data_9BSI
# 
_entry.id   9BSI 
# 
_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   9BSI         pdb_00009bsi 10.2210/pdb9bsi/pdb 
WWPDB D_1000284065 ?            ?                   
# 
_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                        9BSI 
_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 "N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-2-fluoroacetamide" 375.224   1   ?         ? ? 
? 
3 water       nat water                                                                               18.015    276 ?         ? ? 
? 
# 
_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 "N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-2-fluoroacetamide" A1AR9 
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 
A1AR9 non-polymer         . "N-[(1M)-3'-chloro[1,1'-biphenyl]-3-yl]-N-(5-chloropyridin-3-yl)-2-fluoroacetamide" ? 
'C19 H13 Cl2 F N2 O' 375.224 
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        A1AR9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AR9 
_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 A1AR9 1   401 401 A1AR9 LIG A . 
C 3 HOH   1   501 189 HOH   HOH A . 
C 3 HOH   2   502 194 HOH   HOH A . 
C 3 HOH   3   503 256 HOH   HOH A . 
C 3 HOH   4   504 62  HOH   HOH A . 
C 3 HOH   5   505 216 HOH   HOH A . 
C 3 HOH   6   506 254 HOH   HOH A . 
C 3 HOH   7   507 172 HOH   HOH A . 
C 3 HOH   8   508 133 HOH   HOH A . 
C 3 HOH   9   509 90  HOH   HOH A . 
C 3 HOH   10  510 231 HOH   HOH A . 
C 3 HOH   11  511 230 HOH   HOH A . 
C 3 HOH   12  512 169 HOH   HOH A . 
C 3 HOH   13  513 21  HOH   HOH A . 
C 3 HOH   14  514 55  HOH   HOH A . 
C 3 HOH   15  515 158 HOH   HOH A . 
C 3 HOH   16  516 146 HOH   HOH A . 
C 3 HOH   17  517 272 HOH   HOH A . 
C 3 HOH   18  518 222 HOH   HOH A . 
C 3 HOH   19  519 109 HOH   HOH A . 
C 3 HOH   20  520 80  HOH   HOH A . 
C 3 HOH   21  521 217 HOH   HOH A . 
C 3 HOH   22  522 201 HOH   HOH A . 
C 3 HOH   23  523 137 HOH   HOH A . 
C 3 HOH   24  524 84  HOH   HOH A . 
C 3 HOH   25  525 264 HOH   HOH A . 
C 3 HOH   26  526 161 HOH   HOH A . 
C 3 HOH   27  527 265 HOH   HOH A . 
C 3 HOH   28  528 34  HOH   HOH A . 
C 3 HOH   29  529 35  HOH   HOH A . 
C 3 HOH   30  530 205 HOH   HOH A . 
C 3 HOH   31  531 243 HOH   HOH A . 
C 3 HOH   32  532 241 HOH   HOH A . 
C 3 HOH   33  533 52  HOH   HOH A . 
C 3 HOH   34  534 106 HOH   HOH A . 
C 3 HOH   35  535 77  HOH   HOH A . 
C 3 HOH   36  536 148 HOH   HOH A . 
C 3 HOH   37  537 99  HOH   HOH A . 
C 3 HOH   38  538 68  HOH   HOH A . 
C 3 HOH   39  539 111 HOH   HOH A . 
C 3 HOH   40  540 57  HOH   HOH A . 
C 3 HOH   41  541 12  HOH   HOH A . 
C 3 HOH   42  542 72  HOH   HOH A . 
C 3 HOH   43  543 39  HOH   HOH A . 
C 3 HOH   44  544 11  HOH   HOH A . 
C 3 HOH   45  545 266 HOH   HOH A . 
C 3 HOH   46  546 86  HOH   HOH A . 
C 3 HOH   47  547 69  HOH   HOH A . 
C 3 HOH   48  548 238 HOH   HOH A . 
C 3 HOH   49  549 225 HOH   HOH A . 
C 3 HOH   50  550 232 HOH   HOH A . 
C 3 HOH   51  551 25  HOH   HOH A . 
C 3 HOH   52  552 76  HOH   HOH A . 
C 3 HOH   53  553 132 HOH   HOH A . 
C 3 HOH   54  554 20  HOH   HOH A . 
C 3 HOH   55  555 59  HOH   HOH A . 
C 3 HOH   56  556 71  HOH   HOH A . 
C 3 HOH   57  557 83  HOH   HOH A . 
C 3 HOH   58  558 37  HOH   HOH A . 
C 3 HOH   59  559 85  HOH   HOH A . 
C 3 HOH   60  560 173 HOH   HOH A . 
C 3 HOH   61  561 167 HOH   HOH A . 
C 3 HOH   62  562 45  HOH   HOH A . 
C 3 HOH   63  563 153 HOH   HOH A . 
C 3 HOH   64  564 144 HOH   HOH A . 
C 3 HOH   65  565 270 HOH   HOH A . 
C 3 HOH   66  566 157 HOH   HOH A . 
C 3 HOH   67  567 40  HOH   HOH A . 
C 3 HOH   68  568 247 HOH   HOH A . 
C 3 HOH   69  569 196 HOH   HOH A . 
C 3 HOH   70  570 184 HOH   HOH A . 
C 3 HOH   71  571 53  HOH   HOH A . 
C 3 HOH   72  572 14  HOH   HOH A . 
C 3 HOH   73  573 91  HOH   HOH A . 
C 3 HOH   74  574 227 HOH   HOH A . 
C 3 HOH   75  575 4   HOH   HOH A . 
C 3 HOH   76  576 64  HOH   HOH A . 
C 3 HOH   77  577 30  HOH   HOH A . 
C 3 HOH   78  578 220 HOH   HOH A . 
C 3 HOH   79  579 51  HOH   HOH A . 
C 3 HOH   80  580 23  HOH   HOH A . 
C 3 HOH   81  581 228 HOH   HOH A . 
C 3 HOH   82  582 29  HOH   HOH A . 
C 3 HOH   83  583 7   HOH   HOH A . 
C 3 HOH   84  584 16  HOH   HOH A . 
C 3 HOH   85  585 239 HOH   HOH A . 
C 3 HOH   86  586 87  HOH   HOH A . 
C 3 HOH   87  587 41  HOH   HOH A . 
C 3 HOH   88  588 73  HOH   HOH A . 
C 3 HOH   89  589 79  HOH   HOH A . 
C 3 HOH   90  590 38  HOH   HOH A . 
C 3 HOH   91  591 89  HOH   HOH A . 
C 3 HOH   92  592 103 HOH   HOH A . 
C 3 HOH   93  593 181 HOH   HOH A . 
C 3 HOH   94  594 221 HOH   HOH A . 
C 3 HOH   95  595 204 HOH   HOH A . 
C 3 HOH   96  596 74  HOH   HOH A . 
C 3 HOH   97  597 119 HOH   HOH A . 
C 3 HOH   98  598 22  HOH   HOH A . 
C 3 HOH   99  599 93  HOH   HOH A . 
C 3 HOH   100 600 139 HOH   HOH A . 
C 3 HOH   101 601 54  HOH   HOH A . 
C 3 HOH   102 602 81  HOH   HOH A . 
C 3 HOH   103 603 130 HOH   HOH A . 
C 3 HOH   104 604 58  HOH   HOH A . 
C 3 HOH   105 605 47  HOH   HOH A . 
C 3 HOH   106 606 105 HOH   HOH A . 
C 3 HOH   107 607 31  HOH   HOH A . 
C 3 HOH   108 608 6   HOH   HOH A . 
C 3 HOH   109 609 27  HOH   HOH A . 
C 3 HOH   110 610 92  HOH   HOH A . 
C 3 HOH   111 611 149 HOH   HOH A . 
C 3 HOH   112 612 63  HOH   HOH A . 
C 3 HOH   113 613 43  HOH   HOH A . 
C 3 HOH   114 614 1   HOH   HOH A . 
C 3 HOH   115 615 46  HOH   HOH A . 
C 3 HOH   116 616 96  HOH   HOH A . 
C 3 HOH   117 617 163 HOH   HOH A . 
C 3 HOH   118 618 3   HOH   HOH A . 
C 3 HOH   119 619 26  HOH   HOH A . 
C 3 HOH   120 620 180 HOH   HOH A . 
C 3 HOH   121 621 42  HOH   HOH A . 
C 3 HOH   122 622 145 HOH   HOH A . 
C 3 HOH   123 623 5   HOH   HOH A . 
C 3 HOH   124 624 126 HOH   HOH A . 
C 3 HOH   125 625 82  HOH   HOH A . 
C 3 HOH   126 626 61  HOH   HOH A . 
C 3 HOH   127 627 110 HOH   HOH A . 
C 3 HOH   128 628 107 HOH   HOH A . 
C 3 HOH   129 629 160 HOH   HOH A . 
C 3 HOH   130 630 17  HOH   HOH A . 
C 3 HOH   131 631 219 HOH   HOH A . 
C 3 HOH   132 632 32  HOH   HOH A . 
C 3 HOH   133 633 240 HOH   HOH A . 
C 3 HOH   134 634 127 HOH   HOH A . 
C 3 HOH   135 635 24  HOH   HOH A . 
C 3 HOH   136 636 8   HOH   HOH A . 
C 3 HOH   137 637 13  HOH   HOH A . 
C 3 HOH   138 638 170 HOH   HOH A . 
C 3 HOH   139 639 121 HOH   HOH A . 
C 3 HOH   140 640 129 HOH   HOH A . 
C 3 HOH   141 641 49  HOH   HOH A . 
C 3 HOH   142 642 2   HOH   HOH A . 
C 3 HOH   143 643 253 HOH   HOH A . 
C 3 HOH   144 644 94  HOH   HOH A . 
C 3 HOH   145 645 229 HOH   HOH A . 
C 3 HOH   146 646 75  HOH   HOH A . 
C 3 HOH   147 647 36  HOH   HOH A . 
C 3 HOH   148 648 183 HOH   HOH A . 
C 3 HOH   149 649 244 HOH   HOH A . 
C 3 HOH   150 650 152 HOH   HOH A . 
C 3 HOH   151 651 18  HOH   HOH A . 
C 3 HOH   152 652 226 HOH   HOH A . 
C 3 HOH   153 653 10  HOH   HOH A . 
C 3 HOH   154 654 255 HOH   HOH A . 
C 3 HOH   155 655 102 HOH   HOH A . 
C 3 HOH   156 656 104 HOH   HOH A . 
C 3 HOH   157 657 33  HOH   HOH A . 
C 3 HOH   158 658 260 HOH   HOH A . 
C 3 HOH   159 659 150 HOH   HOH A . 
C 3 HOH   160 660 135 HOH   HOH A . 
C 3 HOH   161 661 15  HOH   HOH A . 
C 3 HOH   162 662 235 HOH   HOH A . 
C 3 HOH   163 663 70  HOH   HOH A . 
C 3 HOH   164 664 116 HOH   HOH A . 
C 3 HOH   165 665 120 HOH   HOH A . 
C 3 HOH   166 666 122 HOH   HOH A . 
C 3 HOH   167 667 182 HOH   HOH A . 
C 3 HOH   168 668 48  HOH   HOH A . 
C 3 HOH   169 669 175 HOH   HOH A . 
C 3 HOH   170 670 215 HOH   HOH A . 
C 3 HOH   171 671 66  HOH   HOH A . 
C 3 HOH   172 672 65  HOH   HOH A . 
C 3 HOH   173 673 249 HOH   HOH A . 
C 3 HOH   174 674 44  HOH   HOH A . 
C 3 HOH   175 675 117 HOH   HOH A . 
C 3 HOH   176 676 97  HOH   HOH A . 
C 3 HOH   177 677 9   HOH   HOH A . 
C 3 HOH   178 678 19  HOH   HOH A . 
C 3 HOH   179 679 261 HOH   HOH A . 
C 3 HOH   180 680 95  HOH   HOH A . 
C 3 HOH   181 681 136 HOH   HOH A . 
C 3 HOH   182 682 28  HOH   HOH A . 
C 3 HOH   183 683 128 HOH   HOH A . 
C 3 HOH   184 684 114 HOH   HOH A . 
C 3 HOH   185 685 211 HOH   HOH A . 
C 3 HOH   186 686 191 HOH   HOH A . 
C 3 HOH   187 687 198 HOH   HOH A . 
C 3 HOH   188 688 165 HOH   HOH A . 
C 3 HOH   189 689 142 HOH   HOH A . 
C 3 HOH   190 690 50  HOH   HOH A . 
C 3 HOH   191 691 115 HOH   HOH A . 
C 3 HOH   192 692 207 HOH   HOH A . 
C 3 HOH   193 693 138 HOH   HOH A . 
C 3 HOH   194 694 195 HOH   HOH A . 
C 3 HOH   195 695 193 HOH   HOH A . 
C 3 HOH   196 696 56  HOH   HOH A . 
C 3 HOH   197 697 176 HOH   HOH A . 
C 3 HOH   198 698 154 HOH   HOH A . 
C 3 HOH   199 699 273 HOH   HOH A . 
C 3 HOH   200 700 171 HOH   HOH A . 
C 3 HOH   201 701 140 HOH   HOH A . 
C 3 HOH   202 702 236 HOH   HOH A . 
C 3 HOH   203 703 275 HOH   HOH A . 
C 3 HOH   204 704 190 HOH   HOH A . 
C 3 HOH   205 705 113 HOH   HOH A . 
C 3 HOH   206 706 174 HOH   HOH A . 
C 3 HOH   207 707 210 HOH   HOH A . 
C 3 HOH   208 708 134 HOH   HOH A . 
C 3 HOH   209 709 202 HOH   HOH A . 
C 3 HOH   210 710 166 HOH   HOH A . 
C 3 HOH   211 711 237 HOH   HOH A . 
C 3 HOH   212 712 234 HOH   HOH A . 
C 3 HOH   213 713 258 HOH   HOH A . 
C 3 HOH   214 714 200 HOH   HOH A . 
C 3 HOH   215 715 250 HOH   HOH A . 
C 3 HOH   216 716 112 HOH   HOH A . 
C 3 HOH   217 717 179 HOH   HOH A . 
C 3 HOH   218 718 248 HOH   HOH A . 
C 3 HOH   219 719 197 HOH   HOH A . 
C 3 HOH   220 720 67  HOH   HOH A . 
C 3 HOH   221 721 124 HOH   HOH A . 
C 3 HOH   222 722 259 HOH   HOH A . 
C 3 HOH   223 723 276 HOH   HOH A . 
C 3 HOH   224 724 269 HOH   HOH A . 
C 3 HOH   225 725 274 HOH   HOH A . 
C 3 HOH   226 726 108 HOH   HOH A . 
C 3 HOH   227 727 218 HOH   HOH A . 
C 3 HOH   228 728 209 HOH   HOH A . 
C 3 HOH   229 729 252 HOH   HOH A . 
C 3 HOH   230 730 223 HOH   HOH A . 
C 3 HOH   231 731 245 HOH   HOH A . 
C 3 HOH   232 732 267 HOH   HOH A . 
C 3 HOH   233 733 78  HOH   HOH A . 
C 3 HOH   234 734 151 HOH   HOH A . 
C 3 HOH   235 735 101 HOH   HOH A . 
C 3 HOH   236 736 118 HOH   HOH A . 
C 3 HOH   237 737 212 HOH   HOH A . 
C 3 HOH   238 738 214 HOH   HOH A . 
C 3 HOH   239 739 224 HOH   HOH A . 
C 3 HOH   240 740 203 HOH   HOH A . 
C 3 HOH   241 741 164 HOH   HOH A . 
C 3 HOH   242 742 162 HOH   HOH A . 
C 3 HOH   243 743 141 HOH   HOH A . 
C 3 HOH   244 744 213 HOH   HOH A . 
C 3 HOH   245 745 177 HOH   HOH A . 
C 3 HOH   246 746 263 HOH   HOH A . 
C 3 HOH   247 747 125 HOH   HOH A . 
C 3 HOH   248 748 246 HOH   HOH A . 
C 3 HOH   249 749 155 HOH   HOH A . 
C 3 HOH   250 750 100 HOH   HOH A . 
C 3 HOH   251 751 187 HOH   HOH A . 
C 3 HOH   252 752 262 HOH   HOH A . 
C 3 HOH   253 753 208 HOH   HOH A . 
C 3 HOH   254 754 147 HOH   HOH A . 
C 3 HOH   255 755 123 HOH   HOH A . 
C 3 HOH   256 756 131 HOH   HOH A . 
C 3 HOH   257 757 192 HOH   HOH A . 
C 3 HOH   258 758 188 HOH   HOH A . 
C 3 HOH   259 759 98  HOH   HOH A . 
C 3 HOH   260 760 199 HOH   HOH A . 
C 3 HOH   261 761 178 HOH   HOH A . 
C 3 HOH   262 762 186 HOH   HOH A . 
C 3 HOH   263 763 60  HOH   HOH A . 
C 3 HOH   264 764 233 HOH   HOH A . 
C 3 HOH   265 765 88  HOH   HOH A . 
C 3 HOH   266 766 268 HOH   HOH A . 
C 3 HOH   267 767 159 HOH   HOH A . 
C 3 HOH   268 768 143 HOH   HOH A . 
C 3 HOH   269 769 206 HOH   HOH A . 
C 3 HOH   270 770 168 HOH   HOH A . 
C 3 HOH   271 771 251 HOH   HOH A . 
C 3 HOH   272 772 242 HOH   HOH A . 
C 3 HOH   273 773 271 HOH   HOH A . 
C 3 HOH   274 774 156 HOH   HOH A . 
C 3 HOH   275 775 257 HOH   HOH A . 
C 3 HOH   276 776 185 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                   96.580 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BSI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.718 
_cell.length_a_esd                 ? 
_cell.length_b                     81.530 
_cell.length_b_esd                 ? 
_cell.length_c                     90.264 
_cell.length_c_esd                 ? 
_cell.volume                       378097.236 
_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                         9BSI 
_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                   9BSI 
_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         2022-07-09 
_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                          15.66 
_reflns.entry_id                                       9BSI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.7 
_reflns.d_resolution_low                               24.32 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     35107 
_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                           85.01 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.94 
_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                                0.08435 
_reflns.pdbx_Rpim_I_all                                0.02956 
_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                              0.07863 
_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                                    1.7 
_reflns_shell.d_res_low                                     1.761 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.45 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2575 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.5084 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.857 
_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                                  1.042 
_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                               23.34 
_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                                 9BSI 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.70 
_refine.ls_d_res_low                             24.32 
_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                     34803 
_refine.ls_number_reflns_R_free                  1725 
_refine.ls_number_reflns_R_work                  33078 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    85.05 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2292 
_refine.ls_R_factor_R_free                       0.2485 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2282 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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                 29.8544 
_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                            0.2260 
_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                       1.70 
_refine_hist.d_res_low                        24.32 
_refine_hist.number_atoms_solvent             276 
_refine_hist.number_atoms_total               2668 
_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' ? 0.0088 ? 2447 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.0769 ? 3326 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0607 ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0098 ? 432  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 8.5040 ? 331  ? 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' 1.70 1.75  . . 104 1984 61.57 . . . . 0.3385 . . . . . . . . . . . 0.4000 
'X-RAY DIFFRACTION' 1.75 1.81  . . 123 2017 63.22 . . . . 0.3271 . . . . . . . . . . . 0.3007 
'X-RAY DIFFRACTION' 1.81 1.87  . . 118 2156 67.12 . . . . 0.3067 . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 1.87 1.95  . . 110 2367 72.60 . . . . 0.2909 . . . . . . . . . . . 0.2745 
'X-RAY DIFFRACTION' 1.95 2.03  . . 130 2633 82.21 . . . . 0.2714 . . . . . . . . . . . 0.3074 
'X-RAY DIFFRACTION' 2.03 2.14  . . 152 2936 89.64 . . . . 0.2696 . . . . . . . . . . . 0.2847 
'X-RAY DIFFRACTION' 2.14 2.28  . . 140 3014 92.63 . . . . 0.2681 . . . . . . . . . . . 0.2755 
'X-RAY DIFFRACTION' 2.28 2.45  . . 154 3068 95.13 . . . . 0.2598 . . . . . . . . . . . 0.2858 
'X-RAY DIFFRACTION' 2.45 2.70  . . 165 3145 96.87 . . . . 0.2619 . . . . . . . . . . . 0.2614 
'X-RAY DIFFRACTION' 2.70 3.09  . . 178 3207 99.38 . . . . 0.2313 . . . . . . . . . . . 0.2627 
'X-RAY DIFFRACTION' 3.09 3.89  . . 179 3246 99.85 . . . . 0.1880 . . . . . . . . . . . 0.1999 
'X-RAY DIFFRACTION' 3.89 24.32 . . 172 3305 99.77 . . . . 0.1607 . . . . . . . . . . . 0.2060 
# 
_struct.entry_id                     9BSI 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor SR-B-7' 
_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        9BSI 
_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              9BSI 
_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)' 3310  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  24950 ? 
# 
_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 -51.7180000000 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 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P4  AA4 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P5  AA5 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P6  AA6 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P7  AA7 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P8  AA8 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P9  AA9 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P10 AB1 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        none 
_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           A1AR9 
_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            A1AR9 
_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               1.819 
_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                      A1AR9 
_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                       A1AR9 
_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                        A1AR9 
_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 TYR A 101 ? PHE A 103 ? TYR A 101 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 TYR A 101 ? PHE A 103 ? TYR A 101 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 CYS A 22  ? N CYS A 22  O THR A 25  ? O THR A 25  
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 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O CYS A 156 ? O CYS A 156 N ASP A 153 ? N ASP A 153 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N VAL A 114 ? N VAL A 114 O TYR A 126 ? O TYR A 126 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9BSI 
_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   722 ? ? O  A HOH   746 ? ? 1.82 
2  1 O   A HOH   643 ? ? O  A HOH   714 ? ? 1.85 
3  1 OD1 A ASP   155 ? ? O  A HOH   501 ? ? 1.88 
4  1 F1  A A1AR9 401 ? ? O  A HOH   737 ? ? 1.90 
5  1 O   A HOH   531 ? ? O  A HOH   605 ? ? 1.92 
6  1 O   A HOH   526 ? ? O  A HOH   610 ? ? 1.94 
7  1 O   A HOH   520 ? ? O  A HOH   723 ? ? 1.95 
8  1 OD2 A ASP   245 ? ? O  A HOH   502 ? ? 1.95 
9  1 O   A HOH   522 ? ? O  A HOH   733 ? ? 1.96 
10 1 O   A GLY   302 ? ? O  A HOH   503 ? ? 1.99 
11 1 O   A CYS   300 ? ? O  A HOH   504 ? ? 2.02 
12 1 O   A PHE   305 ? ? O  A HOH   505 ? ? 2.03 
13 1 O   A HOH   508 ? ? O  A HOH   745 ? ? 2.06 
14 1 O   A HOH   704 ? ? O  A HOH   718 ? ? 2.08 
15 1 O   A HOH   703 ? ? O  A HOH   728 ? ? 2.09 
16 1 NH1 A ARG   188 ? ? O  A HOH   506 ? ? 2.11 
17 1 SG  A CYS   145 ? ? C3 A A1AR9 401 ? ? 2.12 
18 1 O   A HOH   633 ? ? O  A HOH   747 ? ? 2.13 
19 1 NZ  A LYS   236 ? ? O  A HOH   507 ? ? 2.14 
20 1 NE2 A GLN   83  ? ? O  A HOH   508 ? ? 2.14 
21 1 O   A HOH   648 ? ? O  A HOH   713 ? ? 2.15 
22 1 F1  A A1AR9 401 ? ? O  A HOH   692 ? ? 2.18 
23 1 OD2 A ASP   263 ? ? O  A HOH   509 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 728 ? ? 1_555 O A HOH 760 ? ? 2_555 1.96 
2 1 O A HOH 728 ? ? 1_555 O A HOH 752 ? ? 2_555 1.97 
3 1 O A HOH 701 ? ? 1_555 O A HOH 751 ? ? 2_455 2.04 
# 
_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                109.56 
_pdbx_validate_rmsd_angle.angle_target_value         122.30 
_pdbx_validate_rmsd_angle.angle_deviation            -12.74 
_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  ? ? 49.39   -132.81 
2 1 MET A 49  ? ? -63.26  4.05    
3 1 ASN A 84  ? ? 48.84   -119.85 
4 1 TYR A 154 ? ? 41.47   -105.12 
5 1 SER A 301 ? ? -140.17 -44.28  
# 
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 582 ? C HOH . 
2 1 A HOH 623 ? C HOH . 
3 1 A HOH 678 ? C HOH . 
4 1 A HOH 707 ? C HOH . 
5 1 A HOH 761 ? 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         -12.9396515344 
_pdbx_refine_tls.origin_y         -14.7388622677 
_pdbx_refine_tls.origin_z         -1.05396409696 
_pdbx_refine_tls.T[1][1]          0.0617056274344 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00504795571655 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0182505597504 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0657286549379 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0038078420027 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0528110282111 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          2.23565339626 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.335676925133 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.377403652144 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.59524791451 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.626478887692 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.32062701874 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0358233722179 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.00800075687489 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0124332706686 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0846601589607 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0275699990232 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0413166798833 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0455749524971 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0257492976645 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.00272125712601 
_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 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       776 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.02 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1AR9 N1   N  N N 1   
A1AR9 C4   C  N N 2   
A1AR9 C5   C  Y N 3   
A1AR9 C6   C  Y N 4   
A1AR9 C7   C  Y N 5   
A1AR9 C8   C  Y N 6   
A1AR9 C10  C  Y N 7   
A1AR9 C13  C  Y N 8   
A1AR9 C15  C  Y N 9   
A1AR9 C17  C  Y N 10  
A1AR9 C1   C  Y N 11  
A1AR9 C11  C  Y N 12  
A1AR9 C12  C  Y N 13  
A1AR9 C14  C  Y N 14  
A1AR9 C16  C  Y N 15  
A1AR9 C18  C  Y N 16  
A1AR9 C19  C  Y N 17  
A1AR9 C2   C  Y N 18  
A1AR9 C3   C  N N 19  
A1AR9 C9   C  Y N 20  
A1AR9 F1   F  N N 21  
A1AR9 N2   N  Y N 22  
A1AR9 O1   O  N N 23  
A1AR9 CL1  CL N N 24  
A1AR9 CL2  CL N N 25  
A1AR9 H1   H  N N 26  
A1AR9 H2   H  N N 27  
A1AR9 H3   H  N N 28  
A1AR9 H4   H  N N 29  
A1AR9 H5   H  N N 30  
A1AR9 H8   H  N N 31  
A1AR9 H10  H  N N 32  
A1AR9 H7   H  N N 33  
A1AR9 H9   H  N N 34  
A1AR9 H11  H  N N 35  
A1AR9 H12  H  N N 36  
A1AR9 H13  H  N N 37  
A1AR9 H6   H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
GLN   N    N  N N 126 
GLN   CA   C  N S 127 
GLN   C    C  N N 128 
GLN   O    O  N N 129 
GLN   CB   C  N N 130 
GLN   CG   C  N N 131 
GLN   CD   C  N N 132 
GLN   OE1  O  N N 133 
GLN   NE2  N  N N 134 
GLN   OXT  O  N N 135 
GLN   H    H  N N 136 
GLN   H2   H  N N 137 
GLN   HA   H  N N 138 
GLN   HB2  H  N N 139 
GLN   HB3  H  N N 140 
GLN   HG2  H  N N 141 
GLN   HG3  H  N N 142 
GLN   HE21 H  N N 143 
GLN   HE22 H  N N 144 
GLN   HXT  H  N N 145 
GLU   N    N  N N 146 
GLU   CA   C  N S 147 
GLU   C    C  N N 148 
GLU   O    O  N N 149 
GLU   CB   C  N N 150 
GLU   CG   C  N N 151 
GLU   CD   C  N N 152 
GLU   OE1  O  N N 153 
GLU   OE2  O  N N 154 
GLU   OXT  O  N N 155 
GLU   H    H  N N 156 
GLU   H2   H  N N 157 
GLU   HA   H  N N 158 
GLU   HB2  H  N N 159 
GLU   HB3  H  N N 160 
GLU   HG2  H  N N 161 
GLU   HG3  H  N N 162 
GLU   HE2  H  N N 163 
GLU   HXT  H  N N 164 
GLY   N    N  N N 165 
GLY   CA   C  N N 166 
GLY   C    C  N N 167 
GLY   O    O  N N 168 
GLY   OXT  O  N N 169 
GLY   H    H  N N 170 
GLY   H2   H  N N 171 
GLY   HA2  H  N N 172 
GLY   HA3  H  N N 173 
GLY   HXT  H  N N 174 
HIS   N    N  N N 175 
HIS   CA   C  N S 176 
HIS   C    C  N N 177 
HIS   O    O  N N 178 
HIS   CB   C  N N 179 
HIS   CG   C  Y N 180 
HIS   ND1  N  Y N 181 
HIS   CD2  C  Y N 182 
HIS   CE1  C  Y N 183 
HIS   NE2  N  Y N 184 
HIS   OXT  O  N N 185 
HIS   H    H  N N 186 
HIS   H2   H  N N 187 
HIS   HA   H  N N 188 
HIS   HB2  H  N N 189 
HIS   HB3  H  N N 190 
HIS   HD1  H  N N 191 
HIS   HD2  H  N N 192 
HIS   HE1  H  N N 193 
HIS   HE2  H  N N 194 
HIS   HXT  H  N N 195 
HOH   O    O  N N 196 
HOH   H1   H  N N 197 
HOH   H2   H  N N 198 
ILE   N    N  N N 199 
ILE   CA   C  N S 200 
ILE   C    C  N N 201 
ILE   O    O  N N 202 
ILE   CB   C  N S 203 
ILE   CG1  C  N N 204 
ILE   CG2  C  N N 205 
ILE   CD1  C  N N 206 
ILE   OXT  O  N N 207 
ILE   H    H  N N 208 
ILE   H2   H  N N 209 
ILE   HA   H  N N 210 
ILE   HB   H  N N 211 
ILE   HG12 H  N N 212 
ILE   HG13 H  N N 213 
ILE   HG21 H  N N 214 
ILE   HG22 H  N N 215 
ILE   HG23 H  N N 216 
ILE   HD11 H  N N 217 
ILE   HD12 H  N N 218 
ILE   HD13 H  N N 219 
ILE   HXT  H  N N 220 
LEU   N    N  N N 221 
LEU   CA   C  N S 222 
LEU   C    C  N N 223 
LEU   O    O  N N 224 
LEU   CB   C  N N 225 
LEU   CG   C  N N 226 
LEU   CD1  C  N N 227 
LEU   CD2  C  N N 228 
LEU   OXT  O  N N 229 
LEU   H    H  N N 230 
LEU   H2   H  N N 231 
LEU   HA   H  N N 232 
LEU   HB2  H  N N 233 
LEU   HB3  H  N N 234 
LEU   HG   H  N N 235 
LEU   HD11 H  N N 236 
LEU   HD12 H  N N 237 
LEU   HD13 H  N N 238 
LEU   HD21 H  N N 239 
LEU   HD22 H  N N 240 
LEU   HD23 H  N N 241 
LEU   HXT  H  N N 242 
LYS   N    N  N N 243 
LYS   CA   C  N S 244 
LYS   C    C  N N 245 
LYS   O    O  N N 246 
LYS   CB   C  N N 247 
LYS   CG   C  N N 248 
LYS   CD   C  N N 249 
LYS   CE   C  N N 250 
LYS   NZ   N  N N 251 
LYS   OXT  O  N N 252 
LYS   H    H  N N 253 
LYS   H2   H  N N 254 
LYS   HA   H  N N 255 
LYS   HB2  H  N N 256 
LYS   HB3  H  N N 257 
LYS   HG2  H  N N 258 
LYS   HG3  H  N N 259 
LYS   HD2  H  N N 260 
LYS   HD3  H  N N 261 
LYS   HE2  H  N N 262 
LYS   HE3  H  N N 263 
LYS   HZ1  H  N N 264 
LYS   HZ2  H  N N 265 
LYS   HZ3  H  N N 266 
LYS   HXT  H  N N 267 
MET   N    N  N N 268 
MET   CA   C  N S 269 
MET   C    C  N N 270 
MET   O    O  N N 271 
MET   CB   C  N N 272 
MET   CG   C  N N 273 
MET   SD   S  N N 274 
MET   CE   C  N N 275 
MET   OXT  O  N N 276 
MET   H    H  N N 277 
MET   H2   H  N N 278 
MET   HA   H  N N 279 
MET   HB2  H  N N 280 
MET   HB3  H  N N 281 
MET   HG2  H  N N 282 
MET   HG3  H  N N 283 
MET   HE1  H  N N 284 
MET   HE2  H  N N 285 
MET   HE3  H  N N 286 
MET   HXT  H  N N 287 
PHE   N    N  N N 288 
PHE   CA   C  N S 289 
PHE   C    C  N N 290 
PHE   O    O  N N 291 
PHE   CB   C  N N 292 
PHE   CG   C  Y N 293 
PHE   CD1  C  Y N 294 
PHE   CD2  C  Y N 295 
PHE   CE1  C  Y N 296 
PHE   CE2  C  Y N 297 
PHE   CZ   C  Y N 298 
PHE   OXT  O  N N 299 
PHE   H    H  N N 300 
PHE   H2   H  N N 301 
PHE   HA   H  N N 302 
PHE   HB2  H  N N 303 
PHE   HB3  H  N N 304 
PHE   HD1  H  N N 305 
PHE   HD2  H  N N 306 
PHE   HE1  H  N N 307 
PHE   HE2  H  N N 308 
PHE   HZ   H  N N 309 
PHE   HXT  H  N N 310 
PRO   N    N  N N 311 
PRO   CA   C  N S 312 
PRO   C    C  N N 313 
PRO   O    O  N N 314 
PRO   CB   C  N N 315 
PRO   CG   C  N N 316 
PRO   CD   C  N N 317 
PRO   OXT  O  N N 318 
PRO   H    H  N N 319 
PRO   HA   H  N N 320 
PRO   HB2  H  N N 321 
PRO   HB3  H  N N 322 
PRO   HG2  H  N N 323 
PRO   HG3  H  N N 324 
PRO   HD2  H  N N 325 
PRO   HD3  H  N N 326 
PRO   HXT  H  N N 327 
SER   N    N  N N 328 
SER   CA   C  N S 329 
SER   C    C  N N 330 
SER   O    O  N N 331 
SER   CB   C  N N 332 
SER   OG   O  N N 333 
SER   OXT  O  N N 334 
SER   H    H  N N 335 
SER   H2   H  N N 336 
SER   HA   H  N N 337 
SER   HB2  H  N N 338 
SER   HB3  H  N N 339 
SER   HG   H  N N 340 
SER   HXT  H  N N 341 
THR   N    N  N N 342 
THR   CA   C  N S 343 
THR   C    C  N N 344 
THR   O    O  N N 345 
THR   CB   C  N R 346 
THR   OG1  O  N N 347 
THR   CG2  C  N N 348 
THR   OXT  O  N N 349 
THR   H    H  N N 350 
THR   H2   H  N N 351 
THR   HA   H  N N 352 
THR   HB   H  N N 353 
THR   HG1  H  N N 354 
THR   HG21 H  N N 355 
THR   HG22 H  N N 356 
THR   HG23 H  N N 357 
THR   HXT  H  N N 358 
TRP   N    N  N N 359 
TRP   CA   C  N S 360 
TRP   C    C  N N 361 
TRP   O    O  N N 362 
TRP   CB   C  N N 363 
TRP   CG   C  Y N 364 
TRP   CD1  C  Y N 365 
TRP   CD2  C  Y N 366 
TRP   NE1  N  Y N 367 
TRP   CE2  C  Y N 368 
TRP   CE3  C  Y N 369 
TRP   CZ2  C  Y N 370 
TRP   CZ3  C  Y N 371 
TRP   CH2  C  Y N 372 
TRP   OXT  O  N N 373 
TRP   H    H  N N 374 
TRP   H2   H  N N 375 
TRP   HA   H  N N 376 
TRP   HB2  H  N N 377 
TRP   HB3  H  N N 378 
TRP   HD1  H  N N 379 
TRP   HE1  H  N N 380 
TRP   HE3  H  N N 381 
TRP   HZ2  H  N N 382 
TRP   HZ3  H  N N 383 
TRP   HH2  H  N N 384 
TRP   HXT  H  N N 385 
TYR   N    N  N N 386 
TYR   CA   C  N S 387 
TYR   C    C  N N 388 
TYR   O    O  N N 389 
TYR   CB   C  N N 390 
TYR   CG   C  Y N 391 
TYR   CD1  C  Y N 392 
TYR   CD2  C  Y N 393 
TYR   CE1  C  Y N 394 
TYR   CE2  C  Y N 395 
TYR   CZ   C  Y N 396 
TYR   OH   O  N N 397 
TYR   OXT  O  N N 398 
TYR   H    H  N N 399 
TYR   H2   H  N N 400 
TYR   HA   H  N N 401 
TYR   HB2  H  N N 402 
TYR   HB3  H  N N 403 
TYR   HD1  H  N N 404 
TYR   HD2  H  N N 405 
TYR   HE1  H  N N 406 
TYR   HE2  H  N N 407 
TYR   HH   H  N N 408 
TYR   HXT  H  N N 409 
VAL   N    N  N N 410 
VAL   CA   C  N S 411 
VAL   C    C  N N 412 
VAL   O    O  N N 413 
VAL   CB   C  N N 414 
VAL   CG1  C  N N 415 
VAL   CG2  C  N N 416 
VAL   OXT  O  N N 417 
VAL   H    H  N N 418 
VAL   H2   H  N N 419 
VAL   HA   H  N N 420 
VAL   HB   H  N N 421 
VAL   HG11 H  N N 422 
VAL   HG12 H  N N 423 
VAL   HG13 H  N N 424 
VAL   HG21 H  N N 425 
VAL   HG22 H  N N 426 
VAL   HG23 H  N N 427 
VAL   HXT  H  N N 428 
# 
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 
A1AR9 C1  N1   sing N N 1   
A1AR9 C1  C16  doub Y N 2   
A1AR9 C1  C19  sing Y N 3   
A1AR9 N1  C2   sing N N 4   
A1AR9 N1  C3   sing N N 5   
A1AR9 C2  C5   doub Y N 6   
A1AR9 C2  C9   sing Y N 7   
A1AR9 C3  C4   sing N N 8   
A1AR9 C3  O1   doub N N 9   
A1AR9 C4  F1   sing N N 10  
A1AR9 C5  C6   sing Y N 11  
A1AR9 C6  C7   doub Y N 12  
A1AR9 C6  C10  sing N N 13  
A1AR9 C7  C8   sing Y N 14  
A1AR9 C8  C9   doub Y N 15  
A1AR9 C10 C11  doub Y N 16  
A1AR9 C10 C15  sing Y N 17  
A1AR9 C11 C12  sing Y N 18  
A1AR9 C12 C13  doub Y N 19  
A1AR9 C12 CL1  sing N N 20  
A1AR9 C13 C14  sing Y N 21  
A1AR9 C14 C15  doub Y N 22  
A1AR9 C16 C17  sing Y N 23  
A1AR9 C17 C18  doub Y N 24  
A1AR9 C17 CL2  sing N N 25  
A1AR9 C18 N2   sing Y N 26  
A1AR9 N2  C19  doub Y N 27  
A1AR9 C4  H1   sing N N 28  
A1AR9 C4  H2   sing N N 29  
A1AR9 C5  H3   sing N N 30  
A1AR9 C7  H4   sing N N 31  
A1AR9 C8  H5   sing N N 32  
A1AR9 C13 H8   sing N N 33  
A1AR9 C15 H10  sing N N 34  
A1AR9 C11 H7   sing N N 35  
A1AR9 C14 H9   sing N N 36  
A1AR9 C16 H11  sing N N 37  
A1AR9 C18 H12  sing N N 38  
A1AR9 C19 H13  sing N N 39  
A1AR9 C9  H6   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
_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                    9BSI 
_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]   0.019336 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002230 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012265 
_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]   0.011152 
_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.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 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   ? -33.13347 -18.77705 15.14473  1.000 22.88036 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -32.45775 -19.95591 14.61685  1.000 21.57111 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -32.48076 -20.04256 13.07727  1.000 22.10989 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -32.93188 -19.11357 12.39409  1.000 20.62522 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -33.06215 -21.20005 15.24850  1.000 24.68919 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -34.33371 -21.47462 14.71798  1.000 25.55658 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -31.97356 -21.15043 12.53901  1.000 17.13653 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -31.65749 -21.25647 11.12918  1.000 20.51557 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -30.20775 -20.88812 10.85110  1.000 21.01420 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -29.56046 -20.16186 11.60689  1.000 20.04970 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -29.68068 -21.43065 9.74856   1.000 19.42780 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -28.28278 -21.23125 9.38079   1.000 19.75561 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -28.18003 -21.11941 7.87074   1.000 20.24428 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -28.49913 -22.07158 7.15636   1.000 20.85907 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -27.38894 -22.36915 9.89598   1.000 19.82106 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -25.94611 -21.96128 10.03445  1.000 18.59752 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -25.54716 -21.14248 11.08562  1.000 21.02376 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -25.01009 -22.34690 9.09704   1.000 18.50803 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -24.22355 -20.72392 11.20614  1.000 22.27879 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -23.68818 -21.93892 9.20755   1.000 17.99356 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -23.29323 -21.12632 10.26763  1.000 17.61436 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -27.74030 -19.95564 7.38690   1.000 20.35793 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -27.70342 -19.64555 5.96711   1.000 18.45117 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -26.30756 -19.17470 5.58448   1.000 15.95266 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -25.58764 -18.60652 6.40423   1.000 16.81206 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -28.73754 -18.55144 5.60859   1.000 17.14490 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -30.16913 -19.04553 5.51345   1.000 18.53839 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -30.39786 -19.60373 4.12934   1.000 18.46029 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -31.80702 -19.85999 3.84768   1.000 19.42813 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -32.21023 -20.54305 2.78634   1.000 20.14710 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -31.33844 -21.01947 1.90776   1.000 23.26601 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -33.50843 -20.77762 2.61696   1.000 16.55959 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -25.93479 -19.38105 4.32361   1.000 15.50326 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -24.73588 -18.72233 3.81761   1.000 17.57849 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -25.03789 -17.23033 3.71032   1.000 18.70938 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -25.80231 -16.80286 2.84684   1.000 18.52051 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -24.30043 -19.30947 2.47642   1.000 21.00173 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -22.78824 -19.58627 2.40499   1.000 22.14018 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -22.47568 -20.76604 1.46852   1.000 24.16734 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -21.09536 -21.37191 1.71807   1.000 25.05481 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -19.92906 -20.71864 0.95603   1.000 21.98000 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -24.48287 -16.45518 4.62316   1.000 14.91489 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -24.79329 -15.05203 4.80031   1.000 15.61770 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? -23.64715 -14.15978 4.34526   1.000 14.05695 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? -22.50477 -14.33825 4.78620   1.000 15.66953 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -25.08365 -14.76263 6.27315   1.000 15.61755 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -25.98876 -13.63303 6.43498   1.000 17.39306 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -26.39733 -13.44827 8.16142   1.000 25.04227 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -27.78649 -14.54690 8.24774   1.000 18.01275 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? -23.94559 -13.20581 3.47492   1.000 14.17574 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? -22.96205 -12.20978 3.08396   1.000 12.82705 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? -23.11996 -10.96768 3.94817   1.000 13.37103 ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? -24.13639 -10.76938 4.61313   1.000 10.58288 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? -23.10935 -11.83471 1.61052   1.000 14.67267 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? -22.09234 -10.13291 3.94837   1.000 13.33269 ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? -22.23792 -8.84415  4.58887   1.000 12.10488 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? -23.11549 -7.93474  3.73726   1.000 10.48796 ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? -23.18441 -8.09457  2.51514   1.000 11.23887 ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? -20.87118 -8.19638  4.80702   1.000 12.57541 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? -20.07680 -8.86353  5.88621   1.000 13.86850 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? -20.33273 -8.57707  7.21718   1.000 19.95468 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? -19.07691 -9.75531  5.57727   1.000 14.39337 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? -19.61249 -9.19028  8.22432   1.000 24.35327 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? -18.33599 -10.36905 6.59640   1.000 17.84429 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? -18.60870 -10.07778 7.91758   1.000 18.67625 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? -23.82231 -6.99612  4.36365   1.000 13.81206 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? -24.56826 -6.00348  3.58514   1.000 12.67870 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? -23.60682 -5.28383  2.65819   1.000 14.43802 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? -22.48898 -4.92449  3.04798   1.000 14.76607 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? -25.15989 -5.07429  4.65033   1.000 15.61896 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? -25.11756 -5.86407  5.94590   1.000 14.41290 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? -23.90265 -6.76213  5.81552   1.000 13.00195 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? -24.02194 -5.12866  1.40800   1.000 13.48720 ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? -23.07750 -4.74848  0.36660   1.000 15.33491 ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? -23.05989 -3.25461  0.10218   1.000 13.30346 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? -22.22718 -2.80040  -0.69234  1.000 12.32100 ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? -23.38301 -5.51828  -0.92190  1.000 12.39531 ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? -24.73390 -5.35432  -1.32050  1.000 11.00362 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? -23.93515 -2.48855  0.76506   1.000 14.24026 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? -24.13165 -1.09351  0.38872   1.000 13.60985 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? -22.84641 -0.28013  0.34235   1.000 15.45840 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? -22.64492 0.51699   -0.57734  1.000 17.16890 ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? -21.97987 -0.44045  1.35060   1.000 13.75877 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? -20.76261 0.37151   1.42489   1.000 14.13579 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? -19.83362 0.09557   0.25300   1.000 14.17727 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? -19.04630 0.96261   -0.13344  1.000 17.81006 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? -20.01174 0.09136   2.73048   1.000 16.39173 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? -20.72192 0.50187   3.99393   1.000 19.79129 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? -19.75364 0.54393   5.15881   1.000 23.33804 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? -20.43840 0.19838   6.47402   1.000 29.77206 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? -21.56515 1.09106   6.83281   1.000 30.16824 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? -19.87189 -1.11929  -0.28641  1.000 14.79439 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? -19.03948 -1.44931  -1.44725  1.000 13.96409 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? -19.69526 -0.96094  -2.74195  1.000 15.24367 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? -19.02080 -0.40411  -3.61984  1.000 12.82469 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? -18.76830 -2.96060  -1.45705  1.000 10.96252 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? -17.95138 -3.36898  -2.68928  1.000 13.04622 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? -17.96690 -3.34531  -0.18864  1.000 11.46372 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? -21.02803 -1.13257  -2.86267  1.000 13.15706 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? -21.75189 -0.67937  -4.05079  1.000 12.78342 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? -21.41960 0.76907   -4.38686  1.000 15.41147 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? -21.28732 1.12970   -5.56265  1.000 16.39204 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? -23.26793 -0.81850  -3.84597  1.000 15.10680 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? -23.77355 -2.24782  -3.65147  1.000 12.67387 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? -25.19714 -2.29901  -3.13911  1.000 14.50050 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? -26.04868 -1.57277  -3.66980  1.000 15.33314 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? -25.47539 -3.07029  -2.19234  1.000 14.02862 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? -21.28830 1.61617   -3.36792  1.000 16.19015 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? -20.98379 3.01252   -3.62121  1.000 16.48493 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? -19.60798 3.27004   -4.17089  1.000 18.68047 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? -19.28699 4.41845   -4.49116  1.000 16.38703 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? -18.78501 2.24101   -4.28901  1.000 13.97575 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? -17.43414 2.40795   -4.79188  1.000 13.70612 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? -17.23502 1.83194   -6.17913  1.000 13.39206 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? -16.12233 1.91562   -6.71073  1.000 14.26841 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? -16.42853 1.76086   -3.83732  1.000 12.67924 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? -16.45703 2.35162   -2.11567  1.000 15.05359 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? -18.25410 1.20253   -6.75760  1.000 13.36730 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? -18.04818 0.41775   -7.96260  1.000 15.20626 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? -18.19741 1.33029   -9.16493  1.000 14.83546 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? -19.07356 2.20718   -9.17857  1.000 15.49945 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? -19.02460 -0.76355  -8.00522  1.000 12.67661 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? -18.73483 -1.77008  -6.88262  1.000 12.32370 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? -17.07057 -2.40923  -6.63654  1.000 11.83281 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? -16.48093 -2.57344  -8.31543  1.000 11.85449 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? -17.24992 1.22009   -10.10726 1.000 15.08173 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? -17.18045 2.06335   -11.29714 1.000 19.08669 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? -16.84719 1.18971   -12.50295 1.000 17.90423 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? -16.46020 0.03308   -12.37467 1.000 15.13582 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? -16.15031 3.21478   -11.16932 1.000 16.47452 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? -16.45979 4.08596   -9.95987  1.000 18.78648 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? -14.70563 2.71346   -11.14878 1.000 15.33965 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? -17.05261 1.75453   -13.68578 1.000 19.55075 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? -16.73745 1.11368   -14.95507 1.000 22.15258 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? -15.41678 1.67501   -15.47011 1.000 19.38720 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? -15.24456 2.89494   -15.52927 1.000 19.54941 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? -17.84533 1.37629   -15.97847 1.000 23.48352 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? -17.80903 0.48793   -17.19621 1.000 25.85238 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? -19.07335 0.58899   -18.03302 1.000 26.90393 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? -19.87258 1.51270   -17.87340 1.000 33.15141 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? -19.28515 -0.39073  -18.90445 1.000 32.14055 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? -14.49502 0.79351   -15.84584 1.000 20.42923 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? -13.21769 1.18851   -16.43499 1.000 21.46679 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? -13.13265 0.61149   -17.84084 1.000 20.84360 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? -13.25059 -0.60556  -18.02876 1.000 18.99708 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? -12.01250 0.72138   -15.60386 1.000 19.96277 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? -10.72991 1.12850   -16.29702 1.000 18.82321 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? -12.04658 1.27761   -14.18815 1.000 17.23394 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? -12.89140 1.47233   -18.82501 1.000 19.79036 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? -12.77450 1.03683   -20.20969 1.000 24.89901 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? -11.43138 1.47668   -20.77353 1.000 24.55497 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? -11.03123 2.63460   -20.61680 1.000 26.31726 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? -13.91349 1.59014   -21.07436 1.000 24.54755 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? -15.16809 1.11179   -20.57168 1.000 24.92953 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? -13.75824 1.11281   -22.51113 1.000 28.35266 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? -10.74039 0.55064   -21.42847 1.000 24.99391 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? -9.50756  0.85972   -22.13669 1.000 25.38183 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? -9.56001  0.10220   -23.45199 1.000 27.27031 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? -9.65457  -1.13067  -23.45205 1.000 26.76853 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? -8.27390  0.47300   -21.30912 1.000 23.13345 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? -6.68958  0.80353   -22.11173 1.000 29.43802 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? -9.54077  0.84013   -24.56192 1.000 25.59912 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? -9.73065  0.25994   -25.87918 1.000 27.50525 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? -11.10291 -0.36227  -26.01326 1.000 29.55903 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? -12.11694 0.31892   -25.84826 1.000 33.27985 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? -11.15984 -1.66084  -26.29509 1.000 31.25957 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? -12.43089 -2.36481  -26.36182 1.000 30.32874 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? -12.68386 -3.20552  -25.12554 1.000 28.97569 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? -13.63665 -3.99066  -25.10582 1.000 33.73014 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? -12.49617 -3.26160  -27.59809 1.000 33.79593 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? -11.35692 -4.12949  -27.61868 1.000 33.93286 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? -12.50647 -2.41290  -28.85833 1.000 30.85627 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? -11.84872 -3.07356  -24.10339 1.000 28.50985 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? -11.99542 -3.83798  -22.87489 1.000 26.35447 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? -12.69563 -2.99020  -21.82258 1.000 24.25359 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? -12.25945 -1.87849  -21.51181 1.000 25.86265 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? -10.63958 -4.32547  -22.35603 1.000 28.68324 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? -9.99673  -5.11593  -23.36613 1.000 32.27103 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? -10.81810 -5.16444  -21.09000 1.000 25.82357 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? -13.78134 -3.52053  -21.28055 1.000 24.13026 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? -14.52506 -2.87855  -20.20977 1.000 22.25639 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? -14.58908 -3.84851  -19.04035 1.000 21.26638 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? -14.93695 -5.01688  -19.22745 1.000 24.52710 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? -15.92231 -2.48650  -20.69706 1.000 22.30805 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? -15.82395 -1.34925  -21.56244 1.000 29.34359 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? -16.82299 -2.16292  -19.55324 1.000 23.60556 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? -14.20184 -3.38892  -17.85325 1.000 17.44969 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? -14.33728 -4.21038  -16.65866 1.000 18.48718 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? -14.67352 -3.29142  -15.48940 1.000 17.95169 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? -15.03263 -2.12345  -15.67546 1.000 17.51064 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? -13.07328 -5.04604  -16.40073 1.000 17.69358 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? -11.67250 -4.43039  -16.53818 1.000 16.70386 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? -11.40979 -3.38553  -15.48807 1.000 15.65337 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? -10.63089 -5.52864  -16.44810 1.000 18.01233 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? -14.56905 -3.81983  -14.27893 1.000 17.14987 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? -14.94680 -3.07000  -13.09141 1.000 15.57466 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? -13.73217 -2.50210  -12.38595 1.000 12.12232 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? -12.66243 -3.11328  -12.36565 1.000 11.61046 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? -15.71384 -3.95871  -12.11193 1.000 12.94047 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? -16.93393 -4.56357  -12.75092 1.000 15.25888 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? -17.94864 -3.89585  -12.91768 1.000 16.68030 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? -16.83534 -5.83352  -13.13858 1.000 15.33244 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? -13.93630 -1.34692  -11.74995 1.000 15.54987 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? -12.93105 -0.76258  -10.89686 1.000 12.17333 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? -13.50903 -0.41934  -9.53280  1.000 11.82851 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? -14.72125 -0.31874  -9.34644  1.000 13.83992 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? -12.61162 -0.22169  -8.58514  1.000 14.33520 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? -12.97169 0.06030   -7.19842  1.000 15.07895 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? -12.45363 1.45263   -6.85507  1.000 13.81073 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? -11.23510 1.70006   -6.88945  1.000 13.08955 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? -12.39886 -1.02049  -6.26317  1.000 11.44609 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? -12.73440 -0.86962  -4.77666  1.000 12.59831 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? -14.15232 -1.31587  -4.44012  1.000 14.37367 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? -11.72008 -1.52944  -3.86536  1.000 13.11660 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? -13.37991 2.36540   -6.52389  1.000 12.99463 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? -13.11317 3.81049   -6.44559  1.000 14.28341 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? -13.10465 4.25538   -4.98214  1.000 14.47687 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? -14.15017 4.25791   -4.31794  1.000 14.58815 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? -14.16853 4.58382   -7.23812  1.000 15.43727 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? -14.00804 6.10491   -7.22690  1.000 17.01079 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? -12.86026 6.80915   -7.00624  1.000 17.53211 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? -15.04615 7.08639   -7.42830  1.000 18.42254 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? -13.11336 8.16676   -7.06940  1.000 19.18740 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? -14.44251 8.35896   -7.33527  1.000 21.66301 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? -16.41411 7.00705   -7.69353  1.000 21.21589 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? -15.16754 9.54770   -7.48319  1.000 22.08822 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? -17.13029 8.18834   -7.84653  1.000 21.25788 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? -16.50542 9.43497   -7.73019  1.000 22.54044 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? -11.93381 4.65577   -4.48820  1.000 14.69645 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? -11.75112 5.01714   -3.08931  1.000 15.01209 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? -10.92986 6.29105   -3.02613  1.000 16.36896 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? -9.85945  6.37425   -3.63706  1.000 17.62538 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? -11.05559 3.90270   -2.29333  1.000 13.83955 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? -11.77738 2.55376   -2.31130  1.000 12.55997 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? -10.83359 1.46633   -1.82254  1.000 11.56512 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? -13.01462 2.64775   -1.43351  1.000 14.89427 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? -11.43359 7.28142   -2.30772  1.000 17.59928 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? -10.80210 8.60663   -2.32361  1.000 19.20463 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? -10.60208 8.95899   -3.80118  1.000 19.56268 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? -11.51254 8.73261   -4.61013  1.000 19.35314 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? -9.55036  8.56649   -1.45312  1.000 19.24634 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? -9.84764  8.09926   -0.02583  1.000 20.04616 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? -10.79801 8.61710   0.59144   1.000 20.06930 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? -9.11300  7.23997   0.50599   1.000 21.24662 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? -9.43166  9.43453   -4.23241  1.000 20.14460 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? -9.28047  9.81160   -5.63504  1.000 20.69415 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? -8.54046  8.77287   -6.48708  1.000 19.48345 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? -7.88809  9.14582   -7.47138  1.000 20.13770 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? -8.58897  11.17099  -5.74030  1.000 23.55958 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? -7.18322  11.15478  -5.19209  1.000 23.54915 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? -6.78809  10.16586  -4.53051  1.000 21.25870 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? -6.47233  12.16755  -5.39521  1.000 24.05572 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? -8.68518  7.46884   -6.19671  1.000 17.87770 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? -8.00082  6.43197   -6.96162  1.000 16.87014 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? -8.99862  5.34429   -7.35671  1.000 15.75491 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? -9.80837  4.91493   -6.52996  1.000 15.13365 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? -6.84258  5.82511   -6.14792  1.000 16.19715 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? -6.17992  4.68863   -6.90591  1.000 15.89029 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? -5.82277  6.88836   -5.80756  1.000 18.53122 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? -8.89847  4.86402   -8.59786  1.000 15.61005 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? -9.67453  3.72045   -9.07531  1.000 14.67038 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? -8.71269  2.55277   -9.26059  1.000 13.71729 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? -7.69875  2.67909   -9.96478  1.000 14.16394 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? -10.41253 4.02447   -10.39105 1.000 15.50093 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? -11.03366 2.73139   -10.97366 1.000 14.65799 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? -11.46864 5.12080   -10.19543 1.000 16.56202 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? -9.04503  1.41702   -8.65507  1.000 14.18820 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? -8.23855  0.20325   -8.68929  1.000 14.72951 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? -8.90137  -0.79126  -9.62380  1.000 13.69124 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? -10.12220 -0.97276  -9.57249  1.000 11.75490 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? -8.10571  -0.43498  -7.29008  1.000 11.09499 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? -7.47982  0.46182   -6.24539  1.000 12.57835 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? -8.22836  1.45508   -5.59550  1.000 11.85375 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? -6.13501  0.33181   -5.91379  1.000 14.21695 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? -7.62917  2.28532   -4.63504  1.000 15.86820 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? -5.53580  1.15413   -4.94827  1.000 13.26687 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? -6.29362  2.12080   -4.31009  1.000 15.64410 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? -5.67437  2.95114   -3.37246  1.000 18.51079 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? -8.11106  -1.44718  -10.47030 1.000 11.70357 ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? -8.70079  -2.39749  -11.40416 1.000 13.69750 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? -7.61169  -3.35454  -11.86776 1.000 13.84586 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? -6.42514  -3.05362  -11.71629 1.000 12.02377 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? -9.34854  -1.66792  -12.59500 1.000 12.35211 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? -8.23256  -0.98932  -13.87223 1.000 18.05680 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? -7.98462  -4.51048  -12.44191 1.000 11.23476 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? -6.95294  -5.43719  -12.95343 1.000 11.79627 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? -6.14850  -4.82435  -14.08444 1.000 13.71863 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? -6.70432  -4.22080  -15.00028 1.000 14.54650 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? -7.76257  -6.63220  -13.45809 1.000 12.69954 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? -9.06187  -6.57535  -12.66126 1.000 12.37272 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? -9.33580  -5.09718  -12.53766 1.000 13.53417 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? -4.82287  -4.98783  -14.01157 1.000 12.31967 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? -3.97997  -4.40146  -15.04816 1.000 13.51438 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? -4.22024  -5.03698  -16.41526 1.000 14.37625 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? -3.88000  -4.41872  -17.42861 1.000 15.54533 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? -2.49959  -4.48707  -14.65179 1.000 13.62809 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? -1.88059  -5.87031  -14.77584 1.000 13.49804 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? -0.40090  -5.92765  -14.37548 1.000 13.78935 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 0.09494   -7.30680  -14.37348 1.000 13.69832 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 1.37632   -7.65955  -14.28701 1.000 15.51154 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 2.34462   -6.75844  -14.19078 1.000 16.47463 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 1.70068   -8.94979  -14.33267 1.000 14.96050 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? -4.83572  -6.22611  -16.48935 1.000 16.53313 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? -5.03558  -6.75660  -17.83821 1.000 21.51910 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? -6.07567  -5.97189  -18.63682 1.000 19.73851 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? -6.26552  -6.27777  -19.82187 1.000 22.44628 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? -5.37897  -8.25749  -17.83046 1.000 20.46754 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? -6.72151  -8.61164  -17.25753 1.000 22.05157 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? -6.86366  -9.31009  -16.07549 1.000 21.87861 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? -7.97718  -8.42289  -17.73281 1.000 23.26155 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? -8.14977  -9.51024  -15.83307 1.000 21.61368 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? -8.84592  -8.98389  -16.82519 1.000 24.96627 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? -6.69574  -4.94138  -18.04828 1.000 17.99519 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? -7.55199  -4.03679  -18.82045 1.000 18.52305 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? -6.80270  -3.41786  -19.99672 1.000 19.66935 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? -7.42045  -3.07355  -21.01148 1.000 22.04227 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? -8.14982  -2.93395  -17.92400 1.000 18.05004 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? -7.09196  -1.89261  -17.55894 1.000 16.98329 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? -9.35525  -2.27072  -18.62353 1.000 17.77560 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? -5.47456  -3.25619  -19.89936 1.000 19.86023 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? -4.75447  -2.61071  -20.99555 1.000 20.34083 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? -4.32922  -3.58713  -22.08337 1.000 23.17674 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? -3.72620  -3.16010  -23.08090 1.000 24.67194 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? -3.49865  -1.82338  -20.54857 1.000 21.27981 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? -2.35771  -2.76733  -20.13406 1.000 19.55658 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? -3.84949  -0.76352  -19.49217 1.000 20.55595 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? -1.20123  -2.06860  -19.37395 1.000 19.15322 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? -4.64160  -4.87030  -21.94406 1.000 25.77635 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? -4.24936  -5.87061  -22.92144 1.000 27.57876 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? -5.33672  -6.10214  -23.95192 1.000 34.18911 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? -6.53380  -6.04162  -23.66207 1.000 33.04783 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? -3.93279  -7.20973  -22.26487 1.000 31.90277 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? -2.52988  -7.15318  -21.17303 1.000 30.45411 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? -4.89321  -6.40223  -25.15933 1.000 38.41494 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? -5.76152  -6.83438  -26.23266 1.000 44.64187 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? -5.81461  -8.35875  -26.25241 1.000 47.60531 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? -5.23288  -9.04026  -25.40303 1.000 45.31823 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? -5.26295  -6.28780  -27.56594 1.000 43.76321 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? -4.17864  -7.10331  -28.02555 1.000 46.56132 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? -4.77423  -4.85561  -27.39672 1.000 41.86387 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? -6.53602  -8.88981  -27.24309 1.000 52.89781 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? -6.62804  -10.33143 -27.45030 1.000 53.74822 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? -5.23499  -10.94236 -27.54047 1.000 52.19878 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? -4.81276  -11.71534 -26.67145 1.000 50.60025 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? -7.43146  -10.60939 -28.73227 1.000 56.43835 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? -8.79775  -10.19851 -28.62388 1.000 60.94271 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? -4.48614  -10.53783 -28.57173 1.000 54.33089 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? -3.12987  -11.03594 -28.80199 1.000 52.10670 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? -2.13678  -10.59915 -27.71635 1.000 52.25560 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? -1.14077  -11.30019 -27.46707 1.000 50.42771 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? -2.66902  -10.59930 -30.19829 1.000 53.37093 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? -2.62316  -9.08295  -30.42623 1.000 56.21318 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? -3.91811  -8.58175  -31.04958 1.000 57.13628 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? -4.99460  -9.07810  -30.63290 1.000 58.11419 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? -3.86374  -7.68521  -31.91968 1.000 54.61837 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? -2.39553  -9.46889  -27.04901 1.000 48.76676 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? -1.56201  -9.06008  -25.92114 1.000 46.97178 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? -1.62863  -10.08389 -24.79873 1.000 46.23878 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? -0.59905  -10.47602 -24.24103 1.000 43.66737 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? -1.99912  -7.68556  -25.40264 1.000 43.51884 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? -1.38938  -6.52977  -26.18698 1.000 42.19094 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? -0.39423  -6.75019  -26.91462 1.000 39.83509 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? -1.92620  -5.40463  -26.08447 1.000 40.39348 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? -2.84099  -10.52025 -24.44908 1.000 46.55326 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? -3.09354  -11.42019 -23.32564 1.000 46.31678 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? -2.45301  -12.79420 -23.47556 1.000 46.58277 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? -2.66002  -13.66664 -22.62609 1.000 48.90175 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? -4.60406  -11.58120 -23.13089 1.000 46.16512 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? -5.21807  -10.74341 -22.01764 1.000 42.82669 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? -4.10867  -10.32326 -20.65614 1.000 39.51891 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? -3.83153  -11.94882 -19.93758 1.000 35.31557 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? -1.67934  -13.01132 -24.53873 1.000 48.31422 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? -0.96391  -14.28031 -24.66828 1.000 47.87700 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? 