data_9BSP
# 
_entry.id   9BSP 
# 
_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   9BSP         pdb_00009bsp 10.2210/pdb9bsp/pdb 
WWPDB D_1000284067 ?            ?                   
# 
_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                        9BSP 
_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 
;methyl 4-{[(1M)-3'-chloro[1,1'-biphenyl]-3-yl](5-chloropyridin-3-yl)amino}-4-oxobutanoate
;
429.296   1   ?         ? ? ? 
3 water       nat water                                                                                       18.015    317 ? ? ? 
? 
# 
_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 
;methyl 4-{[(1M)-3'-chloro[1,1'-biphenyl]-3-yl](5-chloropyridin-3-yl)amino}-4-oxobutanoate
;
A1ARX 
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 
A1ARX non-polymer         . 
;methyl 4-{[(1M)-3'-chloro[1,1'-biphenyl]-3-yl](5-chloropyridin-3-yl)amino}-4-oxobutanoate
;
? 'C22 H18 Cl2 N2 O3' 429.296 
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        A1ARX 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ARX 
_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 A1ARX 1   401 401 A1ARX LIG A . 
C 3 HOH   1   501 177 HOH   HOH A . 
C 3 HOH   2   502 158 HOH   HOH A . 
C 3 HOH   3   503 244 HOH   HOH A . 
C 3 HOH   4   504 123 HOH   HOH A . 
C 3 HOH   5   505 238 HOH   HOH A . 
C 3 HOH   6   506 221 HOH   HOH A . 
C 3 HOH   7   507 205 HOH   HOH A . 
C 3 HOH   8   508 208 HOH   HOH A . 
C 3 HOH   9   509 253 HOH   HOH A . 
C 3 HOH   10  510 262 HOH   HOH A . 
C 3 HOH   11  511 68  HOH   HOH A . 
C 3 HOH   12  512 151 HOH   HOH A . 
C 3 HOH   13  513 204 HOH   HOH A . 
C 3 HOH   14  514 125 HOH   HOH A . 
C 3 HOH   15  515 49  HOH   HOH A . 
C 3 HOH   16  516 23  HOH   HOH A . 
C 3 HOH   17  517 317 HOH   HOH A . 
C 3 HOH   18  518 251 HOH   HOH A . 
C 3 HOH   19  519 139 HOH   HOH A . 
C 3 HOH   20  520 298 HOH   HOH A . 
C 3 HOH   21  521 55  HOH   HOH A . 
C 3 HOH   22  522 293 HOH   HOH A . 
C 3 HOH   23  523 26  HOH   HOH A . 
C 3 HOH   24  524 62  HOH   HOH A . 
C 3 HOH   25  525 79  HOH   HOH A . 
C 3 HOH   26  526 127 HOH   HOH A . 
C 3 HOH   27  527 195 HOH   HOH A . 
C 3 HOH   28  528 197 HOH   HOH A . 
C 3 HOH   29  529 107 HOH   HOH A . 
C 3 HOH   30  530 75  HOH   HOH A . 
C 3 HOH   31  531 247 HOH   HOH A . 
C 3 HOH   32  532 299 HOH   HOH A . 
C 3 HOH   33  533 44  HOH   HOH A . 
C 3 HOH   34  534 67  HOH   HOH A . 
C 3 HOH   35  535 108 HOH   HOH A . 
C 3 HOH   36  536 166 HOH   HOH A . 
C 3 HOH   37  537 245 HOH   HOH A . 
C 3 HOH   38  538 58  HOH   HOH A . 
C 3 HOH   39  539 87  HOH   HOH A . 
C 3 HOH   40  540 59  HOH   HOH A . 
C 3 HOH   41  541 53  HOH   HOH A . 
C 3 HOH   42  542 72  HOH   HOH A . 
C 3 HOH   43  543 113 HOH   HOH A . 
C 3 HOH   44  544 96  HOH   HOH A . 
C 3 HOH   45  545 145 HOH   HOH A . 
C 3 HOH   46  546 142 HOH   HOH A . 
C 3 HOH   47  547 51  HOH   HOH A . 
C 3 HOH   48  548 24  HOH   HOH A . 
C 3 HOH   49  549 22  HOH   HOH A . 
C 3 HOH   50  550 41  HOH   HOH A . 
C 3 HOH   51  551 109 HOH   HOH A . 
C 3 HOH   52  552 148 HOH   HOH A . 
C 3 HOH   53  553 105 HOH   HOH A . 
C 3 HOH   54  554 63  HOH   HOH A . 
C 3 HOH   55  555 13  HOH   HOH A . 
C 3 HOH   56  556 95  HOH   HOH A . 
C 3 HOH   57  557 89  HOH   HOH A . 
C 3 HOH   58  558 210 HOH   HOH A . 
C 3 HOH   59  559 98  HOH   HOH A . 
C 3 HOH   60  560 17  HOH   HOH A . 
C 3 HOH   61  561 100 HOH   HOH A . 
C 3 HOH   62  562 259 HOH   HOH A . 
C 3 HOH   63  563 60  HOH   HOH A . 
C 3 HOH   64  564 114 HOH   HOH A . 
C 3 HOH   65  565 173 HOH   HOH A . 
C 3 HOH   66  566 8   HOH   HOH A . 
C 3 HOH   67  567 249 HOH   HOH A . 
C 3 HOH   68  568 47  HOH   HOH A . 
C 3 HOH   69  569 36  HOH   HOH A . 
C 3 HOH   70  570 300 HOH   HOH A . 
C 3 HOH   71  571 161 HOH   HOH A . 
C 3 HOH   72  572 178 HOH   HOH A . 
C 3 HOH   73  573 3   HOH   HOH A . 
C 3 HOH   74  574 182 HOH   HOH A . 
C 3 HOH   75  575 11  HOH   HOH A . 
C 3 HOH   76  576 209 HOH   HOH A . 
C 3 HOH   77  577 258 HOH   HOH A . 
C 3 HOH   78  578 4   HOH   HOH A . 
C 3 HOH   79  579 66  HOH   HOH A . 
C 3 HOH   80  580 99  HOH   HOH A . 
C 3 HOH   81  581 118 HOH   HOH A . 
C 3 HOH   82  582 69  HOH   HOH A . 
C 3 HOH   83  583 34  HOH   HOH A . 
C 3 HOH   84  584 121 HOH   HOH A . 
C 3 HOH   85  585 308 HOH   HOH A . 
C 3 HOH   86  586 10  HOH   HOH A . 
C 3 HOH   87  587 185 HOH   HOH A . 
C 3 HOH   88  588 295 HOH   HOH A . 
C 3 HOH   89  589 28  HOH   HOH A . 
C 3 HOH   90  590 159 HOH   HOH A . 
C 3 HOH   91  591 301 HOH   HOH A . 
C 3 HOH   92  592 19  HOH   HOH A . 
C 3 HOH   93  593 110 HOH   HOH A . 
C 3 HOH   94  594 175 HOH   HOH A . 
C 3 HOH   95  595 160 HOH   HOH A . 
C 3 HOH   96  596 152 HOH   HOH A . 
C 3 HOH   97  597 27  HOH   HOH A . 
C 3 HOH   98  598 20  HOH   HOH A . 
C 3 HOH   99  599 37  HOH   HOH A . 
C 3 HOH   100 600 65  HOH   HOH A . 
C 3 HOH   101 601 93  HOH   HOH A . 
C 3 HOH   102 602 292 HOH   HOH A . 
C 3 HOH   103 603 162 HOH   HOH A . 
C 3 HOH   104 604 257 HOH   HOH A . 
C 3 HOH   105 605 61  HOH   HOH A . 
C 3 HOH   106 606 281 HOH   HOH A . 
C 3 HOH   107 607 86  HOH   HOH A . 
C 3 HOH   108 608 82  HOH   HOH A . 
C 3 HOH   109 609 71  HOH   HOH A . 
C 3 HOH   110 610 9   HOH   HOH A . 
C 3 HOH   111 611 291 HOH   HOH A . 
C 3 HOH   112 612 91  HOH   HOH A . 
C 3 HOH   113 613 77  HOH   HOH A . 
C 3 HOH   114 614 153 HOH   HOH A . 
C 3 HOH   115 615 265 HOH   HOH A . 
C 3 HOH   116 616 6   HOH   HOH A . 
C 3 HOH   117 617 29  HOH   HOH A . 
C 3 HOH   118 618 149 HOH   HOH A . 
C 3 HOH   119 619 241 HOH   HOH A . 
C 3 HOH   120 620 94  HOH   HOH A . 
C 3 HOH   121 621 255 HOH   HOH A . 
C 3 HOH   122 622 90  HOH   HOH A . 
C 3 HOH   123 623 42  HOH   HOH A . 
C 3 HOH   124 624 269 HOH   HOH A . 
C 3 HOH   125 625 134 HOH   HOH A . 
C 3 HOH   126 626 104 HOH   HOH A . 
C 3 HOH   127 627 239 HOH   HOH A . 
C 3 HOH   128 628 214 HOH   HOH A . 
C 3 HOH   129 629 5   HOH   HOH A . 
C 3 HOH   130 630 136 HOH   HOH A . 
C 3 HOH   131 631 103 HOH   HOH A . 
C 3 HOH   132 632 21  HOH   HOH A . 
C 3 HOH   133 633 227 HOH   HOH A . 
C 3 HOH   134 634 50  HOH   HOH A . 
C 3 HOH   135 635 35  HOH   HOH A . 
C 3 HOH   136 636 80  HOH   HOH A . 
C 3 HOH   137 637 248 HOH   HOH A . 
C 3 HOH   138 638 117 HOH   HOH A . 
C 3 HOH   139 639 237 HOH   HOH A . 
C 3 HOH   140 640 40  HOH   HOH A . 
C 3 HOH   141 641 76  HOH   HOH A . 
C 3 HOH   142 642 111 HOH   HOH A . 
C 3 HOH   143 643 54  HOH   HOH A . 
C 3 HOH   144 644 52  HOH   HOH A . 
C 3 HOH   145 645 31  HOH   HOH A . 
C 3 HOH   146 646 189 HOH   HOH A . 
C 3 HOH   147 647 235 HOH   HOH A . 
C 3 HOH   148 648 120 HOH   HOH A . 
C 3 HOH   149 649 242 HOH   HOH A . 
C 3 HOH   150 650 15  HOH   HOH A . 
C 3 HOH   151 651 150 HOH   HOH A . 
C 3 HOH   152 652 64  HOH   HOH A . 
C 3 HOH   153 653 2   HOH   HOH A . 
C 3 HOH   154 654 14  HOH   HOH A . 
C 3 HOH   155 655 102 HOH   HOH A . 
C 3 HOH   156 656 92  HOH   HOH A . 
C 3 HOH   157 657 184 HOH   HOH A . 
C 3 HOH   158 658 171 HOH   HOH A . 
C 3 HOH   159 659 1   HOH   HOH A . 
C 3 HOH   160 660 45  HOH   HOH A . 
C 3 HOH   161 661 12  HOH   HOH A . 
C 3 HOH   162 662 84  HOH   HOH A . 
C 3 HOH   163 663 116 HOH   HOH A . 
C 3 HOH   164 664 217 HOH   HOH A . 
C 3 HOH   165 665 138 HOH   HOH A . 
C 3 HOH   166 666 135 HOH   HOH A . 
C 3 HOH   167 667 284 HOH   HOH A . 
C 3 HOH   168 668 261 HOH   HOH A . 
C 3 HOH   169 669 271 HOH   HOH A . 
C 3 HOH   170 670 273 HOH   HOH A . 
C 3 HOH   171 671 126 HOH   HOH A . 
C 3 HOH   172 672 16  HOH   HOH A . 
C 3 HOH   173 673 30  HOH   HOH A . 
C 3 HOH   174 674 115 HOH   HOH A . 
C 3 HOH   175 675 83  HOH   HOH A . 
C 3 HOH   176 676 46  HOH   HOH A . 
C 3 HOH   177 677 140 HOH   HOH A . 
C 3 HOH   178 678 282 HOH   HOH A . 
C 3 HOH   179 679 289 HOH   HOH A . 
C 3 HOH   180 680 240 HOH   HOH A . 
C 3 HOH   181 681 101 HOH   HOH A . 
C 3 HOH   182 682 25  HOH   HOH A . 
C 3 HOH   183 683 157 HOH   HOH A . 
C 3 HOH   184 684 38  HOH   HOH A . 
C 3 HOH   185 685 32  HOH   HOH A . 
C 3 HOH   186 686 39  HOH   HOH A . 
C 3 HOH   187 687 88  HOH   HOH A . 
C 3 HOH   188 688 222 HOH   HOH A . 
C 3 HOH   189 689 131 HOH   HOH A . 
C 3 HOH   190 690 57  HOH   HOH A . 
C 3 HOH   191 691 268 HOH   HOH A . 
C 3 HOH   192 692 7   HOH   HOH A . 
C 3 HOH   193 693 304 HOH   HOH A . 
C 3 HOH   194 694 290 HOH   HOH A . 
C 3 HOH   195 695 78  HOH   HOH A . 
C 3 HOH   196 696 163 HOH   HOH A . 
C 3 HOH   197 697 212 HOH   HOH A . 
C 3 HOH   198 698 183 HOH   HOH A . 
C 3 HOH   199 699 18  HOH   HOH A . 
C 3 HOH   200 700 132 HOH   HOH A . 
C 3 HOH   201 701 270 HOH   HOH A . 
C 3 HOH   202 702 198 HOH   HOH A . 
C 3 HOH   203 703 287 HOH   HOH A . 
C 3 HOH   204 704 225 HOH   HOH A . 
C 3 HOH   205 705 188 HOH   HOH A . 
C 3 HOH   206 706 156 HOH   HOH A . 
C 3 HOH   207 707 260 HOH   HOH A . 
C 3 HOH   208 708 231 HOH   HOH A . 
C 3 HOH   209 709 194 HOH   HOH A . 
C 3 HOH   210 710 315 HOH   HOH A . 
C 3 HOH   211 711 179 HOH   HOH A . 
C 3 HOH   212 712 228 HOH   HOH A . 
C 3 HOH   213 713 224 HOH   HOH A . 
C 3 HOH   214 714 309 HOH   HOH A . 
C 3 HOH   215 715 307 HOH   HOH A . 
C 3 HOH   216 716 190 HOH   HOH A . 
C 3 HOH   217 717 106 HOH   HOH A . 
C 3 HOH   218 718 196 HOH   HOH A . 
C 3 HOH   219 719 201 HOH   HOH A . 
C 3 HOH   220 720 85  HOH   HOH A . 
C 3 HOH   221 721 199 HOH   HOH A . 
C 3 HOH   222 722 305 HOH   HOH A . 
C 3 HOH   223 723 312 HOH   HOH A . 
C 3 HOH   224 724 234 HOH   HOH A . 
C 3 HOH   225 725 274 HOH   HOH A . 
C 3 HOH   226 726 143 HOH   HOH A . 
C 3 HOH   227 727 176 HOH   HOH A . 
C 3 HOH   228 728 170 HOH   HOH A . 
C 3 HOH   229 729 219 HOH   HOH A . 
C 3 HOH   230 730 33  HOH   HOH A . 
C 3 HOH   231 731 207 HOH   HOH A . 
C 3 HOH   232 732 56  HOH   HOH A . 
C 3 HOH   233 733 250 HOH   HOH A . 
C 3 HOH   234 734 172 HOH   HOH A . 
C 3 HOH   235 735 167 HOH   HOH A . 
C 3 HOH   236 736 180 HOH   HOH A . 
C 3 HOH   237 737 314 HOH   HOH A . 
C 3 HOH   238 738 155 HOH   HOH A . 
C 3 HOH   239 739 97  HOH   HOH A . 
C 3 HOH   240 740 73  HOH   HOH A . 
C 3 HOH   241 741 256 HOH   HOH A . 
C 3 HOH   242 742 311 HOH   HOH A . 
C 3 HOH   243 743 297 HOH   HOH A . 
C 3 HOH   244 744 216 HOH   HOH A . 
C 3 HOH   245 745 203 HOH   HOH A . 
C 3 HOH   246 746 276 HOH   HOH A . 
C 3 HOH   247 747 81  HOH   HOH A . 
C 3 HOH   248 748 119 HOH   HOH A . 
C 3 HOH   249 749 294 HOH   HOH A . 
C 3 HOH   250 750 263 HOH   HOH A . 
C 3 HOH   251 751 220 HOH   HOH A . 
C 3 HOH   252 752 264 HOH   HOH A . 
C 3 HOH   253 753 316 HOH   HOH A . 
C 3 HOH   254 754 174 HOH   HOH A . 
C 3 HOH   255 755 122 HOH   HOH A . 
C 3 HOH   256 756 278 HOH   HOH A . 
C 3 HOH   257 757 192 HOH   HOH A . 
C 3 HOH   258 758 169 HOH   HOH A . 
C 3 HOH   259 759 232 HOH   HOH A . 
C 3 HOH   260 760 211 HOH   HOH A . 
C 3 HOH   261 761 233 HOH   HOH A . 
C 3 HOH   262 762 243 HOH   HOH A . 
C 3 HOH   263 763 124 HOH   HOH A . 
C 3 HOH   264 764 144 HOH   HOH A . 
C 3 HOH   265 765 285 HOH   HOH A . 
C 3 HOH   266 766 283 HOH   HOH A . 
C 3 HOH   267 767 70  HOH   HOH A . 
C 3 HOH   268 768 146 HOH   HOH A . 
C 3 HOH   269 769 168 HOH   HOH A . 
C 3 HOH   270 770 147 HOH   HOH A . 
C 3 HOH   271 771 141 HOH   HOH A . 
C 3 HOH   272 772 165 HOH   HOH A . 
C 3 HOH   273 773 277 HOH   HOH A . 
C 3 HOH   274 774 313 HOH   HOH A . 
C 3 HOH   275 775 133 HOH   HOH A . 
C 3 HOH   276 776 236 HOH   HOH A . 
C 3 HOH   277 777 254 HOH   HOH A . 
C 3 HOH   278 778 128 HOH   HOH A . 
C 3 HOH   279 779 193 HOH   HOH A . 
C 3 HOH   280 780 296 HOH   HOH A . 
C 3 HOH   281 781 246 HOH   HOH A . 
C 3 HOH   282 782 206 HOH   HOH A . 
C 3 HOH   283 783 288 HOH   HOH A . 
C 3 HOH   284 784 154 HOH   HOH A . 
C 3 HOH   285 785 272 HOH   HOH A . 
C 3 HOH   286 786 275 HOH   HOH A . 
C 3 HOH   287 787 74  HOH   HOH A . 
C 3 HOH   288 788 280 HOH   HOH A . 
C 3 HOH   289 789 112 HOH   HOH A . 
C 3 HOH   290 790 306 HOH   HOH A . 
C 3 HOH   291 791 226 HOH   HOH A . 
C 3 HOH   292 792 137 HOH   HOH A . 
C 3 HOH   293 793 191 HOH   HOH A . 
C 3 HOH   294 794 266 HOH   HOH A . 
C 3 HOH   295 795 48  HOH   HOH A . 
C 3 HOH   296 796 213 HOH   HOH A . 
C 3 HOH   297 797 202 HOH   HOH A . 
