data_9BSQ
# 
_entry.id   9BSQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9BSQ         pdb_00009bsq 10.2210/pdb9bsq/pdb 
WWPDB D_1000284068 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BSQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              wliu@chem.tamu.edu 
_pdbx_contact_author.name_first         Wenshe 
_pdbx_contact_author.name_last          Liu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-7078-6534 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Blankenship, L.R.' 1 0000-0002-1714-4399 
'Liu, W.R.'         2 0000-0002-7078-6534 
# 
_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                     'Structure of the SARS-CoV-2 main protease' 
_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 'Blankenship, L.R.' 1 ? 
primary 'Liu, W.R.'         2 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '3C-like proteinase nsp5'                                                                            33825.547 1 
3.4.22.69 ? ? ? 
2 non-polymer syn "(2R)-N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-2-hydroxy-2-sulfanylacetamide" 405.298   1 
?         ? ? ? 
3 water       nat water                                                                                                18.015    
234 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_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 "(2R)-N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-2-hydroxy-2-sulfanylacetamide" A1ARY 
3 water                                                                                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ARY non-polymer         . "(2R)-N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-2-hydroxy-2-sulfanylacetamide" ? 
'C19 H14 Cl2 N2 O2 S' 405.298 
ALA   'L-peptide linking' y ALANINE                                                                                              ? 
'C3 H7 N O2'          89.093  
ARG   'L-peptide linking' y ARGININE                                                                                             ? 
'C6 H15 N4 O2 1'      175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                           ? 
'C4 H8 N2 O3'         132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                      ? 
'C4 H7 N O4'          133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                             ? 
'C3 H7 N O2 S'        121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                            ? 
'C5 H10 N2 O3'        146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                      ? 
'C5 H9 N O4'          147.129 
GLY   'peptide linking'   y GLYCINE                                                                                              ? 
'C2 H5 N O2'          75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                            ? 
'C6 H10 N3 O2 1'      156.162 
HOH   non-polymer         . WATER                                                                                                ? 
'H2 O'                18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                           ? 
'C6 H13 N O2'         131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                              ? 
'C6 H13 N O2'         131.173 
LYS   'L-peptide linking' y LYSINE                                                                                               ? 
'C6 H15 N2 O2 1'      147.195 
MET   'L-peptide linking' y METHIONINE                                                                                           ? 
'C5 H11 N O2 S'       149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                        ? 
'C9 H11 N O2'         165.189 
PRO   'L-peptide linking' y PROLINE                                                                                              ? 
'C5 H9 N O2'          115.130 
SER   'L-peptide linking' y SERINE                                                                                               ? 
'C3 H7 N O3'          105.093 
THR   'L-peptide linking' y THREONINE                                                                                            ? 
'C4 H9 N O3'          119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                           ? 
'C11 H12 N2 O2'       204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                             ? 
'C9 H11 N O3'         181.189 
VAL   'L-peptide linking' y VALINE                                                                                               ? 
'C5 H11 N O2'         117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 GLY 302 302 302 GLY GLY A . n 
A 1 303 VAL 303 303 303 VAL VAL A . n 
A 1 304 THR 304 304 304 THR THR A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ARY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ARY 
_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 A1ARY 1   401 401 A1ARY LIG A . 
C 3 HOH   1   501 13  HOH   HOH A . 
C 3 HOH   2   502 193 HOH   HOH A . 
C 3 HOH   3   503 111 HOH   HOH A . 
C 3 HOH   4   504 230 HOH   HOH A . 
C 3 HOH   5   505 196 HOH   HOH A . 
C 3 HOH   6   506 166 HOH   HOH A . 
C 3 HOH   7   507 199 HOH   HOH A . 
C 3 HOH   8   508 44  HOH   HOH A . 
C 3 HOH   9   509 128 HOH   HOH A . 
C 3 HOH   10  510 70  HOH   HOH A . 
C 3 HOH   11  511 172 HOH   HOH A . 
C 3 HOH   12  512 206 HOH   HOH A . 
C 3 HOH   13  513 177 HOH   HOH A . 
C 3 HOH   14  514 138 HOH   HOH A . 
C 3 HOH   15  515 48  HOH   HOH A . 
C 3 HOH   16  516 51  HOH   HOH A . 
C 3 HOH   17  517 108 HOH   HOH A . 
C 3 HOH   18  518 167 HOH   HOH A . 
C 3 HOH   19  519 217 HOH   HOH A . 
C 3 HOH   20  520 102 HOH   HOH A . 
C 3 HOH   21  521 63  HOH   HOH A . 
C 3 HOH   22  522 188 HOH   HOH A . 
C 3 HOH   23  523 211 HOH   HOH A . 
C 3 HOH   24  524 76  HOH   HOH A . 
C 3 HOH   25  525 154 HOH   HOH A . 
C 3 HOH   26  526 83  HOH   HOH A . 
C 3 HOH   27  527 169 HOH   HOH A . 
C 3 HOH   28  528 43  HOH   HOH A . 
C 3 HOH   29  529 50  HOH   HOH A . 
C 3 HOH   30  530 62  HOH   HOH A . 
C 3 HOH   31  531 163 HOH   HOH A . 
C 3 HOH   32  532 3   HOH   HOH A . 
C 3 HOH   33  533 35  HOH   HOH A . 
C 3 HOH   34  534 60  HOH   HOH A . 
C 3 HOH   35  535 81  HOH   HOH A . 
C 3 HOH   36  536 4   HOH   HOH A . 
C 3 HOH   37  537 6   HOH   HOH A . 
C 3 HOH   38  538 82  HOH   HOH A . 
C 3 HOH   39  539 17  HOH   HOH A . 
C 3 HOH   40  540 186 HOH   HOH A . 
C 3 HOH   41  541 232 HOH   HOH A . 
C 3 HOH   42  542 210 HOH   HOH A . 
C 3 HOH   43  543 113 HOH   HOH A . 
C 3 HOH   44  544 23  HOH   HOH A . 
C 3 HOH   45  545 158 HOH   HOH A . 
C 3 HOH   46  546 99  HOH   HOH A . 
C 3 HOH   47  547 27  HOH   HOH A . 
C 3 HOH   48  548 119 HOH   HOH A . 
C 3 HOH   49  549 161 HOH   HOH A . 
C 3 HOH   50  550 106 HOH   HOH A . 
C 3 HOH   51  551 135 HOH   HOH A . 
C 3 HOH   52  552 33  HOH   HOH A . 
C 3 HOH   53  553 59  HOH   HOH A . 
C 3 HOH   54  554 97  HOH   HOH A . 
C 3 HOH   55  555 53  HOH   HOH A . 
C 3 HOH   56  556 234 HOH   HOH A . 
C 3 HOH   57  557 74  HOH   HOH A . 
C 3 HOH   58  558 61  HOH   HOH A . 
C 3 HOH   59  559 2   HOH   HOH A . 
C 3 HOH   60  560 157 HOH   HOH A . 
C 3 HOH   61  561 123 HOH   HOH A . 
C 3 HOH   62  562 103 HOH   HOH A . 
C 3 HOH   63  563 68  HOH   HOH A . 
C 3 HOH   64  564 127 HOH   HOH A . 
C 3 HOH   65  565 224 HOH   HOH A . 
C 3 HOH   66  566 159 HOH   HOH A . 
C 3 HOH   67  567 80  HOH   HOH A . 
C 3 HOH   68  568 120 HOH   HOH A . 
C 3 HOH   69  569 78  HOH   HOH A . 
C 3 HOH   70  570 56  HOH   HOH A . 
C 3 HOH   71  571 11  HOH   HOH A . 
C 3 HOH   72  572 121 HOH   HOH A . 
C 3 HOH   73  573 29  HOH   HOH A . 
C 3 HOH   74  574 183 HOH   HOH A . 
C 3 HOH   75  575 148 HOH   HOH A . 
C 3 HOH   76  576 198 HOH   HOH A . 
C 3 HOH   77  577 9   HOH   HOH A . 
C 3 HOH   78  578 86  HOH   HOH A . 
C 3 HOH   79  579 65  HOH   HOH A . 
C 3 HOH   80  580 39  HOH   HOH A . 
C 3 HOH   81  581 215 HOH   HOH A . 
C 3 HOH   82  582 141 HOH   HOH A . 
C 3 HOH   83  583 18  HOH   HOH A . 
C 3 HOH   84  584 15  HOH   HOH A . 
C 3 HOH   85  585 7   HOH   HOH A . 
C 3 HOH   86  586 16  HOH   HOH A . 
C 3 HOH   87  587 28  HOH   HOH A . 
C 3 HOH   88  588 8   HOH   HOH A . 
C 3 HOH   89  589 54  HOH   HOH A . 
C 3 HOH   90  590 55  HOH   HOH A . 
C 3 HOH   91  591 104 HOH   HOH A . 
C 3 HOH   92  592 30  HOH   HOH A . 
C 3 HOH   93  593 101 HOH   HOH A . 
C 3 HOH   94  594 41  HOH   HOH A . 
C 3 HOH   95  595 142 HOH   HOH A . 
C 3 HOH   96  596 94  HOH   HOH A . 
C 3 HOH   97  597 77  HOH   HOH A . 
C 3 HOH   98  598 178 HOH   HOH A . 
C 3 HOH   99  599 124 HOH   HOH A . 
C 3 HOH   100 600 146 HOH   HOH A . 
C 3 HOH   101 601 40  HOH   HOH A . 
C 3 HOH   102 602 72  HOH   HOH A . 
C 3 HOH   103 603 152 HOH   HOH A . 
C 3 HOH   104 604 228 HOH   HOH A . 
C 3 HOH   105 605 132 HOH   HOH A . 
C 3 HOH   106 606 133 HOH   HOH A . 
C 3 HOH   107 607 214 HOH   HOH A . 
C 3 HOH   108 608 1   HOH   HOH A . 
C 3 HOH   109 609 64  HOH   HOH A . 
C 3 HOH   110 610 117 HOH   HOH A . 
C 3 HOH   111 611 26  HOH   HOH A . 
C 3 HOH   112 612 96  HOH   HOH A . 
C 3 HOH   113 613 87  HOH   HOH A . 
C 3 HOH   114 614 42  HOH   HOH A . 
C 3 HOH   115 615 49  HOH   HOH A . 
C 3 HOH   116 616 151 HOH   HOH A . 
C 3 HOH   117 617 21  HOH   HOH A . 
C 3 HOH   118 618 90  HOH   HOH A . 
C 3 HOH   119 619 12  HOH   HOH A . 
C 3 HOH   120 620 38  HOH   HOH A . 
C 3 HOH   121 621 14  HOH   HOH A . 
C 3 HOH   122 622 114 HOH   HOH A . 
C 3 HOH   123 623 220 HOH   HOH A . 
C 3 HOH   124 624 92  HOH   HOH A . 
C 3 HOH   125 625 52  HOH   HOH A . 
C 3 HOH   126 626 58  HOH   HOH A . 
C 3 HOH   127 627 10  HOH   HOH A . 
C 3 HOH   128 628 34  HOH   HOH A . 
C 3 HOH   129 629 131 HOH   HOH A . 
C 3 HOH   130 630 155 HOH   HOH A . 
C 3 HOH   131 631 140 HOH   HOH A . 
C 3 HOH   132 632 125 HOH   HOH A . 
C 3 HOH   133 633 25  HOH   HOH A . 
C 3 HOH   134 634 20  HOH   HOH A . 
C 3 HOH   135 635 22  HOH   HOH A . 
C 3 HOH   136 636 187 HOH   HOH A . 
C 3 HOH   137 637 229 HOH   HOH A . 
C 3 HOH   138 638 5   HOH   HOH A . 
C 3 HOH   139 639 67  HOH   HOH A . 
C 3 HOH   140 640 122 HOH   HOH A . 
C 3 HOH   141 641 93  HOH   HOH A . 
C 3 HOH   142 642 216 HOH   HOH A . 
C 3 HOH   143 643 46  HOH   HOH A . 
C 3 HOH   144 644 95  HOH   HOH A . 
C 3 HOH   145 645 212 HOH   HOH A . 
C 3 HOH   146 646 105 HOH   HOH A . 
C 3 HOH   147 647 36  HOH   HOH A . 
C 3 HOH   148 648 32  HOH   HOH A . 
C 3 HOH   149 649 144 HOH   HOH A . 
C 3 HOH   150 650 226 HOH   HOH A . 
C 3 HOH   151 651 45  HOH   HOH A . 
C 3 HOH   152 652 190 HOH   HOH A . 
C 3 HOH   153 653 115 HOH   HOH A . 
C 3 HOH   154 654 24  HOH   HOH A . 
C 3 HOH   155 655 75  HOH   HOH A . 
C 3 HOH   156 656 147 HOH   HOH A . 
C 3 HOH   157 657 195 HOH   HOH A . 
C 3 HOH   158 658 71  HOH   HOH A . 
C 3 HOH   159 659 66  HOH   HOH A . 
C 3 HOH   160 660 100 HOH   HOH A . 
C 3 HOH   161 661 107 HOH   HOH A . 
C 3 HOH   162 662 179 HOH   HOH A . 
C 3 HOH   163 663 19  HOH   HOH A . 
C 3 HOH   164 664 139 HOH   HOH A . 
C 3 HOH   165 665 207 HOH   HOH A . 
C 3 HOH   166 666 173 HOH   HOH A . 
C 3 HOH   167 667 69  HOH   HOH A . 
C 3 HOH   168 668 225 HOH   HOH A . 
C 3 HOH   169 669 84  HOH   HOH A . 
C 3 HOH   170 670 57  HOH   HOH A . 
C 3 HOH   171 671 181 HOH   HOH A . 
C 3 HOH   172 672 126 HOH   HOH A . 
C 3 HOH   173 673 98  HOH   HOH A . 
C 3 HOH   174 674 162 HOH   HOH A . 
C 3 HOH   175 675 174 HOH   HOH A . 
C 3 HOH   176 676 164 HOH   HOH A . 
C 3 HOH   177 677 221 HOH   HOH A . 
C 3 HOH   178 678 109 HOH   HOH A . 
C 3 HOH   179 679 223 HOH   HOH A . 
C 3 HOH   180 680 112 HOH   HOH A . 
C 3 HOH   181 681 189 HOH   HOH A . 
C 3 HOH   182 682 170 HOH   HOH A . 
C 3 HOH   183 683 200 HOH   HOH A . 
C 3 HOH   184 684 202 HOH   HOH A . 
C 3 HOH   185 685 89  HOH   HOH A . 
C 3 HOH   186 686 233 HOH   HOH A . 
C 3 HOH   187 687 182 HOH   HOH A . 
C 3 HOH   188 688 191 HOH   HOH A . 
C 3 HOH   189 689 176 HOH   HOH A . 
C 3 HOH   190 690 73  HOH   HOH A . 
C 3 HOH   191 691 208 HOH   HOH A . 
C 3 HOH   192 692 129 HOH   HOH A . 
C 3 HOH   193 693 134 HOH   HOH A . 
C 3 HOH   194 694 194 HOH   HOH A . 
C 3 HOH   195 695 165 HOH   HOH A . 
C 3 HOH   196 696 160 HOH   HOH A . 
C 3 HOH   197 697 136 HOH   HOH A . 
C 3 HOH   198 698 175 HOH   HOH A . 
C 3 HOH   199 699 91  HOH   HOH A . 
C 3 HOH   200 700 185 HOH   HOH A . 
C 3 HOH   201 701 204 HOH   HOH A . 
C 3 HOH   202 702 201 HOH   HOH A . 
C 3 HOH   203 703 150 HOH   HOH A . 
C 3 HOH   204 704 85  HOH   HOH A . 
C 3 HOH   205 705 88  HOH   HOH A . 
C 3 HOH   206 706 130 HOH   HOH A . 
C 3 HOH   207 707 227 HOH   HOH A . 
C 3 HOH   208 708 209 HOH   HOH A . 
C 3 HOH   209 709 156 HOH   HOH A . 
C 3 HOH   210 710 180 HOH   HOH A . 
C 3 HOH   211 711 222 HOH   HOH A . 
C 3 HOH   212 712 110 HOH   HOH A . 
C 3 HOH   213 713 205 HOH   HOH A . 
C 3 HOH   214 714 149 HOH   HOH A . 
C 3 HOH   215 715 231 HOH   HOH A . 
C 3 HOH   216 716 118 HOH   HOH A . 
C 3 HOH   217 717 219 HOH   HOH A . 
C 3 HOH   218 718 192 HOH   HOH A . 
C 3 HOH   219 719 37  HOH   HOH A . 
C 3 HOH   220 720 213 HOH   HOH A . 
C 3 HOH   221 721 31  HOH   HOH A . 
C 3 HOH   222 722 116 HOH   HOH A . 
C 3 HOH   223 723 79  HOH   HOH A . 
C 3 HOH   224 724 47  HOH   HOH A . 
C 3 HOH   225 725 153 HOH   HOH A . 
C 3 HOH   226 726 137 HOH   HOH A . 
C 3 HOH   227 727 171 HOH   HOH A . 
C 3 HOH   228 728 203 HOH   HOH A . 
C 3 HOH   229 729 168 HOH   HOH A . 
C 3 HOH   230 730 184 HOH   HOH A . 
C 3 HOH   231 731 197 HOH   HOH A . 
C 3 HOH   232 732 145 HOH   HOH A . 
C 3 HOH   233 733 143 HOH   HOH A . 
C 3 HOH   234 734 218 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? 1.20.1_4487 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT    ? ? ? .           2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless        ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.850 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BSQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.003 
_cell.length_a_esd                 ? 
_cell.length_b                     80.223 
_cell.length_b_esd                 ? 
_cell.length_c                     89.155 
_cell.length_c_esd                 ? 
_cell.volume                       362183.889 
_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                         9BSQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y (x,y,-x+z)' 
_symmetry.space_group_name_H-M             'I 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BSQ 
_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             2.77 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.54 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.2 M Ammonium phosphate dibasic, 17%
W/v PEG3350, pH8.0
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     120 
_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                         'Bruker PHOTON II' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-07-11 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54301 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-002' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54301 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          17.76 
_reflns.entry_id                                       9BSQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               24.0 
_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                                     32145 
_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                           96.74 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.81 
_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                                0.09277 
_reflns.pdbx_Rpim_I_all                                0.03255 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.08642 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.8 
_reflns_shell.d_res_low                                     1.864 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.02 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3051 
_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                               0.7463 
_reflns_shell.pdbx_Rpim_I_all                               0.3731 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.809 
_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                                  0.6401 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               25.65 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BSQ 
_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                            1.80 
_refine.ls_d_res_low                             24.00 
_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                     32003 
_refine.ls_number_reflns_R_free                  1561 
_refine.ls_number_reflns_R_work                  30442 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.78 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2282 
_refine.ls_R_factor_R_free                       0.2477 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2272 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.5544 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.2092 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        24.00 
_refine_hist.number_atoms_solvent             234 
_refine_hist.number_atoms_total               2626 
_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        2367 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0091 ? 2447 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1290 ? 3326 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0564 ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0092 ? 432  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.1755 ? 330  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.86  . . 132 2654 92.22 . . . . 0.3075 . . . . . . . . . . . 0.3274 
'X-RAY DIFFRACTION' 1.86 1.92  . . 121 2660 94.40 . . . . 0.2905 . . . . . . . . . . . 0.2790 
'X-RAY DIFFRACTION' 1.92 2.00  . . 137 2715 95.45 . . . . 0.2812 . . . . . . . . . . . 0.3076 
'X-RAY DIFFRACTION' 2.00 2.09  . . 151 2722 95.61 . . . . 0.2814 . . . . . . . . . . . 0.3165 
'X-RAY DIFFRACTION' 2.09 2.20  . . 151 2742 96.59 . . . . 0.2820 . . . . . . . . . . . 0.3670 
'X-RAY DIFFRACTION' 2.20 2.34  . . 153 2751 96.51 . . . . 0.2812 . . . . . . . . . . . 0.3096 
'X-RAY DIFFRACTION' 2.34 2.52  . . 142 2781 97.24 . . . . 0.2714 . . . . . . . . . . . 0.3042 
'X-RAY DIFFRACTION' 2.52 2.77  . . 138 2816 98.63 . . . . 0.2540 . . . . . . . . . . . 0.2643 
'X-RAY DIFFRACTION' 2.77 3.17  . . 157 2844 99.27 . . . . 0.2185 . . . . . . . . . . . 0.2534 
'X-RAY DIFFRACTION' 3.18 4.00  . . 153 2849 99.60 . . . . 0.1854 . . . . . . . . . . . 0.1852 
'X-RAY DIFFRACTION' 4.00 24.00 . . 126 2908 98.99 . . . . 0.1642 . . . . . . . . . . . 0.1645 
# 
_struct.entry_id                     9BSQ 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor VB-C-70' 
_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        9BSQ 
_struct_keywords.text            'main protease, VIRAL PROTEIN, Hydrolase' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9BSQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 306 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DTD1 
_struct_ref_seq.db_align_beg                  3264 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  3569 
_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       306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4800  ? 
1 MORE         -21   ? 
1 'SSA (A^2)'  24150 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_455 -x-1,y,-z -1.0000000000 0.0000000000 0.0000000000 -51.0030000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        one 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            145 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           A1ARY 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C4 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             145 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            A1ARY 
_struct_conn.ptnr2_auth_seq_id             401 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.852 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1ARY 
_pdbx_modification_feature.label_asym_id                      B 
_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      145 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1ARY 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        401 
_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       145 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C4 
_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                        A1ARY 
_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 ? 7 ? 
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 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? 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 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9BSQ 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 688 ? ? O A HOH 727 ? ? 1.97 
2  1 O   A HOH 503 ? ? O A HOH 681 ? ? 2.01 
3  1 O   A HOH 681 ? ? O A HOH 703 ? ? 2.02 
4  1 O   A ALA 194 ? ? O A HOH 501 ? ? 2.02 
5  1 OE1 A GLU 270 ? ? O A HOH 502 ? ? 2.05 
6  1 O   A HOH 715 ? ? O A HOH 734 ? ? 2.12 
7  1 O   A HOH 505 ? ? O A HOH 717 ? ? 2.13 
8  1 OE1 A GLU 240 ? ? O A HOH 503 ? ? 2.14 
9  1 O   A HOH 515 ? ? O A HOH 681 ? ? 2.15 
10 1 OE2 A GLU 166 ? ? O A HOH 504 ? ? 2.19 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             C 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ALA 
_pdbx_validate_rmsd_angle.auth_seq_id_1              194 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             N 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             GLY 
_pdbx_validate_rmsd_angle.auth_seq_id_2              195 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLY 
_pdbx_validate_rmsd_angle.auth_seq_id_3              195 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                108.49 
_pdbx_validate_rmsd_angle.angle_target_value         122.30 
_pdbx_validate_rmsd_angle.angle_deviation            -13.81 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                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 ASP A 33  ? ? 50.36   -132.26 
2 1 ASN A 72  ? ? -97.28  33.08   
3 1 ASN A 84  ? ? 57.09   -120.74 
4 1 TYR A 154 ? ? 43.99   -107.41 
5 1 SER A 301 ? ? -140.15 -40.42  
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 544 ? C HOH . 
2 1 A HOH 621 ? C HOH . 
3 1 A HOH 654 ? C HOH . 
4 1 A HOH 672 ? C HOH . 
5 1 A HOH 702 ? C HOH . 
6 1 A HOH 722 ? C HOH . 
7 1 A HOH 729 ? C HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -x,y,-z             
3 x+1/2,y+1/2,z+1/2   
4 -x+1/2,y+1/2,-z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -12.7544162589 
_pdbx_refine_tls.origin_y         -15.3178402298 
_pdbx_refine_tls.origin_z         -1.02484487313 
_pdbx_refine_tls.T[1][1]          0.0675787050097 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.000624260249161 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0267767806552 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.091033526227 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0039417650832 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0798138783836 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.93566676766 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.416875160524 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.331255945815 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.80745857094 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.591052302916 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.34601608829 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0309615882379 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.00669578319026 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.00535097264916 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0664335060477 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0209646919565 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0671365194172 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0299745190832 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0241277351451 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.00386726939656 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   B 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     401 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 
A1ARY N1   N  N N 1   
A1ARY C4   C  N R 2   
A1ARY C5   C  Y N 3   
A1ARY C6   C  Y N 4   
A1ARY C7   C  Y N 5   
A1ARY C8   C  Y N 6   
A1ARY C10  C  Y N 7   
A1ARY C13  C  Y N 8   
A1ARY C15  C  Y N 9   
A1ARY C17  C  Y N 10  
A1ARY C1   C  Y N 11  
A1ARY C11  C  Y N 12  
A1ARY C12  C  Y N 13  
A1ARY C14  C  Y N 14  
A1ARY C16  C  Y N 15  
A1ARY C18  C  Y N 16  
A1ARY C19  C  Y N 17  
A1ARY C2   C  Y N 18  
A1ARY C3   C  N N 19  
A1ARY C9   C  Y N 20  
A1ARY N2   N  Y N 21  
A1ARY O1   O  N N 22  
A1ARY O2   O  N N 23  
A1ARY CL1  CL N N 24  
A1ARY CL2  CL N N 25  
A1ARY H1   H  N N 26  
A1ARY H2   H  N N 27  
A1ARY H3   H  N N 28  
A1ARY H4   H  N N 29  
A1ARY H7   H  N N 30  
A1ARY H9   H  N N 31  
A1ARY H6   H  N N 32  
A1ARY H8   H  N N 33  
A1ARY H10  H  N N 34  
A1ARY H11  H  N N 35  
A1ARY H12  H  N N 36  
A1ARY H5   H  N N 37  
A1ARY H13  H  N N 38  
A1ARY S1   S  N N 39  
A1ARY HS   H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
GLN   N    N  N N 128 
GLN   CA   C  N S 129 
GLN   C    C  N N 130 
GLN   O    O  N N 131 
GLN   CB   C  N N 132 
GLN   CG   C  N N 133 
GLN   CD   C  N N 134 
GLN   OE1  O  N N 135 
GLN   NE2  N  N N 136 
GLN   OXT  O  N N 137 
GLN   H    H  N N 138 
GLN   H2   H  N N 139 
GLN   HA   H  N N 140 
GLN   HB2  H  N N 141 
GLN   HB3  H  N N 142 
GLN   HG2  H  N N 143 
GLN   HG3  H  N N 144 
GLN   HE21 H  N N 145 
GLN   HE22 H  N N 146 
GLN   HXT  H  N N 147 
GLU   N    N  N N 148 
GLU   CA   C  N S 149 
GLU   C    C  N N 150 
GLU   O    O  N N 151 
GLU   CB   C  N N 152 
GLU   CG   C  N N 153 
GLU   CD   C  N N 154 
GLU   OE1  O  N N 155 
GLU   OE2  O  N N 156 
GLU   OXT  O  N N 157 
GLU   H    H  N N 158 
GLU   H2   H  N N 159 
GLU   HA   H  N N 160 
GLU   HB2  H  N N 161 
GLU   HB3  H  N N 162 
GLU   HG2  H  N N 163 
GLU   HG3  H  N N 164 
GLU   HE2  H  N N 165 
GLU   HXT  H  N N 166 
GLY   N    N  N N 167 
GLY   CA   C  N N 168 
GLY   C    C  N N 169 
GLY   O    O  N N 170 
GLY   OXT  O  N N 171 
GLY   H    H  N N 172 
GLY   H2   H  N N 173 
GLY   HA2  H  N N 174 
GLY   HA3  H  N N 175 
GLY   HXT  H  N N 176 
HIS   N    N  N N 177 
HIS   CA   C  N S 178 
HIS   C    C  N N 179 
HIS   O    O  N N 180 
HIS   CB   C  N N 181 
HIS   CG   C  Y N 182 
HIS   ND1  N  Y N 183 
HIS   CD2  C  Y N 184 
HIS   CE1  C  Y N 185 
HIS   NE2  N  Y N 186 
HIS   OXT  O  N N 187 
HIS   H    H  N N 188 
HIS   H2   H  N N 189 
HIS   HA   H  N N 190 
HIS   HB2  H  N N 191 
HIS   HB3  H  N N 192 
HIS   HD1  H  N N 193 
HIS   HD2  H  N N 194 
HIS   HE1  H  N N 195 
HIS   HE2  H  N N 196 
HIS   HXT  H  N N 197 
HOH   O    O  N N 198 
HOH   H1   H  N N 199 
HOH   H2   H  N N 200 
ILE   N    N  N N 201 
ILE   CA   C  N S 202 
ILE   C    C  N N 203 
ILE   O    O  N N 204 
ILE   CB   C  N S 205 
ILE   CG1  C  N N 206 
ILE   CG2  C  N N 207 
ILE   CD1  C  N N 208 
ILE   OXT  O  N N 209 
ILE   H    H  N N 210 
ILE   H2   H  N N 211 
ILE   HA   H  N N 212 
ILE   HB   H  N N 213 
ILE   HG12 H  N N 214 
ILE   HG13 H  N N 215 
ILE   HG21 H  N N 216 
ILE   HG22 H  N N 217 
ILE   HG23 H  N N 218 
ILE   HD11 H  N N 219 
ILE   HD12 H  N N 220 
ILE   HD13 H  N N 221 
ILE   HXT  H  N N 222 
LEU   N    N  N N 223 
LEU   CA   C  N S 224 
LEU   C    C  N N 225 
LEU   O    O  N N 226 
LEU   CB   C  N N 227 
LEU   CG   C  N N 228 
LEU   CD1  C  N N 229 
LEU   CD2  C  N N 230 
LEU   OXT  O  N N 231 
LEU   H    H  N N 232 
LEU   H2   H  N N 233 
LEU   HA   H  N N 234 
LEU   HB2  H  N N 235 
LEU   HB3  H  N N 236 
LEU   HG   H  N N 237 
LEU   HD11 H  N N 238 
LEU   HD12 H  N N 239 
LEU   HD13 H  N N 240 
LEU   HD21 H  N N 241 
LEU   HD22 H  N N 242 
LEU   HD23 H  N N 243 
LEU   HXT  H  N N 244 
LYS   N    N  N N 245 
LYS   CA   C  N S 246 
LYS   C    C  N N 247 
LYS   O    O  N N 248 
LYS   CB   C  N N 249 
LYS   CG   C  N N 250 
LYS   CD   C  N N 251 
LYS   CE   C  N N 252 
LYS   NZ   N  N N 253 
LYS   OXT  O  N N 254 
LYS   H    H  N N 255 
LYS   H2   H  N N 256 
LYS   HA   H  N N 257 
LYS   HB2  H  N N 258 
LYS   HB3  H  N N 259 
LYS   HG2  H  N N 260 
LYS   HG3  H  N N 261 
LYS   HD2  H  N N 262 
LYS   HD3  H  N N 263 
LYS   HE2  H  N N 264 
LYS   HE3  H  N N 265 
LYS   HZ1  H  N N 266 
LYS   HZ2  H  N N 267 
LYS   HZ3  H  N N 268 
LYS   HXT  H  N N 269 
MET   N    N  N N 270 
MET   CA   C  N S 271 
MET   C    C  N N 272 
MET   O    O  N N 273 
MET   CB   C  N N 274 
MET   CG   C  N N 275 
MET   SD   S  N N 276 
MET   CE   C  N N 277 
MET   OXT  O  N N 278 
MET   H    H  N N 279 
MET   H2   H  N N 280 
MET   HA   H  N N 281 
MET   HB2  H  N N 282 
MET   HB3  H  N N 283 
MET   HG2  H  N N 284 
MET   HG3  H  N N 285 
MET   HE1  H  N N 286 
MET   HE2  H  N N 287 
MET   HE3  H  N N 288 
MET   HXT  H  N N 289 
PHE   N    N  N N 290 
PHE   CA   C  N S 291 
PHE   C    C  N N 292 
PHE   O    O  N N 293 
PHE   CB   C  N N 294 
PHE   CG   C  Y N 295 
PHE   CD1  C  Y N 296 
PHE   CD2  C  Y N 297 
PHE   CE1  C  Y N 298 
PHE   CE2  C  Y N 299 
PHE   CZ   C  Y N 300 
PHE   OXT  O  N N 301 
PHE   H    H  N N 302 
PHE   H2   H  N N 303 
PHE   HA   H  N N 304 
PHE   HB2  H  N N 305 
PHE   HB3  H  N N 306 
PHE   HD1  H  N N 307 
PHE   HD2  H  N N 308 
PHE   HE1  H  N N 309 
PHE   HE2  H  N N 310 
PHE   HZ   H  N N 311 
PHE   HXT  H  N N 312 
PRO   N    N  N N 313 
PRO   CA   C  N S 314 
PRO   C    C  N N 315 
PRO   O    O  N N 316 
PRO   CB   C  N N 317 
PRO   CG   C  N N 318 
PRO   CD   C  N N 319 
PRO   OXT  O  N N 320 
PRO   H    H  N N 321 
PRO   HA   H  N N 322 
PRO   HB2  H  N N 323 
PRO   HB3  H  N N 324 
PRO   HG2  H  N N 325 
PRO   HG3  H  N N 326 
PRO   HD2  H  N N 327 
PRO   HD3  H  N N 328 
PRO   HXT  H  N N 329 
SER   N    N  N N 330 
SER   CA   C  N S 331 
SER   C    C  N N 332 
SER   O    O  N N 333 
SER   CB   C  N N 334 
SER   OG   O  N N 335 
SER   OXT  O  N N 336 
SER   H    H  N N 337 
SER   H2   H  N N 338 
SER   HA   H  N N 339 
SER   HB2  H  N N 340 
SER   HB3  H  N N 341 
SER   HG   H  N N 342 
SER   HXT  H  N N 343 
THR   N    N  N N 344 
THR   CA   C  N S 345 
THR   C    C  N N 346 
THR   O    O  N N 347 
THR   CB   C  N R 348 
THR   OG1  O  N N 349 
THR   CG2  C  N N 350 
THR   OXT  O  N N 351 
THR   H    H  N N 352 
THR   H2   H  N N 353 
THR   HA   H  N N 354 
THR   HB   H  N N 355 
THR   HG1  H  N N 356 
THR   HG21 H  N N 357 
THR   HG22 H  N N 358 
THR   HG23 H  N N 359 
THR   HXT  H  N N 360 
TRP   N    N  N N 361 
TRP   CA   C  N S 362 
TRP   C    C  N N 363 
TRP   O    O  N N 364 
TRP   CB   C  N N 365 
TRP   CG   C  Y N 366 
TRP   CD1  C  Y N 367 
TRP   CD2  C  Y N 368 
TRP   NE1  N  Y N 369 
TRP   CE2  C  Y N 370 
TRP   CE3  C  Y N 371 
TRP   CZ2  C  Y N 372 
TRP   CZ3  C  Y N 373 
TRP   CH2  C  Y N 374 
TRP   OXT  O  N N 375 
TRP   H    H  N N 376 
TRP   H2   H  N N 377 
TRP   HA   H  N N 378 
TRP   HB2  H  N N 379 
TRP   HB3  H  N N 380 
TRP   HD1  H  N N 381 
TRP   HE1  H  N N 382 
TRP   HE3  H  N N 383 
TRP   HZ2  H  N N 384 
TRP   HZ3  H  N N 385 
TRP   HH2  H  N N 386 
TRP   HXT  H  N N 387 
TYR   N    N  N N 388 
TYR   CA   C  N S 389 
TYR   C    C  N N 390 
TYR   O    O  N N 391 
TYR   CB   C  N N 392 
TYR   CG   C  Y N 393 
TYR   CD1  C  Y N 394 
TYR   CD2  C  Y N 395 
TYR   CE1  C  Y N 396 
TYR   CE2  C  Y N 397 
TYR   CZ   C  Y N 398 
TYR   OH   O  N N 399 
TYR   OXT  O  N N 400 
TYR   H    H  N N 401 
TYR   H2   H  N N 402 
TYR   HA   H  N N 403 
TYR   HB2  H  N N 404 
TYR   HB3  H  N N 405 
TYR   HD1  H  N N 406 
TYR   HD2  H  N N 407 
TYR   HE1  H  N N 408 
TYR   HE2  H  N N 409 
TYR   HH   H  N N 410 
TYR   HXT  H  N N 411 
VAL   N    N  N N 412 
VAL   CA   C  N S 413 
VAL   C    C  N N 414 
VAL   O    O  N N 415 
VAL   CB   C  N N 416 
VAL   CG1  C  N N 417 
VAL   CG2  C  N N 418 
VAL   OXT  O  N N 419 
VAL   H    H  N N 420 
VAL   H2   H  N N 421 
VAL   HA   H  N N 422 
VAL   HB   H  N N 423 
VAL   HG11 H  N N 424 
VAL   HG12 H  N N 425 
VAL   HG13 H  N N 426 
VAL   HG21 H  N N 427 
VAL   HG22 H  N N 428 
VAL   HG23 H  N N 429 
VAL   HXT  H  N N 430 
# 
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 
A1ARY C1  N1   sing N N 1   
A1ARY C1  C16  doub Y N 2   
A1ARY C1  C19  sing Y N 3   
A1ARY N1  C2   sing N N 4   
A1ARY N1  C3   sing N N 5   
A1ARY C2  C5   doub Y N 6   
A1ARY C2  C9   sing Y N 7   
A1ARY C3  C4   sing N N 8   
A1ARY C3  O2   doub N N 9   
A1ARY C4  O1   sing N N 10  
A1ARY C5  C6   sing Y N 11  
A1ARY C6  C7   doub Y N 12  
A1ARY C6  C10  sing N N 13  
A1ARY C7  C8   sing Y N 14  
A1ARY C8  C9   doub Y N 15  
A1ARY C10 C11  doub Y N 16  
A1ARY C10 C15  sing Y N 17  
A1ARY C11 C12  sing Y N 18  
A1ARY C12 C13  doub Y N 19  
A1ARY C12 CL1  sing N N 20  
A1ARY C13 C14  sing Y N 21  
A1ARY C14 C15  doub Y N 22  
A1ARY C16 C17  sing Y N 23  
A1ARY C17 C18  doub Y N 24  
A1ARY C17 CL2  sing N N 25  
A1ARY C18 N2   sing Y N 26  
A1ARY N2  C19  doub Y N 27  
A1ARY C4  H1   sing N N 28  
A1ARY C5  H2   sing N N 29  
A1ARY C7  H3   sing N N 30  
A1ARY C8  H4   sing N N 31  
A1ARY C13 H7   sing N N 32  
A1ARY C15 H9   sing N N 33  
A1ARY C11 H6   sing N N 34  
A1ARY C14 H8   sing N N 35  
A1ARY C16 H10  sing N N 36  
A1ARY C18 H11  sing N N 37  
A1ARY C19 H12  sing N N 38  
A1ARY C9  H5   sing N N 39  
A1ARY O1  H13  sing N N 40  
A1ARY C4  S1   sing N N 41  
A1ARY S1  HS   sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
GLN   N   CA   sing N N 125 
GLN   N   H    sing N N 126 
GLN   N   H2   sing N N 127 
GLN   CA  C    sing N N 128 
GLN   CA  CB   sing N N 129 
GLN   CA  HA   sing N N 130 
GLN   C   O    doub N N 131 
GLN   C   OXT  sing N N 132 
GLN   CB  CG   sing N N 133 
GLN   CB  HB2  sing N N 134 
GLN   CB  HB3  sing N N 135 
GLN   CG  CD   sing N N 136 
GLN   CG  HG2  sing N N 137 
GLN   CG  HG3  sing N N 138 
GLN   CD  OE1  doub N N 139 
GLN   CD  NE2  sing N N 140 
GLN   NE2 HE21 sing N N 141 
GLN   NE2 HE22 sing N N 142 
GLN   OXT HXT  sing N N 143 
GLU   N   CA   sing N N 144 
GLU   N   H    sing N N 145 
GLU   N   H2   sing N N 146 
GLU   CA  C    sing N N 147 
GLU   CA  CB   sing N N 148 
GLU   CA  HA   sing N N 149 
GLU   C   O    doub N N 150 
GLU   C   OXT  sing N N 151 
GLU   CB  CG   sing N N 152 
GLU   CB  HB2  sing N N 153 
GLU   CB  HB3  sing N N 154 
GLU   CG  CD   sing N N 155 
GLU   CG  HG2  sing N N 156 
GLU   CG  HG3  sing N N 157 
GLU   CD  OE1  doub N N 158 
GLU   CD  OE2  sing N N 159 
GLU   OE2 HE2  sing N N 160 
GLU   OXT HXT  sing N N 161 
GLY   N   CA   sing N N 162 
GLY   N   H    sing N N 163 
GLY   N   H2   sing N N 164 
GLY   CA  C    sing N N 165 
GLY   CA  HA2  sing N N 166 
GLY   CA  HA3  sing N N 167 
GLY   C   O    doub N N 168 
GLY   C   OXT  sing N N 169 
GLY   OXT HXT  sing N N 170 
HIS   N   CA   sing N N 171 
HIS   N   H    sing N N 172 
HIS   N   H2   sing N N 173 
HIS   CA  C    sing N N 174 
HIS   CA  CB   sing N N 175 
HIS   CA  HA   sing N N 176 
HIS   C   O    doub N N 177 
HIS   C   OXT  sing N N 178 
HIS   CB  CG   sing N N 179 
HIS   CB  HB2  sing N N 180 
HIS   CB  HB3  sing N N 181 
HIS   CG  ND1  sing Y N 182 
HIS   CG  CD2  doub Y N 183 
HIS   ND1 CE1  doub Y N 184 
HIS   ND1 HD1  sing N N 185 
HIS   CD2 NE2  sing Y N 186 
HIS   CD2 HD2  sing N N 187 
HIS   CE1 NE2  sing Y N 188 
HIS   CE1 HE1  sing N N 189 
HIS   NE2 HE2  sing N N 190 
HIS   OXT HXT  sing N N 191 
HOH   O   H1   sing N N 192 
HOH   O   H2   sing N N 193 
ILE   N   CA   sing N N 194 
ILE   N   H    sing N N 195 
ILE   N   H2   sing N N 196 
ILE   CA  C    sing N N 197 
ILE   CA  CB   sing N N 198 
ILE   CA  HA   sing N N 199 
ILE   C   O    doub N N 200 
ILE   C   OXT  sing N N 201 
ILE   CB  CG1  sing N N 202 
ILE   CB  CG2  sing N N 203 
ILE   CB  HB   sing N N 204 
ILE   CG1 CD1  sing N N 205 
ILE   CG1 HG12 sing N N 206 
ILE   CG1 HG13 sing N N 207 
ILE   CG2 HG21 sing N N 208 
ILE   CG2 HG22 sing N N 209 
ILE   CG2 HG23 sing N N 210 
ILE   CD1 HD11 sing N N 211 
ILE   CD1 HD12 sing N N 212 
ILE   CD1 HD13 sing N N 213 
ILE   OXT HXT  sing N N 214 
LEU   N   CA   sing N N 215 
LEU   N   H    sing N N 216 
LEU   N   H2   sing N N 217 
LEU   CA  C    sing N N 218 
LEU   CA  CB   sing N N 219 
LEU   CA  HA   sing N N 220 
LEU   C   O    doub N N 221 
LEU   C   OXT  sing N N 222 
LEU   CB  CG   sing N N 223 
LEU   CB  HB2  sing N N 224 
LEU   CB  HB3  sing N N 225 
LEU   CG  CD1  sing N N 226 
LEU   CG  CD2  sing N N 227 
LEU   CG  HG   sing N N 228 
LEU   CD1 HD11 sing N N 229 
LEU   CD1 HD12 sing N N 230 
LEU   CD1 HD13 sing N N 231 
LEU   CD2 HD21 sing N N 232 
LEU   CD2 HD22 sing N N 233 
LEU   CD2 HD23 sing N N 234 
LEU   OXT HXT  sing N N 235 
LYS   N   CA   sing N N 236 
LYS   N   H    sing N N 237 
LYS   N   H2   sing N N 238 
LYS   CA  C    sing N N 239 
LYS   CA  CB   sing N N 240 
LYS   CA  HA   sing N N 241 
LYS   C   O    doub N N 242 
LYS   C   OXT  sing N N 243 
LYS   CB  CG   sing N N 244 
LYS   CB  HB2  sing N N 245 
LYS   CB  HB3  sing N N 246 
LYS   CG  CD   sing N N 247 
LYS   CG  HG2  sing N N 248 
LYS   CG  HG3  sing N N 249 
LYS   CD  CE   sing N N 250 
LYS   CD  HD2  sing N N 251 
LYS   CD  HD3  sing N N 252 
LYS   CE  NZ   sing N N 253 
LYS   CE  HE2  sing N N 254 
LYS   CE  HE3  sing N N 255 
LYS   NZ  HZ1  sing N N 256 
LYS   NZ  HZ2  sing N N 257 
LYS   NZ  HZ3  sing N N 258 
LYS   OXT HXT  sing N N 259 
MET   N   CA   sing N N 260 
MET   N   H    sing N N 261 
MET   N   H2   sing N N 262 
MET   CA  C    sing N N 263 
MET   CA  CB   sing N N 264 
MET   CA  HA   sing N N 265 
MET   C   O    doub N N 266 
MET   C   OXT  sing N N 267 
MET   CB  CG   sing N N 268 
MET   CB  HB2  sing N N 269 
MET   CB  HB3  sing N N 270 
MET   CG  SD   sing N N 271 
MET   CG  HG2  sing N N 272 
MET   CG  HG3  sing N N 273 
MET   SD  CE   sing N N 274 
MET   CE  HE1  sing N N 275 
MET   CE  HE2  sing N N 276 
MET   CE  HE3  sing N N 277 
MET   OXT HXT  sing N N 278 
PHE   N   CA   sing N N 279 
PHE   N   H    sing N N 280 
PHE   N   H2   sing N N 281 
PHE   CA  C    sing N N 282 
PHE   CA  CB   sing N N 283 
PHE   CA  HA   sing N N 284 
PHE   C   O    doub N N 285 
PHE   C   OXT  sing N N 286 
PHE   CB  CG   sing N N 287 
PHE   CB  HB2  sing N N 288 
PHE   CB  HB3  sing N N 289 
PHE   CG  CD1  doub Y N 290 
PHE   CG  CD2  sing Y N 291 
PHE   CD1 CE1  sing Y N 292 
PHE   CD1 HD1  sing N N 293 
PHE   CD2 CE2  doub Y N 294 
PHE   CD2 HD2  sing N N 295 
PHE   CE1 CZ   doub Y N 296 
PHE   CE1 HE1  sing N N 297 
PHE   CE2 CZ   sing Y N 298 
PHE   CE2 HE2  sing N N 299 
PHE   CZ  HZ   sing N N 300 
PHE   OXT HXT  sing N N 301 
PRO   N   CA   sing N N 302 
PRO   N   CD   sing N N 303 
PRO   N   H    sing N N 304 
PRO   CA  C    sing N N 305 
PRO   CA  CB   sing N N 306 
PRO   CA  HA   sing N N 307 
PRO   C   O    doub N N 308 
PRO   C   OXT  sing N N 309 
PRO   CB  CG   sing N N 310 
PRO   CB  HB2  sing N N 311 
PRO   CB  HB3  sing N N 312 
PRO   CG  CD   sing N N 313 
PRO   CG  HG2  sing N N 314 
PRO   CG  HG3  sing N N 315 
PRO   CD  HD2  sing N N 316 
PRO   CD  HD3  sing N N 317 
PRO   OXT HXT  sing N N 318 
SER   N   CA   sing N N 319 
SER   N   H    sing N N 320 
SER   N   H2   sing N N 321 
SER   CA  C    sing N N 322 
SER   CA  CB   sing N N 323 
SER   CA  HA   sing N N 324 
SER   C   O    doub N N 325 
SER   C   OXT  sing N N 326 
SER   CB  OG   sing N N 327 
SER   CB  HB2  sing N N 328 
SER   CB  HB3  sing N N 329 
SER   OG  HG   sing N N 330 
SER   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
_pdbx_audit_support.funding_organization   'Welch Foundation' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7JPY 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 1 2 1' 
_space_group.name_Hall        'C 2y (x,y,-x+z)' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BSQ 
_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]   0.019607 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002355 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012465 
_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]   0.011297 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? -32.88375 -19.31498 15.17289  1.000 24.94583 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -32.11383 -20.44515 14.69195  1.000 22.49852 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -32.07384 -20.50513 13.16155  1.000 23.95636 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -32.49701 -19.56904 12.47541  1.000 22.96034 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -32.67017 -21.73244 15.29414  1.000 28.95694 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -33.83032 -22.16636 14.61658  1.000 31.31573 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -31.52725 -21.58744 12.63077  1.000 21.99426 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -31.25019 -21.70497 11.21715  1.000 20.92010 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -29.80536 -21.35353 10.89487  1.000 21.69811 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -29.13877 -20.59412 11.60285  1.000 23.57956 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -29.31671 -21.90020 9.78784   1.000 20.79434 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -27.93417 -21.69508 9.38778   1.000 21.30169 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -27.86430 -21.58215 7.87907   1.000 22.46551 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -28.23726 -22.51601 7.16563   1.000 24.59052 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -27.02973 -22.82790 9.88221   1.000 22.81883 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -25.59790 -22.42091 9.99348   1.000 20.85429 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -25.17930 -21.59673 11.02833  1.000 23.09794 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -24.67829 -22.81003 9.03397   1.000 20.66271 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -23.84849 -21.19109 11.11798  1.000 22.61557 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -23.34748 -22.41137 9.11736   1.000 21.85271 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -22.93873 -21.59862 10.16127  1.000 21.33675 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -27.37243 -20.45098 7.39722   1.000 21.33576 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -27.30141 -20.18762 5.97446   1.000 20.36570 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -25.90287 -19.72298 5.59992   1.000 17.90213 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -25.16112 -19.17203 6.42529   1.000 19.45578 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -28.32534 -19.13532 5.58487   1.000 18.60012 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -29.70463 -19.70414 5.37757   1.000 20.66469 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -30.00320 -19.81670 3.89941   1.000 22.83299 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -31.41569 -20.11528 3.67051   1.000 21.55223 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -31.83759 -20.96553 2.74470   1.000 27.89980 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -30.98542 -21.55583 1.91536   1.000 29.01328 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -33.14395 -21.20516 2.62772   1.000 19.56511 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -25.54325 -19.94873 4.33994   1.000 15.76650 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -24.33910 -19.32765 3.79298   1.000 18.80098 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -24.63556 -17.84369 3.66005   1.000 20.01748 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -25.35988 -17.42139 2.76226   1.000 22.96590 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -23.96747 -19.93867 2.44781   1.000 19.14507 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -22.47345 -20.14242 2.25047   1.000 24.18555 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -22.20846 -21.41630 1.46096   1.000 26.59789 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -20.85674 -22.01737 1.79749   1.000 24.94765 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -19.72117 -21.39538 0.94550   1.000 27.31021 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -24.13021 -17.05458 4.58778   1.000 13.26478 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -24.54417 -15.67224 4.74384   1.000 15.85098 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? -23.41931 -14.76503 4.30287   1.000 14.73402 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? -22.30193 -14.89777 4.79939   1.000 15.83575 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -24.84341 -15.37787 6.20816   1.000 14.69709 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -25.64248 -14.15214 6.41345   1.000 21.51327 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -26.12340 -14.19008 8.12447   1.000 29.15738 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -27.61214 -15.15195 8.06843   1.000 22.37888 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? -23.69523 -13.83795 3.40795   1.000 14.79901 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? -22.65627 -12.87396 3.07579   1.000 12.43920 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? -22.86626 -11.61016 3.89118   1.000 15.45261 ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? -23.93917 -11.38847 4.46602   1.000 12.35980 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? -22.65088 -12.54350 1.58451   1.000 14.47042 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? -21.82586 -10.77772 3.93319   1.000 11.64119 ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? -21.95494 -9.48613  4.57229   1.000 13.25715 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? -22.82355 -8.58262  3.71938   1.000 12.62514 ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? -22.85843 -8.72515  2.49714   1.000 12.55345 ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? -20.59447 -8.82377  4.77626   1.000 12.86135 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? -19.76947 -9.51043  5.81116   1.000 15.52220 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? -20.00366 -9.27830  7.15131   1.000 19.76942 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? -18.77857 -10.39186 5.44374   1.000 19.37466 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? -19.25140 -9.92260  8.11806   1.000 26.08114 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? -18.01272 -11.03538 6.40923   1.000 20.76422 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? -18.25114 -10.79556 7.75021   1.000 21.60857 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? -23.53333 -7.65292  4.34301   1.000 14.51309 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? -24.25105 -6.64350  3.57144   1.000 15.59840 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? -23.26781 -5.96697  2.63999   1.000 16.92841 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? -22.12884 -5.67466  3.01421   1.000 15.00672 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? -24.78713 -5.68582  4.63949   1.000 16.59194 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? -24.79629 -6.47056  5.90223   1.000 19.53747 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? -23.66094 -7.44734  5.79452   1.000 16.48570 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? -23.68423 -5.78759  1.39704   1.000 15.17968 ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? -22.73681 -5.39602  0.36834   1.000 13.32351 ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? -22.75775 -3.91018  0.08199   1.000 13.16578 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? -21.91636 -3.44828  -0.69173  1.000 13.65177 ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? -23.00068 -6.15879  -0.93325  1.000 11.95971 ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? -24.33467 -5.97062  -1.34072  1.000 15.62319 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? -23.68702 -3.16765  0.68653   1.000 16.05862 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? -23.85537 -1.75564  0.35182   1.000 15.44529 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? -22.55844 -0.97411  0.31429   1.000 15.90547 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? -22.30318 -0.22110  -0.62973  1.000 16.81613 ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? -21.71780 -1.13839  1.34636   1.000 14.72352 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? -20.51638 -0.31713  1.44685   1.000 17.57222 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? -19.58016 -0.57628  0.28566   1.000 17.62379 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? -18.86518 0.32851   -0.15184  1.000 19.38249 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? -19.78480 -0.58230  2.76338   1.000 18.36753 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? -20.44564 0.00851   3.99427   1.000 21.02285 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? -19.70610 -0.45823  5.24229   1.000 24.73442 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? -20.11474 0.35318   6.45740   1.000 30.56669 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? -21.58685 0.23197   6.66231   1.000 37.15006 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? -19.57600 -1.80566  -0.22365  1.000 13.45528 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? -18.75221 -2.16678  -1.37649  1.000 15.93636 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? -19.40324 -1.73745  -2.67973  1.000 14.51582 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? -18.71364 -1.34868  -3.62741  1.000 15.04112 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? -18.48525 -3.67989  -1.35245  1.000 11.37523 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? -17.63598 -4.11644  -2.57975  1.000 13.04278 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? -17.74086 -4.00918  -0.06130  1.000 15.94512 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? -20.73509 -1.84983  -2.76360  1.000 13.42479 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? -21.43809 -1.41648  -3.96383  1.000 14.27037 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? -21.08434 0.00720   -4.31268  1.000 15.21708 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? -20.95819 0.34647   -5.49412  1.000 16.75923 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? -22.95343 -1.52990  -3.78221  1.000 15.10637 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? -23.44509 -2.94407  -3.58462  1.000 14.40204 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? -24.89776 -2.97542  -3.15923  1.000 15.35555 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? -25.71626 -2.24545  -3.74399  1.000 17.65945 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? -25.20953 -3.71889  -2.21474  1.000 15.99964 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? -20.94140 0.86747   -3.29847  1.000 15.73514 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? -20.65044 2.25435   -3.59261  1.000 16.83629 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? -19.25956 2.50485   -4.13059  1.000 17.05786 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? -18.92877 3.64976   -4.45584  1.000 17.33958 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? -18.44243 1.46374   -4.23376  1.000 15.05749 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? -17.07863 1.57120   -4.71090  1.000 14.79072 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? -16.87379 0.96556   -6.08190  1.000 15.28431 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? -15.76003 1.04436   -6.62017  1.000 14.09295 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? -16.12372 0.87571   -3.73634  1.000 13.95254 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? -16.27272 1.52729   -2.08293  1.000 19.03453 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? -17.88021 0.32159   -6.63301  1.000 15.03560 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? -17.68401 -0.43989  -7.84667  1.000 15.63561 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? -17.83079 0.51130   -9.01619  1.000 15.27026 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? -18.78761 1.29374   -9.07992  1.000 18.14881 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? -18.67649 -1.58997  -7.93194  1.000 16.52614 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? -18.45021 -2.56457  -6.78847  1.000 12.97425 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? -16.77781 -3.11801  -6.57647  1.000 13.16463 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? -16.32408 -3.60583  -8.24497  1.000 15.42709 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? -16.87473 0.44957   -9.93195  1.000 15.21935 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? -16.86289 1.28501   -11.11869 1.000 16.44063 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? -16.54974 0.40820   -12.31552 1.000 16.75065 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? -16.16941 -0.74684  -12.18540 1.000 17.71816 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? -15.85086 2.44415   -11.03232 1.000 16.94091 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? -16.13962 3.32921   -9.82513  1.000 17.99478 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? -14.42007 1.92814   -11.03484 1.000 16.04704 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? -16.72217 0.98114   -13.49358 1.000 20.83618 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? -16.42192 0.29438   -14.73462 1.000 23.00859 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? -15.11776 0.84723   -15.28919 1.000 20.86597 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? -14.93698 2.06681   -15.37322 1.000 23.03355 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? -17.57503 0.47675   -15.71285 1.000 23.09210 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? -17.36172 -0.09628  -17.06669 1.000 26.25413 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? -18.65779 -0.23715  -17.81479 1.000 28.08065 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? -18.89424 -1.25026  -18.46546 1.000 33.24531 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? -19.53160 0.76081   -17.69818 1.000 33.36763 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? -14.19581 -0.04200  -15.63126 1.000 19.76531 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? -12.91119 0.35640   -16.19243 1.000 21.78055 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? -12.83119 -0.19035  -17.60582 1.000 22.11934 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? -12.94880 -1.40149  -17.81780 1.000 20.74541 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? -11.72633 -0.12760  -15.34061 1.000 20.71331 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? -10.40880 0.30268   -15.98617 1.000 22.41841 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? -11.81437 0.45744   -13.96543 1.000 19.62076 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? -12.64115 0.69541   -18.57349 1.000 23.69487 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? -12.51239 0.28835   -19.96081 1.000 24.45156 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? -11.16361 0.72803   -20.49383 1.000 26.08616 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? -10.73727 1.86848   -20.28430 1.000 28.94541 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? -13.62514 0.87781   -20.83341 1.000 26.89580 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? -14.88009 0.37576   -20.37283 1.000 26.69687 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? -13.43055 0.47774   -22.27800 1.000 30.02003 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? -10.50547 -0.17460  -21.20543 1.000 26.80747 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? -9.25066  0.14957   -21.86116 1.000 28.57939 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? -9.25999  -0.61139  -23.17687 1.000 31.50971 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? -9.30652  -1.84556  -23.17915 1.000 29.83246 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? -8.05812  -0.21635  -20.97568 1.000 25.09363 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? -6.48645  0.10104   -21.75683 1.000 33.71682 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? -9.29854  0.12411   -24.28474 1.000 29.24897 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? -9.42845  -0.51567  -25.58450 1.000 33.15958 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? -10.80613 -1.12977  -25.70346 1.000 34.58401 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? -11.82173 -0.46065  -25.49528 1.000 35.40934 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? -10.86009 -2.41794  -26.02572 1.000 33.07814 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? -12.13327 -3.11545  -26.09105 1.000 35.11237 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? -12.41723 -3.91528  -24.83244 1.000 35.00323 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? -13.47155 -4.55183  -24.74222 1.000 39.36295 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? -12.18477 -4.03746  -27.31493 1.000 37.51171 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? -11.02525 -4.88173  -27.32920 1.000 36.27339 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? -12.21675 -3.20898  -28.58588 1.000 35.94764 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? -11.51770 -3.88135  -23.85500 1.000 31.81141 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? -11.67950 -4.63764  -22.62433 1.000 30.86520 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? -12.38046 -3.77796  -21.57883 1.000 29.30328 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? -11.91160 -2.68454  -21.24547 1.000 28.80487 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? -10.32791 -5.11735  -22.10347 1.000 31.53085 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? -9.66663  -5.87579  -23.12099 1.000 36.09506 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? -10.52804 -5.98746  -20.88527 1.000 30.68410 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? -13.50488 -4.26907  -21.06984 1.000 28.07034 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? -14.19810 -3.64261  -19.95168 1.000 25.91643 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? -14.24648 -4.61837  -18.78436 1.000 23.32812 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? -14.56456 -5.79904  -18.96776 1.000 23.22558 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? -15.60313 -3.19849  -20.35844 1.000 26.81634 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? -15.49881 -2.15634  -21.33196 1.000 33.01520 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? -16.35539 -2.68196  -19.18934 1.000 28.82568 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? -13.90907 -4.13208  -17.59587 1.000 16.97469 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? -14.07956 -4.91917  -16.38255 1.000 19.37336 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? -14.38434 -3.96856  -15.23312 1.000 15.72734 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? -14.63259 -2.77320  -15.42941 1.000 18.80793 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? -12.84347 -5.78365  -16.09556 1.000 20.46556 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? -11.44684 -5.17921  -16.29770 1.000 18.96920 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? -11.15601 -4.05870  -15.30209 1.000 16.73877 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? -10.40276 -6.29540  -16.17408 1.000 20.15235 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? -14.36332 -4.50531  -14.02831 1.000 17.04172 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? -14.74834 -3.75433  -12.84944 1.000 15.19963 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? -13.52454 -3.18447  -12.17826 1.000 15.25661 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? -12.44210 -3.76916  -12.22842 1.000 16.02776 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? -15.50352 -4.66064  -11.88271 1.000 15.02076 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? -16.68884 -5.29023  -12.55311 1.000 16.87915 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? -17.69520 -4.62119  -12.75442 1.000 16.36732 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? -16.55965 -6.56423  -12.97198 1.000 16.73792 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? -13.70341 -2.02302  -11.55763 1.000 14.27082 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? -12.66211 -1.44596  -10.73963 1.000 14.68855 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? -13.21595 -1.13857  -9.36295  1.000 12.75542 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? -14.42299 -1.07880  -9.15471  1.000 14.22136 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? -12.31138 -0.95799  -8.42573  1.000 15.25373 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? -12.68643 -0.63901  -7.05726  1.000 16.30346 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? -12.18098 0.75995   -6.75693  1.000 13.74358 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? -10.97458 1.01936   -6.83659  1.000 15.29193 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? -12.11863 -1.66871  -6.08664  1.000 13.29005 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? -12.57680 -1.44328  -4.65827  1.000 13.32525 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? -14.02298 -1.90294  -4.47328  1.000 14.58486 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? -11.67591 -2.18120  -3.71408  1.000 12.08506 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? -13.11355 1.66103   -6.45849  1.000 15.14019 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? -12.86405 3.09640   -6.35715  1.000 15.01651 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? -12.86838 3.45640   -4.87849  1.000 17.00956 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? -13.92592 3.47973   -4.23862  1.000 17.00568 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? -13.92560 3.87574   -7.12294  1.000 16.14395 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? -13.76803 5.36557   -7.10522  1.000 17.70772 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? -12.62562 6.07778   -6.88108  1.000 19.01540 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? -14.80838 6.32442   -7.30542  1.000 21.31298 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? -12.89210 7.43394   -6.94941  1.000 19.51190 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? -14.22443 7.60790   -7.21352  1.000 22.05246 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? -16.17264 6.22310   -7.57361  1.000 23.63136 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? -14.96606 8.77667   -7.36361  1.000 24.38573 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? -16.90322 7.37388   -7.72643  1.000 24.31129 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? -16.30427 8.63803   -7.61343  1.000 23.50148 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? -11.68322 3.69936   -4.33413  1.000 15.53926 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? -11.50851 4.06898   -2.94187  1.000 17.43091 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? -10.70680 5.34787   -2.91509  1.000 20.94500 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? -9.63373  5.40881   -3.52492  1.000 21.36000 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? -10.77514 2.98865   -2.15496  1.000 18.75538 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? -11.42506 1.62777   -2.19280  1.000 15.55434 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? -10.45840 0.59817   -1.67272  1.000 14.85643 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? -12.65939 1.67902   -1.33601  1.000 16.31286 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? -11.22387 6.36100   -2.21750  1.000 20.05232 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? -10.63187 7.70012   -2.24136  1.000 21.69199 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? -10.44957 8.05821   -3.71786  1.000 23.69253 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? -11.37280 7.82735   -4.51218  1.000 21.58399 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? -9.37537  7.70738   -1.38886  1.000 23.74512 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? -9.64605  7.26830   0.04159   1.000 26.55486 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? -10.55713 7.83800   0.67652   1.000 28.23086 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? -8.97321  6.33360   0.51842   1.000 27.88273 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? -9.28844  8.55588   -4.14621  1.000 20.04427 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? -9.11762  8.92305   -5.54522  1.000 23.03316 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? -8.33325  7.88840   -6.35277  1.000 21.04770 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? -7.66813  8.24349   -7.33489  1.000 23.29444 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? -8.47220  10.30513  -5.65212  1.000 24.38059 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? -7.06022  10.35031  -5.07766  1.000 28.45365 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? -6.65037  9.39076   -4.37809  1.000 29.38770 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? -6.36204  11.35462  -5.33601  1.000 29.52774 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? -8.42487  6.61068   -5.99862  1.000 22.46629 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? -7.76206  5.55159   -6.75296  1.000 17.83131 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? -8.80281  4.52744   -7.18414  1.000 19.15159 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? -9.72271  4.19056   -6.42747  1.000 17.75873 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? -6.63973  4.87346   -5.94174  1.000 19.30329 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? -6.06952  3.70153   -6.70551  1.000 19.57086 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? -5.53401  5.85699   -5.61914  1.000 21.64830 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? -8.65613  4.03402   -8.40696  1.000 15.98116 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? -9.44753  2.92531   -8.91203  1.000 17.10509 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? -8.48944  1.77349   -9.11234  1.000 17.97832 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? -7.47904  1.91227   -9.81918  1.000 16.42861 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? -10.16834 3.26470   -10.22325 1.000 17.31859 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? -10.79196 2.00351   -10.79430 1.000 16.45225 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? -11.20506 4.36176   -9.99748  1.000 18.35716 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? -8.80194  0.65393   -8.47225  1.000 15.42582 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? -8.02267  -0.57225  -8.52724  1.000 16.16028 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? -8.69973  -1.52759  -9.48206  1.000 14.42593 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? -9.90872  -1.74039  -9.38119  1.000 16.87181 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? -7.94549  -1.24481  -7.15396  1.000 12.32878 