A CD1   
2148 C  CD2   . PHE A 277 ? 0.5523 0.4000 0.3410 0.0472  -0.2020 -0.0271 275 PHE A CD2   
2149 C  CE1   . PHE A 277 ? 0.5275 0.4242 0.2424 0.0127  -0.1468 -0.0205 275 PHE A CE1   
2150 C  CE2   . PHE A 277 ? 0.5200 0.3770 0.3499 0.0359  -0.1776 -0.0236 275 PHE A CE2   
2151 C  CZ    . PHE A 277 ? 0.4847 0.3545 0.2394 0.0247  -0.1794 -0.0201 275 PHE A CZ    
2152 N  N     . PRO A 278 ? 0.6901 0.4175 0.3810 0.0216  -0.2473 -0.0639 276 PRO A N     
2153 C  CA    . PRO A 278 ? 0.7871 0.3673 0.3871 0.0380  -0.2626 -0.0933 276 PRO A CA    
2154 C  C     . PRO A 278 ? 0.8104 0.4480 0.4652 0.0784  -0.2935 -0.0834 276 PRO A C     
2155 O  O     . PRO A 278 ? 0.7595 0.4762 0.4313 0.0320  -0.2985 -0.0846 276 PRO A O     
2156 C  CB    . PRO A 278 ? 0.8448 0.3896 0.4562 0.0293  -0.2050 -0.0884 276 PRO A CB    
2157 C  CG    . PRO A 278 ? 0.7833 0.4534 0.3892 -0.0098 -0.2165 -0.0626 276 PRO A CG    
2158 C  CD    . PRO A 278 ? 0.6753 0.4284 0.3803 0.0378  -0.2140 -0.0299 276 PRO A CD    
2159 N  N     . ASP A 279 ? 0.7988 0.4765 0.5083 0.0651  -0.3076 -0.0859 277 ASP A N     
2160 C  CA    . ASP A 279 ? 0.8896 0.5227 0.5935 0.0581  -0.2695 -0.1079 277 ASP A CA    
2161 C  C     . ASP A 279 ? 0.9225 0.5030 0.5202 0.0567  -0.2354 -0.0880 277 ASP A C     
2162 O  O     . ASP A 279 ? 0.8985 0.4910 0.4339 0.0525  -0.2794 -0.1161 277 ASP A O     
2163 C  CB    . ASP A 279 ? 0.9269 0.6237 0.7184 0.0113  -0.2413 -0.1015 277 ASP A CB    
2164 C  CG    . ASP A 279 ? 1.0265 0.7051 0.8150 0.0366  -0.1857 -0.0496 277 ASP A CG    
2165 O  OD1   . ASP A 279 ? 1.0449 0.5384 0.8547 0.0189  -0.2192 0.0188  277 ASP A OD1   
2166 O  OD2   . ASP A 279 ? 1.0852 0.9020 0.9140 0.0503  -0.2130 0.0409  277 ASP A OD2   
2167 N  N     . VAL A 280 ? 0.9357 0.5331 0.4472 0.0944  -0.2423 -0.0789 278 VAL A N     
2168 C  CA    . VAL A 280 ? 0.9514 0.4771 0.4432 0.1233  -0.2259 -0.0918 278 VAL A CA    
2169 C  C     . VAL A 280 ? 0.9357 0.5256 0.4066 0.1411  -0.2250 -0.0747 278 VAL A C     
2170 O  O     . VAL A 280 ? 0.9223 0.4837 0.3788 0.1322  -0.2369 -0.0864 278 VAL A O     
2171 C  CB    . VAL A 280 ? 1.0197 0.5128 0.4503 0.1478  -0.1888 -0.0524 278 VAL A CB    
2172 C  CG1   . VAL A 280 ? 1.0505 0.5298 0.4872 0.1338  -0.1957 -0.0670 278 VAL A CG1   
2173 C  CG2   . VAL A 280 ? 1.0559 0.5463 0.5026 0.1667  -0.1497 -0.0011 278 VAL A CG2   
2174 N  N     . LEU A 281 ? 0.8896 0.5753 0.4202 0.1015  -0.2305 -0.0841 279 LEU A N     
2175 C  CA    . LEU A 281 ? 0.8500 0.5676 0.3628 0.0810  -0.2067 -0.0938 279 LEU A CA    
2176 C  C     . LEU A 281 ? 0.8589 0.5567 0.3706 0.0943  -0.2091 -0.0849 279 LEU A C     
2177 O  O     . LEU A 281 ? 0.8594 0.5534 0.3455 0.1547  -0.2146 -0.1081 279 LEU A O     
2178 C  CB    . LEU A 281 ? 0.7913 0.5330 0.3534 0.0593  -0.2058 -0.0855 279 LEU A CB    
2179 C  CG    . LEU A 281 ? 0.7998 0.5887 0.4105 0.0277  -0.1939 -0.0691 279 LEU A CG    
2180 C  CD1   . LEU A 281 ? 0.8019 0.5753 0.4332 0.0341  -0.2211 -0.0638 279 LEU A CD1   
2181 C  CD2   . LEU A 281 ? 0.8633 0.6635 0.4814 0.0296  -0.1694 -0.0483 279 LEU A CD2   
2182 N  N     . PHE A 282 ? 0.8393 0.5833 0.2934 0.0880  -0.2027 -0.1143 280 PHE A N     
2183 C  CA    . PHE A 282 ? 0.8536 0.5938 0.3812 0.0763  -0.1800 -0.0788 280 PHE A CA    
2184 C  C     . PHE A 282 ? 0.9337 0.6182 0.3668 0.0934  -0.1851 -0.0793 280 PHE A C     
2185 O  O     . PHE A 282 ? 0.9989 0.6227 0.3878 0.1317  -0.2677 -0.1121 280 PHE A O     
2186 C  CB    . PHE A 282 ? 0.7604 0.5243 0.4452 0.0513  -0.2050 -0.0696 280 PHE A CB    
2187 C  CG    . PHE A 282 ? 0.7402 0.5210 0.4043 0.0619  -0.1911 -0.0541 280 PHE A CG    
2188 C  CD1   . PHE A 282 ? 0.7101 0.4682 0.4114 0.0354  -0.1869 -0.0332 280 PHE A CD1   
2189 C  CD2   . PHE A 282 ? 0.6901 0.4897 0.4599 0.0613  -0.1812 -0.0476 280 PHE A CD2   
2190 C  CE1   . PHE A 282 ? 0.6722 0.4214 0.4270 0.0103  -0.1588 -0.0436 280 PHE A CE1   
2191 C  CE2   . PHE A 282 ? 0.6587 0.4606 0.4347 0.0339  -0.2235 -0.0451 280 PHE A CE2   
2192 C  CZ    . PHE A 282 ? 0.6772 0.5064 0.4361 0.0389  -0.1917 -0.0317 280 PHE A CZ    
2193 N  N     . PRO A 283 ? 0.8975 0.6539 0.4572 0.0765  -0.1787 -0.0576 281 PRO A N     
2194 C  CA    . PRO A 283 ? 0.9661 0.6942 0.5430 0.0828  -0.1822 -0.0170 281 PRO A CA    
2195 C  C     . PRO A 283 ? 1.0185 0.8571 0.6301 -0.0121 -0.3495 0.0239  281 PRO A C     
2196 O  O     . PRO A 283 ? 0.9341 0.8400 0.7953 -0.0844 -0.4575 0.0646  281 PRO A O     
2197 C  CB    . PRO A 283 ? 0.9457 0.6269 0.4702 0.0937  -0.1385 -0.0356 281 PRO A CB    
2198 C  CG    . PRO A 283 ? 0.9409 0.6392 0.4447 0.0854  -0.1192 -0.0319 281 PRO A CG    
2199 C  CD    . PRO A 283 ? 0.9297 0.6355 0.4344 0.1048  -0.1282 -0.0690 281 PRO A CD    
2200 N  N     . ALA A 284 ? 1.1249 0.9754 0.5899 0.0069  -0.3894 0.0282  282 ALA A N     
2201 C  CA    . ALA A 284 ? 1.1900 1.0620 0.7302 0.0239  -0.4259 -0.0114 282 ALA A CA    
2202 C  C     . ALA A 284 ? 1.3267 1.0900 0.5641 0.0359  -0.4414 -0.0532 282 ALA A C     
2203 O  O     . ALA A 284 ? 1.3837 1.1037 0.5889 0.1406  -0.3733 -0.0722 282 ALA A O     
2204 C  CB    . ALA A 284 ? 1.0793 1.1655 0.7112 0.1068  -0.5141 0.0412  282 ALA A CB    
2205 N  N     . ASP A 285 ? 1.3635 0.9847 0.6614 -0.0428 -0.3647 -0.1794 283 ASP A N     
2206 C  CA    . ASP A 285 ? 1.4315 1.0422 0.7106 -0.1068 -0.3606 -0.1769 283 ASP A CA    
2207 C  C     . ASP A 285 ? 1.4568 0.9908 0.7684 -0.1271 -0.3627 -0.2206 283 ASP A C     
2208 O  O     . ASP A 285 ? 1.6738 0.9307 1.1221 -0.1352 -0.2783 -0.3388 283 ASP A O     
2209 C  CB    . ASP A 285 ? 1.3882 1.0871 0.8134 -0.1509 -0.3082 -0.1351 283 ASP A CB    
2210 N  N     . SER A 286 ? 1.3040 0.9944 0.7060 -0.0568 -0.4228 -0.1717 284 SER A N     
2211 C  CA    . SER A 286 ? 1.1834 0.8641 0.7687 -0.0291 -0.4685 -0.1900 284 SER A CA    
2212 C  C     . SER A 286 ? 1.1866 0.9136 0.9270 -0.0506 -0.3741 -0.1754 284 SER A C     
2213 O  O     . SER A 286 ? 1.1425 0.8822 0.9903 -0.0407 -0.3999 -0.1602 284 SER A O     
2214 C  CB    . SER A 286 ? 1.1845 0.7615 0.7893 -0.0274 -0.4342 -0.1810 284 SER A CB    
2215 O  OG    . SER A 286 ? 1.0914 0.7181 0.6809 0.0541  -0.4547 -0.1003 284 SER A OG    
2216 N  N     . GLU A 287 ? 1.2757 0.7470 0.9737 -0.1250 -0.3569 -0.1952 285 GLU A N     
2217 C  CA    . GLU A 287 ? 1.2837 0.8268 1.0452 -0.1004 -0.3142 -0.1762 285 GLU A CA    
2218 C  C     . GLU A 287 ? 1.1189 0.8242 1.0351 -0.1367 -0.3735 -0.1353 285 GLU A C     
2219 O  O     . GLU A 287 ? 1.2619 0.7505 1.2785 -0.1662 -0.2615 -0.2550 285 GLU A O     
2220 C  CB    . GLU A 287 ? 1.3150 0.7793 1.0739 -0.1716 -0.2949 -0.2639 285 GLU A CB    
2221 C  CG    . GLU A 287 ? 1.4086 0.8004 1.1113 -0.2010 -0.2641 -0.2335 285 GLU A CG    
2222 C  CD    . GLU A 287 ? 1.4312 0.9400 1.0612 -0.2121 -0.3702 -0.2488 285 GLU A CD    
2223 O  OE1   . GLU A 287 ? 1.5013 1.0377 1.0036 -0.1765 -0.3365 -0.2898 285 GLU A OE1   
2224 O  OE2   . GLU A 287 ? 1.3325 0.9694 0.8363 -0.2144 -0.4851 -0.2776 285 GLU A OE2   
2225 N  N     . HIS A 288 ? 1.0289 0.6652 0.7884 -0.2299 -0.4360 -0.1962 286 HIS A N     
2226 C  CA    . HIS A 288 ? 1.0803 0.7214 0.7845 -0.1302 -0.4326 -0.1134 286 HIS A CA    
2227 C  C     . HIS A 288 ? 1.0927 0.6986 0.7374 -0.1112 -0.4332 -0.1170 286 HIS A C     
2228 O  O     . HIS A 288 ? 1.0874 0.5236 0.7660 -0.0670 -0.4730 -0.0865 286 HIS A O     
2229 C  CB    . HIS A 288 ? 1.0207 0.7359 0.8576 -0.0933 -0.4440 -0.0248 286 HIS A CB    
2230 C  CG    . HIS A 288 ? 1.0702 0.7739 0.8179 -0.0233 -0.4555 0.0531  286 HIS A CG    
2231 N  ND1   . HIS A 288 ? 1.0186 0.8829 0.7997 0.0984  -0.4678 0.0694  286 HIS A ND1   
2232 C  CD2   . HIS A 288 ? 1.0493 0.8204 0.8341 -0.0059 -0.4566 0.0668  286 HIS A CD2   
2233 C  CE1   . HIS A 288 ? 1.0083 0.8284 0.7447 0.0827  -0.4717 0.0823  286 HIS A CE1   
2234 N  NE2   . HIS A 288 ? 1.0037 0.8361 0.7194 0.0641  -0.5382 0.0376  286 HIS A NE2   
2235 N  N     . ASN A 289 ? 1.0925 0.7185 0.7156 -0.0946 -0.4093 -0.1628 287 ASN A N     
2236 C  CA    . ASN A 289 ? 0.9347 0.6712 0.6524 -0.1014 -0.4751 -0.1849 287 ASN A CA    
2237 C  C     . ASN A 289 ? 0.9631 0.7629 0.7858 -0.0256 -0.4323 -0.1980 287 ASN A C     
2238 O  O     . ASN A 289 ? 0.9603 0.6322 0.6948 0.0721  -0.5003 -0.2390 287 ASN A O     
2239 C  CB    . ASN A 289 ? 0.9323 0.6696 0.6990 -0.0301 -0.4272 -0.1585 287 ASN A CB    
2240 C  CG    . ASN A 289 ? 1.0346 0.7383 0.7215 0.0498  -0.3176 -0.1367 287 ASN A CG    
2241 O  OD1   . ASN A 289 ? 1.0006 0.6224 0.7033 0.0217  -0.3403 -0.1403 287 ASN A OD1   