C 3 HOH   298 798 164 HOH   HOH A . 
C 3 HOH   299 799 215 HOH   HOH A . 
C 3 HOH   300 800 279 HOH   HOH A . 
C 3 HOH   301 801 229 HOH   HOH A . 
C 3 HOH   302 802 223 HOH   HOH A . 
C 3 HOH   303 803 267 HOH   HOH A . 
C 3 HOH   304 804 230 HOH   HOH A . 
C 3 HOH   305 805 186 HOH   HOH A . 
C 3 HOH   306 806 43  HOH   HOH A . 
C 3 HOH   307 807 302 HOH   HOH A . 
C 3 HOH   308 808 181 HOH   HOH A . 
C 3 HOH   309 809 130 HOH   HOH A . 
C 3 HOH   310 810 286 HOH   HOH A . 
C 3 HOH   311 811 187 HOH   HOH A . 
C 3 HOH   312 812 129 HOH   HOH A . 
C 3 HOH   313 813 252 HOH   HOH A . 
C 3 HOH   314 814 310 HOH   HOH A . 
C 3 HOH   315 815 303 HOH   HOH A . 
C 3 HOH   316 816 200 HOH   HOH A . 
C 3 HOH   317 817 218 HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? 1.20.1_4487 1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT    ? ? ? .           2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless        ? ? ? .           4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.410 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BSP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.659 
_cell.length_a_esd                 ? 
_cell.length_b                     81.665 
_cell.length_b_esd                 ? 
_cell.length_c                     90.140 
_cell.length_c_esd                 ? 
_cell.volume                       377899.206 
_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                         9BSP 
_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                   9BSP 
_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         2022-07-10 
_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                          16.18 
_reflns.entry_id                                       9BSP 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.6 
_reflns.d_resolution_low                               24.64 
_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                                     48841 
_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                           98.81 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.40 
_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                                0.07762 
_reflns.pdbx_Rpim_I_all                                0.02325 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.07376 
_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                                    1.6 
_reflns_shell.d_res_low                                     1.657 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4752 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.671 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               25.18 
_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                                 9BSP 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.60 
_refine.ls_d_res_low                             24.64 
_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                     48423 
_refine.ls_number_reflns_R_free                  2448 
_refine.ls_number_reflns_R_work                  45975 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.84 
_refine.ls_percent_reflns_R_free                 5.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2112 
_refine.ls_R_factor_R_free                       0.2355 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2099 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.8746 
_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                            0.2065 
_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                       1.60 
_refine_hist.d_res_low                        24.64 
_refine_hist.number_atoms_solvent             317 
_refine_hist.number_atoms_total               2713 
_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         29 
_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' ? 0.0078 ? 2451 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9676 ? 3331 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0568 ? 371  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0087 ? 433  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 7.6588 ? 333  ? 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' 1.60 1.63  . . 128 2618 97.07 . . . . 0.3276 . . . . . . . . . . . 0.3592 
'X-RAY DIFFRACTION' 1.63 1.67  . . 149 2701 98.62 . . . . 0.2878 . . . . . . . . . . . 0.2794 
'X-RAY DIFFRACTION' 1.67 1.71  . . 145 2706 99.62 . . . . 0.2534 . . . . . . . . . . . 0.2785 
'X-RAY DIFFRACTION' 1.71 1.75  . . 144 2721 99.69 . . . . 0.2422 . . . . . . . . . . . 0.2676 
'X-RAY DIFFRACTION' 1.75 1.80  . . 131 2745 99.97 . . . . 0.2550 . . . . . . . . . . . 0.2967 
'X-RAY DIFFRACTION' 1.80 1.85  . . 146 2701 99.34 . . . . 0.2543 . . . . . . . . . . . 0.3391 
'X-RAY DIFFRACTION' 1.85 1.91  . . 136 2714 99.16 . . . . 0.2510 . . . . . . . . . . . 0.2803 
'X-RAY DIFFRACTION' 1.91 1.98  . . 119 2708 98.30 . . . . 0.2508 . . . . . . . . . . . 0.3307 
'X-RAY DIFFRACTION' 1.98 2.06  . . 156 2680 97.79 . . . . 0.2500 . . . . . . . . . . . 0.2765 
'X-RAY DIFFRACTION' 2.06 2.15  . . 137 2668 97.84 . . . . 0.2364 . . . . . . . . . . . 0.2965 
'X-RAY DIFFRACTION' 2.15 2.26  . . 147 2668 98.02 . . . . 0.2276 . . . . . . . . . . . 0.2833 
'X-RAY DIFFRACTION' 2.26 2.41  . . 158 2673 98.57 . . . . 0.2341 . . . . . . . . . . . 0.2684 
'X-RAY DIFFRACTION' 2.41 2.59  . . 150 2711 98.86 . . . . 0.2219 . . . . . . . . . . . 0.2682 
'X-RAY DIFFRACTION' 2.59 2.85  . . 133 2732 99.20 . . . . 0.2070 . . . . . . . . . . . 0.2213 
'X-RAY DIFFRACTION' 2.85 3.26  . . 145 2735 99.59 . . . . 0.1916 . . . . . . . . . . . 0.1819 
'X-RAY DIFFRACTION' 3.26 4.11  . . 169 2727 99.79 . . . . 0.1684 . . . . . . . . . . . 0.1990 
'X-RAY DIFFRACTION' 4.11 24.64 . . 155 2767 98.92 . . . . 0.1584 . . . . . . . . . . . 0.1720 
# 
_struct.entry_id                     9BSP 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor VB-C-68' 
_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        9BSP 
_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              9BSP 
_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)' 3370  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  24740 ? 
# 
_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 -51.6590000000 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 ? GLY A 302 ? THR A 292 GLY A 302 1 ? 11 
# 
_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           A1ARX 
_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            A1ARX 
_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               1.817 
_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                      A1ARX 
_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                       A1ARX 
_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                        A1ARX 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 32  ? N LEU A 32  O VAL A 35  ? O VAL A 35  
AA1 5 6 N VAL A 36  ? N VAL A 36  O LEU A 89  ? O LEU A 89  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
# 
_pdbx_entry_details.entry_id                   9BSP 
_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 802 ? ? O  A HOH   808 ? ? 1.89 
2  1 O   A HOH 572 ? ? O  A HOH   744 ? ? 1.91 
3  1 O   A HOH 505 ? ? O  A HOH   602 ? ? 1.92 
4  1 O   A HOH 621 ? ? O  A HOH   716 ? ? 1.96 
5  1 O   A HOH 697 ? ? O  A HOH   740 ? ? 1.97 
6  1 O   A HOH 588 ? ? O  A HOH   761 ? ? 1.99 
7  1 O   A HOH 790 ? ? O  A HOH   815 ? ? 2.00 
8  1 ND2 A ASN 142 ? ? O  A HOH   501 ? ? 2.00 
9  1 O   A HOH 502 ? ? O  A HOH   729 ? ? 2.08 
10 1 OE1 A GLN 83  ? ? O  A HOH   502 ? ? 2.10 
11 1 O   A PHE 305 ? ? O  A HOH   503 ? ? 2.13 
12 1 SG  A CYS 145 ? ? C3 A A1ARX 401 ? ? 2.14 
13 1 ND2 A ASN 277 ? ? O  A HOH   504 ? ? 2.15 
14 1 O   A HOH 734 ? ? O  A HOH   776 ? ? 2.16 
# 
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 729 ? ? 1_555 O A HOH 802 ? ? 2_555 1.87 
2 1 O A HOH 810 ? ? 1_555 O A HOH 815 ? ? 2_555 1.99 
3 1 O A HOH 729 ? ? 1_555 O A HOH 808 ? ? 2_555 2.12 
# 
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  ? ? 51.74   -131.95 
2 1 HIS A 41  ? ? -69.50  1.77    
3 1 MET A 49  ? ? -67.97  0.95    
4 1 LEU A 50  ? ? -69.83  -80.91  
5 1 ASN A 72  ? ? -97.54  32.99   
6 1 ASN A 84  ? ? 50.66   -120.66 
7 1 TYR A 154 ? ? 44.00   -103.35 
8 1 SER A 301 ? ? -131.66 -39.12  
# 
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 560 ? C HOH . 
2 1 A HOH 653 ? C HOH . 
3 1 A HOH 699 ? C HOH . 
4 1 A HOH 786 ? C HOH . 
5 1 A HOH 798 ? C HOH . 
6 1 A HOH 804 ? 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         -12.9179097522 
_pdbx_refine_tls.origin_y         -15.0962059953 
_pdbx_refine_tls.origin_z         -1.06568232545 
_pdbx_refine_tls.T[1][1]          0.062849418767 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.00107844580662 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0128152335667 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0835890680795 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.000535680682191 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0755527383911 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.97754383784 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.398140067995 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.317746721531 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.66731378813 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.599984416073 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.31903485364 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.021556757344 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0116251425943 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.00514329167192 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0827174535044 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0249802960304 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0504654463572 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0307088298852 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0367411882242 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0148066680477 
_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                       817 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.85 
_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 
A1ARX N1   N  N N 1   
A1ARX C4   C  N N 2   
A1ARX C5   C  Y N 3   
A1ARX C6   C  Y N 4   
A1ARX C7   C  Y N 5   
A1ARX C8   C  Y N 6   
A1ARX C10  C  Y N 7   
A1ARX C13  C  Y N 8   
A1ARX C15  C  Y N 9   
A1ARX C17  C  Y N 10  
A1ARX C20  C  N N 11  
A1ARX C21  C  N N 12  
A1ARX C22  C  N N 13  
A1ARX C1   C  Y N 14  
A1ARX C11  C  Y N 15  
A1ARX C12  C  Y N 16  
A1ARX C14  C  Y N 17  
A1ARX C16  C  Y N 18  
A1ARX C18  C  Y N 19  
A1ARX C19  C  Y N 20  
A1ARX C2   C  Y N 21  
A1ARX C3   C  N N 22  
A1ARX C9   C  Y N 23  
A1ARX N2   N  Y N 24  
A1ARX O1   O  N N 25  
A1ARX O2   O  N N 26  
A1ARX O3   O  N N 27  
A1ARX CL1  CL N N 28  
A1ARX CL2  CL N N 29  
A1ARX H17  H  N N 30  
A1ARX H18  H  N N 31  
A1ARX H1   H  N N 32  
A1ARX H2   H  N N 33  
A1ARX H3   H  N N 34  
A1ARX H6   H  N N 35  
A1ARX H8   H  N N 36  
A1ARX H13  H  N N 37  
A1ARX H12  H  N N 38  
A1ARX H16  H  N N 39  
A1ARX H14  H  N N 40  
A1ARX H15  H  N N 41  
A1ARX H5   H  N N 42  
A1ARX H7   H  N N 43  
A1ARX H9   H  N N 44  
A1ARX H10  H  N N 45  
A1ARX H11  H  N N 46  
A1ARX H4   H  N N 47  
ALA   N    N  N N 48  
ALA   CA   C  N S 49  
ALA   C    C  N N 50  
ALA   O    O  N N 51  
ALA   CB   C  N N 52  
ALA   OXT  O  N N 53  
ALA   H    H  N N 54  
ALA   H2   H  N N 55  
ALA   HA   H  N N 56  
ALA   HB1  H  N N 57  
ALA   HB2  H  N N 58  
ALA   HB3  H  N N 59  
ALA   HXT  H  N N 60  
ARG   N    N  N N 61  
ARG   CA   C  N S 62  
ARG   C    C  N N 63  
ARG   O    O  N N 64  
ARG   CB   C  N N 65  
ARG   CG   C  N N 66  
ARG   CD   C  N N 67  
ARG   NE   N  N N 68  
ARG   CZ   C  N N 69  
ARG   NH1  N  N N 70  
ARG   NH2  N  N N 71  
ARG   OXT  O  N N 72  
ARG   H    H  N N 73  
ARG   H2   H  N N 74  
ARG   HA   H  N N 75  
ARG   HB2  H  N N 76  
ARG   HB3  H  N N 77  
ARG   HG2  H  N N 78  
ARG   HG3  H  N N 79  
ARG   HD2  H  N N 80  
ARG   HD3  H  N N 81  
ARG   HE   H  N N 82  
ARG   HH11 H  N N 83  
ARG   HH12 H  N N 84  
ARG   HH21 H  N N 85  
ARG   HH22 H  N N 86  
ARG   HXT  H  N N 87  
ASN   N    N  N N 88  
ASN   CA   C  N S 89  
ASN   C    C  N N 90  
ASN   O    O  N N 91  
ASN   CB   C  N N 92  
ASN   CG   C  N N 93  
ASN   OD1  O  N N 94  
ASN   ND2  N  N N 95  
ASN   OXT  O  N N 96  
ASN   H    H  N N 97  
ASN   H2   H  N N 98  
ASN   HA   H  N N 99  
ASN   HB2  H  N N 100 
ASN   HB3  H  N N 101 
ASN   HD21 H  N N 102 
ASN   HD22 H  N N 103 
ASN   HXT  H  N N 104 
ASP   N    N  N N 105 
ASP   CA   C  N S 106 
ASP   C    C  N N 107 
ASP   O    O  N N 108 
ASP   CB   C  N N 109 
ASP   CG   C  N N 110 
ASP   OD1  O  N N 111 
ASP   OD2  O  N N 112 
ASP   OXT  O  N N 113 
ASP   H    H  N N 114 
ASP   H2   H  N N 115 
ASP   HA   H  N N 116 
ASP   HB2  H  N N 117 
ASP   HB3  H  N N 118 
ASP   HD2  H  N N 119 