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? -7.35264  -0.37013  -6.12010  1.000 15.84887 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? -8.10476  0.61497   -5.50021  1.000 13.99768 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? -6.00852  -0.49728  -5.78471  1.000 16.80507 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? -7.53647  1.43103   -4.55306  1.000 18.58886 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? -5.44850  0.28878   -4.83811  1.000 14.89716 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? -6.20028  1.25649   -4.23099  1.000 18.84591 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? -5.60898  2.05585   -3.29834  1.000 18.95713 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? -7.92752  -2.12949  -10.37817 1.000 13.16017 ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? -8.52814  -3.09032  -11.28559 1.000 15.04193 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? -7.44898  -4.05628  -11.74265 1.000 14.83302 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? -6.25290  -3.77862  -11.57612 1.000 15.30994 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? -9.18530  -2.38518  -12.48141 1.000 14.59016 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? -8.00760  -1.71937  -13.64331 1.000 20.94867 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? -7.83434  -5.20734  -12.29617 1.000 15.25990 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? -6.82793  -6.15606  -12.77562 1.000 16.37718 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? -6.02280  -5.53197  -13.89862 1.000 18.62232 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? -6.56242  -4.87407  -14.79139 1.000 16.22221 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? -7.66086  -7.34315  -13.26244 1.000 14.34585 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? -8.95210  -7.21772  -12.51001 1.000 12.33003 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? -9.19620  -5.74877  -12.43402 1.000 15.22863 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? -4.70841  -5.70359  -13.82886 1.000 15.54861 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? -3.90240  -5.09746  -14.86949 1.000 16.97223 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? -4.14101  -5.73687  -16.22229 1.000 18.77191 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? -3.79881  -5.12940  -17.23619 1.000 18.43392 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? -2.43031  -5.16606  -14.50946 1.000 16.81883 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? -1.87611  -6.55001  -14.60513 1.000 17.03317 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? -0.42098  -6.54934  -14.25051 1.000 16.47901 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 0.06370   -7.91858  -14.19309 1.000 16.86717 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 1.34389   -8.24414  -14.10458 1.000 20.63913 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 2.28906   -7.31801  -14.01302 1.000 18.95387 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 1.68403   -9.52612  -14.12272 1.000 15.31145 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? -4.73350  -6.93158  -16.27669 1.000 20.24359 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? -4.89925  -7.47565  -17.61799 1.000 25.57181 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? -5.95815  -6.72639  -18.41647 1.000 22.52301 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? -6.13918  -7.04849  -19.59245 1.000 25.20799 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? -5.21112  -8.97800  -17.59556 1.000 25.33270 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? -6.61915  -9.31476  -17.22218 1.000 23.32031 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? -6.99589  -9.64575  -15.93707 1.000 26.50877 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? -7.74889  -9.37725  -17.97274 1.000 26.65514 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? -8.29346  -9.90884  -15.91245 1.000 23.60445 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? -8.77565  -9.74135  -17.13122 1.000 26.46092 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? -6.60669  -5.70937  -17.83011 1.000 20.10536 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? -7.45125  -4.80043  -18.61213 1.000 20.74381 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? -6.68099  -4.15434  -19.75291 1.000 23.93149 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? -7.28452  -3.70313  -20.73477 1.000 24.56083 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? -8.06576  -3.71356  -17.70859 1.000 21.32736 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? -7.00929  -2.69493  -17.32536 1.000 19.96268 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? -9.23355  -3.01951  -18.40779 1.000 20.66157 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? -5.35479  -4.07022  -19.65745 1.000 22.92783 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? -4.63665  -3.33931  -20.69851 1.000 24.90094 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? -4.22561  -4.29089  -21.81145 1.000 27.85864 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? -3.53277  -3.89626  -22.75477 1.000 28.45611 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? -3.40333  -2.58160  -20.16818 1.000 25.69452 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? -2.25691  -3.54971  -19.83205 1.000 23.88945 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? -3.79046  -1.75356  -18.96016 1.000 22.56131 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? -1.15025  -2.93552  -18.99376 1.000 24.09093 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? -4.65231  -5.53922  -21.71946 1.000 28.63703 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? -4.24513  -6.57877  -22.64924 1.000 31.62674 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? -5.26425  -6.78098  -23.75632 1.000 40.29408 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? -6.47706  -6.70922  -23.53242 1.000 41.21665 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? -4.04821  -7.90962  -21.93334 1.000 36.70452 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? -2.51247  -7.98497  -21.04063 1.000 39.31823 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? -4.74966  -7.04647  -24.94822 1.000 43.58503 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? -5.51679  -7.65972  -26.01303 1.000 50.31812 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? -5.49339  -9.17531  -25.81787 1.000 53.66393 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? -4.83343  -9.69634  -24.91423 1.000 52.72168 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? -4.93649  -7.25704  -27.36107 1.000 51.12299 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? -3.69523  -7.94710  -27.55797 1.000 53.16787 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? -4.67538  -5.75914  -27.37792 1.000 48.87954 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? -6.21847  -9.90709  -26.66607 1.000 56.96462 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? -6.15646  -11.36622 -26.59507 1.000 57.93199 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? -4.75410  -11.86756 -26.93708 1.000 57.37285 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? -4.19786  -12.72459 -26.23570 1.000 54.86124 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? -7.20329  -11.98615 -27.52454 1.000 59.20180 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? -7.27175  -11.28007 -28.75354 1.000 62.32575 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? -4.16182  -11.32692 -28.01216 1.000 58.61534 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? -2.79416  -11.68096 -28.38459 1.000 58.26673 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? -1.80658  -11.31497 -27.28531 1.000 57.00456 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? -0.82184  -12.03289 -27.06635 1.000 54.77723 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? -2.37426  -10.99719 -29.69485 1.000 57.92448 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? -3.26382  -11.19162 -30.95048 1.000 64.67981 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? -4.73695  -10.87171 -30.73813 1.000 65.39409 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? -5.06404  -9.68085  -30.52579 1.000 64.93107 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? -5.56387  -11.81208 -30.77886 1.000 65.78058 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? -2.05018  -10.19899 -26.58983 1.000 53.88025 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? -1.19482  -9.82385  -25.46997 1.000 52.28072 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? -1.20025  -10.89432 -24.39137 1.000 49.68197 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? -0.16661  -11.15882 -23.77228 1.000 48.28615 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? -1.63071  -8.46914  -24.89997 1.000 47.26682 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? -1.19102  -7.29212  -25.78037 1.000 48.29644 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? -0.12420  -7.40198  -26.42226 1.000 45.94337 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? -1.91293  -6.26994  -25.84982 1.000 46.76678 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? -2.33804  -11.55933 -24.18880 1.000 50.71763 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? -2.51868  -12.38740 -23.00215 1.000 48.30403 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? -1.73431  -13.69199 -23.05917 1.000 48.76090 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? -1.72459  -14.43017 -22.06724 1.000 45.34418 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? -4.00047  -12.69374 -22.80441 1.000 45.76391 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? -4.72067  -11.62210 -22.01023 1.000 45.89005 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? -3.91743  -11.06750 -20.49525 1.000 47.68231 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? -4.53487  -12.21889 -19.30400 1.000 33.05073 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? -1.07360  -14.00114 -24.17313 1.000 48.82751 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? -0.36502  -15.26846 -24.27948 1.000 50.63601 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? 1.09171   -15.17793 -23.84165 1.000 53.06795 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? 1.64712   -16.19110 -23.40666 1.000 58.63805 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? -0.47150  -15.81937 -25.71038 1.000 53.89236 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? -1.79412  -15.61465 -26.47528 1.000 55.14071 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? -1.80883  -16.40916 -27.78376 1.000 52.31467 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? -3.01770  -15.99276 -25.61851 1.000 54.13364 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? 1.72002   -13.99758 -23.93587 1.000 52.73805 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? 3.01104   -13.71701 -23.30165 1.000 49.28697 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? 3.12923   -12.24772 -22.90851 1.000 45.16832 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? 4.02044   -11.55171 -23.41202 1.000 47.03031 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? 4.18104   -14.07012 -24.22467 1.000 56.35886 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? 4.73939   -15.46134 -23.97162 1.000 62.77402 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? 4.13609   -16.46726 -24.34129 1.000 65.75390 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? 5.90227   -15.52072 -23.33033 1.000 63.78475 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? 2.27762   -11.73794 -22.01762 1.000 43.39022 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? 2.21042   -10.27995 -21.82188 1.000 39.39063 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? 3.46889   -9.76119  -21.14155 1.000 39.08063 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? 3.93070   -10.32626 -20.14789 1.000 38.67408 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? 0.98775   -10.08237 -20.91589 1.000 39.08716 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? 0.53198   -11.43272 -20.50767 1.000 40.62682 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? 1.14414   -12.44666 -21.40176 1.000 41.71568 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? 4.01312   -8.67357  -21.66991 1.000 35.81956 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? 5.00388   -7.88800  -20.93988 1.000 35.70762 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? 4.23938   -6.65460  -20.45043 1.000 34.63171 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? 4.08104   -5.66596  -21.17229 1.000 31.63015 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? 6.21267   -7.56411  -21.80890 1.000 36.64627 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? 7.32728   -6.89817  -21.03430 1.000 37.43421 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? 7.08915   -6.19495  -20.05587 1.000 32.79013 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? 8.56332   -7.14981  -21.44940 1.000 43.29195 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? 3.71404   -6.75142  -19.22397 1.000 30.06077 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? 2.80278   -5.73009  -18.71945 1.000 28.14109 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? 3.48632   -4.38485  -18.54890 1.000 27.84775 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? 2.85953   -3.33876  -18.73767 1.000 26.48997 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? 2.19658   -6.16950  -17.39434 1.000 25.40146 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? 1.09336   -7.17794  -17.55027 1.000 23.34192 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? -0.18779  -6.76739  -17.88436 1.000 22.41861 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? 1.32304   -8.54162  -17.34902 1.000 26.12274 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? -1.20940  -7.66828  -18.01084 1.000 24.36514 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? 0.29231   -9.45955  -17.47717 1.000 24.61839 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? -0.96444  -9.00959  -17.80817 1.000 23.16110 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? -1.98622  -9.89556  -17.94371 1.000 25.97566 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? 4.74866   -4.38433  -18.13816 1.000 29.43295 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? 5.47695   -3.12977  -18.07252 1.000 28.96637 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? 5.54917   -2.49750  -19.45324 1.000 29.06886 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? 5.26945   -1.30452  -19.61403 1.000 26.59667 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? 6.85332   -3.37584  -17.45498 1.000 31.08685 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? 6.73578   -3.82143  -16.00518 1.000 36.33777 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? 6.66069   -5.34677  -15.83092 1.000 42.03728 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? 6.39434   -6.07070  -16.82439 1.000 38.76666 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? 6.81278   -5.81804  -14.67650 1.000 44.53340 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? 5.85417   -3.30773  -20.47184 1.000 30.73784 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? 5.83729   -2.83058  -21.85324 1.000 33.43387 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? 4.45714   -2.31853  -22.24311 1.000 30.60389 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? 4.31962   -1.24767  -22.85028 1.000 27.28045 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? 6.24637   -3.95774  -22.80095 1.000 37.67444 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? 7.71123   -3.94573  -23.12567 1.000 40.34913 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? 8.45867   -3.17203  -22.49001 1.000 41.59787 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? 8.11909   -4.72749  -24.01119 1.000 44.15164 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? 3.42097   -3.09172  -21.91756 1.000 29.75112 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? 2.06949   -2.73182  -22.31669 1.000 29.26565 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? 1.62797   -1.44351  -21.64518 1.000 27.41580 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? 0.99437   -0.59529  -22.28237 1.000 27.01447 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? 1.09688   -3.86542  -21.98568 1.000 28.35400 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? 1.34039   -5.16773  -22.75110 1.000 31.46482 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? 0.46762   -6.28677  -22.20924 1.000 31.82036 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? 1.13106   -4.97495  -24.24103 1.000 33.87707 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? 1.97933   -1.26545  -20.36946 1.000 25.86843 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? 1.49413   -0.10315  -19.63687 1.000 25.24609 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? 2.21478   1.17612   -20.06780 1.000 25.64076 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? 1.59162   2.23860   -20.13976 1.000 24.31730 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? 1.63666   -0.32626  -18.12868 1.000 27.58842 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? 0.97023   0.73398   -17.24443 1.000 26.88033 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? -0.50532  0.89121   -17.62468 1.000 24.81333 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? 1.12737   0.43741   -15.76330 1.000 25.66812 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? 3.51484   1.10462   -20.37956 1.000 24.88155 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? 4.23447   2.31887   -20.76359 1.000 26.65736 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? 3.65840   2.89507   -22.05302 1.000 27.71530 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? 3.73398   4.10858   -22.29185 1.000 28.80759 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? 5.75560   2.04684   -20.87178 1.000 27.29049 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? 6.54883   3.35582   -20.90059 1.000 30.42528 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? 6.09463   1.23082   -22.09519 1.000 28.32390 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? 6.11506   4.36040   -19.85657 1.000 29.81216 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? 3.04871   2.04944   -22.88341 1.000 27.77842 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? 2.42293   2.46201   -24.13139 1.000 29.14475 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? 1.03229   3.02252   -23.92779 1.000 28.62092 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? 0.39414   3.43371   -24.90367 1.000 29.81602 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? 2.36474   1.27651   -25.08509 1.000 29.62630 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? 3.71879   0.67197   -25.30624 1.000 30.31100 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? 3.64906   -0.54704  -26.17266 1.000 30.86341 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? 4.97878   -1.11641  -26.32393 1.000 31.91017 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? 5.22839   -2.40141  -26.51603 1.000 35.18928 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? 4.24939   -3.29258  -26.58446 1.000 34.01870 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? 6.49189   -2.80136  -26.64322 1.000 36.61474 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? 0.55476   3.04053   -22.69246 1.000 27.02292 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? -0.75084  3.57246   -22.36540 1.000 27.30938 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? -0.60832  5.00124   -21.85851 1.000 28.13761 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? 0.44345   5.40308   -21.36305 1.000 30.12821 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? -1.44057  2.70007   -21.31523 1.000 27.15635 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? -1.74305  1.28747   -21.81118 1.000 26.74208 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? -3.02295  1.28144   -22.63030 1.000 29.57081 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? -3.13147  0.02049   -23.47921 1.000 32.35932 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? -4.00934  0.26616   -24.65611 1.000 36.78612 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? -1.67888  5.76845   -22.00835 1.000 31.49470 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? -1.81075  7.10320   -21.44932 1.000 32.07210 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? -3.00945  7.10731   -20.50789 1.000 30.59689 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? -3.85479  6.21518   -20.56329 1.000 29.94106 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? -2.01321  8.15563   -22.55301 1.000 32.71345 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? -1.29031  7.84145   -23.74016 1.000 39.08073 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? -3.08663  8.12300   -19.64402 1.000 29.47959 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? -4.26624  8.28134   -18.79050 1.000 29.11499 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? -5.55924  8.21374   -19.60121 1.000 29.90784 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? -6.51847  7.54784   -19.20157 1.000 30.48569 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? -4.18960  9.60733   -18.03608 1.000 30.10395 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? -3.14969  9.59875   -16.93313 1.000 31.00994 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? -2.71774  8.54102   -16.46554 1.000 29.69534 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? -2.69895  10.79246  -16.54454 1.000 27.43587 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? -5.60208  8.88927   -20.75429 1.000 31.97935 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? -6.84343  8.94790   -21.52223 1.000 32.58889 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? -7.22299  7.60288   -22.12484 1.000 33.00780 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? -8.37637  7.42753   -22.53161 1.000 32.95699 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? -6.75053  10.01071  -22.62305 1.000 35.79979 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? -5.82082  9.65908   -23.74524 1.000 37.55155 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? -6.16777  8.78757   -24.75812 1.000 38.71836 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? -4.55919  10.06810  -24.01841 1.000 38.58485 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? -5.15899  8.67789   -25.60680 1.000 39.37587 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? -4.16906  9.44118   -25.17861 1.000 40.21826 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? -6.30094  6.64172   -22.16161 1.000 32.25207 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? -6.65928  5.30784   -22.61641 1.000 31.77005 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? -7.56538  4.58057   -21.62764 1.000 29.99116 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? -8.12189  3.53809   -21.98196 1.000 31.58691 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? -5.39323  4.48917   -22.86226 1.000 31.57408 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? -4.64488  4.92650   -24.09392 1.000 35.59303 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? -3.41763  4.90719   -24.11927 1.000 33.89375 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? -5.37724  5.33560   -25.12596 1.000 35.99045 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? -7.73143  5.09835   -20.40709 1.000 28.75633 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? -8.54018  4.45517   -19.37079 1.000 29.84022 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? -9.82954  5.23925   -19.16590 1.000 31.94478 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? -9.81388  6.35847   -18.64410 1.000 31.03152 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? -7.77101  4.33520   -18.05945 1.000 27.32884 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? -6.51534  3.53420   -18.16912 1.000 26.59509 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? -6.55756  2.15635   -18.09263 1.000 23.76638 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? -5.28890  4.15594   -18.36363 1.000 28.63782 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? -5.40917  1.41124   -18.19929 1.000 24.46063 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? -4.13455  3.40627   -18.46726 1.000 27.84178 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? -4.19867  2.03446   -18.37558 1.000 24.42313 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? -10.93965 4.64228   -19.56479 1.000 29.94910 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? -12.25861 5.21345   -19.35499 1.000 30.38701 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? -12.80956 4.57688   -18.09231 1.000 26.49251 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? -12.99609 3.36031   -18.05453 1.000 26.86140 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? -13.18237 4.94205   -20.54431 1.000 31.38158 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? -13.00406 5.63284   -21.90954 1.000 33.84831 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? -11.55111 5.76588   -22.37249 1.000 37.23651 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? -13.82094 4.89480   -22.96136 1.000 39.93556 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? -13.00911 5.38061   -17.04941 1.000 27.42615 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? -13.59970 4.91896   -15.79437 1.000 26.10523 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? -14.99208 5.52644   -15.68166 1.000 28.34876 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? -15.15026 6.75144   -15.73542 1.000 28.14940 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? -12.72742 5.28588   -14.57753 1.000 26.70616 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? -13.32978 4.73488   -13.29344 1.000 24.96808 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? -11.31796 4.72148   -14.74739 1.000 26.89363 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? -15.99904 4.67381   -15.52920 1.000 26.48996 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? -17.37910 5.11532   -15.39231 1.000 28.84087 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? -17.83343 4.74336   -13.98976 1.000 28.67961 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? -17.80904 3.56612   -13.62357 1.000 22.12204 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? -18.27669 4.46038   -16.44513 1.000 33.15482 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? -18.23615 5.10730   -17.83096 1.000 38.71719 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? -19.62379 5.49353   -18.34477 1.000 47.94138 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? -20.30279 4.69816   -19.00959 1.000 47.22397 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? -20.04663 6.72912   -18.04776 1.000 48.35197 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? -18.21637 5.73479   -13.19972 1.000 30.19394 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? -18.79824 5.48537   -11.88266 1.000 28.32688 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? -20.28994 5.76128   -12.01641 1.000 33.49719 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? -20.72546 6.90750   -11.92146 1.000 33.68552 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? -18.15054 6.35457   -10.81241 1.000 28.31817 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? -21.06758 4.70816   -12.25091 1.000 36.25542 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? -22.46178 4.90790   -12.61803 1.000 39.57461 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? -22.52886 5.55804   -13.98393 1.000 41.63209 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? -21.83043 5.15201   -14.92143 1.000 42.18121 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? -23.35798 6.59382   -14.10642 1.000 42.85680 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? -23.43154 7.38773   -15.32699 1.000 47.08842 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? -22.58984 8.65700   -15.23102 1.000 46.30703 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? -22.95677 9.69575   -15.79298 1.000 47.41888 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? -24.88759 7.71878   -15.67018 1.000 49.61577 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? -25.68796 8.20745   -14.46373 1.000 54.95882 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? -25.12123 8.71470   -13.49204 1.000 58.28152 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? -27.01534 8.07092   -14.53182 1.000 50.23737 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? -21.47171 8.58885   -14.50976 1.000 41.23897 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? -20.53997 9.69896   -14.34979 1.000 42.32531 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? -19.15768 9.19818   -14.73534 1.000 38.67418 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? -18.70787 8.16253   -14.23728 1.000 34.96425 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? -20.52966 10.24143  -12.90526 1.000 42.83158 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? -19.54518 11.39528  -12.77265 1.000 42.62453 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? -21.91991 10.66776  -12.48075 1.000 45.02001 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? -18.48585 9.91613   -15.61994 1.000 38.86231 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? -17.16564 9.49408   -16.05903 1.000 36.78023 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? -16.11112 10.10506  -15.14456 1.000 36.01997 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? -16.13486 11.31115  -14.88436 1.000 36.53131 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? -16.93527 9.88896   -17.52086 1.000 42.87029 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? -15.69809 9.25422   -18.14545 1.000 41.15145 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? -15.16577 10.04214  -19.33189 1.000 48.89897 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? -15.83401 10.94347  -19.84994 1.000 51.05680 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? -13.94287 9.72297   -19.75156 1.000 48.70894 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? -15.20116 9.26853   -14.64207 1.000 32.57853 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? -14.12170 9.71079   -13.76768 1.000 31.38852 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? -12.88113 9.96544   -14.60970 1.000 33.97911 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? -12.41232 9.06453   -15.31396 1.000 36.78726 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? -13.80896 8.67019   -12.69182 1.000 30.19865 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? -14.89452 8.30512   -11.68562 1.000 29.71461 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? -14.29709 7.43161   -10.57812 1.000 26.50716 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? -15.55158 9.54276   -11.11445 1.000 32.29072 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? -12.33286 11.17270  -14.52262 1.000 33.15435 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? -11.15626 11.49195  -15.31712 1.000 33.44836 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? -9.93614  10.85372  -14.66388 1.000 30.16461 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? -9.66736  11.08173  -13.48068 1.000 29.59422 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? -10.98346 13.00521  -15.45644 1.000 35.00408 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? -9.67090  13.41798  -16.11885 1.000 36.88958 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? -9.57792  14.93417  -16.30202 1.000 42.44815 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? -9.12010  15.62369  -15.09937 1.000 47.22716 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? -7.93882  16.22202  -14.98607 1.000 51.31749 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? -7.09192  16.28356  -16.00557 1.000 49.25032 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? -7.60116  16.78263  -13.82448 1.000 50.32406 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? -9.21993  10.03321  -15.42366 1.000 30.69753 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? -7.98747  9.41564   -14.94426 1.000 30.30187 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? -6.85801  10.43381  -15.07480 1.000 30.45299 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? -6.61809  10.97979  -16.15946 1.000 30.71020 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? -7.67586  8.13038   -15.72362 1.000 27.49649 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? -6.28047  7.63346   -15.40871 1.000 27.40169 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? -8.71781  7.04630   -15.41068 1.000 28.20819 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? -6.17036  10.70574  -13.96474 1.000 29.54009 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? -5.06773  11.66564  -13.94685 1.000 28.18777 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? -3.73905  11.01263  -13.63527 1.000 28.54093 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? -2.70615  11.70337  -13.60115 1.000 27.58495 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? -5.32698  12.81737  -12.95856 1.000 29.90888 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? -5.31707  12.28898  -11.51747 1.000 30.46722 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? -6.62674  13.54081  -13.31038 1.000 32.38230 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? -5.96071  13.22516  -10.52175 1.000 31.53914 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? -3.72574  9.71054   -13.39548 1.000 28.85038 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? -2.49453  8.99435   -13.16214 1.000 26.46242 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? -2.76882  7.50985   -13.22738 1.000 27.56594 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? -3.89557  7.07035   -12.97693 1.000 26.84268 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? -1.75627  6.72697   -13.58277 1.000 27.50333 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? -1.88434  5.28080   -13.57531 1.000 23.71023 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? -0.55630  4.68564   -13.14715 1.000 26.56592 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? 0.50747   5.27490   -13.37208 1.000 26.69683 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? -2.27071  4.73544   -14.94929 1.000 24.26360 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? -1.27814  5.06264   -16.01934 1.000 28.11067 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? -1.27244  6.26762   -16.68606 1.000 27.67069 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? -0.23365  4.35474   -16.50837 1.000 27.25775 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? -0.28235  6.27878   -17.56238 1.000 31.75312 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? 0.36145   5.12784   -17.47502 1.000 31.71343 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? -0.62658  3.51201   -12.52646 1.000 22.99125 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? 0.57811   2.76345   -12.20383 1.000 23.77838 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? 0.20213   1.30631   -12.01813 1.000 21.94612 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? -0.95521  0.96894   -11.77196 1.000 24.11167 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? 1.27645   3.28661   -10.93898 1.000 23.79050 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? 0.38058   3.36939   -9.84576  1.000 25.03028 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? 1.19791   0.44998   -12.13411 1.000 19.54353 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? 1.03643   -0.95413  -11.78927 1.000 22.78715 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? 1.52020   -1.22331  -10.38191 1.000 20.64515 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? 2.61045   -0.77526  -10.00509 1.000 20.61918 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? 1.84001   -1.84072  -12.72097 1.000 23.79488 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? 1.15576   -3.10556  -12.98199 1.000 20.49570 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? 1.68108   -3.70076  -14.55014 1.000 27.65823 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? 3.46592   -3.61414  -14.40495 1.000 29.71342 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? 0.74833   -2.00648  -9.63328  1.000 19.19612 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? 1.25496   -2.59859  -8.39927  1.000 19.93964 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? 0.97290   -4.09178  -8.50105  1.000 17.26079 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? -0.17340  -4.53297  -8.37621  1.000 16.12331 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? 0.65205   -1.94183  -7.16437  1.000 21.46624 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? 0.84689   -2.68670  -5.86659  1.000 25.38271 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? 0.23072   -1.92381  -4.72809  1.000 29.50465 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? 0.57947   -0.76486  -4.50175  1.000 35.72844 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? -0.62675  -2.57471  -3.95979  1.000 29.55762 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? 2.02242   -4.85259  -8.78805  1.000 14.79603 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? 1.91561   -6.30131  -8.98917  1.000 16.88628 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? 0.91475   -6.55951  -10.10510 1.000 14.80931 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? 1.13943   -6.05328  -11.22113 1.000 16.15243 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? 1.60494   -6.95066  -7.65440  1.000 12.42177 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? 2.62073   -6.59373  -6.61791  1.000 14.58571 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? 3.81288   -6.79142  -6.83268  1.000 13.68611 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? 2.17319   -5.99072  -5.52620  1.000 15.66919 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? -0.17616  -7.29438  -9.86651  1.000 15.16759 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? -1.13096  -7.63373  -10.89404 1.000 13.98204 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? -2.33941  -6.70629  -10.91342 1.000 16.60960 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? -3.28417  -6.96060  -11.66615 1.000 17.49484 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? -1.55792  -9.09335  -10.72766 1.000 14.02676 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? -0.14119  -10.15683 -10.99208 1.000 14.96630 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? -2.32865  -5.61850  -10.13955 1.000 13.23240 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? -3.42321  -4.66159  -10.22401 1.000 14.03046 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? -2.90691  -3.34527  -10.79036 1.000 15.21019 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? -1.72187  -2.99459  -10.69372 1.000 15.26680 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? -4.15317  -4.42332  -8.88681  1.000 14.18650 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? -4.77190  -5.74111  -8.33730  1.000 15.30953 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? -3.24958  -3.80906  -7.89675  1.000 16.08096 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? -3.81556  -2.64081  -11.43593 1.000 14.25331 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? -3.60203  -1.27371  -11.84956 1.000 16.18797 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? -4.15916  -0.35186  -10.78505 1.000 19.05320 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? -5.18031  -0.65009  -10.16148 1.000 16.46370 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? -4.29415  -0.99431  -13.17571 1.000 18.09264 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? -3.63372  -1.33399  -14.49403 1.000 21.04129 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? -4.50365  -0.74008  -15.57262 1.000 21.05181 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? -2.23234  -0.74202  -14.54200 1.000 23.10214 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? -3.47142  0.75233   -10.56901 1.000 18.64099 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? -3.95666  1.83474   -9.73316  1.000 20.65394 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? -4.18196  3.02680   -10.65293 1.000 19.95470 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? -3.22869  3.60837   -11.17992 1.000 22.36410 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? -2.96295  2.14999   -8.62612  1.000 21.50486 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? -2.88683  1.08194   -7.56176  1.000 17.84684 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? -1.77696  1.40610   -6.58470  1.000 25.35065 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? -2.29695  1.67862   -5.18688  1.000 28.48529 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? -1.47481  2.69624   -4.45526  1.000 30.51268 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? -5.43696  3.36564   -10.86651 1.000 20.08082 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? -5.80264  4.49110   -11.71178 1.000 19.78523 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? -6.12403  5.66241   -10.79718 1.000 21.58153 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? -7.12386  5.63158   -10.07006 1.000 20.98055 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? -6.99149  4.12801   -12.58628 1.000 21.47033 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? -6.69768  3.00353   -13.57572 1.000 21.11468 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? -7.87491  2.81300   -14.46737 1.000 20.73453 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? -5.46207  3.30767   -14.40672 1.000 22.68932 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? -5.28051  6.68580   -10.82135 1.000 21.66328 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? -5.56198  7.87835   -10.04126 1.000 24.64093 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? -6.61709  8.70766   -10.76360 1.000 24.37824 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? -6.48111  9.00737   -11.95103 1.000 27.32896 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? -4.29430  8.69139   -9.80330  1.000 27.09504 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? -4.17653  9.17807   -8.38079  1.000 30.81441 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? -3.69152  10.61048  -8.35541  1.000 33.56204 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? -3.29397  11.04779  -6.95663  1.000 34.40321 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? -2.43712  12.27197  -7.01430  1.000 34.49136 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? -7.69647  9.03068   -10.06087 1.000 25.14778 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? -8.79280  9.78817   -10.64139 1.000 26.18477 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? -8.91091  11.13044  -9.92907  1.000 26.58638 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? -8.45738  11.31159  -8.79827  1.000 29.04389 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? -10.12011 9.00321   -10.59889 1.000 25.57047 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? -9.98857  7.72547   -11.39836 1.000 25.89709 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? -10.48139 8.65633   -9.16513  1.000 24.12858 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? -9.52223  12.08607  -10.61272 1.000 29.09710 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? -9.54470  13.44619  -10.08895 1.000 33.26426 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? -10.61102 13.64481  -9.01971  1.000 33.18887 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? -10.71790 14.74262  -8.46440  1.000 31.69287 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? -9.73790  14.43588  -11.24643 1.000 34.76551 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? -11.18735 14.59974  -11.63660 1.000 42.21761 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? -11.85975 15.46847  -11.03881 1.000 48.16461 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? -11.66625 13.84277  -12.51071 1.000 41.55306 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? -11.39104 12.61197  -8.71591  1.000 31.61903 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? -12.46821 12.68786  -7.73763  1.000 32.48335 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? -12.28536 11.58691  -6.70082  1.000 28.49981 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? -12.16374 10.41164  -7.05932  1.000 24.61896 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? -13.83733 12.54023  -8.41477  1.000 32.39042 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? -13.91983 13.43248  -9.53208  1.000 36.04196 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? -14.96674 12.84244  -7.43188  1.000 32.02537 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? -12.26644 11.96568  -5.42254  1.000 25.95930 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? -12.30291 10.98012  -4.35522  1.000 23.46135 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? -13.71413 10.42489  -4.23107  1.000 24.99307 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? -14.69037 11.17173  -4.29578  1.000 25.76451 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? -11.87340 11.59657  -3.03115  1.000 24.79826 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? -13.81956 9.11536   -4.07794  1.000 23.47540 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? -15.13156 8.49066   -3.94349  1.000 23.05117 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? -15.81272 8.94298   -2.65899  1.000 22.82906 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? -15.37537 8.54584   -1.57166  1.000 22.88686 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? -14.98817 6.97625   -3.95760  1.000 19.32451 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? -16.32657 6.26038   -3.96683  1.000 19.28115 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? -17.39140 6.88860   -3.95545  1.000 20.90015 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? -16.27578 4.92986   -3.99396  1.000 17.54385 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? -16.88849 9.73238   -2.72736  1.000 26.26347 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? -17.53012 10.18644  -1.48422  1.000 25.13488 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? -18.14992 9.04600   -0.70541  1.000 24.73798 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? -18.44954 9.20031   0.48530   1.000 25.54551 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? -18.59097 11.17347  -1.97903  1.000 26.55898 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? -18.92232 10.70492  -3.34514  1.000 27.53446 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? -17.69024 10.06004  -3.91914  1.000 24.08393 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? -18.33863 7.90079   -1.33864  1.000 22.89057 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? -18.86287 6.72787   -0.66793  1.000 22.96838 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? -17.76503 5.80872   -0.15764  1.000 21.21123 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? -18.06034 4.67257   0.21670   1.000 20.32393 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? -19.81020 5.97613   -1.60163  1.000 22.00703 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? -21.11815 6.71851   -1.78986  1.000 24.63966 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? -22.11809 5.97116   -2.65602  1.000 31.33279 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? -22.29980 6.59245   -4.02667  1.000 32.80140 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? -22.96042 5.63309   -4.96763  1.000 39.21267 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? -16.52014 6.28029   -0.09513  1.000 22.20441 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? -15.44234 5.42926   0.39323   1.000 20.70046 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? -15.71476 5.00870   1.83548   1.000 19.73929 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? -15.77383 5.87166   2.72704   1.000 19.72673 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? -14.09146 6.13600   0.31909   1.000 23.09876 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? -13.83392 6.54517   -1.02462  1.000 21.57049 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? -12.97733 5.18003   0.74458   1.000 20.50987 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? -15.88307 3.72531   2.10969   1.000 20.77219 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? -16.00872 3.28538   3.49292   1.000 20.32759 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? -14.64669 3.29297   4.15469   1.000 19.43876 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? -13.60337 3.40191   3.50282   1.000 20.12113 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? -16.53895 1.85751   3.35612   1.000 17.86947 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? -15.89302 1.36442   2.13854   1.000 18.32651 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? -15.75473 2.57747   1.19937   1.000 19.70231 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? -14.67110 3.15170   5.47208   1.000 20.41693 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? -13.44644 2.80759   6.16032   1.000 21.33140 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? -13.03554 1.43909   5.63511   1.000 21.72749 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? -13.87742 0.54977   5.49195   1.000 16.98965 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? -13.67259 2.79641   7.67158   1.000 26.57245 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? -12.38704 2.69417   8.48912   1.000 32.16631 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? -12.61002 2.24673   9.94184   1.000 37.55927 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? -11.26933 1.84338   10.58615  1.000 38.97563 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? -10.42722 0.95363   9.70375   1.000 33.25408 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? -11.77309 1.28788   5.24528   1.000 18.12703 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? -11.39922 0.01332   4.65494   1.000 17.02966 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? -9.97728  -0.34091  5.03765   1.000 18.69681 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? -9.20418  0.48729   5.52017   1.000 17.61276 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? -11.54120 0.01635   3.12889   1.000 15.40337 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? -10.53718 0.89208   2.41019   1.000 19.73322 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? -10.80583 2.22798   2.17378   1.000 17.91651 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? -9.31638  0.37787   1.96624   1.000 19.66634 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? -9.90119  3.03469   1.51458   1.000 18.87198 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? -8.39395  1.19058   1.29704   1.000 16.42997 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? -8.70252  2.51884   1.08573   1.000 19.82658 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? -7.81383  3.34904   0.43805   1.000 25.08493 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? -9.64495  -1.60014  4.78737   1.000 16.64104 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? -8.28180  -2.09244  4.82902   1.000 15.15813 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? -8.12531  -3.06778  3.68059   1.000 16.21208 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? -9.09914  -3.67261  3.23768   1.000 11.77954 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? -7.95223  -2.82954  6.12382   1.000 17.43253 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? -8.53554  -2.23504  7.34558   1.000 23.88861 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? -7.94313  -2.87570  8.57941   1.000 26.85146 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? -8.62013  -4.19267  8.86568   1.000 25.63679 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? -8.28172  -4.67527  10.24228  1.000 33.51725 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? -6.90036  -3.21941  3.21475   1.000 15.30369 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? -6.52987  -4.29488  2.30494   1.000 10.10555 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? -5.89112  -5.38456  3.15341   1.000 14.47147 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? -4.80648  -5.18794  3.70499   1.000 11.12040 ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? -5.52611  -3.81367  1.26477   1.000 12.63570 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? -6.09052  -2.90564  0.25640   1.000 13.70379 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? -7.45343  -2.71920  0.16379   1.000 10.87101 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? -5.25971  -2.23759  -0.62154  1.000 15.57599 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? -7.97211  -1.89394  -0.77414  1.000 12.87035 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? -5.77475  -1.41005  -1.58227  1.000 15.63844 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? -7.13252  -1.22606  -1.66079  1.000 12.68121 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? -6.53355  -6.53081  3.23695   1.000 9.51320  ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? -5.99892  -7.61667  4.04445   1.000 11.13651 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? -5.86665  -8.81377  3.12940   1.000 14.21453 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? -6.62501  -8.96666  2.17005   1.000 19.03508 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? -6.86665  -7.94174  5.28040   1.000 13.40935 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? -7.23374  -6.65149  6.01774   1.000 15.32274 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? -8.10983  -8.67300  4.89886   1.000 16.33894 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? -4.88555  -9.65156  3.39891   1.000 10.86155 ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? -4.76696  -10.89689 2.66162   1.000 9.42272  ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? -5.25200  -11.99893 3.58289   1.000 10.53759 ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? -4.84435  -12.06028 4.74172   1.000 12.80562 ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? -3.32422  -11.15905 2.23035   1.000 12.72902 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? -3.21363  -12.31736 1.25382   1.000 11.16013 ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? -1.75690  -12.52625 0.91234   1.000 10.16775 ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? -1.55795  -13.76030 0.17440   1.000 11.49371 ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? -1.51356  -13.82237 -1.14687  1.000 10.81564 ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? -1.69254  -12.74316 -1.88225  1.000 11.79127 ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? -1.24562  -14.98655 -1.74074  1.000 9.14770  ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? -6.12239  -12.86170 3.08068   1.000 13.04641 ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? -6.67068  -13.90948 3.90458   1.000 14.65361 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? -5.86773  -15.18560 3.68964   1.000 11.52037 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? -5.10900  -15.31496 2.74235   1.000 14.10630 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? -8.16674  -14.14206 3.63802   1.000 11.58712 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? -8.38135  -14.49951 2.17762   1.000 9.89926  ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? -9.00723  -12.94470 4.13577   1.000 13.68426 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? -9.76531  -15.14224 1.95007   1.000 15.64215 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? -6.03956  -16.12646 4.57558   1.000 10.97504 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? -5.56412  -17.49855 4.65702   1.000 13.65021 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? -6.54520  -18.44372 3.98292   1.000 13.55120 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? -7.75215  -18.23940 4.06285   1.000 14.11280 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? -5.40012  -17.90649 6.10980   1.000 15.86306 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? -4.28932  -17.16206 6.73143   1.000 15.66968 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? -2.98311  -17.60894 6.13725   1.000 16.30978 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? -2.78375  -18.80987 5.90918   1.000 13.69686 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? -2.09426  -16.65607 5.84240   1.000 15.36173 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? -6.03957  -19.47067 3.30769   1.000 15.56514 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? -6.90806  -20.57861 2.91391   1.000 16.49333 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? -7.66087  -21.03985 4.14238   1.000 17.20621 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? -7.12645  -21.02934 5.25614   1.000 18.53342 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? -5.93764  -21.65470 2.39743   1.000 14.61890 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? -4.58383  -21.14402 2.65934   1.000 17.23276 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? -4.65845  -19.66209 2.86561   1.000 11.67074 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? -8.91376  -21.41089 3.93551   1.000 12.54503 ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? -9.79324  -21.76540 5.01645   1.000 17.07478 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? -10.63781 -20.62607 5.52263   1.000 18.05611 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? -11.69379 -20.87755 6.11564   1.000 19.55432 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? -10.21984 -19.38214 5.29552   1.000 14.12096 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? -11.05103 -18.25241 5.67403   1.000 13.74702 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? -12.04852 -17.90389 4.58427   1.000 12.30497 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? -11.87765 -18.22802 3.39785   1.000 12.94370 ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? -10.25737 -16.99551 6.06757   1.000 16.19986 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? -9.14412  -17.19466 7.05984   1.000 20.91675 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? -8.45442  -15.87770 7.47747   1.000 26.42175 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? -7.65477  -15.28454 6.74319   1.000 15.05548 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? -8.80954  -15.40048 8.68309   1.000 33.94496 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? -13.14187 -17.30055 5.01892   1.000 10.56359 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? -14.24133 -16.99542 4.12120   1.000 12.47260 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? -14.32568 -15.50210 3.88146   1.000 15.25073 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? -13.72399 -14.69321 4.59177   1.000 13.26376 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? -15.55270 -17.49313 4.70828   1.000 14.28592 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? -15.66562 -16.93755 6.02090   1.000 14.79451 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? -15.48443 -18.99677 4.80648   1.000 14.21231 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? -15.10250 -15.15996 2.85658   1.000 12.09659 ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? -15.33718 -13.77262 2.50484   1.000 13.24557 ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? -16.54557 -13.70895 1.60323   1.000 12.49151 ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? -16.96311 -14.70534 0.99843   1.000 13.65090 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? -14.14391 -13.11917 1.81821   1.000 11.44133 ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? -13.61872 -13.87036 0.61554   1.000 15.03194 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? -12.76112 -14.94007 0.78560   1.000 13.83427 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? -13.93443 -13.47747 -0.67866  1.000 9.48670  ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? -12.24787 -15.61891 -0.31493  1.000 16.18715 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? -13.40906 -14.15237 -1.79119  1.000 13.87901 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? -12.54849 -15.21812 -1.59811  1.000 13.82178 ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? -17.10610 -12.51609 1.53346   1.000 12.02717 ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? -18.20382 -12.23896 0.64636   1.000 11.17386 ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? -17.64804 -11.69600 -0.65507  1.000 10.85342 ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? -16.75157 -10.85348 -0.65846  1.000 12.26009 ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? -19.16462 -11.23055 1.27476   1.000 13.55049 ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? -19.51958 -11.68444 2.56490   1.000 13.24294 ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? -18.20339 -12.18550 -1.74659  1.000 11.17479 ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? -17.90170 -11.73544 -3.08991  1.000 12.72090 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? -19.08891 -10.93475 -3.58576  1.000 13.89347 ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? -20.21523 -11.44521 -3.63889  1.000 13.94856 ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? -17.63585 -12.91648 -4.03530  1.000 10.30396 ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? -17.54164 -12.40282 -5.49075  1.000 12.63083 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? -16.39446 -13.71037 -3.61478  1.000 14.18965 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? -18.83195 -9.71264  -4.00514  1.000 12.22414 ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? -19.81691 -8.91983  -4.73226  1.000 11.41397 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? -19.53935 -9.04449  -6.22582  1.000 13.75716 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? -18.67928 -8.35019  -6.77464  1.000 14.18538 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? -19.78696 -7.47190  -4.26236  1.000 11.00439 ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? -20.77303 -6.60742  -5.04720  1.000 11.02918 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? -22.22706 -7.08690  -4.82243  1.000 13.57490 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? -20.64887 -5.18589  -4.61132  1.000 12.47584 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? -20.26782 -9.93806  -6.88467  1.000 12.62591 ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? -20.06493 -10.15522 -8.30184  1.000 12.72451 ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? -20.61718 -8.95710  -9.04217  1.000 16.57787 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? -21.75329 -8.54464  -8.79170  1.000 18.00944 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? -20.77089 -11.42720 -8.78260  1.000 14.82936 ? 116 ALA   A CB  1 
ATOM   907  N  N   . CYS   A 1 117 ? -19.81042 -8.39225  -9.93639  1.000 11.97237 ? 117 CYS   A N   1 
ATOM   908  C  CA  . CYS   A 1 117 ? -20.22161 -7.26916  -10.76443 1.000 16.49466 ? 117 CYS   A CA  1 
ATOM   909  C  C   . CYS   A 1 117 ? -19.83314 -7.46092  -12.20772 1.000 16.85298 ? 117 CYS   A C   1 
ATOM   910  O  O   . CYS   A 1 117 ? -18.94147 -8.23221  -12.55457 1.000 18.30774 ? 117 CYS   A O   1 
ATOM   911  C  CB  . CYS   A 1 117 ? -19.69196 -5.90669  -10.32087 1.000 18.31250 ? 117 CYS   A CB  1 
ATOM   912  S  SG  . CYS   A 1 117 ? -19.51595 -5.66380  -8.62432  1.000 22.86873 ? 117 CYS   A SG  1 
ATOM   913  N  N   . TYR   A 1 118 ? -20.57103 -6.74025  -13.03239 1.000 19.02020 ? 118 TYR   A N   1 
ATOM   914  C  CA  . TYR   A 1 118 ? -20.40541 -6.68452  -14.47278 1.000 20.61634 ? 118 TYR   A CA  1 
ATOM   915  C  C   . TYR   A 1 118 ? -20.57886 -5.23032  -14.85628 1.000 23.54930 ? 118 TYR   A C   1 
ATOM   916  O  O   . TYR   A 1 118 ? -21.51509 -4.57826  -14.37728 1.000 22.12356 ? 118 TYR   A O   1 
ATOM   917  C  CB  . TYR   A 1 118 ? -21.41687 -7.59629  -15.18529 1.000 19.97773 ? 118 TYR   A CB  1 
ATOM   918  C  CG  . TYR   A 1 118 ? -21.21747 -9.00664  -14.71102 1.000 21.71098 ? 118 TYR   A CG  1 
ATOM   919  C  CD1 . TYR   A 1 118 ? -21.88804 -9.49034  -13.59235 1.000 20.37612 ? 118 TYR   A CD1 1 
ATOM   920  C  CD2 . TYR   A 1 118 ? -20.27324 -9.82203  -15.31939 1.000 21.78430 ? 118 TYR   A CD2 1 
ATOM   921  C  CE1 . TYR   A 1 118 ? -21.64690 -10.75307 -13.11361 1.000 20.30497 ? 118 TYR   A CE1 1 
ATOM   922  C  CE2 . TYR   A 1 118 ? -20.02730 -11.08136 -14.85677 1.000 21.98070 ? 118 TYR   A CE2 1 
ATOM   923  C  CZ  . TYR   A 1 118 ? -20.71313 -11.54678 -13.76058 1.000 24.08301 ? 118 TYR   A CZ  1 
ATOM   924  O  OH  . TYR   A 1 118 ? -20.44769 -12.81042 -13.30429 1.000 23.30963 ? 118 TYR   A OH  1 
ATOM   925  N  N   . ASN   A 1 119 ? -19.64074 -4.71376  -15.65817 1.000 23.55354 ? 119 ASN   A N   1 
ATOM   926  C  CA  . ASN   A 1 119 ? -19.70038 -3.33725  -16.15146 1.000 22.76087 ? 119 ASN   A CA  1 
ATOM   927  C  C   . ASN   A 1 119 ? -19.81460 -2.32558  -15.01136 1.000 22.51512 ? 119 ASN   A C   1 
ATOM   928  O  O   . ASN   A 1 119 ? -20.49823 -1.30433  -15.14049 1.000 23.08616 ? 119 ASN   A O   1 
ATOM   929  C  CB  . ASN   A 1 119 ? -20.86462 -3.16502  -17.12954 1.000 25.95853 ? 119 ASN   A CB  1 
ATOM   930  C  CG  . ASN   A 1 119 ? -20.82074 -4.17260  -18.24681 1.000 28.14586 ? 119 ASN   A CG  1 
ATOM   931  O  OD1 . ASN   A 1 119 ? -19.89697 -4.16859  -19.06230 1.000 33.18974 ? 119 ASN   A OD1 1 
ATOM   932  N  ND2 . ASN   A 1 119 ? -21.80579 -5.06807  -18.27593 1.000 29.24821 ? 119 ASN   A ND2 1 
ATOM   933  N  N   . GLY   A 1 120 ? -19.17850 -2.62012  -13.87675 1.000 17.89262 ? 120 GLY   A N   1 
ATOM   934  C  CA  . GLY   A 1 120 ? -19.26361 -1.76188  -12.71415 1.000 19.90331 ? 120 GLY   A CA  1 
ATOM   935  C  C   . GLY   A 1 120 ? -20.57037 -1.84433  -11.94813 1.000 23.57659 ? 120 GLY   A C   1 
ATOM   936  O  O   . GLY   A 1 120 ? -20.76229 -1.07743  -10.99889 1.000 24.90246 ? 120 GLY   A O   1 
ATOM   937  N  N   . SER   A 1 121 ? -21.47909 -2.74050  -12.31996 1.000 22.43623 ? 121 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 121 ? -22.77689 -2.81100  -11.66011 1.000 21.24495 ? 121 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 121 ? -22.89664 -4.08894  -10.84865 1.000 24.70540 ? 121 SER   A C   1 
ATOM   940  O  O   . SER   A 1 121 ? -22.74413 -5.19155  -11.40380 1.000 22.95006 ? 121 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 121 ? -23.89096 -2.72604  -12.69017 1.000 26.79830 ? 121 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 121 ? -23.98281 -1.39771  -13.12191 1.000 32.78734 ? 121 SER   A OG  1 