0.25581   -14.28237 -23.75266 1.000 48.18381 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? 0.27201   -14.97334 -22.72726 1.000 49.71591 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? -0.58078  -14.54051 -26.13023 1.000 51.63482 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? -1.77349  -14.82393 -27.05779 1.000 52.57898 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? -1.34678  -14.86992 -28.52663 1.000 50.33385 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? -2.51311  -16.10463 -26.64929 1.000 50.53595 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? 1.26816   -13.47562 -24.07944 1.000 45.88282 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? 2.46141   -13.33812 -23.24052 1.000 45.20978 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? 2.88913   -11.87255 -23.21133 1.000 43.50096 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? 3.78844   -11.45409 -23.95063 1.000 45.69769 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? 3.59285   -14.23003 -23.75741 1.000 49.32554 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? 4.56539   -14.63924 -22.66118 1.000 50.76933 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? 4.57677   -14.06035 -21.56797 1.000 50.24853 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? 5.38876   -15.64453 -22.95045 1.000 46.92643 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? 2.26658   -11.05200 -22.34067 1.000 40.93379 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? 2.50209   -9.60423  -22.39118 1.000 38.91697 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? 3.56369   -9.07417  -21.44417 1.000 34.50232 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? 3.80897   -9.62880  -20.37137 1.000 32.94363 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? 1.12691   -9.04228  -22.03004 1.000 38.33691 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? 0.61110   -10.01814 -21.00672 1.000 36.89443 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? 1.23013   -11.37225 -21.34954 1.000 39.48021 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? 4.19156   -7.97774  -21.84776 1.000 31.61504 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? 5.14734   -7.24616  -21.02125 1.000 31.47468 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? 4.39912   -6.00193  -20.54291 1.000 28.93152 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? 4.31358   -4.99877  -21.25888 1.000 28.06139 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? 6.41646   -6.94193  -21.82289 1.000 31.76662 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? 7.44791   -6.13707  -21.04526 1.000 32.70585 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? 7.16744   -5.56703  -19.99907 1.000 33.12269 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? 8.67430   -6.12227  -21.55551 1.000 37.45284 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? 3.82044   -6.09124  -19.34020 1.000 26.89031 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? 2.89740   -5.05769  -18.88073 1.000 24.45167 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? 3.56000   -3.69103  -18.74733 1.000 25.94157 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? 2.91271   -2.66743  -18.99655 1.000 24.80703 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? 2.25632   -5.46832  -17.55718 1.000 21.91474 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? 1.13321   -6.46446  -17.72507 1.000 17.37104 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? -0.13241  -6.03428  -18.08778 1.000 16.99196 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? 1.32873   -7.82512  -17.49303 1.000 20.17772 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? -1.17215  -6.90951  -18.23233 1.000 20.35025 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? 0.27649   -8.72938  -17.63075 1.000 20.37563 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? -0.97047  -8.25167  -18.00383 1.000 20.12787 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? -2.01913  -9.10719  -18.16475 1.000 19.62002 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? 4.82710   -3.63828  -18.33905 1.000 26.60740 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? 5.51575   -2.35236  -18.32195 1.000 26.51581 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? 5.55320   -1.73907  -19.71519 1.000 26.25461 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? 5.26317   -0.55010  -19.88314 1.000 23.60452 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? 6.92116   -2.50122  -17.72867 1.000 28.02608 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? 6.90468   -2.97346  -16.26780 1.000 33.02481 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? 6.80681   -4.49822  -16.09193 1.000 38.49246 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? 6.50424   -5.22866  -17.07043 1.000 35.21947 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? 6.99327   -4.96430  -14.94388 1.000 40.26969 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? 5.85349   -2.55058  -20.72944 1.000 26.82195 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? 5.88100   -2.05255  -22.10100 1.000 29.63278 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? 4.50275   -1.56009  -22.53181 1.000 28.44763 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? 4.36791   -0.50067  -23.16245 1.000 26.67612 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? 6.34957   -3.15861  -23.04255 1.000 33.64155 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? 7.83876   -3.16568  -23.23905 1.000 36.22766 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? 8.50308   -2.20076  -22.80868 1.000 37.85377 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? 8.33952   -4.13123  -23.85264 1.000 39.91426 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? 3.46227   -2.33204  -22.21401 1.000 25.42622 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? 2.12632   -1.95931  -22.65396 1.000 26.28255 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? 1.66984   -0.67343  -21.98201 1.000 26.30048 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? 1.00928   0.16015   -22.61515 1.000 26.03119 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? 1.14236   -3.09586  -22.37880 1.000 24.98669 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? 1.40222   -4.39767  -23.13828 1.000 27.04797 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? 0.49073   -5.52535  -22.65494 1.000 30.36798 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? 1.25060   -4.18265  -24.64009 1.000 29.33375 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? 2.04966   -0.47135  -20.71708 1.000 23.18017 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? 1.53420   0.67504   -19.97770 1.000 23.21169 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? 2.20264   1.98038   -20.40553 1.000 23.82683 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? 1.54137   3.02051   -20.46627 1.000 24.28328 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? 1.68973   0.44754   -18.47349 1.000 23.50790 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? 1.01217   1.48020   -17.56135 1.000 22.53273 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? -0.44620  1.64741   -17.94107 1.000 20.37010 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? 1.11797   1.06218   -16.10216 1.000 21.90581 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? 3.50128   1.95332   -20.71453 1.000 24.79028 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? 4.19200   3.17981   -21.09828 1.000 26.38204 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? 3.61446   3.74813   -22.39510 1.000 27.83774 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? 3.72542   4.95480   -22.65238 1.000 29.08744 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? 5.71930   2.92041   -21.20221 1.000 27.23400 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? 6.50272   4.22697   -21.27619 1.000 28.74816 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? 6.06403   2.08029   -22.41001 1.000 28.19519 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? 6.05050   5.25631   -20.26859 1.000 31.91085 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? 2.97172   2.90617   -23.20559 1.000 27.83500 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? 2.34592   3.31117   -24.45714 1.000 29.30381 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? 0.97278   3.92015   -24.26115 1.000 28.90298 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? 0.37169   4.38710   -25.23496 1.000 30.24071 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? 2.23638   2.10769   -25.37983 1.000 29.65068 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? 3.55017   1.69826   -25.96283 1.000 30.82043 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? 3.51721   0.26865   -26.40197 1.000 30.64840 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? 4.86995   -0.26204  -26.47905 1.000 31.25806 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? 5.16730   -1.49545  -26.85369 1.000 32.01874 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? 4.21863   -2.39790  -27.06951 1.000 30.94625 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? 6.44576   -1.83803  -26.99416 1.000 32.54685 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? 0.47010   3.91338   -23.03772 1.000 27.24953 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? -0.85017  4.41013   -22.70314 1.000 26.78473 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? -0.73811  5.83129   -22.16822 1.000 27.39405 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? 0.28659   6.22723   -21.61588 1.000 27.50345 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? -1.49375  3.51351   -21.64167 1.000 25.57400 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? -1.95006  2.14290   -22.13909 1.000 24.18472 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? -2.81333  2.22981   -23.37574 1.000 29.12751 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? -3.20790  0.84635   -23.85365 1.000 29.49628 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? -3.97449  0.95059   -25.13447 1.000 31.73016 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? -1.82715  6.58153   -22.30799 1.000 27.89741 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? -1.98218  7.90890   -21.73252 1.000 29.68121 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? -3.19869  7.91714   -20.80929 1.000 28.81400 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? -4.03246  7.01446   -20.85649 1.000 28.98688 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? -2.16584  8.97062   -22.82703 1.000 30.72232 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? -1.40645  8.67442   -23.99107 1.000 36.60411 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? -3.30429  8.96268   -19.98098 1.000 27.97187 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? -4.47964  9.12782   -19.12325 1.000 26.76658 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? -5.78330  9.05170   -19.92165 1.000 27.85528 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? -6.72640  8.35786   -19.52345 1.000 28.36283 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? -4.38848  10.46121  -18.37574 1.000 27.66396 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? -3.35694  10.44714  -17.26168 1.000 29.24872 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? -2.95071  9.38750   -16.78354 1.000 28.42665 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? -2.90576  11.63146  -16.86184 1.000 28.19454 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? -5.85992  9.76787   -21.05239 1.000 29.16965 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? -7.08955  9.82091   -21.84157 1.000 30.00834 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? -7.47830  8.48267   -22.46064 1.000 30.02460 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? -8.61102  8.35483   -22.94118 1.000 29.81485 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? -6.97498  10.87511  -22.94873 1.000 34.14853 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? -6.15838  10.43902  -24.12696 1.000 34.98879 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? -4.79025  10.60821  -24.18958 1.000 36.88972 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? -6.51558  9.83804   -25.28859 1.000 35.40909 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? -4.34107  10.14320  -25.34360 1.000 34.65491 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? -5.36752  9.66712   -26.02794 1.000 38.09926 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? -6.58376  7.49205   -22.46848 1.000 28.23759 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? -6.95391  6.15188   -22.91429 1.000 29.95124 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? -7.83936  5.41945   -21.91103 1.000 27.98495 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? -8.39516  4.37106   -22.25515 1.000 27.06440 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? -5.70158  5.31449   -23.16986 1.000 27.09487 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? -4.87359  5.82127   -24.32409 1.000 29.18839 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? -3.66563  5.61121   -24.36112 1.000 29.04690 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? -5.51966  6.46319   -25.29269 1.000 33.20735 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? -7.96280  5.92616   -20.68499 1.000 26.01855 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? -8.75564  5.28841   -19.63949 1.000 26.41062 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? -10.04868 6.06673   -19.43008 1.000 28.36342 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? -10.02710 7.23099   -19.01751 1.000 27.66087 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? -7.97904  5.18456   -18.32989 1.000 23.44301 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? -6.72097  4.36840   -18.43128 1.000 22.76738 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? -6.76262  2.99178   -18.31369 1.000 23.77082 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? -5.49757  4.98256   -18.66904 1.000 24.49627 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? -5.59985  2.23947   -18.40962 1.000 23.53679 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? -4.33569  4.23982   -18.76679 1.000 23.13530 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? -4.38612  2.86709   -18.63073 1.000 22.55278 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? -11.16127 5.40963   -19.71002 1.000 25.12492 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? -12.49209 5.97139   -19.55893 1.000 29.08934 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? -13.06520 5.37148   -18.28278 1.000 26.72001 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? -13.13088 4.14831   -18.16712 1.000 24.93995 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? -13.34295 5.58625   -20.76625 1.000 29.49763 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? -13.15173 6.42963   -22.02365 1.000 32.52298 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? -13.39488 5.56979   -23.26757 1.000 33.02245 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? -14.09432 7.62430   -22.00944 1.000 33.62047 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? -13.42949 6.21498   -17.31597 1.000 28.05579 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? -14.00259 5.76153   -16.04942 1.000 26.51576 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? -15.39624 6.36561   -15.90401 1.000 26.15438 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? -15.56071 7.58724   -15.99164 1.000 29.55922 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? -13.10970 6.12669   -14.84284 1.000 24.71549 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? -13.69749 5.56154   -13.54405 1.000 24.09135 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? -11.68962 5.60565   -15.04164 1.000 24.74508 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? -16.40030 5.51247   -15.68546 1.000 25.38768 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? -17.78622 5.95537   -15.53492 1.000 27.40547 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? -18.25151 5.60413   -14.13134 1.000 25.86541 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? -18.25739 4.42688   -13.75622 1.000 25.40179 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? -18.71241 5.29579   -16.56132 1.000 30.22296 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? -18.03866 4.95070   -17.87059 1.000 33.63800 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? -18.39745 5.87389   -19.00420 1.000 39.69824 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? -19.47903 6.47071   -19.02603 1.000 42.81823 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? -17.48245 6.00477   -19.96209 1.000 38.54570 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? -18.63833 6.61714   -13.36142 1.000 25.75401 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? -19.19345 6.40785   -12.02594 1.000 29.71539 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? -20.69889 6.58313   -12.17352 1.000 32.05848 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? -21.22878 7.69000   -12.08918 1.000 30.48625 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? -18.57473 7.35902   -11.00896 1.000 29.95266 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? -21.38571 5.47348   -12.42863 1.000 32.16135 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? -22.75570 5.57346   -12.90413 1.000 36.45899 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? -22.76167 6.29277   -14.23874 1.000 37.25439 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? -21.97954 5.97895   -15.14478 1.000 36.38700 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? -23.62842 7.29524   -14.36370 1.000 36.87595 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? -23.70850 8.10057   -15.57546 1.000 42.45042 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? -22.84765 9.36152   -15.50721 1.000 41.21484 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? -23.09130 10.31572  -16.25893 1.000 42.09615 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? -25.17064 8.45361   -15.87339 1.000 43.64203 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? -25.91813 8.93403   -14.63847 1.000 50.12989 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? -25.30630 9.39421   -13.66950 1.000 52.61227 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? -27.24777 8.83811   -14.67013 1.000 49.93054 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? -21.85000 9.38346   -14.62761 1.000 35.68345 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? -20.93990 10.51168  -14.47798 1.000 37.56971 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? -19.53781 10.03637  -14.82868 1.000 36.07925 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? -19.09785 8.98383   -14.35347 1.000 34.42152 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? -20.98756 11.09026  -13.05212 1.000 38.01985 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? -20.46345 12.51390  -13.03751 1.000 41.41105 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? -22.40665 11.05161  -12.52808 1.000 42.30935 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? -18.84206 10.79791  -15.66188 1.000 37.15644 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? -17.52040 10.40758  -16.12880 1.000 35.16587 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? -16.45491 11.05037  -15.25173 1.000 34.71428 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? -16.51597 12.25309  -14.97296 1.000 35.74165 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? -17.31483 10.80215  -17.59030 1.000 41.35154 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? -15.86028 10.73637  -18.01664 1.000 40.02059 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? -15.70023 10.55069  -19.50476 1.000 44.89329 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? -15.49209 9.43416   -19.97878 1.000 44.79805 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? -15.79315 11.64819  -20.25591 1.000 46.41917 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? -15.47679 10.24728  -14.83446 1.000 31.24094 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? -14.40481 10.67996  -13.95060 1.000 30.69949 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? -13.14826 10.92469  -14.77663 1.000 33.70571 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? -12.73113 10.05889  -15.55295 1.000 33.02738 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? -14.13825 9.63092   -12.86872 1.000 29.66520 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? -15.29429 9.29855   -11.92014 1.000 30.06679 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? -14.80870 8.42183   -10.78459 1.000 25.82038 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? -15.94658 10.56900  -11.37734 1.000 29.81988 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? -12.55237 12.10421  -14.61943 1.000 31.89602 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? -11.37200 12.45994  -15.39476 1.000 33.08872 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? -10.14039 11.81295  -14.76795 1.000 30.22965 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? -9.85078  12.04357  -13.58963 1.000 29.93028 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? -11.23318 13.98199  -15.46126 1.000 34.22907 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? -9.93734  14.48078  -16.08213 1.000 35.07109 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? -10.11781 15.85208  -16.70781 1.000 40.31628 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? -9.26337  16.85568  -16.08572 1.000 43.19328 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? -8.03677  17.14803  -16.49917 1.000 49.44004 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? -7.46655  16.48513  -17.49499 1.000 50.33725 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? -7.36271  18.12727  -15.89739 1.000 49.58347 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? -9.43926  10.98062  -15.54321 1.000 27.17689 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? -8.18935  10.36273  -15.10273 1.000 28.98597 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? -7.05224  11.37051  -15.23317 1.000 27.63533 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? -6.82961  11.93291  -16.31109 1.000 27.69468 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? -7.89477  9.09764   -15.92176 1.000 23.91575 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? -6.47146  8.62701   -15.67212 1.000 25.85455 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? -8.91664  7.99928   -15.58952 1.000 24.07100 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? -6.30431  11.57730  -14.14744 1.000 27.28184 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? -5.21275  12.54721  -14.12931 1.000 27.26764 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? -3.86468  11.90912  -13.82948 1.000 26.46395 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? -2.84955  12.61889  -13.76474 1.000 28.35309 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? -5.49254  13.68729  -13.12976 1.000 28.47567 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? -5.73793  13.12543  -11.72486 1.000 27.81103 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? -6.70249  14.50164  -13.58313 1.000 29.62041 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? -5.47500  14.15765  -10.62766 1.000 29.88775 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? -3.82043  10.59919  -13.62821 1.000 27.86008 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? -2.57753  9.89810   -13.39276 1.000 24.00507 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? -2.82484  8.41070   -13.49296 1.000 25.60360 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? -3.95388  7.95610   -13.27700 1.000 24.51555 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? -1.79869  7.63726   -13.83313 1.000 24.89498 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? -1.93879  6.18785   -13.82626 1.000 22.16877 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? -0.62255  5.54783   -13.41340 1.000 22.53969 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? 0.46174   6.06464   -13.71752 1.000 21.09993 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? -2.37567  5.66586   -15.20292 1.000 20.63146 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? -1.38895  5.93571   -16.29353 1.000 25.12566 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? -1.30275  7.15171   -16.94057 1.000 26.45558 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? -0.45451  5.13748   -16.86138 1.000 23.82906 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? -0.34470  7.09234   -17.85151 1.000 29.33900 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? 0.17854   5.87818   -17.82836 1.000 27.42822 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? -0.71437  4.40479   -12.72786 1.000 19.36218 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? 0.49751   3.67388   -12.38079 1.000 19.68531 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? 0.15498   2.21236   -12.13450 1.000 18.52670 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? -0.98317  1.86339   -11.81750 1.000 19.38735 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? 1.18903   4.25891   -11.14200 1.000 20.88546 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? 0.28057   4.36023   -10.05763 1.000 24.12502 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? 1.16088   1.36626   -12.26977 1.000 16.75468 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? 1.01652   -0.04486  -11.95123 1.000 20.11223 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? 1.51744   -0.31876  -10.54411 1.000 20.15312 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? 2.54601   0.22448   -10.11890 1.000 19.03360 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? 1.78597   -0.90983  -12.94426 1.000 19.97720 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? 1.22938   -2.28295  -13.07453 1.000 20.07003 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? 1.75798   -3.02051  -14.61342 1.000 21.81221 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? 3.30571   -2.17074  -14.95838 1.000 24.56736 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? 0.78207   -1.16395  -9.83655  1.000 16.89388 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? 1.21217   -1.78972  -8.58688  1.000 20.35312 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? 0.94261   -3.28064  -8.68895  1.000 14.27720 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? -0.21905  -3.70378  -8.60534  1.000 14.16657 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? 0.47772   -1.21289  -7.38863  1.000 20.24389 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? 1.12408   -1.57324  -6.08546  1.000 23.13311 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? 0.37981   -0.98516  -4.92091  1.000 26.52107 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? -0.37804  -1.67208  -4.23771  1.000 26.61147 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? 0.59626   0.30774   -4.67906  1.000 28.35310 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? 2.01506   -4.06841  -8.87199  1.000 14.18875 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? 1.90930   -5.50897  -9.09695  1.000 15.61681 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? 0.87745   -5.80450  -10.18084 1.000 12.23110 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? 1.05340   -5.33033  -11.30557 1.000 12.76280 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? 1.63334   -6.21320  -7.77538  1.000 12.00358 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? 2.66790   -5.83162  -6.73247  1.000 13.78680 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? 3.86869   -5.93213  -6.98525  1.000 14.70484 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? 2.21607   -5.32231  -5.59596  1.000 14.74807 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? -0.18936  -6.55424  -9.89431  1.000 13.34620 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? -1.12577  -6.91531  -10.94574 1.000 11.10358 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? -2.36144  -6.00654  -11.01014 1.000 11.45428 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? -3.31840  -6.32309  -11.73210 1.000 10.82722 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? -1.53044  -8.38090  -10.80009 1.000 12.30869 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? -0.16218  -9.47101  -11.16391 1.000 11.95851 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? -2.35811  -4.87939  -10.30089 1.000 10.88942 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? -3.45532  -3.92229  -10.40855 1.000 11.22877 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? -2.93773  -2.60695  -10.98795 1.000 13.60772 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? -1.74780  -2.28501  -10.92823 1.000 13.38611 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? -4.18336  -3.68303  -9.06355  1.000 11.74645 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? -4.75534  -4.99757  -8.50056  1.000 14.11558 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? -3.27029  -3.04089  -8.06627  1.000 12.83881 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? -3.85746  -1.87104  -11.60543 1.000 12.46119 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? -3.65426  -0.48299  -11.98964 1.000 14.69105 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? -4.23827  0.44848   -10.94086 1.000 14.10609 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? -5.22701  0.13441   -10.28209 1.000 13.28643 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? -4.31140  -0.16310  -13.33136 1.000 16.16273 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? -3.59533  -0.11871  -14.66552 1.000 18.41936 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? -4.62351  0.30802   -15.71094 1.000 21.68357 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? -2.43807  0.86476   -14.62826 1.000 21.66811 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? -3.61106  1.61023   -10.79053 1.000 16.02585 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? -4.13265  2.66446   -9.92841  1.000 17.11026 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? -4.34403  3.87636   -10.81561 1.000 18.88479 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? -3.37867  4.41983   -11.36327 1.000 17.17028 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? -3.17869  2.97251   -8.77266  1.000 19.65455 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? -3.00014  1.79664   -7.83011  1.000 20.19485 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? -1.95086  2.07208   -6.77024  1.000 20.50520 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? -2.47907  3.03418   -5.71605  1.000 24.45487 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? -1.44630  3.37580   -4.69667  1.000 31.02464 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? -5.60733  4.25162   -11.00559 1.000 18.02189 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? -5.98000  5.34485   -11.89445 1.000 17.64233 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? -6.30264  6.54754   -11.01905 1.000 18.48477 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? -7.29690  6.54411   -10.28569 1.000 18.61015 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? -7.16807  4.93684   -12.76396 1.000 17.58033 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? -6.87547  3.72099   -13.65973 1.000 17.72766 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? -8.06873  3.46454   -14.57902 1.000 19.77179 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? -5.58616  3.89672   -14.49386 1.000 20.03718 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? -5.46288  7.57447   -11.08411 1.000 19.65618 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? -5.70663  8.78653   -10.31166 1.000 23.05567 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? -6.77393  9.63633   -11.01025 1.000 25.17734 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? -6.60803  10.03877  -12.16680 1.000 25.91894 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? -4.39189  9.54585   -10.12656 1.000 25.25312 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? -4.41175  10.71647  -9.14143  1.000 27.69519 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? -4.73105  10.26403  -7.73528  1.000 31.56108 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? -3.58286  10.56075  -6.77283  1.000 32.06408 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? -3.78768  9.83437   -5.47513  1.000 31.87066 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? -7.87932  9.89261   -10.31839 1.000 23.32060 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? -8.96514  10.68707  -10.86844 1.000 26.20193 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? -9.03040  12.01001  -10.11342 1.000 26.96064 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? -8.45127  12.16551  -9.03274  1.000 27.41657 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? -10.29943 9.92085   -10.81986 1.000 27.80990 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? -10.16179 8.60930   -11.59205 1.000 26.51543 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? -10.70348 9.63160   -9.38115  1.000 23.57402 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? -9.72192  12.98648  -10.70445 1.000 26.19661 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? -9.75229  14.33320  -10.14230 1.000 31.67041 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? -10.89476 14.54743  -9.15724  1.000 30.78947 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? -11.12930 15.68444  -8.73785  1.000 30.05948 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? -9.83685  15.39171  -11.25453 1.000 30.29559 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? -11.14955 15.34373  -12.03010 1.000 33.04298 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? -11.99117 14.45076  -11.78807 1.000 32.72665 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? -11.34217 16.23048  -12.88925 1.000 40.33228 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? -11.62589 13.49790  -8.80220  1.000 29.57507 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? -12.69884 13.59839  -7.82227  1.000 29.06565 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? -12.50904 12.49481  -6.79987  1.000 27.86147 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? -12.34793 11.32936  -7.17034  1.000 24.31487 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? -14.08582 13.47417  -8.46754  1.000 29.57934 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? -14.18509 14.38173  -9.56323  1.000 28.68266 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? -15.18433 13.79848  -7.46203  1.000 29.15388 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? -12.50134 12.86622  -5.52208  1.000 28.86390 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? -12.53765 11.87343  -4.46521  1.000 23.74376 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? -13.96412 11.36368  -4.31618  1.000 24.55523 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? -14.92242 12.13810  -4.34741  1.000 24.64398 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? -12.03978 12.46275  -3.14826  1.000 24.58499 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? -14.10160 10.06490  -4.18397  1.000 21.49651 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? -15.42320 9.46405   -4.02550  1.000 21.56540 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? -16.05750 9.94415   -2.72569  1.000 22.00297 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? -15.50571 9.69030   -1.64793  1.000 21.45948 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? -15.27414 7.95567   -4.03239  1.000 19.02879 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? -16.61205 7.20994   -3.98463  1.000 18.50185 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? -17.70788 7.79457   -3.93871  1.000 19.60174 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? -16.50759 5.90365   -3.94632  1.000 17.79146 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? -17.18594 10.65776  -2.76813  1.000 24.49248 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? -17.81585 11.07731  -1.50808  1.000 25.19032 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? -18.38446 9.91508   -0.71486  1.000 22.86891 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? -18.67879 10.07308  0.47910   1.000 23.45266 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? -18.91631 12.03955  -1.96690  1.000 26.03298 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? -19.24134 11.62643  -3.35439  1.000 25.47605 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? -17.98073 11.04053  -3.95055  1.000 24.07268 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? -18.56075 8.75883   -1.34020  1.000 21.74579 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? -19.08707 7.58957   -0.66367  1.000 20.54667 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? -17.99220 6.66995   -0.13497  1.000 18.55950 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? -18.29537 5.54389   0.25310   1.000 18.33349 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? -20.01258 6.81663   -1.60407  1.000 19.37888 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? -21.34510 7.51636   -1.89034  1.000 22.62041 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? -22.15254 6.71942   -2.92112  1.000 25.44086 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? -22.74684 7.60995   -4.00055  1.000 27.43255 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? -24.05071 7.08672   -4.49534  1.000 32.83551 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? -16.74241 7.12261   -0.09484  1.000 19.23375 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? -15.65342 6.27604   0.39224   1.000 19.44932 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? -15.90862 5.86089   1.83634   1.000 17.86517 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? -16.02729 6.73387   2.70788   1.000 19.53227 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? -14.32227 7.02488   0.29053   1.000 20.46687 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? -14.06344 7.37167   -1.07515  1.000 22.19684 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? -13.19966 6.19514   0.81141   1.000 19.61793 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? -16.03006 4.57697   2.13634   1.000 17.62388 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? -16.16812 4.16947   3.53036   1.000 18.45805 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? -14.79764 4.16402   4.18493   1.000 18.57542 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? -13.76705 4.26149   3.52019   1.000 16.28422 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? -16.73804 2.75747   3.42132   1.000 15.27905 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? -16.08419 2.23714   2.21881   1.000 17.65997 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? -15.89690 3.39780   1.26117   1.000 15.89708 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? -14.79940 4.07972   5.50995   1.000 18.27893 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? -13.58331 3.66418   6.19285   1.000 20.32199 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? -13.20792 2.28311   5.66300   1.000 18.99926 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? -14.07645 1.41769   5.51344   1.000 16.87259 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? -13.81332 3.67024   7.70915   1.000 25.24504 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? -12.92616 2.74720   8.53928   1.000 25.97102 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? -11.77543 3.45981   9.26630   1.000 28.88970 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? -10.67550 2.44935   9.68258   1.000 24.28986 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? -9.66364  2.08344   8.59884   1.000 25.50549 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? -11.93324 2.09503   5.29722   1.000 17.55701 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? -11.54781 0.83973   4.66881   1.000 14.67211 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? -10.13388 0.41480   5.05615   1.000 16.94678 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? -9.33806  1.18672   5.59297   1.000 14.18297 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? -11.65915 0.90183   3.13488   1.000 14.52692 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? -10.63979 1.79162   2.43804   1.000 17.54290 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? -10.88015 3.14974   2.24293   1.000 16.64335 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? -9.43373  1.26403   1.96636   1.000 15.24873 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? -9.94068  3.96122   1.60702   1.000 18.96184 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? -8.51055  2.05556   1.31627   1.000 18.34418 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? -8.76532  3.40620   1.14559   1.000 18.94594 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? -7.82258  4.18809   0.50994   1.000 25.46305 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? -9.83623  -0.85089  4.74696   1.000 13.95012 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? -8.49055  -1.40203  4.83348   1.000 13.69030 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? -8.26966  -2.37490  3.68875   1.000 13.62697 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? -9.20593  -3.02830  3.22401   1.000 11.23797 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? -8.24169  -2.15717  6.13550   1.000 18.69064 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? -8.60694  -1.39724  7.38949   1.000 19.53942 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? -8.08169  -2.10237  8.61769   1.000 22.80319 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? -8.85092  -3.38870  8.87545   1.000 18.91828 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? -8.54761  -3.91137  10.25029  1.000 28.63335 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? -7.00597  -2.49388  3.27764   1.000 10.68490 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? -6.55026  -3.54562  2.37265   1.000 11.83358 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? -5.87943  -4.61870  3.22087   1.000 12.53102 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? -4.78632  -4.40836  3.76278   1.000 9.59366  ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? -5.56376  -3.01098  1.34360   1.000 12.67504 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? -6.17545  -2.14420  0.30781   1.000 12.99347 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? -7.55235  -2.04292  0.17906   1.000 10.70745 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? -5.36699  -1.40622  -0.53385  1.000 15.03938 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? -8.11484  -1.20989  -0.76471  1.000 10.95237 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? -5.93151  -0.58947  -1.51080  1.000 14.15460 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? -7.29800  -0.48293  -1.61731  1.000 11.69173 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? -6.55625  -5.75227  3.36923   1.000 10.14454 ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? -6.02137  -6.88468  4.10401   1.000 12.50755 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? -5.84520  -8.01631  3.10883   1.000 10.59635 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? -6.44218  -8.02031  2.03196   1.000 14.42019 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? -6.92929  -7.30815  5.27541   1.000 12.85299 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? -7.31378  -6.08492  6.10015   1.000 15.60599 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? -8.19925  -7.94409  4.74888   1.000 14.18428 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? -4.99609  -8.97257  3.46578   1.000 8.25901  ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? -4.87812  -10.22059 2.72200   1.000 8.31233  ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? -5.33366  -11.33908 3.64419   1.000 10.08707 ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? -4.95124  -11.35209 4.80918   1.000 9.96409  ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? -3.43436  -10.46880 2.27443   1.000 11.94662 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? -3.29351  -11.63044 1.31498   1.000 10.15182 ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? -1.82066  -11.79688 0.97254   1.000 8.93747  ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? -1.56925  -13.04010 0.24357   1.000 11.21349 ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? -1.55690  -13.10274 -1.08105  1.000 9.15183  ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? -1.79531  -12.03408 -1.81427  1.000 9.23433  ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? -1.27380  -14.25176 -1.68072  1.000 8.01005  ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? -6.14892  -12.25637 3.13511   1.000 9.97486  ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? -6.71552  -13.30613 3.94776   1.000 12.00603 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? -5.91566  -14.58474 3.73094   1.000 11.72880 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? -5.14756  -14.71085 2.78808   1.000 10.94177 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? -8.21206  -13.56473 3.64467   1.000 11.05989 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? -8.38396  -14.03849 2.20111   1.000 10.92464 ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? -9.07552  -12.34695 4.02235   1.000 15.15604 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? -9.81334  -14.61717 1.91134   1.000 14.13790 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? -6.13373  -15.55167 4.59151   1.000 11.28816 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? -5.64083  -16.92065 4.68590   1.000 11.80956 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? -6.62110  -17.88457 4.02837   1.000 12.51436 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? -7.83759  -17.72147 4.15841   1.000 11.86933 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? -5.46121  -17.32305 6.14079   1.000 14.25133 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? -4.33123  -16.59289 6.80640   1.000 14.91861 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? -3.01062  -17.04769 6.25516   1.000 14.51323 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? -2.82285  -18.23941 6.02500   1.000 12.38533 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? -2.11808  -16.10402 5.94840   1.000 14.90198 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? -6.12523  -18.89622 3.32832   1.000 12.66180 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? -7.00886  -20.00048 2.93384   1.000 14.85240 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? -7.75572  -20.50430 4.15990   1.000 13.54212 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? -7.21932  -20.52734 5.27160   1.000 16.43350 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? -6.04424  -21.05749 2.37795   1.000 12.58766 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? -4.66355  -20.55533 2.66457   1.000 16.19785 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? -4.73742  -19.08767 2.88542   1.000 13.65986 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? -9.00580  -20.90415 3.95854   1.000 11.33045 ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? -9.87410  -21.28449 5.03821   1.000 12.81578 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? -10.76522 -20.16338 5.52990   1.000 15.09575 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? -11.83554 -20.44469 6.07393   1.000 15.11222 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? -10.35770 -18.90302 5.35385   1.000 10.61658 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? -11.21309 -17.77101 5.71851   1.000 12.71573 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? -12.20949 -17.39535 4.62836   1.000 11.96370 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? -12.03545 -17.71215 3.44710   1.000 11.44636 ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? -10.42057 -16.51008 6.12248   1.000 11.21195 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? -9.34012  -16.73496 7.15364   1.000 17.59486 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? -8.52702  -15.48399 7.54754   1.000 21.57128 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? -7.84097  -14.84060 6.75159   1.000 15.33084 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? -8.66424  -15.11003 8.82259   1.000 30.65309 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? -13.28618 -16.73136 5.05853   1.000 10.14380 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? -14.40014 -16.38635 4.18132   1.000 10.91181 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? -14.44867 -14.88034 3.93576   1.000 10.37603 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? -13.79314 -14.07972 4.61244   1.000 11.56069 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? -15.74999 -16.85235 4.76386   1.000 11.75784 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? -15.89790 -16.32732 6.08445   1.000 12.69192 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? -15.78872 -18.38430 4.83124   1.000 10.93118 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? -15.23306 -14.51778 2.92478   1.000 9.03224  ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? -15.49966 -13.13757 2.55956   1.000 9.58012  ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? -16.73970 -13.09753 1.67051   1.000 10.03800 ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? -17.15457 -14.11498 1.10407   1.000 12.91602 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? -14.28892 -12.49134 1.86407   1.000 8.38695  ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? -13.78592 -13.23272 0.62972   1.000 13.18873 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? -12.96761 -14.35661 0.76132   1.000 12.07096 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? -14.06150 -12.76116 -0.65870  1.000 9.55756  ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? -12.47215 -14.99252 -0.35259  1.000 10.84702 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? -13.54619 -13.41651 -1.79981  1.000 10.47727 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? -12.74059 -14.52731 -1.62789  1.000 12.36843 ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? -17.34557 -11.91501 1.58113   1.000 9.62705  ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? -18.43885 -11.66916 0.63927   1.000 8.72965  ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? -17.89724 -11.13874 -0.68324  1.000 7.21648  ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? -16.91518 -10.40359 -0.70564  1.000 10.05441 ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? -19.44477 -10.67559 1.22368   1.000 12.52886 ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? -19.89015 -11.09458 2.51269   1.000 11.31153 ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? -18.54785 -11.51561 -1.77637  1.000 8.84968  ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? -18.21742 -11.04843 -3.11644  1.000 10.00865 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? -19.39161 -10.22704 -3.62845  1.000 11.09064 ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? -20.53628 -10.69153 -3.59955  1.000 10.80089 ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? -17.90947 -12.21017 -4.07237  1.000 7.97071  ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? -17.75370 -11.66985 -5.51558  1.000 11.77546 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? -16.66951 -13.03428 -3.62352  1.000 11.10995 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? -19.12301 -9.01077  -4.10740  1.000 10.83524 ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? -20.14234 -8.25933  -4.83808  1.000 10.06497 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? -19.82972 -8.42873  -6.32106  1.000 11.06721 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? -18.93623 -7.77295  -6.86091  1.000 11.62546 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? -20.18143 -6.78798  -4.41788  1.000 12.50984 ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? -21.21939 -5.90677  -5.11092  1.000 11.65878 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? -22.65748 -6.35942  -4.72268  1.000 11.82854 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? -20.97022 -4.43525  -4.75926  1.000 12.35355 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? -20.51364 -9.35416  -6.97110  1.000 9.58807  ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? -20.33471 -9.52993  -8.40741  1.000 12.69591 ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? -20.87306 -8.31606  -9.15118  1.000 14.76509 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? -21.99764 -7.87360  -8.88768  1.000 14.82518 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? -21.06298 -10.78042 -8.89636  1.000 13.74466 ? 116 ALA   A CB  1 
ATOM   907  N  N   . CYS   A 1 117 ? -20.09030 -7.80740  -10.11514 1.000 11.77622 ? 117 CYS   A N   1 
ATOM   908  C  CA  . CYS   A 1 117 ? -20.42322 -6.59392  -10.84829 1.000 15.27315 ? 117 CYS   A CA  1 
ATOM   909  C  C   . CYS   A 1 117 ? -20.16348 -6.79081  -12.33554 1.000 16.82438 ? 117 CYS   A C   1 
ATOM   910  O  O   . CYS   A 1 117 ? -19.30638 -7.58275  -12.73560 1.000 16.02857 ? 117 CYS   A O   1 
ATOM   911  C  CB  . CYS   A 1 117 ? -19.59741 -5.40053  -10.37869 1.000 17.95692 ? 117 CYS   A CB  1 
ATOM   912  S  SG  . CYS   A 1 117 ? -20.01224 -4.83725  -8.74941  1.000 20.80104 ? 117 CYS   A SG  1 
ATOM   913  N  N   . TYR   A 1 118 ? -20.91402 -6.04925  -13.14449 1.000 17.72982 ? 118 TYR   A N   1 
ATOM   914  C  CA  . TYR   A 1 118 ? -20.75357 -5.98204  -14.59275 1.000 19.31734 ? 118 TYR   A CA  1 
ATOM   915  C  C   . TYR   A 1 118 ? -20.96133 -4.54018  -15.02061 1.000 20.97093 ? 118 TYR   A C   1 
ATOM   916  O  O   . TYR   A 1 118 ? -21.92987 -3.90791  -14.58795 1.000 20.79151 ? 118 TYR   A O   1 
ATOM   917  C  CB  . TYR   A 1 118 ? -21.73849 -6.91851  -15.31298 1.000 19.58094 ? 118 TYR   A CB  1 
ATOM   918  C  CG  . TYR   A 1 118 ? -21.55264 -8.34609  -14.84750 1.000 19.51366 ? 118 TYR   A CG  1 
ATOM   919  C  CD1 . TYR   A 1 118 ? -22.27218 -8.84899  -13.76743 1.000 19.94747 ? 118 TYR   A CD1 1 
ATOM   920  C  CD2 . TYR   A 1 118 ? -20.58219 -9.16038  -15.42609 1.000 20.79943 ? 118 TYR   A CD2 1 
ATOM   921  C  CE1 . TYR   A 1 118 ? -22.06648 -10.13954 -13.30850 1.000 18.65714 ? 118 TYR   A CE1 1 
ATOM   922  C  CE2 . TYR   A 1 118 ? -20.38253 -10.45128 -14.98903 1.000 21.31672 ? 118 TYR   A CE2 1 
ATOM   923  C  CZ  . TYR   A 1 118 ? -21.12456 -10.93644 -13.92740 1.000 22.09480 ? 118 TYR   A CZ  1 
ATOM   924  O  OH  . TYR   A 1 118 ? -20.89783 -12.21473 -13.46258 1.000 20.66895 ? 118 TYR   A OH  1 
ATOM   925  N  N   . ASN   A 1 119 ? -20.02692 -4.01100  -15.82846 1.000 22.73895 ? 119 ASN   A N   1 
ATOM   926  C  CA  . ASN   A 1 119 ? -20.09805 -2.62880  -16.33614 1.000 20.53446 ? 119 ASN   A CA  1 
ATOM   927  C  C   . ASN   A 1 119 ? -20.20378 -1.61736  -15.19756 1.000 21.07623 ? 119 ASN   A C   1 
ATOM   928  O  O   . ASN   A 1 119 ? -20.88082 -0.59141  -15.32011 1.000 21.59582 ? 119 ASN   A O   1 
ATOM   929  C  CB  . ASN   A 1 119 ? -21.26401 -2.44498  -17.31240 1.000 25.05168 ? 119 ASN   A CB  1 
ATOM   930  C  CG  . ASN   A 1 119 ? -21.22236 -3.43045  -18.44968 1.000 26.05367 ? 119 ASN   A CG  1 
ATOM   931  O  OD1 . ASN   A 1 119 ? -20.29530 -3.41767  -19.26141 1.000 27.88133 ? 119 ASN   A OD1 1 
ATOM   932  N  ND2 . ASN   A 1 119 ? -22.22875 -4.30047  -18.51530 1.000 28.01879 ? 119 ASN   A ND2 1 
ATOM   933  N  N   . GLY   A 1 120 ? -19.53930 -1.91673  -14.07647 1.000 17.39548 ? 120 GLY   A N   1 
ATOM   934  C  CA  . GLY   A 1 120 ? -19.61158 -1.09342  -12.88579 1.000 18.18144 ? 120 GLY   A CA  1 
ATOM   935  C  C   . GLY   A 1 120 ? -20.91227 -1.18704  -12.11217 1.000 21.96539 ? 120 GLY   A C   1 
ATOM   936  O  O   . GLY   A 1 120 ? -21.08261 -0.45150  -11.13053 1.000 20.57855 ? 120 GLY   A O   1 
ATOM   937  N  N   . SER   A 1 121 ? -21.85229 -2.03962  -12.52949 1.000 21.99173 ? 121 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 121 ? -23.15624 -2.12072  -11.86815 1.000 20.90184 ? 121 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 121 ? -23.25534 -3.37413  -11.01768 1.000 23.34152 ? 121 SER   A C   1 
ATOM   940  O  O   . SER   A 1 121 ? -23.05059 -4.48690  -11.52920 1.000 20.60791 ? 121 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 121 ? -24.28784 -2.09363  -12.89287 1.000 25.48515 ? 121 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 121 ? -24.44377 -0.78541  -13.37838 1.000 29.24906 ? 121 SER   A OG  1 
ATOM   943  N  N   . PRO   A 1 122 ? -23.52483 -3.22430  -9.72215  1.000 21.92803 ? 122 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 122 ? -23.61826 -4.39052  -8.84167  1.000 21.57286 ? 122 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 122 ? -24.73878 -5.31775  -9.28963  1.000 20.94975 ? 122 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 122 ? -25.86761 -4.88651  -9.52874  1.000 22.53621 ? 122 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 122 ? -23.91367 -3.76633  -7.47803  1.000 21.21062 ? 122 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 122 ? -23.21346 -2.40231  -7.53993  1.000 21.43538 ? 122 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 122 ? -23.10336 -2.01620  -8.99433  1.000 22.00849 ? 122 PRO   A CD  1 
ATOM   950  N  N   . SER   A 1 123 ? -24.41711 -6.60252  -9.38973  1.000 20.56515 ? 123 SER   A N   1 
ATOM   951  C  CA  . SER   A 1 123 ? -25.35532 -7.64593  -9.80075  1.000 17.89494 ? 123 SER   A CA  1 
ATOM   952  C  C   . SER   A 1 123 ? -25.87597 -8.51831  -8.66408  1.000 17.10548 ? 123 SER   A C   1 
ATOM   953  O  O   . SER   A 1 123 ? -27.07157 -8.86002  -8.64519  1.000 17.99855 ? 123 SER   A O   1 
ATOM   954  C  CB  . SER   A 1 123 ? -24.68491 -8.54673  -10.84052 1.000 20.75145 ? 123 SER   A CB  1 
ATOM   955  O  OG  . SER   A 1 123 ? -25.61961 -9.43806  -11.40799 1.000 28.03761 ? 123 SER   A OG  1 
ATOM   956  N  N   . GLY   A 1 124 ? -25.01727 -8.92565  -7.73533  1.000 13.79152 ? 124 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? -25.43086 -9.80985  -6.66355  1.000 10.95195 ? 124 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? -24.30576 -10.01140 -5.67799  1.000 11.21568 ? 124 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? -23.13496 -9.75933  -5.98292  1.000 11.03530 ? 124 GLY   A O   1 
ATOM   960  N  N   . VAL   A 1 125 ? -24.67732 -10.43408 -4.47854  1.000 10.08587 ? 125 VAL   A N   1 
ATOM   961  C  CA  . VAL   A 1 125 ? -23.72036 -10.61984 -3.39984  1.000 10.97768 ? 125 VAL   A CA  1 
ATOM   962  C  C   . VAL   A 1 125 ? -23.82706 -12.04277 -2.87940  1.000 11.75997 ? 125 VAL   A C   1 
ATOM   963  O  O   . VAL   A 1 125 ? -24.93221 -12.59377 -2.75370  1.000 9.98771  ? 125 VAL   A O   1 
ATOM   964  C  CB  . VAL   A 1 125 ? -23.92417 -9.57528  -2.27913  1.000 12.54146 ? 125 VAL   A CB  1 
ATOM   965  C  CG1 . VAL   A 1 125 ? -25.23232 -9.77537  -1.62117  1.000 14.41447 ? 125 VAL   A CG1 1 
ATOM   966  C  CG2 . VAL   A 1 125 ? -22.79955 -9.67344  -1.26881  1.000 11.64672 ? 125 VAL   A CG2 1 
ATOM   967  N  N   . TYR   A 1 126 ? -22.67115 -12.63615 -2.57167  1.000 12.17966 ? 126 TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 126 ? -22.63405 -13.99350 -2.03047  1.000 13.30439 ? 126 TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 126 ? -21.35382 -14.20607 -1.21837  1.000 11.37105 ? 126 TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 126 ? -20.36895 -13.46290 -1.31359  1.000 10.50228 ? 126 TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 126 ? -22.73974 -15.05466 -3.13805  1.000 12.85194 ? 126 TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 126 ? -21.66914 -14.94816 -4.22249  1.000 13.23829 ? 126 TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 126 ? -20.40372 -15.53392 -4.06527  1.000 16.43768 ? 126 TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 126 ? -21.92248 -14.28253 -5.39942  1.000 13.76701 ? 126 TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 126 ? -19.43728 -15.42645 -5.06249  1.000 14.55446 ? 126 TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 126 ? -20.93213 -14.16082 -6.39789  1.000 14.07133 ? 126 TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 126 ? -19.72219 -14.74184 -6.22286  1.000 14.64970 ? 126 TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 126 ? -18.78672 -14.64399 -7.23152  1.000 19.66263 ? 126 TYR   A OH  1 
ATOM   979  N  N   . GLN   A 1 127 ? -21.35521 -15.28925 -0.45896  1.000 11.83366 ? 127 GLN   A N   1 
ATOM   980  C  CA  . GLN   A 1 127 ? -20.27111 -15.59041 0.45950   1.000 12.33773 ? 127 GLN   A CA  1 
ATOM   981  C  C   . GLN   A 1 127 ? -19.37939 -16.66558 -0.15936  1.000 13.94061 ? 127 GLN   A C   1 
ATOM   982  O  O   . GLN   A 1 127 ? -19.89756 -17.64609 -0.71629  1.000 16.23792 ? 127 GLN   A O   1 
ATOM   983  C  CB  . GLN   A 1 127 ? -20.89228 -16.00672 1.80202   1.000 14.87759 ? 127 GLN   A CB  1 
ATOM   984  C  CG  . GLN   A 1 127 ? -19.96893 -16.08732 2.92902   1.000 15.69347 ? 127 GLN   A CG  1 
ATOM   985  C  CD  . GLN   A 1 127 ? -19.64939 -14.73834 3.54523   1.000 14.78898 ? 127 GLN   A CD  1 
ATOM   986  O  OE1 . GLN   A 1 127 ? -19.93165 -13.68183 2.96361   1.000 14.78732 ? 127 GLN   A OE1 1 
ATOM   987  N  NE2 . GLN   A 1 127 ? -19.00857 -14.77080 4.69886   1.000 15.58372 ? 127 GLN   A NE2 1 
ATOM   988  N  N   . CYS   A 1 128 ? -18.05382 -16.42600 -0.15723  1.000 12.35124 ? 128 CYS   A N   1 
ATOM   989  C  CA  . CYS   A 1 128 ? -17.01649 -17.37757 -0.57769  1.000 13.55629 ? 128 CYS   A CA  1 
ATOM   990  C  C   . CYS   A 1 128 ? -16.02256 -17.67815 0.54150   1.000 13.65730 ? 128 CYS   A C   1 
ATOM   991  O  O   . CYS   A 1 128 ? -15.81512 -16.87037 1.44615   1.000 12.27273 ? 128 CYS   A O   1 
ATOM   992  C  CB  . CYS   A 1 128 ? -16.17251 -16.86919 -1.77165  1.000 12.99453 ? 128 CYS   A CB  1 
ATOM   993  S  SG  . CYS   A 1 128 ? -16.95955 -16.67495 -3.28920  1.000 26.15821 ? 128 CYS   A SG  1 
ATOM   994  N  N   . ALA   A 1 129 ? -15.33086 -18.82382 0.41565   1.000 11.52144 ? 129 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? -14.13188 -19.12148 1.19047   1.000 10.99040 ? 129 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? -12.91364 -19.16620 0.26191   1.000 13.73040 ? 129 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? -13.00354 -19.64961 -0.87289  1.000 11.77478 ? 129 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? -14.24018 -20.45951 1.93487   1.000 13.56531 ? 129 ALA   A CB  1 
ATOM   999  N  N   . MET   A 1 130 ? -11.76864 -18.69275 0.74958   1.000 10.96775 ? 130 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 130 ? -10.49289 -18.89294 0.05466   1.000 10.53528 ? 130 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 130 ? -10.12938 -20.36410 0.22402   1.000 11.62111 ? 130 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 130 ? -9.91599  -20.81902 1.35474   1.000 14.47508 ? 130 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 130 ? -9.41170  -17.98691 0.67160   1.000 9.76116  ? 130 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 130 ? -8.00331  -17.90003 0.03490   1.000 9.78724  ? 130 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 130 ? -7.94373  -17.70411 -1.72416  1.000 15.57567 ? 130 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 130 ? -8.49272  -16.02089 -1.85304  1.000 10.25449 ? 130 MET   A CE  1 
ATOM   1007 N  N   . ARG   A 1 131 ? -10.08886 -21.13781 -0.86901  1.000 11.08607 ? 131 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 131 ? -9.77857  -22.56652 -0.74869  1.000 11.92101 ? 131 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 131 ? -8.32417  -22.78974 -0.31546  1.000 13.50899 ? 131 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 131 ? -7.46932  -21.92011 -0.50513  1.000 10.07585 ? 131 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 131 ? -10.03871 -23.28021 -2.07762  1.000 11.83062 ? 131 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 131 ? -11.48393 -23.17371 -2.60562  1.000 14.31616 ? 131 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 131 ? -12.51211 -23.65739 -1.59970  1.000 13.40055 ? 131 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 131 ? -12.14783 -24.97169 -1.07389  1.000 11.43514 ? 131 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 131 ? -12.78560 -25.56156 -0.06761  1.000 16.38224 ? 131 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 131 ? -13.85291 -25.00494 0.49311   1.000 14.36931 ? 131 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 131 ? -12.34451 -26.74045 0.38289   1.000 15.92276 ? 131 ARG   A NH2 1 