ASP   HXT  H  N N 120 
CYS   N    N  N N 121 
CYS   CA   C  N R 122 
CYS   C    C  N N 123 
CYS   O    O  N N 124 
CYS   CB   C  N N 125 
CYS   SG   S  N N 126 
CYS   OXT  O  N N 127 
CYS   H    H  N N 128 
CYS   H2   H  N N 129 
CYS   HA   H  N N 130 
CYS   HB2  H  N N 131 
CYS   HB3  H  N N 132 
CYS   HG   H  N N 133 
CYS   HXT  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
# 
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 
A1ARX C1  N1   sing N N 1   
A1ARX C1  C16  doub Y N 2   
A1ARX C1  C19  sing Y N 3   
A1ARX N1  C2   sing N N 4   
A1ARX N1  C3   sing N N 5   
A1ARX C2  C5   doub Y N 6   
A1ARX C2  C9   sing Y N 7   
A1ARX C3  C4   sing N N 8   
A1ARX C3  O1   doub N N 9   
A1ARX C4  C20  sing N N 10  
A1ARX C5  C6   sing Y N 11  
A1ARX C6  C7   doub Y N 12  
A1ARX C6  C10  sing N N 13  
A1ARX C7  C8   sing Y N 14  
A1ARX C8  C9   doub Y N 15  
A1ARX C10 C11  doub Y N 16  
A1ARX C10 C15  sing Y N 17  
A1ARX C11 C12  sing Y N 18  
A1ARX C12 C13  doub Y N 19  
A1ARX C12 CL1  sing N N 20  
A1ARX C13 C14  sing Y N 21  
A1ARX C14 C15  doub Y N 22  
A1ARX C16 C17  sing Y N 23  
A1ARX C17 C18  doub Y N 24  
A1ARX C17 CL2  sing N N 25  
A1ARX C18 N2   sing Y N 26  
A1ARX N2  C19  doub Y N 27  
A1ARX C20 C21  sing N N 28  
A1ARX C21 O2   sing N N 29  
A1ARX C21 O3   doub N N 30  
A1ARX O2  C22  sing N N 31  
A1ARX C4  H17  sing N N 32  
A1ARX C4  H18  sing N N 33  
A1ARX C5  H1   sing N N 34  
A1ARX C7  H2   sing N N 35  
A1ARX C8  H3   sing N N 36  
A1ARX C13 H6   sing N N 37  
A1ARX C15 H8   sing N N 38  
A1ARX C20 H13  sing N N 39  
A1ARX C20 H12  sing N N 40  
A1ARX C22 H16  sing N N 41  
A1ARX C22 H14  sing N N 42  
A1ARX C22 H15  sing N N 43  
A1ARX C11 H5   sing N N 44  
A1ARX C14 H7   sing N N 45  
A1ARX C16 H9   sing N N 46  
A1ARX C18 H10  sing N N 47  
A1ARX C19 H11  sing N N 48  
A1ARX C9  H4   sing N N 49  
ALA   N   CA   sing N N 50  
ALA   N   H    sing N N 51  
ALA   N   H2   sing N N 52  
ALA   CA  C    sing N N 53  
ALA   CA  CB   sing N N 54  
ALA   CA  HA   sing N N 55  
ALA   C   O    doub N N 56  
ALA   C   OXT  sing N N 57  
ALA   CB  HB1  sing N N 58  
ALA   CB  HB2  sing N N 59  
ALA   CB  HB3  sing N N 60  
ALA   OXT HXT  sing N N 61  
ARG   N   CA   sing N N 62  
ARG   N   H    sing N N 63  
ARG   N   H2   sing N N 64  
ARG   CA  C    sing N N 65  
ARG   CA  CB   sing N N 66  
ARG   CA  HA   sing N N 67  
ARG   C   O    doub N N 68  
ARG   C   OXT  sing N N 69  
ARG   CB  CG   sing N N 70  
ARG   CB  HB2  sing N N 71  
ARG   CB  HB3  sing N N 72  
ARG   CG  CD   sing N N 73  
ARG   CG  HG2  sing N N 74  
ARG   CG  HG3  sing N N 75  
ARG   CD  NE   sing N N 76  
ARG   CD  HD2  sing N N 77  
ARG   CD  HD3  sing N N 78  
ARG   NE  CZ   sing N N 79  
ARG   NE  HE   sing N N 80  
ARG   CZ  NH1  sing N N 81  
ARG   CZ  NH2  doub N N 82  
ARG   NH1 HH11 sing N N 83  
ARG   NH1 HH12 sing N N 84  
ARG   NH2 HH21 sing N N 85  
ARG   NH2 HH22 sing N N 86  
ARG   OXT HXT  sing N N 87  
ASN   N   CA   sing N N 88  
ASN   N   H    sing N N 89  
ASN   N   H2   sing N N 90  
ASN   CA  C    sing N N 91  
ASN   CA  CB   sing N N 92  
ASN   CA  HA   sing N N 93  
ASN   C   O    doub N N 94  
ASN   C   OXT  sing N N 95  
ASN   CB  CG   sing N N 96  
ASN   CB  HB2  sing N N 97  
ASN   CB  HB3  sing N N 98  
ASN   CG  OD1  doub N N 99  
ASN   CG  ND2  sing N N 100 
ASN   ND2 HD21 sing N N 101 
ASN   ND2 HD22 sing N N 102 
ASN   OXT HXT  sing N N 103 
ASP   N   CA   sing N N 104 
ASP   N   H    sing N N 105 
ASP   N   H2   sing N N 106 
ASP   CA  C    sing N N 107 
ASP   CA  CB   sing N N 108 
ASP   CA  HA   sing N N 109 
ASP   C   O    doub N N 110 
ASP   C   OXT  sing N N 111 
ASP   CB  CG   sing N N 112 
ASP   CB  HB2  sing N N 113 
ASP   CB  HB3  sing N N 114 
ASP   CG  OD1  doub N N 115 
ASP   CG  OD2  sing N N 116 
ASP   OD2 HD2  sing N N 117 
ASP   OXT HXT  sing N N 118 
CYS   N   CA   sing N N 119 
CYS   N   H    sing N N 120 
CYS   N   H2   sing N N 121 
CYS   CA  C    sing N N 122 
CYS   CA  CB   sing N N 123 
CYS   CA  HA   sing N N 124 
CYS   C   O    doub N N 125 
CYS   C   OXT  sing N N 126 
CYS   CB  SG   sing N N 127 
CYS   CB  HB2  sing N N 128 
CYS   CB  HB3  sing N N 129 
CYS   SG  HG   sing N N 130 
CYS   OXT HXT  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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                    9BSP 
_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]   0.019358 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002175 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012245 
_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]   0.011164 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? -33.24944 -19.27726 15.15981  1.000 25.34065 ? 1   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? -32.47593 -20.40188 14.65632  1.000 23.48701 ? 1   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? -32.43591 -20.47403 13.12465  1.000 23.23461 ? 1   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? -32.87334 -19.54684 12.43723  1.000 22.47896 ? 1   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? -33.01368 -21.70664 15.24310  1.000 31.50429 ? 1   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? -34.16087 -22.14080 14.54325  1.000 33.73834 ? 1   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? -31.87403 -21.56132 12.59865  1.000 19.99997 ? 2   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? -31.57754 -21.67091 11.18642  1.000 22.67618 ? 2   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? -30.12093 -21.35457 10.89399  1.000 20.77461 ? 2   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? -29.41997 -20.71807 11.68200  1.000 21.67942 ? 2   GLY   A O   1 
ATOM   11   N  N   . PHE   A 1 3   ? -29.66386 -21.78959 9.71813   1.000 17.84123 ? 3   PHE   A N   1 
ATOM   12   C  CA  . PHE   A 1 3   ? -28.26191 -21.60653 9.33894   1.000 17.39188 ? 3   PHE   A CA  1 
ATOM   13   C  C   . PHE   A 1 3   ? -28.15804 -21.50512 7.83020   1.000 20.47582 ? 3   PHE   A C   1 
ATOM   14   O  O   . PHE   A 1 3   ? -28.48726 -22.45522 7.10952   1.000 22.61773 ? 3   PHE   A O   1 
ATOM   15   C  CB  . PHE   A 1 3   ? -27.37355 -22.73825 9.86778   1.000 20.86300 ? 3   PHE   A CB  1 
ATOM   16   C  CG  . PHE   A 1 3   ? -25.93272 -22.32202 10.03769  1.000 19.48590 ? 3   PHE   A CG  1 
ATOM   17   C  CD1 . PHE   A 1 3   ? -25.56652 -21.52095 11.11066  1.000 23.71775 ? 3   PHE   A CD1 1 
ATOM   18   C  CD2 . PHE   A 1 3   ? -24.96815 -22.69971 9.12375   1.000 22.82653 ? 3   PHE   A CD2 1 
ATOM   19   C  CE1 . PHE   A 1 3   ? -24.25776 -21.10391 11.27176  1.000 22.17303 ? 3   PHE   A CE1 1 
ATOM   20   C  CE2 . PHE   A 1 3   ? -23.65658 -22.28652 9.27967   1.000 19.10074 ? 3   PHE   A CE2 1 
ATOM   21   C  CZ  . PHE   A 1 3   ? -23.30259 -21.49439 10.36133  1.000 20.05148 ? 3   PHE   A CZ  1 
ATOM   22   N  N   . ARG   A 1 4   ? -27.70371 -20.34639 7.36239   1.000 18.49544 ? 4   ARG   A N   1 
ATOM   23   C  CA  . ARG   A 1 4   ? -27.64539 -20.03535 5.94804   1.000 17.97834 ? 4   ARG   A CA  1 
ATOM   24   C  C   . ARG   A 1 4   ? -26.24173 -19.57633 5.57918   1.000 16.06541 ? 4   ARG   A C   1 
ATOM   25   O  O   . ARG   A 1 4   ? -25.51642 -19.00916 6.40086   1.000 18.73075 ? 4   ARG   A O   1 
ATOM   26   C  CB  . ARG   A 1 4   ? -28.64040 -18.94159 5.58456   1.000 18.05791 ? 4   ARG   A CB  1 
ATOM   27   C  CG  . ARG   A 1 4   ? -30.06475 -19.42688 5.54138   1.000 19.51812 ? 4   ARG   A CG  1 
ATOM   28   C  CD  . ARG   A 1 4   ? -30.30333 -20.07519 4.19091   1.000 20.83518 ? 4   ARG   A CD  1 
ATOM   29   N  NE  . ARG   A 1 4   ? -31.70901 -20.40219 3.95898   1.000 23.95952 ? 4   ARG   A NE  1 
ATOM   30   C  CZ  . ARG   A 1 4   ? -32.13112 -21.02094 2.86528   1.000 22.62611 ? 4   ARG   A CZ  1 
ATOM   31   N  NH1 . ARG   A 1 4   ? -31.28501 -21.39123 1.91397   1.000 23.29261 ? 4   ARG   A NH1 1 
ATOM   32   N  NH2 . ARG   A 1 4   ? -33.41807 -21.32005 2.74336   1.000 17.65275 ? 4   ARG   A NH2 1 
ATOM   33   N  N   . LYS   A 1 5   ? -25.87694 -19.79014 4.31945   1.000 17.69911 ? 5   LYS   A N   1 
ATOM   34   C  CA  . LYS   A 1 5   ? -24.66304 -19.17300 3.79573   1.000 18.81770 ? 5   LYS   A CA  1 
ATOM   35   C  C   . LYS   A 1 5   ? -24.94756 -17.68736 3.63858   1.000 18.09693 ? 5   LYS   A C   1 
ATOM   36   O  O   . LYS   A 1 5   ? -25.58909 -17.26418 2.67674   1.000 24.12182 ? 5   LYS   A O   1 
ATOM   37   C  CB  . LYS   A 1 5   ? -24.24459 -19.80585 2.47377   1.000 22.85187 ? 5   LYS   A CB  1 
ATOM   38   C  CG  . LYS   A 1 5   ? -22.73318 -19.80044 2.23203   1.000 26.89321 ? 5   LYS   A CG  1 
ATOM   39   C  CD  . LYS   A 1 5   ? -22.26742 -21.06890 1.53042   1.000 27.06237 ? 5   LYS   A CD  1 
ATOM   40   C  CE  . LYS   A 1 5   ? -21.69870 -22.07904 2.51073   1.000 28.08538 ? 5   LYS   A CE  1 
ATOM   41   N  NZ  . LYS   A 1 5   ? -21.20196 -23.27199 1.78305   1.000 30.37543 ? 5   LYS   A NZ  1 
ATOM   42   N  N   . MET   A 1 6   ? -24.47824 -16.89785 4.59186   1.000 13.18285 ? 6   MET   A N   1 
ATOM   43   C  CA  . MET   A 1 6   ? -24.87209 -15.50737 4.73674   1.000 14.21258 ? 6   MET   A CA  1 
ATOM   44   C  C   . MET   A 1 6   ? -23.71733 -14.58345 4.38254   1.000 16.04277 ? 6   MET   A C   1 
ATOM   45   O  O   . MET   A 1 6   ? -22.58450 -14.77776 4.84699   1.000 15.70506 ? 6   MET   A O   1 
ATOM   46   C  CB  . MET   A 1 6   ? -25.36240 -15.26953 6.17298   1.000 16.05825 ? 6   MET   A CB  1 
ATOM   47   C  CG  . MET   A 1 6   ? -25.78803 -13.86474 6.47079   1.000 21.33515 ? 6   MET   A CG  1 
ATOM   48   S  SD  . MET   A 1 6   ? -26.24697 -13.79571 8.21524   1.000 32.08458 ? 6   MET   A SD  1 
ATOM   49   C  CE  . MET   A 1 6   ? -27.45480 -15.10666 8.27391   1.000 20.57856 ? 6   MET   A CE  1 
ATOM   50   N  N   . ALA   A 1 7   ? -23.98651 -13.61662 3.51936   1.000 12.65202 ? 7   ALA   A N   1 
ATOM   51   C  CA  . ALA   A 1 7   ? -22.96453 -12.65892 3.12795   1.000 10.75873 ? 7   ALA   A CA  1 
ATOM   52   C  C   . ALA   A 1 7   ? -23.11694 -11.39304 3.95969   1.000 13.55986 ? 7   ALA   A C   1 
ATOM   53   O  O   . ALA   A 1 7   ? -24.12900 -11.17400 4.62140   1.000 13.99287 ? 7   ALA   A O   1 
ATOM   54   C  CB  . ALA   A 1 7   ? -23.06559 -12.33980 1.63677   1.000 13.08315 ? 7   ALA   A CB  1 
ATOM   55   N  N   . PHE   A 1 8   ? -22.08511 -10.55629 3.93998   1.000 10.19756 ? 8   PHE   A N   1 
ATOM   56   C  CA  . PHE   A 1 8   ? -22.21074 -9.25402  4.56449   1.000 10.89241 ? 8   PHE   A CA  1 
ATOM   57   C  C   . PHE   A 1 8   ? -23.09207 -8.34385  3.72021   1.000 10.41382 ? 8   PHE   A C   1 
ATOM   58   O  O   . PHE   A 1 8   ? -23.16214 -8.50387  2.49925   1.000 12.60160 ? 8   PHE   A O   1 
ATOM   59   C  CB  . PHE   A 1 8   ? -20.82547 -8.61868  4.75173   1.000 12.03416 ? 8   PHE   A CB  1 
ATOM   60   C  CG  . PHE   A 1 8   ? -20.02517 -9.26284  5.85282   1.000 13.18623 ? 8   PHE   A CG  1 
ATOM   61   C  CD1 . PHE   A 1 8   ? -20.26365 -8.93530  7.17664   1.000 17.69510 ? 8   PHE   A CD1 1 
ATOM   62   C  CD2 . PHE   A 1 8   ? -19.01794 -10.16889 5.56330   1.000 15.91399 ? 8   PHE   A CD2 1 
ATOM   63   C  CE1 . PHE   A 1 8   ? -19.53602 -9.52237  8.18367   1.000 25.33307 ? 8   PHE   A CE1 1 
ATOM   64   C  CE2 . PHE   A 1 8   ? -18.28642 -10.76208 6.59035   1.000 16.77818 ? 8   PHE   A CE2 1 
ATOM   65   C  CZ  . PHE   A 1 8   ? -18.53568 -10.42651 7.88429   1.000 17.60134 ? 8   PHE   A CZ  1 
ATOM   66   N  N   . PRO   A 1 9   ? -23.78608 -7.39019  4.34830   1.000 12.21800 ? 9   PRO   A N   1 
ATOM   67   C  CA  . PRO   A 1 9   ? -24.54376 -6.40201  3.57042   1.000 15.28088 ? 9   PRO   A CA  1 
ATOM   68   C  C   . PRO   A 1 9   ? -23.58572 -5.66604  2.65044   1.000 14.01890 ? 9   PRO   A C   1 
ATOM   69   O  O   . PRO   A 1 9   ? -22.47225 -5.30566  3.04779   1.000 15.87534 ? 9   PRO   A O   1 
ATOM   70   C  CB  . PRO   A 1 9   ? -25.14224 -5.47483  4.63827   1.000 15.24541 ? 9   PRO   A CB  1 
ATOM   71   C  CG  . PRO   A 1 9   ? -25.04237 -6.25081  5.94353   1.000 15.55283 ? 9   PRO   A CG  1 
ATOM   72   C  CD  . PRO   A 1 9   ? -23.81674 -7.11964  5.79636   1.000 12.37493 ? 9   PRO   A CD  1 
ATOM   73   N  N   . SER   A 1 10  ? -23.99402 -5.49744  1.39551   1.000 14.45313 ? 10  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 10  ? -23.06769 -5.08583  0.34743   1.000 14.19213 ? 10  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 10  ? -23.07310 -3.59270  0.04861   1.000 12.88188 ? 10  SER   A C   1 
ATOM   76   O  O   . SER   A 1 10  ? -22.25682 -3.14975  -0.76858  1.000 13.42252 ? 10  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 10  ? -23.35210 -5.86544  -0.93707  1.000 11.22756 ? 10  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 10  ? -24.69973 -5.74456  -1.31774  1.000 14.43629 ? 10  SER   A OG  1 
ATOM   79   N  N   . GLY   A 1 11  ? -23.94657 -2.80980  0.68747   1.000 13.54398 ? 11  GLY   A N   1 
ATOM   80   C  CA  . GLY   A 1 11  ? -24.09783 -1.40889  0.31615   1.000 14.65172 ? 11  GLY   A CA  1 
ATOM   81   C  C   . GLY   A 1 11  ? -22.79917 -0.62884  0.30405   1.000 14.57914 ? 11  GLY   A C   1 