2242 N  ND2   . ASN A 289 ? 1.0659 0.8160 0.7583 0.1064  -0.2277 -0.1429 287 ASN A ND2   
2243 N  N     . LYS A 290 ? 0.9912 0.8358 0.7853 -0.0273 -0.4724 -0.1473 288 LYS A N     
2244 C  CA    . LYS A 290 ? 1.0274 0.8163 0.7844 -0.0253 -0.3808 -0.0918 288 LYS A CA    
2245 C  C     . LYS A 290 ? 0.9198 0.6412 0.7290 -0.0499 -0.3790 -0.0746 288 LYS A C     
2246 O  O     . LYS A 290 ? 0.8511 0.6716 0.6243 -0.0391 -0.4233 -0.1226 288 LYS A O     
2247 C  CB    . LYS A 290 ? 1.0450 0.9167 0.7783 -0.0253 -0.3864 -0.0555 288 LYS A CB    
2248 C  CG    . LYS A 290 ? 1.1262 0.9815 0.8508 0.0117  -0.2424 -0.0461 288 LYS A CG    
2249 N  N     . LEU A 291 ? 0.8183 0.6523 0.7063 -0.0903 -0.3409 -0.0924 289 LEU A N     
2250 C  CA    . LEU A 291 ? 0.6964 0.5522 0.7173 -0.1195 -0.3216 -0.0864 289 LEU A CA    
2251 C  C     . LEU A 291 ? 0.6954 0.4234 0.7049 -0.1141 -0.2796 -0.0885 289 LEU A C     
2252 O  O     . LEU A 291 ? 0.6101 0.4802 0.5705 -0.0925 -0.3109 -0.0884 289 LEU A O     
2253 C  CB    . LEU A 291 ? 0.7093 0.5766 0.7831 -0.1694 -0.3104 -0.0982 289 LEU A CB    
2254 C  CG    . LEU A 291 ? 0.7321 0.5984 0.8211 -0.1452 -0.2609 -0.0889 289 LEU A CG    
2255 C  CD1   . LEU A 291 ? 0.6638 0.6460 0.8379 -0.0976 -0.2841 -0.0370 289 LEU A CD1   
2256 C  CD2   . LEU A 291 ? 0.8209 0.6219 0.8662 -0.1356 -0.2259 -0.0927 289 LEU A CD2   
2257 N  N     . LYS A 292 ? 0.6812 0.3876 0.6675 -0.0908 -0.2944 -0.0996 290 LYS A N     
2258 C  CA    . LYS A 292 ? 0.6445 0.4026 0.6240 -0.0399 -0.2644 -0.0477 290 LYS A CA    
2259 C  C     . LYS A 292 ? 0.5860 0.3868 0.5647 -0.0505 -0.2660 -0.0490 290 LYS A C     
2260 O  O     . LYS A 292 ? 0.5396 0.3110 0.5887 -0.0055 -0.2512 -0.0360 290 LYS A O     
2261 C  CB    . LYS A 292 ? 0.7207 0.4093 0.6173 -0.0165 -0.2305 -0.0351 290 LYS A CB    
2262 C  CG    . LYS A 292 ? 0.7792 0.3907 0.6281 -0.0290 -0.2392 -0.0188 290 LYS A CG    
2263 C  CD    . LYS A 292 ? 0.8309 0.4456 0.6318 -0.0192 -0.2054 0.0487  290 LYS A CD    
2264 C  CE    . LYS A 292 ? 0.8586 0.4816 0.6242 -0.0376 -0.1994 0.0514  290 LYS A CE    
2265 N  NZ    . LYS A 292 ? 0.7134 0.3544 0.5705 -0.0239 -0.2552 0.0556  290 LYS A NZ    
2266 N  N     . ALA A 293 ? 0.6353 0.3811 0.5555 -0.0562 -0.2692 -0.0695 291 ALA A N     
2267 C  CA    . ALA A 293 ? 0.5936 0.4120 0.5321 -0.0542 -0.2827 -0.0667 291 ALA A CA    
2268 C  C     . ALA A 293 ? 0.5337 0.4247 0.5484 -0.0627 -0.2669 -0.0494 291 ALA A C     
2269 O  O     . ALA A 293 ? 0.4912 0.3849 0.4973 -0.0330 -0.2371 -0.0404 291 ALA A O     
2270 C  CB    . ALA A 293 ? 0.6362 0.3666 0.5300 -0.0424 -0.2618 -0.0753 291 ALA A CB    
2271 N  N     A SER A 294 ? 0.5051 0.4351 0.5565 -0.0676 -0.2878 -0.0702 292 SER A N     
2272 N  N     B SER A 294 ? 0.5038 0.4331 0.5488 -0.0671 -0.2865 -0.0632 292 SER A N     
2273 C  CA    A SER A 294 ? 0.4868 0.4129 0.5648 -0.0757 -0.2811 -0.0689 292 SER A CA    
2274 C  CA    B SER A 294 ? 0.4845 0.4082 0.5502 -0.0759 -0.2758 -0.0545 292 SER A CA    
2275 C  C     A SER A 294 ? 0.4561 0.3859 0.5315 -0.0548 -0.2655 -0.0340 292 SER A C     
2276 C  C     B SER A 294 ? 0.4528 0.3863 0.5218 -0.0555 -0.2633 -0.0286 292 SER A C     
2277 O  O     A SER A 294 ? 0.4134 0.3897 0.5152 -0.0648 -0.2779 -0.0246 292 SER A O     
2278 O  O     B SER A 294 ? 0.4059 0.3947 0.5074 -0.0670 -0.2774 -0.0220 292 SER A O     
2279 C  CB    A SER A 294 ? 0.4924 0.4629 0.5813 -0.0812 -0.2981 -0.0835 292 SER A CB    
2280 C  CB    B SER A 294 ? 0.4890 0.4462 0.5390 -0.0806 -0.2907 -0.0554 292 SER A CB    
2281 O  OG    A SER A 294 ? 0.4623 0.4867 0.5661 -0.0820 -0.3321 -0.0869 292 SER A OG    
2282 O  OG    B SER A 294 ? 0.4407 0.4696 0.5269 -0.0750 -0.3073 -0.0376 292 SER A OG    
2283 N  N     . GLN A 295 ? 0.4801 0.3559 0.5278 -0.0617 -0.2334 -0.0341 293 GLN A N     
2284 C  CA    . GLN A 295 ? 0.4167 0.3679 0.5055 -0.0506 -0.2241 -0.0137 293 GLN A CA    
2285 C  C     . GLN A 295 ? 0.4294 0.3356 0.4592 -0.0341 -0.2073 -0.0055 293 GLN A C     
2286 O  O     . GLN A 295 ? 0.3671 0.3553 0.4299 -0.0312 -0.1685 0.0000  293 GLN A O     
2287 C  CB    . GLN A 295 ? 0.3967 0.3692 0.5538 -0.0110 -0.2464 0.0081  293 GLN A CB    
2288 C  CG    . GLN A 295 ? 0.4188 0.4084 0.6314 -0.0272 -0.2365 0.0154  293 GLN A CG    
2289 C  CD    . GLN A 295 ? 0.4391 0.4437 0.6622 -0.0397 -0.2347 0.0347  293 GLN A CD    
2290 O  OE1   . GLN A 295 ? 0.4983 0.4719 0.6308 -0.0065 -0.2708 0.0586  293 GLN A OE1   
2291 N  NE2   . GLN A 295 ? 0.4489 0.3989 0.7110 -0.0602 -0.2132 0.0079  293 GLN A NE2   
2292 N  N     . ALA A 296 ? 0.4898 0.3347 0.4116 -0.0289 -0.1944 -0.0228 294 ALA A N     
2293 C  CA    . ALA A 296 ? 0.4532 0.3768 0.3831 -0.0201 -0.1959 -0.0126 294 ALA A CA    
2294 C  C     . ALA A 296 ? 0.4389 0.3506 0.3465 -0.0466 -0.1848 -0.0188 294 ALA A C     
2295 O  O     . ALA A 296 ? 0.3815 0.3452 0.3622 -0.0677 -0.1426 -0.0145 294 ALA A O     
2296 C  CB    . ALA A 296 ? 0.5130 0.3613 0.3736 -0.0208 -0.2060 -0.0268 294 ALA A CB    
2297 N  N     . ARG A 297 ? 0.3798 0.3462 0.4053 -0.0408 -0.2011 0.0078  295 ARG A N     
2298 C  CA    . ARG A 297 ? 0.4266 0.3491 0.4213 -0.0540 -0.2080 -0.0072 295 ARG A CA    
2299 C  C     . ARG A 297 ? 0.3872 0.3381 0.4111 -0.0541 -0.1984 -0.0058 295 ARG A C     
2300 O  O     . ARG A 297 ? 0.3807 0.2943 0.4230 -0.0546 -0.1694 -0.0025 295 ARG A O     
2301 C  CB    . ARG A 297 ? 0.5338 0.3643 0.4065 -0.0526 -0.2182 0.0018  295 ARG A CB    
2302 C  CG    . ARG A 297 ? 0.5719 0.4255 0.4228 -0.0379 -0.2476 0.0061  295 ARG A CG    
2303 C  CD    . ARG A 297 ? 0.5855 0.4180 0.4597 -0.0419 -0.2931 -0.0283 295 ARG A CD    
2304 N  NE    . ARG A 297 ? 0.6333 0.4874 0.5183 -0.0346 -0.3245 -0.0535 295 ARG A NE    
2305 C  CZ    . ARG A 297 ? 0.6909 0.4972 0.5331 -0.0552 -0.3238 -0.1150 295 ARG A CZ    
2306 N  NH1   . ARG A 297 ? 0.7499 0.4121 0.4884 -0.0572 -0.3339 -0.1432 295 ARG A NH1   
2307 N  NH2   . ARG A 297 ? 0.7471 0.5364 0.6354 -0.0633 -0.3126 -0.0762 295 ARG A NH2   
2308 N  N     . ASP A 298 ? 0.3852 0.3207 0.4410 -0.0687 -0.1827 0.0056  296 ASP A N     
2309 C  CA    . ASP A 298 ? 0.3603 0.3336 0.4591 -0.0728 -0.1725 -0.0146 296 ASP A CA    
2310 C  C     . ASP A 298 ? 0.3063 0.3261 0.4138 -0.0572 -0.1492 0.0051  296 ASP A C     
2311 O  O     . ASP A 298 ? 0.2762 0.3349 0.4298 -0.0786 -0.1513 0.0031  296 ASP A O     
2312 C  CB    . ASP A 298 ? 0.3622 0.3894 0.5242 -0.0530 -0.1650 0.0065  296 ASP A CB    
2313 C  CG    . ASP A 298 ? 0.3258 0.3811 0.5524 -0.0206 -0.1605 0.0117  296 ASP A CG    
2314 O  OD1   . ASP A 298 ? 0.4001 0.3976 0.6020 0.0263  -0.1606 0.0594  296 ASP A OD1   
2315 O  OD2   . ASP A 298 ? 0.3711 0.3296 0.5641 -0.0331 -0.1192 0.0536  296 ASP A OD2   
2316 N  N     . LEU A 299 ? 0.3170 0.2924 0.3892 -0.0546 -0.1359 0.0023  297 LEU A N     
2317 C  CA    . LEU A 299 ? 0.2896 0.3060 0.3551 -0.0467 -0.1075 0.0129  297 LEU A CA    
2318 C  C     . LEU A 299 ? 0.3096 0.3104 0.3446 -0.0426 -0.1166 0.0112  297 LEU A C     
2319 O  O     . LEU A 299 ? 0.2529 0.3117 0.3111 -0.0299 -0.1061 0.0106  297 LEU A O     
2320 C  CB    . LEU A 299 ? 0.2769 0.2968 0.3602 -0.0626 -0.0995 0.0098  297 LEU A CB    
2321 C  CG    . LEU A 299 ? 0.2504 0.2851 0.3182 -0.0410 -0.0889 0.0142  297 LEU A CG    
2322 C  CD1   . LEU A 299 ? 0.2437 0.2932 0.3363 -0.0356 -0.1042 0.0372  297 LEU A CD1   
2323 C  CD2   . LEU A 299 ? 0.2552 0.2967 0.3017 -0.0426 -0.0873 0.0178  297 LEU A CD2   
2324 N  N     . LEU A 300 ? 0.3314 0.3307 0.3651 -0.0370 -0.1241 0.0293  298 LEU A N     
2325 C  CA    . LEU A 300 ? 0.3297 0.3524 0.3370 -0.0496 -0.1422 0.0265  298 LEU A CA    
2326 C  C     . LEU A 300 ? 0.3239 0.3753 0.3620 -0.0514 -0.1149 -0.0035 298 LEU A C     
2327 O  O     . LEU A 300 ? 0.3465 0.3721 0.3270 -0.0313 -0.1080 -0.0069 298 LEU A O     
2328 C  CB    . LEU A 300 ? 0.3229 0.3661 0.3052 -0.0630 -0.1467 -0.0002 298 LEU A CB    
2329 C  CG    . LEU A 300 ? 0.3680 0.4232 0.3163 -0.0469 -0.1395 0.0001  298 LEU A CG    
2330 C  CD1   . LEU A 300 ? 0.4000 0.4846 0.3668 -0.0552 -0.1489 -0.0142 298 LEU A CD1   
2331 C  CD2   . LEU A 300 ? 0.3795 0.3990 0.3162 -0.0563 -0.1102 0.0031  298 LEU A CD2   
2332 N  N     . SER A 301 ? 0.3174 0.3458 0.3633 -0.0452 -0.1347 0.0005  299 SER A N     
2333 C  CA    . SER A 301 ? 0.3182 0.3383 0.3956 -0.0345 -0.1445 0.0210  299 SER A CA    
2334 C  C     . SER A 301 ? 0.3182 0.3575 0.4073 -0.0073 -0.1187 0.0241  299 SER A C     