ATOM   1018 N  N   . PRO   A 1 132 ? -8.00965  -23.94555 0.28608   1.000 12.02397 ? 132 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 132 ? -6.59087  -24.24514 0.55617   1.000 12.62704 ? 132 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 132 ? -5.68282  -24.11414 -0.65363  1.000 14.29348 ? 132 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 132 ? -4.50507  -23.79570 -0.47220  1.000 12.84909 ? 132 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 132 ? -6.62974  -25.69550 1.07991   1.000 18.23820 ? 132 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 132 ? -7.95117  -25.74616 1.79579   1.000 17.57650 ? 132 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 132 ? -8.89479  -24.97072 0.89163   1.000 15.46707 ? 132 PRO   A CD  1 
ATOM   1025 N  N   . ASN   A 1 133 ? -6.15823  -24.35966 -1.88323  1.000 13.29475 ? 133 ASN   A N   1 
ATOM   1026 C  CA  . ASN   A 1 133 ? -5.29796  -24.19111 -3.05155  1.000 11.50497 ? 133 ASN   A CA  1 
ATOM   1027 C  C   . ASN   A 1 133 ? -5.32625  -22.77563 -3.61605  1.000 13.79827 ? 133 ASN   A C   1 
ATOM   1028 O  O   . ASN   A 1 133 ? -4.89348  -22.56378 -4.76341  1.000 13.15848 ? 133 ASN   A O   1 
ATOM   1029 C  CB  . ASN   A 1 133 ? -5.65327  -25.19498 -4.14754  1.000 15.34908 ? 133 ASN   A CB  1 
ATOM   1030 C  CG  . ASN   A 1 133 ? -7.05567  -25.00279 -4.67653  1.000 12.11412 ? 133 ASN   A CG  1 
ATOM   1031 O  OD1 . ASN   A 1 133 ? -7.76003  -24.06865 -4.28531  1.000 11.70699 ? 133 ASN   A OD1 1 
ATOM   1032 N  ND2 . ASN   A 1 133 ? -7.47351  -25.89641 -5.56001  1.000 14.81461 ? 133 ASN   A ND2 1 
ATOM   1033 N  N   . PHE   A 1 134 ? -5.83171  -21.81901 -2.84109  1.000 10.35585 ? 134 PHE   A N   1 
ATOM   1034 C  CA  . PHE   A 1 134 ? -5.86889  -20.39281 -3.17566  1.000 12.45973 ? 134 PHE   A CA  1 
ATOM   1035 C  C   . PHE   A 1 134 ? -6.77885  -20.07988 -4.35132  1.000 10.87738 ? 134 PHE   A C   1 
ATOM   1036 O  O   . PHE   A 1 134 ? -6.59357  -19.05516 -5.01810  1.000 15.45978 ? 134 PHE   A O   1 
ATOM   1037 C  CB  . PHE   A 1 134 ? -4.47322  -19.82792 -3.47242  1.000 10.81360 ? 134 PHE   A CB  1 
ATOM   1038 C  CG  . PHE   A 1 134 ? -3.65093  -19.62514 -2.25176  1.000 10.75932 ? 134 PHE   A CG  1 
ATOM   1039 C  CD1 . PHE   A 1 134 ? -3.82919  -18.52264 -1.44348  1.000 10.00401 ? 134 PHE   A CD1 1 
ATOM   1040 C  CD2 . PHE   A 1 134 ? -2.67131  -20.53975 -1.92341  1.000 13.56430 ? 134 PHE   A CD2 1 
ATOM   1041 C  CE1 . PHE   A 1 134 ? -3.04734  -18.34094 -0.30340  1.000 10.86087 ? 134 PHE   A CE1 1 
ATOM   1042 C  CE2 . PHE   A 1 134 ? -1.87992  -20.37728 -0.78394  1.000 19.51852 ? 134 PHE   A CE2 1 
ATOM   1043 C  CZ  . PHE   A 1 134 ? -2.06411  -19.27984 0.02862   1.000 13.11613 ? 134 PHE   A CZ  1 
ATOM   1044 N  N   . THR   A 1 135 ? -7.73239  -20.94167 -4.66729  1.000 10.93384 ? 135 THR   A N   1 
ATOM   1045 C  CA  . THR   A 1 135 ? -8.79792  -20.57018 -5.59175  1.000 11.13291 ? 135 THR   A CA  1 
ATOM   1046 C  C   . THR   A 1 135 ? -10.03743 -20.24659 -4.77797  1.000 10.83433 ? 135 THR   A C   1 
ATOM   1047 O  O   . THR   A 1 135 ? -10.11237 -20.54464 -3.58525  1.000 7.88298  ? 135 THR   A O   1 
ATOM   1048 C  CB  . THR   A 1 135 ? -9.08805  -21.69620 -6.59606  1.000 12.04722 ? 135 THR   A CB  1 
ATOM   1049 O  OG1 . THR   A 1 135 ? -9.55334  -22.86320 -5.89648  1.000 10.88425 ? 135 THR   A OG1 1 
ATOM   1050 C  CG2 . THR   A 1 135 ? -7.83208  -22.05315 -7.37519  1.000 12.96987 ? 135 THR   A CG2 1 
ATOM   1051 N  N   . ILE   A 1 136 ? -11.01129 -19.63097 -5.43702  1.000 8.79227  ? 136 ILE   A N   1 
ATOM   1052 C  CA  . ILE   A 1 136 ? -12.33969 -19.49367 -4.85673  1.000 13.13462 ? 136 ILE   A CA  1 
ATOM   1053 C  C   . ILE   A 1 136 ? -13.36967 -20.10372 -5.80709  1.000 13.14342 ? 136 ILE   A C   1 
ATOM   1054 O  O   . ILE   A 1 136 ? -13.21971 -20.08434 -7.03064  1.000 11.73208 ? 136 ILE   A O   1 
ATOM   1055 C  CB  . ILE   A 1 136 ? -12.69038 -18.02838 -4.50097  1.000 14.91005 ? 136 ILE   A CB  1 
ATOM   1056 C  CG1 . ILE   A 1 136 ? -12.89319 -17.18832 -5.75595  1.000 13.68124 ? 136 ILE   A CG1 1 
ATOM   1057 C  CG2 . ILE   A 1 136 ? -11.64206 -17.36858 -3.55406  1.000 9.69765  ? 136 ILE   A CG2 1 
ATOM   1058 C  CD1 . ILE   A 1 136 ? -13.60850 -15.88432 -5.50562  1.000 12.52420 ? 136 ILE   A CD1 1 
ATOM   1059 N  N   . LYS   A 1 137 ? -14.38606 -20.73583 -5.22760  1.000 12.24060 ? 137 LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 137 ? -15.45768 -21.33120 -6.02310  1.000 15.69112 ? 137 LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 137 ? -16.55570 -20.28122 -6.12029  1.000 12.43292 ? 137 LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 137 ? -17.51945 -20.27826 -5.35622  1.000 15.86035 ? 137 LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 137 ? -15.95478 -22.62657 -5.39151  1.000 16.45790 ? 137 LYS   A CB  1 
ATOM   1064 C  CG  . LYS   A 1 137 ? -14.92177 -23.73350 -5.36045  1.000 18.96911 ? 137 LYS   A CG  1 
ATOM   1065 C  CD  . LYS   A 1 137 ? -15.39636 -24.93960 -4.55645  1.000 21.09857 ? 137 LYS   A CD  1 
ATOM   1066 C  CE  . LYS   A 1 137 ? -14.41179 -26.12532 -4.70795  1.000 26.25241 ? 137 LYS   A CE  1 
ATOM   1067 N  NZ  . LYS   A 1 137 ? -14.55099 -26.86615 -6.00818  1.000 28.60354 ? 137 LYS   A NZ  1 
ATOM   1068 N  N   . GLY   A 1 138 ? -16.37849 -19.35062 -7.06542  1.000 16.01386 ? 138 GLY   A N   1 
ATOM   1069 C  CA  . GLY   A 1 138 ? -17.25873 -18.21075 -7.19982  1.000 13.98557 ? 138 GLY   A CA  1 
ATOM   1070 C  C   . GLY   A 1 138 ? -18.35727 -18.40611 -8.23690  1.000 14.77101 ? 138 GLY   A C   1 
ATOM   1071 O  O   . GLY   A 1 138 ? -18.64425 -19.50976 -8.70889  1.000 16.18457 ? 138 GLY   A O   1 
ATOM   1072 N  N   . SER   A 1 139 ? -18.99554 -17.29022 -8.58625  1.000 12.22536 ? 139 SER   A N   1 
ATOM   1073 C  CA  . SER   A 1 139 ? -19.94642 -17.25856 -9.69243  1.000 13.35681 ? 139 SER   A CA  1 
ATOM   1074 C  C   . SER   A 1 139 ? -19.67812 -15.97034 -10.45913 1.000 14.93322 ? 139 SER   A C   1 
ATOM   1075 O  O   . SER   A 1 139 ? -19.97271 -14.86665 -9.98192  1.000 13.79079 ? 139 SER   A O   1 
ATOM   1076 C  CB  . SER   A 1 139 ? -21.40206 -17.35818 -9.21441  1.000 15.95656 ? 139 SER   A CB  1 
ATOM   1077 O  OG  . SER   A 1 139 ? -22.30207 -17.10949 -10.28291 1.000 15.54833 ? 139 SER   A OG  1 
ATOM   1078 N  N   . PHE   A 1 140 ? -19.06311 -16.11491 -11.62543 1.000 16.47313 ? 140 PHE   A N   1 
ATOM   1079 C  CA  . PHE   A 1 140 ? -18.50741 -15.00245 -12.38197 1.000 15.09303 ? 140 PHE   A CA  1 
ATOM   1080 C  C   . PHE   A 1 140 ? -18.70034 -15.27724 -13.86583 1.000 21.29176 ? 140 PHE   A C   1 
ATOM   1081 O  O   . PHE   A 1 140 ? -18.40844 -16.38035 -14.33381 1.000 22.72035 ? 140 PHE   A O   1 
ATOM   1082 C  CB  . PHE   A 1 140 ? -17.00571 -14.82477 -12.08074 1.000 16.93817 ? 140 PHE   A CB  1 
ATOM   1083 C  CG  . PHE   A 1 140 ? -16.69107 -14.27212 -10.71254 1.000 14.94760 ? 140 PHE   A CG  1 
ATOM   1084 C  CD1 . PHE   A 1 140 ? -17.15878 -13.03599 -10.31900 1.000 15.06103 ? 140 PHE   A CD1 1 
ATOM   1085 C  CD2 . PHE   A 1 140 ? -15.89708 -14.98170 -9.81752  1.000 16.80277 ? 140 PHE   A CD2 1 
ATOM   1086 C  CE1 . PHE   A 1 140 ? -16.84357 -12.50442 -9.08133  1.000 13.42883 ? 140 PHE   A CE1 1 
ATOM   1087 C  CE2 . PHE   A 1 140 ? -15.57517 -14.43970 -8.54598  1.000 15.05905 ? 140 PHE   A CE2 1 
ATOM   1088 C  CZ  . PHE   A 1 140 ? -16.05975 -13.19745 -8.19059  1.000 11.64073 ? 140 PHE   A CZ  1 
ATOM   1089 N  N   . LEU   A 1 141 ? -19.18903 -14.28903 -14.60347 1.000 19.21849 ? 141 LEU   A N   1 
ATOM   1090 C  CA  . LEU   A 1 141 ? -19.26012 -14.37233 -16.05757 1.000 23.03170 ? 141 LEU   A CA  1 
ATOM   1091 C  C   . LEU   A 1 141 ? -18.34122 -13.31910 -16.66811 1.000 23.31803 ? 141 LEU   A C   1 
ATOM   1092 O  O   . LEU   A 1 141 ? -17.72677 -12.52395 -15.96415 1.000 21.99704 ? 141 LEU   A O   1 
ATOM   1093 C  CB  . LEU   A 1 141 ? -20.70392 -14.20691 -16.54703 1.000 21.73361 ? 141 LEU   A CB  1 
ATOM   1094 C  CG  . LEU   A 1 141 ? -21.73587 -15.14547 -15.91558 1.000 26.07267 ? 141 LEU   A CG  1 
ATOM   1095 C  CD1 . LEU   A 1 141 ? -23.10098 -14.57080 -16.11380 1.000 27.04159 ? 141 LEU   A CD1 1 
ATOM   1096 C  CD2 . LEU   A 1 141 ? -21.69327 -16.52661 -16.54074 1.000 26.01351 ? 141 LEU   A CD2 1 
ATOM   1097 N  N   . ASN   A 1 142 ? -18.23805 -13.33589 -17.99596 1.000 24.52233 ? 142 ASN   A N   1 
ATOM   1098 C  CA  . ASN   A 1 142 ? -17.43932 -12.33911 -18.69267 1.000 24.55319 ? 142 ASN   A CA  1 
ATOM   1099 C  C   . ASN   A 1 142 ? -17.83731 -10.94112 -18.24115 1.000 24.38272 ? 142 ASN   A C   1 
ATOM   1100 O  O   . ASN   A 1 142 ? -19.02748 -10.61891 -18.13934 1.000 23.50317 ? 142 ASN   A O   1 
ATOM   1101 C  CB  . ASN   A 1 142 ? -17.61688 -12.47539 -20.20440 1.000 27.20474 ? 142 ASN   A CB  1 
ATOM   1102 C  CG  . ASN   A 1 142 ? -16.81088 -13.62159 -20.78879 1.000 32.22464 ? 142 ASN   A CG  1 
ATOM   1103 O  OD1 . ASN   A 1 142 ? -15.70879 -13.92142 -20.32271 1.000 34.54882 ? 142 ASN   A OD1 1 
ATOM   1104 N  ND2 . ASN   A 1 142 ? -17.36302 -14.27766 -21.81764 1.000 33.52318 ? 142 ASN   A ND2 1 
ATOM   1105 N  N   . GLY   A 1 143 ? -16.83109 -10.12133 -17.96017 1.000 18.70832 ? 143 GLY   A N   1 
ATOM   1106 C  CA  . GLY   A 1 143 ? -17.04636 -8.76419  -17.51871 1.000 21.20874 ? 143 GLY   A CA  1 
ATOM   1107 C  C   . GLY   A 1 143 ? -17.07137 -8.57993  -16.02161 1.000 18.34430 ? 143 GLY   A C   1 
ATOM   1108 O  O   . GLY   A 1 143 ? -17.23299 -7.44617  -15.55908 1.000 18.07322 ? 143 GLY   A O   1 
ATOM   1109 N  N   . SER   A 1 144 ? -16.94011 -9.65852  -15.24948 1.000 19.44441 ? 144 SER   A N   1 
ATOM   1110 C  CA  . SER   A 1 144 ? -16.90344 -9.56242  -13.80053 1.000 18.50286 ? 144 SER   A CA  1 
ATOM   1111 C  C   . SER   A 1 144 ? -15.53171 -9.15871  -13.27390 1.000 15.78955 ? 144 SER   A C   1 
ATOM   1112 O  O   . SER   A 1 144 ? -15.41594 -8.85910  -12.08259 1.000 13.31426 ? 144 SER   A O   1 
ATOM   1113 C  CB  . SER   A 1 144 ? -17.32703 -10.90209 -13.17834 1.000 16.31695 ? 144 SER   A CB  1 
ATOM   1114 O  OG  . SER   A 1 144 ? -16.45586 -11.95358 -13.58834 1.000 17.72082 ? 144 SER   A OG  1 
ATOM   1115 N  N   . CYS   A 1 145 ? -14.50474 -9.14132  -14.13098 1.000 15.53848 ? 145 CYS   A N   1 
ATOM   1116 C  CA  . CYS   A 1 145 ? -13.16964 -8.77086  -13.68629 1.000 18.67874 ? 145 CYS   A CA  1 
ATOM   1117 C  C   . CYS   A 1 145 ? -13.23804 -7.45042  -12.94771 1.000 14.18796 ? 145 CYS   A C   1 
ATOM   1118 O  O   . CYS   A 1 145 ? -13.96049 -6.53445  -13.35588 1.000 15.96134 ? 145 CYS   A O   1 
ATOM   1119 C  CB  . CYS   A 1 145 ? -12.20981 -8.64937  -14.87366 1.000 19.57730 ? 145 CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A 1 145 ? -11.88910 -10.21975 -15.69308 1.000 32.44153 ? 145 CYS   A SG  1 
ATOM   1121 N  N   . GLY   A 1 146 ? -12.51644 -7.38368  -11.82844 1.000 13.68226 ? 146 GLY   A N   1 
ATOM   1122 C  CA  . GLY   A 1 146 ? -12.50588 -6.21969  -10.98663 1.000 9.91574  ? 146 GLY   A CA  1 
ATOM   1123 C  C   . GLY   A 1 146 ? -13.51680 -6.22428  -9.87190  1.000 12.06770 ? 146 GLY   A C   1 
ATOM   1124 O  O   . GLY   A 1 146 ? -13.49369 -5.30173  -9.04292  1.000 12.87481 ? 146 GLY   A O   1 
ATOM   1125 N  N   . SER   A 1 147 ? -14.44352 -7.18903  -9.85701  1.000 10.35555 ? 147 SER   A N   1 
ATOM   1126 C  CA  . SER   A 1 147 ? -15.31136 -7.35289  -8.70372  1.000 12.23752 ? 147 SER   A CA  1 
ATOM   1127 C  C   . SER   A 1 147 ? -14.45433 -7.67198  -7.49339  1.000 9.54929  ? 147 SER   A C   1 
ATOM   1128 O  O   . SER   A 1 147 ? -13.40534 -8.32523  -7.60224  1.000 8.05572  ? 147 SER   A O   1 
ATOM   1129 C  CB  . SER   A 1 147 ? -16.32808 -8.47762  -8.91206  1.000 11.62610 ? 147 SER   A CB  1 
ATOM   1130 O  OG  . SER   A 1 147 ? -17.10704 -8.32530  -10.09796 1.000 12.04435 ? 147 SER   A OG  1 
ATOM   1131 N  N   . VAL   A 1 148 ? -14.91766 -7.23542  -6.32128  1.000 9.55149  ? 148 VAL   A N   1 
ATOM   1132 C  CA  . VAL   A 1 148 ? -14.09642 -7.36381  -5.13481  1.000 8.62349  ? 148 VAL   A CA  1 
ATOM   1133 C  C   . VAL   A 1 148 ? -14.78433 -8.24221  -4.09867  1.000 8.50332  ? 148 VAL   A C   1 
ATOM   1134 O  O   . VAL   A 1 148 ? -16.01627 -8.46261  -4.12083  1.000 8.66640  ? 148 VAL   A O   1 
ATOM   1135 C  CB  . VAL   A 1 148 ? -13.71783 -5.98843  -4.53469  1.000 8.88488  ? 148 VAL   A CB  1 
ATOM   1136 C  CG1 . VAL   A 1 148 ? -12.90731 -5.10320  -5.58084  1.000 9.47443  ? 148 VAL   A CG1 1 
ATOM   1137 C  CG2 . VAL   A 1 148 ? -14.91433 -5.27624  -4.02023  1.000 7.46139  ? 148 VAL   A CG2 1 
ATOM   1138 N  N   . GLY   A 1 149 ? -13.93529 -8.82749  -3.23949  1.000 6.80905  ? 149 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 149 ? -14.36940 -9.52900  -2.04173  1.000 6.57216  ? 149 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 149 ? -13.95370 -8.74224  -0.81109  1.000 7.80684  ? 149 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 149 ? -12.92941 -8.05167  -0.81728  1.000 6.23277  ? 149 GLY   A O   1 
ATOM   1142 N  N   . PHE   A 1 150 ? -14.73122 -8.87711  0.27019   1.000 7.33617  ? 150 PHE   A N   1 
ATOM   1143 C  CA  . PHE   A 1 150 ? -14.56976 -7.98122  1.41233   1.000 8.38649  ? 150 PHE   A CA  1 
ATOM   1144 C  C   . PHE   A 1 150 ? -15.24196 -8.57656  2.64272   1.000 10.04322 ? 150 PHE   A C   1 
ATOM   1145 O  O   . PHE   A 1 150 ? -16.13094 -9.42353  2.54290   1.000 8.38279  ? 150 PHE   A O   1 
ATOM   1146 C  CB  . PHE   A 1 150 ? -15.18244 -6.60642  1.13321   1.000 9.42747  ? 150 PHE   A CB  1 
ATOM   1147 C  CG  . PHE   A 1 150 ? -16.63820 -6.65433  0.89580   1.000 11.39655 ? 150 PHE   A CG  1 
ATOM   1148 C  CD1 . PHE   A 1 150 ? -17.13390 -6.92004  -0.38549  1.000 10.28590 ? 150 PHE   A CD1 1 
ATOM   1149 C  CD2 . PHE   A 1 150 ? -17.53714 -6.48215  1.94849   1.000 12.03936 ? 150 PHE   A CD2 1 
ATOM   1150 C  CE1 . PHE   A 1 150 ? -18.49313 -7.01209  -0.61847  1.000 10.97873 ? 150 PHE   A CE1 1 
ATOM   1151 C  CE2 . PHE   A 1 150 ? -18.91444 -6.56685  1.72592   1.000 12.02792 ? 150 PHE   A CE2 1 
ATOM   1152 C  CZ  . PHE   A 1 150 ? -19.39753 -6.82621  0.43525   1.000 13.56708 ? 150 PHE   A CZ  1 
ATOM   1153 N  N   . ASN   A 1 151 ? -14.82603 -8.07863  3.80300   1.000 12.43163 ? 151 ASN   A N   1 
ATOM   1154 C  CA  . ASN   A 1 151 ? -15.49331 -8.31835  5.07340   1.000 13.86360 ? 151 ASN   A CA  1 
ATOM   1155 C  C   . ASN   A 1 151 ? -15.79683 -6.96995  5.69625   1.000 12.12086 ? 151 ASN   A C   1 
ATOM   1156 O  O   . ASN   A 1 151 ? -15.22435 -5.95451  5.31710   1.000 11.89179 ? 151 ASN   A O   1 
ATOM   1157 C  CB  . ASN   A 1 151 ? -14.63260 -9.15263  6.02966   1.000 14.50525 ? 151 ASN   A CB  1 
ATOM   1158 C  CG  . ASN   A 1 151 ? -14.52002 -10.59606 5.60130   1.000 13.95459 ? 151 ASN   A CG  1 
ATOM   1159 O  OD1 . ASN   A 1 151 ? -13.49733 -11.00748 5.04739   1.000 12.75594 ? 151 ASN   A OD1 1 
ATOM   1160 N  ND2 . ASN   A 1 151 ? -15.58115 -11.38639 5.85798   1.000 12.50089 ? 151 ASN   A ND2 1 
ATOM   1161 N  N   . ILE   A 1 152 ? -16.72242 -6.95407  6.65030   1.000 13.26373 ? 152 ILE   A N   1 
ATOM   1162 C  CA  . ILE   A 1 152 ? -17.09808 -5.72213  7.33031   1.000 16.93976 ? 152 ILE   A CA  1 
ATOM   1163 C  C   . ILE   A 1 152 ? -16.94588 -5.93228  8.82249   1.000 23.49861 ? 152 ILE   A C   1 
ATOM   1164 O  O   . ILE   A 1 152 ? -17.42043 -6.93515  9.36143   1.000 20.50415 ? 152 ILE   A O   1 
ATOM   1165 C  CB  . ILE   A 1 152 ? -18.53107 -5.26276  6.99512   1.000 19.51444 ? 152 ILE   A CB  1 
ATOM   1166 C  CG1 . ILE   A 1 152 ? -18.76783 -5.33631  5.48924   1.000 18.39568 ? 152 ILE   A CG1 1 
ATOM   1167 C  CG2 . ILE   A 1 152 ? -18.74558 -3.82727  7.47515   1.000 21.74199 ? 152 ILE   A CG2 1 
ATOM   1168 C  CD1 . ILE   A 1 152 ? -18.01152 -4.32055  4.72550   1.000 19.25596 ? 152 ILE   A CD1 1 
ATOM   1169 N  N   . ASP   A 1 153 ? -16.26223 -4.99102  9.46908   1.000 24.94382 ? 153 ASP   A N   1 
ATOM   1170 C  CA  . ASP   A 1 153 ? -15.95193 -4.98643  10.89513  1.000 30.78663 ? 153 ASP   A CA  1 
ATOM   1171 C  C   . ASP   A 1 153 ? -16.46398 -3.66030  11.43069  1.000 34.84015 ? 153 ASP   A C   1 
ATOM   1172 O  O   . ASP   A 1 153 ? -15.91587 -2.60277  11.09927  1.000 31.68351 ? 153 ASP   A O   1 
ATOM   1173 C  CB  . ASP   A 1 153 ? -14.44702 -5.12122  11.13410  1.000 32.72038 ? 153 ASP   A CB  1 
ATOM   1174 C  CG  . ASP   A 1 153 ? -14.11426 -5.99563  12.32060  1.000 41.10537 ? 153 ASP   A CG  1 
ATOM   1175 O  OD1 . ASP   A 1 153 ? -15.05316 -6.36359  13.07034  1.000 41.72470 ? 153 ASP   A OD1 1 
ATOM   1176 O  OD2 . ASP   A 1 153 ? -12.90388 -6.28559  12.51470  1.000 43.20547 ? 153 ASP   A OD2 1 
ATOM   1177 N  N   . TYR   A 1 154 ? -17.50037 -3.72475  12.25884  1.000 37.53745 ? 154 TYR   A N   1 
ATOM   1178 C  CA  . TYR   A 1 154 ? -18.32801 -2.57025  12.56293  1.000 42.51508 ? 154 TYR   A CA  1 
ATOM   1179 C  C   . TYR   A 1 154 ? -18.59339 -1.76290  11.29635  1.000 41.76174 ? 154 TYR   A C   1 
ATOM   1180 O  O   . TYR   A 1 154 ? -19.37610 -2.18628  10.43943  1.000 43.44534 ? 154 TYR   A O   1 
ATOM   1181 C  CB  . TYR   A 1 154 ? -17.69382 -1.70281  13.64659  1.000 44.64863 ? 154 TYR   A CB  1 
ATOM   1182 C  CG  . TYR   A 1 154 ? -18.70207 -0.72569  14.20846  1.000 51.98044 ? 154 TYR   A CG  1 
ATOM   1183 C  CD1 . TYR   A 1 154 ? -20.03956 -1.10136  14.35676  1.000 53.39080 ? 154 TYR   A CD1 1 
ATOM   1184 C  CD2 . TYR   A 1 154 ? -18.33277 0.55676   14.59728  1.000 52.56650 ? 154 TYR   A CD2 1 
ATOM   1185 C  CE1 . TYR   A 1 154 ? -20.98233 -0.22643  14.86601  1.000 57.14927 ? 154 TYR   A CE1 1 
ATOM   1186 C  CE2 . TYR   A 1 154 ? -19.27275 1.44454   15.11644  1.000 56.70710 ? 154 TYR   A CE2 1 
ATOM   1187 C  CZ  . TYR   A 1 154 ? -20.59571 1.04581   15.24886  1.000 60.25743 ? 154 TYR   A CZ  1 
ATOM   1188 O  OH  . TYR   A 1 154 ? -21.53351 1.92018   15.76115  1.000 59.48562 ? 154 TYR   A OH  1 
ATOM   1189 N  N   . ASP   A 1 155 ? -17.93153 -0.61857  11.14768  1.000 38.04803 ? 155 ASP   A N   1 
ATOM   1190 C  CA  . ASP   A 1 155 ? -18.17546 0.26860   10.01706  1.000 36.63705 ? 155 ASP   A CA  1 
ATOM   1191 C  C   . ASP   A 1 155 ? -17.05401 0.25649   8.98168   1.000 30.69145 ? 155 ASP   A C   1 
ATOM   1192 O  O   . ASP   A 1 155 ? -17.08312 1.07218   8.05367   1.000 26.29325 ? 155 ASP   A O   1 
ATOM   1193 C  CB  . ASP   A 1 155 ? -18.38226 1.69434   10.51753  1.000 40.43325 ? 155 ASP   A CB  1 
ATOM   1194 C  CG  . ASP   A 1 155 ? -17.21807 2.18213   11.34945  1.000 43.38949 ? 155 ASP   A CG  1 
ATOM   1195 O  OD1 . ASP   A 1 155 ? -16.38632 1.33647   11.75870  1.000 43.43650 ? 155 ASP   A OD1 1 
ATOM   1196 O  OD2 . ASP   A 1 155 ? -17.13166 3.40812   11.58248  1.000 47.19286 ? 155 ASP   A OD2 1 
ATOM   1197 N  N   . CYS   A 1 156 ? -16.06587 -0.62900  9.12140   1.000 26.55343 ? 156 CYS   A N   1 
ATOM   1198 C  CA  . CYS   A 1 156 ? -14.85734 -0.60042  8.30282   1.000 22.24126 ? 156 CYS   A CA  1 
ATOM   1199 C  C   . CYS   A 1 156 ? -14.86468 -1.76632  7.32788   1.000 19.16919 ? 156 CYS   A C   1 
ATOM   1200 O  O   . CYS   A 1 156 ? -15.07430 -2.91626  7.72917   1.000 14.89338 ? 156 CYS   A O   1 
ATOM   1201 C  CB  . CYS   A 1 156 ? -13.59805 -0.65799  9.16602   1.000 21.87572 ? 156 CYS   A CB  1 
ATOM   1202 S  SG  . CYS   A 1 156 ? -12.08206 -0.90830  8.19497   1.000 17.94124 ? 156 CYS   A SG  1 
ATOM   1203 N  N   . VAL   A 1 157 ? -14.65897 -1.46767  6.04741   1.000 15.52618 ? 157 VAL   A N   1 
ATOM   1204 C  CA  . VAL   A 1 157 ? -14.63574 -2.49536  5.01270   1.000 13.79584 ? 157 VAL   A CA  1 
ATOM   1205 C  C   . VAL   A 1 157 ? -13.20608 -2.97200  4.83207   1.000 14.20397 ? 157 VAL   A C   1 
ATOM   1206 O  O   . VAL   A 1 157 ? -12.34598 -2.18253  4.44608   1.000 10.92085 ? 157 VAL   A O   1 
ATOM   1207 C  CB  . VAL   A 1 157 ? -15.17723 -1.96287  3.68074   1.000 12.53072 ? 157 VAL   A CB  1 
ATOM   1208 C  CG1 . VAL   A 1 157 ? -15.17435 -3.11440  2.66514   1.000 11.92916 ? 157 VAL   A CG1 1 
ATOM   1209 C  CG2 . VAL   A 1 157 ? -16.56582 -1.34569  3.87223   1.000 15.24388 ? 157 VAL   A CG2 1 
ATOM   1210 N  N   . SER   A 1 158 ? -12.95825 -4.27103  5.04955   1.000 12.75405 ? 158 SER   A N   1 
ATOM   1211 C  CA  . SER   A 1 158 ? -11.63633 -4.85461  4.79187   1.000 14.56137 ? 158 SER   A CA  1 
ATOM   1212 C  C   . SER   A 1 158 ? -11.71407 -5.51268  3.42486   1.000 11.33971 ? 158 SER   A C   1 
ATOM   1213 O  O   . SER   A 1 158 ? -12.30269 -6.59465  3.28276   1.000 11.85651 ? 158 SER   A O   1 
ATOM   1214 C  CB  . SER   A 1 158 ? -11.23490 -5.86206  5.86693   1.000 12.79991 ? 158 SER   A CB  1 
ATOM   1215 O  OG  . SER   A 1 158 ? -10.88300 -5.19153  7.07581   1.000 15.42560 ? 158 SER   A OG  1 
ATOM   1216 N  N   . PHE   A 1 159 ? -11.15908 -4.84957  2.40374   1.000 9.18637  ? 159 PHE   A N   1 
ATOM   1217 C  CA  . PHE   A 1 159 ? -11.09892 -5.46757  1.08583   1.000 11.53600 ? 159 PHE   A CA  1 
ATOM   1218 C  C   . PHE   A 1 159 ? -9.99273  -6.52172  1.07832   1.000 9.53983  ? 159 PHE   A C   1 
ATOM   1219 O  O   . PHE   A 1 159 ? -8.86105  -6.23728  1.49322   1.000 10.75934 ? 159 PHE   A O   1 
ATOM   1220 C  CB  . PHE   A 1 159 ? -10.82204 -4.41845  0.01026   1.000 8.80623  ? 159 PHE   A CB  1 
ATOM   1221 C  CG  . PHE   A 1 159 ? -11.93969 -3.43370  -0.17250  1.000 8.93821  ? 159 PHE   A CG  1 
ATOM   1222 C  CD1 . PHE   A 1 159 ? -13.08551 -3.77100  -0.89435  1.000 9.34081  ? 159 PHE   A CD1 1 
ATOM   1223 C  CD2 . PHE   A 1 159 ? -11.84141 -2.17067  0.40312   1.000 12.39983 ? 159 PHE   A CD2 1 
ATOM   1224 C  CE1 . PHE   A 1 159 ? -14.11214 -2.87265  -1.05931  1.000 11.09133 ? 159 PHE   A CE1 1 
ATOM   1225 C  CE2 . PHE   A 1 159 ? -12.85699 -1.25754  0.26263   1.000 12.32953 ? 159 PHE   A CE2 1 
ATOM   1226 C  CZ  . PHE   A 1 159 ? -14.01176 -1.60746  -0.47366  1.000 13.74181 ? 159 PHE   A CZ  1 
ATOM   1227 N  N   . CYS   A 1 160 ? -10.29890 -7.70951  0.57810   1.000 10.42289 ? 160 CYS   A N   1 
ATOM   1228 C  CA  . CYS   A 1 160 ? -9.33446  -8.79709  0.53524   1.000 11.90882 ? 160 CYS   A CA  1 
ATOM   1229 C  C   . CYS   A 1 160 ? -9.19423  -9.45200  -0.82711  1.000 10.25079 ? 160 CYS   A C   1 
ATOM   1230 O  O   . CYS   A 1 160 ? -8.27954  -10.26776 -0.98935  1.000 8.99489  ? 160 CYS   A O   1 
ATOM   1231 C  CB  . CYS   A 1 160 ? -9.69000  -9.89793  1.55774   1.000 7.24041  ? 160 CYS   A CB  1 
ATOM   1232 S  SG  . CYS   A 1 160 ? -11.34868 -10.58357 1.29875   1.000 9.44762  ? 160 CYS   A SG  1 
ATOM   1233 N  N   . TYR   A 1 161 ? -10.00619 -9.08803  -1.82436  1.000 6.02853  ? 161 TYR   A N   1 
ATOM   1234 C  CA  . TYR   A 1 161 ? -9.94852  -9.83197  -3.07245  1.000 8.29401  ? 161 TYR   A CA  1 
ATOM   1235 C  C   . TYR   A 1 161 ? -10.37960 -8.96231  -4.22869  1.000 8.43325  ? 161 TYR   A C   1 
ATOM   1236 O  O   . TYR   A 1 161 ? -11.35364 -8.20355  -4.12042  1.000 7.23360  ? 161 TYR   A O   1 
ATOM   1237 C  CB  . TYR   A 1 161 ? -10.85533 -11.06373 -3.00663  1.000 7.00488  ? 161 TYR   A CB  1 
ATOM   1238 C  CG  . TYR   A 1 161 ? -10.90018 -11.90809 -4.28622  1.000 9.98565  ? 161 TYR   A CG  1 
ATOM   1239 C  CD1 . TYR   A 1 161 ? -9.87733  -12.78125 -4.56718  1.000 10.88066 ? 161 TYR   A CD1 1 
ATOM   1240 C  CD2 . TYR   A 1 161 ? -11.97903 -11.86896 -5.16198  1.000 5.77230  ? 161 TYR   A CD2 1 
ATOM   1241 C  CE1 . TYR   A 1 161 ? -9.89142  -13.55255 -5.69162  1.000 7.83659  ? 161 TYR   A CE1 1 
ATOM   1242 C  CE2 . TYR   A 1 161 ? -11.99398 -12.63110 -6.32356  1.000 6.56924  ? 161 TYR   A CE2 1 
ATOM   1243 C  CZ  . TYR   A 1 161 ? -10.93632 -13.49117 -6.56217  1.000 10.33569 ? 161 TYR   A CZ  1 
ATOM   1244 O  OH  . TYR   A 1 161 ? -10.91484 -14.30574 -7.68140  1.000 9.14589  ? 161 TYR   A OH  1 
ATOM   1245 N  N   . MET   A 1 162 ? -9.68569  -9.10249  -5.34777  1.000 7.43318  ? 162 MET   A N   1 
ATOM   1246 C  CA  . MET   A 1 162 ? -10.18969 -8.54412  -6.59126  1.000 8.15003  ? 162 MET   A CA  1 
ATOM   1247 C  C   . MET   A 1 162 ? -10.14768 -9.64665  -7.63122  1.000 7.88161  ? 162 MET   A C   1 
ATOM   1248 O  O   . MET   A 1 162 ? -9.13499  -10.33768 -7.74451  1.000 6.75226  ? 162 MET   A O   1 
ATOM   1249 C  CB  . MET   A 1 162 ? -9.38244  -7.30822  -7.01352  1.000 9.85041  ? 162 MET   A CB  1 
ATOM   1250 C  CG  . MET   A 1 162 ? -9.85650  -6.68383  -8.32727  1.000 9.44172  ? 162 MET   A CG  1 
ATOM   1251 S  SD  . MET   A 1 162 ? -9.05594  -5.11901  -8.81339  1.000 15.50442 ? 162 MET   A SD  1 
ATOM   1252 C  CE  . MET   A 1 162 ? -9.93581  -3.86912  -7.87081  1.000 16.78516 ? 162 MET   A CE  1 
ATOM   1253 N  N   . HIS   A 1 163 ? -11.24138 -9.80841  -8.37837  1.000 8.21826  ? 163 HIS   A N   1 
ATOM   1254 C  CA  . HIS   A 1 163 ? -11.34657 -10.91391 -9.32049  1.000 8.85447  ? 163 HIS   A CA  1 
ATOM   1255 C  C   . HIS   A 1 163 ? -10.58535 -10.65947 -10.61948 1.000 10.23021 ? 163 HIS   A C   1 
ATOM   1256 O  O   . HIS   A 1 163 ? -10.70423 -9.59617  -11.21821 1.000 11.22057 ? 163 HIS   A O   1 
ATOM   1257 C  CB  . HIS   A 1 163 ? -12.80475 -11.19776 -9.66306  1.000 10.88229 ? 163 HIS   A CB  1 
ATOM   1258 C  CG  . HIS   A 1 163 ? -12.95190 -12.41709 -10.50548 1.000 11.72290 ? 163 HIS   A CG  1 
ATOM   1259 N  ND1 . HIS   A 1 163 ? -12.33401 -13.60051 -10.16966 1.000 12.00269 ? 163 HIS   A ND1 1 
ATOM   1260 C  CD2 . HIS   A 1 163 ? -13.60686 -12.64560 -11.66444 1.000 13.67146 ? 163 HIS   A CD2 1 
ATOM   1261 C  CE1 . HIS   A 1 163 ? -12.60262 -14.50914 -11.08518 1.000 12.32050 ? 163 HIS   A CE1 1 
ATOM   1262 N  NE2 . HIS   A 1 163 ? -13.38383 -13.96009 -11.99541 1.000 14.00270 ? 163 HIS   A NE2 1 
ATOM   1263 N  N   . HIS   A 1 164 ? -9.85455  -11.67810 -11.08894 1.000 11.93707 ? 164 HIS   A N   1 
ATOM   1264 C  CA  . HIS   A 1 164 ? -9.08093  -11.53537 -12.32247 1.000 13.32247 ? 164 HIS   A CA  1 
ATOM   1265 C  C   . HIS   A 1 164 ? -9.46885  -12.52511 -13.40730 1.000 15.77075 ? 164 HIS   A C   1 
ATOM   1266 O  O   . HIS   A 1 164 ? -9.59187  -12.12635 -14.57183 1.000 16.94874 ? 164 HIS   A O   1 
ATOM   1267 C  CB  . HIS   A 1 164 ? -7.56028  -11.65818 -12.05682 1.000 11.06918 ? 164 HIS   A CB  1 
ATOM   1268 C  CG  . HIS   A 1 164 ? -6.95627  -10.43665 -11.42803 1.000 12.80144 ? 164 HIS   A CG  1 
ATOM   1269 N  ND1 . HIS   A 1 164 ? -6.05807  -9.62194  -12.08358 1.000 12.40585 ? 164 HIS   A ND1 1 
ATOM   1270 C  CD2 . HIS   A 1 164 ? -7.08456  -9.92427  -10.17854 1.000 9.47310  ? 164 HIS   A CD2 1 
ATOM   1271 C  CE1 . HIS   A 1 164 ? -5.70553  -8.62133  -11.29094 1.000 10.07526 ? 164 HIS   A CE1 1 
ATOM   1272 N  NE2 . HIS   A 1 164 ? -6.30969  -8.78596  -10.12391 1.000 11.65814 ? 164 HIS   A NE2 1 
ATOM   1273 N  N   . MET   A 1 165 ? -9.64673  -13.80754 -13.08817 1.000 14.96255 ? 165 MET   A N   1 
ATOM   1274 C  CA  . MET   A 1 165 ? -9.74015  -14.79364 -14.16392 1.000 18.81763 ? 165 MET   A CA  1 
ATOM   1275 C  C   . MET   A 1 165 ? -10.44740 -16.05353 -13.68904 1.000 13.64032 ? 165 MET   A C   1 
ATOM   1276 O  O   . MET   A 1 165 ? -10.54019 -16.32213 -12.49402 1.000 12.93929 ? 165 MET   A O   1 
ATOM   1277 C  CB  . MET   A 1 165 ? -8.35546  -15.17524 -14.68821 1.000 18.08236 ? 165 MET   A CB  1 
ATOM   1278 C  CG  . MET   A 1 165 ? -7.25278  -14.92780 -13.68036 1.000 20.25841 ? 165 MET   A CG  1 
ATOM   1279 S  SD  . MET   A 1 165 ? -5.73842  -15.70424 -14.23025 1.000 25.94431 ? 165 MET   A SD  1 
ATOM   1280 C  CE  . MET   A 1 165 ? -6.09341  -17.39941 -13.77901 1.000 23.51183 ? 165 MET   A CE  1 
ATOM   1281 N  N   . GLU   A 1 166 ? -10.91343 -16.84306 -14.65278 1.000 16.62262 ? 166 GLU   A N   1 
ATOM   1282 C  CA  . GLU   A 1 166 ? -11.44917 -18.16720 -14.37893 1.000 14.61860 ? 166 GLU   A CA  1 
ATOM   1283 C  C   . GLU   A 1 166 ? -10.45624 -19.20935 -14.87973 1.000 18.08866 ? 166 GLU   A C   1 
ATOM   1284 O  O   . GLU   A 1 166 ? -9.85015  -19.03422 -15.93877 1.000 19.49130 ? 166 GLU   A O   1 
ATOM   1285 C  CB  . GLU   A 1 166 ? -12.82360 -18.36750 -15.04001 1.000 16.63026 ? 166 GLU   A CB  1 
ATOM   1286 C  CG  . GLU   A 1 166 ? -13.38804 -19.77816 -14.84974 1.000 22.87110 ? 166 GLU   A CG  1 
ATOM   1287 C  CD  . GLU   A 1 166 ? -14.84957 -19.89008 -15.25432 1.000 23.21281 ? 166 GLU   A CD  1 
ATOM   1288 O  OE1 . GLU   A 1 166 ? -15.65267 -19.03484 -14.82316 1.000 23.05896 ? 166 GLU   A OE1 1 
ATOM   1289 O  OE2 . GLU   A 1 166 ? -15.17208 -20.80658 -16.04245 1.000 23.26151 ? 166 GLU   A OE2 1 
ATOM   1290 N  N   . LEU   A 1 167 ? -10.25925 -20.27473 -14.08710 1.000 17.25718 ? 167 LEU   A N   1 
ATOM   1291 C  CA  . LEU   A 1 167 ? -9.38792  -21.40137 -14.39729 1.000 18.37998 ? 167 LEU   A CA  1 
ATOM   1292 C  C   . LEU   A 1 167 ? -10.19831 -22.50954 -15.05872 1.000 21.12273 ? 167 LEU   A C   1 
ATOM   1293 O  O   . LEU   A 1 167 ? -11.43164 -22.50607 -14.98151 1.000 20.60275 ? 167 LEU   A O   1 
ATOM   1294 C  CB  . LEU   A 1 167 ? -8.72544  -21.90337 -13.11501 1.000 17.51796 ? 167 LEU   A CB  1 
ATOM   1295 C  CG  . LEU   A 1 167 ? -7.66771  -20.99264 -12.46522 1.000 17.54670 ? 167 LEU   A CG  1 
ATOM   1296 C  CD1 . LEU   A 1 167 ? -7.35760  -21.47335 -11.05961 1.000 14.58714 ? 167 LEU   A CD1 1 
ATOM   1297 C  CD2 . LEU   A 1 167 ? -6.41032  -21.00052 -13.29358 1.000 19.93547 ? 167 LEU   A CD2 1 
ATOM   1298 N  N   . PRO   A 1 168 ? -9.54022  -23.48289 -15.71469 1.000 22.19428 ? 168 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 168 ? -10.28153 -24.42097 -16.58392 1.000 23.06300 ? 168 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 168 ? -11.26211 -25.32336 -15.85054 1.000 22.99990 ? 168 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 168 ? -12.12310 -25.92641 -16.50817 1.000 25.70734 ? 168 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 168 ? -9.17020  -25.25204 -17.23317 1.000 22.20071 ? 168 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 168 ? -7.92043  -24.40349 -17.10617 1.000 25.44805 ? 168 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 168 ? -8.08250  -23.70035 -15.79725 1.000 22.48250 ? 168 PRO   A CD  1 
ATOM   1305 N  N   . THR   A 1 169 ? -11.13192 -25.49236 -14.53818 1.000 19.48021 ? 169 THR   A N   1 
ATOM   1306 C  CA  . THR   A 1 169 ? -12.11989 -26.25744 -13.78943 1.000 19.61059 ? 169 THR   A CA  1 
ATOM   1307 C  C   . THR   A 1 169 ? -13.34002 -25.42372 -13.41110 1.000 19.60607 ? 169 THR   A C   1 
ATOM   1308 O  O   . THR   A 1 169 ? -14.22865 -25.92747 -12.71942 1.000 19.77403 ? 169 THR   A O   1 
ATOM   1309 C  CB  . THR   A 1 169 ? -11.47776 -26.85596 -12.53011 1.000 21.55987 ? 169 THR   A CB  1 
ATOM   1310 O  OG1 . THR   A 1 169 ? -10.80744 -25.81999 -11.79446 1.000 21.10160 ? 169 THR   A OG1 1 
ATOM   1311 C  CG2 . THR   A 1 169 ? -10.47850 -27.94196 -12.89656 1.000 21.31505 ? 169 THR   A CG2 1 
ATOM   1312 N  N   . GLY   A 1 170 ? -13.41029 -24.17100 -13.84848 1.000 18.59168 ? 170 GLY   A N   1 
ATOM   1313 C  CA  . GLY   A 1 170 ? -14.50708 -23.31032 -13.48448 1.000 19.48653 ? 170 GLY   A CA  1 
ATOM   1314 C  C   . GLY   A 1 170 ? -14.35198 -22.58928 -12.16522 1.000 19.03609 ? 170 GLY   A C   1 
ATOM   1315 O  O   . GLY   A 1 170 ? -15.29370 -21.90255 -11.74788 1.000 19.81344 ? 170 GLY   A O   1 
ATOM   1316 N  N   . VAL   A 1 171 ? -13.21315 -22.73619 -11.47895 1.000 16.48052 ? 171 VAL   A N   1 
ATOM   1317 C  CA  . VAL   A 1 171 ? -12.95727 -21.97063 -10.26157 1.000 14.75921 ? 171 VAL   A CA  1 
ATOM   1318 C  C   . VAL   A 1 171 ? -12.20274 -20.69576 -10.61901 1.000 14.16404 ? 171 VAL   A C   1 
ATOM   1319 O  O   . VAL   A 1 171 ? -11.82061 -20.48902 -11.77602 1.000 13.55424 ? 171 VAL   A O   1 
ATOM   1320 C  CB  . VAL   A 1 171 ? -12.19085 -22.78768 -9.20227  1.000 15.52788 ? 171 VAL   A CB  1 
ATOM   1321 C  CG1 . VAL   A 1 171 ? -12.96114 -24.07943 -8.84025  1.000 17.23896 ? 171 VAL   A CG1 1 
ATOM   1322 C  CG2 . VAL   A 1 171 ? -10.76404 -23.10648 -9.66628  1.000 15.95599 ? 171 VAL   A CG2 1 
ATOM   1323 N  N   . HIS   A 1 172 ? -11.96886 -19.83740 -9.62633  1.000 13.99446 ? 172 HIS   A N   1 
ATOM   1324 C  CA  . HIS   A 1 172 ? -11.63747 -18.44496 -9.89044  1.000 11.10401 ? 172 HIS   A CA  1 
ATOM   1325 C  C   . HIS   A 1 172 ? -10.36900 -18.04277 -9.15297  1.000 13.16528 ? 172 HIS   A C   1 
ATOM   1326 O  O   . HIS   A 1 172 ? -10.03554 -18.59717 -8.10138  1.000 10.58884 ? 172 HIS   A O   1 
ATOM   1327 C  CB  . HIS   A 1 172 ? -12.83908 -17.55147 -9.52075  1.000 13.15739 ? 172 HIS   A CB  1 
ATOM   1328 C  CG  . HIS   A 1 172 ? -14.06892 -17.88909 -10.31328 1.000 13.36928 ? 172 HIS   A CG  1 
ATOM   1329 N  ND1 . HIS   A 1 172 ? -15.16212 -18.52372 -9.76717  1.000 12.66088 ? 172 HIS   A ND1 1 
ATOM   1330 C  CD2 . HIS   A 1 172 ? -14.33208 -17.76018 -11.63489 1.000 15.52556 ? 172 HIS   A CD2 1 
ATOM   1331 C  CE1 . HIS   A 1 172 ? -16.07070 -18.72116 -10.70888 1.000 16.65072 ? 172 HIS   A CE1 1 
ATOM   1332 N  NE2 . HIS   A 1 172 ? -15.59140 -18.26812 -11.85262 1.000 15.08260 ? 172 HIS   A NE2 1 
ATOM   1333 N  N   . ALA   A 1 173 ? -9.61884  -17.13294 -9.77329  1.000 11.02849 ? 173 ALA   A N   1 
ATOM   1334 C  CA  . ALA   A 1 173 ? -8.35308  -16.66463 -9.23215  1.000 9.76896  ? 173 ALA   A CA  1 
ATOM   1335 C  C   . ALA   A 1 173 ? -8.30715  -15.15175 -9.30916  1.000 9.57959  ? 173 ALA   A C   1 
ATOM   1336 O  O   . ALA   A 1 173 ? -8.85436  -14.55170 -10.23236 1.000 10.35751 ? 173 ALA   A O   1 
ATOM   1337 C  CB  . ALA   A 1 173 ? -7.17450  -17.26630 -9.98636  1.000 13.35197 ? 173 ALA   A CB  1 
ATOM   1338 N  N   . GLY   A 1 174 ? -7.61872  -14.55547 -8.33964  1.000 7.67362  ? 174 GLY   A N   1 
ATOM   1339 C  CA  . GLY   A 1 174 ? -7.56843  -13.12722 -8.16716  1.000 8.77324  ? 174 GLY   A CA  1 
ATOM   1340 C  C   . GLY   A 1 174 ? -6.43283  -12.72841 -7.25206  1.000 8.30067  ? 174 GLY   A C   1 
ATOM   1341 O  O   . GLY   A 1 174 ? -5.59739  -13.55047 -6.86053  1.000 6.97345  ? 174 GLY   A O   1 
ATOM   1342 N  N   . THR   A 1 175 ? -6.41540  -11.45087 -6.89724  1.000 7.18084  ? 175 THR   A N   1 
ATOM   1343 C  CA  . THR   A 1 175 ? -5.34781  -10.86665 -6.10512  1.000 6.84494  ? 175 THR   A CA  1 
ATOM   1344 C  C   . THR   A 1 175 ? -5.94166  -10.26519 -4.83910  1.000 6.50581  ? 175 THR   A C   1 
ATOM   1345 O  O   . THR   A 1 175 ? -7.16157  -10.06805 -4.73124  1.000 6.88880  ? 175 THR   A O   1 
ATOM   1346 C  CB  . THR   A 1 175 ? -4.59929  -9.77477  -6.90859  1.000 8.41329  ? 175 THR   A CB  1 
ATOM   1347 O  OG1 . THR   A 1 175 ? -5.49511  -8.68519  -7.20769  1.000 7.49605  ? 175 THR   A OG1 1 
ATOM   1348 C  CG2 . THR   A 1 175 ? -4.02200  -10.32354 -8.20297  1.000 8.14826  ? 175 THR   A CG2 1 
ATOM   1349 N  N   . ASP   A 1 176 ? -5.06276  -9.93326  -3.90085  1.000 7.61136  ? 176 ASP   A N   1 
ATOM   1350 C  CA  . ASP   A 1 176 ? -5.44571  -8.95480  -2.89463  1.000 7.58882  ? 176 ASP   A CA  1 
ATOM   1351 C  C   . ASP   A 1 176 ? -5.45397  -7.57367  -3.54813  1.000 7.97776  ? 176 ASP   A C   1 
ATOM   1352 O  O   . ASP   A 1 176 ? -5.15541  -7.42020  -4.73614  1.000 9.31119  ? 176 ASP   A O   1 
ATOM   1353 C  CB  . ASP   A 1 176 ? -4.52211  -9.04014  -1.67446  1.000 10.94332 ? 176 ASP   A CB  1 
ATOM   1354 C  CG  . ASP   A 1 176 ? -3.06566  -8.73893  -1.97289  1.000 10.46316 ? 176 ASP   A CG  1 
ATOM   1355 O  OD1 . ASP   A 1 176 ? -2.74461  -7.97087  -2.90734  1.000 8.17756  ? 176 ASP   A OD1 1 
ATOM   1356 O  OD2 . ASP   A 1 176 ? -2.18062  -9.25873  -1.22938  1.000 10.21266 ? 176 ASP   A OD2 1 
ATOM   1357 N  N   . LEU   A 1 177 ? -5.79567  -6.54666  -2.77133  1.000 9.02062  ? 177 LEU   A N   1 
ATOM   1358 C  CA  . LEU   A 1 177 ? -5.91305  -5.20617  -3.33496  1.000 10.95493 ? 177 LEU   A CA  1 
ATOM   1359 C  C   . LEU   A 1 177 ? -4.57286  -4.48172  -3.43888  1.000 14.21669 ? 177 LEU   A C   1 
ATOM   1360 O  O   . LEU   A 1 177 ? -4.54561  -3.30409  -3.84264  1.000 15.97430 ? 177 LEU   A O   1 
ATOM   1361 C  CB  . LEU   A 1 177 ? -6.91772  -4.38081  -2.51737  1.000 9.44850  ? 177 LEU   A CB  1 
ATOM   1362 C  CG  . LEU   A 1 177 ? -8.40616  -4.40247  -2.93163  1.000 11.36237 ? 177 LEU   A CG  1 
ATOM   1363 C  CD1 . LEU   A 1 177 ? -8.66787  -3.71185  -4.26701  1.000 9.81530  ? 177 LEU   A CD1 1 
ATOM   1364 C  CD2 . LEU   A 1 177 ? -8.92465  -5.84889  -2.99885  1.000 8.87336  ? 177 LEU   A CD2 1 
ATOM   1365 N  N   . GLU   A 1 178 ? -3.45534  -5.12224  -3.08117  1.000 11.02938 ? 178 GLU   A N   1 
ATOM   1366 C  CA  . GLU   A 1 178 ? -2.16148  -4.58982  -3.50523  1.000 13.52132 ? 178 GLU   A CA  1 
ATOM   1367 C  C   . GLU   A 1 178 ? -1.68517  -5.24314  -4.80027  1.000 10.76956 ? 178 GLU   A C   1 
ATOM   1368 O  O   . GLU   A 1 178 ? -0.54631  -4.99918  -5.22328  1.000 13.92000 ? 178 GLU   A O   1 
ATOM   1369 C  CB  . GLU   A 1 178 ? -1.10705  -4.72282  -2.38750  1.000 12.15682 ? 178 GLU   A CB  1 
ATOM   1370 C  CG  . GLU   A 1 178 ? -1.62151  -4.32662  -0.99427  1.000 11.26975 ? 178 GLU   A CG  1 
ATOM   1371 C  CD  . GLU   A 1 178 ? -1.52106  -2.83454  -0.70789  1.000 20.89586 ? 178 GLU   A CD  1 
ATOM   1372 O  OE1 . GLU   A 1 178 ? -1.72861  -2.41932  0.46691   1.000 24.68204 ? 178 GLU   A OE1 1 
ATOM   1373 O  OE2 . GLU   A 1 178 ? -1.17969  -2.09325  -1.62458  1.000 19.19175 ? 178 GLU   A OE2 1 
ATOM   1374 N  N   . GLY   A 1 179 ? -2.54574  -6.02564  -5.45328  1.000 10.12052 ? 179 GLY   A N   1 
ATOM   1375 C  CA  . GLY   A 1 179 ? -2.24594  -6.63696  -6.74223  1.000 9.52507  ? 179 GLY   A CA  1 
ATOM   1376 C  C   . GLY   A 1 179 ? -1.41659  -7.90580  -6.67899  1.000 9.86011  ? 179 GLY   A C   1 
ATOM   1377 O  O   . GLY   A 1 179 ? -0.87684  -8.33863  -7.69784  1.000 9.44205  ? 179 GLY   A O   1 
ATOM   1378 N  N   . ASN   A 1 180 ? -1.32545  -8.53521  -5.51796  1.000 9.09660  ? 180 ASN   A N   1 
ATOM   1379 C  CA  . ASN   A 1 180 ? -0.55420  -9.75717  -5.37182  1.000 9.16195  ? 180 ASN   A CA  1 
ATOM   1380 C  C   . ASN   A 1 180 ? -1.49634  -10.93405 -5.44706  1.000 8.23830  ? 180 ASN   A C   1 
ATOM   1381 O  O   . ASN   A 1 180 ? -2.43305  -11.02557 -4.66465  1.000 7.64186  ? 180 ASN   A O   1 
ATOM   1382 C  CB  . ASN   A 1 180 ? 0.22606   -9.74978  -4.05679  1.000 10.54967 ? 180 ASN   A CB  1 
ATOM   1383 C  CG  . ASN   A 1 180 ? 1.16739   -8.59923  -4.00128  1.000 11.37927 ? 180 ASN   A CG  1 
ATOM   1384 O  OD1 . ASN   A 1 180 ? 2.03076   -8.45475  -4.85573  1.000 12.45182 ? 180 ASN   A OD1 1 
ATOM   1385 N  ND2 . ASN   A 1 180 ? 0.94124   -7.69658  -3.04725  1.000 16.47312 ? 180 ASN   A ND2 1 
ATOM   1386 N  N   . PHE   A 1 181 ? -1.25779  -11.80856 -6.41694  1.000 8.46249  ? 181 PHE   A N   1 
ATOM   1387 C  CA  . PHE   A 1 181 ? -2.14916  -12.93360 -6.63234  1.000 8.75627  ? 181 PHE   A CA  1 
ATOM   1388 C  C   . PHE   A 1 181 ? -2.23169  -13.83287 -5.40916  1.000 8.33491  ? 181 PHE   A C   1 
ATOM   1389 O  O   . PHE   A 1 181 ? -1.24085  -14.06378 -4.71249  1.000 8.11095  ? 181 PHE   A O   1 
ATOM   1390 C  CB  . PHE   A 1 181 ? -1.66547  -13.74263 -7.81970  1.000 9.29056  ? 181 PHE   A CB  1 
ATOM   1391 C  CG  . PHE   A 1 181 ? -2.43495  -13.49160 -9.07634  1.000 13.51292 ? 181 PHE   A CG  1 
ATOM   1392 C  CD1 . PHE   A 1 181 ? -3.64457  -14.13927 -9.31108  1.000 12.41631 ? 181 PHE   A CD1 1 
ATOM   1393 C  CD2 . PHE   A 1 181 ? -1.98313  -12.54186 -9.98819  1.000 10.63252 ? 181 PHE   A CD2 1 
ATOM   1394 C  CE1 . PHE   A 1 181 ? -4.37490  -13.88738 -10.46819 1.000 10.15556 ? 181 PHE   A CE1 1 
ATOM   1395 C  CE2 . PHE   A 1 181 ? -2.68393  -12.28782 -11.15381 1.000 14.11553 ? 181 PHE   A CE2 1 
ATOM   1396 C  CZ  . PHE   A 1 181 ? -3.88218  -12.95291 -11.39244 1.000 14.16785 ? 181 PHE   A CZ  1 
ATOM   1397 N  N   . TYR   A 1 182 ? -3.43204  -14.35966 -5.16980  1.000 7.47078  ? 182 TYR   A N   1 
ATOM   1398 C  CA  . TYR   A 1 182 ? -3.60857  -15.51466 -4.30032  1.000 8.55466  ? 182 TYR   A CA  1 
ATOM   1399 C  C   . TYR   A 1 182 ? -3.19483  -16.77677 -5.06131  1.000 10.55280 ? 182 TYR   A C   1 
ATOM   1400 O  O   . TYR   A 1 182 ? -3.74657  -17.08163 -6.13095  1.000 9.45668  ? 182 TYR   A O   1 
ATOM   1401 C  CB  . TYR   A 1 182 ? -5.05647  -15.56566 -3.82863  1.000 6.48626  ? 182 TYR   A CB  1 
ATOM   1402 C  CG  . TYR   A 1 182 ? -5.40835  -14.53689 -2.78545  1.000 7.52717  ? 182 TYR   A CG  1 
ATOM   1403 C  CD1 . TYR   A 1 182 ? -5.11995  -14.75232 -1.44573  1.000 10.50902 ? 182 TYR   A CD1 1 
ATOM   1404 C  CD2 . TYR   A 1 182 ? -6.09770  -13.37841 -3.12939  1.000 6.05695  ? 182 TYR   A CD2 1 
ATOM   1405 C  CE1 . TYR   A 1 182 ? -5.47908  -13.82530 -0.47395  1.000 7.65156  ? 182 TYR   A CE1 1 
ATOM   1406 C  CE2 . TYR   A 1 182 ? -6.46553  -12.42925 -2.14969  1.000 6.38058  ? 182 TYR   A CE2 1 
ATOM   1407 C  CZ  . TYR   A 1 182 ? -6.14153  -12.66781 -0.83668  1.000 8.47559  ? 182 TYR   A CZ  1 
ATOM   1408 O  OH  . TYR   A 1 182 ? -6.50234  -11.77250 0.14413   1.000 6.43974  ? 182 TYR   A OH  1 
ATOM   1409 N  N   . GLY   A 1 183 ? -2.18781  -17.48183 -4.54396  1.000 8.46723  ? 183 GLY   A N   1 
ATOM   1410 C  CA  . GLY   A 1 183 ? -1.71189  -18.70212 -5.14990  1.000 11.33602 ? 183 GLY   A CA  1 
ATOM   1411 C  C   . GLY   A 1 183 ? -0.85512  -18.50945 -6.38427  1.000 12.32757 ? 183 GLY   A C   1 
ATOM   1412 O  O   . GLY   A 1 183 ? -0.52242  -17.39663 -6.79917  1.000 10.32167 ? 183 GLY   A O   1 
ATOM   1413 N  N   . PRO   A 1 184 ? -0.49616  -19.61883 -7.00420  1.000 12.43622 ? 184 PRO   A N   1 
ATOM   1414 C  CA  . PRO   A 1 184 ? 0.51116   -19.61571 -8.07882  1.000 13.65543 ? 184 PRO   A CA  1 
ATOM   1415 C  C   . PRO   A 1 184 ? -0.10876  -19.36390 -9.44936  1.000 14.80526 ? 184 PRO   A C   1 
ATOM   1416 O  O   . PRO   A 1 184 ? -0.02027  -20.19633 -10.36842 1.000 18.75174 ? 184 PRO   A O   1 
ATOM   1417 C  CB  . PRO   A 1 184 ? 1.09553   -21.02823 -7.97414  1.000 15.30969 ? 184 PRO   A CB  1 
ATOM   1418 C  CG  . PRO   A 1 184 ? -0.12660  -21.85921 -7.54184  1.000 15.64716 ? 184 PRO   A CG  1 
ATOM   1419 C  CD  . PRO   A 1 184 ? -0.97648  -20.97228 -6.67586  1.000 12.55361 ? 184 PRO   A CD  1 
ATOM   1420 N  N   . PHE   A 1 185 ? -0.74906  -18.21673 -9.59448  1.000 12.15475 ? 185 PHE   A N   1 
ATOM   1421 C  CA  . PHE   A 1 185 ? -1.43919  -17.86269 -10.82416 1.000 13.88498 ? 185 PHE   A CA  1 
ATOM   1422 C  C   . PHE   A 1 185 ? -0.90517  -16.52832 -11.33637 1.000 16.84007 ? 185 PHE   A C   1 
ATOM   1423 O  O   . PHE   A 1 185 ? -0.39641  -15.70104 -10.56690 1.000 15.65425 ? 185 PHE   A O   1 
ATOM   1424 C  CB  . PHE   A 1 185 ? -2.96852  -17.84026 -10.60742 1.000 14.24024 ? 185 PHE   A CB  1 
ATOM   1425 C  CG  . PHE   A 1 185 ? -3.49390  -19.08164 -9.92366  1.000 12.00682 ? 185 PHE   A CG  1 
ATOM   1426 C  CD1 . PHE   A 1 185 ? -3.41769  -20.31070 -10.55272 1.000 13.70891 ? 185 PHE   A CD1 1 
ATOM   1427 C  CD2 . PHE   A 1 185 ? -3.99818  -19.02634 -8.63918  1.000 13.06229 ? 185 PHE   A CD2 1 
ATOM   1428 C  CE1 . PHE   A 1 185 ? -3.88515  -21.46827 -9.92055  1.000 13.18507 ? 185 PHE   A CE1 1 
ATOM   1429 C  CE2 . PHE   A 1 185 ? -4.45166  -20.16850 -8.00105  1.000 12.83393 ? 185 PHE   A CE2 1 
ATOM   1430 C  CZ  . PHE   A 1 185 ? -4.39019  -21.40199 -8.65582  1.000 12.85034 ? 185 PHE   A CZ  1 
ATOM   1431 N  N   . VAL   A 1 186 ? -0.98328  -16.34751 -12.65006 1.000 14.30021 ? 186 VAL   A N   1 
ATOM   1432 C  CA  . VAL   A 1 186 ? -0.46639  -15.16468 -13.32189 1.000 19.50144 ? 186 VAL   A CA  1 
ATOM   1433 C  C   . VAL   A 1 186 ? -1.52642  -14.62346 -14.27304 1.000 18.27034 ? 186 VAL   A C   1 
ATOM   1434 O  O   . VAL   A 1 186 ? -2.35273  -15.37329 -14.80363 1.000 17.30489 ? 186 VAL   A O   1 
ATOM   1435 C  CB  . VAL   A 1 186 ? 0.84131   -15.48484 -14.07483 1.000 20.34342 ? 186 VAL   A CB  1 
ATOM   1436 C  CG1 . VAL   A 1 186 ? 1.93479   -15.83128 -13.07837 1.000 18.00036 ? 186 VAL   A CG1 1 
ATOM   1437 C  CG2 . VAL   A 1 186 ? 0.64460   -16.61330 -15.08751 1.000 19.24237 ? 186 VAL   A CG2 1 
ATOM   1438 N  N   . ASP   A 1 187 ? -1.49196  -13.30964 -14.50117 1.000 18.25231 ? 187 ASP   A N   1 
ATOM   1439 C  CA  . ASP   A 1 187 ? -2.43623  -12.67473 -15.42507 1.000 20.71326 ? 187 ASP   A CA  1 
ATOM   1440 C  C   . ASP   A 1 187 ? -1.88571  -12.70515 -16.85074 1.000 23.82448 ? 187 ASP   A C   1 
ATOM   1441 O  O   . ASP   A 1 187 ? -1.63267  -11.68585 -17.49382 1.000 22.20588 ? 187 ASP   A O   1 
ATOM   1442 C  CB  . ASP   A 1 187 ? -2.78836  -11.26175 -14.96164 1.000 17.07610 ? 187 ASP   A CB  1 
ATOM   1443 C  CG  . ASP   A 1 187 ? -1.57347  -10.40561 -14.63406 1.000 17.53786 ? 187 ASP   A CG  1 
ATOM   1444 O  OD1 . ASP   A 1 187 ? -0.42130  -10.90103 -14.64957 1.000 15.62661 ? 187 ASP   A OD1 1 
ATOM   1445 O  OD2 . ASP   A 1 187 ? -1.80602  -9.23014  -14.27740 1.000 15.38311 ? 187 ASP   A OD2 1 
ATOM   1446 N  N   . ARG   A 1 188 ? -1.69236  -13.94441 -17.30037 1.000 23.76451 ? 188 ARG   A N   1 
ATOM   1447 C  CA  . ARG   A 1 188 ? -1.32331  -14.33991 -18.65078 1.000 28.54430 ? 188 ARG   A CA  1 
ATOM   1448 C  C   . ARG   A 1 188 ? -2.14069  -15.55872 -19.02975 1.000 32.39327 ? 188 ARG   A C   1 
ATOM   1449 O  O   . ARG   A 1 188 ? -2.59000  -16.31425 -18.16432 1.000 29.35413 ? 188 ARG   A O   1 
ATOM   1450 C  CB  . ARG   A 1 188 ? 0.14463   -14.73018 -18.77629 1.000 30.53560 ? 188 ARG   A CB  1 
ATOM   1451 C  CG  . ARG   A 1 188 ? 1.03245   -13.62442 -19.11860 1.000 35.67684 ? 188 ARG   A CG  1 
ATOM   1452 C  CD  . ARG   A 1 188 ? 2.37104   -13.75827 -18.45901 1.000 35.61046 ? 188 ARG   A CD  1 
ATOM   1453 N  NE  . ARG   A 1 188 ? 2.85672   -15.12558 -18.38673 1.000 35.44759 ? 188 ARG   A NE  1 
ATOM   1454 C  CZ  . ARG   A 1 188 ? 3.46630   -15.61192 -17.31802 1.000 33.77394 ? 188 ARG   A CZ  1 
ATOM   1455 N  NH1 . ARG   A 1 188 ? 3.54065   -14.91623 -16.19411 1.000 32.50180 ? 188 ARG   A NH1 1 
ATOM   1456 N  NH2 . ARG   A 1 188 ? 4.00597   -16.82399 -17.37416 1.000 32.43187 ? 188 ARG   A NH2 1 
ATOM   1457 N  N   . GLN   A 1 189 ? -2.27832  -15.79000 -20.33442 1.000 35.10995 ? 189 GLN   A N   1 
ATOM   1458 C  CA  . GLN   A 1 189 ? -2.98360  -16.98757 -20.78343 1.000 36.94636 ? 189 GLN   A CA  1 
ATOM   1459 C  C   . GLN   A 1 189 ? -1.94291  -18.09527 -20.92122 1.000 34.55944 ? 189 GLN   A C   1 
ATOM   1460 O  O   . GLN   A 1 189 ? -1.22056  -18.18515 -21.91480 1.000 38.26363 ? 189 GLN   A O   1 
ATOM   1461 C  CB  . GLN   A 1 189 ? -3.74808  -16.73174 -22.07794 1.000 40.86176 ? 189 GLN   A CB  1 
ATOM   1462 C  CG  . GLN   A 1 189 ? -4.20556  -17.99715 -22.76714 1.000 40.91929 ? 189 GLN   A CG  1 
ATOM   1463 C  CD  . GLN   A 1 189 ? -5.33710  -18.65567 -21.99994 1.000 48.36273 ? 189 GLN   A CD  1 
ATOM   1464 O  OE1 . GLN   A 1 189 ? -5.26440  -19.83753 -21.65724 1.000 51.16819 ? 189 GLN   A OE1 1 
ATOM   1465 N  NE2 . GLN   A 1 189 ? -6.37681  -17.88049 -21.69296 1.000 48.80227 ? 189 GLN   A NE2 1 
ATOM   1466 N  N   . THR   A 1 190 ? -1.84324  -18.92242 -19.88236 1.000 33.18874 ? 190 THR   A N   1 
ATOM   1467 C  CA  . THR   A 1 190 ? -1.03708  -20.13673 -19.84501 1.000 33.13856 ? 190 THR   A CA  1 
ATOM   1468 C  C   . THR   A 1 190 ? -1.95265  -21.32302 -19.57039 1.000 30.78322 ? 190 THR   A C   1 
ATOM   1469 O  O   . THR   A 1 190 ? -3.16917  -21.18529 -19.45365 1.000 30.70566 ? 190 THR   A O   1 
ATOM   1470 C  CB  . THR   A 1 190 ? 0.05488   -20.06467 -18.76755 1.000 30.98155 ? 190 THR   A CB  1 
ATOM   1471 O  OG1 . THR   A 1 190 ? -0.53608  -20.22159 -17.47200 1.000 30.58978 ? 190 THR   A OG1 1 
ATOM   1472 C  CG2 . THR   A 1 190 ? 0.80030   -18.74013 -18.82603 1.000 31.47588 ? 190 THR   A CG2 1 
ATOM   1473 N  N   . ALA   A 1 191 ? -1.35862  -22.50364 -19.44347 1.000 31.48974 ? 191 ALA   A N   1 
ATOM   1474 C  CA  . ALA   A 1 191 ? -2.11960  -23.68909 -19.08052 1.000 29.54053 ? 191 ALA   A CA  1 
ATOM   1475 C  C   . ALA   A 1 191 ? -2.27195  -23.84970 -17.56720 1.000 29.56731 ? 191 ALA   A C   1 
ATOM   1476 O  O   . ALA   A 1 191 ? -2.47920  -24.97679 -17.09834 1.000 30.67567 ? 191 ALA   A O   1 
ATOM   1477 C  CB  . ALA   A 1 191 ? -1.47175  -24.93764 -19.69376 1.000 30.15977 ? 191 ALA   A CB  1 
ATOM   1478 N  N   . GLN   A 1 192 ? -2.18877  -22.75503 -16.79779 1.000 26.32200 ? 192 GLN   A N   1 
ATOM   1479 C  CA  . GLN   A 1 192 ? -2.28505  -22.85223 -15.34270 1.000 24.18114 ? 192 GLN   A CA  1 
ATOM   1480 C  C   . GLN   A 1 192 ? -3.55131  -23.59989 -14.93495 1.000 27.85455 ? 192 GLN   A C   1 
ATOM   1481 O  O   . GLN   A 1 192 ? -4.60401  -23.48085 -15.57504 1.000 27.72183 ? 192 GLN   A O   1 
ATOM   1482 C  CB  . GLN   A 1 192 ? -2.30635  -21.47277 -14.66789 1.000 25.64647 ? 192 GLN   A CB  1 
ATOM   1483 C  CG  . GLN   A 1 192 ? -2.91708  -20.34278 -15.46785 1.000 26.16282 ? 192 GLN   A CG  1 
ATOM   1484 C  CD  . GLN   A 1 192 ? -2.62110  -18.96482 -14.89472 1.000 22.01208 ? 192 GLN   A CD  1 
ATOM   1485 O  OE1 . GLN   A 1 192 ? -2.05172  -18.82185 -13.80379 1.000 21.70555 ? 192 GLN   A OE1 1 
ATOM   1486 N  NE2 . GLN   A 1 192 ? -3.00398  -17.93655 -15.63573 1.000 23.84735 ? 192 GLN   A NE2 1 
ATOM   1487 N  N   . ALA   A 1 193 ? -3.44765  -24.36317 -13.84628 1.000 24.78084 ? 193 ALA   A N   1 
ATOM   1488 C  CA  . ALA   A 1 193 ? -4.56602  -25.13021 -13.32023 1.000 23.01892 ? 193 ALA   A CA  1 
ATOM   1489 C  C   . ALA   A 1 193 ? -4.51612  -25.10898 -11.79797 1.000 22.94346 ? 193 ALA   A C   1 
ATOM   1490 O  O   . ALA   A 1 193 ? -3.46643  -24.87105 -11.19606 1.000 24.62860 ? 193 ALA   A O   1 
ATOM   1491 C  CB  . ALA   A 1 193 ? -4.56199  -26.57767 -13.82968 1.000 26.55709 ? 193 ALA   A CB  1 
ATOM   1492 N  N   . ALA   A 1 194 ? -5.66582  -25.41101 -11.18887 1.000 23.04995 ? 194 ALA   A N   1 
ATOM   1493 C  CA  . ALA   A 1 194 ? -5.85203  -25.21172 -9.75151  1.000 23.24687 ? 194 ALA   A CA  1 
ATOM   1494 C  C   . ALA   A 1 194 ? -4.85349  -26.02122 -8.92079  1.000 25.08811 ? 194 ALA   A C   1 
ATOM   1495 O  O   . ALA   A 1 194 ? -4.26712  -25.50737 -7.96354  1.000 28.27617 ? 194 ALA   A O   1 
ATOM   1496 C  CB  . ALA   A 1 194 ? -7.29229  -25.56259 -9.36486  1.000 19.16492 ? 194 ALA   A CB  1 
ATOM   1497 N  N   . GLY   A 1 195 ? -4.64925  -27.28613 -9.25052  1.000 26.79797 ? 195 GLY   A N   1 
ATOM   1498 C  CA  . GLY   A 1 195 ? -3.85242  -27.94164 -8.21052  1.000 25.48496 ? 195 GLY   A CA  1 
ATOM   1499 C  C   . GLY   A 1 195 ? -4.70580  -28.41486 -7.04590  1.000 26.19805 ? 195 GLY   A C   1 
ATOM   1500 O  O   . GLY   A 1 195 ? -5.76987  -27.87112 -6.75128  1.000 22.81073 ? 195 GLY   A O   1 
ATOM   1501 N  N   . THR   A 1 196 ? -4.22337  -29.45695 -6.36386  1.000 24.99468 ? 196 THR   A N   1 
ATOM   1502 C  CA  . THR   A 1 196 ? -5.09945  -30.24835 -5.50607  1.000 24.89727 ? 196 THR   A CA  1 
ATOM   1503 C  C   . THR   A 1 196 ? -5.56630  -29.44904 -4.29280  1.000 20.86836 ? 196 THR   A C   1 
ATOM   1504 O  O   . THR   A 1 196 ? -4.81570  -28.66120 -3.71079  1.000 20.49158 ? 196 THR   A O   1 
ATOM   1505 C  CB  . THR   A 1 196 ? -4.39878  -31.51610 -5.02961  1.000 24.99806 ? 196 THR   A CB  1 
ATOM   1506 O  OG1 . THR   A 1 196 ? -3.11444  -31.16993 -4.49357  1.000 29.32434 ? 196 THR   A OG1 1 
ATOM   1507 C  CG2 . THR   A 1 196 ? -4.18410  -32.48765 -6.21865  1.000 27.82238 ? 196 THR   A CG2 1 
ATOM   1508 N  N   . ASP   A 1 197 ? -6.81136  -29.67215 -3.91200  1.000 18.69837 ? 197 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 197 ? -7.44698  -29.00389 -2.78683  1.000 18.39703 ? 197 ASP   A CA  1 
ATOM   1510 C  C   . ASP   A 1 197 ? -7.66243  -29.99855 -1.65593  1.000 21.75073 ? 197 ASP   A C   1 
ATOM   1511 O  O   . ASP   A 1 197 ? -7.58336  -31.21181 -1.84197  1.000 22.11028 ? 197 ASP   A O   1 
ATOM   1512 C  CB  . ASP   A 1 197 ? -8.80618  -28.42813 -3.17455  1.000 17.21977 ? 197 ASP   A CB  1 
ATOM   1513 C  CG  . ASP   A 1 197 ? -9.17188  -27.21959 -2.35950  1.000 17.27283 ? 197 ASP   A CG  1 
ATOM   1514 O  OD1 . ASP   A 1 197 ? -10.33565 -26.78319 -2.47438  1.000 14.95315 ? 197 ASP   A OD1 1 
ATOM   1515 O  OD2 . ASP   A 1 197 ? -8.26588  -26.63539 -1.69844  1.000 15.83287 ? 197 ASP   A OD2 1 
ATOM   1516 N  N   . THR   A 1 198 ? -7.98310  -29.46446 -0.48485  1.000 19.21075 ? 198 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 198 ? -8.33763  -30.27269 0.67253   1.000 20.13854 ? 198 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 198 ? -9.56844  -29.65380 1.31185   1.000 17.04964 ? 198 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 198 ? -10.02659 -28.58843 0.89867   1.000 16.30702 ? 198 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 198 ? -7.19451  -30.35733 1.70225   1.000 21.60825 ? 198 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 198 ? -6.70838  -29.04449 1.99885   1.000 23.23699 ? 198 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 198 ? -6.04958  -31.15796 1.15741   1.000 26.31537 ? 198 THR   A CG2 1 
ATOM   1523 N  N   . THR   A 1 199 ? -10.12194 -30.33965 2.31324   1.000 16.77386 ? 199 THR   A N   1 
ATOM   1524 C  CA  . THR   A 1 199 ? -11.27057 -29.84200 3.06764   1.000 17.69149 ? 199 THR   A CA  1 
ATOM   1525 C  C   . THR   A 1 199 ? -10.81353 -29.12400 4.33041   1.000 16.71622 ? 199 THR   A C   1 
ATOM   1526 O  O   . THR   A 1 199 ? -9.90988  -29.58958 5.03063   1.000 15.01194 ? 199 THR   A O   1 
ATOM   1527 C  CB  . THR   A 1 199 ? -12.23112 -30.98795 3.41495   1.000 18.73511 ? 199 THR   A CB  1 
ATOM   1528 O  OG1 . THR   A 1 199 ? -12.75378 -31.55827 2.20996   1.000 20.29420 ? 199 THR   A OG1 1 
ATOM   1529 C  CG2 . THR   A 1 199 ? -13.35455 -30.52553 4.30704   1.000 17.61794 ? 199 THR   A CG2 1 
ATOM   1530 N  N   . ILE   A 1 200 ? -11.42215 -27.96947 4.59871   1.000 14.65184 ? 200 ILE   A N   1 
ATOM   1531 C  CA  . ILE   A 1 200 ? -11.06611 -27.14147 5.74475   1.000 13.27696 ? 200 ILE   A CA  1 
ATOM   1532 C  C   . ILE   A 1 200 ? -11.67701 -27.72650 7.02107   1.000 14.21109 ? 200 ILE   A C   1 
ATOM   1533 O  O   . ILE   A 1 200 ? -12.82476 -27.42671 7.37221   1.000 13.06734 ? 200 ILE   A O   1 
ATOM   1534 C  CB  . ILE   A 1 200 ? -11.49318 -25.67377 5.51708   1.000 13.67464 ? 200 ILE   A CB  1 
ATOM   1535 C  CG1 . ILE   A 1 200 ? -11.00796 -25.15610 4.15386   1.000 12.01128 ? 200 ILE   A CG1 1 
ATOM   1536 C  CG2 . ILE   A 1 200 ? -10.96060 -24.78852 6.62558   1.000 13.62613 ? 200 ILE   A CG2 1 
ATOM   1537 C  CD1 . ILE   A 1 200 ? -11.92173 -24.01858 3.58581   1.000 9.63789  ? 200 ILE   A CD1 1 
ATOM   1538 N  N   . THR   A 1 201 ? -10.88038 -28.55957 7.71596   1.000 15.13605 ? 201 THR   A N   1 
ATOM   1539 C  CA  . THR   A 1 201 ? -11.33796 -29.34322 8.87268   1.000 14.51458 ? 201 THR   A CA  1 
ATOM   1540 C  C   . THR   A 1 201 ? -11.93261 -28.47290 9.97177   1.000 14.47968 ? 201 THR   A C   1 
ATOM   1541 O  O   . THR   A 1 201 ? -12.99783 -28.79686 10.52047  1.000 12.48787 ? 201 THR   A O   1 
ATOM   1542 C  CB  . THR   A 1 201 ? -10.16883 -30.15500 9.42964   1.000 14.96351 ? 201 THR   A CB  1 
ATOM   1543 O  OG1 . THR   A 1 201 ? -9.59697  -30.94357 8.38089   1.000 15.39899 ? 201 THR   A OG1 1 
ATOM   1544 C  CG2 . THR   A 1 201 ? -10.59824 -31.06984 10.60306  1.000 16.41373 ? 201 THR   A CG2 1 
ATOM   1545 N  N   . VAL   A 1 202 ? -11.25448 -27.36844 10.32549  1.000 15.18910 ? 202 VAL   A N   1 
ATOM   1546 C  CA  . VAL   A 1 202 ? -11.74119 -26.59646 11.46013  1.000 14.43584 ? 202 VAL   A CA  1 
ATOM   1547 C  C   . VAL   A 1 202 ? -13.11523 -26.03153 11.13788  1.000 12.46454 ? 202 VAL   A C   1 
ATOM   1548 O  O   . VAL   A 1 202 ? -13.97900 -25.94050 12.01476  1.000 13.06949 ? 202 VAL   A O   1 
ATOM   1549 C  CB  . VAL   A 1 202 ? -10.74964 -25.48828 11.87300  1.000 13.61830 ? 202 VAL   A CB  1 
ATOM   1550 C  CG1 . VAL   A 1 202 ? -10.49183 -24.50194 10.72460  1.000 16.69139 ? 202 VAL   A CG1 1 
ATOM   1551 C  CG2 . VAL   A 1 202 ? -11.24402 -24.77841 13.15185  1.000 15.22747 ? 202 VAL   A CG2 1 
ATOM   1552 N  N   . ASN   A 1 203 ? -13.34371 -25.67125 9.87117   1.000 13.48945 ? 203 ASN   A N   1 
ATOM   1553 C  CA  . ASN   A 1 203 ? -14.62130 -25.10823 9.46482   1.000 11.24928 ? 203 ASN   A CA  1 
ATOM   1554 C  C   . ASN   A 1 203 ? -15.72828 -26.14893 9.53740   1.000 14.02685 ? 203 ASN   A C   1 
ATOM   1555 O  O   . ASN   A 1 203 ? -16.86062 -25.83747 9.93287   1.000 13.07331 ? 203 ASN   A O   1 
ATOM   1556 C  CB  . ASN   A 1 203 ? -14.51744 -24.55894 8.05147   1.000 13.25282 ? 203 ASN   A CB  1 
ATOM   1557 C  CG  . ASN   A 1 203 ? -13.75760 -23.24487 7.99121   1.000 12.93061 ? 203 ASN   A CG  1 
ATOM   1558 O  OD1 . ASN   A 1 203 ? -13.23245 -22.75753 9.00483   1.000 12.52571 ? 203 ASN   A OD1 1 
ATOM   1559 N  ND2 . ASN   A 1 203 ? -13.67622 -22.68663 6.80009   1.000 9.47615  ? 203 ASN   A ND2 1 
ATOM   1560 N  N   . VAL   A 1 204 ? -15.42744 -27.38149 9.13065   1.000 12.59630 ? 204 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 204 ? -16.42055 -28.44919 9.23955   1.000 12.89976 ? 204 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 204 ? -16.83397 -28.62984 10.68964  1.000 12.28071 ? 204 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 204 ? -18.01549 -28.82413 10.99051  1.000 12.65254 ? 204 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 204 ? -15.87581 -29.76042 8.65288   1.000 12.35128 ? 204 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 204 ? -16.88453 -30.89098 8.84811   1.000 13.22244 ? 204 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 204 ? -15.51347 -29.57154 7.18147   1.000 12.98618 ? 204 VAL   A CG2 1 
ATOM   1567 N  N   . LEU   A 1 205 ? -15.86795 -28.58020 11.60799  1.000 12.69931 ? 205 LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 205 ? -16.19562 -28.71409 13.02520  1.000 13.63001 ? 205 LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 205 ? -17.05386 -27.54672 13.48316  1.000 14.85793 ? 205 LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 205 ? -18.05053 -27.74070 14.18731  1.000 13.88484 ? 205 LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 205 ? -14.91138 -28.80364 13.85869  1.000 14.27717 ? 205 LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 205 ? -14.05496 -30.04932 13.64612  1.000 15.08815 ? 205 LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 205 ? -12.70724 -29.85546 14.30561  1.000 17.03098 ? 205 LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 205 ? -14.74402 -31.30585 14.16700  1.000 19.49177 ? 205 LEU   A CD2 1 
ATOM   1575 N  N   . ALA   A 1 206 ? -16.70433 -26.32776 13.05359  1.000 12.23166 ? 206 ALA   A N   1 
ATOM   1576 C  CA  . ALA   A 1 206 ? -17.52437 -25.16805 13.39745  1.000 13.18691 ? 206 ALA   A CA  1 
ATOM   1577 C  C   . ALA   A 1 206 ? -18.95741 -25.34945 12.92758  1.000 14.43246 ? 206 ALA   A C   1 
ATOM   1578 O  O   . ALA   A 1 206 ? -19.90495 -24.91477 13.59593  1.000 14.84178 ? 206 ALA   A O   1 
ATOM   1579 C  CB  . ALA   A 1 206 ? -16.92790 -23.90651 12.77865  1.000 12.37833 ? 206 ALA   A CB  1 
ATOM   1580 N  N   . TRP   A 1 207 ? -19.13470 -25.97316 11.76835  1.000 13.59802 ? 207 TRP   A N   1 
ATOM   1581 C  CA  . TRP   A 1 207 ? -20.45291 -26.09453 11.17815  1.000 13.83402 ? 207 TRP   A CA  1 
ATOM   1582 C  C   . TRP   A 1 207 ? -21.26209 -27.15945 11.90381  1.000 14.78041 ? 207 TRP   A C   1 
ATOM   1583 O  O   . TRP   A 1 207 ? -22.46656 -27.00555 12.10705  1.000 15.55917 ? 207 TRP   A O   1 
ATOM   1584 C  CB  . TRP   A 1 207 ? -20.28824 -26.39920 9.68982   1.000 12.36926 ? 207 TRP   A CB  1 
ATOM   1585 C  CG  . TRP   A 1 207 ? -21.52175 -26.84358 8.94961   1.000 13.61594 ? 207 TRP   A CG  1 
ATOM   1586 C  CD1 . TRP   A 1 207 ? -22.53014 -26.05267 8.47861   1.000 11.40976 ? 207 TRP   A CD1 1 
ATOM   1587 C  CD2 . TRP   A 1 207 ? -21.82524 -28.17675 8.51578   1.000 12.30752 ? 207 TRP   A CD2 1 
ATOM   1588 N  NE1 . TRP   A 1 207 ? -23.45812 -26.81918 7.80736   1.000 14.67461 ? 207 TRP   A NE1 1 
ATOM   1589 C  CE2 . TRP   A 1 207 ? -23.04085 -28.12143 7.81221   1.000 15.39672 ? 207 TRP   A CE2 1 
ATOM   1590 C  CE3 . TRP   A 1 207 ? -21.18005 -29.41601 8.65976   1.000 14.56697 ? 207 TRP   A CE3 1 
ATOM   1591 C  CZ2 . TRP   A 1 207 ? -23.63214 -29.24781 7.25725   1.000 17.65538 ? 207 TRP   A CZ2 1 
ATOM   1592 C  CZ3 . TRP   A 1 207 ? -21.77769 -30.53475 8.11054   1.000 16.40149 ? 207 TRP   A CZ3 1 
ATOM   1593 C  CH2 . TRP   A 1 207 ? -22.98729 -30.44252 7.41724   1.000 14.29855 ? 207 TRP   A CH2 1 
ATOM   1594 N  N   . LEU   A 1 208 ? -20.59170 -28.22283 12.35392  1.000 13.40139 ? 208 LEU   A N   1 
ATOM   1595 C  CA  . LEU   A 1 208 ? -21.24356 -29.20519 13.21898  1.000 14.69554 ? 208 LEU   A CA  1 
ATOM   1596 C  C   . LEU   A 1 208 ? -21.71657 -28.57302 14.52819  1.000 15.63256 ? 208 LEU   A C   1 
ATOM   1597 O  O   . LEU   A 1 208 ? -22.80412 -28.88890 15.02525  1.000 16.11086 ? 208 LEU   A O   1 
ATOM   1598 C  CB  . LEU   A 1 208 ? -20.28330 -30.35396 13.49468  1.000 15.46752 ? 208 LEU   A CB  1 
ATOM   1599 C  CG  . LEU   A 1 208 ? -20.05044 -31.22950 12.26827  1.000 16.66834 ? 208 LEU   A CG  1 
ATOM   1600 C  CD1 . LEU   A 1 208 ? -19.04553 -32.30201 12.61906  1.000 16.31656 ? 208 LEU   A CD1 1 
ATOM   1601 C  CD2 . LEU   A 1 208 ? -21.34336 -31.85776 11.72835  1.000 15.88725 ? 208 LEU   A CD2 1 
ATOM   1602 N  N   . TYR   A 1 209 ? -20.92784 -27.65280 15.08684  1.000 15.54567 ? 209 TYR   A N   1 
ATOM   1603 C  CA  . TYR   A 1 209 ? -21.39232 -26.90052 16.25042  1.000 17.84235 ? 209 TYR   A CA  1 
ATOM   1604 C  C   . TYR   A 1 209 ? -22.58480 -25.99930 15.91131  1.000 18.63690 ? 209 TYR   A C   1 
ATOM   1605 O  O   . TYR   A 1 209 ? -23.48796 -25.83386 16.73735  1.000 17.71966 ? 209 TYR   A O   1 
ATOM   1606 C  CB  . TYR   A 1 209 ? -20.24381 -26.08553 16.83854  1.000 15.40794 ? 209 TYR   A CB  1 
ATOM   1607 C  CG  . TYR   A 1 209 ? -19.30018 -26.88287 17.72912  1.000 17.72555 ? 209 TYR   A CG  1 
ATOM   1608 C  CD1 . TYR   A 1 209 ? -19.69950 -27.37275 18.98270  1.000 17.94143 ? 209 TYR   A CD1 1 
ATOM   1609 C  CD2 . TYR   A 1 209 ? -18.01071 -27.15097 17.31373  1.000 19.07212 ? 209 TYR   A CD2 1 
ATOM   1610 C  CE1 . TYR   A 1 209 ? -18.82249 -28.09604 19.78131  1.000 21.29419 ? 209 TYR   A CE1 1 
ATOM   1611 C  CE2 . TYR   A 1 209 ? -17.12934 -27.87256 18.10770  1.000 18.40664 ? 209 TYR   A CE2 1 
ATOM   1612 C  CZ  . TYR   A 1 209 ? -17.53958 -28.34553 19.33351  1.000 22.13687 ? 209 TYR   A CZ  1 
ATOM   1613 O  OH  . TYR   A 1 209 ? -16.64287 -29.06280 20.09791  1.000 22.07354 ? 209 TYR   A OH  1 
ATOM   1614 N  N   . ALA   A 1 210 ? -22.59598 -25.37891 14.72238  1.000 17.21977 ? 210 ALA   A N   1 
ATOM   1615 C  CA  . ALA   A 1 210 ? -23.79121 -24.64493 14.30097  1.000 17.12313 ? 210 ALA   A CA  1 
ATOM   1616 C  C   . ALA   A 1 210 ? -25.00669 -25.56132 14.25477  1.000 18.85100 ? 210 ALA   A C   1 
ATOM   1617 O  O   . ALA   A 1 210 ? -26.10412 -25.17966 14.66268  1.000 18.32767 ? 210 ALA   A O   1 
ATOM   1618 C  CB  . ALA   A 1 210 ? -23.58535 -24.00487 12.93465  1.000 16.79937 ? 210 ALA   A CB  1 
ATOM   1619 N  N   . ALA   A 1 211 ? -24.82186 -26.77333 13.74361  1.000 16.18121 ? 211 ALA   A N   1 
ATOM   1620 C  CA  . ALA   A 1 211 ? -25.91745 -27.72698 13.67443  1.000 16.56554 ? 211 ALA   A CA  1 
ATOM   1621 C  C   . ALA   A 1 211 ? -26.45273 -28.05054 15.06815  1.000 19.55149 ? 211 ALA   A C   1 
ATOM   1622 O  O   . ALA   A 1 211 ? -27.66183 -27.95916 15.31972  1.000 18.35469 ? 211 ALA   A O   1 
ATOM   1623 C  CB  . ALA   A 1 211 ? -25.43316 -28.98078 12.95558  1.000 16.31696 ? 211 ALA   A CB  1 
ATOM   1624 N  N   . VAL   A 1 212 ? -25.55795 -28.41601 15.99350  1.000 18.63294 ? 212 VAL   A N   1 
ATOM   1625 C  CA  . VAL   A 1 212 ? -25.97873 -28.72731 17.35991  1.000 19.41946 ? 212 VAL   A CA  1 
ATOM   1626 C  C   . VAL   A 1 212 ? -26.71624 -27.54606 17.98038  1.000 22.19379 ? 212 VAL   A C   1 
ATOM   1627 O  O   . VAL   A 1 212 ? -27.72671 -27.72194 18.67137  1.000 22.88574 ? 212 VAL   A O   1 
ATOM   1628 C  CB  . VAL   A 1 212 ? -24.77307 -29.15587 18.22241  1.000 20.77887 ? 212 VAL   A CB  1 
ATOM   1629 C  CG1 . VAL   A 1 212 ? -25.19111 -29.29089 19.67411  1.000 21.28902 ? 212 VAL   A CG1 1 
ATOM   1630 C  CG2 . VAL   A 1 212 ? -24.19513 -30.50042 17.73528  1.000 19.73944 ? 212 VAL   A CG2 1 
ATOM   1631 N  N   . ILE   A 1 213 ? -26.22864 -26.32540 17.74426  1.000 21.48085 ? 213 ILE   A N   1 
ATOM   1632 C  CA  . ILE   A 1 213 ? -26.91424 -25.14923 18.26267  1.000 23.08553 ? 213 ILE   A CA  1 
ATOM   1633 C  C   . ILE   A 1 213 ? -28.31143 -25.06190 17.67680  1.000 20.94636 ? 213 ILE   A C   1 
ATOM   1634 O  O   . ILE   A 1 213 ? -29.25585 -24.62833 18.35225  1.000 25.22035 ? 213 ILE   A O   1 
ATOM   1635 C  CB  . ILE   A 1 213 ? -26.07455 -23.88389 17.97906  1.000 25.32545 ? 213 ILE   A CB  1 
ATOM   1636 C  CG1 . ILE   A 1 213 ? -24.81359 -23.90175 18.86086  1.000 24.58592 ? 213 ILE   A CG1 1 
ATOM   1637 C  CG2 . ILE   A 1 213 ? -26.89043 -22.62449 18.20957  1.000 26.76236 ? 213 ILE   A CG2 1 
ATOM   1638 C  CD1 . ILE   A 1 213 ? -23.74634 -22.92833 18.45940  1.000 23.02890 ? 213 ILE   A CD1 1 
ATOM   1639 N  N   . ASN   A 1 214 ? -28.49018 -25.55860 16.45523  1.000 20.63825 ? 214 ASN   A N   1 
ATOM   1640 C  CA  . ASN   A 1 214 ? -29.75724 -25.47111 15.75636  1.000 20.59210 ? 214 ASN   A CA  1 
ATOM   1641 C  C   . ASN   A 1 214 ? -30.61225 -26.73455 15.86902  1.000 22.07166 ? 214 ASN   A C   1 
ATOM   1642 O  O   . ASN   A 1 214 ? -31.63082 -26.83853 15.17471  1.000 24.16140 ? 214 ASN   A O   1 
ATOM   1643 C  CB  . ASN   A 1 214 ? -29.50543 -25.13609 14.29608  1.000 21.59401 ? 214 ASN   A CB  1 
ATOM   1644 C  CG  . ASN   A 1 214 ? -29.33239 -23.64821 14.08198  1.000 24.95221 ? 214 ASN   A CG  1 
ATOM   1645 O  OD1 . ASN   A 1 214 ? -28.33641 -23.04978 14.50219  1.000 27.93493 ? 214 ASN   A OD1 1 
ATOM   1646 N  ND2 . ASN   A 1 214 ? -30.35714 -23.02234 13.52596  1.000 25.63155 ? 214 ASN   A ND2 1 
ATOM   1647 N  N   . GLY   A 1 215 ? -30.22486 -27.69835 16.71030  1.000 21.11713 ? 215 GLY   A N   1 
ATOM   1648 C  CA  . GLY   A 1 215 ? -31.05146 -28.85011 17.01227  1.000 23.74357 ? 215 GLY   A CA  1 
ATOM   1649 C  C   . GLY   A 1 215 ? -30.73245 -30.13366 16.26759  1.000 24.86153 ? 215 GLY   A C   1 
ATOM   1650 O  O   . GLY   A 1 215 ? -31.38603 -31.14583 16.52693  1.000 24.48162 ? 215 GLY   A O   1 
ATOM   1651 N  N   . ASP   A 1 216 ? -29.79129 -30.12133 15.32560  1.000 21.37344 ? 216 ASP   A N   1 
ATOM   1652 C  CA  . ASP   A 1 216 ? -29.31934 -31.34330 14.67654  1.000 21.31665 ? 216 ASP   A CA  1 
ATOM   1653 C  C   . ASP   A 1 216 ? -28.32245 -32.03527 15.60712  1.000 23.68034 ? 216 ASP   A C   1 
ATOM   1654 O  O   . ASP   A 1 216 ? -27.22110 -31.51948 15.83653  1.000 24.52462 ? 216 ASP   A O   1 
ATOM   1655 C  CB  . ASP   A 1 216 ? -28.65249 -31.01984 13.33877  1.000 23.22466 ? 216 ASP   A CB  1 
ATOM   1656 C  CG  . ASP   A 1 216 ? -29.64693 -30.79251 12.21914  1.000 26.16175 ? 216 ASP   A CG  1 
ATOM   1657 O  OD1 . ASP   A 1 216 ? -30.75828 -31.34281 12.30058  1.000 32.07956 ? 216 ASP   A OD1 1 
ATOM   1658 O  OD2 . ASP   A 1 216 ? -29.32050 -30.03133 11.27379  1.000 22.93511 ? 216 ASP   A OD2 1 
ATOM   1659 N  N   . ARG   A 1 217 ? -28.68032 -33.22151 16.12448  1.000 22.52568 ? 217 ARG   A N   1 