ATOM   943  N  N   . PRO   A 1 122 ? -23.13262 -3.97666  -9.54154  1.000 21.01190 ? 122 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 122 ? -23.25137 -5.17334  -8.69696  1.000 23.25830 ? 122 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 122 ? -24.38518 -6.07338  -9.14629  1.000 22.97176 ? 122 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 122 ? -25.51092 -5.62229  -9.36373  1.000 24.80567 ? 122 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 122 ? -23.51322 -4.59652  -7.30476  1.000 21.62911 ? 122 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 122 ? -22.90561 -3.20984  -7.33787  1.000 24.58470 ? 122 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 122 ? -22.75225 -2.77842  -8.77211  1.000 22.88892 ? 122 PRO   A CD  1 
ATOM   950  N  N   . SER   A 1 123 ? -24.07942 -7.36109  -9.25975  1.000 23.32817 ? 123 SER   A N   1 
ATOM   951  C  CA  . SER   A 1 123 ? -25.02131 -8.37812  -9.70577  1.000 23.08783 ? 123 SER   A CA  1 
ATOM   952  C  C   . SER   A 1 123 ? -25.52910 -9.27231  -8.58796  1.000 23.12099 ? 123 SER   A C   1 
ATOM   953  O  O   . SER   A 1 123 ? -26.72008 -9.59144  -8.54778  1.000 22.57119 ? 123 SER   A O   1 
ATOM   954  C  CB  . SER   A 1 123 ? -24.36330 -9.25872  -10.76918 1.000 26.62093 ? 123 SER   A CB  1 
ATOM   955  O  OG  . SER   A 1 123 ? -25.22332 -10.31323 -11.14346 1.000 34.71091 ? 123 SER   A OG  1 
ATOM   956  N  N   . GLY   A 1 124 ? -24.64655 -9.71545  -7.70734  1.000 17.96380 ? 124 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? -25.03138 -10.61030 -6.64195  1.000 16.74033 ? 124 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? -23.95195 -10.67589 -5.59625  1.000 16.08309 ? 124 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? -22.80954 -10.23564 -5.81139  1.000 14.75617 ? 124 GLY   A O   1 
ATOM   960  N  N   . VAL   A 1 125 ? -24.33026 -11.19455 -4.43999  1.000 12.43921 ? 125 VAL   A N   1 
ATOM   961  C  CA  . VAL   A 1 125 ? -23.38922 -11.33503 -3.34533  1.000 13.89951 ? 125 VAL   A CA  1 
ATOM   962  C  C   . VAL   A 1 125 ? -23.50160 -12.75122 -2.80708  1.000 15.18868 ? 125 VAL   A C   1 
ATOM   963  O  O   . VAL   A 1 125 ? -24.59033 -13.34208 -2.76631  1.000 15.04574 ? 125 VAL   A O   1 
ATOM   964  C  CB  . VAL   A 1 125 ? -23.61423 -10.27091 -2.25313  1.000 14.57643 ? 125 VAL   A CB  1 
ATOM   965  C  CG1 . VAL   A 1 125 ? -24.91585 -10.47052 -1.60775  1.000 16.26229 ? 125 VAL   A CG1 1 
ATOM   966  C  CG2 . VAL   A 1 125 ? -22.53792 -10.33234 -1.21362  1.000 13.49269 ? 125 VAL   A CG2 1 
ATOM   967  N  N   . TYR   A 1 126 ? -22.36110 -13.32616 -2.47940  1.000 14.81571 ? 126 TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 126 ? -22.33751 -14.68283 -1.97018  1.000 12.97291 ? 126 TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 126 ? -21.06167 -14.86776 -1.17430  1.000 14.35581 ? 126 TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 126 ? -20.10382 -14.08702 -1.26818  1.000 14.62072 ? 126 TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 126 ? -22.45038 -15.72791 -3.10057  1.000 14.15408 ? 126 TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 126 ? -21.35383 -15.63137 -4.13430  1.000 14.39924 ? 126 TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 126 ? -20.15849 -16.30113 -3.96777  1.000 17.29767 ? 126 TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 126 ? -21.51004 -14.86291 -5.27666  1.000 17.32759 ? 126 TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 126 ? -19.14609 -16.19142 -4.90673  1.000 17.76069 ? 126 TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 126 ? -20.48747 -14.75660 -6.22408  1.000 15.27234 ? 126 TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 126 ? -19.32781 -15.43214 -6.03422  1.000 16.49755 ? 126 TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 126 ? -18.31281 -15.34495 -6.96715  1.000 19.22293 ? 126 TYR   A OH  1 
ATOM   979  N  N   . GLN   A 1 127 ? -21.07635 -15.90990 -0.37454  1.000 10.90405 ? 127 GLN   A N   1 
ATOM   980  C  CA  . GLN   A 1 127 ? -19.99196 -16.22131 0.53335   1.000 16.36435 ? 127 GLN   A CA  1 
ATOM   981  C  C   . GLN   A 1 127 ? -19.08672 -17.24774 -0.12539  1.000 14.65205 ? 127 GLN   A C   1 
ATOM   982  O  O   . GLN   A 1 127 ? -19.56543 -18.17405 -0.78242  1.000 19.49285 ? 127 GLN   A O   1 
ATOM   983  C  CB  . GLN   A 1 127 ? -20.60017 -16.72467 1.84372   1.000 17.80735 ? 127 GLN   A CB  1 
ATOM   984  C  CG  . GLN   A 1 127 ? -19.65874 -16.82106 2.92696   1.000 18.51968 ? 127 GLN   A CG  1 
ATOM   985  C  CD  . GLN   A 1 127 ? -19.33598 -15.49001 3.55184   1.000 15.63023 ? 127 GLN   A CD  1 
ATOM   986  O  OE1 . GLN   A 1 127 ? -19.60630 -14.42352 2.98833   1.000 17.26244 ? 127 GLN   A OE1 1 
ATOM   987  N  NE2 . GLN   A 1 127 ? -18.74121 -15.54385 4.72552   1.000 16.02414 ? 127 GLN   A NE2 1 
ATOM   988  N  N   . CYS   A 1 128 ? -17.78009 -17.03228 -0.01553  1.000 14.33127 ? 128 CYS   A N   1 
ATOM   989  C  CA  . CYS   A 1 128 ? -16.74786 -17.87862 -0.58819  1.000 20.35504 ? 128 CYS   A CA  1 
ATOM   990  C  C   . CYS   A 1 128 ? -15.76097 -18.25788 0.49877   1.000 15.90860 ? 128 CYS   A C   1 
ATOM   991  O  O   . CYS   A 1 128 ? -15.57514 -17.51284 1.45412   1.000 15.09383 ? 128 CYS   A O   1 
ATOM   992  C  CB  . CYS   A 1 128 ? -15.95284 -17.16012 -1.70709  1.000 14.94300 ? 128 CYS   A CB  1 
ATOM   993  S  SG  . CYS   A 1 128 ? -16.61218 -17.45431 -3.27835  1.000 27.65990 ? 128 CYS   A SG  1 
ATOM   994  N  N   . ALA   A 1 129 ? -15.12774 -19.41676 0.35216   1.000 15.34116 ? 129 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? -13.93455 -19.71635 1.12756   1.000 13.29156 ? 129 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? -12.73441 -19.75174 0.19392   1.000 17.15627 ? 129 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? -12.83616 -20.16401 -0.96759  1.000 14.51807 ? 129 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? -14.02904 -21.05777 1.86155   1.000 18.07008 ? 129 ALA   A CB  1 
ATOM   999  N  N   . MET   A 1 130 ? -11.59686 -19.33053 0.72343   1.000 13.44810 ? 130 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 130 ? -10.30868 -19.51470 0.06559   1.000 12.00113 ? 130 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 130 ? -9.94132  -20.97902 0.23550   1.000 12.44183 ? 130 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 130 ? -9.73674  -21.43843 1.36181   1.000 13.42145 ? 130 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 130 ? -9.28242  -18.57650 0.69808   1.000 14.14392 ? 130 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 130 ? -7.86340  -18.43325 0.06304   1.000 15.67312 ? 130 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 130 ? -7.84933  -18.27209 -1.69316  1.000 18.40257 ? 130 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 130 ? -8.28798  -16.54004 -1.79292  1.000 10.74628 ? 130 MET   A CE  1 
ATOM   1007 N  N   . ARG   A 1 131 ? -9.92916  -21.73185 -0.85675  1.000 13.02680 ? 131 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 131 ? -9.62477  -23.14989 -0.74638  1.000 14.28712 ? 131 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 131 ? -8.18287  -23.31376 -0.29128  1.000 14.73322 ? 131 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 131 ? -7.37719  -22.38818 -0.43464  1.000 16.43042 ? 131 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 131 ? -9.84183  -23.86360 -2.07358  1.000 15.13195 ? 131 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 131 ? -11.24606 -23.77684 -2.65208  1.000 16.10218 ? 131 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 131 ? -12.30428 -24.20342 -1.65819  1.000 14.95221 ? 131 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 131 ? -11.92410 -25.46236 -1.04325  1.000 16.28757 ? 131 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 131 ? -12.57496 -26.02396 -0.03707  1.000 18.02981 ? 131 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 131 ? -13.68815 -25.48805 0.44583   1.000 17.39262 ? 131 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 131 ? -12.10922 -27.16146 0.48114   1.000 18.78156 ? 131 ARG   A NH2 1 
ATOM   1018 N  N   . PRO   A 1 132 ? -7.83754  -24.46269 0.30340   1.000 14.58110 ? 132 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 132 ? -6.42386  -24.72858 0.58355   1.000 15.49565 ? 132 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 132 ? -5.54618  -24.59000 -0.62736  1.000 17.16932 ? 132 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 132 ? -4.38362  -24.23097 -0.46361  1.000 15.08336 ? 132 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 132 ? -6.43900  -26.16887 1.11661   1.000 17.89707 ? 132 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 132 ? -7.74582  -26.27037 1.80063   1.000 18.71167 ? 132 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 132 ? -8.68733  -25.53398 0.86277   1.000 16.64386 ? 132 PRO   A CD  1 
ATOM   1025 N  N   . ASN   A 1 133 ? -6.04962  -24.81895 -1.84713  1.000 14.69433 ? 133 ASN   A N   1 
ATOM   1026 C  CA  . ASN   A 1 133 ? -5.19577  -24.65725 -3.01447  1.000 13.26365 ? 133 ASN   A CA  1 
ATOM   1027 C  C   . ASN   A 1 133 ? -5.25090  -23.25767 -3.59212  1.000 13.80633 ? 133 ASN   A C   1 
ATOM   1028 O  O   . ASN   A 1 133 ? -4.84706  -23.06528 -4.74834  1.000 14.91078 ? 133 ASN   A O   1 
ATOM   1029 C  CB  . ASN   A 1 133 ? -5.53752  -25.68419 -4.09258  1.000 15.89576 ? 133 ASN   A CB  1 
ATOM   1030 C  CG  . ASN   A 1 133 ? -6.94227  -25.50397 -4.63437  1.000 15.90665 ? 133 ASN   A CG  1 
ATOM   1031 O  OD1 . ASN   A 1 133 ? -7.64545  -24.56209 -4.26996  1.000 14.62932 ? 133 ASN   A OD1 1 
ATOM   1032 N  ND2 . ASN   A 1 133 ? -7.36446  -26.42800 -5.48956  1.000 19.10636 ? 133 ASN   A ND2 1 
ATOM   1033 N  N   . PHE   A 1 134 ? -5.76736  -22.29250 -2.82724  1.000 13.76665 ? 134 PHE   A N   1 
ATOM   1034 C  CA  . PHE   A 1 134 ? -5.77144  -20.87701 -3.17571  1.000 14.36335 ? 134 PHE   A CA  1 
ATOM   1035 C  C   . PHE   A 1 134 ? -6.65022  -20.55914 -4.36410  1.000 13.98900 ? 134 PHE   A C   1 
ATOM   1036 O  O   . PHE   A 1 134 ? -6.43151  -19.56140 -5.05521  1.000 16.35058 ? 134 PHE   A O   1 
ATOM   1037 C  CB  . PHE   A 1 134 ? -4.35410  -20.38123 -3.45065  1.000 12.68261 ? 134 PHE   A CB  1 
ATOM   1038 C  CG  . PHE   A 1 134 ? -3.52801  -20.24517 -2.23967  1.000 12.02625 ? 134 PHE   A CG  1 
ATOM   1039 C  CD1 . PHE   A 1 134 ? -3.69414  -19.16429 -1.41114  1.000 12.10520 ? 134 PHE   A CD1 1 
ATOM   1040 C  CD2 . PHE   A 1 134 ? -2.57751  -21.20019 -1.91802  1.000 17.50946 ? 134 PHE   A CD2 1 
ATOM   1041 C  CE1 . PHE   A 1 134 ? -2.89715  -19.01781 -0.27283  1.000 14.19799 ? 134 PHE   A CE1 1 
ATOM   1042 C  CE2 . PHE   A 1 134 ? -1.78824  -21.06559 -0.79303  1.000 19.28904 ? 134 PHE   A CE2 1 
ATOM   1043 C  CZ  . PHE   A 1 134 ? -1.97135  -19.97567 0.04374   1.000 16.45476 ? 134 PHE   A CZ  1 
ATOM   1044 N  N   . THR   A 1 135 ? -7.63371  -21.39456 -4.63903  1.000 15.20817 ? 135 THR   A N   1 
ATOM   1045 C  CA  . THR   A 1 135 ? -8.68573  -21.05175 -5.55768  1.000 14.20948 ? 135 THR   A CA  1 
ATOM   1046 C  C   . THR   A 1 135 ? -9.92324  -20.77290 -4.73520  1.000 12.88558 ? 135 THR   A C   1 
ATOM   1047 O  O   . THR   A 1 135 ? -9.98852  -21.05837 -3.54681  1.000 13.09824 ? 135 THR   A O   1 
ATOM   1048 C  CB  . THR   A 1 135 ? -8.93918  -22.19343 -6.55002  1.000 13.59889 ? 135 THR   A CB  1 
ATOM   1049 O  OG1 . THR   A 1 135 ? -9.36044  -23.35182 -5.82173  1.000 14.67391 ? 135 THR   A OG1 1 
ATOM   1050 C  CG2 . THR   A 1 135 ? -7.68390  -22.54256 -7.32516  1.000 13.34344 ? 135 THR   A CG2 1 
ATOM   1051 N  N   . ILE   A 1 136 ? -10.91336 -20.22719 -5.38235  1.000 13.03215 ? 136 ILE   A N   1 
ATOM   1052 C  CA  . ILE   A 1 136 ? -12.20337 -20.05587 -4.75200  1.000 15.30831 ? 136 ILE   A CA  1 
ATOM   1053 C  C   . ILE   A 1 136 ? -13.22604 -20.65659 -5.68739  1.000 15.62187 ? 136 ILE   A C   1 
ATOM   1054 O  O   . ILE   A 1 136 ? -13.05792 -20.61476 -6.90577  1.000 15.32653 ? 136 ILE   A O   1 
ATOM   1055 C  CB  . ILE   A 1 136 ? -12.51236 -18.57940 -4.44016  1.000 16.77627 ? 136 ILE   A CB  1 
ATOM   1056 C  CG1 . ILE   A 1 136 ? -12.78450 -17.78875 -5.71196  1.000 16.63045 ? 136 ILE   A CG1 1 
ATOM   1057 C  CG2 . ILE   A 1 136 ? -11.37695 -17.96709 -3.58590  1.000 13.55287 ? 136 ILE   A CG2 1 
ATOM   1058 C  CD1 . ILE   A 1 136 ? -13.46616 -16.47054 -5.47333  1.000 13.45766 ? 136 ILE   A CD1 1 
ATOM   1059 N  N   . LYS   A 1 137 ? -14.23204 -21.29884 -5.11763  1.000 14.59066 ? 137 LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 137 ? -15.30804 -21.87555 -5.91802  1.000 13.83954 ? 137 LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 137 ? -16.38611 -20.80103 -5.99900  1.000 16.09273 ? 137 LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 137 ? -17.31465 -20.74909 -5.19435  1.000 16.93551 ? 137 LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 137 ? -15.78905 -23.17347 -5.29092  1.000 16.90905 ? 137 LYS   A CB  1 
ATOM   1064 C  CG  . LYS   A 1 137 ? -14.70372 -24.23179 -5.16815  1.000 18.52353 ? 137 LYS   A CG  1 
ATOM   1065 C  CD  . LYS   A 1 137 ? -15.25879 -25.54151 -4.61444  1.000 24.33521 ? 137 LYS   A CD  1 
ATOM   1066 C  CE  . LYS   A 1 137 ? -14.21294 -26.67528 -4.66336  1.000 26.56536 ? 137 LYS   A CE  1 
ATOM   1067 N  NZ  . LYS   A 1 137 ? -14.31317 -27.55866 -5.86993  1.000 28.58554 ? 137 LYS   A NZ  1 
ATOM   1068 N  N   . GLY   A 1 138 ? -16.23136 -19.89318 -6.96255  1.000 16.43033 ? 138 GLY   A N   1 
ATOM   1069 C  CA  . GLY   A 1 138 ? -17.09011 -18.73954 -7.07442  1.000 16.93992 ? 138 GLY   A CA  1 
ATOM   1070 C  C   . GLY   A 1 138 ? -18.13597 -18.91468 -8.15340  1.000 17.69444 ? 138 GLY   A C   1 
ATOM   1071 O  O   . GLY   A 1 138 ? -18.38164 -20.00343 -8.67097  1.000 17.99587 ? 138 GLY   A O   1 
ATOM   1072 N  N   . SER   A 1 139 ? -18.76143 -17.80610 -8.49772  1.000 16.27459 ? 139 SER   A N   1 
ATOM   1073 C  CA  . SER   A 1 139 ? -19.66191 -17.78971 -9.63111  1.000 15.28096 ? 139 SER   A CA  1 
ATOM   1074 C  C   . SER   A 1 139 ? -19.34697 -16.50493 -10.36623 1.000 16.92805 ? 139 SER   A C   1 
ATOM   1075 O  O   . SER   A 1 139 ? -19.64594 -15.41399 -9.87600  1.000 15.87559 ? 139 SER   A O   1 
ATOM   1076 C  CB  . SER   A 1 139 ? -21.12039 -17.85285 -9.19898  1.000 17.47630 ? 139 SER   A CB  1 
ATOM   1077 O  OG  . SER   A 1 139 ? -21.94826 -17.58644 -10.30488 1.000 20.16488 ? 139 SER   A OG  1 
ATOM   1078 N  N   . PHE   A 1 140 ? -18.72969 -16.64538 -11.52608 1.000 17.09695 ? 140 PHE   A N   1 
ATOM   1079 C  CA  . PHE   A 1 140 ? -18.16203 -15.52548 -12.24872 1.000 20.25386 ? 140 PHE   A CA  1 
ATOM   1080 C  C   . PHE   A 1 140 ? -18.32601 -15.81275 -13.72640 1.000 23.17571 ? 140 PHE   A C   1 
ATOM   1081 O  O   . PHE   A 1 140 ? -17.98677 -16.90550 -14.18343 1.000 23.15236 ? 140 PHE   A O   1 
ATOM   1082 C  CB  . PHE   A 1 140 ? -16.67016 -15.33323 -11.92925 1.000 18.82192 ? 140 PHE   A CB  1 
ATOM   1083 C  CG  . PHE   A 1 140 ? -16.37076 -14.86360 -10.52604 1.000 16.98135 ? 140 PHE   A CG  1 
ATOM   1084 C  CD1 . PHE   A 1 140 ? -16.73930 -13.59312 -10.10028 1.000 17.34167 ? 140 PHE   A CD1 1 
ATOM   1085 C  CD2 . PHE   A 1 140 ? -15.64619 -15.66096 -9.65621  1.000 18.39937 ? 140 PHE   A CD2 1 
ATOM   1086 C  CE1 . PHE   A 1 140 ? -16.41599 -13.15215 -8.81767  1.000 16.56648 ? 140 PHE   A CE1 1 
ATOM   1087 C  CE2 . PHE   A 1 140 ? -15.32942 -15.22639 -8.37774  1.000 16.60349 ? 140 PHE   A CE2 1 
ATOM   1088 C  CZ  . PHE   A 1 140 ? -15.69786 -13.96771 -7.96495  1.000 15.90754 ? 140 PHE   A CZ  1 
ATOM   1089 N  N   . LEU   A 1 141 ? -18.84280 -14.84600 -14.46681 1.000 21.29179 ? 141 LEU   A N   1 
ATOM   1090 C  CA  . LEU   A 1 141 ? -18.89650 -14.95462 -15.91051 1.000 23.62199 ? 141 LEU   A CA  1 
ATOM   1091 C  C   . LEU   A 1 141 ? -17.95558 -13.93457 -16.51967 1.000 22.98766 ? 141 LEU   A C   1 
ATOM   1092 O  O   . LEU   A 1 141 ? -17.36478 -13.11547 -15.82152 1.000 23.40603 ? 141 LEU   A O   1 
ATOM   1093 C  CB  . LEU   A 1 141 ? -20.32168 -14.75166 -16.42563 1.000 21.55678 ? 141 LEU   A CB  1 
ATOM   1094 C  CG  . LEU   A 1 141 ? -21.37117 -15.67454 -15.80868 1.000 29.20171 ? 141 LEU   A CG  1 
ATOM   1095 C  CD1 . LEU   A 1 141 ? -22.74330 -15.10808 -16.06380 1.000 30.77489 ? 141 LEU   A CD1 1 
ATOM   1096 C  CD2 . LEU   A 1 141 ? -21.27213 -17.09150 -16.34902 1.000 27.55531 ? 141 LEU   A CD2 1 
ATOM   1097 N  N   . ASN   A 1 142 ? -17.81967 -13.99473 -17.83765 1.000 24.46735 ? 142 ASN   A N   1 
ATOM   1098 C  CA  . ASN   A 1 142 ? -16.98631 -13.02306 -18.51872 1.000 24.59247 ? 142 ASN   A CA  1 
ATOM   1099 C  C   . ASN   A 1 142 ? -17.43963 -11.62425 -18.12907 1.000 23.40836 ? 142 ASN   A C   1 
ATOM   1100 O  O   . ASN   A 1 142 ? -18.63795 -11.33128 -18.09202 1.000 25.42635 ? 142 ASN   A O   1 
ATOM   1101 C  CB  . ASN   A 1 142 ? -17.06276 -13.21451 -20.02986 1.000 23.60767 ? 142 ASN   A CB  1 
ATOM   1102 C  CG  . ASN   A 1 142 ? -15.96322 -12.47126 -20.75561 1.000 32.03586 ? 142 ASN   A CG  1 
ATOM   1103 O  OD1 . ASN   A 1 142 ? -15.19959 -11.71999 -20.13926 1.000 34.57500 ? 142 ASN   A OD1 1 
ATOM   1104 N  ND2 . ASN   A 1 142 ? -15.89672 -12.63844 -22.07452 1.000 33.47303 ? 142 ASN   A ND2 1 
ATOM   1105 N  N   . GLY   A 1 143 ? -16.48307 -10.78331 -17.78369 1.000 20.23873 ? 143 GLY   A N   1 
ATOM   1106 C  CA  . GLY   A 1 143 ? -16.76463 -9.43652  -17.35479 1.000 22.33401 ? 143 GLY   A CA  1 
ATOM   1107 C  C   . GLY   A 1 143 ? -16.79165 -9.24273  -15.85800 1.000 19.85503 ? 143 GLY   A C   1 
ATOM   1108 O  O   . GLY   A 1 143 ? -16.92230 -8.10075  -15.40537 1.000 18.32214 ? 143 GLY   A O   1 
ATOM   1109 N  N   . SER   A 1 144 ? -16.67722 -10.31917 -15.07747 1.000 16.27278 ? 144 SER   A N   1 
ATOM   1110 C  CA  . SER   A 1 144 ? -16.63127 -10.20013 -13.63085 1.000 18.68065 ? 144 SER   A CA  1 
ATOM   1111 C  C   . SER   A 1 144 ? -15.24358 -9.84589  -13.11125 1.000 15.26450 ? 144 SER   A C   1 
ATOM   1112 O  O   . SER   A 1 144 ? -15.10920 -9.57939  -11.91308 1.000 15.01918 ? 144 SER   A O   1 
ATOM   1113 C  CB  . SER   A 1 144 ? -17.07920 -11.51706 -12.97985 1.000 18.47683 ? 144 SER   A CB  1 
ATOM   1114 O  OG  . SER   A 1 144 ? -16.25426 -12.57060 -13.42469 1.000 19.71781 ? 144 SER   A OG  1 
ATOM   1115 N  N   . CYS   A 1 145 ? -14.20849 -9.85025  -13.96309 1.000 16.85366 ? 145 CYS   A N   1 
ATOM   1116 C  CA  . CYS   A 1 145 ? -12.88270 -9.44239  -13.49690 1.000 18.95881 ? 145 CYS   A CA  1 
ATOM   1117 C  C   . CYS   A 1 145 ? -12.98273 -8.12038  -12.75227 1.000 14.00626 ? 145 CYS   A C   1 
ATOM   1118 O  O   . CYS   A 1 145 ? -13.72433 -7.22304  -13.15080 1.000 16.94024 ? 145 CYS   A O   1 
ATOM   1119 C  CB  . CYS   A 1 145 ? -11.89417 -9.29177  -14.65952 1.000 20.49764 ? 145 CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A 1 145 ? -11.61085 -10.78625 -15.60524 1.000 31.08769 ? 145 CYS   A SG  1 
ATOM   1121 N  N   . GLY   A 1 146 ? -12.27444 -8.02561  -11.63779 1.000 14.00483 ? 146 GLY   A N   1 
ATOM   1122 C  CA  . GLY   A 1 146 ? -12.33091 -6.84024  -10.81748 1.000 13.86476 ? 146 GLY   A CA  1 
ATOM   1123 C  C   . GLY   A 1 146 ? -13.36170 -6.87434  -9.71645  1.000 14.31215 ? 146 GLY   A C   1 
ATOM   1124 O  O   . GLY   A 1 146 ? -13.32896 -5.99711  -8.83874  1.000 12.39843 ? 146 GLY   A O   1 
ATOM   1125 N  N   . SER   A 1 147 ? -14.30140 -7.82267  -9.75211  1.000 13.43520 ? 147 SER   A N   1 
ATOM   1126 C  CA  . SER   A 1 147 ? -15.18304 -7.99479  -8.60706  1.000 12.52771 ? 147 SER   A CA  1 
ATOM   1127 C  C   . SER   A 1 147 ? -14.31224 -8.29873  -7.39886  1.000 13.68133 ? 147 SER   A C   1 
ATOM   1128 O  O   . SER   A 1 147 ? -13.26969 -8.96383  -7.50832  1.000 11.65089 ? 147 SER   A O   1 
ATOM   1129 C  CB  . SER   A 1 147 ? -16.18264 -9.12720  -8.84386  1.000 10.63531 ? 147 SER   A CB  1 
ATOM   1130 O  OG  . SER   A 1 147 ? -16.86360 -8.95023  -10.08063 1.000 13.20561 ? 147 SER   A OG  1 
ATOM   1131 N  N   . VAL   A 1 148 ? -14.71491 -7.79120  -6.23823  1.000 11.52471 ? 148 VAL   A N   1 
ATOM   1132 C  CA  . VAL   A 1 148 ? -13.88521 -7.96985  -5.06548  1.000 11.13161 ? 148 VAL   A CA  1 
ATOM   1133 C  C   . VAL   A 1 148 ? -14.57440 -8.86164  -4.05314  1.000 11.96388 ? 148 VAL   A C   1 
ATOM   1134 O  O   . VAL   A 1 148 ? -15.81148 -9.01054  -4.02107  1.000 12.92254 ? 148 VAL   A O   1 
ATOM   1135 C  CB  . VAL   A 1 148 ? -13.47296 -6.63123  -4.41578  1.000 12.29367 ? 148 VAL   A CB  1 
ATOM   1136 C  CG1 . VAL   A 1 148 ? -12.63939 -5.82632  -5.42805  1.000 11.03239 ? 148 VAL   A CG1 1 
ATOM   1137 C  CG2 . VAL   A 1 148 ? -14.67500 -5.87606  -3.97391  1.000 11.83738 ? 148 VAL   A CG2 1 
ATOM   1138 N  N   . GLY   A 1 149 ? -13.72585 -9.46662  -3.22449  1.000 11.52156 ? 149 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 149 ? -14.12183 -10.22527 -2.05118  1.000 10.30762 ? 149 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 149 ? -13.76627 -9.42743  -0.81219  1.000 9.39181  ? 149 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 149 ? -12.77156 -8.69864  -0.78679  1.000 10.04036 ? 149 GLY   A O   1 
ATOM   1142 N  N   . PHE   A 1 150 ? -14.57094 -9.57695  0.23241   1.000 10.99755 ? 150 PHE   A N   1 
ATOM   1143 C  CA  . PHE   A 1 150 ? -14.37922 -8.72801  1.38675   1.000 11.23273 ? 150 PHE   A CA  1 
ATOM   1144 C  C   . PHE   A 1 150 ? -15.03346 -9.33502  2.61814   1.000 11.82516 ? 150 PHE   A C   1 
ATOM   1145 O  O   . PHE   A 1 150 ? -15.92805 -10.17198 2.52284   1.000 11.29631 ? 150 PHE   A O   1 
ATOM   1146 C  CB  . PHE   A 1 150 ? -14.97974 -7.35560  1.12874   1.000 12.78019 ? 150 PHE   A CB  1 
ATOM   1147 C  CG  . PHE   A 1 150 ? -16.45126 -7.40630  0.92034   1.000 12.95725 ? 150 PHE   A CG  1 
ATOM   1148 C  CD1 . PHE   A 1 150 ? -16.97819 -7.72777  -0.33980  1.000 12.65390 ? 150 PHE   A CD1 1 
ATOM   1149 C  CD2 . PHE   A 1 150 ? -17.31943 -7.19581  1.98162   1.000 12.61942 ? 150 PHE   A CD2 1 
ATOM   1150 C  CE1 . PHE   A 1 150 ? -18.34990 -7.80024  -0.52850  1.000 14.74135 ? 150 PHE   A CE1 1 
ATOM   1151 C  CE2 . PHE   A 1 150 ? -18.69092 -7.27478  1.80235   1.000 15.26121 ? 150 PHE   A CE2 1 
ATOM   1152 C  CZ  . PHE   A 1 150 ? -19.21150 -7.58739  0.54722   1.000 15.17106 ? 150 PHE   A CZ  1 
ATOM   1153 N  N   . ASN   A 1 151 ? -14.61261 -8.82760  3.77169   1.000 12.50488 ? 151 ASN   A N   1 
ATOM   1154 C  CA  . ASN   A 1 151 ? -15.27232 -9.02702  5.04953   1.000 16.53509 ? 151 ASN   A CA  1 
ATOM   1155 C  C   . ASN   A 1 151 ? -15.57679 -7.66131  5.62767   1.000 15.29574 ? 151 ASN   A C   1 
ATOM   1156 O  O   . ASN   A 1 151 ? -15.01234 -6.66158  5.20784   1.000 15.02075 ? 151 ASN   A O   1 
ATOM   1157 C  CB  . ASN   A 1 151 ? -14.39529 -9.81925  6.01304   1.000 14.83992 ? 151 ASN   A CB  1 
ATOM   1158 C  CG  . ASN   A 1 151 ? -14.34597 -11.28362 5.67141   1.000 16.61479 ? 151 ASN   A CG  1 
ATOM   1159 O  OD1 . ASN   A 1 151 ? -15.29587 -12.01040 5.94530   1.000 16.44667 ? 151 ASN   A OD1 1 
ATOM   1160 N  ND2 . ASN   A 1 151 ? -13.28050 -11.71360 5.01025   1.000 13.43869 ? 151 ASN   A ND2 1 
ATOM   1161 N  N   . ILE   A 1 152 ? -16.48713 -7.61448  6.59493   1.000 15.61243 ? 152 ILE   A N   1 
ATOM   1162 C  CA  . ILE   A 1 152 ? -16.84801 -6.36411  7.25392   1.000 18.63751 ? 152 ILE   A CA  1 
ATOM   1163 C  C   . ILE   A 1 152 ? -16.73127 -6.59648  8.73955   1.000 25.35503 ? 152 ILE   A C   1 
ATOM   1164 O  O   . ILE   A 1 152 ? -17.26365 -7.58465  9.25164   1.000 24.50203 ? 152 ILE   A O   1 
ATOM   1165 C  CB  . ILE   A 1 152 ? -18.27686 -5.89181  6.92171   1.000 21.98205 ? 152 ILE   A CB  1 
ATOM   1166 C  CG1 . ILE   A 1 152 ? -18.55294 -5.98929  5.42870   1.000 20.20659 ? 152 ILE   A CG1 1 
ATOM   1167 C  CG2 . ILE   A 1 152 ? -18.53727 -4.47989  7.49833   1.000 22.24141 ? 152 ILE   A CG2 1 
ATOM   1168 C  CD1 . ILE   A 1 152 ? -17.79347 -5.02101  4.62903   1.000 20.05717 ? 152 ILE   A CD1 1 
ATOM   1169 N  N   . ASP   A 1 153 ? -16.03639 -5.69694  9.42063   1.000 27.88660 ? 153 ASP   A N   1 
ATOM   1170 C  CA  . ASP   A 1 153 ? -15.80305 -5.77078  10.85611  1.000 32.18289 ? 153 ASP   A CA  1 
ATOM   1171 C  C   . ASP   A 1 153 ? -16.25860 -4.43469  11.42285  1.000 34.96226 ? 153 ASP   A C   1 
ATOM   1172 O  O   . ASP   A 1 153 ? -15.63283 -3.39978  11.16364  1.000 35.25990 ? 153 ASP   A O   1 
ATOM   1173 C  CB  . ASP   A 1 153 ? -14.33184 -6.04548  11.16120  1.000 33.37673 ? 153 ASP   A CB  1 
ATOM   1174 C  CG  . ASP   A 1 153 ? -14.09405 -6.36634  12.61660  1.000 43.56252 ? 153 ASP   A CG  1 
ATOM   1175 O  OD1 . ASP   A 1 153 ? -15.08060 -6.70865  13.30657  1.000 45.16807 ? 153 ASP   A OD1 1 
ATOM   1176 O  OD2 . ASP   A 1 153 ? -12.92623 -6.27596  13.06899  1.000 50.79312 ? 153 ASP   A OD2 1 
ATOM   1177 N  N   . TYR   A 1 154 ? -17.34856 -4.46770  12.18556  1.000 36.54415 ? 154 TYR   A N   1 
ATOM   1178 C  CA  . TYR   A 1 154 ? -18.15043 -3.28947  12.47692  1.000 42.76196 ? 154 TYR   A CA  1 
ATOM   1179 C  C   . TYR   A 1 154 ? -18.36906 -2.45908  11.21876  1.000 41.24152 ? 154 TYR   A C   1 
ATOM   1180 O  O   . TYR   A 1 154 ? -19.13542 -2.85952  10.33910  1.000 43.28708 ? 154 TYR   A O   1 
ATOM   1181 C  CB  . TYR   A 1 154 ? -17.53095 -2.44164  13.58597  1.000 45.41984 ? 154 TYR   A CB  1 
ATOM   1182 C  CG  . TYR   A 1 154 ? -18.52518 -1.41185  14.09062  1.000 53.15314 ? 154 TYR   A CG  1 
ATOM   1183 C  CD1 . TYR   A 1 154 ? -19.88639 -1.71083  14.14719  1.000 50.96657 ? 154 TYR   A CD1 1 
ATOM   1184 C  CD2 . TYR   A 1 154 ? -18.11300 -0.14570  14.50242  1.000 52.18408 ? 154 TYR   A CD2 1 
ATOM   1185 C  CE1 . TYR   A 1 154 ? -20.80849 -0.77628  14.59667  1.000 57.05370 ? 154 TYR   A CE1 1 
ATOM   1186 C  CE2 . TYR   A 1 154 ? -19.02783 0.79504   14.96129  1.000 54.68490 ? 154 TYR   A CE2 1 
ATOM   1187 C  CZ  . TYR   A 1 154 ? -20.37356 0.47699   15.00617  1.000 59.14959 ? 154 TYR   A CZ  1 
ATOM   1188 O  OH  . TYR   A 1 154 ? -21.28016 1.41433   15.46023  1.000 55.32144 ? 154 TYR   A OH  1 
ATOM   1189 N  N   . ASP   A 1 155 ? -17.71477 -1.30819  11.10956  1.000 36.64710 ? 155 ASP   A N   1 
ATOM   1190 C  CA  . ASP   A 1 155 ? -17.94719 -0.42080  9.97752   1.000 37.94683 ? 155 ASP   A CA  1 
ATOM   1191 C  C   . ASP   A 1 155 ? -16.83540 -0.46332  8.93149   1.000 31.19511 ? 155 ASP   A C   1 
ATOM   1192 O  O   . ASP   A 1 155 ? -16.88539 0.30347   7.96342   1.000 27.87373 ? 155 ASP   A O   1 
ATOM   1193 C  CB  . ASP   A 1 155 ? -18.14956 1.01481   10.48167  1.000 40.78930 ? 155 ASP   A CB  1 
ATOM   1194 C  CG  . ASP   A 1 155 ? -16.92314 1.55572   11.19036  1.000 45.35557 ? 155 ASP   A CG  1 
ATOM   1195 O  OD1 . ASP   A 1 155 ? -16.87453 2.77984   11.46291  1.000 45.28838 ? 155 ASP   A OD1 1 
ATOM   1196 O  OD2 . ASP   A 1 155 ? -16.01511 0.74248   11.48827  1.000 47.88173 ? 155 ASP   A OD2 1 
ATOM   1197 N  N   . CYS   A 1 156 ? -15.84950 -1.34263  9.08711   1.000 27.68387 ? 156 CYS   A N   1 
ATOM   1198 C  CA  . CYS   A 1 156 ? -14.65207 -1.32210  8.25795   1.000 24.31496 ? 156 CYS   A CA  1 
ATOM   1199 C  C   . CYS   A 1 156 ? -14.67332 -2.48936  7.28247   1.000 19.64169 ? 156 CYS   A C   1 
ATOM   1200 O  O   . CYS   A 1 156 ? -14.84681 -3.64206  7.68806   1.000 18.25066 ? 156 CYS   A O   1 
ATOM   1201 C  CB  . CYS   A 1 156 ? -13.39916 -1.38086  9.12350   1.000 26.00232 ? 156 CYS   A CB  1 
ATOM   1202 S  SG  . CYS   A 1 156 ? -11.90753 -1.65413  8.17703   1.000 24.48634 ? 156 CYS   A SG  1 
ATOM   1203 N  N   . VAL   A 1 157 ? -14.50451 -2.18687  5.99961   1.000 16.03494 ? 157 VAL   A N   1 
ATOM   1204 C  CA  . VAL   A 1 157 ? -14.48485 -3.19898  4.95834   1.000 12.10942 ? 157 VAL   A CA  1 
ATOM   1205 C  C   . VAL   A 1 157 ? -13.05636 -3.67452  4.77542   1.000 16.41376 ? 157 VAL   A C   1 
ATOM   1206 O  O   . VAL   A 1 157 ? -12.19027 -2.88762  4.38966   1.000 13.34231 ? 157 VAL   A O   1 
ATOM   1207 C  CB  . VAL   A 1 157 ? -15.01888 -2.64177  3.63611   1.000 14.76945 ? 157 VAL   A CB  1 
ATOM   1208 C  CG1 . VAL   A 1 157 ? -15.03387 -3.73753  2.60716   1.000 12.74910 ? 157 VAL   A CG1 1 
ATOM   1209 C  CG2 . VAL   A 1 157 ? -16.41208 -1.99569  3.84480   1.000 16.42065 ? 157 VAL   A CG2 1 
ATOM   1210 N  N   . SER   A 1 158 ? -12.80894 -4.95478  5.01809   1.000 15.89308 ? 158 SER   A N   1 
ATOM   1211 C  CA  . SER   A 1 158 ? -11.48647 -5.53622  4.76434   1.000 12.97656 ? 158 SER   A CA  1 
ATOM   1212 C  C   . SER   A 1 158 ? -11.55367 -6.20844  3.40596   1.000 12.41518 ? 158 SER   A C   1 
ATOM   1213 O  O   . SER   A 1 158 ? -12.14281 -7.27955  3.27025   1.000 12.68035 ? 158 SER   A O   1 
ATOM   1214 C  CB  . SER   A 1 158 ? -11.11241 -6.53999  5.84269   1.000 15.19185 ? 158 SER   A CB  1 
ATOM   1215 O  OG  . SER   A 1 158 ? -10.84467 -5.85047  7.04274   1.000 19.37333 ? 158 SER   A OG  1 
ATOM   1216 N  N   . PHE   A 1 159 ? -10.97679 -5.56992  2.39769   1.000 11.58368 ? 159 PHE   A N   1 
ATOM   1217 C  CA  . PHE   A 1 159 ? -10.96663 -6.14125  1.06597   1.000 12.19870 ? 159 PHE   A CA  1 
ATOM   1218 C  C   . PHE   A 1 159 ? -9.89227  -7.21092  1.03254   1.000 10.66852 ? 159 PHE   A C   1 
ATOM   1219 O  O   . PHE   A 1 159 ? -8.75432  -6.96083  1.43003   1.000 11.26642 ? 159 PHE   A O   1 
ATOM   1220 C  CB  . PHE   A 1 159 ? -10.67079 -5.06715  0.02778   1.000 12.51275 ? 159 PHE   A CB  1 
ATOM   1221 C  CG  . PHE   A 1 159 ? -11.77779 -4.08527  -0.14206  1.000 11.42720 ? 159 PHE   A CG  1 
ATOM   1222 C  CD1 . PHE   A 1 159 ? -12.91015 -4.44924  -0.84450  1.000 10.00865 ? 159 PHE   A CD1 1 
ATOM   1223 C  CD2 . PHE   A 1 159 ? -11.69588 -2.81033  0.41158   1.000 13.99345 ? 159 PHE   A CD2 1 
ATOM   1224 C  CE1 . PHE   A 1 159 ? -13.92828 -3.55635  -1.04115  1.000 10.99592 ? 159 PHE   A CE1 1 
ATOM   1225 C  CE2 . PHE   A 1 159 ? -12.72934 -1.91523  0.23876   1.000 10.92275 ? 159 PHE   A CE2 1 
ATOM   1226 C  CZ  . PHE   A 1 159 ? -13.84798 -2.29991  -0.49179  1.000 14.09151 ? 159 PHE   A CZ  1 
ATOM   1227 N  N   . CYS   A 1 160 ? -10.23463 -8.39800  0.56457   1.000 11.47520 ? 160 CYS   A N   1 
ATOM   1228 C  CA  . CYS   A 1 160 ? -9.23925  -9.43919  0.51835   1.000 12.17628 ? 160 CYS   A CA  1 
ATOM   1229 C  C   . CYS   A 1 160 ? -9.02725  -10.04564 -0.85447  1.000 12.56829 ? 160 CYS   A C   1 
ATOM   1230 O  O   . CYS   A 1 160 ? -8.00721  -10.70548 -1.04353  1.000 13.51662 ? 160 CYS   A O   1 
ATOM   1231 C  CB  . CYS   A 1 160 ? -9.57145  -10.54961 1.52391   1.000 9.76633  ? 160 CYS   A CB  1 
ATOM   1232 S  SG  . CYS   A 1 160 ? -11.18413 -11.27827 1.29092   1.000 12.25809 ? 160 CYS   A SG  1 
ATOM   1233 N  N   . TYR   A 1 161 ? -9.90627  -9.81091  -1.82572  1.000 8.19689  ? 161 TYR   A N   1 
ATOM   1234 C  CA  . TYR   A 1 161 ? -9.84196  -10.59725 -3.05399  1.000 10.65744 ? 161 TYR   A CA  1 
ATOM   1235 C  C   . TYR   A 1 161 ? -10.22658 -9.72426  -4.22518  1.000 11.16512 ? 161 TYR   A C   1 
ATOM   1236 O  O   . TYR   A 1 161 ? -11.22184 -8.99415  -4.14353  1.000 11.14512 ? 161 TYR   A O   1 
ATOM   1237 C  CB  . TYR   A 1 161 ? -10.77685 -11.80818 -2.97723  1.000 10.41254 ? 161 TYR   A CB  1 
ATOM   1238 C  CG  . TYR   A 1 161 ? -10.80257 -12.62415 -4.24888  1.000 10.26390 ? 161 TYR   A CG  1 
ATOM   1239 C  CD1 . TYR   A 1 161 ? -9.76632  -13.50145 -4.52472  1.000 12.02552 ? 161 TYR   A CD1 1 
ATOM   1240 C  CD2 . TYR   A 1 161 ? -11.87260 -12.55634 -5.14138  1.000 9.74119  ? 161 TYR   A CD2 1 
ATOM   1241 C  CE1 . TYR   A 1 161 ? -9.76666  -14.25971 -5.65245  1.000 10.98813 ? 161 TYR   A CE1 1 
ATOM   1242 C  CE2 . TYR   A 1 161 ? -11.87983 -13.32087 -6.30600  1.000 9.75877  ? 161 TYR   A CE2 1 
ATOM   1243 C  CZ  . TYR   A 1 161 ? -10.80455 -14.15604 -6.54838  1.000 11.19250 ? 161 TYR   A CZ  1 
ATOM   1244 O  OH  . TYR   A 1 161 ? -10.74945 -14.94079 -7.67164  1.000 11.99210 ? 161 TYR   A OH  1 
ATOM   1245 N  N   . MET   A 1 162 ? -9.45855  -9.76431  -5.29711  1.000 9.27743  ? 162 MET   A N   1 
ATOM   1246 C  CA  . MET   A 1 162 ? -10.01507 -9.21532  -6.51061  1.000 10.02031 ? 162 MET   A CA  1 
ATOM   1247 C  C   . MET   A 1 162 ? -9.94003  -10.30883 -7.55480  1.000 11.15129 ? 162 MET   A C   1 
ATOM   1248 O  O   . MET   A 1 162 ? -8.92128  -11.00246 -7.66349  1.000 9.56256  ? 162 MET   A O   1 
ATOM   1249 C  CB  . MET   A 1 162 ? -9.31527  -7.91491  -6.94267  1.000 14.89001 ? 162 MET   A CB  1 
ATOM   1250 C  CG  . MET   A 1 162 ? -9.67556  -7.45474  -8.37221  1.000 12.46623 ? 162 MET   A CG  1 
ATOM   1251 S  SD  . MET   A 1 162 ? -8.80227  -5.91394  -8.72880  1.000 17.85889 ? 162 MET   A SD  1 
ATOM   1252 C  CE  . MET   A 1 162 ? -9.75699  -4.72754  -7.78527  1.000 19.30648 ? 162 MET   A CE  1 
ATOM   1253 N  N   . HIS   A 1 163 ? -11.03849 -10.48918 -8.27676  1.000 11.66537 ? 163 HIS   A N   1 
ATOM   1254 C  CA  . HIS   A 1 163 ? -11.16232 -11.60420 -9.19823  1.000 12.27681 ? 163 HIS   A CA  1 
ATOM   1255 C  C   . HIS   A 1 163 ? -10.40327 -11.32942 -10.48573 1.000 11.22571 ? 163 HIS   A C   1 
ATOM   1256 O  O   . HIS   A 1 163 ? -10.55277 -10.26685 -11.08189 1.000 10.46984 ? 163 HIS   A O   1 
ATOM   1257 C  CB  . HIS   A 1 163 ? -12.61818 -11.86336 -9.54434  1.000 13.86849 ? 163 HIS   A CB  1 
ATOM   1258 C  CG  . HIS   A 1 163 ? -12.77160 -13.06999 -10.39769 1.000 12.48657 ? 163 HIS   A CG  1 
ATOM   1259 N  ND1 . HIS   A 1 163 ? -12.21411 -14.27972 -10.04949 1.000 14.17269 ? 163 HIS   A ND1 1 
ATOM   1260 C  CD2 . HIS   A 1 163 ? -13.32904 -13.24409 -11.61068 1.000 15.23926 ? 163 HIS   A CD2 1 
ATOM   1261 C  CE1 . HIS   A 1 163 ? -12.45414 -15.15867 -10.99978 1.000 13.77975 ? 163 HIS   A CE1 1 
ATOM   1262 N  NE2 . HIS   A 1 163 ? -13.14601 -14.56035 -11.94773 1.000 15.75679 ? 163 HIS   A NE2 1 
ATOM   1263 N  N   . HIS   A 1 164 ? -9.62425  -12.30588 -10.92927 1.000 11.75049 ? 164 HIS   A N   1 
ATOM   1264 C  CA  . HIS   A 1 164 ? -8.88772  -12.14648 -12.17135 1.000 13.29555 ? 164 HIS   A CA  1 
ATOM   1265 C  C   . HIS   A 1 164 ? -9.27282  -13.13815 -13.24631 1.000 15.63870 ? 164 HIS   A C   1 
ATOM   1266 O  O   . HIS   A 1 164 ? -9.35084  -12.75484 -14.41313 1.000 17.01984 ? 164 HIS   A O   1 
ATOM   1267 C  CB  . HIS   A 1 164 ? -7.38399  -12.25710 -11.90525 1.000 10.76167 ? 164 HIS   A CB  1 
ATOM   1268 C  CG  . HIS   A 1 164 ? -6.80009  -11.02800 -11.28150 1.000 12.59327 ? 164 HIS   A CG  1 
ATOM   1269 N  ND1 . HIS   A 1 164 ? -5.85166  -10.25438 -11.91141 1.000 12.31092 ? 164 HIS   A ND1 1 
ATOM   1270 C  CD2 . HIS   A 1 164 ? -7.01828  -10.44629 -10.07912 1.000 14.29425 ? 164 HIS   A CD2 1 
ATOM   1271 C  CE1 . HIS   A 1 164 ? -5.52021  -9.24049  -11.13299 1.000 11.06478 ? 164 HIS   A CE1 1 
ATOM   1272 N  NE2 . HIS   A 1 164 ? -6.19533  -9.34567  -10.00424 1.000 12.05639 ? 164 HIS   A NE2 1 
ATOM   1273 N  N   . MET   A 1 165 ? -9.54919  -14.39062 -12.90511 1.000 16.05446 ? 165 MET   A N   1 
ATOM   1274 C  CA  . MET   A 1 165 ? -9.62974  -15.36040 -13.98663 1.000 17.84357 ? 165 MET   A CA  1 
ATOM   1275 C  C   . MET   A 1 165 ? -10.27912 -16.65039 -13.51597 1.000 17.53119 ? 165 MET   A C   1 
ATOM   1276 O  O   . MET   A 1 165 ? -10.36128 -16.92751 -12.32029 1.000 13.59702 ? 165 MET   A O   1 
ATOM   1277 C  CB  . MET   A 1 165 ? -8.23261  -15.59394 -14.52321 1.000 19.01626 ? 165 MET   A CB  1 
ATOM   1278 C  CG  . MET   A 1 165 ? -7.38128  -16.21700 -13.46661 1.000 19.39846 ? 165 MET   A CG  1 
ATOM   1279 S  SD  . MET   A 1 165 ? -5.70788  -16.38209 -14.07029 1.000 28.14511 ? 165 MET   A SD  1 
ATOM   1280 C  CE  . MET   A 1 165 ? -5.25991  -17.86652 -13.21211 1.000 23.83950 ? 165 MET   A CE  1 
ATOM   1281 N  N   . GLU   A 1 166 ? -10.73661 -17.44111 -14.47753 1.000 16.53797 ? 166 GLU   A N   1 
ATOM   1282 C  CA  . GLU   A 1 166 ? -11.28802 -18.75440 -14.18574 1.000 17.64879 ? 166 GLU   A CA  1 
ATOM   1283 C  C   . GLU   A 1 166 ? -10.31705 -19.81935 -14.66309 1.000 18.87463 ? 166 GLU   A C   1 
ATOM   1284 O  O   . GLU   A 1 166 ? -9.77989  -19.72956 -15.76956 1.000 18.74105 ? 166 GLU   A O   1 
ATOM   1285 C  CB  . GLU   A 1 166 ? -12.65607 -18.94414 -14.83526 1.000 18.54917 ? 166 GLU   A CB  1 
ATOM   1286 C  CG  . GLU   A 1 166 ? -13.21838 -20.35413 -14.64617 1.000 23.04313 ? 166 GLU   A CG  1 
ATOM   1287 C  CD  . GLU   A 1 166 ? -14.68324 -20.44781 -15.03374 1.000 25.55236 ? 166 GLU   A CD  1 
ATOM   1288 O  OE1 . GLU   A 1 166 ? -15.48047 -19.60324 -14.58136 1.000 25.45971 ? 166 GLU   A OE1 1 
ATOM   1289 O  OE2 . GLU   A 1 166 ? -15.02655 -21.34264 -15.83489 1.000 26.97446 ? 166 GLU   A OE2 1 
ATOM   1290 N  N   . LEU   A 1 167 ? -10.07549 -20.78663 -13.83117 1.000 19.79024 ? 167 LEU   A N   1 
ATOM   1291 C  CA  . LEU   A 1 167 ? -9.19052  -21.88674 -14.18304 1.000 20.38508 ? 167 LEU   A CA  1 
ATOM   1292 C  C   . LEU   A 1 167 ? -9.96944  -22.97226 -14.90871 1.000 22.58188 ? 167 LEU   A C   1 
ATOM   1293 O  O   . LEU   A 1 167 ? -11.20200 -23.00111 -14.85367 1.000 26.28301 ? 167 LEU   A O   1 
ATOM   1294 C  CB  . LEU   A 1 167 ? -8.54450  -22.44484 -12.91907 1.000 21.40015 ? 167 LEU   A CB  1 
ATOM   1295 C  CG  . LEU   A 1 167 ? -7.58315  -21.47639 -12.23430 1.000 18.74488 ? 167 LEU   A CG  1 
ATOM   1296 C  CD1 . LEU   A 1 167 ? -7.20038  -22.00106 -10.86999 1.000 19.68166 ? 167 LEU   A CD1 1 
ATOM   1297 C  CD2 . LEU   A 1 167 ? -6.35149  -21.31531 -13.09143 1.000 20.49851 ? 167 LEU   A CD2 1 
ATOM   1298 N  N   . PRO   A 1 168 ? -9.27851  -23.89596 -15.58772 1.000 24.85318 ? 168 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 168 ? -9.98731  -24.86904 -16.43521 1.000 23.76272 ? 168 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 168 ? -10.98125 -25.75341 -15.69849 1.000 25.57073 ? 168 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 168 ? -11.89900 -26.27748 -16.34024 1.000 30.07848 ? 168 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 168 ? -8.85130  -25.70178 -17.04027 1.000 22.61592 ? 168 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 168 ? -7.65006  -24.80346 -16.99147 1.000 26.27090 ? 168 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 168 ? -7.81302  -24.01135 -15.72898 1.000 23.94267 ? 168 PRO   A CD  1 
ATOM   1305 N  N   . THR   A 1 169 ? -10.84920 -25.95771 -14.39382 1.000 22.20878 ? 169 THR   A N   1 
ATOM   1306 C  CA  . THR   A 1 169 ? -11.86001 -26.73794 -13.69331 1.000 24.04236 ? 169 THR   A CA  1 
ATOM   1307 C  C   . THR   A 1 169 ? -13.06387 -25.89819 -13.28038 1.000 24.19630 ? 169 THR   A C   1 
ATOM   1308 O  O   . THR   A 1 169 ? -13.92676 -26.39544 -12.55669 1.000 25.58572 ? 169 THR   A O   1 
ATOM   1309 C  CB  . THR   A 1 169 ? -11.26106 -27.41560 -12.46162 1.000 25.33485 ? 169 THR   A CB  1 
ATOM   1310 O  OG1 . THR   A 1 169 ? -10.61130 -26.42383 -11.65771 1.000 26.92518 ? 169 THR   A OG1 1 
ATOM   1311 C  CG2 . THR   A 1 169 ? -10.26512 -28.49841 -12.87636 1.000 23.25845 ? 169 THR   A CG2 1 
ATOM   1312 N  N   . GLY   A 1 170 ? -13.13914 -24.64108 -13.71124 1.000 24.51327 ? 170 GLY   A N   1 
ATOM   1313 C  CA  . GLY   A 1 170 ? -14.24709 -23.79522 -13.31808 1.000 22.65969 ? 170 GLY   A CA  1 
ATOM   1314 C  C   . GLY   A 1 170 ? -14.09329 -23.10517 -11.98154 1.000 22.82638 ? 170 GLY   A C   1 
ATOM   1315 O  O   . GLY   A 1 170 ? -15.04870 -22.46077 -11.52795 1.000 21.93009 ? 170 GLY   A O   1 
ATOM   1316 N  N   . VAL   A 1 171 ? -12.93635 -23.20805 -11.33700 1.000 18.00985 ? 171 VAL   A N   1 
ATOM   1317 C  CA  . VAL   A 1 171 ? -12.67566 -22.46741 -10.12138 1.000 17.16805 ? 171 VAL   A CA  1 
ATOM   1318 C  C   . VAL   A 1 171 ? -11.95049 -21.17512 -10.46705 1.000 14.93484 ? 171 VAL   A C   1 
ATOM   1319 O  O   . VAL   A 1 171 ? -11.50751 -20.95298 -11.59213 1.000 16.18081 ? 171 VAL   A O   1 
ATOM   1320 C  CB  . VAL   A 1 171 ? -11.88902 -23.29828 -9.07406  1.000 17.67695 ? 171 VAL   A CB  1 
ATOM   1321 C  CG1 . VAL   A 1 171 ? -12.65927 -24.56776 -8.70125  1.000 19.53291 ? 171 VAL   A CG1 1 
ATOM   1322 C  CG2 . VAL   A 1 171 ? -10.48100 -23.61682 -9.56402  1.000 17.12750 ? 171 VAL   A CG2 1 
ATOM   1323 N  N   . HIS   A 1 172 ? -11.81894 -20.30946 -9.48619  1.000 12.60974 ? 172 HIS   A N   1 
ATOM   1324 C  CA  . HIS   A 1 172 ? -11.48757 -18.92886 -9.75033  1.000 13.34550 ? 172 HIS   A CA  1 
ATOM   1325 C  C   . HIS   A 1 172 ? -10.22447 -18.57485 -9.00167  1.000 13.44564 ? 172 HIS   A C   1 
ATOM   1326 O  O   . HIS   A 1 172 ? -9.97583  -19.07855 -7.91310  1.000 12.53225 ? 172 HIS   A O   1 
ATOM   1327 C  CB  . HIS   A 1 172 ? -12.67657 -18.05150 -9.39376  1.000 14.51672 ? 172 HIS   A CB  1 
ATOM   1328 C  CG  . HIS   A 1 172 ? -13.88911 -18.41586 -10.18937 1.000 14.38949 ? 172 HIS   A CG  1 
ATOM   1329 N  ND1 . HIS   A 1 172 ? -14.95097 -19.11039 -9.65655  1.000 14.54379 ? 172 HIS   A ND1 1 
ATOM   1330 C  CD2 . HIS   A 1 172 ? -14.14851 -18.29023 -11.51340 1.000 17.21578 ? 172 HIS   A CD2 1 
ATOM   1331 C  CE1 . HIS   A 1 172 ? -15.84298 -19.34374 -10.60284 1.000 16.89484 ? 172 HIS   A CE1 1 
ATOM   1332 N  NE2 . HIS   A 1 172 ? -15.37819 -18.86180 -11.74157 1.000 14.86519 ? 172 HIS   A NE2 1 
ATOM   1333 N  N   . ALA   A 1 173 ? -9.41856  -17.76406 -9.64249  1.000 13.21177 ? 173 ALA   A N   1 
ATOM   1334 C  CA  . ALA   A 1 173 ? -8.15184  -17.33192 -9.10648  1.000 10.05073 ? 173 ALA   A CA  1 
ATOM   1335 C  C   . ALA   A 1 173 ? -8.11135  -15.81375 -9.13698  1.000 10.98612 ? 173 ALA   A C   1 
ATOM   1336 O  O   . ALA   A 1 173 ? -8.66125  -15.18153 -10.03386 1.000 13.22922 ? 173 ALA   A O   1 
ATOM   1337 C  CB  . ALA   A 1 173 ? -7.01064  -17.96302 -9.89991  1.000 14.37470 ? 173 ALA   A CB  1 
ATOM   1338 N  N   . GLY   A 1 174 ? -7.47061  -15.22651 -8.13687  1.000 12.24709 ? 174 GLY   A N   1 
ATOM   1339 C  CA  . GLY   A 1 174 ? -7.40824  -13.78779 -8.10636  1.000 9.70183  ? 174 GLY   A CA  1 
ATOM   1340 C  C   . GLY   A 1 174 ? -6.30908  -13.33847 -7.18794  1.000 10.56112 ? 174 GLY   A C   1 
ATOM   1341 O  O   . GLY   A 1 174 ? -5.52096  -14.14640 -6.68800  1.000 9.78600  ? 174 GLY   A O   1 
ATOM   1342 N  N   . THR   A 1 175 ? -6.31965  -12.04724 -6.89785  1.000 9.37978  ? 175 THR   A N   1 
ATOM   1343 C  CA  . THR   A 1 175 ? -5.26394  -11.45259 -6.10660  1.000 10.21656 ? 175 THR   A CA  1 
ATOM   1344 C  C   . THR   A 1 175 ? -5.85082  -10.88230 -4.82681  1.000 10.50860 ? 175 THR   A C   1 
ATOM   1345 O  O   . THR   A 1 175 ? -7.06890  -10.71070 -4.69566  1.000 9.11941  ? 175 THR   A O   1 
ATOM   1346 C  CB  . THR   A 1 175 ? -4.53990  -10.34799 -6.89890  1.000 12.19687 ? 175 THR   A CB  1 
ATOM   1347 O  OG1 . THR   A 1 175 ? -5.44080  -9.25650  -7.16104  1.000 10.78049 ? 175 THR   A OG1 1 
ATOM   1348 C  CG2 . THR   A 1 175 ? -3.98464  -10.90204 -8.21491  1.000 10.69190 ? 175 THR   A CG2 1 
ATOM   1349 N  N   . ASP   A 1 176 ? -4.96646  -10.57524 -3.88781  1.000 11.39994 ? 176 ASP   A N   1 
ATOM   1350 C  CA  . ASP   A 1 176 ? -5.35139  -9.62477  -2.85872  1.000 10.36967 ? 176 ASP   A CA  1 
ATOM   1351 C  C   . ASP   A 1 176 ? -5.37454  -8.22905  -3.49592  1.000 9.69795  ? 176 ASP   A C   1 
ATOM   1352 O  O   . ASP   A 1 176 ? -5.12196  -8.06504  -4.68968  1.000 8.94900  ? 176 ASP   A O   1 
ATOM   1353 C  CB  . ASP   A 1 176 ? -4.42719  -9.73216  -1.64470  1.000 13.23703 ? 176 ASP   A CB  1 
ATOM   1354 C  CG  . ASP   A 1 176 ? -2.96748  -9.41487  -1.94582  1.000 15.12469 ? 176 ASP   A CG  1 
ATOM   1355 O  OD1 . ASP   A 1 176 ? -2.65740  -8.63199  -2.87684  1.000 12.66175 ? 176 ASP   A OD1 1 
ATOM   1356 O  OD2 . ASP   A 1 176 ? -2.10534  -9.90966  -1.17413  1.000 15.04081 ? 176 ASP   A OD2 1 
ATOM   1357 N  N   . LEU   A 1 177 ? -5.71451  -7.21785  -2.71090  1.000 11.80786 ? 177 LEU   A N   1 
ATOM   1358 C  CA  . LEU   A 1 177 ? -5.85545  -5.88786  -3.30449  1.000 12.40169 ? 177 LEU   A CA  1 
ATOM   1359 C  C   . LEU   A 1 177 ? -4.52192  -5.17825  -3.43478  1.000 17.29809 ? 177 LEU   A C   1 
ATOM   1360 O  O   . LEU   A 1 177 ? -4.49458  -4.01782  -3.86113  1.000 16.55041 ? 177 LEU   A O   1 
ATOM   1361 C  CB  . LEU   A 1 177 ? -6.83685  -5.03640  -2.48699  1.000 11.10904 ? 177 LEU   A CB  1 
ATOM   1362 C  CG  . LEU   A 1 177 ? -8.30836  -5.13374  -2.92115  1.000 13.56558 ? 177 LEU   A CG  1 
ATOM   1363 C  CD1 . LEU   A 1 177 ? -8.49399  -4.53347  -4.29419  1.000 10.01899 ? 177 LEU   A CD1 1 
ATOM   1364 C  CD2 . LEU   A 1 177 ? -8.80535  -6.59427  -2.92928  1.000 13.09955 ? 177 LEU   A CD2 1 
ATOM   1365 N  N   . GLU   A 1 178 ? -3.42155  -5.81785  -3.04140  1.000 13.21824 ? 178 GLU   A N   1 
ATOM   1366 C  CA  . GLU   A 1 178 ? -2.11877  -5.30762  -3.45196  1.000 15.90996 ? 178 GLU   A CA  1 
ATOM   1367 C  C   . GLU   A 1 178 ? -1.63967  -5.93740  -4.74714  1.000 12.66244 ? 178 GLU   A C   1 
ATOM   1368 O  O   . GLU   A 1 178 ? -0.52471  -5.65239  -5.18401  1.000 16.29767 ? 178 GLU   A O   1 
ATOM   1369 C  CB  . GLU   A 1 178 ? -1.08228  -5.50790  -2.34866  1.000 16.34028 ? 178 GLU   A CB  1 
ATOM   1370 C  CG  . GLU   A 1 178 ? -1.66295  -5.26466  -0.99210  1.000 19.79246 ? 178 GLU   A CG  1 
ATOM   1371 C  CD  . GLU   A 1 178 ? -1.58261  -3.81702  -0.56429  1.000 23.59456 ? 178 GLU   A CD  1 
ATOM   1372 O  OE1 . GLU   A 1 178 ? -1.34869  -2.93061  -1.42818  1.000 23.61811 ? 178 GLU   A OE1 1 
ATOM   1373 O  OE2 . GLU   A 1 178 ? -1.78476  -3.55582  0.65565   1.000 29.76481 ? 178 GLU   A OE2 1 
ATOM   1374 N  N   . GLY   A 1 179 ? -2.46126  -6.76694  -5.37565  1.000 14.32214 ? 179 GLY   A N   1 
ATOM   1375 C  CA  . GLY   A 1 179 ? -2.12043  -7.31531  -6.66470  1.000 13.24874 ? 179 GLY   A CA  1 
ATOM   1376 C  C   . GLY   A 1 179 ? -1.36382  -8.61728  -6.60106  1.000 12.98753 ? 179 GLY   A C   1 
ATOM   1377 O  O   . GLY   A 1 179 ? -0.90153  -9.09565  -7.63844  1.000 12.03009 ? 179 GLY   A O   1 
ATOM   1378 N  N   . ASN   A 1 180 ? -1.25017  -9.22047  -5.42673  1.000 9.96215  ? 180 ASN   A N   1 
ATOM   1379 C  CA  . ASN   A 1 180 ? -0.48535  -10.44325 -5.27907  1.000 12.55129 ? 180 ASN   A CA  1 
ATOM   1380 C  C   . ASN   A 1 180 ? -1.43735  -11.60592 -5.37723  1.000 9.86550  ? 180 ASN   A C   1 
ATOM   1381 O  O   . ASN   A 1 180 ? -2.41946  -11.66510 -4.64617  1.000 9.02453  ? 180 ASN   A O   1 
ATOM   1382 C  CB  . ASN   A 1 180 ? 0.28985   -10.41852 -3.96359  1.000 10.87249 ? 180 ASN   A CB  1 
ATOM   1383 C  CG  . ASN   A 1 180 ? 1.20504   -9.23879  -3.92069  1.000 12.61016 ? 180 ASN   A CG  1 
ATOM   1384 O  OD1 . ASN   A 1 180 ? 2.06901   -9.11028  -4.77027  1.000 13.55859 ? 180 ASN   A OD1 1 
ATOM   1385 N  ND2 . ASN   A 1 180 ? 0.98422   -8.33042  -2.97339  1.000 16.39735 ? 180 ASN   A ND2 1 
ATOM   1386 N  N   . PHE   A 1 181 ? -1.18959  -12.47860 -6.34674  1.000 12.31192 ? 181 PHE   A N   1 
ATOM   1387 C  CA  . PHE   A 1 181 ? -2.08485  -13.58737 -6.55261  1.000 11.24128 ? 181 PHE   A CA  1 
ATOM   1388 C  C   . PHE   A 1 181 ? -2.16190  -14.46430 -5.32396  1.000 11.47586 ? 181 PHE   A C   1 
ATOM   1389 O  O   . PHE   A 1 181 ? -1.16946  -14.68729 -4.62698  1.000 9.50185  ? 181 PHE   A O   1 
ATOM   1390 C  CB  . PHE   A 1 181 ? -1.64110  -14.43301 -7.74070  1.000 13.98284 ? 181 PHE   A CB  1 
ATOM   1391 C  CG  . PHE   A 1 181 ? -2.43009  -14.16470 -8.94814  1.000 14.21275 ? 181 PHE   A CG  1 
ATOM   1392 C  CD1 . PHE   A 1 181 ? -3.68375  -14.74989 -9.12007  1.000 13.48234 ? 181 PHE   A CD1 1 
ATOM   1393 C  CD2 . PHE   A 1 181 ? -1.95688  -13.28067 -9.90325  1.000 13.69011 ? 181 PHE   A CD2 1 
ATOM   1394 C  CE1 . PHE   A 1 181 ? -4.43508  -14.46240 -10.23768 1.000 11.79856 ? 181 PHE   A CE1 1 
ATOM   1395 C  CE2 . PHE   A 1 181 ? -2.68568  -13.00192 -11.01904 1.000 15.53286 ? 181 PHE   A CE2 1 
ATOM   1396 C  CZ  . PHE   A 1 181 ? -3.93128  -13.58365 -11.19329 1.000 16.71197 ? 181 PHE   A CZ  1 
ATOM   1397 N  N   . TYR   A 1 182 ? -3.35567  -14.96256 -5.08465  1.000 9.54453  ? 182 TYR   A N   1 
ATOM   1398 C  CA  . TYR   A 1 182 ? -3.52655  -16.10375 -4.21313  1.000 8.71651  ? 182 TYR   A CA  1 
ATOM   1399 C  C   . TYR   A 1 182 ? -3.13745  -17.35287 -4.98441  1.000 12.37073 ? 182 TYR   A C   1 
ATOM   1400 O  O   . TYR   A 1 182 ? -3.71239  -17.64442 -6.03361  1.000 14.05250 ? 182 TYR   A O   1 
ATOM   1401 C  CB  . TYR   A 1 182 ? -4.95520  -16.18569 -3.72535  1.000 9.95001  ? 182 TYR   A CB  1 
ATOM   1402 C  CG  . TYR   A 1 182 ? -5.30829  -15.13651 -2.70329  1.000 9.54295  ? 182 TYR   A CG  1 
ATOM   1403 C  CD1 . TYR   A 1 182 ? -4.99850  -15.31704 -1.36531  1.000 11.09882 ? 182 TYR   A CD1 1 
ATOM   1404 C  CD2 . TYR   A 1 182 ? -6.02773  -14.00772 -3.07052  1.000 10.56116 ? 182 TYR   A CD2 1 
ATOM   1405 C  CE1 . TYR   A 1 182 ? -5.37308  -14.38391 -0.42522  1.000 12.29749 ? 182 TYR   A CE1 1 
ATOM   1406 C  CE2 . TYR   A 1 182 ? -6.39828  -13.04546 -2.12642  1.000 7.23541  ? 182 TYR   A CE2 1 
ATOM   1407 C  CZ  . TYR   A 1 182 ? -6.07537  -13.24818 -0.82198  1.000 10.73989 ? 182 TYR   A CZ  1 
ATOM   1408 O  OH  . TYR   A 1 182 ? -6.43608  -12.32268 0.11149   1.000 10.26329 ? 182 TYR   A OH  1 
ATOM   1409 N  N   . GLY   A 1 183 ? -2.13982  -18.05949 -4.48910  1.000 11.11190 ? 183 GLY   A N   1 
ATOM   1410 C  CA  . GLY   A 1 183 ? -1.72353  -19.30729 -5.09078  1.000 12.95052 ? 183 GLY   A CA  1 
ATOM   1411 C  C   . GLY   A 1 183 ? -0.84726  -19.13836 -6.31011  1.000 13.30787 ? 183 GLY   A C   1 
ATOM   1412 O  O   . GLY   A 1 183 ? -0.47905  -18.02848 -6.70545  1.000 12.37639 ? 183 GLY   A O   1 
ATOM   1413 N  N   . PRO   A 1 184 ? -0.49741  -20.25190 -6.92678  1.000 12.87086 ? 184 PRO   A N   1 
ATOM   1414 C  CA  . PRO   A 1 184 ? 0.55285   -20.26230 -7.96302  1.000 15.65875 ? 184 PRO   A CA  1 
ATOM   1415 C  C   . PRO   A 1 184 ? -0.00396  -19.97444 -9.35332  1.000 18.71456 ? 184 PRO   A C   1 
ATOM   1416 O  O   . PRO   A 1 184 ? 0.13690   -20.77435 -10.29352 1.000 19.95769 ? 184 PRO   A O   1 
ATOM   1417 C  CB  . PRO   A 1 184 ? 1.10990   -21.68369 -7.84750  1.000 17.14029 ? 184 PRO   A CB  1 
ATOM   1418 C  CG  . PRO   A 1 184 ? -0.09929  -22.49649 -7.42282  1.000 15.43009 ? 184 PRO   A CG  1 
ATOM   1419 C  CD  . PRO   A 1 184 ? -0.94855  -21.60709 -6.56333  1.000 16.05651 ? 184 PRO   A CD  1 
ATOM   1420 N  N   . PHE   A 1 185 ? -0.63955  -18.82496 -9.48419  1.000 16.20069 ? 185 PHE   A N   1 
ATOM   1421 C  CA  . PHE   A 1 185 ? -1.34389  -18.44713 -10.69335 1.000 17.14210 ? 185 PHE   A CA  1 
ATOM   1422 C  C   . PHE   A 1 185 ? -0.81215  -17.11367 -11.19626 1.000 20.78652 ? 185 PHE   A C   1 
ATOM   1423 O  O   . PHE   A 1 185 ? -0.33779  -16.27728 -10.42007 1.000 19.21849 ? 185 PHE   A O   1 
ATOM   1424 C  CB  . PHE   A 1 185 ? -2.85502  -18.38293 -10.45318 1.000 18.29987 ? 185 PHE   A CB  1 
ATOM   1425 C  CG  . PHE   A 1 185 ? -3.39458  -19.61006 -9.78898  1.000 14.29945 ? 185 PHE   A CG  1 
ATOM   1426 C  CD1 . PHE   A 1 185 ? -3.33102  -20.82797 -10.42930 1.000 16.61754 ? 185 PHE   A CD1 1 
ATOM   1427 C  CD2 . PHE   A 1 185 ? -3.95020  -19.55259 -8.52950  1.000 16.32523 ? 185 PHE   A CD2 1 
ATOM   1428 C  CE1 . PHE   A 1 185 ? -3.80106  -21.97909 -9.81418  1.000 16.31721 ? 185 PHE   A CE1 1 
ATOM   1429 C  CE2 . PHE   A 1 185 ? -4.42931  -20.68413 -7.93022  1.000 15.14902 ? 185 PHE   A CE2 1 
ATOM   1430 C  CZ  . PHE   A 1 185 ? -4.34295  -21.91218 -8.58049  1.000 14.87401 ? 185 PHE   A CZ  1 
ATOM   1431 N  N   . VAL   A 1 186 ? -0.86697  -16.93760 -12.50924 1.000 18.62087 ? 186 VAL   A N   1 
ATOM   1432 C  CA  . VAL   A 1 186 ? -0.31790  -15.76092 -13.16289 1.000 20.37534 ? 186 VAL   A CA  1 
ATOM   1433 C  C   . VAL   A 1 186 ? -1.37400  -15.21389 -14.10743 1.000 21.30478 ? 186 VAL   A C   1 
ATOM   1434 O  O   . VAL   A 1 186 ? -2.23777  -15.94932 -14.59404 1.000 19.64961 ? 186 VAL   A O   1 
ATOM   1435 C  CB  . VAL   A 1 186 ? 0.98165   -16.09667 -13.91487 1.000 22.49146 ? 186 VAL   A CB  1 
ATOM   1436 C  CG1 . VAL   A 1 186 ? 2.08083   -16.45239 -12.91701 1.000 23.22927 ? 186 VAL   A CG1 1 
ATOM   1437 C  CG2 . VAL   A 1 186 ? 0.74554   -17.25929 -14.87031 1.000 21.89353 ? 186 VAL   A CG2 1 
ATOM   1438 N  N   . ASP   A 1 187 ? -1.32387  -13.91124 -14.35477 1.000 19.76701 ? 187 ASP   A N   1 
ATOM   1439 C  CA  . ASP   A 1 187 ? -2.35045  -13.30275 -15.19866 1.000 22.66321 ? 187 ASP   A CA  1 
ATOM   1440 C  C   . ASP   A 1 187 ? -1.88468  -13.27396 -16.65341 1.000 24.31775 ? 187 ASP   A C   1 
ATOM   1441 O  O   . ASP   A 1 187 ? -1.72473  -12.23099 -17.28415 1.000 23.15719 ? 187 ASP   A O   1 
ATOM   1442 C  CB  . ASP   A 1 187 ? -2.73991  -11.92333 -14.68459 1.000 20.64374 ? 187 ASP   A CB  1 
ATOM   1443 C  CG  . ASP   A 1 187 ? -1.56239  -11.01777 -14.45064 1.000 19.83058 ? 187 ASP   A CG  1 
ATOM   1444 O  OD1 . ASP   A 1 187 ? -0.39404  -11.47476 -14.46497 1.000 18.10767 ? 187 ASP   A OD1 1 
ATOM   1445 O  OD2 . ASP   A 1 187 ? -1.82643  -9.82100  -14.23853 1.000 18.42274 ? 187 ASP   A OD2 1 
ATOM   1446 N  N   . ARG   A 1 188 ? -1.63479  -14.47674 -17.16297 1.000 25.04444 ? 188 ARG   A N   1 
ATOM   1447 C  CA  . ARG   A 1 188 ? -1.46993  -14.71413 -18.58813 1.000 29.99455 ? 188 ARG   A CA  1 
ATOM   1448 C  C   . ARG   A 1 188 ? -2.15605  -16.02900 -18.90720 1.000 32.35702 ? 188 ARG   A C   1 
ATOM   1449 O  O   . ARG   A 1 188 ? -2.54640  -16.77803 -18.00731 1.000 29.08166 ? 188 ARG   A O   1 
ATOM   1450 C  CB  . ARG   A 1 188 ? -0.00471  -14.79728 -19.01613 1.000 31.88332 ? 188 ARG   A CB  1 
ATOM   1451 C  CG  . ARG   A 1 188 ? 0.88843   -15.38511 -17.98088 1.000 31.21704 ? 188 ARG   A CG  1 
ATOM   1452 C  CD  . ARG   A 1 188 ? 2.33940   -15.02745 -18.19316 1.000 32.83698 ? 188 ARG   A CD  1 
ATOM   1453 N  NE  . ARG   A 1 188 ? 3.15242   -16.11521 -17.67770 1.000 34.46266 ? 188 ARG   A NE  1 
ATOM   1454 C  CZ  . ARG   A 1 188 ? 3.82679   -16.05544 -16.53931 1.000 36.16999 ? 188 ARG   A CZ  1 
ATOM   1455 N  NH1 . ARG   A 1 188 ? 3.82635   -14.95906 -15.79238 1.000 37.53405 ? 188 ARG   A NH1 1 
ATOM   1456 N  NH2 . ARG   A 1 188 ? 4.48130   -17.13433 -16.11683 1.000 38.14617 ? 188 ARG   A NH2 1 
ATOM   1457 N  N   . GLN   A 1 189 ? -2.28015  -16.33227 -20.19370 1.000 34.50949 ? 189 GLN   A N   1 
ATOM   1458 C  CA  . GLN   A 1 189 ? -2.96083  -17.55801 -20.59573 1.000 37.76937 ? 189 GLN   A CA  1 
ATOM   1459 C  C   . GLN   A 1 189 ? -1.90391  -18.64343 -20.74053 1.000 35.76492 ? 189 GLN   A C   1 
ATOM   1460 O  O   . GLN   A 1 189 ? -1.20949  -18.72718 -21.75406 1.000 41.02381 ? 189 GLN   A O   1 
ATOM   1461 C  CB  . GLN   A 1 189 ? -3.77408  -17.34806 -21.86677 1.000 42.78041 ? 189 GLN   A CB  1 
ATOM   1462 C  CG  . GLN   A 1 189 ? -4.54273  -18.58006 -22.31545 1.000 45.58182 ? 189 GLN   A CG  1 
ATOM   1463 C  CD  . GLN   A 1 189 ? -5.88481  -18.21160 -22.94940 1.000 59.29324 ? 189 GLN   A CD  1 
ATOM   1464 O  OE1 . GLN   A 1 189 ? -6.22333  -17.02651 -23.06956 1.000 59.88033 ? 189 GLN   A OE1 1 
ATOM   1465 N  NE2 . GLN   A 1 189 ? -6.65064  -19.22082 -23.36044 1.000 62.37024 ? 189 GLN   A NE2 1 
ATOM   1466 N  N   . THR   A 1 190 ? -1.76030  -19.44593 -19.69397 1.000 30.50311 ? 190 THR   A N   1 
ATOM   1467 C  CA  . THR   A 1 190 ? -0.93299  -20.63989 -19.65267 1.000 32.72492 ? 190 THR   A CA  1 
ATOM   1468 C  C   . THR   A 1 190 ? -1.82251  -21.84432 -19.37764 1.000 31.78224 ? 190 THR   A C   1 
ATOM   1469 O  O   . THR   A 1 190 ? -3.04636  -21.73189 -19.27273 1.000 32.35346 ? 190 THR   A O   1 
ATOM   1470 C  CB  . THR   A 1 190 ? 0.15675   -20.51517 -18.58468 1.000 30.50738 ? 190 THR   A CB  1 
ATOM   1471 O  OG1 . THR   A 1 190 ? -0.36719  -20.93839 -17.31918 1.000 32.24760 ? 190 THR   A OG1 1 
ATOM   1472 C  CG2 . THR   A 1 190 ? 0.63605   -19.07553 -18.46295 1.000 31.51586 ? 190 THR   A CG2 1 
ATOM   1473 N  N   . ALA   A 1 191 ? -1.19814  -23.01231 -19.24737 1.000 34.47403 ? 191 ALA   A N   1 
ATOM   1474 C  CA  . ALA   A 1 191 ? -1.93136  -24.21731 -18.88280 1.000 33.51471 ? 191 ALA   A CA  1 
ATOM   1475 C  C   . ALA   A 1 191 ? -2.06987  -24.38301 -17.37051 1.000 32.57270 ? 191 ALA   A C   1 
ATOM   1476 O  O   . ALA   A 1 191 ? -2.18239  -25.51952 -16.89180 1.000 34.48320 ? 191 ALA   A O   1 
ATOM   1477 C  CB  . ALA   A 1 191 ? -1.26562  -25.44976 -19.50423 1.000 33.61737 ? 191 ALA   A CB  1 
ATOM   1478 N  N   . GLN   A 1 192 ? -2.06847  -23.28594 -16.60739 1.000 28.75791 ? 192 GLN   A N   1 
ATOM   1479 C  CA  . GLN   A 1 192 ? -2.13702  -23.39068 -15.15503 1.000 26.96718 ? 192 GLN   A CA  1 
ATOM   1480 C  C   . GLN   A 1 192 ? -3.40597  -24.10349 -14.73457 1.000 29.75354 ? 192 GLN   A C   1 
ATOM   1481 O  O   . GLN   A 1 192 ? -4.46495  -23.95346 -15.35415 1.000 30.38399 ? 192 GLN   A O   1 
ATOM   1482 C  CB  . GLN   A 1 192 ? -2.13655  -22.02073 -14.48257 1.000 25.82530 ? 192 GLN   A CB  1 
ATOM   1483 C  CG  . GLN   A 1 192 ? -2.74592  -20.92867 -15.30734 1.000 26.89021 ? 192 GLN   A CG  1 
ATOM   1484 C  CD  . GLN   A 1 192 ? -2.50507  -19.56116 -14.71905 1.000 24.80926 ? 192 GLN   A CD  1 
ATOM   1485 O  OE1 . GLN   A 1 192 ? -1.90217  -19.42502 -13.64884 1.000 21.75296 ? 192 GLN   A OE1 1 
ATOM   1486 N  NE2 . GLN   A 1 192 ? -2.92824  -18.53096 -15.43984 1.000 23.00363 ? 192 GLN   A NE2 1 
ATOM   1487 N  N   . ALA   A 1 193 ? -3.30429  -24.84568 -13.63848 1.000 24.31809 ? 193 ALA   A N   1 
ATOM   1488 C  CA  . ALA   A 1 193 ? -4.42505  -25.60472 -13.12156 1.000 23.94012 ? 193 ALA   A CA  1 
ATOM   1489 C  C   . ALA   A 1 193 ? -4.39623  -25.53248 -11.60492 1.000 23.41020 ? 193 ALA   A C   1 
ATOM   1490 O  O   . ALA   A 1 193 ? -3.35362  -25.28017 -10.99685 1.000 25.07463 ? 193 ALA   A O   1 
ATOM   1491 C  CB  . ALA   A 1 193 ? -4.39725  -27.06326 -13.58797 1.000 26.47490 ? 193 ALA   A CB  1 
ATOM   1492 N  N   . ALA   A 1 194 ? -5.56015  -25.78582 -11.00566 1.000 21.63936 ? 194 ALA   A N   1 
ATOM   1493 C  CA  . ALA   A 1 194 ? -5.73518  -25.55705 -9.57560  1.000 24.03929 ? 194 ALA   A CA  1 
ATOM   1494 C  C   . ALA   A 1 194 ? -4.75828  -26.37642 -8.73401  1.000 27.86911 ? 194 ALA   A C   1 
ATOM   1495 O  O   . ALA   A 1 194 ? -4.19072  -25.86802 -7.75754  1.000 32.34734 ? 194 ALA   A O   1 
ATOM   1496 C  CB  . ALA   A 1 194 ? -7.17735  -25.86654 -9.18012  1.000 21.79125 ? 194 ALA   A CB  1 
ATOM   1497 N  N   . GLY   A 1 195 ? -4.55072  -27.63248 -9.07448  1.000 28.59042 ? 195 GLY   A N   1 
ATOM   1498 C  CA  . GLY   A 1 195 ? -3.77770  -28.27887 -8.01436  1.000 30.32217 ? 195 GLY   A CA  1 
ATOM   1499 C  C   . GLY   A 1 195 ? -4.66860  -28.84468 -6.92323  1.000 29.61741 ? 195 GLY   A C   1 
ATOM   1500 O  O   . GLY   A 1 195 ? -5.74783  -28.33050 -6.62519  1.000 25.72547 ? 195 GLY   A O   1 
ATOM   1501 N  N   . THR   A 1 196 ? -4.20358  -29.93857 -6.31379  1.000 27.34502 ? 196 THR   A N   1 
ATOM   1502 C  CA  . THR   A 1 196 ? -5.09934  -30.74722 -5.49806  1.000 27.71662 ? 196 THR   A CA  1 
ATOM   1503 C  C   . THR   A 1 196 ? -5.56819  -29.97488 -4.26731  1.000 25.34932 ? 196 THR   A C   1 
ATOM   1504 O  O   . THR   A 1 196 ? -4.81202  -29.21834 -3.64832  1.000 23.12240 ? 196 THR   A O   1 
ATOM   1505 C  CB  . THR   A 1 196 ? -4.41950  -32.04243 -5.07300  1.000 29.58070 ? 196 THR   A CB  1 
ATOM   1506 O  OG1 . THR   A 1 196 ? -3.29672  -31.72781 -4.24142  1.000 34.57075 ? 196 THR   A OG1 1 
ATOM   1507 C  CG2 . THR   A 1 196 ? -3.93921  -32.83578 -6.30434  1.000 28.61532 ? 196 THR   A CG2 1 
ATOM   1508 N  N   . ASP   A 1 197 ? -6.83900  -30.13817 -3.94317  1.000 24.19227 ? 197 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 197 ? -7.43637  -29.48037 -2.79086  1.000 24.35375 ? 197 ASP   A CA  1 
ATOM   1510 C  C   . ASP   A 1 197 ? -7.59955  -30.46568 -1.63776  1.000 26.12671 ? 197 ASP   A C   1 
ATOM   1511 O  O   . ASP   A 1 197 ? -7.55993  -31.67944 -1.82499  1.000 26.28575 ? 197 ASP   A O   1 
ATOM   1512 C  CB  . ASP   A 1 197 ? -8.79207  -28.89911 -3.15295  1.000 22.93993 ? 197 ASP   A CB  1 
ATOM   1513 C  CG  . ASP   A 1 197 ? -9.10364  -27.64364 -2.38485  1.000 22.36693 ? 197 ASP   A CG  1 
ATOM   1514 O  OD1 . ASP   A 1 197 ? -8.18400  -27.05297 -1.75083  1.000 21.62781 ? 197 ASP   A OD1 1 
ATOM   1515 O  OD2 . ASP   A 1 197 ? -10.27292 -27.23731 -2.43263  1.000 21.43758 ? 197 ASP   A OD2 1 
ATOM   1516 N  N   . THR   A 1 198 ? -7.79713  -29.91613 -0.43992  1.000 22.57293 ? 198 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 198 ? -8.14716  -30.67628 0.74822   1.000 22.25595 ? 198 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 198 ? -9.39728  -30.06597 1.35485   1.000 23.42197 ? 198 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 198 ? -9.80545  -28.95634 0.99580   1.000 20.52387 ? 198 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 198 ? -7.01397  -30.68425 1.78345   1.000 24.78499 ? 198 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 198 ? -6.55016  -29.34356 1.99857   1.000 24.75287 ? 198 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 198 ? -5.87000  -31.50151 1.28555   1.000 27.69047 ? 198 THR   A CG2 1 
ATOM   1523 N  N   . THR   A 1 199 ? -10.01840 -30.80473 2.27436   1.000 21.55134 ? 199 THR   A N   1 
ATOM   1524 C  CA  . THR   A 1 199 ? -11.17364 -30.28410 2.99727   1.000 20.48415 ? 199 THR   A CA  1 
ATOM   1525 C  C   . THR   A 1 199 ? -10.71050 -29.56113 4.25208   1.000 19.57560 ? 199 THR   A C   1 
ATOM   1526 O  O   . THR   A 1 199 ? -9.80120  -30.02765 4.94351   1.000 20.78938 ? 199 THR   A O   1 
ATOM   1527 C  CB  . THR   A 1 199 ? -12.14087 -31.41623 3.35254   1.000 22.99758 ? 199 THR   A CB  1 
ATOM   1528 O  OG1 . THR   A 1 199 ? -12.63355 -32.01253 2.14528   1.000 23.17817 ? 199 THR   A OG1 1 
ATOM   1529 C  CG2 . THR   A 1 199 ? -13.28352 -30.89910 4.16527   1.000 21.72119 ? 199 THR   A CG2 1 
ATOM   1530 N  N   . ILE   A 1 200 ? -11.32034 -28.41056 4.53681   1.000 16.50974 ? 200 ILE   A N   1 
ATOM   1531 C  CA  . ILE   A 1 200 ? -10.88328 -27.57802 5.66147   1.000 16.55497 ? 200 ILE   A CA  1 
ATOM   1532 C  C   . ILE   A 1 200 ? -11.47695 -28.15631 6.94626   1.000 17.41006 ? 200 ILE   A C   1 
ATOM   1533 O  O   . ILE   A 1 200 ? -12.61833 -27.86725 7.30422   1.000 16.26400 ? 200 ILE   A O   1 
ATOM   1534 C  CB  . ILE   A 1 200 ? -11.25759 -26.10669 5.47158   1.000 16.24906 ? 200 ILE   A CB  1 
ATOM   1535 C  CG1 . ILE   A 1 200 ? -10.82801 -25.63221 4.07734   1.000 15.23837 ? 200 ILE   A CG1 1 
ATOM   1536 C  CG2 . ILE   A 1 200 ? -10.61007 -25.25526 6.57712   1.000 15.52171 ? 200 ILE   A CG2 1 
ATOM   1537 C  CD1 . ILE   A 1 200 ? -11.66371 -24.48827 3.50295   1.000 13.14196 ? 200 ILE   A CD1 1 
ATOM   1538 N  N   . THR   A 1 201 ? -10.67767 -28.95356 7.66300   1.000 17.77255 ? 201 THR   A N   1 
ATOM   1539 C  CA  . THR   A 1 201 ? -11.18131 -29.74962 8.78397   1.000 18.17903 ? 201 THR   A CA  1 
ATOM   1540 C  C   . THR   A 1 201 ? -11.77122 -28.87991 9.88409   1.000 17.52193 ? 201 THR   A C   1 
ATOM   1541 O  O   . THR   A 1 201 ? -12.85459 -29.17805 10.40186  1.000 16.81908 ? 201 THR   A O   1 
ATOM   1542 C  CB  . THR   A 1 201 ? -10.06023 -30.62122 9.33695   1.000 19.14006 ? 201 THR   A CB  1 
ATOM   1543 O  OG1 . THR   A 1 201 ? -9.49422  -31.37323 8.26181   1.000 19.57646 ? 201 THR   A OG1 1 
ATOM   1544 C  CG2 . THR   A 1 201 ? -10.58617 -31.58029 10.41374  1.000 20.94589 ? 201 THR   A CG2 1 
ATOM   1545 N  N   . VAL   A 1 202 ? -11.08190 -27.79560 10.25880  1.000 15.23144 ? 202 VAL   A N   1 
ATOM   1546 C  CA  . VAL   A 1 202 ? -11.58383 -27.01766 11.38527  1.000 14.62919 ? 202 VAL   A CA  1 
ATOM   1547 C  C   . VAL   A 1 202 ? -12.94498 -26.43648 11.04438  1.000 12.93038 ? 202 VAL   A C   1 
ATOM   1548 O  O   . VAL   A 1 202 ? -13.81450 -26.32837 11.91552  1.000 16.04144 ? 202 VAL   A O   1 
ATOM   1549 C  CB  . VAL   A 1 202 ? -10.58824 -25.92319 11.82100  1.000 17.91338 ? 202 VAL   A CB  1 
ATOM   1550 C  CG1 . VAL   A 1 202 ? -10.32933 -24.92500 10.71170  1.000 17.86673 ? 202 VAL   A CG1 1 
ATOM   1551 C  CG2 . VAL   A 1 202 ? -11.09153 -25.22308 13.07785  1.000 17.09400 ? 202 VAL   A CG2 1 
ATOM   1552 N  N   . ASN   A 1 203 ? -13.16547 -26.10327 9.77468   1.000 15.09064 ? 203 ASN   A N   1 
ATOM   1553 C  CA  . ASN   A 1 203 ? -14.44527 -25.54739 9.34870   1.000 14.09103 ? 203 ASN   A CA  1 
ATOM   1554 C  C   . ASN   A 1 203 ? -15.55915 -26.58222 9.42951   1.000 14.80919 ? 203 ASN   A C   1 
ATOM   1555 O  O   . ASN   A 1 203 ? -16.67996 -26.26499 9.85382   1.000 14.16683 ? 203 ASN   A O   1 
ATOM   1556 C  CB  . ASN   A 1 203 ? -14.34163 -25.01246 7.92571   1.000 14.02261 ? 203 ASN   A CB  1 
ATOM   1557 C  CG  . ASN   A 1 203 ? -13.59991 -23.69269 7.84668   1.000 13.36130 ? 203 ASN   A CG  1 
ATOM   1558 O  OD1 . ASN   A 1 203 ? -13.09074 -23.18720 8.85111   1.000 12.77615 ? 203 ASN   A OD1 1 
ATOM   1559 N  ND2 . ASN   A 1 203 ? -13.53588 -23.13303 6.65393   1.000 10.59795 ? 203 ASN   A ND2 1 
ATOM   1560 N  N   . VAL   A 1 204 ? -15.29094 -27.80279 8.96589   1.000 14.87149 ? 204 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 204 ? -16.27098 -28.87204 9.09310   1.000 15.14763 ? 204 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 204 ? -16.69643 -29.01642 10.54115  1.000 15.94052 ? 204 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 204 ? -17.88868 -29.10337 10.84418  1.000 15.36398 ? 204 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 204 ? -15.72132 -30.19305 8.53323   1.000 15.27116 ? 204 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 204 ? -16.70721 -31.31187 8.78351   1.000 17.78166 ? 204 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 204 ? -15.46401 -30.04598 7.03635   1.000 15.03667 ? 204 VAL   A CG2 1 
ATOM   1567 N  N   . LEU   A 1 205 ? -15.72488 -29.03684 11.45573  1.000 14.22459 ? 205 LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 205 ? -16.05206 -29.14484 12.87104  1.000 16.97276 ? 205 LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 205 ? -16.89855 -27.96941 13.31781  1.000 16.74576 ? 205 LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 205 ? -17.89046 -28.14710 14.02773  1.000 15.74811 ? 205 LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 205 ? -14.77376 -29.23333 13.70268  1.000 15.28028 ? 205 LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 205 ? -13.94791 -30.49341 13.48945  1.000 15.98561 ? 205 LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 205 ? -12.59252 -30.34556 14.15805  1.000 17.26978 ? 205 LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 205 ? -14.66816 -31.71528 14.02791  1.000 19.91481 ? 205 LEU   A CD2 1 
ATOM   1575 N  N   . ALA   A 1 206 ? -16.53801 -26.76011 12.88605  1.000 15.51247 ? 206 ALA   A N   1 
ATOM   1576 C  CA  . ALA   A 1 206 ? -17.33554 -25.59483 13.24778  1.000 14.17384 ? 206 ALA   A CA  1 
ATOM   1577 C  C   . ALA   A 1 206 ? -18.77813 -25.76624 12.80549  1.000 13.98607 ? 206 ALA   A C   1 
ATOM   1578 O  O   . ALA   A 1 206 ? -19.70287 -25.43758 13.54651  1.000 15.27428 ? 206 ALA   A O   1 
ATOM   1579 C  CB  . ALA   A 1 206 ? -16.72887 -24.33526 12.63371  1.000 14.41066 ? 206 ALA   A CB  1 
ATOM   1580 N  N   . TRP   A 1 207 ? -18.97734 -26.27629 11.59141  1.000 13.95748 ? 207 TRP   A N   1 
ATOM   1581 C  CA  . TRP   A 1 207 ? -20.30205 -26.45158 11.03202  1.000 16.91809 ? 207 TRP   A CA  1 
ATOM   1582 C  C   . TRP   A 1 207 ? -21.05583 -27.55157 11.76851  1.000 17.68038 ? 207 TRP   A C   1 
ATOM   1583 O  O   . TRP   A 1 207 ? -22.27206 -27.44714 11.98950  1.000 17.95883 ? 207 TRP   A O   1 
ATOM   1584 C  CB  . TRP   A 1 207 ? -20.13255 -26.74220 9.53756   1.000 15.93608 ? 207 TRP   A CB  1 
ATOM   1585 C  CG  . TRP   A 1 207 ? -21.32472 -27.23327 8.78076   1.000 15.91508 ? 207 TRP   A CG  1 
ATOM   1586 C  CD1 . TRP   A 1 207 ? -22.33452 -26.49128 8.26668   1.000 16.81361 ? 207 TRP   A CD1 1 
ATOM   1587 C  CD2 . TRP   A 1 207 ? -21.56538 -28.57275 8.38385   1.000 16.72476 ? 207 TRP   A CD2 1 
ATOM   1588 N  NE1 . TRP   A 1 207 ? -23.22498 -27.30032 7.60112   1.000 17.40751 ? 207 TRP   A NE1 1 
ATOM   1589 C  CE2 . TRP   A 1 207 ? -22.77404 -28.58717 7.66376   1.000 16.33350 ? 207 TRP   A CE2 1 
ATOM   1590 C  CE3 . TRP   A 1 207 ? -20.88797 -29.77325 8.59000   1.000 18.20529 ? 207 TRP   A CE3 1 