2335 O  O     . SER A 301 ? 0.3164 0.3640 0.4233 -0.0120 -0.1351 0.0217  299 SER A O     
2336 C  CB    . SER A 301 ? 0.3410 0.3316 0.4563 -0.0559 -0.1555 0.0018  299 SER A CB    
2337 O  OG    . SER A 301 ? 0.2884 0.3447 0.4153 -0.0542 -0.1433 0.0092  299 SER A OG    
2338 N  N     . LYS A 302 ? 0.2813 0.3267 0.3945 0.0052  -0.0851 0.0307  300 LYS A N     
2339 C  CA    . LYS A 302 ? 0.2746 0.3505 0.4078 -0.0260 -0.0790 0.0366  300 LYS A CA    
2340 C  C     . LYS A 302 ? 0.2684 0.3432 0.3959 -0.0229 -0.0604 0.0466  300 LYS A C     
2341 O  O     . LYS A 302 ? 0.2578 0.3608 0.4016 -0.0139 -0.0373 0.0348  300 LYS A O     
2342 C  CB    . LYS A 302 ? 0.2455 0.3517 0.4170 -0.0469 -0.0945 0.0379  300 LYS A CB    
2343 C  CG    . LYS A 302 ? 0.2378 0.3750 0.4468 -0.0480 -0.0737 0.0488  300 LYS A CG    
2344 C  CD    . LYS A 302 ? 0.2152 0.3838 0.4737 -0.0553 -0.0823 0.0344  300 LYS A CD    
2345 C  CE    . LYS A 302 ? 0.2127 0.4061 0.5221 -0.0633 -0.0524 0.0129  300 LYS A CE    
2346 N  NZ    . LYS A 302 ? 0.2312 0.4762 0.6104 -0.0890 -0.0603 0.0205  300 LYS A NZ    
2347 N  N     . MET A 303 ? 0.2484 0.3101 0.3454 -0.0163 -0.0643 0.0355  301 MET A N     
2348 C  CA    . MET A 303 ? 0.2544 0.2816 0.3189 -0.0305 -0.0629 0.0210  301 MET A CA    
2349 C  C     . MET A 303 ? 0.2490 0.2957 0.3009 -0.0144 -0.0585 0.0112  301 MET A C     
2350 O  O     . MET A 303 ? 0.2461 0.2945 0.3417 -0.0139 -0.0615 0.0140  301 MET A O     
2351 C  CB    . MET A 303 ? 0.2578 0.3312 0.2984 -0.0357 -0.0747 0.0167  301 MET A CB    
2352 C  CG    . MET A 303 ? 0.2967 0.3152 0.3634 -0.0471 -0.0858 0.0221  301 MET A CG    
2353 S  SD    . MET A 303 ? 0.3536 0.4517 0.4523 -0.0267 -0.0672 -0.0097 301 MET A SD    
2354 C  CE    . MET A 303 ? 0.2348 0.3039 0.3100 -0.0502 -0.0548 0.0293  301 MET A CE    
2355 N  N     . LEU A 304 ? 0.2905 0.2731 0.3177 -0.0124 -0.0632 0.0274  302 LEU A N     
2356 C  CA    . LEU A 304 ? 0.2932 0.3382 0.2915 -0.0198 -0.0757 0.0353  302 LEU A CA    
2357 C  C     . LEU A 304 ? 0.3234 0.3176 0.3082 -0.0130 -0.0857 0.0439  302 LEU A C     
2358 O  O     . LEU A 304 ? 0.2544 0.3581 0.3286 -0.0121 -0.0974 0.0139  302 LEU A O     
2359 C  CB    . LEU A 304 ? 0.3187 0.3103 0.2710 -0.0234 -0.1008 0.0349  302 LEU A CB    
2360 C  CG    . LEU A 304 ? 0.3066 0.3613 0.2885 -0.0225 -0.1030 0.0178  302 LEU A CG    
2361 C  CD1   . LEU A 304 ? 0.3274 0.3786 0.2851 -0.0235 -0.0803 0.0537  302 LEU A CD1   
2362 C  CD2   . LEU A 304 ? 0.3252 0.3523 0.3656 -0.0386 -0.0785 -0.0194 302 LEU A CD2   
2363 N  N     . VAL A 305 ? 0.2956 0.3216 0.3110 -0.0086 -0.0866 0.0273  303 VAL A N     
2364 C  CA    . VAL A 305 ? 0.2806 0.3467 0.3509 -0.0083 -0.0775 0.0255  303 VAL A CA    
2365 C  C     . VAL A 305 ? 0.2843 0.3312 0.3485 -0.0123 -0.0738 0.0350  303 VAL A C     
2366 O  O     . VAL A 305 ? 0.2652 0.3244 0.3251 -0.0069 -0.0519 0.0329  303 VAL A O     
2367 C  CB    . VAL A 305 ? 0.2761 0.3386 0.3778 -0.0077 -0.0758 0.0235  303 VAL A CB    
2368 C  CG1   . VAL A 305 ? 0.3218 0.3358 0.4151 0.0093  -0.0535 0.0329  303 VAL A CG1   
2369 C  CG2   . VAL A 305 ? 0.2907 0.3065 0.4117 0.0029  -0.0799 0.0196  303 VAL A CG2   
2370 N  N     . ILE A 306 ? 0.2560 0.3283 0.3508 -0.0002 -0.0979 0.0425  304 ILE A N     
2371 C  CA    . ILE A 306 ? 0.2680 0.3045 0.3672 0.0022  -0.0704 0.0437  304 ILE A CA    
2372 C  C     . ILE A 306 ? 0.2610 0.2859 0.3559 -0.0041 -0.0717 0.0473  304 ILE A C     
2373 O  O     . ILE A 306 ? 0.2850 0.3540 0.3920 0.0129  -0.0603 0.0372  304 ILE A O     
2374 C  CB    . ILE A 306 ? 0.2965 0.3130 0.3560 -0.0192 -0.0832 0.0467  304 ILE A CB    
2375 C  CG1   . ILE A 306 ? 0.3055 0.3443 0.3742 -0.0017 -0.0698 0.0428  304 ILE A CG1   
2376 C  CG2   . ILE A 306 ? 0.3450 0.3144 0.3960 0.0066  -0.0807 0.0630  304 ILE A CG2   
2377 C  CD1   . ILE A 306 ? 0.2763 0.3953 0.3413 -0.0132 -0.0985 0.0326  304 ILE A CD1   
2378 N  N     . ASP A 307 ? 0.2878 0.3384 0.3830 -0.0232 -0.0441 0.0470  305 ASP A N     
2379 C  CA    . ASP A 307 ? 0.2885 0.3615 0.3945 0.0053  -0.0287 0.0264  305 ASP A CA    
2380 C  C     . ASP A 307 ? 0.2601 0.3731 0.3975 0.0051  -0.0198 0.0148  305 ASP A C     
2381 O  O     . ASP A 307 ? 0.2352 0.3347 0.3963 0.0068  -0.0298 0.0453  305 ASP A O     
2382 C  CB    . ASP A 307 ? 0.3021 0.4016 0.4309 0.0054  -0.0369 0.0332  305 ASP A CB    
2383 C  CG    . ASP A 307 ? 0.3289 0.4444 0.4703 0.0213  -0.0115 0.0293  305 ASP A CG    
2384 O  OD1   . ASP A 307 ? 0.3729 0.4134 0.4372 0.0459  0.0119  -0.0035 305 ASP A OD1   
2385 O  OD2   . ASP A 307 ? 0.4020 0.5319 0.5818 0.0472  0.0486  0.0434  305 ASP A OD2   
2386 N  N     . ALA A 308 ? 0.2723 0.3606 0.3635 0.0202  -0.0233 0.0086  306 ALA A N     
2387 C  CA    . ALA A 308 ? 0.2522 0.3594 0.3624 0.0025  -0.0061 0.0200  306 ALA A CA    
2388 C  C     . ALA A 308 ? 0.2564 0.3848 0.4019 0.0032  -0.0116 0.0279  306 ALA A C     
2389 O  O     . ALA A 308 ? 0.2792 0.3607 0.4058 -0.0255 0.0164  0.0260  306 ALA A O     
2390 C  CB    . ALA A 308 ? 0.2283 0.3417 0.3490 0.0114  0.0008  0.0154  306 ALA A CB    
2391 N  N     . SER A 309 ? 0.2770 0.3586 0.4086 0.0063  0.0024  0.0033  307 SER A N     
2392 C  CA    . SER A 309 ? 0.2770 0.4078 0.4640 0.0299  0.0219  0.0016  307 SER A CA    
2393 C  C     . SER A 309 ? 0.2774 0.4280 0.4952 0.0121  0.0223  0.0161  307 SER A C     
2394 O  O     . SER A 309 ? 0.2487 0.4997 0.5251 0.0006  0.0534  0.0171  307 SER A O     
2395 C  CB    . SER A 309 ? 0.3143 0.4148 0.4653 0.0794  0.0291  0.0209  307 SER A CB    
2396 O  OG    . SER A 309 ? 0.3304 0.4406 0.5063 0.1118  0.0102  0.0171  307 SER A OG    
2397 N  N     . LYS A 310 ? 0.2629 0.4047 0.5003 0.0254  -0.0011 0.0118  308 LYS A N     
2398 C  CA    . LYS A 310 ? 0.2371 0.4346 0.5307 0.0301  0.0029  0.0087  308 LYS A CA    
2399 C  C     . LYS A 310 ? 0.2315 0.3960 0.4862 -0.0128 -0.0252 -0.0081 308 LYS A C     
2400 O  O     . LYS A 310 ? 0.2468 0.3992 0.5096 -0.0062 -0.0326 -0.0062 308 LYS A O     
2401 C  CB    . LYS A 310 ? 0.2775 0.4548 0.5646 0.0358  -0.0082 0.0275  308 LYS A CB    
2402 C  CG    . LYS A 310 ? 0.3925 0.5073 0.6899 0.0730  0.0186  0.0030  308 LYS A CG    
2403 C  CD    . LYS A 310 ? 0.5208 0.6393 0.7893 0.1029  -0.0101 -0.0159 308 LYS A CD    
2404 C  CE    . LYS A 310 ? 0.6403 0.6780 0.9189 0.1354  -0.0168 -0.0675 308 LYS A CE    
2405 N  NZ    . LYS A 310 ? 0.7753 0.7629 1.0112 0.1205  0.0065  -0.0764 308 LYS A NZ    
2406 N  N     . ARG A 311 ? 0.2114 0.3388 0.3895 0.0035  -0.0083 0.0087  309 ARG A N     
2407 C  CA    . ARG A 311 ? 0.2500 0.3493 0.3914 -0.0135 -0.0066 0.0080  309 ARG A CA    
2408 C  C     . ARG A 311 ? 0.2543 0.3478 0.3843 0.0011  0.0028  0.0202  309 ARG A C     
2409 O  O     . ARG A 311 ? 0.2574 0.3777 0.3770 0.0034  0.0313  0.0098  309 ARG A O     
2410 C  CB    . ARG A 311 ? 0.2348 0.3494 0.3321 -0.0132 -0.0220 0.0362  309 ARG A CB    
2411 C  CG    . ARG A 311 ? 0.2293 0.3308 0.2999 -0.0245 -0.0236 0.0399  309 ARG A CG    
2412 C  CD    . ARG A 311 ? 0.2475 0.3545 0.3427 -0.0263 -0.0393 0.0446  309 ARG A CD    
2413 N  NE    . ARG A 311 ? 0.2484 0.3259 0.3077 -0.0341 -0.0280 0.0406  309 ARG A NE    
2414 C  CZ    . ARG A 311 ? 0.2198 0.3177 0.2770 -0.0279 -0.0239 0.0292  309 ARG A CZ    
2415 N  NH1   . ARG A 311 ? 0.2081 0.3028 0.2693 -0.0179 -0.0167 0.0065  309 ARG A NH1   
2416 N  NH2   . ARG A 311 ? 0.2318 0.3016 0.3331 -0.0397 -0.0161 0.0169  309 ARG A NH2   
2417 N  N     . ILE A 312 ? 0.2645 0.3836 0.4250 -0.0391 -0.0118 0.0320  310 ILE A N     
2418 C  CA    . ILE A 312 ? 0.2497 0.3680 0.4341 -0.0276 -0.0100 0.0247  310 ILE A CA    
2419 C  C     . ILE A 312 ? 0.2477 0.3448 0.4076 -0.0273 0.0135  0.0316  310 ILE A C     
2420 O  O     . ILE A 312 ? 0.2097 0.3392 0.3975 -0.0083 0.0092  0.0315  310 ILE A O     
2421 C  CB    . ILE A 312 ? 0.2661 0.3635 0.4247 -0.0396 -0.0386 0.0249  310 ILE A CB    
2422 C  CG1   . ILE A 312 ? 0.3369 0.4130 0.4546 -0.0552 -0.0421 0.0479  310 ILE A CG1   
2423 C  CG2   . ILE A 312 ? 0.2520 0.3325 0.3847 -0.0120 -0.0317 0.0207  310 ILE A CG2   
2424 C  CD1   . ILE A 312 ? 0.4415 0.3978 0.4759 -0.0077 -0.0466 0.0521  310 ILE A CD1   
2425 N  N     . SER A 313 ? 0.2267 0.3432 0.4009 -0.0324 0.0481  0.0287  311 SER A N     
2426 C  CA    . SER A 313 ? 0.2352 0.3640 0.3775 -0.0383 0.0404  0.0118  311 SER A CA    
2427 C  C     . SER A 313 ? 0.2690 0.3864 0.3656 -0.0331 0.0202  0.0227  311 SER A C     
2428 O  O     . SER A 313 ? 0.2667 0.3368 0.3209 -0.0432 0.0262  0.0228  311 SER A O     