ATOM   1660 C  CA  . ARG   A 1 217 ? -27.82062 -33.91991 17.07611  1.000 23.48121 ? 217 ARG   A CA  1 
ATOM   1661 C  C   . ARG   A 1 217 ? -27.57235 -35.38680 16.74968  1.000 24.32867 ? 217 ARG   A C   1 
ATOM   1662 O  O   . ARG   A 1 217 ? -26.86340 -36.05931 17.50730  1.000 25.22167 ? 217 ARG   A O   1 
ATOM   1663 C  CB  . ARG   A 1 217 ? -28.40989 -33.85268 18.49403  1.000 24.74297 ? 217 ARG   A CB  1 
ATOM   1664 C  CG  . ARG   A 1 217 ? -28.70511 -32.46157 19.02071  1.000 24.95454 ? 217 ARG   A CG  1 
ATOM   1665 C  CD  . ARG   A 1 217 ? -29.34790 -32.56157 20.41099  1.000 25.96264 ? 217 ARG   A CD  1 
ATOM   1666 N  NE  . ARG   A 1 217 ? -28.42963 -33.13859 21.38623  1.000 26.88781 ? 217 ARG   A NE  1 
ATOM   1667 C  CZ  . ARG   A 1 217 ? -27.48942 -32.46340 22.03525  1.000 27.59826 ? 217 ARG   A CZ  1 
ATOM   1668 N  NH1 . ARG   A 1 217 ? -27.35612 -31.15372 21.89625  1.000 25.49134 ? 217 ARG   A NH1 1 
ATOM   1669 N  NH2 . ARG   A 1 217 ? -26.66283 -33.11909 22.84799  1.000 27.64196 ? 217 ARG   A NH2 1 
ATOM   1670 N  N   . TRP   A 1 218 ? -28.14212 -35.90563 15.66299  1.000 24.36403 ? 218 TRP   A N   1 
ATOM   1671 C  CA  . TRP   A 1 218 ? -28.10493 -37.33794 15.40648  1.000 25.65699 ? 218 TRP   A CA  1 
ATOM   1672 C  C   . TRP   A 1 218 ? -26.69203 -37.88026 15.24345  1.000 25.48713 ? 218 TRP   A C   1 
ATOM   1673 O  O   . TRP   A 1 218 ? -26.47925 -39.08012 15.43427  1.000 26.88927 ? 218 TRP   A O   1 
ATOM   1674 C  CB  . TRP   A 1 218 ? -28.93935 -37.64674 14.16557  1.000 25.71034 ? 218 TRP   A CB  1 
ATOM   1675 C  CG  . TRP   A 1 218 ? -28.42882 -37.01565 12.87895  1.000 25.53660 ? 218 TRP   A CG  1 
ATOM   1676 C  CD1 . TRP   A 1 218 ? -28.89244 -35.87737 12.28362  1.000 25.22566 ? 218 TRP   A CD1 1 
ATOM   1677 C  CD2 . TRP   A 1 218 ? -27.40244 -37.52471 12.02392  1.000 23.75756 ? 218 TRP   A CD2 1 
ATOM   1678 N  NE1 . TRP   A 1 218 ? -28.19971 -35.63617 11.11539  1.000 23.20485 ? 218 TRP   A NE1 1 
ATOM   1679 C  CE2 . TRP   A 1 218 ? -27.28595 -36.63821 10.93259  1.000 25.20203 ? 218 TRP   A CE2 1 
ATOM   1680 C  CE3 . TRP   A 1 218 ? -26.55907 -38.63999 12.07835  1.000 26.36199 ? 218 TRP   A CE3 1 
ATOM   1681 C  CZ2 . TRP   A 1 218 ? -26.35680 -36.82847 9.91180   1.000 24.71263 ? 218 TRP   A CZ2 1 
ATOM   1682 C  CZ3 . TRP   A 1 218 ? -25.64217 -38.82965 11.05990  1.000 26.77253 ? 218 TRP   A CZ3 1 
ATOM   1683 C  CH2 . TRP   A 1 218 ? -25.54627 -37.92055 9.99058   1.000 24.28221 ? 218 TRP   A CH2 1 
ATOM   1684 N  N   . PHE   A 1 219 ? -25.73821 -37.03097 14.87137  1.000 23.93598 ? 219 PHE   A N   1 
ATOM   1685 C  CA  . PHE   A 1 219 ? -24.35160 -37.41008 14.62306  1.000 23.69515 ? 219 PHE   A CA  1 
ATOM   1686 C  C   . PHE   A 1 219 ? -23.47795 -37.35310 15.87126  1.000 24.15954 ? 219 PHE   A C   1 
ATOM   1687 O  O   . PHE   A 1 219 ? -22.28297 -37.64968 15.78844  1.000 24.12723 ? 219 PHE   A O   1 
ATOM   1688 C  CB  . PHE   A 1 219 ? -23.76185 -36.49028 13.54155  1.000 21.89131 ? 219 PHE   A CB  1 
ATOM   1689 C  CG  . PHE   A 1 219 ? -23.97665 -35.03736 13.82785  1.000 20.63473 ? 219 PHE   A CG  1 
ATOM   1690 C  CD1 . PHE   A 1 219 ? -23.09935 -34.34010 14.64689  1.000 20.19026 ? 219 PHE   A CD1 1 
ATOM   1691 C  CD2 . PHE   A 1 219 ? -25.08791 -34.37329 13.30783  1.000 20.10821 ? 219 PHE   A CD2 1 
ATOM   1692 C  CE1 . PHE   A 1 219 ? -23.30949 -33.00356 14.92293  1.000 19.23490 ? 219 PHE   A CE1 1 
ATOM   1693 C  CE2 . PHE   A 1 219 ? -25.31433 -33.04937 13.58870  1.000 20.52555 ? 219 PHE   A CE2 1 
ATOM   1694 C  CZ  . PHE   A 1 219 ? -24.42505 -32.35240 14.39577  1.000 18.72034 ? 219 PHE   A CZ  1 
ATOM   1695 N  N   . LEU   A 1 220 ? -24.03420 -36.96779 17.01434  1.000 24.72431 ? 220 LEU   A N   1 
ATOM   1696 C  CA  . LEU   A 1 220 ? -23.27147 -36.96128 18.25008  1.000 25.47738 ? 220 LEU   A CA  1 
ATOM   1697 C  C   . LEU   A 1 220 ? -23.12312 -38.37883 18.79366  1.000 27.43613 ? 220 LEU   A C   1 
ATOM   1698 O  O   . LEU   A 1 220 ? -23.91636 -39.27527 18.50235  1.000 28.42971 ? 220 LEU   A O   1 
ATOM   1699 C  CB  . LEU   A 1 220 ? -23.94144 -36.07076 19.29187  1.000 25.65784 ? 220 LEU   A CB  1 
ATOM   1700 C  CG  . LEU   A 1 220 ? -24.02747 -34.59784 18.89715  1.000 23.94181 ? 220 LEU   A CG  1 
ATOM   1701 C  CD1 . LEU   A 1 220 ? -24.73712 -33.81775 19.97014  1.000 24.47869 ? 220 LEU   A CD1 1 
ATOM   1702 C  CD2 . LEU   A 1 220 ? -22.62501 -34.02690 18.63422  1.000 22.81425 ? 220 LEU   A CD2 1 
ATOM   1703 N  N   . ASN   A 1 221 ? -22.07558 -38.57329 19.58396  1.000 28.12207 ? 221 ASN   A N   1 
ATOM   1704 C  CA  . ASN   A 1 221 ? -21.82859 -39.85555 20.21302  1.000 30.99403 ? 221 ASN   A CA  1 
ATOM   1705 C  C   . ASN   A 1 221 ? -21.12851 -39.64160 21.54553  1.000 33.85701 ? 221 ASN   A C   1 
ATOM   1706 O  O   . ASN   A 1 221 ? -20.72210 -38.52692 21.89261  1.000 31.07539 ? 221 ASN   A O   1 
ATOM   1707 C  CB  . ASN   A 1 221 ? -21.03032 -40.77436 19.28329  1.000 33.68063 ? 221 ASN   A CB  1 
ATOM   1708 C  CG  . ASN   A 1 221 ? -19.94072 -40.03312 18.52876  1.000 33.20172 ? 221 ASN   A CG  1 
ATOM   1709 O  OD1 . ASN   A 1 221 ? -20.17884 -39.55582 17.42396  1.000 35.28620 ? 221 ASN   A OD1 1 
ATOM   1710 N  ND2 . ASN   A 1 221 ? -18.76045 -39.89174 19.13439  1.000 34.00884 ? 221 ASN   A ND2 1 
ATOM   1711 N  N   . ARG   A 1 222 ? -21.02951 -40.73744 22.30516  1.000 34.01621 ? 222 ARG   A N   1 
ATOM   1712 C  CA  . ARG   A 1 222 ? -20.31582 -40.75583 23.57387  1.000 35.23645 ? 222 ARG   A CA  1 
ATOM   1713 C  C   . ARG   A 1 222 ? -18.81222 -40.93684 23.40672  1.000 38.29163 ? 222 ARG   A C   1 
ATOM   1714 O  O   . ARG   A 1 222 ? -18.06592 -40.58656 24.32431  1.000 44.98495 ? 222 ARG   A O   1 
ATOM   1715 C  CB  . ARG   A 1 222 ? -20.84342 -41.88722 24.46550  1.000 40.12890 ? 222 ARG   A CB  1 
ATOM   1716 C  CG  . ARG   A 1 222 ? -20.22055 -43.25089 24.12259  1.000 40.37940 ? 222 ARG   A CG  1 
ATOM   1717 C  CD  . ARG   A 1 222 ? -20.92418 -44.38582 24.81951  1.000 40.81972 ? 222 ARG   A CD  1 
ATOM   1718 N  NE  . ARG   A 1 222 ? -20.53986 -44.50844 26.21926  1.000 46.27365 ? 222 ARG   A NE  1 
ATOM   1719 C  CZ  . ARG   A 1 222 ? -21.03827 -45.41764 27.04660  1.000 45.06071 ? 222 ARG   A CZ  1 
ATOM   1720 N  NH1 . ARG   A 1 222 ? -21.97929 -46.26515 26.65621  1.000 45.88753 ? 222 ARG   A NH1 1 
ATOM   1721 N  NH2 . ARG   A 1 222 ? -20.58935 -45.47336 28.29913  1.000 49.13519 ? 222 ARG   A NH2 1 
ATOM   1722 N  N   . PHE   A 1 223 ? -18.34882 -41.48579 22.28129  1.000 40.22760 ? 223 PHE   A N   1 
ATOM   1723 C  CA  . PHE   A 1 223 ? -16.92069 -41.71612 22.11106  1.000 39.85627 ? 223 PHE   A CA  1 
ATOM   1724 C  C   . PHE   A 1 223 ? -16.15331 -40.40197 22.06699  1.000 36.60518 ? 223 PHE   A C   1 
ATOM   1725 O  O   . PHE   A 1 223 ? -16.69590 -39.32618 21.78321  1.000 35.80627 ? 223 PHE   A O   1 
ATOM   1726 C  CB  . PHE   A 1 223 ? -16.59375 -42.47863 20.82156  1.000 39.93502 ? 223 PHE   A CB  1 
ATOM   1727 C  CG  . PHE   A 1 223 ? -17.69296 -43.35350 20.32165  1.000 41.81138 ? 223 PHE   A CG  1 
ATOM   1728 C  CD1 . PHE   A 1 223 ? -17.95624 -44.57234 20.92188  1.000 45.47047 ? 223 PHE   A CD1 1 
ATOM   1729 C  CD2 . PHE   A 1 223 ? -18.43422 -42.97883 19.21126  1.000 42.62413 ? 223 PHE   A CD2 1 
ATOM   1730 C  CE1 . PHE   A 1 223 ? -18.97066 -45.39473 20.44771  1.000 46.43781 ? 223 PHE   A CE1 1 
ATOM   1731 C  CE2 . PHE   A 1 223 ? -19.45649 -43.78776 18.73325  1.000 43.16129 ? 223 PHE   A CE2 1 
ATOM   1732 C  CZ  . PHE   A 1 223 ? -19.72288 -44.99923 19.35009  1.000 48.23521 ? 223 PHE   A CZ  1 
ATOM   1733 N  N   . THR   A 1 224 ? -14.86061 -40.51246 22.33652  1.000 36.91024 ? 224 THR   A N   1 
ATOM   1734 C  CA  . THR   A 1 224 ? -13.90927 -39.43808 22.12290  1.000 34.64352 ? 224 THR   A CA  1 
ATOM   1735 C  C   . THR   A 1 224 ? -12.73924 -39.97614 21.30406  1.000 35.45323 ? 224 THR   A C   1 
ATOM   1736 O  O   . THR   A 1 224 ? -12.68991 -41.15746 20.94307  1.000 35.76608 ? 224 THR   A O   1 
ATOM   1737 C  CB  . THR   A 1 224 ? -13.44270 -38.83858 23.45856  1.000 36.58131 ? 224 THR   A CB  1 
ATOM   1738 O  OG1 . THR   A 1 224 ? -13.01628 -37.48393 23.25413  1.000 33.90609 ? 224 THR   A OG1 1 
ATOM   1739 C  CG2 . THR   A 1 224 ? -12.31850 -39.67097 24.09283  1.000 35.11472 ? 224 THR   A CG2 1 
ATOM   1740 N  N   . THR   A 1 225 ? -11.79652 -39.09206 21.00109  1.000 33.62179 ? 225 THR   A N   1 
ATOM   1741 C  CA  . THR   A 1 225 ? -10.59947 -39.45424 20.25940  1.000 33.32212 ? 225 THR   A CA  1 
ATOM   1742 C  C   . THR   A 1 225 ? -9.48100  -38.51057 20.67149  1.000 33.72526 ? 225 THR   A C   1 
ATOM   1743 O  O   . THR   A 1 225 ? -9.72850  -37.43068 21.21625  1.000 32.44211 ? 225 THR   A O   1 
ATOM   1744 C  CB  . THR   A 1 225 ? -10.83302 -39.38137 18.74075  1.000 31.97743 ? 225 THR   A CB  1 
ATOM   1745 O  OG1 . THR   A 1 225 ? -9.74617  -40.01005 18.05351  1.000 34.21330 ? 225 THR   A OG1 1 
ATOM   1746 C  CG2 . THR   A 1 225 ? -10.94118 -37.93448 18.28311  1.000 32.51688 ? 225 THR   A CG2 1 
ATOM   1747 N  N   . THR   A 1 226 ? -8.24207  -38.93000 20.41748  1.000 34.84110 ? 226 THR   A N   1 
ATOM   1748 C  CA  . THR   A 1 226 ? -7.13683  -38.00493 20.60987  1.000 33.97325 ? 226 THR   A CA  1 
ATOM   1749 C  C   . THR   A 1 226 ? -6.94472  -37.17220 19.35020  1.000 32.12815 ? 226 THR   A C   1 
ATOM   1750 O  O   . THR   A 1 226 ? -7.39288  -37.53553 18.25831  1.000 29.74085 ? 226 THR   A O   1 
ATOM   1751 C  CB  . THR   A 1 226 ? -5.82811  -38.73127 20.93500  1.000 36.70209 ? 226 THR   A CB  1 
ATOM   1752 O  OG1 . THR   A 1 226 ? -5.64147  -39.82168 20.02671  1.000 38.07697 ? 226 THR   A OG1 1 
ATOM   1753 C  CG2 . THR   A 1 226 ? -5.87182  -39.27717 22.35117  1.000 38.00314 ? 226 THR   A CG2 1 
ATOM   1754 N  N   . LEU   A 1 227 ? -6.27124  -36.03481 19.51931  1.000 31.49926 ? 227 LEU   A N   1 
ATOM   1755 C  CA  . LEU   A 1 227 ? -5.93450  -35.19979 18.37440  1.000 31.65606 ? 227 LEU   A CA  1 
ATOM   1756 C  C   . LEU   A 1 227 ? -5.07373  -35.95675 17.36450  1.000 32.89913 ? 227 LEU   A C   1 
ATOM   1757 O  O   . LEU   A 1 227 ? -5.34387  -35.90962 16.15789  1.000 29.63724 ? 227 LEU   A O   1 
ATOM   1758 C  CB  . LEU   A 1 227 ? -5.23784  -33.92844 18.85524  1.000 29.70300 ? 227 LEU   A CB  1 
ATOM   1759 C  CG  . LEU   A 1 227 ? -4.96309  -32.82697 17.83836  1.000 28.65848 ? 227 LEU   A CG  1 
ATOM   1760 C  CD1 . LEU   A 1 227 ? -6.21667  -32.51283 17.03650  1.000 28.12953 ? 227 LEU   A CD1 1 
ATOM   1761 C  CD2 . LEU   A 1 227 ? -4.47194  -31.58517 18.56068  1.000 26.87959 ? 227 LEU   A CD2 1 
ATOM   1762 N  N   . ASN   A 1 228 ? -4.03922  -36.66812 17.83299  1.000 35.43616 ? 228 ASN   A N   1 
ATOM   1763 C  CA  . ASN   A 1 228 ? -3.19953  -37.43413 16.91025  1.000 34.29004 ? 228 ASN   A CA  1 
ATOM   1764 C  C   . ASN   A 1 228 ? -4.00966  -38.48309 16.16045  1.000 35.42592 ? 228 ASN   A C   1 
ATOM   1765 O  O   . ASN   A 1 228 ? -3.83704  -38.66029 14.94809  1.000 36.73227 ? 228 ASN   A O   1 
ATOM   1766 C  CB  . ASN   A 1 228 ? -2.02837  -38.09208 17.64867  1.000 37.80448 ? 228 ASN   A CB  1 
ATOM   1767 C  CG  . ASN   A 1 228 ? -1.09433  -37.07801 18.27954  1.000 39.15220 ? 228 ASN   A CG  1 
ATOM   1768 O  OD1 . ASN   A 1 228 ? -0.79791  -36.04309 17.68385  1.000 42.67824 ? 228 ASN   A OD1 1 
ATOM   1769 N  ND2 . ASN   A 1 228 ? -0.62637  -37.36640 19.48577  1.000 39.32328 ? 228 ASN   A ND2 1 
ATOM   1770 N  N   . ASP   A 1 229 ? -4.91027  -39.17730 16.85662  1.000 35.10899 ? 229 ASP   A N   1 
ATOM   1771 C  CA  . ASP   A 1 229 ? -5.70233  -40.20983 16.19574  1.000 35.39921 ? 229 ASP   A CA  1 
ATOM   1772 C  C   . ASP   A 1 229 ? -6.72971  -39.60814 15.23656  1.000 33.70679 ? 229 ASP   A C   1 
ATOM   1773 O  O   . ASP   A 1 229 ? -6.96009  -40.15020 14.14689  1.000 34.29175 ? 229 ASP   A O   1 
ATOM   1774 C  CB  . ASP   A 1 229 ? -6.35734  -41.09900 17.24775  1.000 37.40307 ? 229 ASP   A CB  1 
ATOM   1775 C  CG  . ASP   A 1 229 ? -5.40964  -42.17986 17.75162  1.000 44.46713 ? 229 ASP   A CG  1 
ATOM   1776 O  OD1 . ASP   A 1 229 ? -4.51452  -41.87629 18.58048  1.000 43.13149 ? 229 ASP   A OD1 1 
ATOM   1777 O  OD2 . ASP   A 1 229 ? -5.56234  -43.33993 17.31574  1.000 47.59926 ? 229 ASP   A OD2 1 
ATOM   1778 N  N   . PHE   A 1 230 ? -7.34140  -38.47866 15.59760  1.000 31.10271 ? 230 PHE   A N   1 
ATOM   1779 C  CA  . PHE   A 1 230 ? -8.21575  -37.81356 14.63631  1.000 29.81178 ? 230 PHE   A CA  1 
ATOM   1780 C  C   . PHE   A 1 230 ? -7.44843  -37.43175 13.37440  1.000 28.81103 ? 230 PHE   A C   1 
ATOM   1781 O  O   . PHE   A 1 230 ? -7.93742  -37.62906 12.25701  1.000 28.33453 ? 230 PHE   A O   1 
ATOM   1782 C  CB  . PHE   A 1 230 ? -8.87282  -36.57617 15.23947  1.000 27.34616 ? 230 PHE   A CB  1 
ATOM   1783 C  CG  . PHE   A 1 230 ? -9.68806  -35.79142 14.23006  1.000 24.65362 ? 230 PHE   A CG  1 
ATOM   1784 C  CD1 . PHE   A 1 230 ? -10.95412 -36.22270 13.86408  1.000 24.17590 ? 230 PHE   A CD1 1 
ATOM   1785 C  CD2 . PHE   A 1 230 ? -9.15468  -34.66908 13.60022  1.000 23.63674 ? 230 PHE   A CD2 1 
ATOM   1786 C  CE1 . PHE   A 1 230 ? -11.68939 -35.53954 12.93044  1.000 25.31911 ? 230 PHE   A CE1 1 
ATOM   1787 C  CE2 . PHE   A 1 230 ? -9.89242  -33.97434 12.65515  1.000 26.56886 ? 230 PHE   A CE2 1 
ATOM   1788 C  CZ  . PHE   A 1 230 ? -11.15586 -34.40511 12.32168  1.000 18.80259 ? 230 PHE   A CZ  1 
ATOM   1789 N  N   . ASN   A 1 231 ? -6.23309  -36.89578 13.53105  1.000 29.17276 ? 231 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 231 ? -5.51588  -36.36985 12.36839  1.000 30.51681 ? 231 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 231 ? -5.09621  -37.47831 11.41339  1.000 31.53295 ? 231 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 231 ? -4.91848  -37.22686 10.21428  1.000 29.47038 ? 231 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 231 ? -4.29699  -35.55782 12.80209  1.000 28.88801 ? 231 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 231 ? -4.64908  -34.13759 13.15530  1.000 27.12646 ? 231 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 231 ? -5.44907  -33.50443 12.47566  1.000 31.21994 ? 231 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 231 ? -4.03668  -33.61505 14.20941  1.000 28.56243 ? 231 ASN   A ND2 1 
ATOM   1797 N  N   . LEU   A 1 232 ? -4.93568  -38.70109 11.92520  1.000 30.83009 ? 232 LEU   A N   1 
ATOM   1798 C  CA  . LEU   A 1 232 ? -4.68102  -39.84607 11.06372  1.000 30.87562 ? 232 LEU   A CA  1 
ATOM   1799 C  C   . LEU   A 1 232 ? -5.86119  -40.12018 10.14676  1.000 32.44233 ? 232 LEU   A C   1 
ATOM   1800 O  O   . LEU   A 1 232 ? -5.67010  -40.56181 9.00911   1.000 32.49012 ? 232 LEU   A O   1 
ATOM   1801 C  CB  . LEU   A 1 232 ? -4.39101  -41.07843 11.91978  1.000 31.30381 ? 232 LEU   A CB  1 
ATOM   1802 C  CG  . LEU   A 1 232 ? -2.97483  -41.21888 12.48054  1.000 36.22793 ? 232 LEU   A CG  1 
ATOM   1803 C  CD1 . LEU   A 1 232 ? -2.90590  -42.48353 13.32509  1.000 33.53459 ? 232 LEU   A CD1 1 
ATOM   1804 C  CD2 . LEU   A 1 232 ? -1.88930  -41.19925 11.39596  1.000 35.06099 ? 232 LEU   A CD2 1 
ATOM   1805 N  N   . VAL   A 1 233 ? -7.08508  -39.88201 10.62750  1.000 31.19928 ? 233 VAL   A N   1 
ATOM   1806 C  CA  . VAL   A 1 233 ? -8.26720  -40.05951 9.79052   1.000 29.56889 ? 233 VAL   A CA  1 
ATOM   1807 C  C   . VAL   A 1 233 ? -8.42939  -38.87983 8.83918   1.000 31.15000 ? 233 VAL   A C   1 
ATOM   1808 O  O   . VAL   A 1 233 ? -8.79179  -39.05313 7.66713   1.000 30.74334 ? 233 VAL   A O   1 
ATOM   1809 C  CB  . VAL   A 1 233 ? -9.51037  -40.26085 10.68017  1.000 31.91979 ? 233 VAL   A CB  1 
ATOM   1810 C  CG1 . VAL   A 1 233 ? -10.80833 -40.12670 9.87027   1.000 31.26156 ? 233 VAL   A CG1 1 
ATOM   1811 C  CG2 . VAL   A 1 233 ? -9.43771  -41.59842 11.39689  1.000 31.69553 ? 233 VAL   A CG2 1 
ATOM   1812 N  N   . ALA   A 1 234 ? -8.16606  -37.66561 9.33089   1.000 28.58300 ? 234 ALA   A N   1 
ATOM   1813 C  CA  . ALA   A 1 234 ? -8.20346  -36.48350 8.48357   1.000 28.75349 ? 234 ALA   A CA  1 
ATOM   1814 C  C   . ALA   A 1 234 ? -7.32946  -36.66110 7.25068   1.000 28.38039 ? 234 ALA   A C   1 
ATOM   1815 O  O   . ALA   A 1 234 ? -7.73878  -36.32413 6.13096   1.000 27.07752 ? 234 ALA   A O   1 
ATOM   1816 C  CB  . ALA   A 1 234 ? -7.75559  -35.26058 9.28826   1.000 28.91278 ? 234 ALA   A CB  1 
ATOM   1817 N  N   . MET   A 1 235 ? -6.11707  -37.17548 7.44417   1.000 30.75682 ? 235 MET   A N   1 
ATOM   1818 C  CA  . MET   A 1 235 ? -5.19915  -37.38406 6.33166   1.000 31.59788 ? 235 MET   A CA  1 
ATOM   1819 C  C   . MET   A 1 235 ? -5.76118  -38.38282 5.32586   1.000 31.17144 ? 235 MET   A C   1 
ATOM   1820 O  O   . MET   A 1 235 ? -5.70162  -38.14341 4.11358   1.000 31.13952 ? 235 MET   A O   1 
ATOM   1821 C  CB  . MET   A 1 235 ? -3.83878  -37.82829 6.86888   1.000 31.96925 ? 235 MET   A CB  1 
ATOM   1822 C  CG  . MET   A 1 235 ? -2.73686  -37.96478 5.82118   1.000 34.69326 ? 235 MET   A CG  1 
ATOM   1823 S  SD  . MET   A 1 235 ? -1.10943  -37.54618 6.49099   1.000 46.56369 ? 235 MET   A SD  1 
ATOM   1824 C  CE  . MET   A 1 235 ? -0.82624  -38.89807 7.63738   1.000 36.86091 ? 235 MET   A CE  1 
ATOM   1825 N  N   . LYS   A 1 236 ? -6.35516  -39.48473 5.80139   1.000 30.75327 ? 236 LYS   A N   1 
ATOM   1826 C  CA  . LYS   A 1 236 ? -6.80762  -40.50318 4.86385   1.000 29.44228 ? 236 LYS   A CA  1 
ATOM   1827 C  C   . LYS   A 1 236 ? -7.97719  -40.01928 4.01565   1.000 29.38406 ? 236 LYS   A C   1 
ATOM   1828 O  O   . LYS   A 1 236 ? -8.16673  -40.53615 2.91187   1.000 29.02980 ? 236 LYS   A O   1 
ATOM   1829 C  CB  . LYS   A 1 236 ? -7.13862  -41.80606 5.61260   1.000 31.29839 ? 236 LYS   A CB  1 
ATOM   1830 C  CG  . LYS   A 1 236 ? -8.20855  -42.70816 4.98280   1.000 31.66400 ? 236 LYS   A CG  1 
ATOM   1831 C  CD  . LYS   A 1 236 ? -8.47695  -43.95941 5.83520   1.000 33.16654 ? 236 LYS   A CD  1 
ATOM   1832 C  CE  . LYS   A 1 236 ? -9.75207  -44.69446 5.40181   1.000 34.48755 ? 236 LYS   A CE  1 
ATOM   1833 N  NZ  . LYS   A 1 236 ? -10.85859 -44.67362 6.41695   1.000 38.23496 ? 236 LYS   A NZ  1 
ATOM   1834 N  N   . TYR   A 1 237 ? -8.71313  -38.99223 4.46795   1.000 26.60625 ? 237 TYR   A N   1 
ATOM   1835 C  CA  . TYR   A 1 237 ? -9.86477  -38.44166 3.75296   1.000 25.83203 ? 237 TYR   A CA  1 
ATOM   1836 C  C   . TYR   A 1 237 ? -9.60507  -37.06062 3.15195   1.000 24.48576 ? 237 TYR   A C   1 
ATOM   1837 O  O   . TYR   A 1 237 ? -10.56256 -36.33710 2.86051   1.000 23.39549 ? 237 TYR   A O   1 
ATOM   1838 C  CB  . TYR   A 1 237 ? -11.08893 -38.37505 4.66832   1.000 24.73077 ? 237 TYR   A CB  1 
ATOM   1839 C  CG  . TYR   A 1 237 ? -11.70214 -39.72286 4.93756   1.000 27.33146 ? 237 TYR   A CG  1 
ATOM   1840 C  CD1 . TYR   A 1 237 ? -11.24530 -40.51739 5.97898   1.000 29.36730 ? 237 TYR   A CD1 1 
ATOM   1841 C  CD2 . TYR   A 1 237 ? -12.73437 -40.20876 4.13947   1.000 28.43420 ? 237 TYR   A CD2 1 
ATOM   1842 C  CE1 . TYR   A 1 237 ? -11.79286 -41.74993 6.22116   1.000 30.41476 ? 237 TYR   A CE1 1 
ATOM   1843 C  CE2 . TYR   A 1 237 ? -13.28711 -41.45171 4.37139   1.000 27.24076 ? 237 TYR   A CE2 1 
ATOM   1844 C  CZ  . TYR   A 1 237 ? -12.80955 -42.21585 5.42070   1.000 30.81284 ? 237 TYR   A CZ  1 
ATOM   1845 O  OH  . TYR   A 1 237 ? -13.33923 -43.45280 5.68450   1.000 33.79191 ? 237 TYR   A OH  1 
ATOM   1846 N  N   . ASN   A 1 238 ? -8.34145  -36.68170 2.94415   1.000 24.37165 ? 238 ASN   A N   1 
ATOM   1847 C  CA  . ASN   A 1 238 ? -8.01554  -35.41096 2.29160   1.000 25.33291 ? 238 ASN   A CA  1 
ATOM   1848 C  C   . ASN   A 1 238 ? -8.55076  -34.21215 3.08167   1.000 20.61763 ? 238 ASN   A C   1 
ATOM   1849 O  O   . ASN   A 1 238 ? -8.97592  -33.20755 2.50901   1.000 24.52578 ? 238 ASN   A O   1 
ATOM   1850 C  CB  . ASN   A 1 238 ? -8.54367  -35.35723 0.85808   1.000 23.80038 ? 238 ASN   A CB  1 
ATOM   1851 C  CG  . ASN   A 1 238 ? -7.78063  -34.36267 0.01446   1.000 27.80202 ? 238 ASN   A CG  1 
ATOM   1852 O  OD1 . ASN   A 1 238 ? -6.67878  -33.97680 0.38472   1.000 30.06426 ? 238 ASN   A OD1 1 
ATOM   1853 N  ND2 . ASN   A 1 238 ? -8.39329  -33.87326 -1.06605  1.000 29.46156 ? 238 ASN   A ND2 1 
ATOM   1854 N  N   . TYR   A 1 239 ? -8.58320  -34.33996 4.39669   1.000 20.82172 ? 239 TYR   A N   1 
ATOM   1855 C  CA  . TYR   A 1 239 ? -8.87000  -33.25296 5.31126   1.000 20.96209 ? 239 TYR   A CA  1 
ATOM   1856 C  C   . TYR   A 1 239 ? -7.55648  -32.71945 5.86509   1.000 20.17150 ? 239 TYR   A C   1 
ATOM   1857 O  O   . TYR   A 1 239 ? -6.59723  -33.46750 6.08291   1.000 20.50652 ? 239 TYR   A O   1 
ATOM   1858 C  CB  . TYR   A 1 239 ? -9.74836  -33.72224 6.47143   1.000 19.23115 ? 239 TYR   A CB  1 
ATOM   1859 C  CG  . TYR   A 1 239 ? -11.23411 -33.70292 6.23159   1.000 16.21079 ? 239 TYR   A CG  1 
ATOM   1860 C  CD1 . TYR   A 1 239 ? -11.79826 -34.34822 5.13728   1.000 18.79594 ? 239 TYR   A CD1 1 
ATOM   1861 C  CD2 . TYR   A 1 239 ? -12.08387 -33.02350 7.10589   1.000 19.89636 ? 239 TYR   A CD2 1 
ATOM   1862 C  CE1 . TYR   A 1 239 ? -13.17565 -34.33099 4.92905   1.000 19.86444 ? 239 TYR   A CE1 1 
ATOM   1863 C  CE2 . TYR   A 1 239 ? -13.46042 -33.00533 6.91613   1.000 18.47316 ? 239 TYR   A CE2 1 
ATOM   1864 C  CZ  . TYR   A 1 239 ? -14.00219 -33.66396 5.83095   1.000 18.58137 ? 239 TYR   A CZ  1 
ATOM   1865 O  OH  . TYR   A 1 239 ? -15.36341 -33.63460 5.65038   1.000 18.24663 ? 239 TYR   A OH  1 
ATOM   1866 N  N   . GLU   A 1 240 ? -7.52318  -31.44282 6.10066   1.000 19.13728 ? 240 GLU   A N   1 
ATOM   1867 C  CA  . GLU   A 1 240 ? -6.22738  -30.96682 6.53214   1.000 23.60001 ? 240 GLU   A CA  1 
ATOM   1868 C  C   . GLU   A 1 240 ? -6.08154  -31.08652 8.03953   1.000 23.13289 ? 240 GLU   A C   1 
ATOM   1869 O  O   . GLU   A 1 240 ? -7.07638  -31.25573 8.75934   1.000 21.37408 ? 240 GLU   A O   1 
ATOM   1870 C  CB  . GLU   A 1 240 ? -6.02234  -29.54198 6.06653   1.000 25.77624 ? 240 GLU   A CB  1 
ATOM   1871 C  CG  . GLU   A 1 240 ? -6.93584  -28.54342 6.60862   1.000 21.52173 ? 240 GLU   A CG  1 
ATOM   1872 C  CD  . GLU   A 1 240 ? -6.80284  -27.25748 5.83879   1.000 26.04097 ? 240 GLU   A CD  1 
ATOM   1873 O  OE1 . GLU   A 1 240 ? -5.79333  -27.11591 5.09898   1.000 32.71983 ? 240 GLU   A OE1 1 
ATOM   1874 O  OE2 . GLU   A 1 240 ? -7.70854  -26.39716 5.96627   1.000 27.43933 ? 240 GLU   A OE2 1 
ATOM   1875 N  N   . PRO   A 1 241 ? -4.84273  -31.08348 8.53746   1.000 21.65792 ? 241 PRO   A N   1 
ATOM   1876 C  CA  . PRO   A 1 241 ? -4.62947  -31.32479 9.96347   1.000 23.73014 ? 241 PRO   A CA  1 
ATOM   1877 C  C   . PRO   A 1 241 ? -5.33004  -30.30278 10.84137  1.000 22.79953 ? 241 PRO   A C   1 
ATOM   1878 O  O   . PRO   A 1 241 ? -5.54887  -29.15130 10.45615  1.000 24.76404 ? 241 PRO   A O   1 
ATOM   1879 C  CB  . PRO   A 1 241 ? -3.10586  -31.25548 10.11905  1.000 23.44283 ? 241 PRO   A CB  1 
ATOM   1880 C  CG  . PRO   A 1 241 ? -2.54780  -31.39057 8.74560   1.000 25.11902 ? 241 PRO   A CG  1 
ATOM   1881 C  CD  . PRO   A 1 241 ? -3.58360  -30.96465 7.77755   1.000 25.82456 ? 241 PRO   A CD  1 
ATOM   1882 N  N   . LEU   A 1 242 ? -5.70950  -30.76290 12.02915  1.000 24.62781 ? 242 LEU   A N   1 
ATOM   1883 C  CA  . LEU   A 1 242 ? -6.27875  -29.92241 13.06866  1.000 23.85321 ? 242 LEU   A CA  1 
ATOM   1884 C  C   . LEU   A 1 242 ? -5.19531  -29.60764 14.08985  1.000 24.36087 ? 242 LEU   A C   1 
ATOM   1885 O  O   . LEU   A 1 242 ? -4.53673  -30.51589 14.59884  1.000 24.67141 ? 242 LEU   A O   1 
ATOM   1886 C  CB  . LEU   A 1 242 ? -7.45052  -30.63258 13.74647  1.000 22.82709 ? 242 LEU   A CB  1 
ATOM   1887 C  CG  . LEU   A 1 242 ? -8.45347  -29.74151 14.46357  1.000 21.62123 ? 242 LEU   A CG  1 
ATOM   1888 C  CD1 . LEU   A 1 242 ? -9.26536  -28.91687 13.46135  1.000 21.17287 ? 242 LEU   A CD1 1 
ATOM   1889 C  CD2 . LEU   A 1 242 ? -9.34053  -30.60917 15.35099  1.000 20.56423 ? 242 LEU   A CD2 1 
ATOM   1890 N  N   . THR   A 1 243 ? -5.00230  -28.32813 14.37300  1.000 24.01825 ? 243 THR   A N   1 
ATOM   1891 C  CA  . THR   A 1 243 ? -3.98647  -27.88630 15.31475  1.000 26.98422 ? 243 THR   A CA  1 
ATOM   1892 C  C   . THR   A 1 243 ? -4.59798  -27.63273 16.68757  1.000 26.26960 ? 243 THR   A C   1 
ATOM   1893 O  O   . THR   A 1 243 ? -5.82119  -27.54587 16.85032  1.000 26.26536 ? 243 THR   A O   1 
ATOM   1894 C  CB  . THR   A 1 243 ? -3.28538  -26.62201 14.79637  1.000 24.85605 ? 243 THR   A CB  1 
ATOM   1895 O  OG1 . THR   A 1 243 ? -4.19430  -25.51152 14.80985  1.000 25.73911 ? 243 THR   A OG1 1 
ATOM   1896 C  CG2 . THR   A 1 243 ? -2.75544  -26.84454 13.38708  1.000 27.39894 ? 243 THR   A CG2 1 
ATOM   1897 N  N   . GLN   A 1 244 ? -3.72038  -27.52540 17.69188  1.000 24.97314 ? 244 GLN   A N   1 
ATOM   1898 C  CA  . GLN   A 1 244 ? -4.17159  -27.09253 19.01114  1.000 27.63435 ? 244 GLN   A CA  1 
ATOM   1899 C  C   . GLN   A 1 244 ? -4.79123  -25.70746 18.95134  1.000 27.55561 ? 244 GLN   A C   1 
ATOM   1900 O  O   . GLN   A 1 244 ? -5.75132  -25.41570 19.68126  1.000 27.49127 ? 244 GLN   A O   1 
ATOM   1901 C  CB  . GLN   A 1 244 ? -3.01052  -27.10694 20.00857  1.000 25.60129 ? 244 GLN   A CB  1 
ATOM   1902 C  CG  . GLN   A 1 244 ? -3.44131  -26.79999 21.43347  1.000 27.86032 ? 244 GLN   A CG  1 
ATOM   1903 C  CD  . GLN   A 1 244 ? -4.54116  -27.73024 21.91432  1.000 29.21627 ? 244 GLN   A CD  1 
ATOM   1904 O  OE1 . GLN   A 1 244 ? -4.51421  -28.93165 21.64201  1.000 29.74363 ? 244 GLN   A OE1 1 
ATOM   1905 N  NE2 . GLN   A 1 244 ? -5.52776  -27.17512 22.61795  1.000 31.12062 ? 244 GLN   A NE2 1 
ATOM   1906 N  N   . ASP   A 1 245 ? -4.28393  -24.84950 18.06360  1.000 27.39206 ? 245 ASP   A N   1 
ATOM   1907 C  CA  . ASP   A 1 245 ? -4.88584  -23.53017 17.91978  1.000 27.52948 ? 245 ASP   A CA  1 
ATOM   1908 C  C   . ASP   A 1 245 ? -6.29606  -23.60444 17.33630  1.000 25.20721 ? 245 ASP   A C   1 
ATOM   1909 O  O   . ASP   A 1 245 ? -7.16880  -22.82856 17.74100  1.000 26.01108 ? 245 ASP   A O   1 
ATOM   1910 C  CB  . ASP   A 1 245 ? -3.99786  -22.62020 17.07839  1.000 25.78199 ? 245 ASP   A CB  1 
ATOM   1911 C  CG  . ASP   A 1 245 ? -4.43143  -21.17648 17.17295  1.000 29.54904 ? 245 ASP   A CG  1 
ATOM   1912 O  OD1 . ASP   A 1 245 ? -4.22114  -20.57484 18.25118  1.000 33.44508 ? 245 ASP   A OD1 1 
ATOM   1913 O  OD2 . ASP   A 1 245 ? -4.96181  -20.63282 16.17883  1.000 34.46649 ? 245 ASP   A OD2 1 
ATOM   1914 N  N   . HIS   A 1 246 ? -6.53794  -24.50909 16.37706  1.000 24.48762 ? 246 HIS   A N   1 
ATOM   1915 C  CA  . HIS   A 1 246 ? -7.91414  -24.79332 15.95817  1.000 22.78434 ? 246 HIS   A CA  1 
ATOM   1916 C  C   . HIS   A 1 246 ? -8.76960  -25.23499 17.13763  1.000 23.47006 ? 246 HIS   A C   1 
ATOM   1917 O  O   . HIS   A 1 246 ? -9.92061  -24.80762 17.27728  1.000 23.84747 ? 246 HIS   A O   1 
ATOM   1918 C  CB  . HIS   A 1 246 ? -7.95060  -25.88719 14.88907  1.000 22.78341 ? 246 HIS   A CB  1 
ATOM   1919 C  CG  . HIS   A 1 246 ? -7.32204  -25.50752 13.58386  1.000 21.51381 ? 246 HIS   A CG  1 
ATOM   1920 N  ND1 . HIS   A 1 246 ? -6.67041  -26.42480 12.78628  1.000 24.54142 ? 246 HIS   A ND1 1 
ATOM   1921 C  CD2 . HIS   A 1 246 ? -7.24341  -24.32182 12.93489  1.000 23.90167 ? 246 HIS   A CD2 1 
ATOM   1922 C  CE1 . HIS   A 1 246 ? -6.21952  -25.82078 11.70116  1.000 24.61498 ? 246 HIS   A CE1 1 
ATOM   1923 N  NE2 . HIS   A 1 246 ? -6.55813  -24.54521 11.76456  1.000 22.90856 ? 246 HIS   A NE2 1 
ATOM   1924 N  N   . VAL   A 1 247 ? -8.23511  -26.11758 17.97905  1.000 25.83636 ? 247 VAL   A N   1 
ATOM   1925 C  CA  . VAL   A 1 247 ? -8.97864  -26.55979 19.15718  1.000 23.62916 ? 247 VAL   A CA  1 
ATOM   1926 C  C   . VAL   A 1 247 ? -9.30867  -25.36973 20.05066  1.000 27.57571 ? 247 VAL   A C   1 
ATOM   1927 O  O   . VAL   A 1 247 ? -10.45053 -25.20768 20.50408  1.000 26.42512 ? 247 VAL   A O   1 
ATOM   1928 C  CB  . VAL   A 1 247 ? -8.19496  -27.64600 19.91166  1.000 27.26950 ? 247 VAL   A CB  1 
ATOM   1929 C  CG1 . VAL   A 1 247 ? -8.81444  -27.89690 21.26141  1.000 28.01588 ? 247 VAL   A CG1 1 
ATOM   1930 C  CG2 . VAL   A 1 247 ? -8.19056  -28.91595 19.10000  1.000 25.92058 ? 247 VAL   A CG2 1 
ATOM   1931 N  N   . ASP   A 1 248 ? -8.32047  -24.50445 20.29293  1.000 25.88964 ? 248 ASP   A N   1 
ATOM   1932 C  CA  . ASP   A 1 248 ? -8.55714  -23.32027 21.11257  1.000 27.71567 ? 248 ASP   A CA  1 
ATOM   1933 C  C   . ASP   A 1 248 ? -9.61071  -22.41468 20.48529  1.000 27.34965 ? 248 ASP   A C   1 
ATOM   1934 O  O   . ASP   A 1 248 ? -10.49545 -21.90873 21.18457  1.000 28.71962 ? 248 ASP   A O   1 
ATOM   1935 C  CB  . ASP   A 1 248 ? -7.24497  -22.55248 21.32732  1.000 27.42459 ? 248 ASP   A CB  1 
ATOM   1936 C  CG  . ASP   A 1 248 ? -6.21879  -23.33192 22.15115  1.000 27.72689 ? 248 ASP   A CG  1 
ATOM   1937 O  OD1 . ASP   A 1 248 ? -6.59446  -24.28293 22.87777  1.000 30.10615 ? 248 ASP   A OD1 1 
ATOM   1938 O  OD2 . ASP   A 1 248 ? -5.01595  -22.99658 22.06225  1.000 27.25231 ? 248 ASP   A OD2 1 
ATOM   1939 N  N   . ILE   A 1 249 ? -9.53432  -22.19709 19.16704  1.000 26.14655 ? 249 ILE   A N   1 
ATOM   1940 C  CA  . ILE   A 1 249 ? -10.49269 -21.32477 18.48249  1.000 25.20210 ? 249 ILE   A CA  1 
ATOM   1941 C  C   . ILE   A 1 249 ? -11.91332 -21.86779 18.60088  1.000 24.28496 ? 249 ILE   A C   1 
ATOM   1942 O  O   . ILE   A 1 249 ? -12.88039 -21.09747 18.64386  1.000 25.30743 ? 249 ILE   A O   1 
ATOM   1943 C  CB  . ILE   A 1 249 ? -10.06126 -21.12718 17.00787  1.000 22.76245 ? 249 ILE   A CB  1 
ATOM   1944 C  CG1 . ILE   A 1 249 ? -8.89173  -20.14674 16.92028  1.000 27.50965 ? 249 ILE   A CG1 1 
ATOM   1945 C  CG2 . ILE   A 1 249 ? -11.20220 -20.67079 16.13077  1.000 24.20475 ? 249 ILE   A CG2 1 
ATOM   1946 C  CD1 . ILE   A 1 249 ? -8.03418  -20.35658 15.68134  1.000 27.51494 ? 249 ILE   A CD1 1 
ATOM   1947 N  N   . LEU   A 1 250 ? -12.06119 -23.18681 18.69178  1.000 24.23310 ? 250 LEU   A N   1 
ATOM   1948 C  CA  . LEU   A 1 250 ? -13.36135 -23.82959 18.85491  1.000 25.54316 ? 250 LEU   A CA  1 
ATOM   1949 C  C   . LEU   A 1 250 ? -13.84402 -23.84856 20.30543  1.000 23.96260 ? 250 LEU   A C   1 
ATOM   1950 O  O   . LEU   A 1 250 ? -14.95772 -24.32234 20.56073  1.000 21.71271 ? 250 LEU   A O   1 
ATOM   1951 C  CB  . LEU   A 1 250 ? -13.29684 -25.25325 18.28904  1.000 21.36003 ? 250 LEU   A CB  1 
ATOM   1952 C  CG  . LEU   A 1 250 ? -13.12226 -25.36581 16.77336  1.000 18.79873 ? 250 LEU   A CG  1 
ATOM   1953 C  CD1 . LEU   A 1 250 ? -12.81247 -26.79937 16.36530  1.000 17.26224 ? 250 LEU   A CD1 1 
ATOM   1954 C  CD2 . LEU   A 1 250 ? -14.39588 -24.87018 16.07116  1.000 18.74992 ? 250 LEU   A CD2 1 
ATOM   1955 N  N   . GLY   A 1 251 ? -13.05120 -23.32318 21.24720  1.000 24.56068 ? 251 GLY   A N   1 
ATOM   1956 C  CA  . GLY   A 1 251 ? -13.39640 -23.29610 22.65475  1.000 25.26765 ? 251 GLY   A CA  1 
ATOM   1957 C  C   . GLY   A 1 251 ? -14.76818 -22.71984 22.97520  1.000 26.01529 ? 251 GLY   A C   1 
ATOM   1958 O  O   . GLY   A 1 251 ? -15.57602 -23.35336 23.66250  1.000 26.92601 ? 251 GLY   A O   1 
ATOM   1959 N  N   . PRO   A 1 252 ? -15.05256 -21.49581 22.50808  1.000 26.14801 ? 252 PRO   A N   1 
ATOM   1960 C  CA  . PRO   A 1 252 ? -16.36480 -20.89857 22.80608  1.000 26.83891 ? 252 PRO   A CA  1 
ATOM   1961 C  C   . PRO   A 1 252 ? -17.54213 -21.71974 22.31177  1.000 25.88808 ? 252 PRO   A C   1 
ATOM   1962 O  O   . PRO   A 1 252 ? -18.52830 -21.87846 23.04800  1.000 27.08632 ? 252 PRO   A O   1 
ATOM   1963 C  CB  . PRO   A 1 252 ? -16.28784 -19.53730 22.10120  1.000 26.86390 ? 252 PRO   A CB  1 
ATOM   1964 C  CG  . PRO   A 1 252 ? -14.85792 -19.19628 22.12726  1.000 26.06345 ? 252 PRO   A CG  1 
ATOM   1965 C  CD  . PRO   A 1 252 ? -14.12577 -20.49784 21.94009  1.000 28.18321 ? 252 PRO   A CD  1 
ATOM   1966 N  N   . LEU   A 1 253 ? -17.47112 -22.23951 21.08307  1.000 25.12778 ? 253 LEU   A N   1 
ATOM   1967 C  CA  . LEU   A 1 253 ? -18.55991 -23.06031 20.55965  1.000 24.34975 ? 253 LEU   A CA  1 
ATOM   1968 C  C   . LEU   A 1 253 ? -18.69902 -24.33847 21.36841  1.000 23.63189 ? 253 LEU   A C   1 
ATOM   1969 O  O   . LEU   A 1 253 ? -19.81543 -24.77553 21.67472  1.000 23.19112 ? 253 LEU   A O   1 
ATOM   1970 C  CB  . LEU   A 1 253 ? -18.30569 -23.37880 19.08847  1.000 21.29016 ? 253 LEU   A CB  1 
ATOM   1971 C  CG  . LEU   A 1 253 ? -18.54393 -22.28453 18.04790  1.000 21.73692 ? 253 LEU   A CG  1 
ATOM   1972 C  CD1 . LEU   A 1 253 ? -18.18935 -22.81646 16.68138  1.000 19.76885 ? 253 LEU   A CD1 1 
ATOM   1973 C  CD2 . LEU   A 1 253 ? -20.00275 -21.84846 18.08635  1.000 22.89892 ? 253 LEU   A CD2 1 
ATOM   1974 N  N   . SER   A 1 254 ? -17.56308 -24.94108 21.72894  1.000 22.44991 ? 254 SER   A N   1 
ATOM   1975 C  CA  . SER   A 1 254 ? -17.54577 -26.06878 22.65166  1.000 24.81678 ? 254 SER   A CA  1 
ATOM   1976 C  C   . SER   A 1 254 ? -18.25068 -25.72782 23.95751  1.000 25.55231 ? 254 SER   A C   1 
ATOM   1977 O  O   . SER   A 1 254 ? -19.08550 -26.49671 24.44823  1.000 26.95160 ? 254 SER   A O   1 
ATOM   1978 C  CB  . SER   A 1 254 ? -16.09300 -26.48007 22.91850  1.000 26.18944 ? 254 SER   A CB  1 
ATOM   1979 O  OG  . SER   A 1 254 ? -16.01009 -27.71373 23.59598  1.000 28.32452 ? 254 SER   A OG  1 
ATOM   1980 N  N   . ALA   A 1 255 ? -17.90901 -24.58145 24.55179  1.000 26.80630 ? 255 ALA   A N   1 
ATOM   1981 C  CA  . ALA   A 1 255 ? -18.46071 -24.25262 25.86349  1.000 28.08173 ? 255 ALA   A CA  1 
ATOM   1982 C  C   . ALA   A 1 255 ? -19.94971 -23.93062 25.78369  1.000 27.83038 ? 255 ALA   A C   1 
ATOM   1983 O  O   . ALA   A 1 255 ? -20.69061 -24.15544 26.75093  1.000 30.09340 ? 255 ALA   A O   1 
ATOM   1984 C  CB  . ALA   A 1 255 ? -17.68341 -23.08742 26.47745  1.000 26.89906 ? 255 ALA   A CB  1 
ATOM   1985 N  N   . GLN   A 1 256 ? -20.40226 -23.41625 24.64253  1.000 28.09221 ? 256 GLN   A N   1 
ATOM   1986 C  CA  . GLN   A 1 256 ? -21.81519 -23.09840 24.47284  1.000 28.26974 ? 256 GLN   A CA  1 
ATOM   1987 C  C   . GLN   A 1 256 ? -22.65253 -24.36050 24.30366  1.000 28.35128 ? 256 GLN   A C   1 
ATOM   1988 O  O   . GLN   A 1 256 ? -23.77064 -24.44806 24.82845  1.000 33.53753 ? 256 GLN   A O   1 
ATOM   1989 C  CB  . GLN   A 1 256 ? -21.98367 -22.16087 23.27954  1.000 28.52122 ? 256 GLN   A CB  1 
ATOM   1990 C  CG  . GLN   A 1 256 ? -23.37617 -21.58368 23.12850  1.000 32.56049 ? 256 GLN   A CG  1 
ATOM   1991 C  CD  . GLN   A 1 256 ? -23.58176 -20.97875 21.76545  1.000 30.24444 ? 256 GLN   A CD  1 
ATOM   1992 O  OE1 . GLN   A 1 256 ? -22.61395 -20.69859 21.05049  1.000 32.60987 ? 256 GLN   A OE1 1 
ATOM   1993 N  NE2 . GLN   A 1 256 ? -24.83946 -20.79116 21.37814  1.000 32.71404 ? 256 GLN   A NE2 1 
ATOM   1994 N  N   . THR   A 1 257 ? -22.12202 -25.36089 23.59914  1.000 28.90747 ? 257 THR   A N   1 
ATOM   1995 C  CA  . THR   A 1 257 ? -22.85220 -26.60196 23.38293  1.000 27.34161 ? 257 THR   A CA  1 
ATOM   1996 C  C   . THR   A 1 257 ? -22.55454 -27.65546 24.43636  1.000 27.15388 ? 257 THR   A C   1 
ATOM   1997 O  O   . THR   A 1 257 ? -23.30638 -28.62652 24.55014  1.000 29.86740 ? 257 THR   A O   1 
ATOM   1998 C  CB  . THR   A 1 257 ? -22.52443 -27.17426 22.00027  1.000 26.78669 ? 257 THR   A CB  1 
ATOM   1999 O  OG1 . THR   A 1 257 ? -21.10723 -27.34939 21.88177  1.000 24.32591 ? 257 THR   A OG1 1 
ATOM   2000 C  CG2 . THR   A 1 257 ? -22.98539 -26.19752 20.92107  1.000 23.61205 ? 257 THR   A CG2 1 
ATOM   2001 N  N   . GLY   A 1 258 ? -21.47510 -27.49917 25.19383  1.000 28.25186 ? 258 GLY   A N   1 
ATOM   2002 C  CA  . GLY   A 1 258 ? -21.07752 -28.52461 26.12977  1.000 27.32095 ? 258 GLY   A CA  1 
ATOM   2003 C  C   . GLY   A 1 258 ? -20.52781 -29.78153 25.50133  1.000 27.04987 ? 258 GLY   A C   1 
ATOM   2004 O  O   . GLY   A 1 258 ? -20.49330 -30.82167 26.15303  1.000 28.57561 ? 258 GLY   A O   1 
ATOM   2005 N  N   . ILE   A 1 259 ? -20.10353 -29.72498 24.24594  1.000 26.93036 ? 259 ILE   A N   1 
ATOM   2006 C  CA  . ILE   A 1 259 ? -19.51789 -30.87048 23.56521  1.000 27.53336 ? 259 ILE   A CA  1 
ATOM   2007 C  C   . ILE   A 1 259 ? -18.03244 -30.58460 23.39367  1.000 27.32424 ? 259 ILE   A C   1 
ATOM   2008 O  O   . ILE   A 1 259 ? -17.65596 -29.61566 22.72334  1.000 25.83866 ? 259 ILE   A O   1 
ATOM   2009 C  CB  . ILE   A 1 259 ? -20.19401 -31.12262 22.21142  1.000 25.08196 ? 259 ILE   A CB  1 
ATOM   2010 C  CG1 . ILE   A 1 259 ? -21.64990 -31.54543 22.40885  1.000 29.42486 ? 259 ILE   A CG1 1 
ATOM   2011 C  CG2 . ILE   A 1 259 ? -19.43280 -32.17932 21.42335  1.000 23.52932 ? 259 ILE   A CG2 1 
ATOM   2012 C  CD1 . ILE   A 1 259 ? -22.43514 -31.32806 21.19242  1.000 25.61165 ? 259 ILE   A CD1 1 
ATOM   2013 N  N   . ALA   A 1 260 ? -17.18686 -31.40268 24.02193  1.000 25.97437 ? 260 ALA   A N   1 
ATOM   2014 C  CA  . ALA   A 1 260 ? -15.75140 -31.17398 23.93339  1.000 27.76431 ? 260 ALA   A CA  1 
ATOM   2015 C  C   . ALA   A 1 260 ? -15.30405 -31.23972 22.47544  1.000 24.40223 ? 260 ALA   A C   1 
ATOM   2016 O  O   . ALA   A 1 260 ? -15.86511 -31.98117 21.66537  1.000 25.20796 ? 260 ALA   A O   1 
ATOM   2017 C  CB  . ALA   A 1 260 ? -14.99293 -32.19845 24.78245  1.000 27.73156 ? 260 ALA   A CB  1 
ATOM   2018 N  N   . VAL   A 1 261 ? -14.29779 -30.43556 22.13712  1.000 25.70903 ? 261 VAL   A N   1 
ATOM   2019 C  CA  . VAL   A 1 261 ? -13.83601 -30.38433 20.75178  1.000 24.04998 ? 261 VAL   A CA  1 
ATOM   2020 C  C   . VAL   A 1 261 ? -13.43219 -31.77800 20.27404  1.000 23.32306 ? 261 VAL   A C   1 
ATOM   2021 O  O   . VAL   A 1 261 ? -13.85789 -32.22624 19.20423  1.000 23.53437 ? 261 VAL   A O   1 
ATOM   2022 C  CB  . VAL   A 1 261 ? -12.68950 -29.36789 20.59439  1.000 25.31338 ? 261 VAL   A CB  1 
ATOM   2023 C  CG1 . VAL   A 1 261 ? -12.08565 -29.46654 19.19166  1.000 19.72161 ? 261 VAL   A CG1 1 
ATOM   2024 C  CG2 . VAL   A 1 261 ? -13.17172 -27.95021 20.88907  1.000 22.85126 ? 261 VAL   A CG2 1 
ATOM   2025 N  N   . LEU   A 1 262 ? -12.63148 -32.49925 21.07200  1.000 25.28691 ? 262 LEU   A N   1 
ATOM   2026 C  CA  . LEU   A 1 262 ? -12.21855 -33.84618 20.66903  1.000 26.50518 ? 262 LEU   A CA  1 
ATOM   2027 C  C   . LEU   A 1 262 ? -13.39723 -34.81151 20.57802  1.000 25.54931 ? 262 LEU   A C   1 
ATOM   2028 O  O   . LEU   A 1 262 ? -13.32405 -35.80568 19.84216  1.000 25.64065 ? 262 LEU   A O   1 
ATOM   2029 C  CB  . LEU   A 1 262 ? -11.15959 -34.42175 21.62035  1.000 27.22709 ? 262 LEU   A CB  1 
ATOM   2030 C  CG  . LEU   A 1 262 ? -9.69750  -33.95612 21.51249  1.000 28.67302 ? 262 LEU   A CG  1 
ATOM   2031 C  CD1 . LEU   A 1 262 ? -9.25877  -33.84843 20.05512  1.000 29.87743 ? 262 LEU   A CD1 1 
ATOM   2032 C  CD2 . LEU   A 1 262 ? -9.42233  -32.67392 22.26918  1.000 32.20299 ? 262 LEU   A CD2 1 
ATOM   2033 N  N   . ASP   A 1 263 ? -14.47709 -34.56261 21.32643  1.000 25.60774 ? 263 ASP   A N   1 
ATOM   2034 C  CA  . ASP   A 1 263 ? -15.68018 -35.37427 21.14943  1.000 27.39623 ? 263 ASP   A CA  1 
ATOM   2035 C  C   . ASP   A 1 263 ? -16.28543 -35.14713 19.77165  1.000 24.34506 ? 263 ASP   A C   1 
ATOM   2036 O  O   . ASP   A 1 263 ? -16.76122 -36.08744 19.12324  1.000 24.63457 ? 263 ASP   A O   1 
ATOM   2037 C  CB  . ASP   A 1 263 ? -16.71702 -35.04942 22.22942  1.000 26.82620 ? 263 ASP   A CB  1 
ATOM   2038 C  CG  . ASP   A 1 263 ? -16.34466 -35.59795 23.59951  1.000 31.39490 ? 263 ASP   A CG  1 
ATOM   2039 O  OD1 . ASP   A 1 263 ? -15.23857 -36.17073 23.76204  1.000 31.54999 ? 263 ASP   A OD1 1 
ATOM   2040 O  OD2 . ASP   A 1 263 ? -17.18687 -35.45390 24.51596  1.000 33.15198 ? 263 ASP   A OD2 1 
ATOM   2041 N  N   . MET   A 1 264 ? -16.27956 -33.89752 19.31329  1.000 22.73143 ? 264 MET   A N   1 
ATOM   2042 C  CA  . MET   A 1 264 ? -16.89236 -33.56868 18.03402  1.000 21.22649 ? 264 MET   A CA  1 
ATOM   2043 C  C   . MET   A 1 264 ? -16.01388 -34.10681 16.90330  1.000 21.91164 ? 264 MET   A C   1 
ATOM   2044 O  O   . MET   A 1 264 ? -16.51502 -34.56877 15.87112  1.000 20.39595 ? 264 MET   A O   1 
ATOM   2045 C  CB  . MET   A 1 264 ? -17.02950 -32.04631 17.91930  1.000 19.83178 ? 264 MET   A CB  1 
ATOM   2046 C  CG  . MET   A 1 264 ? -17.86598 -31.48022 16.77263  1.000 22.45016 ? 264 MET   A CG  1 
ATOM   2047 S  SD  . MET   A 1 264 ? -19.57816 -32.12276 16.75465  1.000 20.42310 ? 264 MET   A SD  1 
ATOM   2048 C  CE  . MET   A 1 264 ? -20.35877 -30.77455 17.64097  1.000 18.88311 ? 264 MET   A CE  1 
ATOM   2049 N  N   . CYS   A 1 265 ? -14.69117 -34.06770 17.10372  1.000 21.02836 ? 265 CYS   A N   1 
ATOM   2050 C  CA  . CYS   A 1 265 ? -13.76133 -34.78433 16.23497  1.000 21.14513 ? 265 CYS   A CA  1 
ATOM   2051 C  C   . CYS   A 1 265 ? -14.12728 -36.25929 16.11623  1.000 22.52630 ? 265 CYS   A C   1 
ATOM   2052 O  O   . CYS   A 1 265 ? -14.09042 -36.82715 15.02032  1.000 22.36274 ? 265 CYS   A O   1 
ATOM   2053 C  CB  . CYS   A 1 265 ? -12.33184 -34.64028 16.76481  1.000 23.87437 ? 265 CYS   A CB  1 
ATOM   2054 S  SG  . CYS   A 1 265 ? -11.63936 -33.00228 16.61964  1.000 21.80096 ? 265 CYS   A SG  1 
ATOM   2055 N  N   . ALA   A 1 266 ? -14.48047 -36.89977 17.23494  1.000 24.05774 ? 266 ALA   A N   1 
ATOM   2056 C  CA  . ALA   A 1 266 ? -14.90923 -38.28991 17.16212  1.000 25.52603 ? 266 ALA   A CA  1 
ATOM   2057 C  C   . ALA   A 1 266 ? -16.14559 -38.43666 16.28205  1.000 24.90065 ? 266 ALA   A C   1 
ATOM   2058 O  O   . ALA   A 1 266 ? -16.25937 -39.40112 15.51585  1.000 25.65862 ? 266 ALA   A O   1 
ATOM   2059 C  CB  . ALA   A 1 266 ? -15.16656 -38.84052 18.56511  1.000 27.76105 ? 266 ALA   A CB  1 
ATOM   2060 N  N   . SER   A 1 267 ? -17.07702 -37.47642 16.36419  1.000 23.80650 ? 267 SER   A N   1 
ATOM   2061 C  CA  . SER   A 1 267 ? -18.26733 -37.51383 15.52338  1.000 23.25861 ? 267 SER   A CA  1 
ATOM   2062 C  C   . SER   A 1 267 ? -17.91345 -37.33723 14.05479  1.000 24.38029 ? 267 SER   A C   1 
ATOM   2063 O  O   . SER   A 1 267 ? -18.44010 -38.04700 13.18996  1.000 24.96388 ? 267 SER   A O   1 
ATOM   2064 C  CB  . SER   A 1 267 ? -19.24001 -36.42198 15.95477  1.000 22.42592 ? 267 SER   A CB  1 
ATOM   2065 O  OG  . SER   A 1 267 ? -19.79912 -36.70878 17.21829  1.000 23.73808 ? 267 SER   A OG  1 
ATOM   2066 N  N   . LEU   A 1 268 ? -17.04098 -36.37813 13.75563  1.000 21.76228 ? 268 LEU   A N   1 
ATOM   2067 C  CA  . LEU   A 1 268 ? -16.59917 -36.18481 12.38157  1.000 22.55857 ? 268 LEU   A CA  1 
ATOM   2068 C  C   . LEU   A 1 268 ? -15.91271 -37.43745 11.83876  1.000 23.88282 ? 268 LEU   A C   1 
ATOM   2069 O  O   . LEU   A 1 268 ? -16.15923 -37.83680 10.69276  1.000 24.88499 ? 268 LEU   A O   1 
ATOM   2070 C  CB  . LEU   A 1 268 ? -15.67698 -34.96160 12.30426  1.000 23.77289 ? 268 LEU   A CB  1 
ATOM   2071 C  CG  . LEU   A 1 268 ? -15.10684 -34.52538 10.95050  1.000 21.82091 ? 268 LEU   A CG  1 
ATOM   2072 C  CD1 . LEU   A 1 268 ? -16.17295 -34.54354 9.86121   1.000 19.59274 ? 268 LEU   A CD1 1 
ATOM   2073 C  CD2 . LEU   A 1 268 ? -14.46762 -33.15312 11.05999  1.000 17.71633 ? 268 LEU   A CD2 1 
ATOM   2074 N  N   . LYS   A 1 269 ? -15.04323 -38.06386 12.64248  1.000 23.43595 ? 269 LYS   A N   1 
ATOM   2075 C  CA  . LYS   A 1 269 ? -14.46883 -39.36117 12.28158  1.000 26.39763 ? 269 LYS   A CA  1 
ATOM   2076 C  C   . LYS   A 1 269 ? -15.53225 -40.32592 11.77322  1.000 27.07117 ? 269 LYS   A C   1 
ATOM   2077 O  O   . LYS   A 1 269 ? -15.40402 -40.88942 10.67959  1.000 28.93766 ? 269 LYS   A O   1 
ATOM   2078 C  CB  . LYS   A 1 269 ? -13.74406 -39.97218 13.48313  1.000 25.96679 ? 269 LYS   A CB  1 
ATOM   2079 C  CG  . LYS   A 1 269 ? -12.93024 -41.21051 13.14156  1.000 29.53136 ? 269 LYS   A CG  1 
ATOM   2080 C  CD  . LYS   A 1 269 ? -11.97121 -41.59867 14.26368  1.000 29.16373 ? 269 LYS   A CD  1 
ATOM   2081 C  CE  . LYS   A 1 269 ? -11.49137 -43.03480 14.08322  1.000 37.36470 ? 269 LYS   A CE  1 
ATOM   2082 N  NZ  . LYS   A 1 269 ? -10.60406 -43.48225 15.19388  1.000 38.35000 ? 269 LYS   A NZ  1 
ATOM   2083 N  N   . GLU   A 1 270 ? -16.59166 -40.53474 12.56631  1.000 27.91480 ? 270 GLU   A N   1 
ATOM   2084 C  CA  . GLU   A 1 270 ? -17.62868 -41.50004 12.20142  1.000 29.46591 ? 270 GLU   A CA  1 
ATOM   2085 C  C   . GLU   A 1 270 ? -18.35232 -41.08890 10.92691  1.000 28.11836 ? 270 GLU   A C   1 
ATOM   2086 O  O   . GLU   A 1 270 ? -18.66174 -41.93439 10.07862  1.000 26.56677 ? 270 GLU   A O   1 
ATOM   2087 C  CB  . GLU   A 1 270 ? -18.61866 -41.66747 13.35820  1.000 28.83567 ? 270 GLU   A CB  1 
ATOM   2088 C  CG  . GLU   A 1 270 ? -17.94800 -42.17033 14.63337  1.000 30.72685 ? 270 GLU   A CG  1 
ATOM   2089 C  CD  . GLU   A 1 270 ? -17.29718 -43.53158 14.44583  1.000 35.56018 ? 270 GLU   A CD  1 
ATOM   2090 O  OE1 . GLU   A 1 270 ? -17.90815 -44.37648 13.75597  1.000 36.19934 ? 270 GLU   A OE1 1 
ATOM   2091 O  OE2 . GLU   A 1 270 ? -16.15401 -43.73768 14.92690  1.000 37.20257 ? 270 GLU   A OE2 1 
ATOM   2092 N  N   . LEU   A 1 271 ? -18.62464 -39.79290 10.76727  1.000 23.55136 ? 271 LEU   A N   1 
ATOM   2093 C  CA  . LEU   A 1 271 ? -19.25369 -39.32190 9.54000   1.000 24.16109 ? 271 LEU   A CA  1 
ATOM   2094 C  C   . LEU   A 1 271 ? -18.37855 -39.60964 8.32648   1.000 25.15356 ? 271 LEU   A C   1 
ATOM   2095 O  O   . LEU   A 1 271 ? -18.89161 -39.94853 7.25523   1.000 27.54161 ? 271 LEU   A O   1 
ATOM   2096 C  CB  . LEU   A 1 271 ? -19.53425 -37.82800 9.65943   1.000 23.60502 ? 271 LEU   A CB  1 
ATOM   2097 C  CG  . LEU   A 1 271 ? -20.71509 -37.46580 10.56328  1.000 20.86394 ? 271 LEU   A CG  1 
ATOM   2098 C  CD1 . LEU   A 1 271 ? -20.72332 -35.95844 10.81798  1.000 22.32025 ? 271 LEU   A CD1 1 
ATOM   2099 C  CD2 . LEU   A 1 271 ? -22.01996 -37.90322 9.93841   1.000 28.85860 ? 271 LEU   A CD2 1 
ATOM   2100 N  N   . LEU   A 1 272 ? -17.05768 -39.50804 8.48583   1.000 24.33945 ? 272 LEU   A N   1 
ATOM   2101 C  CA  . LEU   A 1 272 ? -16.15107 -39.77540 7.37756   1.000 24.46712 ? 272 LEU   A CA  1 
ATOM   2102 C  C   . LEU   A 1 272 ? -16.10348 -41.26356 7.04947   1.000 27.63896 ? 272 LEU   A C   1 
ATOM   2103 O  O   . LEU   A 1 272 ? -16.04341 -41.63923 5.87153   1.000 26.65836 ? 272 LEU   A O   1 
ATOM   2104 C  CB  . LEU   A 1 272 ? -14.75606 -39.25557 7.71587   1.000 25.75577 ? 272 LEU   A CB  1 
ATOM   2105 C  CG  . LEU   A 1 272 ? -14.62473 -37.73663 7.72383   1.000 23.15140 ? 272 LEU   A CG  1 
ATOM   2106 C  CD1 . LEU   A 1 272 ? -13.26436 -37.31113 8.29570   1.000 25.16100 ? 272 LEU   A CD1 1 
ATOM   2107 C  CD2 . LEU   A 1 272 ? -14.84920 -37.15721 6.32951   1.000 21.51229 ? 272 LEU   A CD2 1 
ATOM   2108 N  N   . GLN   A 1 273 ? -16.13591 -42.12605 8.07266   1.000 29.39769 ? 273 GLN   A N   1 
ATOM   2109 C  CA  . GLN   A 1 273 ? -16.06369 -43.56522 7.81433   1.000 30.09208 ? 273 GLN   A CA  1 
ATOM   2110 C  C   . GLN   A 1 273 ? -17.40853 -44.14692 7.39199   1.000 30.25154 ? 273 GLN   A C   1 
ATOM   2111 O  O   . GLN   A 1 273 ? -17.44268 -45.14200 6.66024   1.000 33.20499 ? 273 GLN   A O   1 
ATOM   2112 C  CB  . GLN   A 1 273 ? -15.53844 -44.33071 9.03371   1.000 31.48660 ? 273 GLN   A CB  1 
ATOM   2113 C  CG  . GLN   A 1 273 ? -14.04440 -44.17187 9.31358   1.000 30.61851 ? 273 GLN   A CG  1 
ATOM   2114 C  CD  . GLN   A 1 273 ? -13.68905 -44.22457 10.79795  1.000 32.45616 ? 273 GLN   A CD  1 
ATOM   2115 O  OE1 . GLN   A 1 273 ? -12.51147 -44.22214 11.16181  1.000 35.06759 ? 273 GLN   A OE1 1 
ATOM   2116 N  NE2 . GLN   A 1 273 ? -14.70187 -44.31527 11.65570  1.000 34.86487 ? 273 GLN   A NE2 1 
ATOM   2117 N  N   . ASN   A 1 274 ? -18.52007 -43.53941 7.80963   1.000 31.18215 ? 274 ASN   A N   1 
ATOM   2118 C  CA  . ASN   A 1 274 ? -19.83698 -44.10968 7.58126   1.000 32.14495 ? 274 ASN   A CA  1 
ATOM   2119 C  C   . ASN   A 1 274 ? -20.69484 -43.30987 6.61737   1.000 32.78825 ? 274 ASN   A C   1 
ATOM   2120 O  O   . ASN   A 1 274 ? -21.76274 -43.78861 6.22146   1.000 35.76061 ? 274 ASN   A O   1 
ATOM   2121 C  CB  . ASN   A 1 274 ? -20.58786 -44.24192 8.91311   1.000 35.12722 ? 274 ASN   A CB  1 
ATOM   2122 C  CG  . ASN   A 1 274 ? -19.92346 -45.21614 9.84933   1.000 37.29455 ? 274 ASN   A CG  1 
ATOM   2123 O  OD1 . ASN   A 1 274 ? -19.34377 -46.21421 9.41473   1.000 38.52260 ? 274 ASN   A OD1 1 
ATOM   2124 N  ND2 . ASN   A 1 274 ? -20.01722 -44.94573 11.14956  1.000 39.07300 ? 274 ASN   A ND2 1 
ATOM   2125 N  N   . GLY   A 1 275 ? -20.26706 -42.12482 6.22706   1.000 32.80693 ? 275 GLY   A N   1 
ATOM   2126 C  CA  . GLY   A 1 275 ? -21.19178 -41.30315 5.49578   1.000 34.99235 ? 275 GLY   A CA  1 
ATOM   2127 C  C   . GLY   A 1 275 ? -22.33852 -40.87868 6.39941   1.000 34.70898 ? 275 GLY   A C   1 
ATOM   2128 O  O   . GLY   A 1 275 ? -22.29072 -40.97562 7.62932   1.000 32.17207 ? 275 GLY   A O   1 
ATOM   2129 N  N   . MET   A 1 276 ? -23.40382 -40.42383 5.76004   1.000 37.32024 ? 276 MET   A N   1 
ATOM   2130 C  CA  . MET   A 1 276 ? -24.46135 -39.74507 6.47799   1.000 36.58886 ? 276 MET   A CA  1 
ATOM   2131 C  C   . MET   A 1 276 ? -25.74557 -40.56323 6.48512   1.000 39.75817 ? 276 MET   A C   1 
ATOM   2132 O  O   . MET   A 1 276 ? -26.70585 -40.19422 7.17330   1.000 38.32570 ? 276 MET   A O   1 
ATOM   2133 C  CB  . MET   A 1 276 ? -24.63992 -38.35893 5.84579   1.000 37.60811 ? 276 MET   A CB  1 
ATOM   2134 C  CG  . MET   A 1 276 ? -23.80822 -37.32986 6.60617   1.000 31.08101 ? 276 MET   A CG  1 
ATOM   2135 S  SD  . MET   A 1 276 ? -23.93738 -35.60668 6.14955   1.000 41.71112 ? 276 MET   A SD  1 
ATOM   2136 C  CE  . MET   A 1 276 ? -25.67913 -35.39532 6.17609   1.000 28.70560 ? 276 MET   A CE  1 
ATOM   2137 N  N   . ASN   A 1 277 ? -25.75013 -41.69512 5.77438   1.000 41.57903 ? 277 ASN   A N   1 
ATOM   2138 C  CA  . ASN   A 1 277 ? -26.80214 -42.70830 5.84060   1.000 41.54445 ? 277 ASN   A CA  1 
ATOM   2139 C  C   . ASN   A 1 277 ? -28.17366 -42.11341 5.54508   1.000 39.19694 ? 277 ASN   A C   1 
ATOM   2140 O  O   . ASN   A 1 277 ? -29.15476 -42.38914 6.24109   1.000 42.82473 ? 277 ASN   A O   1 
ATOM   2141 C  CB  . ASN   A 1 277 ? -26.80027 -43.42807 7.18850   1.000 42.80664 ? 277 ASN   A CB  1 
ATOM   2142 C  CG  . ASN   A 1 277 ? -27.52777 -44.75517 7.13316   1.000 48.46604 ? 277 ASN   A CG  1 
ATOM   2143 O  OD1 . ASN   A 1 277 ? -28.10629 -45.11706 6.10617   1.000 51.33826 ? 277 ASN   A OD1 1 
ATOM   2144 N  ND2 . ASN   A 1 277 ? -27.50944 -45.48715 8.23936   1.000 50.77354 ? 277 ASN   A ND2 1 
ATOM   2145 N  N   . GLY   A 1 278 ? -28.24012 -41.29761 4.49859   1.000 37.34576 ? 278 GLY   A N   1 
ATOM   2146 C  CA  . GLY   A 1 278 ? -29.50056 -40.74610 4.05682   1.000 36.39153 ? 278 GLY   A CA  1 
ATOM   2147 C  C   . GLY   A 1 278 ? -30.07265 -39.65526 4.92868   1.000 35.46298 ? 278 GLY   A C   1 
ATOM   2148 O  O   . GLY   A 1 278 ? -31.23746 -39.28727 4.74453   1.000 35.31655 ? 278 GLY   A O   1 
ATOM   2149 N  N   . ARG   A 1 279 ? -29.29903 -39.12397 5.86797   1.000 34.73808 ? 279 ARG   A N   1 
ATOM   2150 C  CA  . ARG   A 1 279 ? -29.74925 -38.03133 6.70815   1.000 31.20157 ? 279 ARG   A CA  1 
ATOM   2151 C  C   . ARG   A 1 279 ? -29.09199 -36.74400 6.23441   1.000 29.76818 ? 279 ARG   A C   1 
ATOM   2152 O  O   . ARG   A 1 279 ? -28.27686 -36.73898 5.31135   1.000 29.52397 ? 279 ARG   A O   1 
ATOM   2153 C  CB  . ARG   A 1 279 ? -29.43380 -38.32203 8.17413   1.000 31.95728 ? 279 ARG   A CB  1 
ATOM   2154 C  CG  . ARG   A 1 279 ? -30.24607 -39.46632 8.72273   1.000 34.31424 ? 279 ARG   A CG  1 
ATOM   2155 C  CD  . ARG   A 1 279 ? -29.73214 -39.90454 10.06820  1.000 32.88314 ? 279 ARG   A CD  1 
ATOM   2156 N  NE  . ARG   A 1 279 ? -28.53447 -40.72248 9.92841   1.000 37.26049 ? 279 ARG   A NE  1 
ATOM   2157 C  CZ  . ARG   A 1 279 ? -27.98729 -41.42238 10.91228  1.000 34.27084 ? 279 ARG   A CZ  1 
ATOM   2158 N  NH1 . ARG   A 1 279 ? -28.58158 -41.53689 12.09109  1.000 33.70553 ? 279 ARG   A NH1 1 
ATOM   2159 N  NH2 . ARG   A 1 279 ? -26.81334 -42.01606 10.70970  1.000 33.69575 ? 279 ARG   A NH2 1 
ATOM   2160 N  N   . THR   A 1 280 ? -29.47516 -35.63260 6.85325   1.000 29.25517 ? 280 THR   A N   1 
ATOM   2161 C  CA  . THR   A 1 280 ? -28.92891 -34.33355 6.50493   1.000 24.73759 ? 280 THR   A CA  1 
ATOM   2162 C  C   . THR   A 1 280 ? -28.52703 -33.59842 7.77487   1.000 24.00721 ? 280 THR   A C   1 
ATOM   2163 O  O   . THR   A 1 280 ? -28.98882 -33.91231 8.87805   1.000 23.55997 ? 280 THR   A O   1 
ATOM   2164 C  CB  . THR   A 1 280 ? -29.92512 -33.49077 5.69447   1.000 26.04930 ? 280 THR   A CB  1 
ATOM   2165 O  OG1 . THR   A 1 280 ? -31.10795 -33.26526 6.46518   1.000 24.84876 ? 280 THR   A OG1 1 
ATOM   2166 C  CG2 . THR   A 1 280 ? -30.31983 -34.23039 4.42079   1.000 25.34928 ? 280 THR   A CG2 1 
ATOM   2167 N  N   . ILE   A 1 281 ? -27.64068 -32.62705 7.59580   1.000 22.64007 ? 281 ILE   A N   1 
ATOM   2168 C  CA  . ILE   A 1 281 ? -27.18253 -31.72557 8.64624   1.000 19.40201 ? 281 ILE   A CA  1 
ATOM   2169 C  C   . ILE   A 1 281 ? -27.35183 -30.31611 8.11678   1.000 20.34634 ? 281 ILE   A C   1 
ATOM   2170 O  O   . ILE   A 1 281 ? -26.78402 -29.97526 7.07316   1.000 19.12559 ? 281 ILE   A O   1 
ATOM   2171 C  CB  . ILE   A 1 281 ? -25.71673 -31.97731 9.04235   1.000 18.81136 ? 281 ILE   A CB  1 
ATOM   2172 C  CG1 . ILE   A 1 281 ? -25.51082 -33.41419 9.51701   1.000 19.44971 ? 281 ILE   A CG1 1 
ATOM   2173 C  CG2 . ILE   A 1 281 ? -25.27105 -30.96922 10.09944  1.000 15.78709 ? 281 ILE   A CG2 1 
ATOM   2174 C  CD1 . ILE   A 1 281 ? -24.09641 -33.72609 9.98027   1.000 18.74101 ? 281 ILE   A CD1 1 
ATOM   2175 N  N   . LEU   A 1 282 ? -28.11401 -29.49659 8.84096   1.000 20.41821 ? 282 LEU   A N   1 
ATOM   2176 C  CA  . LEU   A 1 282 ? -28.40541 -28.11401 8.43668   1.000 21.96857 ? 282 LEU   A CA  1 
ATOM   2177 C  C   . LEU   A 1 282 ? -28.79038 -28.04781 6.96125   1.000 21.93402 ? 282 LEU   A C   1 
ATOM   2178 O  O   . LEU   A 1 282 ? -28.31039 -27.19338 6.20146   1.000 22.19366 ? 282 LEU   A O   1 
ATOM   2179 C  CB  . LEU   A 1 282 ? -27.23408 -27.17669 8.74663   1.000 19.55464 ? 282 LEU   A CB  1 
ATOM   2180 C  CG  . LEU   A 1 282 ? -27.06646 -26.85929 10.23565  1.000 18.20120 ? 282 LEU   A CG  1 
ATOM   2181 C  CD1 . LEU   A 1 282 ? -25.80208 -26.04482 10.48932  1.000 16.81091 ? 282 LEU   A CD1 1 
ATOM   2182 C  CD2 . LEU   A 1 282 ? -28.29801 -26.20529 10.86007  1.000 16.31249 ? 282 LEU   A CD2 1 
ATOM   2183 N  N   . GLY   A 1 283 ? -29.64001 -28.99268 6.55083   1.000 20.86602 ? 283 GLY   A N   1 
ATOM   2184 C  CA  . GLY   A 1 283 ? -30.13766 -29.03215 5.18980   1.000 22.94487 ? 283 GLY   A CA  1 
ATOM   2185 C  C   . GLY   A 1 283 ? -29.09601 -29.36335 4.14760   1.000 22.86550 ? 283 GLY   A C   1 
ATOM   2186 O  O   . GLY   A 1 283 ? -29.30433 -29.07756 2.96748   1.000 23.74642 ? 283 GLY   A O   1 
ATOM   2187 N  N   . SER   A 1 284 ? -27.96462 -29.94159 4.55206   1.000 21.57839 ? 284 SER   A N   1 
ATOM   2188 C  CA  . SER   A 1 284 ? -26.93481 -30.40652 3.63045   1.000 20.28611 ? 284 SER   A CA  1 
ATOM   2189 C  C   . SER   A 1 284 ? -26.75073 -31.90952 3.78535   1.000 21.29371 ? 284 SER   A C   1 
ATOM   2190 O  O   . SER   A 1 284 ? -26.86612 -32.44816 4.89023   1.000 21.19374 ? 284 SER   A O   1 
ATOM   2191 C  CB  . SER   A 1 284 ? -25.59834 -29.68431 3.87787   1.000 19.28115 ? 284 SER   A CB  1 
ATOM   2192 O  OG  . SER   A 1 284 ? -24.58986 -30.15136 2.99670   1.000 16.52483 ? 284 SER   A OG  1 
ATOM   2193 N  N   . ALA   A 1 285 ? -26.50110 -32.58863 2.66866   1.000 20.87041 ? 285 ALA   A N   1 
ATOM   2194 C  CA  . ALA   A 1 285 ? -26.10754 -33.98662 2.67068   1.000 20.55186 ? 285 ALA   A CA  1 
ATOM   2195 C  C   . ALA   A 1 285 ? -24.60224 -34.16272 2.49147   1.000 21.49638 ? 285 ALA   A C   1 
ATOM   2196 O  O   . ALA   A 1 285 ? -24.13562 -35.29257 2.31964   1.000 25.68823 ? 285 ALA   A O   1 
ATOM   2197 C  CB  . ALA   A 1 285 ? -26.85502 -34.74801 1.58084   1.000 22.87090 ? 285 ALA   A CB  1 
ATOM   2198 N  N   . LEU   A 1 286 ? -23.84935 -33.06273 2.50823   1.000 18.38629 ? 286 LEU   A N   1 
ATOM   2199 C  CA  . LEU   A 1 286 ? -22.39045 -33.03066 2.51153   1.000 24.32380 ? 286 LEU   A CA  1 
ATOM   2200 C  C   . LEU   A 1 286 ? -21.88110 -32.34859 3.76880   1.000 19.03809 ? 286 LEU   A C   1 
ATOM   2201 O  O   . LEU   A 1 286 ? -22.54462 -31.46747 4.32530   1.000 19.17692 ? 286 LEU   A O   1 
ATOM   2202 C  CB  . LEU   A 1 286 ? -21.84501 -32.26671 1.29130   1.000 20.18780 ? 286 LEU   A CB  1 
ATOM   2203 C  CG  . LEU   A 1 286 ? -22.23305 -32.86269 -0.04052  1.000 21.21587 ? 286 LEU   A CG  1 
ATOM   2204 C  CD1 . LEU   A 1 286 ? -21.38119 -32.26866 -1.13208  1.000 19.28048 ? 286 LEU   A CD1 1 
ATOM   2205 C  CD2 . LEU   A 1 286 ? -21.89244 -34.34727 0.11847   1.000 22.46875 ? 286 LEU   A CD2 1 
ATOM   2206 N  N   . LEU   A 1 287 ? -20.68215 -32.73523 4.19669   1.000 19.65110 ? 287 LEU   A N   1 
ATOM   2207 C  CA  . LEU   A 1 287 ? -20.00564 -32.00814 5.26578   1.000 15.12311 ? 287 LEU   A CA  1 
ATOM   2208 C  C   . LEU   A 1 287 ? -19.50302 -30.68286 4.71625   1.000 17.26995 ? 287 LEU   A C   1 
ATOM   2209 O  O   . LEU   A 1 287 ? -18.68339 -30.64933 3.79396   1.000 17.68437 ? 287 LEU   A O   1 
ATOM   2210 C  CB  . LEU   A 1 287 ? -18.86485 -32.84264 5.85070   1.000 16.79992 ? 287 LEU   A CB  1 
ATOM   2211 C  CG  . LEU   A 1 287 ? -19.36004 -34.22341 6.30736   1.000 17.09774 ? 287 LEU   A CG  1 
ATOM   2212 C  CD1 . LEU   A 1 287 ? -18.21214 -35.14816 6.73382   1.000 20.77582 ? 287 LEU   A CD1 1 
ATOM   2213 C  CD2 . LEU   A 1 287 ? -20.42575 -34.13097 7.40432   1.000 18.61646 ? 287 LEU   A CD2 1 
ATOM   2214 N  N   . GLU   A 1 288 ? -20.00195 -29.58938 5.27307   1.000 14.08278 ? 288 GLU   A N   1 
ATOM   2215 C  CA  . GLU   A 1 288 ? -19.76180 -28.27507 4.71967   1.000 15.73676 ? 288 GLU   A CA  1 
ATOM   2216 C  C   . GLU   A 1 288 ? -18.57674 -27.58656 5.38946   1.000 16.24661 ? 288 GLU   A C   1 
ATOM   2217 O  O   . GLU   A 1 288 ? -18.47830 -27.58588 6.62164   1.000 14.64635 ? 288 GLU   A O   1 
ATOM   2218 C  CB  . GLU   A 1 288 ? -21.03321 -27.44765 4.86163   1.000 18.16170 ? 288 GLU   A CB  1 
ATOM   2219 C  CG  . GLU   A 1 288 ? -20.73426 -26.01456 4.68891   1.000 20.60414 ? 288 GLU   A CG  1 
ATOM   2220 C  CD  . GLU   A 1 288 ? -20.93073 -25.57631 3.24982   1.000 24.62542 ? 288 GLU   A CD  1 
ATOM   2221 O  OE1 . GLU   A 1 288 ? -21.73794 -26.20965 2.50704   1.000 22.39331 ? 288 GLU   A OE1 1 
ATOM   2222 O  OE2 . GLU   A 1 288 ? -20.16338 -24.66936 2.84062   1.000 19.93844 ? 288 GLU   A OE2 1 
ATOM   2223 N  N   . ASP   A 1 289 ? -17.68234 -26.97971 4.57873   1.000 12.95319 ? 289 ASP   A N   1 
ATOM   2224 C  CA  . ASP   A 1 289 ? -16.43502 -26.42008 5.10730   1.000 16.46083 ? 289 ASP   A CA  1 
ATOM   2225 C  C   . ASP   A 1 289 ? -16.23541 -24.93459 4.78844   1.000 14.06488 ? 289 ASP   A C   1 
ATOM   2226 O  O   . ASP   A 1 289 ? -15.11481 -24.42216 4.93848   1.000 12.33228 ? 289 ASP   A O   1 
ATOM   2227 C  CB  . ASP   A 1 289 ? -15.22353 -27.23687 4.62809   1.000 14.79468 ? 289 ASP   A CB  1 
ATOM   2228 C  CG  . ASP   A 1 289 ? -14.77531 -26.90387 3.18857   1.000 13.89185 ? 289 ASP   A CG  1 
ATOM   2229 O  OD1 . ASP   A 1 289 ? -15.57161 -26.37210 2.38425   1.000 14.98208 ? 289 ASP   A OD1 1 
ATOM   2230 O  OD2 . ASP   A 1 289 ? -13.60937 -27.21613 2.87066   1.000 16.60835 ? 289 ASP   A OD2 1 
ATOM   2231 N  N   . GLU   A 1 290 ? -17.28453 -24.20181 4.39143   1.000 12.50215 ? 290 GLU   A N   1 
ATOM   2232 C  CA  . GLU   A 1 290 ? -17.08756 -22.78634 4.08335   1.000 12.74474 ? 290 GLU   A CA  1 
ATOM   2233 C  C   . GLU   A 1 290 ? -17.72736 -21.84699 5.11067   1.000 13.93672 ? 290 GLU   A C   1 
ATOM   2234 O  O   . GLU   A 1 290 ? -18.07317 -20.71370 4.77813   1.000 13.23383 ? 290 GLU   A O   1 
ATOM   2235 C  CB  . GLU   A 1 290 ? -17.53786 -22.46560 2.64818   1.000 16.30222 ? 290 GLU   A CB  1 
ATOM   2236 C  CG  . GLU   A 1 290 ? -16.65667 -23.22082 1.58686   1.000 16.06685 ? 290 GLU   A CG  1 
ATOM   2237 C  CD  . GLU   A 1 290 ? -16.50703 -22.54538 0.20786   1.000 19.62532 ? 290 GLU   A CD  1 
ATOM   2238 O  OE1 . GLU   A 1 290 ? -17.30003 -21.62814 -0.11375  1.000 14.41098 ? 290 GLU   A OE1 1 
ATOM   2239 O  OE2 . GLU   A 1 290 ? -15.61972 -23.00002 -0.58524  1.000 16.35833 ? 290 GLU   A OE2 1 
ATOM   2240 N  N   . PHE   A 1 291 ? -17.80760 -22.27038 6.38144   1.000 13.53453 ? 291 PHE   A N   1 
ATOM   2241 C  CA  . PHE   A 1 291 ? -18.12666 -21.38749 7.50705   1.000 12.92914 ? 291 PHE   A CA  1 
ATOM   2242 C  C   . PHE   A 1 291 ? -16.99298 -21.48110 8.52172   1.000 14.80680 ? 291 PHE   A C   1 
ATOM   2243 O  O   . PHE   A 1 291 ? -16.69614 -22.57536 9.02117   1.000 12.23405 ? 291 PHE   A O   1 
ATOM   2244 C  CB  . PHE   A 1 291 ? -19.43047 -21.77029 8.22412   1.000 14.23202 ? 291 PHE   A CB  1 
ATOM   2245 C  CG  . PHE   A 1 291 ? -20.65408 -21.71735 7.37435   1.000 15.07533 ? 291 PHE   A CG  1 
ATOM   2246 C  CD1 . PHE   A 1 291 ? -21.34345 -20.52799 7.18473   1.000 18.23505 ? 291 PHE   A CD1 1 
ATOM   2247 C  CD2 . PHE   A 1 291 ? -21.14258 -22.87180 6.78374   1.000 14.85910 ? 291 PHE   A CD2 1 
ATOM   2248 C  CE1 . PHE   A 1 291 ? -22.50597 -20.49869 6.40452   1.000 19.17111 ? 291 PHE   A CE1 1 
ATOM   2249 C  CE2 . PHE   A 1 291 ? -22.27997 -22.85022 6.00850   1.000 20.75632 ? 291 PHE   A CE2 1 
ATOM   2250 C  CZ  . PHE   A 1 291 ? -22.96839 -21.65758 5.81434   1.000 17.26884 ? 291 PHE   A CZ  1 
ATOM   2251 N  N   . THR   A 1 292 ? -16.38780 -20.34553 8.84955   1.000 13.51123 ? 292 THR   A N   1 
ATOM   2252 C  CA  . THR   A 1 292 ? -15.37454 -20.29011 9.89885   1.000 14.21645 ? 292 THR   A CA  1 
ATOM   2253 C  C   . THR   A 1 292 ? -16.03217 -20.35478 11.27422  1.000 15.08083 ? 292 THR   A C   1 
ATOM   2254 O  O   . THR   A 1 292 ? -17.24919 -20.17757 11.40973  1.000 15.26722 ? 292 THR   A O   1 
ATOM   2255 C  CB  . THR   A 1 292 ? -14.55244 -19.00555 9.78765   1.000 16.38735 ? 292 THR   A CB  1 
ATOM   2256 O  OG1 . THR   A 1 292 ? -15.35756 -17.88640 10.17900  1.000 16.27258 ? 292 THR   A OG1 1 
ATOM   2257 C  CG2 . THR   A 1 292 ? -13.99609 -18.80551 8.39877   1.000 12.67960 ? 292 THR   A CG2 1 
ATOM   2258 N  N   . PRO   A 1 293 ? -15.25275 -20.61484 12.32475  1.000 14.88027 ? 293 PRO   A N   1 
ATOM   2259 C  CA  . PRO   A 1 293 ? -15.81154 -20.46617 13.67857  1.000 16.66635 ? 293 PRO   A CA  1 
ATOM   2260 C  C   . PRO   A 1 293 ? -16.36061 -19.07086 13.93211  1.000 17.12609 ? 293 PRO   A C   1 
ATOM   2261 O  O   . PRO   A 1 293 ? -17.40414 -18.92593 14.57357  1.000 19.29138 ? 293 PRO   A O   1 
ATOM   2262 C  CB  . PRO   A 1 293 ? -14.61878 -20.81581 14.57666  1.000 16.09960 ? 293 PRO   A CB  1 
ATOM   2263 C  CG  . PRO   A 1 293 ? -13.83468 -21.79025 13.76838  1.000 14.60849 ? 293 PRO   A CG  1 
ATOM   2264 C  CD  . PRO   A 1 293 ? -13.93948 -21.29390 12.34248  1.000 15.38180 ? 293 PRO   A CD  1 
ATOM   2265 N  N   . PHE   A 1 294 ? -15.70303 -18.04005 13.39222  1.000 18.41500 ? 294 PHE   A N   1 
ATOM   2266 C  CA  . PHE   A 1 294 ? -16.22744 -16.67409 13.45999  1.000 18.97355 ? 294 PHE   A CA  1 
ATOM   2267 C  C   . PHE   A 1 294 ? -17.61319 -16.55669 12.84257  1.000 19.69228 ? 294 PHE   A C   1 
ATOM   2268 O  O   . PHE   A 1 294 ? -18.49363 -15.88897 13.40174  1.000 18.42235 ? 294 PHE   A O   1 
ATOM   2269 C  CB  . PHE   A 1 294 ? -15.26700 -15.70244 12.75851  1.000 19.18811 ? 294 PHE   A CB  1 
ATOM   2270 C  CG  . PHE   A 1 294 ? -15.69766 -14.24427 12.85734  1.000 26.22824 ? 294 PHE   A CG  1 
ATOM   2271 C  CD1 . PHE   A 1 294 ? -16.65546 -13.72966 11.97918  1.000 28.81590 ? 294 PHE   A CD1 1 
ATOM   2272 C  CD2 . PHE   A 1 294 ? -15.17502 -13.40774 13.82587  1.000 29.07965 ? 294 PHE   A CD2 1 
ATOM   2273 C  CE1 . PHE   A 1 294 ? -17.07270 -12.40190 12.06582  1.000 29.21670 ? 294 PHE   A CE1 1 
ATOM   2274 C  CE2 . PHE   A 1 294 ? -15.59038 -12.08106 13.91354  1.000 33.00643 ? 294 PHE   A CE2 1 
ATOM   2275 C  CZ  . PHE   A 1 294 ? -16.53868 -11.58484 13.03382  1.000 27.93535 ? 294 PHE   A CZ  1 
ATOM   2276 N  N   . ASP   A 1 295 ? -17.80004 -17.14410 11.65280  1.000 17.64064 ? 295 ASP   A N   1 
ATOM   2277 C  CA  . ASP   A 1 295 ? -19.08808 -17.08588 10.96700  1.000 17.32642 ? 295 ASP   A CA  1 
ATOM   2278 C  C   . ASP   A 1 295 ? -20.18975 -17.72690 11.79844  1.000 19.33678 ? 295 ASP   A C   1 
ATOM   2279 O  O   . ASP   A 1 295 ? -21.30671 -17.20504 11.86816  1.000 18.96577 ? 295 ASP   A O   1 
ATOM   2280 C  CB  . ASP   A 1 295 ? -19.00004 -17.78935 9.61211   1.000 16.22680 ? 295 ASP   A CB  1 
ATOM   2281 C  CG  . ASP   A 1 295 ? -18.05550 -17.10703 8.65501   1.000 17.70672 ? 295 ASP   A CG  1 
ATOM   2282 O  OD1 . ASP   A 1 295 ? -17.72477 -15.92564 8.88863   1.000 18.18974 ? 295 ASP   A OD1 1 
ATOM   2283 O  OD2 . ASP   A 1 295 ? -17.63002 -17.77266 7.68029   1.000 15.09633 ? 295 ASP   A OD2 1 
ATOM   2284 N  N   . VAL   A 1 296 ? -19.90193 -18.87283 12.41638  1.000 16.58947 ? 296 VAL   A N   1 
ATOM   2285 C  CA  . VAL   A 1 296 ? -20.90945 -19.55624 13.22189  1.000 16.31241 ? 296 VAL   A CA  1 
ATOM   2286 C  C   . VAL   A 1 296 ? -21.30080 -18.69112 14.41492  1.000 21.04348 ? 296 VAL   A C   1 
ATOM   2287 O  O   . VAL   A 1 296 ? -22.48606 -18.51169 14.71067  1.000 21.47597 ? 296 VAL   A O   1 
ATOM   2288 C  CB  . VAL   A 1 296 ? -20.39829 -20.94329 13.65236  1.000 16.00270 ? 296 VAL   A CB  1 
ATOM   2289 C  CG1 . VAL   A 1 296 ? -21.37105 -21.61561 14.61536  1.000 15.53683 ? 296 VAL   A CG1 1 
ATOM   2290 C  CG2 . VAL   A 1 296 ? -20.18817 -21.82589 12.43145  1.000 14.26565 ? 296 VAL   A CG2 1 
ATOM   2291 N  N   . VAL   A 1 297 ? -20.31208 -18.10389 15.09168  1.000 20.78035 ? 297 VAL   A N   1 
ATOM   2292 C  CA  . VAL   A 1 297 ? -20.61661 -17.29673 16.27236  1.000 22.42661 ? 297 VAL   A CA  1 
ATOM   2293 C  C   . VAL   A 1 297 ? -21.40335 -16.04278 15.88485  1.000 24.45863 ? 297 VAL   A C   1 
ATOM   2294 O  O   . VAL   A 1 297 ? -22.34106 -15.64749 16.58322  1.000 26.06396 ? 297 VAL   A O   1 
ATOM   2295 C  CB  . VAL   A 1 297 ? -19.32321 -16.93766 17.02875  1.000 20.68392 ? 297 VAL   A CB  1 
ATOM   2296 C  CG1 . VAL   A 1 297 ? -19.63286 -15.97296 18.16148  1.000 21.85483 ? 297 VAL   A CG1 1 
ATOM   2297 C  CG2 . VAL   A 1 297 ? -18.62305 -18.17876 17.55502  1.000 24.09857 ? 297 VAL   A CG2 1 
ATOM   2298 N  N   . ARG   A 1 298 ? -21.02728 -15.39014 14.77548  1.000 22.45188 ? 298 ARG   A N   1 
ATOM   2299 C  CA  . ARG   A 1 298 ? -21.73840 -14.19201 14.33581  1.000 27.45446 ? 298 ARG   A CA  1 
ATOM   2300 C  C   . ARG   A 1 298 ? -23.19976 -14.50598 14.04158  1.000 27.95098 ? 298 ARG   A C   1 
ATOM   2301 O  O   . ARG   A 1 298 ? -24.10159 -13.77744 14.46676  1.000 32.57042 ? 298 ARG   A O   1 
ATOM   2302 C  CB  . ARG   A 1 298 ? -21.06548 -13.57893 13.09211  1.000 25.39931 ? 298 ARG   A CB  1 
ATOM   2303 C  CG  . ARG   A 1 298 ? -22.07221 -12.81410 12.18056  1.000 32.34951 ? 298 ARG   A CG  1 
ATOM   2304 C  CD  . ARG   A 1 298 ? -21.47963 -11.93566 11.04174  1.000 33.72848 ? 298 ARG   A CD  1 
ATOM   2305 N  NE  . ARG   A 1 298 ? -21.15487 -12.67085 9.81719   1.000 31.14372 ? 298 ARG   A NE  1 
ATOM   2306 C  CZ  . ARG   A 1 298 ? -21.67458 -12.42735 8.61412   1.000 25.64883 ? 298 ARG   A CZ  1 
ATOM   2307 N  NH1 . ARG   A 1 298 ? -22.59624 -11.48429 8.42061   1.000 24.24602 ? 298 ARG   A NH1 1 