ATOM   1591 C  CZ2 . TRP   A 1 207 ? -23.30786 -29.74938 7.13207   1.000 20.58409 ? 207 TRP   A CZ2 1 
ATOM   1592 C  CZ3 . TRP   A 1 207 ? -21.43269 -30.93536 8.07132   1.000 19.91616 ? 207 TRP   A CZ3 1 
ATOM   1593 C  CH2 . TRP   A 1 207 ? -22.62164 -30.91254 7.34454   1.000 18.47506 ? 207 TRP   A CH2 1 
ATOM   1594 N  N   . LEU   A 1 208 ? -20.34358 -28.60246 12.18577  1.000 16.31398 ? 208 LEU   A N   1 
ATOM   1595 C  CA  . LEU   A 1 208 ? -20.96112 -29.60833 13.05192  1.000 16.88315 ? 208 LEU   A CA  1 
ATOM   1596 C  C   . LEU   A 1 208 ? -21.45352 -28.97759 14.34986  1.000 17.38111 ? 208 LEU   A C   1 
ATOM   1597 O  O   . LEU   A 1 208 ? -22.54600 -29.29538 14.82700  1.000 18.36813 ? 208 LEU   A O   1 
ATOM   1598 C  CB  . LEU   A 1 208 ? -19.96918 -30.72946 13.34693  1.000 17.19371 ? 208 LEU   A CB  1 
ATOM   1599 C  CG  . LEU   A 1 208 ? -19.69195 -31.66191 12.17036  1.000 18.91415 ? 208 LEU   A CG  1 
ATOM   1600 C  CD1 . LEU   A 1 208 ? -18.67645 -32.69968 12.56056  1.000 18.96454 ? 208 LEU   A CD1 1 
ATOM   1601 C  CD2 . LEU   A 1 208 ? -20.99474 -32.32251 11.68352  1.000 18.86316 ? 208 LEU   A CD2 1 
ATOM   1602 N  N   . TYR   A 1 209 ? -20.66861 -28.05803 14.92201  1.000 19.00932 ? 209 TYR   A N   1 
ATOM   1603 C  CA  . TYR   A 1 209 ? -21.14429 -27.30249 16.07646  1.000 18.15026 ? 209 TYR   A CA  1 
ATOM   1604 C  C   . TYR   A 1 209 ? -22.34954 -26.43984 15.72243  1.000 19.86589 ? 209 TYR   A C   1 
ATOM   1605 O  O   . TYR   A 1 209 ? -23.28752 -26.33444 16.51180  1.000 19.22200 ? 209 TYR   A O   1 
ATOM   1606 C  CB  . TYR   A 1 209 ? -20.02969 -26.43468 16.63333  1.000 17.24968 ? 209 TYR   A CB  1 
ATOM   1607 C  CG  . TYR   A 1 209 ? -19.07780 -27.19186 17.51108  1.000 19.09848 ? 209 TYR   A CG  1 
ATOM   1608 C  CD1 . TYR   A 1 209 ? -19.47947 -27.66270 18.76197  1.000 23.03266 ? 209 TYR   A CD1 1 
ATOM   1609 C  CD2 . TYR   A 1 209 ? -17.77898 -27.45341 17.09005  1.000 20.18209 ? 209 TYR   A CD2 1 
ATOM   1610 C  CE1 . TYR   A 1 209 ? -18.61057 -28.36085 19.56613  1.000 23.10184 ? 209 TYR   A CE1 1 
ATOM   1611 C  CE2 . TYR   A 1 209 ? -16.90414 -28.15093 17.88930  1.000 22.06706 ? 209 TYR   A CE2 1 
ATOM   1612 C  CZ  . TYR   A 1 209 ? -17.32092 -28.59379 19.11709  1.000 25.28726 ? 209 TYR   A CZ  1 
ATOM   1613 O  OH  . TYR   A 1 209 ? -16.43811 -29.28820 19.89503  1.000 24.67425 ? 209 TYR   A OH  1 
ATOM   1614 N  N   . ALA   A 1 210 ? -22.32747 -25.78448 14.55712  1.000 17.56448 ? 210 ALA   A N   1 
ATOM   1615 C  CA  . ALA   A 1 210 ? -23.50401 -25.04489 14.11491  1.000 17.76396 ? 210 ALA   A CA  1 
ATOM   1616 C  C   . ALA   A 1 210 ? -24.71930 -25.95271 14.06228  1.000 21.01076 ? 210 ALA   A C   1 
ATOM   1617 O  O   . ALA   A 1 210 ? -25.83006 -25.54370 14.41402  1.000 20.22829 ? 210 ALA   A O   1 
ATOM   1618 C  CB  . ALA   A 1 210 ? -23.26793 -24.43136 12.73869  1.000 18.86855 ? 210 ALA   A CB  1 
ATOM   1619 N  N   . ALA   A 1 211 ? -24.52216 -27.18348 13.58780  1.000 18.89642 ? 211 ALA   A N   1 
ATOM   1620 C  CA  . ALA   A 1 211 ? -25.61527 -28.13153 13.48768  1.000 20.69986 ? 211 ALA   A CA  1 
ATOM   1621 C  C   . ALA   A 1 211 ? -26.17118 -28.44550 14.86526  1.000 21.66071 ? 211 ALA   A C   1 
ATOM   1622 O  O   . ALA   A 1 211 ? -27.38580 -28.39169 15.08080  1.000 20.90024 ? 211 ALA   A O   1 
ATOM   1623 C  CB  . ALA   A 1 211 ? -25.13355 -29.40262 12.80149  1.000 18.28176 ? 211 ALA   A CB  1 
ATOM   1624 N  N   . VAL   A 1 212 ? -25.28460 -28.75718 15.81368  1.000 20.65429 ? 212 VAL   A N   1 
ATOM   1625 C  CA  . VAL   A 1 212 ? -25.71470 -29.04488 17.18045  1.000 21.33639 ? 212 VAL   A CA  1 
ATOM   1626 C  C   . VAL   A 1 212 ? -26.45874 -27.85293 17.76837  1.000 22.47437 ? 212 VAL   A C   1 
ATOM   1627 O  O   . VAL   A 1 212 ? -27.50000 -28.01194 18.41617  1.000 23.13110 ? 212 VAL   A O   1 
ATOM   1628 C  CB  . VAL   A 1 212 ? -24.51022 -29.44200 18.05814  1.000 20.90409 ? 212 VAL   A CB  1 
ATOM   1629 C  CG1 . VAL   A 1 212 ? -24.95510 -29.57300 19.51228  1.000 23.54327 ? 212 VAL   A CG1 1 
ATOM   1630 C  CG2 . VAL   A 1 212 ? -23.91706 -30.77651 17.58148  1.000 20.88897 ? 212 VAL   A CG2 1 
ATOM   1631 N  N   . ILE   A 1 213 ? -25.93465 -26.64167 17.55716  1.000 22.93425 ? 213 ILE   A N   1 
ATOM   1632 C  CA  . ILE   A 1 213 ? -26.60795 -25.45375 18.07397  1.000 23.05612 ? 213 ILE   A CA  1 
ATOM   1633 C  C   . ILE   A 1 213 ? -28.00789 -25.36607 17.50162  1.000 24.37287 ? 213 ILE   A C   1 
ATOM   1634 O  O   . ILE   A 1 213 ? -28.95147 -24.96766 18.19984  1.000 25.92600 ? 213 ILE   A O   1 
ATOM   1635 C  CB  . ILE   A 1 213 ? -25.76835 -24.19271 17.77318  1.000 26.58677 ? 213 ILE   A CB  1 
ATOM   1636 C  CG1 . ILE   A 1 213 ? -24.47378 -24.20144 18.61229  1.000 23.53506 ? 213 ILE   A CG1 1 
ATOM   1637 C  CG2 . ILE   A 1 213 ? -26.58719 -22.92074 17.99663  1.000 26.43621 ? 213 ILE   A CG2 1 
ATOM   1638 C  CD1 . ILE   A 1 213 ? -23.39996 -23.22246 18.17542  1.000 23.56103 ? 213 ILE   A CD1 1 
ATOM   1639 N  N   . ASN   A 1 214 ? -28.18242 -25.83197 16.26419  1.000 22.79488 ? 214 ASN   A N   1 
ATOM   1640 C  CA  . ASN   A 1 214 ? -29.43606 -25.76513 15.53565  1.000 23.65819 ? 214 ASN   A CA  1 
ATOM   1641 C  C   . ASN   A 1 214 ? -30.25228 -27.05406 15.62439  1.000 26.08663 ? 214 ASN   A C   1 
ATOM   1642 O  O   . ASN   A 1 214 ? -31.23810 -27.20521 14.89549  1.000 27.93227 ? 214 ASN   A O   1 
ATOM   1643 C  CB  . ASN   A 1 214 ? -29.14564 -25.37213 14.08945  1.000 26.65707 ? 214 ASN   A CB  1 
ATOM   1644 C  CG  . ASN   A 1 214 ? -28.94556 -23.86298 13.93749  1.000 26.99942 ? 214 ASN   A CG  1 
ATOM   1645 O  OD1 . ASN   A 1 214 ? -29.90277 -23.09817 14.05633  1.000 31.02547 ? 214 ASN   A OD1 1 
ATOM   1646 N  ND2 . ASN   A 1 214 ? -27.71021 -23.43207 13.73705  1.000 27.95986 ? 214 ASN   A ND2 1 
ATOM   1647 N  N   . GLY   A 1 215 ? -29.87559 -27.97953 16.51099  1.000 24.73320 ? 215 GLY   A N   1 
ATOM   1648 C  CA  . GLY   A 1 215 ? -30.71025 -29.11153 16.84799  1.000 25.35515 ? 215 GLY   A CA  1 
ATOM   1649 C  C   . GLY   A 1 215 ? -30.42334 -30.40664 16.11790  1.000 26.35481 ? 215 GLY   A C   1 
ATOM   1650 O  O   . GLY   A 1 215 ? -31.06335 -31.41737 16.43345  1.000 26.30306 ? 215 GLY   A O   1 
ATOM   1651 N  N   . ASP   A 1 216 ? -29.52467 -30.41166 15.13175  1.000 24.28834 ? 216 ASP   A N   1 
ATOM   1652 C  CA  . ASP   A 1 216 ? -29.06400 -31.66228 14.53091  1.000 25.62208 ? 216 ASP   A CA  1 
ATOM   1653 C  C   . ASP   A 1 216 ? -28.04764 -32.29348 15.47014  1.000 27.72247 ? 216 ASP   A C   1 
ATOM   1654 O  O   . ASP   A 1 216 ? -26.95929 -31.74183 15.67537  1.000 27.82069 ? 216 ASP   A O   1 
ATOM   1655 C  CB  . ASP   A 1 216 ? -28.42880 -31.44427 13.15881  1.000 27.58951 ? 216 ASP   A CB  1 
ATOM   1656 C  CG  . ASP   A 1 216 ? -29.38821 -30.87504 12.14816  1.000 30.08766 ? 216 ASP   A CG  1 
ATOM   1657 O  OD1 . ASP   A 1 216 ? -30.60396 -30.84459 12.44528  1.000 37.06449 ? 216 ASP   A OD1 1 
ATOM   1658 O  OD2 . ASP   A 1 216 ? -28.93242 -30.45299 11.06004  1.000 28.79906 ? 216 ASP   A OD2 1 
ATOM   1659 N  N   . ARG   A 1 217 ? -28.38250 -33.46533 16.01413  1.000 26.74752 ? 217 ARG   A N   1 
ATOM   1660 C  CA  . ARG   A 1 217 ? -27.51098 -34.15007 16.95793  1.000 26.15454 ? 217 ARG   A CA  1 
ATOM   1661 C  C   . ARG   A 1 217 ? -27.24588 -35.60456 16.60654  1.000 26.67657 ? 217 ARG   A C   1 
ATOM   1662 O  O   . ARG   A 1 217 ? -26.48548 -36.25943 17.31961  1.000 25.78765 ? 217 ARG   A O   1 
ATOM   1663 C  CB  . ARG   A 1 217 ? -28.11179 -34.10412 18.36525  1.000 26.44669 ? 217 ARG   A CB  1 
ATOM   1664 C  CG  . ARG   A 1 217 ? -28.53037 -32.73909 18.82064  1.000 26.91342 ? 217 ARG   A CG  1 
ATOM   1665 C  CD  . ARG   A 1 217 ? -29.07860 -32.81074 20.24023  1.000 27.29343 ? 217 ARG   A CD  1 
ATOM   1666 N  NE  . ARG   A 1 217 ? -28.13397 -33.45481 21.14238  1.000 28.16703 ? 217 ARG   A NE  1 
ATOM   1667 C  CZ  . ARG   A 1 217 ? -27.19433 -32.80739 21.81350  1.000 27.99614 ? 217 ARG   A CZ  1 
ATOM   1668 N  NH1 . ARG   A 1 217 ? -27.02387 -31.50115 21.67634  1.000 26.71694 ? 217 ARG   A NH1 1 
ATOM   1669 N  NH2 . ARG   A 1 217 ? -26.39418 -33.48864 22.62486  1.000 28.71378 ? 217 ARG   A NH2 1 
ATOM   1670 N  N   . TRP   A 1 218 ? -27.84226 -36.12368 15.53450  1.000 25.21548 ? 218 TRP   A N   1 
ATOM   1671 C  CA  . TRP   A 1 218 ? -27.82907 -37.55503 15.27265  1.000 26.22524 ? 218 TRP   A CA  1 
ATOM   1672 C  C   . TRP   A 1 218 ? -26.42560 -38.11715 15.10834  1.000 25.91703 ? 218 TRP   A C   1 
ATOM   1673 O  O   . TRP   A 1 218 ? -26.21775 -39.31352 15.33626  1.000 27.16675 ? 218 TRP   A O   1 
ATOM   1674 C  CB  . TRP   A 1 218 ? -28.66178 -37.85420 14.02708  1.000 27.77934 ? 218 TRP   A CB  1 
ATOM   1675 C  CG  . TRP   A 1 218 ? -28.15326 -37.24638 12.74015  1.000 27.11889 ? 218 TRP   A CG  1 
ATOM   1676 C  CD1 . TRP   A 1 218 ? -28.61391 -36.11262 12.13881  1.000 27.67991 ? 218 TRP   A CD1 1 
ATOM   1677 C  CD2 . TRP   A 1 218 ? -27.12873 -37.76316 11.88551  1.000 25.91615 ? 218 TRP   A CD2 1 
ATOM   1678 N  NE1 . TRP   A 1 218 ? -27.93767 -35.88820 10.96908  1.000 25.80726 ? 218 TRP   A NE1 1 
ATOM   1679 C  CE2 . TRP   A 1 218 ? -27.02005 -36.88667 10.78969  1.000 25.60429 ? 218 TRP   A CE2 1 
ATOM   1680 C  CE3 . TRP   A 1 218 ? -26.29572 -38.88336 11.93610  1.000 26.36681 ? 218 TRP   A CE3 1 
ATOM   1681 C  CZ2 . TRP   A 1 218 ? -26.10534 -37.08654 9.76360   1.000 27.07466 ? 218 TRP   A CZ2 1 
ATOM   1682 C  CZ3 . TRP   A 1 218 ? -25.39177 -39.08348 10.91232  1.000 29.65708 ? 218 TRP   A CZ3 1 
ATOM   1683 C  CH2 . TRP   A 1 218 ? -25.30063 -38.18259 9.84125   1.000 28.34972 ? 218 TRP   A CH2 1 
ATOM   1684 N  N   . PHE   A 1 219 ? -25.47587 -37.28453 14.69728  1.000 24.41349 ? 219 PHE   A N   1 
ATOM   1685 C  CA  . PHE   A 1 219 ? -24.10223 -37.67317 14.42802  1.000 25.60177 ? 219 PHE   A CA  1 
ATOM   1686 C  C   . PHE   A 1 219 ? -23.22682 -37.62797 15.67034  1.000 25.13968 ? 219 PHE   A C   1 
ATOM   1687 O  O   . PHE   A 1 219 ? -22.04311 -37.97486 15.59641  1.000 25.40192 ? 219 PHE   A O   1 
ATOM   1688 C  CB  . PHE   A 1 219 ? -23.53231 -36.75821 13.34498  1.000 24.76181 ? 219 PHE   A CB  1 
ATOM   1689 C  CG  . PHE   A 1 219 ? -23.72885 -35.30214 13.63702  1.000 21.59741 ? 219 PHE   A CG  1 
ATOM   1690 C  CD1 . PHE   A 1 219 ? -22.83058 -34.61232 14.43045  1.000 20.83848 ? 219 PHE   A CD1 1 
ATOM   1691 C  CD2 . PHE   A 1 219 ? -24.83447 -34.62661 13.14198  1.000 23.46779 ? 219 PHE   A CD2 1 
ATOM   1692 C  CE1 . PHE   A 1 219 ? -23.01673 -33.26924 14.71722  1.000 21.32165 ? 219 PHE   A CE1 1 
ATOM   1693 C  CE2 . PHE   A 1 219 ? -25.02222 -33.27272 13.41714  1.000 22.99466 ? 219 PHE   A CE2 1 
ATOM   1694 C  CZ  . PHE   A 1 219 ? -24.12467 -32.59840 14.21384  1.000 20.02708 ? 219 PHE   A CZ  1 
ATOM   1695 N  N   . LEU   A 1 220 ? -23.77403 -37.19293 16.79902  1.000 25.07115 ? 220 LEU   A N   1 
ATOM   1696 C  CA  . LEU   A 1 220 ? -23.02209 -37.21471 18.04076  1.000 27.87016 ? 220 LEU   A CA  1 
ATOM   1697 C  C   . LEU   A 1 220 ? -22.87240 -38.64374 18.54532  1.000 29.87922 ? 220 LEU   A C   1 
ATOM   1698 O  O   . LEU   A 1 220 ? -23.65644 -39.53919 18.22062  1.000 28.45573 ? 220 LEU   A O   1 
ATOM   1699 C  CB  . LEU   A 1 220 ? -23.71320 -36.36080 19.09897  1.000 26.19307 ? 220 LEU   A CB  1 
ATOM   1700 C  CG  . LEU   A 1 220 ? -23.74264 -34.89047 18.68508  1.000 24.61613 ? 220 LEU   A CG  1 
ATOM   1701 C  CD1 . LEU   A 1 220 ? -24.47066 -34.11149 19.73261  1.000 25.25676 ? 220 LEU   A CD1 1 
ATOM   1702 C  CD2 . LEU   A 1 220 ? -22.31640 -34.36247 18.47891  1.000 23.55503 ? 220 LEU   A CD2 1 
ATOM   1703 N  N   . ASN   A 1 221 ? -21.84004 -38.85999 19.34513  1.000 30.15506 ? 221 ASN   A N   1 
ATOM   1704 C  CA  . ASN   A 1 221 ? -21.68855 -40.15637 19.96901  1.000 34.01842 ? 221 ASN   A CA  1 
ATOM   1705 C  C   . ASN   A 1 221 ? -20.96098 -39.95223 21.28385  1.000 35.42220 ? 221 ASN   A C   1 
ATOM   1706 O  O   . ASN   A 1 221 ? -20.46598 -38.85839 21.57845  1.000 30.16593 ? 221 ASN   A O   1 
ATOM   1707 C  CB  . ASN   A 1 221 ? -20.94990 -41.13803 19.05259  1.000 36.02306 ? 221 ASN   A CB  1 
ATOM   1708 C  CG  . ASN   A 1 221 ? -19.92294 -40.45387 18.16927  1.000 39.75028 ? 221 ASN   A CG  1 
ATOM   1709 O  OD1 . ASN   A 1 221 ? -18.89318 -39.96640 18.65638  1.000 41.53253 ? 221 ASN   A OD1 1 
ATOM   1710 N  ND2 . ASN   A 1 221 ? -20.20730 -40.37958 16.87134  1.000 38.09521 ? 221 ASN   A ND2 1 
ATOM   1711 N  N   . ARG   A 1 222 ? -20.92439 -41.02830 22.07965  1.000 36.08502 ? 222 ARG   A N   1 
ATOM   1712 C  CA  . ARG   A 1 222 ? -20.20081 -41.05505 23.34347  1.000 41.15423 ? 222 ARG   A CA  1 
ATOM   1713 C  C   . ARG   A 1 222 ? -18.69804 -41.23815 23.16638  1.000 43.00853 ? 222 ARG   A C   1 
ATOM   1714 O  O   . ARG   A 1 222 ? -17.94268 -40.86668 24.06880  1.000 47.59240 ? 222 ARG   A O   1 
ATOM   1715 C  CB  . ARG   A 1 222 ? -20.73350 -42.17936 24.24142  1.000 40.16597 ? 222 ARG   A CB  1 
ATOM   1716 C  CG  . ARG   A 1 222 ? -20.13624 -43.54766 23.88923  1.000 44.66421 ? 222 ARG   A CG  1 
ATOM   1717 C  CD  . ARG   A 1 222 ? -20.83850 -44.69282 24.59566  1.000 42.66217 ? 222 ARG   A CD  1 
ATOM   1718 N  NE  . ARG   A 1 222 ? -20.41061 -44.81217 25.98510  1.000 53.16200 ? 222 ARG   A NE  1 
ATOM   1719 C  CZ  . ARG   A 1 222 ? -20.86679 -45.72093 26.83807  1.000 50.11078 ? 222 ARG   A CZ  1 
ATOM   1720 N  NH1 . ARG   A 1 222 ? -21.79445 -46.59955 26.48572  1.000 50.42207 ? 222 ARG   A NH1 1 
ATOM   1721 N  NH2 . ARG   A 1 222 ? -20.37859 -45.75200 28.07625  1.000 56.93379 ? 222 ARG   A NH2 1 
ATOM   1722 N  N   . PHE   A 1 223 ? -18.24535 -41.79228 22.03920  1.000 44.72375 ? 223 PHE   A N   1 
ATOM   1723 C  CA  . PHE   A 1 223 ? -16.81520 -41.95535 21.82038  1.000 43.69127 ? 223 PHE   A CA  1 
ATOM   1724 C  C   . PHE   A 1 223 ? -16.09433 -40.61123 21.84138  1.000 41.96562 ? 223 PHE   A C   1 
ATOM   1725 O  O   . PHE   A 1 223 ? -16.67566 -39.54064 21.63468  1.000 40.02389 ? 223 PHE   A O   1 
ATOM   1726 C  CB  . PHE   A 1 223 ? -16.50214 -42.63793 20.48127  1.000 42.74383 ? 223 PHE   A CB  1 
ATOM   1727 C  CG  . PHE   A 1 223 ? -17.55740 -43.58777 19.99992  1.000 46.66597 ? 223 PHE   A CG  1 
ATOM   1728 C  CD1 . PHE   A 1 223 ? -17.72848 -44.82354 20.60349  1.000 50.41126 ? 223 PHE   A CD1 1 
ATOM   1729 C  CD2 . PHE   A 1 223 ? -18.34529 -43.26617 18.90704  1.000 47.39932 ? 223 PHE   A CD2 1 
ATOM   1730 C  CE1 . PHE   A 1 223 ? -18.69415 -45.71201 20.14788  1.000 52.26155 ? 223 PHE   A CE1 1 
ATOM   1731 C  CE2 . PHE   A 1 223 ? -19.31977 -44.14382 18.44920  1.000 48.68209 ? 223 PHE   A CE2 1 
ATOM   1732 C  CZ  . PHE   A 1 223 ? -19.49300 -45.36986 19.06858  1.000 52.42240 ? 223 PHE   A CZ  1 
ATOM   1733 N  N   . THR   A 1 224 ? -14.79924 -40.69136 22.09972  1.000 40.18393 ? 224 THR   A N   1 
ATOM   1734 C  CA  . THR   A 1 224 ? -13.85170 -39.61429 21.89358  1.000 39.13186 ? 224 THR   A CA  1 
ATOM   1735 C  C   . THR   A 1 224 ? -12.69223 -40.16047 21.07209  1.000 40.70154 ? 224 THR   A C   1 
ATOM   1736 O  O   . THR   A 1 224 ? -12.64019 -41.35023 20.73527  1.000 42.06181 ? 224 THR   A O   1 
ATOM   1737 C  CB  . THR   A 1 224 ? -13.36663 -39.03387 23.23046  1.000 41.55713 ? 224 THR   A CB  1 
ATOM   1738 O  OG1 . THR   A 1 224 ? -12.94011 -37.67464 23.04630  1.000 37.38044 ? 224 THR   A OG1 1 
ATOM   1739 C  CG2 . THR   A 1 224 ? -12.24429 -39.88281 23.83755  1.000 43.08735 ? 224 THR   A CG2 1 
ATOM   1740 N  N   . THR   A 1 225 ? -11.75428 -39.28313 20.74520  1.000 36.96835 ? 225 THR   A N   1 
ATOM   1741 C  CA  . THR   A 1 225 ? -10.54979 -39.70364 20.05395  1.000 40.49777 ? 225 THR   A CA  1 
ATOM   1742 C  C   . THR   A 1 225 ? -9.44434  -38.72464 20.41245  1.000 38.49572 ? 225 THR   A C   1 
ATOM   1743 O  O   . THR   A 1 225 ? -9.70079  -37.58866 20.82214  1.000 38.73596 ? 225 THR   A O   1 
ATOM   1744 C  CB  . THR   A 1 225 ? -10.76875 -39.78195 18.52972  1.000 40.42332 ? 225 THR   A CB  1 
ATOM   1745 O  OG1 . THR   A 1 225 ? -9.67754  -40.47905 17.91289  1.000 40.69800 ? 225 THR   A OG1 1 
ATOM   1746 C  CG2 . THR   A 1 225 ? -10.87629 -38.39217 17.92355  1.000 35.65349 ? 225 THR   A CG2 1 
ATOM   1747 N  N   . THR   A 1 226 ? -8.20965  -39.18784 20.28917  1.000 40.09812 ? 226 THR   A N   1 
ATOM   1748 C  CA  . THR   A 1 226 ? -7.08984  -38.28405 20.46239  1.000 39.17265 ? 226 THR   A CA  1 
ATOM   1749 C  C   . THR   A 1 226 ? -6.88469  -37.46753 19.19398  1.000 35.60050 ? 226 THR   A C   1 
ATOM   1750 O  O   . THR   A 1 226 ? -7.30870  -37.85124 18.09981  1.000 33.91340 ? 226 THR   A O   1 
ATOM   1751 C  CB  . THR   A 1 226 ? -5.81960  -39.05770 20.80550  1.000 39.83630 ? 226 THR   A CB  1 
ATOM   1752 O  OG1 . THR   A 1 226 ? -5.47158  -39.89483 19.69981  1.000 41.47941 ? 226 THR   A OG1 1 
ATOM   1753 C  CG2 . THR   A 1 226 ? -6.05604  -39.93224 22.02174  1.000 40.45058 ? 226 THR   A CG2 1 
ATOM   1754 N  N   . LEU   A 1 227 ? -6.23196  -36.31870 19.36004  1.000 34.31500 ? 227 LEU   A N   1 
ATOM   1755 C  CA  . LEU   A 1 227 ? -5.90523  -35.47718 18.21769  1.000 36.67237 ? 227 LEU   A CA  1 
ATOM   1756 C  C   . LEU   A 1 227 ? -5.11133  -36.25780 17.17057  1.000 38.27858 ? 227 LEU   A C   1 
ATOM   1757 O  O   . LEU   A 1 227 ? -5.44567  -36.23691 15.97952  1.000 34.68296 ? 227 LEU   A O   1 
ATOM   1758 C  CB  . LEU   A 1 227 ? -5.12553  -34.25579 18.69580  1.000 34.94123 ? 227 LEU   A CB  1 
ATOM   1759 C  CG  . LEU   A 1 227 ? -4.90813  -33.12166 17.70391  1.000 33.53765 ? 227 LEU   A CG  1 
ATOM   1760 C  CD1 . LEU   A 1 227 ? -6.14205  -32.94445 16.81695  1.000 31.74996 ? 227 LEU   A CD1 1 
ATOM   1761 C  CD2 . LEU   A 1 227 ? -4.54728  -31.83103 18.41900  1.000 32.09766 ? 227 LEU   A CD2 1 
ATOM   1762 N  N   . ASN   A 1 228 ? -4.06301  -36.97190 17.60394  1.000 37.31347 ? 228 ASN   A N   1 
ATOM   1763 C  CA  . ASN   A 1 228 ? -3.25344  -37.76294 16.67645  1.000 40.11796 ? 228 ASN   A CA  1 
ATOM   1764 C  C   . ASN   A 1 228 ? -4.09197  -38.80378 15.94255  1.000 39.62379 ? 228 ASN   A C   1 
ATOM   1765 O  O   . ASN   A 1 228 ? -4.00241  -38.93659 14.71445  1.000 38.99565 ? 228 ASN   A O   1 
ATOM   1766 C  CB  . ASN   A 1 228 ? -2.09423  -38.43807 17.41905  1.000 40.36665 ? 228 ASN   A CB  1 
ATOM   1767 C  CG  . ASN   A 1 228 ? -1.19120  -37.43999 18.11961  1.000 43.47274 ? 228 ASN   A CG  1 
ATOM   1768 O  OD1 . ASN   A 1 228 ? -1.04811  -36.29569 17.67482  1.000 44.85316 ? 228 ASN   A OD1 1 
ATOM   1769 N  ND2 . ASN   A 1 228 ? -0.56698  -37.86801 19.21179  1.000 48.29495 ? 228 ASN   A ND2 1 
ATOM   1770 N  N   . ASP   A 1 229 ? -4.91717  -39.55393 16.67899  1.000 40.23488 ? 229 ASP   A N   1 
ATOM   1771 C  CA  . ASP   A 1 229 ? -5.73872  -40.57541 16.03751  1.000 38.65381 ? 229 ASP   A CA  1 
ATOM   1772 C  C   . ASP   A 1 229 ? -6.77039  -39.96442 15.08817  1.000 39.26784 ? 229 ASP   A C   1 
ATOM   1773 O  O   . ASP   A 1 229 ? -7.03892  -40.53574 14.02295  1.000 37.83644 ? 229 ASP   A O   1 
ATOM   1774 C  CB  . ASP   A 1 229 ? -6.41150  -41.46096 17.09482  1.000 41.18466 ? 229 ASP   A CB  1 
ATOM   1775 C  CG  . ASP   A 1 229 ? -5.43039  -42.42163 17.77797  1.000 46.16195 ? 229 ASP   A CG  1 
ATOM   1776 O  OD1 . ASP   A 1 229 ? -4.52950  -41.97641 18.53270  1.000 48.82027 ? 229 ASP   A OD1 1 
ATOM   1777 O  OD2 . ASP   A 1 229 ? -5.55995  -43.63741 17.54411  1.000 48.71535 ? 229 ASP   A OD2 1 
ATOM   1778 N  N   . PHE   A 1 230 ? -7.34632  -38.80611 15.42668  1.000 34.55841 ? 230 PHE   A N   1 
ATOM   1779 C  CA  . PHE   A 1 230 ? -8.20570  -38.14390 14.44934  1.000 35.78385 ? 230 PHE   A CA  1 
ATOM   1780 C  C   . PHE   A 1 230 ? -7.42098  -37.77633 13.19833  1.000 34.13144 ? 230 PHE   A C   1 
ATOM   1781 O  O   . PHE   A 1 230 ? -7.89546  -37.98134 12.07469  1.000 34.12149 ? 230 PHE   A O   1 
ATOM   1782 C  CB  . PHE   A 1 230 ? -8.85699  -36.88876 15.02535  1.000 31.88293 ? 230 PHE   A CB  1 
ATOM   1783 C  CG  . PHE   A 1 230 ? -9.64700  -36.11778 14.00286  1.000 32.88005 ? 230 PHE   A CG  1 
ATOM   1784 C  CD1 . PHE   A 1 230 ? -10.91081 -36.54860 13.61564  1.000 27.29252 ? 230 PHE   A CD1 1 
ATOM   1785 C  CD2 . PHE   A 1 230 ? -9.10396  -34.99945 13.38034  1.000 31.42733 ? 230 PHE   A CD2 1 
ATOM   1786 C  CE1 . PHE   A 1 230 ? -11.63206 -35.85184 12.65578  1.000 27.70165 ? 230 PHE   A CE1 1 
ATOM   1787 C  CE2 . PHE   A 1 230 ? -9.81913  -34.30939 12.42268  1.000 30.21240 ? 230 PHE   A CE2 1 
ATOM   1788 C  CZ  . PHE   A 1 230 ? -11.07787 -34.73400 12.06103  1.000 27.13991 ? 230 PHE   A CZ  1 
ATOM   1789 N  N   . ASN   A 1 231 ? -6.21485  -37.23466 13.37353  1.000 34.73108 ? 231 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 231 ? -5.46204  -36.74113 12.22620  1.000 36.32662 ? 231 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 231 ? -5.01655  -37.87689 11.31937  1.000 35.49098 ? 231 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 231 ? -4.84383  -37.67027 10.11472  1.000 35.94566 ? 231 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 231 ? -4.26868  -35.90975 12.69456  1.000 32.87141 ? 231 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 231 ? -4.65571  -34.47402 12.96884  1.000 32.73794 ? 231 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 231 ? -5.42052  -33.89557 12.21552  1.000 35.18934 ? 231 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 231 ? -4.13350  -33.89379 14.04383  1.000 32.97215 ? 231 ASN   A ND2 1 
ATOM   1797 N  N   . LEU   A 1 232 ? -4.83738  -39.07710 11.86969  1.000 36.01924 ? 232 LEU   A N   1 
ATOM   1798 C  CA  . LEU   A 1 232 ? -4.62589  -40.23932 11.01887  1.000 36.54922 ? 232 LEU   A CA  1 
ATOM   1799 C  C   . LEU   A 1 232 ? -5.81379  -40.44673 10.09856  1.000 37.98150 ? 232 LEU   A C   1 
ATOM   1800 O  O   . LEU   A 1 232 ? -5.64466  -40.81242 8.93152   1.000 39.07663 ? 232 LEU   A O   1 
ATOM   1801 C  CB  . LEU   A 1 232 ? -4.38343  -41.48653 11.86692  1.000 36.93653 ? 232 LEU   A CB  1 
ATOM   1802 C  CG  . LEU   A 1 232 ? -3.08779  -41.52020 12.68215  1.000 40.97528 ? 232 LEU   A CG  1 
ATOM   1803 C  CD1 . LEU   A 1 232 ? -2.86130  -42.89663 13.27344  1.000 40.63899 ? 232 LEU   A CD1 1 
ATOM   1804 C  CD2 . LEU   A 1 232 ? -1.89954  -41.10314 11.82042  1.000 40.86740 ? 232 LEU   A CD2 1 
ATOM   1805 N  N   . VAL   A 1 233 ? -7.02721  -40.20094 10.60069  1.000 36.18816 ? 233 VAL   A N   1 
ATOM   1806 C  CA  . VAL   A 1 233 ? -8.21488  -40.38044 9.77381   1.000 35.40553 ? 233 VAL   A CA  1 
ATOM   1807 C  C   . VAL   A 1 233 ? -8.37225  -39.21702 8.80331   1.000 36.36867 ? 233 VAL   A C   1 
ATOM   1808 O  O   . VAL   A 1 233 ? -8.72282  -39.41211 7.63240   1.000 35.31750 ? 233 VAL   A O   1 
ATOM   1809 C  CB  . VAL   A 1 233 ? -9.45609  -40.55906 10.66845  1.000 37.43908 ? 233 VAL   A CB  1 
ATOM   1810 C  CG1 . VAL   A 1 233 ? -10.71784 -40.07802 9.95793   1.000 37.83124 ? 233 VAL   A CG1 1 
ATOM   1811 C  CG2 . VAL   A 1 233 ? -9.58467  -42.00215 11.11697  1.000 38.45967 ? 233 VAL   A CG2 1 
ATOM   1812 N  N   . ALA   A 1 234 ? -8.11540  -37.99258 9.27179   1.000 37.49692 ? 234 ALA   A N   1 
ATOM   1813 C  CA  . ALA   A 1 234 ? -8.18876  -36.82455 8.40121   1.000 34.24653 ? 234 ALA   A CA  1 
ATOM   1814 C  C   . ALA   A 1 234 ? -7.29605  -37.00383 7.18294   1.000 33.19174 ? 234 ALA   A C   1 
ATOM   1815 O  O   . ALA   A 1 234 ? -7.71920  -36.77159 6.04523   1.000 30.92955 ? 234 ALA   A O   1 
ATOM   1816 C  CB  . ALA   A 1 234 ? -7.79261  -35.56401 9.17599   1.000 32.83276 ? 234 ALA   A CB  1 
ATOM   1817 N  N   . MET   A 1 235 ? -6.05712  -37.44540 7.40847   1.000 34.55911 ? 235 MET   A N   1 
ATOM   1818 C  CA  . MET   A 1 235 ? -5.13701  -37.66147 6.29976   1.000 35.86287 ? 235 MET   A CA  1 
ATOM   1819 C  C   . MET   A 1 235 ? -5.72892  -38.63127 5.28354   1.000 36.25446 ? 235 MET   A C   1 
ATOM   1820 O  O   . MET   A 1 235 ? -5.67703  -38.38179 4.07333   1.000 35.13930 ? 235 MET   A O   1 
ATOM   1821 C  CB  . MET   A 1 235 ? -3.79992  -38.17349 6.83255   1.000 37.02484 ? 235 MET   A CB  1 
ATOM   1822 C  CG  . MET   A 1 235 ? -2.71021  -38.33688 5.77929   1.000 40.14152 ? 235 MET   A CG  1 
ATOM   1823 S  SD  . MET   A 1 235 ? -1.06205  -37.92790 6.41687   1.000 53.82997 ? 235 MET   A SD  1 
ATOM   1824 C  CE  . MET   A 1 235 ? -1.20810  -38.38678 8.15182   1.000 43.12329 ? 235 MET   A CE  1 
ATOM   1825 N  N   . LYS   A 1 236 ? -6.34834  -39.71695 5.76178   1.000 36.42540 ? 236 LYS   A N   1 
ATOM   1826 C  CA  . LYS   A 1 236 ? -6.84398  -40.74628 4.85405   1.000 33.12069 ? 236 LYS   A CA  1 
ATOM   1827 C  C   . LYS   A 1 236 ? -7.96100  -40.23059 3.96315   1.000 32.79340 ? 236 LYS   A C   1 
ATOM   1828 O  O   . LYS   A 1 236 ? -8.10030  -40.69408 2.82932   1.000 34.88453 ? 236 LYS   A O   1 
ATOM   1829 C  CB  . LYS   A 1 236 ? -7.31693  -41.97399 5.63570   1.000 34.20530 ? 236 LYS   A CB  1 
ATOM   1830 C  CG  . LYS   A 1 236 ? -6.25494  -42.62651 6.52487   1.000 42.53762 ? 236 LYS   A CG  1 
ATOM   1831 C  CD  . LYS   A 1 236 ? -4.81101  -42.36867 6.03013   1.000 44.15246 ? 236 LYS   A CD  1 
ATOM   1832 C  CE  . LYS   A 1 236 ? -3.77835  -42.85851 7.03159   1.000 43.01269 ? 236 LYS   A CE  1 
ATOM   1833 N  NZ  . LYS   A 1 236 ? -3.48202  -41.81246 8.04410   1.000 40.56513 ? 236 LYS   A NZ  1 
ATOM   1834 N  N   . TYR   A 1 237 ? -8.76203  -39.27859 4.44366   1.000 31.55722 ? 237 TYR   A N   1 
ATOM   1835 C  CA  . TYR   A 1 237 ? -9.87628  -38.73710 3.67556   1.000 29.73511 ? 237 TYR   A CA  1 
ATOM   1836 C  C   . TYR   A 1 237 ? -9.57369  -37.36386 3.10250   1.000 27.35612 ? 237 TYR   A C   1 
ATOM   1837 O  O   . TYR   A 1 237 ? -10.50360 -36.60586 2.82163   1.000 25.68656 ? 237 TYR   A O   1 
ATOM   1838 C  CB  . TYR   A 1 237 ? -11.14256 -38.67351 4.53307   1.000 28.61533 ? 237 TYR   A CB  1 
ATOM   1839 C  CG  . TYR   A 1 237 ? -11.67624 -40.04657 4.86056   1.000 31.19531 ? 237 TYR   A CG  1 
ATOM   1840 C  CD1 . TYR   A 1 237 ? -11.15767 -40.76798 5.93071   1.000 31.63516 ? 237 TYR   A CD1 1 
ATOM   1841 C  CD2 . TYR   A 1 237 ? -12.68419 -40.62778 4.09759   1.000 31.35520 ? 237 TYR   A CD2 1 
ATOM   1842 C  CE1 . TYR   A 1 237 ? -11.62583 -42.03054 6.23913   1.000 30.93073 ? 237 TYR   A CE1 1 
ATOM   1843 C  CE2 . TYR   A 1 237 ? -13.16301 -41.89707 4.40024   1.000 29.68582 ? 237 TYR   A CE2 1 
ATOM   1844 C  CZ  . TYR   A 1 237 ? -12.62487 -42.58816 5.47436   1.000 31.38481 ? 237 TYR   A CZ  1 
ATOM   1845 O  OH  . TYR   A 1 237 ? -13.08345 -43.84167 5.79643   1.000 33.49699 ? 237 TYR   A OH  1 
ATOM   1846 N  N   . ASN   A 1 238 ? -8.29740  -37.02479 2.92671   1.000 27.93402 ? 238 ASN   A N   1 
ATOM   1847 C  CA  . ASN   A 1 238 ? -7.93401  -35.76996 2.27633   1.000 27.03855 ? 238 ASN   A CA  1 
ATOM   1848 C  C   . ASN   A 1 238 ? -8.46036  -34.55641 3.04583   1.000 26.39050 ? 238 ASN   A C   1 
ATOM   1849 O  O   . ASN   A 1 238 ? -8.82513  -33.53697 2.45726   1.000 26.22598 ? 238 ASN   A O   1 
ATOM   1850 C  CB  . ASN   A 1 238 ? -8.43552  -35.74160 0.83186   1.000 27.60122 ? 238 ASN   A CB  1 
ATOM   1851 C  CG  . ASN   A 1 238 ? -7.75588  -34.68001 0.00967   1.000 31.08767 ? 238 ASN   A CG  1 
ATOM   1852 O  OD1 . ASN   A 1 238 ? -8.29835  -34.19632 -0.98853  1.000 34.93696 ? 238 ASN   A OD1 1 
ATOM   1853 N  ND2 . ASN   A 1 238 ? -6.55495  -34.31136 0.42090   1.000 29.43759 ? 238 ASN   A ND2 1 
ATOM   1854 N  N   . TYR   A 1 239 ? -8.52825  -34.66304 4.36370   1.000 26.68222 ? 239 TYR   A N   1 
ATOM   1855 C  CA  . TYR   A 1 239 ? -8.81939  -33.53754 5.23427   1.000 25.98834 ? 239 TYR   A CA  1 
ATOM   1856 C  C   . TYR   A 1 239 ? -7.49995  -32.97866 5.74325   1.000 26.24322 ? 239 TYR   A C   1 
ATOM   1857 O  O   . TYR   A 1 239 ? -6.54234  -33.71949 5.95124   1.000 24.56517 ? 239 TYR   A O   1 
ATOM   1858 C  CB  . TYR   A 1 239 ? -9.68456  -33.96796 6.42003   1.000 23.69403 ? 239 TYR   A CB  1 
ATOM   1859 C  CG  . TYR   A 1 239 ? -11.17561 -33.94121 6.17909   1.000 21.88643 ? 239 TYR   A CG  1 
ATOM   1860 C  CD1 . TYR   A 1 239 ? -11.73814 -34.58963 5.08940   1.000 23.96930 ? 239 TYR   A CD1 1 
ATOM   1861 C  CD2 . TYR   A 1 239 ? -12.01724 -33.27832 7.05580   1.000 22.57392 ? 239 TYR   A CD2 1 
ATOM   1862 C  CE1 . TYR   A 1 239 ? -13.10525 -34.57559 4.87844   1.000 23.90787 ? 239 TYR   A CE1 1 
ATOM   1863 C  CE2 . TYR   A 1 239 ? -13.38753 -33.25594 6.86310   1.000 22.25081 ? 239 TYR   A CE2 1 
ATOM   1864 C  CZ  . TYR   A 1 239 ? -13.92389 -33.90722 5.77337   1.000 22.98375 ? 239 TYR   A CZ  1 
ATOM   1865 O  OH  . TYR   A 1 239 ? -15.27499 -33.88405 5.56569   1.000 21.98062 ? 239 TYR   A OH  1 
ATOM   1866 N  N   . GLU   A 1 240 ? -7.44247  -31.68067 5.95003   1.000 24.98527 ? 240 GLU   A N   1 
ATOM   1867 C  CA  . GLU   A 1 240 ? -6.16285  -31.19925 6.42766   1.000 27.98426 ? 240 GLU   A CA  1 
ATOM   1868 C  C   . GLU   A 1 240 ? -6.02831  -31.43600 7.92365   1.000 29.68275 ? 240 GLU   A C   1 
ATOM   1869 O  O   . GLU   A 1 240 ? -7.01738  -31.68879 8.61956   1.000 26.80242 ? 240 GLU   A O   1 
ATOM   1870 C  CB  . GLU   A 1 240 ? -5.95728  -29.74083 6.05578   1.000 29.20174 ? 240 GLU   A CB  1 
ATOM   1871 C  CG  . GLU   A 1 240 ? -7.15608  -28.94517 5.89925   1.000 27.44268 ? 240 GLU   A CG  1 
ATOM   1872 C  CD  . GLU   A 1 240 ? -6.82826  -27.49036 5.68070   1.000 32.14529 ? 240 GLU   A CD  1 
ATOM   1873 O  OE1 . GLU   A 1 240 ? -7.54661  -26.63096 6.25013   1.000 30.88525 ? 240 GLU   A OE1 1 
ATOM   1874 O  OE2 . GLU   A 1 240 ? -5.84167  -27.21285 4.94990   1.000 34.83310 ? 240 GLU   A OE2 1 
ATOM   1875 N  N   . PRO   A 1 241 ? -4.79983  -31.45125 8.42928   1.000 28.82252 ? 241 PRO   A N   1 
ATOM   1876 C  CA  . PRO   A 1 241 ? -4.60645  -31.81215 9.82944   1.000 30.42062 ? 241 PRO   A CA  1 
ATOM   1877 C  C   . PRO   A 1 241 ? -5.28281  -30.81038 10.74802  1.000 28.86088 ? 241 PRO   A C   1 
ATOM   1878 O  O   . PRO   A 1 241 ? -5.39440  -29.62028 10.44782  1.000 29.78684 ? 241 PRO   A O   1 
ATOM   1879 C  CB  . PRO   A 1 241 ? -3.08310  -31.79919 9.99654   1.000 29.00423 ? 241 PRO   A CB  1 
ATOM   1880 C  CG  . PRO   A 1 241 ? -2.55718  -32.02825 8.62581   1.000 31.23563 ? 241 PRO   A CG  1 
ATOM   1881 C  CD  . PRO   A 1 241 ? -3.51581  -31.33094 7.71194   1.000 30.88444 ? 241 PRO   A CD  1 
ATOM   1882 N  N   . LEU   A 1 242 ? -5.76940  -31.32004 11.86868  1.000 29.79804 ? 242 LEU   A N   1 
ATOM   1883 C  CA  . LEU   A 1 242 ? -6.30299  -30.47168 12.91965  1.000 28.70028 ? 242 LEU   A CA  1 
ATOM   1884 C  C   . LEU   A 1 242 ? -5.19111  -30.16944 13.91232  1.000 28.90220 ? 242 LEU   A C   1 
ATOM   1885 O  O   . LEU   A 1 242 ? -4.46614  -31.07200 14.32745  1.000 26.75007 ? 242 LEU   A O   1 
ATOM   1886 C  CB  . LEU   A 1 242 ? -7.47141  -31.15453 13.62359  1.000 28.73926 ? 242 LEU   A CB  1 
ATOM   1887 C  CG  . LEU   A 1 242 ? -8.35780  -30.18562 14.37411  1.000 26.02544 ? 242 LEU   A CG  1 
ATOM   1888 C  CD1 . LEU   A 1 242 ? -9.10501  -29.32958 13.38012  1.000 24.13746 ? 242 LEU   A CD1 1 
ATOM   1889 C  CD2 . LEU   A 1 242 ? -9.29638  -30.99428 15.22828  1.000 26.28388 ? 242 LEU   A CD2 1 
ATOM   1890 N  N   . THR   A 1 243 ? -5.04693  -28.90219 14.27148  1.000 28.30674 ? 243 THR   A N   1 
ATOM   1891 C  CA  . THR   A 1 243 ? -4.00477  -28.48841 15.19348  1.000 28.59101 ? 243 THR   A CA  1 
ATOM   1892 C  C   . THR   A 1 243 ? -4.61872  -28.08911 16.52308  1.000 30.63739 ? 243 THR   A C   1 
ATOM   1893 O  O   . THR   A 1 243 ? -5.82986  -27.85650 16.63375  1.000 27.51496 ? 243 THR   A O   1 
ATOM   1894 C  CB  . THR   A 1 243 ? -3.19913  -27.31491 14.63136  1.000 29.57437 ? 243 THR   A CB  1 
ATOM   1895 O  OG1 . THR   A 1 243 ? -4.03045  -26.14538 14.59470  1.000 27.88621 ? 243 THR   A OG1 1 
ATOM   1896 C  CG2 . THR   A 1 243 ? -2.67789  -27.63923 13.23426  1.000 28.66462 ? 243 THR   A CG2 1 
ATOM   1897 N  N   . GLN   A 1 244 ? -3.75532  -28.00278 17.53642  1.000 24.61037 ? 244 GLN   A N   1 
ATOM   1898 C  CA  . GLN   A 1 244 ? -4.19946  -27.51066 18.83253  1.000 28.13719 ? 244 GLN   A CA  1 
ATOM   1899 C  C   . GLN   A 1 244 ? -4.79007  -26.11605 18.72746  1.000 30.86455 ? 244 GLN   A C   1 
ATOM   1900 O  O   . GLN   A 1 244 ? -5.71674  -25.78248 19.47688  1.000 30.52733 ? 244 GLN   A O   1 
ATOM   1901 C  CB  . GLN   A 1 244 ? -3.04622  -27.50877 19.82947  1.000 28.01247 ? 244 GLN   A CB  1 
ATOM   1902 C  CG  . GLN   A 1 244 ? -3.47810  -27.23290 21.26781  1.000 31.68094 ? 244 GLN   A CG  1 
ATOM   1903 C  CD  . GLN   A 1 244 ? -4.67617  -28.05398 21.68889  1.000 32.42948 ? 244 GLN   A CD  1 
ATOM   1904 O  OE1 . GLN   A 1 244 ? -4.66443  -29.28474 21.58855  1.000 31.11869 ? 244 GLN   A OE1 1 
ATOM   1905 N  NE2 . GLN   A 1 244 ? -5.71122  -27.38128 22.18942  1.000 34.21268 ? 244 GLN   A NE2 1 
ATOM   1906 N  N   . ASP   A 1 245 ? -4.27976  -25.28517 17.80786  1.000 28.83097 ? 245 ASP   A N   1 
ATOM   1907 C  CA  . ASP   A 1 245 ? -4.85335  -23.95124 17.67016  1.000 30.58192 ? 245 ASP   A CA  1 
ATOM   1908 C  C   . ASP   A 1 245 ? -6.29045  -24.02600 17.17062  1.000 28.01818 ? 245 ASP   A C   1 
ATOM   1909 O  O   . ASP   A 1 245 ? -7.15679  -23.28199 17.64712  1.000 27.62241 ? 245 ASP   A O   1 
ATOM   1910 C  CB  . ASP   A 1 245 ? -4.02362  -23.07749 16.73449  1.000 29.06829 ? 245 ASP   A CB  1 
ATOM   1911 C  CG  . ASP   A 1 245 ? -4.41933  -21.61178 16.83575  1.000 34.59924 ? 245 ASP   A CG  1 
ATOM   1912 O  OD1 . ASP   A 1 245 ? -4.65687  -21.15852 17.98268  1.000 36.65292 ? 245 ASP   A OD1 1 
ATOM   1913 O  OD2 . ASP   A 1 245 ? -4.53354  -20.92286 15.79203  1.000 38.20585 ? 245 ASP   A OD2 1 
ATOM   1914 N  N   . HIS   A 1 246 ? -6.55315  -24.91053 16.20299  1.000 28.15800 ? 246 HIS   A N   1 
ATOM   1915 C  CA  . HIS   A 1 246 ? -7.92468  -25.19298 15.78150  1.000 27.21848 ? 246 HIS   A CA  1 
ATOM   1916 C  C   . HIS   A 1 246 ? -8.78353  -25.63477 16.95532  1.000 26.12956 ? 246 HIS   A C   1 
ATOM   1917 O  O   . HIS   A 1 246 ? -9.93357  -25.20014 17.10241  1.000 26.68839 ? 246 HIS   A O   1 
ATOM   1918 C  CB  . HIS   A 1 246 ? -7.93250  -26.28501 14.71784  1.000 26.45445 ? 246 HIS   A CB  1 
ATOM   1919 C  CG  . HIS   A 1 246 ? -7.25956  -25.89994 13.44195  1.000 23.83726 ? 246 HIS   A CG  1 
ATOM   1920 N  ND1 . HIS   A 1 246 ? -6.56791  -26.80683 12.66829  1.000 24.51803 ? 246 HIS   A ND1 1 
ATOM   1921 C  CD2 . HIS   A 1 246 ? -7.17168  -24.71053 12.80171  1.000 26.11407 ? 246 HIS   A CD2 1 
ATOM   1922 C  CE1 . HIS   A 1 246 ? -6.09011  -26.19384 11.59905  1.000 27.44132 ? 246 HIS   A CE1 1 
ATOM   1923 N  NE2 . HIS   A 1 246 ? -6.45107  -24.92257 11.65114  1.000 25.95522 ? 246 HIS   A NE2 1 
ATOM   1924 N  N   . VAL   A 1 247 ? -8.26123  -26.54904 17.77176  1.000 28.20864 ? 247 VAL   A N   1 
ATOM   1925 C  CA  . VAL   A 1 247 ? -9.00052  -26.99209 18.94778  1.000 27.19314 ? 247 VAL   A CA  1 
ATOM   1926 C  C   . VAL   A 1 247 ? -9.30553  -25.80227 19.84549  1.000 30.04811 ? 247 VAL   A C   1 
ATOM   1927 O  O   . VAL   A 1 247 ? -10.42592 -25.65387 20.35325  1.000 29.13955 ? 247 VAL   A O   1 
ATOM   1928 C  CB  . VAL   A 1 247 ? -8.20768  -28.08458 19.68947  1.000 27.28100 ? 247 VAL   A CB  1 
ATOM   1929 C  CG1 . VAL   A 1 247 ? -8.84885  -28.39098 21.02106  1.000 29.05321 ? 247 VAL   A CG1 1 
ATOM   1930 C  CG2 . VAL   A 1 247 ? -8.10658  -29.32849 18.83214  1.000 26.17132 ? 247 VAL   A CG2 1 
ATOM   1931 N  N   . ASP   A 1 248 ? -8.32266  -24.91829 20.02723  1.000 27.73215 ? 248 ASP   A N   1 
ATOM   1932 C  CA  . ASP   A 1 248 ? -8.53416  -23.74055 20.86076  1.000 28.74854 ? 248 ASP   A CA  1 
ATOM   1933 C  C   . ASP   A 1 248 ? -9.56969  -22.81612 20.23386  1.000 28.08905 ? 248 ASP   A C   1 
ATOM   1934 O  O   . ASP   A 1 248 ? -10.46232 -22.30632 20.91998  1.000 27.42358 ? 248 ASP   A O   1 
ATOM   1935 C  CB  . ASP   A 1 248 ? -7.20716  -22.99900 21.07021  1.000 29.39204 ? 248 ASP   A CB  1 
ATOM   1936 C  CG  . ASP   A 1 248 ? -6.18661  -23.81657 21.85390  1.000 31.34028 ? 248 ASP   A CG  1 
ATOM   1937 O  OD1 . ASP   A 1 248 ? -6.57720  -24.78884 22.53560  1.000 35.19788 ? 248 ASP   A OD1 1 
ATOM   1938 O  OD2 . ASP   A 1 248 ? -4.98368  -23.47955 21.78693  1.000 30.30166 ? 248 ASP   A OD2 1 
ATOM   1939 N  N   . ILE   A 1 249 ? -9.46412  -22.58737 18.92179  1.000 27.91952 ? 249 ILE   A N   1 
ATOM   1940 C  CA  . ILE   A 1 249 ? -10.42834 -21.74490 18.21355  1.000 28.11570 ? 249 ILE   A CA  1 
ATOM   1941 C  C   . ILE   A 1 249 ? -11.83918 -22.30731 18.34526  1.000 26.95420 ? 249 ILE   A C   1 
ATOM   1942 O  O   . ILE   A 1 249 ? -12.82399 -21.55746 18.35180  1.000 26.21659 ? 249 ILE   A O   1 
ATOM   1943 C  CB  . ILE   A 1 249 ? -9.99608  -21.60321 16.73633  1.000 25.83848 ? 249 ILE   A CB  1 
ATOM   1944 C  CG1 . ILE   A 1 249 ? -8.78785  -20.67555 16.62813  1.000 29.83236 ? 249 ILE   A CG1 1 
ATOM   1945 C  CG2 . ILE   A 1 249 ? -11.10773 -21.10060 15.87226  1.000 26.81964 ? 249 ILE   A CG2 1 
ATOM   1946 C  CD1 . ILE   A 1 249 ? -7.93567  -20.94275 15.39869  1.000 29.51824 ? 249 ILE   A CD1 1 
ATOM   1947 N  N   . LEU   A 1 250 ? -11.96009 -23.62305 18.47566  1.000 24.97233 ? 250 LEU   A N   1 
ATOM   1948 C  CA  . LEU   A 1 250 ? -13.25282 -24.26811 18.59768  1.000 25.61625 ? 250 LEU   A CA  1 
ATOM   1949 C  C   . LEU   A 1 250 ? -13.75845 -24.29530 20.03259  1.000 27.22527 ? 250 LEU   A C   1 
ATOM   1950 O  O   . LEU   A 1 250 ? -14.89387 -24.71612 20.25953  1.000 26.29542 ? 250 LEU   A O   1 
ATOM   1951 C  CB  . LEU   A 1 250 ? -13.16910 -25.68896 18.04333  1.000 25.21963 ? 250 LEU   A CB  1 
ATOM   1952 C  CG  . LEU   A 1 250 ? -12.98932 -25.80931 16.53485  1.000 23.35710 ? 250 LEU   A CG  1 
ATOM   1953 C  CD1 . LEU   A 1 250 ? -12.64511 -27.24620 16.19777  1.000 22.50180 ? 250 LEU   A CD1 1 
ATOM   1954 C  CD2 . LEU   A 1 250 ? -14.28029 -25.40090 15.85595  1.000 20.06742 ? 250 LEU   A CD2 1 
ATOM   1955 N  N   . GLY   A 1 251 ? -12.94276 -23.84887 20.99196  1.000 28.69329 ? 251 GLY   A N   1 
ATOM   1956 C  CA  . GLY   A 1 251 ? -13.29178 -23.82118 22.39184  1.000 28.01266 ? 251 GLY   A CA  1 
ATOM   1957 C  C   . GLY   A 1 251 ? -14.63852 -23.19919 22.70156  1.000 30.20033 ? 251 GLY   A C   1 
ATOM   1958 O  O   . GLY   A 1 251 ? -15.47824 -23.81202 23.37158  1.000 30.82625 ? 251 GLY   A O   1 
ATOM   1959 N  N   . PRO   A 1 252 ? -14.86476 -21.95664 22.25056  1.000 28.48195 ? 252 PRO   A N   1 
ATOM   1960 C  CA  . PRO   A 1 252 ? -16.17066 -21.32262 22.50130  1.000 30.31784 ? 252 PRO   A CA  1 
ATOM   1961 C  C   . PRO   A 1 252 ? -17.34747 -22.15695 22.02492  1.000 29.53122 ? 252 PRO   A C   1 
ATOM   1962 O  O   . PRO   A 1 252 ? -18.32628 -22.32113 22.76897  1.000 30.68216 ? 252 PRO   A O   1 
ATOM   1963 C  CB  . PRO   A 1 252 ? -16.05875 -19.99749 21.73324  1.000 30.24363 ? 252 PRO   A CB  1 
ATOM   1964 C  CG  . PRO   A 1 252 ? -14.60418 -19.67928 21.77310  1.000 29.01310 ? 252 PRO   A CG  1 
ATOM   1965 C  CD  . PRO   A 1 252 ? -13.90008 -21.00559 21.66483  1.000 29.06886 ? 252 PRO   A CD  1 
ATOM   1966 N  N   . LEU   A 1 253 ? -17.26658 -22.70012 20.80720  1.000 28.30715 ? 253 LEU   A N   1 
ATOM   1967 C  CA  . LEU   A 1 253 ? -18.32446 -23.56833 20.30127  1.000 25.70435 ? 253 LEU   A CA  1 
ATOM   1968 C  C   . LEU   A 1 253 ? -18.45730 -24.81620 21.15985  1.000 26.54784 ? 253 LEU   A C   1 
ATOM   1969 O  O   . LEU   A 1 253 ? -19.56702 -25.22484 21.51660  1.000 26.78720 ? 253 LEU   A O   1 
ATOM   1970 C  CB  . LEU   A 1 253 ? -18.03654 -23.94135 18.84759  1.000 22.95867 ? 253 LEU   A CB  1 
ATOM   1971 C  CG  . LEU   A 1 253 ? -18.32700 -22.85242 17.81398  1.000 19.93765 ? 253 LEU   A CG  1 
ATOM   1972 C  CD1 . LEU   A 1 253 ? -18.02408 -23.32970 16.39596  1.000 19.75926 ? 253 LEU   A CD1 1 
ATOM   1973 C  CD2 . LEU   A 1 253 ? -19.77408 -22.42631 17.95071  1.000 24.18766 ? 253 LEU   A CD2 1 
ATOM   1974 N  N   . SER   A 1 254 ? -17.32743 -25.42199 21.51594  1.000 25.70354 ? 254 SER   A N   1 
ATOM   1975 C  CA  . SER   A 1 254 ? -17.33735 -26.54228 22.44460  1.000 26.81553 ? 254 SER   A CA  1 
ATOM   1976 C  C   . SER   A 1 254 ? -18.04687 -26.17975 23.74435  1.000 28.66365 ? 254 SER   A C   1 
ATOM   1977 O  O   . SER   A 1 254 ? -18.87051 -26.94680 24.25220  1.000 31.63624 ? 254 SER   A O   1 
ATOM   1978 C  CB  . SER   A 1 254 ? -15.90349 -26.98690 22.72445  1.000 26.10688 ? 254 SER   A CB  1 
ATOM   1979 O  OG  . SER   A 1 254 ? -15.90980 -28.22982 23.37470  1.000 30.31855 ? 254 SER   A OG  1 
ATOM   1980 N  N   . ALA   A 1 255 ? -17.73802 -25.00738 24.29991  1.000 28.37068 ? 255 ALA   A N   1 
ATOM   1981 C  CA  . ALA   A 1 255 ? -18.27998 -24.64902 25.60643  1.000 32.28006 ? 255 ALA   A CA  1 
ATOM   1982 C  C   . ALA   A 1 255 ? -19.77033 -24.35842 25.52072  1.000 31.33576 ? 255 ALA   A C   1 
ATOM   1983 O  O   . ALA   A 1 255 ? -20.53235 -24.67652 26.44254  1.000 34.77115 ? 255 ALA   A O   1 
ATOM   1984 C  CB  . ALA   A 1 255 ? -17.52249 -23.44533 26.16928  1.000 36.60103 ? 255 ALA   A CB  1 
ATOM   1985 N  N   . GLN   A 1 256 ? -20.19715 -23.75081 24.42190  1.000 30.45389 ? 256 GLN   A N   1 
ATOM   1986 C  CA  . GLN   A 1 256 ? -21.60542 -23.44653 24.23152  1.000 30.86775 ? 256 GLN   A CA  1 
ATOM   1987 C  C   . GLN   A 1 256 ? -22.42804 -24.71127 24.05220  1.000 31.81370 ? 256 GLN   A C   1 
ATOM   1988 O  O   . GLN   A 1 256 ? -23.55518 -24.80019 24.55234  1.000 34.79551 ? 256 GLN   A O   1 
ATOM   1989 C  CB  . GLN   A 1 256 ? -21.76085 -22.52431 23.03364  1.000 31.77405 ? 256 GLN   A CB  1 
ATOM   1990 C  CG  . GLN   A 1 256 ? -23.14940 -22.00953 22.84218  1.000 34.61781 ? 256 GLN   A CG  1 
ATOM   1991 C  CD  . GLN   A 1 256 ? -23.31277 -21.41917 21.48031  1.000 35.30841 ? 256 GLN   A CD  1 
ATOM   1992 O  OE1 . GLN   A 1 256 ? -22.32061 -21.08169 20.82120  1.000 39.11587 ? 256 GLN   A OE1 1 
ATOM   1993 N  NE2 . GLN   A 1 256 ? -24.55875 -21.31339 21.02077  1.000 38.15295 ? 256 GLN   A NE2 1 
ATOM   1994 N  N   . THR   A 1 257 ? -21.87856 -25.71001 23.36358  1.000 30.71519 ? 257 THR   A N   1 
ATOM   1995 C  CA  . THR   A 1 257 ? -22.61908 -26.93924 23.12109  1.000 28.67390 ? 257 THR   A CA  1 
ATOM   1996 C  C   . THR   A 1 257 ? -22.37645 -27.99743 24.18137  1.000 30.23375 ? 257 THR   A C   1 
ATOM   1997 O  O   . THR   A 1 257 ? -23.16662 -28.93844 24.28933  1.000 32.39953 ? 257 THR   A O   1 
ATOM   1998 C  CB  . THR   A 1 257 ? -22.25470 -27.50445 21.74750  1.000 29.31847 ? 257 THR   A CB  1 
ATOM   1999 O  OG1 . THR   A 1 257 ? -20.83303 -27.64814 21.65072  1.000 28.19128 ? 257 THR   A OG1 1 
ATOM   2000 C  CG2 . THR   A 1 257 ? -22.70573 -26.54499 20.67077  1.000 23.52502 ? 257 THR   A CG2 1 
ATOM   2001 N  N   . GLY   A 1 258 ? -21.31310 -27.86687 24.96559  1.000 31.31403 ? 258 GLY   A N   1 
ATOM   2002 C  CA  . GLY   A 1 258 ? -20.96794 -28.91614 25.89460  1.000 30.69549 ? 258 GLY   A CA  1 
ATOM   2003 C  C   . GLY   A 1 258 ? -20.35851 -30.13760 25.25875  1.000 29.10042 ? 258 GLY   A C   1 
ATOM   2004 O  O   . GLY   A 1 258 ? -20.24330 -31.17288 25.91548  1.000 32.93697 ? 258 GLY   A O   1 
ATOM   2005 N  N   . ILE   A 1 259 ? -19.97239 -30.05932 23.99752  1.000 26.63098 ? 259 ILE   A N   1 
ATOM   2006 C  CA  . ILE   A 1 259 ? -19.36732 -31.17900 23.29800  1.000 29.36764 ? 259 ILE   A CA  1 
ATOM   2007 C  C   . ILE   A 1 259 ? -17.88797 -30.87717 23.14096  1.000 28.69484 ? 259 ILE   A C   1 
ATOM   2008 O  O   . ILE   A 1 259 ? -17.50734 -29.89328 22.49373  1.000 25.31215 ? 259 ILE   A O   1 
ATOM   2009 C  CB  . ILE   A 1 259 ? -20.03127 -31.42629 21.94108  1.000 28.62938 ? 259 ILE   A CB  1 
ATOM   2010 C  CG1 . ILE   A 1 259 ? -21.46527 -31.88996 22.14876  1.000 30.05597 ? 259 ILE   A CG1 1 
ATOM   2011 C  CG2 . ILE   A 1 259 ? -19.24543 -32.45232 21.14195  1.000 28.10875 ? 259 ILE   A CG2 1 
ATOM   2012 C  CD1 . ILE   A 1 259 ? -22.26316 -31.65869 20.93995  1.000 30.69147 ? 259 ILE   A CD1 1 
ATOM   2013 N  N   . ALA   A 1 260 ? -17.05665 -31.70460 23.76201  1.000 29.07986 ? 260 ALA   A N   1 
ATOM   2014 C  CA  . ALA   A 1 260 ? -15.62152 -31.49773 23.68395  1.000 29.02428 ? 260 ALA   A CA  1 
ATOM   2015 C  C   . ALA   A 1 260 ? -15.18732 -31.55698 22.22934  1.000 26.09528 ? 260 ALA   A C   1 
ATOM   2016 O  O   . ALA   A 1 260 ? -15.75401 -32.30820 21.43303  1.000 27.86104 ? 260 ALA   A O   1 
ATOM   2017 C  CB  . ALA   A 1 260 ? -14.89404 -32.55630 24.51730  1.000 28.15373 ? 260 ALA   A CB  1 
ATOM   2018 N  N   . VAL   A 1 261 ? -14.19474 -30.73934 21.87400  1.000 25.88611 ? 261 VAL   A N   1 
ATOM   2019 C  CA  . VAL   A 1 261 ? -13.74707 -30.68890 20.48300  1.000 25.38354 ? 261 VAL   A CA  1 
ATOM   2020 C  C   . VAL   A 1 261 ? -13.37713 -32.08603 20.00802  1.000 25.28743 ? 261 VAL   A C   1 
ATOM   2021 O  O   . VAL   A 1 261 ? -13.81434 -32.53808 18.94576  1.000 24.81877 ? 261 VAL   A O   1 
ATOM   2022 C  CB  . VAL   A 1 261 ? -12.57328 -29.70458 20.32940  1.000 27.46217 ? 261 VAL   A CB  1 
ATOM   2023 C  CG1 . VAL   A 1 261 ? -11.95865 -29.79401 18.91826  1.000 22.30311 ? 261 VAL   A CG1 1 
ATOM   2024 C  CG2 . VAL   A 1 261 ? -13.02682 -28.29394 20.65544  1.000 24.71559 ? 261 VAL   A CG2 1 
ATOM   2025 N  N   . LEU   A 1 262 ? -12.59329 -32.80272 20.81460  1.000 26.72746 ? 262 LEU   A N   1 
ATOM   2026 C  CA  . LEU   A 1 262 ? -12.15680 -34.14591 20.43930  1.000 30.10031 ? 262 LEU   A CA  1 
ATOM   2027 C  C   . LEU   A 1 262 ? -13.33041 -35.10713 20.31198  1.000 28.31617 ? 262 LEU   A C   1 
ATOM   2028 O  O   . LEU   A 1 262 ? -13.25317 -36.07949 19.55285  1.000 27.77837 ? 262 LEU   A O   1 
ATOM   2029 C  CB  . LEU   A 1 262 ? -11.16199 -34.68261 21.46790  1.000 29.64582 ? 262 LEU   A CB  1 
ATOM   2030 C  CG  . LEU   A 1 262 ? -9.72692  -34.15233 21.40068  1.000 31.23872 ? 262 LEU   A CG  1 
ATOM   2031 C  CD1 . LEU   A 1 262 ? -9.21934  -34.07231 19.97272  1.000 29.82255 ? 262 LEU   A CD1 1 
ATOM   2032 C  CD2 . LEU   A 1 262 ? -9.64859  -32.79726 22.09432  1.000 33.14569 ? 262 LEU   A CD2 1 
ATOM   2033 N  N   . ASP   A 1 263 ? -14.40703 -34.87215 21.06807  1.000 27.50974 ? 263 ASP   A N   1 
ATOM   2034 C  CA  . ASP   A 1 263 ? -15.62424 -35.65925 20.89770  1.000 29.66437 ? 263 ASP   A CA  1 
ATOM   2035 C  C   . ASP   A 1 263 ? -16.25668 -35.37272 19.54823  1.000 26.07472 ? 263 ASP   A C   1 
ATOM   2036 O  O   . ASP   A 1 263 ? -16.74871 -36.28342 18.86828  1.000 24.72494 ? 263 ASP   A O   1 
ATOM   2037 C  CB  . ASP   A 1 263 ? -16.62804 -35.33657 22.00723  1.000 28.92230 ? 263 ASP   A CB  1 
ATOM   2038 C  CG  . ASP   A 1 263 ? -16.23462 -35.92330 23.34837  1.000 34.33016 ? 263 ASP   A CG  1 
ATOM   2039 O  OD1 . ASP   A 1 263 ? -15.13993 -36.51243 23.45611  1.000 34.39087 ? 263 ASP   A OD1 1 
ATOM   2040 O  OD2 . ASP   A 1 263 ? -17.03182 -35.78918 24.29853  1.000 31.39843 ? 263 ASP   A OD2 1 
ATOM   2041 N  N   . MET   A 1 264 ? -16.27212 -34.10471 19.15153  1.000 26.34735 ? 264 MET   A N   1 
ATOM   2042 C  CA  . MET   A 1 264 ? -16.81300 -33.79062 17.84537  1.000 23.43259 ? 264 MET   A CA  1 
ATOM   2043 C  C   . MET   A 1 264 ? -15.93234 -34.38342 16.76030  1.000 26.04482 ? 264 MET   A C   1 
ATOM   2044 O  O   . MET   A 1 264 ? -16.44002 -34.83247 15.73162  1.000 25.27240 ? 264 MET   A O   1 
ATOM   2045 C  CB  . MET   A 1 264 ? -16.94118 -32.28161 17.68936  1.000 20.42206 ? 264 MET   A CB  1 
ATOM   2046 C  CG  . MET   A 1 264 ? -17.69265 -31.83739 16.45185  1.000 22.98868 ? 264 MET   A CG  1 
ATOM   2047 S  SD  . MET   A 1 264 ? -19.38919 -32.44459 16.59890  1.000 23.85238 ? 264 MET   A SD  1 
ATOM   2048 C  CE  . MET   A 1 264 ? -20.20922 -31.00939 17.30012  1.000 22.02101 ? 264 MET   A CE  1 
ATOM   2049 N  N   . CYS   A 1 265 ? -14.61637 -34.41465 16.98878  1.000 23.39815 ? 265 CYS   A N   1 
ATOM   2050 C  CA  . CYS   A 1 265 ? -13.72004 -35.08450 16.05606  1.000 25.38305 ? 265 CYS   A CA  1 
ATOM   2051 C  C   . CYS   A 1 265 ? -14.07704 -36.55318 15.91058  1.000 24.63806 ? 265 CYS   A C   1 
ATOM   2052 O  O   . CYS   A 1 265 ? -14.08709 -37.08315 14.79716  1.000 23.67651 ? 265 CYS   A O   1 
ATOM   2053 C  CB  . CYS   A 1 265 ? -12.26525 -34.94361 16.50910  1.000 25.83771 ? 265 CYS   A CB  1 
ATOM   2054 S  SG  . CYS   A 1 265 ? -11.59793 -33.29116 16.39603  1.000 25.25682 ? 265 CYS   A SG  1 
ATOM   2055 N  N   . ALA   A 1 266 ? -14.36019 -37.23686 17.02629  1.000 26.19950 ? 266 ALA   A N   1 
ATOM   2056 C  CA  . ALA   A 1 266 ? -14.79382 -38.62432 16.93103  1.000 28.35739 ? 266 ALA   A CA  1 
ATOM   2057 C  C   . ALA   A 1 266 ? -16.05259 -38.74653 16.08253  1.000 29.45914 ? 266 ALA   A C   1 
ATOM   2058 O  O   . ALA   A 1 266 ? -16.19896 -39.70714 15.31802  1.000 30.47952 ? 266 ALA   A O   1 
ATOM   2059 C  CB  . ALA   A 1 266 ? -15.02084 -39.20746 18.32632  1.000 30.97910 ? 266 ALA   A CB  1 
ATOM   2060 N  N   . SER   A 1 267 ? -16.96458 -37.76995 16.18724  1.000 26.10201 ? 267 SER   A N   1 
ATOM   2061 C  CA  . SER   A 1 267 ? -18.16144 -37.77696 15.35413  1.000 27.55539 ? 267 SER   A CA  1 
ATOM   2062 C  C   . SER   A 1 267 ? -17.80365 -37.59223 13.88904  1.000 26.13846 ? 267 SER   A C   1 
ATOM   2063 O  O   . SER   A 1 267 ? -18.31983 -38.30317 13.01920  1.000 27.60191 ? 267 SER   A O   1 
ATOM   2064 C  CB  . SER   A 1 267 ? -19.13074 -36.68061 15.80138  1.000 26.15280 ? 267 SER   A CB  1 
ATOM   2065 O  OG  . SER   A 1 267 ? -19.53303 -36.86999 17.13877  1.000 30.11451 ? 267 SER   A OG  1 
ATOM   2066 N  N   . LEU   A 1 268 ? -16.93171 -36.62731 13.59583  1.000 26.86300 ? 268 LEU   A N   1 
ATOM   2067 C  CA  . LEU   A 1 268 ? -16.45825 -36.45007 12.22987  1.000 24.23238 ? 268 LEU   A CA  1 
ATOM   2068 C  C   . LEU   A 1 268 ? -15.78171 -37.71659 11.71221  1.000 26.30765 ? 268 LEU   A C   1 
ATOM   2069 O  O   . LEU   A 1 268 ? -16.00267 -38.11951 10.56544  1.000 27.40160 ? 268 LEU   A O   1 
ATOM   2070 C  CB  . LEU   A 1 268 ? -15.50523 -35.25194 12.15918  1.000 24.14062 ? 268 LEU   A CB  1 
ATOM   2071 C  CG  . LEU   A 1 268 ? -14.95166 -34.85116 10.79026  1.000 21.11289 ? 268 LEU   A CG  1 
ATOM   2072 C  CD1 . LEU   A 1 268 ? -16.05604 -34.79207 9.74273   1.000 21.30887 ? 268 LEU   A CD1 1 
ATOM   2073 C  CD2 . LEU   A 1 268 ? -14.24136 -33.49875 10.86500  1.000 23.18267 ? 268 LEU   A CD2 1 
ATOM   2074 N  N   . LYS   A 1 269 ? -14.95454 -38.35455 12.54294  1.000 28.37494 ? 269 LYS   A N   1 
ATOM   2075 C  CA  . LYS   A 1 269 ? -14.33763 -39.62447 12.16920  1.000 28.26663 ? 269 LYS   A CA  1 
ATOM   2076 C  C   . LYS   A 1 269 ? -15.38568 -40.62730 11.69596  1.000 28.54855 ? 269 LYS   A C   1 
ATOM   2077 O  O   . LYS   A 1 269 ? -15.25818 -41.21134 10.61372  1.000 28.71139 ? 269 LYS   A O   1 
ATOM   2078 C  CB  . LYS   A 1 269 ? -13.54359 -40.17906 13.35823  1.000 30.62045 ? 269 LYS   A CB  1 
ATOM   2079 C  CG  . LYS   A 1 269 ? -13.05521 -41.60730 13.19921  1.000 35.87283 ? 269 LYS   A CG  1 
ATOM   2080 C  CD  . LYS   A 1 269 ? -11.90564 -41.91580 14.16336  1.000 34.75921 ? 269 LYS   A CD  1 
ATOM   2081 C  CE  . LYS   A 1 269 ? -11.60807 -43.42485 14.20348  1.000 45.02101 ? 269 LYS   A CE  1 
ATOM   2082 N  NZ  . LYS   A 1 269 ? -10.23836 -43.76181 14.70553  1.000 42.83395 ? 269 LYS   A NZ  1 
ATOM   2083 N  N   . GLU   A 1 270 ? -16.44666 -40.82243 12.48953  1.000 28.76435 ? 270 GLU   A N   1 
ATOM   2084 C  CA  . GLU   A 1 270 ? -17.50429 -41.75048 12.09124  1.000 31.91045 ? 270 GLU   A CA  1 
ATOM   2085 C  C   . GLU   A 1 270 ? -18.21139 -41.29732 10.82813  1.000 29.87556 ? 270 GLU   A C   1 
ATOM   2086 O  O   . GLU   A 1 270 ? -18.54747 -42.12642 9.97543   1.000 31.35783 ? 270 GLU   A O   1 
ATOM   2087 C  CB  . GLU   A 1 270 ? -18.50373 -41.94881 13.22655  1.000 31.45737 ? 270 GLU   A CB  1 
ATOM   2088 C  CG  . GLU   A 1 270 ? -17.81004 -42.36485 14.49066  1.000 34.43466 ? 270 GLU   A CG  1 
ATOM   2089 C  CD  . GLU   A 1 270 ? -17.15495 -43.72475 14.31687  1.000 41.39743 ? 270 GLU   A CD  1 
ATOM   2090 O  OE1 . GLU   A 1 270 ? -16.09988 -43.98536 14.93630  1.000 42.45763 ? 270 GLU   A OE1 1 
ATOM   2091 O  OE2 . GLU   A 1 270 ? -17.71644 -44.54819 13.55837  1.000 43.43291 ? 270 GLU   A OE2 1 
ATOM   2092 N  N   . LEU   A 1 271 ? -18.44218 -39.99212 10.68143  1.000 27.60310 ? 271 LEU   A N   1 
ATOM   2093 C  CA  . LEU   A 1 271 ? -19.08655 -39.50871 9.46855   1.000 26.26736 ? 271 LEU   A CA  1 
ATOM   2094 C  C   . LEU   A 1 271 ? -18.22890 -39.80104 8.25281   1.000 27.77850 ? 271 LEU   A C   1 
ATOM   2095 O  O   . LEU   A 1 271 ? -18.74488 -40.13418 7.18169   1.000 29.11107 ? 271 LEU   A O   1 
ATOM   2096 C  CB  . LEU   A 1 271 ? -19.36227 -38.01726 9.58946   1.000 26.81333 ? 271 LEU   A CB  1 
ATOM   2097 C  CG  . LEU   A 1 271 ? -20.54136 -37.71821 10.50358  1.000 23.64390 ? 271 LEU   A CG  1 
ATOM   2098 C  CD1 . LEU   A 1 271 ? -20.62428 -36.23561 10.78557  1.000 24.29724 ? 271 LEU   A CD1 1 
ATOM   2099 C  CD2 . LEU   A 1 271 ? -21.81308 -38.21449 9.85605   1.000 28.56756 ? 271 LEU   A CD2 1 
ATOM   2100 N  N   . LEU   A 1 272 ? -16.90957 -39.69804 8.40930   1.000 27.90190 ? 272 LEU   A N   1 
ATOM   2101 C  CA  . LEU   A 1 272 ? -16.00470 -39.95306 7.29766   1.000 28.51834 ? 272 LEU   A CA  1 
ATOM   2102 C  C   . LEU   A 1 272 ? -15.96726 -41.43290 6.94992   1.000 31.89742 ? 272 LEU   A C   1 
ATOM   2103 O  O   . LEU   A 1 272 ? -15.98175 -41.79803 5.76888   1.000 33.86622 ? 272 LEU   A O   1 
ATOM   2104 C  CB  . LEU   A 1 272 ? -14.61170 -39.44429 7.64604   1.000 26.25376 ? 272 LEU   A CB  1 
ATOM   2105 C  CG  . LEU   A 1 272 ? -14.53834 -37.92741 7.69615   1.000 25.07558 ? 272 LEU   A CG  1 
ATOM   2106 C  CD1 . LEU   A 1 272 ? -13.20536 -37.49290 8.26564   1.000 28.26173 ? 272 LEU   A CD1 1 
ATOM   2107 C  CD2 . LEU   A 1 272 ? -14.76516 -37.35401 6.31196   1.000 26.63088 ? 272 LEU   A CD2 1 
ATOM   2108 N  N   . GLN   A 1 273 ? -15.94236 -42.29815 7.96513   1.000 32.06876 ? 273 GLN   A N   1 
ATOM   2109 C  CA  . GLN   A 1 273 ? -15.84204 -43.73205 7.71976   1.000 33.99791 ? 273 GLN   A CA  1 
ATOM   2110 C  C   . GLN   A 1 273 ? -17.16808 -44.33837 7.28355   1.000 35.60905 ? 273 GLN   A C   1 
ATOM   2111 O  O   . GLN   A 1 273 ? -17.18110 -45.30798 6.51515   1.000 37.67274 ? 273 GLN   A O   1 
ATOM   2112 C  CB  . GLN   A 1 273 ? -15.33209 -44.44573 8.96748   1.000 35.02403 ? 273 GLN   A CB  1 
ATOM   2113 C  CG  . GLN   A 1 273 ? -13.84349 -44.26975 9.23283   1.000 35.22263 ? 273 GLN   A CG  1 
ATOM   2114 C  CD  . GLN   A 1 273 ? -13.47554 -44.53711 10.68101  1.000 39.17537 ? 273 GLN   A CD  1 
ATOM   2115 O  OE1 . GLN   A 1 273 ? -12.36264 -44.23956 11.11655  1.000 41.74164 ? 273 GLN   A OE1 1 
ATOM   2116 N  NE2 . GLN   A 1 273 ? -14.41875 -45.08967 11.44083  1.000 42.33416 ? 273 GLN   A NE2 1 
ATOM   2117 N  N   . ASN   A 1 274 ? -18.28376 -43.78740 7.74478   1.000 33.50133 ? 274 ASN   A N   1 
ATOM   2118 C  CA  . ASN   A 1 274 ? -19.58101 -44.39740 7.51503   1.000 34.08344 ? 274 ASN   A CA  1 
ATOM   2119 C  C   . ASN   A 1 274 ? -20.44121 -43.62778 6.53703   1.000 34.99226 ? 274 ASN   A C   1 
ATOM   2120 O  O   . ASN   A 1 274 ? -21.48398 -44.13996 6.11582   1.000 35.58698 ? 274 ASN   A O   1 
ATOM   2121 C  CB  . ASN   A 1 274 ? -20.33596 -44.52651 8.83956   1.000 37.77474 ? 274 ASN   A CB  1 
ATOM   2122 C  CG  . ASN   A 1 274 ? -19.65383 -45.46854 9.78766   1.000 40.61524 ? 274 ASN   A CG  1 
ATOM   2123 O  OD1 . ASN   A 1 274 ? -18.88758 -46.34349 9.37075   1.000 42.21720 ? 274 ASN   A OD1 1 
ATOM   2124 N  ND2 . ASN   A 1 274 ? -19.92566 -45.30502 11.07724  1.000 42.58036 ? 274 ASN   A ND2 1 
ATOM   2125 N  N   . GLY   A 1 275 ? -20.03626 -42.42547 6.16301   1.000 37.00280 ? 275 GLY   A N   1 
ATOM   2126 C  CA  . GLY   A 1 275 ? -20.94127 -41.58370 5.44116   1.000 36.40381 ? 275 GLY   A CA  1 
ATOM   2127 C  C   . GLY   A 1 275 ? -22.08349 -41.17953 6.35642   1.000 37.84634 ? 275 GLY   A C   1 
ATOM   2128 O  O   . GLY   A 1 275 ? -22.05610 -41.34616 7.57749   1.000 35.85613 ? 275 GLY   A O   1 
ATOM   2129 N  N   . MET   A 1 276 ? -23.12022 -40.65822 5.72264   1.000 40.10696 ? 276 MET   A N   1 
ATOM   2130 C  CA  . MET   A 1 276 ? -24.22771 -40.05555 6.43672   1.000 38.18882 ? 276 MET   A CA  1 
ATOM   2131 C  C   . MET   A 1 276 ? -25.46056 -40.94726 6.46694   1.000 41.49818 ? 276 MET   A C   1 
ATOM   2132 O  O   . MET   A 1 276 ? -26.40285 -40.65752 7.21298   1.000 40.88646 ? 276 MET   A O   1 
ATOM   2133 C  CB  . MET   A 1 276 ? -24.52975 -38.71550 5.78720   1.000 39.47310 ? 276 MET   A CB  1 
ATOM   2134 C  CG  . MET   A 1 276 ? -23.84891 -37.59792 6.51962   1.000 36.15024 ? 276 MET   A CG  1 
ATOM   2135 S  SD  . MET   A 1 276 ? -24.50296 -36.02390 6.05706   1.000 39.42454 ? 276 MET   A SD  1 
ATOM   2136 C  CE  . MET   A 1 276 ? -22.97223 -35.22462 5.60650   1.000 25.99457 ? 276 MET   A CE  1 
ATOM   2137 N  N   . ASN   A 1 277 ? -25.45646 -42.03148 5.69021   1.000 44.47552 ? 277 ASN   A N   1 
ATOM   2138 C  CA  . ASN   A 1 277 ? -26.48444 -43.06420 5.75059   1.000 45.04455 ? 277 ASN   A CA  1 
ATOM   2139 C  C   . ASN   A 1 277 ? -27.87300 -42.48912 5.48620   1.000 43.63940 ? 277 ASN   A C   1 
ATOM   2140 O  O   . ASN   A 1 277 ? -28.84358 -42.81351 6.17861   1.000 43.38905 ? 277 ASN   A O   1 
ATOM   2141 C  CB  . ASN   A 1 277 ? -26.44625 -43.80568 7.08769   1.000 45.84041 ? 277 ASN   A CB  1 
ATOM   2142 C  CG  . ASN   A 1 277 ? -27.13529 -45.14396 7.01949   1.000 52.01685 ? 277 ASN   A CG  1 
ATOM   2143 O  OD1 . ASN   A 1 277 ? -27.69493 -45.51267 5.98345   1.000 54.35208 ? 277 ASN   A OD1 1 
ATOM   2144 N  ND2 . ASN   A 1 277 ? -27.12026 -45.87751 8.12876   1.000 56.40745 ? 277 ASN   A ND2 1 
ATOM   2145 N  N   . GLY   A 1 278 ? -27.96913 -41.63455 4.46873   1.000 41.28446 ? 278 GLY   A N   1 
ATOM   2146 C  CA  . GLY   A 1 278 ? -29.24179 -41.08358 4.06470   1.000 38.98920 ? 278 GLY   A CA  1 
ATOM   2147 C  C   . GLY   A 1 278 ? -29.71720 -39.90721 4.88172   1.000 39.58484 ? 278 GLY   A C   1 
ATOM   2148 O  O   . GLY   A 1 278 ? -30.82196 -39.40911 4.63455   1.000 42.91048 ? 278 GLY   A O   1 
ATOM   2149 N  N   . ARG   A 1 279 ? -28.93113 -39.44692 5.84388   1.000 37.55226 ? 279 ARG   A N   1 
ATOM   2150 C  CA  . ARG   A 1 279 ? -29.32003 -38.32019 6.67136   1.000 32.96362 ? 279 ARG   A CA  1 
ATOM   2151 C  C   . ARG   A 1 279 ? -28.59505 -37.06750 6.21517   1.000 31.21278 ? 279 ARG   A C   1 
ATOM   2152 O  O   . ARG   A 1 279 ? -27.64409 -37.10867 5.42880   1.000 32.95334 ? 279 ARG   A O   1 
ATOM   2153 C  CB  . ARG   A 1 279 ? -29.04131 -38.60657 8.15194   1.000 33.66702 ? 279 ARG   A CB  1 
ATOM   2154 C  CG  . ARG   A 1 279 ? -29.97338 -39.67324 8.71591   1.000 35.38936 ? 279 ARG   A CG  1 
ATOM   2155 C  CD  . ARG   A 1 279 ? -29.46278 -40.30391 9.99941   1.000 36.33880 ? 279 ARG   A CD  1 
ATOM   2156 N  NE  . ARG   A 1 279 ? -28.18384 -40.98671 9.83122   1.000 41.10290 ? 279 ARG   A NE  1 
ATOM   2157 C  CZ  . ARG   A 1 279 ? -27.56588 -41.65564 10.79688  1.000 36.84589 ? 279 ARG   A CZ  1 
ATOM   2158 N  NH1 . ARG   A 1 279 ? -28.12052 -41.81660 11.98976  1.000 38.90762 ? 279 ARG   A NH1 1 
ATOM   2159 N  NH2 . ARG   A 1 279 ? -26.36287 -42.17438 10.56129  1.000 34.56501 ? 279 ARG   A NH2 1 
ATOM   2160 N  N   . THR   A 1 280 ? -29.06954 -35.93699 6.71473   1.000 29.26118 ? 280 THR   A N   1 
ATOM   2161 C  CA  . THR   A 1 280 ? -28.49540 -34.65439 6.36773   1.000 26.58882 ? 280 THR   A CA  1 
ATOM   2162 C  C   . THR   A 1 280 ? -28.12586 -33.90078 7.63358   1.000 23.56024 ? 280 THR   A C   1 
ATOM   2163 O  O   . THR   A 1 280 ? -28.57700 -34.20757 8.73971   1.000 23.06557 ? 280 THR   A O   1 
ATOM   2164 C  CB  . THR   A 1 280 ? -29.45111 -33.81700 5.50554   1.000 27.61046 ? 280 THR   A CB  1 
ATOM   2165 O  OG1 . THR   A 1 280 ? -30.65205 -33.54848 6.23363   1.000 26.17851 ? 280 THR   A OG1 1 
ATOM   2166 C  CG2 . THR   A 1 280 ? -29.79615 -34.57021 4.22215   1.000 28.74485 ? 280 THR   A CG2 1 
ATOM   2167 N  N   . ILE   A 1 281 ? -27.26768 -32.91888 7.45206   1.000 22.99111 ? 281 ILE   A N   1 
ATOM   2168 C  CA  . ILE   A 1 281 ? -26.83592 -32.04113 8.52267   1.000 22.60776 ? 281 ILE   A CA  1 
ATOM   2169 C  C   . ILE   A 1 281 ? -26.99226 -30.62490 8.00989   1.000 23.51374 ? 281 ILE   A C   1 
ATOM   2170 O  O   . ILE   A 1 281 ? -26.36377 -30.25500 7.01075   1.000 21.26989 ? 281 ILE   A O   1 
ATOM   2171 C  CB  . ILE   A 1 281 ? -25.38418 -32.30488 8.93582   1.000 21.07507 ? 281 ILE   A CB  1 
ATOM   2172 C  CG1 . ILE   A 1 281 ? -25.18621 -33.76535 9.34734   1.000 21.51225 ? 281 ILE   A CG1 1 
ATOM   2173 C  CG2 . ILE   A 1 281 ? -24.99175 -31.35172 10.02518  1.000 19.04206 ? 281 ILE   A CG2 1 
ATOM   2174 C  CD1 . ILE   A 1 281 ? -23.75792 -34.08085 9.82919   1.000 21.31252 ? 281 ILE   A CD1 1 
ATOM   2175 N  N   . LEU   A 1 282 ? -27.82713 -29.83943 8.68691   1.000 23.83955 ? 282 LEU   A N   1 
ATOM   2176 C  CA  . LEU   A 1 282 ? -28.10252 -28.46004 8.29351   1.000 24.86958 ? 282 LEU   A CA  1 
ATOM   2177 C  C   . LEU   A 1 282 ? -28.46539 -28.38955 6.81338   1.000 24.46834 ? 282 LEU   A C   1 
ATOM   2178 O  O   . LEU   A 1 282 ? -27.97565 -27.53923 6.06340   1.000 21.75067 ? 282 LEU   A O   1 
ATOM   2179 C  CB  . LEU   A 1 282 ? -26.91834 -27.54655 8.62226   1.000 19.66213 ? 282 LEU   A CB  1 
ATOM   2180 C  CG  . LEU   A 1 282 ? -26.76768 -27.23683 10.11578  1.000 21.48758 ? 282 LEU   A CG  1 
ATOM   2181 C  CD1 . LEU   A 1 282 ? -25.48135 -26.44968 10.41643  1.000 19.83285 ? 282 LEU   A CD1 1 
ATOM   2182 C  CD2 . LEU   A 1 282 ? -28.00175 -26.52655 10.68618  1.000 22.29060 ? 282 LEU   A CD2 1 
ATOM   2183 N  N   . GLY   A 1 283 ? -29.33560 -29.31573 6.39870   1.000 24.46779 ? 283 GLY   A N   1 
ATOM   2184 C  CA  . GLY   A 1 283 ? -29.80577 -29.36187 5.02629   1.000 25.74939 ? 283 GLY   A CA  1 
ATOM   2185 C  C   . GLY   A 1 283 ? -28.76268 -29.76181 4.00514   1.000 27.94791 ? 283 GLY   A C   1 
ATOM   2186 O  O   . GLY   A 1 283 ? -28.95787 -29.52710 2.81012   1.000 26.51641 ? 283 GLY   A O   1 
ATOM   2187 N  N   . SER   A 1 284 ? -27.64943 -30.34602 4.43766   1.000 23.18424 ? 284 SER   A N   1 
ATOM   2188 C  CA  . SER   A 1 284 ? -26.60466 -30.80334 3.53137   1.000 23.95035 ? 284 SER   A CA  1 
ATOM   2189 C  C   . SER   A 1 284 ? -26.38638 -32.30210 3.70102   1.000 24.40920 ? 284 SER   A C   1 
ATOM   2190 O  O   . SER   A 1 284 ? -26.42654 -32.82247 4.81793   1.000 21.99990 ? 284 SER   A O   1 
ATOM   2191 C  CB  . SER   A 1 284 ? -25.29401 -30.04953 3.77344   1.000 23.72783 ? 284 SER   A CB  1 
ATOM   2192 O  OG  . SER   A 1 284 ? -24.29127 -30.50157 2.88260   1.000 24.71011 ? 284 SER   A OG  1 
ATOM   2193 N  N   . ALA   A 1 285 ? -26.18364 -33.00133 2.58671   1.000 23.58061 ? 285 ALA   A N   1 
ATOM   2194 C  CA  . ALA   A 1 285 ? -25.81065 -34.40492 2.61054   1.000 23.88800 ? 285 ALA   A CA  1 
ATOM   2195 C  C   . ALA   A 1 285 ? -24.30241 -34.59193 2.49562   1.000 24.32198 ? 285 ALA   A C   1 
ATOM   2196 O  O   . ALA   A 1 285 ? -23.83167 -35.72780 2.36414   1.000 25.96010 ? 285 ALA   A O   1 
ATOM   2197 C  CB  . ALA   A 1 285 ? -26.52318 -35.16418 1.49419   1.000 26.45527 ? 285 ALA   A CB  1 
ATOM   2198 N  N   . LEU   A 1 286 ? -23.55187 -33.49956 2.56993   1.000 22.98788 ? 286 LEU   A N   1 
ATOM   2199 C  CA  . LEU   A 1 286 ? -22.10097 -33.46479 2.47568   1.000 25.79782 ? 286 LEU   A CA  1 
ATOM   2200 C  C   . LEU   A 1 286 ? -21.55729 -32.75441 3.70721   1.000 24.68364 ? 286 LEU   A C   1 
ATOM   2201 O  O   . LEU   A 1 286 ? -22.22671 -31.89512 4.28228   1.000 22.28726 ? 286 LEU   A O   1 
ATOM   2202 C  CB  . LEU   A 1 286 ? -21.64300 -32.68171 1.24172   1.000 25.85130 ? 286 LEU   A CB  1 
ATOM   2203 C  CG  . LEU   A 1 286 ? -21.66423 -33.37474 -0.10716  1.000 25.89119 ? 286 LEU   A CG  1 
ATOM   2204 C  CD1 . LEU   A 1 286 ? -21.11529 -32.42276 -1.15825  1.000 27.59706 ? 286 LEU   A CD1 1 
ATOM   2205 C  CD2 . LEU   A 1 286 ? -20.91537 -34.71997 -0.07936  1.000 32.39681 ? 286 LEU   A CD2 1 
ATOM   2206 N  N   . LEU   A 1 287 ? -20.33445 -33.08160 4.10465   1.000 21.60915 ? 287 LEU   A N   1 
ATOM   2207 C  CA  . LEU   A 1 287 ? -19.71359 -32.31226 5.17372   1.000 21.60400 ? 287 LEU   A CA  1 
ATOM   2208 C  C   . LEU   A 1 287 ? -19.27431 -30.95923 4.61613   1.000 19.92949 ? 287 LEU   A C   1 
ATOM   2209 O  O   . LEU   A 1 287 ? -18.41730 -30.89186 3.73744   1.000 21.48160 ? 287 LEU   A O   1 
ATOM   2210 C  CB  . LEU   A 1 287 ? -18.54368 -33.09141 5.77295   1.000 20.48184 ? 287 LEU   A CB  1 
ATOM   2211 C  CG  . LEU   A 1 287 ? -19.00293 -34.47532 6.25551   1.000 22.81932 ? 287 LEU   A CG  1 
ATOM   2212 C  CD1 . LEU   A 1 287 ? -17.85066 -35.38403 6.69677   1.000 24.67564 ? 287 LEU   A CD1 1 
ATOM   2213 C  CD2 . LEU   A 1 287 ? -20.03793 -34.33647 7.36262   1.000 23.06292 ? 287 LEU   A CD2 1 
ATOM   2214 N  N   . GLU   A 1 288 ? -19.89769 -29.89006 5.10245   1.000 18.71541 ? 288 GLU   A N   1 
ATOM   2215 C  CA  . GLU   A 1 288 ? -19.66208 -28.52133 4.65180   1.000 18.81413 ? 288 GLU   A CA  1 
ATOM   2216 C  C   . GLU   A 1 288 ? -18.39460 -27.94936 5.27628   1.000 16.30481 ? 288 GLU   A C   1 
ATOM   2217 O  O   . GLU   A 1 288 ? -18.23967 -27.97874 6.49589   1.000 16.12924 ? 288 GLU   A O   1 
ATOM   2218 C  CB  . GLU   A 1 288 ? -20.85902 -27.66394 5.06549   1.000 20.19748 ? 288 GLU   A CB  1 
ATOM   2219 C  CG  . GLU   A 1 288 ? -21.05894 -26.29729 4.41339   1.000 25.48318 ? 288 GLU   A CG  1 
ATOM   2220 C  CD  . GLU   A 1 288 ? -20.65775 -26.21956 2.95798   1.000 29.82540 ? 288 GLU   A CD  1 
ATOM   2221 O  OE1 . GLU   A 1 288 ? -21.10538 -27.09976 2.17839   1.000 25.68709 ? 288 GLU   A OE1 1 
ATOM   2222 O  OE2 . GLU   A 1 288 ? -19.85840 -25.29960 2.62163   1.000 26.76175 ? 288 GLU   A OE2 1 
ATOM   2223 N  N   . ASP   A 1 289 ? -17.50772 -27.37097 4.46504   1.000 16.99008 ? 289 ASP   A N   1 
ATOM   2224 C  CA  . ASP   A 1 289 ? -16.26813 -26.84170 5.02939   1.000 17.14064 ? 289 ASP   A CA  1 
ATOM   2225 C  C   . ASP   A 1 289 ? -16.02483 -25.36054 4.72154   1.000 16.78367 ? 289 ASP   A C   1 
ATOM   2226 O  O   . ASP   A 1 289 ? -14.90595 -24.87744 4.89172   1.000 15.65679 ? 289 ASP   A O   1 
ATOM   2227 C  CB  . ASP   A 1 289 ? -15.09882 -27.72524 4.59138   1.000 16.37297 ? 289 ASP   A CB  1 
ATOM   2228 C  CG  . ASP   A 1 289 ? -14.56175 -27.38698 3.20962   1.000 19.16818 ? 289 ASP   A CG  1 
ATOM   2229 O  OD1 . ASP   A 1 289 ? -15.33767 -26.91702 2.34089   1.000 17.38711 ? 289 ASP   A OD1 1 
ATOM   2230 O  OD2 . ASP   A 1 289 ? -13.36660 -27.69629 2.98551   1.000 18.09687 ? 289 ASP   A OD2 1 
ATOM   2231 N  N   . GLU   A 1 290 ? -17.05102 -24.60270 4.33483   1.000 14.97628 ? 290 GLU   A N   1 
ATOM   2232 C  CA  . GLU   A 1 290 ? -16.87065 -23.18633 4.03646   1.000 17.59348 ? 290 GLU   A CA  1 
ATOM   2233 C  C   . GLU   A 1 290 ? -17.51788 -22.27882 5.07431   1.000 16.68236 ? 290 GLU   A C   1 
ATOM   2234 O  O   . GLU   A 1 290 ? -17.83308 -21.12486 4.78670   1.000 17.20299 ? 290 GLU   A O   1 
ATOM   2235 C  CB  . GLU   A 1 290 ? -17.32764 -22.88368 2.60532   1.000 19.22392 ? 290 GLU   A CB  1 
ATOM   2236 C  CG  . GLU   A 1 290 ? -16.44172 -23.65740 1.60006   1.000 18.33556 ? 290 GLU   A CG  1 
ATOM   2237 C  CD  . GLU   A 1 290 ? -16.25897 -22.96758 0.25158   1.000 24.95068 ? 290 GLU   A CD  1 
ATOM   2238 O  OE1 . GLU   A 1 290 ? -15.49397 -23.52244 -0.59056  1.000 19.72774 ? 290 GLU   A OE1 1 
ATOM   2239 O  OE2 . GLU   A 1 290 ? -16.99700 -21.97784 -0.02879  1.000 20.07221 ? 290 GLU   A OE2 1 
ATOM   2240 N  N   . PHE   A 1 291 ? -17.63342 -22.76278 6.31024   1.000 14.84779 ? 291 PHE   A N   1 
ATOM   2241 C  CA  . PHE   A 1 291 ? -18.00299 -21.93320 7.45091   1.000 14.00446 ? 291 PHE   A CA  1 
ATOM   2242 C  C   . PHE   A 1 291 ? -16.86005 -21.97205 8.45424   1.000 14.97374 ? 291 PHE   A C   1 
ATOM   2243 O  O   . PHE   A 1 291 ? -16.48795 -23.05044 8.93334   1.000 14.09604 ? 291 PHE   A O   1 