2429 C  CB    . SER A 313 ? 0.2952 0.4210 0.4057 -0.0501 0.0647  -0.0044 311 SER A CB    
2430 O  OG    . SER A 313 ? 0.2999 0.3946 0.3779 -0.0360 0.1006  0.0401  311 SER A OG    
2431 N  N     . VAL A 314 ? 0.2517 0.3586 0.3076 -0.0149 0.0294  0.0199  312 VAL A N     
2432 C  CA    . VAL A 314 ? 0.2425 0.3723 0.3138 -0.0271 0.0525  0.0388  312 VAL A CA    
2433 C  C     . VAL A 314 ? 0.2718 0.3694 0.3359 -0.0216 0.0393  0.0309  312 VAL A C     
2434 O  O     . VAL A 314 ? 0.2683 0.3523 0.3286 -0.0177 0.0417  0.0199  312 VAL A O     
2435 C  CB    . VAL A 314 ? 0.2635 0.3856 0.3271 -0.0244 0.0529  0.0341  312 VAL A CB    
2436 C  CG1   . VAL A 314 ? 0.3140 0.3851 0.3430 -0.0278 0.0489  0.0348  312 VAL A CG1   
2437 C  CG2   . VAL A 314 ? 0.2552 0.3424 0.3173 -0.0292 0.0328  0.0323  312 VAL A CG2   
2438 N  N     . ASP A 315 ? 0.2272 0.3291 0.3480 -0.0249 0.0618  0.0359  313 ASP A N     
2439 C  CA    . ASP A 315 ? 0.2747 0.3585 0.3866 -0.0416 0.0683  0.0497  313 ASP A CA    
2440 C  C     . ASP A 315 ? 0.2630 0.3680 0.3878 -0.0328 0.0393  0.0515  313 ASP A C     
2441 O  O     . ASP A 315 ? 0.2954 0.3686 0.4354 -0.0462 0.0305  0.0746  313 ASP A O     
2442 C  CB    . ASP A 315 ? 0.2929 0.3867 0.3868 -0.0531 0.0754  0.0565  313 ASP A CB    
2443 C  CG    . ASP A 315 ? 0.3531 0.4574 0.4269 -0.0157 0.0930  0.0792  313 ASP A CG    
2444 O  OD1   . ASP A 315 ? 0.3726 0.4438 0.4873 -0.0087 0.0376  0.0941  313 ASP A OD1   
2445 O  OD2   . ASP A 315 ? 0.5465 0.5667 0.4480 -0.0026 0.0647  0.0470  313 ASP A OD2   
2446 N  N     . GLU A 316 ? 0.2666 0.3494 0.4233 -0.0517 0.0345  0.0291  314 GLU A N     
2447 C  CA    . GLU A 316 ? 0.2466 0.3722 0.4169 -0.0330 0.0188  0.0419  314 GLU A CA    
2448 C  C     . GLU A 316 ? 0.2637 0.3680 0.4303 -0.0410 0.0057  0.0492  314 GLU A C     
2449 O  O     . GLU A 316 ? 0.2822 0.4128 0.4585 -0.0403 -0.0232 0.0247  314 GLU A O     
2450 C  CB    . GLU A 316 ? 0.2620 0.3928 0.4407 -0.0363 0.0405  0.0520  314 GLU A CB    
2451 C  CG    . GLU A 316 ? 0.2869 0.4347 0.4983 -0.0457 0.0418  0.0551  314 GLU A CG    
2452 C  CD    . GLU A 316 ? 0.3553 0.4771 0.5969 -0.0374 0.0659  0.0442  314 GLU A CD    
2453 O  OE1   . GLU A 316 ? 0.4278 0.4920 0.6205 -0.0385 0.0662  0.0517  314 GLU A OE1   
2454 O  OE2   . GLU A 316 ? 0.4042 0.6254 0.7347 -0.0301 0.0807  0.0585  314 GLU A OE2   
2455 N  N     . ALA A 317 ? 0.2445 0.2788 0.3691 -0.0300 -0.0202 0.0345  315 ALA A N     
2456 C  CA    . ALA A 317 ? 0.2580 0.3247 0.3889 -0.0252 -0.0246 0.0517  315 ALA A CA    
2457 C  C     . ALA A 317 ? 0.2920 0.3281 0.3870 -0.0312 -0.0167 0.0470  315 ALA A C     
2458 O  O     . ALA A 317 ? 0.2752 0.3220 0.4027 -0.0316 -0.0250 0.0608  315 ALA A O     
2459 C  CB    . ALA A 317 ? 0.2781 0.3192 0.3622 -0.0385 -0.0408 0.0380  315 ALA A CB    
2460 N  N     . LEU A 318 ? 0.3238 0.3190 0.3955 -0.0204 -0.0223 0.0577  316 LEU A N     
2461 C  CA    . LEU A 318 ? 0.2895 0.3224 0.3540 -0.0188 -0.0110 0.0588  316 LEU A CA    
2462 C  C     . LEU A 318 ? 0.3144 0.3501 0.4034 -0.0320 -0.0409 0.0561  316 LEU A C     
2463 O  O     . LEU A 318 ? 0.3655 0.3396 0.4844 -0.0309 -0.0586 0.0493  316 LEU A O     
2464 C  CB    . LEU A 318 ? 0.2782 0.2828 0.3178 -0.0226 -0.0075 0.0396  316 LEU A CB    
2465 C  CG    . LEU A 318 ? 0.2802 0.3041 0.2953 -0.0308 0.0069  0.0507  316 LEU A CG    
2466 C  CD1   . LEU A 318 ? 0.2737 0.2934 0.2880 -0.0324 0.0059  0.0427  316 LEU A CD1   
2467 C  CD2   . LEU A 318 ? 0.2940 0.3147 0.3190 -0.0326 -0.0166 0.0515  316 LEU A CD2   
2468 N  N     . GLN A 319 ? 0.3182 0.3516 0.4536 -0.0463 0.0076  0.0521  317 GLN A N     
2469 C  CA    . GLN A 319 ? 0.3390 0.4023 0.4939 -0.0642 -0.0164 0.0656  317 GLN A CA    
2470 C  C     . GLN A 319 ? 0.2873 0.3782 0.4905 -0.0767 -0.0249 0.0553  317 GLN A C     
2471 O  O     . GLN A 319 ? 0.2809 0.3786 0.5213 -0.0916 -0.0120 0.0609  317 GLN A O     
2472 C  CB    . GLN A 319 ? 0.4007 0.4228 0.5436 -0.0639 -0.0148 0.0950  317 GLN A CB    
2473 C  CG    . GLN A 319 ? 0.4887 0.5180 0.5578 -0.0764 -0.0249 0.0952  317 GLN A CG    
2474 C  CD    . GLN A 319 ? 0.6279 0.6187 0.6870 -0.0987 -0.0728 0.1463  317 GLN A CD    
2475 O  OE1   . GLN A 319 ? 0.6411 0.7481 0.7807 -0.1706 -0.0869 0.1213  317 GLN A OE1   
2476 N  NE2   . GLN A 319 ? 0.6574 0.5817 0.7884 -0.1052 -0.1105 0.1982  317 GLN A NE2   
2477 N  N     . HIS A 320 ? 0.2736 0.3183 0.4852 -0.0922 -0.0428 0.0442  318 HIS A N     
2478 C  CA    . HIS A 320 ? 0.2799 0.3119 0.4879 -0.0818 -0.0602 0.0314  318 HIS A CA    
2479 C  C     . HIS A 320 ? 0.2966 0.3200 0.4890 -0.0804 -0.0594 0.0589  318 HIS A C     
2480 O  O     . HIS A 320 ? 0.3177 0.3171 0.5025 -0.0386 -0.0199 0.0639  318 HIS A O     
2481 C  CB    . HIS A 320 ? 0.2853 0.2941 0.4640 -0.0624 -0.0483 0.0307  318 HIS A CB    
2482 C  CG    . HIS A 320 ? 0.2943 0.3133 0.4571 -0.0619 -0.0990 0.0088  318 HIS A CG    
2483 N  ND1   . HIS A 320 ? 0.3321 0.3317 0.4539 -0.0546 -0.1218 0.0199  318 HIS A ND1   
2484 C  CD2   . HIS A 320 ? 0.3386 0.3603 0.4840 -0.0505 -0.0943 0.0128  318 HIS A CD2   
2485 C  CE1   . HIS A 320 ? 0.3605 0.3469 0.4492 -0.0544 -0.1030 0.0229  318 HIS A CE1   
2486 N  NE2   . HIS A 320 ? 0.3108 0.3477 0.4598 -0.0429 -0.1254 0.0456  318 HIS A NE2   
2487 N  N     . PRO A 321 ? 0.3213 0.3377 0.5074 -0.0600 -0.0959 0.0371  319 PRO A N     
2488 C  CA    . PRO A 321 ? 0.3631 0.3498 0.5391 -0.0626 -0.1086 0.0397  319 PRO A CA    
2489 C  C     . PRO A 321 ? 0.3939 0.3378 0.5145 -0.0794 -0.1179 0.0257  319 PRO A C     
2490 O  O     . PRO A 321 ? 0.3752 0.2879 0.4941 -0.0992 -0.1164 0.0393  319 PRO A O     
2491 C  CB    . PRO A 321 ? 0.3670 0.4072 0.5558 -0.0546 -0.1082 -0.0008 319 PRO A CB    
2492 C  CG    . PRO A 321 ? 0.3649 0.3801 0.5948 -0.0351 -0.1171 0.0168  319 PRO A CG    
2493 C  CD    . PRO A 321 ? 0.3476 0.3485 0.5575 -0.0380 -0.0979 0.0187  319 PRO A CD    
2494 N  N     . TYR A 322 ? 0.3608 0.3655 0.4666 -0.0834 -0.1309 0.0469  320 TYR A N     
2495 C  CA    . TYR A 322 ? 0.3298 0.2991 0.4140 -0.0425 -0.1385 0.0153  320 TYR A CA    
2496 C  C     . TYR A 322 ? 0.3342 0.3158 0.3958 -0.0432 -0.1225 0.0117  320 TYR A C     
2497 O  O     . TYR A 322 ? 0.3602 0.3512 0.3744 -0.0381 -0.1302 -0.0292 320 TYR A O     
2498 C  CB    . TYR A 322 ? 0.3444 0.3370 0.3807 -0.0462 -0.1606 0.0029  320 TYR A CB    
2499 C  CG    . TYR A 322 ? 0.3738 0.3264 0.3746 -0.0300 -0.1432 -0.0192 320 TYR A CG    
2500 C  CD1   . TYR A 322 ? 0.4203 0.3941 0.3736 -0.0186 -0.1674 -0.0023 320 TYR A CD1   
2501 C  CD2   . TYR A 322 ? 0.3907 0.3209 0.3296 -0.0295 -0.1445 -0.0471 320 TYR A CD2   
2502 C  CE1   . TYR A 322 ? 0.4463 0.3961 0.4219 0.0099  -0.1647 -0.0312 320 TYR A CE1   
2503 C  CE2   . TYR A 322 ? 0.4157 0.3478 0.3550 -0.0112 -0.1548 -0.0369 320 TYR A CE2   
2504 C  CZ    . TYR A 322 ? 0.4649 0.3550 0.3742 0.0166  -0.1532 -0.0293 320 TYR A CZ    
2505 O  OH    . TYR A 322 ? 0.4592 0.3977 0.3485 0.0134  -0.1349 -0.0045 320 TYR A OH    
2506 N  N     . ILE A 323 ? 0.2926 0.2768 0.3798 -0.0371 -0.0833 0.0165  321 ILE A N     
2507 C  CA    . ILE A 323 ? 0.2788 0.2978 0.3714 -0.0533 -0.0792 0.0127  321 ILE A CA    
2508 C  C     . ILE A 323 ? 0.3044 0.3023 0.4096 -0.0459 -0.0689 0.0096  321 ILE A C     
2509 O  O     . ILE A 323 ? 0.3067 0.2924 0.3950 -0.0568 -0.0652 -0.0052 321 ILE A O     
2510 C  CB    . ILE A 323 ? 0.2843 0.3335 0.3481 -0.0519 -0.0776 0.0292  321 ILE A CB    
2511 C  CG1   . ILE A 323 ? 0.2895 0.3172 0.3421 -0.0548 -0.0720 0.0273  321 ILE A CG1   
2512 C  CG2   . ILE A 323 ? 0.2927 0.3135 0.3234 -0.0694 -0.0751 0.0340  321 ILE A CG2   
2513 C  CD1   . ILE A 323 ? 0.3321 0.3579 0.3345 -0.0332 -0.0644 0.0086  321 ILE A CD1   
2514 N  N     . ASN A 324 ? 0.3023 0.2513 0.4632 -0.0471 -0.0718 0.0305  322 ASN A N     
2515 C  CA    . ASN A 324 ? 0.3530 0.2792 0.4709 -0.0700 -0.0682 0.0169  322 ASN A CA    
2516 C  C     . ASN A 324 ? 0.3645 0.2683 0.4471 -0.0607 -0.0681 0.0389  322 ASN A C     
2517 O  O     . ASN A 324 ? 0.2988 0.3213 0.3956 -0.0975 -0.0318 0.0583  322 ASN A O     
2518 C  CB    . ASN A 324 ? 0.3426 0.2251 0.5245 -0.0607 -0.0640 0.0091  322 ASN A CB    
2519 C  CG    . ASN A 324 ? 0.3803 0.3026 0.5566 -0.0607 -0.0884 0.0378  322 ASN A CG    
2520 O  OD1   . ASN A 324 ? 0.4591 0.2713 0.5969 -0.0446 -0.1017 0.0265  322 ASN A OD1   
2521 N  ND2   . ASN A 324 ? 0.3952 0.3049 0.5216 -0.0950 -0.0613 0.0404  322 ASN A ND2   
2522 N  N     . VAL A 325 ? 0.3726 0.3066 0.4428 -0.0508 -0.1033 0.0311  323 VAL A N     