ATOM   2308 N  NH2 . ARG   A 1 298 ? -21.27118 -13.15333 7.57662   1.000 23.41951 ? 298 ARG   A NH2 1 
ATOM   2309 N  N   . GLN   A 1 299 ? -23.45161 -15.59655 13.31765  1.000 23.61971 ? 299 GLN   A N   1 
ATOM   2310 C  CA  . GLN   A 1 299 ? -24.81148 -15.92140 12.91069  1.000 25.55262 ? 299 GLN   A CA  1 
ATOM   2311 C  C   . GLN   A 1 299 ? -25.61455 -16.54265 14.04377  1.000 27.78380 ? 299 GLN   A C   1 
ATOM   2312 O  O   . GLN   A 1 299 ? -26.78721 -16.20378 14.22225  1.000 32.42655 ? 299 GLN   A O   1 
ATOM   2313 C  CB  . GLN   A 1 299 ? -24.79351 -16.85589 11.70122  1.000 24.08112 ? 299 GLN   A CB  1 
ATOM   2314 C  CG  . GLN   A 1 299 ? -26.12887 -16.93089 11.01107  1.000 20.71988 ? 299 GLN   A CG  1 
ATOM   2315 C  CD  . GLN   A 1 299 ? -26.06022 -17.62225 9.68039   1.000 18.84420 ? 299 GLN   A CD  1 
ATOM   2316 O  OE1 . GLN   A 1 299 ? -27.06081 -18.16097 9.21025   1.000 19.86735 ? 299 GLN   A OE1 1 
ATOM   2317 N  NE2 . GLN   A 1 299 ? -24.87628 -17.65185 9.07564   1.000 18.83222 ? 299 GLN   A NE2 1 
ATOM   2318 N  N   . CYS   A 1 300 ? -25.02422 -17.45737 14.81337  1.000 28.32939 ? 300 CYS   A N   1 
ATOM   2319 C  CA  . CYS   A 1 300 ? -25.71823 -18.04663 15.95521  1.000 29.92981 ? 300 CYS   A CA  1 
ATOM   2320 C  C   . CYS   A 1 300 ? -25.66508 -17.15830 17.22805  1.000 34.67350 ? 300 CYS   A C   1 
ATOM   2321 O  O   . CYS   A 1 300 ? -25.92923 -17.66533 18.32506  1.000 41.52866 ? 300 CYS   A O   1 
ATOM   2322 C  CB  . CYS   A 1 300 ? -25.15977 -19.44652 16.25586  1.000 27.72873 ? 300 CYS   A CB  1 
ATOM   2323 S  SG  . CYS   A 1 300 ? -25.19518 -20.64857 14.86724  1.000 27.48914 ? 300 CYS   A SG  1 
ATOM   2324 N  N   . SER   A 1 301 ? -25.34000 -15.86269 17.10366  1.000 36.81511 ? 301 SER   A N   1 
ATOM   2325 C  CA  . SER   A 1 301 ? -25.35309 -14.92539 18.22986  1.000 40.19939 ? 301 SER   A CA  1 
ATOM   2326 C  C   . SER   A 1 301 ? -25.90996 -13.56186 17.80477  1.000 43.14288 ? 301 SER   A C   1 
ATOM   2327 O  O   . SER   A 1 301 ? -26.72304 -12.97042 18.52828  1.000 44.03809 ? 301 SER   A O   1 
ATOM   2328 C  CB  . SER   A 1 301 ? -23.95081 -14.78571 18.83802  1.000 41.66591 ? 301 SER   A CB  1 
ATOM   2329 O  OG  . SER   A 1 301 ? -23.83293 -13.63207 19.65474  1.000 50.48543 ? 301 SER   A OG  1 
ATOM   2330 N  N   . GLY   A 1 302 ? -25.48443 -13.04759 16.64378  1.000 43.16149 ? 302 GLY   A N   1 
ATOM   2331 C  CA  . GLY   A 1 302 ? -26.22546 -11.98341 15.97523  1.000 44.48931 ? 302 GLY   A CA  1 
ATOM   2332 C  C   . GLY   A 1 302 ? -25.59273 -10.60972 15.82666  1.000 47.46981 ? 302 GLY   A C   1 
ATOM   2333 O  O   . GLY   A 1 302 ? -26.28730 -9.59443  15.95836  1.000 45.18225 ? 302 GLY   A O   1 
ATOM   2334 N  N   . VAL   A 1 303 ? -24.29664 -10.55558 15.51244  1.000 49.80327 ? 303 VAL   A N   1 
ATOM   2335 C  CA  . VAL   A 1 303 ? -23.55896 -9.29256  15.48528  1.000 53.29209 ? 303 VAL   A CA  1 
ATOM   2336 C  C   . VAL   A 1 303 ? -23.90912 -8.51554  14.21789  1.000 51.48101 ? 303 VAL   A C   1 
ATOM   2337 O  O   . VAL   A 1 303 ? -24.01316 -9.08889  13.12385  1.000 48.10038 ? 303 VAL   A O   1 
ATOM   2338 C  CB  . VAL   A 1 303 ? -22.03910 -9.55203  15.59149  1.000 52.02128 ? 303 VAL   A CB  1 
ATOM   2339 C  CG1 . VAL   A 1 303 ? -21.23351 -8.25794  15.39933  1.000 56.19560 ? 303 VAL   A CG1 1 
ATOM   2340 C  CG2 . VAL   A 1 303 ? -21.68719 -10.20978 16.92714  1.000 50.91213 ? 303 VAL   A CG2 1 
ATOM   2341 N  N   . THR   A 1 304 ? -24.08132 -7.19540  14.36394  1.000 52.26710 ? 304 THR   A N   1 
ATOM   2342 C  CA  . THR   A 1 304 ? -24.42080 -6.27370  13.28251  1.000 46.28323 ? 304 THR   A CA  1 
ATOM   2343 C  C   . THR   A 1 304 ? -23.22765 -5.38120  12.94342  1.000 52.91836 ? 304 THR   A C   1 
ATOM   2344 O  O   . THR   A 1 304 ? -22.14550 -5.48287  13.53663  1.000 54.23655 ? 304 THR   A O   1 
ATOM   2345 C  CB  . THR   A 1 304 ? -25.64098 -5.41899  13.65148  1.000 41.74186 ? 304 THR   A CB  1 
ATOM   2346 O  OG1 . THR   A 1 304 ? -25.46558 -4.84941  14.95897  1.000 47.99694 ? 304 THR   A OG1 1 
ATOM   2347 C  CG2 . THR   A 1 304 ? -26.90622 -6.24627  13.62649  1.000 29.60347 ? 304 THR   A CG2 1 
ATOM   2348 N  N   . PHE   A 1 305 ? -23.44098 -4.48993  11.97183  1.000 51.78698 ? 305 PHE   A N   1 
ATOM   2349 C  CA  . PHE   A 1 305 ? -22.38315 -3.62736  11.45046  1.000 54.94203 ? 305 PHE   A CA  1 
ATOM   2350 C  C   . PHE   A 1 305 ? -22.98191 -2.28135  11.06640  1.000 55.38770 ? 305 PHE   A C   1 
ATOM   2351 O  O   . PHE   A 1 305 ? -24.05873 -2.22692  10.46278  1.000 54.73144 ? 305 PHE   A O   1 
ATOM   2352 C  CB  . PHE   A 1 305 ? -21.68011 -4.29302  10.25122  1.000 51.03332 ? 305 PHE   A CB  1 
ATOM   2353 C  CG  . PHE   A 1 305 ? -21.36324 -5.74165  10.48965  1.000 49.35522 ? 305 PHE   A CG  1 
ATOM   2354 C  CD1 . PHE   A 1 305 ? -20.20741 -6.10389  11.17537  1.000 47.91306 ? 305 PHE   A CD1 1 
ATOM   2355 C  CD2 . PHE   A 1 305 ? -22.26666 -6.73544  10.11745  1.000 47.96189 ? 305 PHE   A CD2 1 
ATOM   2356 C  CE1 . PHE   A 1 305 ? -19.92628 -7.43217  11.44056  1.000 47.82046 ? 305 PHE   A CE1 1 
ATOM   2357 C  CE2 . PHE   A 1 305 ? -22.00079 -8.07136  10.38385  1.000 47.23979 ? 305 PHE   A CE2 1 
ATOM   2358 C  CZ  . PHE   A 1 305 ? -20.82548 -8.41989  11.05284  1.000 48.85773 ? 305 PHE   A CZ  1 
ATOM   2359 N  N   . GLN   A 1 306 ? -22.29565 -1.20275  11.43404  1.000 56.15638 ? 306 GLN   A N   1 
ATOM   2360 C  CA  . GLN   A 1 306 ? -22.79527 0.14079   11.16150  1.000 56.72393 ? 306 GLN   A CA  1 
ATOM   2361 C  C   . GLN   A 1 306 ? -21.67159 1.07564   10.71974  1.000 53.19244 ? 306 GLN   A C   1 
ATOM   2362 O  O   . GLN   A 1 306 ? -21.38519 1.19318   9.52571   1.000 49.88825 ? 306 GLN   A O   1 
ATOM   2363 C  CB  . GLN   A 1 306 ? -23.50250 0.70604   12.39576  1.000 58.10465 ? 306 GLN   A CB  1 
ATOM   2364 C  CG  . GLN   A 1 306 ? -24.45329 1.85891   12.09775  1.000 60.72857 ? 306 GLN   A CG  1 
ATOM   2365 C  CD  . GLN   A 1 306 ? -25.33360 2.19597   13.28484  1.000 62.07311 ? 306 GLN   A CD  1 
ATOM   2366 O  OE1 . GLN   A 1 306 ? -25.09163 1.72011   14.39620  1.000 67.77154 ? 306 GLN   A OE1 1 
ATOM   2367 N  NE2 . GLN   A 1 306 ? -26.35139 3.03006   13.06353  1.000 56.66674 ? 306 GLN   A NE2 1 
HETATM 2368 N  N1  . A1AR9 B 2 .   ? -13.07932 -12.34019 -17.22140 1.000 29.60071 ? 401 A1AR9 A N1  1 
HETATM 2369 C  C4  . A1AR9 B 2 .   ? -12.85429 -9.82431  -17.18347 1.000 28.23602 ? 401 A1AR9 A C4  1 
HETATM 2370 C  C5  . A1AR9 B 2 .   ? -10.71789 -12.87748 -17.88528 1.000 28.92231 ? 401 A1AR9 A C5  1 
HETATM 2371 C  C6  . A1AR9 B 2 .   ? -9.75106  -13.11416 -18.88610 1.000 31.97842 ? 401 A1AR9 A C6  1 
HETATM 2372 C  C7  . A1AR9 B 2 .   ? -10.11887 -13.03604 -20.23448 1.000 33.10613 ? 401 A1AR9 A C7  1 
HETATM 2373 C  C8  . A1AR9 B 2 .   ? -11.43227 -12.73668 -20.58106 1.000 33.52949 ? 401 A1AR9 A C8  1 
HETATM 2374 C  C10 . A1AR9 B 2 .   ? -8.34224  -13.43010 -18.52897 1.000 30.31394 ? 401 A1AR9 A C10 1 
HETATM 2375 C  C13 . A1AR9 B 2 .   ? -5.68099  -13.96550 -17.79023 1.000 29.57569 ? 401 A1AR9 A C13 1 
HETATM 2376 C  C15 . A1AR9 B 2 .   ? -7.55249  -14.32883 -19.26185 1.000 34.71891 ? 401 A1AR9 A C15 1 
HETATM 2377 C  C17 . A1AR9 B 2 .   ? -15.13286 -15.43633 -16.70145 1.000 26.09875 ? 401 A1AR9 A C17 1 
HETATM 2378 C  C1  . A1AR9 B 2 .   ? -13.76492 -13.48781 -16.63465 1.000 26.43783 ? 401 A1AR9 A C1  1 
HETATM 2379 C  C11 . A1AR9 B 2 .   ? -7.76912  -12.79924 -17.42438 1.000 29.01494 ? 401 A1AR9 A C11 1 
HETATM 2380 C  C12 . A1AR9 B 2 .   ? -6.46167  -13.07100 -17.07681 1.000 28.25525 ? 401 A1AR9 A C12 1 
HETATM 2381 C  C14 . A1AR9 B 2 .   ? -6.23639  -14.59113 -18.88946 1.000 32.86638 ? 401 A1AR9 A C14 1 
HETATM 2382 C  C16 . A1AR9 B 2 .   ? -14.51581 -14.39085 -17.37729 1.000 27.40523 ? 401 A1AR9 A C16 1 
HETATM 2383 C  C18 . A1AR9 B 2 .   ? -15.00509 -15.55476 -15.33460 1.000 23.17857 ? 401 A1AR9 A C18 1 
HETATM 2384 C  C19 . A1AR9 B 2 .   ? -13.67747 -13.69789 -15.25732 1.000 24.86360 ? 401 A1AR9 A C19 1 
HETATM 2385 C  C2  . A1AR9 B 2 .   ? -12.03836 -12.56683 -18.23412 1.000 31.28993 ? 401 A1AR9 A C2  1 
HETATM 2386 C  C3  . A1AR9 B 2 .   ? -13.50243 -11.10025 -16.74918 1.000 28.59499 ? 401 A1AR9 A C3  1 
HETATM 2387 C  C9  . A1AR9 B 2 .   ? -12.37950 -12.51049 -19.59124 1.000 31.84599 ? 401 A1AR9 A C9  1 
HETATM 2388 F  F1  . A1AR9 B 2 .   ? -12.69259 -9.67981  -18.49865 1.000 37.91376 ? 401 A1AR9 A F1  1 
HETATM 2389 N  N2  . A1AR9 B 2 .   ? -14.27878 -14.70264 -14.60430 1.000 21.72546 ? 401 A1AR9 A N2  1 
HETATM 2390 O  O1  . A1AR9 B 2 .   ? -14.36813 -11.01158 -15.87918 1.000 29.70596 ? 401 A1AR9 A O1  1 
HETATM 2391 CL CL1 . A1AR9 B 2 .   ? -5.83271  -12.24532 -15.68400 1.000 36.97006 ? 401 A1AR9 A CL1 1 
HETATM 2392 CL CL2 . A1AR9 B 2 .   ? -16.07990 -16.60239 -17.56657 1.000 35.36357 ? 401 A1AR9 A CL2 1 
HETATM 2393 O  O   . HOH   C 3 .   ? -14.70817 0.85941   12.45738  1.000 37.49991 ? 501 HOH   A O   1 
HETATM 2394 O  O   . HOH   C 3 .   ? -4.34701  -18.78524 16.08946  1.000 30.08723 ? 502 HOH   A O   1 
HETATM 2395 O  O   . HOH   C 3 .   ? -27.89512 -10.14674 16.99856  1.000 37.28927 ? 503 HOH   A O   1 
HETATM 2396 O  O   . HOH   C 3 .   ? -25.88594 -19.56479 19.02455  1.000 31.90136 ? 504 HOH   A O   1 
HETATM 2397 O  O   . HOH   C 3 .   ? -24.63073 -2.36335  8.52400   1.000 33.26935 ? 505 HOH   A O   1 
HETATM 2398 O  O   . HOH   C 3 .   ? 5.08484   -14.33989 -14.87885 1.000 33.17823 ? 506 HOH   A O   1 
HETATM 2399 O  O   . HOH   C 3 .   ? -10.53067 -44.40403 8.51666   1.000 36.47604 ? 507 HOH   A O   1 
HETATM 2400 O  O   . HOH   C 3 .   ? 0.25782   1.30575   -2.81357  1.000 41.01838 ? 508 HOH   A O   1 
HETATM 2401 O  O   . HOH   C 3 .   ? -18.33093 -33.81752 25.41552  1.000 29.44196 ? 509 HOH   A O   1 
HETATM 2402 O  O   . HOH   C 3 .   ? -5.70789  2.26544   -25.82346 1.000 34.59603 ? 510 HOH   A O   1 
HETATM 2403 O  O   . HOH   C 3 .   ? -5.02114  -28.59551 3.51358   1.000 36.65138 ? 511 HOH   A O   1 
HETATM 2404 O  O   . HOH   C 3 .   ? -7.43141  -25.09009 7.85028   1.000 31.38193 ? 512 HOH   A O   1 
HETATM 2405 O  O   . HOH   C 3 .   ? -3.36266  -24.08616 -6.35264  1.000 18.20266 ? 513 HOH   A O   1 
HETATM 2406 O  O   . HOH   C 3 .   ? -22.98508 -28.12261 2.02013   1.000 27.59166 ? 514 HOH   A O   1 
HETATM 2407 O  O   . HOH   C 3 .   ? -27.63549 -13.99341 20.44465  1.000 36.83867 ? 515 HOH   A O   1 
HETATM 2408 O  O   . HOH   C 3 .   ? -19.80646 -43.40502 29.13584  1.000 39.52586 ? 516 HOH   A O   1 
HETATM 2409 O  O   . HOH   C 3 .   ? -26.96884 -4.01508  16.63448  1.000 32.22047 ? 517 HOH   A O   1 
HETATM 2410 O  O   . HOH   C 3 .   ? -23.73111 4.92599   -5.59250  1.000 35.31847 ? 518 HOH   A O   1 
HETATM 2411 O  O   . HOH   C 3 .   ? -17.65872 3.13663   6.86232   1.000 25.02308 ? 519 HOH   A O   1 
HETATM 2412 O  O   . HOH   C 3 .   ? -1.78656  -37.94716 13.78558  1.000 33.92810 ? 520 HOH   A O   1 
HETATM 2413 O  O   . HOH   C 3 .   ? -2.87962  -0.75592  -2.82603  1.000 30.30517 ? 521 HOH   A O   1 
HETATM 2414 O  O   . HOH   C 3 .   ? -6.76741  -16.29462 9.88631   1.000 29.40757 ? 522 HOH   A O   1 
HETATM 2415 O  O   . HOH   C 3 .   ? -15.76160 14.38878  -3.69178  1.000 33.25783 ? 523 HOH   A O   1 
HETATM 2416 O  O   . HOH   C 3 .   ? -0.17680  -0.49710  -24.70936 1.000 28.35512 ? 524 HOH   A O   1 
HETATM 2417 O  O   . HOH   C 3 .   ? -13.67732 -22.42315 -17.21713 1.000 31.90517 ? 525 HOH   A O   1 
HETATM 2418 O  O   . HOH   C 3 .   ? -17.26206 -29.39095 2.11136   1.000 21.97354 ? 526 HOH   A O   1 
HETATM 2419 O  O   . HOH   C 3 .   ? -17.59483 -37.19426 26.32986  1.000 39.61364 ? 527 HOH   A O   1 
HETATM 2420 O  O   . HOH   C 3 .   ? -16.19660 -34.64482 3.46336   1.000 20.08298 ? 528 HOH   A O   1 
HETATM 2421 O  O   . HOH   C 3 .   ? -15.82106 2.85033   -18.81768 1.000 26.21772 ? 529 HOH   A O   1 
HETATM 2422 O  O   . HOH   C 3 .   ? -1.696    0.130     0.692     1.000 29.80808 ? 530 HOH   A O   1 
HETATM 2423 O  O   . HOH   C 3 .   ? -12.73071 -28.53450 -5.32423  1.000 49.49223 ? 531 HOH   A O   1 
HETATM 2424 O  O   . HOH   C 3 .   ? -2.27785  -2.30105  -25.01877 1.000 37.21851 ? 532 HOH   A O   1 
HETATM 2425 O  O   . HOH   C 3 .   ? -12.94483 9.00503   -17.89466 1.000 31.38686 ? 533 HOH   A O   1 
HETATM 2426 O  O   . HOH   C 3 .   ? 5.30268   -6.67640  -14.01147 1.000 27.83390 ? 534 HOH   A O   1 
HETATM 2427 O  O   . HOH   C 3 .   ? -7.22702  4.73510   -2.32862  1.000 22.51470 ? 535 HOH   A O   1 
HETATM 2428 O  O   . HOH   C 3 .   ? 1.22435   8.27212   -20.33822 1.000 28.49610 ? 536 HOH   A O   1 
HETATM 2429 O  O   . HOH   C 3 .   ? -12.94784 -4.15426  8.54835   1.000 20.71092 ? 537 HOH   A O   1 
HETATM 2430 O  O   . HOH   C 3 .   ? -15.46009 -21.04219 18.91549  1.000 24.22188 ? 538 HOH   A O   1 
HETATM 2431 O  O   . HOH   C 3 .   ? -3.35449  -21.49883 20.52499  1.000 28.84166 ? 539 HOH   A O   1 
HETATM 2432 O  O   . HOH   C 3 .   ? -29.69064 -19.07119 13.96918  1.000 24.78330 ? 540 HOH   A O   1 
HETATM 2433 O  O   . HOH   C 3 .   ? -6.17964  -6.52590  -0.08722  1.000 13.50636 ? 541 HOH   A O   1 
HETATM 2434 O  O   . HOH   C 3 .   ? -20.11744 3.74702   -0.24336  1.000 20.99455 ? 542 HOH   A O   1 
HETATM 2435 O  O   . HOH   C 3 .   ? -3.51641  -23.57631 13.19353  1.000 24.31661 ? 543 HOH   A O   1 
HETATM 2436 O  O   . HOH   C 3 .   ? -6.61240  -16.97298 -6.59398  1.000 10.49541 ? 544 HOH   A O   1 
HETATM 2437 O  O   . HOH   C 3 .   ? 2.28833   2.06767   -5.62051  1.000 32.44659 ? 545 HOH   A O   1 
HETATM 2438 O  O   . HOH   C 3 .   ? -7.47718  13.89420  -7.10512  1.000 29.64188 ? 546 HOH   A O   1 
HETATM 2439 O  O   . HOH   C 3 .   ? 2.20077   5.43067   -19.44987 1.000 27.56108 ? 547 HOH   A O   1 
HETATM 2440 O  O   . HOH   C 3 .   ? -3.74932  -41.73491 7.64114   1.000 34.35204 ? 548 HOH   A O   1 
HETATM 2441 O  O   . HOH   C 3 .   ? 1.117     -23.366   -19.745   1.000 31.62059 ? 549 HOH   A O   1 
HETATM 2442 O  O   . HOH   C 3 .   ? -29.923   -24.289   7.010     1.000 28.61914 ? 550 HOH   A O   1 
HETATM 2443 O  O   . HOH   C 3 .   ? -16.80542 -13.69661 6.24345   1.000 15.78723 ? 551 HOH   A O   1 
HETATM 2444 O  O   . HOH   C 3 .   ? -3.68274  -34.96794 9.60129   1.000 29.53886 ? 552 HOH   A O   1 
HETATM 2445 O  O   . HOH   C 3 .   ? -8.67740  -25.05099 24.32504  1.000 36.09332 ? 553 HOH   A O   1 
HETATM 2446 O  O   . HOH   C 3 .   ? -28.67405 -1.90833  -3.53507  1.000 17.19240 ? 554 HOH   A O   1 
HETATM 2447 O  O   . HOH   C 3 .   ? -9.61794  -6.64330  8.89800   1.000 23.06382 ? 555 HOH   A O   1 
HETATM 2448 O  O   . HOH   C 3 .   ? -7.31850  -6.26121  10.18871  1.000 26.79981 ? 556 HOH   A O   1 
HETATM 2449 O  O   . HOH   C 3 .   ? -22.12194 -13.06762 -11.26663 1.000 20.77052 ? 557 HOH   A O   1 
HETATM 2450 O  O   . HOH   C 3 .   ? -7.47132  -23.80314 5.36481   1.000 19.49114 ? 558 HOH   A O   1 
HETATM 2451 O  O   . HOH   C 3 .   ? -15.14611 -32.66760 1.76692   1.000 23.44163 ? 559 HOH   A O   1 
HETATM 2452 O  O   . HOH   C 3 .   ? -2.40305  -27.58953 -4.23080  1.000 25.54217 ? 560 HOH   A O   1 
HETATM 2453 O  O   . HOH   C 3 .   ? -22.35510 -16.34194 -12.86172 1.000 23.88596 ? 561 HOH   A O   1 
HETATM 2454 O  O   . HOH   C 3 .   ? -20.07478 -36.25959 19.87149  1.000 26.88341 ? 562 HOH   A O   1 
HETATM 2455 O  O   . HOH   C 3 .   ? -6.09881  -10.94972 7.22564   1.000 30.42447 ? 563 HOH   A O   1 
HETATM 2456 O  O   . HOH   C 3 .   ? -19.73622 -25.61553 28.81903  1.000 32.97888 ? 564 HOH   A O   1 
HETATM 2457 O  O   . HOH   C 3 .   ? -4.23247  8.41783   -3.20768  1.000 39.09542 ? 565 HOH   A O   1 
HETATM 2458 O  O   . HOH   C 3 .   ? -21.31297 -11.58948 -19.23247 1.000 28.48431 ? 566 HOH   A O   1 
HETATM 2459 O  O   . HOH   C 3 .   ? -31.29548 -30.87888 7.74239   1.000 22.68100 ? 567 HOH   A O   1 
HETATM 2460 O  O   . HOH   C 3 .   ? -31.26547 -33.59029 10.32231  1.000 29.42566 ? 568 HOH   A O   1 
HETATM 2461 O  O   . HOH   C 3 .   ? -3.06093  -23.73624 1.82872   1.000 22.26857 ? 569 HOH   A O   1 
HETATM 2462 O  O   . HOH   C 3 .   ? -11.20599 -33.25745 0.75635   1.000 32.27274 ? 570 HOH   A O   1 
HETATM 2463 O  O   . HOH   C 3 .   ? -20.09965 7.86238   -5.24561  1.000 24.63176 ? 571 HOH   A O   1 
HETATM 2464 O  O   . HOH   C 3 .   ? -17.35817 -5.58087  -6.42638  1.000 13.03151 ? 572 HOH   A O   1 
HETATM 2465 O  O   . HOH   C 3 .   ? 0.52179   -20.16752 -13.05274 1.000 21.45528 ? 573 HOH   A O   1 
HETATM 2466 O  O   . HOH   C 3 .   ? -24.30088 -26.10866 3.47191   1.000 32.45264 ? 574 HOH   A O   1 
HETATM 2467 O  O   . HOH   C 3 .   ? -2.44762  -4.90630  2.40958   1.000 10.34437 ? 575 HOH   A O   1 
HETATM 2468 O  O   . HOH   C 3 .   ? -5.43226  -22.07665 -17.78700 1.000 26.55222 ? 576 HOH   A O   1 
HETATM 2469 O  O   . HOH   C 3 .   ? -10.93258 -21.26380 9.18082   1.000 17.80763 ? 577 HOH   A O   1 
HETATM 2470 O  O   . HOH   C 3 .   ? 4.05737   -7.25628  -24.49669 1.000 36.03498 ? 578 HOH   A O   1 
HETATM 2471 O  O   . HOH   C 3 .   ? 1.40810   -20.51332 -15.54281 1.000 26.05892 ? 579 HOH   A O   1 
HETATM 2472 O  O   . HOH   C 3 .   ? -16.51546 -22.12178 -9.28814  1.000 16.60967 ? 580 HOH   A O   1 
HETATM 2473 O  O   . HOH   C 3 .   ? -14.86982 -41.83433 16.46272  1.000 34.11638 ? 581 HOH   A O   1 
HETATM 2474 O  O   . HOH   C 3 .   ? -0.00000  -8.08388  0.00000   0.50  11.20256 ? 582 HOH   A O   1 
HETATM 2475 O  O   . HOH   C 3 .   ? -14.84562 -20.96732 -2.46156  1.000 13.96804 ? 583 HOH   A O   1 
HETATM 2476 O  O   . HOH   C 3 .   ? -10.13323 -25.40782 -6.82246  1.000 18.09146 ? 584 HOH   A O   1 
HETATM 2477 O  O   . HOH   C 3 .   ? -8.63768  3.43406   -24.91757 1.000 35.24661 ? 585 HOH   A O   1 
HETATM 2478 O  O   . HOH   C 3 .   ? -12.91072 -37.06136 1.57928   1.000 25.89112 ? 586 HOH   A O   1 
HETATM 2479 O  O   . HOH   C 3 .   ? -17.78042 -5.09712  -17.04034 1.000 21.05556 ? 587 HOH   A O   1 
HETATM 2480 O  O   . HOH   C 3 .   ? -0.80021  -24.66151 -13.07220 1.000 27.13305 ? 588 HOH   A O   1 
HETATM 2481 O  O   . HOH   C 3 .   ? -20.81414 2.81134   -11.88776 1.000 24.73319 ? 589 HOH   A O   1 
HETATM 2482 O  O   . HOH   C 3 .   ? -10.83280 -15.96242 -17.28516 1.000 23.27350 ? 590 HOH   A O   1 
HETATM 2483 O  O   . HOH   C 3 .   ? 3.62353   2.44058   -12.97478 1.000 20.92759 ? 591 HOH   A O   1 
HETATM 2484 O  O   . HOH   C 3 .   ? -31.86288 -28.39352 2.09535   1.000 28.85640 ? 592 HOH   A O   1 
HETATM 2485 O  O   . HOH   C 3 .   ? 2.04868   -16.52712 -21.23091 1.000 38.56159 ? 593 HOH   A O   1 
HETATM 2486 O  O   . HOH   C 3 .   ? -19.14750 -15.53900 -19.45787 1.000 32.10648 ? 594 HOH   A O   1 
HETATM 2487 O  O   . HOH   C 3 .   ? -3.01173  -1.14654  -5.01634  1.000 25.10837 ? 595 HOH   A O   1 
HETATM 2488 O  O   . HOH   C 3 .   ? -7.80624  -19.90056 7.95001   1.000 21.47038 ? 596 HOH   A O   1 
HETATM 2489 O  O   . HOH   C 3 .   ? -19.58956 -23.61325 0.29560   1.000 27.62041 ? 597 HOH   A O   1 
HETATM 2490 O  O   . HOH   C 3 .   ? 1.03721   -12.31667 -12.69859 1.000 18.03053 ? 598 HOH   A O   1 
HETATM 2491 O  O   . HOH   C 3 .   ? 3.76839   -4.89582  -11.93651 1.000 20.51239 ? 599 HOH   A O   1 
HETATM 2492 O  O   . HOH   C 3 .   ? -23.97998 -43.58844 4.48482   1.000 36.35207 ? 600 HOH   A O   1 
HETATM 2493 O  O   . HOH   C 3 .   ? -1.66790  6.40880   -9.96371  1.000 25.22684 ? 601 HOH   A O   1 
HETATM 2494 O  O   . HOH   C 3 .   ? -1.85785  -24.37182 -8.91953  1.000 23.28175 ? 602 HOH   A O   1 
HETATM 2495 O  O   . HOH   C 3 .   ? 3.20654   -11.04956 -17.99903 1.000 31.46746 ? 603 HOH   A O   1 
HETATM 2496 O  O   . HOH   C 3 .   ? 5.15345   -7.81880  -17.53275 1.000 27.65669 ? 604 HOH   A O   1 
HETATM 2497 O  O   . HOH   C 3 .   ? -11.46658 -27.11974 -5.05495  1.000 24.09413 ? 605 HOH   A O   1 
HETATM 2498 O  O   . HOH   C 3 .   ? -3.47133  -27.48439 9.47703   1.000 25.41815 ? 606 HOH   A O   1 
HETATM 2499 O  O   . HOH   C 3 .   ? 1.65309   -11.80935 -16.36036 1.000 25.00203 ? 607 HOH   A O   1 
HETATM 2500 O  O   . HOH   C 3 .   ? -18.07075 -24.88423 7.45774   1.000 11.88303 ? 608 HOH   A O   1 
HETATM 2501 O  O   . HOH   C 3 .   ? -14.99103 -15.22489 9.22373   1.000 17.51232 ? 609 HOH   A O   1 
HETATM 2502 O  O   . HOH   C 3 .   ? -17.29585 -31.18266 1.36395   1.000 23.46296 ? 610 HOH   A O   1 
HETATM 2503 O  O   . HOH   C 3 .   ? -19.14115 -19.76893 24.86320  1.000 30.16691 ? 611 HOH   A O   1 
HETATM 2504 O  O   . HOH   C 3 .   ? 5.29516   1.47921   -17.88004 1.000 24.41656 ? 612 HOH   A O   1 
HETATM 2505 O  O   . HOH   C 3 .   ? -32.84400 -18.44255 17.96681  1.000 25.78256 ? 613 HOH   A O   1 
HETATM 2506 O  O   . HOH   C 3 .   ? 1.42433   -13.09923 -4.35132  1.000 9.91593  ? 614 HOH   A O   1 
HETATM 2507 O  O   . HOH   C 3 .   ? -10.74393 -26.69788 -9.07239  1.000 23.13800 ? 615 HOH   A O   1 
HETATM 2508 O  O   . HOH   C 3 .   ? -16.17309 -39.72104 3.75172   1.000 27.22411 ? 616 HOH   A O   1 
HETATM 2509 O  O   . HOH   C 3 .   ? -25.98098 -0.93972  -6.46400  1.000 26.23061 ? 617 HOH   A O   1 
HETATM 2510 O  O   . HOH   C 3 .   ? 1.12550   -11.72065 -8.02215  1.000 9.41198  ? 618 HOH   A O   1 
HETATM 2511 O  O   . HOH   C 3 .   ? 1.38356   -13.47004 -10.21888 1.000 13.82451 ? 619 HOH   A O   1 
HETATM 2512 O  O   . HOH   C 3 .   ? -12.54606 -18.32297 19.32459  1.000 27.47385 ? 620 HOH   A O   1 
HETATM 2513 O  O   . HOH   C 3 .   ? -18.45322 -26.63163 1.61607   1.000 21.75831 ? 621 HOH   A O   1 
HETATM 2514 O  O   . HOH   C 3 .   ? 0.53038   9.07908   -14.71889 1.000 26.89532 ? 622 HOH   A O   1 
HETATM 2515 O  O   . HOH   C 3 .   ? -0.00000  -16.21227 0.00000   0.50  12.26496 ? 623 HOH   A O   1 
HETATM 2516 O  O   . HOH   C 3 .   ? -12.97310 -29.27593 24.41671  1.000 31.15262 ? 624 HOH   A O   1 
HETATM 2517 O  O   . HOH   C 3 .   ? -5.18965  -0.76121  4.69024   1.000 22.68573 ? 625 HOH   A O   1 
HETATM 2518 O  O   . HOH   C 3 .   ? -1.81877  -24.14011 -1.45389  1.000 21.64955 ? 626 HOH   A O   1 
HETATM 2519 O  O   . HOH   C 3 .   ? 4.71354   -3.12398  -9.23522  1.000 20.67014 ? 627 HOH   A O   1 
HETATM 2520 O  O   . HOH   C 3 .   ? -12.87222 15.61933  -4.75383  1.000 30.46813 ? 628 HOH   A O   1 
HETATM 2521 O  O   . HOH   C 3 .   ? -24.20812 -42.10855 9.47961   1.000 38.35961 ? 629 HOH   A O   1 
HETATM 2522 O  O   . HOH   C 3 .   ? -4.53572  -8.06096  -14.26611 1.000 16.34574 ? 630 HOH   A O   1 
HETATM 2523 O  O   . HOH   C 3 .   ? 4.82883   -1.46390  -10.70671 1.000 29.28225 ? 631 HOH   A O   1 
HETATM 2524 O  O   . HOH   C 3 .   ? -2.97426  -13.37926 6.45635   1.000 14.24302 ? 632 HOH   A O   1 
HETATM 2525 O  O   . HOH   C 3 .   ? -0.61173  5.27958   -6.73036  1.000 41.82019 ? 633 HOH   A O   1 
HETATM 2526 O  O   . HOH   C 3 .   ? -6.34473  -31.17756 21.89578  1.000 29.76148 ? 634 HOH   A O   1 
HETATM 2527 O  O   . HOH   C 3 .   ? -19.48757 -17.75487 5.44028   1.000 17.59331 ? 635 HOH   A O   1 
HETATM 2528 O  O   . HOH   C 3 .   ? -11.36017 -9.10119  4.53027   1.000 14.10602 ? 636 HOH   A O   1 
HETATM 2529 O  O   . HOH   C 3 .   ? -1.12456  -19.45021 3.99359   1.000 14.77174 ? 637 HOH   A O   1 
HETATM 2530 O  O   . HOH   C 3 .   ? -10.38924 -21.52249 24.07198  1.000 31.45738 ? 638 HOH   A O   1 
HETATM 2531 O  O   . HOH   C 3 .   ? -21.04413 -39.50447 13.90511  1.000 25.47764 ? 639 HOH   A O   1 
HETATM 2532 O  O   . HOH   C 3 .   ? -10.86477 -25.41251 23.38883  1.000 29.12614 ? 640 HOH   A O   1 
HETATM 2533 O  O   . HOH   C 3 .   ? -4.32262  -20.71791 6.52855   1.000 18.98271 ? 641 HOH   A O   1 
HETATM 2534 O  O   . HOH   C 3 .   ? -2.23460  -15.02879 2.50132   1.000 10.84930 ? 642 HOH   A O   1 
HETATM 2535 O  O   . HOH   C 3 .   ? -20.47795 4.73112   -8.58432  1.000 34.25170 ? 643 HOH   A O   1 
HETATM 2536 O  O   . HOH   C 3 .   ? -3.78622  11.84287  -21.46217 1.000 29.98746 ? 644 HOH   A O   1 
HETATM 2537 O  O   . HOH   C 3 .   ? -25.11643 -37.95049 1.45449   1.000 34.39774 ? 645 HOH   A O   1 
HETATM 2538 O  O   . HOH   C 3 .   ? -8.08217  -25.66742 -12.94567 1.000 26.18567 ? 646 HOH   A O   1 
HETATM 2539 O  O   . HOH   C 3 .   ? -13.05565 -14.58443 7.43753   1.000 16.76518 ? 647 HOH   A O   1 
HETATM 2540 O  O   . HOH   C 3 .   ? -29.39321 -23.53441 21.10721  1.000 33.07593 ? 648 HOH   A O   1 
HETATM 2541 O  O   . HOH   C 3 .   ? -9.57932  -21.42254 -17.85763 1.000 31.58223 ? 649 HOH   A O   1 
HETATM 2542 O  O   . HOH   C 3 .   ? -25.13361 -31.53695 24.85711  1.000 30.63209 ? 650 HOH   A O   1 
HETATM 2543 O  O   . HOH   C 3 .   ? -8.38752  -27.05930 9.55432   1.000 17.15532 ? 651 HOH   A O   1 
HETATM 2544 O  O   . HOH   C 3 .   ? -26.05303 -28.94233 23.42344  1.000 31.32850 ? 652 HOH   A O   1 
HETATM 2545 O  O   . HOH   C 3 .   ? -22.22298 -16.27495 9.18252   1.000 15.87710 ? 653 HOH   A O   1 
HETATM 2546 O  O   . HOH   C 3 .   ? 5.19976   -5.09206  -26.23422 1.000 37.32429 ? 654 HOH   A O   1 
HETATM 2547 O  O   . HOH   C 3 .   ? -25.60312 -25.96177 5.87478   1.000 21.45616 ? 655 HOH   A O   1 
HETATM 2548 O  O   . HOH   C 3 .   ? -11.91447 6.42460   4.43930   1.000 22.13310 ? 656 HOH   A O   1 
HETATM 2549 O  O   . HOH   C 3 .   ? -19.08266 -34.73261 2.64287   1.000 19.50806 ? 657 HOH   A O   1 
HETATM 2550 O  O   . HOH   C 3 .   ? -22.54392 -43.45531 11.79632  1.000 35.27961 ? 658 HOH   A O   1 
HETATM 2551 O  O   . HOH   C 3 .   ? -25.64345 -22.50568 26.15358  1.000 37.61057 ? 659 HOH   A O   1 
HETATM 2552 O  O   . HOH   C 3 .   ? -31.39043 -23.87710 9.37780   1.000 24.55356 ? 660 HOH   A O   1 
HETATM 2553 O  O   . HOH   C 3 .   ? -22.02786 -16.91869 6.30025   1.000 14.90724 ? 661 HOH   A O   1 
HETATM 2554 O  O   . HOH   C 3 .   ? -11.32357 -6.80664  -25.47298 1.000 32.78270 ? 662 HOH   A O   1 
HETATM 2555 O  O   . HOH   C 3 .   ? -11.55710 -31.40337 23.67179  1.000 27.58937 ? 663 HOH   A O   1 
HETATM 2556 O  O   . HOH   C 3 .   ? -7.60603  -28.37227 24.49107  1.000 31.19738 ? 664 HOH   A O   1 
HETATM 2557 O  O   . HOH   C 3 .   ? -23.87488 2.88943   -4.36246  1.000 26.20662 ? 665 HOH   A O   1 
HETATM 2558 O  O   . HOH   C 3 .   ? -0.91318  10.79484  -19.49235 1.000 28.75431 ? 666 HOH   A O   1 
HETATM 2559 O  O   . HOH   C 3 .   ? -21.29357 -26.10213 -0.51401  1.000 31.85635 ? 667 HOH   A O   1 
HETATM 2560 O  O   . HOH   C 3 .   ? -4.54527  -18.68401 -18.35729 1.000 32.45336 ? 668 HOH   A O   1 
HETATM 2561 O  O   . HOH   C 3 .   ? -7.33090  -3.01935  -24.08965 1.000 29.12214 ? 669 HOH   A O   1 
HETATM 2562 O  O   . HOH   C 3 .   ? 4.78005   -3.01166  -6.85034  1.000 31.46179 ? 670 HOH   A O   1 
HETATM 2563 O  O   . HOH   C 3 .   ? -10.08384 4.47197   5.85350   1.000 27.21780 ? 671 HOH   A O   1 
HETATM 2564 O  O   . HOH   C 3 .   ? -12.10207 -29.26209 -2.10302  1.000 22.63270 ? 672 HOH   A O   1 
HETATM 2565 O  O   . HOH   C 3 .   ? -10.43099 10.16492  -24.62891 1.000 38.90862 ? 673 HOH   A O   1 
HETATM 2566 O  O   . HOH   C 3 .   ? -24.07346 -16.67715 -0.08853  1.000 16.16694 ? 674 HOH   A O   1 
HETATM 2567 O  O   . HOH   C 3 .   ? -5.49708  -13.33112 8.05745   1.000 20.77977 ? 675 HOH   A O   1 
HETATM 2568 O  O   . HOH   C 3 .   ? -1.26521  -29.83443 -7.13565  1.000 25.99194 ? 676 HOH   A O   1 
HETATM 2569 O  O   . HOH   C 3 .   ? 0.23877   -17.15376 -2.65979  1.000 11.43155 ? 677 HOH   A O   1 
HETATM 2570 O  O   . HOH   C 3 .   ? -25.85900 -31.16764 0.00000   0.50  19.32000 ? 678 HOH   A O   1 
HETATM 2571 O  O   . HOH   C 3 .   ? -8.02749  -38.87394 0.30849   1.000 33.29359 ? 679 HOH   A O   1 
HETATM 2572 O  O   . HOH   C 3 .   ? -1.28558  -24.61450 17.31636  1.000 27.07054 ? 680 HOH   A O   1 
HETATM 2573 O  O   . HOH   C 3 .   ? -4.96616  -24.30225 4.09127   1.000 21.45192 ? 681 HOH   A O   1 
HETATM 2574 O  O   . HOH   C 3 .   ? -3.71565  -7.13424  0.84244   1.000 15.47649 ? 682 HOH   A O   1 
HETATM 2575 O  O   . HOH   C 3 .   ? -27.67456 -28.54418 0.37299   1.000 32.45627 ? 683 HOH   A O   1 
HETATM 2576 O  O   . HOH   C 3 .   ? 0.05240   11.29014  -15.94424 1.000 28.60806 ? 684 HOH   A O   1 
HETATM 2577 O  O   . HOH   C 3 .   ? 0.18867   -23.28565 -10.75751 1.000 31.48926 ? 685 HOH   A O   1 
HETATM 2578 O  O   . HOH   C 3 .   ? 4.829     -8.684    -8.103    1.000 31.56026 ? 686 HOH   A O   1 
HETATM 2579 O  O   . HOH   C 3 .   ? -31.06878 -34.92765 15.03061  1.000 25.25737 ? 687 HOH   A O   1 
HETATM 2580 O  O   . HOH   C 3 .   ? -13.64161 -29.54711 -0.12075  1.000 28.34353 ? 688 HOH   A O   1 
HETATM 2581 O  O   . HOH   C 3 .   ? -8.17739  -29.70969 -7.54958  1.000 30.61838 ? 689 HOH   A O   1 
HETATM 2582 O  O   . HOH   C 3 .   ? 1.12283   -2.07048  -27.43839 1.000 30.38256 ? 690 HOH   A O   1 
HETATM 2583 O  O   . HOH   C 3 .   ? -12.61470 -17.83776 12.80268  1.000 20.93204 ? 691 HOH   A O   1 
HETATM 2584 O  O   . HOH   C 3 .   ? -13.55470 -7.84885  -19.31911 1.000 30.12080 ? 692 HOH   A O   1 
HETATM 2585 O  O   . HOH   C 3 .   ? -13.88496 -20.06510 25.07971  1.000 33.81988 ? 693 HOH   A O   1 
HETATM 2586 O  O   . HOH   C 3 .   ? -0.58381  -27.76909 17.24361  1.000 25.50739 ? 694 HOH   A O   1 
HETATM 2587 O  O   . HOH   C 3 .   ? -8.33379  -13.29407 11.42055  1.000 36.39554 ? 695 HOH   A O   1 
HETATM 2588 O  O   . HOH   C 3 .   ? 2.32273   -16.98828 -9.48614  1.000 16.73569 ? 696 HOH   A O   1 
HETATM 2589 O  O   . HOH   C 3 .   ? -10.27634 -32.81428 -3.44421  1.000 31.04983 ? 697 HOH   A O   1 
HETATM 2590 O  O   . HOH   C 3 .   ? -7.87336  -32.48931 -5.03465  1.000 29.81173 ? 698 HOH   A O   1 
HETATM 2591 O  O   . HOH   C 3 .   ? -12.59737 -42.63115 17.57058  1.000 38.85461 ? 699 HOH   A O   1 
HETATM 2592 O  O   . HOH   C 3 .   ? -18.95566 -39.08161 4.15677   1.000 30.05682 ? 700 HOH   A O   1 
HETATM 2593 O  O   . HOH   C 3 .   ? -19.52264 -22.19444 -7.16583  1.000 27.60059 ? 701 HOH   A O   1 
HETATM 2594 O  O   . HOH   C 3 .   ? -8.28090  -17.26420 -18.12390 1.000 30.58290 ? 702 HOH   A O   1 
HETATM 2595 O  O   . HOH   C 3 .   ? 3.141     -0.572    -2.883    1.000 37.77625 ? 703 HOH   A O   1 
HETATM 2596 O  O   . HOH   C 3 .   ? -4.47762  -28.18704 -0.48443  1.000 22.98550 ? 704 HOH   A O   1 
HETATM 2597 O  O   . HOH   C 3 .   ? 3.43887   -12.26155 -14.25009 1.000 25.95365 ? 705 HOH   A O   1 
HETATM 2598 O  O   . HOH   C 3 .   ? -7.20279  -28.32242 -11.54012 1.000 31.45286 ? 706 HOH   A O   1 
HETATM 2599 O  O   . HOH   C 3 .   ? -25.85900 -15.09010 0.00000   0.50  22.33340 ? 707 HOH   A O   1 
HETATM 2600 O  O   . HOH   C 3 .   ? -15.08546 -11.36664 9.14478   1.000 24.14779 ? 708 HOH   A O   1 
HETATM 2601 O  O   . HOH   C 3 .   ? 4.19327   -9.78580  -16.37459 1.000 27.78220 ? 709 HOH   A O   1 
HETATM 2602 O  O   . HOH   C 3 .   ? -29.21897 -20.26422 16.18177  1.000 27.85810 ? 710 HOH   A O   1 
HETATM 2603 O  O   . HOH   C 3 .   ? -24.42226 2.34200   1.67726   1.000 32.38275 ? 711 HOH   A O   1 
HETATM 2604 O  O   . HOH   C 3 .   ? -0.87733  8.73521   -10.74088 1.000 30.73861 ? 712 HOH   A O   1 
HETATM 2605 O  O   . HOH   C 3 .   ? -28.87079 -25.54783 21.63610  1.000 40.62531 ? 713 HOH   A O   1 
HETATM 2606 O  O   . HOH   C 3 .   ? -21.53095 4.76690   -7.06754  1.000 29.42904 ? 714 HOH   A O   1 
HETATM 2607 O  O   . HOH   C 3 .   ? 2.69688   4.05106   -15.37424 1.000 25.88352 ? 715 HOH   A O   1 
HETATM 2608 O  O   . HOH   C 3 .   ? -1.18689  -27.17847 -12.36898 1.000 29.35181 ? 716 HOH   A O   1 
HETATM 2609 O  O   . HOH   C 3 .   ? -24.31047 3.20503   -1.96064  1.000 26.07637 ? 717 HOH   A O   1 
HETATM 2610 O  O   . HOH   C 3 .   ? -3.48814  -27.99141 1.33922   1.000 35.35563 ? 718 HOH   A O   1 
HETATM 2611 O  O   . HOH   C 3 .   ? -22.383   -2.265    6.283     1.000 25.55367 ? 719 HOH   A O   1 
HETATM 2612 O  O   . HOH   C 3 .   ? -1.229    -23.635   14.676    1.000 26.51688 ? 720 HOH   A O   1 
HETATM 2613 O  O   . HOH   C 3 .   ? -14.91297 -9.27837  10.14082  1.000 28.58504 ? 721 HOH   A O   1 
HETATM 2614 O  O   . HOH   C 3 .   ? -26.70997 -24.44711 22.88557  1.000 34.39830 ? 722 HOH   A O   1 
HETATM 2615 O  O   . HOH   C 3 .   ? -0.94877  -36.23313 14.16786  1.000 38.40723 ? 723 HOH   A O   1 
HETATM 2616 O  O   . HOH   C 3 .   ? -21.05766 -34.26742 25.43842  1.000 35.19717 ? 724 HOH   A O   1 
HETATM 2617 O  O   . HOH   C 3 .   ? -13.09681 -28.10558 -9.05297  1.000 40.44268 ? 725 HOH   A O   1 
HETATM 2618 O  O   . HOH   C 3 .   ? 3.99090   3.86409   -17.69273 1.000 25.60029 ? 726 HOH   A O   1 
HETATM 2619 O  O   . HOH   C 3 .   ? -7.79837  4.40988   4.83386   1.000 31.76556 ? 727 HOH   A O   1 
HETATM 2620 O  O   . HOH   C 3 .   ? 2.95738   1.35404   -2.09529  1.000 40.46988 ? 728 HOH   A O   1 
HETATM 2621 O  O   . HOH   C 3 .   ? 1.729     -20.389   -22.373   1.000 35.05876 ? 729 HOH   A O   1 
HETATM 2622 O  O   . HOH   C 3 .   ? 5.42851   -16.81816 -13.57364 1.000 30.55010 ? 730 HOH   A O   1 
HETATM 2623 O  O   . HOH   C 3 .   ? -1.96281  -26.55247 -0.58743  1.000 35.64835 ? 731 HOH   A O   1 
HETATM 2624 O  O   . HOH   C 3 .   ? -9.35621  15.59251  -5.43249  1.000 33.25070 ? 732 HOH   A O   1 
HETATM 2625 O  O   . HOH   C 3 .   ? -6.60922  -18.21831 9.52349   1.000 24.14524 ? 733 HOH   A O   1 
HETATM 2626 O  O   . HOH   C 3 .   ? -22.53520 4.15855   0.50121   1.000 23.97304 ? 734 HOH   A O   1 
HETATM 2627 O  O   . HOH   C 3 .   ? -8.39614  -21.94273 8.66860   1.000 22.13832 ? 735 HOH   A O   1 
HETATM 2628 O  O   . HOH   C 3 .   ? -10.63161 -9.55967  7.22967   1.000 23.18125 ? 736 HOH   A O   1 
HETATM 2629 O  O   . HOH   C 3 .   ? -11.34515 -9.30301  -19.78772 1.000 31.97740 ? 737 HOH   A O   1 
HETATM 2630 O  O   . HOH   C 3 .   ? -12.26684 -8.42057  8.76661   1.000 28.17825 ? 738 HOH   A O   1 
HETATM 2631 O  O   . HOH   C 3 .   ? -33.43967 -30.19414 5.84932   1.000 27.63499 ? 739 HOH   A O   1 
HETATM 2632 O  O   . HOH   C 3 .   ? -1.38436  -25.24759 -5.32931  1.000 26.20393 ? 740 HOH   A O   1 
HETATM 2633 O  O   . HOH   C 3 .   ? -3.07958  -23.25298 10.51264  1.000 26.12347 ? 741 HOH   A O   1 
HETATM 2634 O  O   . HOH   C 3 .   ? -25.54783 -26.74302 1.30608   1.000 28.63312 ? 742 HOH   A O   1 
HETATM 2635 O  O   . HOH   C 3 .   ? 3.66578   -18.84810 -10.42324 1.000 21.14303 ? 743 HOH   A O   1 
HETATM 2636 O  O   . HOH   C 3 .   ? -5.42362  1.04801   6.17101   1.000 31.30842 ? 744 HOH   A O   1 
HETATM 2637 O  O   . HOH   C 3 .   ? 0.87894   2.53601   -1.28561  1.000 36.98676 ? 745 HOH   A O   1 
HETATM 2638 O  O   . HOH   C 3 .   ? -26.52408 -26.14795 22.26879  1.000 34.75925 ? 746 HOH   A O   1 
HETATM 2639 O  O   . HOH   C 3 .   ? -1.74085  6.91238   -7.51128  1.000 29.58711 ? 747 HOH   A O   1 
HETATM 2640 O  O   . HOH   C 3 .   ? -18.13922 14.54784  -5.21229  1.000 35.26325 ? 748 HOH   A O   1 
HETATM 2641 O  O   . HOH   C 3 .   ? -12.32394 1.42326   12.42854  1.000 35.58440 ? 749 HOH   A O   1 
HETATM 2642 O  O   . HOH   C 3 .   ? -4.289    -20.757   8.944     1.000 20.34148 ? 750 HOH   A O   1 
HETATM 2643 O  O   . HOH   C 3 .   ? -32.091   -23.848   5.975     1.000 27.46887 ? 751 HOH   A O   1 
HETATM 2644 O  O   . HOH   C 3 .   ? -4.639    2.316     2.473     1.000 38.44289 ? 752 HOH   A O   1 
HETATM 2645 O  O   . HOH   C 3 .   ? -8.51336  -10.81625 7.78413   1.000 25.43949 ? 753 HOH   A O   1 
HETATM 2646 O  O   . HOH   C 3 .   ? -15.42270 -17.68857 18.98565  1.000 32.14898 ? 754 HOH   A O   1 
HETATM 2647 O  O   . HOH   C 3 .   ? -9.06941  -29.21035 -9.62503  1.000 29.47166 ? 755 HOH   A O   1 
HETATM 2648 O  O   . HOH   C 3 .   ? -1.20014  -34.79256 10.61027  1.000 34.82831 ? 756 HOH   A O   1 
HETATM 2649 O  O   . HOH   C 3 .   ? -3.43492  -22.87862 5.62556   1.000 20.44146 ? 757 HOH   A O   1 
HETATM 2650 O  O   . HOH   C 3 .   ? -22.73448 -41.41670 13.34196  1.000 33.70049 ? 758 HOH   A O   1 
HETATM 2651 O  O   . HOH   C 3 .   ? -0.66411  -23.70000 -3.61529  1.000 22.03112 ? 759 HOH   A O   1 
HETATM 2652 O  O   . HOH   C 3 .   ? -3.417    2.442     0.526     1.000 35.75199 ? 760 HOH   A O   1 
HETATM 2653 O  O   . HOH   C 3 .   ? -0.00000  -23.29606 0.00000   0.50  28.46569 ? 761 HOH   A O   1 
HETATM 2654 O  O   . HOH   C 3 .   ? -19.74938 -37.02274 2.93411   1.000 29.38512 ? 762 HOH   A O   1 
HETATM 2655 O  O   . HOH   C 3 .   ? -3.95547  -14.39425 9.78270   1.000 24.20871 ? 763 HOH   A O   1 
HETATM 2656 O  O   . HOH   C 3 .   ? -1.96123  -29.12423 -15.02075 1.000 35.48558 ? 764 HOH   A O   1 
HETATM 2657 O  O   . HOH   C 3 .   ? -1.58550  -22.05446 3.49507   1.000 21.05451 ? 765 HOH   A O   1 
HETATM 2658 O  O   . HOH   C 3 .   ? -19.11328 12.29448  -6.80085  1.000 34.33869 ? 766 HOH   A O   1 
HETATM 2659 O  O   . HOH   C 3 .   ? -11.16026 -33.31215 25.57462  1.000 32.69966 ? 767 HOH   A O   1 
HETATM 2660 O  O   . HOH   C 3 .   ? -10.55931 -19.70516 11.79249  1.000 28.38062 ? 768 HOH   A O   1 
HETATM 2661 O  O   . HOH   C 3 .   ? 0.40666   -28.41176 20.10874  1.000 29.52818 ? 769 HOH   A O   1 
HETATM 2662 O  O   . HOH   C 3 .   ? -15.40931 -37.50147 2.63333   1.000 25.89593 ? 770 HOH   A O   1 
HETATM 2663 O  O   . HOH   C 3 .   ? -7.86446  -32.81007 -7.54831  1.000 36.77365 ? 771 HOH   A O   1 
HETATM 2664 O  O   . HOH   C 3 .   ? -6.99741  -29.79304 -13.16897 1.000 36.74520 ? 772 HOH   A O   1 
HETATM 2665 O  O   . HOH   C 3 .   ? -3.76456  -30.66855 -13.53185 1.000 40.56327 ? 773 HOH   A O   1 
HETATM 2666 O  O   . HOH   C 3 .   ? -10.57461 -31.35806 -10.46890 1.000 38.13035 ? 774 HOH   A O   1 
HETATM 2667 O  O   . HOH   C 3 .   ? -0.86993  -28.01893 0.75647   1.000 35.03779 ? 775 HOH   A O   1 
HETATM 2668 O  O   . HOH   C 3 .   ? -12.47590 -31.88347 27.73795  1.000 34.77553 ? 776 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   ? 0.19568 0.35674 0.31693 0.00716  0.08921  0.07317  1   SER   A N   
2    C  CA  . SER   A 1   ? 0.18241 0.33618 0.30102 0.00083  0.07871  0.07978  1   SER   A CA  
3    C  C   . SER   A 1   ? 0.18644 0.33362 0.32002 -0.00243 0.06655  0.08033  1   SER   A C   
4    O  O   . SER   A 1   ? 0.16340 0.31194 0.30833 0.00067  0.06521  0.07620  1   SER   A O   
5    C  CB  . SER   A 1   ? 0.21867 0.37750 0.34191 -0.00357 0.08066  0.09081  1   SER   A CB  
6    O  OG  . SER   A 1   ? 0.21974 0.38449 0.36681 -0.00596 0.07897  0.09667  1   SER   A OG  
7    N  N   . GLY   A 2   ? 0.12639 0.26562 0.25910 -0.00868 0.05765  0.08512  2   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.16994 0.30038 0.30918 -0.01264 0.04590  0.08314  2   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.18463 0.30621 0.30760 -0.01113 0.04269  0.07677  2   GLY   A C   
10   O  O   . GLY   A 2   ? 0.17657 0.30018 0.28504 -0.00588 0.04929  0.07182  2   GLY   A O   
11   N  N   . PHE   A 3   ? 0.16749 0.27880 0.29187 -0.01640 0.03235  0.07632  3   PHE   A N   
12   C  CA  . PHE   A 3   ? 0.17976 0.28145 0.28941 -0.01565 0.02831  0.07086  3   PHE   A CA  
13   C  C   . PHE   A 3   ? 0.18773 0.27983 0.30163 -0.01919 0.01697  0.06592  3   PHE   A C   
14   O  O   . PHE   A 3   ? 0.19421 0.28165 0.31669 -0.02654 0.01065  0.06932  3   PHE   A O   
15   C  CB  . PHE   A 3   ? 0.18724 0.28102 0.28485 -0.01781 0.02816  0.07526  3   PHE   A CB  
16   C  CG  . PHE   A 3   ? 0.18170 0.26687 0.25806 -0.01351 0.02605  0.06807  3   PHE   A CG  
17   C  CD1 . PHE   A 3   ? 0.21465 0.30709 0.27706 -0.00817 0.03253  0.06466  3   PHE   A CD1 
18   C  CD2 . PHE   A 3   ? 0.18731 0.25794 0.25797 -0.01522 0.01786  0.06405  3   PHE   A CD2 
19   C  CE1 . PHE   A 3   ? 0.23855 0.32489 0.28305 -0.00547 0.02947  0.05815  3   PHE   A CE1 
20   C  CE2 . PHE   A 3   ? 0.18814 0.25324 0.24229 -0.01137 0.01604  0.05840  3   PHE   A CE2 
21   C  CZ  . PHE   A 3   ? 0.18464 0.25818 0.22645 -0.00691 0.02117  0.05585  3   PHE   A CZ  
22   N  N   . ARG   A 4   ? 0.19246 0.28134 0.29972 -0.01458 0.01458  0.05784  4   ARG   A N   
23   C  CA  . ARG   A 4   ? 0.16942 0.25201 0.27964 -0.01726 0.00456  0.05408  4   ARG   A CA  
24   C  C   . ARG   A 4   ? 0.14842 0.21825 0.23946 -0.01438 0.00125  0.04576  4   ARG   A C   
25   O  O   . ARG   A 4   ? 0.16340 0.23254 0.24284 -0.00917 0.00669  0.04190  4   ARG   A O   
26   C  CB  . ARG   A 4   ? 0.14347 0.23749 0.27047 -0.01429 0.00487  0.05546  4   ARG   A CB  
27   C  CG  . ARG   A 4   ? 0.15185 0.25555 0.29697 -0.01808 0.00409  0.06280  4   ARG   A CG  
28   C  CD  . ARG   A 4   ? 0.15276 0.25001 0.29864 -0.02572 -0.00844 0.06257  4   ARG   A CD  
29   N  NE  . ARG   A 4   ? 0.15755 0.26282 0.31781 -0.02877 -0.01102 0.06805  4   ARG   A NE  
30   C  CZ  . ARG   A 4   ? 0.16764 0.26933 0.32853 -0.03665 -0.02098 0.06819  4   ARG   A CZ  
31   N  NH1 . ARG   A 4   ? 0.21603 0.30506 0.36292 -0.04172 -0.02832 0.06233  4   ARG   A NH1 
32   N  NH2 . ARG   A 4   ? 0.11428 0.22540 0.28951 -0.03972 -0.02311 0.07384  4   ARG   A NH2 
33   N  N   . LYS   A 5   ? 0.14693 0.20765 0.23448 -0.01837 -0.00763 0.04282  5   LYS   A N   
34   C  CA  . LYS   A 5   ? 0.18130 0.23255 0.25405 -0.01538 -0.01031 0.03578  5   LYS   A CA  
35   C  C   . LYS   A 5   ? 0.19214 0.24882 0.26992 -0.01036 -0.00902 0.03386  5   LYS   A C   
36   O  O   . LYS   A 5   ? 0.18457 0.24571 0.27341 -0.01177 -0.01387 0.03646  5   LYS   A O   
37   C  CB  . LYS   A 5   ? 0.23014 0.27099 0.29684 -0.02078 -0.01864 0.03306  5   LYS   A CB  
38   C  CG  . LYS   A 5   ? 0.25396 0.28308 0.30418 -0.01888 -0.01815 0.02801  5   LYS   A CG  
39   C  CD  . LYS   A 5   ? 0.28512 0.30263 0.33050 -0.02457 -0.02254 0.02596  5   LYS   A CD  
40   C  CE  . LYS   A 5   ? 0.30335 0.31083 0.33779 -0.02161 -0.01936 0.02357  5   LYS   A CE  
41   N  NZ  . LYS   A 5   ? 0.27007 0.27221 0.29287 -0.01886 -0.02080 0.01783  5   LYS   A NZ  
42   N  N   . MET   A 6   ? 0.14648 0.20311 0.21711 -0.00482 -0.00249 0.02979  6   MET   A N   
43   C  CA  . MET   A 6   ? 0.15241 0.21213 0.22887 0.00060  0.00153  0.02712  6   MET   A CA  
44   C  C   . MET   A 6   ? 0.13958 0.18955 0.20497 0.00234  -0.00099 0.02072  6   MET   A C   
45   O  O   . MET   A 6   ? 0.16666 0.21127 0.21745 0.00207  -0.00035 0.01630  6   MET   A O   
46   C  CB  . MET   A 6   ? 0.15047 0.21665 0.22628 0.00480  0.01227  0.02545  6   MET   A CB  
47   C  CG  . MET   A 6   ? 0.16645 0.23804 0.25637 0.01013  0.01825  0.02495  6   MET   A CG  
48   S  SD  . MET   A 6   ? 0.26181 0.34130 0.34839 0.01447  0.03250  0.02194  6   MET   A SD  
49   C  CE  . MET   A 6   ? 0.16162 0.25579 0.26699 0.01180  0.03421  0.03382  6   MET   A CE  
50   N  N   . ALA   A 7   ? 0.13863 0.18753 0.21245 0.00392  -0.00400 0.02155  7   ALA   A N   
51   C  CA  . ALA   A 7   ? 0.12698 0.16704 0.19335 0.00558  -0.00523 0.01665  7   ALA   A CA  
52   C  C   . ALA   A 7   ? 0.13267 0.17167 0.20370 0.01113  0.00305  0.01177  7   ALA   A C   
53   O  O   . ALA   A 7   ? 0.09135 0.13714 0.17360 0.01465  0.00967  0.01302  7   ALA   A O   
54   C  CB  . ALA   A 7   ? 0.14906 0.18760 0.22083 0.00394  -0.01303 0.02134  7   ALA   A CB  
55   N  N   . PHE   A 8   ? 0.13795 0.16798 0.20065 0.01163  0.00338  0.00563  8   PHE   A N   
56   C  CA  . PHE   A 8   ? 0.12217 0.14772 0.19004 0.01613  0.01090  -0.00032 8   PHE   A CA  
57   C  C   . PHE   A 8   ? 0.09531 0.12037 0.18281 0.02016  0.01050  0.00578  8   PHE   A C   
58   O  O   . PHE   A 8   ? 0.10291 0.12933 0.19478 0.01810  0.00233  0.01353  8   PHE   A O   
59   C  CB  . PHE   A 8   ? 0.13573 0.15145 0.19063 0.01401  0.01056  -0.00860 8   PHE   A CB  
60   C  CG  . PHE   A 8   ? 0.15690 0.17535 0.19469 0.01102  0.01190  -0.01440 8   PHE   A CG  
61   C  CD1 . PHE   A 8   ? 0.23508 0.25557 0.26754 0.01259  0.02003  -0.02165 8   PHE   A CD1 
62   C  CD2 . PHE   A 8   ? 0.16670 0.18635 0.19384 0.00694  0.00548  -0.01222 8   PHE   A CD2 
63   C  CE1 . PHE   A 8   ? 0.29477 0.32007 0.31047 0.00940  0.02027  -0.02537 8   PHE   A CE1 
64   C  CE2 . PHE   A 8   ? 0.21350 0.23757 0.22694 0.00470  0.00611  -0.01536 8   PHE   A CE2 
65   C  CZ  . PHE   A 8   ? 0.22493 0.25252 0.23216 0.00557  0.01279  -0.02139 8   PHE   A CZ  
66   N  N   . PRO   A 9   ? 0.13377 0.15754 0.23348 0.02614  0.01953  0.00291  9   PRO   A N   
67   C  CA  . PRO   A 9   ? 0.11271 0.13521 0.23381 0.03121  0.01971  0.00987  9   PRO   A CA  
68   C  C   . PRO   A 9   ? 0.13991 0.15140 0.25727 0.02901  0.01375  0.01064  9   PRO   A C   
69   O  O   . PRO   A 9   ? 0.15207 0.15324 0.25573 0.02631  0.01516  0.00152  9   PRO   A O   
70   C  CB  . PRO   A 9   ? 0.14792 0.16656 0.27897 0.03835  0.03316  0.00274  9   PRO   A CB  
71   C  CG  . PRO   A 9   ? 0.13588 0.15994 0.25181 0.03661  0.03943  -0.00514 9   PRO   A CG  
72   C  CD  . PRO   A 9   ? 0.12589 0.14869 0.21943 0.02867  0.03057  -0.00713 9   PRO   A CD  
73   N  N   . SER   A 10  ? 0.12265 0.13810 0.25170 0.02925  0.00638  0.02245  10  SER   A N   
74   C  CA  . SER   A 10  ? 0.15072 0.15898 0.27295 0.02562  -0.00064 0.02564  10  SER   A CA  
75   C  C   . SER   A 10  ? 0.12364 0.12123 0.26060 0.03034  0.00318  0.02803  10  SER   A C   
76   O  O   . SER   A 10  ? 0.11500 0.10580 0.24735 0.02734  -0.00128 0.03112  10  SER   A O   
77   C  CB  . SER   A 10  ? 0.11040 0.12903 0.23154 0.02151  -0.01173 0.03693  10  SER   A CB  
78   O  OG  . SER   A 10  ? 0.08281 0.11209 0.22319 0.02475  -0.01339 0.04730  10  SER   A OG  
79   N  N   . GLY   A 11  ? 0.13048 0.12585 0.28474 0.03748  0.01230  0.02660  11  GLY   A N   
80   C  CA  . GLY   A 11  ? 0.12183 0.10825 0.28704 0.03991  0.01555  0.03012  11  GLY   A CA  
81   C  C   . GLY   A 11  ? 0.15308 0.12292 0.31135 0.03713  0.01657  0.02379  11  GLY   A C   
82   O  O   . GLY   A 11  ? 0.17419 0.14036 0.33779 0.03599  0.01339  0.03195  11  GLY   A O   
83   N  N   . LYS   A 12  ? 0.13866 0.09919 0.28492 0.03517  0.02122  0.00910  12  LYS   A N   
84   C  CA  . LYS   A 12  ? 0.15090 0.09587 0.29032 0.03060  0.02223  0.00158  12  LYS   A CA  
85   C  C   . LYS   A 12  ? 0.15317 0.10027 0.28523 0.02470  0.01227  0.01048  12  LYS   A C   
86   O  O   . LYS   A 12  ? 0.20210 0.13861 0.33599 0.02167  0.01207  0.01110  12  LYS   A O   
87   C  CB  . LYS   A 12  ? 0.18709 0.12745 0.30828 0.02623  0.02666  -0.01606 12  LYS   A CB  
88   C  CG  . LYS   A 12  ? 0.23083 0.16678 0.35437 0.03083  0.03806  -0.02768 12  LYS   A CG  
89   C  CD  . LYS   A 12  ? 0.28467 0.21357 0.38850 0.02453  0.04125  -0.04535 12  LYS   A CD  
90   C  CE  . LYS   A 12  ? 0.36723 0.30168 0.46229 0.02726  0.04984  -0.05530 12  LYS   A CE  
91   N  NZ  . LYS   A 12  ? 0.36950 0.29991 0.47685 0.03407  0.05891  -0.05510 12  LYS   A NZ  
92   N  N   . VAL   A 13  ? 0.15984 0.12140 0.28088 0.02190  0.00458  0.01644  13  VAL   A N   
93   C  CA  . VAL   A 13  ? 0.15140 0.11631 0.26286 0.01643  -0.00370 0.02432  13  VAL   A CA  
94   C  C   . VAL   A 13  ? 0.16179 0.13024 0.28716 0.01917  -0.00838 0.04094  13  VAL   A C   
95   O  O   . VAL   A 13  ? 0.13274 0.09772 0.25681 0.01614  -0.01104 0.04754  13  VAL   A O   
96   C  CB  . VAL   A 13  ? 0.11565 0.09211 0.20877 0.01227  -0.00879 0.02206  13  VAL   A CB  
97   C  CG1 . VAL   A 13  ? 0.14452 0.12444 0.22673 0.00727  -0.01573 0.02911  13  VAL   A CG1 
98   C  CG2 . VAL   A 13  ? 0.12726 0.10102 0.20729 0.00945  -0.00484 0.00797  13  VAL   A CG2 
99   N  N   . GLU   A 14  ? 0.12839 0.10734 0.26417 0.02333  -0.00897 0.04719  14  GLU   A N   
100  C  CA  . GLU   A 14  ? 0.11827 0.10601 0.26143 0.02325  -0.01334 0.06059  14  GLU   A CA  
101  C  C   . GLU   A 14  ? 0.15159 0.12934 0.30463 0.02443  -0.00946 0.06411  14  GLU   A C   
102  O  O   . GLU   A 14  ? 0.16267 0.14490 0.31526 0.02198  -0.01426 0.07479  14  GLU   A O   
103  C  CB  . GLU   A 14  ? 0.13972 0.13821 0.29606 0.02727  -0.01208 0.06460  14  GLU   A CB  
104  C  CG  . GLU   A 14  ? 0.10745 0.11797 0.25613 0.02510  -0.01650 0.06309  14  GLU   A CG  
105  C  CD  . GLU   A 14  ? 0.12268 0.14188 0.28639 0.02924  -0.01273 0.06518  14  GLU   A CD  
106  O  OE1 . GLU   A 14  ? 0.12708 0.15075 0.30477 0.03134  -0.01270 0.07431  14  GLU   A OE1 
107  O  OE2 . GLU   A 14  ? 0.11605 0.13849 0.27849 0.03044  -0.00943 0.05839  14  GLU   A OE2 
108  N  N   . GLY   A 15  ? 0.16320 0.12749 0.32445 0.02771  -0.00048 0.05468  15  GLY   A N   
109  C  CA  . GLY   A 15  ? 0.16709 0.12065 0.33861 0.02842  0.00358  0.05716  15  GLY   A CA  
110  C  C   . GLY   A 15  ? 0.20036 0.14719 0.36222 0.02247  0.00075  0.05778  15  GLY   A C   
111  O  O   . GLY   A 15  ? 0.17116 0.10977 0.34171 0.02229  0.00347  0.06117  15  GLY   A O   
112  N  N   . CYS   A 16  ? 0.14520 0.09544 0.29037 0.01754  -0.00422 0.05512  16  CYS   A N   
113  C  CA  . CYS   A 16  ? 0.14642 0.09189 0.28246 0.01141  -0.00623 0.05598  16  CYS   A CA  
114  C  C   . CYS   A 16  ? 0.14163 0.09972 0.26748 0.00822  -0.01378 0.06838  16  CYS   A C   
115  O  O   . CYS   A 16  ? 0.15599 0.11238 0.27377 0.00325  -0.01484 0.07050  16  CYS   A O   
116  C  CB  . CYS   A 16  ? 0.13949 0.07847 0.26380 0.00699  -0.00501 0.04253  16  CYS   A CB  
117  S  SG  . CYS   A 16  ? 0.17275 0.09757 0.30164 0.00824  0.00389  0.02374  16  CYS   A SG  
118  N  N   . MET   A 17  ? 0.13730 0.10872 0.26187 0.01006  -0.01873 0.07548  17  MET   A N   
119  C  CA  . MET   A 17  ? 0.16173 0.14513 0.27091 0.00569  -0.02581 0.08308  17  MET   A CA  
120  C  C   . MET   A 17  ? 0.15364 0.14152 0.26852 0.00528  -0.02738 0.09575  17  MET   A C   
121  O  O   . MET   A 17  ? 0.15623 0.14421 0.28847 0.00948  -0.02561 0.10137  17  MET   A O   
122  C  CB  . MET   A 17  ? 0.12779 0.12311 0.23075 0.00586  -0.03084 0.08257  17  MET   A CB  
123  C  CG  . MET   A 17  ? 0.12692 0.11862 0.22271 0.00590  -0.02972 0.07111  17  MET   A CG  
124  S  SD  . MET   A 17  ? 0.12887 0.11410 0.20661 0.00076  -0.02891 0.06304  17  MET   A SD  
125  C  CE  . MET   A 17  ? 0.13156 0.12448 0.19437 -0.00436 -0.03360 0.07319  17  MET   A CE  
126  N  N   . VAL   A 18  ? 0.16032 0.15088 0.26184 0.00049  -0.02946 0.10023  18  VAL   A N   
127  C  CA  . VAL   A 18  ? 0.20856 0.20346 0.31319 -0.00055 -0.03065 0.11263  18  VAL   A CA  
128  C  C   . VAL   A 18  ? 0.19694 0.20343 0.27991 -0.00562 -0.03575 0.11672  18  VAL   A C   
129  O  O   . VAL   A 18  ? 0.16679 0.17533 0.23297 -0.00841 -0.03711 0.10909  18  VAL   A O   
130  C  CB  . VAL   A 18  ? 0.17657 0.15955 0.28984 -0.00122 -0.02499 0.11366  18  VAL   A CB  
131  C  CG1 . VAL   A 18  ? 0.20398 0.17336 0.33646 0.00313  -0.01910 0.10683  18  VAL   A CG1 
132  C  CG2 . VAL   A 18  ? 0.16823 0.14812 0.26648 -0.00650 -0.02334 0.10821  18  VAL   A CG2 
133  N  N   . GLN   A 19  ? 0.21513 0.22912 0.29859 -0.00667 -0.03823 0.12869  19  GLN   A N   
134  C  CA  . GLN   A 19  ? 0.25164 0.27603 0.31402 -0.01156 -0.04209 0.13287  19  GLN   A CA  
135  C  C   . GLN   A 19  ? 0.21963 0.24010 0.27690 -0.01401 -0.03766 0.13676  19  GLN   A C   
136  O  O   . GLN   A 19  ? 0.21802 0.23360 0.29117 -0.01231 -0.03480 0.14445  19  GLN   A O   
137  C  CB  . GLN   A 19  ? 0.26329 0.30010 0.32888 -0.01174 -0.04806 0.14453  19  GLN   A CB  
138  C  CG  . GLN   A 19  ? 0.29761 0.34560 0.33907 -0.01718 -0.05306 0.14593  19  GLN   A CG  
139  C  CD  . GLN   A 19  ? 0.30528 0.36652 0.35042 -0.01811 -0.06033 0.15603  19  GLN   A CD  
140  O  OE1 . GLN   A 19  ? 0.37632 0.43949 0.44379 -0.01428 -0.06102 0.16521  19  GLN   A OE1 
141  N  NE2 . GLN   A 19  ? 0.37571 0.44605 0.39943 -0.02334 -0.06561 0.15394  19  GLN   A NE2 
142  N  N   . VAL   A 20  ? 0.23915 0.26172 0.27535 -0.01796 -0.03643 0.13156  20  VAL   A N   
143  C  CA  . VAL   A 20  ? 0.25480 0.27618 0.28466 -0.02078 -0.03156 0.13555  20  VAL   A CA  
144  C  C   . VAL   A 20  ? 0.25061 0.28314 0.25821 -0.02426 -0.03373 0.13994  20  VAL   A C   
145  O  O   . VAL   A 20  ? 0.23211 0.26866 0.22104 -0.02610 -0.03562 0.13186  20  VAL   A O   
146  C  CB  . VAL   A 20  ? 0.23948 0.25360 0.26542 -0.02231 -0.02596 0.12544  20  VAL   A CB  
147  C  CG1 . VAL   A 20  ? 0.22631 0.24156 0.24732 -0.02552 -0.02048 0.13062  20  VAL   A CG1 
148  C  CG2 . VAL   A 20  ? 0.20222 0.20452 0.24808 -0.01980 -0.02386 0.11966  20  VAL   A CG2 
149  N  N   . THR   A 21  ? 0.23545 0.27215 0.24434 -0.02535 -0.03298 0.15216  21  THR   A N   
150  C  CA  . THR   A 21  ? 0.30407 0.35113 0.29085 -0.02883 -0.03446 0.15692  21  THR   A CA  
151  C  C   . THR   A 21  ? 0.30179 0.34813 0.28305 -0.03102 -0.02721 0.16174  21  THR   A C   
152  O  O   . THR   A 21  ? 0.31960 0.36142 0.31892 -0.03017 -0.02417 0.16991  21  THR   A O   
153  C  CB  . THR   A 21  ? 0.29492 0.35159 0.28618 -0.02869 -0.04147 0.16951  21  THR   A CB  
154  O  OG1 . THR   A 21  ? 0.29702 0.35601 0.29417 -0.02715 -0.04781 0.16508  21  THR   A OG1 
155  C  CG2 . THR   A 21  ? 0.34809 0.41537 0.31381 -0.03300 -0.04316 0.17367  21  THR   A CG2 
156  N  N   . CYS   A 22  ? 0.31410 0.36447 0.27109 -0.03383 -0.02379 0.15632  22  CYS   A N   
157  C  CA  . CYS   A 22  ? 0.32099 0.37313 0.27028 -0.03608 -0.01617 0.16142  22  CYS   A CA  
158  C  C   . CYS   A 22  ? 0.35156 0.41251 0.27208 -0.03877 -0.01653 0.16151  22  CYS   A C   
159  O  O   . CYS   A 22  ? 0.35133 0.41222 0.25353 -0.03934 -0.01662 0.14935  22  CYS   A O   
160  C  CB  . CYS   A 22  ? 0.29378 0.33970 0.24548 -0.03625 -0.00805 0.15193  22  CYS   A CB  
161  S  SG  . CYS   A 22  ? 0.37455 0.42416 0.31980 -0.03915 0.00268  0.15783  22  CYS   A SG  
162  N  N   . GLY   A 23  ? 0.32940 0.39733 0.24592 -0.04049 -0.01683 0.17505  23  GLY   A N   
163  C  CA  . GLY   A 23  ? 0.35985 0.43666 0.24856 -0.04345 -0.01822 0.17651  23  GLY   A CA  
164  C  C   . GLY   A 23  ? 0.38669 0.46809 0.26832 -0.04408 -0.02862 0.17273  23  GLY   A C   
165  O  O   . GLY   A 23  ? 0.42679 0.51152 0.32617 -0.04292 -0.03634 0.18141  23  GLY   A O   
166  N  N   . THR   A 24  ? 0.41629 0.49779 0.27364 -0.04592 -0.02857 0.15962  24  THR   A N   
167  C  CA  . THR   A 24  ? 0.40520 0.49070 0.25646 -0.04752 -0.03846 0.15431  24  THR   A CA  
168  C  C   . THR   A 24  ? 0.38828 0.46543 0.24724 -0.04550 -0.03910 0.13979  24  THR   A C   
169  O  O   . THR   A 24  ? 0.44977 0.52904 0.30278 -0.04732 -0.04612 0.13287  24  THR   A O   
170  C  CB  . THR   A 24  ? 0.45816 0.54942 0.27651 -0.05192 -0.03942 0.14930  24  THR   A CB  
171  O  OG1 . THR   A 24  ? 0.46848 0.55230 0.26851 -0.05138 -0.02874 0.13663  24  THR   A OG1 
172  C  CG2 . THR   A 24  ? 0.42007 0.52200 0.23032 -0.05448 -0.04106 0.16542  24  THR   A CG2 
173  N  N   . THR   A 25  ? 0.38093 0.44930 0.25301 -0.04234 -0.03210 0.13536  25  THR   A N   
174  C  CA  . THR   A 25  ? 0.35371 0.41451 0.23312 -0.04034 -0.03218 0.12258  25  THR   A CA  
175  C  C   . THR   A 25  ? 0.31827 0.37666 0.22660 -0.03734 -0.03670 0.12798  25  THR   A C   
176  O  O   . THR   A 25  ? 0.33357 0.38946 0.25962 -0.03542 -0.03367 0.13661  25  THR   A O   
177  C  CB  . THR   A 25  ? 0.38700 0.44072 0.26211 -0.03892 -0.02169 0.11379  25  THR   A CB  
178  O  OG1 . THR   A 25  ? 0.44078 0.49611 0.28927 -0.04081 -0.01584 0.10836  25  THR   A OG1 
179  C  CG2 . THR   A 25  ? 0.35082 0.39771 0.23265 -0.03703 -0.02230 0.10137  25  THR   A CG2 
180  N  N   . THR   A 26  ? 0.31495 0.37353 0.22836 -0.03703 -0.04333 0.12248  26  THR   A N   
181  C  CA  . THR   A 26  ? 0.28347 0.33917 0.22299 -0.03359 -0.04655 0.12545  26  THR   A CA  
182  C  C   . THR   A 26  ? 0.27284 0.32166 0.21352 -0.03235 -0.04575 0.11178  26  THR   A C   
183  O  O   . THR   A 26  ? 0.31875 0.36886 0.24431 -0.03476 -0.04822 0.10262  26  THR   A O   
184  C  CB  . THR   A 26  ? 0.27831 0.34322 0.22607 -0.03419 -0.05524 0.13456  26  THR   A CB  
185  O  OG1 . THR   A 26  ? 0.36385 0.43439 0.31669 -0.03427 -0.05552 0.14953  26  THR   A OG1 
186  C  CG2 . THR   A 26  ? 0.28767 0.34967 0.25956 -0.03038 -0.05772 0.13432  26  THR   A CG2 
187  N  N   . LEU   A 27  ? 0.22137 0.26242 0.17922 -0.02900 -0.04206 0.11013  27  LEU   A N   
188  C  CA  . LEU   A 27  ? 0.23546 0.27073 0.19624 -0.02759 -0.04182 0.09883  27  LEU   A CA  
189  C  C   . LEU   A 27  ? 0.22221 0.25176 0.20810 -0.02351 -0.04150 0.10161  27  LEU   A C   
190  O  O   . LEU   A 27  ? 0.21129 0.24154 0.21249 -0.02168 -0.04221 0.11153  27  LEU   A O   
191  C  CB  . LEU   A 27  ? 0.23154 0.26217 0.17857 -0.02852 -0.03526 0.08947  27  LEU   A CB  
192  C  CG  . LEU   A 27  ? 0.21945 0.24803 0.16719 -0.02869 -0.02763 0.09338  27  LEU   A CG  
193  C  CD1 . LEU   A 27  ? 0.20054 0.22289 0.17133 -0.02653 -0.02588 0.09703  27  LEU   A CD1 
194  C  CD2 . LEU   A 27  ? 0.24162 0.26876 0.17400 -0.02960 -0.02131 0.08368  27  LEU   A CD2 
195  N  N   . ASN   A 28  ? 0.21270 0.23608 0.20284 -0.02190 -0.04004 0.09260  28  ASN   A N   
196  C  CA  . ASN   A 28  ? 0.18767 0.20447 0.19963 -0.01791 -0.03921 0.09288  28  ASN   A CA  
197  C  C   . ASN   A 28  ? 0.14467 0.15249 0.16343 -0.01767 -0.03319 0.09125  28  ASN   A C   
198  O  O   . ASN   A 28  ? 0.14234 0.14953 0.14927 -0.02020 -0.02993 0.08674  28  ASN   A O   
199  C  CB  . ASN   A 28  ? 0.15395 0.16993 0.16779 -0.01636 -0.04163 0.08434  28  ASN   A CB  
200  C  CG  . ASN   A 28  ? 0.18188 0.20681 0.19108 -0.01783 -0.04751 0.08537  28  ASN   A CG  
201  O  OD1 . ASN   A 28  ? 0.19384 0.22316 0.21677 -0.01600 -0.05023 0.09256  28  ASN   A OD1 
202  N  ND2 . ASN   A 28  ? 0.18818 0.21562 0.17876 -0.02146 -0.04914 0.07814  28  ASN   A ND2 
203  N  N   . GLY   A 29  ? 0.18369 0.18429 0.22285 -0.01479 -0.03126 0.09405  29  GLY   A N   
204  C  CA  . GLY   A 29  ? 0.14126 0.13154 0.18973 -0.01549 -0.02597 0.09023  29  GLY   A CA  
205  C  C   . GLY   A 29  ? 0.13481 0.11558 0.19904 -0.01193 -0.02472 0.08318  29  GLY   A C   
206  O  O   . GLY   A 29  ? 0.15706 0.13949 0.22930 -0.00781 -0.02678 0.08409  29  GLY   A O   
207  N  N   . LEU   A 30  ? 0.16805 0.13964 0.23698 -0.01409 -0.02073 0.07553  30  LEU   A N   
208  C  CA  . LEU   A 30  ? 0.17693 0.13861 0.25740 -0.01178 -0.01824 0.06509  30  LEU   A CA  
209  C  C   . LEU   A 30  ? 0.15989 0.11040 0.25446 -0.01311 -0.01343 0.06319  30  LEU   A C   
210  O  O   . LEU   A 30  ? 0.15181 0.10053 0.24500 -0.01863 -0.01158 0.06172  30  LEU   A O   
211  C  CB  . LEU   A 30  ? 0.13374 0.09955 0.20161 -0.01355 -0.01748 0.05042  30  LEU   A CB  
212  C  CG  . LEU   A 30  ? 0.14855 0.10765 0.22247 -0.01172 -0.01464 0.03737  30  LEU   A CG  
213  C  CD1 . LEU   A 30  ? 0.16936 0.13134 0.24543 -0.00597 -0.01563 0.03660  30  LEU   A CD1 
214  C  CD2 . LEU   A 30  ? 0.15727 0.11964 0.22146 -0.01549 -0.01378 0.02553  30  LEU   A CD2 
215  N  N   . TRP   A 31  ? 0.14713 0.09106 0.25555 -0.00821 -0.01107 0.06288  31  TRP   A N   
216  C  CA  . TRP   A 31  ? 0.16252 0.09575 0.28444 -0.00861 -0.00663 0.06323  31  TRP   A CA  
217  C  C   . TRP   A 31  ? 0.16735 0.08753 0.29517 -0.00866 -0.00172 0.04761  31  TRP   A C   
218  O  O   . TRP   A 31  ? 0.16784 0.08552 0.30093 -0.00314 0.00052  0.04266  31  TRP   A O   
219  C  CB  . TRP   A 31  ? 0.17237 0.10825 0.30593 -0.00313 -0.00695 0.07517  31  TRP   A CB  
220  C  CG  . TRP   A 31  ? 0.19098 0.11502 0.34033 -0.00279 -0.00219 0.07719  31  TRP   A CG  
221  C  CD1 . TRP   A 31  ? 0.20025 0.11436 0.35154 -0.00837 0.00078  0.07299  31  TRP   A CD1 
222  C  CD2 . TRP   A 31  ? 0.20412 0.12528 0.37057 0.00313  0.00015  0.08406  31  TRP   A CD2 
223  N  NE1 . TRP   A 31  ? 0.21925 0.12292 0.38686 -0.00636 0.00477  0.07653  31  TRP   A NE1 
224  C  CE2 . TRP   A 31  ? 0.24594 0.15369 0.42347 0.00105  0.00473  0.08364  31  TRP   A CE2 
225  C  CE3 . TRP   A 31  ? 0.23405 0.16350 0.40856 0.00951  -0.00126 0.09106  31  TRP   A CE3 
226  C  CZ2 . TRP   A 31  ? 0.24721 0.14824 0.44380 0.00589  0.00849  0.08993  31  TRP   A CZ2 
227  C  CZ3 . TRP   A 31  ? 0.22968 0.15418 0.42384 0.01423  0.00240  0.09783  31  TRP   A CZ3 
228  C  CH2 . TRP   A 31  ? 0.24723 0.15700 0.45221 0.01276  0.00748  0.09712  31  TRP   A CH2 
229  N  N   . LEU   A 32  ? 0.17296 0.08613 0.29931 -0.01534 0.00012  0.03964  32  LEU   A N   
230  C  CA  . LEU   A 32  ? 0.18039 0.08282 0.30718 -0.01761 0.00382  0.02294  32  LEU   A CA  
231  C  C   . LEU   A 32  ? 0.19886 0.09024 0.33285 -0.02293 0.00651  0.02087  32  LEU   A C   
232  O  O   . LEU   A 32  ? 0.21395 0.10911 0.34662 -0.02894 0.00454  0.02651  32  LEU   A O   
233  C  CB  . LEU   A 32  ? 0.16785 0.07656 0.28143 -0.02271 0.00122  0.01206  32  LEU   A CB  
234  C  CG  . LEU   A 32  ? 0.15075 0.06938 0.25709 -0.01839 -0.00169 0.01363  32  LEU   A CG  
235  C  CD1 . LEU   A 32  ? 0.13937 0.06922 0.23082 -0.02356 -0.00497 0.00624  32  LEU   A CD1 
236  C  CD2 . LEU   A 32  ? 0.18081 0.09435 0.29076 -0.01178 0.00225  0.00600  32  LEU   A CD2 
237  N  N   . ASP   A 33  ? 0.21628 0.09418 0.35824 -0.02079 0.01144  0.01311  33  ASP   A N   
238  C  CA  . ASP   A 33  ? 0.23794 0.10297 0.38877 -0.02544 0.01415  0.01224  33  ASP   A CA  
239  C  C   . ASP   A 33  ? 0.23801 0.10834 0.39694 -0.02468 0.01243  0.03092  33  ASP   A C   
240  O  O   . ASP   A 33  ? 0.23147 0.10942 0.39445 -0.01759 0.01140  0.04296  33  ASP   A O   
241  C  CB  . ASP   A 33  ? 0.24248 0.10503 0.38376 -0.03584 0.01248  -0.00093 33  ASP   A CB  
242  C  CG  . ASP   A 33  ? 0.25694 0.11772 0.38701 -0.03614 0.01341  -0.01840 33  ASP   A CG  
243  O  OD1 . ASP   A 33  ? 0.25928 0.11011 0.39315 -0.03061 0.01864  -0.02513 33  ASP   A OD1 
244  O  OD2 . ASP   A 33  ? 0.27314 0.14345 0.39068 -0.04194 0.00926  -0.02526 33  ASP   A OD2 
245  N  N   . ASP   A 34  ? 0.24530 0.11439 0.40572 -0.03218 0.01159  0.03465  34  ASP   A N   
246  C  CA  . ASP   A 34  ? 0.24809 0.12285 0.41534 -0.03117 0.01076  0.05268  34  ASP   A CA  
247  C  C   . ASP   A 34  ? 0.23086 0.12277 0.38666 -0.03420 0.00675  0.06108  34  ASP   A C   
248  O  O   . ASP   A 34  ? 0.23675 0.13299 0.39540 -0.03706 0.00678  0.07274  34  ASP   A O   
249  C  CB  . ASP   A 34  ? 0.28466 0.14649 0.46400 -0.03646 0.01379  0.05432  34  ASP   A CB  
250  C  CG  . ASP   A 34  ? 0.28677 0.14740 0.46059 -0.04747 0.01274  0.04512  34  ASP   A CG  
251  O  OD1 . ASP   A 34  ? 0.25924 0.12784 0.42066 -0.05071 0.01001  0.03543  34  ASP   A OD1 
252  O  OD2 . ASP   A 34  ? 0.29291 0.14502 0.47607 -0.05331 0.01448  0.04784  34  ASP   A OD2 
253  N  N   . VAL   A 35  ? 0.21136 0.11345 0.35446 -0.03307 0.00387  0.05632  35  VAL   A N   
254  C  CA  . VAL   A 35  ? 0.19717 0.11482 0.32900 -0.03557 0.00104  0.06323  35  VAL   A CA  
255  C  C   . VAL   A 35  ? 0.18289 0.11037 0.30536 -0.02921 -0.00205 0.06761  35  VAL   A C   
256  O  O   . VAL   A 35  ? 0.17639 0.10098 0.29764 -0.02555 -0.00260 0.05916  35  VAL   A O   
257  C  CB  . VAL   A 35  ? 0.18941 0.11101 0.31500 -0.04300 0.00029  0.05212  35  VAL   A CB  
258  C  CG1 . VAL   A 35  ? 0.18347 0.12168 0.29861 -0.04444 -0.00136 0.05903  35  VAL   A CG1 
259  C  CG2 . VAL   A 35  ? 0.21868 0.13244 0.35298 -0.05068 0.00226  0.04823  35  VAL   A CG2 
260  N  N   . VAL   A 36  ? 0.17969 0.11928 0.29414 -0.02859 -0.00395 0.08001  36  VAL   A N   
261  C  CA  . VAL   A 36  ? 0.16835 0.11871 0.27035 -0.02461 -0.00770 0.08373  36  VAL   A CA  
262  C  C   . VAL   A 36  ? 0.15774 0.11827 0.24518 -0.02880 -0.00812 0.08198  36  VAL   A C   
263  O  O   . VAL   A 36  ? 0.16246 0.12859 0.24712 -0.03267 -0.00592 0.08760  36  VAL   A O   
264  C  CB  . VAL   A 36  ? 0.17677 0.13438 0.27782 -0.02106 -0.00987 0.09801  36  VAL   A CB  
265  C  CG1 . VAL   A 36  ? 0.16748 0.13779 0.25167 -0.01923 -0.01445 0.10033  36  VAL   A CG1 
266  C  CG2 . VAL   A 36  ? 0.18720 0.13677 0.30531 -0.01602 -0.00919 0.10085  36  VAL   A CG2 
267  N  N   . TYR   A 37  ? 0.16556 0.12903 0.24450 -0.02770 -0.01034 0.07482  37  TYR   A N   
268  C  CA  . TYR   A 37  ? 0.17359 0.14665 0.23942 -0.03073 -0.01027 0.07196  37  TYR   A CA  
269  C  C   . TYR   A 37  ? 0.16301 0.14542 0.21177 -0.02741 -0.01298 0.07686  37  TYR   A C   
270  O  O   . TYR   A 37  ? 0.13913 0.12039 0.18712 -0.02338 -0.01676 0.07725  37  TYR   A O   
271  C  CB  . TYR   A 37  ? 0.12825 0.10100 0.19231 -0.03032 -0.01075 0.05571  37  TYR   A CB  
272  C  CG  . TYR   A 37  ? 0.14536 0.10958 0.22297 -0.03494 -0.00919 0.04796  37  TYR   A CG  
273  C  CD1 . TYR   A 37  ? 0.13681 0.08675 0.22682 -0.03387 -0.00856 0.04431  37  TYR   A CD1 
274  C  CD2 . TYR   A 37  ? 0.16360 0.13421 0.24236 -0.04072 -0.00817 0.04401  37  TYR   A CD2 
275  C  CE1 . TYR   A 37  ? 0.18767 0.12935 0.28590 -0.03866 -0.00685 0.03424  37  TYR   A CE1 
276  C  CE2 . TYR   A 37  ? 0.15000 0.11375 0.24033 -0.04688 -0.00808 0.03607  37  TYR   A CE2 
277  C  CZ  . TYR   A 37  ? 0.18271 0.13137 0.28032 -0.04584 -0.00737 0.03004  37  TYR   A CZ  
278  O  OH  . TYR   A 37  ? 0.21948 0.16157 0.32228 -0.05164 -0.00680 0.01970  37  TYR   A OH  
279  N  N   . CYS   A 38  ? 0.13912 0.13109 0.17448 -0.02942 -0.01077 0.08002  38  CYS   A N   
280  C  CA  . CYS   A 38  ? 0.16812 0.16763 0.18470 -0.02762 -0.01316 0.08282  38  CYS   A CA  
281  C  C   . CYS   A 38  ? 0.17204 0.17982 0.17423 -0.02910 -0.00820 0.07916  38  CYS   A C   
282  O  O   . CYS   A 38  ? 0.14589 0.15578 0.15518 -0.03158 -0.00312 0.07939  38  CYS   A O   
283  C  CB  . CYS   A 38  ? 0.15057 0.15272 0.16604 -0.02654 -0.01527 0.09302  38  CYS   A CB  
284  S  SG  . CYS   A 38  ? 0.22206 0.22984 0.23418 -0.02957 -0.00983 0.10247  38  CYS   A SG  
285  N  N   . PRO   A 39  ? 0.14373 0.15622 0.12692 -0.02779 -0.00914 0.07559  39  PRO   A N   
286  C  CA  . PRO   A 39  ? 0.15322 0.17204 0.12295 -0.02819 -0.00252 0.07160  39  PRO   A CA  
287  C  C   . PRO   A 39  ? 0.17686 0.20130 0.14308 -0.03075 0.00297  0.08168  39  PRO   A C   
288  O  O   . PRO   A 39  ? 0.18855 0.21314 0.15101 -0.03096 0.00028  0.08819  39  PRO   A O   
289  C  CB  . PRO   A 39  ? 0.17111 0.19054 0.12088 -0.02710 -0.00531 0.06583  39  PRO   A CB  
290  C  CG  . PRO   A 39  ? 0.16599 0.18028 0.12384 -0.02550 -0.01337 0.06304  39  PRO   A CG  
291  C  CD  . PRO   A 39  ? 0.17590 0.18765 0.15069 -0.02606 -0.01578 0.07339  39  PRO   A CD  
292  N  N   . ARG   A 40  ? 0.15611 0.18596 0.12602 -0.03161 0.01088  0.08101  40  ARG   A N   
293  C  CA  . ARG   A 40  ? 0.16989 0.20473 0.13886 -0.03300 0.01694  0.08799  40  ARG   A CA  
294  C  C   . ARG   A 40  ? 0.18800 0.22557 0.13266 -0.03198 0.01937  0.08747  40  ARG   A C   
295  O  O   . ARG   A 40  ? 0.20304 0.24361 0.14401 -0.03338 0.02244  0.09494  40  ARG   A O   
296  C  CB  . ARG   A 40  ? 0.16505 0.20686 0.14589 -0.03387 0.02499  0.08705  40  ARG   A CB  
297  C  CG  . ARG   A 40  ? 0.16518 0.21330 0.13439 -0.03055 0.03243  0.07945  40  ARG   A CG  
298  C  CD  . ARG   A 40  ? 0.16024 0.21788 0.14581 -0.03039 0.04015  0.07957  40  ARG   A CD  
299  N  NE  . ARG   A 40  ? 0.16001 0.22270 0.13776 -0.02526 0.04760  0.07184  40  ARG   A NE  
300  C  CZ  . ARG   A 40  ? 0.17599 0.24826 0.16512 -0.02294 0.05591  0.07126  40  ARG   A CZ  
301  N  NH1 . ARG   A 40  ? 0.17956 0.25887 0.18753 -0.02639 0.05718  0.07774  40  ARG   A NH1 
302  N  NH2 . ARG   A 40  ? 0.17062 0.24488 0.15293 -0.01682 0.06309  0.06383  40  ARG   A NH2 
303  N  N   . HIS   A 41  ? 0.22160 0.25737 0.14921 -0.03016 0.01773  0.07854  41  HIS   A N   
304  C  CA  . HIS   A 41  ? 0.29221 0.32906 0.19636 -0.03024 0.01996  0.07696  41  HIS   A CA  
305  C  C   . HIS   A 41  ? 0.27097 0.30772 0.17128 -0.03201 0.01191  0.08503  41  HIS   A C   
306  O  O   . HIS   A 41  ? 0.31106 0.34988 0.19191 -0.03292 0.01278  0.08512  41  HIS   A O   
307  C  CB  . HIS   A 41  ? 0.28592 0.31926 0.17249 -0.02846 0.02080  0.06395  41  HIS   A CB  