ATOM   2244 C  CB  . PHE   A 1 291 ? -19.29086 -22.43500 8.09251   1.000 15.71855 ? 291 PHE   A CB  1 
ATOM   2245 C  CG  . PHE   A 1 291 ? -20.49447 -22.25398 7.24162   1.000 18.11829 ? 291 PHE   A CG  1 
ATOM   2246 C  CD1 . PHE   A 1 291 ? -21.04686 -20.99466 7.08149   1.000 21.16486 ? 291 PHE   A CD1 1 
ATOM   2247 C  CD2 . PHE   A 1 291 ? -21.06898 -23.32708 6.58947   1.000 19.77325 ? 291 PHE   A CD2 1 
ATOM   2248 C  CE1 . PHE   A 1 291 ? -22.17749 -20.80639 6.29598   1.000 22.12558 ? 291 PHE   A CE1 1 
ATOM   2249 C  CE2 . PHE   A 1 291 ? -22.19838 -23.14505 5.79599   1.000 24.54654 ? 291 PHE   A CE2 1 
ATOM   2250 C  CZ  . PHE   A 1 291 ? -22.75111 -21.88399 5.65695   1.000 20.12267 ? 291 PHE   A CZ  1 
ATOM   2251 N  N   . THR   A 1 292 ? -16.30910 -20.80991 8.78053   1.000 14.71879 ? 292 THR   A N   1 
ATOM   2252 C  CA  . THR   A 1 292 ? -15.27117 -20.79010 9.79693   1.000 16.41797 ? 292 THR   A CA  1 
ATOM   2253 C  C   . THR   A 1 292 ? -15.90765 -20.83452 11.17811  1.000 15.14051 ? 292 THR   A C   1 
ATOM   2254 O  O   . THR   A 1 292 ? -17.10921 -20.59811 11.33096  1.000 15.21983 ? 292 THR   A O   1 
ATOM   2255 C  CB  . THR   A 1 292 ? -14.42797 -19.52968 9.68957   1.000 17.24692 ? 292 THR   A CB  1 
ATOM   2256 O  OG1 . THR   A 1 292 ? -15.24981 -18.40346 10.02162  1.000 19.16516 ? 292 THR   A OG1 1 
ATOM   2257 C  CG2 . THR   A 1 292 ? -13.86007 -19.37532 8.29383   1.000 15.12299 ? 292 THR   A CG2 1 
ATOM   2258 N  N   . PRO   A 1 293 ? -15.13427 -21.15140 12.19597  1.000 17.05808 ? 293 PRO   A N   1 
ATOM   2259 C  CA  . PRO   A 1 293 ? -15.64934 -20.99364 13.55852  1.000 16.32474 ? 293 PRO   A CA  1 
ATOM   2260 C  C   . PRO   A 1 293 ? -16.20814 -19.60094 13.81023  1.000 20.02688 ? 293 PRO   A C   1 
ATOM   2261 O  O   . PRO   A 1 293 ? -17.24614 -19.46332 14.46412  1.000 18.80606 ? 293 PRO   A O   1 
ATOM   2262 C  CB  . PRO   A 1 293 ? -14.41926 -21.31978 14.41399  1.000 17.53420 ? 293 PRO   A CB  1 
ATOM   2263 C  CG  . PRO   A 1 293 ? -13.66851 -22.30541 13.58326  1.000 15.31046 ? 293 PRO   A CG  1 
ATOM   2264 C  CD  . PRO   A 1 293 ? -13.82766 -21.83327 12.17046  1.000 17.60611 ? 293 PRO   A CD  1 
ATOM   2265 N  N   . PHE   A 1 294 ? -15.58922 -18.56763 13.23844  1.000 18.68211 ? 294 PHE   A N   1 
ATOM   2266 C  CA  . PHE   A 1 294 ? -16.10549 -17.21787 13.42387  1.000 20.66282 ? 294 PHE   A CA  1 
ATOM   2267 C  C   . PHE   A 1 294 ? -17.46777 -17.07118 12.76627  1.000 20.13176 ? 294 PHE   A C   1 
ATOM   2268 O  O   . PHE   A 1 294 ? -18.37742 -16.47875 13.35356  1.000 21.34293 ? 294 PHE   A O   1 
ATOM   2269 C  CB  . PHE   A 1 294 ? -15.12831 -16.17188 12.86382  1.000 25.68553 ? 294 PHE   A CB  1 
ATOM   2270 C  CG  . PHE   A 1 294 ? -15.78587 -14.83622 12.51738  1.000 30.40977 ? 294 PHE   A CG  1 
ATOM   2271 C  CD1 . PHE   A 1 294 ? -16.55089 -14.65417 11.35097  1.000 29.62610 ? 294 PHE   A CD1 1 
ATOM   2272 C  CD2 . PHE   A 1 294 ? -15.67538 -13.77146 13.39795  1.000 28.23551 ? 294 PHE   A CD2 1 
ATOM   2273 C  CE1 . PHE   A 1 294 ? -17.16893 -13.43073 11.08407  1.000 31.73336 ? 294 PHE   A CE1 1 
ATOM   2274 C  CE2 . PHE   A 1 294 ? -16.28161 -12.55225 13.13165  1.000 29.00313 ? 294 PHE   A CE2 1 
ATOM   2275 C  CZ  . PHE   A 1 294 ? -17.02219 -12.37941 11.97548  1.000 32.81817 ? 294 PHE   A CZ  1 
ATOM   2276 N  N   . ASP   A 1 295 ? -17.60165 -17.55259 11.51752  1.000 16.87531 ? 295 ASP   A N   1 
ATOM   2277 C  CA  . ASP   A 1 295 ? -18.88873 -17.53749 10.82063  1.000 18.09748 ? 295 ASP   A CA  1 
ATOM   2278 C  C   . ASP   A 1 295 ? -19.97667 -18.18787 11.64841  1.000 19.50266 ? 295 ASP   A C   1 
ATOM   2279 O  O   . ASP   A 1 295 ? -21.10672 -17.68942 11.70331  1.000 19.07092 ? 295 ASP   A O   1 
ATOM   2280 C  CB  . ASP   A 1 295 ? -18.79552 -18.27575 9.48997   1.000 17.50167 ? 295 ASP   A CB  1 
ATOM   2281 C  CG  . ASP   A 1 295 ? -17.84414 -17.62155 8.54146   1.000 20.12060 ? 295 ASP   A CG  1 
ATOM   2282 O  OD1 . ASP   A 1 295 ? -17.51526 -16.44039 8.76774   1.000 19.81040 ? 295 ASP   A OD1 1 
ATOM   2283 O  OD2 . ASP   A 1 295 ? -17.40457 -18.30689 7.59726   1.000 18.54013 ? 295 ASP   A OD2 1 
ATOM   2284 N  N   . VAL   A 1 296 ? -19.66931 -19.32485 12.27516  1.000 18.32564 ? 296 VAL   A N   1 
ATOM   2285 C  CA  . VAL   A 1 296 ? -20.68497 -20.01669 13.05373  1.000 18.18971 ? 296 VAL   A CA  1 
ATOM   2286 C  C   . VAL   A 1 296 ? -21.07565 -19.18026 14.26186  1.000 20.71429 ? 296 VAL   A C   1 
ATOM   2287 O  O   . VAL   A 1 296 ? -22.26016 -18.95336 14.51849  1.000 21.64655 ? 296 VAL   A O   1 
ATOM   2288 C  CB  . VAL   A 1 296 ? -20.19424 -21.41541 13.46397  1.000 15.91810 ? 296 VAL   A CB  1 
ATOM   2289 C  CG1 . VAL   A 1 296 ? -21.19729 -22.07817 14.41342  1.000 17.99139 ? 296 VAL   A CG1 1 
ATOM   2290 C  CG2 . VAL   A 1 296 ? -19.92101 -22.27040 12.24085  1.000 16.90417 ? 296 VAL   A CG2 1 
ATOM   2291 N  N   . VAL   A 1 297 ? -20.08683 -18.68254 15.00115  1.000 21.64931 ? 297 VAL   A N   1 
ATOM   2292 C  CA  . VAL   A 1 297 ? -20.37778 -17.83857 16.15572  1.000 22.39976 ? 297 VAL   A CA  1 
ATOM   2293 C  C   . VAL   A 1 297 ? -21.17678 -16.61087 15.72975  1.000 25.18759 ? 297 VAL   A C   1 
ATOM   2294 O  O   . VAL   A 1 297 ? -22.18171 -16.26492 16.35507  1.000 28.28122 ? 297 VAL   A O   1 
ATOM   2295 C  CB  . VAL   A 1 297 ? -19.07743 -17.43026 16.87008  1.000 22.56496 ? 297 VAL   A CB  1 
ATOM   2296 C  CG1 . VAL   A 1 297 ? -19.38883 -16.42945 17.95178  1.000 24.92981 ? 297 VAL   A CG1 1 
ATOM   2297 C  CG2 . VAL   A 1 297 ? -18.35755 -18.63866 17.44003  1.000 26.03120 ? 297 VAL   A CG2 1 
ATOM   2298 N  N   . ARG   A 1 298 ? -20.72563 -15.92247 14.67064  1.000 25.94189 ? 298 ARG   A N   1 
ATOM   2299 C  CA  . ARG   A 1 298 ? -21.43470 -14.73712 14.18599  1.000 29.12910 ? 298 ARG   A CA  1 
ATOM   2300 C  C   . ARG   A 1 298 ? -22.89908 -15.04850 13.92040  1.000 30.74154 ? 298 ARG   A C   1 
ATOM   2301 O  O   . ARG   A 1 298 ? -23.79270 -14.31479 14.35507  1.000 35.26141 ? 298 ARG   A O   1 
ATOM   2302 C  CB  . ARG   A 1 298 ? -20.78864 -14.18133 12.90379  1.000 28.77697 ? 298 ARG   A CB  1 
ATOM   2303 C  CG  . ARG   A 1 298 ? -21.84170 -13.47645 11.98358  1.000 33.76131 ? 298 ARG   A CG  1 
ATOM   2304 C  CD  . ARG   A 1 298 ? -21.31322 -12.63331 10.78985  1.000 35.49772 ? 298 ARG   A CD  1 
ATOM   2305 N  NE  . ARG   A 1 298 ? -20.99914 -13.40679 9.58641   1.000 34.25462 ? 298 ARG   A NE  1 
ATOM   2306 C  CZ  . ARG   A 1 298 ? -21.43220 -13.13249 8.35825   1.000 27.39057 ? 298 ARG   A CZ  1 
ATOM   2307 N  NH1 . ARG   A 1 298 ? -22.34904 -12.19313 8.12884   1.000 26.90982 ? 298 ARG   A NH1 1 
ATOM   2308 N  NH2 . ARG   A 1 298 ? -20.94952 -13.82785 7.33303   1.000 26.05739 ? 298 ARG   A NH2 1 
ATOM   2309 N  N   . GLN   A 1 299 ? -23.16244 -16.14190 13.20926  1.000 28.95121 ? 299 GLN   A N   1 
ATOM   2310 C  CA  . GLN   A 1 299 ? -24.52429 -16.45424 12.81352  1.000 27.96213 ? 299 GLN   A CA  1 
ATOM   2311 C  C   . GLN   A 1 299 ? -25.32239 -17.05699 13.95347  1.000 30.76344 ? 299 GLN   A C   1 
ATOM   2312 O  O   . GLN   A 1 299 ? -26.51507 -16.76354 14.08165  1.000 35.59301 ? 299 GLN   A O   1 
ATOM   2313 C  CB  . GLN   A 1 299 ? -24.51935 -17.39687 11.60738  1.000 26.32955 ? 299 GLN   A CB  1 
ATOM   2314 C  CG  . GLN   A 1 299 ? -25.83864 -17.44540 10.92187  1.000 24.36046 ? 299 GLN   A CG  1 
ATOM   2315 C  CD  . GLN   A 1 299 ? -25.79949 -18.15484 9.59765   1.000 21.78341 ? 299 GLN   A CD  1 
ATOM   2316 O  OE1 . GLN   A 1 299 ? -26.82201 -18.66389 9.15132   1.000 21.65772 ? 299 GLN   A OE1 1 
ATOM   2317 N  NE2 . GLN   A 1 299 ? -24.62811 -18.18756 8.94550   1.000 17.21247 ? 299 GLN   A NE2 1 
ATOM   2318 N  N   . CYS   A 1 300 ? -24.69672 -17.87255 14.80099  1.000 28.57590 ? 300 CYS   A N   1 
ATOM   2319 C  CA  . CYS   A 1 300 ? -25.37908 -18.49397 15.93036  1.000 31.76172 ? 300 CYS   A CA  1 
ATOM   2320 C  C   . CYS   A 1 300 ? -25.29871 -17.65211 17.21618  1.000 36.17790 ? 300 CYS   A C   1 
ATOM   2321 O  O   . CYS   A 1 300 ? -25.53644 -18.18413 18.30892  1.000 42.20838 ? 300 CYS   A O   1 
ATOM   2322 C  CB  . CYS   A 1 300 ? -24.82361 -19.90576 16.16790  1.000 28.37852 ? 300 CYS   A CB  1 
ATOM   2323 S  SG  . CYS   A 1 300 ? -24.90709 -21.03889 14.70495  1.000 30.83232 ? 300 CYS   A SG  1 
ATOM   2324 N  N   . SER   A 1 301 ? -24.97995 -16.35360 17.09920  1.000 38.40346 ? 301 SER   A N   1 
ATOM   2325 C  CA  . SER   A 1 301 ? -24.97113 -15.40818 18.21910  1.000 41.29797 ? 301 SER   A CA  1 
ATOM   2326 C  C   . SER   A 1 301 ? -25.53684 -14.04479 17.80054  1.000 42.33783 ? 301 SER   A C   1 
ATOM   2327 O  O   . SER   A 1 301 ? -26.26750 -13.41373 18.57407  1.000 42.72983 ? 301 SER   A O   1 
ATOM   2328 C  CB  . SER   A 1 301 ? -23.55017 -15.26408 18.79126  1.000 45.87515 ? 301 SER   A CB  1 
ATOM   2329 O  OG  . SER   A 1 301 ? -23.40154 -14.09843 19.59049  1.000 51.29723 ? 301 SER   A OG  1 
ATOM   2330 N  N   . GLY   A 1 302 ? -25.19923 -13.56824 16.59400  1.000 43.14299 ? 302 GLY   A N   1 
ATOM   2331 C  CA  . GLY   A 1 302 ? -25.95057 -12.48132 15.97498  1.000 43.32229 ? 302 GLY   A CA  1 
ATOM   2332 C  C   . GLY   A 1 302 ? -25.29424 -11.11897 15.85747  1.000 47.45823 ? 302 GLY   A C   1 
ATOM   2333 O  O   . GLY   A 1 302 ? -25.93304 -10.08899 16.11486  1.000 47.62000 ? 302 GLY   A O   1 
ATOM   2334 N  N   . VAL   A 1 303 ? -24.03044 -11.09701 15.44167  1.000 49.29196 ? 303 VAL   A N   1 
ATOM   2335 C  CA  . VAL   A 1 303 ? -23.26139 -9.85619  15.36525  1.000 51.99932 ? 303 VAL   A CA  1 
ATOM   2336 C  C   . VAL   A 1 303 ? -23.63199 -9.09523  14.09478  1.000 48.96790 ? 303 VAL   A C   1 
ATOM   2337 O  O   . VAL   A 1 303 ? -23.78183 -9.68691  13.01605  1.000 47.36545 ? 303 VAL   A O   1 
ATOM   2338 C  CB  . VAL   A 1 303 ? -21.75067 -10.16297 15.42881  1.000 48.65789 ? 303 VAL   A CB  1 
ATOM   2339 C  CG1 . VAL   A 1 303 ? -20.91856 -8.90477  15.17111  1.000 51.72433 ? 303 VAL   A CG1 1 
ATOM   2340 C  CG2 . VAL   A 1 303 ? -21.39233 -10.79454 16.78181  1.000 49.29147 ? 303 VAL   A CG2 1 
ATOM   2341 N  N   . THR   A 1 304 ? -23.78386 -7.77209  14.22300  1.000 48.33446 ? 304 THR   A N   1 
ATOM   2342 C  CA  . THR   A 1 304 ? -24.09513 -6.86643  13.12153  1.000 43.87480 ? 304 THR   A CA  1 
ATOM   2343 C  C   . THR   A 1 304 ? -22.89589 -5.97385  12.81070  1.000 49.85306 ? 304 THR   A C   1 
ATOM   2344 O  O   . THR   A 1 304 ? -21.80097 -6.13315  13.36661  1.000 50.61574 ? 304 THR   A O   1 
ATOM   2345 C  CB  . THR   A 1 304 ? -25.32007 -6.00765  13.44841  1.000 41.29355 ? 304 THR   A CB  1 
ATOM   2346 O  OG1 . THR   A 1 304 ? -25.17155 -5.43432  14.75570  1.000 48.52927 ? 304 THR   A OG1 1 
ATOM   2347 C  CG2 . THR   A 1 304 ? -26.58256 -6.84838  13.41648  1.000 34.12379 ? 304 THR   A CG2 1 
ATOM   2348 N  N   . PHE   A 1 305 ? -23.12486 -5.01379  11.91083  1.000 46.26764 ? 305 PHE   A N   1 
ATOM   2349 C  CA  . PHE   A 1 305 ? -22.07759 -4.14085  11.38786  1.000 49.49016 ? 305 PHE   A CA  1 
ATOM   2350 C  C   . PHE   A 1 305 ? -22.70999 -2.79761  11.03253  1.000 49.31378 ? 305 PHE   A C   1 
ATOM   2351 O  O   . PHE   A 1 305 ? -23.77365 -2.75845  10.40006  1.000 45.89684 ? 305 PHE   A O   1 
ATOM   2352 C  CB  . PHE   A 1 305 ? -21.40970 -4.77938  10.15339  1.000 43.83036 ? 305 PHE   A CB  1 
ATOM   2353 C  CG  . PHE   A 1 305 ? -21.10959 -6.24089  10.33087  1.000 43.13493 ? 305 PHE   A CG  1 
ATOM   2354 C  CD1 . PHE   A 1 305 ? -19.94716 -6.65782  10.97816  1.000 40.07946 ? 305 PHE   A CD1 1 
ATOM   2355 C  CD2 . PHE   A 1 305 ? -22.03629 -7.20222  9.91287   1.000 40.02650 ? 305 PHE   A CD2 1 
ATOM   2356 C  CE1 . PHE   A 1 305 ? -19.69530 -8.00973  11.18615  1.000 40.21238 ? 305 PHE   A CE1 1 
ATOM   2357 C  CE2 . PHE   A 1 305 ? -21.79849 -8.55738  10.11420  1.000 37.52096 ? 305 PHE   A CE2 1 
ATOM   2358 C  CZ  . PHE   A 1 305 ? -20.62841 -8.96229  10.75905  1.000 43.37996 ? 305 PHE   A CZ  1 
ATOM   2359 N  N   . GLN   A 1 306 ? -22.07089 -1.70407  11.44587  1.000 53.08588 ? 306 GLN   A N   1 
ATOM   2360 C  CA  . GLN   A 1 306 ? -22.58920 -0.36963  11.13744  1.000 54.39589 ? 306 GLN   A CA  1 
ATOM   2361 C  C   . GLN   A 1 306 ? -21.47450 0.61117   10.75963  1.000 52.70038 ? 306 GLN   A C   1 
ATOM   2362 O  O   . GLN   A 1 306 ? -21.21699 0.86235   9.57692   1.000 49.53355 ? 306 GLN   A O   1 
ATOM   2363 C  CB  . GLN   A 1 306 ? -23.38387 0.17971   12.32368  1.000 55.69171 ? 306 GLN   A CB  1 
ATOM   2364 C  CG  . GLN   A 1 306 ? -24.35616 1.29817   11.96300  1.000 55.88186 ? 306 GLN   A CG  1 
ATOM   2365 C  CD  . GLN   A 1 306 ? -25.30181 1.61615   13.10151  1.000 61.74549 ? 306 GLN   A CD  1 
ATOM   2366 O  OE1 . GLN   A 1 306 ? -25.09400 1.16847   14.23078  1.000 69.33332 ? 306 GLN   A OE1 1 
ATOM   2367 N  NE2 . GLN   A 1 306 ? -26.34677 2.39211   12.81668  1.000 56.41382 ? 306 GLN   A NE2 1 
HETATM 2368 N  N1  . A1ARY B 2 .   ? -12.89817 -13.00240 -17.21784 1.000 27.76666 ? 401 A1ARY A N1  1 
HETATM 2369 C  C4  . A1ARY B 2 .   ? -12.65219 -10.46135 -17.10148 1.000 30.38478 ? 401 A1ARY A C4  1 
HETATM 2370 C  C5  . A1ARY B 2 .   ? -10.54913 -13.57774 -17.84029 1.000 27.01980 ? 401 A1ARY A C5  1 
HETATM 2371 C  C6  . A1ARY B 2 .   ? -9.59039  -13.86056 -18.83176 1.000 29.49871 ? 401 A1ARY A C6  1 
HETATM 2372 C  C7  . A1ARY B 2 .   ? -9.94724  -13.84082 -20.17831 1.000 29.85195 ? 401 A1ARY A C7  1 
HETATM 2373 C  C8  . A1ARY B 2 .   ? -11.25307 -13.54826 -20.53655 1.000 32.21287 ? 401 A1ARY A C8  1 
HETATM 2374 C  C10 . A1ARY B 2 .   ? -8.20426  -14.17385 -18.42370 1.000 30.35442 ? 401 A1ARY A C10 1 
HETATM 2375 C  C13 . A1ARY B 2 .   ? -5.58832  -14.68510 -17.52530 1.000 28.67352 ? 401 A1ARY A C13 1 
HETATM 2376 C  C15 . A1ARY B 2 .   ? -7.41703  -15.16470 -19.02879 1.000 33.20206 ? 401 A1ARY A C15 1 
HETATM 2377 C  C17 . A1ARY B 2 .   ? -14.86228 -16.12438 -16.55084 1.000 26.89182 ? 401 A1ARY A C17 1 
HETATM 2378 C  C1  . A1ARY B 2 .   ? -13.56546 -14.14975 -16.62711 1.000 25.29460 ? 401 A1ARY A C1  1 
HETATM 2379 C  C11 . A1ARY B 2 .   ? -7.66326  -13.44552 -17.36977 1.000 28.92954 ? 401 A1ARY A C11 1 
HETATM 2380 C  C12 . A1ARY B 2 .   ? -6.37986  -13.70143 -16.95036 1.000 26.97992 ? 401 A1ARY A C12 1 
HETATM 2381 C  C14 . A1ARY B 2 .   ? -6.11972  -15.40578 -18.58682 1.000 34.36376 ? 401 A1ARY A C14 1 
HETATM 2382 C  C16 . A1ARY B 2 .   ? -14.31502 -15.09875 -17.30489 1.000 27.32021 ? 401 A1ARY A C16 1 
HETATM 2383 C  C18 . A1ARY B 2 .   ? -14.66032 -16.20050 -15.19033 1.000 24.86781 ? 401 A1ARY A C18 1 
HETATM 2384 C  C19 . A1ARY B 2 .   ? -13.38868 -14.31424 -15.25069 1.000 23.40244 ? 401 A1ARY A C19 1 
HETATM 2385 C  C2  . A1ARY B 2 .   ? -11.85629 -13.27051 -18.20402 1.000 30.06354 ? 401 A1ARY A C2  1 
HETATM 2386 C  C3  . A1ARY B 2 .   ? -13.31268 -11.76483 -16.72726 1.000 28.84460 ? 401 A1ARY A C3  1 
HETATM 2387 C  C9  . A1ARY B 2 .   ? -12.19920 -13.27504 -19.55762 1.000 29.04853 ? 401 A1ARY A C9  1 
HETATM 2388 N  N2  . A1ARY B 2 .   ? -13.92518 -15.30721 -14.52725 1.000 22.43162 ? 401 A1ARY A N2  1 
HETATM 2389 O  O1  . A1ARY B 2 .   ? -12.29496 -10.36171 -18.44064 1.000 35.71565 ? 401 A1ARY A O1  1 
HETATM 2390 O  O2  . A1ARY B 2 .   ? -14.18521 -11.67459 -15.86665 1.000 30.59135 ? 401 A1ARY A O2  1 
HETATM 2391 CL CL1 . A1ARY B 2 .   ? -5.82496  -12.72800 -15.63125 1.000 33.07133 ? 401 A1ARY A CL1 1 
HETATM 2392 CL CL2 . A1ARY B 2 .   ? -15.81883 -17.33827 -17.32066 1.000 33.63973 ? 401 A1ARY A CL2 1 
HETATM 2393 O  O   . HOH   C 3 .   ? -3.42596  -24.54265 -6.43783  1.000 20.50644 ? 501 HOH   A O   1 
HETATM 2394 O  O   . HOH   C 3 .   ? -15.09207 -42.41855 15.79827  1.000 38.03921 ? 502 HOH   A O   1 
HETATM 2395 O  O   . HOH   C 3 .   ? -7.41898  -25.49656 8.06570   1.000 30.57537 ? 503 HOH   A O   1 
HETATM 2396 O  O   . HOH   C 3 .   ? -13.53994 -22.47613 -16.97349 1.000 35.17625 ? 504 HOH   A O   1 
HETATM 2397 O  O   . HOH   C 3 .   ? 0.68143   0.38582   -2.61298  1.000 52.49505 ? 505 HOH   A O   1 
HETATM 2398 O  O   . HOH   C 3 .   ? -22.82365 -28.53356 1.89304   1.000 26.78474 ? 506 HOH   A O   1 
HETATM 2399 O  O   . HOH   C 3 .   ? -13.98197 -1.10591  -25.30440 1.000 55.87036 ? 507 HOH   A O   1 
HETATM 2400 O  O   . HOH   C 3 .   ? -16.03428 -34.81234 3.56586   1.000 26.89506 ? 508 HOH   A O   1 
HETATM 2401 O  O   . HOH   C 3 .   ? -3.36152  -21.89974 19.77714  1.000 32.19254 ? 509 HOH   A O   1 
HETATM 2402 O  O   . HOH   C 3 .   ? -7.09631  12.95335  -6.90478  1.000 31.07021 ? 510 HOH   A O   1 
HETATM 2403 O  O   . HOH   C 3 .   ? 5.17253   -7.35615  -13.82608 1.000 32.46905 ? 511 HOH   A O   1 
HETATM 2404 O  O   . HOH   C 3 .   ? -11.69675 -36.45618 24.71832  1.000 38.53003 ? 512 HOH   A O   1 
HETATM 2405 O  O   . HOH   C 3 .   ? -9.26532  -42.01349 16.08513  1.000 43.34061 ? 513 HOH   A O   1 
HETATM 2406 O  O   . HOH   C 3 .   ? -4.70221  -28.85539 3.55414   1.000 37.08541 ? 514 HOH   A O   1 
HETATM 2407 O  O   . HOH   C 3 .   ? -7.32590  -24.31313 5.50862   1.000 25.42441 ? 515 HOH   A O   1 
HETATM 2408 O  O   . HOH   C 3 .   ? -15.44265 2.05760   -18.69010 1.000 27.66036 ? 516 HOH   A O   1 
HETATM 2409 O  O   . HOH   C 3 .   ? -18.14786 -33.79895 25.18789  1.000 31.04835 ? 517 HOH   A O   1 
HETATM 2410 O  O   . HOH   C 3 .   ? -21.91798 -16.58608 -12.54859 1.000 32.52711 ? 518 HOH   A O   1 
HETATM 2411 O  O   . HOH   C 3 .   ? -15.45302 -46.82283 5.64516   1.000 40.00017 ? 519 HOH   A O   1 
HETATM 2412 O  O   . HOH   C 3 .   ? -19.87748 -36.52132 19.55948  1.000 30.59624 ? 520 HOH   A O   1 
HETATM 2413 O  O   . HOH   C 3 .   ? -29.44960 -19.49711 13.79434  1.000 30.60874 ? 521 HOH   A O   1 
HETATM 2414 O  O   . HOH   C 3 .   ? -13.39399 -8.25595  -19.16153 1.000 36.57892 ? 522 HOH   A O   1 
HETATM 2415 O  O   . HOH   C 3 .   ? -11.10899 -33.39660 0.73524   1.000 35.63477 ? 523 HOH   A O   1 
HETATM 2416 O  O   . HOH   C 3 .   ? -17.18711 2.53670   6.85202   1.000 27.08073 ? 524 HOH   A O   1 
HETATM 2417 O  O   . HOH   C 3 .   ? -15.28411 -2.21052  -23.84333 1.000 37.28524 ? 525 HOH   A O   1 
HETATM 2418 O  O   . HOH   C 3 .   ? 2.24045   4.52163   -19.27969 1.000 29.35794 ? 526 HOH   A O   1 
HETATM 2419 O  O   . HOH   C 3 .   ? -12.74776 -5.12454  8.53432   1.000 23.90337 ? 527 HOH   A O   1 
HETATM 2420 O  O   . HOH   C 3 .   ? -19.73444 2.70071   -0.23706  1.000 21.73042 ? 528 HOH   A O   1 
HETATM 2421 O  O   . HOH   C 3 .   ? -28.45354 -29.36072 20.33525  1.000 26.99544 ? 529 HOH   A O   1 
HETATM 2422 O  O   . HOH   C 3 .   ? -15.36170 -21.61622 18.53728  1.000 26.60356 ? 530 HOH   A O   1 
HETATM 2423 O  O   . HOH   C 3 .   ? -8.50593  -25.49641 24.03845  1.000 33.57510 ? 531 HOH   A O   1 
HETATM 2424 O  O   . HOH   C 3 .   ? -6.51608  -17.43552 -6.45495  1.000 11.52676 ? 532 HOH   A O   1 
HETATM 2425 O  O   . HOH   C 3 .   ? -12.57783 8.29847   -17.74252 1.000 31.69393 ? 533 HOH   A O   1 
HETATM 2426 O  O   . HOH   C 3 .   ? -30.77558 -31.39691 7.62299   1.000 26.89402 ? 534 HOH   A O   1 
HETATM 2427 O  O   . HOH   C 3 .   ? -31.27357 -28.76046 2.00377   1.000 31.41504 ? 535 HOH   A O   1 
HETATM 2428 O  O   . HOH   C 3 .   ? -17.17842 -6.27881  -6.48627  1.000 13.27720 ? 536 HOH   A O   1 
HETATM 2429 O  O   . HOH   C 3 .   ? -14.58967 -21.47475 -2.34178  1.000 16.31085 ? 537 HOH   A O   1 
HETATM 2430 O  O   . HOH   C 3 .   ? -14.96456 -33.03087 1.67563   1.000 28.74643 ? 538 HOH   A O   1 
HETATM 2431 O  O   . HOH   C 3 .   ? -16.75612 -14.14511 6.03757   1.000 19.11083 ? 539 HOH   A O   1 
HETATM 2432 O  O   . HOH   C 3 .   ? -9.89231  8.94286   -18.43944 1.000 32.55749 ? 540 HOH   A O   1 
HETATM 2433 O  O   . HOH   C 3 .   ? -1.96947  -34.63331 15.90054  1.000 38.71223 ? 541 HOH   A O   1 
HETATM 2434 O  O   . HOH   C 3 .   ? 1.26550   -23.83113 -19.46603 1.000 47.03859 ? 542 HOH   A O   1 
HETATM 2435 O  O   . HOH   C 3 .   ? 1.42682   -21.06471 -15.42802 1.000 30.84004 ? 543 HOH   A O   1 
HETATM 2436 O  O   . HOH   C 3 .   ? -0.00000  -8.90147  0.00000   0.50  16.19921 ? 544 HOH   A O   1 
HETATM 2437 O  O   . HOH   C 3 .   ? -2.21203  -2.95411  -24.80307 1.000 36.73707 ? 545 HOH   A O   1 
HETATM 2438 O  O   . HOH   C 3 .   ? -3.03120  -1.70875  -3.40900  1.000 23.85957 ? 546 HOH   A O   1 
HETATM 2439 O  O   . HOH   C 3 .   ? -32.43354 -19.00582 17.73863  1.000 25.06517 ? 547 HOH   A O   1 
HETATM 2440 O  O   . HOH   C 3 .   ? -24.05836 -42.29118 9.28507   1.000 38.70964 ? 548 HOH   A O   1 
HETATM 2441 O  O   . HOH   C 3 .   ? -8.61684  2.66533   -24.56879 1.000 34.60346 ? 549 HOH   A O   1 
HETATM 2442 O  O   . HOH   C 3 .   ? -20.70889 -39.47337 13.87058  1.000 29.11108 ? 550 HOH   A O   1 
HETATM 2443 O  O   . HOH   C 3 .   ? -17.27730 -37.93775 25.83252  1.000 35.73341 ? 551 HOH   A O   1 
HETATM 2444 O  O   . HOH   C 3 .   ? -10.84930 -21.80342 9.18145   1.000 19.82837 ? 552 HOH   A O   1 
HETATM 2445 O  O   . HOH   C 3 .   ? 3.65315   -5.40714  -11.80349 1.000 22.48938 ? 553 HOH   A O   1 
HETATM 2446 O  O   . HOH   C 3 .   ? -1.84553  -25.10050 -8.75468  1.000 25.30872 ? 554 HOH   A O   1 
HETATM 2447 O  O   . HOH   C 3 .   ? -21.72322 -13.77913 -11.16629 1.000 25.21483 ? 555 HOH   A O   1 
HETATM 2448 O  O   . HOH   C 3 .   ? 6.38390   -6.45901  -25.08531 1.000 40.81669 ? 556 HOH   A O   1 
HETATM 2449 O  O   . HOH   C 3 .   ? -19.70112 6.99812   -5.30493  1.000 25.84780 ? 557 HOH   A O   1 
HETATM 2450 O  O   . HOH   C 3 .   ? -11.29119 -27.52646 -4.89415  1.000 24.67545 ? 558 HOH   A O   1 
HETATM 2451 O  O   . HOH   C 3 .   ? -17.93949 -25.44520 7.32342   1.000 14.08184 ? 559 HOH   A O   1 
HETATM 2452 O  O   . HOH   C 3 .   ? -4.21796  8.61438   -3.55669  1.000 33.05274 ? 560 HOH   A O   1 
HETATM 2453 O  O   . HOH   C 3 .   ? 1.23685   7.62636   -20.08732 1.000 30.56799 ? 561 HOH   A O   1 
HETATM 2454 O  O   . HOH   C 3 .   ? 3.22120   -11.78273 -18.00714 1.000 32.84926 ? 562 HOH   A O   1 
HETATM 2455 O  O   . HOH   C 3 .   ? -18.18535 -27.10614 1.54779   1.000 29.73945 ? 563 HOH   A O   1 
HETATM 2456 O  O   . HOH   C 3 .   ? 0.80003   -20.52534 -12.88878 1.000 27.58000 ? 564 HOH   A O   1 
HETATM 2457 O  O   . HOH   C 3 .   ? -19.16908 -4.87558  -21.56090 1.000 37.77021 ? 565 HOH   A O   1 
HETATM 2458 O  O   . HOH   C 3 .   ? -25.55977 -1.74273  -6.38890  1.000 24.95931 ? 566 HOH   A O   1 
HETATM 2459 O  O   . HOH   C 3 .   ? -1.94589  -24.63267 -1.54547  1.000 24.62567 ? 567 HOH   A O   1 
HETATM 2460 O  O   . HOH   C 3 .   ? -24.67647 -38.19923 1.69005   1.000 37.37847 ? 568 HOH   A O   1 
HETATM 2461 O  O   . HOH   C 3 .   ? 3.36497   -12.86678 -14.15154 1.000 30.63735 ? 569 HOH   A O   1 
HETATM 2462 O  O   . HOH   C 3 .   ? -10.64065 -16.80408 -17.10372 1.000 24.47272 ? 570 HOH   A O   1 
HETATM 2463 O  O   . HOH   C 3 .   ? -4.37248  -8.93427  -14.01343 1.000 18.77463 ? 571 HOH   A O   1 
HETATM 2464 O  O   . HOH   C 3 .   ? -4.74007  -3.95445  6.11508   1.000 27.16067 ? 572 HOH   A O   1 
HETATM 2465 O  O   . HOH   C 3 .   ? -17.38894 -5.76601  -16.73626 1.000 22.97476 ? 573 HOH   A O   1 
HETATM 2466 O  O   . HOH   C 3 .   ? -4.875    -24.802   4.176     1.000 38.45846 ? 574 HOH   A O   1 
HETATM 2467 O  O   . HOH   C 3 .   ? -23.64865 -43.78615 4.52245   1.000 39.97192 ? 575 HOH   A O   1 
HETATM 2468 O  O   . HOH   C 3 .   ? -4.00757  -34.12366 6.82712   1.000 36.62310 ? 576 HOH   A O   1 
HETATM 2469 O  O   . HOH   C 3 .   ? -5.96343  -7.17408  -0.00842  1.000 16.29219 ? 577 HOH   A O   1 
HETATM 2470 O  O   . HOH   C 3 .   ? -1.65834  5.46009   -9.95784  1.000 26.78628 ? 578 HOH   A O   1 
HETATM 2471 O  O   . HOH   C 3 .   ? -12.74754 -37.53427 1.59569   1.000 28.95103 ? 579 HOH   A O   1 
HETATM 2472 O  O   . HOH   C 3 .   ? -3.59620  -23.98993 12.99147  1.000 28.32850 ? 580 HOH   A O   1 
HETATM 2473 O  O   . HOH   C 3 .   ? -19.16626 -24.26291 0.19600   1.000 37.93685 ? 581 HOH   A O   1 
HETATM 2474 O  O   . HOH   C 3 .   ? -15.84206 13.56852  -3.67792  1.000 35.58575 ? 582 HOH   A O   1 
HETATM 2475 O  O   . HOH   C 3 .   ? -28.38672 -2.79916  -3.59280  1.000 18.08411 ? 583 HOH   A O   1 
HETATM 2476 O  O   . HOH   C 3 .   ? -19.09554 -18.34912 5.44617   1.000 17.61868 ? 584 HOH   A O   1 
HETATM 2477 O  O   . HOH   C 3 .   ? 1.39035   -13.77122 -4.26450  1.000 13.78509 ? 585 HOH   A O   1 
HETATM 2478 O  O   . HOH   C 3 .   ? -2.46437  -5.62558  2.32718   1.000 15.88541 ? 586 HOH   A O   1 
HETATM 2479 O  O   . HOH   C 3 .   ? -10.28442 -27.19350 -9.04090  1.000 21.98370 ? 587 HOH   A O   1 
HETATM 2480 O  O   . HOH   C 3 .   ? -1.14988  -19.85876 3.95892   1.000 14.95259 ? 588 HOH   A O   1 
HETATM 2481 O  O   . HOH   C 3 .   ? -9.45144  -7.46619  8.78230   1.000 26.12346 ? 589 HOH   A O   1 
HETATM 2482 O  O   . HOH   C 3 .   ? -5.23364  -22.46643 -17.54424 1.000 28.33854 ? 590 HOH   A O   1 
HETATM 2483 O  O   . HOH   C 3 .   ? -30.86322 -24.14243 9.32880   1.000 27.51111 ? 591 HOH   A O   1 
HETATM 2484 O  O   . HOH   C 3 .   ? -14.72709 -15.89169 8.99739   1.000 23.01600 ? 592 HOH   A O   1 
HETATM 2485 O  O   . HOH   C 3 .   ? -16.15092 -40.00952 3.66698   1.000 33.65292 ? 593 HOH   A O   1 
HETATM 2486 O  O   . HOH   C 3 .   ? -18.92723 -34.97610 2.65896   1.000 25.78451 ? 594 HOH   A O   1 
HETATM 2487 O  O   . HOH   C 3 .   ? -1.58993  -37.97171 13.75604  1.000 41.25863 ? 595 HOH   A O   1 
HETATM 2488 O  O   . HOH   C 3 .   ? -3.73874  -35.26814 9.24936   1.000 35.27154 ? 596 HOH   A O   1 
HETATM 2489 O  O   . HOH   C 3 .   ? -10.80850 -25.77279 23.10873  1.000 31.02876 ? 597 HOH   A O   1 
HETATM 2490 O  O   . HOH   C 3 .   ? -24.31789 -12.94581 -10.97900 1.000 35.91521 ? 598 HOH   A O   1 
HETATM 2491 O  O   . HOH   C 3 .   ? -2.88497  -24.10117 1.88823   1.000 24.28881 ? 599 HOH   A O   1 
HETATM 2492 O  O   . HOH   C 3 .   ? -0.18857  -1.33003  -24.70311 1.000 32.97826 ? 600 HOH   A O   1 
HETATM 2493 O  O   . HOH   C 3 .   ? -16.14487 -22.67656 -8.96635  1.000 20.26597 ? 601 HOH   A O   1 
HETATM 2494 O  O   . HOH   C 3 .   ? -25.46153 -26.31676 5.92486   1.000 24.21740 ? 602 HOH   A O   1 
HETATM 2495 O  O   . HOH   C 3 .   ? -0.95577  9.92630   -19.39687 1.000 32.80045 ? 603 HOH   A O   1 
HETATM 2496 O  O   . HOH   C 3 .   ? -28.31940 -25.88323 3.82751   1.000 36.99369 ? 604 HOH   A O   1 
HETATM 2497 O  O   . HOH   C 3 .   ? 4.44124   -3.52580  -9.31054  1.000 27.77822 ? 605 HOH   A O   1 
HETATM 2498 O  O   . HOH   C 3 .   ? -29.53826 -25.00568 7.02774   1.000 28.61040 ? 606 HOH   A O   1 
HETATM 2499 O  O   . HOH   C 3 .   ? -11.90969 -29.48518 -2.00432  1.000 33.13661 ? 607 HOH   A O   1 
HETATM 2500 O  O   . HOH   C 3 .   ? -2.33532  -15.66363 2.42303   1.000 13.26824 ? 608 HOH   A O   1 
HETATM 2501 O  O   . HOH   C 3 .   ? 5.01828   -8.49299  -17.23609 1.000 31.15015 ? 609 HOH   A O   1 
HETATM 2502 O  O   . HOH   C 3 .   ? -3.63808  -27.78692 9.22071   1.000 32.85982 ? 610 HOH   A O   1 
HETATM 2503 O  O   . HOH   C 3 .   ? -11.28367 -9.81989  4.39177   1.000 16.59371 ? 611 HOH   A O   1 
HETATM 2504 O  O   . HOH   C 3 .   ? 5.25563   0.59754   -17.52789 1.000 28.57900 ? 612 HOH   A O   1 
HETATM 2505 O  O   . HOH   C 3 .   ? -7.84318  -25.95615 -12.67169 1.000 24.33937 ? 613 HOH   A O   1 
HETATM 2506 O  O   . HOH   C 3 .   ? -7.89476  -20.25814 7.87179   1.000 23.47172 ? 614 HOH   A O   1 
HETATM 2507 O  O   . HOH   C 3 .   ? -7.25349  4.17715   -2.39104  1.000 22.41370 ? 615 HOH   A O   1 
HETATM 2508 O  O   . HOH   C 3 .   ? -13.41060 1.87029   -25.76087 1.000 35.93913 ? 616 HOH   A O   1 
HETATM 2509 O  O   . HOH   C 3 .   ? 1.19198   -12.88708 -12.58689 1.000 20.19756 ? 617 HOH   A O   1 
HETATM 2510 O  O   . HOH   C 3 .   ? 3.72841   1.58499   -12.73400 1.000 27.08797 ? 618 HOH   A O   1 
HETATM 2511 O  O   . HOH   C 3 .   ? -9.89946  -25.97383 -6.76927  1.000 19.10535 ? 619 HOH   A O   1 
HETATM 2512 O  O   . HOH   C 3 .   ? -12.79278 -15.09876 7.26978   1.000 25.12686 ? 620 HOH   A O   1 
HETATM 2513 O  O   . HOH   C 3 .   ? -0.00000  -16.89868 0.00000   0.50  15.63810 ? 621 HOH   A O   1 
HETATM 2514 O  O   . HOH   C 3 .   ? -12.64905 14.71607  -4.69586  1.000 29.93262 ? 622 HOH   A O   1 
HETATM 2515 O  O   . HOH   C 3 .   ? 3.56264   -7.68382  -24.32979 1.000 38.36942 ? 623 HOH   A O   1 
HETATM 2516 O  O   . HOH   C 3 .   ? -20.46400 1.98849   -11.51137 1.000 25.08744 ? 624 HOH   A O   1 
HETATM 2517 O  O   . HOH   C 3 .   ? 0.54609   8.26635   -14.39924 1.000 26.53854 ? 625 HOH   A O   1 
HETATM 2518 O  O   . HOH   C 3 .   ? 1.62964   -12.65303 -16.17144 1.000 25.16046 ? 626 HOH   A O   1 
HETATM 2519 O  O   . HOH   C 3 .   ? -22.07569 -16.81520 9.02978   1.000 17.76448 ? 627 HOH   A O   1 
HETATM 2520 O  O   . HOH   C 3 .   ? -2.93914  -13.95137 6.45721   1.000 18.52297 ? 628 HOH   A O   1 
HETATM 2521 O  O   . HOH   C 3 .   ? 0.28390   -23.63866 -10.73553 1.000 27.33138 ? 629 HOH   A O   1 
HETATM 2522 O  O   . HOH   C 3 .   ? -12.86753 18.03902  -10.13328 1.000 38.97954 ? 630 HOH   A O   1 
HETATM 2523 O  O   . HOH   C 3 .   ? -17.19068 -6.68430  -19.85129 1.000 32.37850 ? 631 HOH   A O   1 
HETATM 2524 O  O   . HOH   C 3 .   ? 0.04454   10.38774  -15.66401 1.000 35.75705 ? 632 HOH   A O   1 
HETATM 2525 O  O   . HOH   C 3 .   ? -8.27105  -27.67370 9.49274   1.000 22.31259 ? 633 HOH   A O   1 
HETATM 2526 O  O   . HOH   C 3 .   ? 1.37719   -13.95385 -10.01535 1.000 16.38262 ? 634 HOH   A O   1 
HETATM 2527 O  O   . HOH   C 3 .   ? -21.81572 -17.47813 6.31615   1.000 18.38964 ? 635 HOH   A O   1 
HETATM 2528 O  O   . HOH   C 3 .   ? -12.65956 -18.67803 18.80623  1.000 31.55353 ? 636 HOH   A O   1 
HETATM 2529 O  O   . HOH   C 3 .   ? -7.80716  -44.56468 13.29972  1.000 42.85304 ? 637 HOH   A O   1 
HETATM 2530 O  O   . HOH   C 3 .   ? 1.11992   -12.22003 -8.11631  1.000 13.48413 ? 638 HOH   A O   1 
HETATM 2531 O  O   . HOH   C 3 .   ? -12.75837 -18.47188 12.49186  1.000 23.51501 ? 639 HOH   A O   1 
HETATM 2532 O  O   . HOH   C 3 .   ? -0.52913  -25.28372 -12.80386 1.000 30.66583 ? 640 HOH   A O   1 
HETATM 2533 O  O   . HOH   C 3 .   ? -18.68298 -16.41342 -19.25294 1.000 25.54855 ? 641 HOH   A O   1 
HETATM 2534 O  O   . HOH   C 3 .   ? -3.11565  -29.47852 -10.85857 1.000 36.85969 ? 642 HOH   A O   1 
HETATM 2535 O  O   . HOH   C 3 .   ? -23.81566 -16.95669 -0.06452  1.000 19.86985 ? 643 HOH   A O   1 
HETATM 2536 O  O   . HOH   C 3 .   ? -4.35310  -21.19876 6.64703   1.000 20.66459 ? 644 HOH   A O   1 
HETATM 2537 O  O   . HOH   C 3 .   ? -3.46034  5.91560   -27.29731 1.000 38.66358 ? 645 HOH   A O   1 
HETATM 2538 O  O   . HOH   C 3 .   ? -6.59135  -31.52461 21.56149  1.000 30.03867 ? 646 HOH   A O   1 
HETATM 2539 O  O   . HOH   C 3 .   ? -4.92588  -1.58392  4.71877   1.000 24.04626 ? 647 HOH   A O   1 
HETATM 2540 O  O   . HOH   C 3 .   ? -10.04845 3.61586   5.91702   1.000 22.09416 ? 648 HOH   A O   1 
HETATM 2541 O  O   . HOH   C 3 .   ? -7.73541  3.00607   4.93213   1.000 35.18600 ? 649 HOH   A O   1 
HETATM 2542 O  O   . HOH   C 3 .   ? -19.44709 -20.10344 24.42420  1.000 39.41591 ? 650 HOH   A O   1 
HETATM 2543 O  O   . HOH   C 3 .   ? -4.47457  -19.34437 -18.14484 1.000 30.45871 ? 651 HOH   A O   1 
HETATM 2544 O  O   . HOH   C 3 .   ? -11.06556 -17.02470 9.84390   1.000 31.56964 ? 652 HOH   A O   1 
HETATM 2545 O  O   . HOH   C 3 .   ? -15.76357 -28.94741 0.15474   1.000 27.43185 ? 653 HOH   A O   1 
HETATM 2546 O  O   . HOH   C 3 .   ? -25.50150 -31.58069 0.00000   0.50  24.52421 ? 654 HOH   A O   1 
HETATM 2547 O  O   . HOH   C 3 .   ? -0.26819  2.41090   -27.68134 1.000 31.35483 ? 655 HOH   A O   1 
HETATM 2548 O  O   . HOH   C 3 .   ? -24.73994 -32.01959 24.70000  1.000 34.56232 ? 656 HOH   A O   1 
HETATM 2549 O  O   . HOH   C 3 .   ? -7.74831  -32.80256 -5.08756  1.000 32.81449 ? 657 HOH   A O   1 
HETATM 2550 O  O   . HOH   C 3 .   ? 1.24499   -2.80570  -26.77892 1.000 32.12036 ? 658 HOH   A O   1 
HETATM 2551 O  O   . HOH   C 3 .   ? -5.27225  -13.80107 7.94000   1.000 21.38941 ? 659 HOH   A O   1 
HETATM 2552 O  O   . HOH   C 3 .   ? -15.00443 -12.14538 8.98443   1.000 26.87743 ? 660 HOH   A O   1 
HETATM 2553 O  O   . HOH   C 3 .   ? -12.72528 -29.55414 24.30474  1.000 33.87443 ? 661 HOH   A O   1 
HETATM 2554 O  O   . HOH   C 3 .   ? -30.87219 -34.85756 14.84591  1.000 31.65976 ? 662 HOH   A O   1 
HETATM 2555 O  O   . HOH   C 3 .   ? 0.30671   -17.47653 -2.69844  1.000 14.99590 ? 663 HOH   A O   1 
HETATM 2556 O  O   . HOH   C 3 .   ? -1.30693  -25.10487 16.95323  1.000 30.34143 ? 664 HOH   A O   1 
HETATM 2557 O  O   . HOH   C 3 .   ? -31.37013 -36.59069 8.68714   1.000 34.81708 ? 665 HOH   A O   1 
HETATM 2558 O  O   . HOH   C 3 .   ? -5.04031  -21.89079 12.88710  1.000 34.43834 ? 666 HOH   A O   1 
HETATM 2559 O  O   . HOH   C 3 .   ? -22.02554 -2.79532  6.13167   1.000 27.34024 ? 667 HOH   A O   1 
HETATM 2560 O  O   . HOH   C 3 .   ? -14.46505 -25.23514 25.94735  1.000 33.86740 ? 668 HOH   A O   1 
HETATM 2561 O  O   . HOH   C 3 .   ? 2.40241   -17.43148 -9.49581  1.000 21.65732 ? 669 HOH   A O   1 
HETATM 2562 O  O   . HOH   C 3 .   ? -3.21158  -7.68284  0.71358   1.000 23.02496 ? 670 HOH   A O   1 
HETATM 2563 O  O   . HOH   C 3 .   ? -13.58465 -29.94471 0.00523   1.000 35.10348 ? 671 HOH   A O   1 
HETATM 2564 O  O   . HOH   C 3 .   ? -25.50150 -14.50523 0.00000   0.50  18.98686 ? 672 HOH   A O   1 
HETATM 2565 O  O   . HOH   C 3 .   ? -1.19453  -30.37644 -7.14617  1.000 31.05649 ? 673 HOH   A O   1 
HETATM 2566 O  O   . HOH   C 3 .   ? -27.30068 -29.05855 0.16388   1.000 32.99865 ? 674 HOH   A O   1 
HETATM 2567 O  O   . HOH   C 3 .   ? -3.48452  -28.90692 1.36547   1.000 35.07077 ? 675 HOH   A O   1 
HETATM 2568 O  O   . HOH   C 3 .   ? -4.51195  -28.36197 -0.59921  1.000 24.43393 ? 676 HOH   A O   1 
HETATM 2569 O  O   . HOH   C 3 .   ? -28.81189 -20.78900 15.98762  1.000 35.20853 ? 677 HOH   A O   1 
HETATM 2570 O  O   . HOH   C 3 .   ? -15.30470 -10.04199 9.87987   1.000 28.79024 ? 678 HOH   A O   1 
HETATM 2571 O  O   . HOH   C 3 .   ? 2.97698   3.73898   -14.72915 1.000 34.76210 ? 679 HOH   A O   1 
HETATM 2572 O  O   . HOH   C 3 .   ? -11.65541 5.71194   4.64206   1.000 26.96420 ? 680 HOH   A O   1 
HETATM 2573 O  O   . HOH   C 3 .   ? -7.91063  -23.64695 7.46332   1.000 40.31221 ? 681 HOH   A O   1 
HETATM 2574 O  O   . HOH   C 3 .   ? -27.73108 -21.01943 1.89618   1.000 25.50167 ? 682 HOH   A O   1 
HETATM 2575 O  O   . HOH   C 3 .   ? -10.18084 -33.31671 -3.55624  1.000 36.91190 ? 683 HOH   A O   1 
HETATM 2576 O  O   . HOH   C 3 .   ? -12.94631 -42.35568 17.44410  1.000 39.13923 ? 684 HOH   A O   1 
HETATM 2577 O  O   . HOH   C 3 .   ? -1.223    -24.092   14.573    1.000 29.67222 ? 685 HOH   A O   1 
HETATM 2578 O  O   . HOH   C 3 .   ? -24.42997 -26.81969 3.17313   1.000 34.61532 ? 686 HOH   A O   1 
HETATM 2579 O  O   . HOH   C 3 .   ? -0.78566  7.72962   -10.39072 1.000 34.80228 ? 687 HOH   A O   1 
HETATM 2580 O  O   . HOH   C 3 .   ? -13.38880 -7.88708  8.82651   1.000 33.38237 ? 688 HOH   A O   1 
HETATM 2581 O  O   . HOH   C 3 .   ? 4.18493   -10.58141 -16.38437 1.000 33.57588 ? 689 HOH   A O   1 
HETATM 2582 O  O   . HOH   C 3 .   ? 4.06998   3.15781   -17.45682 1.000 29.16709 ? 690 HOH   A O   1 
HETATM 2583 O  O   . HOH   C 3 .   ? -14.88028 -16.89514 16.38488  1.000 33.74770 ? 691 HOH   A O   1 
HETATM 2584 O  O   . HOH   C 3 .   ? -3.11269  -23.98052 10.53394  1.000 28.17414 ? 692 HOH   A O   1 
HETATM 2585 O  O   . HOH   C 3 .   ? -0.82445  -27.62942 -12.24637 1.000 30.29724 ? 693 HOH   A O   1 
HETATM 2586 O  O   . HOH   C 3 .   ? -12.82794 -28.53259 -9.08623  1.000 28.66584 ? 694 HOH   A O   1 
HETATM 2587 O  O   . HOH   C 3 .   ? -7.57420  -21.45934 12.24858  1.000 28.08278 ? 695 HOH   A O   1 
HETATM 2588 O  O   . HOH   C 3 .   ? -20.63867 -34.71751 24.58256  1.000 34.26911 ? 696 HOH   A O   1 
HETATM 2589 O  O   . HOH   C 3 .   ? -22.19153 3.37865   0.58319   1.000 27.88533 ? 697 HOH   A O   1 
HETATM 2590 O  O   . HOH   C 3 .   ? -8.85578  -11.71329 7.63794   1.000 24.70191 ? 698 HOH   A O   1 
HETATM 2591 O  O   . HOH   C 3 .   ? -10.63305 -10.00758 7.20920   1.000 24.54294 ? 699 HOH   A O   1 
HETATM 2592 O  O   . HOH   C 3 .   ? -33.03467 -30.26857 5.85167   1.000 32.17123 ? 700 HOH   A O   1 
HETATM 2593 O  O   . HOH   C 3 .   ? -5.27602  2.79061   -28.09936 1.000 43.32804 ? 701 HOH   A O   1 
HETATM 2594 O  O   . HOH   C 3 .   ? -25.50150 -38.44413 0.00000   0.50  64.88163 ? 702 HOH   A O   1 
HETATM 2595 O  O   . HOH   C 3 .   ? -8.42515  -22.23835 8.81218   1.000 28.19548 ? 703 HOH   A O   1 
HETATM 2596 O  O   . HOH   C 3 .   ? -6.71584  -18.69710 9.42586   1.000 25.65724 ? 704 HOH   A O   1 
HETATM 2597 O  O   . HOH   C 3 .   ? -2.23098  -26.52873 2.23762   1.000 29.56443 ? 705 HOH   A O   1 
HETATM 2598 O  O   . HOH   C 3 .   ? -1.91755  5.87732   -7.46097  1.000 31.37825 ? 706 HOH   A O   1 
HETATM 2599 O  O   . HOH   C 3 .   ? -14.08968 -29.86239 26.83351  1.000 40.45528 ? 707 HOH   A O   1 
HETATM 2600 O  O   . HOH   C 3 .   ? -22.88321 -41.06667 12.78338  1.000 34.65473 ? 708 HOH   A O   1 
HETATM 2601 O  O   . HOH   C 3 .   ? -19.93924 -37.43049 2.81639   1.000 36.90260 ? 709 HOH   A O   1 
HETATM 2602 O  O   . HOH   C 3 .   ? 4.845     0.079     -6.459    1.000 28.52101 ? 710 HOH   A O   1 
HETATM 2603 O  O   . HOH   C 3 .   ? -32.86105 -28.32527 4.08585   1.000 35.89150 ? 711 HOH   A O   1 
HETATM 2604 O  O   . HOH   C 3 .   ? -2.468    -25.205   6.682     1.000 28.47568 ? 712 HOH   A O   1 
HETATM 2605 O  O   . HOH   C 3 .   ? 5.41834   2.19125   -11.36434 1.000 36.42542 ? 713 HOH   A O   1 
HETATM 2606 O  O   . HOH   C 3 .   ? -28.68051 -27.10913 22.46416  1.000 33.58435 ? 714 HOH   A O   1 
HETATM 2607 O  O   . HOH   C 3 .   ? -8.32908  -11.36943 10.17342  1.000 35.49128 ? 715 HOH   A O   1 
HETATM 2608 O  O   . HOH   C 3 .   ? -31.99603 -25.56548 10.95501  1.000 29.09190 ? 716 HOH   A O   1 
HETATM 2609 O  O   . HOH   C 3 .   ? 0.921     1.630     -0.903    1.000 43.30823 ? 717 HOH   A O   1 
HETATM 2610 O  O   . HOH   C 3 .   ? -15.24279 -17.94865 18.41329  1.000 32.05143 ? 718 HOH   A O   1 
HETATM 2611 O  O   . HOH   C 3 .   ? -3.407    -23.325   5.459     1.000 24.04326 ? 719 HOH   A O   1 
HETATM 2612 O  O   . HOH   C 3 .   ? -18.619   -25.773   -2.670    1.000 38.93315 ? 720 HOH   A O   1 
HETATM 2613 O  O   . HOH   C 3 .   ? 3.81324   -14.99279 -9.82049  1.000 21.92574 ? 721 HOH   A O   1 
HETATM 2614 O  O   . HOH   C 3 .   ? -0.00000  -24.24010 0.00000   0.50  27.71683 ? 722 HOH   A O   1 
HETATM 2615 O  O   . HOH   C 3 .   ? -0.61613  -23.89102 -3.73164  1.000 22.86941 ? 723 HOH   A O   1 
HETATM 2616 O  O   . HOH   C 3 .   ? 1.408     -22.429   -3.540    1.000 21.64994 ? 724 HOH   A O   1 
HETATM 2617 O  O   . HOH   C 3 .   ? -1.19952  -35.11908 10.56179  1.000 36.56553 ? 725 HOH   A O   1 
HETATM 2618 O  O   . HOH   C 3 .   ? -10.63423 -20.47588 11.44985  1.000 27.08672 ? 726 HOH   A O   1 
HETATM 2619 O  O   . HOH   C 3 .   ? -12.43528 -9.61178  8.95230   1.000 27.32335 ? 727 HOH   A O   1 
HETATM 2620 O  O   . HOH   C 3 .   ? 4.87160   0.00029   -14.71655 1.000 32.51320 ? 728 HOH   A O   1 
HETATM 2621 O  O   . HOH   C 3 .   ? -25.50150 -21.54525 0.00000   0.50  24.83492 ? 729 HOH   A O   1 
HETATM 2622 O  O   . HOH   C 3 .   ? -13.44484 -13.58288 9.97925   1.000 38.78612 ? 730 HOH   A O   1 
HETATM 2623 O  O   . HOH   C 3 .   ? -11.28027 -33.61035 25.34938  1.000 38.25250 ? 731 HOH   A O   1 
HETATM 2624 O  O   . HOH   C 3 .   ? -15.17537 -37.89261 2.64676   1.000 31.71667 ? 732 HOH   A O   1 
HETATM 2625 O  O   . HOH   C 3 .   ? -3.14194  2.23885   -29.02787 1.000 44.23554 ? 733 HOH   A O   1 
HETATM 2626 O  O   . HOH   C 3 .   ? -8.08846  -9.70550  11.46644  1.000 38.79189 ? 734 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   . SER   A 1   ? 0.21062 0.36713 0.37008 0.00278  0.11797  0.06064  1   SER   A N   
2    C  CA  . SER   A 1   ? 0.18328 0.33421 0.33735 -0.00390 0.10658  0.06691  1   SER   A CA  
3    C  C   . SER   A 1   ? 0.19618 0.34535 0.36871 -0.00551 0.09115  0.06748  1   SER   A C   
4    O  O   . SER   A 1   ? 0.17800 0.32979 0.36460 -0.00091 0.08843  0.06324  1   SER   A O   
5    C  CB  . SER   A 1   ? 0.26308 0.41769 0.41946 -0.01055 0.10940  0.07677  1   SER   A CB  
6    O  OG  . SER   A 1   ? 0.28112 0.44319 0.46554 -0.01369 0.10478  0.08196  1   SER   A OG  
7    N  N   . GLY   A 2   ? 0.17391 0.31730 0.34448 -0.01209 0.08082  0.07252  2   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.15839 0.29747 0.33901 -0.01478 0.06580  0.07141  2   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.17865 0.30657 0.33921 -0.01259 0.05965  0.06537  2   GLY   A C   
10   O  O   . GLY   A 2   ? 0.21066 0.33415 0.35111 -0.00725 0.06549  0.05914  2   GLY   A O   
11   N  N   . PHE   A 3   ? 0.17024 0.28922 0.33063 -0.01684 0.04570  0.06448  3   PHE   A N   
12   C  CA  . PHE   A 3   ? 0.18895 0.29358 0.32684 -0.01474 0.03765  0.05742  3   PHE   A CA  
13   C  C   . PHE   A 3   ? 0.20247 0.30293 0.34819 -0.01685 0.02452  0.05409  3   PHE   A C   
14   O  O   . PHE   A 3   ? 0.22644 0.32553 0.38236 -0.02370 0.01751  0.05756  3   PHE   A O   
15   C  CB  . PHE   A 3   ? 0.21721 0.31177 0.33803 -0.01781 0.03653  0.06093  3   PHE   A CB  
16   C  CG  . PHE   A 3   ? 0.20351 0.28816 0.30069 -0.01381 0.03296  0.05487  3   PHE   A CG  
17   C  CD1 . PHE   A 3   ? 0.23650 0.32352 0.31759 -0.00939 0.04021  0.05146  3   PHE   A CD1 
18   C  CD2 . PHE   A 3   ? 0.20677 0.28018 0.29814 -0.01487 0.02259  0.05195  3   PHE   A CD2 
19   C  CE1 . PHE   A 3   ? 0.23956 0.31910 0.30062 -0.00694 0.03565  0.04615  3   PHE   A CE1 
20   C  CE2 . PHE   A 3   ? 0.23028 0.29690 0.30312 -0.01126 0.01946  0.04725  3   PHE   A CE2 
21   C  CZ  . PHE   A 3   ? 0.22721 0.29762 0.28586 -0.00769 0.02528  0.04476  3   PHE   A CZ  
22   N  N   . ARG   A 4   ? 0.19118 0.28876 0.33072 -0.01172 0.02126  0.04731  4   ARG   A N   
23   C  CA  . ARG   A 4   ? 0.17817 0.27283 0.32280 -0.01334 0.00941  0.04476  4   ARG   A CA  
24   C  C   . ARG   A 4   ? 0.15822 0.24047 0.28150 -0.01034 0.00467  0.03778  4   ARG   A C   
25   O  O   . ARG   A 4   ? 0.18383 0.26269 0.29271 -0.00586 0.01046  0.03415  4   ARG   A O   
26   C  CB  . ARG   A 4   ? 0.14488 0.25156 0.31027 -0.01002 0.00987  0.04621  4   ARG   A CB  
27   C  CG  . ARG   A 4   ? 0.15779 0.27822 0.34915 -0.01513 0.00893  0.05402  4   ARG   A CG  
28   C  CD  . ARG   A 4   ? 0.18544 0.30296 0.37914 -0.01985 -0.00561 0.05362  4   ARG   A CD  
29   N  NE  . ARG   A 4   ? 0.16078 0.28710 0.37101 -0.02316 -0.00736 0.05876  4   ARG   A NE  
30   C  CZ  . ARG   A 4   ? 0.24132 0.36574 0.45301 -0.03153 -0.01784 0.05991  4   ARG   A CZ  
31   N  NH1 . ARG   A 4   ? 0.26441 0.37702 0.46094 -0.03696 -0.02684 0.05546  4   ARG   A NH1 
32   N  NH2 . ARG   A 4   ? 0.12683 0.26131 0.35525 -0.03460 -0.01903 0.06513  4   ARG   A NH2 
33   N  N   . LYS   A 5   ? 0.13404 0.21007 0.25494 -0.01358 -0.00589 0.03584  5   LYS   A N   
34   C  CA  . LYS   A 5   ? 0.18092 0.24775 0.28569 -0.01063 -0.01016 0.02996  5   LYS   A CA  
35   C  C   . LYS   A 5   ? 0.19247 0.26438 0.30372 -0.00541 -0.00887 0.02837  5   LYS   A C   
36   O  O   . LYS   A 5   ? 0.22356 0.30100 0.34804 -0.00620 -0.01451 0.03082  5   LYS   A O   
37   C  CB  . LYS   A 5   ? 0.18943 0.24866 0.28934 -0.01554 -0.02018 0.02823  5   LYS   A CB  
38   C  CG  . LYS   A 5   ? 0.26359 0.31104 0.34431 -0.01397 -0.02133 0.02361  5   LYS   A CG  
39   C  CD  . LYS   A 5   ? 0.29895 0.33676 0.37489 -0.01941 -0.02608 0.02246  5   LYS   A CD  
40   C  CE  . LYS   A 5   ? 0.28590 0.31375 0.34825 -0.01673 -0.02313 0.02060  5   LYS   A CE  
41   N  NZ  . LYS   A 5   ? 0.32151 0.34422 0.37193 -0.01410 -0.02606 0.01559  5   LYS   A NZ  
42   N  N   . MET   A 6   ? 0.11041 0.18047 0.21312 -0.00038 -0.00149 0.02474  6   MET   A N   
43   C  CA  . MET   A 6   ? 0.13947 0.21261 0.25018 0.00510  0.00301  0.02287  6   MET   A CA  
44   C  C   . MET   A 6   ? 0.13278 0.19652 0.23053 0.00714  -0.00054 0.01754  6   MET   A C   
45   O  O   . MET   A 6   ? 0.15471 0.21195 0.23502 0.00658  0.00034  0.01349  6   MET   A O   
46   C  CB  . MET   A 6   ? 0.12446 0.20061 0.23336 0.00848  0.01568  0.02098  6   MET   A CB  
47   C  CG  . MET   A 6   ? 0.20477 0.28482 0.32782 0.01440  0.02289  0.01971  6   MET   A CG  
48   S  SD  . MET   A 6   ? 0.30155 0.38591 0.42038 0.01673  0.03914  0.01760  6   MET   A SD  
49   C  CE  . MET   A 6   ? 0.20187 0.30211 0.34632 0.01446  0.04156  0.02787  6   MET   A CE  
50   N  N   . ALA   A 7   ? 0.13039 0.19430 0.23760 0.00926  -0.00465 0.01861  7   ALA   A N   
51   C  CA  . ALA   A 7   ? 0.10720 0.16194 0.20349 0.01097  -0.00661 0.01420  7   ALA   A CA  
52   C  C   . ALA   A 7   ? 0.14493 0.19694 0.24526 0.01639  0.00243  0.01012  7   ALA   A C   
53   O  O   . ALA   A 7   ? 0.09900 0.15714 0.21347 0.01992  0.00990  0.01155  7   ALA   A O   
54   C  CB  . ALA   A 7   ? 0.13162 0.18575 0.23244 0.00971  -0.01632 0.01812  7   ALA   A CB  
55   N  N   . PHE   A 8   ? 0.10387 0.14616 0.19229 0.01680  0.00239  0.00467  8   PHE   A N   
56   C  CA  . PHE   A 8   ? 0.12549 0.16143 0.21680 0.02118  0.01054  -0.00063 8   PHE   A CA  
57   C  C   . PHE   A 8   ? 0.11014 0.14698 0.22258 0.02590  0.00944  0.00483  8   PHE   A C   
58   O  O   . PHE   A 8   ? 0.10640 0.14622 0.22436 0.02431  -0.00016 0.01167  8   PHE   A O   
59   C  CB  . PHE   A 8   ? 0.12980 0.15474 0.20413 0.01879  0.00954  -0.00764 8   PHE   A CB  
60   C  CG  . PHE   A 8   ? 0.16978 0.19505 0.22494 0.01485  0.01113  -0.01256 8   PHE   A CG  
61   C  CD1 . PHE   A 8   ? 0.22650 0.25050 0.27415 0.01560  0.02055  -0.01890 8   PHE   A CD1 
62   C  CD2 . PHE   A 8   ? 0.22136 0.24864 0.26615 0.01067  0.00359  -0.01029 8   PHE   A CD2 
63   C  CE1 . PHE   A 8   ? 0.31207 0.33792 0.34097 0.01147  0.02076  -0.02179 8   PHE   A CE1 
64   C  CE2 . PHE   A 8   ? 0.24347 0.27258 0.27289 0.00760  0.00425  -0.01273 8   PHE   A CE2 
65   C  CZ  . PHE   A 8   ? 0.25703 0.28598 0.27801 0.00764  0.01203  -0.01793 8   PHE   A CZ  
66   N  N   . PRO   A 9   ? 0.13098 0.16526 0.25520 0.03186  0.01942  0.00226  9   PRO   A N   
67   C  CA  . PRO   A 9   ? 0.13759 0.17132 0.28375 0.03757  0.01878  0.00834  9   PRO   A CA  
68   C  C   . PRO   A 9   ? 0.16030 0.18391 0.29899 0.03534  0.01073  0.00924  9   PRO   A C   
69   O  O   . PRO   A 9   ? 0.14562 0.15845 0.26612 0.03195  0.01165  0.00140  9   PRO   A O   
70   C  CB  . PRO   A 9   ? 0.14981 0.17685 0.30376 0.04437  0.03371  0.00153  9   PRO   A CB  
71   C  CG  . PRO   A 9   ? 0.19062 0.22120 0.33051 0.04205  0.04184  -0.00530 9   PRO   A CG  
72   C  CD  . PRO   A 9   ? 0.15960 0.19037 0.27641 0.03380  0.03241  -0.00654 9   PRO   A CD  
73   N  N   . SER   A 10  ? 0.13194 0.16066 0.28416 0.03624  0.00200  0.01974  10  SER   A N   
74   C  CA  . SER   A 10  ? 0.11390 0.13568 0.25665 0.03271  -0.00663 0.02258  10  SER   A CA  
75   C  C   . SER   A 10  ? 0.11166 0.12239 0.26620 0.03769  -0.00386 0.02510  10  SER   A C   
76   O  O   . SER   A 10  ? 0.12277 0.12639 0.26954 0.03461  -0.00952 0.02764  10  SER   A O   
77   C  CB  . SER   A 10  ? 0.09249 0.12529 0.23664 0.02880  -0.01911 0.03258  10  SER   A CB  
78   O  OG  . SER   A 10  ? 0.12804 0.17112 0.29445 0.03263  -0.02108 0.04194  10  SER   A OG  
79   N  N   . GLY   A 11  ? 0.14258 0.15123 0.31634 0.04545  0.00562  0.02474  11  GLY   A N   
80   C  CA  . GLY   A 11  ? 0.13432 0.13158 0.32095 0.05042  0.00863  0.02836  11  GLY   A CA  
81   C  C   . GLY   A 11  ? 0.15049 0.12967 0.32418 0.04728  0.00892  0.02252  11  GLY   A C   
82   O  O   . GLY   A 11  ? 0.16232 0.13584 0.34077 0.04710  0.00361  0.03072  11  GLY   A O   
83   N  N   . LYS   A 12  ? 0.14489 0.11601 0.29853 0.04270  0.01462  0.00854  12  LYS   A N   
84   C  CA  . LYS   A 12  ? 0.19073 0.14511 0.33183 0.03792  0.01534  0.00174  12  LYS   A CA  
85   C  C   . LYS   A 12  ? 0.19335 0.15113 0.32514 0.03148  0.00373  0.00942  12  LYS   A C   
86   O  O   . LYS   A 12  ? 0.21974 0.16562 0.35109 0.02907  0.00256  0.01084  12  LYS   A O   
87   C  CB  . LYS   A 12  ? 0.20958 0.15853 0.32977 0.03274  0.02129  -0.01373 12  LYS   A CB  
88   C  CG  . LYS   A 12  ? 0.24519 0.18446 0.36912 0.03777  0.03518  -0.02456 12  LYS   A CG  
89   C  CD  . LYS   A 12  ? 0.30115 0.23878 0.39987 0.03098  0.03858  -0.03837 12  LYS   A CD  
90   C  CE  . LYS   A 12  ? 0.38064 0.30376 0.47699 0.03397  0.05301  -0.05192 12  LYS   A CE  
91   N  NZ  . LYS   A 12  ? 0.45520 0.38551 0.57082 0.04415  0.06256  -0.04810 12  LYS   A NZ  
92   N  N   . VAL   A 13  ? 0.13793 0.11106 0.26224 0.02845  -0.00400 0.01420  13  VAL   A N   
93   C  CA  . VAL   A 13  ? 0.17137 0.14857 0.28557 0.02279  -0.01364 0.02102  13  VAL   A CA  
94   C  C   . VAL   A 13  ? 0.14769 0.12845 0.27539 0.02564  -0.02018 0.03550  13  VAL   A C   
95   O  O   . VAL   A 13  ? 0.15718 0.13463 0.27968 0.02217  -0.02520 0.04189  13  VAL   A O   
96   C  CB  . VAL   A 13  ? 0.11421 0.10387 0.21413 0.01856  -0.01797 0.01884  13  VAL   A CB  
97   C  CG1 . VAL   A 13  ? 0.13796 0.13128 0.22633 0.01320  -0.02615 0.02475  13  VAL   A CG1 
98   C  CG2 . VAL   A 13  ? 0.17758 0.16403 0.26423 0.01565  -0.01243 0.00662  13  VAL   A CG2 
99   N  N   . GLU   A 14  ? 0.12512 0.11460 0.27035 0.03150  -0.02065 0.04194  14  GLU   A N   
100  C  CA  . GLU   A 14  ? 0.12988 0.12518 0.28715 0.03336  -0.02769 0.05636  14  GLU   A CA  
101  C  C   . GLU   A 14  ? 0.14467 0.12625 0.30726 0.03474  -0.02496 0.06032  14  GLU   A C   
102  O  O   . GLU   A 14  ? 0.16446 0.14849 0.32382 0.03179  -0.03160 0.07047  14  GLU   A O   
103  C  CB  . GLU   A 14  ? 0.13159 0.13810 0.30428 0.03746  -0.02548 0.05954  14  GLU   A CB  
104  C  CG  . GLU   A 14  ? 0.11934 0.14010 0.28777 0.03466  -0.02874 0.05736  14  GLU   A CG  
105  C  CD  . GLU   A 14  ? 0.12247 0.15253 0.30844 0.03883  -0.02434 0.05961  14  GLU   A CD  
106  O  OE1 . GLU   A 14  ? 0.14635 0.17925 0.34537 0.04118  -0.02568 0.06826  14  GLU   A OE1 
107  O  OE2 . GLU   A 14  ? 0.12849 0.16341 0.31601 0.03979  -0.01914 0.05325  14  GLU   A OE2 
108  N  N   . GLY   A 15  ? 0.15393 0.12046 0.32347 0.03860  -0.01460 0.05175  15  GLY   A N   
109  C  CA  . GLY   A 15  ? 0.17078 0.12304 0.34588 0.03932  -0.01141 0.05482  15  GLY   A CA  
110  C  C   . GLY   A 15  ? 0.18104 0.12383 0.34326 0.03249  -0.01537 0.05609  15  GLY   A C   
111  O  O   . GLY   A 15  ? 0.18717 0.11830 0.35335 0.03186  -0.01319 0.05947  15  GLY   A O   
112  N  N   . CYS   A 16  ? 0.15921 0.10851 0.30439 0.02640  -0.02041 0.05290  16  CYS   A N   
113  C  CA  . CYS   A 16  ? 0.16246 0.10741 0.29212 0.01829  -0.02293 0.05261  16  CYS   A CA  
114  C  C   . CYS   A 16  ? 0.16790 0.12511 0.28772 0.01459  -0.03221 0.06432  16  CYS   A C   
115  O  O   . CYS   A 16  ? 0.15748 0.11275 0.26524 0.00824  -0.03353 0.06583  16  CYS   A O   
116  C  CB  . CYS   A 16  ? 0.15721 0.10293 0.26999 0.01256  -0.01976 0.03755  16  CYS   A CB  
117  S  SG  . CYS   A 16  ? 0.22481 0.15617 0.34225 0.01477  -0.00915 0.02194  16  CYS   A SG  
118  N  N   . MET   A 17  ? 0.15915 0.12943 0.28270 0.01758  -0.03832 0.07181  17  MET   A N   
119  C  CA  . MET   A 17  ? 0.16778 0.14966 0.27664 0.01265  -0.04690 0.07953  17  MET   A CA  
120  C  C   . MET   A 17  ? 0.16266 0.14427 0.27326 0.01160  -0.04927 0.09122  17  MET   A C   
121  O  O   . MET   A 17  ? 0.19390 0.17546 0.32022 0.01631  -0.04814 0.09618  17  MET   A O   
122  C  CB  . MET   A 17  ? 0.17474 0.17165 0.28153 0.01303  -0.05126 0.07796  17  MET   A CB  
123  C  CG  . MET   A 17  ? 0.13101 0.12930 0.23265 0.01287  -0.04717 0.06476  17  MET   A CG  
124  S  SD  . MET   A 17  ? 0.14215 0.13652 0.22152 0.00613  -0.04371 0.05444  17  MET   A SD  
125  C  CE  . MET   A 17  ? 0.17430 0.17524 0.23662 0.00045  -0.05131 0.06358  17  MET   A CE  
126  N  N   . VAL   A 18  ? 0.16720 0.14907 0.26200 0.00560  -0.05197 0.09595  18  VAL   A N   
127  C  CA  . VAL   A 18  ? 0.18301 0.16521 0.27644 0.00380  -0.05424 0.10749  18  VAL   A CA  
128  C  C   . VAL   A 18  ? 0.19076 0.18373 0.26195 -0.00233 -0.05990 0.11090  18  VAL   A C   
129  O  O   . VAL   A 18  ? 0.20611 0.20386 0.26324 -0.00528 -0.06085 0.10373  18  VAL   A O   
130  C  CB  . VAL   A 18  ? 0.19283 0.16065 0.29020 0.00217  -0.04871 0.10987  18  VAL   A CB  
131  C  CG1 . VAL   A 18  ? 0.20420 0.15832 0.32121 0.00752  -0.04186 0.10358  18  VAL   A CG1 
132  C  CG2 . VAL   A 18  ? 0.18756 0.15323 0.26893 -0.00459 -0.04695 0.10614  18  VAL   A CG2 
133  N  N   . GLN   A 19  ? 0.24267 0.23870 0.31032 -0.00412 -0.06314 0.12156  19  GLN   A N   
134  C  CA  . GLN   A 19  ? 0.27499 0.27939 0.31985 -0.01014 -0.06742 0.12461  19  GLN   A CA  
135  C  C   . GLN   A 19  ? 0.25337 0.25178 0.28766 -0.01432 -0.06314 0.12922  19  GLN   A C   
136  O  O   . GLN   A 19  ? 0.27949 0.27040 0.32528 -0.01297 -0.06062 0.13679  19  GLN   A O   
137  C  CB  . GLN   A 19  ? 0.27241 0.28573 0.31926 -0.00995 -0.07457 0.13366  19  GLN   A CB  
138  C  CG  . GLN   A 19  ? 0.31810 0.33856 0.34088 -0.01632 -0.07908 0.13699  19  GLN   A CG  
139  C  CD  . GLN   A 19  ? 0.33707 0.36786 0.36201 -0.01688 -0.08765 0.14324  19  GLN   A CD  
140  O  OE1 . GLN   A 19  ? 0.40601 0.44374 0.41342 -0.02174 -0.09230 0.13953  19  GLN   A OE1 
141  N  NE2 . GLN   A 19  ? 0.39626 0.42787 0.44369 -0.01200 -0.08961 0.15249  19  GLN   A NE2 
142  N  N   . VAL   A 20  ? 0.24541 0.24671 0.25887 -0.01936 -0.06126 0.12438  20  VAL   A N   
143  C  CA  . VAL   A 20  ? 0.27564 0.27350 0.27843 -0.02392 -0.05581 0.12856  20  VAL   A CA  
144  C  C   . VAL   A 20  ? 0.28527 0.29102 0.26414 -0.02837 -0.05799 0.13191  20  VAL   A C   
145  O  O   . VAL   A 20  ? 0.27126 0.28273 0.23424 -0.03021 -0.05959 0.12410  20  VAL   A O   
146  C  CB  . VAL   A 20  ? 0.26412 0.25853 0.26436 -0.02612 -0.04927 0.12028  20  VAL   A CB  
147  C  CG1 . VAL   A 20  ? 0.28905 0.28221 0.28054 -0.03141 -0.04255 0.12537  20  VAL   A CG1 
148  C  CG2 . VAL   A 20  ? 0.24609 0.23105 0.26836 -0.02256 -0.04739 0.11640  20  VAL   A CG2 
149  N  N   . THR   A 21  ? 0.30654 0.31148 0.28228 -0.03020 -0.05774 0.14301  21  THR   A N   
150  C  CA  . THR   A 21  ? 0.32213 0.33333 0.27359 -0.03467 -0.05913 0.14673  21  THR   A CA  
151  C  C   . THR   A 21  ? 0.34714 0.35536 0.28866 -0.03858 -0.05058 0.15120  21  THR   A C   
152  O  O   . THR   A 21  ? 0.38059 0.38237 0.33684 -0.03812 -0.04721 0.15862  21  THR   A O   
153  C  CB  . THR   A 21  ? 0.35084 0.36623 0.30485 -0.03390 -0.06749 0.15772  21  THR   A CB  
154  O  OG1 . THR   A 21  ? 0.34339 0.36359 0.30738 -0.03092 -0.07472 0.15341  21  THR   A OG1 
155  C  CG2 . THR   A 21  ? 0.39773 0.41867 0.32423 -0.03922 -0.06888 0.16139  21  THR   A CG2 
156  N  N   . CYS   A 22  ? 0.36305 0.37549 0.28002 -0.04250 -0.04631 0.14634  22  CYS   A N   
157  C  CA  . CYS   A 22  ? 0.38947 0.40107 0.29535 -0.04632 -0.03695 0.15076  22  CYS   A CA  
158  C  C   . CYS   A 22  ? 0.43490 0.45153 0.31079 -0.04961 -0.03665 0.14965  22  CYS   A C   
159  O  O   . CYS   A 22  ? 0.41774 0.43692 0.27883 -0.05012 -0.03595 0.13814  22  CYS   A O   
160  C  CB  . CYS   A 22  ? 0.34385 0.35433 0.25526 -0.04713 -0.02732 0.14286  22  CYS   A CB  
161  S  SG  . CYS   A 22  ? 0.45603 0.46801 0.35704 -0.05190 -0.01419 0.14775  22  CYS   A SG  
162  N  N   . GLY   A 23  ? 0.40910 0.42624 0.27599 -0.05182 -0.03766 0.16140  23  GLY   A N   
163  C  CA  . GLY   A 23  ? 0.46721 0.48842 0.30428 -0.05523 -0.03844 0.16096  23  GLY   A CA  
164  C  C   . GLY   A 23  ? 0.48497 0.51027 0.31879 -0.05469 -0.05075 0.15720  23  GLY   A C   
165  O  O   . GLY   A 23  ? 0.48897 0.51573 0.34069 -0.05244 -0.06023 0.16490  23  GLY   A O   
166  N  N   . THR   A 24  ? 0.47240 0.49950 0.28492 -0.05677 -0.05014 0.14508  24  THR   A N   
167  C  CA  . THR   A 24  ? 0.49758 0.52859 0.30794 -0.05743 -0.06151 0.14008  24  THR   A CA  
168  C  C   . THR   A 24  ? 0.49180 0.52148 0.31668 -0.05446 -0.06223 0.12767  24  THR   A C   
169  O  O   . THR   A 24  ? 0.54550 0.57828 0.37182 -0.05509 -0.07089 0.12273  24  THR   A O   
170  C  CB  . THR   A 24  ? 0.53845 0.57120 0.31563 -0.06257 -0.06198 0.13437  24  THR   A CB  
171  O  OG1 . THR   A 24  ? 0.52992 0.55820 0.29011 -0.06299 -0.04898 0.12271  24  THR   A OG1 
172  C  CG2 . THR   A 24  ? 0.52243 0.55797 0.28545 -0.06575 -0.06443 0.14843  24  THR   A CG2 
173  N  N   . THR   A 25  ? 0.44887 0.47457 0.28525 -0.05169 -0.05357 0.12327  25  THR   A N   
174  C  CA  . THR   A 25  ? 0.43319 0.45750 0.28204 -0.04890 -0.05357 0.11209  25  THR   A CA  
175  C  C   . THR   A 25  ? 0.40339 0.42742 0.28259 -0.04451 -0.05930 0.11788  25  THR   A C   
176  O  O   . THR   A 25  ? 0.39314 0.41421 0.28710 -0.04276 -0.05606 0.12611  25  THR   A O   
177  C  CB  . THR   A 25  ? 0.44396 0.46529 0.28879 -0.04845 -0.04125 0.10436  25  THR   A CB  
178  O  OG1 . THR   A 25  ? 0.51107 0.53204 0.32834 -0.05156 -0.03388 0.09879  25  THR   A OG1 
179  C  CG2 . THR   A 25  ? 0.43015 0.45036 0.28534 -0.04585 -0.04195 0.09314  25  THR   A CG2 
180  N  N   . THR   A 26  ? 0.38370 0.41017 0.27268 -0.04284 -0.06699 0.11326  26  THR   A N   
181  C  CA  . THR   A 26  ? 0.34714 0.37295 0.26462 -0.03780 -0.07053 0.11602  26  THR   A CA  
182  C  C   . THR   A 26  ? 0.31277 0.33732 0.23628 -0.03574 -0.06897 0.10354  26  THR   A C   
183  O  O   . THR   A 26  ? 0.31501 0.34151 0.22595 -0.03803 -0.07086 0.09449  26  THR   A O   
184  C  CB  . THR   A 26  ? 0.35316 0.38456 0.28118 -0.03698 -0.08042 0.12405  26  THR   A CB  
185  O  OG1 . THR   A 26  ? 0.43244 0.46454 0.35745 -0.03824 -0.08174 0.13726  26  THR   A OG1 
186  C  CG2 . THR   A 26  ? 0.36926 0.39991 0.32607 -0.03113 -0.08217 0.12514  26  THR   A CG2 
187  N  N   . LEU   A 27  ? 0.22745 0.24791 0.16960 -0.03177 -0.06540 0.10297  27  LEU   A N   
188  C  CA  . LEU   A 27  ? 0.25525 0.27494 0.20591 -0.02914 -0.06480 0.09277  27  LEU   A CA  
189  C  C   . LEU   A 27  ? 0.20164 0.21755 0.17838 -0.02386 -0.06459 0.09603  27  LEU   A C   
190  O  O   . LEU   A 27  ? 0.23738 0.25092 0.22632 -0.02208 -0.06542 0.10555  27  LEU   A O   
191  C  CB  . LEU   A 27  ? 0.27437 0.29206 0.21117 -0.03105 -0.05756 0.08415  27  LEU   A CB  
192  C  CG  . LEU   A 27  ? 0.25782 0.27306 0.18987 -0.03298 -0.04952 0.08881  27  LEU   A CG  
193  C  CD1 . LEU   A 27  ? 0.22366 0.23411 0.17822 -0.03039 -0.04797 0.09412  27  LEU   A CD1 
194  C  CD2 . LEU   A 27  ? 0.27725 0.29334 0.19511 -0.03456 -0.04160 0.07878  27  LEU   A CD2 
195  N  N   . ASN   A 28  ? 0.21602 0.23046 0.20103 -0.02121 -0.06299 0.08771  28  ASN   A N   
196  C  CA  . ASN   A 28  ? 0.18642 0.19635 0.19475 -0.01591 -0.06220 0.08830  28  ASN   A CA  
197  C  C   . ASN   A 28  ? 0.18831 0.19054 0.20083 -0.01610 -0.05479 0.08565  28  ASN   A C   
198  O  O   . ASN   A 28  ? 0.20177 0.20511 0.20210 -0.01921 -0.04949 0.07908  28  ASN   A O   
199  C  CB  . ASN   A 28  ? 0.18069 0.19395 0.19608 -0.01304 -0.06361 0.07925  28  ASN   A CB  
200  C  CG  . ASN   A 28  ? 0.20274 0.22363 0.21496 -0.01437 -0.06900 0.07930  28  ASN   A CG  
201  O  OD1 . ASN   A 28  ? 0.19096 0.21452 0.21641 -0.01208 -0.07209 0.08600  28  ASN   A OD1 
202  N  ND2 . ASN   A 28  ? 0.20577 0.22966 0.20053 -0.01850 -0.07005 0.07227  28  ASN   A ND2 
203  N  N   . GLY   A 29  ? 0.17222 0.16657 0.20344 -0.01285 -0.05290 0.08883  29  GLY   A N   
204  C  CA  . GLY   A 29  ? 0.17810 0.16449 0.21551 -0.01397 -0.04540 0.08243  29  GLY   A CA  
205  C  C   . GLY   A 29  ? 0.15022 0.13055 0.20387 -0.00930 -0.04289 0.07405  29  GLY   A C   
206  O  O   . GLY   A 29  ? 0.16500 0.14621 0.22913 -0.00427 -0.04585 0.07624  29  GLY   A O   
207  N  N   . LEU   A 30  ? 0.18298 0.15822 0.23837 -0.01140 -0.03723 0.06451  30  LEU   A N   
208  C  CA  . LEU   A 30  ? 0.19487 0.16322 0.26136 -0.00826 -0.03372 0.05484  30  LEU   A CA  
209  C  C   . LEU   A 30  ? 0.16377 0.11785 0.24056 -0.01035 -0.02979 0.05554  30  LEU   A C   
210  O  O   . LEU   A 30  ? 0.18530 0.13780 0.25793 -0.01661 -0.02787 0.05454  30  LEU   A O   
211  C  CB  . LEU   A 30  ? 0.15750 0.13186 0.21559 -0.00989 -0.03149 0.04222  30  LEU   A CB  
212  C  CG  . LEU   A 30  ? 0.15749 0.12596 0.22285 -0.00715 -0.02781 0.03203  30  LEU   A CG  
213  C  CD1 . LEU   A 30  ? 0.17009 0.14259 0.24148 -0.00071 -0.02894 0.03278  30  LEU   A CD1 
214  C  CD2 . LEU   A 30  ? 0.14312 0.11650 0.19956 -0.01067 -0.02609 0.02169  30  LEU   A CD2 
215  N  N   . TRP   A 31  ? 0.17994 0.12360 0.27172 -0.00518 -0.02830 0.05782  31  TRP   A N   
216  C  CA  . TRP   A 31  ? 0.18001 0.10658 0.28397 -0.00625 -0.02453 0.06049  31  TRP   A CA  
217  C  C   . TRP   A 31  ? 0.20749 0.12286 0.31594 -0.00587 -0.01832 0.04506  31  TRP   A C   
218  O  O   . TRP   A 31  ? 0.20567 0.11820 0.32226 0.00107  -0.01546 0.04084  31  TRP   A O   
219  C  CB  . TRP   A 31  ? 0.19102 0.11255 0.30983 0.00017  -0.02658 0.07493  31  TRP   A CB  
220  C  CG  . TRP   A 31  ? 0.21241 0.11794 0.34246 0.00004  -0.02164 0.07697  31  TRP   A CG  
221  C  CD1 . TRP   A 31  ? 0.23338 0.12711 0.36200 -0.00734 -0.01803 0.07299  31  TRP   A CD1 
222  C  CD2 . TRP   A 31  ? 0.25486 0.15606 0.39888 0.00726  -0.01957 0.08253  31  TRP   A CD2 
223  N  NE1 . TRP   A 31  ? 0.24045 0.12093 0.37999 -0.00498 -0.01388 0.07565  31  TRP   A NE1 
224  C  CE2 . TRP   A 31  ? 0.26794 0.15254 0.41741 0.00436  -0.01457 0.08185  31  TRP   A CE2 
225  C  CE3 . TRP   A 31  ? 0.27793 0.18863 0.43132 0.01526  -0.02167 0.08847  31  TRP   A CE3 
226  C  CZ2 . TRP   A 31  ? 0.29572 0.17137 0.45946 0.01016  -0.01127 0.08701  31  TRP   A CZ2 
227  C  CZ3 . TRP   A 31  ? 0.28376 0.18749 0.45246 0.02072  -0.01850 0.09401  31  TRP   A CZ3 
228  C  CH2 . TRP   A 31  ? 0.27786 0.16348 0.45161 0.01867  -0.01315 0.09330  31  TRP   A CH2 
229  N  N   . LEU   A 32  ? 0.19250 0.10287 0.29505 -0.01383 -0.01622 0.03663  32  LEU   A N   
230  C  CA  . LEU   A 32  ? 0.22015 0.11962 0.32252 -0.01606 -0.01127 0.02107  32  LEU   A CA  
231  C  C   . LEU   A 32  ? 0.26830 0.15031 0.37720 -0.02313 -0.00874 0.02034  32  LEU   A C   
232  O  O   . LEU   A 32  ? 0.27301 0.15957 0.37900 -0.03067 -0.01149 0.02595  32  LEU   A O   
233  C  CB  . LEU   A 32  ? 0.23751 0.15015 0.32496 -0.02085 -0.01300 0.01049  32  LEU   A CB  
234  C  CG  . LEU   A 32  ? 0.19377 0.12294 0.27428 -0.01526 -0.01546 0.01133  32  LEU   A CG  
235  C  CD1 . LEU   A 32  ? 0.18493 0.12704 0.25251 -0.02044 -0.01776 0.00486  32  LEU   A CD1 
236  C  CD2 . LEU   A 32  ? 0.20342 0.12740 0.28900 -0.00815 -0.01098 0.00492  32  LEU   A CD2 
237  N  N   . ASP   A 33  ? 0.26061 0.12225 0.37903 -0.02088 -0.00273 0.01331  33  ASP   A N   
238  C  CA  . ASP   A 33  ? 0.28560 0.13050 0.40809 -0.02648 0.00034  0.01260  33  ASP   A CA  
239  C  C   . ASP   A 33  ? 0.30748 0.15693 0.43580 -0.02608 -0.00291 0.03132  33  ASP   A C   
240  O  O   . ASP   A 33  ? 0.27657 0.13347 0.41006 -0.01755 -0.00482 0.04310  33  ASP   A O   
241  C  CB  . ASP   A 33  ? 0.31557 0.15857 0.42807 -0.03888 -0.00062 -0.00036 33  ASP   A CB  
242  C  CG  . ASP   A 33  ? 0.35497 0.19619 0.45780 -0.03902 0.00193  -0.01822 33  ASP   A CG  
243  O  OD1 . ASP   A 33  ? 0.38015 0.20850 0.48400 -0.03246 0.00853  -0.02526 33  ASP   A OD1 
244  O  OD2 . ASP   A 33  ? 0.37057 0.22669 0.46216 -0.04466 -0.00247 -0.02410 33  ASP   A OD2 
245  N  N   . ASP   A 34  ? 0.26242 0.11015 0.38902 -0.03548 -0.00400 0.03498  34  ASP   A N   
246  C  CA  . ASP   A 34  ? 0.29760 0.14992 0.42763 -0.03518 -0.00598 0.05260  34  ASP   A CA  
247  C  C   . ASP   A 34  ? 0.26869 0.14047 0.39055 -0.04000 -0.01070 0.06091  34  ASP   A C   
248  O  O   . ASP   A 34  ? 0.29616 0.17171 0.41721 -0.04420 -0.01098 0.07208  34  ASP   A O   
249  C  CB  . ASP   A 34  ? 0.31826 0.15483 0.45327 -0.04124 -0.00257 0.05370  34  ASP   A CB  
250  C  CG  . ASP   A 34  ? 0.37167 0.20807 0.50137 -0.05435 -0.00276 0.04447  34  ASP   A CG  
251  O  OD1 . ASP   A 34  ? 0.38225 0.22932 0.50503 -0.05816 -0.00519 0.03486  34  ASP   A OD1 
252  O  OD2 . ASP   A 34  ? 0.38733 0.21402 0.52056 -0.06110 -0.00093 0.04743  34  ASP   A OD2 
253  N  N   . VAL   A 35  ? 0.28469 0.16891 0.40002 -0.03913 -0.01376 0.05615  35  VAL   A N   
254  C  CA  . VAL   A 35  ? 0.22299 0.12806 0.32645 -0.04167 -0.01686 0.06191  35  VAL   A CA  
255  C  C   . VAL   A 35  ? 0.23821 0.15554 0.33392 -0.03275 -0.02010 0.06532  35  VAL   A C   
256  O  O   . VAL   A 35  ? 0.22056 0.13670 0.31750 -0.02652 -0.02015 0.05734  35  VAL   A O   
257  C  CB  . VAL   A 35  ? 0.24039 0.15636 0.33669 -0.04865 -0.01703 0.04986  35  VAL   A CB  
258  C  CG1 . VAL   A 35  ? 0.24045 0.17744 0.32572 -0.04877 -0.01848 0.05507  35  VAL   A CG1 
259  C  CG2 . VAL   A 35  ? 0.27043 0.17709 0.37502 -0.05951 -0.01530 0.04762  35  VAL   A CG2 
260  N  N   . VAL   A 36  ? 0.19697 0.12608 0.28416 -0.03290 -0.02248 0.07700  36  VAL   A N   
261  C  CA  . VAL   A 36  ? 0.21033 0.15253 0.28706 -0.02714 -0.02642 0.07932  36  VAL   A CA  
262  C  C   . VAL   A 36  ? 0.22115 0.17849 0.28345 -0.03096 -0.02574 0.07493  36  VAL   A C   
263  O  O   . VAL   A 36  ? 0.20152 0.16290 0.25979 -0.03654 -0.02339 0.08103  36  VAL   A O   
264  C  CB  . VAL   A 36  ? 0.21300 0.15581 0.28922 -0.02435 -0.03026 0.09626  36  VAL   A CB  
265  C  CG1 . VAL   A 36  ? 0.20179 0.15943 0.26389 -0.02128 -0.03511 0.09706  36  VAL   A CG1 
266  C  CG2 . VAL   A 36  ? 0.22473 0.15458 0.31819 -0.01840 -0.03039 0.10048  36  VAL   A CG2 
267  N  N   . TYR   A 37  ? 0.18823 0.15358 0.24431 -0.02766 -0.02686 0.06486  37  TYR   A N   
268  C  CA  . TYR   A 37  ? 0.19699 0.17560 0.24143 -0.02936 -0.02575 0.05973  37  TYR   A CA  
269  C  C   . TYR   A 37  ? 0.17667 0.16302 0.20842 -0.02604 -0.02865 0.06407  37  TYR   A C   
270  O  O   . TYR   A 37  ? 0.20757 0.19281 0.24067 -0.02141 -0.03264 0.06403  37  TYR   A O   
271  C  CB  . TYR   A 37  ? 0.14713 0.12857 0.19273 -0.02810 -0.02537 0.04640  37  TYR   A CB  
272  C  CG  . TYR   A 37  ? 0.19110 0.16497 0.24611 -0.03247 -0.02368 0.04016  37  TYR   A CG  
273  C  CD1 . TYR   A 37  ? 0.16942 0.12907 0.23336 -0.03093 -0.02334 0.03743  37  TYR   A CD1 
274  C  CD2 . TYR   A 37  ? 0.20064 0.18153 0.25634 -0.03862 -0.02224 0.03699  37  TYR   A CD2 
275  C  CE1 . TYR   A 37  ? 0.22855 0.17911 0.29863 -0.03628 -0.02163 0.02990  37  TYR   A CE1 
276  C  CE2 . TYR   A 37  ? 0.17610 0.15070 0.23922 -0.04441 -0.02210 0.03073  37  TYR   A CE2 
277  C  CZ  . TYR   A 37  ? 0.22963 0.18804 0.29839 -0.04378 -0.02180 0.02649  37  TYR   A CZ  
278  O  OH  . TYR   A 37  ? 0.23210 0.18227 0.30592 -0.05091 -0.02154 0.01865  37  TYR   A OH  
279  N  N   . CYS   A 38  ? 0.16199 0.15640 0.18164 -0.02876 -0.02629 0.06712  38  CYS   A N   
280  C  CA  . CYS   A 38  ? 0.18899 0.18916 0.19338 -0.02695 -0.02891 0.06913  38  CYS   A CA  
281  C  C   . CYS   A 38  ? 0.18769 0.19605 0.17984 -0.02897 -0.02321 0.06560  38  CYS   A C   
282  O  O   . CYS   A 38  ? 0.19104 0.20219 0.18848 -0.03191 -0.01761 0.06545  38  CYS   A O   
283  C  CB  . CYS   A 38  ? 0.18569 0.18331 0.18536 -0.02787 -0.03304 0.08262  38  CYS   A CB  
284  S  SG  . CYS   A 38  ? 0.26839 0.26720 0.26036 -0.03389 -0.02755 0.09374  38  CYS   A SG  
285  N  N   . PRO   A 39  ? 0.19680 0.20902 0.17398 -0.02757 -0.02409 0.06236  39  PRO   A N   
286  C  CA  . PRO   A 39  ? 0.21279 0.23092 0.17855 -0.02843 -0.01686 0.05831  39  PRO   A CA  
287  C  C   . PRO   A 39  ? 0.24306 0.26323 0.20127 -0.03263 -0.01153 0.06750  39  PRO   A C   
288  O  O   . PRO   A 39  ? 0.21619 0.23361 0.16657 -0.03499 -0.01516 0.07715  39  PRO   A O   
289  C  CB  . PRO   A 39  ? 0.19247 0.21030 0.14231 -0.02701 -0.01988 0.05338  39  PRO   A CB  