ATOM   82   O  O   . GLY   A 1 11  ? -22.54763 0.14404   -0.61947  1.000 16.87585 ? 11  GLY   A O   1 
ATOM   83   N  N   . LYS   A 1 12  ? -21.97350 -0.80374  1.34267   1.000 14.04181 ? 12  LYS   A N   1 
ATOM   84   C  CA  . LYS   A 1 12  ? -20.73310 -0.03116  1.44140   1.000 15.08656 ? 12  LYS   A CA  1 
ATOM   85   C  C   . LYS   A 1 12  ? -19.81380 -0.31606  0.26899   1.000 17.77703 ? 12  LYS   A C   1 
ATOM   86   O  O   . LYS   A 1 12  ? -19.03869 0.55784   -0.14378  1.000 18.31669 ? 12  LYS   A O   1 
ATOM   87   C  CB  . LYS   A 1 12  ? -20.02392 -0.34372  2.76313   1.000 17.88113 ? 12  LYS   A CB  1 
ATOM   88   C  CG  . LYS   A 1 12  ? -20.57191 0.41422   3.96710   1.000 19.62201 ? 12  LYS   A CG  1 
ATOM   89   C  CD  . LYS   A 1 12  ? -19.92631 -0.07288  5.26262   1.000 24.88012 ? 12  LYS   A CD  1 
ATOM   90   C  CE  . LYS   A 1 12  ? -20.46764 0.68747   6.47087   1.000 30.80074 ? 12  LYS   A CE  1 
ATOM   91   N  NZ  . LYS   A 1 12  ? -21.92893 0.46577   6.65430   1.000 35.96103 ? 12  LYS   A NZ  1 
ATOM   92   N  N   . VAL   A 1 13  ? -19.87433 -1.52512  -0.27702  1.000 14.12358 ? 13  VAL   A N   1 
ATOM   93   C  CA  . VAL   A 1 13  ? -19.04827 -1.84335  -1.44020  1.000 14.35684 ? 13  VAL   A CA  1 
ATOM   94   C  C   . VAL   A 1 13  ? -19.72858 -1.40377  -2.73056  1.000 12.31701 ? 13  VAL   A C   1 
ATOM   95   O  O   . VAL   A 1 13  ? -19.06016 -0.96475  -3.66854  1.000 14.34643 ? 13  VAL   A O   1 
ATOM   96   C  CB  . VAL   A 1 13  ? -18.72967 -3.34430  -1.44569  1.000 12.65266 ? 13  VAL   A CB  1 
ATOM   97   C  CG1 . VAL   A 1 13  ? -17.86374 -3.72793  -2.66780  1.000 14.31238 ? 13  VAL   A CG1 1 
ATOM   98   C  CG2 . VAL   A 1 13  ? -18.00187 -3.71372  -0.15035  1.000 14.61885 ? 13  VAL   A CG2 1 
ATOM   99   N  N   . GLU   A 1 14  ? -21.06703 -1.49181  -2.79676  1.000 12.86105 ? 14  GLU   A N   1 
ATOM   100  C  CA  . GLU   A 1 14  ? -21.74820 -1.05548  -4.01134  1.000 13.67349 ? 14  GLU   A CA  1 
ATOM   101  C  C   . GLU   A 1 14  ? -21.37239 0.37002   -4.37094  1.000 14.63980 ? 14  GLU   A C   1 
ATOM   102  O  O   . GLU   A 1 14  ? -21.23003 0.70509   -5.55267  1.000 17.58456 ? 14  GLU   A O   1 
ATOM   103  C  CB  . GLU   A 1 14  ? -23.26894 -1.15835  -3.85223  1.000 14.44856 ? 14  GLU   A CB  1 
ATOM   104  C  CG  . GLU   A 1 14  ? -23.78996 -2.58517  -3.67083  1.000 13.72033 ? 14  GLU   A CG  1 
ATOM   105  C  CD  . GLU   A 1 14  ? -25.25170 -2.61504  -3.23254  1.000 14.60176 ? 14  GLU   A CD  1 
ATOM   106  O  OE1 . GLU   A 1 14  ? -26.09741 -1.90393  -3.82449  1.000 18.79257 ? 14  GLU   A OE1 1 
ATOM   107  O  OE2 . GLU   A 1 14  ? -25.52750 -3.34263  -2.26141  1.000 14.59831 ? 14  GLU   A OE2 1 
ATOM   108  N  N   . GLY   A 1 15  ? -21.20001 1.22718   -3.36893  1.000 15.84026 ? 15  GLY   A N   1 
ATOM   109  C  CA  . GLY   A 1 15  ? -20.91252 2.62139   -3.63666  1.000 18.74277 ? 15  GLY   A CA  1 
ATOM   110  C  C   . GLY   A 1 15  ? -19.51435 2.89992   -4.12515  1.000 18.53727 ? 15  GLY   A C   1 
ATOM   111  O  O   . GLY   A 1 15  ? -19.17093 4.05425   -4.40959  1.000 18.88085 ? 15  GLY   A O   1 
ATOM   112  N  N   . CYS   A 1 16  ? -18.69039 1.86134   -4.20264  1.000 14.61277 ? 16  CYS   A N   1 
ATOM   113  C  CA  . CYS   A 1 16  ? -17.33209 1.96150   -4.71035  1.000 14.49740 ? 16  CYS   A CA  1 
ATOM   114  C  C   . CYS   A 1 16  ? -17.15921 1.39684   -6.11291  1.000 15.90030 ? 16  CYS   A C   1 
ATOM   115  O  O   . CYS   A 1 16  ? -16.08211 1.56204   -6.69678  1.000 16.70631 ? 16  CYS   A O   1 
ATOM   116  C  CB  . CYS   A 1 16  ? -16.36202 1.24816   -3.76266  1.000 13.61517 ? 16  CYS   A CB  1 
ATOM   117  S  SG  . CYS   A 1 16  ? -16.40456 1.90810   -2.08534  1.000 17.91240 ? 16  CYS   A SG  1 
ATOM   118  N  N   . MET   A 1 17  ? -18.15781 0.71437   -6.66337  1.000 16.24521 ? 17  MET   A N   1 
ATOM   119  C  CA  . MET   A 1 17  ? -17.94762 -0.00580  -7.91195  1.000 13.65871 ? 17  MET   A CA  1 
ATOM   120  C  C   . MET   A 1 17  ? -18.10859 0.94594   -9.09215  1.000 16.36310 ? 17  MET   A C   1 
ATOM   121  O  O   . MET   A 1 17  ? -19.05062 1.74356   -9.13805  1.000 18.72471 ? 17  MET   A O   1 
ATOM   122  C  CB  . MET   A 1 17  ? -18.92804 -1.17075  -8.04387  1.000 14.24149 ? 17  MET   A CB  1 
ATOM   123  C  CG  . MET   A 1 17  ? -18.75177 -2.22250  -6.94628  1.000 12.12942 ? 17  MET   A CG  1 
ATOM   124  S  SD  . MET   A 1 17  ? -17.06631 -2.80664  -6.69086  1.000 13.61784 ? 17  MET   A SD  1 
ATOM   125  C  CE  . MET   A 1 17  ? -16.59627 -3.38490  -8.33741  1.000 13.20866 ? 17  MET   A CE  1 
ATOM   126  N  N   . VAL   A 1 18  ? -17.17599 0.85463   -10.04015 1.000 15.77435 ? 18  VAL   A N   1 
ATOM   127  C  CA  . VAL   A 1 18  ? -17.14989 1.66221   -11.25266 1.000 18.62865 ? 18  VAL   A CA  1 
ATOM   128  C  C   . VAL   A 1 18  ? -16.81603 0.76022   -12.43696 1.000 17.18980 ? 18  VAL   A C   1 
ATOM   129  O  O   . VAL   A 1 18  ? -16.38301 -0.37977  -12.28333 1.000 16.34297 ? 18  VAL   A O   1 
ATOM   130  C  CB  . VAL   A 1 18  ? -16.12946 2.82195   -11.17503 1.000 18.51061 ? 18  VAL   A CB  1 
ATOM   131  C  CG1 . VAL   A 1 18  ? -16.42876 3.72831   -9.98802  1.000 21.05472 ? 18  VAL   A CG1 1 
ATOM   132  C  CG2 . VAL   A 1 18  ? -14.70580 2.27050   -11.09766 1.000 18.76635 ? 18  VAL   A CG2 1 
ATOM   133  N  N   . GLN   A 1 19  ? -17.02101 1.30707   -13.63122 1.000 20.43991 ? 19  GLN   A N   1 
ATOM   134  C  CA  . GLN   A 1 19  ? -16.69346 0.66269   -14.89645 1.000 23.38514 ? 19  GLN   A CA  1 
ATOM   135  C  C   . GLN   A 1 19  ? -15.37584 1.23124   -15.41190 1.000 19.03998 ? 19  GLN   A C   1 
ATOM   136  O  O   . GLN   A 1 19  ? -15.19469 2.45323   -15.44448 1.000 20.62895 ? 19  GLN   A O   1 
ATOM   137  C  CB  . GLN   A 1 19  ? -17.81534 0.89889   -15.91024 1.000 25.61688 ? 19  GLN   A CB  1 
ATOM   138  C  CG  . GLN   A 1 19  ? -17.74766 0.06966   -17.17219 1.000 30.13614 ? 19  GLN   A CG  1 
ATOM   139  C  CD  . GLN   A 1 19  ? -19.00645 0.19691   -18.02168 1.000 30.95594 ? 19  GLN   A CD  1 
ATOM   140  O  OE1 . GLN   A 1 19  ? -19.71032 1.20945   -17.97248 1.000 40.08184 ? 19  GLN   A OE1 1 
ATOM   141  N  NE2 . GLN   A 1 19  ? -19.28868 -0.82686  -18.81484 1.000 36.82337 ? 19  GLN   A NE2 1 
ATOM   142  N  N   . VAL   A 1 20  ? -14.44771 0.35488   -15.78708 1.000 18.41017 ? 20  VAL   A N   1 
ATOM   143  C  CA  . VAL   A 1 20  ? -13.17284 0.77908   -16.35768 1.000 23.05583 ? 20  VAL   A CA  1 
ATOM   144  C  C   . VAL   A 1 20  ? -13.06967 0.24140   -17.77883 1.000 20.41506 ? 20  VAL   A C   1 
ATOM   145  O  O   . VAL   A 1 20  ? -13.19857 -0.96378  -17.99938 1.000 21.75562 ? 20  VAL   A O   1 
ATOM   146  C  CB  . VAL   A 1 20  ? -11.97997 0.30853   -15.50445 1.000 22.44747 ? 20  VAL   A CB  1 
ATOM   147  C  CG1 . VAL   A 1 20  ? -10.67697 0.74029   -16.15443 1.000 22.69521 ? 20  VAL   A CG1 1 
ATOM   148  C  CG2 . VAL   A 1 20  ? -12.06877 0.89255   -14.11249 1.000 20.37922 ? 20  VAL   A CG2 1 
ATOM   149  N  N   . THR   A 1 21  ? -12.83453 1.12897   -18.74468 1.000 21.88672 ? 21  THR   A N   1 
ATOM   150  C  CA  . THR   A 1 21  ? -12.70862 0.72394   -20.13744 1.000 24.66479 ? 21  THR   A CA  1 
ATOM   151  C  C   . THR   A 1 21  ? -11.37651 1.20357   -20.69259 1.000 25.50913 ? 21  THR   A C   1 
ATOM   152  O  O   . THR   A 1 21  ? -11.02740 2.38091   -20.55452 1.000 27.94847 ? 21  THR   A O   1 
ATOM   153  C  CB  . THR   A 1 21  ? -13.85078 1.28430   -20.99267 1.000 27.27161 ? 21  THR   A CB  1 
ATOM   154  O  OG1 . THR   A 1 21  ? -15.09550 0.75621   -20.52729 1.000 27.07361 ? 21  THR   A OG1 1 
ATOM   155  C  CG2 . THR   A 1 21  ? -13.66150 0.87794   -22.44170 1.000 28.60056 ? 21  THR   A CG2 1 
ATOM   156  N  N   . CYS   A 1 22  ? -10.64071 0.29387   -21.32410 1.000 27.46835 ? 22  CYS   A N   1 
ATOM   157  C  CA  . CYS   A 1 22  ? -9.42233  0.64839   -22.03599 1.000 27.85596 ? 22  CYS   A CA  1 
ATOM   158  C  C   . CYS   A 1 22  ? -9.46779  -0.07479  -23.37266 1.000 31.26078 ? 22  CYS   A C   1 
ATOM   159  O  O   . CYS   A 1 22  ? -9.49806  -1.30849  -23.41070 1.000 31.27090 ? 22  CYS   A O   1 
ATOM   160  C  CB  . CYS   A 1 22  ? -8.17056  0.27485   -21.22717 1.000 27.06208 ? 22  CYS   A CB  1 
ATOM   161  S  SG  . CYS   A 1 22  ? -6.60699  0.56167   -22.08270 1.000 33.41254 ? 22  CYS   A SG  1 
ATOM   162  N  N   . GLY   A 1 23  ? -9.53450  0.69009   -24.46027 1.000 32.23041 ? 23  GLY   A N   1 
ATOM   163  C  CA  . GLY   A 1 23  ? -9.71559  0.11075   -25.77974 1.000 31.74820 ? 23  GLY   A CA  1 
ATOM   164  C  C   . GLY   A 1 23  ? -11.06711 -0.56154  -25.90894 1.000 32.79291 ? 23  GLY   A C   1 
ATOM   165  O  O   . GLY   A 1 23  ? -12.10109 0.07607   -25.69579 1.000 36.53288 ? 23  GLY   A O   1 
ATOM   166  N  N   . THR   A 1 24  ? -11.08513 -1.84738  -26.24770 1.000 32.40338 ? 24  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 24  ? -12.33557 -2.58954  -26.32900 1.000 36.05909 ? 24  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 24  ? -12.59432 -3.44644  -25.10005 1.000 33.66032 ? 24  THR   A C   1 
ATOM   169  O  O   . THR   A 1 24  ? -13.60842 -4.15277  -25.05952 1.000 37.62016 ? 24  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 24  ? -12.36781 -3.47307  -27.58643 1.000 36.91869 ? 24  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 24  ? -11.36281 -4.49037  -27.49905 1.000 40.42312 ? 24  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 24  ? -12.14010 -2.63968  -28.83376 1.000 35.51203 ? 24  THR   A CG2 1 
ATOM   173  N  N   . THR   A 1 25  ? -11.71799 -3.39016  -24.09666 1.000 32.89918 ? 25  THR   A N   1 
ATOM   174  C  CA  . THR   A 1 25  ? -11.86296 -4.18242  -22.88213 1.000 32.86087 ? 25  THR   A CA  1 
ATOM   175  C  C   . THR   A 1 25  ? -12.57046 -3.35270  -21.81343 1.000 28.66158 ? 25  THR   A C   1 
ATOM   176  O  O   . THR   A 1 25  ? -12.12879 -2.24709  -21.48438 1.000 28.57749 ? 25  THR   A O   1 
ATOM   177  C  CB  . THR   A 1 25  ? -10.49724 -4.65127  -22.37921 1.000 32.24299 ? 25  THR   A CB  1 
ATOM   178  O  OG1 . THR   A 1 25  ? -9.92221  -5.56374  -23.32405 1.000 37.07379 ? 25  THR   A OG1 1 
ATOM   179  C  CG2 . THR   A 1 25  ? -10.64109 -5.35708  -21.03564 1.000 31.56184 ? 25  THR   A CG2 1 
ATOM   180  N  N   . THR   A 1 26  ? -13.67363 -3.87301  -21.28691 1.000 27.47972 ? 26  THR   A N   1 
ATOM   181  C  CA  . THR   A 1 26  ? -14.38732 -3.23252  -20.18957 1.000 27.74546 ? 26  THR   A CA  1 
ATOM   182  C  C   . THR   A 1 26  ? -14.43732 -4.20078  -19.01191 1.000 24.80808 ? 26  THR   A C   1 
ATOM   183  O  O   . THR   A 1 26  ? -14.74553 -5.38360  -19.19208 1.000 25.44513 ? 26  THR   A O   1 
ATOM   184  C  CB  . THR   A 1 26  ? -15.79865 -2.82032  -20.61959 1.000 28.98336 ? 26  THR   A CB  1 
ATOM   185  O  OG1 . THR   A 1 26  ? -15.72751 -1.71450  -21.52912 1.000 34.19978 ? 26  THR   A OG1 1 
ATOM   186  C  CG2 . THR   A 1 26  ? -16.61463 -2.40329  -19.42860 1.000 29.28843 ? 26  THR   A CG2 1 
ATOM   187  N  N   . LEU   A 1 27  ? -14.10544 -3.71521  -17.81785 1.000 19.71290 ? 27  LEU   A N   1 
ATOM   188  C  CA  . LEU   A 1 27  ? -14.27447 -4.52001  -16.61164 1.000 19.49495 ? 27  LEU   A CA  1 
ATOM   189  C  C   . LEU   A 1 27  ? -14.60720 -3.58833  -15.44561 1.000 16.21227 ? 27  LEU   A C   1 
ATOM   190  O  O   . LEU   A 1 27  ? -14.95751 -2.41712  -15.64047 1.000 18.16118 ? 27  LEU   A O   1 
ATOM   191  C  CB  . LEU   A 1 27  ? -13.03776 -5.39282  -16.34983 1.000 18.27308 ? 27  LEU   A CB  1 
ATOM   192  C  CG  . LEU   A 1 27  ? -11.64891 -4.77375  -16.53997 1.000 16.96532 ? 27  LEU   A CG  1 
ATOM   193  C  CD1 . LEU   A 1 27  ? -11.38477 -3.66922  -15.52741 1.000 17.01361 ? 27  LEU   A CD1 1 
ATOM   194  C  CD2 . LEU   A 1 27  ? -10.58887 -5.86954  -16.41768 1.000 20.92290 ? 27  LEU   A CD2 1 
ATOM   195  N  N   . ASN   A 1 28  ? -14.54307 -4.12336  -14.23736 1.000 16.97090 ? 28  ASN   A N   1 
ATOM   196  C  CA  . ASN   A 1 28  ? -14.93602 -3.39719  -13.04002 1.000 15.70624 ? 28  ASN   A CA  1 
ATOM   197  C  C   . ASN   A 1 28  ? -13.71686 -2.83620  -12.34089 1.000 13.40089 ? 28  ASN   A C   1 
ATOM   198  O  O   . ASN   A 1 28  ? -12.63755 -3.43299  -12.37716 1.000 14.17408 ? 28  ASN   A O   1 
ATOM   199  C  CB  . ASN   A 1 28  ? -15.68853 -4.31745  -12.07601 1.000 14.69293 ? 28  ASN   A CB  1 
ATOM   200  C  CG  . ASN   A 1 28  ? -16.87953 -4.97076  -12.73421 1.000 17.55151 ? 28  ASN   A CG  1 
ATOM   201  O  OD1 . ASN   A 1 28  ? -17.92151 -4.33840  -12.92324 1.000 17.54586 ? 28  ASN   A OD1 1 
ATOM   202  N  ND2 . ASN   A 1 28  ? -16.71675 -6.23427  -13.13862 1.000 16.14716 ? 28  ASN   A ND2 1 
ATOM   203  N  N   . GLY   A 1 29  ? -13.90528 -1.68692  -11.68048 1.000 14.42942 ? 29  GLY   A N   1 
ATOM   204  C  CA  . GLY   A 1 29  ? -12.88428 -1.12920  -10.81949 1.000 15.91440 ? 29  GLY   A CA  1 
ATOM   205  C  C   . GLY   A 1 29  ? -13.46142 -0.75577  -9.46437  1.000 14.27995 ? 29  GLY   A C   1 
ATOM   206  O  O   . GLY   A 1 29  ? -14.67445 -0.67308  -9.28715  1.000 13.94603 ? 29  GLY   A O   1 
ATOM   207  N  N   . LEU   A 1 30  ? -12.56416 -0.51739  -8.51633  1.000 13.82934 ? 30  LEU   A N   1 
ATOM   208  C  CA  . LEU   A 1 30  ? -12.92138 -0.20869  -7.13530  1.000 16.16877 ? 30  LEU   A CA  1 