308  C  CG  . HIS   A 41  ? 0.30757 0.33605 0.19424 -0.02879 0.01016  0.05940  41  HIS   A CG  
309  N  ND1 . HIS   A 41  ? 0.30441 0.32935 0.19753 -0.02741 0.00875  0.05181  41  HIS   A ND1 
310  C  CD2 . HIS   A 41  ? 0.32475 0.35254 0.20654 -0.03041 0.00084  0.06150  41  HIS   A CD2 
311  C  CE1 . HIS   A 41  ? 0.30252 0.32375 0.19494 -0.02821 -0.00075 0.04931  41  HIS   A CE1 
312  N  NE2 . HIS   A 41  ? 0.34604 0.36972 0.23284 -0.02996 -0.00562 0.05511  41  HIS   A NE2 
313  N  N   . VAL   A 42  ? 0.24330 0.27807 0.16237 -0.03233 0.00495  0.09206  42  VAL   A N   
314  C  CA  . VAL   A 42  ? 0.24899 0.28552 0.16928 -0.03330 -0.00129 0.10205  42  VAL   A CA  
315  C  C   . VAL   A 42  ? 0.26399 0.30557 0.17778 -0.03510 0.00435  0.11118  42  VAL   A C   
316  O  O   . VAL   A 42  ? 0.29571 0.34120 0.20060 -0.03625 0.00042  0.11823  42  VAL   A O   
317  C  CB  . VAL   A 42  ? 0.23617 0.26830 0.18135 -0.03229 -0.00688 0.10795  42  VAL   A CB  
318  C  CG1 . VAL   A 42  ? 0.21737 0.24740 0.18051 -0.03328 -0.00135 0.11391  42  VAL   A CG1 
319  C  CG2 . VAL   A 42  ? 0.23116 0.26607 0.17816 -0.03211 -0.01443 0.11676  42  VAL   A CG2 
320  N  N   . ILE   A 43  ? 0.26427 0.30716 0.18317 -0.03565 0.01351  0.11197  43  ILE   A N   
321  C  CA  . ILE   A 43  ? 0.27019 0.31821 0.18446 -0.03759 0.01933  0.12151  43  ILE   A CA  
322  C  C   . ILE   A 43  ? 0.31396 0.36568 0.20097 -0.03776 0.02632  0.11649  43  ILE   A C   
323  O  O   . ILE   A 43  ? 0.33381 0.39021 0.21340 -0.03944 0.03214  0.12400  43  ILE   A O   
324  C  CB  . ILE   A 43  ? 0.27499 0.32410 0.20945 -0.03895 0.02622  0.12646  43  ILE   A CB  
325  C  CG1 . ILE   A 43  ? 0.25281 0.30478 0.18546 -0.03808 0.03538  0.11720  43  ILE   A CG1 
326  C  CG2 . ILE   A 43  ? 0.25902 0.30190 0.22011 -0.03924 0.02019  0.13036  43  ILE   A CG2 
327  C  CD1 . ILE   A 43  ? 0.23855 0.29280 0.19638 -0.03987 0.03984  0.12030  43  ILE   A CD1 
328  N  N   . CYS   A 44  ? 0.35296 0.40186 0.22456 -0.03610 0.02635  0.10389  44  CYS   A N   
329  C  CA  . CYS   A 44  ? 0.38434 0.43387 0.22966 -0.03571 0.03400  0.09674  44  CYS   A CA  
330  C  C   . CYS   A 44  ? 0.47489 0.52529 0.29885 -0.03739 0.02669  0.09700  44  CYS   A C   
331  O  O   . CYS   A 44  ? 0.45926 0.50900 0.28740 -0.03807 0.01531  0.09714  44  CYS   A O   
332  C  CB  . CYS   A 44  ? 0.44232 0.48719 0.28265 -0.03267 0.03914  0.08194  44  CYS   A CB  
333  S  SG  . CYS   A 44  ? 0.41531 0.46273 0.27908 -0.03081 0.04872  0.08099  44  CYS   A SG  
334  N  N   . THR   A 45  ? 0.53523 0.58790 0.33646 -0.03822 0.03372  0.09678  45  THR   A N   
335  C  CA  . THR   A 45  ? 0.62171 0.67611 0.39837 -0.04027 0.02811  0.09476  45  THR   A CA  
336  C  C   . THR   A 45  ? 0.66754 0.71571 0.42553 -0.03836 0.03154  0.07728  45  THR   A C   
337  O  O   . THR   A 45  ? 0.63784 0.68058 0.40347 -0.03489 0.03801  0.06798  45  THR   A O   
338  C  CB  . THR   A 45  ? 0.61397 0.67432 0.37451 -0.04243 0.03392  0.10436  45  THR   A CB  
339  O  OG1 . THR   A 45  ? 0.65626 0.71349 0.39936 -0.04030 0.04857  0.09560  45  THR   A OG1 
340  C  CG2 . THR   A 45  ? 0.58075 0.64587 0.36401 -0.04350 0.03483  0.12048  45  THR   A CG2 
341  N  N   . SER   A 46  ? 0.74200 0.79162 0.47625 -0.04088 0.02678  0.07300  46  SER   A N   
342  C  CA  . SER   A 46  ? 0.76117 0.80484 0.47618 -0.03973 0.02976  0.05585  46  SER   A CA  
343  C  C   . SER   A 46  ? 0.74528 0.78462 0.45341 -0.03445 0.04720  0.04860  46  SER   A C   
344  O  O   . SER   A 46  ? 0.72366 0.75743 0.44148 -0.03020 0.05262  0.03867  46  SER   A O   
345  C  CB  . SER   A 46  ? 0.80266 0.85047 0.49127 -0.04453 0.02313  0.05425  46  SER   A CB  
346  O  OG  . SER   A 46  ? 0.85520 0.90823 0.55212 -0.04922 0.00695  0.06017  46  SER   A OG  
347  N  N   . GLU   A 47  ? 0.77596 0.81889 0.46948 -0.03443 0.05669  0.05496  47  GLU   A N   
348  C  CA  . GLU   A 47  ? 0.75079 0.79096 0.43807 -0.02901 0.07506  0.04983  47  GLU   A CA  
349  C  C   . GLU   A 47  ? 0.74343 0.78289 0.45916 -0.02640 0.08289  0.05460  47  GLU   A C   
350  O  O   . GLU   A 47  ? 0.72037 0.75673 0.43892 -0.02078 0.09679  0.04727  47  GLU   A O   
351  C  CB  . GLU   A 47  ? 0.77292 0.81753 0.43741 -0.03079 0.08282  0.05703  47  GLU   A CB  
352  C  CG  . GLU   A 47  ? 0.80259 0.85480 0.47846 -0.03595 0.07874  0.07634  47  GLU   A CG  
353  C  CD  . GLU   A 47  ? 0.81548 0.87383 0.48160 -0.04142 0.06257  0.08363  47  GLU   A CD  
354  O  OE1 . GLU   A 47  ? 0.82794 0.88450 0.49564 -0.04252 0.05021  0.07644  47  GLU   A OE1 
355  O  OE2 . GLU   A 47  ? 0.78346 0.84924 0.44255 -0.04489 0.06219  0.09717  47  GLU   A OE2 
356  N  N   . ASP   A 48  ? 0.69023 0.73374 0.42895 -0.03023 0.07399  0.06651  48  ASP   A N   
357  C  CA  . ASP   A 48  ? 0.65752 0.70220 0.42499 -0.02936 0.07854  0.06975  48  ASP   A CA  
358  C  C   . ASP   A 48  ? 0.64709 0.68591 0.42386 -0.02508 0.07850  0.05723  48  ASP   A C   
359  O  O   . ASP   A 48  ? 0.61069 0.64911 0.39937 -0.02232 0.08947  0.05311  48  ASP   A O   
360  C  CB  . ASP   A 48  ? 0.60429 0.65459 0.39464 -0.03325 0.06715  0.08368  48  ASP   A CB  
361  C  CG  . ASP   A 48  ? 0.58404 0.64176 0.37727 -0.03655 0.07133  0.09812  48  ASP   A CG  
362  O  OD1 . ASP   A 48  ? 0.55715 0.61689 0.33951 -0.03640 0.08469  0.09753  48  ASP   A OD1 
363  O  OD2 . ASP   A 48  ? 0.55549 0.61679 0.36249 -0.03912 0.06170  0.11015  48  ASP   A OD2 
364  N  N   . MET   A 49  ? 0.65333 0.68880 0.42667 -0.02537 0.06599  0.05144  49  MET   A N   
365  C  CA  . MET   A 49  ? 0.64857 0.67929 0.43197 -0.02226 0.06353  0.04074  49  MET   A CA  
366  C  C   . MET   A 49  ? 0.65611 0.68386 0.42996 -0.01578 0.07526  0.02721  49  MET   A C   
367  O  O   . MET   A 49  ? 0.68366 0.70870 0.46569 -0.01324 0.07337  0.01749  49  MET   A O   
368  C  CB  . MET   A 49  ? 0.64853 0.67686 0.42868 -0.02573 0.04763  0.03764  49  MET   A CB  
369  C  CG  . MET   A 49  ? 0.59803 0.62775 0.40144 -0.02792 0.03682  0.04518  49  MET   A CG  
370  S  SD  . MET   A 49  ? 0.54623 0.57804 0.37727 -0.02540 0.04348  0.04879  49  MET   A SD  
371  C  CE  . MET   A 49  ? 0.49586 0.52153 0.32444 -0.02055 0.04984  0.03261  49  MET   A CE  
372  N  N   . LEU   A 50  ? 0.68249 0.71235 0.44087 -0.01273 0.08743  0.02647  50  LEU   A N   
373  C  CA  . LEU   A 50  ? 0.67634 0.71059 0.43218 -0.00493 0.09879  0.01411  50  LEU   A CA  
374  C  C   . LEU   A 50  ? 0.66597 0.71138 0.45341 -0.00038 0.10682  0.01677  50  LEU   A C   
375  O  O   . LEU   A 50  ? 0.67829 0.72832 0.48236 -0.00063 0.10453  0.00838  50  LEU   A O   
376  C  CB  . LEU   A 50  ? 0.73113 0.76854 0.46223 -0.00320 0.10791  0.01157  50  LEU   A CB  
377  C  CG  . LEU   A 50  ? 0.75480 0.78555 0.45742 -0.00928 0.09770  0.00510  50  LEU   A CG  
378  C  CD1 . LEU   A 50  ? 0.73431 0.76825 0.40989 -0.00819 0.10718  0.00487  50  LEU   A CD1 
379  C  CD2 . LEU   A 50  ? 0.73222 0.75511 0.43281 -0.01068 0.09125  -0.01244 50  LEU   A CD2 
380  N  N   . ASN   A 51  ? 0.63836 0.67534 0.42963 -0.00169 0.11823  0.02620  51  ASN   A N   
381  C  CA  . ASN   A 51  ? 0.61208 0.67169 0.43400 -0.01954 0.12208  0.02058  51  ASN   A CA  
382  C  C   . ASN   A 51  ? 0.58826 0.64583 0.41874 -0.02106 0.12374  0.03776  51  ASN   A C   
383  O  O   . ASN   A 51  ? 0.61305 0.67962 0.44363 -0.02294 0.13339  0.04312  51  ASN   A O   
384  C  CB  . ASN   A 51  ? 0.65578 0.73571 0.48265 -0.01241 0.13561  0.01376  51  ASN   A CB  
385  C  CG  . ASN   A 51  ? 0.66377 0.74547 0.51976 -0.00379 0.14274  0.01342  51  ASN   A CG  
386  O  OD1 . ASN   A 51  ? 0.65125 0.73001 0.52795 -0.00337 0.13616  0.02115  51  ASN   A OD1 
387  N  ND2 . ASN   A 51  ? 0.61264 0.69786 0.47249 0.00465  0.15476  0.00523  51  ASN   A ND2 
388  N  N   . PRO   A 52  ? 0.55165 0.60745 0.39620 -0.02066 0.11125  0.04670  52  PRO   A N   
389  C  CA  . PRO   A 52  ? 0.51855 0.58244 0.37768 -0.02365 0.10657  0.06220  52  PRO   A CA  
390  C  C   . PRO   A 52  ? 0.44681 0.52370 0.34042 -0.02244 0.10785  0.06856  52  PRO   A C   
391  O  O   . PRO   A 52  ? 0.42049 0.49991 0.33131 -0.01838 0.10686  0.06354  52  PRO   A O   
392  C  CB  . PRO   A 52  ? 0.51447 0.57131 0.37085 -0.02508 0.09086  0.06644  52  PRO   A CB  
393  C  CG  . PRO   A 52  ? 0.49711 0.54807 0.35664 -0.02154 0.08676  0.05571  52  PRO   A CG  
394  C  CD  . PRO   A 52  ? 0.53478 0.58270 0.38259 -0.01856 0.09974  0.04262  52  PRO   A CD  
395  N  N   . ASN   A 53  ? 0.40416 0.48893 0.30813 -0.02577 0.10959  0.08032  53  ASN   A N   
396  C  CA  . ASN   A 53  ? 0.38787 0.48355 0.32448 -0.02607 0.10892  0.08797  53  ASN   A CA  
397  C  C   . ASN   A 53  ? 0.35374 0.44512 0.30041 -0.03042 0.09591  0.09700  53  ASN   A C   
398  O  O   . ASN   A 53  ? 0.34354 0.43509 0.28757 -0.03451 0.09463  0.10691  53  ASN   A O   
399  C  CB  . ASN   A 53  ? 0.38585 0.49307 0.32807 -0.02716 0.12076  0.09393  53  ASN   A CB  
400  C  CG  . ASN   A 53  ? 0.38266 0.50131 0.35870 -0.02849 0.11947  0.10228  53  ASN   A CG  
401  O  OD1 . ASN   A 53  ? 0.38269 0.49942 0.37641 -0.03025 0.10899  0.10473  53  ASN   A OD1 
402  N  ND2 . ASN   A 53  ? 0.43578 0.56655 0.42071 -0.02807 0.13044  0.10596  53  ASN   A ND2 
403  N  N   . TYR   A 54  ? 0.32552 0.41265 0.28355 -0.02937 0.08661  0.09334  54  TYR   A N   
404  C  CA  . TYR   A 54  ? 0.29460 0.37507 0.25938 -0.03305 0.07446  0.09926  54  TYR   A CA  
405  C  C   . TYR   A 54  ? 0.30459 0.38943 0.29164 -0.03783 0.07306  0.10997  54  TYR   A C   
406  O  O   . TYR   A 54  ? 0.29194 0.37095 0.27967 -0.04109 0.06668  0.11745  54  TYR   A O   
407  C  CB  . TYR   A 54  ? 0.26122 0.33700 0.23444 -0.03129 0.06633  0.09247  54  TYR   A CB  
408  C  CG  . TYR   A 54  ? 0.21405 0.28173 0.16425 -0.02830 0.06342  0.08412  54  TYR   A CG  
409  C  CD1 . TYR   A 54  ? 0.21597 0.27571 0.15394 -0.03025 0.05454  0.08674  54  TYR   A CD1 
410  C  CD2 . TYR   A 54  ? 0.25194 0.31993 0.19479 -0.02343 0.06905  0.07364  54  TYR   A CD2 
411  C  CE1 . TYR   A 54  ? 0.26720 0.32031 0.18570 -0.02841 0.05044  0.07909  54  TYR   A CE1 
412  C  CE2 . TYR   A 54  ? 0.26433 0.32351 0.18635 -0.02155 0.06580  0.06518  54  TYR   A CE2 
413  C  CZ  . TYR   A 54  ? 0.26763 0.31978 0.17737 -0.02457 0.05594  0.06794  54  TYR   A CZ  
414  O  OH  . TYR   A 54  ? 0.27009 0.31448 0.16090 -0.02357 0.05130  0.05969  54  TYR   A OH  
415  N  N   . GLU   A 55  ? 0.30310 0.39794 0.30991 -0.03830 0.07843  0.11092  55  GLU   A N   
416  C  CA  . GLU   A 55  ? 0.29405 0.39264 0.32079 -0.04377 0.07757  0.12070  55  GLU   A CA  
417  C  C   . GLU   A 55  ? 0.29471 0.39399 0.30885 -0.04588 0.08265  0.13020  55  GLU   A C   
418  O  O   . GLU   A 55  ? 0.26036 0.35499 0.28152 -0.05007 0.07779  0.13909  55  GLU   A O   
419  C  CB  . GLU   A 55  ? 0.30144 0.41269 0.35073 -0.04410 0.08227  0.12007  55  GLU   A CB  
420  C  CG  . GLU   A 55  ? 0.35988 0.47151 0.42340 -0.04288 0.07556  0.11209  55  GLU   A CG  
421  C  CD  . GLU   A 55  ? 0.43191 0.54597 0.48466 -0.03537 0.07978  0.10274  55  GLU   A CD  
422  O  OE1 . GLU   A 55  ? 0.39865 0.51031 0.42922 -0.03138 0.08690  0.10004  55  GLU   A OE1 
423  O  OE2 . GLU   A 55  ? 0.44892 0.56630 0.51485 -0.03377 0.07553  0.09757  55  GLU   A OE2 
424  N  N   . ASP   A 56  ? 0.30683 0.41091 0.30137 -0.04299 0.09257  0.12809  56  ASP   A N   
425  C  CA  . ASP   A 56  ? 0.34709 0.45254 0.32628 -0.04526 0.09790  0.13686  56  ASP   A CA  
426  C  C   . ASP   A 56  ? 0.34083 0.43575 0.30430 -0.04638 0.08875  0.14088  56  ASP   A C   
427  O  O   . ASP   A 56  ? 0.31800 0.41255 0.28302 -0.04977 0.08696  0.15259  56  ASP   A O   
428  C  CB  . ASP   A 56  ? 0.40344 0.51386 0.36092 -0.04207 0.11047  0.13081  56  ASP   A CB  
429  C  CG  . ASP   A 56  ? 0.42661 0.55072 0.39915 -0.04221 0.12202  0.13387  56  ASP   A CG  
430  O  OD1 . ASP   A 56  ? 0.43675 0.56677 0.43475 -0.04577 0.11983  0.14247  56  ASP   A OD1 
431  O  OD2 . ASP   A 56  ? 0.47630 0.60500 0.43526 -0.03902 0.13352  0.12738  56  ASP   A OD2 
432  N  N   . LEU   A 57  ? 0.30990 0.39700 0.25919 -0.04336 0.08274  0.13187  57  LEU   A N   
433  C  CA  . LEU   A 57  ? 0.32809 0.40733 0.26320 -0.04392 0.07354  0.13559  57  LEU   A CA  
434  C  C   . LEU   A 57  ? 0.32233 0.39683 0.28013 -0.04642 0.06386  0.14379  57  LEU   A C   
435  O  O   . LEU   A 57  ? 0.32081 0.39283 0.27542 -0.04792 0.05906  0.15350  57  LEU   A O   
436  C  CB  . LEU   A 57  ? 0.31975 0.39235 0.23729 -0.04047 0.06887  0.12369  57  LEU   A CB  
437  C  CG  . LEU   A 57  ? 0.35434 0.42750 0.24585 -0.03803 0.07829  0.11395  57  LEU   A CG  
438  C  CD1 . LEU   A 57  ? 0.40323 0.46860 0.28202 -0.03485 0.07323  0.10129  57  LEU   A CD1 
439  C  CD2 . LEU   A 57  ? 0.39092 0.46525 0.25838 -0.04001 0.08187  0.12013  57  LEU   A CD2 
440  N  N   . LEU   A 58  ? 0.27544 0.34854 0.25676 -0.04698 0.06132  0.14009  58  LEU   A N   
441  C  CA  . LEU   A 58  ? 0.27181 0.33697 0.27316 -0.04929 0.05257  0.14484  58  LEU   A CA  
442  C  C   . LEU   A 58  ? 0.27390 0.34072 0.29069 -0.05362 0.05504  0.15709  58  LEU   A C   
443  O  O   . LEU   A 58  ? 0.27948 0.33897 0.30420 -0.05490 0.04924  0.16465  58  LEU   A O   
444  C  CB  . LEU   A 58  ? 0.27083 0.33277 0.28959 -0.04931 0.04887  0.13557  58  LEU   A CB  
445  C  CG  . LEU   A 58  ? 0.25635 0.30684 0.29295 -0.05132 0.04011  0.13654  58  LEU   A CG  
446  C  CD1 . LEU   A 58  ? 0.23519 0.27817 0.26061 -0.04857 0.03332  0.13923  58  LEU   A CD1 
447  C  CD2 . LEU   A 58  ? 0.24534 0.29315 0.29384 -0.05156 0.03669  0.12565  58  LEU   A CD2 
448  N  N   . ILE   A 59  ? 0.28097 0.35748 0.30346 -0.05570 0.06392  0.15960  59  ILE   A N   
449  C  CA  . ILE   A 59  ? 0.29521 0.37367 0.33352 -0.06044 0.06650  0.17151  59  ILE   A CA  
450  C  C   . ILE   A 59  ? 0.31855 0.39657 0.34259 -0.06056 0.06677  0.18363  59  ILE   A C   
451  O  O   . ILE   A 59  ? 0.33067 0.40616 0.36836 -0.06394 0.06578  0.19505  59  ILE   A O   
452  C  CB  . ILE   A 59  ? 0.29871 0.39001 0.34605 -0.06243 0.07639  0.17180  59  ILE   A CB  
453  C  CG1 . ILE   A 59  ? 0.31008 0.40266 0.37956 -0.06848 0.07776  0.18275  59  ILE   A CG1 
454  C  CG2 . ILE   A 59  ? 0.31544 0.41627 0.33959 -0.05974 0.08648  0.17268  59  ILE   A CG2 
455  C  CD1 . ILE   A 59  ? 0.34775 0.42724 0.43747 -0.07193 0.06840  0.18230  59  ILE   A CD1 
456  N  N   . ARG   A 60  ? 0.32693 0.40702 0.32366 -0.05721 0.06763  0.18129  60  ARG   A N   
457  C  CA  . ARG   A 60  ? 0.35076 0.43201 0.33064 -0.05741 0.06676  0.19213  60  ARG   A CA  
458  C  C   . ARG   A 60  ? 0.34749 0.41993 0.33076 -0.05607 0.05525  0.19606  60  ARG   A C   
459  O  O   . ARG   A 60  ? 0.36718 0.44149 0.34034 -0.05624 0.05279  0.20677  60  ARG   A O   
460  C  CB  . ARG   A 60  ? 0.36411 0.45061 0.31187 -0.05515 0.07217  0.18616  60  ARG   A CB  
461  C  CG  . ARG   A 60  ? 0.37756 0.47368 0.31979 -0.05630 0.08559  0.18594  60  ARG   A CG  
462  C  CD  . ARG   A 60  ? 0.38423 0.48157 0.29870 -0.05322 0.09174  0.17362  60  ARG   A CD  
463  N  NE  . ARG   A 60  ? 0.38801 0.49374 0.30592 -0.05307 0.10497  0.16951  60  ARG   A NE  
464  C  CZ  . ARG   A 60  ? 0.40389 0.51103 0.30164 -0.05036 0.11406  0.15831  60  ARG   A CZ  
465  N  NH1 . ARG   A 60  ? 0.40137 0.50055 0.27390 -0.04786 0.11071  0.14851  60  ARG   A NH1 
466  N  NH2 . ARG   A 60  ? 0.40522 0.52176 0.30966 -0.05013 0.12688  0.15653  60  ARG   A NH2 
467  N  N   . LYS   A 61  ? 0.32467 0.38853 0.32215 -0.05463 0.04848  0.18794  61  LYS   A N   
468  C  CA  . LYS   A 61  ? 0.31974 0.37513 0.32283 -0.05255 0.03837  0.18987  61  LYS   A CA  
469  C  C   . LYS   A 61  ? 0.32080 0.36800 0.35205 -0.05474 0.03622  0.19751  61  LYS   A C   
470  O  O   . LYS   A 61  ? 0.31709 0.36295 0.36496 -0.05815 0.04048  0.19618  61  LYS   A O   
471  C  CB  . LYS   A 61  ? 0.30686 0.35686 0.30797 -0.04954 0.03325  0.17551  61  LYS   A CB  
472  C  CG  . LYS   A 61  ? 0.29692 0.35177 0.27022 -0.04702 0.03329  0.16746  61  LYS   A CG  
473  C  CD  . LYS   A 61  ? 0.36433 0.42320 0.31918 -0.04660 0.02960  0.17570  61  LYS   A CD  
474  C  CE  . LYS   A 61  ? 0.37746 0.43946 0.30381 -0.04511 0.02975  0.16568  61  LYS   A CE  
475  N  NZ  . LYS   A 61  ? 0.41038 0.47770 0.31752 -0.04586 0.02581  0.17383  61  LYS   A NZ  
476  N  N   . SER   A 62  ? 0.32705 0.36858 0.36434 -0.05280 0.02945  0.20490  62  SER   A N   
477  C  CA  . SER   A 62  ? 0.34452 0.37494 0.40829 -0.05369 0.02700  0.21048  62  SER   A CA  
478  C  C   . SER   A 62  ? 0.33437 0.35476 0.40567 -0.04959 0.01948  0.20312  62  SER   A C   
479  O  O   . SER   A 62  ? 0.34046 0.36453 0.39638 -0.04627 0.01525  0.19756  62  SER   A O   
480  C  CB  . SER   A 62  ? 0.35542 0.38845 0.42344 -0.05438 0.02723  0.22875  62  SER   A CB  
481  O  OG  . SER   A 62  ? 0.43127 0.47690 0.48263 -0.05687 0.03341  0.23634  62  SER   A OG  
482  N  N   . ASN   A 63  ? 0.32013 0.32736 0.41531 -0.05004 0.01831  0.20285  63  ASN   A N   
483  C  CA  . ASN   A 63  ? 0.30523 0.30214 0.40963 -0.04568 0.01259  0.19666  63  ASN   A CA  
484  C  C   . ASN   A 63  ? 0.31960 0.32281 0.41596 -0.04088 0.00707  0.20537  63  ASN   A C   
485  O  O   . ASN   A 63  ? 0.32800 0.33173 0.41792 -0.03723 0.00230  0.19800  63  ASN   A O   
486  C  CB  . ASN   A 63  ? 0.31317 0.29421 0.44373 -0.04698 0.01368  0.19720  63  ASN   A CB  
487  C  CG  . ASN   A 63  ? 0.33304 0.30635 0.47193 -0.05208 0.01679  0.18432  63  ASN   A CG  
488  O  OD1 . ASN   A 63  ? 0.32451 0.30326 0.45231 -0.05310 0.01700  0.17346  63  ASN   A OD1 
489  N  ND2 . ASN   A 63  ? 0.31715 0.27818 0.47594 -0.05584 0.01909  0.18575  63  ASN   A ND2 
490  N  N   . HIS   A 64  ? 0.33394 0.34299 0.43138 -0.04125 0.00735  0.22169  64  HIS   A N   
491  C  CA  . HIS   A 64  ? 0.34370 0.36038 0.43611 -0.03746 0.00138  0.23173  64  HIS   A CA  
492  C  C   . HIS   A 64  ? 0.34897 0.37876 0.41307 -0.03721 -0.00196 0.22740  64  HIS   A C   
493  O  O   . HIS   A 64  ? 0.34564 0.38216 0.40503 -0.03460 -0.00835 0.23267  64  HIS   A O   
494  C  CB  . HIS   A 64  ? 0.39228 0.41363 0.49157 -0.03860 0.00259  0.25131  64  HIS   A CB  
495  C  CG  . HIS   A 64  ? 0.40579 0.44026 0.48337 -0.04261 0.00625  0.25814  64  HIS   A CG  
496  N  ND1 . HIS   A 64  ? 0.42983 0.46345 0.50835 -0.04721 0.01396  0.25826  64  HIS   A ND1 
497  C  CD2 . HIS   A 64  ? 0.41421 0.46308 0.46809 -0.04296 0.00374  0.26455  64  HIS   A CD2 
498  C  CE1 . HIS   A 64  ? 0.40443 0.45120 0.46110 -0.04956 0.01694  0.26478  64  HIS   A CE1 
499  N  NE2 . HIS   A 64  ? 0.45065 0.50614 0.49081 -0.04720 0.01080  0.26815  64  HIS   A NE2 
500  N  N   . ASN   A 65  ? 0.33108 0.36470 0.37712 -0.04001 0.00232  0.21788  65  ASN   A N   
501  C  CA  . ASN   A 65  ? 0.35868 0.40146 0.37787 -0.03971 -0.00017 0.21066  65  ASN   A CA  
502  C  C   . ASN   A 65  ? 0.33501 0.37306 0.35523 -0.03659 -0.00548 0.19768  65  ASN   A C   
503  O  O   . ASN   A 65  ? 0.32778 0.37242 0.32812 -0.03625 -0.00908 0.19208  65  ASN   A O   
504  C  CB  . ASN   A 65  ? 0.32692 0.37403 0.32853 -0.04286 0.00756  0.20382  65  ASN   A CB  
505  C  CG  . ASN   A 65  ? 0.35310 0.40752 0.34840 -0.04604 0.01346  0.21634  65  ASN   A CG  
506  O  OD1 . ASN   A 65  ? 0.35170 0.40785 0.34410 -0.04863 0.02159  0.21362  65  ASN   A OD1 
507  N  ND2 . ASN   A 65  ? 0.40276 0.46288 0.39609 -0.04589 0.00960  0.23072  65  ASN   A ND2 
508  N  N   . PHE   A 66  ? 0.30672 0.33313 0.34874 -0.03472 -0.00568 0.19218  66  PHE   A N   
509  C  CA  . PHE   A 66  ? 0.31255 0.33400 0.35693 -0.03173 -0.00976 0.18010  66  PHE   A CA  
510  C  C   . PHE   A 66  ? 0.33245 0.35073 0.39450 -0.02757 -0.01507 0.18613  66  PHE   A C   
511  O  O   . PHE   A 66  ? 0.31928 0.32822 0.40348 -0.02627 -0.01308 0.19078  66  PHE   A O   
512  C  CB  . PHE   A 66  ? 0.27515 0.28618 0.32940 -0.03267 -0.00566 0.16790  66  PHE   A CB  
513  C  CG  . PHE   A 66  ? 0.26968 0.28542 0.30995 -0.03626 -0.00008 0.16193  66  PHE   A CG  
514  C  CD1 . PHE   A 66  ? 0.28692 0.30760 0.30866 -0.03583 -0.00057 0.15193  66  PHE   A CD1 
515  C  CD2 . PHE   A 66  ? 0.28935 0.30508 0.33632 -0.03999 0.00614  0.16674  66  PHE   A CD2 
516  C  CE1 . PHE   A 66  ? 0.28600 0.31147 0.29682 -0.03826 0.00573  0.14668  66  PHE   A CE1 
517  C  CE2 . PHE   A 66  ? 0.27349 0.29536 0.31018 -0.04281 0.01209  0.16181  66  PHE   A CE2 
518  C  CZ  . PHE   A 66  ? 0.27040 0.29716 0.28935 -0.04154 0.01222  0.15175  66  PHE   A CZ  
519  N  N   . LEU   A 67  ? 0.29190 0.31792 0.34481 -0.02567 -0.02135 0.18560  67  LEU   A N   
520  C  CA  . LEU   A 67  ? 0.33652 0.36291 0.40583 -0.02151 -0.02645 0.19140  67  LEU   A CA  
521  C  C   . LEU   A 67  ? 0.30700 0.32675 0.38149 -0.01868 -0.02764 0.17758  67  LEU   A C   
522  O  O   . LEU   A 67  ? 0.28888 0.31291 0.34582 -0.02003 -0.02971 0.16809  67  LEU   A O   
523  C  CB  . LEU   A 67  ? 0.34114 0.38293 0.39671 -0.02244 -0.03310 0.20043  67  LEU   A CB  
524  C  CG  . LEU   A 67  ? 0.37691 0.42641 0.43241 -0.02411 -0.03323 0.21772  67  LEU   A CG  
525  C  CD1 . LEU   A 67  ? 0.38734 0.45189 0.41548 -0.02784 -0.03798 0.22084  67  LEU   A CD1 
526  C  CD2 . LEU   A 67  ? 0.38206 0.43121 0.46415 -0.01997 -0.03578 0.23071  67  LEU   A CD2 
527  N  N   . VAL   A 68  ? 0.31989 0.32839 0.41771 -0.01487 -0.02558 0.17585  68  VAL   A N   
528  C  CA  . VAL   A 68  ? 0.30062 0.30227 0.40458 -0.01179 -0.02575 0.16317  68  VAL   A CA  
529  C  C   . VAL   A 68  ? 0.28931 0.29225 0.41218 -0.00648 -0.02826 0.16913  68  VAL   A C   
530  O  O   . VAL   A 68  ? 0.32774 0.32533 0.47005 -0.00394 -0.02575 0.17779  68  VAL   A O   
531  C  CB  . VAL   A 68  ? 0.28006 0.26588 0.39314 -0.01235 -0.01956 0.15225  68  VAL   A CB  
532  C  CG1 . VAL   A 68  ? 0.27307 0.25281 0.38948 -0.00939 -0.01963 0.13884  68  VAL   A CG1 
533  C  CG2 . VAL   A 68  ? 0.28525 0.27198 0.38297 -0.01789 -0.01668 0.14840  68  VAL   A CG2 
534  N  N   . GLN   A 69  ? 0.27865 0.28889 0.39708 -0.00488 -0.03278 0.16488  69  GLN   A N   
535  C  CA  . GLN   A 69  ? 0.29680 0.31080 0.43369 0.00004  -0.03492 0.17061  69  GLN   A CA  
536  C  C   . GLN   A 69  ? 0.27751 0.28318 0.42208 0.00366  -0.03211 0.15727  69  GLN   A C   
537  O  O   . GLN   A 69  ? 0.27559 0.28421 0.40535 0.00182  -0.03433 0.14750  69  GLN   A O   
538  C  CB  . GLN   A 69  ? 0.32978 0.36188 0.45668 -0.00189 -0.04302 0.17874  69  GLN   A CB  
539  C  CG  . GLN   A 69  ? 0.37716 0.41862 0.48231 -0.00757 -0.04629 0.18515  69  GLN   A CG  
540  C  CD  . GLN   A 69  ? 0.44812 0.49872 0.56151 -0.00751 -0.04903 0.20327  69  GLN   A CD  
541  O  OE1 . GLN   A 69  ? 0.47948 0.53499 0.61243 -0.00383 -0.05129 0.21239  69  GLN   A OE1 
542  N  NE2 . GLN   A 69  ? 0.43725 0.49091 0.53640 -0.01149 -0.04840 0.20943  69  GLN   A NE2 
543  N  N   . ALA   A 70  ? 0.27209 0.26705 0.43939 0.00880  -0.02669 0.15668  70  ALA   A N   
544  C  CA  . ALA   A 70  ? 0.32205 0.30927 0.49773 0.01289  -0.02287 0.14448  70  ALA   A CA  
545  C  C   . ALA   A 70  ? 0.34319 0.34031 0.53458 0.01761  -0.02489 0.15265  70  ALA   A C   
546  O  O   . ALA   A 70  ? 0.31747 0.31012 0.53075 0.02238  -0.02080 0.15928  70  ALA   A O   
547  C  CB  . ALA   A 70  ? 0.32752 0.29514 0.51541 0.01480  -0.01442 0.13574  70  ALA   A CB  
548  N  N   . GLY   A 71  ? 0.34346 0.35437 0.52415 0.01584  -0.03117 0.15257  71  GLY   A N   
549  C  CA  . GLY   A 71  ? 0.38903 0.41355 0.58270 0.01823  -0.03510 0.16363  71  GLY   A CA  
550  C  C   . GLY   A 71  ? 0.39498 0.42817 0.59235 0.01664  -0.03911 0.18055  71  GLY   A C   
551  O  O   . GLY   A 71  ? 0.38874 0.42639 0.56741 0.01116  -0.04318 0.18362  71  GLY   A O   
552  N  N   . ASN   A 72  ? 0.38117 0.41673 0.60323 0.02171  -0.03727 0.19212  72  ASN   A N   
553  C  CA  . ASN   A 72  ? 0.44651 0.49055 0.67586 0.02101  -0.04070 0.21012  72  ASN   A CA  
554  C  C   . ASN   A 72  ? 0.43199 0.46085 0.67313 0.02332  -0.03367 0.21315  72  ASN   A C   
555  O  O   . ASN   A 72  ? 0.43672 0.46975 0.69299 0.02509  -0.03413 0.22912  72  ASN   A O   
556  C  CB  . ASN   A 72  ? 0.44990 0.50742 0.70088 0.02486  -0.04351 0.22368  72  ASN   A CB  
557  C  CG  . ASN   A 72  ? 0.52728 0.57516 0.80227 0.03263  -0.03512 0.21786  72  ASN   A CG  
558  O  OD1 . ASN   A 72  ? 0.56352 0.59260 0.84290 0.03577  -0.02636 0.20627  72  ASN   A OD1 
559  N  ND2 . ASN   A 72  ? 0.51530 0.57614 0.80569 0.03548  -0.03747 0.22578  72  ASN   A ND2 
560  N  N   . VAL   A 73  ? 0.36973 0.38130 0.60477 0.02289  -0.02743 0.19863  73  VAL   A N   
561  C  CA  . VAL   A 73  ? 0.39579 0.39117 0.64052 0.02363  -0.02075 0.19918  73  VAL   A CA  
562  C  C   . VAL   A 73  ? 0.38559 0.37840 0.60686 0.01680  -0.02215 0.19422  73  VAL   A C   
563  O  O   . VAL   A 73  ? 0.37103 0.36328 0.57356 0.01372  -0.02326 0.18123  73  VAL   A O   
564  C  CB  . VAL   A 73  ? 0.40292 0.37867 0.66299 0.02853  -0.01126 0.18565  73  VAL   A CB  
565  C  CG1 . VAL   A 73  ? 0.44518 0.40526 0.72299 0.03017  -0.00457 0.19010  73  VAL   A CG1 
566  C  CG2 . VAL   A 73  ? 0.45012 0.43095 0.72649 0.03484  -0.00975 0.18608  73  VAL   A CG2 
567  N  N   . GLN   A 74  ? 0.39893 0.39076 0.62209 0.01452  -0.02168 0.20528  74  GLN   A N   
568  C  CA  . GLN   A 74  ? 0.38082 0.37222 0.58310 0.00802  -0.02231 0.20296  74  GLN   A CA  
569  C  C   . GLN   A 74  ? 0.37973 0.35098 0.58828 0.00692  -0.01469 0.19278  74  GLN   A C   
570  O  O   . GLN   A 74  ? 0.38965 0.34873 0.61964 0.00984  -0.00952 0.19628  74  GLN   A O   
571  C  CB  . GLN   A 74  ? 0.45642 0.45981 0.65494 0.00528  -0.02599 0.22115  74  GLN   A CB  
572  C  CG  . GLN   A 74  ? 0.44591 0.44607 0.62862 -0.00067 -0.02378 0.22017  74  GLN   A CG  
573  C  CD  . GLN   A 74  ? 0.50717 0.52385 0.67473 -0.00448 -0.02858 0.23463  74  GLN   A CD  
574  O  OE1 . GLN   A 74  ? 0.51086 0.53788 0.65338 -0.00841 -0.03233 0.23036  74  GLN   A OE1 
575  N  NE2 . GLN   A 74  ? 0.52088 0.53971 0.70313 -0.00340 -0.02810 0.25173  74  GLN   A NE2 
576  N  N   . LEU   A 75  ? 0.34300 0.31084 0.53317 0.00224  -0.01404 0.18030  75  LEU   A N   
577  C  CA  . LEU   A 75  ? 0.34083 0.29140 0.53421 -0.00054 -0.00791 0.16899  75  LEU   A CA  
578  C  C   . LEU   A 75  ? 0.38096 0.33319 0.56651 -0.00658 -0.00712 0.17615  75  LEU   A C   
579  O  O   . LEU   A 75  ? 0.37461 0.33989 0.54039 -0.01006 -0.01051 0.17933  75  LEU   A O   
580  C  CB  . LEU   A 75  ? 0.33330 0.28022 0.51362 -0.00199 -0.00757 0.15107  75  LEU   A CB  
581  C  CG  . LEU   A 75  ? 0.33692 0.28191 0.52357 0.00358  -0.00735 0.14235  75  LEU   A CG  
582  C  CD1 . LEU   A 75  ? 0.28904 0.22816 0.46386 0.00136  -0.00603 0.12490  75  LEU   A CD1 
583  C  CD2 . LEU   A 75  ? 0.32988 0.26207 0.54107 0.00882  -0.00176 0.14296  75  LEU   A CD2 
584  N  N   . ARG   A 76  ? 0.35734 0.29618 0.55838 -0.00800 -0.00208 0.17847  76  ARG   A N   
585  C  CA  . ARG   A 76  ? 0.37332 0.31371 0.57019 -0.01386 -0.00054 0.18656  76  ARG   A CA  
586  C  C   . ARG   A 76  ? 0.34270 0.27929 0.52660 -0.02012 0.00152  0.17292  76  ARG   A C   
587  O  O   . ARG   A 76  ? 0.34143 0.26369 0.53209 -0.02150 0.00464  0.15906  76  ARG   A O   
588  C  CB  . ARG   A 76  ? 0.38439 0.31162 0.60454 -0.01349 0.00395  0.19482  76  ARG   A CB  
589  C  CG  . ARG   A 76  ? 0.39567 0.32187 0.61500 -0.02021 0.00666  0.20215  76  ARG   A CG  
590  C  CD  . ARG   A 76  ? 0.45692 0.37755 0.69736 -0.01865 0.00902  0.21831  76  ARG   A CD  
591  N  NE  . ARG   A 76  ? 0.49482 0.39616 0.75017 -0.02318 0.01475  0.21304  76  ARG   A NE  
592  C  CZ  . ARG   A 76  ? 0.57461 0.47562 0.82827 -0.03042 0.01712  0.21749  76  ARG   A CZ  
593  N  NH1 . ARG   A 76  ? 0.58574 0.50438 0.82247 -0.03347 0.01524  0.22635  76  ARG   A NH1 
594  N  NH2 . ARG   A 76  ? 0.57743 0.45999 0.84652 -0.03511 0.02185  0.21250  76  ARG   A NH2 
595  N  N   . VAL   A 77  ? 0.30584 0.25595 0.47082 -0.02401 -0.00003 0.17647  77  VAL   A N   
596  C  CA  . VAL   A 77  ? 0.33242 0.28210 0.48681 -0.03002 0.00239  0.16620  77  VAL   A CA  
597  C  C   . VAL   A 77  ? 0.31394 0.25631 0.47977 -0.03571 0.00706  0.17059  77  VAL   A C   
598  O  O   . VAL   A 77  ? 0.31204 0.26000 0.48023 -0.03665 0.00800  0.18555  77  VAL   A O   
599  C  CB  . VAL   A 77  ? 0.27038 0.23726 0.40104 -0.03142 0.00032  0.16838  77  VAL   A CB  
600  C  CG1 . VAL   A 77  ? 0.29676 0.26533 0.42027 -0.03754 0.00419  0.16152  77  VAL   A CG1 
601  C  CG2 . VAL   A 77  ? 0.27438 0.24660 0.39361 -0.02721 -0.00436 0.16101  77  VAL   A CG2 
602  N  N   . ILE   A 78  ? 0.31116 0.24193 0.48349 -0.04029 0.00974  0.15767  78  ILE   A N   
603  C  CA  . ILE   A 78  ? 0.30955 0.23239 0.49411 -0.04700 0.01376  0.15998  78  ILE   A CA  
604  C  C   . ILE   A 78  ? 0.29993 0.22907 0.47651 -0.05440 0.01535  0.15241  78  ILE   A C   
605  O  O   . ILE   A 78  ? 0.32204 0.24660 0.50865 -0.06127 0.01837  0.15346  78  ILE   A O   
606  C  CB  . ILE   A 78  ? 0.32562 0.22724 0.52909 -0.04742 0.01577  0.15212  78  ILE   A CB  
607  C  CG1 . ILE   A 78  ? 0.32123 0.21533 0.52013 -0.04731 0.01473  0.13237  78  ILE   A CG1 
608  C  CG2 . ILE   A 78  ? 0.33758 0.23408 0.55378 -0.03997 0.01564  0.16295  78  ILE   A CG2 
609  C  CD1 . ILE   A 78  ? 0.34986 0.22325 0.56248 -0.05181 0.01764  0.12050  78  ILE   A CD1 
610  N  N   . GLY   A 79  ? 0.31942 0.25934 0.47980 -0.05338 0.01349  0.14509  79  GLY   A N   
611  C  CA  . GLY   A 79  ? 0.26974 0.21853 0.42381 -0.05936 0.01521  0.13909  79  GLY   A CA  
612  C  C   . GLY   A 79  ? 0.29194 0.25368 0.42720 -0.05578 0.01337  0.13503  79  GLY   A C   
613  O  O   . GLY   A 79  ? 0.28084 0.24067 0.40997 -0.05007 0.00994  0.13178  79  GLY   A O   
614  N  N   . HIS   A 80  ? 0.28133 0.25647 0.40809 -0.05890 0.01604  0.13538  80  HIS   A N   
615  C  CA  . HIS   A 80  ? 0.24890 0.23488 0.35853 -0.05587 0.01516  0.13001  80  HIS   A CA  
616  C  C   . HIS   A 80  ? 0.25022 0.24584 0.36035 -0.06053 0.01828  0.12392  80  HIS   A C   
617  O  O   . HIS   A 80  ? 0.22766 0.22767 0.34637 -0.06547 0.02211  0.12872  80  HIS   A O   
618  C  CB  . HIS   A 80  ? 0.23163 0.22823 0.32404 -0.05185 0.01586  0.14039  80  HIS   A CB  
619  C  CG  . HIS   A 80  ? 0.28609 0.29219 0.37638 -0.05491 0.02141  0.15091  80  HIS   A CG  
620  N  ND1 . HIS   A 80  ? 0.30067 0.30312 0.40140 -0.05669 0.02269  0.16277  80  HIS   A ND1 
621  C  CD2 . HIS   A 80  ? 0.26895 0.28824 0.34821 -0.05616 0.02677  0.15156  80  HIS   A CD2 
622  C  CE1 . HIS   A 80  ? 0.33522 0.34858 0.43094 -0.05939 0.02835  0.17050  80  HIS   A CE1 
623  N  NE2 . HIS   A 80  ? 0.31198 0.33566 0.39451 -0.05888 0.03124  0.16350  80  HIS   A NE2 
624  N  N   . SER   A 81  ? 0.21109 0.21127 0.31331 -0.05883 0.01665  0.11408  81  SER   A N   
625  C  CA  . SER   A 81  ? 0.21072 0.22304 0.31419 -0.06199 0.01955  0.10933  81  SER   A CA  
626  C  C   . SER   A 81  ? 0.19831 0.21789 0.28773 -0.05756 0.01884  0.10295  81  SER   A C   
627  O  O   . SER   A 81  ? 0.21390 0.22668 0.29606 -0.05384 0.01471  0.09908  81  SER   A O   
628  C  CB  . SER   A 81  ? 0.22189 0.22959 0.34207 -0.06852 0.01727  0.10052  81  SER   A CB  
629  O  OG  . SER   A 81  ? 0.26670 0.26196 0.38798 -0.06770 0.01208  0.09024  81  SER   A OG  
630  N  N   . MET   A 82  ? 0.17199 0.20560 0.25902 -0.05777 0.02333  0.10208  82  MET   A N   
631  C  CA  . MET   A 82  ? 0.21571 0.25658 0.29188 -0.05370 0.02372  0.09563  82  MET   A CA  
632  C  C   . MET   A 82  ? 0.21110 0.25496 0.29967 -0.05651 0.02016  0.08611  82  MET   A C   
633  O  O   . MET   A 82  ? 0.19048 0.23894 0.29377 -0.06157 0.02022  0.08537  82  MET   A O   
634  C  CB  . MET   A 82  ? 0.21298 0.26739 0.27867 -0.05066 0.03189  0.09937  82  MET   A CB  
635  C  CG  . MET   A 82  ? 0.21922 0.27636 0.26699 -0.04496 0.03330  0.09432  82  MET   A CG  
636  S  SD  . MET   A 82  ? 0.24456 0.31067 0.27353 -0.04109 0.04369  0.09809  82  MET   A SD  
637  C  CE  . MET   A 82  ? 0.27018 0.34603 0.31723 -0.04527 0.04992  0.10544  82  MET   A CE  
638  N  N   . GLN   A 83  ? 0.17262 0.21472 0.25456 -0.05365 0.01651  0.07901  83  GLN   A N   
639  C  CA  . GLN   A 83  ? 0.21173 0.26067 0.30092 -0.05488 0.01316  0.07020  83  GLN   A CA  
640  C  C   . GLN   A 83  ? 0.13761 0.19275 0.21211 -0.04727 0.01524  0.06641  83  GLN   A C   
641  O  O   . GLN   A 83  ? 0.14399 0.18953 0.20474 -0.04263 0.01198  0.06129  83  GLN   A O   
642  C  CB  . GLN   A 83  ? 0.21280 0.24940 0.30698 -0.05802 0.00551  0.06139  83  GLN   A CB  
643  C  CG  . GLN   A 83  ? 0.24419 0.28904 0.34573 -0.06095 0.00099  0.05232  83  GLN   A CG  
644  C  CD  . GLN   A 83  ? 0.29117 0.32302 0.39348 -0.06390 -0.00550 0.04175  83  GLN   A CD  
645  O  OE1 . GLN   A 83  ? 0.29672 0.32598 0.38842 -0.05910 -0.00855 0.03392  83  GLN   A OE1 
646  N  NE2 . GLN   A 83  ? 0.31498 0.33692 0.42539 -0.06954 -0.00628 0.03919  83  GLN   A NE2 
647  N  N   . ASN   A 84  ? 0.13032 0.20052 0.20828 -0.04514 0.02092  0.06816  84  ASN   A N   
648  C  CA  . ASN   A 84  ? 0.15168 0.22564 0.21605 -0.03671 0.02487  0.06392  84  ASN   A CA  
649  C  C   . ASN   A 84  ? 0.11927 0.18347 0.16199 -0.03291 0.02727  0.06476  84  ASN   A C   
650  O  O   . ASN   A 84  ? 0.12690 0.19280 0.16522 -0.03473 0.03269  0.07325  84  ASN   A O   
651  C  CB  . ASN   A 84  ? 0.10577 0.17908 0.17123 -0.03405 0.01826  0.05442  84  ASN   A CB  
652  C  CG  . ASN   A 84  ? 0.11771 0.20286 0.20326 -0.03941 0.01435  0.05442  84  ASN   A CG  
653  O  OD1 . ASN   A 84  ? 0.11993 0.22022 0.21857 -0.04031 0.01931  0.06047  84  ASN   A OD1 
654  N  ND2 . ASN   A 84  ? 0.13094 0.21013 0.21928 -0.04372 0.00566  0.04788  84  ASN   A ND2 
655  N  N   . CYS   A 85  ? 0.14089 0.19619 0.17002 -0.02851 0.02308  0.05706  85  CYS   A N   
656  C  CA  . CYS   A 85  ? 0.12162 0.16999 0.13027 -0.02610 0.02433  0.05764  85  CYS   A CA  
657  C  C   . CYS   A 85  ? 0.13049 0.16836 0.13636 -0.02878 0.01691  0.06036  85  CYS   A C   
658  O  O   . CYS   A 85  ? 0.12948 0.16266 0.11925 -0.02729 0.01522  0.06076  85  CYS   A O   
659  C  CB  . CYS   A 85  ? 0.14206 0.18765 0.13796 -0.02016 0.02519  0.04852  85  CYS   A CB  
660  S  SG  . CYS   A 85  ? 0.13356 0.18982 0.13099 -0.01519 0.03696  0.04744  85  CYS   A SG  
661  N  N   . VAL   A 86  ? 0.11921 0.15343 0.14111 -0.03285 0.01262  0.06233  86  VAL   A N   
662  C  CA  . VAL   A 86  ? 0.12654 0.15045 0.14966 -0.03437 0.00734  0.06634  86  VAL   A CA  
663  C  C   . VAL   A 86  ? 0.15289 0.17651 0.18764 -0.03962 0.00976  0.07795  86  VAL   A C   
664  O  O   . VAL   A 86  ? 0.14399 0.17449 0.19014 -0.04348 0.01394  0.08076  86  VAL   A O   
665  C  CB  . VAL   A 86  ? 0.13318 0.14861 0.16452 -0.03385 0.00101  0.05769  86  VAL   A CB  
666  C  CG1 . VAL   A 86  ? 0.16661 0.18266 0.18706 -0.02893 -0.00113 0.04809  86  VAL   A CG1 
667  C  CG2 . VAL   A 86  ? 0.14111 0.15762 0.18909 -0.03853 0.00069  0.05421  86  VAL   A CG2 
668  N  N   . LEU   A 87  ? 0.14135 0.15792 0.17420 -0.03967 0.00705  0.08597  87  LEU   A N   
669  C  CA  . LEU   A 87  ? 0.16718 0.17896 0.21205 -0.04186 0.00752  0.09281  87  LEU   A CA  
670  C  C   . LEU   A 87  ? 0.15879 0.15760 0.21957 -0.04274 0.00315  0.08849  87  LEU   A C   
671  O  O   . LEU   A 87  ? 0.15086 0.14367 0.21029 -0.04006 -0.00095 0.08310  87  LEU   A O   
672  C  CB  . LEU   A 87  ? 0.18920 0.20180 0.22311 -0.03947 0.00702  0.10218  87  LEU   A CB  
673  C  CG  . LEU   A 87  ? 0.21805 0.23946 0.24234 -0.04037 0.01248  0.11006  87  LEU   A CG  
674  C  CD1 . LEU   A 87  ? 0.26261 0.28310 0.27817 -0.03836 0.00880  0.11825  87  LEU   A CD1 
675  C  CD2 . LEU   A 87  ? 0.25349 0.27551 0.29428 -0.04458 0.01679  0.11455  87  LEU   A CD2 
676  N  N   . LYS   A 88  ? 0.17981 0.17374 0.25537 -0.04649 0.00469  0.09014  88  LYS   A N   
677  C  CA  . LYS   A 88  ? 0.19373 0.17325 0.28313 -0.04718 0.00221  0.08523  88  LYS   A CA  
678  C  C   . LYS   A 88  ? 0.21575 0.18997 0.31181 -0.04657 0.00352  0.09591  88  LYS   A C   
679  O  O   . LYS   A 88  ? 0.19123 0.16898 0.29218 -0.05052 0.00686  0.10198  88  LYS   A O   
680  C  CB  . LYS   A 88  ? 0.22301 0.20025 0.32352 -0.05332 0.00238  0.07504  88  LYS   A CB  
681  C  CG  . LYS   A 88  ? 0.22924 0.21350 0.32457 -0.05384 0.00019  0.06495  88  LYS   A CG  
682  C  CD  . LYS   A 88  ? 0.22931 0.21570 0.33409 -0.06060 -0.00083 0.05556  88  LYS   A CD  
683  C  CE  . LYS   A 88  ? 0.28256 0.25299 0.39363 -0.06271 -0.00304 0.04517  88  LYS   A CE  
684  N  NZ  . LYS   A 88  ? 0.36293 0.33583 0.48004 -0.07078 -0.00482 0.03539  88  LYS   A NZ  
685  N  N   . LEU   A 89  ? 0.20673 0.17435 0.30367 -0.04142 0.00097  0.09923  89  LEU   A N   
686  C  CA  . LEU   A 89  ? 0.20066 0.16500 0.30467 -0.03983 0.00155  0.11091  89  LEU   A CA  
687  C  C   . LEU   A 89  ? 0.21081 0.15893 0.33259 -0.03992 0.00217  0.10590  89  LEU   A C   
688  O  O   . LEU   A 89  ? 0.21377 0.15454 0.33879 -0.03570 0.00050  0.09924  89  LEU   A O   
689  C  CB  . LEU   A 89  ? 0.20101 0.17191 0.29505 -0.03414 -0.00197 0.11870  89  LEU   A CB  
690  C  CG  . LEU   A 89  ? 0.20507 0.19050 0.27801 -0.03459 -0.00214 0.12149  89  LEU   A CG  
691  C  CD1 . LEU   A 89  ? 0.23210 0.22404 0.29509 -0.03054 -0.00664 0.12873  89  LEU   A CD1 
692  C  CD2 . LEU   A 89  ? 0.23305 0.22569 0.30258 -0.03895 0.00293  0.12804  89  LEU   A CD2 
693  N  N   . LYS   A 90  ? 0.22380 0.16610 0.35695 -0.04481 0.00517  0.10856  90  LYS   A N   
694  C  CA  . LYS   A 90  ? 0.26724 0.19246 0.41632 -0.04560 0.00657  0.10323  90  LYS   A CA  
695  C  C   . LYS   A 90  ? 0.29264 0.21327 0.45072 -0.03943 0.00659  0.11468  90  LYS   A C   
696  O  O   . LYS   A 90  ? 0.29949 0.22632 0.45899 -0.03943 0.00713  0.12915  90  LYS   A O   
697  C  CB  . LYS   A 90  ? 0.29358 0.21437 0.45155 -0.05420 0.00933  0.10172  90  LYS   A CB  
698  C  CG  . LYS   A 90  ? 0.32630 0.22797 0.49802 -0.05749 0.01092  0.09229  90  LYS   A CG  
699  C  CD  . LYS   A 90  ? 0.37899 0.27434 0.54584 -0.05779 0.00942  0.07432  90  LYS   A CD  
700  C  CE  . LYS   A 90  ? 0.38618 0.27702 0.55509 -0.06821 0.00931  0.06200  90  LYS   A CE  
701  N  NZ  . LYS   A 90  ? 0.38703 0.27743 0.54648 -0.06897 0.00687  0.04524  90  LYS   A NZ  
702  N  N   . VAL   A 91  ? 0.27008 0.18135 0.43465 -0.03402 0.00625  0.10871  91  VAL   A N   
703  C  CA  . VAL   A 91  ? 0.30368 0.21197 0.47990 -0.02756 0.00642  0.11931  91  VAL   A CA  
704  C  C   . VAL   A 91  ? 0.31376 0.20251 0.50811 -0.02803 0.01079  0.11364  91  VAL   A C   
705  O  O   . VAL   A 91  ? 0.32314 0.20076 0.51781 -0.03295 0.01280  0.09894  91  VAL   A O   
706  C  CB  . VAL   A 91  ? 0.32330 0.23894 0.49442 -0.02016 0.00313  0.11902  91  VAL   A CB  
707  C  CG1 . VAL   A 91  ? 0.30752 0.24096 0.45899 -0.02095 -0.00118 0.12357  91  VAL   A CG1 
708  C  CG2 . VAL   A 91  ? 0.27266 0.17871 0.44434 -0.01858 0.00455  0.10182  91  VAL   A CG2 
709  N  N   . ASP   A 92  ? 0.30040 0.18520 0.50976 -0.02339 0.01223  0.12545  92  ASP   A N   
710  C  CA  . ASP   A 92  ? 0.37010 0.23524 0.59799 -0.02379 0.01724  0.12181  92  ASP   A CA  
711  C  C   . ASP   A 92  ? 0.35980 0.21449 0.59557 -0.01712 0.01997  0.11139  92  ASP   A C   
712  O  O   . ASP   A 92  ? 0.35073 0.18868 0.60271 -0.01587 0.02495  0.10878  92  ASP   A O   
713  C  CB  . ASP   A 92  ? 0.34772 0.21252 0.59086 -0.02229 0.01852  0.14064  92  ASP   A CB  
714  C  CG  . ASP   A 92  ? 0.37686 0.25289 0.62573 -0.01340 0.01617  0.15461  92  ASP   A CG  
715  O  OD1 . ASP   A 92  ? 0.37261 0.25764 0.61321 -0.00871 0.01328  0.15032  92  ASP   A OD1 
716  O  OD2 . ASP   A 92  ? 0.46443 0.34081 0.72721 -0.01153 0.01703  0.17062  92  ASP   A OD2 
717  N  N   . THR   A 93  ? 0.34475 0.20883 0.57013 -0.01272 0.01745  0.10576  93  THR   A N   
718  C  CA  . THR   A 93  ? 0.33881 0.19490 0.57065 -0.00641 0.02081  0.09539  93  THR   A CA  
719  C  C   . THR   A 93  ? 0.32852 0.18673 0.54336 -0.00873 0.01948  0.07873  93  THR   A C   
720  O  O   . THR   A 93  ? 0.28343 0.15666 0.48376 -0.00975 0.01446  0.08125  93  THR   A O   
721  C  CB  . THR   A 93  ? 0.33859 0.20639 0.57890 0.00266  0.01925  0.10817  93  THR   A CB  
722  O  OG1 . THR   A 93  ? 0.32188 0.19147 0.57646 0.00416  0.01921  0.12608  93  THR   A OG1 
723  C  CG2 . THR   A 93  ? 0.33260 0.19111 0.58400 0.00949  0.02472  0.09859  93  THR   A CG2 
724  N  N   . ALA   A 94  ? 0.34588 0.18896 0.56186 -0.00992 0.02408  0.06167  94  ALA   A N   
725  C  CA  . ALA   A 94  ? 0.28516 0.13069 0.48631 -0.01092 0.02333  0.04612  94  ALA   A CA  
726  C  C   . ALA   A 94  ? 0.29207 0.14486 0.49606 -0.00146 0.02425  0.04760  94  ALA   A C   
727  O  O   . ALA   A 94  ? 0.28973 0.13713 0.50950 0.00525  0.02870  0.05174  94  ALA   A O   
728  C  CB  . ALA   A 94  ? 0.30232 0.13054 0.50126 -0.01627 0.02759  0.02705  94  ALA   A CB  
729  N  N   . ASN   A 95  ? 0.25367 0.11925 0.44385 -0.00108 0.02020  0.04510  95  ASN   A N   
730  C  CA  . ASN   A 95  ? 0.25098 0.12509 0.44332 0.00686  0.02051  0.04659  95  ASN   A CA  
731  C  C   . ASN   A 95  ? 0.25893 0.12060 0.45648 0.01047  0.02818  0.03189  95  ASN   A C   
732  O  O   . ASN   A 95  ? 0.25822 0.11323 0.44392 0.00598  0.02992  0.01558  95  ASN   A O   
733  C  CB  . ASN   A 95  ? 0.21987 0.10782 0.39532 0.00511  0.01482  0.04499  95  ASN   A CB  
734  C  CG  . ASN   A 95  ? 0.20890 0.10789 0.38619 0.01228  0.01391  0.04817  95  ASN   A CG  
735  O  OD1 . ASN   A 95  ? 0.21824 0.11640 0.41014 0.01883  0.01768  0.05199  95  ASN   A OD1 
736  N  ND2 . ASN   A 95  ? 0.20109 0.11049 0.36442 0.01068  0.00919  0.04637  95  ASN   A ND2 
737  N  N   . PRO   A 96  ? 0.28573 0.14457 0.50031 0.01814  0.03318  0.03690  96  PRO   A N   
738  C  CA  . PRO   A 96  ? 0.29715 0.14449 0.51548 0.02194  0.04178  0.02229  96  PRO   A CA  
739  C  C   . PRO   A 96  ? 0.26850 0.12522 0.47519 0.02433  0.04198  0.01362  96  PRO   A C   
740  O  O   . PRO   A 96  ? 0.27985 0.12809 0.48315 0.02573  0.04894  -0.00137 96  PRO   A O   
741  C  CB  . PRO   A 96  ? 0.30069 0.14591 0.54253 0.03014  0.04672  0.03355  96  PRO   A CB  
742  C  CG  . PRO   A 96  ? 0.28600 0.14908 0.53289 0.03188  0.03897  0.05400  96  PRO   A CG  
743  C  CD  . PRO   A 96  ? 0.27204 0.14003 0.50258 0.02363  0.03121  0.05629  96  PRO   A CD  
744  N  N   . LYS   A 97  ? 0.25081 0.12467 0.45076 0.02468  0.03481  0.02257  97  LYS   A N   
745  C  CA  . LYS   A 97  ? 0.23580 0.11916 0.42572 0.02671  0.03455  0.01592  97  LYS   A CA  
746  C  C   . LYS   A 97  ? 0.21730 0.10136 0.38652 0.01936  0.03075  0.00491  97  LYS   A C   
747  O  O   . LYS   A 97  ? 0.21429 0.10786 0.37444 0.02036  0.02908  0.00158  97  LYS   A O   
748  C  CB  . LYS   A 97  ? 0.21310 0.11489 0.40833 0.03102  0.02869  0.03169  97  LYS   A CB  
749  C  CG  . LYS   A 97  ? 0.24606 0.15117 0.46225 0.03876  0.03271  0.04152  97  LYS   A CG  
750  C  CD  . LYS   A 97  ? 0.27397 0.19946 0.49321 0.04051  0.02468  0.05753  97  LYS   A CD  
751  C  CE  . LYS   A 97  ? 0.29155 0.22165 0.52911 0.04348  0.02317  0.07438  97  LYS   A CE  
752  N  NZ  . LYS   A 97  ? 0.35093 0.29931 0.59736 0.04712  0.01931  0.08614  97  LYS   A NZ  
753  N  N   . THR   A 98  ? 0.23100 0.10600 0.39380 0.01179  0.02938  -0.00035 98  THR   A N   
754  C  CA  . THR   A 98  ? 0.23888 0.11653 0.38357 0.00407  0.02528  -0.00988 98  THR   A CA  
755  C  C   . THR   A 98  ? 0.22304 0.09905 0.35670 0.00420  0.02977  -0.02689 98  THR   A C   
756  O  O   . THR   A 98  ? 0.24783 0.11208 0.38222 0.00413  0.03621  -0.03810 98  THR   A O   
757  C  CB  . THR   A 98  ? 0.25555 0.12419 0.39790 -0.00459 0.02372  -0.01284 98  THR   A CB  
758  O  OG1 . THR   A 98  ? 0.27344 0.14520 0.42473 -0.00475 0.02018  0.00373  98  THR   A OG1 
759  C  CG2 . THR   A 98  ? 0.24859 0.12255 0.37425 -0.01297 0.01915  -0.02182 98  THR   A CG2 
760  N  N   . PRO   A 99  ? 0.21979 0.10712 0.34271 0.00444  0.02699  -0.02925 99  PRO   A N   
761  C  CA  . PRO   A 99  ? 0.23461 0.12225 0.34447 0.00369  0.03120  -0.04513 99  PRO   A CA  
762  C  C   . PRO   A 99  ? 0.24205 0.12761 0.33612 -0.00666 0.02770  -0.05657 99  PRO   A C   
763  O  O   . PRO   A 99  ? 0.21285 0.09873 0.30715 -0.01284 0.02192  -0.05144 99  PRO   A O   
764  C  CB  . PRO   A 99  ? 0.19088 0.09276 0.29689 0.00743  0.02852  -0.04064 99  PRO   A CB  
765  C  CG  . PRO   A 99  ? 0.21872 0.12633 0.32594 0.00428  0.02000  -0.02845 99  PRO   A CG  
766  C  CD  . PRO   A 99  ? 0.19466 0.09497 0.31439 0.00416  0.01954  -0.01839 99  PRO   A CD  
767  N  N   . LYS   A 100 ? 0.24307 0.12822 0.32322 -0.00876 0.03113  -0.07123 100 LYS   A N   
768  C  CA  . LYS   A 100 ? 0.27297 0.16379 0.33538 -0.01848 0.02542  -0.07999 100 LYS   A CA  
769  C  C   . LYS   A 100 ? 0.25263 0.15895 0.31030 -0.01976 0.01848  -0.07270 100 LYS   A C   
770  O  O   . LYS   A 100 ? 0.22283 0.13624 0.28202 -0.01345 0.01992  -0.06869 100 LYS   A O   
771  C  CB  . LYS   A 100 ? 0.34063 0.23174 0.38682 -0.01962 0.02979  -0.09480 100 LYS   A CB  
772  C  CG  . LYS   A 100 ? 0.35200 0.25716 0.37762 -0.02700 0.02329  -0.10065 100 LYS   A CG  
773  C  CD  . LYS   A 100 ? 0.39370 0.29474 0.40924 -0.03690 0.01905  -0.10970 100 LYS   A CD  
774  C  CE  . LYS   A 100 ? 0.33425 0.25342 0.33523 -0.04411 0.00947  -0.10871 100 LYS   A CE  
775  N  NZ  . LYS   A 100 ? 0.34436 0.27070 0.35404 -0.04818 0.00160  -0.09778 100 LYS   A NZ  
776  N  N   . TYR   A 101 ? 0.23378 0.14539 0.28792 -0.02766 0.01113  -0.06999 101 TYR   A N   
777  C  CA  . TYR   A 101 ? 0.19327 0.11917 0.24503 -0.02845 0.00496  -0.06210 101 TYR   A CA  
778  C  C   . TYR   A 101 ? 0.22182 0.15922 0.26286 -0.03747 -0.00197 -0.06480 101 TYR   A C   
779  O  O   . TYR   A 101 ? 0.18922 0.12282 0.22685 -0.04395 -0.00339 -0.07042 101 TYR   A O   
780  C  CB  . TYR   A 101 ? 0.18726 0.11277 0.25193 -0.02483 0.00302  -0.04578 101 TYR   A CB  
781  C  CG  . TYR   A 101 ? 0.22467 0.14320 0.29867 -0.03131 0.00108  -0.04160 101 TYR   A CG  
782  C  CD1 . TYR   A 101 ? 0.21468 0.11893 0.29875 -0.03014 0.00541  -0.04047 101 TYR   A CD1 
783  C  CD2 . TYR   A 101 ? 0.19297 0.12306 0.26335 -0.03719 -0.00467 -0.03620 101 TYR   A CD2 
784  C  CE1 . TYR   A 101 ? 0.24328 0.14332 0.33386 -0.03577 0.00382  -0.03490 101 TYR   A CE1 
785  C  CE2 . TYR   A 101 ? 0.23067 0.15695 0.30937 -0.04284 -0.00566 -0.03074 101 TYR   A CE2 
786  C  CZ  . TYR   A 101 ? 0.24032 0.15159 0.32795 -0.04224 -0.00153 -0.02998 101 TYR   A CZ  
787  O  OH  . TYR   A 101 ? 0.32138 0.23000 0.41611 -0.04795 -0.00229 -0.02382 101 TYR   A OH  
788  N  N   . LYS   A 102 ? 0.18057 0.13448 0.21499 -0.03588 -0.00673 -0.05658 102 LYS   A N   
789  C  CA  . LYS   A 102 ? 0.17444 0.14195 0.20378 -0.04243 -0.01327 -0.05467 102 LYS   A CA  
790  C  C   . LYS   A 102 ? 0.16955 0.14716 0.20106 -0.03814 -0.01565 -0.04067 102 LYS   A C   
791  O  O   . LYS   A 102 ? 0.13949 0.11790 0.16961 -0.03088 -0.01387 -0.03486 102 LYS   A O   
792  C  CB  . LYS   A 102 ? 0.23865 0.21869 0.25282 -0.04492 -0.01605 -0.06182 102 LYS   A CB  
793  C  CG  . LYS   A 102 ? 0.25510 0.22708 0.26023 -0.04666 -0.01286 -0.07383 102 LYS   A CG  
794  C  CD  . LYS   A 102 ? 0.29678 0.28348 0.28616 -0.04929 -0.01723 -0.07613 102 LYS   A CD  
795  C  CE  . LYS   A 102 ? 0.24658 0.24415 0.22808 -0.04323 -0.01577 -0.07249 102 LYS   A CE  
796  N  NZ  . LYS   A 102 ? 0.37087 0.38025 0.33682 -0.04501 -0.01833 -0.07435 102 LYS   A NZ  
797  N  N   . PHE   A 103 ? 0.12838 0.11440 0.16320 -0.04319 -0.01947 -0.03597 103 PHE   A N   
798  C  CA  . PHE   A 103 ? 0.13926 0.13663 0.17373 -0.03976 -0.02091 -0.02497 103 PHE   A CA  
799  C  C   . PHE   A 103 ? 0.14539 0.15853 0.17220 -0.04060 -0.02462 -0.02599 103 PHE   A C   
800  O  O   . PHE   A 103 ? 0.10457 0.12631 0.13363 -0.04735 -0.02848 -0.02830 103 PHE   A O   
801  C  CB  . PHE   A 103 ? 0.14622 0.14429 0.19108 -0.04379 -0.02106 -0.01774 103 PHE   A CB  
802  C  CG  . PHE   A 103 ? 0.15206 0.13713 0.20451 -0.04201 -0.01771 -0.01233 103 PHE   A CG  
803  C  CD1 . PHE   A 103 ? 0.12669 0.10243 0.17771 -0.03584 -0.01532 -0.01236 103 PHE   A CD1 
804  C  CD2 . PHE   A 103 ? 0.17504 0.15864 0.23775 -0.04663 -0.01698 -0.00570 103 PHE   A CD2 
805  C  CE1 . PHE   A 103 ? 0.13030 0.09570 0.19014 -0.03395 -0.01301 -0.00535 103 PHE   A CE1 
806  C  CE2 . PHE   A 103 ? 0.16514 0.13748 0.23519 -0.04490 -0.01412 0.00162  103 PHE   A CE2 
807  C  CZ  . PHE   A 103 ? 0.13736 0.10076 0.20611 -0.03845 -0.01255 0.00201  103 PHE   A CZ  
808  N  N   . VAL   A 104 ? 0.11632 0.13373 0.13539 -0.03415 -0.02386 -0.02356 104 VAL   A N   
809  C  CA  . VAL   A 104 ? 0.14341 0.17520 0.15663 -0.03341 -0.02683 -0.02179 104 VAL   A CA  
810  C  C   . VAL   A 104 ? 0.11717 0.15329 0.13216 -0.02763 -0.02533 -0.01234 104 VAL   A C   
811  O  O   . VAL   A 104 ? 0.16797 0.19588 0.18405 -0.02423 -0.02236 -0.00902 104 VAL   A O   
812  C  CB  . VAL   A 104 ? 0.15104 0.18369 0.15362 -0.03133 -0.02637 -0.02701 104 VAL   A CB  
813  C  CG1 . VAL   A 104 ? 0.18977 0.21397 0.18922 -0.03616 -0.02535 -0.03845 104 VAL   A CG1 
814  C  CG2 . VAL   A 104 ? 0.17060 0.19677 0.17156 -0.02409 -0.02246 -0.02345 104 VAL   A CG2 
815  N  N   . ARG   A 105 ? 0.08306 0.13232 0.09843 -0.02668 -0.02739 -0.00796 105 ARG   A N   
816  C  CA  . ARG   A 105 ? 0.08260 0.13447 0.09877 -0.02037 -0.02474 -0.00065 105 ARG   A CA  
817  C  C   . ARG   A 105 ? 0.10554 0.16205 0.11567 -0.01664 -0.02558 0.00059  105 ARG   A C   
818  O  O   . ARG   A 105 ? 0.10131 0.16782 0.10947 -0.01935 -0.02940 -0.00030 105 ARG   A O   
819  C  CB  . ARG   A 105 ? 0.12167 0.18482 0.14743 -0.02086 -0.02466 0.00542  105 ARG   A CB  
820  C  CG  . ARG   A 105 ? 0.09887 0.16125 0.12560 -0.01399 -0.01964 0.01124  105 ARG   A CG  
821  C  CD  . ARG   A 105 ? 0.07528 0.15049 0.11382 -0.01385 -0.01821 0.01729  105 ARG   A CD  
822  N  NE  . ARG   A 105 ? 0.10373 0.17860 0.14373 -0.00634 -0.01212 0.02192  105 ARG   A NE  
823  C  CZ  . ARG   A 105 ? 0.08071 0.14847 0.11855 -0.00419 -0.00581 0.02233  105 ARG   A CZ  
824  N  NH1 . ARG   A 105 ? 0.08467 0.14652 0.11967 -0.00857 -0.00542 0.02061  105 ARG   A NH1 
825  N  NH2 . ARG   A 105 ? 0.06652 0.13294 0.10489 0.00242  0.00062  0.02472  105 ARG   A NH2 
826  N  N   . ILE   A 106 ? 0.10747 0.15716 0.11437 -0.01133 -0.02237 0.00295  106 ILE   A N   
827  C  CA  . ILE   A 106 ? 0.13385 0.18598 0.13634 -0.00812 -0.02241 0.00509  106 ILE   A CA  
828  C  C   . ILE   A 106 ? 0.12668 0.18449 0.13446 -0.00351 -0.02100 0.01261  106 ILE   A C   
829  O  O   . ILE   A 106 ? 0.11486 0.17250 0.12838 -0.00193 -0.01857 0.01489  106 ILE   A O   
830  C  CB  . ILE   A 106 ? 0.12711 0.16819 0.12493 -0.00598 -0.01991 0.00317  106 ILE   A CB  
831  C  CG1 . ILE   A 106 ? 0.12781 0.16033 0.12694 -0.00360 -0.01724 0.00503  106 ILE   A CG1 
832  C  CG2 . ILE   A 106 ? 0.18145 0.21778 0.17663 -0.00893 -0.02012 -0.00341 106 ILE   A CG2 
833  C  CD1 . ILE   A 106 ? 0.17235 0.19660 0.16822 -0.00220 -0.01613 0.00462  106 ILE   A CD1 
834  N  N   . GLN   A 107 ? 0.12007 0.18235 0.12648 -0.00086 -0.02151 0.01693  107 GLN   A N   
835  C  CA  . GLN   A 107 ? 0.12344 0.18947 0.13580 0.00457  -0.01970 0.02522  107 GLN   A CA  
836  C  C   . GLN   A 107 ? 0.13778 0.18952 0.14819 0.00808  -0.01514 0.02509  107 GLN   A C   
837  O  O   . GLN   A 107 ? 0.13398 0.17894 0.13806 0.00617  -0.01524 0.02140  107 GLN   A O   
838  C  CB  . GLN   A 107 ? 0.15031 0.22959 0.16159 0.00437  -0.02362 0.03114  107 GLN   A CB  
839  C  CG  . GLN   A 107 ? 0.15375 0.24595 0.16714 0.00009  -0.02799 0.03109  107 GLN   A CG  
840  C  CD  . GLN   A 107 ? 0.14171 0.24110 0.16862 0.00349  -0.02691 0.03792  107 GLN   A CD  
841  O  OE1 . GLN   A 107 ? 0.11263 0.21101 0.14694 0.01008  -0.02331 0.04541  107 GLN   A OE1 
842  N  NE2 . GLN   A 107 ? 0.14304 0.24840 0.17477 -0.00065 -0.02894 0.03534  107 GLN   A NE2 
843  N  N   . PRO   A 108 ? 0.13916 0.18616 0.15577 0.01292  -0.01080 0.02872  108 PRO   A N   
844  C  CA  . PRO   A 108 ? 0.17191 0.20535 0.18706 0.01527  -0.00706 0.02869  108 PRO   A CA  
845  C  C   . PRO   A 108 ? 0.15456 0.19136 0.16862 0.01498  -0.00908 0.03353  108 PRO   A C   
846  O  O   . PRO   A 108 ? 0.18594 0.23614 0.20231 0.01564  -0.01194 0.04000  108 PRO   A O   
847  C  CB  . PRO   A 108 ? 0.14124 0.17159 0.16544 0.02137  -0.00154 0.03289  108 PRO   A CB  
848  C  CG  . PRO   A 108 ? 0.17892 0.22513 0.21140 0.02283  -0.00296 0.03750  108 PRO   A CG  
849  C  CD  . PRO   A 108 ? 0.14632 0.20000 0.17269 0.01636  -0.00842 0.03271  108 PRO   A CD  
850  N  N   . GLY   A 109 ? 0.13132 0.15745 0.14174 0.01338  -0.00782 0.03106  109 GLY   A N   
851  C  CA  . GLY   A 109 ? 0.14945 0.17882 0.15868 0.01237  -0.00869 0.03553  109 GLY   A CA  
852  C  C   . GLY   A 109 ? 0.17919 0.21327 0.18111 0.00809  -0.01109 0.03045  109 GLY   A C   
853  O  O   . GLY   A 109 ? 0.17992 0.21355 0.18073 0.00679  -0.01013 0.03214  109 GLY   A O   
854  N  N   . GLN   A 110 ? 0.12228 0.16043 0.12067 0.00600  -0.01333 0.02450  110 GLN   A N   
855  C  CA  . GLN   A 110 ? 0.15013 0.18976 0.14325 0.00273  -0.01421 0.01853  110 GLN   A CA  
856  C  C   . GLN   A 110 ? 0.14373 0.17295 0.13789 0.00144  -0.01341 0.01373  110 GLN   A C   
857  O  O   . GLN   A 110 ? 0.13924 0.16067 0.13500 0.00176  -0.01320 0.01294  110 GLN   A O   
858  C  CB  . GLN   A 110 ? 0.12973 0.17676 0.11952 0.00023  -0.01686 0.01388  110 GLN   A CB  
859  C  CG  . GLN   A 110 ? 0.20653 0.26695 0.19505 0.00004  -0.01968 0.01857  110 GLN   A CG  
860  C  CD  . GLN   A 110 ? 0.25544 0.32329 0.24088 -0.00444 -0.02336 0.01290  110 GLN   A CD  
861  O  OE1 . GLN   A 110 ? 0.17566 0.24114 0.16571 -0.00584 -0.02433 0.01004  110 GLN   A OE1 
862  N  NE2 . GLN   A 110 ? 0.37047 0.44710 0.34710 -0.00752 -0.02509 0.01076  110 GLN   A NE2 
863  N  N   . THR   A 111 ? 0.12068 0.15090 0.11384 0.00004  -0.01271 0.01090  111 THR   A N   
864  C  CA  . THR   A 111 ? 0.13144 0.15511 0.12806 -0.00100 -0.01268 0.00862  111 THR   A CA  
865  C  C   . THR   A 111 ? 0.12479 0.14768 0.12177 -0.00178 -0.01322 0.00337  111 THR   A C   
866  O  O   . THR   A 111 ? 0.13960 0.16608 0.13358 -0.00232 -0.01304 -0.00006 111 THR   A O   
867  C  CB  . THR   A 111 ? 0.14023 0.16610 0.14042 -0.00121 -0.01051 0.01131  111 THR   A CB  
868  O  OG1 . THR   A 111 ? 0.15053 0.18437 0.14734 -0.00056 -0.00776 0.01017  111 THR   A OG1 
869  C  CG2 . THR   A 111 ? 0.12984 0.15355 0.13195 -0.00122 -0.00991 0.01725  111 THR   A CG2 
870  N  N   . PHE   A 112 ? 0.10800 0.12593 0.10926 -0.00234 -0.01431 0.00322  112 PHE   A N   
871  C  CA  . PHE   A 112 ? 0.11444 0.13022 0.11934 -0.00239 -0.01450 0.00050  112 PHE   A CA  
872  C  C   . PHE   A 112 ? 0.11853 0.13265 0.13022 -0.00258 -0.01618 0.00364  112 PHE   A C   
873  O  O   . PHE   A 112 ? 0.15531 0.16881 0.16663 -0.00413 -0.01830 0.00652  112 PHE   A O   
874  C  CB  . PHE   A 112 ? 0.10113 0.11391 0.10363 -0.00356 -0.01613 -0.00086 112 PHE   A CB  
875  C  CG  . PHE   A 112 ? 0.16404 0.17378 0.16329 -0.00433 -0.01799 0.00193  112 PHE   A CG  
876  C  CD1 . PHE   A 112 ? 0.15080 0.16158 0.14626 -0.00364 -0.01716 0.00289  112 PHE   A CD1 
877  C  CD2 . PHE   A 112 ? 0.11915 0.12516 0.11883 -0.00552 -0.01998 0.00374  112 PHE   A CD2 
878  C  CE1 . PHE   A 112 ? 0.13785 0.14446 0.12982 -0.00383 -0.01701 0.00374  112 PHE   A CE1 
879  C  CE2 . PHE   A 112 ? 0.13383 0.13703 0.12722 -0.00666 -0.02067 0.00487  112 PHE   A CE2 
880  C  CZ  . PHE   A 112 ? 0.15924 0.16200 0.14870 -0.00563 -0.01849 0.00391  112 PHE   A CZ  
881  N  N   . SER   A 113 ? 0.11110 0.12463 0.13005 -0.00125 -0.01534 0.00321  113 SER   A N   
882  C  CA  . SER   A 113 ? 0.09659 0.11084 0.12425 -0.00125 -0.01816 0.00809  113 SER   A CA  
883  C  C   . SER   A 113 ? 0.07955 0.08982 0.10482 -0.00284 -0.02215 0.01054  113 SER   A C   
884  O  O   . SER   A 113 ? 0.11772 0.12412 0.14018 -0.00276 -0.02093 0.00829  113 SER   A O   
885  C  CB  . SER   A 113 ? 0.13987 0.15633 0.17983 0.00234  -0.01426 0.00824  113 SER   A CB  
886  O  OG  . SER   A 113 ? 0.12283 0.14386 0.16310 0.00386  -0.00902 0.00561  113 SER   A OG  
887  N  N   . VAL   A 114 ? 0.09933 0.11150 0.12542 -0.00504 -0.02710 0.01549  114 VAL   A N   
888  C  CA  . VAL   A 114 ? 0.11586 0.12631 0.13811 -0.00699 -0.03116 0.01937  114 VAL   A CA  
889  C  C   . VAL   A 114 ? 0.12374 0.13891 0.15874 -0.00586 -0.03448 0.02681  114 VAL   A C   
890  O  O   . VAL   A 114 ? 0.11543 0.13710 0.15785 -0.00653 -0.03712 0.02990  114 VAL   A O   
891  C  CB  . VAL   A 114 ? 0.09474 0.10406 0.10405 -0.01134 -0.03465 0.01868  114 VAL   A CB  
892  C  CG1 . VAL   A 114 ? 0.14472 0.15444 0.14825 -0.01381 -0.03888 0.02361  114 VAL   A CG1 
893  C  CG2 . VAL   A 114 ? 0.13926 0.14393 0.13894 -0.01107 -0.03048 0.01273  114 VAL   A CG2 
894  N  N   . LEU   A 115 ? 0.11975 0.13247 0.15946 -0.00422 -0.03443 0.03097  115 LEU   A N   
895  C  CA  . LEU   A 115 ? 0.10404 0.12206 0.15633 -0.00295 -0.03863 0.04090  115 LEU   A CA  
896  C  C   . LEU   A 115 ? 0.11988 0.14023 0.16040 -0.00764 -0.04524 0.04680  115 LEU   A C   
897  O  O   . LEU   A 115 ? 0.13017 0.14607 0.16547 -0.00801 -0.04416 0.04889  115 LEU   A O   
898  C  CB  . LEU   A 115 ? 0.13168 0.14465 0.19898 0.00233  -0.03381 0.04320  115 LEU   A CB  
899  C  CG  . LEU   A 115 ? 0.11334 0.13166 0.19797 0.00535  -0.03727 0.05557  115 LEU   A CG  
900  C  CD1 . LEU   A 115 ? 0.10855 0.13657 0.20431 0.00672  -0.03713 0.05690  115 LEU   A CD1 
901  C  CD2 . LEU   A 115 ? 0.12083 0.12937 0.21918 0.01043  -0.03108 0.05674  115 LEU   A CD2 
902  N  N   . ALA   A 116 ? 0.10158 0.12745 0.13527 -0.01208 -0.04934 0.04685  116 ALA   A N   
903  C  CA  . ALA   A 116 ? 0.14505 0.17248 0.16485 -0.01691 -0.05277 0.04923  116 ALA   A CA  
904  C  C   . ALA   A 116 ? 0.16636 0.19862 0.19603 -0.01554 -0.05459 0.05951  116 ALA   A C   
905  O  O   . ALA   A 116 ? 0.15981 0.19761 0.20586 -0.01314 -0.05541 0.06469  116 ALA   A O   
906  C  CB  . ALA   A 116 ? 0.15983 0.19080 0.17160 -0.02225 -0.05653 0.04587  116 ALA   A CB  
907  N  N   . CYS   A 117 ? 0.13209 0.16304 0.15231 -0.01710 -0.05477 0.06308  117 CYS   A N   
908  C  CA  . CYS   A 117 ? 0.17195 0.20692 0.20144 -0.01579 -0.05599 0.07377  117 CYS   A CA  
909  C  C   . CYS   A 117 ? 0.19563 0.23525 0.20837 -0.02094 -0.05950 0.07702  117 CYS   A C   
910  O  O   . CYS   A 117 ? 0.19290 0.22937 0.18674 -0.02421 -0.05847 0.07046  117 CYS   A O   
911  C  CB  . CYS   A 117 ? 0.20526 0.23266 0.24436 -0.01142 -0.05093 0.07665  117 CYS   A CB  
912  S  SG  . CYS   A 117 ? 0.23609 0.25738 0.29687 -0.00460 -0.04601 0.07359  117 CYS   A SG  
913  N  N   . TYR   A 118 ? 0.20198 0.24945 0.22223 -0.02129 -0.06315 0.08737  118 TYR   A N   
914  C  CA  . TYR   A 118 ? 0.22471 0.27823 0.23103 -0.02569 -0.06676 0.09282  118 TYR   A CA  
915  C  C   . TYR   A 118 ? 0.23941 0.29677 0.26062 -0.02276 -0.06688 0.10612  118 TYR   A C   
916  O  O   . TYR   A 118 ? 0.22908 0.28987 0.27103 -0.01923 -0.06769 0.11234  118 TYR   A O   
917  C  CB  . TYR   A 118 ? 0.22806 0.29024 0.22569 -0.03131 -0.07368 0.09176  118 TYR   A CB  
918  C  CG  . TYR   A 118 ? 0.23322 0.28981 0.21840 -0.03409 -0.07285 0.07842  118 TYR   A CG  
919  C  CD1 . TYR   A 118 ? 0.23503 0.29062 0.23227 -0.03260 -0.07271 0.07425  118 TYR   A CD1 
920  C  CD2 . TYR   A 118 ? 0.25878 0.31030 0.22120 -0.03752 -0.07091 0.07011  118 TYR   A CD2 
921  C  CE1 . TYR   A 118 ? 0.22388 0.27374 0.21126 -0.03501 -0.07152 0.06292  118 TYR   A CE1 
922  C  CE2 . TYR   A 118 ? 0.27062 0.31579 0.22353 -0.03956 -0.06934 0.05815  118 TYR   A CE2 
923  C  CZ  . TYR   A 118 ? 0.27652 0.32073 0.24225 -0.03847 -0.06995 0.05491  118 TYR   A CZ  
924  O  OH  . TYR   A 118 ? 0.26345 0.30075 0.22113 -0.04045 -0.06807 0.04391  118 TYR   A OH  
925  N  N   . ASN   A 119 ? 0.26527 0.32162 0.27708 -0.02382 -0.06509 0.11062  119 ASN   A N   
926  C  CA  . ASN   A 119 ? 0.23185 0.29117 0.25720 -0.02142 -0.06480 0.12409  119 ASN   A CA  
927  C  C   . ASN   A 119 ? 0.23302 0.28448 0.28331 -0.01490 -0.05980 0.12594  119 ASN   A C   
928  O  O   . ASN   A 119 ? 0.23220 0.28687 0.30147 -0.01169 -0.06023 0.13637  119 ASN   A O   
929  C  CB  . ASN   A 119 ? 0.28337 0.35630 0.31218 -0.02379 -0.07218 0.13484  119 ASN   A CB  
930  C  CG  . ASN   A 119 ? 0.30220 0.38226 0.30547 -0.03076 -0.07734 0.13199  119 ASN   A CG  
931  O  OD1 . ASN   A 119 ? 0.33133 0.41069 0.31735 -0.03317 -0.07561 0.13249  119 ASN   A OD1 
932  N  ND2 . ASN   A 119 ? 0.32576 0.41242 0.32641 -0.03422 -0.08326 0.12861  119 ASN   A ND2 
933  N  N   . GLY   A 120 ? 0.18990 0.23078 0.24027 -0.01290 -0.05477 0.11553  120 GLY   A N   
934  C  CA  . GLY   A 120 ? 0.19593 0.22762 0.26725 -0.00712 -0.04949 0.11414  120 GLY   A CA  
935  C  C   . GLY   A 120 ? 0.23755 0.27221 0.32482 -0.00345 -0.05016 0.11307  120 GLY   A C   
936  O  O   . GLY   A 120 ? 0.21668 0.24349 0.32172 0.00194  -0.04473 0.11135  120 GLY   A O   
937  N  N   . SER   A 121 ? 0.23606 0.28151 0.31802 -0.00640 -0.05601 0.11382  121 SER   A N   
938  C  CA  . SER   A 121 ? 0.21508 0.26538 0.31372 -0.00328 -0.05640 0.11452  121 SER   A CA  
939  C  C   . SER   A 121 ? 0.24914 0.29800 0.33974 -0.00459 -0.05630 0.10300  121 SER   A C   
940  O  O   . SER   A 121 ? 0.21980 0.27181 0.29140 -0.01036 -0.06060 0.09828  121 SER   A O   
941  C  CB  . SER   A 121 ? 0.26691 0.33158 0.36983 -0.00594 -0.06328 0.12548  121 SER   A CB  
942  O  OG  . SER   A 121 ? 0.30897 0.37529 0.42707 -0.00271 -0.06221 0.13756  121 SER   A OG  
943  N  N   . PRO   A 122 ? 0.22851 0.27193 0.33273 0.00070  -0.05079 0.09783  122 PRO   A N   
944  C  CA  . PRO   A 122 ? 0.22630 0.26907 0.32430 -0.00021 -0.05029 0.08786  122 PRO   A CA  
945  C  C   . PRO   A 122 ? 0.21513 0.26952 0.31134 -0.00454 -0.05626 0.09002  122 PRO   A C   
946  O  O   . PRO   A 122 ? 0.22734 0.29028 0.33866 -0.00321 -0.05794 0.09842  122 PRO   A O   
947  C  CB  . PRO   A 122 ? 0.21756 0.25430 0.33405 0.00714  -0.04252 0.08445  122 PRO   A CB  
948  C  CG  . PRO   A 122 ? 0.22116 0.24809 0.34519 0.01067  -0.03788 0.08731  122 PRO   A CG  
949  C  CD  . PRO   A 122 ? 0.22826 0.26092 0.34704 0.00684  -0.04334 0.09757  122 PRO   A CD  
950  N  N   . SER   A 123 ? 0.21624 0.27036 0.29478 -0.00990 -0.05921 0.08240  123 SER   A N   
951  C  CA  . SER   A 123 ? 0.18088 0.24355 0.25549 -0.01538 -0.06489 0.08235  123 SER   A CA  
952  C  C   . SER   A 123 ? 0.16883 0.23175 0.24935 -0.01466 -0.06254 0.07613  123 SER   A C   
953  O  O   . SER   A 123 ? 0.17379 0.24559 0.26448 -0.01621 -0.06525 0.08003  123 SER   A O   
954  C  CB  . SER   A 123 ? 0.22571 0.28683 0.27592 -0.02257 -0.06934 0.07760  123 SER   A CB  
955  O  OG  . SER   A 123 ? 0.31663 0.38545 0.36322 -0.02861 -0.07552 0.07798  123 SER   A OG  
956  N  N   . GLY   A 124 ? 0.13161 0.18613 0.20627 -0.01279 -0.05787 0.06732  124 GLY   A N   
957  C  CA  . GLY   A 124 ? 0.09380 0.14928 0.17305 -0.01250 -0.05544 0.06195  124 GLY   A CA  
958  C  C   . GLY   A 124 ? 0.10205 0.14888 0.17521 -0.00978 -0.05035 0.05373  124 GLY   A C   
959  O  O   . GLY   A 124 ? 0.10606 0.14570 0.16753 -0.00992 -0.04999 0.05106  124 GLY   A O   
960  N  N   . VAL   A 125 ? 0.08408 0.13296 0.16618 -0.00730 -0.04623 0.05056  125 VAL   A N   
961  C  CA  . VAL   A 125 ? 0.09835 0.14168 0.17707 -0.00452 -0.04151 0.04352  125 VAL   A CA  
962  C  C   . VAL   A 125 ? 0.10986 0.15434 0.18262 -0.00870 -0.04145 0.03888  125 VAL   A C   
963  O  O   . VAL   A 125 ? 0.08198 0.13381 0.16369 -0.01073 -0.04236 0.04194  125 VAL   A O   
964  C  CB  . VAL   A 125 ? 0.11379 0.15581 0.20692 0.00336  -0.03263 0.04229  125 VAL   A CB  
965  C  CG1 . VAL   A 125 ? 0.12804 0.18070 0.23894 0.00582  -0.02984 0.04586  125 VAL   A CG1 
966  C  CG2 . VAL   A 125 ? 0.11012 0.14234 0.19007 0.00440  -0.02553 0.03172  125 VAL   A CG2 
967  N  N   . TYR   A 126 ? 0.12374 0.15884 0.18019 -0.00987 -0.03843 0.03123  126 TYR   A N   
968  C  CA  . TYR   A 126 ? 0.14037 0.17393 0.19120 -0.01309 -0.03708 0.02741  126 TYR   A CA  
969  C  C   . TYR   A 126 ? 0.12243 0.14793 0.16169 -0.01062 -0.03100 0.02083  126 TYR   A C   
970  O  O   . TYR   A 126 ? 0.11514 0.13581 0.14809 -0.00834 -0.02937 0.01824  126 TYR   A O   
971  C  CB  . TYR   A 126 ? 0.13810 0.16996 0.18025 -0.02067 -0.04443 0.02722  126 TYR   A CB  
972  C  CG  . TYR   A 126 ? 0.15108 0.17538 0.17653 -0.02252 -0.04699 0.02418  126 TYR   A CG  
973  C  CD1 . TYR   A 126 ? 0.19933 0.21382 0.21141 -0.02184 -0.04258 0.01771  126 TYR   A CD1 
974  C  CD2 . TYR   A 126 ? 0.15788 0.18457 0.18063 -0.02386 -0.05097 0.02797  126 TYR   A CD2 
975  C  CE1 . TYR   A 126 ? 0.18197 0.19096 0.18008 -0.02307 -0.04339 0.01529  126 TYR   A CE1 
976  C  CE2 . TYR   A 126 ? 0.16893 0.18981 0.17590 -0.02529 -0.05148 0.02565  126 TYR   A CE2 
977  C  CZ  . TYR   A 126 ? 0.18296 0.19569 0.17797 -0.02534 -0.04845 0.01939  126 TYR   A CZ  
978  O  OH  . TYR   A 126 ? 0.25281 0.26115 0.23313 -0.02657 -0.04783 0.01748  126 TYR   A OH  
979  N  N   . GLN   A 127 ? 0.12910 0.15402 0.16650 -0.01174 -0.02828 0.01929  127 GLN   A N   
980  C  CA  . GLN   A 127 ? 0.13974 0.16044 0.16860 -0.00930 -0.02318 0.01535  127 GLN   A CA  
981  C  C   . GLN   A 127 ? 0.16629 0.17904 0.18435 -0.01209 -0.02496 0.01313  127 GLN   A C   
982  O  O   . GLN   A 127 ? 0.19616 0.20633 0.21448 -0.01649 -0.02790 0.01383  127 GLN   A O   
983  C  CB  . GLN   A 127 ? 0.16788 0.19453 0.20287 -0.00778 -0.01804 0.01710  127 GLN   A CB  
984  C  CG  . GLN   A 127 ? 0.18093 0.20722 0.20813 -0.00510 -0.01327 0.01464  127 GLN   A CG  
985  C  CD  . GLN   A 127 ? 0.16931 0.19732 0.19528 -0.00157 -0.00985 0.01051  127 GLN   A CD  
986  O  OE1 . GLN   A 127 ? 0.16794 0.19465 0.19926 -0.00044 -0.01087 0.00956  127 GLN   A OE1 
987  N  NE2 . GLN   A 127 ? 0.18101 0.21145 0.19965 -0.00027 -0.00613 0.00817  127 GLN   A NE2 
988  N  N   . CYS   A 128 ? 0.15032 0.15902 0.15996 -0.00987 -0.02311 0.01013  128 CYS   A N   
989  C  CA  . CYS   A 128 ? 0.17073 0.17239 0.17196 -0.01041 -0.02234 0.00804  128 CYS   A CA  
990  C  C   . CYS   A 128 ? 0.17188 0.17512 0.17192 -0.00684 -0.01822 0.00837  128 CYS   A C   
991  O  O   . CYS   A 128 ? 0.15191 0.16114 0.15326 -0.00473 -0.01676 0.00830  128 CYS   A O   
992  C  CB  . CYS   A 128 ? 0.16749 0.16532 0.16092 -0.01090 -0.02367 0.00575  128 CYS   A CB  
993  S  SG  . CYS   A 128 ? 0.33594 0.33242 0.32554 -0.01570 -0.02929 0.00608  128 CYS   A SG  
994  N  N   . ALA   A 129 ? 0.14761 0.14523 0.14491 -0.00628 -0.01643 0.00856  129 ALA   A N   
995  C  CA  . ALA   A 129 ? 0.14017 0.14038 0.13704 -0.00252 -0.01352 0.01043  129 ALA   A CA  
996  C  C   . ALA   A 129 ? 0.17763 0.17357 0.17049 -0.00105 -0.01219 0.00812  129 ALA   A C   
997  O  O   . ALA   A 129 ? 0.15708 0.14446 0.14585 -0.00272 -0.01181 0.00504  129 ALA   A O   
998  C  CB  . ALA   A 129 ? 0.17209 0.17040 0.17293 -0.00140 -0.01113 0.01511  129 ALA   A CB  
999  N  N   . MET   A 130 ? 0.14005 0.14277 0.13390 0.00160  -0.01125 0.00944  130 MET   A N   
1000 C  CA  . MET   A 130 ? 0.13520 0.13649 0.12860 0.00397  -0.00851 0.00905  130 MET   A CA  
1001 C  C   . MET   A 130 ? 0.14940 0.14547 0.14668 0.00746  -0.00467 0.01196  130 MET   A C   
1002 O  O   . MET   A 130 ? 0.18170 0.18376 0.18453 0.00985  -0.00465 0.01769  130 MET   A O   