290  C  CG  . PRO   A 39  ? 0.16478 0.17946 0.12425 -0.02458 -0.02831 0.05214  39  PRO   A CG  
291  C  CD  . PRO   A 39  ? 0.19859 0.20978 0.17024 -0.02530 -0.03126 0.06127  39  PRO   A CD  
292  N  N   . ARG   A 40  ? 0.20079 0.22698 0.16300 -0.03363 -0.00283 0.06583  40  ARG   A N   
293  C  CA  . ARG   A 40  ? 0.21976 0.24902 0.17609 -0.03794 0.00372  0.07519  40  ARG   A CA  
294  C  C   . ARG   A 40  ? 0.25108 0.28083 0.18134 -0.03883 0.00654  0.07686  40  ARG   A C   
295  O  O   . ARG   A 40  ? 0.24958 0.28062 0.17021 -0.04290 0.01034  0.08674  40  ARG   A O   
296  C  CB  . ARG   A 40  ? 0.21063 0.24873 0.17968 -0.03890 0.01293  0.07369  40  ARG   A CB  
297  C  CG  . ARG   A 40  ? 0.21355 0.25794 0.17569 -0.03485 0.02046  0.06523  40  ARG   A CG  
298  C  CD  . ARG   A 40  ? 0.19711 0.25288 0.17613 -0.03533 0.02913  0.06593  40  ARG   A CD  
299  N  NE  . ARG   A 40  ? 0.20106 0.26215 0.17766 -0.02965 0.03638  0.05788  40  ARG   A NE  
300  C  CZ  . ARG   A 40  ? 0.24043 0.31353 0.23023 -0.02816 0.04606  0.05850  40  ARG   A CZ  
301  N  NH1 . ARG   A 40  ? 0.21030 0.29276 0.21709 -0.03300 0.04890  0.06640  40  ARG   A NH1 
302  N  NH2 . ARG   A 40  ? 0.17279 0.24860 0.16038 -0.02175 0.05329  0.05153  40  ARG   A NH2 
303  N  N   . HIS   A 41  ? 0.27458 0.30263 0.19195 -0.03597 0.00476  0.06753  41  HIS   A N   
304  C  CA  . HIS   A 41  ? 0.35155 0.37886 0.24121 -0.03848 0.00764  0.06814  41  HIS   A CA  
305  C  C   . HIS   A 41  ? 0.31795 0.34216 0.19565 -0.04244 -0.00238 0.07878  41  HIS   A C   
306  O  O   . HIS   A 41  ? 0.36006 0.38345 0.21428 -0.04503 -0.00145 0.07929  41  HIS   A O   
307  C  CB  . HIS   A 41  ? 0.35374 0.37806 0.23073 -0.03574 0.00895  0.05480  41  HIS   A CB  
308  C  CG  . HIS   A 41  ? 0.33018 0.34960 0.20629 -0.03534 -0.00356 0.05135  41  HIS   A CG  
309  N  ND1 . HIS   A 41  ? 0.36464 0.38303 0.25955 -0.03115 -0.00772 0.04521  41  HIS   A ND1 
310  C  CD2 . HIS   A 41  ? 0.37893 0.39570 0.23814 -0.03910 -0.01295 0.05398  41  HIS   A CD2 
311  C  CE1 . HIS   A 41  ? 0.33020 0.34548 0.22118 -0.03202 -0.01797 0.04404  41  HIS   A CE1 
312  N  NE2 . HIS   A 41  ? 0.37332 0.38813 0.24394 -0.03693 -0.02200 0.04947  41  HIS   A NE2 
313  N  N   . VAL   A 42  ? 0.28214 0.30389 0.17788 -0.04187 -0.01115 0.08615  42  VAL   A N   
314  C  CA  . VAL   A 42  ? 0.29215 0.31150 0.18452 -0.04358 -0.01917 0.09724  42  VAL   A CA  
315  C  C   . VAL   A 42  ? 0.33540 0.35590 0.21799 -0.04664 -0.01221 0.10534  42  VAL   A C   
316  O  O   . VAL   A 42  ? 0.34689 0.36624 0.22007 -0.04770 -0.01713 0.11192  42  VAL   A O   
317  C  CB  . VAL   A 42  ? 0.29251 0.30776 0.21007 -0.04135 -0.02636 0.10374  42  VAL   A CB  
318  C  CG1 . VAL   A 42  ? 0.27059 0.28417 0.20373 -0.04329 -0.01967 0.11025  42  VAL   A CG1 
319  C  CG2 . VAL   A 42  ? 0.28429 0.29787 0.20289 -0.04038 -0.03530 0.11142  42  VAL   A CG2 
320  N  N   . ILE   A 43  ? 0.32042 0.34430 0.20644 -0.04819 -0.00069 0.10580  43  ILE   A N   
321  C  CA  . ILE   A 43  ? 0.34732 0.37206 0.22674 -0.05109 0.00620  0.11457  43  ILE   A CA  
322  C  C   . ILE   A 43  ? 0.39321 0.42012 0.24516 -0.05176 0.01454  0.10881  43  ILE   A C   
323  O  O   . ILE   A 43  ? 0.40363 0.43161 0.24596 -0.05394 0.02253  0.11468  43  ILE   A O   
324  C  CB  . ILE   A 43  ? 0.34955 0.37724 0.24948 -0.05314 0.01473  0.11942  43  ILE   A CB  
325  C  CG1 . ILE   A 43  ? 0.32367 0.35981 0.22421 -0.05261 0.02674  0.11092  43  ILE   A CG1 
326  C  CG2 . ILE   A 43  ? 0.30274 0.32572 0.22877 -0.05265 0.00714  0.12211  43  ILE   A CG2 
327  C  CD1 . ILE   A 43  ? 0.31542 0.35715 0.24278 -0.05468 0.03247  0.11381  43  ILE   A CD1 
328  N  N   . CYS   A 44  ? 0.40763 0.43384 0.24661 -0.04993 0.01330  0.09695  44  CYS   A N   
329  C  CA  . CYS   A 44  ? 0.45411 0.47987 0.26770 -0.04987 0.02246  0.08845  44  CYS   A CA  
330  C  C   . CYS   A 44  ? 0.57294 0.59465 0.36341 -0.05164 0.01411  0.08829  44  CYS   A C   
331  O  O   . CYS   A 44  ? 0.58378 0.60394 0.37833 -0.05184 0.00040  0.08897  44  CYS   A O   
332  C  CB  . CYS   A 44  ? 0.51857 0.54437 0.33166 -0.04694 0.02724  0.07415  44  CYS   A CB  
333  S  SG  . CYS   A 44  ? 0.54147 0.57621 0.37623 -0.04476 0.04199  0.07310  44  CYS   A SG  
334  N  N   . THR   A 45  ? 0.62254 0.64362 0.38987 -0.05290 0.02291  0.08745  45  THR   A N   
335  C  CA  . THR   A 45  ? 0.71768 0.73562 0.45856 -0.05488 0.01766  0.08271  45  THR   A CA  
336  C  C   . THR   A 45  ? 0.76488 0.77899 0.49512 -0.05303 0.02223  0.06534  45  THR   A C   
337  O  O   . THR   A 45  ? 0.74860 0.76297 0.49161 -0.04963 0.03030  0.05834  45  THR   A O   
338  C  CB  . THR   A 45  ? 0.73474 0.75327 0.45442 -0.05701 0.02580  0.08947  45  THR   A CB  
339  O  OG1 . THR   A 45  ? 0.76331 0.78199 0.47484 -0.05438 0.04393  0.08170  45  THR   A OG1 
340  C  CG2 . THR   A 45  ? 0.70039 0.72156 0.43524 -0.05849 0.02459  0.10645  45  THR   A CG2 
341  N  N   . SER   A 46  ? 0.81546 0.82589 0.52304 -0.05561 0.01699  0.05820  46  SER   A N   
342  C  CA  . SER   A 46  ? 0.83328 0.83787 0.53000 -0.05434 0.02233  0.04096  46  SER   A CA  
343  C  C   . SER   A 46  ? 0.82907 0.83329 0.51754 -0.05052 0.04240  0.03484  46  SER   A C   
344  O  O   . SER   A 46  ? 0.79504 0.79702 0.49242 -0.04629 0.05139  0.02437  46  SER   A O   
345  C  CB  . SER   A 46  ? 0.85822 0.85886 0.53232 -0.05935 0.01241  0.03486  46  SER   A CB  
346  O  OG  . SER   A 46  ? 0.90292 0.90669 0.55848 -0.06293 0.01066  0.04448  46  SER   A OG  
347  N  N   . GLU   A 47  ? 0.84895 0.85610 0.52207 -0.05147 0.05019  0.04204  47  GLU   A N   
348  C  CA  . GLU   A 47  ? 0.84530 0.85482 0.51376 -0.04711 0.07044  0.03833  47  GLU   A CA  
349  C  C   . GLU   A 47  ? 0.81727 0.83307 0.51557 -0.04261 0.07972  0.04278  47  GLU   A C   
350  O  O   . GLU   A 47  ? 0.78578 0.80460 0.49090 -0.03730 0.09477  0.03513  47  GLU   A O   
351  C  CB  . GLU   A 47  ? 0.84669 0.85925 0.49492 -0.04920 0.07674  0.04798  47  GLU   A CB  
352  C  CG  . GLU   A 47  ? 0.94440 0.95278 0.56036 -0.05473 0.06785  0.04609  47  GLU   A CG  
353  C  CD  . GLU   A 47  ? 0.95308 0.95971 0.57188 -0.05991 0.04586  0.05003  47  GLU   A CD  
354  O  OE1 . GLU   A 47  ? 0.94123 0.95191 0.57395 -0.06145 0.03714  0.06517  47  GLU   A OE1 
355  O  OE2 . GLU   A 47  ? 0.96289 0.96434 0.57213 -0.06240 0.03770  0.03812  47  GLU   A OE2 
356  N  N   . ASP   A 48  ? 0.77004 0.78889 0.48828 -0.04486 0.07072  0.05511  48  ASP   A N   
357  C  CA  . ASP   A 48  ? 0.73791 0.76294 0.48558 -0.04238 0.07734  0.05897  48  ASP   A CA  
358  C  C   . ASP   A 48  ? 0.70117 0.72530 0.46121 -0.03839 0.07846  0.04632  48  ASP   A C   
359  O  O   . ASP   A 48  ? 0.67529 0.70583 0.45353 -0.03428 0.09065  0.04434  48  ASP   A O   
360  C  CB  . ASP   A 48  ? 0.66733 0.69469 0.43390 -0.04639 0.06501  0.07274  48  ASP   A CB  
361  C  CG  . ASP   A 48  ? 0.68104 0.71018 0.44383 -0.04974 0.06855  0.08682  48  ASP   A CG  
362  O  OD1 . ASP   A 48  ? 0.65269 0.68422 0.40873 -0.04857 0.08447  0.08732  48  ASP   A OD1 
363  O  OD2 . ASP   A 48  ? 0.66059 0.68847 0.42786 -0.05311 0.05613  0.09757  48  ASP   A OD2 
364  N  N   . MET   A 49  ? 0.71968 0.73626 0.47109 -0.03954 0.06634  0.03783  49  MET   A N   
365  C  CA  . MET   A 49  ? 0.68522 0.69935 0.45076 -0.03669 0.06467  0.02814  49  MET   A CA  
366  C  C   . MET   A 49  ? 0.69295 0.70407 0.45567 -0.03094 0.07991  0.01448  49  MET   A C   
367  O  O   . MET   A 49  ? 0.64622 0.65432 0.42232 -0.02749 0.08106  0.00668  49  MET   A O   
368  C  CB  . MET   A 49  ? 0.65771 0.66444 0.41667 -0.03989 0.04731  0.02400  49  MET   A CB  
369  C  CG  . MET   A 49  ? 0.65179 0.66293 0.42889 -0.04228 0.03299  0.03529  49  MET   A CG  
370  S  SD  . MET   A 49  ? 0.66073 0.68086 0.47012 -0.03965 0.03690  0.04079  49  MET   A SD  
371  C  CE  . MET   A 49  ? 0.47288 0.48673 0.29617 -0.03430 0.03103  0.02763  49  MET   A CE  
372  N  N   . LEU   A 50  ? 0.69873 0.71056 0.44593 -0.02927 0.09190  0.01158  50  LEU   A N   
373  C  CA  . LEU   A 50  ? 0.72281 0.73148 0.46965 -0.02326 0.10608  -0.00194 50  LEU   A CA  
374  C  C   . LEU   A 50  ? 0.74070 0.76264 0.51300 -0.01715 0.12208  0.00171  50  LEU   A C   
375  O  O   . LEU   A 50  ? 0.80777 0.82759 0.59262 -0.01068 0.13148  -0.00802 50  LEU   A O   
376  C  CB  . LEU   A 50  ? 0.77626 0.77857 0.49283 -0.02493 0.11048  -0.00950 50  LEU   A CB  
377  C  CG  . LEU   A 50  ? 0.80332 0.79778 0.49400 -0.03267 0.09441  -0.00902 50  LEU   A CG  
378  C  CD1 . LEU   A 50  ? 0.77988 0.76696 0.44087 -0.03426 0.10041  -0.01971 50  LEU   A CD1 
379  C  CD2 . LEU   A 50  ? 0.79130 0.77752 0.48801 -0.03550 0.07824  -0.01374 50  LEU   A CD2 
380  N  N   . ASN   A 51  ? 0.72842 0.76395 0.51143 -0.01911 0.12482  0.01613  51  ASN   A N   
381  C  CA  . ASN   A 51  ? 0.66870 0.72072 0.48326 -0.01605 0.13577  0.02176  51  ASN   A CA  
382  C  C   . ASN   A 51  ? 0.60817 0.67019 0.43783 -0.02140 0.12979  0.03846  51  ASN   A C   
383  O  O   . ASN   A 51  ? 0.62509 0.69954 0.46231 -0.02640 0.13644  0.04583  51  ASN   A O   
384  C  CB  . ASN   A 51  ? 0.75536 0.81718 0.56884 -0.01350 0.15259  0.01917  51  ASN   A CB  
385  C  CG  . ASN   A 51  ? 0.83505 0.89192 0.65816 -0.00487 0.16349  0.00522  51  ASN   A CG  
386  O  OD1 . ASN   A 51  ? 0.88467 0.92591 0.68776 -0.00249 0.16306  -0.00730 51  ASN   A OD1 
387  N  ND2 . ASN   A 51  ? 0.83282 0.90209 0.68862 -0.00009 0.17256  0.00800  51  ASN   A ND2 
388  N  N   . PRO   A 52  ? 0.58698 0.63965 0.42200 -0.02409 0.11662  0.04208  52  PRO   A N   
389  C  CA  . PRO   A 52  ? 0.53134 0.58758 0.37775 -0.03137 0.10783  0.05579  52  PRO   A CA  
390  C  C   . PRO   A 52  ? 0.51064 0.58251 0.39173 -0.03091 0.11466  0.06230  52  PRO   A C   
391  O  O   . PRO   A 52  ? 0.49464 0.57508 0.39971 -0.02504 0.11667  0.05844  52  PRO   A O   
392  C  CB  . PRO   A 52  ? 0.52694 0.58051 0.37769 -0.03363 0.08914  0.05594  52  PRO   A CB  
393  C  CG  . PRO   A 52  ? 0.55095 0.59596 0.39672 -0.02809 0.08816  0.04110  52  PRO   A CG  
394  C  CD  . PRO   A 52  ? 0.57176 0.61371 0.39954 -0.02439 0.10470  0.03217  52  PRO   A CD  
395  N  N   . ASN   A 53  ? 0.46684 0.54201 0.35213 -0.03641 0.11702  0.07279  53  ASN   A N   
396  C  CA  . ASN   A 53  ? 0.44914 0.53828 0.36931 -0.03802 0.11773  0.08074  53  ASN   A CA  
397  C  C   . ASN   A 53  ? 0.43442 0.51971 0.36172 -0.04354 0.10181  0.09029  53  ASN   A C   
398  O  O   . ASN   A 53  ? 0.40121 0.48100 0.31959 -0.04900 0.09954  0.09904  53  ASN   A O   
399  C  CB  . ASN   A 53  ? 0.45784 0.55392 0.38063 -0.04094 0.13185  0.08473  53  ASN   A CB  
400  C  CG  . ASN   A 53  ? 0.45013 0.56170 0.41050 -0.04246 0.13235  0.09143  53  ASN   A CG  
401  O  OD1 . ASN   A 53  ? 0.38421 0.49760 0.36407 -0.04479 0.12025  0.09623  53  ASN   A OD1 
402  N  ND2 . ASN   A 53  ? 0.51689 0.64009 0.48792 -0.04157 0.14597  0.09095  53  ASN   A ND2 
403  N  N   . TYR   A 54  ? 0.37081 0.45777 0.31360 -0.04184 0.09099  0.08816  54  TYR   A N   
404  C  CA  . TYR   A 54  ? 0.34729 0.42740 0.29455 -0.04661 0.07587  0.09460  54  TYR   A CA  
405  C  C   . TYR   A 54  ? 0.33550 0.41847 0.30412 -0.05260 0.07467  0.10438  54  TYR   A C   
406  O  O   . TYR   A 54  ? 0.32240 0.39590 0.28820 -0.05691 0.06635  0.11162  54  TYR   A O   
407  C  CB  . TYR   A 54  ? 0.30957 0.38573 0.26984 -0.04242 0.06439  0.08521  54  TYR   A CB  
408  C  CG  . TYR   A 54  ? 0.29421 0.36004 0.23264 -0.03791 0.05940  0.07529  54  TYR   A CG  
409  C  CD1 . TYR   A 54  ? 0.29147 0.34644 0.21390 -0.04039 0.04830  0.07780  54  TYR   A CD1 
410  C  CD2 . TYR   A 54  ? 0.32984 0.39687 0.26583 -0.03132 0.06551  0.06408  54  TYR   A CD2 
411  C  CE1 . TYR   A 54  ? 0.32473 0.37169 0.22935 -0.03763 0.04271  0.06922  54  TYR   A CE1 
412  C  CE2 . TYR   A 54  ? 0.32075 0.37701 0.23763 -0.02852 0.06053  0.05480  54  TYR   A CE2 
413  C  CZ  . TYR   A 54  ? 0.31057 0.35758 0.21186 -0.03228 0.04884  0.05734  54  TYR   A CZ  
414  O  OH  . TYR   A 54  ? 0.35495 0.39289 0.23912 -0.03084 0.04312  0.04877  54  TYR   A OH  
415  N  N   . GLU   A 55  ? 0.34359 0.43915 0.33558 -0.05281 0.08199  0.10440  55  GLU   A N   
416  C  CA  . GLU   A 55  ? 0.33062 0.42858 0.34139 -0.05959 0.08129  0.11270  55  GLU   A CA  
417  C  C   . GLU   A 55  ? 0.34001 0.43192 0.33255 -0.06305 0.08746  0.12047  55  GLU   A C   
418  O  O   . GLU   A 55  ? 0.31063 0.39444 0.30548 -0.06838 0.08146  0.12872  55  GLU   A O   
419  C  CB  . GLU   A 55  ? 0.34288 0.45729 0.38098 -0.05921 0.08740  0.11068  55  GLU   A CB  
420  C  CG  . GLU   A 55  ? 0.40141 0.52111 0.45815 -0.05689 0.07859  0.10438  55  GLU   A CG  
421  C  CD  . GLU   A 55  ? 0.47350 0.59887 0.52485 -0.04756 0.08380  0.09588  55  GLU   A CD  
422  O  OE1 . GLU   A 55  ? 0.44138 0.56214 0.46943 -0.04307 0.09268  0.09303  55  GLU   A OE1 
423  O  OE2 . GLU   A 55  ? 0.49673 0.62950 0.56583 -0.04492 0.07832  0.09145  55  GLU   A OE2 
424  N  N   . ASP   A 56  ? 0.36706 0.46111 0.33973 -0.05988 0.09951  0.11746  56  ASP   A N   
425  C  CA  . ASP   A 56  ? 0.41094 0.49840 0.36099 -0.06322 0.10560  0.12418  56  ASP   A CA  
426  C  C   . ASP   A 56  ? 0.38681 0.45957 0.31643 -0.06437 0.09356  0.12864  56  ASP   A C   
427  O  O   . ASP   A 56  ? 0.34796 0.41470 0.27387 -0.06890 0.09110  0.13896  56  ASP   A O   
428  C  CB  . ASP   A 56  ? 0.47129 0.56074 0.39943 -0.05950 0.12028  0.11705  56  ASP   A CB  
429  C  CG  . ASP   A 56  ? 0.49597 0.59847 0.43865 -0.06114 0.13503  0.11858  56  ASP   A CG  
430  O  OD1 . ASP   A 56  ? 0.49884 0.61064 0.47105 -0.06465 0.13293  0.12450  56  ASP   A OD1 
431  O  OD2 . ASP   A 56  ? 0.54979 0.65332 0.47445 -0.05937 0.14860  0.11314  56  ASP   A OD2 
432  N  N   . LEU   A 57  ? 0.38189 0.44937 0.29915 -0.06007 0.08575  0.12122  57  LEU   A N   
433  C  CA  . LEU   A 57  ? 0.38580 0.44139 0.28478 -0.06052 0.07347  0.12475  57  LEU   A CA  
434  C  C   . LEU   A 57  ? 0.35722 0.40778 0.27668 -0.06372 0.06182  0.13321  57  LEU   A C   
435  O  O   . LEU   A 57  ? 0.35756 0.40003 0.26884 -0.06568 0.05577  0.14200  57  LEU   A O   
436  C  CB  . LEU   A 57  ? 0.37993 0.43221 0.26518 -0.05590 0.06700  0.11408  57  LEU   A CB  
437  C  CG  . LEU   A 57  ? 0.42741 0.47990 0.28821 -0.05245 0.07792  0.10409  57  LEU   A CG  
438  C  CD1 . LEU   A 57  ? 0.43575 0.48494 0.28834 -0.04848 0.07121  0.09248  57  LEU   A CD1 
439  C  CD2 . LEU   A 57  ? 0.46990 0.51568 0.30159 -0.05436 0.08107  0.10852  57  LEU   A CD2 
440  N  N   . LEU   A 58  ? 0.32721 0.38189 0.27378 -0.06416 0.05897  0.13052  58  LEU   A N   
441  C  CA  . LEU   A 58  ? 0.31590 0.36244 0.28089 -0.06689 0.04837  0.13587  58  LEU   A CA  
442  C  C   . LEU   A 58  ? 0.31790 0.36242 0.29391 -0.07253 0.05209  0.14608  58  LEU   A C   
443  O  O   . LEU   A 58  ? 0.30357 0.33710 0.28327 -0.07422 0.04485  0.15333  58  LEU   A O   
444  C  CB  . LEU   A 58  ? 0.33680 0.38674 0.32469 -0.06647 0.04404  0.12848  58  LEU   A CB  
445  C  CG  . LEU   A 58  ? 0.32631 0.36439 0.33062 -0.06860 0.03313  0.13052  58  LEU   A CG  
446  C  CD1 . LEU   A 58  ? 0.30892 0.33538 0.29849 -0.06506 0.02396  0.13339  58  LEU   A CD1 
447  C  CD2 . LEU   A 58  ? 0.30360 0.34459 0.32708 -0.06895 0.02913  0.12181  58  LEU   A CD2 
448  N  N   . ILE   A 59  ? 0.30277 0.35760 0.28502 -0.07525 0.06368  0.14702  59  ILE   A N   
449  C  CA  . ILE   A 59  ? 0.32203 0.37524 0.31559 -0.08147 0.06727  0.15679  59  ILE   A CA  
450  C  C   . ILE   A 59  ? 0.34559 0.38993 0.31753 -0.08222 0.06717  0.16707  59  ILE   A C   
451  O  O   . ILE   A 59  ? 0.35905 0.39634 0.33917 -0.08661 0.06548  0.17683  59  ILE   A O   
452  C  CB  . ILE   A 59  ? 0.32113 0.38924 0.32654 -0.08414 0.08000  0.15577  59  ILE   A CB  
453  C  CG1 . ILE   A 59  ? 0.35489 0.42198 0.37915 -0.09185 0.08163  0.16451  59  ILE   A CG1 
454  C  CG2 . ILE   A 59  ? 0.34029 0.41407 0.32183 -0.08168 0.09239  0.15564  59  ILE   A CG2 
455  C  CD1 . ILE   A 59  ? 0.34440 0.40041 0.38792 -0.09521 0.06989  0.16459  59  ILE   A CD1 
456  N  N   . ARG   A 60  ? 0.35586 0.39975 0.29984 -0.07818 0.06831  0.16490  60  ARG   A N   
457  C  CA  . ARG   A 60  ? 0.38337 0.42008 0.30391 -0.07869 0.06679  0.17402  60  ARG   A CA  
458  C  C   . ARG   A 60  ? 0.38031 0.40634 0.30081 -0.07648 0.05188  0.17798  60  ARG   A C   
459  O  O   . ARG   A 60  ? 0.40270 0.42364 0.30653 -0.07656 0.04825  0.18661  60  ARG   A O   
460  C  CB  . ARG   A 60  ? 0.39867 0.43878 0.28821 -0.07581 0.07388  0.16826  60  ARG   A CB  
461  C  CG  . ARG   A 60  ? 0.40365 0.45386 0.29417 -0.07683 0.09030  0.16365  60  ARG   A CG  
462  C  CD  . ARG   A 60  ? 0.42085 0.47131 0.28052 -0.07337 0.09859  0.15571  60  ARG   A CD  
463  N  NE  . ARG   A 60  ? 0.42943 0.48939 0.29362 -0.07370 0.11570  0.15078  60  ARG   A NE  
464  C  CZ  . ARG   A 60  ? 0.47487 0.53705 0.32512 -0.06938 0.12540  0.13902  60  ARG   A CZ  
465  N  NH1 . ARG   A 60  ? 0.46940 0.52447 0.29869 -0.06458 0.11948  0.13051  60  ARG   A NH1 
466  N  NH2 . ARG   A 60  ? 0.48675 0.55873 0.34571 -0.07002 0.14137  0.13540  60  ARG   A NH2 
467  N  N   . LYS   A 61  ? 0.35482 0.37791 0.29402 -0.07437 0.04353  0.17205  61  LYS   A N   
468  C  CA  . LYS   A 61  ? 0.36032 0.37349 0.30382 -0.07150 0.03049  0.17485  61  LYS   A CA  
469  C  C   . LYS   A 61  ? 0.36575 0.36968 0.33367 -0.07447 0.02797  0.18207  61  LYS   A C   
470  O  O   . LYS   A 61  ? 0.38471 0.39037 0.36965 -0.07894 0.03402  0.18112  61  LYS   A O   
471  C  CB  . LYS   A 61  ? 0.35677 0.37059 0.30446 -0.06711 0.02369  0.16329  61  LYS   A CB  
472  C  CG  . LYS   A 61  ? 0.35763 0.37799 0.28046 -0.06410 0.02501  0.15534  61  LYS   A CG  
473  C  CD  . LYS   A 61  ? 0.40093 0.41705 0.30557 -0.06182 0.01562  0.15944  61  LYS   A CD  
474  C  CE  . LYS   A 61  ? 0.44443 0.46539 0.31969 -0.06087 0.01878  0.15237  61  LYS   A CE  
475  N  NZ  . LYS   A 61  ? 0.50784 0.52642 0.36344 -0.06123 0.01206  0.15972  61  LYS   A NZ  
476  N  N   . SER   A 62  ? 0.41082 0.40494 0.38089 -0.07200 0.01905  0.18904  62  SER   A N   
477  C  CA  . SER   A 62  ? 0.41461 0.39644 0.40754 -0.07323 0.01577  0.19431  62  SER   A CA  
478  C  C   . SER   A 62  ? 0.39491 0.36915 0.39848 -0.06748 0.00599  0.18848  62  SER   A C   
479  O  O   . SER   A 62  ? 0.38899 0.36804 0.38060 -0.06287 0.00061  0.18404  62  SER   A O   
480  C  CB  . SER   A 62  ? 0.42624 0.40231 0.41442 -0.07464 0.01545  0.20975  62  SER   A CB  
481  O  OG  . SER   A 62  ? 0.51070 0.49542 0.47876 -0.07820 0.02334  0.21562  62  SER   A OG  
482  N  N   . ASN   A 63  ? 0.37751 0.33914 0.40344 -0.06794 0.00424  0.18789  63  ASN   A N   
483  C  CA  . ASN   A 63  ? 0.37217 0.32483 0.40923 -0.06184 -0.00349 0.18296  63  ASN   A CA  
484  C  C   . ASN   A 63  ? 0.38503 0.33950 0.41183 -0.05583 -0.01083 0.19073  63  ASN   A C   
485  O  O   . ASN   A 63  ? 0.39196 0.34910 0.41726 -0.05054 -0.01689 0.18478  63  ASN   A O   
486  C  CB  . ASN   A 63  ? 0.38276 0.31867 0.44238 -0.06326 -0.00279 0.18303  63  ASN   A CB  
487  C  CG  . ASN   A 63  ? 0.39097 0.32464 0.46262 -0.06919 0.00167  0.17169  63  ASN   A CG  
488  O  OD1 . ASN   A 63  ? 0.37230 0.31673 0.43926 -0.07030 0.00273  0.16259  63  ASN   A OD1 
489  N  ND2 . ASN   A 63  ? 0.34509 0.26514 0.43221 -0.07371 0.00420  0.17240  63  ASN   A ND2 
490  N  N   . HIS   A 64  ? 0.41366 0.36772 0.43369 -0.05705 -0.01069 0.20439  64  HIS   A N   
491  C  CA  . HIS   A 64  ? 0.42293 0.37954 0.43575 -0.05207 -0.01876 0.21287  64  HIS   A CA  
492  C  C   . HIS   A 64  ? 0.43164 0.40207 0.42044 -0.05124 -0.02220 0.20876  64  HIS   A C   
493  O  O   . HIS   A 64  ? 0.43120 0.40551 0.41551 -0.04728 -0.03054 0.21227  64  HIS   A O   
494  C  CB  . HIS   A 64  ? 0.46545 0.41848 0.47630 -0.05420 -0.01801 0.22946  64  HIS   A CB  
495  C  CG  . HIS   A 64  ? 0.49230 0.45389 0.48060 -0.06015 -0.01192 0.23488  64  HIS   A CG  
496  N  ND1 . HIS   A 64  ? 0.51200 0.48488 0.47423 -0.06010 -0.01468 0.23669  64  HIS   A ND1 
497  C  CD2 . HIS   A 64  ? 0.50602 0.46623 0.49380 -0.06653 -0.00252 0.23840  64  HIS   A CD2 
498  C  CE1 . HIS   A 64  ? 0.52448 0.50166 0.46996 -0.06560 -0.00638 0.24083  64  HIS   A CE1 
499  N  NE2 . HIS   A 64  ? 0.53201 0.50255 0.49355 -0.06947 0.00122  0.24241  64  HIS   A NE2 
500  N  N   . ASN   A 65  ? 0.42436 0.40225 0.39882 -0.05495 -0.01585 0.20079  65  ASN   A N   
501  C  CA  . ASN   A 65  ? 0.42234 0.41074 0.37404 -0.05407 -0.01835 0.19425  65  ASN   A CA  
502  C  C   . ASN   A 65  ? 0.39704 0.38626 0.35622 -0.04927 -0.02509 0.18344  65  ASN   A C   
503  O  O   . ASN   A 65  ? 0.42040 0.41696 0.36280 -0.04826 -0.02921 0.17816  65  ASN   A O   
504  C  CB  . ASN   A 65  ? 0.42270 0.41780 0.35916 -0.05844 -0.00796 0.18802  65  ASN   A CB  
505  C  CG  . ASN   A 65  ? 0.47783 0.47470 0.39983 -0.06292 -0.00101 0.19827  65  ASN   A CG  
506  O  OD1 . ASN   A 65  ? 0.45545 0.45467 0.37769 -0.06686 0.00955  0.19710  65  ASN   A OD1 
507  N  ND2 . ASN   A 65  ? 0.48689 0.48350 0.39708 -0.06251 -0.00676 0.20894  65  ASN   A ND2 
508  N  N   . PHE   A 66  ? 0.37613 0.35720 0.35927 -0.04664 -0.02595 0.17948  66  PHE   A N   
509  C  CA  . PHE   A 66  ? 0.38709 0.36818 0.37852 -0.04206 -0.03107 0.16925  66  PHE   A CA  
510  C  C   . PHE   A 66  ? 0.40999 0.38565 0.41811 -0.03636 -0.03826 0.17453  66  PHE   A C   
511  O  O   . PHE   A 66  ? 0.39555 0.36010 0.42341 -0.03484 -0.03638 0.17772  66  PHE   A O   
512  C  CB  . PHE   A 66  ? 0.35243 0.32871 0.35723 -0.04326 -0.02588 0.15917  66  PHE   A CB  
513  C  CG  . PHE   A 66  ? 0.34469 0.32856 0.33724 -0.04827 -0.01836 0.15412  66  PHE   A CG  
514  C  CD1 . PHE   A 66  ? 0.31085 0.30342 0.28874 -0.04753 -0.01859 0.14541  66  PHE   A CD1 
515  C  CD2 . PHE   A 66  ? 0.36947 0.35226 0.36637 -0.05363 -0.01043 0.15804  66  PHE   A CD2 
516  C  CE1 . PHE   A 66  ? 0.32030 0.32045 0.28864 -0.05112 -0.01035 0.14076  66  PHE   A CE1 
517  C  CE2 . PHE   A 66  ? 0.35907 0.35113 0.34766 -0.05755 -0.00247 0.15356  66  PHE   A CE2 
518  C  CZ  . PHE   A 66  ? 0.31749 0.31827 0.29221 -0.05582 -0.00207 0.14494  66  PHE   A CZ  
519  N  N   . LEU   A 67  ? 0.38449 0.36795 0.38549 -0.03342 -0.04592 0.17480  67  LEU   A N   
520  C  CA  . LEU   A 67  ? 0.38482 0.36665 0.40310 -0.02755 -0.05254 0.17932  67  LEU   A CA  
521  C  C   . LEU   A 67  ? 0.33199 0.31321 0.36140 -0.02337 -0.05367 0.16708  67  LEU   A C   
522  O  O   . LEU   A 67  ? 0.33822 0.32772 0.35467 -0.02428 -0.05620 0.15917  67  LEU   A O   
523  C  CB  . LEU   A 67  ? 0.39799 0.39056 0.40381 -0.02777 -0.06074 0.18742  67  LEU   A CB  
524  C  CG  . LEU   A 67  ? 0.43224 0.42666 0.42718 -0.03098 -0.06197 0.20207  67  LEU   A CG  
525  C  CD1 . LEU   A 67  ? 0.48110 0.47214 0.46158 -0.03670 -0.05327 0.20355  67  LEU   A CD1 
526  C  CD2 . LEU   A 67  ? 0.51141 0.51824 0.48772 -0.03288 -0.07049 0.20510  67  LEU   A CD2 
527  N  N   . VAL   A 68  ? 0.33987 0.31015 0.39204 -0.01912 -0.05091 0.16472  68  VAL   A N   
528  C  CA  . VAL   A 68  ? 0.31979 0.28818 0.38390 -0.01451 -0.05105 0.15360  68  VAL   A CA  
529  C  C   . VAL   A 68  ? 0.34198 0.31040 0.42474 -0.00757 -0.05480 0.15850  68  VAL   A C   
530  O  O   . VAL   A 68  ? 0.33748 0.29690 0.43516 -0.00490 -0.05268 0.16579  68  VAL   A O   
531  C  CB  . VAL   A 68  ? 0.32839 0.28361 0.40271 -0.01539 -0.04372 0.14457  68  VAL   A CB  
532  C  CG1 . VAL   A 68  ? 0.30380 0.25725 0.38763 -0.01079 -0.04356 0.13275  68  VAL   A CG1 
533  C  CG2 . VAL   A 68  ? 0.33521 0.29287 0.39376 -0.02281 -0.03977 0.14144  68  VAL   A CG2 
534  N  N   . GLN   A 69  ? 0.31499 0.29364 0.39786 -0.00484 -0.05986 0.15467  69  GLN   A N   
535  C  CA  . GLN   A 69  ? 0.33736 0.31907 0.43938 0.00156  -0.06300 0.15920  69  GLN   A CA  
536  C  C   . GLN   A 69  ? 0.33209 0.31054 0.44706 0.00647  -0.05924 0.14703  69  GLN   A C   
537  O  O   . GLN   A 69  ? 0.25025 0.23523 0.35506 0.00471  -0.06069 0.13814  69  GLN   A O   
538  C  CB  . GLN   A 69  ? 0.38973 0.38753 0.48247 -0.00030 -0.07216 0.16584  69  GLN   A CB  
539  C  CG  . GLN   A 69  ? 0.46144 0.46269 0.54694 -0.00325 -0.07657 0.18060  69  GLN   A CG  
540  C  CD  . GLN   A 69  ? 0.57037 0.58094 0.67025 0.00024  -0.08369 0.19161  69  GLN   A CD  
541  O  OE1 . GLN   A 69  ? 0.56016 0.58405 0.65009 -0.00286 -0.09155 0.19332  69  GLN   A OE1 
542  N  NE2 . GLN   A 69  ? 0.57002 0.57323 0.69390 0.00642  -0.08081 0.19918  69  GLN   A NE2 
543  N  N   . ALA   A 70  ? 0.34780 0.31533 0.48410 0.01252  -0.05370 0.14613  70  ALA   A N   
544  C  CA  . ALA   A 70  ? 0.32089 0.28532 0.47008 0.01794  -0.04904 0.13497  70  ALA   A CA  
545  C  C   . ALA   A 70  ? 0.37752 0.35044 0.54478 0.02415  -0.05145 0.14169  70  ALA   A C   
546  O  O   . ALA   A 70  ? 0.37650 0.34161 0.56179 0.02933  -0.04766 0.14709  70  ALA   A O   
547  C  CB  . ALA   A 70  ? 0.32425 0.26913 0.48258 0.01978  -0.03953 0.12655  70  ALA   A CB  
548  N  N   . GLY   A 71  ? 0.40860 0.39735 0.57160 0.02320  -0.05761 0.14154  71  GLY   A N   
549  C  CA  . GLY   A 71  ? 0.44151 0.44135 0.62079 0.02719  -0.06168 0.15049  71  GLY   A CA  
550  C  C   . GLY   A 71  ? 0.46682 0.47092 0.64409 0.02484  -0.06829 0.16595  71  GLY   A C   
551  O  O   . GLY   A 71  ? 0.47972 0.48744 0.63554 0.01793  -0.07355 0.16907  71  GLY   A O   
552  N  N   . ASN   A 72  ? 0.47513 0.47855 0.67467 0.03077  -0.06745 0.17601  72  ASN   A N   
553  C  CA  . ASN   A 72  ? 0.52745 0.53352 0.72818 0.02952  -0.07311 0.19217  72  ASN   A CA  
554  C  C   . ASN   A 72  ? 0.52187 0.50961 0.72797 0.03153  -0.06611 0.19500  72  ASN   A C   
555  O  O   . ASN   A 72  ? 0.53202 0.51772 0.75196 0.03469  -0.06710 0.20825  72  ASN   A O   
556  C  CB  . ASN   A 72  ? 0.54804 0.56642 0.77072 0.03425  -0.07791 0.20407  72  ASN   A CB  
557  C  CG  . ASN   A 72  ? 0.60842 0.62133 0.85843 0.04354  -0.06893 0.19911  72  ASN   A CG  
558  O  OD1 . ASN   A 72  ? 0.65463 0.65068 0.90913 0.04721  -0.05857 0.18925  72  ASN   A OD1 
559  N  ND2 . ASN   A 72  ? 0.53787 0.56489 0.80603 0.04703  -0.07255 0.20592  72  ASN   A ND2 
560  N  N   . VAL   A 73  ? 0.46553 0.43965 0.66172 0.02940  -0.05916 0.18298  73  VAL   A N   
561  C  CA  . VAL   A 73  ? 0.48460 0.43987 0.68370 0.02938  -0.05227 0.18351  73  VAL   A CA  
562  C  C   . VAL   A 73  ? 0.44738 0.40056 0.62150 0.02075  -0.05304 0.18005  73  VAL   A C   
563  O  O   . VAL   A 73  ? 0.40380 0.36008 0.56460 0.01753  -0.05261 0.16856  73  VAL   A O   
564  C  CB  . VAL   A 73  ? 0.49163 0.42984 0.70593 0.03495  -0.04135 0.17065  73  VAL   A CB  
565  C  CG1 . VAL   A 73  ? 0.49535 0.41264 0.71154 0.03333  -0.03469 0.17040  73  VAL   A CG1 
566  C  CG2 . VAL   A 73  ? 0.51013 0.45124 0.74919 0.04396  -0.03893 0.17332  73  VAL   A CG2 
567  N  N   . GLN   A 74  ? 0.45326 0.40168 0.62165 0.01707  -0.05374 0.19049  74  GLN   A N   
568  C  CA  . GLN   A 74  ? 0.43475 0.38227 0.58046 0.00879  -0.05336 0.18852  74  GLN   A CA  
569  C  C   . GLN   A 74  ? 0.43006 0.35860 0.57994 0.00712  -0.04420 0.17937  74  GLN   A C   
570  O  O   . GLN   A 74  ? 0.43611 0.34999 0.60192 0.01002  -0.03937 0.18234  74  GLN   A O   
571  C  CB  . GLN   A 74  ? 0.51350 0.46671 0.64866 0.00469  -0.05823 0.20448  74  GLN   A CB  
572  C  CG  . GLN   A 74  ? 0.49930 0.45589 0.60838 -0.00390 -0.05780 0.20307  74  GLN   A CG  
573  C  CD  . GLN   A 74  ? 0.60037 0.55540 0.70217 -0.00785 -0.05825 0.21784  74  GLN   A CD  
574  O  OE1 . GLN   A 74  ? 0.62388 0.57789 0.73816 -0.00440 -0.06113 0.23084  74  GLN   A OE1 
575  N  NE2 . GLN   A 74  ? 0.60442 0.55938 0.68692 -0.01502 -0.05475 0.21645  74  GLN   A NE2 
576  N  N   . LEU   A 75  ? 0.39109 0.31965 0.52709 0.00204  -0.04193 0.16799  75  LEU   A N   
577  C  CA  . LEU   A 75  ? 0.38064 0.29316 0.51882 -0.00158 -0.03426 0.15835  75  LEU   A CA  
578  C  C   . LEU   A 75  ? 0.41794 0.32960 0.54352 -0.00974 -0.03310 0.16530  75  LEU   A C   
579  O  O   . LEU   A 75  ? 0.45535 0.38001 0.56239 -0.01436 -0.03606 0.16749  75  LEU   A O   
580  C  CB  . LEU   A 75  ? 0.36709 0.28103 0.49929 -0.00290 -0.03248 0.14274  75  LEU   A CB  
581  C  CG  . LEU   A 75  ? 0.35713 0.27162 0.50027 0.00441  -0.03191 0.13361  75  LEU   A CG  
582  C  CD1 . LEU   A 75  ? 0.31944 0.23198 0.45573 0.00158  -0.02912 0.11837  75  LEU   A CD1 
583  C  CD2 . LEU   A 75  ? 0.38780 0.28763 0.55146 0.01071  -0.02649 0.13292  75  LEU   A CD2 
584  N  N   . ARG   A 76  ? 0.40948 0.30556 0.54468 -0.01179 -0.02798 0.16808  76  ARG   A N   
585  C  CA  . ARG   A 76  ? 0.41669 0.31222 0.54198 -0.01981 -0.02597 0.17542  76  ARG   A CA  
586  C  C   . ARG   A 76  ? 0.37790 0.27354 0.49467 -0.02720 -0.02194 0.16349  76  ARG   A C   
587  O  O   . ARG   A 76  ? 0.37164 0.25550 0.49730 -0.02822 -0.01797 0.15097  76  ARG   A O   
588  C  CB  . ARG   A 76  ? 0.43734 0.31596 0.57669 -0.02022 -0.02203 0.18293  76  ARG   A CB  
589  C  CG  . ARG   A 76  ? 0.46459 0.34101 0.59604 -0.02941 -0.01850 0.18940  76  ARG   A CG  
590  C  CD  . ARG   A 76  ? 0.53605 0.39485 0.68194 -0.02986 -0.01503 0.19794  76  ARG   A CD  
591  N  NE  . ARG   A 76  ? 0.59912 0.43817 0.75714 -0.03259 -0.00905 0.18504  76  ARG   A NE  
592  C  CZ  . ARG   A 76  ? 0.65400 0.48307 0.81276 -0.04181 -0.00419 0.18336  76  ARG   A CZ  
593  N  NH1 . ARG   A 76  ? 0.62817 0.46486 0.77826 -0.04842 -0.00347 0.19475  76  ARG   A NH1 
594  N  NH2 . ARG   A 76  ? 0.64436 0.45555 0.81218 -0.04504 0.00023  0.16962  76  ARG   A NH2 
595  N  N   . VAL   A 77  ? 0.38589 0.29538 0.48510 -0.03245 -0.02277 0.16687  77  VAL   A N   
596  C  CA  . VAL   A 77  ? 0.38204 0.29476 0.47453 -0.03971 -0.01866 0.15775  77  VAL   A CA  
597  C  C   . VAL   A 77  ? 0.38507 0.28849 0.48351 -0.04716 -0.01291 0.16121  77  VAL   A C   
598  O  O   . VAL   A 77  ? 0.38923 0.29404 0.48358 -0.04919 -0.01204 0.17414  77  VAL   A O   
599  C  CB  . VAL   A 77  ? 0.34727 0.27844 0.41903 -0.04179 -0.02031 0.15963  77  VAL   A CB  
600  C  CG1 . VAL   A 77  ? 0.34592 0.28208 0.41314 -0.04940 -0.01473 0.15312  77  VAL   A CG1 
601  C  CG2 . VAL   A 77  ? 0.35539 0.29462 0.42177 -0.03578 -0.02604 0.15368  77  VAL   A CG2 
602  N  N   . ILE   A 78  ? 0.37352 0.26752 0.48134 -0.05190 -0.00922 0.14951  78  ILE   A N   
603  C  CA  . ILE   A 78  ? 0.35704 0.24208 0.47189 -0.06035 -0.00419 0.15082  78  ILE   A CA  
604  C  C   . ILE   A 78  ? 0.35921 0.25510 0.47012 -0.06903 -0.00113 0.14392  78  ILE   A C   
605  O  O   . ILE   A 78  ? 0.34638 0.23809 0.46364 -0.07732 0.00288  0.14443  78  ILE   A O   
606  C  CB  . ILE   A 78  ? 0.38109 0.24382 0.51149 -0.06032 -0.00237 0.14315  78  ILE   A CB  
607  C  CG1 . ILE   A 78  ? 0.38851 0.24810 0.52101 -0.06113 -0.00257 0.12474  78  ILE   A CG1 
608  C  CG2 . ILE   A 78  ? 0.41328 0.26625 0.55085 -0.05089 -0.00435 0.15132  78  ILE   A CG2 
609  C  CD1 . ILE   A 78  ? 0.40571 0.24347 0.54917 -0.05820 -0.00082 0.11531  78  ILE   A CD1 
610  N  N   . GLY   A 79  ? 0.36130 0.27160 0.46328 -0.06756 -0.00289 0.13774  79  GLY   A N   
611  C  CA  . GLY   A 79  ? 0.32737 0.25116 0.42692 -0.07464 0.00007  0.13237  79  GLY   A CA  
612  C  C   . GLY   A 79  ? 0.34029 0.27980 0.42729 -0.07051 -0.00199 0.12936  79  GLY   A C   
613  O  O   . GLY   A 79  ? 0.33313 0.27013 0.41664 -0.06346 -0.00658 0.12673  79  GLY   A O   
614  N  N   . HIS   A 80  ? 0.33614 0.29204 0.41682 -0.07459 0.00193  0.12984  80  HIS   A N   
615  C  CA  . HIS   A 80  ? 0.28727 0.25741 0.35620 -0.07131 0.00121  0.12578  80  HIS   A CA  
616  C  C   . HIS   A 80  ? 0.31695 0.30142 0.39101 -0.07702 0.00577  0.11997  80  HIS   A C   
617  O  O   . HIS   A 80  ? 0.31493 0.30262 0.39681 -0.08310 0.01047  0.12306  80  HIS   A O   
618  C  CB  . HIS   A 80  ? 0.29817 0.27625 0.34748 -0.06740 0.00228  0.13515  80  HIS   A CB  
619  C  CG  . HIS   A 80  ? 0.34631 0.33112 0.39065 -0.07190 0.00949  0.14385  80  HIS   A CG  
620  N  ND1 . HIS   A 80  ? 0.34263 0.31841 0.39031 -0.07390 0.01039  0.15392  80  HIS   A ND1 
621  C  CD2 . HIS   A 80  ? 0.33290 0.33244 0.37033 -0.07456 0.01706  0.14386  80  HIS   A CD2 
622  C  CE1 . HIS   A 80  ? 0.39336 0.37800 0.43511 -0.07814 0.01788  0.16012  80  HIS   A CE1 
623  N  NE2 . HIS   A 80  ? 0.39003 0.38920 0.42574 -0.07830 0.02244  0.15381  80  HIS   A NE2 
624  N  N   . SER   A 81  ? 0.26953 0.26354 0.34049 -0.07484 0.00426  0.11201  81  SER   A N   
625  C  CA  . SER   A 81  ? 0.27199 0.28337 0.34810 -0.07829 0.00859  0.10743  81  SER   A CA  
626  C  C   . SER   A 81  ? 0.24978 0.27078 0.31329 -0.07039 0.00780  0.09871  81  SER   A C   
627  O  O   . SER   A 81  ? 0.28273 0.29600 0.33740 -0.06402 0.00243  0.09356  81  SER   A O   
628  C  CB  . SER   A 81  ? 0.26653 0.27668 0.36072 -0.08454 0.00564  0.09847  81  SER   A CB  
629  O  OG  . SER   A 81  ? 0.28566 0.28378 0.38159 -0.08265 -0.00134 0.08884  81  SER   A OG  
630  N  N   . MET   A 82  ? 0.21347 0.25131 0.27778 -0.07033 0.01369  0.09692  82  MET   A N   
631  C  CA  . MET   A 82  ? 0.25452 0.30077 0.31052 -0.06282 0.01359  0.08720  82  MET   A CA  
632  C  C   . MET   A 82  ? 0.22050 0.27289 0.29103 -0.06383 0.00935  0.07762  82  MET   A C   
633  O  O   . MET   A 82  ? 0.21172 0.27282 0.29890 -0.07069 0.01062  0.07958  82  MET   A O   
634  C  CB  . MET   A 82  ? 0.26489 0.32540 0.31381 -0.06064 0.02369  0.09044  82  MET   A CB  
635  C  CG  . MET   A 82  ? 0.22918 0.28938 0.26018 -0.05245 0.02411  0.08364  82  MET   A CG  
636  S  SD  . MET   A 82  ? 0.32320 0.39087 0.33681 -0.05120 0.03678  0.08953  82  MET   A SD  
637  C  CE  . MET   A 82  ? 0.33526 0.42176 0.37195 -0.05489 0.04724  0.09371  82  MET   A CE  
638  N  N   . GLN   A 83  ? 0.20524 0.25482 0.26931 -0.05758 0.00424  0.06810  83  GLN   A N   
639  C  CA  . GLN   A 83  ? 0.20834 0.26726 0.28202 -0.05724 0.00095  0.06001  83  GLN   A CA  
640  C  C   . GLN   A 83  ? 0.17587 0.24083 0.23914 -0.04828 0.00317  0.05553  83  GLN   A C   
641  O  O   . GLN   A 83  ? 0.16849 0.22426 0.21986 -0.04309 -0.00035 0.05077  83  GLN   A O   
642  C  CB  . GLN   A 83  ? 0.23011 0.27795 0.30756 -0.06001 -0.00733 0.05262  83  GLN   A CB  
643  C  CG  . GLN   A 83  ? 0.27596 0.33181 0.35666 -0.05861 -0.01205 0.04398  83  GLN   A CG  
644  C  CD  . GLN   A 83  ? 0.33230 0.37552 0.41323 -0.06222 -0.01867 0.03619  83  GLN   A CD  
645  O  OE1 . GLN   A 83  ? 0.41067 0.44710 0.49975 -0.07057 -0.02026 0.03639  83  GLN   A OE1 
646  N  NE2 . GLN   A 83  ? 0.33695 0.37681 0.40930 -0.05658 -0.02185 0.02882  83  GLN   A NE2 
647  N  N   . ASN   A 84  ? 0.13762 0.21774 0.20682 -0.04654 0.00983  0.05766  84  ASN   A N   
648  C  CA  . ASN   A 84  ? 0.16536 0.24994 0.22630 -0.03797 0.01405  0.05373  84  ASN   A CA  
649  C  C   . ASN   A 84  ? 0.15011 0.22303 0.18954 -0.03458 0.01660  0.05384  84  ASN   A C   
650  O  O   . ASN   A 84  ? 0.16941 0.24167 0.20264 -0.03744 0.02225  0.06063  84  ASN   A O   
651  C  CB  . ASN   A 84  ? 0.10713 0.19282 0.17202 -0.03475 0.00692  0.04645  84  ASN   A CB  
652  C  CG  . ASN   A 84  ? 0.12389 0.22231 0.20799 -0.03989 0.00294  0.04738  84  ASN   A CG  
653  O  OD1 . ASN   A 84  ? 0.10268 0.21664 0.20069 -0.04069 0.00812  0.05246  84  ASN   A OD1 
654  N  ND2 . ASN   A 84  ? 0.13926 0.23160 0.22449 -0.04415 -0.00604 0.04271  84  ASN   A ND2 
655  N  N   . CYS   A 85  ? 0.16137 0.22587 0.18906 -0.02956 0.01226  0.04743  85  CYS   A N   
656  C  CA  . CYS   A 85  ? 0.15615 0.21139 0.16372 -0.02741 0.01305  0.04720  85  CYS   A CA  
657  C  C   . CYS   A 85  ? 0.19491 0.23867 0.19751 -0.02982 0.00478  0.04948  85  CYS   A C   
658  O  O   . CYS   A 85  ? 0.21343 0.25069 0.20060 -0.02855 0.00275  0.04995  85  CYS   A O   
659  C  CB  . CYS   A 85  ? 0.15998 0.21363 0.15935 -0.02106 0.01389  0.03933  85  CYS   A CB  
660  S  SG  . CYS   A 85  ? 0.16589 0.23127 0.17149 -0.01671 0.02613  0.03830  85  CYS   A SG  
661  N  N   . VAL   A 86  ? 0.14866 0.18967 0.16444 -0.03350 0.00008  0.05109  86  VAL   A N   
662  C  CA  . VAL   A 86  ? 0.16324 0.19264 0.17721 -0.03474 -0.00599 0.05431  86  VAL   A CA  
663  C  C   . VAL   A 86  ? 0.17703 0.20379 0.19710 -0.04070 -0.00402 0.06386  86  VAL   A C   
664  O  O   . VAL   A 86  ? 0.17203 0.20566 0.20238 -0.04519 0.00032  0.06620  86  VAL   A O   
665  C  CB  . VAL   A 86  ? 0.16446 0.18776 0.18680 -0.03329 -0.01234 0.04754  86  VAL   A CB  
666  C  CG1 . VAL   A 86  ? 0.17994 0.20552 0.19624 -0.02767 -0.01420 0.03962  86  VAL   A CG1 
667  C  CG2 . VAL   A 86  ? 0.18291 0.20874 0.21935 -0.03783 -0.01245 0.04499  86  VAL   A CG2 
668  N  N   . LEU   A 87  ? 0.16978 0.18730 0.18448 -0.04088 -0.00738 0.07068  87  LEU   A N   
669  C  CA  . LEU   A 87  ? 0.19397 0.20500 0.21610 -0.04597 -0.00689 0.08073  87  LEU   A CA  
670  C  C   . LEU   A 87  ? 0.22945 0.22873 0.26575 -0.04627 -0.01187 0.07726  87  LEU   A C   
671  O  O   . LEU   A 87  ? 0.19838 0.19310 0.23407 -0.04129 -0.01640 0.07098  87  LEU   A O   
672  C  CB  . LEU   A 87  ? 0.22374 0.23120 0.23250 -0.04561 -0.00806 0.09201  87  LEU   A CB  
673  C  CG  . LEU   A 87  ? 0.26357 0.27900 0.25691 -0.04816 -0.00149 0.09939  87  LEU   A CG  
674  C  CD1 . LEU   A 87  ? 0.26936 0.27907 0.25145 -0.04881 -0.00573 0.11194  87  LEU   A CD1 
675  C  CD2 . LEU   A 87  ? 0.28411 0.30484 0.28883 -0.05411 0.00628  0.10406  87  LEU   A CD2 
676  N  N   . LYS   A 88  ? 0.22167 0.21575 0.27086 -0.05249 -0.01018 0.08083  88  LYS   A N   
677  C  CA  . LYS   A 88  ? 0.24801 0.22699 0.30976 -0.05377 -0.01331 0.07812  88  LYS   A CA  
678  C  C   . LYS   A 88  ? 0.24141 0.20941 0.30737 -0.05616 -0.01257 0.09208  88  LYS   A C   
679  O  O   . LYS   A 88  ? 0.26990 0.23930 0.34054 -0.06302 -0.00862 0.10004  88  LYS   A O   
680  C  CB  . LYS   A 88  ? 0.25464 0.23446 0.32799 -0.06041 -0.01271 0.06958  88  LYS   A CB  
681  C  CG  . LYS   A 88  ? 0.20630 0.19544 0.27637 -0.05764 -0.01481 0.05697  88  LYS   A CG  
682  C  CD  . LYS   A 88  ? 0.29648 0.28959 0.37714 -0.06579 -0.01555 0.05065  88  LYS   A CD  
683  C  CE  . LYS   A 88  ? 0.33907 0.32225 0.42100 -0.06618 -0.01955 0.03828  88  LYS   A CE  
684  N  NZ  . LYS   A 88  ? 0.36324 0.34030 0.45580 -0.07702 -0.02098 0.03392  88  LYS   A NZ  
685  N  N   . LEU   A 89  ? 0.24633 0.20467 0.31198 -0.05042 -0.01627 0.09640  89  LEU   A N   
686  C  CA  . LEU   A 89  ? 0.24445 0.19229 0.31501 -0.05084 -0.01648 0.11064  89  LEU   A CA  
687  C  C   . LEU   A 89  ? 0.26768 0.19779 0.35453 -0.05027 -0.01614 0.10483  89  LEU   A C   
688  O  O   . LEU   A 89  ? 0.26085 0.18354 0.35277 -0.04437 -0.01852 0.09862  89  LEU   A O   
689  C  CB  . LEU   A 89  ? 0.26802 0.21967 0.32808 -0.04366 -0.02111 0.11812  89  LEU   A CB  
690  C  CG  . LEU   A 89  ? 0.26515 0.23234 0.30478 -0.04471 -0.02086 0.12191  89  LEU   A CG  
691  C  CD1 . LEU   A 89  ? 0.26263 0.23315 0.29204 -0.03930 -0.02663 0.12806  89  LEU   A CD1 
692  C  CD2 . LEU   A 89  ? 0.28496 0.25767 0.31946 -0.05088 -0.01436 0.12801  89  LEU   A CD2 
693  N  N   . LYS   A 90  ? 0.26852 0.19160 0.36299 -0.05635 -0.01242 0.10609  90  LYS   A N   
694  C  CA  . LYS   A 90  ? 0.30831 0.21235 0.41558 -0.05631 -0.01112 0.10013  90  LYS   A CA  
695  C  C   . LYS   A 90  ? 0.30675 0.20185 0.41767 -0.04899 -0.01189 0.11056  90  LYS   A C   
696  O  O   . LYS   A 90  ? 0.34401 0.24370 0.45066 -0.04940 -0.01180 0.12382  90  LYS   A O   
697  C  CB  . LYS   A 90  ? 0.33891 0.23803 0.45255 -0.06635 -0.00743 0.09751  90  LYS   A CB  
698  C  CG  . LYS   A 90  ? 0.38812 0.27380 0.50889 -0.07010 -0.00691 0.08172  90  LYS   A CG  
699  C  CD  . LYS   A 90  ? 0.42571 0.29500 0.55450 -0.07614 -0.00360 0.08243  90  LYS   A CD  
700  C  CE  . LYS   A 90  ? 0.43937 0.29693 0.57087 -0.08311 -0.00317 0.06538  90  LYS   A CE  
701  N  NZ  . LYS   A 90  ? 0.44242 0.28807 0.58002 -0.09271 -0.00044 0.06642  90  LYS   A NZ  
702  N  N   . VAL   A 91  ? 0.31759 0.20164 0.43628 -0.04196 -0.01248 0.10472  91  VAL   A N   
703  C  CA  . VAL   A 91  ? 0.33054 0.20833 0.45604 -0.03403 -0.01340 0.11432  91  VAL   A CA  
704  C  C   . VAL   A 91  ? 0.33840 0.19451 0.47725 -0.03382 -0.00874 0.10873  91  VAL   A C   
705  O  O   . VAL   A 91  ? 0.37232 0.21805 0.51316 -0.03825 -0.00560 0.09442  91  VAL   A O   
706  C  CB  . VAL   A 91  ? 0.32015 0.20652 0.44489 -0.02456 -0.01761 0.11440  91  VAL   A CB  
707  C  CG1 . VAL   A 91  ? 0.32299 0.22895 0.43203 -0.02575 -0.02235 0.11985  91  VAL   A CG1 
708  C  CG2 . VAL   A 91  ? 0.30250 0.18240 0.43187 -0.02205 -0.01555 0.09825  91  VAL   A CG2 
709  N  N   . ASP   A 92  ? 0.36978 0.21897 0.51680 -0.02909 -0.00846 0.12001  92  ASP   A N   
710  C  CA  . ASP   A 92  ? 0.42588 0.25292 0.58509 -0.02943 -0.00342 0.11634  92  ASP   A CA  
711  C  C   . ASP   A 92  ? 0.42555 0.24184 0.59363 -0.02127 -0.00059 0.10510  92  ASP   A C   
712  O  O   . ASP   A 92  ? 0.41025 0.20651 0.58742 -0.02085 0.00445  0.09982  92  ASP   A O   
713  C  CB  . ASP   A 92  ? 0.44396 0.26720 0.60977 -0.02762 -0.00380 0.13380  92  ASP   A CB  
714  C  CG  . ASP   A 92  ? 0.53416 0.36067 0.70924 -0.01606 -0.00632 0.14250  92  ASP   A CG  
715  O  OD1 . ASP   A 92  ? 0.61006 0.42084 0.79913 -0.01045 -0.00233 0.13866  92  ASP   A OD1 
716  O  OD2 . ASP   A 92  ? 0.52174 0.36701 0.69008 -0.01291 -0.01220 0.15250  92  ASP   A OD2 
717  N  N   . THR   A 93  ? 0.40242 0.23124 0.56772 -0.01501 -0.00310 0.10110  93  THR   A N   
718  C  CA  . THR   A 93  ? 0.41289 0.23480 0.58653 -0.00661 0.00046  0.09107  93  THR   A CA  
719  C  C   . THR   A 93  ? 0.36374 0.19130 0.52782 -0.00866 0.00063  0.07570  93  THR   A C   
720  O  O   . THR   A 93  ? 0.31167 0.15678 0.46696 -0.00965 -0.00453 0.07866  93  THR   A O   
721  C  CB  . THR   A 93  ? 0.40468 0.23845 0.58757 0.00413  -0.00277 0.10312  93  THR   A CB  
722  O  OG1 . THR   A 93  ? 0.44918 0.28118 0.63907 0.00500  -0.00455 0.11952  93  THR   A OG1 
723  C  CG2 . THR   A 93  ? 0.39856 0.22444 0.59382 0.01319  0.00292  0.09405  93  THR   A CG2 
724  N  N   . ALA   A 94  ? 0.33647 0.14884 0.50103 -0.00960 0.00653  0.05920  94  ALA   A N   
725  C  CA  . ALA   A 94  ? 0.30598 0.12338 0.46206 -0.01019 0.00721  0.04444  94  ALA   A CA  
726  C  C   . ALA   A 94  ? 0.31999 0.14679 0.48285 0.00149  0.00785  0.04604  94  ALA   A C   
727  O  O   . ALA   A 94  ? 0.32748 0.14831 0.50315 0.00972  0.01160  0.05003  94  ALA   A O   
728  C  CB  . ALA   A 94  ? 0.33067 0.12954 0.48200 -0.01557 0.01313  0.02592  94  ALA   A CB  
729  N  N   . ASN   A 95  ? 0.29802 0.14033 0.45361 0.00196  0.00412  0.04368  95  ASN   A N   
730  C  CA  . ASN   A 95  ? 0.28682 0.14012 0.44889 0.01192  0.00431  0.04524  95  ASN   A CA  
731  C  C   . ASN   A 95  ? 0.28648 0.12775 0.45317 0.01699  0.01364  0.03097  95  ASN   A C   
732  O  O   . ASN   A 95  ? 0.29236 0.12906 0.44818 0.01275  0.01690  0.01545  95  ASN   A O   
733  C  CB  . ASN   A 95  ? 0.23730 0.10755 0.38940 0.01017  -0.00143 0.04437  95  ASN   A CB  
734  C  CG  . ASN   A 95  ? 0.22981 0.11402 0.38877 0.01928  -0.00257 0.04794  95  ASN   A CG  
735  O  OD1 . ASN   A 95  ? 0.24621 0.12926 0.41865 0.02689  0.00111  0.05136  95  ASN   A OD1 
736  N  ND2 . ASN   A 95  ? 0.20591 0.10415 0.35652 0.01807  -0.00780 0.04753  95  ASN   A ND2 
737  N  N   . PRO   A 96  ? 0.32635 0.16346 0.50809 0.02575  0.01829  0.03557  96  PRO   A N   
738  C  CA  . PRO   A 96  ? 0.31485 0.14021 0.49995 0.03063  0.02867  0.02156  96  PRO   A CA  
739  C  C   . PRO   A 96  ? 0.30707 0.14501 0.48786 0.03423  0.03069  0.01364  96  PRO   A C   
740  O  O   . PRO   A 96  ? 0.32141 0.15078 0.49842 0.03601  0.03961  -0.00080 96  PRO   A O   
741  C  CB  . PRO   A 96  ? 0.32710 0.14943 0.53259 0.03979  0.03207  0.03228  96  PRO   A CB  
742  C  CG  . PRO   A 96  ? 0.33084 0.17246 0.54289 0.04160  0.02212  0.05140  96  PRO   A CG  
743  C  CD  . PRO   A 96  ? 0.29078 0.13753 0.48677 0.03192  0.01396  0.05392  96  PRO   A CD  
744  N  N   . LYS   A 97  ? 0.27733 0.13518 0.45723 0.03487  0.02280  0.02254  97  LYS   A N   
745  C  CA  . LYS   A 97  ? 0.27541 0.14596 0.45132 0.03754  0.02391  0.01619  97  LYS   A CA  
746  C  C   . LYS   A 97  ? 0.25909 0.13025 0.41659 0.02913  0.02103  0.00588  97  LYS   A C   
747  O  O   . LYS   A 97  ? 0.24514 0.12854 0.39854 0.03054  0.02002  0.00275  97  LYS   A O   
748  C  CB  . LYS   A 97  ? 0.25259 0.14491 0.43866 0.04270  0.01661  0.03130  97  LYS   A CB  
749  C  CG  . LYS   A 97  ? 0.27849 0.17332 0.48438 0.05134  0.02074  0.03894  97  LYS   A CG  
750  C  CD  . LYS   A 97  ? 0.35246 0.27024 0.56780 0.05457  0.01273  0.05291  97  LYS   A CD  
751  C  CE  . LYS   A 97  ? 0.36674 0.28898 0.59059 0.05461  0.00506  0.06974  97  LYS   A CE  
752  N  NZ  . LYS   A 97  ? 0.44008 0.38517 0.66465 0.05361  -0.00562 0.08148  97  LYS   A NZ  
753  N  N   . THR   A 98  ? 0.27914 0.13807 0.42646 0.02000  0.01975  0.00051  98  THR   A N   
754  C  CA  . THR   A 98  ? 0.26455 0.12626 0.39571 0.01085  0.01625  -0.00900 98  THR   A CA  
755  C  C   . THR   A 98  ? 0.25629 0.11768 0.37604 0.01115  0.02318  -0.02584 98  THR   A C   
756  O  O   . THR   A 98  ? 0.26247 0.10825 0.37881 0.01049  0.03124  -0.03753 98  THR   A O   
757  C  CB  . THR   A 98  ? 0.30119 0.15162 0.42484 -0.00019 0.01407  -0.01237 98  THR   A CB  
758  O  OG1 . THR   A 98  ? 0.27847 0.13108 0.41003 -0.00071 0.00865  0.00410  98  THR   A OG1 
759  C  CG2 . THR   A 98  ? 0.27044 0.13440 0.37445 -0.00988 0.00843  -0.01954 98  THR   A CG2 
760  N  N   . PRO   A 99  ? 0.26640 0.14738 0.37547 0.01148  0.01995  -0.02664 99  PRO   A N   
761  C  CA  . PRO   A 99  ? 0.26516 0.14688 0.36031 0.01033  0.02603  -0.04144 99  PRO   A CA  
762  C  C   . PRO   A 99  ? 0.26165 0.14001 0.33692 -0.00169 0.02272  -0.05224 99  PRO   A C   
763  O  O   . PRO   A 99  ? 0.27038 0.15038 0.34375 -0.00880 0.01526  -0.04724 99  PRO   A O   
764  C  CB  . PRO   A 99  ? 0.22738 0.13203 0.31954 0.01374  0.02184  -0.03508 99  PRO   A CB  
765  C  CG  . PRO   A 99  ? 0.22966 0.14531 0.32135 0.01024  0.01104  -0.02302 99  PRO   A CG  
766  C  CD  . PRO   A 99  ? 0.24694 0.14917 0.35249 0.01086  0.01027  -0.01506 99  PRO   A CD  
767  N  N   . LYS   A 100 ? 0.28001 0.15533 0.34041 -0.00423 0.02830  -0.06656 100 LYS   A N   
768  C  CA  . LYS   A 100 ? 0.29690 0.17669 0.33691 -0.01577 0.02257  -0.07479 100 LYS   A CA  
769  C  C   . LYS   A 100 ? 0.29522 0.19904 0.33129 -0.01642 0.01311  -0.06414 100 LYS   A C   
770  O  O   . LYS   A 100 ? 0.23006 0.14604 0.26943 -0.00919 0.01399  -0.05818 100 LYS   A O   
771  C  CB  . LYS   A 100 ? 0.37107 0.24533 0.39323 -0.01809 0.02990  -0.09088 100 LYS   A CB  
772  C  CG  . LYS   A 100 ? 0.44831 0.32477 0.44908 -0.03152 0.02330  -0.10037 100 LYS   A CG  
773  C  CD  . LYS   A 100 ? 0.52326 0.40237 0.50145 -0.03404 0.02795  -0.11279 100 LYS   A CD  
774  C  CE  . LYS   A 100 ? 0.54377 0.43450 0.50262 -0.04647 0.01667  -0.11514 100 LYS   A CE  
775  N  NZ  . LYS   A 100 ? 0.46231 0.37247 0.42872 -0.04879 0.00518  -0.10202 100 LYS   A NZ  
776  N  N   . TYR   A 101 ? 0.24891 0.15919 0.28065 -0.02471 0.00456  -0.06085 101 TYR   A N   
777  C  CA  . TYR   A 101 ? 0.22870 0.15968 0.25867 -0.02401 -0.00271 -0.05077 101 TYR   A CA  
778  C  C   . TYR   A 101 ? 0.25028 0.19055 0.26957 -0.03390 -0.00975 -0.05311 101 TYR   A C   
779  O  O   . TYR   A 101 ? 0.24078 0.17233 0.25609 -0.04256 -0.01084 -0.06063 101 TYR   A O   
780  C  CB  . TYR   A 101 ? 0.20246 0.13653 0.24627 -0.01984 -0.00577 -0.03700 101 TYR   A CB  
781  C  CG  . TYR   A 101 ? 0.25776 0.18504 0.30698 -0.02640 -0.00885 -0.03330 101 TYR   A CG  
782  C  CD1 . TYR   A 101 ? 0.23759 0.14599 0.29717 -0.02620 -0.00471 -0.03385 101 TYR   A CD1 
783  C  CD2 . TYR   A 101 ? 0.25393 0.19369 0.29962 -0.03257 -0.01506 -0.02852 101 TYR   A CD2 
784  C  CE1 . TYR   A 101 ? 0.24997 0.15169 0.31539 -0.03285 -0.00712 -0.02936 101 TYR   A CE1 
785  C  CE2 . TYR   A 101 ? 0.21244 0.14727 0.26456 -0.03908 -0.01697 -0.02419 101 TYR   A CE2 
786  C  CZ  . TYR   A 101 ? 0.25877 0.17432 0.32022 -0.03964 -0.01319 -0.02456 101 TYR   A CZ  
787  O  OH  . TYR   A 101 ? 0.32491 0.23464 0.39357 -0.04672 -0.01463 -0.01942 101 TYR   A OH  
788  N  N   . LYS   A 102 ? 0.21921 0.17754 0.23553 -0.03259 -0.01468 -0.04608 102 LYS   A N   
789  C  CA  . LYS   A 102 ? 0.19747 0.16870 0.20977 -0.03968 -0.02177 -0.04370 102 LYS   A CA  
790  C  C   . LYS   A 102 ? 0.20441 0.18835 0.22322 -0.03490 -0.02439 -0.03190 102 LYS   A C   
791  O  O   . LYS   A 102 ? 0.14706 0.13251 0.16800 -0.02733 -0.02212 -0.02770 102 LYS   A O   
792  C  CB  . LYS   A 102 ? 0.22770 0.20880 0.22585 -0.04316 -0.02438 -0.04928 102 LYS   A CB  
793  C  CG  . LYS   A 102 ? 0.31721 0.28683 0.30362 -0.04528 -0.01963 -0.06163 102 LYS   A CG  
794  C  CD  . LYS   A 102 ? 0.35639 0.33735 0.32650 -0.05128 -0.02426 -0.06580 102 LYS   A CD  
795  C  CE  . LYS   A 102 ? 0.33862 0.33116 0.30430 -0.04393 -0.02268 -0.06032 102 LYS   A CE  
796  N  NZ  . LYS   A 102 ? 0.44182 0.44265 0.38902 -0.04937 -0.02566 -0.06472 102 LYS   A NZ  
797  N  N   . PHE   A 103 ? 0.18875 0.18189 0.21082 -0.03978 -0.02880 -0.02706 103 PHE   A N   
798  C  CA  . PHE   A 103 ? 0.11747 0.12366 0.14284 -0.03597 -0.03038 -0.01781 103 PHE   A CA  
799  C  C   . PHE   A 103 ? 0.16977 0.19044 0.18964 -0.03695 -0.03386 -0.01815 103 PHE   A C   
800  O  O   . PHE   A 103 ? 0.12480 0.15266 0.14506 -0.04390 -0.03802 -0.01943 103 PHE   A O   
801  C  CB  . PHE   A 103 ? 0.14587 0.15452 0.17971 -0.04001 -0.03132 -0.01141 103 PHE   A CB  
802  C  CG  . PHE   A 103 ? 0.16163 0.15805 0.20101 -0.03847 -0.02845 -0.00755 103 PHE   A CG  
803  C  CD1 . PHE   A 103 ? 0.12919 0.11571 0.16815 -0.03229 -0.02582 -0.00837 103 PHE   A CD1 
804  C  CD2 . PHE   A 103 ? 0.18308 0.17916 0.22958 -0.04314 -0.02834 -0.00156 103 PHE   A CD2 
805  C  CE1 . PHE   A 103 ? 0.15558 0.13228 0.20115 -0.03043 -0.02414 -0.00276 103 PHE   A CE1 
806  C  CE2 . PHE   A 103 ? 0.18593 0.17107 0.23719 -0.04169 -0.02608 0.00409  103 PHE   A CE2 
807  C  CZ  . PHE   A 103 ? 0.15185 0.12722 0.20276 -0.03518 -0.02447 0.00380  103 PHE   A CZ  
808  N  N   . VAL   A 104 ? 0.10657 0.13213 0.12276 -0.03048 -0.03274 -0.01594 104 VAL   A N   
809  C  CA  . VAL   A 104 ? 0.12424 0.16264 0.13626 -0.03044 -0.03579 -0.01443 104 VAL   A CA  
810  C  C   . VAL   A 104 ? 0.15925 0.20474 0.17610 -0.02443 -0.03469 -0.00680 104 VAL   A C   
811  O  O   . VAL   A 104 ? 0.22190 0.26122 0.24013 -0.02003 -0.03161 -0.00491 104 VAL   A O   
812  C  CB  . VAL   A 104 ? 0.15724 0.19367 0.15859 -0.02917 -0.03470 -0.01949 104 VAL   A CB  
813  C  CG1 . VAL   A 104 ? 0.18746 0.21212 0.18261 -0.03408 -0.03301 -0.02918 104 VAL   A CG1 
814  C  CG2 . VAL   A 104 ? 0.19537 0.22830 0.19713 -0.02166 -0.03045 -0.01722 104 VAL   A CG2 
815  N  N   . ARG   A 105 ? 0.11154 0.16983 0.13132 -0.02445 -0.03729 -0.00235 105 ARG   A N   
816  C  CA  . ARG   A 105 ? 0.09041 0.15337 0.11424 -0.01812 -0.03488 0.00360  105 ARG   A CA  
817  C  C   . ARG   A 105 ? 0.10521 0.17108 0.12409 -0.01459 -0.03551 0.00468  105 ARG   A C   
818  O  O   . ARG   A 105 ? 0.13248 0.20577 0.14831 -0.01753 -0.03947 0.00489  105 ARG   A O   
819  C  CB  . ARG   A 105 ? 0.12476 0.19992 0.15897 -0.01881 -0.03550 0.00932  105 ARG   A CB  
820  C  CG  . ARG   A 105 ? 0.10327 0.17948 0.14128 -0.01183 -0.03054 0.01378  105 ARG   A CG  
821  C  CD  . ARG   A 105 ? 0.08209 0.17157 0.13267 -0.01174 -0.02954 0.01952  105 ARG   A CD  
822  N  NE  . ARG   A 105 ? 0.09746 0.18753 0.15172 -0.00427 -0.02355 0.02292  105 ARG   A NE  
823  C  CZ  . ARG   A 105 ? 0.09096 0.17582 0.14417 -0.00211 -0.01702 0.02261  105 ARG   A CZ  
824  N  NH1 . ARG   A 105 ? 0.10639 0.18603 0.15560 -0.00654 -0.01631 0.02086  105 ARG   A NH1 
825  N  NH2 . ARG   A 105 ? 0.06914 0.15351 0.12493 0.00449  -0.01068 0.02432  105 ARG   A NH2 
826  N  N   . ILE   A 106 ? 0.13935 0.19952 0.15684 -0.00921 -0.03207 0.00579  106 ILE   A N   
827  C  CA  . ILE   A 106 ? 0.16048 0.22198 0.17431 -0.00627 -0.03193 0.00767  106 ILE   A CA  
828  C  C   . ILE   A 106 ? 0.11635 0.18441 0.13696 -0.00191 -0.03132 0.01437  106 ILE   A C   
829  O  O   . ILE   A 106 ? 0.14624 0.21608 0.17366 -0.00021 -0.02936 0.01630  106 ILE   A O   
830  C  CB  . ILE   A 106 ? 0.12609 0.17780 0.13636 -0.00387 -0.02875 0.00522  106 ILE   A CB  
831  C  CG1 . ILE   A 106 ? 0.10551 0.15153 0.11908 -0.00133 -0.02649 0.00603  106 ILE   A CG1 
832  C  CG2 . ILE   A 106 ? 0.15598 0.20223 0.16174 -0.00673 -0.02821 -0.00067 106 ILE   A CG2 
833  C  CD1 . ILE   A 106 ? 0.18097 0.22032 0.19304 0.00057  -0.02487 0.00545  106 ILE   A CD1 
834  N  N   . GLN   A 107 ? 0.10887 0.18009 0.12804 0.00023  -0.03209 0.01834  107 GLN   A N   
835  C  CA  . GLN   A 107 ? 0.13928 0.21423 0.16514 0.00543  -0.03099 0.02567  107 GLN   A CA  
836  C  C   . GLN   A 107 ? 0.14227 0.20516 0.16745 0.00923  -0.02610 0.02473  107 GLN   A C   
837  O  O   . GLN   A 107 ? 0.15384 0.20970 0.17268 0.00746  -0.02533 0.02083  107 GLN   A O   
838  C  CB  . GLN   A 107 ? 0.16537 0.24918 0.18817 0.00454  -0.03517 0.03138  107 GLN   A CB  
839  C  CG  . GLN   A 107 ? 0.15871 0.25421 0.18246 0.00001  -0.04068 0.03247  107 GLN   A CG  
840  C  CD  . GLN   A 107 ? 0.15969 0.26195 0.19806 0.00354  -0.03982 0.03804  107 GLN   A CD  
841  O  OE1 . GLN   A 107 ? 0.12380 0.22600 0.17062 0.01011  -0.03679 0.04452  107 GLN   A OE1 
842  N  NE2 . GLN   A 107 ? 0.14438 0.25212 0.18718 -0.00057 -0.04166 0.03578  107 GLN   A NE2 
843  N  N   . PRO   A 108 ? 0.16617 0.22649 0.19874 0.01419  -0.02249 0.02797  108 PRO   A N   
844  C  CA  . PRO   A 108 ? 0.18222 0.23053 0.21392 0.01680  -0.01860 0.02747  108 PRO   A CA  
845  C  C   . PRO   A 108 ? 0.19195 0.24111 0.22069 0.01594  -0.02042 0.03154  108 PRO   A C   
846  O  O   . PRO   A 108 ? 0.20517 0.26462 0.23439 0.01584  -0.02375 0.03753  108 PRO   A O   
847  C  CB  . PRO   A 108 ? 0.15569 0.20256 0.19720 0.02292  -0.01410 0.03153  108 PRO   A CB  
848  C  CG  . PRO   A 108 ? 0.18123 0.24266 0.23087 0.02398  -0.01612 0.03602  108 PRO   A CG  
849  C  CD  . PRO   A 108 ? 0.11084 0.17867 0.15393 0.01750  -0.02098 0.03185  108 PRO   A CD  
850  N  N   . GLY   A 109 ? 0.13729 0.17678 0.16258 0.01454  -0.01852 0.02871  109 GLY   A N   
851  C  CA  . GLY   A 109 ? 0.19537 0.23560 0.21780 0.01302  -0.01882 0.03231  109 GLY   A CA  
852  C  C   . GLY   A 109 ? 0.20906 0.25273 0.22427 0.00883  -0.02003 0.02774  109 GLY   A C   
853  O  O   . GLY   A 109 ? 0.22909 0.27145 0.24243 0.00733  -0.01824 0.02889  109 GLY   A O   
854  N  N   . GLN   A 110 ? 0.15895 0.20632 0.17126 0.00700  -0.02209 0.02272  110 GLN   A N   
855  C  CA  . GLN   A 110 ? 0.15589 0.20360 0.16283 0.00385  -0.02186 0.01740  110 GLN   A CA  
856  C  C   . GLN   A 110 ? 0.13897 0.17935 0.14921 0.00342  -0.02056 0.01291  110 GLN   A C   
857  O  O   . GLN   A 110 ? 0.14768 0.18314 0.16098 0.00423  -0.02095 0.01218  110 GLN   A O   
858  C  CB  . GLN   A 110 ? 0.18668 0.23981 0.18903 0.00116  -0.02460 0.01381  110 GLN   A CB  
859  C  CG  . GLN   A 110 ? 0.24418 0.30716 0.24340 0.00014  -0.02820 0.01840  110 GLN   A CG  
860  C  CD  . GLN   A 110 ? 0.31413 0.38170 0.30808 -0.00473 -0.03170 0.01341  110 GLN   A CD  
861  O  OE1 . GLN   A 110 ? 0.16807 0.23660 0.16737 -0.00582 -0.03359 0.01178  110 GLN   A OE1 
862  N  NE2 . GLN   A 110 ? 0.41258 0.48213 0.39504 -0.00838 -0.03190 0.01046  110 GLN   A NE2 
863  N  N   . THR   A 111 ? 0.11722 0.15742 0.12673 0.00216  -0.01870 0.01040  111 THR   A N   
864  C  CA  . THR   A 111 ? 0.14092 0.17686 0.15612 0.00183  -0.01832 0.00821  111 THR   A CA  
865  C  C   . THR   A 111 ? 0.17629 0.21146 0.19172 0.00138  -0.01864 0.00378  111 THR   A C   
866  O  O   . THR   A 111 ? 0.15228 0.18900 0.16269 0.00056  -0.01817 0.00100  111 THR   A O   
867  C  CB  . THR   A 111 ? 0.16204 0.19930 0.18145 0.00150  -0.01512 0.01031  111 THR   A CB  
868  O  OG1 . THR   A 111 ? 0.16880 0.21040 0.18292 0.00153  -0.01148 0.00920  111 THR   A OG1 
869  C  CG2 . THR   A 111 ? 0.16129 0.19682 0.18189 0.00138  -0.01488 0.01531  111 THR   A CG2 
870  N  N   . PHE   A 112 ? 0.13524 0.16757 0.15680 0.00142  -0.01990 0.00352  112 PHE   A N   
871  C  CA  . PHE   A 112 ? 0.14942 0.17976 0.17409 0.00172  -0.02007 0.00116  112 PHE   A CA  
872  C  C   . PHE   A 112 ? 0.13687 0.16709 0.17067 0.00209  -0.02186 0.00368  112 PHE   A C   
873  O  O   . PHE   A 112 ? 0.15084 0.18166 0.18616 0.00069  -0.02438 0.00612  112 PHE   A O   
874  C  CB  . PHE   A 112 ? 0.12867 0.15659 0.14947 0.00061  -0.02262 0.00015  112 PHE   A CB  
875  C  CG  . PHE   A 112 ? 0.17523 0.20207 0.19385 -0.00001 -0.02537 0.00247  112 PHE   A CG  
876  C  CD1 . PHE   A 112 ? 0.16082 0.18911 0.17571 0.00037  -0.02482 0.00333  112 PHE   A CD1 
877  C  CD2 . PHE   A 112 ? 0.10553 0.12968 0.12524 -0.00082 -0.02802 0.00396  112 PHE   A CD2 
878  C  CE1 . PHE   A 112 ? 0.19237 0.21798 0.20469 0.00037  -0.02533 0.00405  112 PHE   A CE1 
879  C  CE2 . PHE   A 112 ? 0.16367 0.18590 0.17777 -0.00191 -0.02938 0.00475  112 PHE   A CE2 
880  C  CZ  . PHE   A 112 ? 0.16416 0.18645 0.17456 -0.00110 -0.02723 0.00397  112 PHE   A CZ  
881  N  N   . SER   A 113 ? 0.12906 0.15829 0.16963 0.00369  -0.02080 0.00321  113 SER   A N   
882  C  CA  . SER   A 113 ? 0.11396 0.14502 0.16557 0.00439  -0.02369 0.00732  113 SER   A CA  
883  C  C   . SER   A 113 ? 0.11207 0.13973 0.16058 0.00307  -0.02893 0.00950  113 SER   A C   
884  O  O   . SER   A 113 ? 0.13281 0.15600 0.17701 0.00313  -0.02794 0.00768  113 SER   A O   
885  C  CB  . SER   A 113 ? 0.13973 0.17178 0.20334 0.00816  -0.01872 0.00710  113 SER   A CB  
886  O  OG  . SER   A 113 ? 0.13509 0.17007 0.19801 0.00906  -0.01223 0.00442  113 SER   A OG  
887  N  N   . VAL   A 114 ? 0.11478 0.14486 0.16495 0.00100  -0.03457 0.01359  114 VAL   A N   
888  C  CA  . VAL   A 114 ? 0.13645 0.16462 0.18227 -0.00085 -0.03990 0.01704  114 VAL   A CA  
889  C  C   . VAL   A 114 ? 0.14533 0.17765 0.20491 0.00066  -0.04368 0.02359  114 VAL   A C   
890  O  O   . VAL   A 114 ? 0.14064 0.17971 0.20963 -0.00004 -0.04657 0.02654  114 VAL   A O   
891  C  CB  . VAL   A 114 ? 0.10987 0.13737 0.14427 -0.00518 -0.04400 0.01648  114 VAL   A CB  
892  C  CG1 . VAL   A 114 ? 0.14169 0.16845 0.16977 -0.00775 -0.04970 0.02086  114 VAL   A CG1 
893  C  CG2 . VAL   A 114 ? 0.16395 0.18745 0.18774 -0.00528 -0.03959 0.01132  114 VAL   A CG2 
894  N  N   . LEU   A 115 ? 0.12445 0.15332 0.18669 0.00240  -0.04411 0.02697  115 LEU   A N   
895  C  CA  . LEU   A 115 ? 0.10852 0.14129 0.18387 0.00409  -0.04905 0.03574  115 LEU   A CA  
896  C  C   . LEU   A 115 ? 0.14171 0.17540 0.20560 -0.00057 -0.05716 0.04130  115 LEU   A C   
897  O  O   . LEU   A 115 ? 0.15156 0.17972 0.20770 -0.00123 -0.05688 0.04323  115 LEU   A O   
898  C  CB  . LEU   A 115 ? 0.10163 0.12830 0.18819 0.00922  -0.04395 0.03701  115 LEU   A CB  
899  C  CG  . LEU   A 115 ? 0.09519 0.12575 0.19811 0.01218  -0.04899 0.04821  115 LEU   A CG  
900  C  CD1 . LEU   A 115 ? 0.11942 0.16024 0.23612 0.01354  -0.04925 0.05057  115 LEU   A CD1 
901  C  CD2 . LEU   A 115 ? 0.11301 0.13402 0.22699 0.01746  -0.04282 0.04892  115 LEU   A CD2 
902  N  N   . ALA   A 116 ? 0.12730 0.16588 0.18654 -0.00467 -0.06136 0.04191  116 ALA   A N   
903  C  CA  . ALA   A 116 ? 0.13403 0.17183 0.17761 -0.00985 -0.06642 0.04431  116 ALA   A CA  
904  C  C   . ALA   A 116 ? 0.17954 0.21945 0.23089 -0.00843 -0.06956 0.05383  116 ALA   A C   
905  O  O   . ALA   A 116 ? 0.19016 0.23544 0.25867 -0.00563 -0.07025 0.05844  116 ALA   A O   
906  C  CB  . ALA   A 116 ? 0.16168 0.20289 0.19889 -0.01513 -0.07023 0.04148  116 ALA   A CB  
907  N  N   . CYS   A 117 ? 0.12640 0.16244 0.16606 -0.01022 -0.07091 0.05746  117 CYS   A N   
908  C  CA  . CYS   A 117 ? 0.18132 0.21883 0.22657 -0.00951 -0.07414 0.06765  117 CYS   A CA  
909  C  C   . CYS   A 117 ? 0.19240 0.23030 0.21764 -0.01539 -0.07853 0.07059  117 CYS   A C   
910  O  O   . CYS   A 117 ? 0.21827 0.25289 0.22446 -0.01918 -0.07724 0.06460  117 CYS   A O   
911  C  CB  . CYS   A 117 ? 0.20277 0.23396 0.25907 -0.00455 -0.07013 0.07224  117 CYS   A CB  
912  S  SG  . CYS   A 117 ? 0.25685 0.28321 0.32885 0.00166  -0.06317 0.06585  117 CYS   A SG  
913  N  N   . TYR   A 118 ? 0.21657 0.25894 0.24718 -0.01581 -0.08339 0.08017  118 TYR   A N   
914  C  CA  . TYR   A 118 ? 0.24187 0.28601 0.25544 -0.02111 -0.08830 0.08536  118 TYR   A CA  
915  C  C   . TYR   A 118 ? 0.27503 0.31945 0.30029 -0.01806 -0.08940 0.09755  118 TYR   A C   
916  O  O   . TYR   A 118 ? 0.24850 0.29616 0.29594 -0.01339 -0.09005 0.10289  118 TYR   A O   
917  C  CB  . TYR   A 118 ? 0.23330 0.28486 0.24090 -0.02640 -0.09552 0.08459  118 TYR   A CB  
918  C  CG  . TYR   A 118 ? 0.25921 0.30826 0.25745 -0.02904 -0.09341 0.07238  118 TYR   A CG  
919  C  CD1 . TYR   A 118 ? 0.23622 0.28749 0.25049 -0.02634 -0.09171 0.06816  118 TYR   A CD1 
920  C  CD2 . TYR   A 118 ? 0.27008 0.31369 0.24393 -0.03370 -0.09175 0.06512  118 TYR   A CD2 
921  C  CE1 . TYR   A 118 ? 0.23887 0.28701 0.24561 -0.02860 -0.08936 0.05785  118 TYR   A CE1 
922  C  CE2 . TYR   A 118 ? 0.27625 0.31603 0.24288 -0.03555 -0.08906 0.05419  118 TYR   A CE2 
923  C  CZ  . TYR   A 118 ? 0.29660 0.33856 0.27989 -0.03316 -0.08828 0.05092  118 TYR   A CZ  
924  O  OH  . TYR   A 118 ? 0.29051 0.32804 0.26712 -0.03522 -0.08563 0.04091  118 TYR   A OH  
925  N  N   . ASN   A 119 ? 0.28103 0.32149 0.29241 -0.02030 -0.08844 0.10193  119 ASN   A N   
926  C  CA  . ASN   A 119 ? 0.26816 0.30779 0.28887 -0.01811 -0.08934 0.11436  119 ASN   A CA  
927  C  C   . ASN   A 119 ? 0.25860 0.29250 0.30438 -0.01078 -0.08419 0.11629  119 ASN   A C   
928  O  O   . ASN   A 119 ? 0.25977 0.29469 0.32272 -0.00710 -0.08558 0.12581  119 ASN   A O   
929  C  CB  . ASN   A 119 ? 0.30452 0.35369 0.32809 -0.02017 -0.09796 0.12378  119 ASN   A CB  
930  C  CG  . ASN   A 119 ? 0.33926 0.39294 0.33722 -0.02791 -0.10327 0.12080  119 ASN   A CG  
931  O  OD1 . ASN   A 119 ? 0.41120 0.46162 0.38824 -0.03165 -0.10178 0.12136  119 ASN   A OD1 
932  N  ND2 . ASN   A 119 ? 0.35051 0.41117 0.34961 -0.03059 -0.10881 0.11710  119 ASN   A ND2 
933  N  N   . GLY   A 120 ? 0.20134 0.22892 0.24958 -0.00853 -0.07810 0.10700  120 GLY   A N   
934  C  CA  . GLY   A 120 ? 0.22197 0.24246 0.29181 -0.00194 -0.07252 0.10639  120 GLY   A CA  
935  C  C   . GLY   A 120 ? 0.26019 0.28570 0.34991 0.00305  -0.07245 0.10486  120 GLY   A C   
936  O  O   . GLY   A 120 ? 0.27301 0.29212 0.38106 0.00916  -0.06667 0.10384  120 GLY   A O   
937  N  N   . SER   A 121 ? 0.24318 0.27927 0.33002 0.00040  -0.07789 0.10435  121 SER   A N   
938  C  CA  . SER   A 121 ? 0.21923 0.26175 0.32623 0.00460  -0.07754 0.10451  121 SER   A CA  
939  C  C   . SER   A 121 ? 0.26350 0.30887 0.36633 0.00331  -0.07595 0.09368  121 SER   A C   
940  O  O   . SER   A 121 ? 0.24589 0.29491 0.33120 -0.00290 -0.08031 0.08971  121 SER   A O   
941  C  CB  . SER   A 121 ? 0.28432 0.33774 0.39615 0.00241  -0.08550 0.11462  121 SER   A CB  
942  O  OG  . SER   A 121 ? 0.35722 0.40809 0.48046 0.00589  -0.08542 0.12538  121 SER   A OG  
943  N  N   . PRO   A 122 ? 0.21257 0.25541 0.33037 0.00897  -0.06908 0.08837  122 PRO   A N   
944  C  CA  . PRO   A 122 ? 0.24097 0.28691 0.35583 0.00792  -0.06703 0.07892  122 PRO   A CA  
945  C  C   . PRO   A 122 ? 0.23311 0.29026 0.34945 0.00399  -0.07277 0.08083  122 PRO   A C   
946  O  O   . PRO   A 122 ? 0.24850 0.31287 0.38113 0.00597  -0.07488 0.08845  122 PRO   A O   
947  C  CB  . PRO   A 122 ? 0.21534 0.25743 0.34904 0.01557  -0.05808 0.07528  122 PRO   A CB  
948  C  CG  . PRO   A 122 ? 0.25462 0.28582 0.39367 0.01953  -0.05446 0.07877  122 PRO   A CG  
949  C  CD  . PRO   A 122 ? 0.23539 0.26795 0.36634 0.01552  -0.06159 0.08839  122 PRO   A CD  
950  N  N   . SER   A 123 ? 0.24262 0.30077 0.34297 -0.00167 -0.07508 0.07390  123 SER   A N   
951  C  CA  . SER   A 123 ? 0.23714 0.30379 0.33631 -0.00694 -0.08084 0.07418  123 SER   A CA  
952  C  C   . SER   A 123 ? 0.23354 0.30345 0.34150 -0.00616 -0.07679 0.06816  123 SER   A C   
953  O  O   . SER   A 123 ? 0.21923 0.29814 0.34024 -0.00718 -0.07923 0.07174  123 SER   A O   
954  C  CB  . SER   A 123 ? 0.29119 0.35512 0.36516 -0.01468 -0.08615 0.07042  123 SER   A CB  
955  O  OG  . SER   A 123 ? 0.39212 0.46238 0.46436 -0.02044 -0.09165 0.06923  123 SER   A OG  
956  N  N   . GLY   A 124 ? 0.17257 0.23618 0.27378 -0.00491 -0.07101 0.05984  124 GLY   A N   
957  C  CA  . GLY   A 124 ? 0.15379 0.22044 0.26183 -0.00465 -0.06692 0.05466  124 GLY   A CA  
958  C  C   . GLY   A 124 ? 0.14935 0.20921 0.25253 -0.00153 -0.06009 0.04748  124 GLY   A C   
959  O  O   . GLY   A 124 ? 0.13880 0.19126 0.23061 -0.00098 -0.05962 0.04556  124 GLY   A O   
960  N  N   . VAL   A 125 ? 0.09879 0.16218 0.21166 0.00035  -0.05474 0.04425  125 VAL   A N   
961  C  CA  . VAL   A 125 ? 0.11993 0.17887 0.22932 0.00299  -0.04859 0.03782  125 VAL   A CA  
962  C  C   . VAL   A 125 ? 0.13637 0.19804 0.24270 -0.00105 -0.04783 0.03404  125 VAL   A C   
963  O  O   . VAL   A 125 ? 0.12911 0.19765 0.24490 -0.00335 -0.04861 0.03668  125 VAL   A O   
964  C  CB  . VAL   A 125 ? 0.12287 0.18222 0.24876 0.01096  -0.04011 0.03766  125 VAL   A CB  
965  C  CG1 . VAL   A 125 ? 0.13549 0.20376 0.27865 0.01313  -0.03536 0.03997  125 VAL   A CG1 
966  C  CG2 . VAL   A 125 ? 0.11740 0.16712 0.22814 0.01174  -0.03175 0.02819  125 VAL   A CG2 
967  N  N   . TYR   A 126 ? 0.13965 0.19354 0.22974 -0.00245 -0.04526 0.02771  126 TYR   A N   
968  C  CA  . TYR   A 126 ? 0.11817 0.17138 0.20336 -0.00595 -0.04338 0.02444  126 TYR   A CA  
969  C  C   . TYR   A 126 ? 0.14317 0.18821 0.21408 -0.00398 -0.03690 0.01849  126 TYR   A C   
970  O  O   . TYR   A 126 ? 0.15093 0.19086 0.21373 -0.00180 -0.03570 0.01627  126 TYR   A O   
971  C  CB  . TYR   A 126 ? 0.13603 0.18799 0.21377 -0.01329 -0.05183 0.02462  126 TYR   A CB  
972  C  CG  . TYR   A 126 ? 0.14810 0.19175 0.20726 -0.01506 -0.05524 0.02178  126 TYR   A CG  
973  C  CD1 . TYR   A 126 ? 0.19284 0.22730 0.23709 -0.01505 -0.05095 0.01595  126 TYR   A CD1 
974  C  CD2 . TYR   A 126 ? 0.18612 0.23051 0.24173 -0.01593 -0.06025 0.02525  126 TYR   A CD2 
975  C  CE1 . TYR   A 126 ? 0.20598 0.23404 0.23481 -0.01613 -0.05227 0.01357  126 TYR   A CE1 
976  C  CE2 . TYR   A 126 ? 0.16818 0.20584 0.20626 -0.01769 -0.06203 0.02319  126 TYR   A CE2 
977  C  CZ  . TYR   A 126 ? 0.19041 0.22055 0.21587 -0.01804 -0.05838 0.01723  126 TYR   A CZ  
978  O  OH  . TYR   A 126 ? 0.23241 0.25664 0.24133 -0.01942 -0.05836 0.01521  126 TYR   A OH  
979  N  N   . GLN   A 127 ? 0.10005 0.14485 0.16941 -0.00520 -0.03316 0.01705  127 GLN   A N   
980  C  CA  . GLN   A 127 ? 0.17457 0.21443 0.23277 -0.00343 -0.02776 0.01346  127 GLN   A CA  
981  C  C   . GLN   A 127 ? 0.15910 0.19192 0.20570 -0.00622 -0.03059 0.01158  127 GLN   A C   
982  O  O   . GLN   A 127 ? 0.22073 0.25167 0.26825 -0.01038 -0.03421 0.01214  127 GLN   A O   
983  C  CB  . GLN   A 127 ? 0.18944 0.23380 0.25335 -0.00265 -0.02142 0.01483  127 GLN   A CB  
984  C  CG  . GLN   A 127 ? 0.20279 0.24480 0.25607 -0.00075 -0.01645 0.01264  127 GLN   A CG  
985  C  CD  . GLN   A 127 ? 0.16710 0.20929 0.21748 0.00253  -0.01264 0.00912  127 GLN   A CD  
986  O  OE1 . GLN   A 127 ? 0.18608 0.22765 0.24217 0.00411  -0.01388 0.00824  127 GLN   A OE1 
987  N  NE2 . GLN   A 127 ? 0.17517 0.21751 0.21616 0.00313  -0.00827 0.00729  127 GLN   A NE2 
988  N  N   . CYS   A 128 ? 0.15973 0.18852 0.19627 -0.00419 -0.02888 0.00906  128 CYS   A N   
989  C  CA  . CYS   A 128 ? 0.24129 0.26372 0.26839 -0.00503 -0.02943 0.00724  128 CYS   A CA  
990  C  C   . CYS   A 128 ? 0.18599 0.20867 0.20980 -0.00222 -0.02514 0.00751  128 CYS   A C   