2523 C  CA    . VAL A 325 ? 0.3809 0.2792 0.4405 -0.0328 -0.1216 0.0208  323 VAL A CA    
2524 C  C     . VAL A 325 ? 0.3383 0.2940 0.4282 -0.0512 -0.0907 0.0182  323 VAL A C     
2525 O  O     . VAL A 325 ? 0.3112 0.2604 0.4023 -0.0443 -0.0959 0.0107  323 VAL A O     
2526 C  CB    . VAL A 325 ? 0.3949 0.3115 0.4338 -0.0291 -0.1347 0.0524  323 VAL A CB    
2527 C  CG1   . VAL A 325 ? 0.3831 0.3067 0.4492 -0.0143 -0.1147 0.0465  323 VAL A CG1   
2528 C  CG2   . VAL A 325 ? 0.4008 0.3581 0.4277 0.0122  -0.1329 0.0216  323 VAL A CG2   
2529 N  N     . TRP A 326 ? 0.3234 0.2722 0.3988 -0.0503 -0.0831 0.0297  324 TRP A N     
2530 C  CA    . TRP A 326 ? 0.3423 0.2967 0.4040 -0.0320 -0.0470 0.0280  324 TRP A CA    
2531 C  C     . TRP A 326 ? 0.3023 0.2477 0.3691 -0.0519 -0.0311 0.0278  324 TRP A C     
2532 O  O     . TRP A 326 ? 0.3056 0.2530 0.3401 -0.0476 -0.0022 0.0290  324 TRP A O     
2533 C  CB    . TRP A 326 ? 0.3685 0.2926 0.3852 -0.0320 -0.0449 0.0227  324 TRP A CB    
2534 C  CG    . TRP A 326 ? 0.3773 0.2954 0.3356 -0.0267 -0.0630 0.0058  324 TRP A CG    
2535 C  CD1   . TRP A 326 ? 0.3936 0.3154 0.3170 -0.0429 -0.0864 -0.0128 324 TRP A CD1   
2536 C  CD2   . TRP A 326 ? 0.3620 0.2551 0.3631 -0.0621 -0.0726 0.0051  324 TRP A CD2   
2537 N  NE1   . TRP A 326 ? 0.3969 0.3223 0.3340 -0.0252 -0.0745 0.0019  324 TRP A NE1   
2538 C  CE2   . TRP A 326 ? 0.3947 0.3017 0.3574 -0.0393 -0.0845 -0.0022 324 TRP A CE2   
2539 C  CE3   . TRP A 326 ? 0.3720 0.2518 0.3703 -0.0557 -0.0646 0.0199  324 TRP A CE3   
2540 C  CZ2   . TRP A 326 ? 0.4108 0.3131 0.3630 -0.0199 -0.0467 0.0059  324 TRP A CZ2   
2541 C  CZ3   . TRP A 326 ? 0.4355 0.2585 0.3651 -0.0364 -0.0727 0.0374  324 TRP A CZ3   
2542 C  CH2   . TRP A 326 ? 0.4523 0.3056 0.3842 -0.0481 -0.0472 0.0070  324 TRP A CH2   
2543 N  N     . TYR A 327 ? 0.3065 0.2414 0.4056 -0.0562 -0.0249 0.0279  325 TYR A N     
2544 C  CA    . TYR A 327 ? 0.3001 0.2965 0.4002 -0.0545 -0.0097 0.0647  325 TYR A CA    
2545 C  C     . TYR A 327 ? 0.3117 0.3130 0.4407 -0.0553 -0.0251 0.0733  325 TYR A C     
2546 O  O     . TYR A 327 ? 0.2900 0.2860 0.4354 -0.0465 -0.0323 0.0675  325 TYR A O     
2547 C  CB    . TYR A 327 ? 0.3148 0.2679 0.4066 -0.0369 0.0175  0.0676  325 TYR A CB    
2548 C  CG    . TYR A 327 ? 0.3595 0.2823 0.4211 -0.0613 0.0047  0.0422  325 TYR A CG    
2549 C  CD1   . TYR A 327 ? 0.3713 0.2978 0.4605 -0.0325 0.0214  0.0448  325 TYR A CD1   
2550 C  CD2   . TYR A 327 ? 0.4460 0.3071 0.4371 -0.0531 0.0472  0.0730  325 TYR A CD2   
2551 C  CE1   . TYR A 327 ? 0.4102 0.3399 0.5061 -0.0258 0.0582  0.0413  325 TYR A CE1   
2552 C  CE2   . TYR A 327 ? 0.4412 0.3029 0.4760 -0.0562 0.0549  0.0517  325 TYR A CE2   
2553 C  CZ    . TYR A 327 ? 0.4474 0.3610 0.4879 -0.0690 0.0687  0.0479  325 TYR A CZ    
2554 O  OH    . TYR A 327 ? 0.4632 0.3603 0.5023 -0.0534 0.1112  0.0334  325 TYR A OH    
2555 N  N     . ASP A 328 ? 0.3068 0.2908 0.3931 -0.0316 -0.0150 0.0541  326 ASP A N     
2556 C  CA    . ASP A 328 ? 0.3381 0.3133 0.3804 -0.0394 -0.0057 0.0594  326 ASP A CA    
2557 C  C     . ASP A 328 ? 0.3681 0.3665 0.3593 -0.0384 0.0028  0.0621  326 ASP A C     
2558 O  O     . ASP A 328 ? 0.3591 0.3341 0.2643 -0.0465 0.0048  0.0664  326 ASP A O     
2559 C  CB    . ASP A 328 ? 0.3525 0.2863 0.3885 -0.0083 -0.0193 0.0487  326 ASP A CB    
2560 C  CG    . ASP A 328 ? 0.3715 0.3128 0.3923 -0.0098 -0.0066 0.0779  326 ASP A CG    
2561 O  OD1   . ASP A 328 ? 0.3701 0.2989 0.3897 0.0203  0.0073  0.1128  326 ASP A OD1   
2562 O  OD2   . ASP A 328 ? 0.3556 0.3233 0.3927 0.0162  -0.0213 0.0627  326 ASP A OD2   
2563 N  N     . PRO A 329 ? 0.4122 0.3575 0.3276 -0.0268 0.0019  0.0549  327 PRO A N     
2564 C  CA    . PRO A 329 ? 0.4735 0.4059 0.3532 -0.0408 0.0223  0.0298  327 PRO A CA    
2565 C  C     . PRO A 329 ? 0.4692 0.4193 0.3530 -0.0540 0.0212  0.0323  327 PRO A C     
2566 O  O     . PRO A 329 ? 0.4994 0.4037 0.3621 -0.0400 -0.0318 0.0254  327 PRO A O     
2567 C  CB    . PRO A 329 ? 0.4374 0.4437 0.3818 -0.0666 0.0287  -0.0068 327 PRO A CB    
2568 C  CG    . PRO A 329 ? 0.4465 0.4265 0.4183 -0.0722 0.0483  -0.0012 327 PRO A CG    
2569 C  CD    . PRO A 329 ? 0.4200 0.4128 0.3911 -0.0382 0.0369  0.0324  327 PRO A CD    
2570 N  N     . SER A 330 ? 0.5262 0.4464 0.3504 -0.0541 -0.0214 0.0594  328 SER A N     
2571 C  CA    . SER A 330 ? 0.6028 0.4567 0.4655 -0.0607 -0.0272 0.0997  328 SER A CA    
2572 C  C     . SER A 330 ? 0.5892 0.5138 0.4488 -0.0787 -0.0331 0.0974  328 SER A C     
2573 O  O     . SER A 330 ? 0.6362 0.5445 0.5184 -0.1206 -0.0730 0.0938  328 SER A O     
2574 C  CB    . SER A 330 ? 0.6302 0.4990 0.5736 -0.0108 -0.0530 0.0603  328 SER A CB    
2575 O  OG    . SER A 330 ? 0.7073 0.5620 0.5971 0.0016  -0.0489 0.0684  328 SER A OG    
2576 N  N     . GLU A 331 ? 0.5158 0.4544 0.3496 -0.0746 -0.0255 0.0476  329 GLU A N     
2577 C  CA    . GLU A 331 ? 0.4835 0.4102 0.3118 -0.0218 -0.0348 0.0586  329 GLU A CA    
2578 C  C     . GLU A 331 ? 0.5199 0.4175 0.3754 -0.0660 0.0138  0.0059  329 GLU A C     
2579 O  O     . GLU A 331 ? 0.5104 0.4057 0.3604 -0.0391 0.0070  -0.0105 329 GLU A O     
2580 C  CB    . GLU A 331 ? 0.5491 0.4867 0.3809 -0.0281 -0.0186 0.0624  329 GLU A CB    
2581 C  CG    . GLU A 331 ? 0.5610 0.5174 0.4456 0.0112  -0.0284 0.0531  329 GLU A CG    
2582 C  CD    . GLU A 331 ? 0.5624 0.5005 0.5376 0.0115  -0.0333 0.0240  329 GLU A CD    
2583 O  OE1   . GLU A 331 ? 0.5143 0.3550 0.3925 -0.0206 -0.0390 0.1044  329 GLU A OE1   
2584 O  OE2   . GLU A 331 ? 0.6060 0.5698 0.6941 0.0635  -0.0361 0.0487  329 GLU A OE2   
2585 N  N     . ALA A 332 ? 0.4925 0.3483 0.3480 -0.0491 0.0463  -0.0256 330 ALA A N     
2586 C  CA    . ALA A 332 ? 0.5225 0.3569 0.3347 -0.0580 0.0549  0.0171  330 ALA A CA    
2587 C  C     . ALA A 332 ? 0.6283 0.3728 0.3759 -0.0295 0.0557  0.0051  330 ALA A C     
2588 O  O     . ALA A 332 ? 0.5702 0.3789 0.3836 -0.0427 0.0530  0.0155  330 ALA A O     
2589 C  CB    . ALA A 332 ? 0.5040 0.3726 0.3574 -0.0538 0.0765  -0.0122 330 ALA A CB    
2590 N  N     . GLU A 333 ? 0.5953 0.3245 0.3489 -0.0479 0.0329  0.0038  331 GLU A N     
2591 C  CA    . GLU A 333 ? 0.5921 0.3917 0.3905 -0.0733 0.0605  0.0276  331 GLU A CA    
2592 C  C     . GLU A 333 ? 0.6313 0.4183 0.3856 -0.0770 0.0588  0.0462  331 GLU A C     
2593 O  O     . GLU A 333 ? 0.6178 0.4524 0.3761 -0.0916 0.1513  0.0097  331 GLU A O     
2594 C  CB    . GLU A 333 ? 0.5794 0.3706 0.3872 -0.0958 0.0640  0.0549  331 GLU A CB    
2595 C  CG    . GLU A 333 ? 0.5970 0.3803 0.4258 -0.1041 0.0621  0.0268  331 GLU A CG    
2596 C  CD    . GLU A 333 ? 0.5654 0.4627 0.4309 -0.0985 0.0721  0.0161  331 GLU A CD    
2597 O  OE1   . GLU A 333 ? 0.5805 0.5261 0.4107 -0.1158 0.0939  0.0010  331 GLU A OE1   
2598 O  OE2   . GLU A 333 ? 0.5731 0.4462 0.4136 -0.0712 0.0721  -0.0254 331 GLU A OE2   
2599 N  N     . ALA A 334 ? 0.6380 0.4506 0.3155 -0.1158 0.0888  0.0856  332 ALA A N     
2600 C  CA    . ALA A 334 ? 0.6204 0.4330 0.4103 -0.1096 0.0498  0.0374  332 ALA A CA    
2601 C  C     . ALA A 334 ? 0.5743 0.4217 0.3862 -0.1105 0.0170  0.0257  332 ALA A C     
2602 O  O     . ALA A 334 ? 0.5946 0.3689 0.3525 -0.1180 -0.0086 -0.0151 332 ALA A O     
2603 C  CB    . ALA A 334 ? 0.6669 0.4754 0.4901 -0.1249 0.0380  0.0134  332 ALA A CB    
2604 N  N     . PRO A 335 ? 0.5637 0.4146 0.3976 -0.1366 0.0270  0.0575  333 PRO A N     
2605 C  CA    . PRO A 335 ? 0.6026 0.4299 0.3879 -0.1138 0.0055  0.0653  333 PRO A CA    
2606 C  C     . PRO A 335 ? 0.6012 0.4248 0.3065 -0.1065 0.0106  0.0450  333 PRO A C     
2607 O  O     . PRO A 335 ? 0.5971 0.3934 0.3035 -0.1525 0.0197  0.0719  333 PRO A O     
2608 C  CB    . PRO A 335 ? 0.6200 0.4682 0.3940 -0.1214 -0.0081 0.0794  333 PRO A CB    
2609 C  CG    . PRO A 335 ? 0.6467 0.4844 0.4436 -0.1042 0.0075  0.0720  333 PRO A CG    
2610 C  CD    . PRO A 335 ? 0.6056 0.4805 0.4657 -0.1120 0.0183  0.0610  333 PRO A CD    
2611 N  N     . PRO A 336 ? 0.6082 0.4228 0.2840 -0.0899 0.0035  0.0856  334 PRO A N     
2612 C  CA    . PRO A 336 ? 0.6035 0.4075 0.3041 -0.0770 -0.0032 0.0498  334 PRO A CA    
2613 C  C     . PRO A 336 ? 0.6488 0.3945 0.2971 -0.0746 -0.0266 0.0551  334 PRO A C     
2614 O  O     . PRO A 336 ? 0.6831 0.3410 0.3030 -0.0787 -0.0345 0.0868  334 PRO A O     
2615 C  CB    . PRO A 336 ? 0.6229 0.4661 0.3914 -0.0765 0.0170  0.0236  334 PRO A CB    
2616 C  CG    . PRO A 336 ? 0.6490 0.4798 0.4386 -0.0826 0.0373  0.0021  334 PRO A CG    