1003 C  CB  . MET   A 130 ? 0.12061 0.13310 0.11717 0.00492  -0.00943 0.01083  130 MET   A CB  
1004 C  CG  . MET   A 130 ? 0.11900 0.13452 0.11836 0.00703  -0.00658 0.01169  130 MET   A CG  
1005 S  SD  . MET   A 130 ? 0.19752 0.20421 0.19007 0.00584  -0.00340 0.00745  130 MET   A SD  
1006 C  CE  . MET   A 130 ? 0.12992 0.13952 0.12018 0.00097  -0.00816 0.00603  130 MET   A CE  
1007 N  N   . ARG   A 131 ? 0.14758 0.13196 0.14169 0.00767  -0.00117 0.00821  131 ARG   A N   
1008 C  CA  . ARG   A 131 ? 0.15919 0.13511 0.15865 0.01136  0.00371  0.01025  131 ARG   A CA  
1009 C  C   . ARG   A 131 ? 0.17384 0.15725 0.18219 0.01798  0.00757  0.01595  131 ARG   A C   
1010 O  O   . ARG   A 131 ? 0.12713 0.11997 0.13574 0.01879  0.00732  0.01607  131 ARG   A O   
1011 C  CB  . ARG   A 131 ? 0.16577 0.12572 0.15802 0.00939  0.00732  0.00244  131 ARG   A CB  
1012 C  CG  . ARG   A 131 ? 0.20177 0.15585 0.18632 0.00180  0.00223  -0.00250 131 ARG   A CG  
1013 C  CD  . ARG   A 131 ? 0.18754 0.14222 0.17940 -0.00032 -0.00067 0.00216  131 ARG   A CD  
1014 N  NE  . ARG   A 131 ? 0.16260 0.10904 0.16285 0.00340  0.00439  0.00588  131 ARG   A NE  
1015 C  CZ  . ARG   A 131 ? 0.22221 0.16954 0.23070 0.00280  0.00363  0.01253  131 ARG   A CZ  
1016 N  NH1 . ARG   A 131 ? 0.19366 0.14968 0.20263 -0.00137 -0.00120 0.01497  131 ARG   A NH1 
1017 N  NH2 . ARG   A 131 ? 0.21598 0.15547 0.23353 0.00689  0.00864  0.01769  131 ARG   A NH2 
1018 N  N   . PRO   A 132 ? 0.15286 0.13326 0.17073 0.02273  0.01102  0.02207  132 PRO   A N   
1019 C  CA  . PRO   A 132 ? 0.15408 0.14245 0.18324 0.02988  0.01498  0.02875  132 PRO   A CA  
1020 C  C   . PRO   A 132 ? 0.17667 0.16155 0.20487 0.03261  0.02127  0.02331  132 PRO   A C   
1021 O  O   . PRO   A 132 ? 0.15103 0.14893 0.18825 0.03674  0.02268  0.02855  132 PRO   A O   
1022 C  CB  . PRO   A 132 ? 0.22446 0.20426 0.26425 0.03472  0.01910  0.03559  132 PRO   A CB  
1023 C  CG  . PRO   A 132 ? 0.21812 0.19643 0.25328 0.02917  0.01394  0.03692  132 PRO   A CG  
1024 C  CD  . PRO   A 132 ? 0.19791 0.17020 0.21957 0.02197  0.01107  0.02569  132 PRO   A CD  
1025 N  N   . ASN   A 133 ? 0.17281 0.14201 0.19032 0.03008  0.02521  0.01331  133 ASN   A N   
1026 C  CA  . ASN   A 133 ? 0.15206 0.11907 0.16601 0.03246  0.03228  0.00801  133 ASN   A CA  
1027 C  C   . ASN   A 133 ? 0.18143 0.15750 0.18535 0.02708  0.02802  0.00500  133 ASN   A C   
1028 O  O   . ASN   A 133 ? 0.17689 0.14985 0.17322 0.02704  0.03351  -0.00023 133 ASN   A O   
1029 C  CB  . ASN   A 133 ? 0.21080 0.15645 0.21594 0.03228  0.03970  -0.00196 133 ASN   A CB  
1030 C  CG  . ASN   A 133 ? 0.17830 0.11458 0.16740 0.02298  0.03352  -0.00991 133 ASN   A CG  
1031 O  OD1 . ASN   A 133 ? 0.17106 0.11690 0.15685 0.01779  0.02470  -0.00750 133 ASN   A OD1 
1032 N  ND2 . ASN   A 133 ? 0.22176 0.13942 0.20171 0.02071  0.03822  -0.01954 133 ASN   A ND2 
1033 N  N   . PHE   A 134 ? 0.13447 0.12087 0.13814 0.02270  0.01924  0.00830  134 PHE   A N   
1034 C  CA  . PHE   A 134 ? 0.16033 0.15495 0.15813 0.01788  0.01484  0.00711  134 PHE   A CA  
1035 C  C   . PHE   A 134 ? 0.14853 0.13345 0.13131 0.01258  0.01381  0.00015  134 PHE   A C   
1036 O  O   . PHE   A 134 ? 0.20674 0.19623 0.18443 0.00980  0.01293  -0.00026 134 PHE   A O   
1037 C  CB  . PHE   A 134 ? 0.13341 0.13928 0.13818 0.02053  0.01884  0.01035  134 PHE   A CB  
1038 C  CG  . PHE   A 134 ? 0.12276 0.14408 0.14197 0.02277  0.01578  0.01818  134 PHE   A CG  
1039 C  CD1 . PHE   A 134 ? 0.10967 0.14088 0.12956 0.01783  0.00794  0.01979  134 PHE   A CD1 
1040 C  CD2 . PHE   A 134 ? 0.15221 0.17847 0.18470 0.02977  0.02085  0.02397  134 PHE   A CD2 
1041 C  CE1 . PHE   A 134 ? 0.11169 0.15830 0.14267 0.01844  0.00409  0.02618  134 PHE   A CE1 
1042 C  CE2 . PHE   A 134 ? 0.21730 0.26087 0.26344 0.03127  0.01657  0.03266  134 PHE   A CE2 
1043 C  CZ  . PHE   A 134 ? 0.13337 0.18755 0.17743 0.02491  0.00766  0.03334  134 PHE   A CZ  
1044 N  N   . THR   A 135 ? 0.15574 0.12799 0.13171 0.01056  0.01363  -0.00460 135 THR   A N   
1045 C  CA  . THR   A 135 ? 0.16461 0.13122 0.12717 0.00400  0.00944  -0.00968 135 THR   A CA  
1046 C  C   . THR   A 135 ? 0.15875 0.12815 0.12476 0.00033  0.00148  -0.00722 135 THR   A C   
1047 O  O   . THR   A 135 ? 0.11701 0.08980 0.09271 0.00263  0.00056  -0.00311 135 THR   A O   
1048 C  CB  . THR   A 135 ? 0.18492 0.13627 0.13654 0.00229  0.01379  -0.01785 135 THR   A CB  
1049 O  OG1 . THR   A 135 ? 0.17086 0.11319 0.12951 0.00322  0.01434  -0.01827 135 THR   A OG1 
1050 C  CG2 . THR   A 135 ? 0.19872 0.14695 0.14713 0.00710  0.02406  -0.02104 135 THR   A CG2 
1051 N  N   . ILE   A 136 ? 0.13548 0.10476 0.09383 -0.00519 -0.00395 -0.00888 136 ILE   A N   
1052 C  CA  . ILE   A 136 ? 0.18847 0.15961 0.15097 -0.00862 -0.01035 -0.00706 136 ILE   A CA  
1053 C  C   . ILE   A 136 ? 0.19409 0.15746 0.14784 -0.01480 -0.01370 -0.01165 136 ILE   A C   
1054 O  O   . ILE   A 136 ? 0.18166 0.14129 0.12282 -0.01773 -0.01341 -0.01580 136 ILE   A O   
1055 C  CB  . ILE   A 136 ? 0.20606 0.18739 0.17307 -0.00921 -0.01486 -0.00277 136 ILE   A CB  
1056 C  CG1 . ILE   A 136 ? 0.19289 0.17530 0.15163 -0.01261 -0.01769 -0.00270 136 ILE   A CG1 
1057 C  CG2 . ILE   A 136 ? 0.13509 0.12387 0.10951 -0.00500 -0.01242 0.00018  136 ILE   A CG2 
1058 C  CD1 . ILE   A 136 ? 0.17365 0.16311 0.13910 -0.01348 -0.02249 0.00199  136 ILE   A CD1 
1059 N  N   . LYS   A 137 ? 0.18128 0.14257 0.14124 -0.01742 -0.01668 -0.01099 137 LYS   A N   
1060 C  CA  . LYS   A 137 ? 0.22891 0.18437 0.18291 -0.02494 -0.02139 -0.01507 137 LYS   A CA  
1061 C  C   . LYS   A 137 ? 0.18256 0.14953 0.14031 -0.02845 -0.02931 -0.01016 137 LYS   A C   
1062 O  O   . LYS   A 137 ? 0.22035 0.19267 0.18960 -0.02956 -0.03231 -0.00607 137 LYS   A O   
1063 C  CB  . LYS   A 137 ? 0.23899 0.18598 0.20035 -0.02662 -0.02001 -0.01609 137 LYS   A CB  
1064 C  CG  . LYS   A 137 ? 0.27562 0.20945 0.23566 -0.02250 -0.01165 -0.02014 137 LYS   A CG  
1065 C  CD  . LYS   A 137 ? 0.30174 0.22731 0.27260 -0.02338 -0.00991 -0.01836 137 LYS   A CD  
1066 C  CE  . LYS   A 137 ? 0.37242 0.28186 0.34319 -0.01906 -0.00095 -0.02261 137 LYS   A CE  
1067 N  NZ  . LYS   A 137 ? 0.41211 0.30494 0.36975 -0.02516 0.00057  -0.03473 137 LYS   A NZ  
1068 N  N   . GLY   A 138 ? 0.22921 0.20078 0.17846 -0.02957 -0.03191 -0.00942 138 GLY   A N   
1069 C  CA  . GLY   A 138 ? 0.19789 0.18061 0.15289 -0.03114 -0.03859 -0.00290 138 GLY   A CA  
1070 C  C   . GLY   A 138 ? 0.20848 0.19416 0.15859 -0.03859 -0.04610 -0.00284 138 GLY   A C   
1071 O  O   . GLY   A 138 ? 0.23079 0.20968 0.17447 -0.04348 -0.04653 -0.00884 138 GLY   A O   
1072 N  N   . SER   A 139 ? 0.17041 0.16690 0.12720 -0.03760 -0.04970 0.00453  139 SER   A N   
1073 C  CA  . SER   A 139 ? 0.18369 0.18598 0.13783 -0.04234 -0.05505 0.00661  139 SER   A CA  
1074 C  C   . SER   A 139 ? 0.20240 0.21102 0.15398 -0.04016 -0.05594 0.01302  139 SER   A C   
1075 O  O   . SER   A 139 ? 0.18143 0.19633 0.14622 -0.03617 -0.05650 0.02055  139 SER   A O   
1076 C  CB  . SER   A 139 ? 0.20873 0.21879 0.17876 -0.04430 -0.05962 0.01132  139 SER   A CB  
1077 O  OG  . SER   A 139 ? 0.20136 0.21928 0.17012 -0.04848 -0.06562 0.01519  139 SER   A OG  
1078 N  N   . PHE   A 140 ? 0.22838 0.23446 0.16307 -0.04265 -0.05523 0.00985  140 PHE   A N   
1079 C  CA  . PHE   A 140 ? 0.21109 0.22156 0.14082 -0.04082 -0.05463 0.01572  140 PHE   A CA  
1080 C  C   . PHE   A 140 ? 0.29408 0.30697 0.20794 -0.04611 -0.05770 0.01433  140 PHE   A C   
1081 O  O   . PHE   A 140 ? 0.31924 0.32514 0.21889 -0.04956 -0.05587 0.00484  140 PHE   A O   
1082 C  CB  . PHE   A 140 ? 0.23874 0.24291 0.16193 -0.03689 -0.04742 0.01299  140 PHE   A CB  
1083 C  CG  . PHE   A 140 ? 0.20894 0.21248 0.14652 -0.03182 -0.04519 0.01563  140 PHE   A CG  
1084 C  CD1 . PHE   A 140 ? 0.20334 0.21304 0.15588 -0.02893 -0.04741 0.02416  140 PHE   A CD1 
1085 C  CD2 . PHE   A 140 ? 0.23540 0.23169 0.17135 -0.02989 -0.04063 0.00940  140 PHE   A CD2 
1086 C  CE1 . PHE   A 140 ? 0.17903 0.18759 0.14361 -0.02455 -0.04522 0.02532  140 PHE   A CE1 
1087 C  CE2 . PHE   A 140 ? 0.20822 0.20522 0.15873 -0.02450 -0.03744 0.01124  140 PHE   A CE2 
1088 C  CZ  . PHE   A 140 ? 0.15868 0.16148 0.12214 -0.02238 -0.03995 0.01837  140 PHE   A CZ  
1089 N  N   . LEU   A 141 ? 0.26391 0.28621 0.18010 -0.04677 -0.06213 0.02359  141 LEU   A N   
1090 C  CA  . LEU   A 141 ? 0.31644 0.34266 0.21600 -0.05160 -0.06520 0.02371  141 LEU   A CA  
1091 C  C   . LEU   A 141 ? 0.32121 0.34997 0.21480 -0.04878 -0.06180 0.03027  141 LEU   A C   
1092 O  O   . LEU   A 141 ? 0.30156 0.32893 0.20530 -0.04368 -0.05775 0.03472  141 LEU   A O   
1093 C  CB  . LEU   A 141 ? 0.29421 0.33103 0.20054 -0.05605 -0.07435 0.03023  141 LEU   A CB  
1094 C  CG  . LEU   A 141 ? 0.34631 0.38257 0.26177 -0.05926 -0.07806 0.02586  141 LEU   A CG  
1095 C  CD1 . LEU   A 141 ? 0.34962 0.39883 0.27900 -0.06133 -0.08600 0.03627  141 LEU   A CD1 
1096 C  CD2 . LEU   A 141 ? 0.35366 0.38317 0.25157 -0.06580 -0.07882 0.01381  141 LEU   A CD2 
1097 N  N   . ASN   A 142 ? 0.34092 0.37341 0.21740 -0.05260 -0.06343 0.03080  142 ASN   A N   
1098 C  CA  . ASN   A 142 ? 0.34214 0.37820 0.21257 -0.05056 -0.06031 0.03846  142 ASN   A CA  
1099 C  C   . ASN   A 142 ? 0.33078 0.37331 0.22234 -0.04690 -0.06286 0.05203  142 ASN   A C   
1100 O  O   . ASN   A 142 ? 0.31290 0.36241 0.21771 -0.04795 -0.06966 0.05836  142 ASN   A O   
1101 C  CB  . ASN   A 142 ? 0.38043 0.42232 0.23091 -0.05584 -0.06373 0.03923  142 ASN   A CB  
1102 C  CG  . ASN   A 142 ? 0.45458 0.48824 0.28157 -0.05794 -0.05774 0.02577  142 ASN   A CG  
1103 O  OD1 . ASN   A 142 ? 0.48771 0.51299 0.31200 -0.05397 -0.04868 0.01967  142 ASN   A OD1 
1104 N  ND2 . ASN   A 142 ? 0.47582 0.51194 0.28598 -0.06427 -0.06255 0.02089  142 ASN   A ND2 
1105 N  N   . GLY   A 143 ? 0.25839 0.29831 0.15413 -0.04264 -0.05685 0.05642  143 GLY   A N   
1106 C  CA  . GLY   A 143 ? 0.28214 0.32552 0.19818 -0.03894 -0.05782 0.06822  143 GLY   A CA  
1107 C  C   . GLY   A 143 ? 0.24150 0.27932 0.17618 -0.03454 -0.05567 0.06623  143 GLY   A C   
1108 O  O   . GLY   A 143 ? 0.23183 0.27052 0.18436 -0.03105 -0.05556 0.07465  143 GLY   A O   
1109 N  N   . SER   A 144 ? 0.25859 0.29033 0.18988 -0.03458 -0.05381 0.05533  144 SER   A N   
1110 C  CA  . SER   A 144 ? 0.24320 0.27006 0.18977 -0.03062 -0.05170 0.05297  144 SER   A CA  
1111 C  C   . SER   A 144 ? 0.21077 0.23196 0.15721 -0.02787 -0.04515 0.05231  144 SER   A C   
1112 O  O   . SER   A 144 ? 0.17631 0.19385 0.13572 -0.02468 -0.04376 0.05165  144 SER   A O   
1113 C  CB  . SER   A 144 ? 0.21768 0.24096 0.16133 -0.03207 -0.05249 0.04274  144 SER   A CB  
1114 O  OG  . SER   A 144 ? 0.24354 0.26123 0.16854 -0.03424 -0.04856 0.03358  144 SER   A OG  
1115 N  N   . CYS   A 145 ? 0.21233 0.23338 0.14468 -0.02927 -0.04092 0.05272  145 CYS   A N   
1116 C  CA  . CYS   A 145 ? 0.25294 0.27039 0.18638 -0.02749 -0.03425 0.05321  145 CYS   A CA  
1117 C  C   . CYS   A 145 ? 0.18954 0.20591 0.14363 -0.02482 -0.03486 0.06138  145 CYS   A C   
1118 O  O   . CYS   A 145 ? 0.20775 0.22722 0.17149 -0.02425 -0.03818 0.06966  145 CYS   A O   
1119 C  CB  . CYS   A 145 ? 0.26831 0.28825 0.18729 -0.02916 -0.02908 0.05577  145 CYS   A CB  
1120 S  SG  . CYS   A 145 ? 0.44024 0.45824 0.33415 -0.03143 -0.02547 0.04388  145 CYS   A SG  
1121 N  N   . GLY   A 146 ? 0.18218 0.19359 0.14409 -0.02308 -0.03132 0.05816  146 GLY   A N   
1122 C  CA  . GLY   A 146 ? 0.12906 0.13633 0.11136 -0.02055 -0.03025 0.06142  146 GLY   A CA  
1123 C  C   . GLY   A 146 ? 0.15289 0.15738 0.14825 -0.01740 -0.03289 0.05701  146 GLY   A C   
1124 O  O   . GLY   A 146 ? 0.15958 0.15882 0.17079 -0.01517 -0.03071 0.05687  146 GLY   A O   
1125 N  N   . SER   A 147 ? 0.13206 0.13978 0.12163 -0.01762 -0.03714 0.05352  147 SER   A N   
1126 C  CA  . SER   A 147 ? 0.15236 0.15873 0.15388 -0.01462 -0.03793 0.04866  147 SER   A CA  
1127 C  C   . SER   A 147 ? 0.11940 0.12101 0.12242 -0.01312 -0.03218 0.03839  147 SER   A C   
1128 O  O   . SER   A 147 ? 0.10401 0.10527 0.09680 -0.01448 -0.02907 0.03379  147 SER   A O   
1129 C  CB  . SER   A 147 ? 0.14512 0.15644 0.14018 -0.01646 -0.04315 0.04664  147 SER   A CB  
1130 O  OG  . SER   A 147 ? 0.14928 0.16679 0.14156 -0.01889 -0.04736 0.05294  147 SER   A OG  
1131 N  N   . VAL   A 148 ? 0.11604 0.11501 0.13186 -0.01013 -0.03054 0.03500  148 VAL   A N   
1132 C  CA  . VAL   A 148 ? 0.10502 0.10102 0.12162 -0.00951 -0.02607 0.02627  148 VAL   A CA  
1133 C  C   . VAL   A 148 ? 0.10279 0.10068 0.11962 -0.00773 -0.02578 0.02026  148 VAL   A C   
1134 O  O   . VAL   A 148 ? 0.10239 0.10302 0.12388 -0.00649 -0.02818 0.02273  148 VAL   A O   
1135 C  CB  . VAL   A 148 ? 0.10637 0.09641 0.13480 -0.00897 -0.02297 0.02552  148 VAL   A CB  
1136 C  CG1 . VAL   A 148 ? 0.11410 0.10210 0.14379 -0.01154 -0.02265 0.03309  148 VAL   A CG1 
1137 C  CG2 . VAL   A 148 ? 0.08500 0.07203 0.12646 -0.00543 -0.02244 0.02640  148 VAL   A CG2 
1138 N  N   . GLY   A 149 ? 0.08282 0.08099 0.09491 -0.00797 -0.02308 0.01368  149 GLY   A N   
1139 C  CA  . GLY   A 149 ? 0.07904 0.07926 0.09141 -0.00640 -0.02175 0.00867  149 GLY   A CA  
1140 C  C   . GLY   A 149 ? 0.09374 0.09253 0.11035 -0.00596 -0.01862 0.00314  149 GLY   A C   
1141 O  O   . GLY   A 149 ? 0.07427 0.07112 0.09142 -0.00800 -0.01792 0.00173  149 GLY   A O   
1142 N  N   . PHE   A 150 ? 0.08649 0.08682 0.10543 -0.00404 -0.01655 -0.00040 150 PHE   A N   
1143 C  CA  . PHE   A 150 ? 0.09979 0.09768 0.12118 -0.00399 -0.01307 -0.00711 150 PHE   A CA  
1144 C  C   . PHE   A 150 ? 0.12015 0.12274 0.13871 -0.00224 -0.01019 -0.01082 150 PHE   A C   
1145 O  O   . PHE   A 150 ? 0.09738 0.10394 0.11719 -0.00050 -0.01044 -0.00694 150 PHE   A O   
1146 C  CB  . PHE   A 150 ? 0.11166 0.10211 0.14443 -0.00233 -0.01096 -0.00660 150 PHE   A CB  
1147 C  CG  . PHE   A 150 ? 0.13306 0.12521 0.17475 0.00174  -0.01019 -0.00192 150 PHE   A CG  
1148 C  CD1 . PHE   A 150 ? 0.11700 0.11178 0.16204 0.00192  -0.01480 0.00727  150 PHE   A CD1 
1149 C  CD2 . PHE   A 150 ? 0.13933 0.13227 0.18585 0.00504  -0.00491 -0.00634 150 PHE   A CD2 
1150 C  CE1 . PHE   A 150 ? 0.12092 0.12023 0.17599 0.00486  -0.01551 0.01279  150 PHE   A CE1 
1151 C  CE2 . PHE   A 150 ? 0.13395 0.13111 0.19195 0.00901  -0.00397 -0.00067 150 PHE   A CE2 
1152 C  CZ  . PHE   A 150 ? 0.15037 0.15131 0.21381 0.00872  -0.00998 0.00938  150 PHE   A CZ  
1153 N  N   . ASN   A 151 ? 0.15182 0.15419 0.16634 -0.00350 -0.00740 -0.01838 151 ASN   A N   
1154 C  CA  . ASN   A 151 ? 0.16986 0.17638 0.18051 -0.00197 -0.00305 -0.02282 151 ASN   A CA  
1155 C  C   . ASN   A 151 ? 0.14912 0.14821 0.16320 -0.00142 0.00233  -0.03135 151 ASN   A C   
1156 O  O   . ASN   A 151 ? 0.14764 0.13846 0.16572 -0.00350 0.00171  -0.03433 151 ASN   A O   
1157 C  CB  . ASN   A 151 ? 0.17933 0.19415 0.17766 -0.00465 -0.00468 -0.02448 151 ASN   A CB  
1158 C  CG  . ASN   A 151 ? 0.17099 0.19151 0.16772 -0.00386 -0.00782 -0.01630 151 ASN   A CG  
1159 O  OD1 . ASN   A 151 ? 0.15600 0.17750 0.15117 -0.00536 -0.01157 -0.01340 151 ASN   A OD1 
1160 N  ND2 . ASN   A 151 ? 0.15089 0.17479 0.14929 -0.00151 -0.00552 -0.01257 151 ASN   A ND2 
1161 N  N   . ILE   A 152 ? 0.16315 0.16444 0.17637 0.00141  0.00861  -0.03538 152 ILE   A N   
1162 C  CA  . ILE   A 152 ? 0.21165 0.20449 0.22750 0.00273  0.01589  -0.04531 152 ILE   A CA  
1163 C  C   . ILE   A 152 ? 0.29818 0.29655 0.29811 0.00051  0.01995  -0.05437 152 ILE   A C   
1164 O  O   . ILE   A 152 ? 0.25856 0.26765 0.25285 0.00194  0.02130  -0.05030 152 ILE   A O   
1165 C  CB  . ILE   A 152 ? 0.23970 0.22944 0.27231 0.00966  0.02211  -0.04187 152 ILE   A CB  
1166 C  CG1 . ILE   A 152 ? 0.22130 0.21040 0.26725 0.01120  0.01607  -0.02998 152 ILE   A CG1 
1167 C  CG2 . ILE   A 152 ? 0.27032 0.24702 0.30875 0.01166  0.03028  -0.05234 152 ILE   A CG2 
1168 C  CD1 . ILE   A 152 ? 0.23416 0.21237 0.28510 0.00914  0.01337  -0.03021 152 ILE   A CD1 
1169 N  N   . ASP   A 153 ? 0.32143 0.31264 0.31368 -0.00384 0.02151  -0.06632 153 ASP   A N   
1170 C  CA  . ASP   A 153 ? 0.40007 0.39604 0.37365 -0.00792 0.02436  -0.07706 153 ASP   A CA  
1171 C  C   . ASP   A 153 ? 0.45552 0.43751 0.43074 -0.00675 0.03411  -0.09109 153 ASP   A C   
1172 O  O   . ASP   A 153 ? 0.41816 0.38685 0.39882 -0.00993 0.03295  -0.09696 153 ASP   A O   
1173 C  CB  . ASP   A 153 ? 0.42681 0.42791 0.38850 -0.01641 0.01523  -0.07928 153 ASP   A CB  
1174 C  CG  . ASP   A 153 ? 0.53423 0.55082 0.47678 -0.01972 0.01327  -0.07972 153 ASP   A CG  
1175 O  OD1 . ASP   A 153 ? 0.54254 0.56416 0.47865 -0.01605 0.02041  -0.08044 153 ASP   A OD1 
1176 O  OD2 . ASP   A 153 ? 0.56039 0.58439 0.49683 -0.02527 0.00455  -0.07630 153 ASP   A OD2 
1177 N  N   . TYR   A 154 ? 0.49002 0.47475 0.46148 -0.00207 0.04411  -0.09527 154 TYR   A N   
1178 C  CA  . TYR   A 154 ? 0.55474 0.52638 0.53426 0.00287  0.05374  -0.10149 154 TYR   A CA  
1179 C  C   . TYR   A 154 ? 0.54155 0.49989 0.54532 0.00706  0.05416  -0.09733 154 TYR   A C   
1180 O  O   . TYR   A 154 ? 0.55576 0.51812 0.57685 0.01343  0.05510  -0.08689 154 TYR   A O   
1181 C  CB  . TYR   A 154 ? 0.58974 0.55403 0.55267 -0.00294 0.05383  -0.11314 154 TYR   A CB  
1182 C  CG  . TYR   A 154 ? 0.68467 0.63821 0.65214 0.00309  0.06554  -0.12038 154 TYR   A CG  
1183 C  CD1 . TYR   A 154 ? 0.69773 0.65754 0.67333 0.01191  0.07506  -0.11592 154 TYR   A CD1 
1184 C  CD2 . TYR   A 154 ? 0.69815 0.63614 0.66299 0.00008  0.06737  -0.13122 154 TYR   A CD2 
1185 C  CE1 . TYR   A 154 ? 0.74623 0.69771 0.72747 0.01821  0.08613  -0.12175 154 TYR   A CE1 
1186 C  CE2 . TYR   A 154 ? 0.75250 0.68030 0.72181 0.00618  0.07878  -0.13828 154 TYR   A CE2 
1187 C  CZ  . TYR   A 154 ? 0.79233 0.72728 0.76990 0.01556  0.08821  -0.13339 154 TYR   A CZ  
1188 O  OH  . TYR   A 154 ? 0.78358 0.70965 0.76696 0.02223  0.09993  -0.13987 154 TYR   A OH  
1189 N  N   . ASP   A 155 ? 0.49860 0.44258 0.50447 0.00319  0.05210  -0.10267 155 ASP   A N   
1190 C  CA  . ASP   A 155 ? 0.47746 0.40864 0.50594 0.00703  0.05262  -0.09682 155 ASP   A CA  
1191 C  C   . ASP   A 155 ? 0.40162 0.33032 0.43420 0.00116  0.04252  -0.09143 155 ASP   A C   
1192 O  O   . ASP   A 155 ? 0.34383 0.26203 0.39317 0.00302  0.04199  -0.08540 155 ASP   A O   
1193 C  CB  . ASP   A 155 ? 0.52973 0.44527 0.56128 0.00791  0.05937  -0.10520 155 ASP   A CB  
1194 C  CG  . ASP   A 155 ? 0.57510 0.48553 0.58797 -0.00184 0.05552  -0.11701 155 ASP   A CG  
1195 O  OD1 . ASP   A 155 ? 0.57741 0.49964 0.57334 -0.00848 0.04832  -0.11820 155 ASP   A OD1 
1196 O  OD2 . ASP   A 155 ? 0.62719 0.52253 0.64340 -0.00288 0.05926  -0.12423 155 ASP   A OD2 
1197 N  N   . CYS   A 156 ? 0.35051 0.28984 0.36856 -0.00578 0.03452  -0.09203 156 CYS   A N   
1198 C  CA  . CYS   A 156 ? 0.29544 0.23402 0.31560 -0.01240 0.02519  -0.08766 156 CYS   A CA  
1199 C  C   . CYS   A 156 ? 0.25097 0.20330 0.27407 -0.00969 0.01804  -0.07130 156 CYS   A C   
1200 O  O   . CYS   A 156 ? 0.19552 0.16155 0.20881 -0.00844 0.01645  -0.06789 156 CYS   A O   
1201 C  CB  . CYS   A 156 ? 0.29475 0.23967 0.29676 -0.02189 0.01900  -0.09409 156 CYS   A CB  
1202 S  SG  . CYS   A 156 ? 0.24183 0.19232 0.24753 -0.02946 0.00773  -0.08616 156 CYS   A SG  
1203 N  N   . VAL   A 157 ? 0.20194 0.14989 0.23810 -0.00900 0.01429  -0.06125 157 VAL   A N   
1204 C  CA  . VAL   A 157 ? 0.17593 0.13485 0.21340 -0.00717 0.00799  -0.04735 157 VAL   A CA  
1205 C  C   . VAL   A 157 ? 0.18171 0.14755 0.21042 -0.01398 0.00091  -0.04598 157 VAL   A C   
1206 O  O   . VAL   A 157 ? 0.14072 0.10005 0.17418 -0.01879 -0.00089 -0.04683 157 VAL   A O   
1207 C  CB  . VAL   A 157 ? 0.15642 0.10927 0.21041 -0.00306 0.00758  -0.03629 157 VAL   A CB  
1208 C  CG1 . VAL   A 157 ? 0.14591 0.11039 0.19695 -0.00228 0.00114  -0.02422 157 VAL   A CG1 
1209 C  CG2 . VAL   A 157 ? 0.18842 0.13500 0.25578 0.00438  0.01496  -0.03657 157 VAL   A CG2 
1210 N  N   . SER   A 158 ? 0.16232 0.14150 0.18078 -0.01407 -0.00271 -0.04247 158 SER   A N   
1211 C  CA  . SER   A 158 ? 0.18414 0.17171 0.19742 -0.01876 -0.00873 -0.03901 158 SER   A CA  
1212 C  C   . SER   A 158 ? 0.14097 0.13103 0.15885 -0.01566 -0.01112 -0.02746 158 SER   A C   
1213 O  O   . SER   A 158 ? 0.14670 0.14259 0.16120 -0.01200 -0.01154 -0.02277 158 SER   A O   
1214 C  CB  . SER   A 158 ? 0.16186 0.16200 0.16249 -0.02032 -0.01085 -0.04133 158 SER   A CB  
1215 O  OG  . SER   A 158 ? 0.19780 0.19730 0.19100 -0.02548 -0.01015 -0.05258 158 SER   A OG  
1216 N  N   . PHE   A 159 ? 0.11292 0.09809 0.13804 -0.01766 -0.01235 -0.02300 159 PHE   A N   
1217 C  CA  . PHE   A 159 ? 0.14136 0.12972 0.16723 -0.01575 -0.01438 -0.01299 159 PHE   A CA  
1218 C  C   . PHE   A 159 ? 0.11496 0.11357 0.13394 -0.01746 -0.01680 -0.01121 159 PHE   A C   
1219 O  O   . PHE   A 159 ? 0.12889 0.13135 0.14857 -0.02189 -0.01807 -0.01380 159 PHE   A O   
1220 C  CB  . PHE   A 159 ? 0.10619 0.08748 0.14093 -0.01742 -0.01419 -0.00748 159 PHE   A CB  
1221 C  CG  . PHE   A 159 ? 0.10785 0.07914 0.15262 -0.01430 -0.01171 -0.00610 159 PHE   A CG  
1222 C  CD1 . PHE   A 159 ? 0.11164 0.08444 0.15882 -0.00947 -0.01246 0.00128  159 PHE   A CD1 
1223 C  CD2 . PHE   A 159 ? 0.15255 0.11300 0.20559 -0.01639 -0.00863 -0.01230 159 PHE   A CD2 
1224 C  CE1 . PHE   A 159 ? 0.13202 0.09778 0.19161 -0.00572 -0.01028 0.00445  159 PHE   A CE1 
1225 C  CE2 . PHE   A 159 ? 0.15106 0.10134 0.21606 -0.01227 -0.00511 -0.01059 159 PHE   A CE2 
1226 C  CZ  . PHE   A 159 ? 0.16627 0.12020 0.23565 -0.00629 -0.00593 -0.00121 159 PHE   A CZ  
1227 N  N   . CYS   A 160 ? 0.12635 0.12927 0.14040 -0.01418 -0.01736 -0.00659 160 CYS   A N   
1228 C  CA  . CYS   A 160 ? 0.14394 0.15503 0.15352 -0.01415 -0.01820 -0.00441 160 CYS   A CA  
1229 C  C   . CYS   A 160 ? 0.12388 0.13456 0.13104 -0.01246 -0.01748 0.00143  160 CYS   A C   
1230 O  O   . CYS   A 160 ? 0.10673 0.12292 0.11211 -0.01175 -0.01655 0.00318  160 CYS   A O   
1231 C  CB  . CYS   A 160 ? 0.08483 0.10120 0.08907 -0.01185 -0.01843 -0.00607 160 CYS   A CB  
1232 S  SG  . CYS   A 160 ? 0.11485 0.12681 0.11730 -0.00811 -0.01750 -0.00437 160 CYS   A SG  
1233 N  N   . TYR   A 161 ? 0.07231 0.07734 0.07941 -0.01190 -0.01766 0.00467  161 TYR   A N   
1234 C  CA  . TYR   A 161 ? 0.10314 0.10823 0.10376 -0.01114 -0.01717 0.00870  161 TYR   A CA  
1235 C  C   . TYR   A 161 ? 0.10586 0.10741 0.10715 -0.01244 -0.01811 0.01404  161 TYR   A C   
1236 O  O   . TYR   A 161 ? 0.08988 0.08800 0.09696 -0.01202 -0.01990 0.01546  161 TYR   A O   
1237 C  CB  . TYR   A 161 ? 0.08897 0.09325 0.08393 -0.00907 -0.01807 0.00744  161 TYR   A CB  
1238 C  CG  . TYR   A 161 ? 0.13040 0.13277 0.11624 -0.00936 -0.01766 0.00911  161 TYR   A CG  
1239 C  CD1 . TYR   A 161 ? 0.14293 0.14625 0.12423 -0.00821 -0.01394 0.00795  161 TYR   A CD1 
1240 C  CD2 . TYR   A 161 ? 0.07911 0.07922 0.06099 -0.01084 -0.02087 0.01146  161 TYR   A CD2 
1241 C  CE1 . TYR   A 161 ? 0.10889 0.10876 0.08011 -0.00861 -0.01222 0.00728  161 TYR   A CE1 
1242 C  CE2 . TYR   A 161 ? 0.09363 0.09189 0.06408 -0.01249 -0.02086 0.01133  161 TYR   A CE2 
1243 C  CZ  . TYR   A 161 ? 0.14384 0.14082 0.10805 -0.01132 -0.01586 0.00818  161 TYR   A CZ  
1244 O  OH  . TYR   A 161 ? 0.13439 0.12763 0.08548 -0.01292 -0.01429 0.00577  161 TYR   A OH  
1245 N  N   . MET   A 162 ? 0.09455 0.09767 0.09021 -0.01356 -0.01641 0.01782  162 MET   A N   
1246 C  CA  . MET   A 162 ? 0.10522 0.10683 0.09762 -0.01491 -0.01789 0.02451  162 MET   A CA  
1247 C  C   . MET   A 162 ? 0.10619 0.10926 0.08402 -0.01518 -0.01702 0.02437  162 MET   A C   
1248 O  O   . MET   A 162 ? 0.09278 0.09774 0.06604 -0.01447 -0.01245 0.02165  162 MET   A O   
1249 C  CB  . MET   A 162 ? 0.12450 0.12609 0.12368 -0.01728 -0.01593 0.03023  162 MET   A CB  
1250 C  CG  . MET   A 162 ? 0.12055 0.12188 0.11631 -0.01865 -0.01751 0.03979  162 MET   A CG  
1251 S  SD  . MET   A 162 ? 0.19415 0.19402 0.20092 -0.02172 -0.01499 0.04918  162 MET   A SD  
1252 C  CE  . MET   A 162 ? 0.20736 0.19806 0.23234 -0.02055 -0.01736 0.04909  162 MET   A CE  
1253 N  N   . HIS   A 163 ? 0.11287 0.11534 0.08404 -0.01635 -0.02127 0.02705  163 HIS   A N   
1254 C  CA  . HIS   A 163 ? 0.12636 0.12867 0.08141 -0.01794 -0.02111 0.02450  163 HIS   A CA  
1255 C  C   . HIS   A 163 ? 0.14680 0.15159 0.09030 -0.02003 -0.01777 0.02875  163 HIS   A C   
1256 O  O   . HIS   A 163 ? 0.15776 0.16535 0.10322 -0.02167 -0.01969 0.03745  163 HIS   A O   
1257 C  CB  . HIS   A 163 ? 0.15303 0.15575 0.10470 -0.02010 -0.02819 0.02573  163 HIS   A CB  
1258 C  CG  . HIS   A 163 ? 0.17008 0.17088 0.10445 -0.02318 -0.02855 0.02050  163 HIS   A CG  
1259 N  ND1 . HIS   A 163 ? 0.17702 0.17244 0.10659 -0.02169 -0.02317 0.01192  163 HIS   A ND1 
1260 C  CD2 . HIS   A 163 ? 0.19856 0.20146 0.11944 -0.02785 -0.03325 0.02202  163 HIS   A CD2 
1261 C  CE1 . HIS   A 163 ? 0.18755 0.17955 0.10102 -0.02539 -0.02376 0.00708  163 HIS   A CE1 
1262 N  NE2 . HIS   A 163 ? 0.20924 0.20631 0.11649 -0.02962 -0.03022 0.01248  163 HIS   A NE2 
1263 N  N   . HIS   A 164 ? 0.17292 0.17643 0.10421 -0.01973 -0.01210 0.02300  164 HIS   A N   
1264 C  CA  . HIS   A 164 ? 0.19376 0.20031 0.11213 -0.02139 -0.00688 0.02606  164 HIS   A CA  
1265 C  C   . HIS   A 164 ? 0.23309 0.23703 0.12910 -0.02432 -0.00660 0.02066  164 HIS   A C   
1266 O  O   . HIS   A 164 ? 0.25119 0.25906 0.13372 -0.02778 -0.00751 0.02565  164 HIS   A O   
1267 C  CB  . HIS   A 164 ? 0.16238 0.17132 0.08688 -0.01818 0.00262  0.02460  164 HIS   A CB  
1268 C  CG  . HIS   A 164 ? 0.17681 0.19022 0.11937 -0.01808 0.00261  0.03136  164 HIS   A CG  
1269 N  ND1 . HIS   A 164 ? 0.16929 0.18830 0.11377 -0.01971 0.00743  0.03883  164 HIS   A ND1 
1270 C  CD2 . HIS   A 164 ? 0.12940 0.14202 0.08851 -0.01726 -0.00113 0.03090  164 HIS   A CD2 
1271 C  CE1 . HIS   A 164 ? 0.13325 0.15371 0.09585 -0.02056 0.00579  0.04271  164 HIS   A CE1 
1272 N  NE2 . HIS   A 164 ? 0.15200 0.16837 0.12259 -0.01909 0.00067  0.03718  164 HIS   A NE2 
1273 N  N   . MET   A 165 ? 0.22669 0.22366 0.11816 -0.02335 -0.00515 0.01048  165 MET   A N   
1274 C  CA  . MET   A 165 ? 0.28466 0.27680 0.15352 -0.02657 -0.00244 0.00278  165 MET   A CA  
1275 C  C   . MET   A 165 ? 0.22261 0.20528 0.09037 -0.02736 -0.00484 -0.00708 165 MET   A C   
1276 O  O   . MET   A 165 ? 0.20899 0.18926 0.09338 -0.02378 -0.00553 -0.00790 165 MET   A O   
1277 C  CB  . MET   A 165 ? 0.27810 0.26945 0.13949 -0.02325 0.01041  -0.00092 165 MET   A CB  
1278 C  CG  . MET   A 165 ? 0.29743 0.29210 0.18020 -0.01685 0.01654  0.00199  165 MET   A CG  
1279 S  SD  . MET   A 165 ? 0.37142 0.36544 0.24890 -0.01178 0.03247  -0.00330 165 MET   A SD  
1280 C  CE  . MET   A 165 ? 0.34627 0.32570 0.22137 -0.00898 0.03482  -0.01629 165 MET   A CE  
1281 N  N   . GLU   A 166 ? 0.26640 0.24497 0.12021 -0.03077 -0.00562 -0.01410 166 GLU   A N   
1282 C  CA  . GLU   A 166 ? 0.24506 0.21292 0.09746 -0.03231 -0.00616 -0.02429 166 GLU   A CA  
1283 C  C   . GLU   A 166 ? 0.29589 0.25387 0.13753 -0.02947 0.00576  -0.03467 166 GLU   A C   
1284 O  O   . GLU   A 166 ? 0.31643 0.27779 0.14636 -0.02896 0.01106  -0.03539 166 GLU   A O   
1285 C  CB  . GLU   A 166 ? 0.27070 0.24123 0.11994 -0.03853 -0.01620 -0.02487 166 GLU   A CB  
1286 C  CG  . GLU   A 166 ? 0.35384 0.31300 0.20215 -0.04144 -0.01664 -0.03529 166 GLU   A CG  
1287 C  CD  . GLU   A 166 ? 0.35601 0.32020 0.20577 -0.04811 -0.02752 -0.03401 166 GLU   A CD  
1288 O  OE1 . GLU   A 166 ? 0.34647 0.32077 0.20890 -0.04857 -0.03510 -0.02434 166 GLU   A OE1 
1289 O  OE2 . GLU   A 166 ? 0.36231 0.32064 0.20088 -0.05268 -0.02794 -0.04265 166 GLU   A OE2 
1290 N  N   . LEU   A 167 ? 0.28748 0.23324 0.13498 -0.02670 0.01081  -0.04191 167 LEU   A N   
1291 C  CA  . LEU   A 167 ? 0.30688 0.24121 0.15027 -0.02233 0.02295  -0.05166 167 LEU   A CA  
1292 C  C   . LEU   A 167 ? 0.34762 0.27216 0.18279 -0.02757 0.01986  -0.06153 167 LEU   A C   
1293 O  O   . LEU   A 167 ? 0.33997 0.26637 0.17647 -0.03404 0.00868  -0.06030 167 LEU   A O   
1294 C  CB  . LEU   A 167 ? 0.29256 0.22017 0.15288 -0.01478 0.02999  -0.05118 167 LEU   A CB  
1295 C  CG  . LEU   A 167 ? 0.28242 0.22410 0.16017 -0.00745 0.03344  -0.04028 167 LEU   A CG  
1296 C  CD1 . LEU   A 167 ? 0.23736 0.17858 0.13831 -0.00085 0.03438  -0.03629 167 LEU   A CD1 
1297 C  CD2 . LEU   A 167 ? 0.31445 0.25776 0.18524 -0.00301 0.04637  -0.04239 167 LEU   A CD2 
1298 N  N   . PRO   A 168 ? 0.36689 0.28144 0.19495 -0.02487 0.02983  -0.07124 168 PRO   A N   
1299 C  CA  . PRO   A 168 ? 0.38469 0.29066 0.20095 -0.03110 0.02662  -0.08139 168 PRO   A CA  
1300 C  C   . PRO   A 168 ? 0.38404 0.27952 0.21033 -0.03502 0.02064  -0.08487 168 PRO   A C   
1301 O  O   . PRO   A 168 ? 0.42259 0.31370 0.24048 -0.04218 0.01483  -0.09162 168 PRO   A O   
1302 C  CB  . PRO   A 168 ? 0.37917 0.27549 0.18887 -0.02541 0.04073  -0.09075 168 PRO   A CB  
1303 C  CG  . PRO   A 168 ? 0.41530 0.32197 0.22964 -0.01766 0.04956  -0.08323 168 PRO   A CG  
1304 C  CD  . PRO   A 168 ? 0.37032 0.28278 0.20114 -0.01602 0.04451  -0.07293 168 PRO   A CD  
1305 N  N   . THR   A 169 ? 0.33508 0.22619 0.17889 -0.03065 0.02236  -0.08060 169 THR   A N   
1306 C  CA  . THR   A 169 ? 0.33578 0.21879 0.19054 -0.03471 0.01627  -0.08173 169 THR   A CA  
1307 C  C   . THR   A 169 ? 0.32989 0.22589 0.18916 -0.04118 0.00256  -0.07341 169 THR   A C   
1308 O  O   . THR   A 169 ? 0.32949 0.22197 0.19987 -0.04479 -0.00292 -0.07244 169 THR   A O   
1309 C  CB  . THR   A 169 ? 0.35791 0.23082 0.23044 -0.02674 0.02431  -0.07941 169 THR   A CB  
1310 O  OG1 . THR   A 169 ? 0.34678 0.22952 0.22546 -0.02077 0.02631  -0.07033 169 THR   A OG1 
1311 C  CG2 . THR   A 169 ? 0.35910 0.21834 0.23244 -0.02013 0.03732  -0.08710 169 THR   A CG2 
1312 N  N   . GLY   A 170 ? 0.31393 0.22539 0.16709 -0.04226 -0.00259 -0.06640 170 GLY   A N   
1313 C  CA  . GLY   A 170 ? 0.31817 0.24303 0.17919 -0.04646 -0.01441 -0.05705 170 GLY   A CA  
1314 C  C   . GLY   A 170 ? 0.30609 0.23578 0.18141 -0.04202 -0.01528 -0.04819 170 GLY   A C   
1315 O  O   . GLY   A 170 ? 0.30907 0.24972 0.19403 -0.04443 -0.02422 -0.04024 170 GLY   A O   
1316 N  N   . VAL   A 171 ? 0.27537 0.19749 0.15332 -0.03512 -0.00593 -0.04921 171 VAL   A N   
1317 C  CA  . VAL   A 171 ? 0.24357 0.17642 0.14079 -0.02841 -0.00663 -0.03852 171 VAL   A CA  
1318 C  C   . VAL   A 171 ? 0.23297 0.17767 0.12753 -0.02516 -0.00531 -0.03245 171 VAL   A C   
1319 O  O   . VAL   A 171 ? 0.23085 0.17539 0.10876 -0.02740 -0.00274 -0.03568 171 VAL   A O   
1320 C  CB  . VAL   A 171 ? 0.25062 0.17684 0.16253 -0.02059 0.00144  -0.03804 171 VAL   A CB  
1321 C  CG1 . VAL   A 171 ? 0.27525 0.18822 0.19153 -0.02416 0.00064  -0.04273 171 VAL   A CG1 
1322 C  CG2 . VAL   A 171 ? 0.25916 0.18037 0.16673 -0.01406 0.01319  -0.04189 171 VAL   A CG2 
1323 N  N   . HIS   A 172 ? 0.22221 0.17693 0.13258 -0.02043 -0.00663 -0.02381 172 HIS   A N   
1324 C  CA  . HIS   A 172 ? 0.18171 0.14767 0.09252 -0.01974 -0.00841 -0.01680 172 HIS   A CA  
1325 C  C   . HIS   A 172 ? 0.20220 0.17314 0.12488 -0.01287 -0.00202 -0.01295 172 HIS   A C   
1326 O  O   . HIS   A 172 ? 0.16610 0.13581 0.10041 -0.00859 0.00050  -0.01282 172 HIS   A O   
1327 C  CB  . HIS   A 172 ? 0.20252 0.17629 0.12111 -0.02286 -0.01823 -0.01027 172 HIS   A CB  
1328 C  CG  . HIS   A 172 ? 0.20885 0.18142 0.11771 -0.03032 -0.02581 -0.01232 172 HIS   A CG  
1329 N  ND1 . HIS   A 172 ? 0.19808 0.16880 0.11417 -0.03339 -0.03090 -0.01353 172 HIS   A ND1 
1330 C  CD2 . HIS   A 172 ? 0.24047 0.21495 0.13448 -0.03533 -0.02867 -0.01314 172 HIS   A CD2 
1331 C  CE1 . HIS   A 172 ? 0.25013 0.22298 0.15955 -0.03950 -0.03661 -0.01459 172 HIS   A CE1 
1332 N  NE2 . HIS   A 172 ? 0.23341 0.20907 0.13060 -0.03998 -0.03510 -0.01430 172 HIS   A NE2 
1333 N  N   . ALA   A 173 ? 0.17411 0.15144 0.09348 -0.01243 0.00059  -0.00924 173 ALA   A N   
1334 C  CA  . ALA   A 173 ? 0.15206 0.13608 0.08304 -0.00752 0.00606  -0.00523 173 ALA   A CA  
1335 C  C   . ALA   A 173 ? 0.14525 0.13784 0.08089 -0.00960 0.00228  0.00218  173 ALA   A C   
1336 O  O   . ALA   A 173 ? 0.15797 0.15144 0.08412 -0.01361 -0.00107 0.00483  173 ALA   A O   
1337 C  CB  . ALA   A 173 ? 0.20010 0.18231 0.12490 -0.00427 0.01662  -0.00847 173 ALA   A CB  
1338 N  N   . GLY   A 174 ? 0.11405 0.11291 0.06460 -0.00723 0.00274  0.00581  174 GLY   A N   
1339 C  CA  . GLY   A 174 ? 0.12352 0.12795 0.08188 -0.00942 -0.00064 0.01173  174 GLY   A CA  
1340 C  C   . GLY   A 174 ? 0.11046 0.12187 0.08305 -0.00770 0.00164  0.01362  174 GLY   A C   
1341 O  O   . GLY   A 174 ? 0.09129 0.10555 0.06811 -0.00419 0.00601  0.01205  174 GLY   A O   
1342 N  N   . THR   A 175 ? 0.09249 0.10671 0.07363 -0.01044 -0.00164 0.01726  175 THR   A N   
1343 C  CA  . THR   A 175 ? 0.08144 0.10289 0.07575 -0.01121 -0.00091 0.01882  175 THR   A CA  
1344 C  C   . THR   A 175 ? 0.07528 0.09528 0.07664 -0.01274 -0.00661 0.01622  175 THR   A C   
1345 O  O   . THR   A 175 ? 0.08330 0.09701 0.08143 -0.01283 -0.01003 0.01480  175 THR   A O   
1346 C  CB  . THR   A 175 ? 0.09870 0.12380 0.09717 -0.01462 0.00172  0.02489  175 THR   A CB  
1347 O  OG1 . THR   A 175 ? 0.08919 0.10825 0.08737 -0.01763 -0.00228 0.02787  175 THR   A OG1 
1348 C  CG2 . THR   A 175 ? 0.09762 0.12507 0.08691 -0.01312 0.00885  0.02736  175 THR   A CG2 
1349 N  N   . ASP   A 176 ? 0.08372 0.11057 0.09491 -0.01430 -0.00743 0.01561  176 ASP   A N   
1350 C  CA  . ASP   A 176 ? 0.08230 0.10700 0.09904 -0.01765 -0.01177 0.01245  176 ASP   A CA  
1351 C  C   . ASP   A 176 ? 0.08720 0.10691 0.10901 -0.02167 -0.01159 0.01561  176 ASP   A C   
1352 O  O   . ASP   A 176 ? 0.10454 0.12446 0.12478 -0.02196 -0.00858 0.02140  176 ASP   A O   
1353 C  CB  . ASP   A 176 ? 0.11933 0.15364 0.14283 -0.01953 -0.01389 0.01019  176 ASP   A CB  
1354 C  CG  . ASP   A 176 ? 0.10662 0.15102 0.13991 -0.02246 -0.01226 0.01446  176 ASP   A CG  
1355 O  OD1 . ASP   A 176 ? 0.07711 0.11957 0.11403 -0.02509 -0.00973 0.01834  176 ASP   A OD1 
1356 O  OD2 . ASP   A 176 ? 0.09756 0.15383 0.13664 -0.02240 -0.01368 0.01523  176 ASP   A OD2 
1357 N  N   . LEU   A 177 ? 0.10012 0.11470 0.12791 -0.02483 -0.01417 0.01197  177 LEU   A N   
1358 C  CA  . LEU   A 177 ? 0.12475 0.13181 0.15968 -0.02819 -0.01362 0.01549  177 LEU   A CA  
1359 C  C   . LEU   A 177 ? 0.16107 0.17291 0.20619 -0.03413 -0.01259 0.01818  177 LEU   A C   
1360 O  O   . LEU   A 177 ? 0.18293 0.18772 0.23629 -0.03787 -0.01183 0.02172  177 LEU   A O   
1361 C  CB  . LEU   A 177 ? 0.10788 0.10466 0.14646 -0.02842 -0.01521 0.00982  177 LEU   A CB  
1362 C  CG  . LEU   A 177 ? 0.13533 0.12523 0.17116 -0.02352 -0.01537 0.01213  177 LEU   A CG  
1363 C  CD1 . LEU   A 177 ? 0.11590 0.10172 0.15531 -0.02347 -0.01470 0.02232  177 LEU   A CD1 
1364 C  CD2 . LEU   A 177 ? 0.10551 0.10123 0.13040 -0.01927 -0.01626 0.01158  177 LEU   A CD2 
1365 N  N   . GLU   A 178 ? 0.11593 0.14002 0.16312 -0.03527 -0.01252 0.01770  178 GLU   A N   
1366 C  CA  . GLU   A 178 ? 0.14123 0.17305 0.19947 -0.04047 -0.01064 0.02312  178 GLU   A CA  
1367 C  C   . GLU   A 178 ? 0.10538 0.14381 0.16000 -0.03680 -0.00480 0.03130  178 GLU   A C   
1368 O  O   . GLU   A 178 ? 0.13900 0.18681 0.20308 -0.03999 -0.00161 0.03698  178 GLU   A O   
1369 C  CB  . GLU   A 178 ? 0.11715 0.16122 0.18353 -0.04492 -0.01422 0.01929  178 GLU   A CB  
1370 C  CG  . GLU   A 178 ? 0.10841 0.14720 0.17258 -0.04827 -0.01978 0.00907  178 GLU   A CG  
1371 C  CD  . GLU   A 178 ? 0.23054 0.25968 0.30373 -0.05686 -0.02143 0.00507  178 GLU   A CD  
1372 O  OE1 . GLU   A 178 ? 0.28041 0.30575 0.35164 -0.06119 -0.02534 -0.00493 178 GLU   A OE1 
1373 O  OE2 . GLU   A 178 ? 0.20724 0.23269 0.28927 -0.05976 -0.01849 0.01172  178 GLU   A OE2 
1374 N  N   . GLY   A 179 ? 0.10320 0.13701 0.14432 -0.03084 -0.00302 0.03168  179 GLY   A N   
1375 C  CA  . GLY   A 179 ? 0.09699 0.13463 0.13029 -0.02773 0.00307  0.03733  179 GLY   A CA  
1376 C  C   . GLY   A 179 ? 0.09819 0.14582 0.13062 -0.02330 0.00737  0.03602  179 GLY   A C   
1377 O  O   . GLY   A 179 ? 0.09286 0.14489 0.12101 -0.02107 0.01443  0.03995  179 GLY   A O   
1378 N  N   . ASN   A 180 ? 0.08609 0.13730 0.12224 -0.02148 0.00396  0.03101  180 ASN   A N   
1379 C  CA  . ASN   A 180 ? 0.08305 0.14344 0.12161 -0.01626 0.00797  0.03123  180 ASN   A CA  
1380 C  C   . ASN   A 180 ? 0.07878 0.13037 0.10387 -0.01049 0.00864  0.02660  180 ASN   A C   
1381 O  O   . ASN   A 180 ? 0.07459 0.12008 0.09568 -0.01060 0.00302  0.02236  180 ASN   A O   
1382 C  CB  . ASN   A 180 ? 0.09208 0.16426 0.14450 -0.01822 0.00321  0.03101  180 ASN   A CB  
1383 C  CG  . ASN   A 180 ? 0.09494 0.17581 0.16161 -0.02556 0.00190  0.03493  180 ASN   A CG  
1384 O  OD1 . ASN   A 180 ? 0.10368 0.19198 0.17745 -0.02589 0.00809  0.04111  180 ASN   A OD1 
1385 N  ND2 . ASN   A 180 ? 0.15899 0.23758 0.22934 -0.03221 -0.00554 0.03084  180 ASN   A ND2 
1386 N  N   . PHE   A 181 ? 0.08433 0.13481 0.10240 -0.00596 0.01618  0.02703  181 PHE   A N   
1387 C  CA  . PHE   A 181 ? 0.09587 0.13602 0.10081 -0.00182 0.01716  0.02181  181 PHE   A CA  
1388 C  C   . PHE   A 181 ? 0.08818 0.12946 0.09905 0.00175  0.01424  0.01970  181 PHE   A C   
1389 O  O   . PHE   A 181 ? 0.07719 0.12956 0.10143 0.00381  0.01497  0.02308  181 PHE   A O   
1390 C  CB  . PHE   A 181 ? 0.10583 0.14439 0.10278 0.00212  0.02711  0.02109  181 PHE   A CB  
1391 C  CG  . PHE   A 181 ? 0.16816 0.19842 0.14685 -0.00075 0.02813  0.01958  181 PHE   A CG  
1392 C  CD1 . PHE   A 181 ? 0.16292 0.18170 0.12714 -0.00106 0.02484  0.01375  181 PHE   A CD1 
1393 C  CD2 . PHE   A 181 ? 0.13060 0.16598 0.10741 -0.00411 0.03133  0.02525  181 PHE   A CD2 
1394 C  CE1 . PHE   A 181 ? 0.14174 0.15539 0.08874 -0.00472 0.02401  0.01322  181 PHE   A CE1 
1395 C  CE2 . PHE   A 181 ? 0.18249 0.21239 0.14144 -0.00710 0.03143  0.02565  181 PHE   A CE2 
1396 C  CZ  . PHE   A 181 ? 0.19167 0.21132 0.13533 -0.00753 0.02720  0.01954  181 PHE   A CZ  
1397 N  N   . TYR   A 182 ? 0.08373 0.11480 0.08532 0.00226  0.01072  0.01534  182 TYR   A N   
1398 C  CA  . TYR   A 182 ? 0.09703 0.12662 0.10139 0.00646  0.01022  0.01411  182 TYR   A CA  
1399 C  C   . TYR   A 182 ? 0.12510 0.14924 0.12662 0.01205  0.01891  0.01253  182 TYR   A C   
1400 O  O   . TYR   A 182 ? 0.11920 0.13288 0.10723 0.01127  0.02211  0.00787  182 TYR   A O   
1401 C  CB  . TYR   A 182 ? 0.07611 0.09725 0.07308 0.00427  0.00422  0.01068  182 TYR   A CB  
1402 C  CG  . TYR   A 182 ? 0.08616 0.11220 0.08764 0.00055  -0.00251 0.01117  182 TYR   A CG  
1403 C  CD1 . TYR   A 182 ? 0.11910 0.15279 0.12740 0.00136  -0.00546 0.01262  182 TYR   A CD1 
1404 C  CD2 . TYR   A 182 ? 0.06986 0.09222 0.06806 -0.00366 -0.00564 0.01010  182 TYR   A CD2 
1405 C  CE1 . TYR   A 182 ? 0.08144 0.11841 0.09087 -0.00255 -0.01076 0.01096  182 TYR   A CE1 
1406 C  CE2 . TYR   A 182 ? 0.07193 0.09619 0.07432 -0.00664 -0.01030 0.00882  182 TYR   A CE2 
1407 C  CZ  . TYR   A 182 ? 0.09471 0.12589 0.10143 -0.00633 -0.01251 0.00822  182 TYR   A CZ  
1408 O  OH  . TYR   A 182 ? 0.06815 0.10038 0.07615 -0.00964 -0.01617 0.00504  182 TYR   A OH  
1409 N  N   . GLY   A 183 ? 0.09188 0.12349 0.10634 0.01755  0.02294  0.01642  183 GLY   A N   
1410 C  CA  . GLY   A 183 ? 0.13003 0.15549 0.14520 0.02423  0.03274  0.01488  183 GLY   A CA  
1411 C  C   . GLY   A 183 ? 0.14253 0.17027 0.15559 0.02577  0.04235  0.01425  183 GLY   A C   
1412 O  O   . GLY   A 183 ? 0.11460 0.15037 0.12721 0.02143  0.04134  0.01676  183 GLY   A O   
1413 N  N   . PRO   A 184 ? 0.14704 0.16674 0.15874 0.03206  0.05287  0.01077  184 PRO   A N   
1414 C  CA  . PRO   A 184 ? 0.16106 0.18474 0.17304 0.03551  0.06498  0.01055  184 PRO   A CA  
1415 C  C   . PRO   A 184 ? 0.18742 0.20025 0.17487 0.03071  0.06831  0.00273  184 PRO   A C   
1416 O  O   . PRO   A 184 ? 0.24482 0.24667 0.22099 0.03399  0.07887  -0.00473 184 PRO   A O   
1417 C  CB  . PRO   A 184 ? 0.18037 0.19835 0.20297 0.04543  0.07538  0.00962  184 PRO   A CB  
1418 C  CG  . PRO   A 184 ? 0.19355 0.19390 0.20707 0.04412  0.06984  0.00375  184 PRO   A CG  
1419 C  CD  . PRO   A 184 ? 0.15318 0.15912 0.16468 0.03662  0.05513  0.00701  184 PRO   A CD  
1420 N  N   . PHE   A 185 ? 0.15580 0.17150 0.13452 0.02281  0.05939  0.00440  185 PHE   A N   
1421 C  CA  . PHE   A 185 ? 0.18791 0.19612 0.14354 0.01732  0.05980  -0.00042 185 PHE   A CA  
1422 C  C   . PHE   A 185 ? 0.22066 0.24152 0.17767 0.01330  0.05998  0.00716  185 PHE   A C   
1423 O  O   . PHE   A 185 ? 0.19583 0.22847 0.17049 0.01216  0.05549  0.01476  185 PHE   A O   
1424 C  CB  . PHE   A 185 ? 0.19977 0.19765 0.14365 0.01159  0.04831  -0.00444 185 PHE   A CB  
1425 C  CG  . PHE   A 185 ? 0.17435 0.16095 0.12090 0.01462  0.04730  -0.00990 185 PHE   A CG  
1426 C  CD1 . PHE   A 185 ? 0.20325 0.17684 0.14079 0.01781  0.05631  -0.01845 185 PHE   A CD1 
1427 C  CD2 . PHE   A 185 ? 0.18302 0.17171 0.14158 0.01434  0.03850  -0.00638 185 PHE   A CD2 
1428 C  CE1 . PHE   A 185 ? 0.19905 0.16070 0.14122 0.02030  0.05586  -0.02257 185 PHE   A CE1 
1429 C  CE2 . PHE   A 185 ? 0.18212 0.16125 0.14426 0.01698  0.03815  -0.00946 185 PHE   A CE2 
1430 C  CZ  . PHE   A 185 ? 0.18942 0.15448 0.14436 0.01992  0.04676  -0.01714 185 PHE   A CZ  
1431 N  N   . VAL   A 186 ? 0.19565 0.21405 0.13364 0.01066  0.06554  0.00513  186 VAL   A N   
1432 C  CA  . VAL   A 186 ? 0.25793 0.28750 0.19554 0.00684  0.06759  0.01342  186 VAL   A CA  
1433 C  C   . VAL   A 186 ? 0.25186 0.27595 0.16638 -0.00008 0.06190  0.01313  186 VAL   A C   
1434 O  O   . VAL   A 186 ? 0.24992 0.26299 0.14460 -0.00141 0.06092  0.00465  186 VAL   A O   
1435 C  CB  . VAL   A 186 ? 0.26529 0.30268 0.20498 0.01177  0.08351  0.01455  186 VAL   A CB  
1436 C  CG1 . VAL   A 186 ? 0.22292 0.27028 0.19073 0.01835  0.08739  0.01841  186 VAL   A CG1 
1437 C  CG2 . VAL   A 186 ? 0.26289 0.28832 0.17991 0.01430  0.09301  0.00315  186 VAL   A CG2 
1438 N  N   . ASP   A 187 ? 0.24773 0.27993 0.16585 -0.00495 0.05782  0.02314  187 ASP   A N   
1439 C  CA  . ASP   A 187 ? 0.28606 0.31590 0.18505 -0.01115 0.05199  0.02643  187 ASP   A CA  
1440 C  C   . ASP   A 187 ? 0.33047 0.36460 0.21015 -0.01216 0.06280  0.02792  187 ASP   A C   
1441 O  O   . ASP   A 187 ? 0.30830 0.34672 0.18870 -0.01535 0.06259  0.03722  187 ASP   A O   
1442 C  CB  . ASP   A 187 ? 0.23390 0.26792 0.14700 -0.01540 0.04236  0.03702  187 ASP   A CB  
1443 C  CG  . ASP   A 187 ? 0.22922 0.27379 0.16335 -0.01543 0.04717  0.04560  187 ASP   A CG  
1444 O  OD1 . ASP   A 187 ? 0.20040 0.25177 0.14157 -0.01161 0.05738  0.04452  187 ASP   A OD1 
1445 O  OD2 . ASP   A 187 ? 0.19755 0.24329 0.14365 -0.01938 0.04031  0.05331  187 ASP   A OD2 
1446 N  N   . ARG   A 188 ? 0.33596 0.36420 0.20278 -0.00799 0.07099  0.01675  188 ARG   A N   
1447 C  CA  . ARG   A 188 ? 0.40060 0.43252 0.25143 -0.00610 0.07829  0.01336  188 ARG   A CA  
1448 C  C   . ARG   A 188 ? 0.45958 0.47845 0.29278 -0.00586 0.07557  -0.00088 188 ARG   A C   
1449 O  O   . ARG   A 188 ? 0.42275 0.43121 0.26137 -0.00513 0.07235  -0.00857 188 ARG   A O   
1450 C  CB  . ARG   A 188 ? 0.41869 0.45962 0.28190 -0.00405 0.09216  0.01068  188 ARG   A CB  
1451 C  CG  . ARG   A 188 ? 0.47838 0.52720 0.34998 -0.00845 0.09710  0.02153  188 ARG   A CG  
1452 C  CD  . ARG   A 188 ? 0.46529 0.52336 0.36439 -0.00168 0.10528  0.02441  188 ARG   A CD  
1453 N  NE  . ARG   A 188 ? 0.46306 0.51872 0.36506 0.00642  0.11378  0.01373  188 ARG   A NE  
1454 C  CZ  . ARG   A 188 ? 0.43349 0.49039 0.35938 0.01350  0.11569  0.01405  188 ARG   A CZ  
1455 N  NH1 . ARG   A 188 ? 0.40863 0.47111 0.35518 0.01296  0.10839  0.02281  188 ARG   A NH1 
1456 N  NH2 . ARG   A 188 ? 0.41644 0.46955 0.34628 0.02118  0.12444  0.00584  188 ARG   A NH2 
1457 N  N   . GLN   A 189 ? 0.50103 0.51968 0.31331 -0.00638 0.07771  -0.00434 189 GLN   A N   
1458 C  CA  . GLN   A 189 ? 0.53381 0.54025 0.32974 -0.00743 0.07558  -0.01881 189 GLN   A CA  
1459 C  C   . GLN   A 189 ? 0.50325 0.50734 0.30251 -0.00120 0.08987  -0.02927 189 GLN   A C   
1460 O  O   . GLN   A 189 ? 0.55109 0.56192 0.34083 0.00113  0.09947  -0.03064 189 GLN   A O   
1461 C  CB  . GLN   A 189 ? 0.59162 0.59792 0.36303 -0.01219 0.06952  -0.01828 189 GLN   A CB  
1462 C  CG  . GLN   A 189 ? 0.60193 0.59769 0.35512 -0.01365 0.07010  -0.03397 189 GLN   A CG  
1463 C  CD  . GLN   A 189 ? 0.69855 0.68259 0.45643 -0.01780 0.05926  -0.04121 189 GLN   A CD  
1464 O  OE1 . GLN   A 189 ? 0.73712 0.70935 0.49769 -0.01588 0.06366  -0.05334 189 GLN   A OE1 
1465 N  NE2 . GLN   A 189 ? 0.70187 0.68911 0.46328 -0.02314 0.04550  -0.03284 189 GLN   A NE2 
1466 N  N   . THR   A 190 ? 0.48414 0.47828 0.29860 0.00224  0.09174  -0.03564 190 THR   A N   
1467 C  CA  . THR   A 190 ? 0.48377 0.47032 0.30502 0.00919  0.10389  -0.04562 190 THR   A CA  
1468 C  C   . THR   A 190 ? 0.46236 0.42932 0.27795 0.00793  0.09914  -0.05784 190 THR   A C   
1469 O  O   . THR   A 190 ? 0.46609 0.42775 0.27283 0.00116  0.08658  -0.05862 190 THR   A O   
1470 C  CB  . THR   A 190 ? 0.44473 0.43739 0.29504 0.01617  0.11105  -0.03885 190 THR   A CB  
1471 O  OG1 . THR   A 190 ? 0.43819 0.42275 0.30133 0.01651  0.10340  -0.03750 190 THR   A OG1 
1472 C  CG2 . THR   A 190 ? 0.44131 0.45342 0.30120 0.01466  0.11262  -0.02515 190 THR   A CG2 
1473 N  N   . ALA   A 191 ? 0.47220 0.42871 0.29556 0.01442  0.10916  -0.06651 191 ALA   A N   
1474 C  CA  . ALA   A 191 ? 0.45432 0.39142 0.27666 0.01349  0.10584  -0.07696 191 ALA   A CA  
1475 C  C   . ALA   A 191 ? 0.44855 0.38115 0.29372 0.01655  0.10199  -0.07163 191 ALA   A C   
1476 O  O   . ALA   A 191 ? 0.46521 0.38268 0.31765 0.01906  0.10355  -0.07812 191 ALA   A O   
1477 C  CB  . ALA   A 191 ? 0.46683 0.39253 0.28657 0.01906  0.11852  -0.08862 191 ALA   A CB  
1478 N  N   . GLN   A 192 ? 0.39952 0.34472 0.25588 0.01630  0.09706  -0.05968 192 GLN   A N   
1479 C  CA  . GLN   A 192 ? 0.36634 0.30913 0.24330 0.01983  0.09383  -0.05415 192 GLN   A CA  
1480 C  C   . GLN   A 192 ? 0.41996 0.34681 0.29158 0.01501  0.08507  -0.06106 192 GLN   A C   
1481 O  O   . GLN   A 192 ? 0.42554 0.34898 0.27878 0.00626  0.07615  -0.06578 192 GLN   A O   
1482 C  CB  . GLN   A 192 ? 0.37768 0.33491 0.26186 0.01784  0.08752  -0.04188 192 GLN   A CB  
1483 C  CG  . GLN   A 192 ? 0.38769 0.35279 0.25360 0.00915  0.07964  -0.03846 192 GLN   A CG  
1484 C  CD  . GLN   A 192 ? 0.32657 0.30623 0.20356 0.00823  0.07602  -0.02518 192 GLN   A CD  
1485 O  OE1 . GLN   A 192 ? 0.31193 0.29891 0.21387 0.01311  0.07497  -0.01844 192 GLN   A OE1 
1486 N  NE2 . GLN   A 192 ? 0.35179 0.33867 0.21563 0.00151  0.07056  -0.01995 192 GLN   A NE2 
1487 N  N   . ALA   A 193 ? 0.37744 0.29653 0.26759 0.02069  0.08693  -0.05999 193 ALA   A N   
1488 C  CA  . ALA   A 193 ? 0.36017 0.26470 0.24974 0.01659  0.07955  -0.06489 193 ALA   A CA  
1489 C  C   . ALA   A 193 ? 0.35143 0.25769 0.26263 0.02197  0.07768  -0.05607 193 ALA   A C   
1490 O  O   . ALA   A 193 ? 0.36300 0.28017 0.29260 0.03044  0.08354  -0.04742 193 ALA   A O   
1491 C  CB  . ALA   A 193 ? 0.41120 0.29903 0.29882 0.01779  0.08549  -0.07547 193 ALA   A CB  
1492 N  N   . ALA   A 194 ? 0.35551 0.25358 0.26670 0.01668  0.06819  -0.05713 194 ALA   A N   
1493 C  CA  . ALA   A 194 ? 0.34772 0.25522 0.28033 0.01909  0.06005  -0.04545 194 ALA   A CA  
1494 C  C   . ALA   A 194 ? 0.36379 0.27035 0.31910 0.03006  0.06874  -0.03962 194 ALA   A C   
1495 O  O   . ALA   A 194 ? 0.39285 0.31593 0.36559 0.03461  0.06575  -0.02782 194 ALA   A O   
1496 C  CB  . ALA   A 194 ? 0.29996 0.19901 0.22920 0.01126  0.04957  -0.04773 194 ALA   A CB  
1497 N  N   . GLY   A 195 ? 0.39109 0.27951 0.34760 0.03398  0.07861  -0.04701 195 GLY   A N   
1498 C  CA  . GLY   A 195 ? 0.36438 0.25678 0.34716 0.04382  0.08262  -0.03651 195 GLY   A CA  
1499 C  C   . GLY   A 195 ? 0.37178 0.25862 0.36500 0.04259  0.07537  -0.03069 195 GLY   A C   
1500 O  O   . GLY   A 195 ? 0.33019 0.22102 0.31550 0.03401  0.06363  -0.03003 195 GLY   A O   
1501 N  N   . THR   A 196 ? 0.35083 0.23555 0.36331 0.04899  0.07867  -0.02352 196 THR   A N   
1502 C  CA  . THR   A 196 ? 0.35009 0.22576 0.37013 0.04646  0.07339  -0.01954 196 THR   A CA  
1503 C  C   . THR   A 196 ? 0.29206 0.18203 0.31881 0.04549  0.06368  -0.00796 196 THR   A C   
1504 O  O   . THR   A 196 ? 0.27737 0.18882 0.31240 0.04938  0.06069  0.00179  196 THR   A O   
1505 C  CB  . THR   A 196 ? 0.34625 0.21834 0.38523 0.05363  0.07929  -0.01271 196 THR   A CB  
1506 O  OG1 . THR   A 196 ? 0.38918 0.28077 0.44424 0.06223  0.08178  -0.00075 196 THR   A OG1 
1507 C  CG2 . THR   A 196 ? 0.39069 0.24436 0.42207 0.05348  0.08855  -0.02582 196 THR   A CG2 
1508 N  N   . ASP   A 197 ? 0.26827 0.15147 0.29071 0.03779  0.05621  -0.00872 197 ASP   A N   
1509 C  CA  . ASP   A 197 ? 0.25781 0.15770 0.28349 0.03400  0.04509  0.00128  197 ASP   A CA  
1510 C  C   . ASP   A 197 ? 0.29616 0.19207 0.33820 0.03725  0.04547  0.01228  197 ASP   A C   
1511 O  O   . ASP   A 197 ? 0.30370 0.18410 0.35228 0.03926  0.05162  0.01051  197 ASP   A O   
1512 C  CB  . ASP   A 197 ? 0.24863 0.14700 0.25863 0.02268  0.03643  -0.00611 197 ASP   A CB  
1513 C  CG  . ASP   A 197 ? 0.24250 0.16186 0.25193 0.01992  0.02691  0.00108  197 ASP   A CG  
1514 O  OD1 . ASP   A 197 ? 0.21559 0.13558 0.21699 0.01201  0.02005  -0.00221 197 ASP   A OD1 
1515 O  OD2 . ASP   A 197 ? 0.21646 0.15199 0.23313 0.02532  0.02647  0.00906  197 ASP   A OD2 
1516 N  N   . THR   A 198 ? 0.25677 0.17022 0.30294 0.03590  0.03744  0.02314  198 THR   A N   
1517 C  CA  . THR   A 198 ? 0.26433 0.17745 0.32340 0.03752  0.03652  0.03539  198 THR   A CA  
1518 C  C   . THR   A 198 ? 0.22459 0.14704 0.27618 0.02914  0.02760  0.03704  198 THR   A C   
1519 O  O   . THR   A 198 ? 0.21704 0.14658 0.25597 0.02352  0.02234  0.02959  198 THR   A O   
1520 C  CB  . THR   A 198 ? 0.27203 0.20485 0.34413 0.04507  0.03625  0.04927  198 THR   A CB  
1521 O  OG1 . THR   A 198 ? 0.28718 0.24008 0.35564 0.04601  0.03099  0.05239  198 THR   A OG1 
1522 C  CG2 . THR   A 198 ? 0.33045 0.25780 0.41162 0.05180  0.04466  0.04790  198 THR   A CG2 
1523 N  N   . THR   A 199 ? 0.21812 0.14047 0.27875 0.02868  0.02673  0.04762  199 THR   A N   
1524 C  CA  . THR   A 199 ? 0.22782 0.16066 0.28371 0.02187  0.02013  0.05099  199 THR   A CA  
1525 C  C   . THR   A 199 ? 0.20728 0.16416 0.26370 0.02512  0.01598  0.06223  199 THR   A C   
1526 O  O   . THR   A 199 ? 0.18012 0.14556 0.24471 0.03085  0.01741  0.07150  199 THR   A O   
1527 C  CB  . THR   A 199 ? 0.24247 0.16314 0.30624 0.01786  0.02183  0.05533  199 THR   A CB  
1528 O  OG1 . THR   A 199 ? 0.27057 0.16899 0.33153 0.01249  0.02423  0.04272  199 THR   A OG1 
1529 C  CG2 . THR   A 199 ? 0.22473 0.15788 0.28680 0.01222  0.01696  0.06162  199 THR   A CG2 
1530 N  N   . ILE   A 200 ? 0.18032 0.15020 0.22619 0.02013  0.01039  0.05847  200 ILE   A N   
1531 C  CA  . ILE   A 200 ? 0.15680 0.14843 0.19924 0.02142  0.00627  0.06550  200 ILE   A CA  
1532 C  C   . ILE   A 200 ? 0.16505 0.16360 0.21131 0.02071  0.00627  0.07789  200 ILE   A C   
1533 O  O   . ILE   A 200 ? 0.15118 0.15250 0.19281 0.01550  0.00514  0.07679  200 ILE   A O   
1534 C  CB  . ILE   A 200 ? 0.16310 0.16305 0.19342 0.01668  0.00184  0.05554  200 ILE   A CB  
1535 C  CG1 . ILE   A 200 ? 0.14596 0.13814 0.17228 0.01657  0.00225  0.04448  200 ILE   A CG1 
1536 C  CG2 . ILE   A 200 ? 0.15739 0.17744 0.18290 0.01748  -0.00193 0.06002  200 ILE   A CG2 
1537 C  CD1 . ILE   A 200 ? 0.11885 0.11153 0.13582 0.01071  -0.00126 0.03484  200 ILE   A CD1 
1538 N  N   . THR   A 201 ? 0.17233 0.17641 0.22636 0.02470  0.00796  0.08574  201 THR   A N   
1539 C  CA  . THR   A 201 ? 0.16093 0.17141 0.21915 0.02364  0.00889  0.09531  201 THR   A CA  
1540 C  C   . THR   A 201 ? 0.15813 0.18643 0.20560 0.01989  0.00550  0.09720  201 THR   A C   
1541 O  O   . THR   A 201 ? 0.13268 0.16157 0.18023 0.01662  0.00701  0.10082  201 THR   A O   
1542 C  CB  . THR   A 201 ? 0.16110 0.17811 0.22934 0.02897  0.01031  0.10421  201 THR   A CB  
1543 O  OG1 . THR   A 201 ? 0.16899 0.16889 0.24721 0.03312  0.01501  0.10122  201 THR   A OG1 
1544 C  CG2 . THR   A 201 ? 0.17546 0.19874 0.24944 0.02836  0.01154  0.11571  201 THR   A CG2 
1545 N  N   . VAL   A 202 ? 0.16529 0.20821 0.20362 0.01998  0.00146  0.09410  202 VAL   A N   
1546 C  CA  . VAL   A 202 ? 0.15424 0.21297 0.18128 0.01645  -0.00071 0.09439  202 VAL   A CA  
1547 C  C   . VAL   A 202 ? 0.13294 0.18658 0.15408 0.01249  0.00063  0.08880  202 VAL   A C   
1548 O  O   . VAL   A 202 ? 0.13951 0.20095 0.15612 0.00997  0.00227  0.09142  202 VAL   A O   
1549 C  CB  . VAL   A 202 ? 0.14206 0.21517 0.16020 0.01587  -0.00538 0.08987  202 VAL   A CB  
1550 C  CG1 . VAL   A 202 ? 0.18416 0.25110 0.19893 0.01557  -0.00728 0.07941  202 VAL   A CG1 
1551 C  CG2 . VAL   A 202 ? 0.16190 0.24952 0.16716 0.01199  -0.00667 0.08895  202 VAL   A CG2 
1552 N  N   . ASN   A 203 ? 0.14975 0.19096 0.17182 0.01194  0.00037  0.08176  203 ASN   A N   
1553 C  CA  . ASN   A 203 ? 0.12370 0.16077 0.14296 0.00750  0.00130  0.07455  203 ASN   A CA  
1554 C  C   . ASN   A 203 ? 0.15829 0.18788 0.18678 0.00484  0.00493  0.08115  203 ASN   A C   
1555 O  O   . ASN   A 203 ? 0.14466 0.17986 0.17221 0.00137  0.00674  0.08086  203 ASN   A O   
1556 C  CB  . ASN   A 203 ? 0.15291 0.17855 0.17208 0.00650  -0.00049 0.06185  203 ASN   A CB  
1557 C  CG  . ASN   A 203 ? 0.14901 0.18281 0.15948 0.00722  -0.00367 0.05428  203 ASN   A CG  
1558 O  OD1 . ASN   A 203 ? 0.14142 0.18897 0.14553 0.00800  -0.00513 0.05722  203 ASN   A OD1 
1559 N  ND2 . ASN   A 203 ? 0.10826 0.13372 0.11807 0.00625  -0.00499 0.04481  203 ASN   A ND2 
1560 N  N   . VAL   A 204 ? 0.14106 0.15752 0.18002 0.00626  0.00662  0.08612  204 VAL   A N   
1561 C  CA  . VAL   A 204 ? 0.14417 0.15285 0.19311 0.00276  0.00972  0.09054  204 VAL   A CA  
1562 C  C   . VAL   A 204 ? 0.13149 0.15596 0.17916 0.00282  0.01158  0.09931  204 VAL   A C   
1563 O  O   . VAL   A 204 ? 0.13425 0.16063 0.18585 -0.00121 0.01388  0.10177  204 VAL   A O   
1564 C  CB  . VAL   A 204 ? 0.13951 0.13097 0.19881 0.00477  0.01174  0.09147  204 VAL   A CB  
1565 C  CG1 . VAL   A 204 ? 0.14970 0.13344 0.21925 0.00052  0.01451  0.09584  204 VAL   A CG1 
1566 C  CG2 . VAL   A 204 ? 0.15331 0.12817 0.21193 0.00441  0.01090  0.08105  204 VAL   A CG2 
1567 N  N   . LEU   A 205 ? 0.13432 0.17112 0.17708 0.00697  0.01051  0.10413  205 LEU   A N   
1568 C  CA  . LEU   A 205 ? 0.14208 0.19441 0.18139 0.00671  0.01196  0.11213  205 LEU   A CA  
1569 C  C   . LEU   A 205 ? 0.15765 0.22134 0.18554 0.00381  0.01285  0.10726  205 LEU   A C   
1570 O  O   . LEU   A 205 ? 0.14303 0.21281 0.17172 0.00167  0.01645  0.11168  205 LEU   A O   
1571 C  CB  . LEU   A 205 ? 0.14744 0.21166 0.18336 0.01058  0.00941  0.11742  205 LEU   A CB  
1572 C  CG  . LEU   A 205 ? 0.15581 0.21212 0.20535 0.01448  0.01005  0.12476  205 LEU   A CG  
1573 C  CD1 . LEU   A 205 ? 0.17662 0.24710 0.22338 0.01774  0.00663  0.12875  205 LEU   A CD1 
1574 C  CD2 . LEU   A 205 ? 0.20916 0.26194 0.26949 0.01383  0.01383  0.13518  205 LEU   A CD2 
1575 N  N   . ALA   A 206 ? 0.12684 0.19297 0.14493 0.00388  0.01035  0.09789  206 ALA   A N   
1576 C  CA  . ALA   A 206 ? 0.13920 0.21447 0.14737 0.00163  0.01248  0.09186  206 ALA   A CA  
1577 C  C   . ALA   A 206 ? 0.15343 0.22360 0.17134 -0.00177 0.01661  0.09244  206 ALA   A C   
1578 O  O   . ALA   A 206 ? 0.15629 0.23611 0.17152 -0.00308 0.02114  0.09222  206 ALA   A O   
1579 C  CB  . ALA   A 206 ? 0.13196 0.20739 0.13097 0.00208  0.00917  0.08137  206 ALA   A CB  
1580 N  N   . TRP   A 207 ? 0.14387 0.19897 0.17382 -0.00362 0.01518  0.09224  207 TRP   A N   
1581 C  CA  . TRP   A 207 ? 0.14455 0.19521 0.18587 -0.00849 0.01719  0.09137  207 TRP   A CA  
1582 C  C   . TRP   A 207 ? 0.15281 0.20543 0.20335 -0.01021 0.02063  0.09981  207 TRP   A C   
1583 O  O   . TRP   A 207 ? 0.15846 0.21753 0.21519 -0.01317 0.02386  0.10066  207 TRP   A O   
1584 C  CB  . TRP   A 207 ? 0.12966 0.16248 0.17784 -0.01057 0.01244  0.08328  207 TRP   A CB  
1585 C  CG  . TRP   A 207 ? 0.14325 0.16934 0.20476 -0.01709 0.01195  0.08202  207 TRP   A CG  
1586 C  CD1 . TRP   A 207 ? 0.11217 0.14379 0.17756 -0.02014 0.01056  0.07573  207 TRP   A CD1 
1587 C  CD2 . TRP   A 207 ? 0.12735 0.13956 0.20071 -0.02160 0.01183  0.08603  207 TRP   A CD2 
1588 N  NE1 . TRP   A 207 ? 0.15129 0.17584 0.23044 -0.02723 0.00877  0.07699  207 TRP   A NE1 
1589 C  CE2 . TRP   A 207 ? 0.16350 0.17491 0.24660 -0.02860 0.00954  0.08198  207 TRP   A CE2 
1590 C  CE3 . TRP   A 207 ? 0.15885 0.15966 0.23496 -0.01955 0.01298  0.08997  207 TRP   A CE3 
1591 C  CZ2 . TRP   A 207 ? 0.19290 0.19217 0.28575 -0.03448 0.00791  0.08083  207 TRP   A CZ2 
1592 C  CZ3 . TRP   A 207 ? 0.18313 0.17025 0.26980 -0.02494 0.01269  0.08892  207 TRP   A CZ3 
1593 C  CH2 . TRP   A 207 ? 0.15444 0.14061 0.24823 -0.03279 0.00997  0.08390  207 TRP   A CH2 
1594 N  N   . LEU   A 208 ? 0.13603 0.18461 0.18855 -0.00794 0.02032  0.10673  208 LEU   A N   
1595 C  CA  . LEU   A 208 ? 0.14871 0.20100 0.20865 -0.00906 0.02383  0.11640  208 LEU   A CA  
1596 C  C   . LEU   A 208 ? 0.15753 0.22868 0.20775 -0.00794 0.02778  0.11967  208 LEU   A C   
1597 O  O   . LEU   A 208 ? 0.15972 0.23622 0.21620 -0.01037 0.03198  0.12460  208 LEU   A O   
1598 C  CB  . LEU   A 208 ? 0.15926 0.20521 0.22322 -0.00591 0.02294  0.12371  208 LEU   A CB  
1599 C  CG  . LEU   A 208 ? 0.17784 0.20250 0.25298 -0.00743 0.02138  0.12027  208 LEU   A CG  
1600 C  CD1 . LEU   A 208 ? 0.17333 0.19309 0.25354 -0.00298 0.02189  0.12777  208 LEU   A CD1 
1601 C  CD2 . LEU   A 208 ? 0.16694 0.18221 0.25449 -0.01425 0.02264  0.11939  208 LEU   A CD2 
1602 N  N   . TYR   A 209 ? 0.15842 0.23947 0.19278 -0.00471 0.02667  0.11593  209 TYR   A N   
1603 C  CA  . TYR   A 209 ? 0.18634 0.28321 0.20838 -0.00428 0.03093  0.11541  209 TYR   A CA  
1604 C  C   . TYR   A 209 ? 0.19463 0.29447 0.21902 -0.00623 0.03548  0.10847  209 TYR   A C   
1605 O  O   . TYR   A 209 ? 0.18029 0.28988 0.20309 -0.00668 0.04159  0.11049  209 TYR   A O   
1606 C  CB  . TYR   A 209 ? 0.15878 0.26369 0.16296 -0.00174 0.02779  0.11046  209 TYR   A CB  
1607 C  CG  . TYR   A 209 ? 0.18726 0.29774 0.18849 0.00004  0.02491  0.11965  209 TYR   A CG  
1608 C  CD1 . TYR   A 209 ? 0.18765 0.30889 0.18516 -0.00041 0.02837  0.12862  209 TYR   A CD1 
1609 C  CD2 . TYR   A 209 ? 0.20506 0.31115 0.20845 0.00226  0.01911  0.12012  209 TYR   A CD2 
1610 C  CE1 . TYR   A 209 ? 0.22835 0.35628 0.22446 0.00111  0.02536  0.13830  209 TYR   A CE1 
1611 C  CE2 . TYR   A 209 ? 0.19421 0.30727 0.19789 0.00411  0.01658  0.12948  209 TYR   A CE2 
1612 C  CZ  . TYR   A 209 ? 0.23892 0.36308 0.23910 0.00343  0.01938  0.13887  209 TYR   A CZ  
1613 O  OH  . TYR   A 209 ? 0.23492 0.36728 0.23649 0.00519  0.01648  0.14942  209 TYR   A OH  
1614 N  N   . ALA   A 210 ? 0.17763 0.27018 0.20646 -0.00711 0.03305  0.10052  210 ALA   A N   
1615 C  CA  . ALA   A 210 ? 0.17254 0.26866 0.20940 -0.00881 0.03701  0.09548  210 ALA   A CA  
1616 C  C   . ALA   A 210 ? 0.18891 0.28422 0.24312 -0.01239 0.03928  0.10264  210 ALA   A C   
1617 O  O   . ALA   A 210 ? 0.17750 0.28217 0.23670 -0.01264 0.04497  0.10266  210 ALA   A O   
1618 C  CB  . ALA   A 210 ? 0.16934 0.25772 0.21123 -0.00994 0.03275  0.08779  210 ALA   A CB  
1619 N  N   . ALA   A 211 ? 0.15570 0.23928 0.21984 -0.01516 0.03514  0.10802  211 ALA   A N   
1620 C  CA  . ALA   A 211 ? 0.15576 0.23734 0.23632 -0.01957 0.03644  0.11422  211 ALA   A CA  
1621 C  C   . ALA   A 211 ? 0.19027 0.28421 0.26839 -0.01826 0.04306  0.12288  211 ALA   A C   
1622 O  O   . ALA   A 211 ? 0.16941 0.27145 0.25654 -0.02018 0.04760  0.12496  211 ALA   A O   
1623 C  CB  . ALA   A 211 ? 0.15558 0.22007 0.24432 -0.02242 0.03152  0.11665  211 ALA   A CB  
1624 N  N   . VAL   A 212 ? 0.18172 0.27830 0.24796 -0.01501 0.04352  0.12832  212 VAL   A N   
1625 C  CA  . VAL   A 212 ? 0.18912 0.29797 0.25076 -0.01413 0.04945  0.13699  212 VAL   A CA  
1626 C  C   . VAL   A 212 ? 0.22263 0.34510 0.27553 -0.01277 0.05629  0.13143  212 VAL   A C   
1627 O  O   . VAL   A 212 ? 0.22691 0.35828 0.28437 -0.01386 0.06289  0.13673  212 VAL   A O   
1628 C  CB  . VAL   A 212 ? 0.20972 0.32109 0.25869 -0.01089 0.04735  0.14295  212 VAL   A CB  
1629 C  CG1 . VAL   A 212 ? 0.21411 0.33998 0.25479 -0.01036 0.05341  0.15101  212 VAL   A CG1 
1630 C  CG2 . VAL   A 212 ? 0.19676 0.29481 0.25844 -0.01149 0.04292  0.15019  212 VAL   A CG2 
1631 N  N   . ILE   A 213 ? 0.21718 0.34095 0.25804 -0.01025 0.05560  0.12035  213 ILE   A N   
1632 C  CA  . ILE   A 213 ? 0.23647 0.37064 0.27003 -0.00847 0.06319  0.11296  213 ILE   A CA  
1633 C  C   . ILE   A 213 ? 0.20201 0.33801 0.25585 -0.01035 0.06681  0.11298  213 ILE   A C   
1634 O  O   . ILE   A 213 ? 0.25240 0.39863 0.30723 -0.00933 0.07536  0.11256  213 ILE   A O   
1635 C  CB  . ILE   A 213 ? 0.27019 0.40285 0.28921 -0.00572 0.06122  0.10023  213 ILE   A CB  
1636 C  CG1 . ILE   A 213 ? 0.26714 0.40210 0.26491 -0.00446 0.05806  0.10037  213 ILE   A CG1 
1637 C  CG2 . ILE   A 213 ? 0.28681 0.42634 0.30371 -0.00357 0.06961  0.09052  213 ILE   A CG2 
1638 C  CD1 . ILE   A 213 ? 0.25279 0.38414 0.23806 -0.00295 0.05321  0.08934  213 ILE   A CD1 
1639 N  N   . ASN   A 214 ? 0.19561 0.32208 0.26646 -0.01358 0.06028  0.11394  214 ASN   A N   
1640 C  CA  . ASN   A 214 ? 0.18754 0.31609 0.27878 -0.01625 0.06094  0.11362  214 ASN   A CA  
1641 C  C   . ASN   A 214 ? 0.20096 0.32948 0.30818 -0.02107 0.06107  0.12425  214 ASN   A C   
1642 O  O   . ASN   A 214 ? 0.22096 0.35049 0.34657 -0.02467 0.05936  0.12463  214 ASN   A O   
1643 C  CB  . ASN   A 214 ? 0.20079 0.31978 0.29991 -0.01806 0.05276  0.10671  214 ASN   A CB  
1644 C  CG  . ASN   A 214 ? 0.24407 0.36729 0.33671 -0.01352 0.05483  0.09639  214 ASN   A CG  
1645 O  OD1 . ASN   A 214 ? 0.28801 0.41084 0.36256 -0.00992 0.05607  0.09126  214 ASN   A OD1 
1646 N  ND2 . ASN   A 214 ? 0.24590 0.37420 0.35378 -0.01338 0.05560  0.09352  214 ASN   A ND2 
1647 N  N   . GLY   A 215 ? 0.19103 0.31883 0.29249 -0.02147 0.06250  0.13314  215 GLY   A N   
1648 C  CA  . GLY   A 215 ? 0.21903 0.34811 0.33501 -0.02571 0.06432  0.14391  215 GLY   A CA  
1649 C  C   . GLY   A 215 ? 0.23466 0.34833 0.36164 -0.03058 0.05710  0.14804  215 GLY   A C   
1650 O  O   . GLY   A 215 ? 0.22572 0.33922 0.36525 -0.03459 0.05868  0.15698  215 GLY   A O   
1651 N  N   . ASP   A 216 ? 0.19624 0.29634 0.31951 -0.03066 0.04991  0.14124  216 ASP   A N   
1652 C  CA  . ASP   A 216 ? 0.19870 0.28174 0.32949 -0.03448 0.04443  0.14344  216 ASP   A CA  
1653 C  C   . ASP   A 216 ? 0.23232 0.31368 0.35375 -0.03044 0.04617  0.15167  216 ASP   A C   
1654 O  O   . ASP   A 216 ? 0.24779 0.32992 0.35411 -0.02529 0.04491  0.14875  216 ASP   A O   
1655 C  CB  . ASP   A 216 ? 0.22807 0.29745 0.35691 -0.03562 0.03713  0.13245  216 ASP   A CB  
1656 C  CG  . ASP   A 216 ? 0.26152 0.32912 0.40339 -0.04184 0.03284  0.12595  216 ASP   A CG  
1657 O  OD1 . ASP   A 216 ? 0.33044 0.40200 0.48644 -0.04683 0.03402  0.13077  216 ASP   A OD1 
1658 O  OD2 . ASP   A 216 ? 0.22327 0.28691 0.36125 -0.04183 0.02795  0.11648  216 ASP   A OD2 
1659 N  N   . ARG   A 217 ? 0.21499 0.29450 0.34639 -0.03294 0.04854  0.16246  217 ARG   A N   
1660 C  CA  . ARG   A 217 ? 0.22900 0.30925 0.35393 -0.02895 0.05015  0.17237  217 ARG   A CA  
1661 C  C   . ARG   A 217 ? 0.24066 0.30461 0.37911 -0.03170 0.04834  0.17867  217 ARG   A C   
1662 O  O   . ARG   A 217 ? 0.25249 0.31706 0.38876 -0.02811 0.04955  0.18835  217 ARG   A O   
1663 C  CB  . ARG   A 217 ? 0.24042 0.33902 0.36068 -0.02751 0.05722  0.18258  217 ARG   A CB  
1664 C  CG  . ARG   A 217 ? 0.24271 0.35717 0.34828 -0.02458 0.06127  0.17637  217 ARG   A CG  
1665 C  CD  . ARG   A 217 ? 0.25157 0.38238 0.35252 -0.02400 0.06935  0.18645  217 ARG   A CD  
1666 N  NE  . ARG   A 217 ? 0.26568 0.39992 0.35601 -0.02101 0.06910  0.19608  217 ARG   A NE  
1667 C  CZ  . ARG   A 217 ? 0.27921 0.42084 0.34856 -0.01677 0.06817  0.19309  217 ARG   A CZ  
1668 N  NH1 . ARG   A 217 ? 0.25584 0.40155 0.31117 -0.01491 0.06855  0.18029  217 ARG   A NH1 
1669 N  NH2 . ARG   A 217 ? 0.28063 0.42598 0.34365 -0.01467 0.06660  0.20330  217 ARG   A NH2 
1670 N  N   . TRP   A 218 ? 0.24127 0.29087 0.39358 -0.03823 0.04553  0.17337  218 TRP   A N   
1671 C  CA  . TRP   A 218 ? 0.25864 0.29172 0.42449 -0.04202 0.04521  0.17874  218 TRP   A CA  
1672 C  C   . TRP   A 218 ? 0.26246 0.28200 0.42393 -0.03683 0.04335  0.17887  218 TRP   A C   
1673 O  O   . TRP   A 218 ? 0.28041 0.28942 0.45184 -0.03733 0.04498  0.18690  218 TRP   A O   
1674 C  CB  . TRP   A 218 ? 0.25972 0.27946 0.43769 -0.05107 0.04163  0.16973  218 TRP   A CB  
1675 C  CG  . TRP   A 218 ? 0.26367 0.27222 0.43438 -0.05173 0.03578  0.15436  218 TRP   A CG  
1676 C  CD1 . TRP   A 218 ? 0.25835 0.27497 0.42514 -0.05325 0.03273  0.14506  218 TRP   A CD1 
1677 C  CD2 . TRP   A 218 ? 0.24930 0.23665 0.41673 -0.05095 0.03281  0.14712  218 TRP   A CD2 
1678 N  NE1 . TRP   A 218 ? 0.23970 0.24193 0.40004 -0.05387 0.02753  0.13287  218 TRP   A NE1 
1679 C  CE2 . TRP   A 218 ? 0.27124 0.25506 0.43127 -0.05250 0.02786  0.13342  218 TRP   A CE2 
1680 C  CE3 . TRP   A 218 ? 0.28664 0.25780 0.45720 -0.04857 0.03439  0.15116  218 TRP   A CE3 
1681 C  CZ2 . TRP   A 218 ? 0.27344 0.23812 0.42741 -0.05201 0.02481  0.12328  218 TRP   A CZ2 
1682 C  CZ3 . TRP   A 218 ? 0.29994 0.25174 0.46556 -0.04752 0.03180  0.14072  218 TRP   A CZ3 
1683 C  CH2 . TRP   A 218 ? 0.27247 0.22116 0.42898 -0.04934 0.02720  0.12666  218 TRP   A CH2 
1684 N  N   . PHE   A 219 ? 0.24719 0.26673 0.39554 -0.03183 0.04028  0.17041  219 PHE   A N   
1685 C  CA  . PHE   A 219 ? 0.24909 0.25736 0.39386 -0.02631 0.03850  0.16948  219 PHE   A CA  
1686 C  C   . PHE   A 219 ? 0.25257 0.27585 0.38953 -0.01882 0.04005  0.18051  219 PHE   A C   
1687 O  O   . PHE   A 219 ? 0.25449 0.27212 0.39011 -0.01354 0.03861  0.18150  219 PHE   A O   
1688 C  CB  . PHE   A 219 ? 0.23167 0.23330 0.36680 -0.02523 0.03421  0.15488  219 PHE   A CB  
1689 C  CG  . PHE   A 219 ? 0.21401 0.23348 0.33654 -0.02367 0.03345  0.15055  219 PHE   A CG  
1690 C  CD1 . PHE   A 219 ? 0.20826 0.24160 0.31728 -0.01706 0.03351  0.15334  219 PHE   A CD1 
1691 C  CD2 . PHE   A 219 ? 0.20535 0.22844 0.33024 -0.02915 0.03269  0.14375  219 PHE   A CD2 
1692 C  CE1 . PHE   A 219 ? 0.19543 0.24337 0.29204 -0.01601 0.03352  0.14820  219 PHE   A CE1 
1693 C  CE2 . PHE   A 219 ? 0.20877 0.24751 0.32360 -0.02718 0.03313  0.13994  219 PHE   A CE2 
1694 C  CZ  . PHE   A 219 ? 0.18710 0.23722 0.28696 -0.02064 0.03396  0.14158  219 PHE   A CZ  
1695 N  N   . LEU   A 220 ? 0.25499 0.29792 0.38650 -0.01843 0.04294  0.18851  220 LEU   A N   
1696 C  CA  . LEU   A 220 ? 0.26236 0.32060 0.38507 -0.01274 0.04381  0.19913  220 LEU   A CA  
1697 C  C   . LEU   A 220 ? 0.28407 0.33780 0.42058 -0.01205 0.04617  0.21401  220 LEU   A C   