991  O  O   . CYS   A 128 ? 0.17406 0.20124 0.19820 -0.00044 -0.02304 0.00763  128 CYS   A O   
992  C  CB  . CYS   A 128 ? 0.17598 0.19588 0.19590 -0.00513 -0.03173 0.00562  128 CYS   A CB  
993  S  SG  . CYS   A 128 ? 0.33949 0.35616 0.35530 -0.00986 -0.03756 0.00525  128 CYS   A SG  
994  N  N   . ALA   A 129 ? 0.18159 0.19914 0.20216 -0.00196 -0.02396 0.00769  129 ALA   A N   
995  C  CA  . ALA   A 129 ? 0.15587 0.17494 0.17422 0.00126  -0.02126 0.00947  129 ALA   A CA  
996  C  C   . ALA   A 129 ? 0.20725 0.22314 0.22148 0.00275  -0.02086 0.00754  129 ALA   A C   
997  O  O   . ALA   A 129 ? 0.17729 0.18623 0.18810 0.00129  -0.02107 0.00464  129 ALA   A O   
998  C  CB  . ALA   A 129 ? 0.21632 0.23277 0.23749 0.00202  -0.01884 0.01344  129 ALA   A CB  
999  N  N   . MET   A 130 ? 0.15833 0.18003 0.17261 0.00512  -0.02006 0.00913  130 MET   A N   
1000 C  CA  . MET   A 130 ? 0.14023 0.16160 0.15415 0.00745  -0.01809 0.00901  130 MET   A CA  
1001 C  C   . MET   A 130 ? 0.14624 0.16281 0.16368 0.01078  -0.01475 0.01164  130 MET   A C   
1002 O  O   . MET   A 130 ? 0.15575 0.17675 0.17746 0.01272  -0.01482 0.01689  130 MET   A O   
1003 C  CB  . MET   A 130 ? 0.16341 0.19471 0.17929 0.00788  -0.01930 0.01088  130 MET   A CB  
1004 C  CG  . MET   A 130 ? 0.18048 0.21574 0.19929 0.00971  -0.01724 0.01179  130 MET   A CG  
1005 S  SD  . MET   A 130 ? 0.21947 0.24719 0.23255 0.00886  -0.01422 0.00762  130 MET   A SD  
1006 C  CE  . MET   A 130 ? 0.12244 0.15298 0.13289 0.00422  -0.01848 0.00645  130 MET   A CE  
1007 N  N   . ARG   A 131 ? 0.15789 0.16433 0.17274 0.01116  -0.01170 0.00810  131 ARG   A N   
1008 C  CA  . ARG   A 131 ? 0.17505 0.17348 0.19431 0.01467  -0.00738 0.00987  131 ARG   A CA  
1009 C  C   . ARG   A 131 ? 0.17546 0.18143 0.20291 0.02071  -0.00446 0.01527  131 ARG   A C   
1010 O  O   . ARG   A 131 ? 0.19351 0.20912 0.22166 0.02110  -0.00518 0.01559  131 ARG   A O   
1011 C  CB  . ARG   A 131 ? 0.19274 0.17676 0.20545 0.01326  -0.00385 0.00285  131 ARG   A CB  
1012 C  CG  . ARG   A 131 ? 0.20947 0.18744 0.21490 0.00620  -0.00827 -0.00194 131 ARG   A CG  
1013 C  CD  . ARG   A 131 ? 0.19258 0.17114 0.20440 0.00385  -0.01109 0.00204  131 ARG   A CD  
1014 N  NE  . ARG   A 131 ? 0.20956 0.18107 0.22823 0.00750  -0.00665 0.00583  131 ARG   A NE  
1015 C  CZ  . ARG   A 131 ? 0.22932 0.20114 0.25459 0.00657  -0.00729 0.01152  131 ARG   A CZ  
1016 N  NH1 . ARG   A 131 ? 0.21859 0.19752 0.24473 0.00209  -0.01128 0.01302  131 ARG   A NH1 
1017 N  NH2 . ARG   A 131 ? 0.23888 0.20370 0.27103 0.01054  -0.00307 0.01655  131 ARG   A NH2 
1018 N  N   . PRO   A 132 ? 0.17185 0.17465 0.20752 0.02526  -0.00159 0.02083  132 PRO   A N   
1019 C  CA  . PRO   A 132 ? 0.17711 0.18788 0.22377 0.03190  0.00131  0.02712  132 PRO   A CA  
1020 C  C   . PRO   A 132 ? 0.19882 0.20762 0.24591 0.03465  0.00734  0.02224  132 PRO   A C   
1021 O  O   . PRO   A 132 ? 0.16507 0.18660 0.22143 0.03823  0.00819  0.02702  132 PRO   A O   
1022 C  CB  . PRO   A 132 ? 0.20746 0.20970 0.26284 0.03662  0.00463  0.03332  132 PRO   A CB  
1023 C  CG  . PRO   A 132 ? 0.22085 0.21968 0.27043 0.03122  0.00043  0.03410  132 PRO   A CG  
1024 C  CD  . PRO   A 132 ? 0.20030 0.19393 0.23817 0.02466  -0.00121 0.02370  132 PRO   A CD  
1025 N  N   . ASN   A 133 ? 0.17563 0.17021 0.21248 0.03238  0.01143  0.01306  133 ASN   A N   
1026 C  CA  . ASN   A 133 ? 0.15877 0.15184 0.19335 0.03473  0.01848  0.00832  133 ASN   A CA  
1027 C  C   . ASN   A 133 ? 0.16600 0.16718 0.19139 0.02932  0.01487  0.00536  133 ASN   A C   
1028 O  O   . ASN   A 133 ? 0.18351 0.18125 0.20177 0.02915  0.02053  0.00037  133 ASN   A O   
1029 C  CB  . ASN   A 133 ? 0.20187 0.17446 0.22764 0.03499  0.02595  -0.00058 133 ASN   A CB  
1030 C  CG  . ASN   A 133 ? 0.21067 0.17349 0.22021 0.02612  0.02036  -0.00793 133 ASN   A CG  
1031 O  OD1 . ASN   A 133 ? 0.19256 0.16428 0.19901 0.02099  0.01202  -0.00598 133 ASN   A OD1 
1032 N  ND2 . ASN   A 133 ? 0.26051 0.20484 0.26060 0.02418  0.02497  -0.01641 133 ASN   A ND2 
1033 N  N   . PHE   A 134 ? 0.16258 0.17315 0.18734 0.02490  0.00641  0.00828  134 PHE   A N   
1034 C  CA  . PHE   A 134 ? 0.16937 0.18757 0.18880 0.02025  0.00267  0.00719  134 PHE   A CA  
1035 C  C   . PHE   A 134 ? 0.17268 0.18130 0.17754 0.01536  0.00211  0.00073  134 PHE   A C   
1036 O  O   . PHE   A 134 ? 0.20302 0.21541 0.20282 0.01262  0.00172  0.00019  134 PHE   A O   
1037 C  CB  . PHE   A 134 ? 0.14182 0.17097 0.16909 0.02283  0.00676  0.01032  134 PHE   A CB  
1038 C  CG  . PHE   A 134 ? 0.12395 0.16751 0.16548 0.02504  0.00359  0.01783  134 PHE   A CG  
1039 C  CD1 . PHE   A 134 ? 0.12202 0.17445 0.16347 0.02014  -0.00409 0.01967  134 PHE   A CD1 
1040 C  CD2 . PHE   A 134 ? 0.18731 0.23549 0.24248 0.03192  0.00812  0.02320  134 PHE   A CD2 
1041 C  CE1 . PHE   A 134 ? 0.14023 0.20678 0.19245 0.02060  -0.00831 0.02617  134 PHE   A CE1 
1042 C  CE2 . PHE   A 134 ? 0.20009 0.26412 0.26868 0.03326  0.00343  0.03161  134 PHE   A CE2 
1043 C  CZ  . PHE   A 134 ? 0.16211 0.23545 0.22765 0.02682  -0.00544 0.03272  134 PHE   A CZ  
1044 N  N   . THR   A 135 ? 0.19432 0.19098 0.19255 0.01355  0.00158  -0.00343 135 THR   A N   
1045 C  CA  . THR   A 135 ? 0.18805 0.17839 0.17345 0.00747  -0.00230 -0.00808 135 THR   A CA  
1046 C  C   . THR   A 135 ? 0.16921 0.16209 0.15829 0.00422  -0.00980 -0.00588 135 THR   A C   
1047 O  O   . THR   A 135 ? 0.16760 0.16419 0.16588 0.00645  -0.01056 -0.00212 135 THR   A O   
1048 C  CB  . THR   A 135 ? 0.18893 0.16415 0.16362 0.00610  0.00201  -0.01528 135 THR   A CB  
1049 O  OG1 . THR   A 135 ? 0.20277 0.17043 0.18434 0.00749  0.00256  -0.01529 135 THR   A OG1 
1050 C  CG2 . THR   A 135 ? 0.18788 0.15981 0.15930 0.01050  0.01212  -0.01817 135 THR   A CG2 
1051 N  N   . ILE   A 136 ? 0.17380 0.16547 0.15589 -0.00096 -0.01505 -0.00754 136 ILE   A N   
1052 C  CA  . ILE   A 136 ? 0.20007 0.19420 0.18738 -0.00382 -0.02101 -0.00562 136 ILE   A CA  
1053 C  C   . ILE   A 136 ? 0.20921 0.19552 0.18883 -0.00955 -0.02460 -0.00952 136 ILE   A C   
1054 O  O   . ILE   A 136 ? 0.21116 0.19283 0.17836 -0.01240 -0.02472 -0.01312 136 ILE   A O   
1055 C  CB  . ILE   A 136 ? 0.21417 0.21764 0.20561 -0.00435 -0.02508 -0.00199 136 ILE   A CB  
1056 C  CG1 . ILE   A 136 ? 0.21520 0.21829 0.19840 -0.00786 -0.02854 -0.00214 136 ILE   A CG1 
1057 C  CG2 . ILE   A 136 ? 0.16922 0.17953 0.16620 -0.00050 -0.02212 0.00049  136 ILE   A CG2 
1058 C  CD1 . ILE   A 136 ? 0.17069 0.18021 0.16042 -0.00848 -0.03310 0.00202  136 ILE   A CD1 
1059 N  N   . LYS   A 137 ? 0.19447 0.17926 0.18065 -0.01190 -0.02721 -0.00886 137 LYS   A N   
1060 C  CA  . LYS   A 137 ? 0.18861 0.16751 0.16972 -0.01903 -0.03226 -0.01220 137 LYS   A CA  
1061 C  C   . LYS   A 137 ? 0.21167 0.20150 0.19828 -0.02203 -0.03993 -0.00768 137 LYS   A C   
1062 O  O   . LYS   A 137 ? 0.21603 0.21212 0.21532 -0.02257 -0.04214 -0.00385 137 LYS   A O   
1063 C  CB  . LYS   A 137 ? 0.22772 0.19924 0.21550 -0.02057 -0.03062 -0.01302 137 LYS   A CB  
1064 C  CG  . LYS   A 137 ? 0.25284 0.21273 0.23824 -0.01613 -0.02239 -0.01608 137 LYS   A CG  
1065 C  CD  . LYS   A 137 ? 0.32725 0.27755 0.31983 -0.01834 -0.02093 -0.01600 137 LYS   A CD  
1066 C  CE  . LYS   A 137 ? 0.36081 0.29656 0.35199 -0.01350 -0.01225 -0.01909 137 LYS   A CE  
1067 N  NZ  . LYS   A 137 ? 0.39661 0.31422 0.37529 -0.01882 -0.01045 -0.02938 137 LYS   A NZ  
1068 N  N   . GLY   A 138 ? 0.21780 0.21052 0.19596 -0.02336 -0.04316 -0.00713 138 GLY   A N   
1069 C  CA  . GLY   A 138 ? 0.21848 0.22144 0.20371 -0.02448 -0.04975 -0.00125 138 GLY   A CA  
1070 C  C   . GLY   A 138 ? 0.22942 0.23345 0.20944 -0.03227 -0.05884 -0.00093 138 GLY   A C   
1071 O  O   . GLY   A 138 ? 0.23864 0.23498 0.21014 -0.03812 -0.06058 -0.00634 138 GLY   A O   
1072 N  N   . SER   A 139 ? 0.20640 0.21991 0.19205 -0.03267 -0.06514 0.00581  139 SER   A N   
1073 C  CA  . SER   A 139 ? 0.19429 0.21088 0.17543 -0.03801 -0.07149 0.00768  139 SER   A CA  
1074 C  C   . SER   A 139 ? 0.21538 0.23576 0.19205 -0.03552 -0.07232 0.01333  139 SER   A C   
1075 O  O   . SER   A 139 ? 0.19503 0.22203 0.18614 -0.03063 -0.07196 0.01995  139 SER   A O   
1076 C  CB  . SER   A 139 ? 0.21288 0.23841 0.21273 -0.03909 -0.07514 0.01227  139 SER   A CB  
1077 O  OG  . SER   A 139 ? 0.24619 0.27669 0.24329 -0.04314 -0.08155 0.01587  139 SER   A OG  
1078 N  N   . PHE   A 140 ? 0.22607 0.24110 0.18245 -0.03906 -0.07269 0.01050  140 PHE   A N   
1079 C  CA  . PHE   A 140 ? 0.26782 0.28472 0.21702 -0.03738 -0.07237 0.01586  140 PHE   A CA  
1080 C  C   . PHE   A 140 ? 0.31180 0.32683 0.24195 -0.04360 -0.07606 0.01462  140 PHE   A C   
1081 O  O   . PHE   A 140 ? 0.31972 0.32648 0.23348 -0.04793 -0.07418 0.00577  140 PHE   A O   
1082 C  CB  . PHE   A 140 ? 0.25423 0.26575 0.19516 -0.03418 -0.06546 0.01329  140 PHE   A CB  
1083 C  CG  . PHE   A 140 ? 0.22418 0.23810 0.18293 -0.02786 -0.06158 0.01490  140 PHE   A CG  
1084 C  CD1 . PHE   A 140 ? 0.22158 0.24167 0.19565 -0.02413 -0.06335 0.02262  140 PHE   A CD1 
1085 C  CD2 . PHE   A 140 ? 0.24311 0.25200 0.20398 -0.02448 -0.05353 0.00817  140 PHE   A CD2 
1086 C  CE1 . PHE   A 140 ? 0.20688 0.22740 0.19517 -0.01841 -0.05765 0.02191  140 PHE   A CE1 
1087 C  CE2 . PHE   A 140 ? 0.21461 0.22611 0.19013 -0.01878 -0.04891 0.00913  140 PHE   A CE2 
1088 C  CZ  . PHE   A 140 ? 0.19996 0.21682 0.18763 -0.01624 -0.05082 0.01508  140 PHE   A CZ  
1089 N  N   . LEU   A 141 ? 0.28511 0.30687 0.21701 -0.04412 -0.08098 0.02320  141 LEU   A N   
1090 C  CA  . LEU   A 141 ? 0.32147 0.34245 0.23360 -0.04997 -0.08465 0.02327  141 LEU   A CA  
1091 C  C   . LEU   A 141 ? 0.31686 0.33754 0.21903 -0.04808 -0.08143 0.02884  141 LEU   A C   
1092 O  O   . LEU   A 141 ? 0.31849 0.33981 0.23102 -0.04271 -0.07736 0.03305  141 LEU   A O   
1093 C  CB  . LEU   A 141 ? 0.28953 0.31943 0.21010 -0.05357 -0.09427 0.02984  141 LEU   A CB  
1094 C  CG  . LEU   A 141 ? 0.38133 0.41349 0.31471 -0.05598 -0.09773 0.02620  141 LEU   A CG  
1095 C  CD1 . LEU   A 141 ? 0.39220 0.43618 0.34093 -0.05735 -0.10631 0.03597  141 LEU   A CD1 
1096 C  CD2 . LEU   A 141 ? 0.36948 0.39311 0.28439 -0.06318 -0.09805 0.01493  141 LEU   A CD2 
1097 N  N   . ASN   A 142 ? 0.34286 0.36244 0.22435 -0.05307 -0.08321 0.02891  142 ASN   A N   
1098 C  CA  . ASN   A 142 ? 0.34767 0.36765 0.21909 -0.05203 -0.08005 0.03548  142 ASN   A CA  
1099 C  C   . ASN   A 142 ? 0.32308 0.35037 0.21597 -0.04765 -0.08369 0.04831  142 ASN   A C   
1100 O  O   . ASN   A 142 ? 0.34156 0.37561 0.24891 -0.04787 -0.09117 0.05413  142 ASN   A O   
1101 C  CB  . ASN   A 142 ? 0.34329 0.36296 0.19073 -0.05840 -0.08301 0.03536  142 ASN   A CB  
1102 C  CG  . ASN   A 142 ? 0.45547 0.47373 0.28801 -0.05772 -0.07681 0.04001  142 ASN   A CG  
1103 O  OD1 . ASN   A 142 ? 0.48441 0.50260 0.32668 -0.05288 -0.07119 0.04456  142 ASN   A OD1 
1104 N  ND2 . ASN   A 142 ? 0.48175 0.49928 0.29080 -0.06297 -0.07785 0.03949  142 ASN   A ND2 
1105 N  N   . GLY   A 143 ? 0.28238 0.30790 0.17870 -0.04367 -0.07778 0.05250  143 GLY   A N   
1106 C  CA  . GLY   A 143 ? 0.30084 0.33024 0.21751 -0.03929 -0.07963 0.06354  143 GLY   A CA  
1107 C  C   . GLY   A 143 ? 0.26246 0.29097 0.20097 -0.03359 -0.07685 0.06172  143 GLY   A C   
1108 O  O   . GLY   A 143 ? 0.23705 0.26650 0.19260 -0.02953 -0.07688 0.06953  143 GLY   A O   
1109 N  N   . SER   A 144 ? 0.21799 0.24398 0.15633 -0.03321 -0.07423 0.05159  144 SER   A N   
1110 C  CA  . SER   A 144 ? 0.24254 0.26791 0.19933 -0.02807 -0.07126 0.04933  144 SER   A CA  
1111 C  C   . SER   A 144 ? 0.20149 0.22274 0.15574 -0.02603 -0.06475 0.04842  144 SER   A C   
1112 O  O   . SER   A 144 ? 0.19357 0.21432 0.16277 -0.02197 -0.06266 0.04720  144 SER   A O   
1113 C  CB  . SER   A 144 ? 0.23964 0.26446 0.19793 -0.02880 -0.07125 0.03996  144 SER   A CB  
1114 O  OG  . SER   A 144 ? 0.26401 0.28325 0.20193 -0.03235 -0.06792 0.03181  144 SER   A OG  
1115 N  N   . CYS   A 145 ? 0.22857 0.24747 0.16432 -0.02905 -0.06102 0.04896  145 CYS   A N   
1116 C  CA  . CYS   A 145 ? 0.25535 0.27164 0.19335 -0.02681 -0.05231 0.04793  145 CYS   A CA  
1117 C  C   . CYS   A 145 ? 0.18579 0.20173 0.14466 -0.02316 -0.05260 0.05452  145 CYS   A C   
1118 O  O   . CYS   A 145 ? 0.22049 0.23763 0.18553 -0.02320 -0.05881 0.06465  145 CYS   A O   
1119 C  CB  . CYS   A 145 ? 0.28146 0.29703 0.20033 -0.03040 -0.04731 0.05091  145 CYS   A CB  
1120 S  SG  . CYS   A 145 ? 0.42575 0.43853 0.31691 -0.03460 -0.04385 0.04111  145 CYS   A SG  
1121 N  N   . GLY   A 146 ? 0.18269 0.19661 0.15282 -0.02007 -0.04616 0.04866  146 GLY   A N   
1122 C  CA  . GLY   A 146 ? 0.17584 0.18693 0.16402 -0.01737 -0.04547 0.05188  146 GLY   A CA  
1123 C  C   . GLY   A 146 ? 0.17660 0.18755 0.17965 -0.01341 -0.04781 0.04841  146 GLY   A C   
1124 O  O   . GLY   A 146 ? 0.14919 0.15600 0.16590 -0.01095 -0.04525 0.04781  146 GLY   A O   
1125 N  N   . SER   A 147 ? 0.16491 0.17982 0.16574 -0.01325 -0.05214 0.04606  147 SER   A N   
1126 C  CA  . SER   A 147 ? 0.14826 0.16436 0.16337 -0.00957 -0.05229 0.04219  147 SER   A CA  
1127 C  C   . SER   A 147 ? 0.16322 0.17693 0.17968 -0.00812 -0.04528 0.03320  147 SER   A C   
1128 O  O   . SER   A 147 ? 0.14090 0.15472 0.14706 -0.00989 -0.04192 0.02900  147 SER   A O   
1129 C  CB  . SER   A 147 ? 0.12346 0.14488 0.13575 -0.01111 -0.05756 0.04081  147 SER   A CB  
1130 O  OG  . SER   A 147 ? 0.15646 0.18134 0.16395 -0.01410 -0.06472 0.04853  147 SER   A OG  
1131 N  N   . VAL   A 148 ? 0.13223 0.14420 0.16145 -0.00483 -0.04278 0.03054  148 VAL   A N   
1132 C  CA  . VAL   A 148 ? 0.12788 0.13840 0.15667 -0.00447 -0.03742 0.02283  148 VAL   A CA  
1133 C  C   . VAL   A 148 ? 0.13637 0.15010 0.16810 -0.00241 -0.03625 0.01783  148 VAL   A C   
1134 O  O   . VAL   A 148 ? 0.14512 0.16148 0.18440 -0.00057 -0.03830 0.02000  148 VAL   A O   
1135 C  CB  . VAL   A 148 ? 0.14218 0.14628 0.17864 -0.00410 -0.03414 0.02178  148 VAL   A CB  
1136 C  CG1 . VAL   A 148 ? 0.12814 0.12915 0.16189 -0.00715 -0.03472 0.02769  148 VAL   A CG1 
1137 C  CG2 . VAL   A 148 ? 0.13323 0.13389 0.18265 -0.00016 -0.03360 0.02311  148 VAL   A CG2 
1138 N  N   . GLY   A 149 ? 0.13210 0.14685 0.15881 -0.00296 -0.03300 0.01225  149 GLY   A N   
1139 C  CA  . GLY   A 149 ? 0.11540 0.13275 0.14350 -0.00142 -0.03077 0.00800  149 GLY   A CA  
1140 C  C   . GLY   A 149 ? 0.10388 0.11889 0.13408 -0.00109 -0.02706 0.00345  149 GLY   A C   
1141 O  O   . GLY   A 149 ? 0.11359 0.12603 0.14187 -0.00332 -0.02661 0.00223  149 GLY   A O   
1142 N  N   . PHE   A 150 ? 0.12282 0.13881 0.15623 0.00091  -0.02414 0.00060  150 PHE   A N   
1143 C  CA  . PHE   A 150 ? 0.12728 0.13941 0.16009 0.00069  -0.02006 -0.00505 150 PHE   A CA  
1144 C  C   . PHE   A 150 ? 0.13425 0.14980 0.16525 0.00217  -0.01602 -0.00826 150 PHE   A C   
1145 O  O   . PHE   A 150 ? 0.12463 0.14477 0.15982 0.00405  -0.01585 -0.00512 150 PHE   A O   
1146 C  CB  . PHE   A 150 ? 0.14632 0.15080 0.18847 0.00262  -0.01812 -0.00480 150 PHE   A CB  
1147 C  CG  . PHE   A 150 ? 0.14397 0.15065 0.19770 0.00713  -0.01694 -0.00103 150 PHE   A CG  
1148 C  CD1 . PHE   A 150 ? 0.13689 0.14774 0.19616 0.00767  -0.02246 0.00681  150 PHE   A CD1 
1149 C  CD2 . PHE   A 150 ? 0.13817 0.14424 0.19706 0.01035  -0.01036 -0.00506 150 PHE   A CD2 
1150 C  CE1 . PHE   A 150 ? 0.15737 0.17301 0.22973 0.01107  -0.02278 0.01142  150 PHE   A CE1 
1151 C  CE2 . PHE   A 150 ? 0.16531 0.17606 0.23849 0.01474  -0.00884 -0.00050 150 PHE   A CE2 
1152 C  CZ  . PHE   A 150 ? 0.15962 0.17601 0.24080 0.01492  -0.01580 0.00822  150 PHE   A CZ  
1153 N  N   . ASN   A 151 ? 0.14593 0.15889 0.17030 0.00050  -0.01267 -0.01456 151 ASN   A N   
1154 C  CA  . ASN   A 151 ? 0.19778 0.21217 0.21831 0.00162  -0.00696 -0.01861 151 ASN   A CA  
1155 C  C   . ASN   A 151 ? 0.18495 0.18985 0.20637 0.00219  -0.00112 -0.02584 151 ASN   A C   
1156 O  O   . ASN   A 151 ? 0.18350 0.18064 0.20657 0.00037  -0.00260 -0.02793 151 ASN   A O   
1157 C  CB  . ASN   A 151 ? 0.17883 0.19900 0.18601 -0.00184 -0.00842 -0.01993 151 ASN   A CB  
1158 C  CG  . ASN   A 151 ? 0.19854 0.22621 0.20654 -0.00096 -0.01156 -0.01303 151 ASN   A CG  
1159 O  OD1 . ASN   A 151 ? 0.19437 0.22512 0.20541 0.00111  -0.00862 -0.01044 151 ASN   A OD1 
1160 N  ND2 . ASN   A 151 ? 0.15790 0.18782 0.16489 -0.00242 -0.01673 -0.00993 151 ASN   A ND2 
1161 N  N   . ILE   A 152 ? 0.18931 0.19390 0.20999 0.00470  0.00660  -0.02977 152 ILE   A N   
1162 C  CA  . ILE   A 152 ? 0.23130 0.22496 0.25188 0.00591  0.01454  -0.03839 152 ILE   A CA  
1163 C  C   . ILE   A 152 ? 0.32191 0.31659 0.32488 0.00298  0.01993  -0.04602 152 ILE   A C   
1164 O  O   . ILE   A 152 ? 0.30894 0.31289 0.30914 0.00428  0.02243  -0.04262 152 ILE   A O   
1165 C  CB  . ILE   A 152 ? 0.26803 0.25970 0.30749 0.01339  0.02140  -0.03584 152 ILE   A CB  
1166 C  CG1 . ILE   A 152 ? 0.23896 0.23427 0.29453 0.01582  0.01416  -0.02538 152 ILE   A CG1 
1167 C  CG2 . ILE   A 152 ? 0.27571 0.25257 0.31679 0.01554  0.03076  -0.04539 152 ILE   A CG2 
1168 C  CD1 . ILE   A 152 ? 0.23957 0.22546 0.29706 0.01400  0.00976  -0.02496 152 ILE   A CD1 
1169 N  N   . ASP   A 153 ? 0.36140 0.34644 0.35173 -0.00180 0.02144  -0.05601 153 ASP   A N   
1170 C  CA  . ASP   A 153 ? 0.42293 0.40793 0.39195 -0.00639 0.02557  -0.06457 153 ASP   A CA  
1171 C  C   . ASP   A 153 ? 0.46448 0.43308 0.43084 -0.00562 0.03600  -0.07718 153 ASP   A C   
1172 O  O   . ASP   A 153 ? 0.47230 0.42849 0.43893 -0.00924 0.03392  -0.08319 153 ASP   A O   
1173 C  CB  . ASP   A 153 ? 0.44151 0.43144 0.39521 -0.01511 0.01529  -0.06512 153 ASP   A CB  
1174 C  CG  . ASP   A 153 ? 0.57704 0.57105 0.50709 -0.02048 0.01707  -0.07091 153 ASP   A CG  
1175 O  OD1 . ASP   A 153 ? 0.59833 0.59411 0.52374 -0.01680 0.02627  -0.07195 153 ASP   A OD1 
1176 O  OD2 . ASP   A 153 ? 0.67233 0.66894 0.58864 -0.02876 0.00912  -0.07368 153 ASP   A OD2 
1177 N  N   . TYR   A 154 ? 0.48526 0.45326 0.45000 -0.00088 0.04809  -0.08107 154 TYR   A N   
1178 C  CA  . TYR   A 154 ? 0.56719 0.51970 0.53787 0.00392  0.06121  -0.09091 154 TYR   A CA  
1179 C  C   . TYR   A 154 ? 0.54244 0.48630 0.53825 0.00918  0.05939  -0.08623 154 TYR   A C   
1180 O  O   . TYR   A 154 ? 0.55826 0.51087 0.57557 0.01606  0.05811  -0.07469 154 TYR   A O   
1181 C  CB  . TYR   A 154 ? 0.61393 0.55202 0.55980 -0.00361 0.06572  -0.10749 154 TYR   A CB  
1182 C  CG  . TYR   A 154 ? 0.71565 0.63803 0.66590 0.00267  0.08219  -0.11787 154 TYR   A CG  
1183 C  CD1 . TYR   A 154 ? 0.68046 0.60955 0.64649 0.01287  0.09362  -0.11273 154 TYR   A CD1 
1184 C  CD2 . TYR   A 154 ? 0.71204 0.61655 0.65417 -0.00105 0.08294  -0.12749 154 TYR   A CD2 
1185 C  CE1 . TYR   A 154 ? 0.75845 0.67744 0.73189 0.01955  0.10539  -0.11699 154 TYR   A CE1 
1186 C  CE2 . TYR   A 154 ? 0.74575 0.63819 0.69383 0.00562  0.09541  -0.13296 154 TYR   A CE2 
1187 C  CZ  . TYR   A 154 ? 0.79455 0.69456 0.75830 0.01613  0.10666  -0.12765 154 TYR   A CZ  
1188 O  OH  . TYR   A 154 ? 0.74722 0.63651 0.71823 0.02292  0.11909  -0.13267 154 TYR   A OH  
1189 N  N   . ASP   A 155 ? 0.49069 0.41760 0.48413 0.00536  0.05872  -0.09432 155 ASP   A N   
1190 C  CA  . ASP   A 155 ? 0.50261 0.41961 0.51959 0.01045  0.05804  -0.08907 155 ASP   A CA  
1191 C  C   . ASP   A 155 ? 0.41532 0.33506 0.43489 0.00467  0.04387  -0.08119 155 ASP   A C   
1192 O  O   . ASP   A 155 ? 0.37039 0.28170 0.40699 0.00750  0.04231  -0.07585 155 ASP   A O   
1193 C  CB  . ASP   A 155 ? 0.54648 0.43939 0.56394 0.01163  0.06960  -0.10257 155 ASP   A CB  
1194 C  CG  . ASP   A 155 ? 0.61604 0.49797 0.60929 -0.00046 0.06528  -0.11464 155 ASP   A CG  
1195 O  OD1 . ASP   A 155 ? 0.62104 0.48606 0.61365 -0.00126 0.06907  -0.12079 155 ASP   A OD1 
1196 O  OD2 . ASP   A 155 ? 0.65004 0.54361 0.62564 -0.00910 0.05606  -0.11496 155 ASP   A OD2 
1197 N  N   . CYS   A 156 ? 0.37187 0.30379 0.37620 -0.00284 0.03417  -0.07925 156 CYS   A N   
1198 C  CA  . CYS   A 156 ? 0.32811 0.26249 0.33326 -0.00909 0.02264  -0.07371 156 CYS   A CA  
1199 C  C   . CYS   A 156 ? 0.26047 0.21207 0.27375 -0.00606 0.01491  -0.05968 156 CYS   A C   
1200 O  O   . CYS   A 156 ? 0.24078 0.20548 0.24719 -0.00535 0.01377  -0.05688 156 CYS   A O   
1201 C  CB  . CYS   A 156 ? 0.35601 0.29171 0.34024 -0.02012 0.01719  -0.08176 156 CYS   A CB  
1202 S  SG  . CYS   A 156 ? 0.33251 0.27781 0.32004 -0.02718 0.00365  -0.07286 156 CYS   A SG  
1203 N  N   . VAL   A 157 ? 0.21063 0.16107 0.23756 -0.00464 0.01006  -0.05099 157 VAL   A N   
1204 C  CA  . VAL   A 157 ? 0.15443 0.11859 0.18708 -0.00261 0.00307  -0.03912 157 VAL   A CA  
1205 C  C   . VAL   A 157 ? 0.20972 0.18100 0.23292 -0.00976 -0.00480 -0.03757 157 VAL   A C   
1206 O  O   . VAL   A 157 ? 0.17244 0.13750 0.19701 -0.01460 -0.00747 -0.03807 157 VAL   A O   
1207 C  CB  . VAL   A 157 ? 0.18369 0.14406 0.23341 0.00203  0.00169  -0.02990 157 VAL   A CB  
1208 C  CG1 . VAL   A 157 ? 0.15304 0.12681 0.20456 0.00299  -0.00526 -0.01957 157 VAL   A CG1 
1209 C  CG2 . VAL   A 157 ? 0.20225 0.15568 0.26598 0.00989  0.00989  -0.03056 157 VAL   A CG2 
1210 N  N   . SER   A 158 ? 0.20116 0.18561 0.21709 -0.01021 -0.00810 -0.03473 158 SER   A N   
1211 C  CA  . SER   A 158 ? 0.16295 0.15632 0.17378 -0.01521 -0.01494 -0.03140 158 SER   A CA  
1212 C  C   . SER   A 158 ? 0.15134 0.15053 0.16985 -0.01183 -0.01810 -0.02173 158 SER   A C   
1213 O  O   . SER   A 158 ? 0.15244 0.15826 0.17109 -0.00811 -0.01821 -0.01797 158 SER   A O   
1214 C  CB  . SER   A 158 ? 0.19154 0.19502 0.19067 -0.01725 -0.01647 -0.03312 158 SER   A CB  
1215 O  OG  . SER   A 158 ? 0.24977 0.24823 0.23809 -0.02246 -0.01487 -0.04253 158 SER   A OG  
1216 N  N   . PHE   A 159 ? 0.14009 0.13598 0.16406 -0.01375 -0.02032 -0.01794 159 PHE   A N   
1217 C  CA  . PHE   A 159 ? 0.14506 0.14576 0.17267 -0.01155 -0.02289 -0.00959 159 PHE   A CA  
1218 C  C   . PHE   A 159 ? 0.12387 0.13523 0.14625 -0.01347 -0.02551 -0.00770 159 PHE   A C   
1219 O  O   . PHE   A 159 ? 0.13082 0.14541 0.15184 -0.01814 -0.02701 -0.00937 159 PHE   A O   
1220 C  CB  . PHE   A 159 ? 0.14924 0.14316 0.18302 -0.01328 -0.02354 -0.00521 159 PHE   A CB  
1221 C  CG  . PHE   A 159 ? 0.13612 0.11970 0.17837 -0.00980 -0.02110 -0.00431 159 PHE   A CG  
1222 C  CD1 . PHE   A 159 ? 0.11563 0.10166 0.16299 -0.00462 -0.02203 0.00170  159 PHE   A CD1 
1223 C  CD2 . PHE   A 159 ? 0.17137 0.14270 0.21762 -0.01181 -0.01796 -0.00939 159 PHE   A CD2 
1224 C  CE1 . PHE   A 159 ? 0.12684 0.10549 0.18547 -0.00053 -0.02016 0.00455  159 PHE   A CE1 
1225 C  CE2 . PHE   A 159 ? 0.13238 0.09342 0.18921 -0.00717 -0.01465 -0.00776 159 PHE   A CE2 
1226 C  CZ  . PHE   A 159 ? 0.16845 0.13437 0.23260 -0.00099 -0.01586 0.00007  159 PHE   A CZ  
1227 N  N   . CYS   A 160 ? 0.13278 0.14957 0.15365 -0.01008 -0.02606 -0.00409 160 CYS   A N   
1228 C  CA  . CYS   A 160 ? 0.13977 0.16509 0.15778 -0.01053 -0.02716 -0.00208 160 CYS   A CA  
1229 C  C   . CYS   A 160 ? 0.14439 0.17104 0.16210 -0.00901 -0.02699 0.00267  160 CYS   A C   
1230 O  O   . CYS   A 160 ? 0.15445 0.18721 0.17190 -0.00905 -0.02635 0.00438  160 CYS   A O   
1231 C  CB  . CYS   A 160 ? 0.10889 0.13887 0.12331 -0.00839 -0.02687 -0.00331 160 CYS   A CB  
1232 S  SG  . CYS   A 160 ? 0.14123 0.16804 0.15649 -0.00429 -0.02544 -0.00230 160 CYS   A SG  
1233 N  N   . TYR   A 161 ? 0.09072 0.11234 0.10838 -0.00784 -0.02742 0.00502  161 TYR   A N   
1234 C  CA  . TYR   A 161 ? 0.12321 0.14563 0.13610 -0.00706 -0.02734 0.00806  161 TYR   A CA  
1235 C  C   . TYR   A 161 ? 0.13127 0.14954 0.14341 -0.00839 -0.02880 0.01235  161 TYR   A C   
1236 O  O   . TYR   A 161 ? 0.13067 0.14515 0.14764 -0.00767 -0.03076 0.01367  161 TYR   A O   
1237 C  CB  . TYR   A 161 ? 0.12102 0.14322 0.13139 -0.00478 -0.02803 0.00689  161 TYR   A CB  
1238 C  CG  . TYR   A 161 ? 0.12216 0.14269 0.12513 -0.00513 -0.02807 0.00803  161 TYR   A CG  
1239 C  CD1 . TYR   A 161 ? 0.14533 0.16723 0.14436 -0.00425 -0.02441 0.00696  161 TYR   A CD1 
1240 C  CD2 . TYR   A 161 ? 0.11745 0.13525 0.11742 -0.00641 -0.03167 0.00997  161 TYR   A CD2 
1241 C  CE1 . TYR   A 161 ? 0.13638 0.15465 0.12647 -0.00473 -0.02296 0.00610  161 TYR   A CE1 
1242 C  CE2 . TYR   A 161 ? 0.12194 0.13737 0.11148 -0.00816 -0.03209 0.00963  161 TYR   A CE2 
1243 C  CZ  . TYR   A 161 ? 0.14238 0.15693 0.12595 -0.00732 -0.02698 0.00682  161 TYR   A CZ  
1244 O  OH  . TYR   A 161 ? 0.15811 0.16821 0.12932 -0.00903 -0.02561 0.00457  161 TYR   A OH  
1245 N  N   . MET   A 162 ? 0.10877 0.12813 0.11559 -0.01000 -0.02737 0.01537  162 MET   A N   
1246 C  CA  . MET   A 162 ? 0.12063 0.13678 0.12331 -0.01132 -0.02962 0.02071  162 MET   A CA  
1247 C  C   . MET   A 162 ? 0.13878 0.15587 0.12904 -0.01176 -0.02879 0.02038  162 MET   A C   
1248 O  O   . MET   A 162 ? 0.11911 0.13865 0.10557 -0.01136 -0.02392 0.01796  162 MET   A O   
1249 C  CB  . MET   A 162 ? 0.18179 0.19620 0.18776 -0.01411 -0.02843 0.02578  162 MET   A CB  
1250 C  CG  . MET   A 162 ? 0.15411 0.16651 0.15304 -0.01586 -0.03044 0.03358  162 MET   A CG  
1251 S  SD  . MET   A 162 ? 0.22135 0.23071 0.22650 -0.01948 -0.02815 0.04072  162 MET   A SD  
1252 C  CE  . MET   A 162 ? 0.23745 0.23842 0.25769 -0.01759 -0.03113 0.04082  162 MET   A CE  
1253 N  N   . HIS   A 163 ? 0.14776 0.16300 0.13247 -0.01263 -0.03347 0.02249  163 HIS   A N   
1254 C  CA  . HIS   A 163 ? 0.16057 0.17468 0.13122 -0.01426 -0.03353 0.02007  163 HIS   A CA  
1255 C  C   . HIS   A 163 ? 0.15173 0.16553 0.10926 -0.01705 -0.03062 0.02338  163 HIS   A C   
1256 O  O   . HIS   A 163 ? 0.14219 0.15641 0.09920 -0.01901 -0.03331 0.03076  163 HIS   A O   
1257 C  CB  . HIS   A 163 ? 0.18137 0.19512 0.15046 -0.01596 -0.04105 0.02147  163 HIS   A CB  
1258 C  CG  . HIS   A 163 ? 0.17005 0.18089 0.12349 -0.01912 -0.04163 0.01701  163 HIS   A CG  
1259 N  ND1 . HIS   A 163 ? 0.19374 0.20095 0.14381 -0.01771 -0.03596 0.00946  163 HIS   A ND1 
1260 C  CD2 . HIS   A 163 ? 0.20999 0.21999 0.14904 -0.02401 -0.04682 0.01869  163 HIS   A CD2 
1261 C  CE1 . HIS   A 163 ? 0.19562 0.19791 0.13004 -0.02153 -0.03679 0.00536  163 HIS   A CE1 
1262 N  NE2 . HIS   A 163 ? 0.22267 0.22704 0.14898 -0.02601 -0.04387 0.01043  163 HIS   A NE2 
1263 N  N   . HIS   A 164 ? 0.16229 0.17487 0.10930 -0.01696 -0.02441 0.01838  164 HIS   A N   
1264 C  CA  . HIS   A 164 ? 0.18674 0.19921 0.11922 -0.01952 -0.01957 0.02070  164 HIS   A CA  
1265 C  C   . HIS   A 164 ? 0.22516 0.23249 0.13654 -0.02253 -0.01946 0.01588  164 HIS   A C   
1266 O  O   . HIS   A 164 ? 0.24808 0.25513 0.14346 -0.02673 -0.02053 0.01989  164 HIS   A O   
1267 C  CB  . HIS   A 164 ? 0.15143 0.16764 0.08982 -0.01686 -0.00956 0.01932  164 HIS   A CB  
1268 C  CG  . HIS   A 164 ? 0.16768 0.18908 0.12173 -0.01701 -0.00966 0.02525  164 HIS   A CG  
1269 N  ND1 . HIS   A 164 ? 0.16301 0.18812 0.11663 -0.01930 -0.00448 0.03106  164 HIS   A ND1 
1270 C  CD2 . HIS   A 164 ? 0.18355 0.20618 0.15338 -0.01595 -0.01386 0.02564  164 HIS   A CD2 
1271 C  CE1 . HIS   A 164 ? 0.14105 0.16882 0.11053 -0.02020 -0.00631 0.03471  164 HIS   A CE1 
1272 N  NE2 . HIS   A 164 ? 0.15124 0.17714 0.12971 -0.01813 -0.01180 0.03076  164 HIS   A NE2 
1273 N  N   . MET   A 165 ? 0.23264 0.23509 0.14227 -0.02128 -0.01853 0.00754  165 MET   A N   
1274 C  CA  . MET   A 165 ? 0.26511 0.26025 0.15262 -0.02476 -0.01592 0.00086  165 MET   A CA  
1275 C  C   . MET   A 165 ? 0.26325 0.25115 0.15170 -0.02466 -0.01768 -0.00751 165 MET   A C   
1276 O  O   . MET   A 165 ? 0.20705 0.19627 0.11330 -0.02052 -0.01794 -0.00801 165 MET   A O   
1277 C  CB  . MET   A 165 ? 0.28276 0.27709 0.16268 -0.02239 -0.00284 -0.00177 165 MET   A CB  
1278 C  CG  . MET   A 165 ? 0.28135 0.27666 0.17904 -0.01548 0.00470  -0.00522 165 MET   A CG  
1279 S  SD  . MET   A 165 ? 0.39217 0.39014 0.28708 -0.01170 0.02071  -0.00623 165 MET   A SD  
1280 C  CE  . MET   A 165 ? 0.33534 0.32787 0.24258 -0.00439 0.02778  -0.01393 165 MET   A CE  
1281 N  N   . GLU   A 166 ? 0.26025 0.23997 0.12815 -0.03009 -0.01888 -0.01406 166 GLU   A N   
1282 C  CA  . GLU   A 166 ? 0.27783 0.24795 0.14480 -0.03136 -0.01957 -0.02293 166 GLU   A CA  
1283 C  C   . GLU   A 166 ? 0.30135 0.25991 0.15588 -0.02914 -0.00659 -0.03297 166 GLU   A C   
1284 O  O   . GLU   A 166 ? 0.30743 0.26300 0.14164 -0.03147 -0.00072 -0.03574 166 GLU   A O   
1285 C  CB  . GLU   A 166 ? 0.29387 0.26212 0.14879 -0.04044 -0.03175 -0.02403 166 GLU   A CB  
1286 C  CG  . GLU   A 166 ? 0.35542 0.31195 0.20817 -0.04367 -0.03230 -0.03395 166 GLU   A CG  
1287 C  CD  . GLU   A 166 ? 0.38630 0.34623 0.23834 -0.05178 -0.04558 -0.03242 166 GLU   A CD  
1288 O  OE1 . GLU   A 166 ? 0.37519 0.34783 0.24434 -0.05104 -0.05407 -0.02256 166 GLU   A OE1 
1289 O  OE2 . GLU   A 166 ? 0.41116 0.36295 0.25079 -0.05690 -0.04569 -0.04019 166 GLU   A OE2 
1290 N  N   . LEU   A 167 ? 0.31088 0.26313 0.17793 -0.02424 -0.00133 -0.03762 167 LEU   A N   
1291 C  CA  . LEU   A 167 ? 0.32512 0.26480 0.18462 -0.02058 0.01200  -0.04702 167 LEU   A CA  
1292 C  C   . LEU   A 167 ? 0.36505 0.28802 0.20494 -0.02803 0.01019  -0.05843 167 LEU   A C   
1293 O  O   . LEU   A 167 ? 0.41236 0.33545 0.25083 -0.03536 -0.00227 -0.05790 167 LEU   A O   
1294 C  CB  . LEU   A 167 ? 0.32950 0.27002 0.21359 -0.01140 0.01812  -0.04504 167 LEU   A CB  
1295 C  CG  . LEU   A 167 ? 0.28453 0.24105 0.18664 -0.00491 0.02073  -0.03532 167 LEU   A CG  
1296 C  CD1 . LEU   A 167 ? 0.28763 0.24703 0.21315 0.00229  0.02256  -0.03186 167 LEU   A CD1 
1297 C  CD2 . LEU   A 167 ? 0.30886 0.26672 0.20327 -0.00182 0.03307  -0.03668 167 LEU   A CD2 
1298 N  N   . PRO   A 168 ? 0.40359 0.31169 0.22903 -0.02659 0.02285  -0.06926 168 PRO   A N   
1299 C  CA  . PRO   A 168 ? 0.40258 0.29376 0.20653 -0.03511 0.02103  -0.08142 168 PRO   A CA  
1300 C  C   . PRO   A 168 ? 0.42467 0.30705 0.23985 -0.03868 0.01345  -0.08432 168 PRO   A C   
1301 O  O   . PRO   A 168 ? 0.48578 0.36408 0.29298 -0.04669 0.00565  -0.08875 168 PRO   A O   
1302 C  CB  . PRO   A 168 ? 0.39390 0.27360 0.19180 -0.02864 0.03837  -0.09021 168 PRO   A CB  
1303 C  CG  . PRO   A 168 ? 0.43516 0.32631 0.23671 -0.02121 0.04854  -0.08373 168 PRO   A CG  
1304 C  CD  . PRO   A 168 ? 0.39109 0.29885 0.21978 -0.01736 0.03954  -0.07048 168 PRO   A CD  
1305 N  N   . THR   A 169 ? 0.37228 0.25777 0.21378 -0.03142 0.01453  -0.07834 169 THR   A N   
1306 C  CA  . THR   A 169 ? 0.39405 0.27271 0.24673 -0.03558 0.00719  -0.07928 169 THR   A CA  
1307 C  C   . THR   A 169 ? 0.38767 0.28258 0.24910 -0.04162 -0.00885 -0.06991 169 THR   A C   
1308 O  O   . THR   A 169 ? 0.40122 0.29483 0.27609 -0.04456 -0.01491 -0.06813 169 THR   A O   
1309 C  CB  . THR   A 169 ? 0.40315 0.27875 0.28071 -0.02520 0.01520  -0.07539 169 THR   A CB  
1310 O  OG1 . THR   A 169 ? 0.41104 0.30614 0.30586 -0.01687 0.01546  -0.06347 169 THR   A OG1 
1311 C  CG2 . THR   A 169 ? 0.38520 0.24129 0.25723 -0.01935 0.03116  -0.08531 169 THR   A CG2 
1312 N  N   . GLY   A 170 ? 0.38850 0.29859 0.24430 -0.04312 -0.01497 -0.06317 170 GLY   A N   
1313 C  CA  . GLY   A 170 ? 0.35618 0.28165 0.22314 -0.04718 -0.02875 -0.05363 170 GLY   A CA  
1314 C  C   . GLY   A 170 ? 0.34517 0.28418 0.23795 -0.03875 -0.02860 -0.04304 170 GLY   A C   
1315 O  O   . GLY   A 170 ? 0.32601 0.27664 0.23060 -0.04097 -0.03818 -0.03569 170 GLY   A O   
1316 N  N   . VAL   A 171 ? 0.28128 0.21972 0.18329 -0.02938 -0.01811 -0.04201 171 VAL   A N   
1317 C  CA  . VAL   A 171 ? 0.25943 0.21096 0.18192 -0.02253 -0.01832 -0.03277 171 VAL   A CA  
1318 C  C   . VAL   A 171 ? 0.22846 0.19059 0.14840 -0.01990 -0.01721 -0.02763 171 VAL   A C   
1319 O  O   . VAL   A 171 ? 0.25067 0.21018 0.15395 -0.02211 -0.01440 -0.03045 171 VAL   A O   
1320 C  CB  . VAL   A 171 ? 0.26256 0.21003 0.19906 -0.01473 -0.00984 -0.03247 171 VAL   A CB  
1321 C  CG1 . VAL   A 171 ? 0.28867 0.22444 0.22906 -0.01779 -0.01084 -0.03615 171 VAL   A CG1 
1322 C  CG2 . VAL   A 171 ? 0.25912 0.20130 0.19034 -0.00886 0.00182  -0.03614 171 VAL   A CG2 
1323 N  N   . HIS   A 172 ? 0.18993 0.16348 0.12571 -0.01571 -0.01896 -0.02014 172 HIS   A N   
1324 C  CA  . HIS   A 172 ? 0.19606 0.17924 0.13177 -0.01533 -0.02072 -0.01430 172 HIS   A CA  
1325 C  C   . HIS   A 172 ? 0.19160 0.18075 0.13853 -0.00885 -0.01390 -0.01131 172 HIS   A C   
1326 O  O   . HIS   A 172 ? 0.17559 0.16589 0.13469 -0.00474 -0.01180 -0.01077 172 HIS   A O   
1327 C  CB  . HIS   A 172 ? 0.20570 0.19630 0.14957 -0.01801 -0.03048 -0.00852 172 HIS   A CB  
1328 C  CG  . HIS   A 172 ? 0.20808 0.19569 0.14297 -0.02506 -0.03840 -0.01017 172 HIS   A CG  
1329 N  ND1 . HIS   A 172 ? 0.20765 0.19429 0.15066 -0.02759 -0.04306 -0.01126 172 HIS   A ND1 
1330 C  CD2 . HIS   A 172 ? 0.25040 0.23599 0.16773 -0.03105 -0.04250 -0.01106 172 HIS   A CD2 
1331 C  CE1 . HIS   A 172 ? 0.24130 0.22642 0.17421 -0.03519 -0.05070 -0.01262 172 HIS   A CE1 
1332 N  NE2 . HIS   A 172 ? 0.22151 0.20585 0.13745 -0.03751 -0.05091 -0.01266 172 HIS   A NE2 
1333 N  N   . ALA   A 173 ? 0.18882 0.18214 0.13103 -0.00870 -0.01068 -0.00886 173 ALA   A N   
1334 C  CA  . ALA   A 173 ? 0.14264 0.14344 0.09579 -0.00413 -0.00485 -0.00552 173 ALA   A CA  
1335 C  C   . ALA   A 173 ? 0.15076 0.15916 0.10751 -0.00638 -0.00886 0.00083  173 ALA   A C   
1336 O  O   . ALA   A 173 ? 0.18294 0.19002 0.12970 -0.01048 -0.01264 0.00299  173 ALA   A O   
1337 C  CB  . ALA   A 173 ? 0.20064 0.19850 0.14703 -0.00151 0.00586  -0.00886 173 ALA   A CB  
1338 N  N   . GLY   A 174 ? 0.15944 0.17535 0.13054 -0.00413 -0.00853 0.00417  174 GLY   A N   
1339 C  CA  . GLY   A 174 ? 0.12421 0.14467 0.09975 -0.00670 -0.01174 0.00930  174 GLY   A CA  
1340 C  C   . GLY   A 174 ? 0.12789 0.15640 0.11699 -0.00534 -0.00952 0.01139  174 GLY   A C   
1341 O  O   . GLY   A 174 ? 0.11467 0.14725 0.10990 -0.00197 -0.00554 0.01022  174 GLY   A O   
1342 N  N   . THR   A 175 ? 0.11033 0.14086 0.10520 -0.00822 -0.01288 0.01473  175 THR   A N   
1343 C  CA  . THR   A 175 ? 0.11444 0.15256 0.12118 -0.00925 -0.01205 0.01646  175 THR   A CA  
1344 C  C   . THR   A 175 ? 0.11648 0.15350 0.12930 -0.01029 -0.01762 0.01456  175 THR   A C   
1345 O  O   . THR   A 175 ? 0.10205 0.13269 0.11175 -0.00990 -0.02101 0.01316  175 THR   A O   
1346 C  CB  . THR   A 175 ? 0.13832 0.17856 0.14655 -0.01323 -0.00969 0.02145  175 THR   A CB  
1347 O  OG1 . THR   A 175 ? 0.12362 0.15658 0.12941 -0.01604 -0.01411 0.02380  175 THR   A OG1 
1348 C  CG2 . THR   A 175 ? 0.12181 0.16318 0.12125 -0.01230 -0.00251 0.02307  175 THR   A CG2 
1349 N  N   . ASP   A 176 ? 0.12250 0.16652 0.14412 -0.01194 -0.01832 0.01453  176 ASP   A N   
1350 C  CA  . ASP   A 176 ? 0.10928 0.15058 0.13414 -0.01502 -0.02258 0.01208  176 ASP   A CA  
1351 C  C   . ASP   A 176 ? 0.10216 0.13753 0.12878 -0.01916 -0.02272 0.01447  176 ASP   A C   
1352 O  O   . ASP   A 176 ? 0.09357 0.12845 0.11800 -0.01969 -0.02004 0.01900  176 ASP   A O   
1353 C  CB  . ASP   A 176 ? 0.14039 0.19098 0.17157 -0.01702 -0.02466 0.01093  176 ASP   A CB  
1354 C  CG  . ASP   A 176 ? 0.15791 0.21859 0.19817 -0.02045 -0.02334 0.01494  176 ASP   A CG  
1355 O  OD1 . ASP   A 176 ? 0.12682 0.18534 0.16893 -0.02333 -0.02094 0.01787  176 ASP   A OD1 
1356 O  OD2 . ASP   A 176 ? 0.15079 0.22296 0.19773 -0.02071 -0.02512 0.01617  176 ASP   A OD2 
1357 N  N   . LEU   A 177 ? 0.12976 0.15937 0.15952 -0.02211 -0.02523 0.01152  177 LEU   A N   
1358 C  CA  . LEU   A 177 ? 0.13904 0.16018 0.17199 -0.02539 -0.02500 0.01441  177 LEU   A CA  
1359 C  C   . LEU   A 177 ? 0.19724 0.22274 0.23728 -0.03170 -0.02414 0.01707  177 LEU   A C   
1360 O  O   . LEU   A 177 ? 0.18899 0.20673 0.23313 -0.03547 -0.02369 0.02009  177 LEU   A O   
1361 C  CB  . LEU   A 177 ? 0.12572 0.13595 0.16042 -0.02533 -0.02641 0.00967  177 LEU   A CB  
1362 C  CG  . LEU   A 177 ? 0.15949 0.16348 0.19246 -0.01986 -0.02662 0.01138  177 LEU   A CG  
1363 C  CD1 . LEU   A 177 ? 0.11555 0.11559 0.14954 -0.02003 -0.02672 0.01982  177 LEU   A CD1 
1364 C  CD2 . LEU   A 177 ? 0.15336 0.16420 0.18017 -0.01551 -0.02716 0.01052  177 LEU   A CD2 
1365 N  N   . GLU   A 178 ? 0.14015 0.17822 0.18386 -0.03312 -0.02404 0.01688  178 GLU   A N   
1366 C  CA  . GLU   A 178 ? 0.16866 0.21441 0.22143 -0.03878 -0.02237 0.02163  178 GLU   A CA  
1367 C  C   . GLU   A 178 ? 0.12575 0.17821 0.17716 -0.03567 -0.01650 0.02812  178 GLU   A C   
1368 O  O   . GLU   A 178 ? 0.16606 0.22721 0.22596 -0.03951 -0.01333 0.03310  178 GLU   A O   
1369 C  CB  . GLU   A 178 ? 0.16727 0.22547 0.22811 -0.04293 -0.02585 0.01935  178 GLU   A CB  
1370 C  CG  . GLU   A 178 ? 0.21450 0.26686 0.27066 -0.04484 -0.03110 0.01139  178 GLU   A CG  
1371 C  CD  . GLU   A 178 ? 0.26507 0.30722 0.32419 -0.05337 -0.03345 0.00745  178 GLU   A CD  
1372 O  OE1 . GLU   A 178 ? 0.26541 0.30170 0.33027 -0.05686 -0.03094 0.01188  178 GLU   A OE1 
1373 O  OE2 . GLU   A 178 ? 0.34591 0.38452 0.40050 -0.05689 -0.03741 -0.00036 178 GLU   A OE2 
1374 N  N   . GLY   A 179 ? 0.15167 0.20019 0.19232 -0.02946 -0.01459 0.02782  179 GLY   A N   
1375 C  CA  . GLY   A 179 ? 0.13884 0.19072 0.17383 -0.02712 -0.00835 0.03227  179 GLY   A CA  
1376 C  C   . GLY   A 179 ? 0.13123 0.19369 0.16855 -0.02258 -0.00388 0.03112  179 GLY   A C   
1377 O  O   . GLY   A 179 ? 0.11949 0.18500 0.15260 -0.02056 0.00333  0.03373  179 GLY   A O   
1378 N  N   . ASN   A 180 ? 0.08923 0.15674 0.13254 -0.02056 -0.00736 0.02758  180 ASN   A N   
1379 C  CA  . ASN   A 180 ? 0.11672 0.19437 0.16581 -0.01544 -0.00329 0.02809  180 ASN   A CA  
1380 C  C   . ASN   A 180 ? 0.08923 0.15847 0.12714 -0.00934 -0.00251 0.02384  180 ASN   A C   
1381 O  O   . ASN   A 180 ? 0.08228 0.14506 0.11556 -0.00911 -0.00817 0.02034  180 ASN   A O   
1382 C  CB  . ASN   A 180 ? 0.08675 0.17652 0.14983 -0.01747 -0.00840 0.02895  180 ASN   A CB  
1383 C  CG  . ASN   A 180 ? 0.10243 0.19987 0.17683 -0.02531 -0.00986 0.03260  180 ASN   A CG  
1384 O  OD1 . ASN   A 180 ? 0.10954 0.21443 0.19119 -0.02605 -0.00348 0.03766  180 ASN   A OD1 
1385 N  ND2 . ASN   A 180 ? 0.15113 0.24551 0.22639 -0.03179 -0.01747 0.02960  180 ASN   A ND2 
1386 N  N   . PHE   A 181 ? 0.12222 0.19046 0.15511 -0.00505 0.00524  0.02375  181 PHE   A N   
1387 C  CA  . PHE   A 181 ? 0.11570 0.17402 0.13739 -0.00065 0.00612  0.01900  181 PHE   A CA  
1388 C  C   . PHE   A 181 ? 0.11531 0.17616 0.14456 0.00318  0.00291  0.01789  181 PHE   A C   
1389 O  O   . PHE   A 181 ? 0.08176 0.15421 0.12506 0.00501  0.00340  0.02145  181 PHE   A O   
1390 C  CB  . PHE   A 181 ? 0.15362 0.20938 0.16828 0.00301  0.01625  0.01761  181 PHE   A CB  
1391 C  CG  . PHE   A 181 ? 0.16626 0.21178 0.16198 -0.00009 0.01696  0.01556  181 PHE   A CG  
1392 C  CD1 . PHE   A 181 ? 0.16524 0.19926 0.14777 -0.00020 0.01280  0.01058  181 PHE   A CD1 
1393 C  CD2 . PHE   A 181 ? 0.16016 0.20852 0.15148 -0.00382 0.02083  0.01973  181 PHE   A CD2 
1394 C  CE1 . PHE   A 181 ? 0.15224 0.17884 0.11721 -0.00408 0.01145  0.00977  181 PHE   A CE1 
1395 C  CE2 . PHE   A 181 ? 0.19251 0.23265 0.16502 -0.00718 0.02034  0.01945  181 PHE   A CE2 
1396 C  CZ  . PHE   A 181 ? 0.21540 0.24512 0.17446 -0.00743 0.01501  0.01448  181 PHE   A CZ  
1397 N  N   . TYR   A 182 ? 0.09705 0.14806 0.11754 0.00402  -0.00065 0.01405  182 TYR   A N   
1398 C  CA  . TYR   A 182 ? 0.08537 0.13586 0.10996 0.00837  -0.00137 0.01341  182 TYR   A CA  
1399 C  C   . TYR   A 182 ? 0.13379 0.17935 0.15689 0.01375  0.00712  0.01175  182 TYR   A C   
1400 O  O   . TYR   A 182 ? 0.16308 0.19788 0.17297 0.01296  0.01025  0.00717  182 TYR   A O   
1401 C  CB  . TYR   A 182 ? 0.10630 0.14834 0.12341 0.00678  -0.00709 0.01038  182 TYR   A CB  
1402 C  CG  . TYR   A 182 ? 0.09889 0.14494 0.11876 0.00304  -0.01364 0.01109  182 TYR   A CG  
1403 C  CD1 . TYR   A 182 ? 0.11404 0.16730 0.14037 0.00358  -0.01673 0.01298  182 TYR   A CD1 
1404 C  CD2 . TYR   A 182 ? 0.11494 0.15641 0.12993 -0.00091 -0.01649 0.00978  182 TYR   A CD2 
1405 C  CE1 . TYR   A 182 ? 0.12897 0.18383 0.15445 -0.00034 -0.02170 0.01171  182 TYR   A CE1 
1406 C  CE2 . TYR   A 182 ? 0.07174 0.11410 0.08907 -0.00382 -0.02086 0.00897  182 TYR   A CE2 
1407 C  CZ  . TYR   A 182 ? 0.11280 0.16122 0.13405 -0.00378 -0.02302 0.00896  182 TYR   A CZ  
1408 O  OH  . TYR   A 182 ? 0.10719 0.15497 0.12780 -0.00711 -0.02628 0.00646  182 TYR   A OH  
1409 N  N   . GLY   A 183 ? 0.11069 0.16412 0.14739 0.01901  0.01088  0.01551  183 GLY   A N   
1410 C  CA  . GLY   A 183 ? 0.13554 0.18285 0.17367 0.02552  0.02038  0.01376  183 GLY   A CA  
1411 C  C   . GLY   A 183 ? 0.13981 0.18907 0.17676 0.02682  0.03044  0.01282  183 GLY   A C   
1412 O  O   . GLY   A 183 ? 0.12567 0.18254 0.16204 0.02234  0.02982  0.01499  183 GLY   A O   
1413 N  N   . PRO   A 184 ? 0.13702 0.17846 0.17355 0.03298  0.04092  0.00952  184 PRO   A N   
1414 C  CA  . PRO   A 184 ? 0.17037 0.21562 0.20897 0.03616  0.05356  0.00919  184 PRO   A CA  
1415 C  C   . PRO   A 184 ? 0.22143 0.25457 0.23506 0.03120  0.05785  0.00173  184 PRO   A C   
1416 O  O   . PRO   A 184 ? 0.24446 0.26637 0.24747 0.03436  0.06909  -0.00500 184 PRO   A O   
1417 C  CB  . PRO   A 184 ? 0.18686 0.22720 0.23719 0.04605  0.06343  0.00856  184 PRO   A CB  
1418 C  CG  . PRO   A 184 ? 0.17414 0.19767 0.21446 0.04522  0.05750  0.00359  184 PRO   A CG  
1419 C  CD  . PRO   A 184 ? 0.18126 0.21032 0.21849 0.03799  0.04270  0.00668  184 PRO   A CD  
1420 N  N   . PHE   A 185 ? 0.19232 0.22728 0.19595 0.02332  0.04895  0.00303  185 PHE   A N   
1421 C  CA  . PHE   A 185 ? 0.21566 0.24063 0.19503 0.01748  0.04936  -0.00178 185 PHE   A CA  
1422 C  C   . PHE   A 185 ? 0.25819 0.29396 0.23764 0.01284  0.04982  0.00446  185 PHE   A C   
1423 O  O   . PHE   A 185 ? 0.22847 0.27689 0.22486 0.01153  0.04491  0.01139  185 PHE   A O   
1424 C  CB  . PHE   A 185 ? 0.23761 0.25269 0.20501 0.01234  0.03731  -0.00490 185 PHE   A CB  
1425 C  CG  . PHE   A 185 ? 0.18899 0.19473 0.15959 0.01583  0.03591  -0.00930 185 PHE   A CG  
1426 C  CD1 . PHE   A 185 ? 0.22573 0.21821 0.18745 0.01889  0.04486  -0.01692 185 PHE   A CD1 
1427 C  CD2 . PHE   A 185 ? 0.20975 0.21889 0.19165 0.01579  0.02660  -0.00596 185 PHE   A CD2 
1428 C  CE1 . PHE   A 185 ? 0.22379 0.20611 0.19008 0.02180  0.04405  -0.02024 185 PHE   A CE1 
1429 C  CE2 . PHE   A 185 ? 0.19656 0.19731 0.18173 0.01861  0.02593  -0.00854 185 PHE   A CE2 
1430 C  CZ  . PHE   A 185 ? 0.19993 0.18693 0.17828 0.02161  0.03453  -0.01531 185 PHE   A CZ  
1431 N  N   . VAL   A 186 ? 0.23923 0.26945 0.19883 0.00972  0.05597  0.00201  186 VAL   A N   
1432 C  CA  . VAL   A 186 ? 0.25902 0.29819 0.21696 0.00525  0.05855  0.00881  186 VAL   A CA  
1433 C  C   . VAL   A 186 ? 0.28230 0.31227 0.21492 -0.00185 0.05260  0.00807  186 VAL   A C   
1434 O  O   . VAL   A 186 ? 0.27185 0.28936 0.18539 -0.00298 0.05086  0.00068  186 VAL   A O   
1435 C  CB  . VAL   A 186 ? 0.28274 0.32830 0.24354 0.00936  0.07535  0.00925  186 VAL   A CB  
1436 C  CG1 . VAL   A 186 ? 0.27733 0.33650 0.26878 0.01618  0.07931  0.01331  186 VAL   A CG1 
1437 C  CG2 . VAL   A 186 ? 0.28753 0.31825 0.22608 0.01205  0.08546  -0.00125 186 VAL   A CG2 
1438 N  N   . ASP   A 187 ? 0.26048 0.29670 0.19388 -0.00715 0.04867  0.01644  187 ASP   A N   
1439 C  CA  . ASP   A 187 ? 0.30657 0.33581 0.21872 -0.01355 0.04144  0.01853  187 ASP   A CA  
1440 C  C   . ASP   A 187 ? 0.33513 0.36348 0.22535 -0.01628 0.05195  0.01937  187 ASP   A C   
1441 O  O   . ASP   A 187 ? 0.32072 0.35337 0.20577 -0.02107 0.05195  0.02828  187 ASP   A O   
1442 C  CB  . ASP   A 187 ? 0.27571 0.30905 0.19960 -0.01752 0.03087  0.02750  187 ASP   A CB  
1443 C  CG  . ASP   A 187 ? 0.25577 0.30016 0.19755 -0.01849 0.03600  0.03521  187 ASP   A CG  
1444 O  OD1 . ASP   A 187 ? 0.22834 0.28063 0.17903 -0.01525 0.04690  0.03446  187 ASP   A OD1 
1445 O  OD2 . ASP   A 187 ? 0.23540 0.28048 0.18410 -0.02267 0.02900  0.04237  187 ASP   A OD2 
1446 N  N   . ARG   A 188 ? 0.35090 0.37266 0.22802 -0.01302 0.06207  0.00976  188 ARG   A N   
1447 C  CA  . ARG   A 188 ? 0.42491 0.44160 0.27314 -0.01610 0.07188  0.00667  188 ARG   A CA  
1448 C  C   . ARG   A 188 ? 0.46655 0.46805 0.29481 -0.01566 0.07244  -0.00692 188 ARG   A C   
1449 O  O   . ARG   A 188 ? 0.42255 0.41892 0.26350 -0.01186 0.06770  -0.01263 188 ARG   A O   
1450 C  CB  . ARG   A 188 ? 0.44402 0.46909 0.29831 -0.01206 0.09049  0.00811  188 ARG   A CB  
1451 C  CG  . ARG   A 188 ? 0.42307 0.45511 0.30793 -0.00342 0.09690  0.00648  188 ARG   A CG  
1452 C  CD  . ARG   A 188 ? 0.43312 0.48016 0.33438 -0.00048 0.11166  0.01323  188 ARG   A CD  
1453 N  NE  . ARG   A 188 ? 0.44643 0.49602 0.36697 0.00928  0.12260  0.00791  188 ARG   A NE  
1454 C  CZ  . ARG   A 188 ? 0.45232 0.51523 0.40674 0.01391  0.12014  0.01362  188 ARG   A CZ  
1455 N  NH1 . ARG   A 188 ? 0.46035 0.53413 0.43164 0.00900  0.10797  0.02303  188 ARG   A NH1 
1456 N  NH2 . ARG   A 188 ? 0.47114 0.53567 0.44257 0.02346  0.12949  0.00971  188 ARG   A NH2 
1457 N  N   . GLN   A 189 ? 0.50719 0.50086 0.30315 -0.02021 0.07866  -0.01229 189 GLN   A N   
1458 C  CA  . GLN   A 189 ? 0.55925 0.53795 0.33786 -0.02071 0.07704  -0.02586 189 GLN   A CA  
1459 C  C   . GLN   A 189 ? 0.53340 0.50783 0.31768 -0.01245 0.09470  -0.03534 189 GLN   A C   
1460 O  O   . GLN   A 189 ? 0.60260 0.57934 0.37678 -0.01125 0.10509  -0.03692 189 GLN   A O   
1461 C  CB  . GLN   A 189 ? 0.63242 0.60800 0.38504 -0.02787 0.06794  -0.02581 189 GLN   A CB  
1462 C  CG  . GLN   A 189 ? 0.67795 0.63909 0.41487 -0.03010 0.06427  -0.03949 189 GLN   A CG  
1463 C  CD  . GLN   A 189 ? 0.85691 0.81751 0.57845 -0.03876 0.04662  -0.03634 189 GLN   A CD  
1464 O  OE1 . GLN   A 189 ? 0.86046 0.83087 0.58384 -0.04190 0.03760  -0.02354 189 GLN   A OE1 
1465 N  NE2 . GLN   A 189 ? 0.90385 0.85328 0.61266 -0.04255 0.04172  -0.04731 189 GLN   A NE2 
1466 N  N   . THR   A 190 ? 0.46238 0.43152 0.26509 -0.00609 0.09810  -0.04048 190 THR   A N   
1467 C  CA  . THR   A 190 ? 0.48893 0.45206 0.30241 0.00289  0.11226  -0.04912 190 THR   A CA  
1468 C  C   . THR   A 190 ? 0.48503 0.42973 0.29282 0.00241  0.10675  -0.06061 190 THR   A C   
1469 O  O   . THR   A 190 ? 0.49824 0.43696 0.29409 -0.00524 0.09210  -0.06181 190 THR   A O   
1470 C  CB  . THR   A 190 ? 0.44517 0.42098 0.29299 0.01237  0.12099  -0.04167 190 THR   A CB  
1471 O  OG1 . THR   A 190 ? 0.46169 0.43472 0.32886 0.01539  0.11099  -0.04123 190 THR   A OG1 
1472 C  CG2 . THR   A 190 ? 0.44783 0.44300 0.30663 0.00960  0.11837  -0.02748 190 THR   A CG2 
1473 N  N   . ALA   A 191 ? 0.51811 0.45448 0.33726 0.01054  0.11811  -0.06806 191 ALA   A N   
1474 C  CA  . ALA   A 191 ? 0.51230 0.43044 0.33066 0.01066  0.11422  -0.07782 191 ALA   A CA  
1475 C  C   . ALA   A 191 ? 0.49133 0.41065 0.33563 0.01613  0.11037  -0.07295 191 ALA   A C   
1476 O  O   . ALA   A 191 ? 0.51641 0.42296 0.37084 0.02057  0.11250  -0.07851 191 ALA   A O   
1477 C  CB  . ALA   A 191 ? 0.51800 0.42398 0.33533 0.01642  0.12788  -0.08789 191 ALA   A CB  
1478 N  N   . GLN   A 192 ? 0.43255 0.36884 0.29128 0.01573  0.10223  -0.06092 192 GLN   A N   
1479 C  CA  . GLN   A 192 ? 0.39721 0.34104 0.28638 0.02081  0.09384  -0.05319 192 GLN   A CA  
1480 C  C   . GLN   A 192 ? 0.43913 0.36856 0.32281 0.01627  0.08272  -0.05881 192 GLN   A C   
1481 O  O   . GLN   A 192 ? 0.45727 0.37918 0.31800 0.00654  0.07374  -0.06375 192 GLN   A O   
1482 C  CB  . GLN   A 192 ? 0.37092 0.33551 0.27482 0.01836  0.08203  -0.03991 192 GLN   A CB  
1483 C  CG  . GLN   A 192 ? 0.39036 0.35834 0.27300 0.00880  0.07427  -0.03769 192 GLN   A CG  
1484 C  CD  . GLN   A 192 ? 0.35234 0.33879 0.25151 0.00754  0.06640  -0.02503 192 GLN   A CD  
1485 O  OE1 . GLN   A 192 ? 0.30131 0.29866 0.22655 0.01281  0.06569  -0.01874 192 GLN   A OE1 
1486 N  NE2 . GLN   A 192 ? 0.33350 0.32327 0.21726 0.00019  0.06062  -0.02094 192 GLN   A NE2 
1487 N  N   . ALA   A 193 ? 0.36330 0.29082 0.26986 0.02295  0.08247  -0.05641 193 ALA   A N   
1488 C  CA  . ALA   A 193 ? 0.36320 0.27765 0.26877 0.01924  0.07344  -0.06035 193 ALA   A CA  
1489 C  C   . ALA   A 193 ? 0.34312 0.26939 0.27698 0.02427  0.06613  -0.04924 193 ALA   A C   
1490 O  O   . ALA   A 193 ? 0.35265 0.29288 0.30719 0.03208  0.07067  -0.04088 193 ALA   A O   
1491 C  CB  . ALA   A 193 ? 0.40624 0.29629 0.30340 0.02153  0.08473  -0.07297 193 ALA   A CB  
1492 N  N   . ALA   A 194 ? 0.32230 0.24345 0.25645 0.01912  0.05477  -0.04909 194 ALA   A N   
1493 C  CA  . ALA   A 194 ? 0.34146 0.27471 0.29722 0.02177  0.04635  -0.03853 194 ALA   A CA  
1494 C  C   . ALA   A 194 ? 0.38217 0.31637 0.36036 0.03243  0.05439  -0.03324 194 ALA   A C   
1495 O  O   . ALA   A 194 ? 0.42710 0.37853 0.42342 0.03670  0.05107  -0.02272 194 ALA   A O   
1496 C  CB  . ALA   A 194 ? 0.31680 0.24267 0.26850 0.01453  0.03546  -0.04010 194 ALA   A CB  
1497 N  N   . GLY   A 195 ? 0.39757 0.31343 0.37531 0.03664  0.06454  -0.03996 195 GLY   A N   
1498 C  CA  . GLY   A 195 ? 0.40938 0.32977 0.41295 0.04685  0.06865  -0.03074 195 GLY   A CA  
1499 C  C   . GLY   A 195 ? 0.39927 0.31511 0.41095 0.04492  0.05990  -0.02577 195 GLY   A C   
1500 O  O   . GLY   A 195 ? 0.35146 0.27067 0.35533 0.03656  0.04845  -0.02527 195 GLY   A O   
1501 N  N   . THR   A 196 ? 0.36721 0.27551 0.39627 0.05326  0.06619  -0.02105 196 THR   A N   
1502 C  CA  . THR   A 196 ? 0.37376 0.27153 0.40781 0.05091  0.06079  -0.01788 196 THR   A CA  
1503 C  C   . THR   A 196 ? 0.33497 0.25255 0.37564 0.04762  0.04774  -0.00647 196 THR   A C   
1504 O  O   . THR   A 196 ? 0.29637 0.23485 0.34733 0.05147  0.04477  0.00264  196 THR   A O   
1505 C  CB  . THR   A 196 ? 0.39495 0.28084 0.44814 0.06143  0.07060  -0.01295 196 THR   A CB  
1506 O  OG1 . THR   A 196 ? 0.44375 0.35131 0.51846 0.07079  0.07072  0.00113  196 THR   A OG1 
1507 C  CG2 . THR   A 196 ? 0.39211 0.25745 0.43769 0.06455  0.08472  -0.02575 196 THR   A CG2 
1508 N  N   . ASP   A 197 ? 0.32470 0.23575 0.35875 0.03967  0.04020  -0.00773 197 ASP   A N   
1509 C  CA  . ASP   A 197 ? 0.31998 0.24716 0.35819 0.03617  0.02959  0.00150  197 ASP   A CA  
1510 C  C   . ASP   A 197 ? 0.33909 0.26232 0.39128 0.03950  0.02944  0.01157  197 ASP   A C   
1511 O  O   . ASP   A 197 ? 0.34560 0.25004 0.40309 0.04245  0.03627  0.01012  197 ASP   A O   
1512 C  CB  . ASP   A 197 ? 0.30726 0.23329 0.33107 0.02533  0.02165  -0.00489 197 ASP   A CB  
1513 C  CG  . ASP   A 197 ? 0.29305 0.23942 0.31738 0.02266  0.01297  0.00124  197 ASP   A CG  
1514 O  OD1 . ASP   A 197 ? 0.27611 0.23767 0.30798 0.02771  0.01252  0.00823  197 ASP   A OD1 
1515 O  OD2 . ASP   A 197 ? 0.28323 0.23032 0.30098 0.01523  0.00669  -0.00125 197 ASP   A OD2 
1516 N  N   . THR   A 198 ? 0.28680 0.22702 0.34385 0.03862  0.02195  0.02177  198 THR   A N   
1517 C  CA  . THR   A 198 ? 0.27985 0.21921 0.34657 0.03975  0.02021  0.03275  198 THR   A CA  
1518 C  C   . THR   A 198 ? 0.29467 0.24151 0.35374 0.03118  0.01245  0.03353  198 THR   A C   
1519 O  O   . THR   A 198 ? 0.25837 0.21378 0.30766 0.02617  0.00799  0.02741  198 THR   A O   
1520 C  CB  . THR   A 198 ? 0.30201 0.25719 0.38252 0.04801  0.01951  0.04670  198 THR   A CB  
1521 O  OG1 . THR   A 198 ? 0.29599 0.27225 0.37226 0.04669  0.01379  0.04721  198 THR   A OG1 
1522 C  CG2 . THR   A 198 ? 0.33717 0.28431 0.43063 0.05780  0.02846  0.04814  198 THR   A CG2 
1523 N  N   . THR   A 199 ? 0.27025 0.21360 0.33500 0.02984  0.01170  0.04182  199 THR   A N   
1524 C  CA  . THR   A 199 ? 0.25545 0.20762 0.31524 0.02273  0.00618  0.04415  199 THR   A CA  
1525 C  C   . THR   A 199 ? 0.23706 0.20967 0.29705 0.02527  0.00219  0.05410  199 THR   A C   
1526 O  O   . THR   A 199 ? 0.24833 0.22553 0.31604 0.03150  0.00296  0.06450  199 THR   A O   
1527 C  CB  . THR   A 199 ? 0.28992 0.22878 0.35511 0.01869  0.00807  0.04825  199 THR   A CB  
1528 O  OG1 . THR   A 199 ? 0.29947 0.21890 0.36229 0.01416  0.01057  0.03703  199 THR   A OG1 
1529 C  CG2 . THR   A 199 ? 0.27097 0.22111 0.33322 0.01222  0.00409  0.05193  199 THR   A CG2 
1530 N  N   . ILE   A 200 ? 0.19701 0.18177 0.24852 0.02036  -0.00220 0.05089  200 ILE   A N   
1531 C  CA  . ILE   A 200 ? 0.19275 0.19562 0.24065 0.02133  -0.00601 0.05726  200 ILE   A CA  
1532 C  C   . ILE   A 200 ? 0.20238 0.20830 0.25082 0.01982  -0.00579 0.06804  200 ILE   A C   
1533 O  O   . ILE   A 200 ? 0.18877 0.19648 0.23270 0.01451  -0.00559 0.06656  200 ILE   A O   
1534 C  CB  . ILE   A 200 ? 0.18887 0.20092 0.22760 0.01717  -0.00932 0.04890  200 ILE   A CB  
1535 C  CG1 . ILE   A 200 ? 0.17806 0.18522 0.21571 0.01773  -0.00897 0.03925  200 ILE   A CG1 
1536 C  CG2 . ILE   A 200 ? 0.17590 0.20431 0.20955 0.01766  -0.01305 0.05357  200 ILE   A CG2 
1537 C  CD1 . ILE   A 200 ? 0.15314 0.16223 0.18397 0.01271  -0.01136 0.03072  200 ILE   A CD1 
1538 N  N   . THR   A 201 ? 0.20421 0.21210 0.25897 0.02481  -0.00556 0.08010  201 THR   A N   
1539 C  CA  . THR   A 201 ? 0.20883 0.21701 0.26487 0.02376  -0.00451 0.09258  201 THR   A CA  
1540 C  C   . THR   A 201 ? 0.19984 0.22285 0.24306 0.01884  -0.00689 0.09444  201 THR   A C   
1541 O  O   . THR   A 201 ? 0.19223 0.21341 0.23341 0.01455  -0.00394 0.09761  201 THR   A O   
1542 C  CB  . THR   A 201 ? 0.21728 0.22741 0.28255 0.03061  -0.00494 0.10599  201 THR   A CB  
1543 O  OG1 . THR   A 201 ? 0.22377 0.21901 0.30103 0.03586  -0.00071 0.10204  201 THR   A OG1 
1544 C  CG2 . THR   A 201 ? 0.24039 0.24923 0.30623 0.02843  -0.00304 0.11649  201 THR   A CG2 
1545 N  N   . VAL   A 202 ? 0.16894 0.20634 0.20344 0.01893  -0.01150 0.09205  202 VAL   A N   
1546 C  CA  . VAL   A 202 ? 0.16205 0.21159 0.18220 0.01426  -0.01267 0.09301  202 VAL   A CA  
1547 C  C   . VAL   A 202 ? 0.14306 0.18840 0.15983 0.00948  -0.00859 0.08278  202 VAL   A C   
1548 O  O   . VAL   A 202 ? 0.18330 0.23321 0.19299 0.00598  -0.00538 0.08552  202 VAL   A O   
1549 C  CB  . VAL   A 202 ? 0.20201 0.26591 0.21270 0.01382  -0.01877 0.09059  202 VAL   A CB  
1550 C  CG1 . VAL   A 202 ? 0.20158 0.26328 0.21400 0.01364  -0.01983 0.07701  202 VAL   A CG1 
1551 C  CG2 . VAL   A 202 ? 0.19411 0.26831 0.18707 0.00857  -0.01903 0.09097  202 VAL   A CG2 
1552 N  N   . ASN   A 203 ? 0.17116 0.20853 0.19369 0.00941  -0.00830 0.07197  203 ASN   A N   
1553 C  CA  . ASN   A 203 ? 0.15929 0.19424 0.18187 0.00531  -0.00564 0.06360  203 ASN   A CA  
1554 C  C   . ASN   A 203 ? 0.16808 0.19603 0.19857 0.00246  -0.00142 0.06876  203 ASN   A C   
1555 O  O   . ASN   A 203 ? 0.15859 0.19112 0.18857 -0.00115 0.00199  0.06819  203 ASN   A O   
1556 C  CB  . ASN   A 203 ? 0.15924 0.18806 0.18549 0.00557  -0.00768 0.05280  203 ASN   A CB  
1557 C  CG  . ASN   A 203 ? 0.15071 0.18718 0.16978 0.00645  -0.01088 0.04652  203 ASN   A CG  
1558 O  OD1 . ASN   A 203 ? 0.14283 0.18876 0.15385 0.00643  -0.01224 0.04916  203 ASN   A OD1 
1559 N  ND2 . ASN   A 203 ? 0.11647 0.14860 0.13761 0.00636  -0.01235 0.03840  203 ASN   A ND2 
1560 N  N   . VAL   A 204 ? 0.16982 0.18600 0.20923 0.00385  -0.00095 0.07325  204 VAL   A N   
1561 C  CA  . VAL   A 204 ? 0.17317 0.18125 0.22112 0.00011  0.00282  0.07902  204 VAL   A CA  
1562 C  C   . VAL   A 204 ? 0.18150 0.19933 0.22484 -0.00137 0.00619  0.09020  204 VAL   A C   
1563 O  O   . VAL   A 204 ? 0.17231 0.19232 0.21913 -0.00618 0.01024  0.09177  204 VAL   A O   
1564 C  CB  . VAL   A 204 ? 0.17708 0.16879 0.23437 0.00251  0.00356  0.08272  204 VAL   A CB  
1565 C  CG1 . VAL   A 204 ? 0.20891 0.19128 0.27544 -0.00240 0.00742  0.08966  204 VAL   A CG1 
1566 C  CG2 . VAL   A 204 ? 0.17702 0.15832 0.23598 0.00276  0.00171  0.06996  204 VAL   A CG2 
1567 N  N   . LEU   A 205 ? 0.15996 0.18512 0.19539 0.00237  0.00453  0.09868  205 LEU   A N   
1568 C  CA  . LEU   A 205 ? 0.19430 0.22953 0.22106 0.00049  0.00748  0.10972  205 LEU   A CA  
1569 C  C   . LEU   A 205 ? 0.19119 0.23732 0.20776 -0.00307 0.01066  0.10212  205 LEU   A C   
1570 O  O   . LEU   A 205 ? 0.17754 0.22778 0.19304 -0.00665 0.01686  0.10717  205 LEU   A O   
1571 C  CB  . LEU   A 205 ? 0.17301 0.21634 0.19123 0.00450  0.00292  0.11954  205 LEU   A CB  
1572 C  CG  . LEU   A 205 ? 0.18090 0.21469 0.21179 0.00923  0.00127  0.12760  205 LEU   A CG  
1573 C  CD1 . LEU   A 205 ? 0.19529 0.24018 0.22070 0.01289  -0.00461 0.13081  205 LEU   A CD1 
1574 C  CD2 . LEU   A 205 ? 0.23082 0.25744 0.26842 0.00704  0.00611  0.13661  205 LEU   A CD2 
1575 N  N   . ALA   A 206 ? 0.17624 0.22649 0.18667 -0.00196 0.00750  0.09008  206 ALA   A N   
1576 C  CA  . ALA   A 206 ? 0.15925 0.21741 0.16188 -0.00436 0.01154  0.08190  206 ALA   A CA  
1577 C  C   . ALA   A 206 ? 0.15333 0.20889 0.16919 -0.00736 0.01712  0.07983  206 ALA   A C   
1578 O  O   . ALA   A 206 ? 0.16808 0.23105 0.18122 -0.00948 0.02417  0.08078  206 ALA   A O   
1579 C  CB  . ALA   A 206 ? 0.16341 0.22277 0.16135 -0.00271 0.00707  0.06944  206 ALA   A CB  
1580 N  N   . TRP   A 207 ? 0.15143 0.19718 0.18171 -0.00792 0.01413  0.07688  207 TRP   A N   
1581 C  CA  . TRP   A 207 ? 0.18455 0.22896 0.22930 -0.01194 0.01699  0.07493  207 TRP   A CA  
1582 C  C   . TRP   A 207 ? 0.19190 0.23643 0.24345 -0.01573 0.02275  0.08672  207 TRP   A C   
1583 O  O   . TRP   A 207 ? 0.19026 0.24151 0.25059 -0.01931 0.02832  0.08797  207 TRP   A O   
1584 C  CB  . TRP   A 207 ? 0.17280 0.20594 0.22676 -0.01262 0.01079  0.06825  207 TRP   A CB  
1585 C  CG  . TRP   A 207 ? 0.16854 0.19811 0.23805 -0.01836 0.01067  0.06720  207 TRP   A CG  
1586 C  CD1 . TRP   A 207 ? 0.17471 0.21135 0.25278 -0.02086 0.01014  0.06185  207 TRP   A CD1 
1587 C  CD2 . TRP   A 207 ? 0.17956 0.19717 0.25873 -0.02274 0.01001  0.07150  207 TRP   A CD2 
1588 N  NE1 . TRP   A 207 ? 0.17892 0.21102 0.27146 -0.02744 0.00826  0.06310  207 TRP   A NE1 
1589 C  CE2 . TRP   A 207 ? 0.16961 0.18879 0.26220 -0.02920 0.00839  0.06818  207 TRP   A CE2 
1590 C  CE3 . TRP   A 207 ? 0.20245 0.20780 0.28147 -0.02192 0.01072  0.07836  207 TRP   A CE3 
1591 C  CZ2 . TRP   A 207 ? 0.22334 0.23152 0.32724 -0.03619 0.00690  0.07005  207 TRP   A CZ2 
1592 C  CZ3 . TRP   A 207 ? 0.22450 0.21686 0.31536 -0.02787 0.01062  0.08020  207 TRP   A CZ3 
1593 C  CH2 . TRP   A 207 ? 0.20211 0.19557 0.30429 -0.03558 0.00847  0.07535  207 TRP   A CH2 
1594 N  N   . LEU   A 208 ? 0.17758 0.21550 0.22677 -0.01477 0.02197  0.09666  208 LEU   A N   
1595 C  CA  . LEU   A 208 ? 0.18314 0.22140 0.23694 -0.01829 0.02797  0.11010  208 LEU   A CA  
1596 C  C   . LEU   A 208 ? 0.18834 0.24181 0.23025 -0.01896 0.03532  0.11425  208 LEU   A C   
1597 O  O   . LEU   A 208 ? 0.19671 0.25523 0.24597 -0.02322 0.04283  0.12036  208 LEU   A O   
1598 C  CB  . LEU   A 208 ? 0.19064 0.21943 0.24322 -0.01568 0.02563  0.12137  208 LEU   A CB  
1599 C  CG  . LEU   A 208 ? 0.21395 0.22433 0.28037 -0.01577 0.02188  0.11871  208 LEU   A CG  
1600 C  CD1 . LEU   A 208 ? 0.21740 0.21908 0.28408 -0.01127 0.02076  0.12963  208 LEU   A CD1 
1601 C  CD2 . LEU   A 208 ? 0.21020 0.21363 0.29288 -0.02356 0.02488  0.11853  208 LEU   A CD2 
1602 N  N   . TYR   A 209 ? 0.21271 0.27362 0.23594 -0.01536 0.03375  0.11033  209 TYR   A N   
1603 C  CA  . TYR   A 209 ? 0.20244 0.27618 0.21101 -0.01632 0.04146  0.11051  209 TYR   A CA  
1604 C  C   . TYR   A 209 ? 0.21913 0.29825 0.23743 -0.01743 0.04776  0.10074  209 TYR   A C   
1605 O  O   . TYR   A 209 ? 0.20828 0.29613 0.22594 -0.01948 0.05796  0.10433  209 TYR   A O   
1606 C  CB  . TYR   A 209 ? 0.19678 0.27552 0.18311 -0.01357 0.03714  0.10579  209 TYR   A CB  
1607 C  CG  . TYR   A 209 ? 0.22379 0.30424 0.19763 -0.01320 0.03330  0.11903  209 TYR   A CG  
1608 C  CD1 . TYR   A 209 ? 0.27564 0.35969 0.23980 -0.01538 0.03824  0.12575  209 TYR   A CD1 
1609 C  CD2 . TYR   A 209 ? 0.23872 0.31482 0.21329 -0.00978 0.02327  0.12061  209 TYR   A CD2 
1610 C  CE1 . TYR   A 209 ? 0.27953 0.36336 0.23488 -0.01452 0.03262  0.13440  209 TYR   A CE1 
1611 C  CE2 . TYR   A 209 ? 0.26439 0.34119 0.23287 -0.00836 0.01812  0.12871  209 TYR   A CE2 
1612 C  CZ  . TYR   A 209 ? 0.30707 0.38789 0.26584 -0.01089 0.02239  0.13587  209 TYR   A CZ  
1613 O  OH  . TYR   A 209 ? 0.30043 0.38286 0.25422 -0.00961 0.01679  0.14504  209 TYR   A OH  
1614 N  N   . ALA   A 210 ? 0.18825 0.26323 0.21588 -0.01570 0.04230  0.08915  210 ALA   A N   
1615 C  CA  . ALA   A 210 ? 0.18431 0.26490 0.22574 -0.01625 0.04708  0.08214  210 ALA   A CA  
1616 C  C   . ALA   A 210 ? 0.21786 0.30118 0.27928 -0.02112 0.05215  0.09069  210 ALA   A C   
1617 O  O   . ALA   A 210 ? 0.20138 0.29518 0.27202 -0.02198 0.06104  0.09094  210 ALA   A O   
1618 C  CB  . ALA   A 210 ? 0.19741 0.27224 0.24727 -0.01444 0.03855  0.07155  210 ALA   A CB  
1619 N  N   . ALA   A 211 ? 0.19147 0.26503 0.26148 -0.02445 0.04691  0.09746  211 ALA   A N   
1620 C  CA  . ALA   A 211 ? 0.20743 0.28171 0.29736 -0.03075 0.05052  0.10564  211 ALA   A CA  
1621 C  C   . ALA   A 211 ? 0.21845 0.30144 0.30312 -0.03208 0.06138  0.11558  211 ALA   A C   
1622 O  O   . ALA   A 211 ? 0.20201 0.29311 0.29899 -0.03444 0.06756  0.11570  211 ALA   A O   
1623 C  CB  . ALA   A 211 ? 0.17999 0.23811 0.27652 -0.03394 0.04327  0.10975  211 ALA   A CB  
1624 N  N   . VAL   A 212 ? 0.21344 0.29374 0.27759 -0.02972 0.06186  0.12141  212 VAL   A N   
1625 C  CA  . VAL   A 212 ? 0.22377 0.30994 0.27698 -0.03055 0.07010  0.12798  212 VAL   A CA  
1626 C  C   . VAL   A 212 ? 0.23571 0.33505 0.28317 -0.02901 0.08015  0.12103  212 VAL   A C   
1627 O  O   . VAL   A 212 ? 0.24023 0.34598 0.29267 -0.03128 0.08908  0.12382  212 VAL   A O   
1628 C  CB  . VAL   A 212 ? 0.22717 0.30932 0.25777 -0.02815 0.06656  0.13448  212 VAL   A CB  
1629 C  CG1 . VAL   A 212 ? 0.26319 0.35229 0.27906 -0.02968 0.07519  0.14023  212 VAL   A CG1 
1630 C  CG2 . VAL   A 212 ? 0.22842 0.29667 0.26860 -0.02871 0.05882  0.14230  212 VAL   A CG2 
1631 N  N   . ILE   A 213 ? 0.24375 0.34663 0.28101 -0.02496 0.07951  0.11148  213 ILE   A N   
1632 C  CA  . ILE   A 213 ? 0.24370 0.35635 0.27598 -0.02255 0.08993  0.10294  213 ILE   A CA  
1633 C  C   . ILE   A 213 ? 0.24893 0.36766 0.30947 -0.02366 0.09461  0.10129  213 ILE   A C   
1634 O  O   . ILE   A 213 ? 0.26540 0.39211 0.32757 -0.02316 0.10566  0.09943  213 ILE   A O   
1635 C  CB  . ILE   A 213 ? 0.29279 0.40564 0.31175 -0.01801 0.08717  0.09186  213 ILE   A CB  
1636 C  CG1 . ILE   A 213 ? 0.26545 0.37518 0.25359 -0.01783 0.08272  0.09319  213 ILE   A CG1 
1637 C  CG2 . ILE   A 213 ? 0.28766 0.40787 0.30892 -0.01452 0.09827  0.08135  213 ILE   A CG2 
1638 C  CD1 . ILE   A 213 ? 0.27182 0.37569 0.24770 -0.01467 0.07345  0.08056  213 ILE   A CD1 
1639 N  N   . ASN   A 214 ? 0.22280 0.33763 0.30567 -0.02593 0.08577  0.10237  214 ASN   A N   
1640 C  CA  . ASN   A 214 ? 0.22251 0.34332 0.33308 -0.02776 0.08601  0.10064  214 ASN   A CA  
1641 C  C   . ASN   A 214 ? 0.24888 0.36853 0.37376 -0.03420 0.08581  0.10970  214 ASN   A C   
1642 O  O   . ASN   A 214 ? 0.26309 0.38687 0.41134 -0.03729 0.08294  0.10923  214 ASN   A O   
1643 C  CB  . ASN   A 214 ? 0.25725 0.37468 0.38092 -0.02732 0.07508  0.09458  214 ASN   A CB  
1644 C  CG  . ASN   A 214 ? 0.26130 0.38382 0.38074 -0.02057 0.07770  0.08451  214 ASN   A CG  
1645 O  OD1 . ASN   A 214 ? 0.30548 0.43688 0.43646 -0.01757 0.08445  0.08079  214 ASN   A OD1 
1646 N  ND2 . ASN   A 214 ? 0.28389 0.39574 0.38271 -0.01725 0.07012  0.07699  214 ASN   A ND2 
1647 N  N   . GLY   A 215 ? 0.23806 0.35239 0.34930 -0.03643 0.08825  0.11817  215 GLY   A N   
1648 C  CA  . GLY   A 215 ? 0.24208 0.35628 0.36502 -0.04217 0.09092  0.12708  215 GLY   A CA  
1649 C  C   . GLY   A 215 ? 0.25615 0.35663 0.38859 -0.04738 0.08112  0.13216  215 GLY   A C   
1650 O  O   . GLY   A 215 ? 0.25304 0.35186 0.39450 -0.05257 0.08340  0.13983  215 GLY   A O   
1651 N  N   . ASP   A 216 ? 0.23386 0.32380 0.36518 -0.04647 0.07096  0.12756  216 ASP   A N   
1652 C  CA  . ASP   A 216 ? 0.25471 0.32808 0.39073 -0.05053 0.06297  0.13109  216 ASP   A CA  
1653 C  C   . ASP   A 216 ? 0.29019 0.35575 0.40739 -0.04759 0.06445  0.13936  216 ASP   A C   
1654 O  O   . ASP   A 216 ? 0.29744 0.36219 0.39743 -0.04207 0.06252  0.13769  216 ASP   A O   
1655 C  CB  . ASP   A 216 ? 0.28151 0.34539 0.42138 -0.05046 0.05249  0.12255  216 ASP   A CB  
1656 C  CG  . ASP   A 216 ? 0.30465 0.37608 0.46247 -0.05375 0.04848  0.11481  216 ASP   A CG  
1657 O  OD1 . ASP   A 216 ? 0.38488 0.46775 0.55566 -0.05649 0.05324  0.11698  216 ASP   A OD1 
1658 O  OD2 . ASP   A 216 ? 0.28957 0.35612 0.44853 -0.05349 0.04027  0.10698  216 ASP   A OD2 
1659 N  N   . ARG   A 217 ? 0.27837 0.33844 0.39948 -0.05140 0.06701  0.14866  217 ARG   A N   
1660 C  CA  . ARG   A 217 ? 0.27824 0.33194 0.38357 -0.04863 0.06791  0.15819  217 ARG   A CA  
1661 C  C   . ARG   A 217 ? 0.28765 0.32367 0.40226 -0.05154 0.06345  0.16408  217 ARG   A C   
1662 O  O   . ARG   A 217 ? 0.28178 0.31186 0.38618 -0.04865 0.06330  0.17282  217 ARG   A O   
1663 C  CB  . ARG   A 217 ? 0.28112 0.34673 0.37700 -0.04942 0.07805  0.16595  217 ARG   A CB  
1664 C  CG  . ARG   A 217 ? 0.28472 0.36636 0.37151 -0.04691 0.08509  0.15928  217 ARG   A CG  
1665 C  CD  . ARG   A 217 ? 0.29038 0.38124 0.36541 -0.04826 0.09599  0.16656  217 ARG   A CD  
1666 N  NE  . ARG   A 217 ? 0.30991 0.39482 0.36549 -0.04683 0.09416  0.17602  217 ARG   A NE  
1667 C  CZ  . ARG   A 217 ? 0.31519 0.40295 0.34559 -0.04263 0.09310  0.17437  217 ARG   A CZ  
1668 N  NH1 . ARG   A 217 ? 0.29998 0.39465 0.32049 -0.03945 0.09429  0.16297  217 ARG   A NH1 
1669 N  NH2 . ARG   A 217 ? 0.33072 0.41418 0.34609 -0.04181 0.09015  0.18428  217 ARG   A NH2 
1670 N  N   . TRP   A 218 ? 0.26590 0.29312 0.39905 -0.05730 0.05959  0.15912  218 TRP   A N   
1671 C  CA  . TRP   A 218 ? 0.28141 0.29103 0.42400 -0.06153 0.05741  0.16385  218 TRP   A CA  
1672 C  C   . TRP   A 218 ? 0.28577 0.27915 0.41981 -0.05565 0.05264  0.16540  218 TRP   A C   
1673 O  O   . TRP   A 218 ? 0.30484 0.28481 0.44256 -0.05664 0.05313  0.17273  218 TRP   A O   
1674 C  CB  . TRP   A 218 ? 0.29729 0.30019 0.45802 -0.06950 0.05286  0.15512  218 TRP   A CB  
1675 C  CG  . TRP   A 218 ? 0.29101 0.28805 0.45134 -0.06820 0.04497  0.14223  218 TRP   A CG  
1676 C  CD1 . TRP   A 218 ? 0.29264 0.30248 0.45660 -0.06874 0.04247  0.13361  218 TRP   A CD1 
1677 C  CD2 . TRP   A 218 ? 0.28381 0.26050 0.44038 -0.06622 0.03905  0.13664  218 TRP   A CD2 
1678 N  NE1 . TRP   A 218 ? 0.27332 0.27233 0.43491 -0.06793 0.03477  0.12344  218 TRP   A NE1 
1679 C  CE2 . TRP   A 218 ? 0.27932 0.25764 0.43588 -0.06636 0.03306  0.12459  218 TRP   A CE2 
1680 C  CE3 . TRP   A 218 ? 0.29698 0.25412 0.45072 -0.06388 0.03877  0.14063  218 TRP   A CE3 
1681 C  CZ2 . TRP   A 218 ? 0.30527 0.26615 0.45729 -0.06461 0.02737  0.11600  218 TRP   A CZ2 
1682 C  CZ3 . TRP   A 218 ? 0.34546 0.28526 0.49611 -0.06134 0.03371  0.13174  218 TRP   A CZ3 
1683 C  CH2 . TRP   A 218 ? 0.32886 0.27050 0.47780 -0.06189 0.02833  0.11928  218 TRP   A CH2 
1684 N  N   . PHE   A 219 ? 0.26963 0.26409 0.39388 -0.04942 0.04834  0.15881  219 PHE   A N   
1685 C  CA  . PHE   A 219 ? 0.29119 0.27241 0.40915 -0.04287 0.04370  0.15901  219 PHE   A CA  
1686 C  C   . PHE   A 219 ? 0.28777 0.27677 0.39065 -0.03612 0.04501  0.16955  219 PHE   A C   
1687 O  O   . PHE   A 219 ? 0.29501 0.27606 0.39409 -0.02988 0.04113  0.17156  219 PHE   A O   
1688 C  CB  . PHE   A 219 ? 0.28182 0.26170 0.39732 -0.04005 0.03828  0.14682  219 PHE   A CB  
1689 C  CG  . PHE   A 219 ? 0.23820 0.23748 0.34492 -0.03848 0.03950  0.14334  219 PHE   A CG  
1690 C  CD1 . PHE   A 219 ? 0.23093 0.24007 0.32076 -0.03183 0.03955  0.14674  219 PHE   A CD1 
1691 C  CD2 . PHE   A 219 ? 0.25591 0.26415 0.37160 -0.04385 0.04049  0.13644  219 PHE   A CD2 