ATOM   209  C  C   . LEU   A 1 30  ? -12.43667 1.19613   -6.82075  1.000 14.32534 ? 30  LEU   A C   1 
ATOM   210  O  O   . LEU   A 1 30  ? -11.23003 1.46364   -6.84108  1.000 15.58758 ? 30  LEU   A O   1 
ATOM   211  C  CB  . LEU   A 1 30  ? -12.33876 -1.23645  -6.15535  1.000 13.26199 ? 30  LEU   A CB  1 
ATOM   212  C  CG  . LEU   A 1 30  ? -12.66931 -1.07867  -4.66260  1.000 10.80603 ? 30  LEU   A CG  1 
ATOM   213  C  CD1 . LEU   A 1 30  ? -14.13078 -1.46295  -4.34903  1.000 12.97952 ? 30  LEU   A CD1 1 
ATOM   214  C  CD2 . LEU   A 1 30  ? -11.76145 -1.95230  -3.78306  1.000 12.01179 ? 30  LEU   A CD2 1 
ATOM   215  N  N   . TRP   A 1 31  ? -13.37254 2.08768   -6.53110  1.000 14.82730 ? 31  TRP   A N   1 
ATOM   216  C  CA  . TRP   A 1 31  ? -13.09488 3.51746   -6.41414  1.000 14.81872 ? 31  TRP   A CA  1 
ATOM   217  C  C   . TRP   A 1 31  ? -13.07919 3.86404   -4.92987  1.000 16.92101 ? 31  TRP   A C   1 
ATOM   218  O  O   . TRP   A 1 31  ? -14.12633 3.85977   -4.27641  1.000 16.67750 ? 31  TRP   A O   1 
ATOM   219  C  CB  . TRP   A 1 31  ? -14.15917 4.31689   -7.16484  1.000 15.93832 ? 31  TRP   A CB  1 
ATOM   220  C  CG  . TRP   A 1 31  ? -14.02172 5.81279   -7.15808  1.000 19.62117 ? 31  TRP   A CG  1 
ATOM   221  C  CD1 . TRP   A 1 31  ? -12.88069 6.54345   -6.96530  1.000 17.87810 ? 31  TRP   A CD1 1 
ATOM   222  C  CD2 . TRP   A 1 31  ? -15.07675 6.76411   -7.35793  1.000 19.95319 ? 31  TRP   A CD2 1 
ATOM   223  N  NE1 . TRP   A 1 31  ? -13.16486 7.88998   -7.03549  1.000 19.42662 ? 31  TRP   A NE1 1 
ATOM   224  C  CE2 . TRP   A 1 31  ? -14.50388 8.05426   -7.28027  1.000 22.50787 ? 31  TRP   A CE2 1 
ATOM   225  C  CE3 . TRP   A 1 31  ? -16.45243 6.64701   -7.59152  1.000 26.32026 ? 31  TRP   A CE3 1 
ATOM   226  C  CZ2 . TRP   A 1 31  ? -15.26011 9.22341   -7.42884  1.000 25.17515 ? 31  TRP   A CZ2 1 
ATOM   227  C  CZ3 . TRP   A 1 31  ? -17.19794 7.79659   -7.74025  1.000 24.28552 ? 31  TRP   A CZ3 1 
ATOM   228  C  CH2 . TRP   A 1 31  ? -16.60345 9.07313   -7.65164  1.000 23.59419 ? 31  TRP   A CH2 1 
ATOM   229  N  N   . LEU   A 1 32  ? -11.88893 4.13094   -4.39181  1.000 15.39675 ? 32  LEU   A N   1 
ATOM   230  C  CA  . LEU   A 1 32  ? -11.71959 4.51398   -2.99573  1.000 16.31796 ? 32  LEU   A CA  1 
ATOM   231  C  C   . LEU   A 1 32  ? -10.90773 5.79447   -2.95356  1.000 18.52154 ? 32  LEU   A C   1 
ATOM   232  O  O   . LEU   A 1 32  ? -9.81712  5.85169   -3.53189  1.000 20.02471 ? 32  LEU   A O   1 
ATOM   233  C  CB  . LEU   A 1 32  ? -10.99570 3.43282   -2.19053  1.000 15.51902 ? 32  LEU   A CB  1 
ATOM   234  C  CG  . LEU   A 1 32  ? -11.62739 2.05193   -2.18906  1.000 14.92469 ? 32  LEU   A CG  1 
ATOM   235  C  CD1 . LEU   A 1 32  ? -10.65326 0.99726   -1.68166  1.000 15.13180 ? 32  LEU   A CD1 1 
ATOM   236  C  CD2 . LEU   A 1 32  ? -12.85285 2.10170   -1.32268  1.000 15.92515 ? 32  LEU   A CD2 1 
ATOM   237  N  N   . ASP   A 1 33  ? -11.41656 6.80669   -2.25193  1.000 21.52129 ? 33  ASP   A N   1 
ATOM   238  C  CA  . ASP   A 1 33  ? -10.80368 8.13719   -2.25820  1.000 23.02289 ? 33  ASP   A CA  1 
ATOM   239  C  C   . ASP   A 1 33  ? -10.63532 8.51789   -3.73150  1.000 23.81984 ? 33  ASP   A C   1 
ATOM   240  O  O   . ASP   A 1 33  ? -11.57626 8.32269   -4.51411  1.000 24.14585 ? 33  ASP   A O   1 
ATOM   241  C  CB  . ASP   A 1 33  ? -9.53181  8.12893   -1.41055  1.000 24.58124 ? 33  ASP   A CB  1 
ATOM   242  C  CG  . ASP   A 1 33  ? -9.79483  7.70044   0.03445   1.000 27.65504 ? 33  ASP   A CG  1 
ATOM   243  O  OD1 . ASP   A 1 33  ? -10.70812 8.27084   0.66710   1.000 32.72528 ? 33  ASP   A OD1 1 
ATOM   244  O  OD2 . ASP   A 1 33  ? -9.10315  6.78964   0.53585   1.000 29.50666 ? 33  ASP   A OD2 1 
ATOM   245  N  N   . ASP   A 1 34  ? -9.46903  8.99919   -4.16774  1.000 21.95599 ? 34  ASP   A N   1 
ATOM   246  C  CA  . ASP   A 1 34  ? -9.29982  9.41060   -5.55879  1.000 23.24352 ? 34  ASP   A CA  1 
ATOM   247  C  C   . ASP   A 1 34  ? -8.51550  8.39275   -6.38900  1.000 23.60841 ? 34  ASP   A C   1 
ATOM   248  O  O   . ASP   A 1 34  ? -7.81431  8.76852   -7.33474  1.000 22.35377 ? 34  ASP   A O   1 
ATOM   249  C  CB  . ASP   A 1 34  ? -8.64493  10.79387  -5.63995  1.000 24.76171 ? 34  ASP   A CB  1 
ATOM   250  C  CG  . ASP   A 1 34  ? -7.24741  10.81972  -5.05634  1.000 27.48882 ? 34  ASP   A CG  1 
ATOM   251  O  OD1 . ASP   A 1 34  ? -6.86701  9.85091   -4.36429  1.000 24.97860 ? 34  ASP   A OD1 1 
ATOM   252  O  OD2 . ASP   A 1 34  ? -6.52277  11.81771  -5.29912  1.000 29.94790 ? 34  ASP   A OD2 1 
ATOM   253  N  N   . VAL   A 1 35  ? -8.64918  7.10642   -6.08558  1.000 20.81214 ? 35  VAL   A N   1 
ATOM   254  C  CA  . VAL   A 1 35  ? -7.96704  6.05741   -6.83800  1.000 17.97335 ? 35  VAL   A CA  1 
ATOM   255  C  C   . VAL   A 1 35  ? -8.97913  4.99537   -7.24549  1.000 19.74848 ? 35  VAL   A C   1 
ATOM   256  O  O   . VAL   A 1 35  ? -9.84270  4.59922   -6.45176  1.000 16.74252 ? 35  VAL   A O   1 
ATOM   257  C  CB  . VAL   A 1 35  ? -6.82001  5.41849   -6.02432  1.000 21.05581 ? 35  VAL   A CB  1 
ATOM   258  C  CG1 . VAL   A 1 35  ? -6.18726  4.26752   -6.79482  1.000 18.79883 ? 35  VAL   A CG1 1 
ATOM   259  C  CG2 . VAL   A 1 35  ? -5.77432  6.45525   -5.65971  1.000 23.20750 ? 35  VAL   A CG2 1 
ATOM   260  N  N   . VAL   A 1 36  ? -8.84530  4.50381   -8.47489  1.000 15.90885 ? 36  VAL   A N   1 
ATOM   261  C  CA  . VAL   A 1 36  ? -9.61788  3.37175   -8.96614  1.000 15.71863 ? 36  VAL   A CA  1 
ATOM   262  C  C   . VAL   A 1 36  ? -8.65597  2.21156   -9.16397  1.000 17.98873 ? 36  VAL   A C   1 
ATOM   263  O  O   . VAL   A 1 36  ? -7.62609  2.35924   -9.84005  1.000 18.04644 ? 36  VAL   A O   1 
ATOM   264  C  CB  . VAL   A 1 36  ? -10.35925 3.71456   -10.27288 1.000 18.34942 ? 36  VAL   A CB  1 
ATOM   265  C  CG1 . VAL   A 1 36  ? -10.93395 2.47452   -10.89359 1.000 17.03241 ? 36  VAL   A CG1 1 
ATOM   266  C  CG2 . VAL   A 1 36  ? -11.44941 4.77878   -10.02697 1.000 18.69915 ? 36  VAL   A CG2 1 
ATOM   267  N  N   . TYR   A 1 37  ? -8.98783  1.06824   -8.56683  1.000 13.10085 ? 37  TYR   A N   1 
ATOM   268  C  CA  . TYR   A 1 37  ? -8.18147  -0.14868  -8.61565  1.000 14.98199 ? 37  TYR   A CA  1 
ATOM   269  C  C   . TYR   A 1 37  ? -8.85089  -1.13367  -9.56175  1.000 12.85452 ? 37  TYR   A C   1 
ATOM   270  O  O   . TYR   A 1 37  ? -10.06385 -1.37009  -9.46187  1.000 16.00107 ? 37  TYR   A O   1 
ATOM   271  C  CB  . TYR   A 1 37  ? -8.03158  -0.80494  -7.23057  1.000 12.55957 ? 37  TYR   A CB  1 
ATOM   272  C  CG  . TYR   A 1 37  ? -7.42314  0.07562   -6.17862  1.000 12.65767 ? 37  TYR   A CG  1 
ATOM   273  C  CD1 . TYR   A 1 37  ? -8.18709  1.00750   -5.49755  1.000 13.86817 ? 37  TYR   A CD1 1 
ATOM   274  C  CD2 . TYR   A 1 37  ? -6.04922  0.01073   -5.88515  1.000 13.44276 ? 37  TYR   A CD2 1 
ATOM   275  C  CE1 . TYR   A 1 37  ? -7.62695  1.82574   -4.53506  1.000 17.29791 ? 37  TYR   A CE1 1 
ATOM   276  C  CE2 . TYR   A 1 37  ? -5.50170  0.81660   -4.92365  1.000 15.92781 ? 37  TYR   A CE2 1 
ATOM   277  C  CZ  . TYR   A 1 37  ? -6.28527  1.72711   -4.25914  1.000 18.40112 ? 37  TYR   A CZ  1 
ATOM   278  O  OH  . TYR   A 1 37  ? -5.72268  2.54974   -3.31000  1.000 22.34710 ? 37  TYR   A OH  1 
ATOM   279  N  N   . CYS   A 1 38  ? -8.07420  -1.74790  -10.44582 1.000 13.18584 ? 38  CYS   A N   1 
ATOM   280  C  CA  . CYS   A 1 38  ? -8.65990  -2.71138  -11.36952 1.000 13.29467 ? 38  CYS   A CA  1 
ATOM   281  C  C   . CYS   A 1 38  ? -7.57800  -3.67497  -11.82851 1.000 13.99498 ? 38  CYS   A C   1 
ATOM   282  O  O   . CYS   A 1 38  ? -6.38670  -3.39446  -11.65281 1.000 14.27170 ? 38  CYS   A O   1 
ATOM   283  C  CB  . CYS   A 1 38  ? -9.32100  -2.00258  -12.56493 1.000 15.31847 ? 38  CYS   A CB  1 
ATOM   284  S  SG  . CYS   A 1 38  ? -8.16650  -1.30067  -13.78496 1.000 18.85117 ? 38  CYS   A SG  1 
ATOM   285  N  N   . PRO   A 1 39  ? -7.94576  -4.81212  -12.41865 1.000 12.10302 ? 39  PRO   A N   1 
ATOM   286  C  CA  . PRO   A 1 39  ? -6.91303  -5.74297  -12.90415 1.000 14.03696 ? 39  PRO   A CA  1 
ATOM   287  C  C   . PRO   A 1 39  ? -6.09288  -5.11401  -14.02663 1.000 14.81326 ? 39  PRO   A C   1 
ATOM   288  O  O   . PRO   A 1 39  ? -6.62130  -4.44081  -14.91177 1.000 15.41400 ? 39  PRO   A O   1 
ATOM   289  C  CB  . PRO   A 1 39  ? -7.71319  -6.94987  -13.40119 1.000 15.31104 ? 39  PRO   A CB  1 
ATOM   290  C  CG  . PRO   A 1 39  ? -9.02569  -6.87345  -12.63894 1.000 12.86544 ? 39  PRO   A CG  1 
ATOM   291  C  CD  . PRO   A 1 39  ? -9.29927  -5.38881  -12.54537 1.000 13.89223 ? 39  PRO   A CD  1 
ATOM   292  N  N   . ARG   A 1 40  ? -4.77611  -5.31129  -13.97021 1.000 14.37972 ? 40  ARG   A N   1 
ATOM   293  C  CA  . ARG   A 1 40  ? -3.95475  -4.70652  -15.00332 1.000 15.93119 ? 40  ARG   A CA  1 
ATOM   294  C  C   . ARG   A 1 40  ? -4.20744  -5.29756  -16.38670 1.000 16.82745 ? 40  ARG   A C   1 
ATOM   295  O  O   . ARG   A 1 40  ? -3.88062  -4.64242  -17.38343 1.000 18.27352 ? 40  ARG   A O   1 
ATOM   296  C  CB  . ARG   A 1 40  ? -2.48021  -4.81130  -14.62223 1.000 14.55239 ? 40  ARG   A CB  1 
ATOM   297  C  CG  . ARG   A 1 40  ? -1.90307  -6.20843  -14.71857 1.000 14.26768 ? 40  ARG   A CG  1 
ATOM   298  C  CD  . ARG   A 1 40  ? -0.42266  -6.20594  -14.36190 1.000 14.64497 ? 40  ARG   A CD  1 
ATOM   299  N  NE  . ARG   A 1 40  ? 0.08628   -7.56786  -14.35028 1.000 14.60602 ? 40  ARG   A NE  1 
ATOM   300  C  CZ  . ARG   A 1 40  ? 1.37656   -7.87118  -14.28997 1.000 16.90296 ? 40  ARG   A CZ  1 
ATOM   301  N  NH1 . ARG   A 1 40  ? 2.29987   -6.93024  -14.18980 1.000 18.16959 ? 40  ARG   A NH1 1 
ATOM   302  N  NH2 . ARG   A 1 40  ? 1.74775   -9.14723  -14.36030 1.000 16.99943 ? 40  ARG   A NH2 1 
ATOM   303  N  N   . HIS   A 1 41  ? -4.79591  -6.49963  -16.48460 1.000 15.84539 ? 41  HIS   A N   1 
ATOM   304  C  CA  . HIS   A 1 41  ? -5.02627  -7.02295  -17.82960 1.000 20.45356 ? 41  HIS   A CA  1 
ATOM   305  C  C   . HIS   A 1 41  ? -6.10010  -6.25047  -18.59555 1.000 21.34325 ? 41  HIS   A C   1 
ATOM   306  O  O   . HIS   A 1 41  ? -6.34765  -6.58624  -19.75449 1.000 21.62598 ? 41  HIS   A O   1 
ATOM   307  C  CB  . HIS   A 1 41  ? -5.33526  -8.53167  -17.78614 1.000 21.60741 ? 41  HIS   A CB  1 
ATOM   308  C  CG  . HIS   A 1 41  ? -6.67855  -8.89293  -17.22548 1.000 21.06386 ? 41  HIS   A CG  1 
ATOM   309  N  ND1 . HIS   A 1 41  ? -6.83112  -9.52155  -16.00500 1.000 23.55800 ? 41  HIS   A ND1 1 
ATOM   310  C  CD2 . HIS   A 1 41  ? -7.92356  -8.78003  -17.74503 1.000 24.48001 ? 41  HIS   A CD2 1 
ATOM   311  C  CE1 . HIS   A 1 41  ? -8.11592  -9.74735  -15.78290 1.000 22.06728 ? 41  HIS   A CE1 1 
ATOM   312  N  NE2 . HIS   A 1 41  ? -8.79862  -9.30730  -16.82381 1.000 24.73243 ? 41  HIS   A NE2 1 
ATOM   313  N  N   . VAL   A 1 42  ? -6.68251  -5.19326  -18.01779 1.000 19.76429 ? 42  VAL   A N   1 
ATOM   314  C  CA  . VAL   A 1 42  ? -7.55798  -4.30476  -18.78029 1.000 20.24513 ? 42  VAL   A CA  1 
ATOM   315  C  C   . VAL   A 1 42  ? -6.82840  -3.65927  -19.95274 1.000 22.21568 ? 42  VAL   A C   1 
ATOM   316  O  O   . VAL   A 1 42  ? -7.46959  -3.26340  -20.93714 1.000 23.18849 ? 42  VAL   A O   1 
ATOM   317  C  CB  . VAL   A 1 42  ? -8.16769  -3.21842  -17.86396 1.000 20.93930 ? 42  VAL   A CB  1 
ATOM   318  C  CG1 . VAL   A 1 42  ? -7.11973  -2.19656  -17.47395 1.000 16.60992 ? 42  VAL   A CG1 1 
ATOM   319  C  CG2 . VAL   A 1 42  ? -9.34376  -2.52568  -18.55872 1.000 21.51446 ? 42  VAL   A CG2 1 
ATOM   320  N  N   . ILE   A 1 43  ? -5.49512  -3.54490  -19.88752 1.000 20.86042 ? 43  ILE   A N   1 
ATOM   321  C  CA  . ILE   A 1 43  ? -4.75948  -2.91018  -20.98126 1.000 20.06552 ? 43  ILE   A CA  1 
ATOM   322  C  C   . ILE   A 1 43  ? -4.39769  -3.88929  -22.08546 1.000 24.39332 ? 43  ILE   A C   1 
ATOM   323  O  O   . ILE   A 1 43  ? -3.77304  -3.48697  -23.07688 1.000 28.52048 ? 43  ILE   A O   1 
ATOM   324  C  CB  . ILE   A 1 43  ? -3.46621  -2.20237  -20.50739 1.000 22.69542 ? 43  ILE   A CB  1 
ATOM   325  C  CG1 . ILE   A 1 43  ? -2.38983  -3.21735  -20.09007 1.000 23.98699 ? 43  ILE   A CG1 1 
ATOM   326  C  CG2 . ILE   A 1 43  ? -3.76883  -1.20944  -19.38760 1.000 25.21653 ? 43  ILE   A CG2 1 
ATOM   327  C  CD1 . ILE   A 1 43  ? -1.23136  -2.58635  -19.30093 1.000 25.41108 ? 43  ILE   A CD1 1 
ATOM   328  N  N   . CYS   A 1 44  ? -4.76546  -5.15625  -21.95071 1.000 25.89674 ? 44  CYS   A N   1 
ATOM   329  C  CA  . CYS   A 1 44  ? -4.40330  -6.18356  -22.91232 1.000 24.72884 ? 44  CYS   A CA  1 
ATOM   330  C  C   . CYS   A 1 44  ? -5.53975  -6.44076  -23.88725 1.000 34.12454 ? 44  CYS   A C   1 
ATOM   331  O  O   . CYS   A 1 44  ? -6.71450  -6.44713  -23.50852 1.000 35.79581 ? 44  CYS   A O   1 
ATOM   332  C  CB  . CYS   A 1 44  ? -4.05523  -7.49554  -22.21651 1.000 31.99524 ? 44  CYS   A CB  1 
ATOM   333  S  SG  . CYS   A 1 44  ? -2.62060  -7.40950  -21.14269 1.000 27.34178 ? 44  CYS   A SG  1 
ATOM   334  N  N   . THR   A 1 45  ? -5.17734  -6.68811  -25.13598 1.000 41.07640 ? 45  THR   A N   1 