2617 C  CD    . PRO A 336 ? 0.6353 0.4640 0.3492 -0.0687 -0.0038 0.0377  334 PRO A CD    
2618 N  N     . PRO A 337 ? 0.6419 0.4557 0.3664 -0.0752 -0.0329 0.0435  335 PRO A N     
2619 C  CA    . PRO A 337 ? 0.6215 0.4701 0.3976 -0.0378 -0.0293 0.0308  335 PRO A CA    
2620 C  C     . PRO A 337 ? 0.6758 0.4715 0.4191 -0.0589 -0.0329 0.0466  335 PRO A C     
2621 O  O     . PRO A 337 ? 0.6515 0.4117 0.3947 -0.0482 -0.0342 -0.0248 335 PRO A O     
2622 C  CB    . PRO A 337 ? 0.5789 0.5046 0.3552 -0.0444 -0.0131 0.0256  335 PRO A CB    
2623 C  CG    . PRO A 337 ? 0.5867 0.5119 0.4281 -0.0531 -0.0236 0.0326  335 PRO A CG    
2624 C  CD    . PRO A 337 ? 0.5796 0.4726 0.3392 -0.0676 -0.0040 0.0653  335 PRO A CD    
2625 N  N     . LYS A 338 ? 0.6163 0.4382 0.4281 -0.1087 -0.0555 0.0566  336 LYS A N     
2626 C  CA    . LYS A 338 ? 0.6530 0.4780 0.4771 -0.1065 -0.0534 0.0796  336 LYS A CA    
2627 C  C     . LYS A 338 ? 0.6532 0.4686 0.4083 -0.1022 -0.0548 0.1058  336 LYS A C     
2628 O  O     . LYS A 338 ? 0.6552 0.4712 0.4861 -0.0842 -0.0986 0.1132  336 LYS A O     
2629 C  CB    . LYS A 338 ? 0.7085 0.4930 0.5149 -0.1329 -0.0393 0.1477  336 LYS A CB    
2630 C  CG    . LYS A 338 ? 0.7795 0.6657 0.6129 -0.1513 -0.0217 0.0804  336 LYS A CG    
2631 C  CD    . LYS A 338 ? 0.8590 0.7184 0.7185 -0.1345 -0.0185 0.0894  336 LYS A CD    
2632 C  CE    . LYS A 338 ? 0.8899 0.8506 0.8659 -0.1577 0.0036  -0.0320 336 LYS A CE    
2633 N  NZ    . LYS A 338 ? 0.8687 0.9085 0.9021 -0.1793 0.0072  -0.0904 336 LYS A NZ    
2634 N  N     . ILE A 339 ? 0.6364 0.4792 0.4124 -0.0718 -0.0535 0.0305  337 ILE A N     
2635 C  CA    . ILE A 339 ? 0.6317 0.4418 0.3506 -0.0617 -0.0693 0.0264  337 ILE A CA    
2636 C  C     . ILE A 339 ? 0.6779 0.4836 0.3378 -0.0659 -0.1087 0.0505  337 ILE A C     
2637 O  O     . ILE A 339 ? 0.7328 0.5199 0.3458 -0.0961 -0.0829 0.0318  337 ILE A O     
2638 C  CB    . ILE A 339 ? 0.5665 0.4464 0.3113 -0.0616 -0.0818 0.0372  337 ILE A CB    
2639 C  CG1   . ILE A 339 ? 0.5454 0.4865 0.2540 -0.0316 -0.0255 0.0245  337 ILE A CG1   
2640 C  CG2   . ILE A 339 ? 0.5867 0.4505 0.4020 -0.0517 -0.0789 0.0450  337 ILE A CG2   
2641 C  CD1   . ILE A 339 ? 0.5735 0.4797 0.2914 -0.0164 -0.0495 0.0057  337 ILE A CD1   
2642 N  N     . PRO A 340 ? 0.7099 0.5275 0.4019 -0.1086 -0.1140 0.0506  338 PRO A N     
2643 C  CA    . PRO A 340 ? 0.7621 0.5424 0.3740 -0.1020 -0.1429 0.0635  338 PRO A CA    
2644 C  C     . PRO A 340 ? 0.8082 0.5316 0.3567 -0.0891 -0.1180 0.0662  338 PRO A C     
2645 O  O     . PRO A 340 ? 0.8714 0.5626 0.3689 -0.0886 -0.1691 0.0841  338 PRO A O     
2646 C  CB    . PRO A 340 ? 0.7316 0.5244 0.3858 -0.0849 -0.1601 0.0652  338 PRO A CB    
2647 C  CG    . PRO A 340 ? 0.7280 0.5526 0.4193 -0.1001 -0.1643 0.0392  338 PRO A CG    
2648 C  CD    . PRO A 340 ? 0.7046 0.4788 0.4561 -0.0793 -0.1577 0.0718  338 PRO A CD    
2649 N  N     . ASP A 341 ? 0.7632 0.4709 0.3991 -0.0840 -0.1123 0.0387  339 ASP A N     
2650 C  CA    . ASP A 341 ? 0.7438 0.5031 0.4256 -0.0795 -0.0871 0.0040  339 ASP A CA    
2651 C  C     . ASP A 341 ? 0.7530 0.4969 0.4459 -0.0471 -0.0839 0.0193  339 ASP A C     
2652 O  O     . ASP A 341 ? 0.6682 0.4839 0.4332 -0.0533 -0.1022 0.0048  339 ASP A O     
2653 C  CB    . ASP A 341 ? 0.7125 0.4099 0.4139 -0.1158 -0.0534 -0.0337 339 ASP A CB    
2654 C  CG    . ASP A 341 ? 0.7035 0.4564 0.4350 -0.0923 -0.0686 -0.0329 339 ASP A CG    
2655 O  OD1   . ASP A 341 ? 0.7043 0.5212 0.3906 -0.1148 -0.0750 -0.0492 339 ASP A OD1   
2656 O  OD2   . ASP A 341 ? 0.6741 0.4193 0.3931 -0.1043 -0.0681 -0.0302 339 ASP A OD2   
2657 N  N     . LYS A 342 ? 0.7930 0.5288 0.4085 -0.0793 -0.0826 0.0139  340 LYS A N     
2658 C  CA    . LYS A 342 ? 0.8251 0.5789 0.5011 -0.1225 -0.0267 0.0431  340 LYS A CA    
2659 C  C     . LYS A 342 ? 0.7722 0.5521 0.5320 -0.0953 -0.0223 -0.0139 340 LYS A C     
2660 O  O     . LYS A 342 ? 0.6547 0.5305 0.5204 -0.1422 -0.0413 -0.0289 340 LYS A O     
2661 C  CB    . LYS A 342 ? 0.9268 0.6375 0.5325 -0.1273 -0.0285 0.0503  340 LYS A CB    
2662 C  CG    . LYS A 342 ? 1.0313 0.6492 0.6207 -0.1401 -0.0402 0.0650  340 LYS A CG    
2663 C  CD    . LYS A 342 ? 1.0658 0.6637 0.6948 -0.1859 -0.0190 0.0935  340 LYS A CD    
2664 C  CE    . LYS A 342 ? 1.1173 0.6606 0.7262 -0.1510 -0.0093 0.1115  340 LYS A CE    
2665 N  NZ    . LYS A 342 ? 1.1150 0.6888 0.7220 -0.1459 0.0139  0.1473  340 LYS A NZ    
2666 N  N     . GLN A 343 ? 0.7651 0.4976 0.5041 -0.0883 -0.0319 -0.0271 341 GLN A N     
2667 C  CA    . GLN A 343 ? 0.7346 0.5099 0.4515 -0.1070 -0.0127 -0.0358 341 GLN A CA    
2668 C  C     . GLN A 343 ? 0.6674 0.4901 0.3897 -0.0581 -0.0527 -0.0322 341 GLN A C     
2669 O  O     . GLN A 343 ? 0.6895 0.5230 0.3475 -0.0600 -0.0240 -0.0640 341 GLN A O     
2670 C  CB    . GLN A 343 ? 0.7758 0.5320 0.4562 -0.0681 -0.0371 -0.0707 341 GLN A CB    
2671 C  CG    . GLN A 343 ? 0.8324 0.5260 0.4758 -0.0558 -0.0404 -0.1117 341 GLN A CG    
2672 C  CD    . GLN A 343 ? 0.9069 0.6255 0.6498 -0.0523 -0.0549 -0.1121 341 GLN A CD    
2673 O  OE1   . GLN A 343 ? 0.9943 0.6450 0.7628 -0.0387 -0.0149 -0.1363 341 GLN A OE1   
2674 N  NE2   . GLN A 343 ? 0.9584 0.6364 0.7525 0.0197  -0.0390 -0.1339 341 GLN A NE2   
2675 N  N     . LEU A 344 ? 0.5657 0.4326 0.3881 -0.1098 -0.0658 0.0025  342 LEU A N     
2676 C  CA    . LEU A 344 ? 0.6028 0.4236 0.3777 -0.0638 -0.0739 -0.0110 342 LEU A CA    
2677 C  C     . LEU A 344 ? 0.5981 0.4549 0.4004 -0.0319 -0.0751 -0.0683 342 LEU A C     
2678 O  O     . LEU A 344 ? 0.6760 0.5234 0.4874 -0.0184 -0.0714 -0.1199 342 LEU A O     
2679 C  CB    . LEU A 344 ? 0.5518 0.4197 0.3857 -0.0387 -0.0683 0.0196  342 LEU A CB    
2680 C  CG    . LEU A 344 ? 0.5670 0.4759 0.4009 -0.0617 -0.0823 0.0079  342 LEU A CG    
2681 C  CD1   . LEU A 344 ? 0.5811 0.5557 0.3594 -0.0327 -0.1184 0.0078  342 LEU A CD1   
2682 C  CD2   . LEU A 344 ? 0.5742 0.4875 0.4784 -0.0593 -0.0317 -0.0353 342 LEU A CD2   
2683 N  N     . ASP A 345 ? 0.6430 0.4193 0.4615 -0.0405 -0.0582 -0.0498 343 ASP A N     
2684 C  CA    . ASP A 345 ? 0.5649 0.4748 0.4804 0.0141  -0.0739 -0.0693 343 ASP A CA    
2685 C  C     . ASP A 345 ? 0.5451 0.4292 0.4881 -0.0314 -0.0819 -0.0576 343 ASP A C     
2686 O  O     . ASP A 345 ? 0.5787 0.3841 0.5105 -0.0220 -0.0899 -0.0594 343 ASP A O     
2687 C  CB    . ASP A 345 ? 0.6235 0.4757 0.5212 0.0148  -0.0660 -0.0719 343 ASP A CB    
2688 C  CG    . ASP A 345 ? 0.6173 0.4886 0.5092 0.0149  -0.0401 -0.0712 343 ASP A CG    
2689 O  OD1   . ASP A 345 ? 0.5758 0.4845 0.4646 0.0513  -0.0442 -0.0230 343 ASP A OD1   
2690 O  OD2   . ASP A 345 ? 0.6741 0.5083 0.5288 0.0268  -0.0631 -0.0703 343 ASP A OD2   
2691 N  N     . GLU A 346 ? 0.5042 0.4629 0.4679 -0.0637 -0.0809 -0.0842 344 GLU A N     
2692 C  CA    . GLU A 346 ? 0.5808 0.5715 0.5087 -0.0580 -0.0650 -0.0729 344 GLU A CA    
2693 C  C     . GLU A 346 ? 0.5324 0.5179 0.4377 -0.0490 -0.0858 -0.0577 344 GLU A C     
2694 O  O     . GLU A 346 ? 0.5868 0.5081 0.4832 0.0016  -0.0402 -0.0819 344 GLU A O     
2695 C  CB    . GLU A 346 ? 0.6373 0.6668 0.5310 -0.0996 -0.0140 -0.0320 344 GLU A CB    
2696 C  CG    . GLU A 346 ? 0.7035 0.8137 0.6268 -0.1338 -0.0017 -0.0397 344 GLU A CG    
2697 C  CD    . GLU A 346 ? 0.8268 0.8956 0.7401 -0.1474 0.0625  -0.0212 344 GLU A CD    
2698 O  OE1   . GLU A 346 ? 0.9035 0.9728 0.8208 -0.1387 0.1408  -0.0108 344 GLU A OE1   
2699 O  OE2   . GLU A 346 ? 0.8949 1.0796 0.7730 -0.0896 0.0567  -0.1051 344 GLU A OE2   
2700 N  N     . ARG A 347 ? 0.5499 0.5023 0.3532 -0.0600 -0.1224 -0.0703 345 ARG A N     
2701 C  CA    . ARG A 347 ? 0.5162 0.5499 0.4421 -0.0626 -0.1444 -0.0267 345 ARG A CA    
2702 C  C     . ARG A 347 ? 0.5039 0.4756 0.4134 -0.0655 -0.1332 -0.0490 345 ARG A C     
2703 O  O     . ARG A 347 ? 0.4529 0.3728 0.3912 -0.0395 -0.1325 -0.0482 345 ARG A O     
2704 C  CB    . ARG A 347 ? 0.5156 0.6172 0.5437 -0.0367 -0.1626 -0.0868 345 ARG A CB    
2705 C  CG    . ARG A 347 ? 0.5630 0.6184 0.5788 -0.0357 -0.1635 -0.0877 345 ARG A CG    
2706 C  CD    . ARG A 347 ? 0.6327 0.5880 0.5565 -0.0670 -0.1192 0.0109  345 ARG A CD    
2707 N  NE    . ARG A 347 ? 0.6340 0.6055 0.4473 -0.0673 -0.1143 -0.0358 345 ARG A NE    
2708 C  CZ    . ARG A 347 ? 0.6650 0.5832 0.5526 -0.0977 -0.1441 0.0585  345 ARG A CZ    
2709 N  NH1   . ARG A 347 ? 0.6968 0.6461 0.5855 -0.0451 -0.2074 0.0982  345 ARG A NH1   