1698 O  O   . LEU   A 220 ? 0.29533 0.33788 0.44698 -0.01687 0.04857  0.21750  220 LEU   A O   
1699 C  CB  . LEU   A 220 ? 0.26180 0.34150 0.37158 -0.01305 0.04683  0.20149  220 LEU   A CB  
1700 C  CG  . LEU   A 220 ? 0.24287 0.32822 0.33858 -0.01285 0.04536  0.18751  220 LEU   A CG  
1701 C  CD1 . LEU   A 220 ? 0.24735 0.35192 0.33081 -0.01305 0.05011  0.18944  220 LEU   A CD1 
1702 C  CD2 . LEU   A 220 ? 0.23275 0.31705 0.31704 -0.00807 0.04029  0.18104  220 LEU   A CD2 
1703 N  N   . ASN   A 221 ? 0.29123 0.35415 0.42314 -0.00632 0.04517  0.22304  221 ASN   A N   
1704 C  CA  . ASN   A 221 ? 0.32369 0.38512 0.46882 -0.00463 0.04743  0.23911  221 ASN   A CA  
1705 C  C   . ASN   A 221 ? 0.35622 0.43998 0.49021 -0.00006 0.04660  0.25082  221 ASN   A C   
1706 O  O   . ASN   A 221 ? 0.32240 0.42030 0.43802 0.00159  0.04386  0.24467  221 ASN   A O   
1707 C  CB  . ASN   A 221 ? 0.36019 0.39974 0.51978 -0.00232 0.04651  0.23724  221 ASN   A CB  
1708 C  CG  . ASN   A 221 ? 0.35832 0.39412 0.50908 0.00181  0.04234  0.22493  221 ASN   A CG  
1709 O  OD1 . ASN   A 221 ? 0.38977 0.41293 0.53801 -0.00097 0.04096  0.21022  221 ASN   A OD1 
1710 N  ND2 . ASN   A 221 ? 0.36599 0.41430 0.51189 0.00793  0.04007  0.23122  221 ASN   A ND2 
1711 N  N   . ARG   A 222 ? 0.35346 0.44021 0.49880 0.00128  0.04895  0.26799  222 ARG   A N   
1712 C  CA  . ARG   A 222 ? 0.36460 0.47237 0.50185 0.00516  0.04769  0.28168  222 ARG   A CA  
1713 C  C   . ARG   A 222 ? 0.40231 0.50973 0.54287 0.01121  0.04331  0.28356  222 ARG   A C   
1714 O  O   . ARG   A 222 ? 0.48416 0.61137 0.61370 0.01387  0.04016  0.29055  222 ARG   A O   
1715 C  CB  . ARG   A 222 ? 0.42097 0.53321 0.57053 0.00409  0.05215  0.30129  222 ARG   A CB  
1716 C  CG  . ARG   A 222 ? 0.42146 0.51825 0.59452 0.00729  0.05294  0.31163  222 ARG   A CG  
1717 C  CD  . ARG   A 222 ? 0.42199 0.51912 0.60986 0.00516  0.05797  0.32981  222 ARG   A CD  
1718 N  NE  . ARG   A 222 ? 0.48529 0.60647 0.66643 0.00788  0.05763  0.34792  222 ARG   A NE  
1719 C  CZ  . ARG   A 222 ? 0.46466 0.59131 0.65613 0.00665  0.06180  0.36674  222 ARG   A CZ  
1720 N  NH1 . ARG   A 222 ? 0.47469 0.58472 0.68411 0.00237  0.06676  0.36979  222 ARG   A NH1 
1721 N  NH2 . ARG   A 222 ? 0.51127 0.66102 0.69463 0.00915  0.06075  0.38308  222 ARG   A NH2 
1722 N  N   . PHE   A 223 ? 0.42902 0.51506 0.58439 0.01314  0.04326  0.27762  223 PHE   A N   
1723 C  CA  . PHE   A 223 ? 0.42241 0.50846 0.58348 0.01939  0.04035  0.28030  223 PHE   A CA  
1724 C  C   . PHE   A 223 ? 0.38326 0.48210 0.52547 0.02082  0.03489  0.26922  223 PHE   A C   
1725 O  O   . PHE   A 223 ? 0.37780 0.47814 0.50453 0.01733  0.03370  0.25556  223 PHE   A O   
1726 C  CB  . PHE   A 223 ? 0.42664 0.48546 0.60525 0.02122  0.04253  0.27347  223 PHE   A CB  
1727 C  CG  . PHE   A 223 ? 0.45278 0.49108 0.64479 0.01641  0.04732  0.27302  223 PHE   A CG  
1728 C  CD1 . PHE   A 223 ? 0.49443 0.53014 0.70310 0.01659  0.05126  0.28976  223 PHE   A CD1 
1729 C  CD2 . PHE   A 223 ? 0.46982 0.49103 0.65867 0.01120  0.04756  0.25600  223 PHE   A CD2 
1730 C  CE1 . PHE   A 223 ? 0.50894 0.52487 0.73062 0.01110  0.05544  0.28893  223 PHE   A CE1 
1731 C  CE2 . PHE   A 223 ? 0.47869 0.48135 0.67989 0.00534  0.05118  0.25496  223 PHE   A CE2 
1732 C  CZ  . PHE   A 223 ? 0.53853 0.53803 0.75616 0.00509  0.05515  0.27104  223 PHE   A CZ  
1733 N  N   . THR   A 224 ? 0.38304 0.49113 0.52825 0.02590  0.03170  0.27571  224 THR   A N   
1734 C  CA  . THR   A 224 ? 0.35566 0.47277 0.48787 0.02745  0.02637  0.26554  224 THR   A CA  
1735 C  C   . THR   A 224 ? 0.36431 0.47011 0.51264 0.03310  0.02639  0.26535  224 THR   A C   
1736 O  O   . THR   A 224 ? 0.36665 0.45728 0.53502 0.03592  0.03081  0.27248  224 THR   A O   
1737 C  CB  . THR   A 224 ? 0.37601 0.52145 0.49246 0.02689  0.02168  0.27370  224 THR   A CB  
1738 O  OG1 . THR   A 224 ? 0.34588 0.49852 0.44388 0.02530  0.01690  0.25899  224 THR   A OG1 
1739 C  CG2 . THR   A 224 ? 0.34904 0.50626 0.47890 0.03166  0.01983  0.29159  224 THR   A CG2 
1740 N  N   . THR   A 225 ? 0.34168 0.45438 0.48141 0.03464  0.02196  0.25676  225 THR   A N   
1741 C  CA  . THR   A 225 ? 0.33582 0.44084 0.48943 0.04022  0.02225  0.25625  225 THR   A CA  
1742 C  C   . THR   A 225 ? 0.33744 0.46353 0.48043 0.04099  0.01582  0.25536  225 THR   A C   
1743 O  O   . THR   A 225 ? 0.32318 0.46361 0.44587 0.03653  0.01134  0.24941  225 THR   A O   
1744 C  CB  . THR   A 225 ? 0.32648 0.40529 0.48324 0.04026  0.02549  0.23950  225 THR   A CB  
1745 O  OG1 . THR   A 225 ? 0.35263 0.42159 0.52573 0.04643  0.02802  0.24098  225 THR   A OG1 
1746 C  CG2 . THR   A 225 ? 0.33883 0.42089 0.47578 0.03680  0.02143  0.22282  225 THR   A CG2 
1747 N  N   . THR   A 226 ? 0.34623 0.47395 0.50362 0.04643  0.01568  0.26124  226 THR   A N   
1748 C  CA  . THR   A 226 ? 0.33207 0.47766 0.48110 0.04647  0.00950  0.25870  226 THR   A CA  
1749 C  C   . THR   A 226 ? 0.31531 0.44710 0.45832 0.04622  0.00961  0.23980  226 THR   A C   
1750 O  O   . THR   A 226 ? 0.29076 0.39894 0.44031 0.04763  0.01487  0.23101  226 THR   A O   
1751 C  CB  . THR   A 226 ? 0.35661 0.51349 0.52441 0.05218  0.00898  0.27453  226 THR   A CB  
1752 O  OG1 . THR   A 226 ? 0.37384 0.50894 0.56397 0.05828  0.01646  0.27651  226 THR   A OG1 
1753 C  CG2 . THR   A 226 ? 0.36561 0.54303 0.53530 0.05150  0.00657  0.29412  226 THR   A CG2 
1754 N  N   . LEU   A 227 ? 0.30670 0.45356 0.43658 0.04385  0.00350  0.23356  227 LEU   A N   
1755 C  CA  . LEU   A 227 ? 0.31377 0.45024 0.43878 0.04383  0.00318  0.21744  227 LEU   A CA  
1756 C  C   . LEU   A 227 ? 0.32736 0.45012 0.47254 0.05060  0.00819  0.21879  227 LEU   A C   
1757 O  O   . LEU   A 227 ? 0.29263 0.39462 0.43883 0.05173  0.01228  0.20648  227 LEU   A O   
1758 C  CB  . LEU   A 227 ? 0.28745 0.44388 0.39724 0.03989  -0.00442 0.21268  227 LEU   A CB  
1759 C  CG  . LEU   A 227 ? 0.27946 0.42855 0.38088 0.03846  -0.00587 0.19595  227 LEU   A CG  
1760 C  CD1 . LEU   A 227 ? 0.28217 0.41166 0.37497 0.03636  -0.00239 0.18250  227 LEU   A CD1 
1761 C  CD2 . LEU   A 227 ? 0.25576 0.42487 0.34067 0.03296  -0.01364 0.19175  227 LEU   A CD2 
1762 N  N   . ASN   A 228 ? 0.35028 0.48443 0.51170 0.05522  0.00831  0.23381  228 ASN   A N   
1763 C  CA  . ASN   A 228 ? 0.33328 0.45441 0.51517 0.06243  0.01445  0.23561  228 ASN   A CA  
1764 C  C   . ASN   A 228 ? 0.35340 0.44699 0.54563 0.06512  0.02284  0.23259  228 ASN   A C   
1765 O  O   . ASN   A 228 ? 0.37476 0.44829 0.57261 0.06829  0.02830  0.22222  228 ASN   A O   
1766 C  CB  . ASN   A 228 ? 0.36578 0.50511 0.56551 0.06713  0.01355  0.25462  228 ASN   A CB  
1767 C  CG  . ASN   A 228 ? 0.37700 0.54278 0.56782 0.06387  0.00487  0.25696  228 ASN   A CG  
1768 O  OD1 . ASN   A 228 ? 0.42534 0.59083 0.60541 0.06142  0.00220  0.24368  228 ASN   A OD1 
1769 N  ND2 . ASN   A 228 ? 0.37000 0.55883 0.56528 0.06338  0.00019  0.27403  228 ASN   A ND2 
1770 N  N   . ASP   A 229 ? 0.34929 0.44122 0.54347 0.06337  0.02401  0.24103  229 ASP   A N   
1771 C  CA  . ASP   A 229 ? 0.35836 0.42370 0.56295 0.06476  0.03154  0.23837  229 ASP   A CA  
1772 C  C   . ASP   A 229 ? 0.34819 0.39467 0.53785 0.05976  0.03218  0.21918  229 ASP   A C   
1773 O  O   . ASP   A 229 ? 0.36176 0.38324 0.55793 0.06121  0.03808  0.21001  229 ASP   A O   
1774 C  CB  . ASP   A 229 ? 0.37968 0.44995 0.59152 0.06381  0.03238  0.25404  229 ASP   A CB  
1775 C  CG  . ASP   A 229 ? 0.45911 0.53626 0.69418 0.07067  0.03535  0.27295  229 ASP   A CG  
1776 O  OD1 . ASP   A 229 ? 0.43343 0.53600 0.66938 0.07202  0.03025  0.28450  229 ASP   A OD1 
1777 O  OD2 . ASP   A 229 ? 0.49959 0.55647 0.75250 0.07443  0.04277  0.27633  229 ASP   A OD2 
1778 N  N   . PHE   A 230 ? 0.31814 0.37596 0.48766 0.05371  0.02633  0.21251  230 PHE   A N   
1779 C  CA  . PHE   A 230 ? 0.31142 0.35327 0.46803 0.04932  0.02659  0.19510  230 PHE   A CA  
1780 C  C   . PHE   A 230 ? 0.30233 0.33283 0.45953 0.05241  0.02829  0.18285  230 PHE   A C   
1781 O  O   . PHE   A 230 ? 0.30393 0.31171 0.46095 0.05160  0.03219  0.17113  230 PHE   A O   
1782 C  CB  . PHE   A 230 ? 0.28193 0.33918 0.41792 0.04320  0.02057  0.19025  230 PHE   A CB  
1783 C  CG  . PHE   A 230 ? 0.25658 0.29957 0.38057 0.03905  0.02049  0.17342  230 PHE   A CG  
1784 C  CD1 . PHE   A 230 ? 0.25574 0.28251 0.38033 0.03514  0.02353  0.16950  230 PHE   A CD1 
1785 C  CD2 . PHE   A 230 ? 0.24617 0.29183 0.36008 0.03889  0.01740  0.16229  230 PHE   A CD2 
1786 C  CE1 . PHE   A 230 ? 0.27737 0.29218 0.39246 0.03102  0.02309  0.15540  230 PHE   A CE1 
1787 C  CE2 . PHE   A 230 ? 0.29078 0.32379 0.39493 0.03534  0.01731  0.14831  230 PHE   A CE2 
1788 C  CZ  . PHE   A 230 ? 0.19724 0.21524 0.30194 0.03140  0.02000  0.14504  230 PHE   A CZ  
1789 N  N   . ASN   A 231 ? 0.30138 0.34782 0.45924 0.05553  0.02542  0.18553  231 ASN   A N   
1790 C  CA  . ASN   A 231 ? 0.32143 0.35984 0.47824 0.05804  0.02689  0.17391  231 ASN   A CA  
1791 C  C   . ASN   A 231 ? 0.33589 0.35288 0.50934 0.06407  0.03550  0.17250  231 ASN   A C   
1792 O  O   . ASN   A 231 ? 0.31559 0.31782 0.48633 0.06531  0.03880  0.15960  231 ASN   A O   
1793 C  CB  . ASN   A 231 ? 0.29366 0.35516 0.44880 0.05927  0.02176  0.17800  231 ASN   A CB  
1794 C  CG  . ASN   A 231 ? 0.27370 0.34861 0.40837 0.05283  0.01427  0.17042  231 ASN   A CG  
1795 O  OD1 . ASN   A 231 ? 0.33329 0.39684 0.45609 0.04942  0.01408  0.15763  231 ASN   A OD1 
1796 N  ND2 . ASN   A 231 ? 0.28527 0.38419 0.41578 0.05087  0.00805  0.17802  231 ASN   A ND2 
1797 N  N   . LEU   A 232 ? 0.32208 0.33685 0.51248 0.06785  0.03963  0.18541  232 LEU   A N   
1798 C  CA  . LEU   A 232 ? 0.32515 0.31665 0.53134 0.07318  0.04880  0.18325  232 LEU   A CA  
1799 C  C   . LEU   A 232 ? 0.35649 0.32080 0.55537 0.06868  0.05207  0.16885  232 LEU   A C   
1800 O  O   . LEU   A 232 ? 0.36307 0.30570 0.56571 0.07117  0.05866  0.15814  232 LEU   A O   
1801 C  CB  . LEU   A 232 ? 0.32264 0.31784 0.54893 0.07758  0.05215  0.20134  232 LEU   A CB  
1802 C  CG  . LEU   A 232 ? 0.37327 0.38881 0.61441 0.08416  0.05201  0.21594  232 LEU   A CG  
1803 C  CD1 . LEU   A 232 ? 0.33183 0.34933 0.59300 0.08795  0.05535  0.23448  232 LEU   A CD1 
1804 C  CD2 . LEU   A 232 ? 0.35856 0.36588 0.60771 0.09040  0.05799  0.20863  232 LEU   A CD2 
1805 N  N   . VAL   A 233 ? 0.34387 0.30931 0.53225 0.06166  0.04775  0.16834  233 VAL   A N   
1806 C  CA  . VAL   A 233 ? 0.33350 0.27537 0.51461 0.05580  0.04954  0.15512  233 VAL   A CA  
1807 C  C   . VAL   A 233 ? 0.36033 0.29893 0.52429 0.05249  0.04661  0.13882  233 VAL   A C   
1808 O  O   . VAL   A 233 ? 0.36391 0.28024 0.52395 0.05035  0.04993  0.12483  233 VAL   A O   
1809 C  CB  . VAL   A 233 ? 0.36275 0.30876 0.54130 0.04951  0.04653  0.16216  233 VAL   A CB  
1810 C  CG1 . VAL   A 233 ? 0.36407 0.29114 0.53258 0.04148  0.04618  0.14826  233 VAL   A CG1 
1811 C  CG2 . VAL   A 233 ? 0.35456 0.29802 0.55171 0.05262  0.05080  0.17723  233 VAL   A CG2 
1812 N  N   . ALA   A 234 ? 0.32412 0.28469 0.47722 0.05158  0.04025  0.14021  234 ALA   A N   
1813 C  CA  . ALA   A 234 ? 0.33154 0.29095 0.47001 0.04920  0.03746  0.12657  234 ALA   A CA  
1814 C  C   . ALA   A 234 ? 0.33021 0.27547 0.47264 0.05412  0.04314  0.11716  234 ALA   A C   
1815 O  O   . ALA   A 234 ? 0.32203 0.25165 0.45514 0.05127  0.04436  0.10282  234 ALA   A O   
1816 C  CB  . ALA   A 234 ? 0.32773 0.31377 0.45705 0.04865  0.03049  0.13103  234 ALA   A CB  
1817 N  N   . MET   A 235 ? 0.35362 0.30519 0.50981 0.06135  0.04692  0.12533  235 MET   A N   
1818 C  CA  . MET   A 235 ? 0.36643 0.30641 0.52774 0.06687  0.05377  0.11738  235 MET   A CA  
1819 C  C   . MET   A 235 ? 0.37049 0.28034 0.53354 0.06598  0.06110  0.10637  235 MET   A C   
1820 O  O   . MET   A 235 ? 0.37760 0.27311 0.53245 0.06555  0.06465  0.09160  235 MET   A O   
1821 C  CB  . MET   A 235 ? 0.36064 0.31490 0.53915 0.07464  0.05663  0.13070  235 MET   A CB  
1822 C  CG  . MET   A 235 ? 0.39535 0.34208 0.58075 0.08119  0.06440  0.12435  235 MET   A CG  
1823 S  SD  . MET   A 235 ? 0.53169 0.50760 0.72993 0.08728  0.06250  0.13879  235 MET   A SD  
1824 C  CE  . MET   A 235 ? 0.39968 0.38099 0.61988 0.09179  0.06487  0.15865  235 MET   A CE  
1825 N  N   . LYS   A 236 ? 0.36542 0.26527 0.53780 0.06479  0.06321  0.11269  236 LYS   A N   
1826 C  CA  . LYS   A 236 ? 0.35786 0.22831 0.53250 0.06338  0.07010  0.10182  236 LYS   A CA  
1827 C  C   . LYS   A 236 ? 0.36806 0.22394 0.52447 0.05412  0.06673  0.08560  236 LYS   A C   
1828 O  O   . LYS   A 236 ? 0.37269 0.20524 0.52507 0.05214  0.07166  0.07155  236 LYS   A O   
1829 C  CB  . LYS   A 236 ? 0.37839 0.24174 0.56907 0.06407  0.07307  0.11351  236 LYS   A CB  
1830 C  CG  . LYS   A 236 ? 0.39308 0.22795 0.58206 0.05758  0.07601  0.10328  236 LYS   A CG  
1831 C  CD  . LYS   A 236 ? 0.40782 0.23765 0.61471 0.05861  0.07894  0.11718  236 LYS   A CD  
1832 C  CE  . LYS   A 236 ? 0.43384 0.23892 0.63760 0.04951  0.07933  0.10841  236 LYS   A CE  
1833 N  NZ  . LYS   A 236 ? 0.47784 0.29313 0.68178 0.04270  0.07332  0.11910  236 LYS   A NZ  
1834 N  N   . TYR   A 237 ? 0.33207 0.20200 0.47685 0.04829  0.05847  0.08674  237 TYR   A N   
1835 C  CA  . TYR   A 237 ? 0.33099 0.19051 0.46001 0.03902  0.05437  0.07349  237 TYR   A CA  
1836 C  C   . TYR   A 237 ? 0.31570 0.18405 0.43059 0.03857  0.05096  0.06493  237 TYR   A C   
1837 O  O   . TYR   A 237 ? 0.30625 0.17365 0.40902 0.03101  0.04576  0.05804  237 TYR   A O   
1838 C  CB  . TYR   A 237 ? 0.31491 0.18183 0.44292 0.03194  0.04855  0.08115  237 TYR   A CB  
1839 C  CG  . TYR   A 237 ? 0.34905 0.20126 0.48816 0.02921  0.05173  0.08548  237 TYR   A CG  
1840 C  CD1 . TYR   A 237 ? 0.36699 0.22709 0.52175 0.03483  0.05447  0.10137  237 TYR   A CD1 
1841 C  CD2 . TYR   A 237 ? 0.37181 0.20254 0.50602 0.02037  0.05163  0.07391  237 TYR   A CD2 
1842 C  CE1 . TYR   A 237 ? 0.38118 0.22717 0.54727 0.03249  0.05777  0.10605  237 TYR   A CE1 
1843 C  CE2 . TYR   A 237 ? 0.35791 0.17427 0.50285 0.01726  0.05446  0.07777  237 TYR   A CE2 
1844 C  CZ  . TYR   A 237 ? 0.39525 0.21887 0.55663 0.02373  0.05792  0.09412  237 TYR   A CZ  
1845 O  OH  . TYR   A 237 ? 0.43376 0.24294 0.60724 0.02092  0.06113  0.09914  237 TYR   A OH  
1846 N  N   . ASN   A 238 ? 0.31046 0.18768 0.42787 0.04621  0.05395  0.06573  238 ASN   A N   
1847 C  CA  . ASN   A 238 ? 0.32432 0.20872 0.42950 0.04612  0.05170  0.05759  238 ASN   A CA  
1848 C  C   . ASN   A 238 ? 0.26065 0.16446 0.35827 0.04226  0.04289  0.06335  238 ASN   A C   
1849 O  O   . ASN   A 238 ? 0.31431 0.21802 0.39954 0.03818  0.03956  0.05491  238 ASN   A O   
1850 C  CB  . ASN   A 238 ? 0.31634 0.17979 0.40817 0.04077  0.05400  0.03922  238 ASN   A CB  
1851 C  CG  . ASN   A 238 ? 0.36830 0.23692 0.45113 0.04367  0.05567  0.03123  238 ASN   A CG  
1852 O  OD1 . ASN   A 238 ? 0.38917 0.27387 0.47926 0.05083  0.05698  0.03904  238 ASN   A OD1 
1853 N  ND2 . ASN   A 238 ? 0.39836 0.25590 0.46514 0.03718  0.05473  0.01655  238 ASN   A ND2 
1854 N  N   . TYR   A 239 ? 0.25553 0.17559 0.36001 0.04310  0.03943  0.07742  239 TYR   A N   
1855 C  CA  . TYR   A 239 ? 0.25253 0.19403 0.34990 0.04048  0.03194  0.08366  239 TYR   A CA  
1856 C  C   . TYR   A 239 ? 0.23420 0.19695 0.33527 0.04618  0.03024  0.09113  239 TYR   A C   
1857 O  O   . TYR   A 239 ? 0.23335 0.19881 0.34699 0.05192  0.03413  0.09810  239 TYR   A O   
1858 C  CB  . TYR   A 239 ? 0.22749 0.17542 0.32778 0.03679  0.02944  0.09367  239 TYR   A CB  
1859 C  CG  . TYR   A 239 ? 0.19492 0.13207 0.28894 0.02866  0.02779  0.08808  239 TYR   A CG  
1860 C  CD1 . TYR   A 239 ? 0.23559 0.14883 0.32975 0.02482  0.03103  0.07744  239 TYR   A CD1 
1861 C  CD2 . TYR   A 239 ? 0.23875 0.19078 0.32644 0.02408  0.02300  0.09288  239 TYR   A CD2 
1862 C  CE1 . TYR   A 239 ? 0.25310 0.15874 0.34292 0.01591  0.02854  0.07278  239 TYR   A CE1 
1863 C  CE2 . TYR   A 239 ? 0.22418 0.16894 0.30878 0.01641  0.02182  0.08898  239 TYR   A CE2 
1864 C  CZ  . TYR   A 239 ? 0.23240 0.15462 0.31899 0.01201  0.02409  0.07944  239 TYR   A CZ  
1865 O  OH  . TYR   A 239 ? 0.23020 0.14787 0.31522 0.00324  0.02195  0.07595  239 TYR   A OH  
1866 N  N   . GLU   A 240 ? 0.21939 0.19736 0.31038 0.04400  0.02432  0.08983  240 GLU   A N   
1867 C  CA  . GLU   A 240 ? 0.26817 0.26544 0.36308 0.04797  0.02234  0.09555  240 GLU   A CA  
1868 C  C   . GLU   A 240 ? 0.25484 0.27195 0.35215 0.04693  0.01793  0.10814  240 GLU   A C   
1869 O  O   . GLU   A 240 ? 0.23368 0.25185 0.32659 0.04293  0.01599  0.11139  240 GLU   A O   
1870 C  CB  . GLU   A 240 ? 0.29663 0.30192 0.38084 0.04611  0.01814  0.08801  240 GLU   A CB  
1871 C  CG  . GLU   A 240 ? 0.24430 0.25813 0.31530 0.03993  0.01155  0.08601  240 GLU   A CG  
1872 C  CD  . GLU   A 240 ? 0.30364 0.31982 0.36598 0.03859  0.00888  0.07716  240 GLU   A CD  
1873 O  OE1 . GLU   A 240 ? 0.38647 0.40271 0.45403 0.04268  0.01166  0.07467  240 GLU   A OE1 
1874 O  OE2 . GLU   A 240 ? 0.32427 0.34278 0.37552 0.03360  0.00462  0.07311  240 GLU   A OE2 
1875 N  N   . PRO   A 241 ? 0.22824 0.26130 0.33337 0.05034  0.01688  0.11592  241 PRO   A N   
1876 C  CA  . PRO   A 241 ? 0.24741 0.29898 0.35525 0.04930  0.01303  0.12849  241 PRO   A CA  
1877 C  C   . PRO   A 241 ? 0.23657 0.30163 0.32808 0.04255  0.00606  0.12657  241 PRO   A C   
1878 O  O   . PRO   A 241 ? 0.26503 0.33135 0.34454 0.03910  0.00278  0.11671  241 PRO   A O   
1879 C  CB  . PRO   A 241 ? 0.23544 0.30188 0.35340 0.05315  0.01233  0.13511  241 PRO   A CB  
1880 C  CG  . PRO   A 241 ? 0.25912 0.31126 0.38403 0.05802  0.01862  0.12772  241 PRO   A CG  
1881 C  CD  . PRO   A 241 ? 0.27791 0.31222 0.39109 0.05531  0.01997  0.11417  241 PRO   A CD  
1882 N  N   . LEU   A 242 ? 0.25654 0.33121 0.34799 0.04087  0.00454  0.13613  242 LEU   A N   
1883 C  CA  . LEU   A 242 ? 0.24689 0.33622 0.32321 0.03499  -0.00092 0.13551  242 LEU   A CA  
1884 C  C   . LEU   A 242 ? 0.24587 0.35781 0.32192 0.03420  -0.00610 0.14309  242 LEU   A C   
1885 O  O   . LEU   A 242 ? 0.24325 0.36216 0.33199 0.03766  -0.00515 0.15566  242 LEU   A O   
1886 C  CB  . LEU   A 242 ? 0.23521 0.32135 0.31076 0.03328  0.00126  0.14131  242 LEU   A CB  
1887 C  CG  . LEU   A 242 ? 0.22295 0.31715 0.28141 0.02739  -0.00165 0.13667  242 LEU   A CG  
1888 C  CD1 . LEU   A 242 ? 0.22442 0.30570 0.27435 0.02488  -0.00099 0.12314  242 LEU   A CD1 
1889 C  CD2 . LEU   A 242 ? 0.20817 0.30413 0.26905 0.02653  0.00085  0.14647  242 LEU   A CD2 
1890 N  N   . THR   A 243 ? 0.24246 0.36538 0.30474 0.02934  -0.01161 0.13552  243 THR   A N   
1891 C  CA  . THR   A 243 ? 0.27378 0.41771 0.33379 0.02688  -0.01753 0.14072  243 THR   A CA  
1892 C  C   . THR   A 243 ? 0.26498 0.42196 0.31118 0.02183  -0.02097 0.14345  243 THR   A C   
1893 O  O   . THR   A 243 ? 0.27029 0.42056 0.30712 0.01988  -0.01873 0.13922  243 THR   A O   
1894 C  CB  . THR   A 243 ? 0.24767 0.39510 0.30164 0.02387  -0.02153 0.13012  243 THR   A CB  
1895 O  OG1 . THR   A 243 ? 0.26591 0.40959 0.30247 0.01850  -0.02325 0.11737  243 THR   A OG1 
1896 C  CG2 . THR   A 243 ? 0.28002 0.41457 0.34644 0.02907  -0.01727 0.12707  243 THR   A CG2 
1897 N  N   . GLN   A 244 ? 0.24237 0.41900 0.28749 0.01962  -0.02632 0.15108  244 GLN   A N   
1898 C  CA  . GLN   A 244 ? 0.27698 0.46739 0.30562 0.01400  -0.03020 0.15176  244 GLN   A CA  
1899 C  C   . GLN   A 244 ? 0.28367 0.47028 0.29304 0.00826  -0.03186 0.13509  244 GLN   A C   
1900 O  O   . GLN   A 244 ? 0.28710 0.47544 0.28200 0.00498  -0.03108 0.13182  244 GLN   A O   
1901 C  CB  . GLN   A 244 ? 0.24343 0.45603 0.27328 0.01175  -0.03676 0.16181  244 GLN   A CB  
1902 C  CG  . GLN   A 244 ? 0.27304 0.50050 0.28502 0.00605  -0.04060 0.16374  244 GLN   A CG  
1903 C  CD  . GLN   A 244 ? 0.29136 0.51529 0.30344 0.00844  -0.03548 0.17195  244 GLN   A CD  
1904 O  OE1 . GLN   A 244 ? 0.29370 0.51282 0.32361 0.01425  -0.03146 0.18390  244 GLN   A OE1 
1905 N  NE2 . GLN   A 244 ? 0.32145 0.54688 0.31411 0.00398  -0.03497 0.16535  244 GLN   A NE2 
1906 N  N   . ASP   A 245 ? 0.28342 0.46427 0.29307 0.00728  -0.03336 0.12460  245 ASP   A N   
1907 C  CA  . ASP   A 245 ? 0.29237 0.46773 0.28589 0.00226  -0.03425 0.10879  245 ASP   A CA  
1908 C  C   . ASP   A 245 ? 0.26937 0.42871 0.25968 0.00401  -0.02824 0.10295  245 ASP   A C   
1909 O  O   . ASP   A 245 ? 0.28486 0.44307 0.26038 0.00026  -0.02750 0.09422  245 ASP   A O   
1910 C  CB  . ASP   A 245 ? 0.27006 0.44308 0.26646 0.00075  -0.03719 0.10019  245 ASP   A CB  
1911 C  CG  . ASP   A 245 ? 0.32423 0.49422 0.30428 -0.00538 -0.03908 0.08478  245 ASP   A CG  
1912 O  OD1 . ASP   A 245 ? 0.37396 0.55526 0.34154 -0.01104 -0.04340 0.08220  245 ASP   A OD1 
1913 O  OD2 . ASP   A 245 ? 0.39122 0.54747 0.37088 -0.00468 -0.03624 0.07524  245 ASP   A OD2 
1914 N  N   . HIS   A 246 ? 0.25991 0.40652 0.26398 0.00949  -0.02367 0.10731  246 HIS   A N   
1915 C  CA  . HIS   A 246 ? 0.24331 0.37652 0.24587 0.01063  -0.01841 0.10471  246 HIS   A CA  
1916 C  C   . HIS   A 246 ? 0.25182 0.39222 0.24772 0.00914  -0.01668 0.11126  246 HIS   A C   
1917 O  O   . HIS   A 246 ? 0.26107 0.39770 0.24733 0.00698  -0.01387 0.10549  246 HIS   A O   
1918 C  CB  . HIS   A 246 ? 0.24275 0.36127 0.26164 0.01616  -0.01406 0.10977  246 HIS   A CB  
1919 C  CG  . HIS   A 246 ? 0.22794 0.33704 0.25245 0.01818  -0.01416 0.10279  246 HIS   A CG  
1920 N  ND1 . HIS   A 246 ? 0.26392 0.36477 0.30376 0.02359  -0.01120 0.10794  246 HIS   A ND1 
1921 C  CD2 . HIS   A 246 ? 0.26146 0.36802 0.27867 0.01573  -0.01628 0.09124  246 HIS   A CD2 
1922 C  CE1 . HIS   A 246 ? 0.26664 0.36110 0.30752 0.02447  -0.01140 0.09998  246 HIS   A CE1 
1923 N  NE2 . HIS   A 246 ? 0.24822 0.34631 0.27589 0.01960  -0.01482 0.09027  246 HIS   A NE2 
1924 N  N   . VAL   A 247 ? 0.27614 0.42749 0.27803 0.01053  -0.01783 0.12425  247 VAL   A N   
1925 C  CA  . VAL   A 247 ? 0.24755 0.40744 0.24282 0.00906  -0.01630 0.13184  247 VAL   A CA  
1926 C  C   . VAL   A 247 ? 0.30144 0.47105 0.27527 0.00337  -0.01849 0.12267  247 VAL   A C   
1927 O  O   . VAL   A 247 ? 0.29052 0.45903 0.25448 0.00174  -0.01454 0.12024  247 VAL   A O   
1928 C  CB  . VAL   A 247 ? 0.28617 0.45802 0.29193 0.01145  -0.01799 0.14829  247 VAL   A CB  
1929 C  CG1 . VAL   A 247 ? 0.29491 0.47918 0.29039 0.00897  -0.01759 0.15589  247 VAL   A CG1 
1930 C  CG2 . VAL   A 247 ? 0.26655 0.42522 0.29309 0.01728  -0.01346 0.15667  247 VAL   A CG2 
1931 N  N   . ASP   A 248 ? 0.27954 0.45794 0.24621 0.00009  -0.02426 0.11690  248 ASP   A N   
1932 C  CA  . ASP   A 248 ? 0.30739 0.49259 0.25309 -0.00581 -0.02617 0.10621  248 ASP   A CA  
1933 C  C   . ASP   A 248 ? 0.30984 0.48155 0.24777 -0.00674 -0.02163 0.09192  248 ASP   A C   
1934 O  O   . ASP   A 248 ? 0.33169 0.50486 0.25467 -0.00932 -0.01831 0.08630  248 ASP   A O   
1935 C  CB  . ASP   A 248 ? 0.30178 0.49655 0.24368 -0.00977 -0.03354 0.10193  248 ASP   A CB  
1936 C  CG  . ASP   A 248 ? 0.29790 0.51004 0.24556 -0.00978 -0.03860 0.11669  248 ASP   A CG  
1937 O  OD1 . ASP   A 248 ? 0.32528 0.54431 0.27431 -0.00795 -0.03676 0.12909  248 ASP   A OD1 
1938 O  OD2 . ASP   A 248 ? 0.28795 0.50761 0.23991 -0.01168 -0.04447 0.11678  248 ASP   A OD2 
1939 N  N   . ILE   A 249 ? 0.29556 0.45447 0.24343 -0.00449 -0.02095 0.08625  249 ILE   A N   
1940 C  CA  . ILE   A 249 ? 0.28938 0.43647 0.23171 -0.00520 -0.01706 0.07378  249 ILE   A CA  
1941 C  C   . ILE   A 249 ? 0.27926 0.42196 0.22150 -0.00342 -0.01023 0.07752  249 ILE   A C   
1942 O  O   . ILE   A 249 ? 0.29650 0.43560 0.22947 -0.00493 -0.00591 0.06856  249 ILE   A O   
1943 C  CB  . ILE   A 249 ? 0.25849 0.39402 0.21236 -0.00298 -0.01818 0.06935  249 ILE   A CB  
1944 C  CG1 . ILE   A 249 ? 0.31835 0.45769 0.26920 -0.00627 -0.02382 0.06174  249 ILE   A CG1 
1945 C  CG2 . ILE   A 249 ? 0.28110 0.40429 0.23429 -0.00225 -0.01362 0.06158  249 ILE   A CG2 
1946 C  CD1 . ILE   A 249 ? 0.31574 0.44871 0.28099 -0.00330 -0.02555 0.06314  249 ILE   A CD1 
1947 N  N   . LEU   A 250 ? 0.27468 0.41783 0.22824 -0.00033 -0.00858 0.09096  250 LEU   A N   
1948 C  CA  . LEU   A 250 ? 0.29160 0.43126 0.24767 0.00071  -0.00224 0.09645  250 LEU   A CA  
1949 C  C   . LEU   A 250 ? 0.27180 0.42387 0.21480 -0.00154 0.00012  0.10027  250 LEU   A C   
1950 O  O   . LEU   A 250 ? 0.24319 0.39402 0.18777 -0.00110 0.00607  0.10506  250 LEU   A O   
1951 C  CB  . LEU   A 250 ? 0.23472 0.36710 0.20977 0.00447  -0.00122 0.10861  250 LEU   A CB  
1952 C  CG  . LEU   A 250 ? 0.20343 0.32032 0.19051 0.00673  -0.00144 0.10458  250 LEU   A CG  
1953 C  CD1 . LEU   A 250 ? 0.18070 0.28985 0.18533 0.01033  -0.00031 0.11561  250 LEU   A CD1 
1954 C  CD2 . LEU   A 250 ? 0.20648 0.31383 0.19210 0.00532  0.00275  0.09723  250 LEU   A CD2 
1955 N  N   . GLY   A 251 ? 0.27978 0.44373 0.20968 -0.00444 -0.00423 0.09809  251 GLY   A N   
1956 C  CA  . GLY   A 251 ? 0.28981 0.46592 0.20433 -0.00705 -0.00240 0.10116  251 GLY   A CA  
1957 C  C   . GLY   A 251 ? 0.30418 0.47710 0.20718 -0.00816 0.00591  0.09367  251 GLY   A C   
1958 O  O   . GLY   A 251 ? 0.31470 0.49221 0.21616 -0.00775 0.01121  0.10209  251 GLY   A O   
1959 N  N   . PRO   A 252 ? 0.31085 0.47623 0.20642 -0.00947 0.00792  0.07805  252 PRO   A N   
1960 C  CA  . PRO   A 252 ? 0.32364 0.48612 0.21000 -0.00979 0.01741  0.07056  252 PRO   A CA  
1961 C  C   . PRO   A 252 ? 0.30815 0.46601 0.20947 -0.00688 0.02409  0.07897  252 PRO   A C   
1962 O  O   . PRO   A 252 ? 0.32360 0.48575 0.21981 -0.00709 0.03183  0.08188  252 PRO   A O   
1963 C  CB  . PRO   A 252 ? 0.32844 0.48171 0.21055 -0.01070 0.01754  0.05350  252 PRO   A CB  
1964 C  CG  . PRO   A 252 ? 0.31849 0.47467 0.19713 -0.01327 0.00793  0.05047  252 PRO   A CG  
1965 C  CD  . PRO   A 252 ? 0.33883 0.50009 0.23192 -0.01126 0.00213  0.06627  252 PRO   A CD  
1966 N  N   . LEU   A 253 ? 0.29533 0.44433 0.21508 -0.00461 0.02157  0.08275  253 LEU   A N   
1967 C  CA  . LEU   A 253 ? 0.28197 0.42570 0.21751 -0.00298 0.02691  0.09068  253 LEU   A CA  
1968 C  C   . LEU   A 253 ? 0.26910 0.41934 0.20946 -0.00273 0.02783  0.10616  253 LEU   A C   
1969 O  O   . LEU   A 253 ? 0.26153 0.41312 0.20651 -0.00300 0.03467  0.11173  253 LEU   A O   
1970 C  CB  . LEU   A 253 ? 0.24166 0.37338 0.19389 -0.00141 0.02313  0.09097  253 LEU   A CB  
1971 C  CG  . LEU   A 253 ? 0.24972 0.37397 0.20221 -0.00143 0.02387  0.07836  253 LEU   A CG  
1972 C  CD1 . LEU   A 253 ? 0.22357 0.33645 0.19110 -0.00030 0.01965  0.08106  253 LEU   A CD1 
1973 C  CD2 . LEU   A 253 ? 0.26344 0.38848 0.21813 -0.00168 0.03286  0.07493  253 LEU   A CD2 
1974 N  N   . SER   A 254 ? 0.25233 0.40751 0.19316 -0.00222 0.02122  0.11376  254 SER   A N   
1975 C  CA  . SER   A 254 ? 0.27849 0.44213 0.22230 -0.00189 0.02170  0.12895  254 SER   A CA  
1976 C  C   . SER   A 254 ? 0.28984 0.46480 0.21623 -0.00416 0.02750  0.12916  254 SER   A C   
1977 O  O   . SER   A 254 ? 0.30491 0.48299 0.23614 -0.00414 0.03298  0.13943  254 SER   A O   
1978 C  CB  . SER   A 254 ? 0.29326 0.46340 0.23842 -0.00102 0.01364  0.13533  254 SER   A CB  
1979 O  OG  . SER   A 254 ? 0.31540 0.49225 0.26855 0.00018  0.01383  0.15189  254 SER   A OG  
1980 N  N   . ALA   A 255 ? 0.31074 0.49137 0.21640 -0.00646 0.02675  0.11759  255 ALA   A N   
1981 C  CA  . ALA   A 255 ? 0.33003 0.52083 0.21611 -0.00878 0.03268  0.11691  255 ALA   A CA  
1982 C  C   . ALA   A 255 ? 0.32811 0.51442 0.21489 -0.00839 0.04406  0.11224  255 ALA   A C   
1983 O  O   . ALA   A 255 ? 0.35704 0.55095 0.23542 -0.00933 0.05137  0.11737  255 ALA   A O   
1984 C  CB  . ALA   A 255 ? 0.32101 0.51658 0.18445 -0.01190 0.02902  0.10405  255 ALA   A CB  
1985 N  N   . GLN   A 256 ? 0.33151 0.50667 0.22919 -0.00702 0.04601  0.10329  256 GLN   A N   
1986 C  CA  . GLN   A 256 ? 0.33305 0.50531 0.23577 -0.00641 0.05678  0.09942  256 GLN   A CA  
1987 C  C   . GLN   A 256 ? 0.32739 0.50002 0.24981 -0.00588 0.05987  0.11444  256 GLN   A C   
1988 O  O   . GLN   A 256 ? 0.39124 0.56857 0.31445 -0.00637 0.06929  0.11728  256 GLN   A O   
1989 C  CB  . GLN   A 256 ? 0.33726 0.49913 0.24728 -0.00515 0.05704  0.08636  256 GLN   A CB  
1990 C  CG  . GLN   A 256 ? 0.38691 0.54751 0.30273 -0.00412 0.06848  0.08035  256 GLN   A CG  
1991 C  CD  . GLN   A 256 ? 0.35584 0.50733 0.28598 -0.00250 0.06740  0.07230  256 GLN   A CD  
1992 O  OE1 . GLN   A 256 ? 0.38800 0.53359 0.31744 -0.00240 0.05909  0.06768  256 GLN   A OE1 
1993 N  NE2 . GLN   A 256 ? 0.38229 0.53370 0.32699 -0.00128 0.07558  0.07139  256 GLN   A NE2 
1994 N  N   . THR   A 257 ? 0.33073 0.49790 0.26973 -0.00508 0.05257  0.12396  257 THR   A N   
1995 C  CA  . THR   A 257 ? 0.30508 0.46984 0.26393 -0.00522 0.05483  0.13743  257 THR   A CA  
1996 C  C   . THR   A 257 ? 0.30041 0.47406 0.25725 -0.00550 0.05407  0.15265  257 THR   A C   
1997 O  O   . THR   A 257 ? 0.33018 0.50378 0.30087 -0.00617 0.05785  0.16417  257 THR   A O   
1998 C  CB  . THR   A 257 ? 0.29596 0.44704 0.27477 -0.00442 0.04872  0.13868  257 THR   A CB  
1999 O  OG1 . THR   A 257 ? 0.26644 0.41601 0.24183 -0.00289 0.04031  0.13954  257 THR   A OG1 
2000 C  CG2 . THR   A 257 ? 0.25697 0.40048 0.23970 -0.00452 0.04993  0.12564  257 THR   A CG2 
2001 N  N   . GLY   A 258 ? 0.31681 0.49858 0.25805 -0.00535 0.04893  0.15350  258 GLY   A N   
2002 C  CA  . GLY   A 258 ? 0.30187 0.49319 0.24301 -0.00532 0.04712  0.16935  258 GLY   A CA  
2003 C  C   . GLY   A 258 ? 0.29341 0.47749 0.25687 -0.00324 0.04177  0.18135  258 GLY   A C   
2004 O  O   . GLY   A 258 ? 0.30867 0.49865 0.27842 -0.00290 0.04222  0.19671  258 GLY   A O   
2005 N  N   . ILE   A 259 ? 0.29224 0.46302 0.26796 -0.00178 0.03744  0.17474  259 ILE   A N   
2006 C  CA  . ILE   A 259 ? 0.29624 0.45740 0.29251 0.00046  0.03345  0.18375  259 ILE   A CA  
2007 C  C   . ILE   A 259 ? 0.29425 0.45745 0.28650 0.00255  0.02566  0.18060  259 ILE   A C   
2008 O  O   . ILE   A 259 ? 0.27902 0.43774 0.26499 0.00245  0.02284  0.16718  259 ILE   A O   
2009 C  CB  . ILE   A 259 ? 0.26530 0.40859 0.27912 -0.00000 0.03522  0.17867  259 ILE   A CB  
2010 C  CG1 . ILE   A 259 ? 0.31784 0.46064 0.33953 -0.00275 0.04246  0.18376  259 ILE   A CG1 
2011 C  CG2 . ILE   A 259 ? 0.24377 0.37429 0.27594 0.00234  0.03146  0.18439  259 ILE   A CG2 
2012 C  CD1 . ILE   A 259 ? 0.27012 0.39971 0.30329 -0.00468 0.04384  0.17499  259 ILE   A CD1 
2013 N  N   . ALA   A 260 ? 0.27300 0.44419 0.26972 0.00434  0.02234  0.19360  260 ALA   A N   
2014 C  CA  . ALA   A 260 ? 0.29468 0.47045 0.28979 0.00612  0.01513  0.19220  260 ALA   A CA  
2015 C  C   . ALA   A 260 ? 0.25299 0.41161 0.26258 0.00854  0.01334  0.18488  260 ALA   A C   
2016 O  O   . ALA   A 260 ? 0.26296 0.40636 0.28846 0.00952  0.01678  0.18671  260 ALA   A O   
2017 C  CB  . ALA   A 260 ? 0.28800 0.47541 0.29026 0.00805  0.01260  0.20985  260 ALA   A CB  
2018 N  N   . VAL   A 261 ? 0.27093 0.43172 0.27418 0.00889  0.00805  0.17600  261 VAL   A N   
2019 C  CA  . VAL   A 261 ? 0.25135 0.39664 0.26580 0.01110  0.00677  0.16831  261 VAL   A CA  
2020 C  C   . VAL   A 261 ? 0.23813 0.37356 0.27447 0.01509  0.00811  0.17937  261 VAL   A C   
2021 O  O   . VAL   A 261 ? 0.24298 0.36016 0.29106 0.01597  0.01113  0.17584  261 VAL   A O   
2022 C  CB  . VAL   A 261 ? 0.26831 0.41985 0.27364 0.01074  0.00083  0.15922  261 VAL   A CB  
2023 C  CG1 . VAL   A 261 ? 0.19826 0.33474 0.21633 0.01367  0.00003  0.15366  261 VAL   A CG1 
2024 C  CG2 . VAL   A 261 ? 0.24235 0.39880 0.22709 0.00664  0.00048  0.14571  261 VAL   A CG2 
2025 N  N   . LEU   A 262 ? 0.25719 0.40418 0.29942 0.01729  0.00616  0.19293  262 LEU   A N   
2026 C  CA  . LEU   A 262 ? 0.26853 0.40575 0.33280 0.02167  0.00842  0.20387  262 LEU   A CA  
2027 C  C   . LEU   A 262 ? 0.25700 0.38194 0.33182 0.02094  0.01435  0.20974  262 LEU   A C   
2028 O  O   . LEU   A 262 ? 0.25767 0.36614 0.35042 0.02358  0.01744  0.21291  262 LEU   A O   
2029 C  CB  . LEU   A 262 ? 0.27013 0.42437 0.34001 0.02426  0.00533  0.21916  262 LEU   A CB  
2030 C  CG  . LEU   A 262 ? 0.28516 0.44903 0.35526 0.02613  -0.00017 0.21773  262 LEU   A CG  
2031 C  CD1 . LEU   A 262 ? 0.30339 0.44899 0.38282 0.02899  0.00125  0.20693  262 LEU   A CD1 
2032 C  CD2 . LEU   A 262 ? 0.33123 0.51313 0.37920 0.02143  -0.00604 0.21084  262 LEU   A CD2 
2033 N  N   . ASP   A 263 ? 0.25877 0.39103 0.32317 0.01716  0.01647  0.21118  263 ASP   A N   
2034 C  CA  . ASP   A 263 ? 0.28185 0.40226 0.35683 0.01539  0.02211  0.21546  263 ASP   A CA  
2035 C  C   . ASP   A 263 ? 0.24849 0.34836 0.32815 0.01362  0.02388  0.20178  263 ASP   A C   
2036 O  O   . ASP   A 263 ? 0.25264 0.33552 0.34784 0.01306  0.02718  0.20372  263 ASP   A O   
2037 C  CB  . ASP   A 263 ? 0.27432 0.40835 0.33660 0.01167  0.02474  0.21936  263 ASP   A CB  
2038 C  CG  . ASP   A 263 ? 0.32684 0.47913 0.38689 0.01270  0.02408  0.23596  263 ASP   A CG  
2039 O  OD1 . ASP   A 263 ? 0.32451 0.48094 0.39331 0.01632  0.02091  0.24501  263 ASP   A OD1 
2040 O  OD2 . ASP   A 263 ? 0.34894 0.51203 0.39866 0.00983  0.02718  0.24040  263 ASP   A OD2 
2041 N  N   . MET   A 264 ? 0.23218 0.33322 0.29830 0.01219  0.02155  0.18778  264 MET   A N   
2042 C  CA  . MET   A 264 ? 0.21783 0.30178 0.28691 0.00998  0.02269  0.17530  264 MET   A CA  
2043 C  C   . MET   A 264 ? 0.22820 0.29532 0.30902 0.01310  0.02161  0.17186  264 MET   A C   
2044 O  O   . MET   A 264 ? 0.21222 0.26036 0.30237 0.01130  0.02368  0.16654  264 MET   A O   
2045 C  CB  . MET   A 264 ? 0.20352 0.29478 0.25522 0.00819  0.02062  0.16260  264 MET   A CB  
2046 C  CG  . MET   A 264 ? 0.24064 0.31919 0.29318 0.00513  0.02176  0.15070  264 MET   A CG  
2047 S  SD  . MET   A 264 ? 0.21329 0.28608 0.27662 0.00016  0.02722  0.15465  264 MET   A SD  
2048 C  CE  . MET   A 264 ? 0.19338 0.28472 0.23937 -0.00154 0.02966  0.15024  264 MET   A CE  
2049 N  N   . CYS   A 265 ? 0.21475 0.28904 0.29519 0.01744  0.01859  0.17473  265 CYS   A N   
2050 C  CA  . CYS   A 265 ? 0.21642 0.27674 0.31026 0.02166  0.01919  0.17457  265 CYS   A CA  
2051 C  C   . CYS   A 265 ? 0.23276 0.27872 0.34442 0.02239  0.02389  0.18320  265 CYS   A C   
2052 O  O   . CYS   A 265 ? 0.23451 0.25944 0.35573 0.02301  0.02642  0.17715  265 CYS   A O   
2053 C  CB  . CYS   A 265 ? 0.24611 0.32137 0.33963 0.02607  0.01575  0.18041  265 CYS   A CB  
2054 S  SG  . CYS   A 265 ? 0.22176 0.30897 0.29760 0.02500  0.01005  0.16829  265 CYS   A SG  
2055 N  N   . ALA   A 266 ? 0.24730 0.30370 0.36308 0.02205  0.02529  0.19703  266 ALA   A N   
2056 C  CA  . ALA   A 266 ? 0.26473 0.30706 0.39808 0.02212  0.02993  0.20564  266 ALA   A CA  
2057 C  C   . ALA   A 266 ? 0.26236 0.28568 0.39808 0.01632  0.03247  0.19606  266 ALA   A C   
2058 O  O   . ALA   A 266 ? 0.27459 0.27674 0.42358 0.01587  0.03561  0.19436  266 ALA   A O   
2059 C  CB  . ALA   A 266 ? 0.28665 0.34544 0.42270 0.02217  0.03085  0.22287  266 ALA   A CB  
2060 N  N   . SER   A 267 ? 0.25027 0.28085 0.37342 0.01146  0.03120  0.18925  267 SER   A N   
2061 C  CA  . SER   A 267 ? 0.24735 0.26298 0.37339 0.00516  0.03277  0.18039  267 SER   A CA  
2062 C  C   . SER   A 267 ? 0.26795 0.26417 0.39422 0.00478  0.03154  0.16590  267 SER   A C   
2063 O  O   . SER   A 267 ? 0.27910 0.25522 0.41419 0.00075  0.03328  0.16065  267 SER   A O   
2064 C  CB  . SER   A 267 ? 0.23606 0.26639 0.34963 0.00109  0.03209  0.17684  267 SER   A CB  
2065 O  OG  . SER   A 267 ? 0.24765 0.29301 0.36128 0.00036  0.03457  0.18938  267 SER   A OG  
2066 N  N   . LEU   A 268 ? 0.23639 0.23838 0.35210 0.00827  0.02846  0.15886  268 LEU   A N   
2067 C  CA  . LEU   A 268 ? 0.25251 0.23719 0.36743 0.00857  0.02765  0.14580  268 LEU   A CA  
2068 C  C   . LEU   A 268 ? 0.27104 0.23708 0.39931 0.01200  0.03103  0.14724  268 LEU   A C   
2069 O  O   . LEU   A 268 ? 0.28992 0.23439 0.42121 0.00904  0.03243  0.13700  268 LEU   A O   
2070 C  CB  . LEU   A 268 ? 0.26812 0.26461 0.37053 0.01229  0.02404  0.14031  268 LEU   A CB  
2071 C  CG  . LEU   A 268 ? 0.24913 0.23167 0.34830 0.01333  0.02307  0.12732  268 LEU   A CG  
2072 C  CD1 . LEU   A 268 ? 0.22673 0.19180 0.32590 0.00651  0.02336  0.11662  268 LEU   A CD1 
2073 C  CD2 . LEU   A 268 ? 0.19644 0.19412 0.28258 0.01541  0.01911  0.12306  268 LEU   A CD2 
2074 N  N   . LYS   A 269 ? 0.26002 0.23423 0.39621 0.01802  0.03249  0.15957  269 LYS   A N   
2075 C  CA  . LYS   A 269 ? 0.29796 0.25529 0.44974 0.02181  0.03699  0.16318  269 LYS   A CA  
2076 C  C   . LYS   A 269 ? 0.31087 0.24665 0.47106 0.01567  0.04017  0.16015  269 LYS   A C   
2077 O  O   . LYS   A 269 ? 0.34085 0.25344 0.50520 0.01495  0.04281  0.15021  269 LYS   A O   
2078 C  CB  . LYS   A 269 ? 0.28411 0.25686 0.44565 0.02755  0.03799  0.18083  269 LYS   A CB  
2079 C  CG  . LYS   A 269 ? 0.32839 0.28604 0.50763 0.03325  0.04314  0.18560  269 LYS   A CG  
2080 C  CD  . LYS   A 269 ? 0.31415 0.29099 0.50295 0.03978  0.04312  0.20331  269 LYS   A CD  
2081 C  CE  . LYS   A 269 ? 0.41623 0.37700 0.62647 0.04470  0.04951  0.21110  269 LYS   A CE  
2082 N  NZ  . LYS   A 269 ? 0.41828 0.39862 0.64023 0.05086  0.04942  0.23044  269 LYS   A NZ  
2083 N  N   . GLU   A 270 ? 0.31831 0.26167 0.48066 0.01071  0.04011  0.16831  270 GLU   A N   
2084 C  CA  . GLU   A 270 ? 0.34091 0.26573 0.51293 0.00389  0.04279  0.16712  270 GLU   A CA  
2085 C  C   . GLU   A 270 ? 0.33160 0.24060 0.49618 -0.00370 0.04081  0.14959  270 GLU   A C   
2086 O  O   . GLU   A 270 ? 0.31773 0.20326 0.48843 -0.00821 0.04277  0.14229  270 GLU   A O   
2087 C  CB  . GLU   A 270 ? 0.32677 0.26659 0.50227 0.00013  0.04319  0.18009  270 GLU   A CB  
2088 C  CG  . GLU   A 270 ? 0.34313 0.29861 0.52575 0.00678  0.04487  0.19841  270 GLU   A CG  
2089 C  CD  . GLU   A 270 ? 0.40427 0.34242 0.60443 0.01087  0.04927  0.20474  270 GLU   A CD  
2090 O  OE1 . GLU   A 270 ? 0.41703 0.33218 0.62620 0.00578  0.05207  0.19966  270 GLU   A OE1 
2091 O  OE2 . GLU   A 270 ? 0.42048 0.36742 0.62562 0.01886  0.04990  0.21394  270 GLU   A OE2 
2092 N  N   . LEU   A 271 ? 0.27409 0.19558 0.42518 -0.00564 0.03675  0.14250  271 LEU   A N   
2093 C  CA  . LEU   A 271 ? 0.28832 0.19725 0.43244 -0.01279 0.03415  0.12664  271 LEU   A CA  
2094 C  C   . LEU   A 271 ? 0.30867 0.19650 0.45055 -0.01041 0.03519  0.11452  271 LEU   A C   
2095 O  O   . LEU   A 271 ? 0.34586 0.21436 0.48624 -0.01744 0.03463  0.10245  271 LEU   A O   
2096 C  CB  . LEU   A 271 ? 0.27920 0.20692 0.41076 -0.01356 0.03012  0.12295  271 LEU   A CB  
2097 C  CG  . LEU   A 271 ? 0.23821 0.18372 0.37080 -0.01799 0.02971  0.13046  271 LEU   A CG  
2098 C  CD1 . LEU   A 271 ? 0.25450 0.21922 0.37435 -0.01631 0.02694  0.12758  271 LEU   A CD1 
2099 C  CD2 . LEU   A 271 ? 0.34073 0.27558 0.48019 -0.02815 0.02908  0.12519  271 LEU   A CD2 
2100 N  N   . LEU   A 272 ? 0.29706 0.18912 0.43861 -0.00091 0.03682  0.11750  272 LEU   A N   
2101 C  CA  . LEU   A 272 ? 0.30522 0.17901 0.44541 0.00266  0.03918  0.10654  272 LEU   A CA  
2102 C  C   . LEU   A 272 ? 0.34898 0.19977 0.50140 0.00228  0.04442  0.10640  272 LEU   A C   
2103 O  O   . LEU   A 272 ? 0.34506 0.17373 0.49410 -0.00044 0.04607  0.09248  272 LEU   A O   
2104 C  CB  . LEU   A 272 ? 0.31727 0.20504 0.45630 0.01291  0.03979  0.11131  272 LEU   A CB  
2105 C  CG  . LEU   A 272 ? 0.28308 0.18830 0.40826 0.01315  0.03483  0.10741  272 LEU   A CG  
2106 C  CD1 . LEU   A 272 ? 0.30265 0.22494 0.42842 0.02223  0.03474  0.11474  272 LEU   A CD1 
2107 C  CD2 . LEU   A 272 ? 0.27057 0.16163 0.38517 0.00873  0.03336  0.09033  272 LEU   A CD2 
2108 N  N   . GLN   A 273 ? 0.36518 0.22049 0.53130 0.00474  0.04720  0.12151  273 GLN   A N   
2109 C  CA  . GLN   A 273 ? 0.37702 0.20969 0.55665 0.00481  0.05273  0.12246  273 GLN   A CA  
2110 C  C   . GLN   A 273 ? 0.38433 0.20024 0.56485 -0.00709 0.05172  0.11630  273 GLN   A C   
2111 O  O   . GLN   A 273 ? 0.42857 0.21897 0.61409 -0.00993 0.05518  0.10875  273 GLN   A O   
2112 C  CB  . GLN   A 273 ? 0.38577 0.22891 0.58167 0.01206  0.05631  0.14207  273 GLN   A CB  
2113 C  CG  . GLN   A 273 ? 0.36954 0.22416 0.56966 0.02370  0.05846  0.14848  273 GLN   A CG  
2114 C  CD  . GLN   A 273 ? 0.38158 0.26156 0.59004 0.02891  0.05760  0.16923  273 GLN   A CD  
2115 O  OE1 . GLN   A 273 ? 0.40883 0.30022 0.62336 0.03746  0.05886  0.17713  273 GLN   A OE1 
2116 N  NE2 . GLN   A 273 ? 0.40869 0.29807 0.61794 0.02344  0.05562  0.17846  273 GLN   A NE2 
2117 N  N   . ASN   A 274 ? 0.39302 0.22285 0.56891 -0.01453 0.04716  0.11878  274 ASN   A N   
2118 C  CA  . ASN   A 274 ? 0.40772 0.22624 0.58740 -0.02631 0.04602  0.11592  274 ASN   A CA  
2119 C  C   . ASN   A 274 ? 0.42097 0.23744 0.58740 -0.03637 0.04036  0.10073  274 ASN   A C   
2120 O  O   . ASN   A 274 ? 0.46133 0.26720 0.63020 -0.04757 0.03865  0.09600  274 ASN   A O   
2121 C  CB  . ASN   A 274 ? 0.43596 0.27346 0.62526 -0.02766 0.04629  0.13325  274 ASN   A CB  
2122 C  CG  . ASN   A 274 ? 0.45824 0.29644 0.66235 -0.01984 0.05149  0.14946  274 ASN   A CG  
2123 O  OD1 . ASN   A 274 ? 0.47797 0.29502 0.69069 -0.01717 0.05574  0.14756  274 ASN   A OD1 
2124 N  ND2 . ASN   A 274 ? 0.47152 0.33431 0.67876 -0.01620 0.05139  0.16568  274 ASN   A ND2 
2125 N  N   . GLY   A 275 ? 0.42208 0.24892 0.57551 -0.03324 0.03721  0.09355  275 GLY   A N   
2126 C  CA  . GLY   A 275 ? 0.45214 0.28202 0.59539 -0.04280 0.03148  0.08249  275 GLY   A CA  
2127 C  C   . GLY   A 275 ? 0.43956 0.29081 0.58841 -0.04748 0.02936  0.09260  275 GLY   A C   
2128 O  O   . GLY   A 275 ? 0.39980 0.26630 0.55630 -0.04215 0.03201  0.10762  275 GLY   A O   
2129 N  N   . MET   A 276 ? 0.47321 0.32645 0.61834 -0.05780 0.02460  0.08418  276 MET   A N   
2130 C  CA  . MET   A 276 ? 0.45459 0.33126 0.60436 -0.06107 0.02259  0.09184  276 MET   A CA  
2131 C  C   . MET   A 276 ? 0.49222 0.36481 0.65360 -0.07223 0.02215  0.09399  276 MET   A C   
2132 O  O   . MET   A 276 ? 0.46515 0.35724 0.63382 -0.07477 0.02172  0.10209  276 MET   A O   
2133 C  CB  . MET   A 276 ? 0.46712 0.35569 0.60613 -0.06241 0.01735  0.08258  276 MET   A CB  
2134 C  CG  . MET   A 276 ? 0.38063 0.28689 0.51342 -0.05136 0.01855  0.08890  276 MET   A CG  
2135 S  SD  . MET   A 276 ? 0.51329 0.43597 0.63557 -0.05099 0.01345  0.08151  276 MET   A SD  
2136 C  CE  . MET   A 276 ? 0.34080 0.27707 0.47281 -0.06085 0.01036  0.08282  276 MET   A CE  
2137 N  N   . ASN   A 277 ? 0.52294 0.37036 0.68651 -0.07866 0.02282  0.08719  277 ASN   A N   
2138 C  CA  . ASN   A 277 ? 0.52100 0.36055 0.69695 -0.08935 0.02327  0.09020  277 ASN   A CA  
2139 C  C   . ASN   A 277 ? 0.48518 0.34016 0.66397 -0.10006 0.01797  0.08695  277 ASN   A C   
2140 O  O   . ASN   A 277 ? 0.52266 0.38938 0.71511 -0.10448 0.01902  0.09707  277 ASN   A O   
2141 C  CB  . ASN   A 277 ? 0.53003 0.37591 0.72052 -0.08400 0.02909  0.10850  277 ASN   A CB  
2142 C  CG  . ASN   A 277 ? 0.60298 0.43197 0.80654 -0.09395 0.03083  0.11087  277 ASN   A CG  
2143 O  OD1 . ASN   A 277 ? 0.64538 0.45872 0.84653 -0.10591 0.02728  0.09832  277 ASN   A OD1 
2144 N  ND2 . ASN   A 277 ? 0.62660 0.45898 0.84358 -0.08977 0.03609  0.12712  277 ASN   A ND2 
2145 N  N   . GLY   A 278 ? 0.46529 0.32147 0.63220 -0.10396 0.01234  0.07334  278 GLY   A N   
2146 C  CA  . GLY   A 278 ? 0.44689 0.31815 0.61767 -0.11401 0.00654  0.06934  278 GLY   A CA  
2147 C  C   . GLY   A 278 ? 0.42254 0.32465 0.60024 -0.10844 0.00611  0.07987  278 GLY   A C   
2148 O  O   . GLY   A 278 ? 0.41291 0.33022 0.59874 -0.11564 0.00201  0.07978  278 GLY   A O   
2149 N  N   . ARG   A 279 ? 0.41101 0.32326 0.58562 -0.09592 0.01029  0.08876  279 ARG   A N   
2150 C  CA  . ARG   A 279 ? 0.35605 0.29574 0.53373 -0.09024 0.01084  0.09734  279 ARG   A CA  
2151 C  C   . ARG   A 279 ? 0.34019 0.28648 0.50438 -0.08423 0.00760  0.08965  279 ARG   A C   
2152 O  O   . ARG   A 279 ? 0.34606 0.27661 0.49910 -0.08417 0.00521  0.07879  279 ARG   A O   
2153 C  CB  . ARG   A 279 ? 0.36124 0.30953 0.54346 -0.08183 0.01794  0.11284  279 ARG   A CB  
2154 C  CG  . ARG   A 279 ? 0.38684 0.33259 0.58435 -0.08794 0.02116  0.12239  279 ARG   A CG  
2155 C  CD  . ARG   A 279 ? 0.36610 0.31718 0.56612 -0.07953 0.02789  0.13738  279 ARG   A CD  
2156 N  NE  . ARG   A 279 ? 0.42978 0.36009 0.62586 -0.07513 0.02971  0.13661  279 ARG   A NE  
2157 C  CZ  . ARG   A 279 ? 0.39057 0.32054 0.59102 -0.06887 0.03479  0.14942  279 ARG   A CZ  
2158 N  NH1 . ARG   A 279 ? 0.37514 0.32230 0.58322 -0.06773 0.03868  0.16386  279 ARG   A NH1 
2159 N  NH2 . ARG   A 279 ? 0.38998 0.30293 0.58737 -0.06335 0.03617  0.14812  279 ARG   A NH2 
2160 N  N   . THR   A 280 ? 0.32571 0.29501 0.49084 -0.07935 0.00798  0.09507  280 THR   A N   
2161 C  CA  . THR   A 280 ? 0.26966 0.24667 0.42359 -0.07377 0.00526  0.08909  280 THR   A CA  
2162 C  C   . THR   A 280 ? 0.25618 0.24958 0.40641 -0.06367 0.01082  0.09862  280 THR   A C   
2163 O  O   . THR   A 280 ? 0.24483 0.24855 0.40180 -0.06194 0.01602  0.10954  280 THR   A O   
2164 C  CB  . THR   A 280 ? 0.28114 0.27001 0.43861 -0.07936 -0.00126 0.08289  280 THR   A CB  
2165 O  OG1 . THR   A 280 ? 0.25503 0.26346 0.42564 -0.08001 0.00106  0.09211  280 THR   A OG1 
2166 C  CG2 . THR   A 280 ? 0.27694 0.25091 0.43531 -0.09046 -0.00735 0.07261  280 THR   A CG2 
2167 N  N   . ILE   A 281 ? 0.24219 0.23761 0.38042 -0.05757 0.00976  0.09394  281 ILE   A N   
2168 C  CA  . ILE   A 281 ? 0.19846 0.20932 0.32940 -0.04888 0.01420  0.09990  281 ILE   A CA  
2169 C  C   . ILE   A 281 ? 0.20849 0.22946 0.33512 -0.04794 0.01094  0.09302  281 ILE   A C   
2170 O  O   . ILE   A 281 ? 0.19830 0.20966 0.31873 -0.04906 0.00583  0.08396  281 ILE   A O   
2171 C  CB  . ILE   A 281 ? 0.19724 0.20001 0.31749 -0.04174 0.01645  0.10193  281 ILE   A CB  
2172 C  CG1 . ILE   A 281 ? 0.20676 0.19897 0.33328 -0.04196 0.01954  0.10940  281 ILE   A CG1 
2173 C  CG2 . ILE   A 281 ? 0.15655 0.17668 0.26661 -0.03414 0.02001  0.10658  281 ILE   A CG2 
2174 C  CD1 . ILE   A 281 ? 0.20203 0.18909 0.32096 -0.03404 0.02157  0.11323  281 ILE   A CD1 
2175 N  N   . LEU   A 282 ? 0.20203 0.24196 0.33181 -0.04546 0.01451  0.09725  282 LEU   A N   
2176 C  CA  . LEU   A 282 ? 0.21845 0.26934 0.34691 -0.04371 0.01264  0.09170  282 LEU   A CA  
2177 C  C   . LEU   A 282 ? 0.21879 0.26256 0.35204 -0.05026 0.00372  0.08327  282 LEU   A C   
2178 O  O   . LEU   A 282 ? 0.22477 0.26707 0.35142 -0.04910 -0.00063 0.07622  282 LEU   A O   
2179 C  CB  . LEU   A 282 ? 0.19220 0.24501 0.30578 -0.03673 0.01476  0.08912  282 LEU   A CB  
2180 C  CG  . LEU   A 282 ? 0.17341 0.23900 0.27916 -0.03031 0.02310  0.09559  282 LEU   A CG  
2181 C  CD1 . LEU   A 282 ? 0.16110 0.22746 0.25018 -0.02458 0.02398  0.09211  282 LEU   A CD1 
2182 C  CD2 . LEU   A 282 ? 0.14148 0.22389 0.25443 -0.02906 0.02863  0.09773  282 LEU   A CD2 
2183 N  N   . GLY   A 283 ? 0.20327 0.24263 0.34692 -0.05770 0.00070  0.08396  283 GLY   A N   
2184 C  CA  . GLY   A 283 ? 0.23033 0.26470 0.37678 -0.06508 -0.00820 0.07602  283 GLY   A CA  
2185 C  C   . GLY   A 283 ? 0.23999 0.25500 0.37379 -0.06752 -0.01308 0.06617  283 GLY   A C   
2186 O  O   . GLY   A 283 ? 0.25304 0.26571 0.38351 -0.07216 -0.02059 0.05811  283 GLY   A O   
2187 N  N   . SER   A 284 ? 0.23074 0.23244 0.35670 -0.06384 -0.00867 0.06689  284 SER   A N   
2188 C  CA  . SER   A 284 ? 0.22494 0.20616 0.33968 -0.06524 -0.01123 0.05771  284 SER   A CA  
2189 C  C   . SER   A 284 ? 0.24248 0.20645 0.36014 -0.06820 -0.00758 0.05899  284 SER   A C   
2190 O  O   . SER   A 284 ? 0.23763 0.20534 0.36229 -0.06533 -0.00188 0.06923  284 SER   A O   
2191 C  CB  . SER   A 284 ? 0.21653 0.19611 0.31995 -0.05670 -0.00887 0.05729  284 SER   A CB  
2192 O  OG  . SER   A 284 ? 0.19156 0.15129 0.28502 -0.05705 -0.01021 0.04863  284 SER   A OG  
2193 N  N   . ALA   A 285 ? 0.24538 0.19054 0.35706 -0.07414 -0.01053 0.04841  285 ALA   A N   
2194 C  CA  . ALA   A 285 ? 0.24811 0.17236 0.36041 -0.07617 -0.00627 0.04757  285 ALA   A CA  
2195 C  C   . ALA   A 285 ? 0.26909 0.17720 0.37047 -0.06865 -0.00261 0.04378  285 ALA   A C   
2196 O  O   . ALA   A 285 ? 0.32906 0.21731 0.42967 -0.06919 0.00102  0.04152  285 ALA   A O   
2197 C  CB  . ALA   A 285 ? 0.28147 0.19367 0.39384 -0.08838 -0.01033 0.03747  285 ALA   A CB  
2198 N  N   . LEU   A 286 ? 0.22949 0.14580 0.32330 -0.06156 -0.00345 0.04317  286 LEU   A N   
2199 C  CA  . LEU   A 286 ? 0.31060 0.21721 0.39638 -0.05265 0.00031  0.04197  286 LEU   A CA  
2200 C  C   . LEU   A 286 ? 0.23736 0.16099 0.32501 -0.04325 0.00342  0.05390  286 LEU   A C   
2201 O  O   . LEU   A 286 ? 0.23197 0.17457 0.32209 -0.04359 0.00174  0.05895  286 LEU   A O   
2202 C  CB  . LEU   A 286 ? 0.26432 0.16540 0.33733 -0.05336 -0.00378 0.02938  286 LEU   A CB  
2203 C  CG  . LEU   A 286 ? 0.28506 0.17028 0.35077 -0.06287 -0.00682 0.01574  286 LEU   A CG  
2204 C  CD1 . LEU   A 286 ? 0.26793 0.14603 0.31861 -0.06120 -0.00857 0.00405  286 LEU   A CD1 
2205 C  CD2 . LEU   A 286 ? 0.30686 0.17147 0.37538 -0.06256 -0.00074 0.01626  286 LEU   A CD2 
2206 N  N   . LEU   A 287 ? 0.24771 0.16554 0.33340 -0.03470 0.00808  0.05796  287 LEU   A N   
2207 C  CA  . LEU   A 287 ? 0.18557 0.12021 0.26883 -0.02612 0.00996  0.06744  287 LEU   A CA  
2208 C  C   . LEU   A 287 ? 0.21412 0.15415 0.28791 -0.02415 0.00666  0.06127  287 LEU   A C   
2209 O  O   . LEU   A 287 ? 0.22541 0.15369 0.29283 -0.02209 0.00630  0.05239  287 LEU   A O   
2210 C  CB  . LEU   A 287 ? 0.20773 0.13753 0.29307 -0.01788 0.01463  0.07415  287 LEU   A CB  
2211 C  CG  . LEU   A 287 ? 0.21045 0.13260 0.30658 -0.02028 0.01777  0.08047  287 LEU   A CG  
2212 C  CD1 . LEU   A 287 ? 0.25747 0.17353 0.35839 -0.01223 0.02212  0.08693  287 LEU   A CD1 
2213 C  CD2 . LEU   A 287 ? 0.22219 0.16142 0.32374 -0.02321 0.01798  0.09054  287 LEU   A CD2 
2214 N  N   . GLU   A 288 ? 0.16841 0.12767 0.23900 -0.02395 0.00475  0.06377  288 GLU   A N   
2215 C  CA  . GLU   A 288 ? 0.19052 0.15784 0.24956 -0.02206 0.00084  0.05421  288 GLU   A CA  
2216 C  C   . GLU   A 288 ? 0.19663 0.17371 0.24695 -0.01356 0.00229  0.05651  288 GLU   A C   
2217 O  O   . GLU   A 288 ? 0.17221 0.16094 0.22334 -0.01039 0.00495  0.06628  288 GLU   A O   
2218 C  CB  . GLU   A 288 ? 0.21549 0.19705 0.27752 -0.02641 -0.00165 0.05401  288 GLU   A CB  
2219 C  CG  . GLU   A 288 ? 0.24630 0.23810 0.29846 -0.02257 -0.00398 0.04778  288 GLU   A CG  
2220 C  CD  . GLU   A 288 ? 0.30064 0.28611 0.34890 -0.02658 -0.00970 0.03756  288 GLU   A CD  
2221 O  OE1 . GLU   A 288 ? 0.27274 0.25119 0.32691 -0.03417 -0.01294 0.03539  288 GLU   A OE1 
2222 O  OE2 . GLU   A 288 ? 0.24406 0.23096 0.28255 -0.02262 -0.01111 0.03196  288 GLU   A OE2 
2223 N  N   . ASP   A 289 ? 0.15900 0.13264 0.20053 -0.01066 0.00030  0.04774  289 ASP   A N   
2224 C  CA  . ASP   A 289 ? 0.20264 0.18481 0.23798 -0.00368 0.00101  0.04973  289 ASP   A CA  
2225 C  C   . ASP   A 289 ? 0.17238 0.16363 0.19839 -0.00311 -0.00226 0.04188  289 ASP   A C   
2226 O  O   . ASP   A 289 ? 0.15034 0.14672 0.17151 0.00122  -0.00253 0.04126  289 ASP   A O   
2227 C  CB  . ASP   A 289 ? 0.18482 0.15496 0.22235 0.00090  0.00364  0.04984  289 ASP   A CB  
2228 C  CG  . ASP   A 289 ? 0.17897 0.13896 0.20990 0.00025  0.00271  0.03763  289 ASP   A CG  
2229 O  OD1 . ASP   A 289 ? 0.19510 0.15320 0.22095 -0.00531 -0.00069 0.02969  289 ASP   A OD1 
2230 O  OD2 . ASP   A 289 ? 0.21487 0.16978 0.24639 0.00556  0.00576  0.03713  289 ASP   A OD2 
2231 N  N   . GLU   A 290 ? 0.15183 0.14609 0.17711 -0.00736 -0.00479 0.03696  290 GLU   A N   
2232 C  CA  . GLU   A 290 ? 0.15491 0.15591 0.17342 -0.00635 -0.00728 0.03064  290 GLU   A CA  
2233 C  C   . GLU   A 290 ? 0.16553 0.18012 0.18388 -0.00575 -0.00624 0.03236  290 GLU   A C   
2234 O  O   . GLU   A 290 ? 0.15596 0.17401 0.17286 -0.00609 -0.00780 0.02728  290 GLU   A O   
2235 C  CB  . GLU   A 290 ? 0.20291 0.19665 0.21985 -0.01029 -0.01100 0.02332  290 GLU   A CB  
2236 C  CG  . GLU   A 290 ? 0.20596 0.18596 0.21854 -0.01022 -0.01058 0.01894  290 GLU   A CG  
2237 C  CD  . GLU   A 290 ? 0.25497 0.23109 0.25961 -0.01236 -0.01373 0.01130  290 GLU   A CD  
2238 O  OE1 . GLU   A 290 ? 0.18684 0.16928 0.19143 -0.01503 -0.01766 0.01020  290 GLU   A OE1 
2239 O  OE2 . GLU   A 290 ? 0.21863 0.18529 0.21762 -0.01119 -0.01168 0.00710  290 GLU   A OE2 
2240 N  N   . PHE   A 291 ? 0.15760 0.17987 0.17679 -0.00437 -0.00290 0.03963  291 PHE   A N   
2241 C  CA  . PHE   A 291 ? 0.14702 0.18234 0.16189 -0.00306 -0.00037 0.04002  291 PHE   A CA  
2242 C  C   . PHE   A 291 ? 0.17110 0.21365 0.17784 -0.00019 0.00012  0.04403  291 PHE   A C   
2243 O  O   . PHE   A 291 ? 0.13756 0.18053 0.14675 0.00071  0.00125  0.05319  291 PHE   A O   
2244 C  CB  . PHE   A 291 ? 0.15907 0.20098 0.18070 -0.00496 0.00383  0.04603  291 PHE   A CB  
2245 C  CG  . PHE   A 291 ? 0.16714 0.20609 0.19956 -0.00847 0.00270  0.04413  291 PHE   A CG  
2246 C  CD1 . PHE   A 291 ? 0.20457 0.24893 0.23935 -0.00783 0.00306  0.03895  291 PHE   A CD1 
2247 C  CD2 . PHE   A 291 ? 0.16398 0.19503 0.20557 -0.01277 0.00113  0.04802  291 PHE   A CD2 
2248 C  CE1 . PHE   A 291 ? 0.21221 0.25691 0.25930 -0.01112 0.00100  0.03931  291 PHE   A CE1 
2249 C  CE2 . PHE   A 291 ? 0.23538 0.26600 0.28727 -0.01742 -0.00142 0.04676  291 PHE   A CE2 
2250 C  CZ  . PHE   A 291 ? 0.18737 0.22630 0.24247 -0.01645 -0.00192 0.04320  291 PHE   A CZ  
2251 N  N   . THR   A 292 ? 0.15554 0.20418 0.15365 0.00078  -0.00105 0.03797  292 THR   A N   
2252 C  CA  . THR   A 292 ? 0.16397 0.22286 0.15333 0.00200  -0.00197 0.04128  292 THR   A CA  
2253 C  C   . THR   A 292 ? 0.17309 0.24374 0.15617 0.00136  0.00215  0.04604  292 THR   A C   
2254 O  O   . THR   A 292 ? 0.17429 0.24550 0.16029 0.00049  0.00665  0.04484  292 THR   A O   
2255 C  CB  . THR   A 292 ? 0.19307 0.25421 0.17537 0.00145  -0.00499 0.03201  292 THR   A CB  
2256 O  OG1 . THR   A 292 ? 0.19241 0.25582 0.17005 0.00016  -0.00203 0.02417  292 THR   A OG1 
2257 C  CG2 . THR   A 292 ? 0.14771 0.19849 0.13556 0.00186  -0.00786 0.02756  292 THR   A CG2 
2258 N  N   . PRO   A 293 ? 0.16963 0.25157 0.14418 0.00173  0.00087  0.05234  293 PRO   A N   
2259 C  CA  . PRO   A 293 ? 0.19154 0.28630 0.15541 0.00051  0.00508  0.05506  293 PRO   A CA  
2260 C  C   . PRO   A 293 ? 0.19971 0.29620 0.15480 -0.00092 0.00844  0.04181  293 PRO   A C   
2261 O  O   . PRO   A 293 ? 0.22642 0.32785 0.17871 -0.00108 0.01530  0.04159  293 PRO   A O   
2262 C  CB  . PRO   A 293 ? 0.18321 0.28528 0.14322 0.00046  0.00051  0.05867  293 PRO   A CB  
2263 C  CG  . PRO   A 293 ? 0.16239 0.25738 0.13528 0.00307  -0.00278 0.06581  293 PRO   A CG  
2264 C  CD  . PRO   A 293 ? 0.17453 0.25854 0.15137 0.00354  -0.00374 0.05940  293 PRO   A CD  
2265 N  N   . PHE   A 294 ? 0.21849 0.30993 0.17126 -0.00169 0.00466  0.03087  294 PHE   A N   
2266 C  CA  . PHE   A 294 ? 0.22804 0.31666 0.17621 -0.00250 0.00838  0.01762  294 PHE   A CA  
2267 C  C   . PHE   A 294 ? 0.23522 0.31694 0.19605 -0.00044 0.01400  0.01638  294 PHE   A C   
2268 O  O   . PHE   A 294 ? 0.21904 0.30353 0.17740 0.00034  0.02110  0.01097  294 PHE   A O   
2269 C  CB  . PHE   A 294 ? 0.23305 0.31483 0.18118 -0.00393 0.00295  0.00828  294 PHE   A CB  
2270 C  CG  . PHE   A 294 ? 0.32513 0.40172 0.26970 -0.00478 0.00696  -0.00535 294 PHE   A CG  
2271 C  CD1 . PHE   A 294 ? 0.35703 0.42360 0.31425 -0.00217 0.01059  -0.00875 294 PHE   A CD1 
2272 C  CD2 . PHE   A 294 ? 0.36466 0.44620 0.29404 -0.00833 0.00711  -0.01445 294 PHE   A CD2 
2273 C  CE1 . PHE   A 294 ? 0.36418 0.42472 0.32120 -0.00176 0.01526  -0.02003 294 PHE   A CE1 
2274 C  CE2 . PHE   A 294 ? 0.41770 0.49137 0.34502 -0.00887 0.01209  -0.02792 294 PHE   A CE2 
2275 C  CZ  . PHE   A 294 ? 0.35214 0.41483 0.29445 -0.00490 0.01666  -0.03014 294 PHE   A CZ  
2276 N  N   . ASP   A 295 ? 0.20750 0.28056 0.18220 0.00031  0.01090  0.02069  295 ASP   A N   
2277 C  CA  . ASP   A 295 ? 0.20049 0.26909 0.18874 0.00118  0.01405  0.02081  295 ASP   A CA  
2278 C  C   . ASP   A 295 ? 0.22196 0.29930 0.21345 0.00134  0.02085  0.02805  295 ASP   A C   
2279 O  O   . ASP   A 295 ? 0.21392 0.29389 0.21280 0.00262  0.02664  0.02580  295 ASP   A O   
2280 C  CB  . ASP   A 295 ? 0.18619 0.24519 0.18517 0.00031  0.00846  0.02439  295 ASP   A CB  
2281 C  CG  . ASP   A 295 ? 0.20818 0.25926 0.20533 0.00030  0.00313  0.01794  295 ASP   A CG  
2282 O  OD1 . ASP   A 295 ? 0.21594 0.26743 0.20775 0.00072  0.00375  0.01032  295 ASP   A OD1 
2283 O  OD2 . ASP   A 295 ? 0.17624 0.22019 0.17716 -0.00041 -0.00101 0.02034  295 ASP   A OD2 
2284 N  N   . VAL   A 296 ? 0.18659 0.26906 0.17468 0.00034  0.02071  0.03808  296 VAL   A N   
2285 C  CA  . VAL   A 296 ? 0.17888 0.27031 0.17061 -0.00009 0.02757  0.04698  296 VAL   A CA  
2286 C  C   . VAL   A 296 ? 0.23923 0.34160 0.21873 0.00114  0.03568  0.04177  296 VAL   A C   
2287 O  O   . VAL   A 296 ? 0.24047 0.34841 0.22711 0.00215  0.04373  0.04250  296 VAL   A O   
2288 C  CB  . VAL   A 296 ? 0.17451 0.26822 0.16530 -0.00123 0.02567  0.06022  296 VAL   A CB  
2289 C  CG1 . VAL   A 296 ? 0.16427 0.26837 0.15768 -0.00213 0.03328  0.07074  296 VAL   A CG1 
2290 C  CG2 . VAL   A 296 ? 0.15253 0.23279 0.15672 -0.00233 0.01991  0.06353  296 VAL   A CG2 
2291 N  N   . VAL   A 297 ? 0.24086 0.34665 0.20205 0.00079  0.03394  0.03561  297 VAL   A N   
2292 C  CA  . VAL   A 297 ? 0.26391 0.37830 0.20991 0.00104  0.04173  0.02840  297 VAL   A CA  
2293 C  C   . VAL   A 297 ? 0.28929 0.39799 0.24204 0.00367  0.04796  0.01595  297 VAL   A C   
2294 O  O   . VAL   A 297 ? 0.30800 0.42292 0.25938 0.00563  0.05862  0.01310  297 VAL   A O   
2295 C  CB  . VAL   A 297 ? 0.24796 0.36260 0.17533 -0.00154 0.03525  0.02269  297 VAL   A CB  
2296 C  CG1 . VAL   A 297 ? 0.26738 0.38342 0.17959 -0.00219 0.04197  0.01163  297 VAL   A CG1 
2297 C  CG2 . VAL   A 297 ? 0.29014 0.40947 0.21603 -0.00285 0.02902  0.03562  297 VAL   A CG2 
2298 N  N   . ARG   A 298 ? 0.26513 0.36157 0.22636 0.00420  0.04192  0.00900  298 ARG   A N   
2299 C  CA  . ARG   A 298 ? 0.32758 0.41722 0.29834 0.00733  0.04704  -0.00089 298 ARG   A CA  
2300 C  C   . ARG   A 298 ? 0.32587 0.41970 0.31644 0.01020  0.05338  0.00609  298 ARG   A C   
2301 O  O   . ARG   A 298 ? 0.38178 0.47871 0.37704 0.01384  0.06357  0.00120  298 ARG   A O   
2302 C  CB  . ARG   A 298 ? 0.30350 0.38019 0.28137 0.00700  0.03854  -0.00593 298 ARG   A CB  
2303 C  CG  . ARG   A 298 ? 0.38704 0.45744 0.38465 0.01076  0.04144  -0.00802 298 ARG   A CG  
2304 C  CD  . ARG   A 298 ? 0.40675 0.46470 0.41008 0.01077  0.03483  -0.01331 298 ARG   A CD  
2305 N  NE  . ARG   A 298 ? 0.37271 0.42717 0.38343 0.00872  0.02529  -0.00568 298 ARG   A NE  
2306 C  CZ  . ARG   A 298 ? 0.29963 0.34958 0.32533 0.00977  0.02183  -0.00264 298 ARG   A CZ  
2307 N  NH1 . ARG   A 298 ? 0.27773 0.32685 0.31665 0.01367  0.02664  -0.00439 298 ARG   A NH1 
2308 N  NH2 . ARG   A 298 ? 0.27187 0.31853 0.29943 0.00701  0.01359  0.00262  298 ARG   A NH2 
2309 N  N   . GLN   A 299 ? 0.26664 0.36076 0.27004 0.00838  0.04776  0.01735  299 GLN   A N   
2310 C  CA  . GLN   A 299 ? 0.28241 0.38141 0.30706 0.00944  0.05154  0.02452  299 GLN   A CA  
2311 C  C   . GLN   A 299 ? 0.30620 0.41898 0.33048 0.00953  0.06151  0.03207  299 GLN   A C   
2312 O  O   . GLN   A 299 ? 0.35789 0.47825 0.39592 0.01242  0.07031  0.03324  299 GLN   A O   
2313 C  CB  . GLN   A 299 ? 0.26149 0.35475 0.29874 0.00581  0.04150  0.03219  299 GLN   A CB  
2314 C  CG  . GLN   A 299 ? 0.20965 0.30730 0.27031 0.00569  0.04231  0.03756  299 GLN   A CG  
2315 C  CD  . GLN   A 299 ? 0.18528 0.27546 0.25525 0.00112  0.03133  0.04148  299 GLN   A CD  
2316 O  OE1 . GLN   A 299 ? 0.19076 0.28598 0.27813 -0.00190 0.02988  0.04842  299 GLN   A OE1 
2317 N  NE2 . GLN   A 299 ? 0.19283 0.27163 0.25108 -0.00004 0.02374  0.03697  299 GLN   A NE2 
2318 N  N   . CYS   A 300 ? 0.31621 0.43363 0.32655 0.00671  0.06078  0.03868  300 CYS   A N   
2319 C  CA  . CYS   A 300 ? 0.33414 0.46147 0.34158 0.00612  0.06874  0.04571  300 CYS   A CA  
2320 C  C   . CYS   A 300 ? 0.39991 0.53006 0.38747 0.00803  0.07715  0.03546  300 CYS   A C   
2321 O  O   . CYS   A 300 ? 0.48793 0.62355 0.46642 0.00659  0.08162  0.04003  300 CYS   A O   
2322 C  CB  . CYS   A 300 ? 0.30805 0.43482 0.31070 0.00229  0.06253  0.05747  300 CYS   A CB  
2323 S  SG  . CYS   A 300 ? 0.30054 0.41944 0.32448 -0.00139 0.05352  0.06803  300 CYS   A SG  
2324 N  N   . SER   A 301 ? 0.43091 0.55622 0.41167 0.01078  0.07951  0.02152  301 SER   A N   
2325 C  CA  . SER   A 301 ? 0.48025 0.60416 0.44299 0.01184  0.08816  0.00950  301 SER   A CA  
2326 C  C   . SER   A 301 ? 0.51606 0.63403 0.48915 0.01698  0.09580  -0.00295 301 SER   A C   
2327 O  O   . SER   A 301 ? 0.52732 0.64561 0.50032 0.01944  0.10787  -0.00900 301 SER   A O   
2328 C  CB  . SER   A 301 ? 0.50880 0.62879 0.44552 0.00817  0.08082  0.00381  301 SER   A CB  
2329 O  OG  . SER   A 301 ? 0.62815 0.74204 0.54803 0.00886  0.08732  -0.01066 301 SER   A OG  
2330 N  N   . GLY   A 302 ? 0.51491 0.62709 0.49794 0.01894  0.08948  -0.00670 302 GLY   A N   
2331 C  CA  . GLY   A 302 ? 0.52718 0.63332 0.52990 0.02484  0.09488  -0.01299 302 GLY   A CA  
2332 C  C   . GLY   A 302 ? 0.57221 0.66345 0.56797 0.02634  0.09490  -0.02892 302 GLY   A C   
2333 O  O   . GLY   A 302 ? 0.54169 0.62857 0.54646 0.03220  0.10461  -0.03652 302 GLY   A O   
2334 N  N   . VAL   A 303 ? 0.60907 0.69180 0.59143 0.02135  0.08329  -0.03290 303 VAL   A N   
2335 C  CA  . VAL   A 303 ? 0.66076 0.72943 0.63467 0.02081  0.08280  -0.04810 303 VAL   A CA  
2336 C  C   . VAL   A 303 ? 0.63359 0.69058 0.63187 0.02498  0.08037  -0.04772 303 VAL   A C   
2337 O  O   . VAL   A 303 ? 0.58540 0.64335 0.59884 0.02466  0.07136  -0.03634 303 VAL   A O   
2338 C  CB  . VAL   A 303 ? 0.65205 0.71875 0.60577 0.01343  0.07085  -0.05052 303 VAL   A CB  
2339 C  CG1 . VAL   A 303 ? 0.71163 0.76323 0.66032 0.01137  0.06868  -0.06514 303 VAL   A CG1 
2340 C  CG2 . VAL   A 303 ? 0.64254 0.71943 0.57246 0.00953  0.07158  -0.04866 303 VAL   A CG2 
2341 N  N   . THR   A 304 ? 0.64634 0.69175 0.64782 0.02867  0.08855  -0.06025 304 THR   A N   
2342 C  CA  . THR   A 304 ? 0.56667 0.60034 0.59155 0.03342  0.08779  -0.05977 304 THR   A CA  
2343 C  C   . THR   A 304 ? 0.65889 0.67630 0.67547 0.02917  0.08125  -0.06973 304 THR   A C   
2344 O  O   . THR   A 304 ? 0.68354 0.69993 0.67727 0.02223  0.07674  -0.07728 304 THR   A O   
2345 C  CB  . THR   A 304 ? 0.50532 0.53687 0.54381 0.04147  0.09874  -0.06145 304 THR   A CB  
2346 O  OG1 . THR   A 304 ? 0.59331 0.62034 0.61001 0.04084  0.10544  -0.07388 304 THR   A OG1 
2347 C  CG2 . THR   A 304 ? 0.34029 0.38903 0.39547 0.04549  0.10279  -0.04855 304 THR   A CG2 
2348 N  N   . PHE   A 305 ? 0.64163 0.64745 0.67860 0.03311  0.08048  -0.06839 305 PHE   A N   
2349 C  CA  . PHE   A 305 ? 0.68766 0.67785 0.72204 0.02907  0.07407  -0.07489 305 PHE   A CA  
2350 C  C   . PHE   A 305 ? 0.69183 0.66804 0.74460 0.03487  0.07891  -0.07563 305 PHE   A C   
2351 O  O   . PHE   A 305 ? 0.67469 0.65515 0.74970 0.04179  0.08127  -0.06508 305 PHE   A O   
2352 C  CB  . PHE   A 305 ? 0.63613 0.62946 0.67344 0.02475  0.05901  -0.06261 305 PHE   A CB  
2353 C  CG  . PHE   A 305 ? 0.61449 0.62257 0.63822 0.02046  0.05235  -0.05553 305 PHE   A CG  
2354 C  CD1 . PHE   A 305 ? 0.60283 0.61330 0.60435 0.01360  0.04772  -0.06131 305 PHE   A CD1 
2355 C  CD2 . PHE   A 305 ? 0.58931 0.60931 0.62371 0.02317  0.05125  -0.04295 305 PHE   A CD2 
2356 C  CE1 . PHE   A 305 ? 0.60075 0.62423 0.59198 0.01067  0.04245  -0.05348 305 PHE   A CE1 
2357 C  CE2 . PHE   A 305 ? 0.58008 0.61129 0.60352 0.01934  0.04628  -0.03647 305 PHE   A CE2 
2358 C  CZ  . PHE   A 305 ? 0.60722 0.63976 0.60939 0.01372  0.04228  -0.04131 305 PHE   A CZ  
2359 N  N   . GLN   A 306 ? 0.70964 0.67065 0.75340 0.03131  0.07928  -0.08657 306 GLN   A N   
2360 C  CA  . GLN   A 306 ? 0.71615 0.66293 0.77617 0.03612  0.08427  -0.08751 306 GLN   A CA  
2361 C  C   . GLN   A 306 ? 0.67733 0.60809 0.73566 0.03007  0.07843  -0.09250 306 GLN   A C   
2362 O  O   . GLN   A 306 ? 0.63182 0.55953 0.70419 0.02989  0.07179  -0.08316 306 GLN   A O   
2363 C  CB  . GLN   A 306 ? 0.73683 0.68092 0.78996 0.03980  0.09579  -0.09728 306 GLN   A CB  
2364 C  CG  . GLN   A 306 ? 0.76590 0.70005 0.84145 0.04770  0.10339  -0.09502 306 GLN   A CG  
2365 C  CD  . GLN   A 306 ? 0.78433 0.71917 0.85500 0.05292  0.11602  -0.10340 306 GLN   A CD  
2366 O  OE1 . GLN   A 306 ? 0.86241 0.80294 0.90966 0.04962  0.11870  -0.11245 306 GLN   A OE1 
2367 N  NE2 . GLN   A 306 ? 0.71029 0.64001 0.80278 0.06112  0.12385  -0.09986 306 GLN   A NE2 
2368 N  N1  . A1AR9 B .   ? 0.41524 0.43108 0.27837 -0.03780 -0.03041 0.02809  401 A1AR9 A N1  
2369 C  C4  . A1AR9 B .   ? 0.38751 0.41271 0.27262 -0.03487 -0.03199 0.05053  401 A1AR9 A C4  
2370 C  C5  . A1AR9 B .   ? 0.41522 0.42623 0.25747 -0.03443 -0.01185 0.02102  401 A1AR9 A C5  
2371 C  C6  . A1AR9 B .   ? 0.45928 0.47062 0.28514 -0.03367 -0.00279 0.01854  401 A1AR9 A C6  
2372 C  C7  . A1AR9 B .   ? 0.47777 0.49299 0.28712 -0.03680 -0.00523 0.02011  401 A1AR9 A C7  
2373 C  C8  . A1AR9 B .   ? 0.48125 0.50097 0.29175 -0.04098 -0.01691 0.02455  401 A1AR9 A C8  
2374 C  C10 . A1AR9 B .   ? 0.43874 0.44765 0.26540 -0.02939 0.00985  0.01490  401 A1AR9 A C10 
2375 C  C13 . A1AR9 B .   ? 0.42611 0.43540 0.26224 -0.02061 0.03464  0.01055  401 A1AR9 A C13 
2376 C  C15 . A1AR9 B .   ? 0.50070 0.50640 0.31206 -0.02734 0.02027  0.00598  401 A1AR9 A C15 
2377 C  C17 . A1AR9 B .   ? 0.37714 0.38031 0.23419 -0.04554 -0.03947 0.00359  401 A1AR9 A C17 
2378 C  C1  . A1AR9 B .   ? 0.37668 0.38690 0.24093 -0.03927 -0.03328 0.01838  401 A1AR9 A C1  
2379 C  C11 . A1AR9 B .   ? 0.41551 0.42649 0.26044 -0.02715 0.01191  0.02075  401 A1AR9 A C11 
2380 C  C12 . A1AR9 B .   ? 0.40440 0.41600 0.25317 -0.02354 0.02363  0.01858  401 A1AR9 A C12 
2381 C  C14 . A1AR9 B .   ? 0.47544 0.48109 0.29225 -0.02233 0.03297  0.00384  401 A1AR9 A C14 
2382 C  C16 . A1AR9 B .   ? 0.39311 0.40240 0.24576 -0.04394 -0.03728 0.01176  401 A1AR9 A C16 
2383 C  C18 . A1AR9 B .   ? 0.33679 0.33557 0.20831 -0.04210 -0.03771 0.00263  401 A1AR9 A C18 
2384 C  C19 . A1AR9 B .   ? 0.35381 0.35932 0.23157 -0.03641 -0.03215 0.01589  401 A1AR9 A C19 
2385 C  C2  . A1AR9 B .   ? 0.44295 0.45827 0.28766 -0.03784 -0.02249 0.02541  401 A1AR9 A C2  
2386 C  C3  . A1AR9 B .   ? 0.39481 0.41563 0.27604 -0.03621 -0.03474 0.03935  401 A1AR9 A C3  
2387 C  C9  . A1AR9 B .   ? 0.45359 0.47367 0.28274 -0.04128 -0.02510 0.02733  401 A1AR9 A C9  
2388 F  F1  . A1AR9 B .   ? 0.51357 0.54315 0.38384 -0.03712 -0.03125 0.05386  401 A1AR9 A F1  
2389 N  N2  . A1AR9 B .   ? 0.31478 0.31489 0.19581 -0.03751 -0.03426 0.00840  401 A1AR9 A N2  
2390 O  O1  . A1AR9 B .   ? 0.40388 0.42470 0.30011 -0.03545 -0.03984 0.04026  401 A1AR9 A O1  
2391 CL CL1 . A1AR9 B .   ? 0.50427 0.52092 0.37951 -0.02168 0.02391  0.02605  401 A1AR9 A CL1 
2392 CL CL2 . A1AR9 B .   ? 0.49942 0.50048 0.34375 -0.05260 -0.04471 -0.00514 401 A1AR9 A CL2 
# 