ATOM   335  C  CA  . THR   A 1 45  ? -6.13680  -7.14860  -26.11871 1.000 47.01316 ? 45  THR   A CA  1 
ATOM   336  C  C   . THR   A 1 45  ? -6.12452  -8.67501  -26.15122 1.000 50.35831 ? 45  THR   A C   1 
ATOM   337  O  O   . THR   A 1 45  ? -5.47698  -9.33698  -25.33426 1.000 49.42187 ? 45  THR   A O   1 
ATOM   338  C  CB  . THR   A 1 45  ? -5.82153  -6.55980  -27.49117 1.000 48.12913 ? 45  THR   A CB  1 
ATOM   339  O  OG1 . THR   A 1 45  ? -4.42767  -6.73817  -27.77513 1.000 46.01371 ? 45  THR   A OG1 1 
ATOM   340  C  CG2 . THR   A 1 45  ? -6.15005  -5.06630  -27.51202 1.000 50.00906 ? 45  THR   A CG2 1 
ATOM   341  N  N   . SER   A 1 46  ? -6.84696  -9.23929  -27.12031 1.000 56.51819 ? 46  SER   A N   1 
ATOM   342  C  CA  . SER   A 1 46  ? -6.91608  -10.68879 -27.27078 1.000 58.09862 ? 46  SER   A CA  1 
ATOM   343  C  C   . SER   A 1 46  ? -5.52161  -11.29289 -27.41289 1.000 54.61775 ? 46  SER   A C   1 
ATOM   344  O  O   . SER   A 1 46  ? -5.11260  -12.15181 -26.62288 1.000 52.29393 ? 46  SER   A O   1 
ATOM   345  C  CB  . SER   A 1 46  ? -7.78704  -11.03380 -28.48247 1.000 57.82573 ? 46  SER   A CB  1 
ATOM   346  O  OG  . SER   A 1 46  ? -9.13709  -10.65762 -28.26310 1.000 63.88407 ? 46  SER   A OG  1 
ATOM   347  N  N   . GLU   A 1 47  ? -4.76872  -10.83584 -28.41543 1.000 57.01591 ? 47  GLU   A N   1 
ATOM   348  C  CA  . GLU   A 1 47  ? -3.42713  -11.36130 -28.64096 1.000 54.87177 ? 47  GLU   A CA  1 
ATOM   349  C  C   . GLU   A 1 47  ? -2.43763  -10.95413 -27.55205 1.000 53.56317 ? 47  GLU   A C   1 
ATOM   350  O  O   . GLU   A 1 47  ? -1.44661  -11.66300 -27.34227 1.000 50.49883 ? 47  GLU   A O   1 
ATOM   351  C  CB  . GLU   A 1 47  ? -2.92445  -10.92832 -30.02297 1.000 55.64223 ? 47  GLU   A CB  1 
ATOM   352  C  CG  . GLU   A 1 47  ? -2.81499  -9.41939  -30.23898 1.000 60.30649 ? 47  GLU   A CG  1 
ATOM   353  C  CD  . GLU   A 1 47  ? -4.07242  -8.82764  -30.86988 1.000 62.70544 ? 47  GLU   A CD  1 
ATOM   354  O  OE1 . GLU   A 1 47  ? -5.19117  -9.23912  -30.48092 1.000 61.66229 ? 47  GLU   A OE1 1 
ATOM   355  O  OE2 . GLU   A 1 47  ? -3.93893  -7.95968  -31.76199 1.000 60.14716 ? 47  GLU   A OE2 1 
ATOM   356  N  N   . ASP   A 1 48  ? -2.67892  -9.84307  -26.84978 1.000 50.32239 ? 48  ASP   A N   1 
ATOM   357  C  CA  . ASP   A 1 48  ? -1.78414  -9.45612  -25.76092 1.000 49.20684 ? 48  ASP   A CA  1 
ATOM   358  C  C   . ASP   A 1 48  ? -1.80499  -10.48635 -24.64001 1.000 45.00228 ? 48  ASP   A C   1 
ATOM   359  O  O   . ASP   A 1 48  ? -0.75219  -10.86245 -24.11050 1.000 39.36774 ? 48  ASP   A O   1 
ATOM   360  C  CB  . ASP   A 1 48  ? -2.16758  -8.07952  -25.21589 1.000 45.06348 ? 48  ASP   A CB  1 
ATOM   361  C  CG  . ASP   A 1 48  ? -1.57842  -6.94092  -26.02607 1.000 43.03710 ? 48  ASP   A CG  1 
ATOM   362  O  OD1 . ASP   A 1 48  ? -0.63668  -7.18038  -26.81347 1.000 43.23383 ? 48  ASP   A OD1 1 
ATOM   363  O  OD2 . ASP   A 1 48  ? -2.07065  -5.80251  -25.88078 1.000 42.83788 ? 48  ASP   A OD2 1 
ATOM   364  N  N   . MET   A 1 49  ? -2.99659  -10.97546 -24.28516 1.000 48.72267 ? 49  MET   A N   1 
ATOM   365  C  CA  . MET   A 1 49  ? -3.18284  -11.79642 -23.09365 1.000 49.15903 ? 49  MET   A CA  1 
ATOM   366  C  C   . MET   A 1 49  ? -2.49448  -13.14471 -23.26115 1.000 47.23776 ? 49  MET   A C   1 
ATOM   367  O  O   . MET   A 1 49  ? -2.55667  -13.99411 -22.36859 1.000 50.00321 ? 49  MET   A O   1 
ATOM   368  C  CB  . MET   A 1 49  ? -4.67255  -11.99451 -22.80093 1.000 46.39215 ? 49  MET   A CB  1 
ATOM   369  C  CG  . MET   A 1 49  ? -5.24007  -10.98197 -21.84073 1.000 49.57458 ? 49  MET   A CG  1 
ATOM   370  S  SD  . MET   A 1 49  ? -4.03911  -10.53157 -20.58801 1.000 58.24277 ? 49  MET   A SD  1 
ATOM   371  C  CE  . MET   A 1 49  ? -4.25894  -11.84100 -19.38945 1.000 36.40667 ? 49  MET   A CE  1 
ATOM   372  N  N   . LEU   A 1 50  ? -1.84052  -13.35691 -24.40298 1.000 49.21019 ? 50  LEU   A N   1 
ATOM   373  C  CA  . LEU   A 1 50  ? -1.07394  -14.57702 -24.61058 1.000 47.40089 ? 50  LEU   A CA  1 
ATOM   374  C  C   . LEU   A 1 50  ? 0.15271   -14.54041 -23.70849 1.000 49.26496 ? 50  LEU   A C   1 
ATOM   375  O  O   . LEU   A 1 50  ? 0.12704   -15.11205 -22.61164 1.000 51.76460 ? 50  LEU   A O   1 
ATOM   376  C  CB  . LEU   A 1 50  ? -0.69331  -14.74303 -26.08604 1.000 51.28715 ? 50  LEU   A CB  1 
ATOM   377  C  CG  . LEU   A 1 50  ? -1.87087  -15.05557 -27.02269 1.000 54.89096 ? 50  LEU   A CG  1 
ATOM   378  C  CD1 . LEU   A 1 50  ? -1.44887  -15.00850 -28.49063 1.000 52.22951 ? 50  LEU   A CD1 1 
ATOM   379  C  CD2 . LEU   A 1 50  ? -2.51302  -16.39631 -26.67703 1.000 51.44976 ? 50  LEU   A CD2 1 
ATOM   380  N  N   . ASN   A 1 51  ? 1.20857   -13.83359 -24.12039 1.000 45.91264 ? 51  ASN   A N   1 
ATOM   381  C  CA  . ASN   A 1 51  ? 2.40294   -13.65966 -23.28999 1.000 44.92675 ? 51  ASN   A CA  1 
ATOM   382  C  C   . ASN   A 1 51  ? 2.77215   -12.18077 -23.19880 1.000 42.78434 ? 51  ASN   A C   1 
ATOM   383  O  O   . ASN   A 1 51  ? 3.62214   -11.68863 -23.95256 1.000 45.75004 ? 51  ASN   A O   1 
ATOM   384  C  CB  . ASN   A 1 51  ? 3.56599   -14.48956 -23.82729 1.000 50.97062 ? 51  ASN   A CB  1 
ATOM   385  C  CG  . ASN   A 1 51  ? 4.55957   -14.86327 -22.74020 1.000 52.17461 ? 51  ASN   A CG  1 
ATOM   386  O  OD1 . ASN   A 1 51  ? 4.55158   -14.28572 -21.65042 1.000 52.54955 ? 51  ASN   A OD1 1 
ATOM   387  N  ND2 . ASN   A 1 51  ? 5.40775   -15.84865 -23.02411 1.000 51.59493 ? 51  ASN   A ND2 1 
ATOM   388  N  N   . PRO   A 1 52  ? 2.17913   -11.44926 -22.25805 1.000 38.78726 ? 52  PRO   A N   1 
ATOM   389  C  CA  . PRO   A 1 52  ? 2.33058   -9.99085  -22.21542 1.000 35.05537 ? 52  PRO   A CA  1 
ATOM   390  C  C   . PRO   A 1 52  ? 3.51177   -9.49311  -21.39598 1.000 32.01706 ? 52  PRO   A C   1 
ATOM   391  O  O   . PRO   A 1 52  ? 3.90643   -10.06982 -20.37924 1.000 34.80282 ? 52  PRO   A O   1 
ATOM   392  C  CB  . PRO   A 1 52  ? 1.01684   -9.54644  -21.55853 1.000 31.91031 ? 52  PRO   A CB  1 
ATOM   393  C  CG  . PRO   A 1 52  ? 0.71739   -10.66485 -20.59741 1.000 35.11757 ? 52  PRO   A CG  1 
ATOM   394  C  CD  . PRO   A 1 52  ? 1.22914   -11.93612 -21.24472 1.000 36.85770 ? 52  PRO   A CD  1 
ATOM   395  N  N   . ASN   A 1 53  ? 4.07330   -8.37473  -21.85845 1.000 31.12150 ? 53  ASN   A N   1 
ATOM   396  C  CA  . ASN   A 1 53  ? 5.03318   -7.59793  -21.07695 1.000 27.55420 ? 53  ASN   A CA  1 
ATOM   397  C  C   . ASN   A 1 53  ? 4.29097   -6.34788  -20.60797 1.000 29.29914 ? 53  ASN   A C   1 
ATOM   398  O  O   . ASN   A 1 53  ? 4.20882   -5.34933  -21.33174 1.000 27.31712 ? 53  ASN   A O   1 
ATOM   399  C  CB  . ASN   A 1 53  ? 6.27930   -7.26006  -21.89181 1.000 32.85272 ? 53  ASN   A CB  1 
ATOM   400  C  CG  . ASN   A 1 53  ? 7.33625   -6.54087  -21.07335 1.000 35.67198 ? 53  ASN   A CG  1 
ATOM   401  O  OD1 . ASN   A 1 53  ? 7.04629   -5.59873  -20.33706 1.000 32.36368 ? 53  ASN   A OD1 1 
ATOM   402  N  ND2 . ASN   A 1 53  ? 8.57667   -6.99864  -21.18956 1.000 40.48129 ? 53  ASN   A ND2 1 
ATOM   403  N  N   . TYR   A 1 54  ? 3.74360   -6.41348  -19.39111 1.000 24.55989 ? 54  TYR   A N   1 
ATOM   404  C  CA  . TYR   A 1 54  ? 2.86662   -5.35360  -18.90620 1.000 23.78922 ? 54  TYR   A CA  1 
ATOM   405  C  C   . TYR   A 1 54  ? 3.57067   -4.00857  -18.78762 1.000 24.52508 ? 54  TYR   A C   1 
ATOM   406  O  O   . TYR   A 1 54  ? 2.94607   -2.96444  -19.00450 1.000 24.04594 ? 54  TYR   A O   1 
ATOM   407  C  CB  . TYR   A 1 54  ? 2.27774   -5.75884  -17.56233 1.000 19.48695 ? 54  TYR   A CB  1 
ATOM   408  C  CG  . TYR   A 1 54  ? 1.15304   -6.73436  -17.69117 1.000 20.02697 ? 54  TYR   A CG  1 
ATOM   409  C  CD1 . TYR   A 1 54  ? -0.12861  -6.29397  -17.97603 1.000 19.50153 ? 54  TYR   A CD1 1 
ATOM   410  C  CD2 . TYR   A 1 54  ? 1.36493   -8.10146  -17.52334 1.000 20.44909 ? 54  TYR   A CD2 1 
ATOM   411  C  CE1 . TYR   A 1 54  ? -1.17989  -7.17406  -18.07263 1.000 18.19544 ? 54  TYR   A CE1 1 
ATOM   412  C  CE2 . TYR   A 1 54  ? 0.31462   -9.00418  -17.62466 1.000 20.36871 ? 54  TYR   A CE2 1 
ATOM   413  C  CZ  . TYR   A 1 54  ? -0.95096  -8.53113  -17.90646 1.000 20.45818 ? 54  TYR   A CZ  1 
ATOM   414  O  OH  . TYR   A 1 54  ? -1.97094  -9.42390  -18.01615 1.000 20.18436 ? 54  TYR   A OH  1 
ATOM   415  N  N   . GLU   A 1 55  ? 4.84804   -3.99477  -18.41200 1.000 25.66206 ? 55  GLU   A N   1 
ATOM   416  C  CA  . GLU   A 1 55  ? 5.54284   -2.71761  -18.33486 1.000 25.38871 ? 55  GLU   A CA  1 
ATOM   417  C  C   . GLU   A 1 55  ? 5.58554   -2.06172  -19.70597 1.000 23.72715 ? 55  GLU   A C   1 
ATOM   418  O  O   . GLU   A 1 55  ? 5.32114   -0.86142  -19.83779 1.000 25.75105 ? 55  GLU   A O   1 
ATOM   419  C  CB  . GLU   A 1 55  ? 6.94794   -2.91463  -17.76318 1.000 26.75268 ? 55  GLU   A CB  1 
ATOM   420  C  CG  . GLU   A 1 55  ? 6.94017   -3.19512  -16.26342 1.000 31.68989 ? 55  GLU   A CG  1 
ATOM   421  C  CD  . GLU   A 1 55  ? 6.81510   -4.68889  -15.92794 1.000 43.45184 ? 55  GLU   A CD  1 
ATOM   422  O  OE1 . GLU   A 1 55  ? 6.48852   -5.49377  -16.83675 1.000 38.47012 ? 55  GLU   A OE1 1 
ATOM   423  O  OE2 . GLU   A 1 55  ? 7.00049   -5.05402  -14.73896 1.000 41.73131 ? 55  GLU   A OE2 1 
ATOM   424  N  N   . ASP   A 1 56  ? 5.85584   -2.85856  -20.74082 1.000 26.58204 ? 56  ASP   A N   1 
ATOM   425  C  CA  . ASP   A 1 56  ? 5.87444   -2.35396  -22.11035 1.000 31.02229 ? 56  ASP   A CA  1 
ATOM   426  C  C   . ASP   A 1 56  ? 4.49415   -1.87728  -22.53965 1.000 29.33287 ? 56  ASP   A C   1 
ATOM   427  O  O   . ASP   A 1 56  ? 4.34966   -0.82713  -23.17974 1.000 28.78706 ? 56  ASP   A O   1 
ATOM   428  C  CB  . ASP   A 1 56  ? 6.34945   -3.45420  -23.05664 1.000 37.54443 ? 56  ASP   A CB  1 
ATOM   429  C  CG  . ASP   A 1 56  ? 7.82658   -3.43313  -23.27495 1.000 39.30012 ? 56  ASP   A CG  1 
ATOM   430  O  OD1 . ASP   A 1 56  ? 8.46443   -2.44674  -22.86472 1.000 42.01468 ? 56  ASP   A OD1 1 
ATOM   431  O  OD2 . ASP   A 1 56  ? 8.34734   -4.39827  -23.87554 1.000 44.73142 ? 56  ASP   A OD2 1 
ATOM   432  N  N   . LEU   A 1 57  ? 3.47050   -2.67251  -22.23613 1.000 25.50300 ? 57  LEU   A N   1 
ATOM   433  C  CA  . LEU   A 1 57  ? 2.11445   -2.33387  -22.63808 1.000 26.83693 ? 57  LEU   A CA  1 
ATOM   434  C  C   . LEU   A 1 57  ? 1.65897   -1.03161  -22.00106 1.000 25.23169 ? 57  LEU   A C   1 
ATOM   435  O  O   . LEU   A 1 57  ? 0.97961   -0.22310  -22.64386 1.000 26.29839 ? 57  LEU   A O   1 
ATOM   436  C  CB  . LEU   A 1 57  ? 1.17905   -3.47984  -22.25446 1.000 23.43140 ? 57  LEU   A CB  1 
ATOM   437  C  CG  . LEU   A 1 57  ? 1.35424   -4.77589  -23.04293 1.000 26.42346 ? 57  LEU   A CG  1 
ATOM   438  C  CD1 . LEU   A 1 57  ? 0.19540   -5.72823  -22.75863 1.000 29.90514 ? 57  LEU   A CD1 1 
ATOM   439  C  CD2 . LEU   A 1 57  ? 1.41604   -4.46276  -24.52122 1.000 29.16188 ? 57  LEU   A CD2 1 
ATOM   440  N  N   . LEU   A 1 58  ? 2.03810   -0.80292  -20.74096 1.000 23.10106 ? 58  LEU   A N   1 
ATOM   441  C  CA  . LEU   A 1 58  ? 1.50163   0.33221   -19.99866 1.000 22.65767 ? 58  LEU   A CA  1 
ATOM   442  C  C   . LEU   A 1 58  ? 2.16830   1.64734   -20.38810 1.000 24.07952 ? 58  LEU   A C   1 
ATOM   443  O  O   . LEU   A 1 58  ? 1.51158   2.69187   -20.39607 1.000 24.59086 ? 58  LEU   A O   1 
ATOM   444  C  CB  . LEU   A 1 58  ? 1.64054   0.08951   -18.49355 1.000 22.39598 ? 58  LEU   A CB  1 
ATOM   445  C  CG  . LEU   A 1 58  ? 0.94896   1.09187   -17.56501 1.000 24.39811 ? 58  LEU   A CG  1 
ATOM   446  C  CD1 . LEU   A 1 58  ? -0.51669  1.26496   -17.93712 1.000 24.74604 ? 58  LEU   A CD1 1 
ATOM   447  C  CD2 . LEU   A 1 58  ? 1.08246   0.63542   -16.10994 1.000 23.14995 ? 58  LEU   A CD2 1 
ATOM   448  N  N   . ILE   A 1 59  ? 3.46346   1.62702   -20.71610 1.000 25.07624 ? 59  ILE   A N   1 
ATOM   449  C  CA  . ILE   A 1 59  ? 4.13527   2.86728   -21.09483 1.000 26.57048 ? 59  ILE   A CA  1 
ATOM   450  C  C   . ILE   A 1 59  ? 3.55562   3.42435   -22.39050 1.000 27.90702 ? 59  ILE   A C   1 
ATOM   451  O  O   . ILE   A 1 59  ? 3.67473   4.62674   -22.66535 1.000 29.07314 ? 59  ILE   A O   1 
ATOM   452  C  CB  . ILE   A 1 59  ? 5.66620   2.65086   -21.20280 1.000 27.49895 ? 59  ILE   A CB  1 
ATOM   453  C  CG1 . ILE   A 1 59  ? 6.39665   3.99087   -21.29594 1.000 28.93273 ? 59  ILE   A CG1 1 
ATOM   454  C  CG2 . ILE   A 1 59  ? 6.02555   1.83852   -22.44025 1.000 28.53066 ? 59  ILE   A CG2 1 
ATOM   455  C  CD1 . ILE   A 1 59  ? 6.08385   4.93535   -20.15745 1.000 32.88135 ? 59  ILE   A CD1 1 
ATOM   456  N  N   . ARG   A 1 60  ? 2.89651   2.58111   -23.17821 1.000 27.88043 ? 60  ARG   A N   1 
ATOM   457  C  CA  . ARG   A 1 60  ? 2.26874   3.00144   -24.42069 1.000 29.24083 ? 60  ARG   A CA  1 
ATOM   458  C  C   . ARG   A 1 60  ? 0.89516   3.60522   -24.20733 1.000 28.76031 ? 60  ARG   A C   1 
ATOM   459  O  O   . ARG   A 1 60  ? 0.25933   4.01600   -25.18338 1.000 29.94987 ? 60  ARG   A O   1 
ATOM   460  C  CB  . ARG   A 1 60  ? 2.16172   1.80962   -25.35928 1.000 29.64107 ? 60  ARG   A CB  1 
ATOM   461  C  CG  . ARG   A 1 60  ? 3.47675   1.40644   -25.92999 1.000 30.81946 ? 60  ARG   A CG  1 