1692 C  CE1 . PHE   A 219 ? 0.23487 0.26017 0.31508 -0.03072 0.04155  0.14231  219 PHE   A CE1 
1693 C  CE2 . PHE   A 219 ? 0.24652 0.27193 0.35525 -0.04162 0.04285  0.13281  219 PHE   A CE2 
1694 C  CZ  . PHE   A 219 ? 0.21261 0.24554 0.30279 -0.03522 0.04404  0.13535  219 PHE   A CZ  
1695 N  N   . LEU   A 220 ? 0.28457 0.28948 0.37853 -0.03735 0.05032  0.17575  220 LEU   A N   
1696 C  CA  . LEU   A 220 ? 0.32301 0.33536 0.40056 -0.03267 0.05088  0.18573  220 LEU   A CA  
1697 C  C   . LEU   A 220 ? 0.35002 0.35156 0.43369 -0.03308 0.05172  0.19823  220 LEU   A C   
1698 O  O   . LEU   A 220 ? 0.33044 0.32166 0.42909 -0.03852 0.05438  0.20015  220 LEU   A O   
1699 C  CB  . LEU   A 220 ? 0.30028 0.33080 0.36414 -0.03473 0.05742  0.18734  220 LEU   A CB  
1700 C  CG  . LEU   A 220 ? 0.27921 0.32019 0.33591 -0.03325 0.05710  0.17513  220 LEU   A CG  
1701 C  CD1 . LEU   A 220 ? 0.28653 0.34311 0.33000 -0.03508 0.06540  0.17542  220 LEU   A CD1 
1702 C  CD2 . LEU   A 220 ? 0.26998 0.31033 0.31468 -0.02676 0.04940  0.17160  220 LEU   A CD2 
1703 N  N   . ASN   A 221 ? 0.35636 0.36053 0.42886 -0.02758 0.04894  0.20697  221 ASN   A N   
1704 C  CA  . ASN   A 221 ? 0.40628 0.40226 0.48400 -0.02748 0.05008  0.22069  221 ASN   A CA  
1705 C  C   . ASN   A 221 ? 0.42591 0.43495 0.48503 -0.02383 0.04855  0.23115  221 ASN   A C   
1706 O  O   . ASN   A 221 ? 0.36046 0.38242 0.40328 -0.02138 0.04574  0.22607  221 ASN   A O   
1707 C  CB  . ASN   A 221 ? 0.43312 0.40939 0.52620 -0.02377 0.04613  0.21983  221 ASN   A CB  
1708 C  CG  . ASN   A 221 ? 0.48133 0.45633 0.57267 -0.01761 0.04018  0.20907  221 ASN   A CG  
1709 O  OD1 . ASN   A 221 ? 0.50414 0.48943 0.58448 -0.01171 0.03590  0.21182  221 ASN   A OD1 
1710 N  ND2 . ASN   A 221 ? 0.46090 0.42410 0.56245 -0.01965 0.03960  0.19656  221 ASN   A ND2 
1711 N  N   . ARG   A 222 ? 0.43487 0.44000 0.49620 -0.02425 0.05020  0.24586  222 ARG   A N   
1712 C  CA  . ARG   A 222 ? 0.50091 0.51698 0.54578 -0.02141 0.04778  0.25797  222 ARG   A CA  
1713 C  C   . ARG   A 222 ? 0.52422 0.53874 0.57116 -0.01343 0.03915  0.26045  222 ARG   A C   
1714 O  O   . ARG   A 222 ? 0.58323 0.61075 0.61431 -0.01107 0.03470  0.26648  222 ARG   A O   
1715 C  CB  . ARG   A 222 ? 0.48864 0.50111 0.53638 -0.02494 0.05277  0.27425  222 ARG   A CB  
1716 C  CG  . ARG   A 222 ? 0.54483 0.54048 0.61173 -0.02115 0.05015  0.28340  222 ARG   A CG  
1717 C  CD  . ARG   A 222 ? 0.51954 0.50878 0.59265 -0.02572 0.05595  0.29855  222 ARG   A CD  
1718 N  NE  . ARG   A 222 ? 0.65398 0.65536 0.71058 -0.02456 0.05488  0.31417  222 ARG   A NE  
1719 C  CZ  . ARG   A 222 ? 0.61586 0.61487 0.67325 -0.02800 0.05941  0.33016  222 ARG   A CZ  
1720 N  NH1 . ARG   A 222 ? 0.61871 0.60382 0.69329 -0.03319 0.06562  0.33277  222 ARG   A NH1 
1721 N  NH2 . ARG   A 222 ? 0.70410 0.71491 0.74421 -0.02680 0.05735  0.34404  222 ARG   A NH2 
1722 N  N   . PHE   A 223 ? 0.54472 0.54404 0.61053 -0.00958 0.03692  0.25558  223 PHE   A N   
1723 C  CA  . PHE   A 223 ? 0.53036 0.52909 0.60062 -0.00150 0.03002  0.25752  223 PHE   A CA  
1724 C  C   . PHE   A 223 ? 0.50828 0.52281 0.56342 0.00089  0.02422  0.24874  223 PHE   A C   
1725 O  O   . PHE   A 223 ? 0.48499 0.50612 0.52961 -0.00277 0.02572  0.23756  223 PHE   A O   
1726 C  CB  . PHE   A 223 ? 0.51805 0.49669 0.60934 0.00214  0.03032  0.25040  223 PHE   A CB  
1727 C  CG  . PHE   A 223 ? 0.56929 0.52940 0.67440 -0.00322 0.03660  0.25007  223 PHE   A CG  
1728 C  CD1 . PHE   A 223 ? 0.61682 0.56827 0.73031 -0.00397 0.03956  0.26444  223 PHE   A CD1 
1729 C  CD2 . PHE   A 223 ? 0.57985 0.53077 0.69033 -0.00795 0.03896  0.23546  223 PHE   A CD2 
1730 C  CE1 . PHE   A 223 ? 0.64187 0.57543 0.76840 -0.00992 0.04501  0.26363  223 PHE   A CE1 
1731 C  CE2 . PHE   A 223 ? 0.59743 0.53161 0.72066 -0.01430 0.04374  0.23439  223 PHE   A CE2 
1732 C  CZ  . PHE   A 223 ? 0.64517 0.57028 0.77637 -0.01547 0.04685  0.24815  223 PHE   A CZ  
1733 N  N   . THR   A 224 ? 0.48352 0.50429 0.53899 0.00698  0.01757  0.25433  224 THR   A N   
1734 C  CA  . THR   A 224 ? 0.46898 0.50171 0.51614 0.01006  0.01094  0.24593  224 THR   A CA  
1735 C  C   . THR   A 224 ? 0.48510 0.51019 0.55118 0.01783  0.00759  0.24586  224 THR   A C   
1736 O  O   . THR   A 224 ? 0.50140 0.51162 0.58513 0.02092  0.01074  0.25210  224 THR   A O   
1737 C  CB  . THR   A 224 ? 0.50019 0.55251 0.52628 0.00843  0.00562  0.25318  224 THR   A CB  
1738 O  OG1 . THR   A 224 ? 0.44797 0.51150 0.46082 0.00778  0.00106  0.24067  224 THR   A OG1 
1739 C  CG2 . THR   A 224 ? 0.51556 0.57222 0.54934 0.01345  -0.00003 0.26864  224 THR   A CG2 
1740 N  N   . THR   A 225 ? 0.43572 0.47059 0.49832 0.02090  0.00187  0.23841  225 THR   A N   
1741 C  CA  . THR   A 225 ? 0.47599 0.50687 0.55587 0.02854  -0.00078 0.23873  225 THR   A CA  
1742 C  C   . THR   A 225 ? 0.44715 0.49750 0.51801 0.02992  -0.00894 0.23723  225 THR   A C   
1743 O  O   . THR   A 225 ? 0.45265 0.51490 0.50424 0.02485  -0.01181 0.23064  225 THR   A O   
1744 C  CB  . THR   A 225 ? 0.47678 0.48963 0.56949 0.03061  0.00393  0.22503  225 THR   A CB  
1745 O  OG1 . THR   A 225 ? 0.47654 0.48221 0.58759 0.03854  0.00395  0.22701  225 THR   A OG1 
1746 C  CG2 . THR   A 225 ? 0.41791 0.43737 0.49940 0.02818  0.00191  0.20988  225 THR   A CG2 
1747 N  N   . THR   A 226 ? 0.46152 0.51502 0.54700 0.03646  -0.01237 0.24357  226 THR   A N   
1748 C  CA  . THR   A 226 ? 0.44545 0.51677 0.52616 0.03739  -0.02016 0.24130  226 THR   A CA  
1749 C  C   . THR   A 226 ? 0.40060 0.46751 0.48455 0.03883  -0.01900 0.22469  226 THR   A C   
1750 O  O   . THR   A 226 ? 0.38155 0.43088 0.47613 0.04127  -0.01252 0.21710  226 THR   A O   
1751 C  CB  . THR   A 226 ? 0.44595 0.52445 0.54320 0.04371  -0.02413 0.25531  226 THR   A CB  
1752 O  OG1 . THR   A 226 ? 0.46438 0.52669 0.58496 0.05117  -0.01805 0.25347  226 THR   A OG1 
1753 C  CG2 . THR   A 226 ? 0.45348 0.53526 0.54820 0.04251  -0.02520 0.27302  226 THR   A CG2 
1754 N  N   . LEU   A 227 ? 0.38248 0.46515 0.45618 0.03663  -0.02556 0.21893  227 LEU   A N   
1755 C  CA  . LEU   A 227 ? 0.41207 0.49266 0.48865 0.03793  -0.02519 0.20445  227 LEU   A CA  
1756 C  C   . LEU   A 227 ? 0.42792 0.49834 0.52816 0.04621  -0.02126 0.20476  227 LEU   A C   
1757 O  O   . LEU   A 227 ? 0.38537 0.44121 0.49121 0.04817  -0.01564 0.19384  227 LEU   A O   
1758 C  CB  . LEU   A 227 ? 0.38779 0.48760 0.45221 0.03422  -0.03353 0.20071  227 LEU   A CB  
1759 C  CG  . LEU   A 227 ? 0.37064 0.47066 0.43297 0.03348  -0.03398 0.18535  227 LEU   A CG  
1760 C  CD1 . LEU   A 227 ? 0.35452 0.43862 0.41321 0.03232  -0.02706 0.17439  227 LEU   A CD1 
1761 C  CD2 . LEU   A 227 ? 0.35288 0.46946 0.39722 0.02690  -0.04169 0.18055  227 LEU   A CD2 
1762 N  N   . ASN   A 228 ? 0.40862 0.48631 0.52281 0.05116  -0.02375 0.21743  228 ASN   A N   
1763 C  CA  . ASN   A 228 ? 0.43953 0.50780 0.57698 0.05974  -0.01874 0.21843  228 ASN   A CA  
1764 C  C   . ASN   A 228 ? 0.43874 0.48185 0.58493 0.06253  -0.00927 0.21567  228 ASN   A C   
1765 O  O   . ASN   A 228 ? 0.43262 0.46139 0.58765 0.06640  -0.00315 0.20529  228 ASN   A O   
1766 C  CB  . ASN   A 228 ? 0.43355 0.51462 0.58557 0.06450  -0.02277 0.23504  228 ASN   A CB  
1767 C  CG  . ASN   A 228 ? 0.46719 0.57299 0.61158 0.06083  -0.03289 0.23769  228 ASN   A CG  
1768 O  OD1 . ASN   A 228 ? 0.48577 0.59729 0.62116 0.05742  -0.03532 0.22543  228 ASN   A OD1 
1769 N  ND2 . ASN   A 228 ? 0.52220 0.64245 0.67034 0.06112  -0.03914 0.25388  228 ASN   A ND2 
1770 N  N   . ASP   A 229 ? 0.44960 0.48647 0.59268 0.06001  -0.00784 0.22454  229 ASP   A N   
1771 C  CA  . ASP   A 229 ? 0.43500 0.44714 0.58653 0.06128  0.00070  0.22202  229 ASP   A CA  
1772 C  C   . ASP   A 229 ? 0.45032 0.44983 0.59185 0.05645  0.00434  0.20529  229 ASP   A C   
1773 O  O   . ASP   A 229 ? 0.43620 0.41485 0.58656 0.05858  0.01108  0.19702  229 ASP   A O   
1774 C  CB  . ASP   A 229 ? 0.46835 0.47785 0.61862 0.05866  0.00117  0.23607  229 ASP   A CB  
1775 C  CG  . ASP   A 229 ? 0.52422 0.53948 0.69024 0.06504  -0.00043 0.25355  229 ASP   A CG  
1776 O  OD1 . ASP   A 229 ? 0.55135 0.58825 0.71534 0.06586  -0.00796 0.26194  229 ASP   A OD1 
1777 O  OD2 . ASP   A 229 ? 0.55744 0.55500 0.73852 0.06900  0.00576  0.25898  229 ASP   A OD2 
1778 N  N   . PHE   A 230 ? 0.39291 0.40412 0.51603 0.04982  0.00010  0.19972  230 PHE   A N   
1779 C  CA  . PHE   A 230 ? 0.41421 0.41531 0.53011 0.04594  0.00300  0.18447  230 PHE   A CA  
1780 C  C   . PHE   A 230 ? 0.39241 0.38886 0.51557 0.05085  0.00445  0.17327  230 PHE   A C   
1781 O  O   . PHE   A 230 ? 0.39725 0.37543 0.52378 0.05087  0.00978  0.16263  230 PHE   A O   
1782 C  CB  . PHE   A 230 ? 0.36659 0.38218 0.46263 0.03888  -0.00135 0.18061  230 PHE   A CB  
1783 C  CG  . PHE   A 230 ? 0.38381 0.39126 0.47422 0.03545  0.00096  0.16607  230 PHE   A CG  
1784 C  CD1 . PHE   A 230 ? 0.31788 0.30993 0.40919 0.03099  0.00612  0.16266  230 PHE   A CD1 
1785 C  CD2 . PHE   A 230 ? 0.36445 0.37936 0.45029 0.03639  -0.00217 0.15621  230 PHE   A CD2 
1786 C  CE1 . PHE   A 230 ? 0.32658 0.31184 0.41411 0.02743  0.00758  0.15019  230 PHE   A CE1 
1787 C  CE2 . PHE   A 230 ? 0.35302 0.36044 0.43447 0.03352  -0.00037 0.14407  230 PHE   A CE2 
1788 C  CZ  . PHE   A 230 ? 0.31865 0.31149 0.40106 0.02909  0.00428  0.14130  230 PHE   A CZ  
1789 N  N   . ASN   A 231 ? 0.39380 0.40669 0.51913 0.05441  -0.00019 0.17543  231 ASN   A N   
1790 C  CA  . ASN   A 231 ? 0.41270 0.42386 0.54368 0.05850  0.00142  0.16492  231 ASN   A CA  
1791 C  C   . ASN   A 231 ? 0.40246 0.39510 0.55094 0.06569  0.00942  0.16360  231 ASN   A C   
1792 O  O   . ASN   A 231 ? 0.41080 0.39331 0.56166 0.06808  0.01391  0.15171  231 ASN   A O   
1793 C  CB  . ASN   A 231 ? 0.36148 0.39561 0.49188 0.05952  -0.00550 0.16836  231 ASN   A CB  
1794 C  CG  . ASN   A 231 ? 0.36173 0.40870 0.47346 0.05250  -0.01154 0.16117  231 ASN   A CG  
1795 O  OD1 . ASN   A 231 ? 0.39810 0.43668 0.50226 0.04980  -0.00935 0.14988  231 ASN   A OD1 
1796 N  ND2 . ASN   A 231 ? 0.36067 0.42734 0.46478 0.04925  -0.01916 0.16744  231 ASN   A ND2 
1797 N  N   . LEU   A 232 ? 0.40707 0.39434 0.56716 0.06914  0.01177  0.17531  232 LEU   A N   
1798 C  CA  . LEU   A 232 ? 0.41599 0.38147 0.59124 0.07519  0.02063  0.17277  232 LEU   A CA  
1799 C  C   . LEU   A 232 ? 0.44432 0.38603 0.61278 0.07063  0.02603  0.15952  232 LEU   A C   
1800 O  O   . LEU   A 232 ? 0.46238 0.38641 0.63595 0.07384  0.03291  0.14862  232 LEU   A O   
1801 C  CB  . LEU   A 232 ? 0.41734 0.38034 0.60574 0.07889  0.02190  0.18862  232 LEU   A CB  
1802 C  CG  . LEU   A 232 ? 0.45766 0.44213 0.65709 0.08429  0.01714  0.20306  232 LEU   A CG  
1803 C  CD1 . LEU   A 232 ? 0.45041 0.42781 0.66588 0.08922  0.02014  0.21805  232 LEU   A CD1 
1804 C  CD2 . LEU   A 232 ? 0.45117 0.44131 0.66030 0.09047  0.01936  0.19681  232 LEU   A CD2 
1805 N  N   . VAL   A 233 ? 0.42574 0.36709 0.58215 0.06256  0.02313  0.15994  233 VAL   A N   
1806 C  CA  . VAL   A 233 ? 0.42469 0.34501 0.57555 0.05667  0.02720  0.14817  233 VAL   A CA  
1807 C  C   . VAL   A 233 ? 0.43982 0.36146 0.58056 0.05424  0.02608  0.13349  233 VAL   A C   
1808 O  O   . VAL   A 233 ? 0.43318 0.33558 0.57315 0.05290  0.03079  0.12047  233 VAL   A O   
1809 C  CB  . VAL   A 233 ? 0.45247 0.37343 0.59661 0.04871  0.02521  0.15505  233 VAL   A CB  
1810 C  CG1 . VAL   A 233 ? 0.46399 0.37475 0.59868 0.04024  0.02594  0.14264  233 VAL   A CG1 
1811 C  CG2 . VAL   A 233 ? 0.46607 0.37358 0.62165 0.05007  0.02925  0.16506  233 VAL   A CG2 
1812 N  N   . ALA   A 234 ? 0.44967 0.39341 0.58163 0.05314  0.01968  0.13503  234 ALA   A N   
1813 C  CA  . ALA   A 234 ? 0.41048 0.35697 0.53376 0.05140  0.01824  0.12257  234 ALA   A CA  
1814 C  C   . ALA   A 234 ? 0.39807 0.33446 0.52861 0.05777  0.02363  0.11331  234 ALA   A C   
1815 O  O   . ALA   A 234 ? 0.37570 0.29810 0.50138 0.05571  0.02687  0.10007  234 ALA   A O   
1816 C  CB  . ALA   A 234 ? 0.38695 0.35925 0.50130 0.05017  0.01062  0.12657  234 ALA   A CB  
1817 N  N   . MET   A 235 ? 0.40911 0.35257 0.55141 0.06527  0.02508  0.12032  235 MET   A N   
1818 C  CA  . MET   A 235 ? 0.42569 0.36097 0.57597 0.07193  0.03178  0.11237  235 MET   A CA  
1819 C  C   . MET   A 235 ? 0.44026 0.34614 0.59110 0.07133  0.04020  0.10161  235 MET   A C   
1820 O  O   . MET   A 235 ? 0.43151 0.32620 0.57742 0.07163  0.04499  0.08769  235 MET   A O   
1821 C  CB  . MET   A 235 ? 0.43118 0.37836 0.59724 0.07977  0.03257  0.12406  235 MET   A CB  
1822 C  CG  . MET   A 235 ? 0.46880 0.41149 0.64490 0.08730  0.04030  0.11749  235 MET   A CG  
1823 S  SD  . MET   A 235 ? 0.62786 0.59920 0.81824 0.09338  0.03636  0.13006  235 MET   A SD  
1824 C  CE  . MET   A 235 ? 0.48673 0.47150 0.68026 0.09114  0.02787  0.14904  235 MET   A CE  
1825 N  N   . LYS   A 236 ? 0.44540 0.33815 0.60045 0.06932  0.04184  0.10725  236 LYS   A N   
1826 C  CA  . LYS   A 236 ? 0.41295 0.27675 0.56874 0.06789  0.04944  0.09693  236 LYS   A CA  
1827 C  C   . LYS   A 236 ? 0.41805 0.26919 0.55876 0.05885  0.04865  0.08176  236 LYS   A C   
1828 O  O   . LYS   A 236 ? 0.45300 0.28273 0.58973 0.05751  0.05458  0.06786  236 LYS   A O   
1829 C  CB  . LYS   A 236 ? 0.42746 0.28082 0.59137 0.06664  0.05053  0.10725  236 LYS   A CB  
1830 C  CG  . LYS   A 236 ? 0.52400 0.38809 0.70415 0.07536  0.05133  0.12339  236 LYS   A CG  
1831 C  CD  . LYS   A 236 ? 0.53833 0.41179 0.72747 0.08482  0.05489  0.12212  236 LYS   A CD  
1832 C  CE  . LYS   A 236 ? 0.51314 0.40205 0.71910 0.09228  0.05362  0.14002  236 LYS   A CE  
1833 N  NZ  . LYS   A 236 ? 0.47368 0.39253 0.67508 0.09028  0.04343  0.15020  236 LYS   A NZ  
1834 N  N   . TYR   A 237 ? 0.40105 0.26516 0.53282 0.05214  0.04141  0.08386  237 TYR   A N   
1835 C  CA  . TYR   A 237 ? 0.38525 0.23978 0.50478 0.04282  0.03968  0.07120  237 TYR   A CA  
1836 C  C   . TYR   A 237 ? 0.35383 0.22048 0.46509 0.04353  0.03708  0.06397  237 TYR   A C   
1837 O  O   . TYR   A 237 ? 0.33550 0.20261 0.43786 0.03580  0.03313  0.05802  237 TYR   A O   
1838 C  CB  . TYR   A 237 ? 0.37038 0.22941 0.48746 0.03394  0.03453  0.07825  237 TYR   A CB  
1839 C  CG  . TYR   A 237 ? 0.40622 0.24900 0.53006 0.03092  0.03762  0.08263  237 TYR   A CG  
1840 C  CD1 . TYR   A 237 ? 0.40634 0.25544 0.54021 0.03659  0.03849  0.09771  237 TYR   A CD1 
1841 C  CD2 . TYR   A 237 ? 0.41658 0.23804 0.53674 0.02173  0.03908  0.07184  237 TYR   A CD2 
1842 C  CE1 . TYR   A 237 ? 0.40025 0.23383 0.54115 0.03411  0.04160  0.10257  237 TYR   A CE1 
1843 C  CE2 . TYR   A 237 ? 0.39838 0.20440 0.52515 0.01851  0.04176  0.07603  237 TYR   A CE2 
1844 C  CZ  . TYR   A 237 ? 0.41442 0.22611 0.55195 0.02519  0.04344  0.09168  237 TYR   A CZ  
1845 O  OH  . TYR   A 237 ? 0.44398 0.23991 0.58884 0.02224  0.04634  0.09678  237 TYR   A OH  
1846 N  N   . ASN   A 238 ? 0.35621 0.23347 0.47169 0.05229  0.03920  0.06497  238 ASN   A N   
1847 C  CA  . ASN   A 238 ? 0.34386 0.23131 0.45217 0.05324  0.03775  0.05763  238 ASN   A CA  
1848 C  C   . ASN   A 238 ? 0.33089 0.23824 0.43360 0.04899  0.02887  0.06384  238 ASN   A C   
1849 O  O   . ASN   A 238 ? 0.33082 0.24372 0.42193 0.04401  0.02568  0.05414  238 ASN   A O   
1850 C  CB  . ASN   A 238 ? 0.36154 0.22839 0.45878 0.04843  0.04228  0.03962  238 ASN   A CB  
1851 C  CG  . ASN   A 238 ? 0.40498 0.27999 0.49622 0.05166  0.04388  0.03185  238 ASN   A CG  
1852 O  OD1 . ASN   A 238 ? 0.46082 0.33066 0.53597 0.04422  0.04286  0.01778  238 ASN   A OD1 
1853 N  ND2 . ASN   A 238 ? 0.37466 0.26889 0.47494 0.05991  0.04401  0.04018  238 ASN   A ND2 
1854 N  N   . TYR   A 239 ? 0.32874 0.25017 0.43489 0.04869  0.02411  0.07744  239 TYR   A N   
1855 C  CA  . TYR   A 239 ? 0.31513 0.25785 0.41446 0.04541  0.01630  0.08365  239 TYR   A CA  
1856 C  C   . TYR   A 239 ? 0.31013 0.27451 0.41249 0.05106  0.01299  0.08969  239 TYR   A C   
1857 O  O   . TYR   A 239 ? 0.28502 0.25077 0.39758 0.05676  0.01563  0.09532  239 TYR   A O   
1858 C  CB  . TYR   A 239 ? 0.28542 0.23143 0.38342 0.04038  0.01372  0.09377  239 TYR   A CB  
1859 C  CG  . TYR   A 239 ? 0.26777 0.20290 0.36092 0.03153  0.01380  0.08911  239 TYR   A CG  
1860 C  CD1 . TYR   A 239 ? 0.30111 0.21415 0.39547 0.02762  0.01796  0.07786  239 TYR   A CD1 
1861 C  CD2 . TYR   A 239 ? 0.27427 0.22415 0.35928 0.02536  0.00961  0.09291  239 TYR   A CD2 
1862 C  CE1 . TYR   A 239 ? 0.30358 0.21152 0.39329 0.01730  0.01641  0.07182  239 TYR   A CE1 
1863 C  CE2 . TYR   A 239 ? 0.27294 0.21783 0.35466 0.01637  0.00976  0.08715  239 TYR   A CE2 
1864 C  CZ  . TYR   A 239 ? 0.28772 0.21267 0.37290 0.01215  0.01241  0.07726  239 TYR   A CZ  
1865 O  OH  . TYR   A 239 ? 0.27618 0.19859 0.36039 0.00248  0.01126  0.07244  239 TYR   A OH  
1866 N  N   . GLU   A 240 ? 0.29118 0.27262 0.38553 0.04873  0.00701  0.08851  240 GLU   A N   
1867 C  CA  . GLU   A 240 ? 0.32147 0.32268 0.41912 0.05204  0.00342  0.09330  240 GLU   A CA  
1868 C  C   . GLU   A 240 ? 0.33893 0.35360 0.43527 0.05008  -0.00159 0.10534  240 GLU   A C   
1869 O  O   . GLU   A 240 ? 0.30550 0.31735 0.39552 0.04573  -0.00257 0.10936  240 GLU   A O   
1870 C  CB  . GLU   A 240 ? 0.33505 0.34923 0.42525 0.04979  -0.00096 0.08654  240 GLU   A CB  
1871 C  CG  . GLU   A 240 ? 0.31826 0.33023 0.39420 0.04205  -0.00328 0.07772  240 GLU   A CG  
1872 C  CD  . GLU   A 240 ? 0.37598 0.40162 0.44377 0.03863  -0.00765 0.07038  240 GLU   A CD  
1873 O  OE1 . GLU   A 240 ? 0.36153 0.39410 0.41787 0.03238  -0.01192 0.06776  240 GLU   A OE1 
1874 O  OE2 . GLU   A 240 ? 0.40692 0.43590 0.48068 0.04233  -0.00594 0.06750  240 GLU   A OE2 
1875 N  N   . PRO   A 241 ? 0.32104 0.34987 0.42421 0.05313  -0.00415 0.11184  241 PRO   A N   
1876 C  CA  . PRO   A 241 ? 0.33775 0.37802 0.44008 0.05149  -0.00870 0.12387  241 PRO   A CA  
1877 C  C   . PRO   A 241 ? 0.31992 0.37199 0.40468 0.04380  -0.01514 0.12327  241 PRO   A C   
1878 O  O   . PRO   A 241 ? 0.33272 0.39079 0.40825 0.04026  -0.01805 0.11475  241 PRO   A O   
1879 C  CB  . PRO   A 241 ? 0.31136 0.36565 0.42502 0.05558  -0.01092 0.12938  241 PRO   A CB  
1880 C  CG  . PRO   A 241 ? 0.33928 0.38319 0.46433 0.06168  -0.00374 0.12225  241 PRO   A CG  
1881 C  CD  . PRO   A 241 ? 0.34188 0.37549 0.45609 0.05855  -0.00189 0.10966  241 PRO   A CD  
1882 N  N   . LEU   A 242 ? 0.33261 0.38708 0.41250 0.04122  -0.01654 0.13219  242 LEU   A N   
1883 C  CA  . LEU   A 242 ? 0.32063 0.38698 0.38287 0.03425  -0.02158 0.13247  242 LEU   A CA  
1884 C  C   . LEU   A 242 ? 0.31787 0.40222 0.37806 0.03305  -0.02848 0.13890  242 LEU   A C   
1885 O  O   . LEU   A 242 ? 0.28590 0.37322 0.35727 0.03687  -0.02905 0.14955  242 LEU   A O   
1886 C  CB  . LEU   A 242 ? 0.32516 0.38499 0.38181 0.03146  -0.01859 0.13868  242 LEU   A CB  
1887 C  CG  . LEU   A 242 ? 0.29470 0.36236 0.33179 0.02439  -0.02048 0.13520  242 LEU   A CG  
1888 C  CD1 . LEU   A 242 ? 0.27418 0.33555 0.30739 0.02259  -0.01830 0.12330  242 LEU   A CD1 
1889 C  CD2 . LEU   A 242 ? 0.30045 0.36440 0.33382 0.02203  -0.01702 0.14400  242 LEU   A CD2 
1890 N  N   . THR   A 243 ? 0.31108 0.40678 0.35767 0.02751  -0.03376 0.13235  243 THR   A N   
1891 C  CA  . THR   A 243 ? 0.31032 0.42250 0.35351 0.02472  -0.04116 0.13692  243 THR   A CA  
1892 C  C   . THR   A 243 ? 0.34080 0.45985 0.36342 0.01783  -0.04460 0.13865  243 THR   A C   
1893 O  O   . THR   A 243 ? 0.30756 0.42002 0.31786 0.01490  -0.04083 0.13407  243 THR   A O   
1894 C  CB  . THR   A 243 ? 0.32033 0.43961 0.36375 0.02270  -0.04480 0.12754  243 THR   A CB  
1895 O  OG1 . THR   A 243 ? 0.30527 0.42263 0.33165 0.01680  -0.04512 0.11589  243 THR   A OG1 
1896 C  CG2 . THR   A 243 ? 0.30518 0.41711 0.36684 0.02946  -0.03995 0.12469  243 THR   A CG2 
1897 N  N   . GLN   A 244 ? 0.26111 0.39398 0.28000 0.01511  -0.05156 0.14548  244 GLN   A N   
1898 C  CA  . GLN   A 244 ? 0.31091 0.45077 0.30740 0.00793  -0.05520 0.14581  244 GLN   A CA  
1899 C  C   . GLN   A 244 ? 0.35195 0.49008 0.33069 0.00189  -0.05488 0.13068  244 GLN   A C   
1900 O  O   . GLN   A 244 ? 0.35454 0.49131 0.31405 -0.00273 -0.05285 0.12778  244 GLN   A O   
1901 C  CB  . GLN   A 244 ? 0.30456 0.46011 0.29968 0.00524  -0.06406 0.15439  244 GLN   A CB  
1902 C  CG  . GLN   A 244 ? 0.35699 0.51896 0.32777 -0.00183 -0.06760 0.15669  244 GLN   A CG  
1903 C  CD  . GLN   A 244 ? 0.37147 0.52512 0.33559 -0.00063 -0.06092 0.16268  244 GLN   A CD  
1904 O  OE1 . GLN   A 244 ? 0.35095 0.50106 0.33036 0.00501  -0.05831 0.17460  244 GLN   A OE1 
1905 N  NE2 . GLN   A 244 ? 0.40272 0.55286 0.34435 -0.00606 -0.05750 0.15463  244 GLN   A NE2 
1906 N  N   . ASP   A 245 ? 0.32424 0.46199 0.30922 0.00194  -0.05606 0.12099  245 ASP   A N   
1907 C  CA  . ASP   A 245 ? 0.35253 0.48737 0.32208 -0.00353 -0.05537 0.10668  245 ASP   A CA  
1908 C  C   . ASP   A 245 ? 0.32532 0.44851 0.29073 -0.00208 -0.04734 0.10202  245 ASP   A C   
1909 O  O   . ASP   A 245 ? 0.32681 0.44836 0.27436 -0.00683 -0.04494 0.09469  245 ASP   A O   
1910 C  CB  . ASP   A 245 ? 0.32990 0.46608 0.30848 -0.00378 -0.05795 0.09824  245 ASP   A CB  
1911 C  CG  . ASP   A 245 ? 0.40613 0.54043 0.36805 -0.01058 -0.05867 0.08420  245 ASP   A CG  
1912 O  OD1 . ASP   A 245 ? 0.43741 0.57503 0.38021 -0.01659 -0.06090 0.08208  245 ASP   A OD1 
1913 O  OD2 . ASP   A 245 ? 0.45200 0.58058 0.41907 -0.00992 -0.05649 0.07516  245 ASP   A OD2 
1914 N  N   . HIS   A 246 ? 0.32437 0.43915 0.30635 0.00432  -0.04269 0.10598  246 HIS   A N   
1915 C  CA  . HIS   A 246 ? 0.31648 0.42081 0.29689 0.00545  -0.03552 0.10440  246 HIS   A CA  
1916 C  C   . HIS   A 246 ? 0.30663 0.41206 0.27412 0.00252  -0.03258 0.11085  246 HIS   A C   
1917 O  O   . HIS   A 246 ? 0.31850 0.42087 0.27467 -0.00042 -0.02735 0.10600  246 HIS   A O   
1918 C  CB  . HIS   A 246 ? 0.30359 0.39756 0.30400 0.01225  -0.03168 0.10926  246 HIS   A CB  
1919 C  CG  . HIS   A 246 ? 0.26752 0.35860 0.27959 0.01554  -0.03241 0.10230  246 HIS   A CG  
1920 N  ND1 . HIS   A 246 ? 0.27201 0.35751 0.30205 0.02192  -0.03057 0.10660  246 HIS   A ND1 
1921 C  CD2 . HIS   A 246 ? 0.29718 0.38973 0.30530 0.01334  -0.03399 0.09127  246 HIS   A CD2 
1922 C  CE1 . HIS   A 246 ? 0.30751 0.39182 0.34332 0.02352  -0.03065 0.09859  246 HIS   A CE1 
1923 N  NE2 . HIS   A 246 ? 0.29145 0.38010 0.31463 0.01822  -0.03310 0.08960  246 HIS   A NE2 
1924 N  N   . VAL   A 247 ? 0.33055 0.44051 0.30074 0.00360  -0.03504 0.12261  247 VAL   A N   
1925 C  CA  . VAL   A 247 ? 0.32150 0.43311 0.27861 0.00059  -0.03232 0.12970  247 VAL   A CA  
1926 C  C   . VAL   A 247 ? 0.36384 0.48166 0.29620 -0.00632 -0.03311 0.12104  247 VAL   A C   
1927 O  O   . VAL   A 247 ? 0.35766 0.47294 0.27657 -0.00921 -0.02650 0.11922  247 VAL   A O   
1928 C  CB  . VAL   A 247 ? 0.31849 0.43549 0.28257 0.00282  -0.03635 0.14430  247 VAL   A CB  
1929 C  CG1 . VAL   A 247 ? 0.34543 0.46589 0.29256 -0.00122 -0.03459 0.15149  247 VAL   A CG1 
1930 C  CG2 . VAL   A 247 ? 0.29978 0.40708 0.28753 0.00981  -0.03302 0.15184  247 VAL   A CG2 
1931 N  N   . ASP   A 248 ? 0.33401 0.45912 0.26057 -0.00925 -0.04025 0.11486  248 ASP   A N   
1932 C  CA  . ASP   A 248 ? 0.35381 0.48220 0.25629 -0.01619 -0.04092 0.10479  248 ASP   A CA  
1933 C  C   . ASP   A 248 ? 0.35001 0.47071 0.24653 -0.01728 -0.03371 0.09154  248 ASP   A C   
1934 O  O   . ASP   A 248 ? 0.34840 0.46727 0.22631 -0.02098 -0.02763 0.08581  248 ASP   A O   
1935 C  CB  . ASP   A 248 ? 0.35987 0.49639 0.26051 -0.01963 -0.05050 0.10081  248 ASP   A CB  
1936 C  CG  . ASP   A 248 ? 0.37966 0.52662 0.28451 -0.01939 -0.05799 0.11449  248 ASP   A CG  
1937 O  OD1 . ASP   A 248 ? 0.42910 0.57693 0.33133 -0.01805 -0.05594 0.12586  248 ASP   A OD1 
1938 O  OD2 . ASP   A 248 ? 0.36160 0.51646 0.27327 -0.02072 -0.06586 0.11451  248 ASP   A OD2 
1939 N  N   . ILE   A 249 ? 0.34409 0.46034 0.25638 -0.01385 -0.03364 0.08663  249 ILE   A N   
1940 C  CA  . ILE   A 249 ? 0.34968 0.45969 0.25890 -0.01436 -0.02733 0.07535  249 ILE   A CA  
1941 C  C   . ILE   A 249 ? 0.33694 0.44292 0.24428 -0.01327 -0.01749 0.07943  249 ILE   A C   
1942 O  O   . ILE   A 249 ? 0.33140 0.43523 0.22949 -0.01523 -0.01001 0.07078  249 ILE   A O   
1943 C  CB  . ILE   A 249 ? 0.31580 0.42222 0.24372 -0.01034 -0.02982 0.07206  249 ILE   A CB  
1944 C  CG1 . ILE   A 249 ? 0.36515 0.47548 0.29286 -0.01309 -0.03724 0.06487  249 ILE   A CG1 
1945 C  CG2 . ILE   A 249 ? 0.32982 0.43035 0.25885 -0.00946 -0.02336 0.06478  249 ILE   A CG2 
1946 C  CD1 . ILE   A 249 ? 0.35453 0.46380 0.30324 -0.00838 -0.04046 0.06659  249 ILE   A CD1 
1947 N  N   . LEU   A 250 ? 0.30884 0.41367 0.22632 -0.01027 -0.01644 0.09259  250 LEU   A N   
1948 C  CA  . LEU   A 250 ? 0.31776 0.41853 0.23701 -0.00992 -0.00709 0.09798  250 LEU   A CA  
1949 C  C   . LEU   A 250 ? 0.34319 0.44792 0.24333 -0.01395 -0.00247 0.10053  250 LEU   A C   
1950 O  O   . LEU   A 250 ? 0.33197 0.43442 0.23271 -0.01447 0.00670  0.10423  250 LEU   A O   
1951 C  CB  . LEU   A 250 ? 0.30783 0.40257 0.24784 -0.00542 -0.00758 0.11011  250 LEU   A CB  
1952 C  CG  . LEU   A 250 ? 0.28055 0.36766 0.23925 -0.00126 -0.00906 0.10741  250 LEU   A CG  
1953 C  CD1 . LEU   A 250 ? 0.26626 0.34571 0.24300 0.00303  -0.00977 0.11813  250 LEU   A CD1 
1954 C  CD2 . LEU   A 250 ? 0.23957 0.32077 0.20213 -0.00256 -0.00150 0.09979  250 LEU   A CD2 
1955 N  N   . GLY   A 251 ? 0.36535 0.47582 0.24905 -0.01720 -0.00839 0.09861  251 GLY   A N   
1956 C  CA  . GLY   A 251 ? 0.36288 0.47645 0.22503 -0.02131 -0.00483 0.10050  251 GLY   A CA  
1957 C  C   . GLY   A 251 ? 0.39578 0.50617 0.24552 -0.02345 0.00800  0.09221  251 GLY   A C   
1958 O  O   . GLY   A 251 ? 0.40530 0.51541 0.25054 -0.02417 0.01599  0.09922  251 GLY   A O   
1959 N  N   . PRO   A 252 ? 0.37645 0.48438 0.22135 -0.02439 0.01105  0.07711  252 PRO   A N   
1960 C  CA  . PRO   A 252 ? 0.40343 0.50852 0.23999 -0.02524 0.02519  0.06846  252 PRO   A CA  
1961 C  C   . PRO   A 252 ? 0.38748 0.49219 0.24238 -0.02250 0.03466  0.07669  252 PRO   A C   
1962 O  O   . PRO   A 252 ? 0.40417 0.50916 0.25245 -0.02369 0.04577  0.07845  252 PRO   A O   
1963 C  CB  . PRO   A 252 ? 0.40335 0.50525 0.24052 -0.02514 0.02514  0.05241  252 PRO   A CB  
1964 C  CG  . PRO   A 252 ? 0.38900 0.49213 0.22123 -0.02734 0.01112  0.05043  252 PRO   A CG  
1965 C  CD  . PRO   A 252 ? 0.38375 0.49142 0.22931 -0.02513 0.00245  0.06681  252 PRO   A CD  
1966 N  N   . LEU   A 253 ? 0.36456 0.46807 0.24291 -0.01919 0.03064  0.08183  253 LEU   A N   
1967 C  CA  . LEU   A 253 ? 0.32539 0.42739 0.22387 -0.01757 0.03802  0.09013  253 LEU   A CA  
1968 C  C   . LEU   A 253 ? 0.33647 0.43812 0.23411 -0.01877 0.03884  0.10415  253 LEU   A C   
1969 O  O   . LEU   A 253 ? 0.33797 0.43990 0.23993 -0.02007 0.04895  0.10825  253 LEU   A O   
1970 C  CB  . LEU   A 253 ? 0.28441 0.38202 0.20590 -0.01438 0.03188  0.09225  253 LEU   A CB  
1971 C  CG  . LEU   A 253 ? 0.24443 0.33664 0.17646 -0.01235 0.03217  0.07585  253 LEU   A CG  
1972 C  CD1 . LEU   A 253 ? 0.23755 0.32130 0.19191 -0.00946 0.02495  0.07564  253 LEU   A CD1 
1973 C  CD2 . LEU   A 253 ? 0.29582 0.38960 0.23360 -0.01270 0.04472  0.07080  253 LEU   A CD2 
1974 N  N   . SER   A 254 ? 0.32706 0.42885 0.22071 -0.01830 0.02849  0.11183  254 SER   A N   
1975 C  CA  . SER   A 254 ? 0.34197 0.44414 0.23276 -0.01932 0.02872  0.12540  254 SER   A CA  
1976 C  C   . SER   A 254 ? 0.37175 0.47736 0.23998 -0.02330 0.03792  0.12374  254 SER   A C   
1977 O  O   . SER   A 254 ? 0.40880 0.51379 0.27944 -0.02467 0.04554  0.13249  254 SER   A O   
1978 C  CB  . SER   A 254 ? 0.33293 0.43736 0.22166 -0.01792 0.01615  0.13219  254 SER   A CB  
1979 O  OG  . SER   A 254 ? 0.38528 0.48918 0.27750 -0.01773 0.01608  0.14706  254 SER   A OG  
1980 N  N   . ALA   A 255 ? 0.37469 0.48273 0.22053 -0.02545 0.03783  0.11199  255 ALA   A N   
1981 C  CA  . ALA   A 255 ? 0.43214 0.54141 0.25295 -0.02906 0.04670  0.10957  255 ALA   A CA  
1982 C  C   . ALA   A 255 ? 0.41895 0.52673 0.24493 -0.02908 0.06306  0.10447  255 ALA   A C   
1983 O  O   . ALA   A 255 ? 0.46564 0.57396 0.28154 -0.03129 0.07319  0.10905  255 ALA   A O   
1984 C  CB  . ALA   A 255 ? 0.49497 0.60468 0.29102 -0.03148 0.04213  0.09679  255 ALA   A CB  
1985 N  N   . GLN   A 256 ? 0.40248 0.50927 0.24535 -0.02659 0.06606  0.09545  256 GLN   A N   
1986 C  CA  . GLN   A 256 ? 0.40377 0.51133 0.25774 -0.02595 0.08114  0.09079  256 GLN   A CA  
1987 C  C   . GLN   A 256 ? 0.40814 0.51693 0.28371 -0.02648 0.08512  0.10459  256 GLN   A C   
1988 O  O   . GLN   A 256 ? 0.44440 0.55548 0.32219 -0.02806 0.09806  0.10562  256 GLN   A O   
1989 C  CB  . GLN   A 256 ? 0.41009 0.51757 0.27960 -0.02272 0.08143  0.07914  256 GLN   A CB  
1990 C  CG  . GLN   A 256 ? 0.44071 0.55063 0.32398 -0.02111 0.09655  0.07283  256 GLN   A CG  
1991 C  CD  . GLN   A 256 ? 0.44146 0.55257 0.34753 -0.01720 0.09464  0.06605  256 GLN   A CD  
1992 O  OE1 . GLN   A 256 ? 0.49110 0.60020 0.39492 -0.01622 0.08366  0.06226  256 GLN   A OE1 
1993 N  NE2 . GLN   A 256 ? 0.46823 0.58321 0.39821 -0.01506 0.10459  0.06520  256 GLN   A NE2 
1994 N  N   . THR   A 257 ? 0.38949 0.49587 0.28167 -0.02540 0.07456  0.11490  257 THR   A N   
1995 C  CA  . THR   A 257 ? 0.35698 0.46168 0.27082 -0.02639 0.07740  0.12698  257 THR   A CA  
1996 C  C   . THR   A 257 ? 0.38056 0.48437 0.28382 -0.02869 0.07618  0.14058  257 THR   A C   
1997 O  O   . THR   A 257 ? 0.40387 0.50650 0.32067 -0.03067 0.08145  0.15006  257 THR   A O   
1998 C  CB  . THR   A 257 ? 0.35872 0.45782 0.29743 -0.02405 0.06827  0.12987  257 THR   A CB  
1999 O  OG1 . THR   A 257 ? 0.34805 0.44433 0.27876 -0.02183 0.05579  0.13193  257 THR   A OG1 
2000 C  CG2 . THR   A 257 ? 0.28043 0.38113 0.23228 -0.02232 0.07063  0.11824  257 THR   A CG2 
2001 N  N   . GLY   A 258 ? 0.40152 0.50629 0.28198 -0.02879 0.06896  0.14203  258 GLY   A N   
2002 C  CA  . GLY   A 258 ? 0.39636 0.50097 0.26897 -0.03034 0.06608  0.15646  258 GLY   A CA  
2003 C  C   . GLY   A 258 ? 0.37075 0.47019 0.26475 -0.02772 0.05655  0.16824  258 GLY   A C   
2004 O  O   . GLY   A 258 ? 0.41983 0.51820 0.31342 -0.02857 0.05551  0.18183  258 GLY   A O   
2005 N  N   . ILE   A 259 ? 0.33469 0.42989 0.24728 -0.02440 0.05035  0.16339  259 ILE   A N   
2006 C  CA  . ILE   A 259 ? 0.36497 0.45265 0.29822 -0.02130 0.04265  0.17238  259 ILE   A CA  
2007 C  C   . ILE   A 259 ? 0.35755 0.44725 0.28547 -0.01771 0.03075  0.17047  259 ILE   A C   
2008 O  O   . ILE   A 259 ? 0.31479 0.40616 0.24080 -0.01644 0.02742  0.15892  259 ILE   A O   
2009 C  CB  . ILE   A 259 ? 0.34972 0.42934 0.30873 -0.02064 0.04499  0.16840  259 ILE   A CB  
2010 C  CG1 . ILE   A 259 ? 0.36495 0.44383 0.33320 -0.02492 0.05570  0.17206  259 ILE   A CG1 
2011 C  CG2 . ILE   A 259 ? 0.34045 0.40957 0.31799 -0.01697 0.03723  0.17440  259 ILE   A CG2 
2012 C  CD1 . ILE   A 259 ? 0.36736 0.44264 0.35614 -0.02580 0.05844  0.16424  259 ILE   A CD1 
2013 N  N   . ALA   A 260 ? 0.36263 0.45321 0.28907 -0.01626 0.02451  0.18221  260 ALA   A N   
2014 C  CA  . ALA   A 260 ? 0.36116 0.45583 0.28580 -0.01303 0.01323  0.18182  260 ALA   A CA  
2015 C  C   . ALA   A 260 ? 0.31925 0.40654 0.26572 -0.00849 0.00954  0.17630  260 ALA   A C   
2016 O  O   . ALA   A 260 ? 0.33877 0.41549 0.30434 -0.00718 0.01357  0.17848  260 ALA   A O   
2017 C  CB  . ALA   A 260 ? 0.34914 0.44623 0.27435 -0.01167 0.00804  0.19757  260 ALA   A CB  
2018 N  N   . VAL   A 261 ? 0.31612 0.40831 0.25912 -0.00675 0.00210  0.16843  261 VAL   A N   
2019 C  CA  . VAL   A 261 ? 0.30591 0.39130 0.26725 -0.00251 -0.00077 0.16235  261 VAL   A CA  
2020 C  C   . VAL   A 261 ? 0.30066 0.37632 0.28383 0.00215  -0.00152 0.17245  261 VAL   A C   
2021 O  O   . VAL   A 261 ? 0.29338 0.35675 0.29288 0.00388  0.00204  0.16983  261 VAL   A O   
2022 C  CB  . VAL   A 261 ? 0.33171 0.42514 0.28659 -0.00159 -0.00911 0.15445  261 VAL   A CB  
2023 C  CG1 . VAL   A 261 ? 0.26217 0.34858 0.23667 0.00347  -0.01184 0.14990  261 VAL   A CG1 
2024 C  CG2 . VAL   A 261 ? 0.30180 0.40117 0.23611 -0.00635 -0.00723 0.14215  261 VAL   A CG2 
2025 N  N   . LEU   A 262 ? 0.31726 0.39761 0.30065 0.00391  -0.00585 0.18406  262 LEU   A N   
2026 C  CA  . LEU   A 262 ? 0.35612 0.42700 0.36056 0.00897  -0.00593 0.19395  262 LEU   A CA  
2027 C  C   . LEU   A 262 ? 0.33483 0.39273 0.34832 0.00726  0.00209  0.19887  262 LEU   A C   
2028 O  O   . LEU   A 262 ? 0.32620 0.37032 0.35893 0.01075  0.00408  0.20131  262 LEU   A O   
2029 C  CB  . LEU   A 262 ? 0.34778 0.42838 0.35024 0.01077  -0.01195 0.20707  262 LEU   A CB  
2030 C  CG  . LEU   A 262 ? 0.36384 0.45544 0.36765 0.01362  -0.02068 0.20521  262 LEU   A CG  
2031 C  CD1 . LEU   A 262 ? 0.34269 0.42609 0.36434 0.01873  -0.02032 0.19642  262 LEU   A CD1 
2032 C  CD2 . LEU   A 262 ? 0.39157 0.49664 0.37118 0.00784  -0.02502 0.19724  262 LEU   A CD2 
2033 N  N   . ASP   A 263 ? 0.32787 0.38949 0.32788 0.00158  0.00727  0.20006  263 ASP   A N   
2034 C  CA  . ASP   A 263 ? 0.35561 0.40620 0.36530 -0.00140 0.01528  0.20343  263 ASP   A CA  
2035 C  C   . ASP   A 263 ? 0.30955 0.34980 0.33137 -0.00216 0.01848  0.19148  263 ASP   A C   
2036 O  O   . ASP   A 263 ? 0.29163 0.31741 0.33039 -0.00265 0.02187  0.19261  263 ASP   A O   
2037 C  CB  . ASP   A 263 ? 0.34921 0.40817 0.34153 -0.00741 0.02118  0.20643  263 ASP   A CB  
2038 C  CG  . ASP   A 263 ? 0.41905 0.48485 0.40048 -0.00780 0.01934  0.22070  263 ASP   A CG  
2039 O  OD1 . ASP   A 263 ? 0.41754 0.48359 0.40556 -0.00328 0.01265  0.22866  263 ASP   A OD1 
2040 O  OD2 . ASP   A 263 ? 0.38506 0.45638 0.35155 -0.01264 0.02506  0.22421  263 ASP   A OD2 
2041 N  N   . MET   A 264 ? 0.31374 0.36074 0.32660 -0.00292 0.01726  0.17976  264 MET   A N   
2042 C  CA  . MET   A 264 ? 0.27601 0.31411 0.30022 -0.00371 0.01935  0.16921  264 MET   A CA  
2043 C  C   . MET   A 264 ? 0.30816 0.33359 0.34783 0.00148  0.01538  0.16714  264 MET   A C   
2044 O  O   . MET   A 264 ? 0.29854 0.30980 0.35190 0.00029  0.01791  0.16234  264 MET   A O   
2045 C  CB  . MET   A 264 ? 0.23875 0.28722 0.24998 -0.00510 0.01887  0.15812  264 MET   A CB  
2046 C  CG  . MET   A 264 ? 0.26991 0.31178 0.29177 -0.00705 0.02151  0.14832  264 MET   A CG  
2047 S  SD  . MET   A 264 ? 0.27849 0.31692 0.31087 -0.01372 0.03056  0.15149  264 MET   A SD  
2048 C  CE  . MET   A 264 ? 0.25485 0.31039 0.27146 -0.01674 0.03680  0.14525  264 MET   A CE  
2049 N  N   . CYS   A 265 ? 0.27359 0.30395 0.31148 0.00683  0.00951  0.17029  265 CYS   A N   
2050 C  CA  . CYS   A 265 ? 0.29740 0.31614 0.35090 0.01267  0.00756  0.16916  265 CYS   A CA  
2051 C  C   . CYS   A 265 ? 0.28842 0.29083 0.35688 0.01301  0.01195  0.17604  265 CYS   A C   
2052 O  O   . CYS   A 265 ? 0.27756 0.26327 0.35876 0.01450  0.01411  0.16993  265 CYS   A O   
2053 C  CB  . CYS   A 265 ? 0.30012 0.33005 0.35154 0.01794  0.00118  0.17356  265 CYS   A CB  
2054 S  SG  . CYS   A 265 ? 0.29221 0.33771 0.32972 0.01757  -0.00488 0.16309  265 CYS   A SG  
2055 N  N   . ALA   A 266 ? 0.30778 0.31375 0.37393 0.01130  0.01345  0.18837  266 ALA   A N   
2056 C  CA  . ALA   A 266 ? 0.33581 0.32560 0.41605 0.01075  0.01793  0.19514  266 ALA   A CA  
2057 C  C   . ALA   A 266 ? 0.35207 0.32850 0.43875 0.00454  0.02290  0.18652  266 ALA   A C   
2058 O  O   . ALA   A 266 ? 0.36674 0.32418 0.46716 0.00442  0.02549  0.18434  266 ALA   A O   
2059 C  CB  . ALA   A 266 ? 0.36832 0.36566 0.44308 0.00891  0.01891  0.21030  266 ALA   A CB  
2060 N  N   . SER   A 267 ? 0.30947 0.29562 0.38667 -0.00105 0.02428  0.18093  267 SER   A N   
2061 C  CA  . SER   A 267 ? 0.32840 0.30512 0.41345 -0.00765 0.02797  0.17261  267 SER   A CA  
2062 C  C   . SER   A 267 ? 0.31230 0.27632 0.40452 -0.00600 0.02570  0.15982  267 SER   A C   
2063 O  O   . SER   A 267 ? 0.33284 0.27973 0.43618 -0.00976 0.02751  0.15436  267 SER   A O   
2064 C  CB  . SER   A 267 ? 0.30876 0.30122 0.38370 -0.01290 0.03042  0.16970  267 SER   A CB  
2065 O  OG  . SER   A 267 ? 0.35825 0.36114 0.42483 -0.01491 0.03386  0.18042  267 SER   A OG  
2066 N  N   . LEU   A 268 ? 0.32131 0.29328 0.40608 -0.00112 0.02163  0.15432  268 LEU   A N   
2067 C  CA  . LEU   A 268 ? 0.29017 0.25022 0.38033 0.00125  0.01981  0.14276  268 LEU   A CA  
2068 C  C   . LEU   A 268 ? 0.31896 0.26021 0.42040 0.00561  0.02127  0.14339  268 LEU   A C   
2069 O  O   . LEU   A 268 ? 0.33658 0.25990 0.44466 0.00357  0.02276  0.13351  268 LEU   A O   
2070 C  CB  . LEU   A 268 ? 0.28783 0.26117 0.36824 0.00638  0.01529  0.13884  268 LEU   A CB  
2071 C  CG  . LEU   A 268 ? 0.25151 0.21551 0.33517 0.00930  0.01355  0.12703  268 LEU   A CG  
2072 C  CD1 . LEU   A 268 ? 0.25652 0.20813 0.34498 0.00208  0.01517  0.11708  268 LEU   A CD1 
2073 C  CD2 . LEU   A 268 ? 0.27582 0.25615 0.34886 0.01257  0.00899  0.12387  268 LEU   A CD2 
2074 N  N   . LYS   A 269 ? 0.34328 0.28825 0.44658 0.01131  0.02096  0.15453  269 LYS   A N   
2075 C  CA  . LYS   A 269 ? 0.34360 0.27115 0.45925 0.01600  0.02355  0.15671  269 LYS   A CA  
2076 C  C   . LYS   A 269 ? 0.35136 0.25836 0.47500 0.00927  0.02794  0.15372  269 LYS   A C   
2077 O  O   . LYS   A 269 ? 0.35800 0.24485 0.48805 0.00962  0.03022  0.14422  269 LYS   A O   
2078 C  CB  . LYS   A 269 ? 0.36944 0.30692 0.48708 0.02144  0.02235  0.17220  269 LYS   A CB  
2079 C  CG  . LYS   A 269 ? 0.43686 0.35702 0.56912 0.02605  0.02598  0.17771  269 LYS   A CG  
2080 C  CD  . LYS   A 269 ? 0.41720 0.35042 0.55308 0.03342  0.02327  0.19193  269 LYS   A CD  
2081 C  CE  . LYS   A 269 ? 0.54754 0.46379 0.69927 0.03750  0.02764  0.20042  269 LYS   A CE  
2082 N  NZ  . LYS   A 269 ? 0.51364 0.43965 0.67421 0.04659  0.02548  0.21157  269 LYS   A NZ  
2083 N  N   . GLU   A 270 ? 0.35284 0.26476 0.47532 0.00241  0.02934  0.16099  270 GLU   A N   
2084 C  CA  . GLU   A 270 ? 0.39581 0.29008 0.52657 -0.00548 0.03288  0.15849  270 GLU   A CA  
2085 C  C   . GLU   A 270 ? 0.37306 0.25844 0.50364 -0.01230 0.03203  0.14242  270 GLU   A C   
2086 O  O   . GLU   A 270 ? 0.39678 0.26108 0.53360 -0.01671 0.03363  0.13479  270 GLU   A O   
2087 C  CB  . GLU   A 270 ? 0.38695 0.29139 0.51690 -0.01158 0.03495  0.16992  270 GLU   A CB  
2088 C  CG  . GLU   A 270 ? 0.42220 0.33601 0.55015 -0.00562 0.03501  0.18597  270 GLU   A CG  
2089 C  CD  . GLU   A 270 ? 0.51272 0.40744 0.65275 -0.00097 0.03697  0.19111  270 GLU   A CD  
2090 O  OE1 . GLU   A 270 ? 0.52384 0.42450 0.66485 0.00704  0.03550  0.20114  270 GLU   A OE1 
2091 O  OE2 . GLU   A 270 ? 0.54258 0.41619 0.69148 -0.00581 0.03994  0.18501  270 GLU   A OE2 
2092 N  N   . LEU   A 271 ? 0.34169 0.24251 0.46459 -0.01376 0.02918  0.13689  271 LEU   A N   
2093 C  CA  . LEU   A 271 ? 0.32689 0.22103 0.45012 -0.02041 0.02734  0.12229  271 LEU   A CA  
2094 C  C   . LEU   A 271 ? 0.35226 0.22773 0.47548 -0.01636 0.02692  0.11077  271 LEU   A C   
2095 O  O   . LEU   A 271 ? 0.37399 0.23346 0.49864 -0.02311 0.02646  0.09886  271 LEU   A O   
2096 C  CB  . LEU   A 271 ? 0.32935 0.24414 0.44529 -0.02131 0.02458  0.11989  271 LEU   A CB  
2097 C  CG  . LEU   A 271 ? 0.28361 0.21446 0.40030 -0.02762 0.02654  0.12698  271 LEU   A CG  
2098 C  CD1 . LEU   A 271 ? 0.28785 0.23933 0.39601 -0.02645 0.02518  0.12562  271 LEU   A CD1 
2099 C  CD2 . LEU   A 271 ? 0.34539 0.26789 0.47215 -0.03831 0.02676  0.12097  271 LEU   A CD2 
2100 N  N   . LEU   A 272 ? 0.35366 0.23176 0.47473 -0.00569 0.02713  0.11387  272 LEU   A N   
2101 C  CA  . LEU   A 272 ? 0.36673 0.22882 0.48802 -0.00045 0.02840  0.10321  272 LEU   A CA  
2102 C  C   . LEU   A 272 ? 0.41514 0.25312 0.54370 -0.00093 0.03280  0.10174  272 LEU   A C   
2103 O  O   . LEU   A 272 ? 0.44721 0.26563 0.57393 -0.00353 0.03430  0.08801  272 LEU   A O   
2104 C  CB  . LEU   A 272 ? 0.33428 0.20932 0.45393 0.01099  0.02764  0.10831  272 LEU   A CB  
2105 C  CG  . LEU   A 272 ? 0.31575 0.21044 0.42657 0.01127  0.02317  0.10611  272 LEU   A CG  
2106 C  CD1 . LEU   A 272 ? 0.35128 0.26172 0.46081 0.02104  0.02135  0.11314  272 LEU   A CD1 
2107 C  CD2 . LEU   A 272 ? 0.34007 0.22486 0.44692 0.00773  0.02244  0.09018  272 LEU   A CD2 
2108 N  N   . GLN   A 273 ? 0.41479 0.25324 0.55044 0.00101  0.03492  0.11550  273 GLN   A N   
2109 C  CA  . GLN   A 273 ? 0.44433 0.25928 0.58816 0.00134  0.03945  0.11563  273 GLN   A CA  
2110 C  C   . GLN   A 273 ? 0.46975 0.26885 0.61438 -0.01148 0.03971  0.10923  273 GLN   A C   
2111 O  O   . GLN   A 273 ? 0.50338 0.27776 0.65026 -0.01385 0.04258  0.10106  273 GLN   A O   
2112 C  CB  . GLN   A 273 ? 0.45244 0.27376 0.60455 0.00781  0.04120  0.13374  273 GLN   A CB  
2113 C  CG  . GLN   A 273 ? 0.45056 0.28205 0.60568 0.02054  0.04129  0.13960  273 GLN   A CG  
2114 C  CD  . GLN   A 273 ? 0.49372 0.34147 0.65329 0.02492  0.03996  0.15906  273 GLN   A CD  
2115 O  OE1 . GLN   A 273 ? 0.52078 0.38308 0.68213 0.03348  0.03806  0.16599  273 GLN   A OE1 
2116 N  NE2 . GLN   A 273 ? 0.53371 0.38002 0.69477 0.01834  0.04067  0.16814  273 GLN   A NE2 
2117 N  N   . ASN   A 274 ? 0.43888 0.25215 0.58187 -0.02015 0.03686  0.11241  274 ASN   A N   
2118 C  CA  . ASN   A 274 ? 0.44864 0.25126 0.59512 -0.03292 0.03677  0.10919  274 ASN   A CA  
2119 C  C   . ASN   A 274 ? 0.46127 0.26613 0.60215 -0.04289 0.03230  0.09495  274 ASN   A C   
2120 O  O   . ASN   A 274 ? 0.47114 0.26637 0.61463 -0.05465 0.03111  0.08971  274 ASN   A O   
2121 C  CB  . ASN   A 274 ? 0.48843 0.30646 0.64038 -0.03623 0.03786  0.12506  274 ASN   A CB  
2122 C  CG  . ASN   A 274 ? 0.52379 0.33767 0.68173 -0.02868 0.04161  0.13984  274 ASN   A CG  
2123 O  OD1 . ASN   A 274 ? 0.54927 0.34356 0.71123 -0.02342 0.04413  0.13782  274 ASN   A OD1 
2124 N  ND2 . ASN   A 274 ? 0.54231 0.37481 0.70075 -0.02804 0.04227  0.15493  274 ASN   A ND2 
2125 N  N   . GLY   A 275 ? 0.48476 0.30260 0.61858 -0.03903 0.02932  0.08900  275 GLY   A N   
2126 C  CA  . GLY   A 275 ? 0.47577 0.30123 0.60617 -0.04845 0.02435  0.07872  275 GLY   A CA  
2127 C  C   . GLY   A 275 ? 0.48484 0.33140 0.62175 -0.05462 0.02351  0.08847  275 GLY   A C   
2128 O  O   . GLY   A 275 ? 0.45491 0.31197 0.59549 -0.05064 0.02687  0.10271  275 GLY   A O   
2129 N  N   . MET   A 276 ? 0.51076 0.36423 0.64889 -0.06469 0.01898  0.08033  276 MET   A N   
2130 C  CA  . MET   A 276 ? 0.47631 0.35305 0.62164 -0.06973 0.01841  0.08760  276 MET   A CA  
2131 C  C   . MET   A 276 ? 0.51636 0.38877 0.67161 -0.08138 0.01876  0.08911  276 MET   A C   
2132 O  O   . MET   A 276 ? 0.49963 0.39081 0.66306 -0.08490 0.02023  0.09715  276 MET   A O   
2133 C  CB  . MET   A 276 ? 0.48817 0.38072 0.63091 -0.07154 0.01281  0.07925  276 MET   A CB  
2134 C  CG  . MET   A 276 ? 0.44194 0.35197 0.57964 -0.06160 0.01436  0.08570  276 MET   A CG  
2135 S  SD  . MET   A 276 ? 0.47571 0.40794 0.61431 -0.06449 0.00897  0.07952  276 MET   A SD  
2136 C  CE  . MET   A 276 ? 0.31137 0.23887 0.43743 -0.05454 0.00723  0.07438  276 MET   A CE  
2137 N  N   . ASN   A 277 ? 0.56263 0.41033 0.71691 -0.08738 0.01809  0.08148  277 ASN   A N   
2138 C  CA  . ASN   A 277 ? 0.56960 0.40904 0.73285 -0.09873 0.01890  0.08354  277 ASN   A CA  
2139 C  C   . ASN   A 277 ? 0.54254 0.40142 0.71414 -0.10961 0.01424  0.08076  277 ASN   A C   
2140 O  O   . ASN   A 277 ? 0.53204 0.40104 0.71551 -0.11535 0.01664  0.08968  277 ASN   A O   
2141 C  CB  . ASN   A 277 ? 0.57708 0.41716 0.74749 -0.09476 0.02573  0.10012  277 ASN   A CB  
2142 C  CG  . ASN   A 277 ? 0.65883 0.48075 0.83682 -0.10513 0.02736  0.10140  277 ASN   A CG  
2143 O  OD1 . ASN   A 277 ? 0.69284 0.50213 0.87016 -0.11624 0.02320  0.08943  277 ASN   A OD1 
2144 N  ND2 . ASN   A 277 ? 0.71271 0.53340 0.89712 -0.10242 0.03316  0.11609  277 ASN   A ND2 
2145 N  N   . GLY   A 278 ? 0.51245 0.37756 0.67861 -0.11215 0.00753  0.06879  278 GLY   A N   
2146 C  CA  . GLY   A 278 ? 0.47406 0.35832 0.64903 -0.12175 0.00181  0.06554  278 GLY   A CA  
2147 C  C   . GLY   A 278 ? 0.46855 0.38356 0.65193 -0.11627 0.00288  0.07455  278 GLY   A C   
2148 O  O   . GLY   A 278 ? 0.50114 0.43461 0.69465 -0.12259 -0.00129 0.07354  278 GLY   A O   
2149 N  N   . ARG   A 279 ? 0.44210 0.36336 0.62135 -0.10469 0.00854  0.08322  279 ARG   A N   
2150 C  CA  . ARG   A 279 ? 0.37337 0.32162 0.55748 -0.09934 0.01114  0.09081  279 ARG   A CA  
2151 C  C   . ARG   A 279 ? 0.35183 0.30745 0.52666 -0.09210 0.00742  0.08446  279 ARG   A C   
2152 O  O   . ARG   A 279 ? 0.38268 0.32267 0.54674 -0.08969 0.00395  0.07609  279 ARG   A O   
2153 C  CB  . ARG   A 279 ? 0.38105 0.33347 0.56468 -0.09276 0.02032  0.10513  279 ARG   A CB  
2154 C  CG  . ARG   A 279 ? 0.39973 0.35007 0.59483 -0.10044 0.02444  0.11318  279 ARG   A CG  
2155 C  CD  . ARG   A 279 ? 0.41436 0.36083 0.60552 -0.09462 0.03239  0.12663  279 ARG   A CD  
2156 N  NE  . ARG   A 279 ? 0.48545 0.40953 0.66675 -0.08890 0.03203  0.12585  279 ARG   A NE  
2157 C  CZ  . ARG   A 279 ? 0.43482 0.35277 0.61239 -0.08320 0.03720  0.13727  279 ARG   A CZ  
2158 N  NH1 . ARG   A 279 ? 0.45565 0.38611 0.63655 -0.08371 0.04319  0.15008  279 ARG   A NH1 
2159 N  NH2 . ARG   A 279 ? 0.41445 0.31399 0.58487 -0.07659 0.03646  0.13608  279 ARG   A NH2 
2160 N  N   . THR   A 280 ? 0.31775 0.29704 0.49701 -0.08858 0.00890  0.08829  280 THR   A N   
2161 C  CA  . THR   A 280 ? 0.28332 0.27157 0.45536 -0.08216 0.00586  0.08324  280 THR   A CA  
2162 C  C   . THR   A 280 ? 0.24170 0.24406 0.40942 -0.07317 0.01385  0.09224  280 THR   A C   
2163 O  O   . THR   A 280 ? 0.23183 0.24160 0.40296 -0.07257 0.02131  0.10184  280 THR   A O   
2164 C  CB  . THR   A 280 ? 0.28852 0.29186 0.46870 -0.08665 -0.00132 0.07655  280 THR   A CB  
2165 O  OG1 . THR   A 280 ? 0.25902 0.28226 0.45338 -0.08789 0.00319  0.08385  280 THR   A OG1 
2166 C  CG2 . THR   A 280 ? 0.30740 0.29711 0.48767 -0.09658 -0.00991 0.06699  280 THR   A CG2 
2167 N  N   . ILE   A 281 ? 0.23663 0.24202 0.39491 -0.06669 0.01233  0.08862  281 ILE   A N   
2168 C  CA  . ILE   A 281 ? 0.22987 0.24860 0.38051 -0.05875 0.01913  0.09477  281 ILE   A CA  
2169 C  C   . ILE   A 281 ? 0.23665 0.26923 0.38753 -0.05605 0.01591  0.08733  281 ILE   A C   
2170 O  O   . ILE   A 281 ? 0.21357 0.23858 0.35601 -0.05392 0.00842  0.07726  281 ILE   A O   
2171 C  CB  . ILE   A 281 ? 0.21944 0.22642 0.35490 -0.05189 0.02066  0.09828  281 ILE   A CB  
2172 C  CG1 . ILE   A 281 ? 0.22998 0.22159 0.36580 -0.05308 0.02298  0.10498  281 ILE   A CG1 
2173 C  CG2 . ILE   A 281 ? 0.19318 0.21503 0.31531 -0.04399 0.02601  0.10159  281 ILE   A CG2 
2174 C  CD1 . ILE   A 281 ? 0.23491 0.21706 0.35781 -0.04482 0.02410  0.11010  281 ILE   A CD1 
2175 N  N   . LEU   A 282 ? 0.23202 0.28383 0.38994 -0.05453 0.02198  0.09073  282 LEU   A N   
2176 C  CA  . LEU   A 282 ? 0.24019 0.30515 0.39958 -0.05030 0.02005  0.08365  282 LEU   A CA  
2177 C  C   . LEU   A 282 ? 0.23298 0.29512 0.40159 -0.05573 0.00859  0.07624  282 LEU   A C   
2178 O  O   . LEU   A 282 ? 0.20180 0.26288 0.36175 -0.05150 0.00260  0.06794  282 LEU   A O   
2179 C  CB  . LEU   A 282 ? 0.18232 0.24515 0.31960 -0.04047 0.02100  0.07803  282 LEU   A CB  
2180 C  CG  . LEU   A 282 ? 0.20616 0.27720 0.33307 -0.03558 0.03191  0.08395  282 LEU   A CG  
2181 C  CD1 . LEU   A 282 ? 0.19399 0.26147 0.29810 -0.02787 0.03083  0.07808  282 LEU   A CD1 
2182 C  CD2 . LEU   A 282 ? 0.20585 0.29502 0.34607 -0.03536 0.04083  0.08641  282 LEU   A CD2 
2183 N  N   . GLY   A 283 ? 0.23053 0.28928 0.40985 -0.06365 0.00493  0.07711  283 GLY   A N   
2184 C  CA  . GLY   A 283 ? 0.24615 0.30232 0.42989 -0.06962 -0.00643 0.06972  283 GLY   A CA  
2185 C  C   . GLY   A 283 ? 0.28500 0.32188 0.45501 -0.07202 -0.01419 0.06165  283 GLY   A C   
2186 O  O   . GLY   A 283 ? 0.26807 0.30366 0.43577 -0.07563 -0.02367 0.05418  283 GLY   A O   
2187 N  N   . SER   A 284 ? 0.23318 0.25489 0.39282 -0.06948 -0.01001 0.06322  284 SER   A N   
2188 C  CA  . SER   A 284 ? 0.25487 0.25590 0.39923 -0.06931 -0.01506 0.05446  284 SER   A CA  
2189 C  C   . SER   A 284 ? 0.26703 0.24808 0.41233 -0.07398 -0.01213 0.05701  284 SER   A C   
2190 O  O   . SER   A 284 ? 0.23500 0.21687 0.38402 -0.07172 -0.00437 0.06664  284 SER   A O   
2191 C  CB  . SER   A 284 ? 0.25871 0.25813 0.38471 -0.05733 -0.01237 0.05132  284 SER   A CB  
2192 O  OG  . SER   A 284 ? 0.28179 0.26252 0.39456 -0.05638 -0.01571 0.04311  284 SER   A OG  
2193 N  N   . ALA   A 285 ? 0.26484 0.22776 0.40335 -0.07940 -0.01766 0.04730  285 ALA   A N   
2194 C  CA  . ALA   A 285 ? 0.27730 0.21745 0.41289 -0.08161 -0.01396 0.04675  285 ALA   A CA  
2195 C  C   . ALA   A 285 ? 0.29276 0.21494 0.41642 -0.07346 -0.01092 0.04405  285 ALA   A C   
2196 O  O   . ALA   A 285 ? 0.32174 0.22267 0.44196 -0.07343 -0.00738 0.04210  285 ALA   A O   
2197 C  CB  . ALA   A 285 ? 0.31383 0.24310 0.44824 -0.09283 -0.01985 0.03689  285 ALA   A CB  
2198 N  N   . LEU   A 286 ? 0.27562 0.20860 0.38921 -0.06391 -0.01100 0.04259  286 LEU   A N   
2199 C  CA  . LEU   A 286 ? 0.31898 0.24206 0.41916 -0.05350 -0.00790 0.03944  286 LEU   A CA  
2200 C  C   . LEU   A 286 ? 0.30023 0.23940 0.39824 -0.04355 -0.00347 0.04905  286 LEU   A C   
2201 O  O   . LEU   A 286 ? 0.26235 0.22077 0.36370 -0.04382 -0.00373 0.05300  286 LEU   A O   
2202 C  CB  . LEU   A 286 ? 0.32429 0.24695 0.41100 -0.05224 -0.01328 0.02676  286 LEU   A CB  
2203 C  CG  . LEU   A 286 ? 0.33375 0.23636 0.41364 -0.05978 -0.01679 0.01446  286 LEU   A CG  
2204 C  CD1 . LEU   A 286 ? 0.35932 0.26560 0.42364 -0.05699 -0.02095 0.00450  286 LEU   A CD1 
2205 C  CD2 . LEU   A 286 ? 0.42479 0.30153 0.50461 -0.05766 -0.00987 0.01353  286 LEU   A CD2 
2206 N  N   . LEU   A 287 ? 0.26562 0.19737 0.35805 -0.03482 0.00058  0.05254  287 LEU   A N   
2207 C  CA  . LEU   A 287 ? 0.26194 0.20974 0.34918 -0.02647 0.00279  0.06010  287 LEU   A CA  
2208 C  C   . LEU   A 287 ? 0.24050 0.19921 0.31751 -0.02267 -0.00117 0.05121  287 LEU   A C   
2209 O  O   . LEU   A 287 ? 0.26514 0.21553 0.33553 -0.01941 -0.00260 0.04358  287 LEU   A O   
2210 C  CB  . LEU   A 287 ? 0.25084 0.18976 0.33762 -0.01879 0.00686  0.06839  287 LEU   A CB  
2211 C  CG  . LEU   A 287 ? 0.28115 0.20653 0.37935 -0.02278 0.01102  0.07811  287 LEU   A CG  
2212 C  CD1 . LEU   A 287 ? 0.30766 0.22128 0.40862 -0.01462 0.01492  0.08726  287 LEU   A CD1 
2213 C  CD2 . LEU   A 287 ? 0.27771 0.21785 0.38072 -0.02746 0.01314  0.08865  287 LEU   A CD2 
2214 N  N   . GLU   A 288 ? 0.21938 0.19585 0.29587 -0.02323 -0.00202 0.05221  288 GLU   A N   
2215 C  CA  . GLU   A 288 ? 0.21972 0.20645 0.28869 -0.02040 -0.00545 0.04488  288 GLU   A CA  
2216 C  C   . GLU   A 288 ? 0.18930 0.18154 0.24867 -0.01237 -0.00417 0.04687  288 GLU   A C   
2217 O  O   . GLU   A 288 ? 0.18516 0.18473 0.24295 -0.00997 -0.00098 0.05508  288 GLU   A O   
2218 C  CB  . GLU   A 288 ? 0.23008 0.23234 0.30499 -0.02341 -0.00522 0.04616  288 GLU   A CB  
2219 C  CG  . GLU   A 288 ? 0.29485 0.30609 0.36730 -0.02240 -0.00915 0.03899  288 GLU   A CG  
2220 C  CD  . GLU   A 288 ? 0.35453 0.35687 0.42183 -0.02385 -0.01518 0.03051  288 GLU   A CD  
2221 O  OE1 . GLU   A 288 ? 0.30415 0.29670 0.37514 -0.03015 -0.01806 0.02810  288 GLU   A OE1 
2222 O  OE2 . GLU   A 288 ? 0.31792 0.32249 0.37641 -0.01926 -0.01668 0.02623  288 GLU   A OE2 
2223 N  N   . ASP   A 289 ? 0.20093 0.19122 0.25339 -0.00900 -0.00693 0.03974  289 ASP   A N   
2224 C  CA  . ASP   A 289 ? 0.20296 0.19973 0.24857 -0.00251 -0.00656 0.04197  289 ASP   A CA  
2225 C  C   . ASP   A 289 ? 0.19748 0.20365 0.23658 -0.00135 -0.00937 0.03546  289 ASP   A C   
2226 O  O   . ASP   A 289 ? 0.18350 0.19384 0.21755 0.00276  -0.01016 0.03541  289 ASP   A O   
2227 C  CB  . ASP   A 289 ? 0.19666 0.18230 0.24313 0.00193  -0.00535 0.04279  289 ASP   A CB  
2228 C  CG  . ASP   A 289 ? 0.23555 0.21484 0.27791 0.00266  -0.00679 0.03285  289 ASP   A CG  
2229 O  OD1 . ASP   A 289 ? 0.21425 0.19230 0.25409 -0.00226 -0.00953 0.02557  289 ASP   A OD1 
2230 O  OD2 . ASP   A 289 ? 0.22317 0.19873 0.26570 0.00820  -0.00479 0.03339  289 ASP   A OD2 
2231 N  N   . GLU   A 290 ? 0.17257 0.18299 0.21347 -0.00494 -0.01096 0.03107  290 GLU   A N   
2232 C  CA  . GLU   A 290 ? 0.20491 0.22228 0.24128 -0.00364 -0.01316 0.02580  290 GLU   A CA  
2233 C  C   . GLU   A 290 ? 0.18976 0.21780 0.22630 -0.00346 -0.01065 0.02718  290 GLU   A C   
2234 O  O   . GLU   A 290 ? 0.19489 0.22709 0.23166 -0.00323 -0.01165 0.02287  290 GLU   A O   
2235 C  CB  . GLU   A 290 ? 0.22654 0.23965 0.26423 -0.00664 -0.01722 0.01972  290 GLU   A CB  
2236 C  CG  . GLU   A 290 ? 0.22072 0.22230 0.25365 -0.00619 -0.01798 0.01640  290 GLU   A CG  
2237 C  CD  . GLU   A 290 ? 0.30716 0.30664 0.33422 -0.00749 -0.02158 0.01008  290 GLU   A CD  
2238 O  OE1 . GLU   A 290 ? 0.24604 0.23624 0.26728 -0.00688 -0.02063 0.00642  290 GLU   A OE1 
2239 O  OE2 . GLU   A 290 ? 0.24254 0.24876 0.27136 -0.00942 -0.02490 0.00920  290 GLU   A OE2 
2240 N  N   . PHE   A 291 ? 0.16564 0.19750 0.20101 -0.00317 -0.00669 0.03334  291 PHE   A N   
2241 C  CA  . PHE   A 291 ? 0.15337 0.19449 0.18425 -0.00259 -0.00266 0.03380  291 PHE   A CA  
2242 C  C   . PHE   A 291 ? 0.16847 0.21283 0.18764 -0.00062 -0.00271 0.03715  291 PHE   A C   
2243 O  O   . PHE   A 291 ? 0.15797 0.20090 0.17672 -0.00026 -0.00238 0.04491  291 PHE   A O   
2244 C  CB  . PHE   A 291 ? 0.17127 0.21638 0.20959 -0.00514 0.00272  0.03886  291 PHE   A CB  
2245 C  CG  . PHE   A 291 ? 0.19680 0.24282 0.24880 -0.00765 0.00203  0.03651  291 PHE   A CG  
2246 C  CD1 . PHE   A 291 ? 0.23228 0.28406 0.28783 -0.00613 0.00311  0.03166  291 PHE   A CD1 
2247 C  CD2 . PHE   A 291 ? 0.21603 0.25703 0.27824 -0.01182 -0.00017 0.03940  291 PHE   A CD2 
2248 C  CE1 . PHE   A 291 ? 0.23829 0.29345 0.30894 -0.00814 0.00141  0.03140  291 PHE   A CE1 
2249 C  CE2 . PHE   A 291 ? 0.27099 0.31520 0.34647 -0.01532 -0.00258 0.03793  291 PHE   A CE2 
2250 C  CZ  . PHE   A 291 ? 0.21054 0.26312 0.29091 -0.01316 -0.00211 0.03476  291 PHE   A CZ  
2251 N  N   . THR   A 292 ? 0.16672 0.21539 0.17713 0.00021  -0.00360 0.03198  292 THR   A N   
2252 C  CA  . THR   A 292 ? 0.19039 0.24434 0.18908 0.00053  -0.00509 0.03526  292 THR   A CA  
2253 C  C   . THR   A 292 ? 0.17510 0.23517 0.16500 -0.00121 0.00039  0.03889  292 THR   A C   
2254 O  O   . THR   A 292 ? 0.17464 0.23538 0.16827 -0.00202 0.00644  0.03697  292 THR   A O   
2255 C  CB  . THR   A 292 ? 0.20251 0.25849 0.19430 0.00030  -0.00849 0.02788  292 THR   A CB  
2256 O  OG1 . THR   A 292 ? 0.22786 0.28431 0.21602 -0.00087 -0.00410 0.02069  292 THR   A OG1 
2257 C  CG2 . THR   A 292 ? 0.17471 0.22546 0.17444 0.00175  -0.01251 0.02451  292 THR   A CG2 
2258 N  N   . PRO   A 293 ? 0.20130 0.26701 0.17982 -0.00187 -0.00141 0.04494  293 PRO   A N   
2259 C  CA  . PRO   A 293 ? 0.19446 0.26658 0.15923 -0.00432 0.00404  0.04709  293 PRO   A CA  
2260 C  C   . PRO   A 293 ? 0.24374 0.31618 0.20101 -0.00556 0.00899  0.03533  293 PRO   A C   
2261 O  O   . PRO   A 293 ? 0.22864 0.30319 0.18271 -0.00629 0.01766  0.03462  293 PRO   A O   
2262 C  CB  . PRO   A 293 ? 0.21168 0.29072 0.16381 -0.00536 -0.00211 0.05438  293 PRO   A CB  
2263 C  CG  . PRO   A 293 ? 0.17995 0.25533 0.14645 -0.00193 -0.00756 0.06157  293 PRO   A CG  
2264 C  CD  . PRO   A 293 ? 0.20756 0.27494 0.18645 -0.00024 -0.00800 0.05207  293 PRO   A CD  
2265 N  N   . PHE   A 294 ? 0.22790 0.29742 0.18451 -0.00547 0.00476  0.02625  294 PHE   A N   
2266 C  CA  . PHE   A 294 ? 0.25559 0.32251 0.20700 -0.00612 0.01002  0.01487  294 PHE   A CA  
2267 C  C   . PHE   A 294 ? 0.24447 0.30819 0.21225 -0.00325 0.01671  0.01293  294 PHE   A C   
2268 O  O   . PHE   A 294 ? 0.26035 0.32474 0.22585 -0.00273 0.02574  0.00842  294 PHE   A O   
2269 C  CB  . PHE   A 294 ? 0.32101 0.38418 0.27074 -0.00711 0.00371  0.00682  294 PHE   A CB  
2270 C  CG  . PHE   A 294 ? 0.38192 0.43810 0.33541 -0.00610 0.00895  -0.00406 294 PHE   A CG  
2271 C  CD1 . PHE   A 294 ? 0.36727 0.41909 0.33929 -0.00246 0.01026  -0.00452 294 PHE   A CD1 
2272 C  CD2 . PHE   A 294 ? 0.36038 0.41392 0.29852 -0.00896 0.01271  -0.01354 294 PHE   A CD2 
2273 C  CE1 . PHE   A 294 ? 0.39412 0.43998 0.37163 -0.00064 0.01514  -0.01248 294 PHE   A CE1 
2274 C  CE2 . PHE   A 294 ? 0.37128 0.41642 0.31429 -0.00721 0.01874  -0.02323 294 PHE   A CE2 
2275 C  CZ  . PHE   A 294 ? 0.41376 0.45546 0.37772 -0.00250 0.01994  -0.02182 294 PHE   A CZ  
2276 N  N   . ASP   A 295 ? 0.19870 0.25930 0.18318 -0.00150 0.01236  0.01590  295 ASP   A N   
2277 C  CA  . ASP   A 295 ? 0.20868 0.26857 0.21038 0.00017  0.01629  0.01595  295 ASP   A CA  
2278 C  C   . ASP   A 295 ? 0.22359 0.28922 0.22820 -0.00045 0.02463  0.02160  295 ASP   A C   
2279 O  O   . ASP   A 295 ? 0.21389 0.28236 0.22835 0.00103  0.03185  0.01949  295 ASP   A O   
2280 C  CB  . ASP   A 295 ? 0.19807 0.25426 0.21265 0.00020  0.00934  0.01950  295 ASP   A CB  
2281 C  CG  . ASP   A 295 ? 0.23330 0.28460 0.24659 0.00091  0.00261  0.01458  295 ASP   A CG  
2282 O  OD1 . ASP   A 295 ? 0.23171 0.28205 0.23894 0.00137  0.00342  0.00817  295 ASP   A OD1 
2283 O  OD2 . ASP   A 295 ? 0.21298 0.26070 0.23076 0.00070  -0.00273 0.01697  295 ASP   A OD2 
2284 N  N   . VAL   A 296 ? 0.21001 0.27796 0.20832 -0.00239 0.02415  0.03005  296 VAL   A N   
2285 C  CA  . VAL   A 296 ? 0.20536 0.27892 0.20685 -0.00371 0.03247  0.03709  296 VAL   A CA  
2286 C  C   . VAL   A 296 ? 0.24032 0.31874 0.22799 -0.00349 0.04251  0.03244  296 VAL   A C   
2287 O  O   . VAL   A 296 ? 0.24760 0.33052 0.24435 -0.00252 0.05230  0.03207  296 VAL   A O   
2288 C  CB  . VAL   A 296 ? 0.17790 0.25140 0.17551 -0.00575 0.02965  0.04852  296 VAL   A CB  
2289 C  CG1 . VAL   A 296 ? 0.20168 0.28143 0.20048 -0.00787 0.03920  0.05697  296 VAL   A CG1 
2290 C  CG2 . VAL   A 296 ? 0.18810 0.25424 0.19994 -0.00578 0.02197  0.05142  296 VAL   A CG2 
2291 N  N   . VAL   A 297 ? 0.25965 0.33746 0.22547 -0.00465 0.04046  0.02831  297 VAL   A N   
2292 C  CA  . VAL   A 297 ? 0.27425 0.35442 0.22242 -0.00539 0.05011  0.02152  297 VAL   A CA  
2293 C  C   . VAL   A 297 ? 0.30716 0.38362 0.26623 -0.00182 0.05717  0.01067  297 VAL   A C   
2294 O  O   . VAL   A 297 ? 0.34501 0.42463 0.30492 -0.00026 0.06994  0.00823  297 VAL   A O   
2295 C  CB  . VAL   A 297 ? 0.28508 0.36453 0.20775 -0.00878 0.04391  0.01750  297 VAL   A CB  
2296 C  CG1 . VAL   A 297 ? 0.32199 0.40092 0.22431 -0.01039 0.05400  0.00720  297 VAL   A CG1 
2297 C  CG2 . VAL   A 297 ? 0.33027 0.41553 0.24326 -0.01153 0.03768  0.03047  297 VAL   A CG2 
2298 N  N   . ARG   A 298 ? 0.31588 0.38574 0.28405 -0.00009 0.04965  0.00473  298 ARG   A N   
2299 C  CA  . ARG   A 298 ? 0.35347 0.41901 0.33429 0.00394  0.05533  -0.00379 298 ARG   A CA  
2300 C  C   . ARG   A 298 ? 0.36397 0.43616 0.36791 0.00715  0.06327  0.00163  298 ARG   A C   
2301 O  O   . ARG   A 298 ? 0.41901 0.49245 0.42831 0.01063  0.07525  -0.00310 298 ARG   A O   
2302 C  CB  . ARG   A 298 ? 0.34813 0.40679 0.33847 0.00498  0.04481  -0.00696 298 ARG   A CB  
2303 C  CG  . ARG   A 298 ? 0.40358 0.46111 0.41808 0.00987  0.04809  -0.00833 298 ARG   A CG  
2304 C  CD  . ARG   A 298 ? 0.42555 0.47547 0.44774 0.01118  0.03979  -0.01187 298 ARG   A CD  
2305 N  NE  . ARG   A 298 ? 0.40627 0.45768 0.43757 0.00974  0.02868  -0.00493 298 ARG   A NE  
2306 C  CZ  . ARG   A 298 ? 0.31383 0.36475 0.36213 0.01161  0.02393  -0.00249 298 ARG   A CZ  
2307 N  NH1 . ARG   A 298 ? 0.30268 0.35368 0.36610 0.01592  0.02896  -0.00386 298 ARG   A NH1 
2308 N  NH2 . ARG   A 298 ? 0.29646 0.34695 0.34665 0.00925  0.01416  0.00184  298 ARG   A NH2 
2309 N  N   . GLN   A 299 ? 0.33487 0.41140 0.35374 0.00579  0.05703  0.01144  299 GLN   A N   
2310 C  CA  . GLN   A 299 ? 0.31146 0.39568 0.35530 0.00735  0.06201  0.01722  299 GLN   A CA  
2311 C  C   . GLN   A 299 ? 0.34461 0.43757 0.38670 0.00618  0.07415  0.02284  299 GLN   A C   
2312 O  O   . GLN   A 299 ? 0.39744 0.49796 0.45697 0.00897  0.08431  0.02390  299 GLN   A O   
2313 C  CB  . GLN   A 299 ? 0.28573 0.37003 0.34464 0.00466  0.05039  0.02432  299 GLN   A CB  
2314 C  CG  . GLN   A 299 ? 0.24894 0.34116 0.33549 0.00542  0.05185  0.02873  299 GLN   A CG  
2315 C  CD  . GLN   A 299 ? 0.21296 0.30334 0.31137 0.00186  0.03919  0.03286  299 GLN   A CD  
2316 O  OE1 . GLN   A 299 ? 0.20197 0.30002 0.32091 -0.00059 0.03838  0.03885  299 GLN   A OE1 
2317 N  NE2 . GLN   A 299 ? 0.16257 0.24320 0.24823 0.00102  0.02943  0.02940  299 GLN   A NE2 
2318 N  N   . CYS   A 300 ? 0.32342 0.41654 0.34580 0.00234  0.07384  0.02749  300 CYS   A N   
2319 C  CA  . CYS   A 300 ? 0.36256 0.46397 0.38027 0.00050  0.08554  0.03437  300 CYS   A CA  
2320 C  C   . CYS   A 300 ? 0.42659 0.52804 0.41996 0.00156  0.09758  0.02634  300 CYS   A C   
2321 O  O   . CYS   A 300 ? 0.50554 0.61288 0.48530 -0.00099 0.10636  0.03193  300 CYS   A O   
2322 C  CB  . CYS   A 300 ? 0.32213 0.42368 0.33244 -0.00435 0.07904  0.04598  300 CYS   A CB  
2323 S  SG  . CYS   A 300 ? 0.34588 0.44389 0.38172 -0.00675 0.06626  0.05383  300 CYS   A SG  
2324 N  N   . SER   A 301 ? 0.45943 0.55349 0.44624 0.00472  0.09847  0.01327  301 SER   A N   
2325 C  CA  . SER   A 301 ? 0.50470 0.59573 0.46870 0.00549  0.11069  0.00242  301 SER   A CA  
2326 C  C   . SER   A 301 ? 0.51518 0.60024 0.49323 0.01179  0.11818  -0.00915 301 SER   A C   
2327 O  O   . SER   A 301 ? 0.52115 0.60674 0.49565 0.01496  0.13471  -0.01569 301 SER   A O   
2328 C  CB  . SER   A 301 ? 0.57573 0.66030 0.50702 0.00045  0.10191  -0.00260 301 SER   A CB  
2329 O  OG  . SER   A 301 ? 0.65404 0.73155 0.56347 0.00031  0.11069  -0.01706 301 SER   A OG  
2330 N  N   . GLY   A 302 ? 0.52223 0.60103 0.51598 0.01397  0.10705  -0.01146 302 GLY   A N   
2331 C  CA  . GLY   A 302 ? 0.51805 0.59351 0.53449 0.02086  0.11300  -0.01724 302 GLY   A CA  
2332 C  C   . GLY   A 302 ? 0.57869 0.63920 0.58531 0.02271  0.11228  -0.03078 302 GLY   A C   
2333 O  O   . GLY   A 302 ? 0.58027 0.63547 0.59360 0.02839  0.12520  -0.03905 302 GLY   A O   
2334 N  N   . VAL   A 303 ? 0.60884 0.66217 0.60187 0.01812  0.09785  -0.03280 303 VAL   A N   
2335 C  CA  . VAL   A 303 ? 0.65162 0.69032 0.63380 0.01782  0.09587  -0.04520 303 VAL   A CA  
2336 C  C   . VAL   A 303 ? 0.60555 0.63945 0.61556 0.02361  0.09247  -0.04434 303 VAL   A C   
2337 O  O   . VAL   A 303 ? 0.57665 0.61739 0.60563 0.02428  0.08253  -0.03404 303 VAL   A O   
2338 C  CB  . VAL   A 303 ? 0.61790 0.65362 0.57725 0.01014  0.08169  -0.04603 303 VAL   A CB  
2339 C  CG1 . VAL   A 303 ? 0.66388 0.68514 0.61627 0.00857  0.07772  -0.05751 303 VAL   A CG1 
2340 C  CG2 . VAL   A 303 ? 0.63383 0.67474 0.56428 0.00441  0.08485  -0.04624 303 VAL   A CG2 
2341 N  N   . THR   A 304 ? 0.60120 0.62243 0.61285 0.02752  0.10084  -0.05515 304 THR   A N   
2342 C  CA  . THR   A 304 ? 0.53852 0.55321 0.57531 0.03341  0.09858  -0.05424 304 THR   A CA  
2343 C  C   . THR   A 304 ? 0.62372 0.62271 0.64776 0.02944  0.09054  -0.06247 304 THR   A C   
2344 O  O   . THR   A 304 ? 0.64333 0.63869 0.64115 0.02169  0.08497  -0.06810 304 THR   A O   
2345 C  CB  . THR   A 304 ? 0.50072 0.51244 0.55581 0.04251  0.11601  -0.05841 304 THR   A CB  
2346 O  OG1 . THR   A 304 ? 0.60434 0.60551 0.63404 0.04076  0.12732  -0.07168 304 THR   A OG1 
2347 C  CG2 . THR   A 304 ? 0.39620 0.42653 0.47382 0.04681  0.12186  -0.04698 304 THR   A CG2 
2348 N  N   . PHE   A 305 ? 0.57429 0.56484 0.61883 0.03460  0.08973  -0.06197 305 PHE   A N   
2349 C  CA  . PHE   A 305 ? 0.62189 0.59800 0.66051 0.03104  0.08167  -0.06707 305 PHE   A CA  
2350 C  C   . PHE   A 305 ? 0.61745 0.57986 0.67639 0.03885  0.09038  -0.07057 305 PHE   A C   
2351 O  O   . PHE   A 305 ? 0.56247 0.53208 0.64931 0.04703  0.09323  -0.06125 305 PHE   A O   
2352 C  CB  . PHE   A 305 ? 0.54564 0.52949 0.59022 0.02760  0.06461  -0.05573 305 PHE   A CB  
2353 C  CG  . PHE   A 305 ? 0.53556 0.53408 0.56929 0.02288  0.05765  -0.04918 305 PHE   A CG  
2354 C  CD1 . PHE   A 305 ? 0.50529 0.50363 0.51392 0.01514  0.05227  -0.05347 305 PHE   A CD1 
2355 C  CD2 . PHE   A 305 ? 0.48610 0.49869 0.53603 0.02603  0.05685  -0.03837 305 PHE   A CD2 
2356 C  CE1 . PHE   A 305 ? 0.50547 0.51634 0.50607 0.01185  0.04678  -0.04631 305 PHE   A CE1 
2357 C  CE2 . PHE   A 305 ? 0.45372 0.47726 0.49465 0.02175  0.05161  -0.03246 305 PHE   A CE2 
2358 C  CZ  . PHE   A 305 ? 0.53652 0.55867 0.55305 0.01529  0.04704  -0.03612 305 PHE   A CZ  
2359 N  N   . GLN   A 306 ? 0.67598 0.61876 0.72229 0.03611  0.09437  -0.08346 306 GLN   A N   
2360 C  CA  . GLN   A 306 ? 0.69164 0.61992 0.75524 0.04249  0.10017  -0.08463 306 GLN   A CA  
2361 C  C   . GLN   A 306 ? 0.67871 0.58865 0.73501 0.03664  0.09346  -0.09050 306 GLN   A C   
2362 O  O   . GLN   A 306 ? 0.63361 0.54184 0.70660 0.03792  0.08518  -0.08190 306 GLN   A O   
2363 C  CB  . GLN   A 306 ? 0.71217 0.63509 0.76876 0.04573  0.11401  -0.09260 306 GLN   A CB  
2364 C  CG  . GLN   A 306 ? 0.70885 0.62421 0.79020 0.05474  0.12059  -0.08874 306 GLN   A CG  
2365 C  CD  . GLN   A 306 ? 0.78477 0.69869 0.86259 0.05924  0.13549  -0.09539 306 GLN   A CD  
2366 O  OE1 . GLN   A 306 ? 0.88881 0.80411 0.94144 0.05456  0.14063  -0.10451 306 GLN   A OE1 
2367 N  NE2 . GLN   A 306 ? 0.70966 0.62142 0.81239 0.06821  0.14242  -0.09030 306 GLN   A NE2 
2368 N  N1  . A1ARY B .   ? 0.39731 0.40344 0.25426 -0.04299 -0.04987 0.02590  401 A1ARY A N1  
2369 C  C4  . A1ARY B .   ? 0.42051 0.43534 0.29864 -0.03938 -0.05240 0.04762  401 A1ARY A C4  
2370 C  C5  . A1ARY B .   ? 0.39944 0.39852 0.22867 -0.04265 -0.02852 0.01770  401 A1ARY A C5  
2371 C  C6  . A1ARY B .   ? 0.43859 0.43451 0.24771 -0.04370 -0.01749 0.01397  401 A1ARY A C6  
2372 C  C7  . A1ARY B .   ? 0.44936 0.44441 0.24047 -0.04760 -0.01991 0.01462  401 A1ARY A C7  
2373 C  C8  . A1ARY B .   ? 0.47727 0.47549 0.27118 -0.05086 -0.03351 0.01946  401 A1ARY A C8  
2374 C  C10 . A1ARY B .   ? 0.44828 0.44332 0.26173 -0.03881 -0.00245 0.00945  401 A1ARY A C10 
2375 C  C13 . A1ARY B .   ? 0.41700 0.41645 0.25601 -0.02619 0.02475  0.00397  401 A1ARY A C13 
2376 C  C15 . A1ARY B .   ? 0.49242 0.48051 0.28860 -0.03813 0.01062  -0.00095 401 A1ARY A C15 
2377 C  C17 . A1ARY B .   ? 0.38939 0.38456 0.24781 -0.04866 -0.05812 0.00272  401 A1ARY A C17 
2378 C  C1  . A1ARY B .   ? 0.36578 0.36828 0.22702 -0.04354 -0.05259 0.01681  401 A1ARY A C1  
2379 C  C11 . A1ARY B .   ? 0.41875 0.42058 0.25987 -0.03333 -0.00080 0.01546  401 A1ARY A C11 
2380 C  C12 . A1ARY B .   ? 0.38959 0.39373 0.24180 -0.02796 0.01183  0.01258  401 A1ARY A C12 
2381 C  C14 . A1ARY B .   ? 0.50189 0.49203 0.31176 -0.03114 0.02486  -0.00340 401 A1ARY A C14 
2382 C  C16 . A1ARY B .   ? 0.39617 0.39519 0.24668 -0.04827 -0.05645 0.01020  401 A1ARY A C16 
2383 C  C18 . A1ARY B .   ? 0.35822 0.35338 0.23326 -0.04414 -0.05602 0.00204  401 A1ARY A C18 
2384 C  C19 . A1ARY B .   ? 0.33651 0.33879 0.21389 -0.03947 -0.05099 0.01482  401 A1ARY A C19 
2385 C  C2  . A1ARY B .   ? 0.43541 0.43754 0.26933 -0.04501 -0.04065 0.02235  401 A1ARY A C2  
2386 C  C3  . A1ARY B .   ? 0.40228 0.41454 0.27914 -0.04016 -0.05499 0.03685  401 A1ARY A C3  
2387 C  C9  . A1ARY B .   ? 0.42845 0.43051 0.24475 -0.04936 -0.04326 0.02336  401 A1ARY A C9  
2388 N  N2  . A1ARY B .   ? 0.32308 0.32202 0.20719 -0.03946 -0.05268 0.00777  401 A1ARY A N2  
2389 O  O1  . A1ARY B .   ? 0.49490 0.50933 0.35280 -0.04302 -0.04996 0.04984  401 A1ARY A O1  
2390 O  O2  . A1ARY B .   ? 0.41715 0.43205 0.31314 -0.03775 -0.06044 0.03792  401 A1ARY A O2  
2391 CL CL1 . A1ARY B .   ? 0.45294 0.46612 0.33750 -0.02374 0.01066  0.01996  401 A1ARY A CL1 
2392 CL CL2 . A1ARY B .   ? 0.48027 0.47043 0.32745 -0.05574 -0.06324 -0.00552 401 A1ARY A CL2 
# 