2710 N  NH2   . ARG A 347 ? 0.7118 0.5739 0.4499 -0.1397 -0.1359 0.0096  345 ARG A NH2   
2711 N  N     . GLU A 348 ? 0.4892 0.4521 0.3294 -0.0267 -0.1077 -0.0370 346 GLU A N     
2712 C  CA    . GLU A 348 ? 0.4271 0.3427 0.3681 -0.0290 -0.1432 -0.0269 346 GLU A CA    
2713 C  C     . GLU A 348 ? 0.4289 0.2940 0.3802 0.0006  -0.1421 -0.0361 346 GLU A C     
2714 O  O     . GLU A 348 ? 0.4274 0.3363 0.3627 -0.0106 -0.1327 -0.0410 346 GLU A O     
2715 C  CB    . GLU A 348 ? 0.4066 0.3925 0.3613 0.0132  -0.0979 -0.0499 346 GLU A CB    
2716 C  CG    . GLU A 348 ? 0.4218 0.4373 0.3992 0.0168  -0.0965 -0.0248 346 GLU A CG    
2717 C  CD    . GLU A 348 ? 0.4308 0.3976 0.4080 -0.0008 -0.1020 -0.0266 346 GLU A CD    
2718 O  OE1   . GLU A 348 ? 0.4337 0.2910 0.4068 0.0352  -0.0974 -0.0055 346 GLU A OE1   
2719 O  OE2   . GLU A 348 ? 0.4525 0.5088 0.4504 0.0089  -0.0971 -0.0003 346 GLU A OE2   
2720 N  N     . HIS A 349 ? 0.4090 0.3106 0.3421 0.0040  -0.1504 -0.0221 347 HIS A N     
2721 C  CA    . HIS A 349 ? 0.4073 0.2993 0.3780 0.0056  -0.1522 -0.0127 347 HIS A CA    
2722 C  C     . HIS A 349 ? 0.3999 0.2941 0.3987 0.0204  -0.1544 -0.0054 347 HIS A C     
2723 O  O     . HIS A 349 ? 0.3548 0.2913 0.4115 0.0399  -0.1599 -0.0219 347 HIS A O     
2724 C  CB    . HIS A 349 ? 0.4496 0.3093 0.3671 0.0122  -0.1594 -0.0173 347 HIS A CB    
2725 C  CG    . HIS A 349 ? 0.4761 0.3279 0.3859 -0.0107 -0.1515 -0.0070 347 HIS A CG    
2726 N  ND1   . HIS A 349 ? 0.5454 0.3615 0.3937 -0.0244 -0.1574 -0.0158 347 HIS A ND1   
2727 C  CD2   . HIS A 349 ? 0.5216 0.3884 0.4030 -0.0255 -0.1582 -0.0320 347 HIS A CD2   
2728 C  CE1   . HIS A 349 ? 0.5826 0.3988 0.4160 -0.0634 -0.1613 -0.0288 347 HIS A CE1   
2729 N  NE2   . HIS A 349 ? 0.5690 0.3630 0.3688 -0.0365 -0.1588 -0.0134 347 HIS A NE2   
2730 N  N     . THR A 350 ? 0.3722 0.2852 0.4327 0.0265  -0.1656 -0.0034 348 THR A N     
2731 C  CA    . THR A 350 ? 0.3935 0.2553 0.4606 0.0479  -0.1815 0.0008  348 THR A CA    
2732 C  C     . THR A 350 ? 0.3864 0.3140 0.4732 0.0303  -0.1750 -0.0016 348 THR A C     
2733 O  O     . THR A 350 ? 0.3758 0.2751 0.4925 0.0568  -0.1702 0.0105  348 THR A O     
2734 C  CB    . THR A 350 ? 0.3563 0.2759 0.4810 0.0401  -0.1948 -0.0055 348 THR A CB    
2735 O  OG1   . THR A 350 ? 0.4297 0.2714 0.4411 0.0225  -0.2124 0.0009  348 THR A OG1   
2736 C  CG2   . THR A 350 ? 0.3889 0.3029 0.4923 0.0302  -0.1987 -0.0240 348 THR A CG2   
2737 N  N     . ILE A 351 ? 0.3604 0.3026 0.4708 0.0327  -0.1906 0.0117  349 ILE A N     
2738 C  CA    . ILE A 351 ? 0.3295 0.3379 0.5004 0.0339  -0.1708 0.0068  349 ILE A CA    
2739 C  C     . ILE A 351 ? 0.3896 0.3358 0.5431 0.0315  -0.1617 -0.0003 349 ILE A C     
2740 O  O     . ILE A 351 ? 0.4195 0.3187 0.5380 0.0643  -0.1805 0.0068  349 ILE A O     
2741 C  CB    . ILE A 351 ? 0.3368 0.2855 0.5474 0.0382  -0.1387 0.0046  349 ILE A CB    
2742 C  CG1   . ILE A 351 ? 0.3488 0.2734 0.5458 0.0245  -0.1073 -0.0025 349 ILE A CG1   
2743 C  CG2   . ILE A 351 ? 0.3420 0.3252 0.6147 0.0164  -0.1053 0.0199  349 ILE A CG2   
2744 C  CD1   . ILE A 351 ? 0.4297 0.2862 0.5738 0.0172  -0.0871 -0.0026 349 ILE A CD1   
2745 N  N     . GLU A 352 ? 0.3830 0.3255 0.5628 0.0293  -0.1970 -0.0356 350 GLU A N     
2746 C  CA    . GLU A 352 ? 0.4198 0.4026 0.6105 0.0369  -0.2018 -0.0254 350 GLU A CA    
2747 C  C     . GLU A 352 ? 0.3960 0.3102 0.5590 0.0292  -0.2399 -0.0371 350 GLU A C     
2748 O  O     . GLU A 352 ? 0.3808 0.3693 0.5874 0.0606  -0.2744 -0.0247 350 GLU A O     
2749 C  CB    . GLU A 352 ? 0.4753 0.4091 0.6803 0.0126  -0.1924 -0.0772 350 GLU A CB    
2750 C  CG    . GLU A 352 ? 0.5288 0.4677 0.7470 0.0384  -0.1886 -0.0275 350 GLU A CG    
2751 C  CD    . GLU A 352 ? 0.6042 0.4839 0.7962 0.1016  -0.1698 0.0146  350 GLU A CD    
2752 O  OE1   . GLU A 352 ? 0.6332 0.5316 0.8072 0.0902  -0.2453 0.0509  350 GLU A OE1   
2753 O  OE2   . GLU A 352 ? 0.6829 0.6104 0.8065 0.1300  -0.1717 -0.0265 350 GLU A OE2   
2754 N  N     . GLU A 353 ? 0.4210 0.3095 0.5505 0.0085  -0.2324 -0.0241 351 GLU A N     
2755 C  CA    . GLU A 353 ? 0.4430 0.3014 0.5223 0.0193  -0.2210 -0.0030 351 GLU A CA    
2756 C  C     . GLU A 353 ? 0.4525 0.3200 0.4814 0.0179  -0.2263 0.0121  351 GLU A C     
2757 O  O     . GLU A 353 ? 0.4351 0.2874 0.5178 -0.0006 -0.2217 -0.0116 351 GLU A O     
2758 C  CB    . GLU A 353 ? 0.4554 0.3291 0.4816 0.0122  -0.2012 -0.0187 351 GLU A CB    
2759 C  CG    . GLU A 353 ? 0.5147 0.4263 0.4707 0.0131  -0.2053 -0.0031 351 GLU A CG    
2760 C  CD    . GLU A 353 ? 0.5207 0.3891 0.4432 0.0282  -0.2227 -0.0252 351 GLU A CD    
2761 O  OE1   . GLU A 353 ? 0.5073 0.3261 0.4139 0.0368  -0.1954 0.0031  351 GLU A OE1   
2762 O  OE2   . GLU A 353 ? 0.5827 0.4301 0.4903 -0.0262 -0.2760 -0.0524 351 GLU A OE2   
2763 N  N     . TRP A 354 ? 0.3924 0.2923 0.4706 0.0266  -0.2373 0.0099  352 TRP A N     
2764 C  CA    . TRP A 354 ? 0.3903 0.3129 0.4718 0.0309  -0.2264 -0.0061 352 TRP A CA    
2765 C  C     . TRP A 354 ? 0.4258 0.3205 0.5357 0.0225  -0.2122 -0.0252 352 TRP A C     
2766 O  O     . TRP A 354 ? 0.3547 0.2691 0.5007 0.0431  -0.1908 -0.0155 352 TRP A O     
2767 C  CB    . TRP A 354 ? 0.4132 0.2712 0.4541 0.0255  -0.1768 -0.0159 352 TRP A CB    
2768 C  CG    . TRP A 354 ? 0.4023 0.2976 0.4314 0.0408  -0.1561 -0.0038 352 TRP A CG    
2769 C  CD1   . TRP A 354 ? 0.3792 0.2883 0.3857 0.0551  -0.1432 -0.0004 352 TRP A CD1   
2770 C  CD2   . TRP A 354 ? 0.4235 0.2868 0.4327 0.0267  -0.1355 -0.0095 352 TRP A CD2   
2771 N  NE1   . TRP A 354 ? 0.3924 0.2934 0.4050 0.0314  -0.1506 0.0048  352 TRP A NE1   
2772 C  CE2   . TRP A 354 ? 0.4108 0.2889 0.3942 0.0233  -0.1548 -0.0151 352 TRP A CE2   
2773 C  CE3   . TRP A 354 ? 0.4646 0.2797 0.4593 0.0395  -0.1251 -0.0401 352 TRP A CE3   
2774 C  CZ2   . TRP A 354 ? 0.4519 0.3143 0.4100 0.0266  -0.1153 -0.0411 352 TRP A CZ2   
2775 C  CZ3   . TRP A 354 ? 0.4540 0.3285 0.4481 0.0212  -0.1237 -0.0001 352 TRP A CZ3   
2776 C  CH2   . TRP A 354 ? 0.4484 0.3159 0.3934 0.0090  -0.1383 -0.0136 352 TRP A CH2   
2777 N  N     . LYS A 355 ? 0.4563 0.2797 0.6448 0.0083  -0.1792 0.0013  353 LYS A N     
2778 C  CA    . LYS A 355 ? 0.4349 0.3752 0.6591 0.0132  -0.2370 -0.0189 353 LYS A CA    
2779 C  C     . LYS A 355 ? 0.5276 0.3709 0.6863 0.0266  -0.2285 0.0019  353 LYS A C     
2780 O  O     . LYS A 355 ? 0.4962 0.3448 0.7424 0.0356  -0.2262 0.0090  353 LYS A O     
2781 C  CB    . LYS A 355 ? 0.4284 0.4057 0.7378 0.0104  -0.2309 -0.0266 353 LYS A CB    
2782 C  CG    . LYS A 355 ? 0.4343 0.4368 0.7985 0.0352  -0.2472 -0.0368 353 LYS A CG    
2783 C  CD    . LYS A 355 ? 0.4263 0.4485 0.8984 0.0214  -0.2582 -0.0368 353 LYS A CD    
2784 C  CE    . LYS A 355 ? 0.4629 0.4475 1.0283 0.0332  -0.2320 -0.0981 353 LYS A CE    
2785 N  NZ    . LYS A 355 ? 0.4469 0.5643 1.0696 0.0293  -0.2600 -0.1121 353 LYS A NZ    
2786 N  N     . GLU A 356 ? 0.5468 0.3261 0.6731 0.0120  -0.2357 -0.0067 354 GLU A N     
2787 C  CA    . GLU A 356 ? 0.5204 0.4118 0.6405 0.0317  -0.3205 0.0387  354 GLU A CA    
2788 C  C     . GLU A 356 ? 0.5588 0.3279 0.6580 0.0223  -0.3005 0.0721  354 GLU A C     
2789 O  O     . GLU A 356 ? 0.5724 0.3315 0.6386 0.0253  -0.3246 0.0557  354 GLU A O     
2790 C  CB    . GLU A 356 ? 0.5669 0.4645 0.7061 0.0151  -0.3205 0.0023  354 GLU A CB    
2791 C  CG    . GLU A 356 ? 0.6689 0.5621 0.7216 0.0101  -0.3329 0.0138  354 GLU A CG    
2792 C  CD    . GLU A 356 ? 0.7998 0.6234 0.7081 0.0034  -0.3576 0.0032  354 GLU A CD    
2793 O  OE1   . GLU A 356 ? 0.8780 0.6207 0.7492 -0.0161 -0.3449 -0.1072 354 GLU A OE1   
2794 O  OE2   . GLU A 356 ? 0.9753 0.7358 0.6297 -0.0357 -0.3210 0.0224  354 GLU A OE2   
2795 N  N     . LEU A 357 ? 0.5277 0.3150 0.5438 0.0057  -0.2521 0.0597  355 LEU A N     
2796 C  CA    . LEU A 357 ? 0.5602 0.3679 0.5373 0.0205  -0.2423 0.0709  355 LEU A CA    
2797 C  C     . LEU A 357 ? 0.5493 0.3218 0.5286 -0.0090 -0.2655 0.0484  355 LEU A C     
2798 O  O     . LEU A 357 ? 0.5246 0.2750 0.6095 -0.0144 -0.2721 0.0706  355 LEU A O     
2799 C  CB    . LEU A 357 ? 0.5613 0.4188 0.4783 0.0340  -0.2456 0.0697  355 LEU A CB    
2800 C  CG    . LEU A 357 ? 0.5923 0.4945 0.5069 0.0259  -0.2227 0.0702  355 LEU A CG    
2801 C  CD1   . LEU A 357 ? 0.5790 0.5092 0.5494 0.0433  -0.2107 0.0471  355 LEU A CD1   
2802 C  CD2   . LEU A 357 ? 0.6057 0.4718 0.5574 0.0238  -0.2263 0.0612  355 LEU A CD2   
2803 N  N     . ILE A 358 ? 0.4414 0.2840 0.5544 0.0143  -0.2523 0.0123  356 ILE A N     