ATOM   462  C  CD  . ARG   A 1 60  ? 3.45378   -0.02879  -26.36708 1.000 30.70604 ? 60  ARG   A CD  1 
ATOM   463  N  NE  . ARG   A 1 60  ? 4.80368   -0.56507  -26.46085 1.000 31.39479 ? 60  ARG   A NE  1 
ATOM   464  C  CZ  . ARG   A 1 60  ? 5.08243   -1.81216  -26.80649 1.000 34.71272 ? 60  ARG   A CZ  1 
ATOM   465  N  NH1 . ARG   A 1 60  ? 4.12291   -2.70598  -26.98833 1.000 35.58948 ? 60  ARG   A NH1 1 
ATOM   466  N  NH2 . ARG   A 1 60  ? 6.35412   -2.17511  -26.95585 1.000 37.22646 ? 60  ARG   A NH2 1 
ATOM   467  N  N   . LYS   A 1 61  ? 0.42569   3.65973   -22.96718 1.000 28.29175 ? 61  LYS   A N   1 
ATOM   468  C  CA  . LYS   A 1 61  ? -0.89902  4.15321   -22.64335 1.000 29.71440 ? 61  LYS   A CA  1 
ATOM   469  C  C   . LYS   A 1 61  ? -0.80892  5.59062   -22.14064 1.000 28.62336 ? 61  LYS   A C   1 
ATOM   470  O  O   . LYS   A 1 61  ? 0.21464   6.02029   -21.61071 1.000 29.81818 ? 61  LYS   A O   1 
ATOM   471  C  CB  . LYS   A 1 61  ? -1.53952  3.27070   -21.57027 1.000 28.55936 ? 61  LYS   A CB  1 
ATOM   472  C  CG  . LYS   A 1 61  ? -2.03712  1.91044   -22.06593 1.000 25.97753 ? 61  LYS   A CG  1 
ATOM   473  C  CD  . LYS   A 1 61  ? -2.76760  1.99664   -23.39164 1.000 31.27173 ? 61  LYS   A CD  1 
ATOM   474  C  CE  . LYS   A 1 61  ? -3.43546  0.67317   -23.73768 1.000 28.13404 ? 61  LYS   A CE  1 
ATOM   475  N  NZ  . LYS   A 1 61  ? -3.95289  0.69905   -25.14218 1.000 33.98564 ? 61  LYS   A NZ  1 
ATOM   476  N  N   . SER   A 1 62  ? -1.91277  6.31912   -22.28750 1.000 34.19000 ? 62  SER   A N   1 
ATOM   477  C  CA  . SER   A 1 62  ? -2.09299  7.64602   -21.71393 1.000 33.82854 ? 62  SER   A CA  1 
ATOM   478  C  C   . SER   A 1 62  ? -3.27792  7.63979   -20.75389 1.000 32.79305 ? 62  SER   A C   1 
ATOM   479  O  O   . SER   A 1 62  ? -4.13629  6.75806   -20.81233 1.000 30.62062 ? 62  SER   A O   1 
ATOM   480  C  CB  . SER   A 1 62  ? -2.35291  8.69134   -22.79895 1.000 31.83033 ? 62  SER   A CB  1 
ATOM   481  O  OG  . SER   A 1 62  ? -1.25771  8.79918   -23.68592 1.000 39.46282 ? 62  SER   A OG  1 
ATOM   482  N  N   . ASN   A 1 63  ? -3.33331  8.65483   -19.88192 1.000 31.45497 ? 63  ASN   A N   1 
ATOM   483  C  CA  . ASN   A 1 63  ? -4.50126  8.81894   -19.01442 1.000 27.70680 ? 63  ASN   A CA  1 
ATOM   484  C  C   . ASN   A 1 63  ? -5.80178  8.75417   -19.81536 1.000 30.73248 ? 63  ASN   A C   1 
ATOM   485  O  O   . ASN   A 1 63  ? -6.76055  8.08859   -19.40200 1.000 31.37221 ? 63  ASN   A O   1 
ATOM   486  C  CB  . ASN   A 1 63  ? -4.41986  10.14576  -18.25664 1.000 32.19975 ? 63  ASN   A CB  1 
ATOM   487  C  CG  . ASN   A 1 63  ? -3.38008  10.13726  -17.14123 1.000 32.32480 ? 63  ASN   A CG  1 
ATOM   488  O  OD1 . ASN   A 1 63  ? -2.94838  9.08283   -16.67462 1.000 32.43209 ? 63  ASN   A OD1 1 
ATOM   489  N  ND2 . ASN   A 1 63  ? -2.94632  11.33269  -16.73587 1.000 30.87858 ? 63  ASN   A ND2 1 
ATOM   490  N  N   . HIS   A 1 64  ? -5.84511  9.41825   -20.97794 1.000 32.00957 ? 64  HIS   A N   1 
ATOM   491  C  CA  . HIS   A 1 64  ? -7.07979  9.48714   -21.75563 1.000 33.09316 ? 64  HIS   A CA  1 
ATOM   492  C  C   . HIS   A 1 64  ? -7.46998  8.15067   -22.37593 1.000 31.35124 ? 64  HIS   A C   1 
ATOM   493  O  O   . HIS   A 1 64  ? -8.59800  8.02116   -22.86152 1.000 33.58041 ? 64  HIS   A O   1 
ATOM   494  C  CB  . HIS   A 1 64  ? -6.96276  10.57236  -22.83786 1.000 36.08793 ? 64  HIS   A CB  1 
ATOM   495  C  CG  . HIS   A 1 64  ? -6.15032  10.17364  -24.03059 1.000 36.81321 ? 64  HIS   A CG  1 
ATOM   496  N  ND1 . HIS   A 1 64  ? -4.84687  10.58724  -24.21057 1.000 41.36308 ? 64  HIS   A ND1 1 
ATOM   497  C  CD2 . HIS   A 1 64  ? -6.47092  9.45316   -25.13341 1.000 38.20844 ? 64  HIS   A CD2 1 
ATOM   498  C  CE1 . HIS   A 1 64  ? -4.38873  10.11469  -25.35716 1.000 39.64536 ? 64  HIS   A CE1 1 
ATOM   499  N  NE2 . HIS   A 1 64  ? -5.35381  9.42171   -25.93646 1.000 42.86406 ? 64  HIS   A NE2 1 
ATOM   500  N  N   . ASN   A 1 65  ? -6.58573  7.15570   -22.35366 1.000 30.28807 ? 65  ASN   A N   1 
ATOM   501  C  CA  . ASN   A 1 65  ? -6.92872  5.81867   -22.81604 1.000 30.10876 ? 65  ASN   A CA  1 
ATOM   502  C  C   . ASN   A 1 65  ? -7.79446  5.05190   -21.82367 1.000 30.12184 ? 65  ASN   A C   1 
ATOM   503  O  O   . ASN   A 1 65  ? -8.29360  3.97841   -22.16978 1.000 31.89895 ? 65  ASN   A O   1 
ATOM   504  C  CB  . ASN   A 1 65  ? -5.65313  5.01830   -23.09764 1.000 31.94480 ? 65  ASN   A CB  1 
ATOM   505  C  CG  . ASN   A 1 65  ? -4.86096  5.56962   -24.25476 1.000 36.42292 ? 65  ASN   A CG  1 
ATOM   506  O  OD1 . ASN   A 1 65  ? -3.64273  5.41873   -24.31331 1.000 32.69585 ? 65  ASN   A OD1 1 
ATOM   507  N  ND2 . ASN   A 1 65  ? -5.55166  6.18970   -25.20250 1.000 36.10389 ? 65  ASN   A ND2 1 
ATOM   508  N  N   . PHE   A 1 66  ? -7.97824  5.56615   -20.60653 1.000 28.82938 ? 66  PHE   A N   1 
ATOM   509  C  CA  . PHE   A 1 66  ? -8.77128  4.90585   -19.57171 1.000 31.60105 ? 66  PHE   A CA  1 
ATOM   510  C  C   . PHE   A 1 66  ? -10.05119 5.70659   -19.34735 1.000 29.94306 ? 66  PHE   A C   1 
ATOM   511  O  O   . PHE   A 1 66  ? -10.00714 6.82661   -18.82729 1.000 30.64001 ? 66  PHE   A O   1 
ATOM   512  C  CB  . PHE   A 1 66  ? -7.98624  4.78440   -18.26740 1.000 26.41023 ? 66  PHE   A CB  1 
ATOM   513  C  CG  . PHE   A 1 66  ? -6.70695  4.00333   -18.38643 1.000 26.65752 ? 66  PHE   A CG  1 
ATOM   514  C  CD1 . PHE   A 1 66  ? -6.70612  2.62420   -18.28291 1.000 22.91776 ? 66  PHE   A CD1 1 
ATOM   515  C  CD2 . PHE   A 1 66  ? -5.49683  4.65965   -18.58999 1.000 26.61847 ? 66  PHE   A CD2 1 
ATOM   516  C  CE1 . PHE   A 1 66  ? -5.52503  1.90885   -18.38327 1.000 24.16438 ? 66  PHE   A CE1 1 
ATOM   517  C  CE2 . PHE   A 1 66  ? -4.31590  3.94715   -18.69049 1.000 27.10352 ? 66  PHE   A CE2 1 
ATOM   518  C  CZ  . PHE   A 1 66  ? -4.33187  2.56959   -18.58047 1.000 24.46471 ? 66  PHE   A CZ  1 
ATOM   519  N  N   . LEU   A 1 67  ? -11.18680 5.12839   -19.71810 1.000 26.61487 ? 67  LEU   A N   1 
ATOM   520  C  CA  . LEU   A 1 67  ? -12.48864 5.72476   -19.45054 1.000 30.05876 ? 67  LEU   A CA  1 
ATOM   521  C  C   . LEU   A 1 67  ? -13.05364 5.07184   -18.19730 1.000 26.04755 ? 67  LEU   A C   1 
ATOM   522  O  O   . LEU   A 1 67  ? -13.20179 3.84926   -18.15478 1.000 28.52644 ? 67  LEU   A O   1 
ATOM   523  C  CB  . LEU   A 1 67  ? -13.43910 5.53394   -20.63164 1.000 32.30982 ? 67  LEU   A CB  1 
ATOM   524  C  CG  . LEU   A 1 67  ? -12.83483 5.66424   -22.03759 1.000 35.86068 ? 67  LEU   A CG  1 
ATOM   525  C  CD1 . LEU   A 1 67  ? -13.86320 5.28379   -23.09771 1.000 38.18258 ? 67  LEU   A CD1 1 
ATOM   526  C  CD2 . LEU   A 1 67  ? -12.27005 7.05501   -22.28811 1.000 40.17774 ? 67  LEU   A CD2 1 
ATOM   527  N  N   . VAL   A 1 68  ? -13.33947 5.88117   -17.17699 1.000 28.59407 ? 68  VAL   A N   1 
ATOM   528  C  CA  . VAL   A 1 68  ? -13.92351 5.41412   -15.92370 1.000 25.21934 ? 68  VAL   A CA  1 
ATOM   529  C  C   . VAL   A 1 68  ? -15.30775 6.03195   -15.77165 1.000 27.56611 ? 68  VAL   A C   1 
ATOM   530  O  O   . VAL   A 1 68  ? -15.44991 7.25992   -15.79550 1.000 28.64365 ? 68  VAL   A O   1 
ATOM   531  C  CB  . VAL   A 1 68  ? -13.03992 5.76748   -14.71043 1.000 26.04727 ? 68  VAL   A CB  1 
ATOM   532  C  CG1 . VAL   A 1 68  ? -13.64637 5.19697   -13.44428 1.000 24.10401 ? 68  VAL   A CG1 1 
ATOM   533  C  CG2 . VAL   A 1 68  ? -11.63200 5.23301   -14.89413 1.000 27.71472 ? 68  VAL   A CG2 1 
ATOM   534  N  N   . GLN   A 1 69  ? -16.32230 5.18406   -15.59361 1.000 24.58637 ? 69  GLN   A N   1 
ATOM   535  C  CA  . GLN   A 1 69  ? -17.70000 5.62630   -15.40656 1.000 28.56289 ? 69  GLN   A CA  1 
ATOM   536  C  C   . GLN   A 1 69  ? -18.18617 5.16389   -14.04273 1.000 26.01532 ? 69  GLN   A C   1 
ATOM   537  O  O   . GLN   A 1 69  ? -18.15387 3.96457   -13.74032 1.000 23.88697 ? 69  GLN   A O   1 
ATOM   538  C  CB  . GLN   A 1 69  ? -18.61131 5.08380   -16.50787 1.000 32.60500 ? 69  GLN   A CB  1 
ATOM   539  C  CG  . GLN   A 1 69  ? -17.95606 5.00964   -17.87631 1.000 35.37132 ? 69  GLN   A CG  1 
ATOM   540  C  CD  . GLN   A 1 69  ? -18.93939 4.66417   -18.97873 1.000 43.06774 ? 69  GLN   A CD  1 
ATOM   541  O  OE1 . GLN   A 1 69  ? -20.11713 5.03739   -18.92261 1.000 48.65696 ? 69  GLN   A OE1 1 
ATOM   542  N  NE2 . GLN   A 1 69  ? -18.45789 3.94988   -19.99687 1.000 44.00636 ? 69  GLN   A NE2 1 
ATOM   543  N  N   . ALA   A 1 70  ? -18.62356 6.11415   -13.22449 1.000 25.39174 ? 70  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 70  ? -19.25981 5.82885   -11.94365 1.000 30.45950 ? 70  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 70  ? -20.74339 6.11063   -12.13916 1.000 35.51512 ? 70  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 70  ? -21.17645 7.26510   -12.10189 1.000 33.05513 ? 70  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 70  ? -18.65258 6.66698   -10.82413 1.000 32.08443 ? 70  ALA   A CB  1 
ATOM   548  N  N   . GLY   A 1 71  ? -21.51630 5.05143   -12.36679 1.000 36.03202 ? 71  GLY   A N   1 
ATOM   549  C  CA  . GLY   A 1 71  ? -22.88921 5.24546   -12.79930 1.000 39.37090 ? 71  GLY   A CA  1 
ATOM   550  C  C   . GLY   A 1 71  ? -22.89195 5.92529   -14.15220 1.000 40.41739 ? 71  GLY   A C   1 
ATOM   551  O  O   . GLY   A 1 71  ? -22.15779 5.53429   -15.06808 1.000 41.62566 ? 71  GLY   A O   1 
ATOM   552  N  N   . ASN   A 1 72  ? -23.70422 6.97545   -14.28139 1.000 42.49084 ? 72  ASN   A N   1 
ATOM   553  C  CA  . ASN   A 1 72  ? -23.75946 7.78164   -15.49523 1.000 45.19676 ? 72  ASN   A CA  1 
ATOM   554  C  C   . ASN   A 1 72  ? -22.91108 9.04745   -15.39309 1.000 43.33411 ? 72  ASN   A C   1 
ATOM   555  O  O   . ASN   A 1 72  ? -23.26323 10.08050  -15.97451 1.000 47.83617 ? 72  ASN   A O   1 
ATOM   556  C  CB  . ASN   A 1 72  ? -25.21181 8.12681   -15.83707 1.000 46.76285 ? 72  ASN   A CB  1 
ATOM   557  C  CG  . ASN   A 1 72  ? -26.00382 8.60827   -14.62761 1.000 54.49811 ? 72  ASN   A CG  1 
ATOM   558  O  OD1 . ASN   A 1 72  ? -25.43102 9.10012   -13.65263 1.000 59.09902 ? 72  ASN   A OD1 1 
ATOM   559  N  ND2 . ASN   A 1 72  ? -27.32997 8.46186   -14.68499 1.000 52.57479 ? 72  ASN   A ND2 1 
ATOM   560  N  N   . VAL   A 1 73  ? -21.79442 8.98701   -14.66828 1.000 41.11848 ? 73  VAL   A N   1 
ATOM   561  C  CA  . VAL   A 1 73  ? -20.90368 10.12806  -14.49165 1.000 39.84097 ? 73  VAL   A CA  1 
ATOM   562  C  C   . VAL   A 1 73  ? -19.48855 9.68068   -14.83076 1.000 36.08574 ? 73  VAL   A C   1 
ATOM   563  O  O   . VAL   A 1 73  ? -19.00569 8.67670   -14.29669 1.000 34.15500 ? 73  VAL   A O   1 
ATOM   564  C  CB  . VAL   A 1 73  ? -20.96506 10.68702  -13.05630 1.000 41.13298 ? 73  VAL   A CB  1 
ATOM   565  C  CG1 . VAL   A 1 73  ? -19.87015 11.72623  -12.84305 1.000 41.15319 ? 73  VAL   A CG1 1 
ATOM   566  C  CG2 . VAL   A 1 73  ? -22.33497 11.27075  -12.76590 1.000 44.84441 ? 73  VAL   A CG2 1 
ATOM   567  N  N   . GLN   A 1 74  ? -18.82655 10.41617  -15.71574 1.000 37.77177 ? 74  GLN   A N   1 
ATOM   568  C  CA  . GLN   A 1 74  ? -17.49082 10.04401  -16.15636 1.000 35.95330 ? 74  GLN   A CA  1 
ATOM   569  C  C   . GLN   A 1 74  ? -16.43654 10.67524  -15.25395 1.000 36.78265 ? 74  GLN   A C   1 
ATOM   570  O  O   . GLN   A 1 74  ? -16.48936 11.87235  -14.95791 1.000 38.24109 ? 74  GLN   A O   1 
ATOM   571  C  CB  . GLN   A 1 74  ? -17.26717 10.46044  -17.61447 1.000 41.53399 ? 74  GLN   A CB  1 
ATOM   572  C  CG  . GLN   A 1 74  ? -16.01115 9.86077   -18.23942 1.000 40.43554 ? 74  GLN   A CG  1 
ATOM   573  C  CD  . GLN   A 1 74  ? -15.47072 10.68134  -19.39871 1.000 47.83115 ? 74  GLN   A CD  1 
ATOM   574  O  OE1 . GLN   A 1 74  ? -16.13457 11.59651  -19.89624 1.000 49.56468 ? 74  GLN   A OE1 1 
ATOM   575  N  NE2 . GLN   A 1 74  ? -14.24845 10.36867  -19.82366 1.000 49.00238 ? 74  GLN   A NE2 1 
ATOM   576  N  N   . LEU   A 1 75  ? -15.47278 9.85943   -14.82829 1.000 31.15091 ? 75  LEU   A N   1 
ATOM   577  C  CA  . LEU   A 1 75  ? -14.38490 10.28730  -13.95768 1.000 32.26180 ? 75  LEU   A CA  1 
ATOM   578  C  C   . LEU   A 1 75  ? -13.12926 10.51496  -14.78787 1.000 35.43911 ? 75  LEU   A C   1 
ATOM   579  O  O   . LEU   A 1 75  ? -12.67640 9.61034   -15.49756 1.000 37.14735 ? 75  LEU   A O   1 
ATOM   580  C  CB  . LEU   A 1 75  ? -14.10728 9.24066   -12.87604 1.000 29.23530 ? 75  LEU   A CB  1 
ATOM   581  C  CG  . LEU   A 1 75  ? -15.23311 8.91648   -11.89354 1.000 30.97840 ? 75  LEU   A CG  1 
ATOM   582  C  CD1 . LEU   A 1 75  ? -14.71786 7.99089   -10.79781 1.000 27.76760 ? 75  LEU   A CD1 1 
ATOM   583  C  CD2 . LEU   A 1 75  ? -15.79885 10.18533  -11.28995 1.000 34.35281 ? 75  LEU   A CD2 1 
ATOM   584  N  N   . ARG   A 1 76  ? -12.55785 11.70981  -14.68421 1.000 32.45625 ? 76  ARG   A N   1 
ATOM   585  C  CA  . ARG   A 1 76  ? -11.36258 12.03414  -15.45007 1.000 32.76354 ? 76  ARG   A CA  1 
ATOM   586  C  C   . ARG   A 1 76  ? -10.14699 11.40281  -14.77901 1.000 32.06799 ? 76  ARG   A C   1 
ATOM   587  O  O   . ARG   A 1 76  ? -9.88671  11.65009  -13.59732 1.000 30.70806 ? 76  ARG   A O   1 