2804 C  CA    . ILE A 358 ? 0.4192 0.3274 0.5533 0.0341  -0.2385 -0.0028 356 ILE A CA    
2805 C  C     . ILE A 358 ? 0.4993 0.2901 0.6357 0.0454  -0.2859 -0.0134 356 ILE A C     
2806 O  O     . ILE A 358 ? 0.4390 0.2441 0.6056 0.0693  -0.2749 -0.0011 356 ILE A O     
2807 C  CB    . ILE A 358 ? 0.3970 0.3222 0.5480 0.0433  -0.1965 0.0072  356 ILE A CB    
2808 C  CG1   . ILE A 358 ? 0.3710 0.3304 0.4991 0.0393  -0.1581 0.0233  356 ILE A CG1   
2809 C  CG2   . ILE A 358 ? 0.3845 0.3220 0.5732 0.0584  -0.2018 -0.0163 356 ILE A CG2   
2810 C  CD1   . ILE A 358 ? 0.3568 0.2764 0.4902 -0.0048 -0.1557 0.0068  356 ILE A CD1   
2811 N  N     . TYR A 359 ? 0.5237 0.2315 0.7061 0.0479  -0.3058 -0.0252 357 TYR A N     
2812 C  CA    . TYR A 359 ? 0.5378 0.3166 0.7408 0.0539  -0.3529 -0.0149 357 TYR A CA    
2813 C  C     . TYR A 359 ? 0.5814 0.2989 0.7099 0.0635  -0.3836 -0.0101 357 TYR A C     
2814 O  O     . TYR A 359 ? 0.5359 0.2808 0.7757 0.0776  -0.4297 -0.0159 357 TYR A O     
2815 C  CB    . TYR A 359 ? 0.5441 0.3596 0.7913 0.0429  -0.3534 -0.0048 357 TYR A CB    
2816 C  CG    . TYR A 359 ? 0.5286 0.3627 0.8721 0.0530  -0.3710 -0.0149 357 TYR A CG    
2817 C  CD1   . TYR A 359 ? 0.5629 0.3737 0.9512 0.0592  -0.3584 -0.0196 357 TYR A CD1   
2818 C  CD2   . TYR A 359 ? 0.6299 0.3407 0.9111 0.1204  -0.3656 -0.0372 357 TYR A CD2   
2819 C  CE1   . TYR A 359 ? 0.6562 0.3953 0.9872 0.1012  -0.3771 0.0494  357 TYR A CE1   
2820 C  CE2   . TYR A 359 ? 0.6402 0.4735 0.9828 0.1513  -0.4033 0.0020  357 TYR A CE2   
2821 C  CZ    . TYR A 359 ? 0.6749 0.4593 0.9997 0.1563  -0.4109 -0.0005 357 TYR A CZ    
2822 O  OH    . TYR A 359 ? 0.7543 0.4851 1.1789 0.2363  -0.4256 -0.0516 357 TYR A OH    
2823 N  N     . LYS A 360 ? 0.6446 0.3067 0.7298 0.0619  -0.3551 0.0127  358 LYS A N     
2824 C  CA    . LYS A 360 ? 0.6976 0.3892 0.7072 0.0392  -0.3696 0.0821  358 LYS A CA    
2825 C  C     . LYS A 360 ? 0.7070 0.3907 0.7347 0.0185  -0.3720 0.1307  358 LYS A C     
2826 O  O     . LYS A 360 ? 0.6757 0.4067 0.7332 0.0135  -0.4460 0.1381  358 LYS A O     
2827 C  CB    . LYS A 360 ? 0.7034 0.4686 0.7858 0.0426  -0.3274 0.0662  358 LYS A CB    
2828 C  CG    . LYS A 360 ? 0.7989 0.4994 0.7906 0.0514  -0.3206 0.0593  358 LYS A CG    
2829 C  CD    . LYS A 360 ? 0.8295 0.5664 0.7663 0.0227  -0.2754 0.0617  358 LYS A CD    
2830 C  CE    . LYS A 360 ? 0.9376 0.5862 0.8363 0.0047  -0.2344 0.0070  358 LYS A CE    
2831 N  NZ    . LYS A 360 ? 1.0043 0.6903 0.9206 0.0175  -0.2146 0.0544  358 LYS A NZ    
2832 N  N     . GLU A 361 ? 0.6969 0.4400 0.7306 -0.0192 -0.3530 0.1563  359 GLU A N     
2833 C  CA    . GLU A 361 ? 0.7119 0.4400 0.7319 -0.0315 -0.3312 0.1396  359 GLU A CA    
2834 C  C     . GLU A 361 ? 0.6905 0.4332 0.7933 0.0088  -0.3645 0.1580  359 GLU A C     
2835 O  O     . GLU A 361 ? 0.6847 0.4997 1.0280 -0.0053 -0.4322 0.1314  359 GLU A O     
2836 C  CB    . GLU A 361 ? 0.6757 0.4410 0.6578 -0.0213 -0.3068 0.1405  359 GLU A CB    
2837 C  CG    . GLU A 361 ? 0.6916 0.4672 0.5687 0.0127  -0.3163 0.1037  359 GLU A CG    
2838 C  CD    . GLU A 361 ? 0.7355 0.4587 0.5387 0.0311  -0.2958 0.1008  359 GLU A CD    
2839 O  OE1   . GLU A 361 ? 0.7427 0.5255 0.5330 0.0080  -0.3473 0.0615  359 GLU A OE1   
2840 O  OE2   . GLU A 361 ? 0.8519 0.5069 0.5864 0.0406  -0.2970 0.0831  359 GLU A OE2   
2841 N  N     . VAL A 362 ? 0.6999 0.3535 0.6576 0.0267  -0.3797 0.2046  360 VAL A N     
2842 C  CA    . VAL A 362 ? 0.7589 0.3044 0.7581 0.0897  -0.3458 0.1247  360 VAL A CA    
2843 C  C     . VAL A 362 ? 0.9258 0.4689 0.8318 0.1085  -0.4081 0.1609  360 VAL A C     
2844 O  O     . VAL A 362 ? 0.9647 0.4895 0.9735 -0.0151 -0.4220 -0.0043 360 VAL A O     
2845 C  CB    . VAL A 362 ? 0.7769 0.3512 0.7827 0.0789  -0.3433 0.0602  360 VAL A CB    
2846 C  CG1   . VAL A 362 ? 0.8250 0.4069 0.8623 0.0205  -0.2942 -0.0260 360 VAL A CG1   
2847 C  CG2   . VAL A 362 ? 0.8848 0.4115 0.7697 0.0581  -0.2480 0.0979  360 VAL A CG2   
2848 N  N     . MET A 363 ? 0.9708 0.4502 0.9293 0.0396  -0.4251 0.1003  361 MET A N     
2849 C  CA    . MET A 363 ? 0.9856 0.5855 1.0160 0.0320  -0.4412 0.1803  361 MET A CA    
2850 C  C     . MET A 363 ? 1.1108 0.4678 1.1030 0.0626  -0.3576 0.2121  361 MET A C     
2851 O  O     . MET A 363 ? 1.1544 0.5513 1.1804 0.1863  -0.3411 0.2633  361 MET A O     
2852 C  CB    . MET A 363 ? 0.8965 0.4917 1.1080 0.0104  -0.4528 0.2076  361 MET A CB    
2853 C  CG    . MET A 363 ? 0.7324 0.4691 1.1042 -0.0407 -0.5383 0.2466  361 MET A CG    
2854 S  SD    . MET A 363 ? 0.8937 0.8707 1.2139 -0.1825 -0.4321 0.0036  361 MET A SD    
2855 C  CE    . MET A 363 ? 0.9392 0.9778 1.2340 -0.1228 -0.3878 0.1410  361 MET A CE    
2856 N  N     . ASP A 364 ? 1.0972 0.5013 1.1210 -0.0401 -0.2681 0.2074  362 ASP A N     
2857 C  CA    . ASP A 364 ? 1.1153 0.5614 1.1527 -0.0739 -0.1873 0.1688  362 ASP A CA    
2858 C  C     . ASP A 364 ? 1.1380 0.6666 1.2040 -0.0565 -0.1356 0.1322  362 ASP A C     
2859 O  O     . ASP A 364 ? 1.0358 0.6833 1.2269 0.0064  -0.0518 0.1394  362 ASP A O     
2860 C  CB    . ASP A 364 ? 1.0350 0.5653 1.2015 -0.1619 -0.1471 0.1785  362 ASP A CB    
2861 N  N     . LEU A 365 ? 1.2005 0.5759 1.1259 0.0498  -0.1568 0.0218  363 LEU A N     
2862 C  CA    . LEU A 365 ? 1.1725 0.6190 1.0912 0.0353  -0.1700 0.0249  363 LEU A CA    
2863 C  C     . LEU A 365 ? 1.1881 0.5614 1.0218 -0.0073 -0.1752 -0.0491 363 LEU A C     
2864 O  O     . LEU A 365 ? 1.0811 0.7132 1.0641 -0.0834 -0.2527 -0.1101 363 LEU A O     
2865 C  CB    . LEU A 365 ? 1.1032 0.5207 1.0390 0.0515  -0.2348 0.0515  363 LEU A CB    
2866 MG MG    . MG  B .   ? 0.5884 0.8950 0.8885 -0.0810 -0.0251 -0.0226 401 MG  A MG    
2867 P  PG    . ANP C .   ? 0.8974 1.1046 1.4900 -0.1084 0.2035  0.2482  402 ANP A PG    
2868 O  O1G   . ANP C .   ? 0.8230 0.9481 1.3850 -0.0377 0.0462  0.1728  402 ANP A O1G   
2869 O  O2G   . ANP C .   ? 1.0673 0.9514 1.4883 -0.1297 0.2237  0.3354  402 ANP A O2G   
2870 O  O3G   . ANP C .   ? 0.6559 1.0475 1.4241 -0.1635 0.1295  0.1670  402 ANP A O3G   
2871 P  PB    . ANP C .   ? 1.1230 1.2321 1.5508 -0.3336 -0.1599 0.1682  402 ANP A PB    
2872 O  O1B   . ANP C .   ? 1.2935 1.3379 1.5700 -0.2812 -0.0275 0.1822  402 ANP A O1B   
2873 O  O2B   . ANP C .   ? 1.1275 1.3427 1.6243 -0.4193 -0.1591 0.1153  402 ANP A O2B   
2874 N  N3B   . ANP C .   ? 0.8799 1.1496 1.5186 -0.2265 0.0347  0.1801  402 ANP A N3B   
2875 P  PA    . ANP C .   ? 1.0558 0.8091 1.1404 -0.1413 -0.0069 0.0851  402 ANP A PA    
2876 O  O1A   . ANP C .   ? 1.0939 1.0606 1.1735 -0.1087 -0.1003 0.1035  402 ANP A O1A   
2877 O  O2A   . ANP C .   ? 1.0842 0.6601 1.2441 -0.0847 0.0600  0.0035  402 ANP A O2A   
2878 O  O3A   . ANP C .   ? 1.0783 1.0893 1.2635 -0.2312 -0.1383 0.1569  402 ANP A O3A   
2879 O  "O5'" . ANP C .   ? 0.9650 0.6448 1.0779 -0.1032 -0.0042 0.1354  402 ANP A "O5'" 
2880 C  "C5'" . ANP C .   ? 0.9148 0.6140 0.8850 -0.0508 0.1085  0.0440  402 ANP A "C5'" 
2881 C  "C4'" . ANP C .   ? 0.8261 0.6511 0.7928 -0.0593 0.1015  0.0372  402 ANP A "C4'" 
2882 O  "O4'" . ANP C .   ? 0.8012 0.5912 0.7683 -0.0385 0.1726  0.0182  402 ANP A "O4'" 
2883 C  "C3'" . ANP C .   ? 0.7640 0.6911 0.7344 0.0155  0.0825  0.0652  402 ANP A "C3'" 
2884 O  "O3'" . ANP C .   ? 0.8138 0.6679 0.5198 0.0411  0.1172  0.1933  402 ANP A "O3'" 
2885 C  "C2'" . ANP C .   ? 0.7373 0.6365 0.6966 0.0256  0.1062  0.0284  402 ANP A "C2'" 
2886 O  "O2'" . ANP C .   ? 0.6637 0.7648 0.6684 0.0643  0.0984  0.0944  402 ANP A "O2'" 
2887 C  "C1'" . ANP C .   ? 0.7129 0.5954 0.7171 0.0149  0.1379  -0.0146 402 ANP A "C1'" 
2888 N  N9    . ANP C .   ? 0.6723 0.5345 0.7220 -0.0084 0.1122  -0.0122 402 ANP A N9    
2889 C  C8    . ANP C .   ? 0.5526 0.4807 0.6811 -0.0387 0.0479  -0.0538 402 ANP A C8    
2890 N  N7    . ANP C .   ? 0.4803 0.4623 0.6373 -0.0061 0.0455  -0.0762 402 ANP A N7    
2891 C  C5    . ANP C .   ? 0.5342 0.4776 0.6363 -0.0217 0.0488  -0.0384 402 ANP A C5    
2892 C  C6    . ANP C .   ? 0.4668 0.4793 0.5859 -0.0075 0.0510  -0.0395 402 ANP A C6    
2893 N  N6    . ANP C .   ? 0.4086 0.4368 0.5553 -0.0313 0.0221  -0.0687 402 ANP A N6    
2894 N  N1    . ANP C .   ? 0.4631 0.4997 0.5953 -0.0146 0.0077  -0.0425 402 ANP A N1    
2895 C  C2    . ANP C .   ? 0.5123 0.5585 0.6351 -0.0065 0.0731  -0.0481 402 ANP A C2    
2896 N  N3    . ANP C .   ? 0.5401 0.5337 0.5578 -0.0609 0.0805  -0.0113 402 ANP A N3    
2897 C  C4    . ANP C .   ? 0.6046 0.5190 0.6651 -0.0250 0.1000  -0.0230 402 ANP A C4    
# 