ATOM   588  C  CB  . ARG   A 1 76  ? -11.19186 13.54854  -15.56867 1.000 35.04943 ? 76  ARG   A CB  1 
ATOM   589  C  CG  . ARG   A 1 76  ? -9.94776  13.95464  -16.34742 1.000 37.18716 ? 76  ARG   A CG  1 
ATOM   590  C  CD  . ARG   A 1 76  ? -9.95615  15.44511  -16.66980 1.000 42.51911 ? 76  ARG   A CD  1 
ATOM   591  N  NE  . ARG   A 1 76  ? -9.46549  16.25415  -15.55895 1.000 48.42906 ? 76  ARG   A NE  1 
ATOM   592  C  CZ  . ARG   A 1 76  ? -8.24028  16.76368  -15.48800 1.000 49.45387 ? 76  ARG   A CZ  1 
ATOM   593  N  NH1 . ARG   A 1 76  ? -7.37070  16.61952  -16.47805 1.000 48.01676 ? 76  ARG   A NH1 1 
ATOM   594  N  NH2 . ARG   A 1 76  ? -7.88304  17.44972  -14.40379 1.000 48.07732 ? 76  ARG   A NH2 1 
ATOM   595  N  N   . VAL   A 1 77  ? -9.41461  10.58400  -15.52984 1.000 31.35651 ? 77  VAL   A N   1 
ATOM   596  C  CA  . VAL   A 1 77  ? -8.18722  9.96282   -15.04031 1.000 28.12624 ? 77  VAL   A CA  1 
ATOM   597  C  C   . VAL   A 1 77  ? -7.04868  10.96378  -15.18200 1.000 31.16332 ? 77  VAL   A C   1 
ATOM   598  O  O   . VAL   A 1 77  ? -6.82682  11.50657  -16.26957 1.000 28.84884 ? 77  VAL   A O   1 
ATOM   599  C  CB  . VAL   A 1 77  ? -7.88901  8.67512   -15.82262 1.000 30.53304 ? 77  VAL   A CB  1 
ATOM   600  C  CG1 . VAL   A 1 77  ? -6.49263  8.16181   -15.50834 1.000 27.46208 ? 77  VAL   A CG1 1 
ATOM   601  C  CG2 . VAL   A 1 77  ? -8.95633  7.61501   -15.54227 1.000 29.57175 ? 77  VAL   A CG2 1 
ATOM   602  N  N   . ILE   A 1 78  ? -6.32106  11.20980  -14.09073 1.000 28.12511 ? 78  ILE   A N   1 
ATOM   603  C  CA  . ILE   A 1 78  ? -5.22691  12.17659  -14.08605 1.000 28.86892 ? 78  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 78  ? -3.87935  11.53735  -13.79475 1.000 27.77056 ? 78  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 78  ? -2.85599  12.23048  -13.82263 1.000 29.25162 ? 78  ILE   A O   1 
ATOM   606  C  CB  . ILE   A 1 78  ? -5.48678  13.33021  -13.09502 1.000 30.85901 ? 78  ILE   A CB  1 
ATOM   607  C  CG1 . ILE   A 1 78  ? -5.56678  12.79679  -11.66100 1.000 30.64864 ? 78  ILE   A CG1 1 
ATOM   608  C  CG2 . ILE   A 1 78  ? -6.74455  14.10707  -13.48747 1.000 32.29037 ? 78  ILE   A CG2 1 
ATOM   609  C  CD1 . ILE   A 1 78  ? -6.03497  13.83295  -10.66043 1.000 34.53630 ? 78  ILE   A CD1 1 
ATOM   610  N  N   . GLY   A 1 79  ? -3.84233  10.24171  -13.52570 1.000 28.02457 ? 79  GLY   A N   1 
ATOM   611  C  CA  . GLY   A 1 79  ? -2.58582  9.54222   -13.35095 1.000 26.95797 ? 79  GLY   A CA  1 
ATOM   612  C  C   . GLY   A 1 79  ? -2.84511  8.05633   -13.38469 1.000 26.55483 ? 79  GLY   A C   1 
ATOM   613  O  O   . GLY   A 1 79  ? -3.98104  7.60275   -13.20882 1.000 25.64045 ? 79  GLY   A O   1 
ATOM   614  N  N   . HIS   A 1 80  ? -1.78090  7.29924   -13.63120 1.000 24.94434 ? 80  HIS   A N   1 
ATOM   615  C  CA  . HIS   A 1 80  ? -1.91388  5.85044   -13.64485 1.000 24.86333 ? 80  HIS   A CA  1 
ATOM   616  C  C   . HIS   A 1 80  ? -0.59214  5.21863   -13.25064 1.000 25.43457 ? 80  HIS   A C   1 
ATOM   617  O  O   . HIS   A 1 80  ? 0.48262   5.77319   -13.51761 1.000 25.19854 ? 80  HIS   A O   1 
ATOM   618  C  CB  . HIS   A 1 80  ? -2.34242  5.33183   -15.01891 1.000 25.58904 ? 80  HIS   A CB  1 
ATOM   619  C  CG  . HIS   A 1 80  ? -1.38117  5.67275   -16.11291 1.000 27.18543 ? 80  HIS   A CG  1 
ATOM   620  N  ND1 . HIS   A 1 80  ? -1.30348  6.92923   -16.67256 1.000 31.36166 ? 80  HIS   A ND1 1 
ATOM   621  C  CD2 . HIS   A 1 80  ? -0.44013  4.92354   -16.73285 1.000 29.77859 ? 80  HIS   A CD2 1 
ATOM   622  C  CE1 . HIS   A 1 80  ? -0.36243  6.93577   -17.60162 1.000 34.72824 ? 80  HIS   A CE1 1 
ATOM   623  N  NE2 . HIS   A 1 80  ? 0.17671   5.73080   -17.65642 1.000 32.23911 ? 80  HIS   A NE2 1 
ATOM   624  N  N   . SER   A 1 81  ? -0.68025  4.04593   -12.61854 1.000 22.06269 ? 81  SER   A N   1 
ATOM   625  C  CA  . SER   A 1 81  ? 0.51464   3.28010   -12.28708 1.000 22.22069 ? 81  SER   A CA  1 
ATOM   626  C  C   . SER   A 1 81  ? 0.13543   1.81751   -12.09390 1.000 21.45116 ? 81  SER   A C   1 
ATOM   627  O  O   . SER   A 1 81  ? -1.02140  1.48215   -11.82697 1.000 21.64797 ? 81  SER   A O   1 
ATOM   628  C  CB  . SER   A 1 81  ? 1.19841   3.80754   -11.02132 1.000 22.86347 ? 81  SER   A CB  1 
ATOM   629  O  OG  . SER   A 1 81  ? 0.28685   3.85604   -9.93439  1.000 27.31372 ? 81  SER   A OG  1 
ATOM   630  N  N   . MET   A 1 82  ? 1.13675   0.95533   -12.22143 1.000 17.33070 ? 82  MET   A N   1 
ATOM   631  C  CA  . MET   A 1 82  ? 1.02213   -0.46433  -11.90547 1.000 20.31260 ? 82  MET   A CA  1 
ATOM   632  C  C   . MET   A 1 82  ? 1.51879   -0.77614  -10.50826 1.000 18.68017 ? 82  MET   A C   1 
ATOM   633  O  O   . MET   A 1 82  ? 2.58640   -0.30326  -10.09831 1.000 19.19247 ? 82  MET   A O   1 
ATOM   634  C  CB  . MET   A 1 82  ? 1.83890   -1.30822  -12.87256 1.000 24.91970 ? 82  MET   A CB  1 
ATOM   635  C  CG  . MET   A 1 82  ? 1.29931   -2.67360  -13.06816 1.000 21.54371 ? 82  MET   A CG  1 
ATOM   636  S  SD  . MET   A 1 82  ? 1.78863   -3.27271  -14.66222 1.000 24.66615 ? 82  MET   A SD  1 
ATOM   637  C  CE  . MET   A 1 82  ? 3.58004   -3.05185  -14.63136 1.000 28.30415 ? 82  MET   A CE  1 
ATOM   638  N  N   . GLN   A 1 83  ? 0.78955   -1.64577  -9.82146  1.000 18.37131 ? 83  GLN   A N   1 
ATOM   639  C  CA  . GLN   A 1 83  ? 1.24074   -2.21238  -8.55168  1.000 18.11993 ? 83  GLN   A CA  1 
ATOM   640  C  C   . GLN   A 1 83  ? 0.99252   -3.71388  -8.63763  1.000 13.68479 ? 83  GLN   A C   1 
ATOM   641  O  O   . GLN   A 1 83  ? -0.15211  -4.15251  -8.55075  1.000 13.61427 ? 83  GLN   A O   1 
ATOM   642  C  CB  . GLN   A 1 83  ? 0.51460   -1.57883  -7.37357  1.000 23.75223 ? 83  GLN   A CB  1 
ATOM   643  C  CG  . GLN   A 1 83  ? 0.72626   -2.30367  -6.06716  1.000 25.88548 ? 83  GLN   A CG  1 
ATOM   644  C  CD  . GLN   A 1 83  ? 0.24324   -1.49023  -4.89011  1.000 31.63072 ? 83  GLN   A CD  1 
ATOM   645  O  OE1 . GLN   A 1 83  ? 0.51594   -0.28947  -4.79823  1.000 32.71887 ? 83  GLN   A OE1 1 
ATOM   646  N  NE2 . GLN   A 1 83  ? -0.49721  -2.13305  -3.98712  1.000 27.56476 ? 83  GLN   A NE2 1 
ATOM   647  N  N   . ASN   A 1 84  ? 2.05657   -4.48745  -8.83441  1.000 16.82461 ? 84  ASN   A N   1 
ATOM   648  C  CA  . ASN   A 1 84  ? 1.93100   -5.92573  -9.04933  1.000 13.97809 ? 84  ASN   A CA  1 
ATOM   649  C  C   . ASN   A 1 84  ? 0.90062   -6.18901  -10.14691 1.000 15.18055 ? 84  ASN   A C   1 
ATOM   650  O  O   . ASN   A 1 84  ? 1.06604   -5.66874  -11.25019 1.000 14.21533 ? 84  ASN   A O   1 
ATOM   651  C  CB  . ASN   A 1 84  ? 1.62102   -6.61194  -7.72382  1.000 12.85933 ? 84  ASN   A CB  1 
ATOM   652  C  CG  . ASN   A 1 84  ? 2.66402   -6.27410  -6.67360  1.000 15.33851 ? 84  ASN   A CG  1 
ATOM   653  O  OD1 . ASN   A 1 84  ? 3.86351   -6.45624  -6.90709  1.000 16.36747 ? 84  ASN   A OD1 1 
ATOM   654  N  ND2 . ASN   A 1 84  ? 2.22885   -5.70424  -5.55353  1.000 15.83515 ? 84  ASN   A ND2 1 
ATOM   655  N  N   . CYS   A 1 85  ? -0.18016  -6.92456  -9.87696  1.000 13.02210 ? 85  CYS   A N   1 
ATOM   656  C  CA  . CYS   A 1 85  ? -1.10971  -7.25261  -10.94548 1.000 12.04032 ? 85  CYS   A CA  1 
ATOM   657  C  C   . CYS   A 1 85  ? -2.33923  -6.34072  -10.97879 1.000 13.49759 ? 85  CYS   A C   1 
ATOM   658  O  O   . CYS   A 1 85  ? -3.29363  -6.64658  -11.70271 1.000 14.51290 ? 85  CYS   A O   1 
ATOM   659  C  CB  . CYS   A 1 85  ? -1.55321  -8.72225  -10.85053 1.000 12.14060 ? 85  CYS   A CB  1 
ATOM   660  S  SG  . CYS   A 1 85  ? -0.21125  -9.87201  -11.14193 1.000 14.50166 ? 85  CYS   A SG  1 
ATOM   661  N  N   . VAL   A 1 86  ? -2.33975  -5.22667  -10.24558 1.000 12.60320 ? 86  VAL   A N   1 
ATOM   662  C  CA  . VAL   A 1 86  ? -3.43591  -4.26426  -10.33696 1.000 15.61345 ? 86  VAL   A CA  1 
ATOM   663  C  C   . VAL   A 1 86  ? -2.92875  -2.94033  -10.91148 1.000 14.73655 ? 86  VAL   A C   1 
ATOM   664  O  O   . VAL   A 1 86  ? -1.73872  -2.59455  -10.83174 1.000 16.42999 ? 86  VAL   A O   1 
ATOM   665  C  CB  . VAL   A 1 86  ? -4.16887  -4.02666  -8.99605  1.000 17.76777 ? 86  VAL   A CB  1 
ATOM   666  C  CG1 . VAL   A 1 86  ? -4.82892  -5.31315  -8.49060  1.000 18.19157 ? 86  VAL   A CG1 1 
ATOM   667  C  CG2 . VAL   A 1 86  ? -3.23056  -3.52472  -7.96086  1.000 14.87647 ? 86  VAL   A CG2 1 
ATOM   668  N  N   . LEU   A 1 87  ? -3.85020  -2.22347  -11.54494 1.000 14.24166 ? 87  LEU   A N   1 
ATOM   669  C  CA  . LEU   A 1 87  ? -3.66411  -0.84837  -11.97772 1.000 16.45390 ? 87  LEU   A CA  1 
ATOM   670  C  C   . LEU   A 1 87  ? -4.27784  0.09497   -10.95718 1.000 16.20055 ? 87  LEU   A C   1 
ATOM   671  O  O   . LEU   A 1 87  ? -5.35230  -0.18014  -10.41929 1.000 17.53314 ? 87  LEU   A O   1 
ATOM   672  C  CB  . LEU   A 1 87  ? -4.32374  -0.59937  -13.33175 1.000 19.17540 ? 87  LEU   A CB  1 
ATOM   673  C  CG  . LEU   A 1 87  ? -3.62522  -0.63654  -14.67113 1.000 24.51922 ? 87  LEU   A CG  1 
ATOM   674  C  CD1 . LEU   A 1 87  ? -4.65620  -0.24307  -15.72610 1.000 22.18964 ? 87  LEU   A CD1 1 
ATOM   675  C  CD2 . LEU   A 1 87  ? -2.48203  0.36233   -14.68110 1.000 24.84410 ? 87  LEU   A CD2 1 
ATOM   676  N  N   . LYS   A 1 88  ? -3.59713  1.20155   -10.69123 1.000 16.01461 ? 88  LYS   A N   1 
ATOM   677  C  CA  . LYS   A 1 88  ? -4.11797  2.26460   -9.84038  1.000 16.49791 ? 88  LYS   A CA  1 
ATOM   678  C  C   . LYS   A 1 88  ? -4.31681  3.48852   -10.72409 1.000 19.72153 ? 88  LYS   A C   1 
ATOM   679  O  O   . LYS   A 1 88  ? -3.34390  4.07015   -11.21157 1.000 20.93428 ? 88  LYS   A O   1 
ATOM   680  C  CB  . LYS   A 1 88  ? -3.17298  2.55135   -8.67654  1.000 18.43030 ? 88  LYS   A CB  1 
ATOM   681  C  CG  . LYS   A 1 88  ? -3.01960  1.40192   -7.69987  1.000 17.98225 ? 88  LYS   A CG  1 
ATOM   682  C  CD  . LYS   A 1 88  ? -1.93492  1.65383   -6.67973  1.000 21.98868 ? 88  LYS   A CD  1 
ATOM   683  C  CE  . LYS   A 1 88  ? -2.38734  2.54431   -5.53548  1.000 28.23246 ? 88  LYS   A CE  1 
ATOM   684  N  NZ  . LYS   A 1 88  ? -1.25988  2.82994   -4.58774  1.000 37.29277 ? 88  LYS   A NZ  1 
ATOM   685  N  N   . LEU   A 1 89  ? -5.57530  3.85353   -10.95090 1.000 18.61087 ? 89  LEU   A N   1 
ATOM   686  C  CA  . LEU   A 1 89  ? -5.93692  4.98356   -11.79906 1.000 19.21629 ? 89  LEU   A CA  1 
ATOM   687  C  C   . LEU   A 1 89  ? -6.26187  6.15933   -10.88655 1.000 20.76476 ? 89  LEU   A C   1 
ATOM   688  O  O   . LEU   A 1 89  ? -7.23558  6.11663   -10.12519 1.000 22.45897 ? 89  LEU   A O   1 
ATOM   689  C  CB  . LEU   A 1 89  ? -7.12164  4.61861   -12.68696 1.000 21.20266 ? 89  LEU   A CB  1 
ATOM   690  C  CG  . LEU   A 1 89  ? -6.86148  3.49091   -13.68870 1.000 21.34072 ? 89  LEU   A CG  1 
ATOM   691  C  CD1 . LEU   A 1 89  ? -8.07223  3.30056   -14.57496 1.000 23.27079 ? 89  LEU   A CD1 1 
ATOM   692  C  CD2 . LEU   A 1 89  ? -5.63820  3.81033   -14.55301 1.000 22.22785 ? 89  LEU   A CD2 1 
ATOM   693  N  N   . LYS   A 1 90  ? -5.42856  7.18869   -10.92687 1.000 21.13246 ? 90  LYS   A N   1 
ATOM   694  C  CA  . LYS   A 1 90  ? -5.72123  8.39978   -10.17828 1.000 22.17026 ? 90  LYS   A CA  1 
ATOM   695  C  C   . LYS   A 1 90  ? -6.79782  9.20287   -10.90277 1.000 24.54832 ? 90  LYS   A C   1 
ATOM   696  O  O   . LYS   A 1 90  ? -6.66784  9.50149   -12.09345 1.000 28.71180 ? 90  LYS   A O   1 
ATOM   697  C  CB  . LYS   A 1 90  ? -4.44706  9.22410   -10.00231 1.000 24.47543 ? 90  LYS   A CB  1 
ATOM   698  C  CG  . LYS   A 1 90  ? -4.40879  10.02877  -8.72548  1.000 30.17937 ? 90  LYS   A CG  1 
ATOM   699  C  CD  . LYS   A 1 90  ? -3.86620  9.19027   -7.57924  1.000 35.65218 ? 90  LYS   A CD  1 
ATOM   700  C  CE  . LYS   A 1 90  ? -3.85264  9.99825   -6.29430  1.000 37.26686 ? 90  LYS   A CE  1 
ATOM   701  N  NZ  . LYS   A 1 90  ? -3.48356  11.42203  -6.59175  1.000 40.65366 ? 90  LYS   A NZ  1 
ATOM   702  N  N   . VAL   A 1 91  ? -7.88125  9.52194   -10.19814 1.000 26.04804 ? 91  VAL   A N   1 
ATOM   703  C  CA  . VAL   A 1 91  ? -8.95156  10.32555  -10.77127 1.000 25.16615 ? 91  VAL   A CA  1 
ATOM   704  C  C   . VAL   A 1 91  ? -9.05322  11.64200  -10.01167 1.000 26.62099 ? 91  VAL   A C   1 
ATOM   705  O  O   . VAL   A 1 91  ? -8.53529  11.79365  -8.90271  1.000 26.80084 ? 91  VAL   A O   1 
ATOM   706  C  CB  . VAL   A 1 91  ? -10.29953 9.56935   -10.79587 1.000 26.98154 ? 91  VAL   A CB  1 
ATOM   707  C  CG1 . VAL   A 1 91  ? -10.16484 8.31043   -11.63941 1.000 26.55225 ? 91  VAL   A CG1 1 
ATOM   708  C  CG2 . VAL   A 1 91  ? -10.71530 9.17499   -9.38294  1.000 24.13755 ? 91  VAL   A CG2 1 
ATOM   709  N  N   . ASP   A 1 92  ? -9.70303  12.61648  -10.64267 1.000 29.60448 ? 92  ASP   A N   1 
ATOM   710  C  CA  . ASP   A 1 92  ? -9.74419  13.97016  -10.10615 1.000 34.08799 ? 92  ASP   A CA  1 
ATOM   711  C  C   . ASP   A 1 92  ? -10.86736 14.18007  -9.10221  1.000 32.66860 ? 92  ASP   A C   1 
ATOM   712  O  O   . ASP   A 1 92  ? -11.09774 15.31763  -8.67968  1.000 33.91543 ? 92  ASP   A O   1 
ATOM   713  C  CB  . ASP   A 1 92  ? -9.84620  14.99984  -11.24567 1.000 35.64224 ? 92  ASP   A CB  1 
ATOM   714  C  CG  . ASP   A 1 92  ? -11.19812 14.98185  -11.96147 1.000 38.20308 ? 92  ASP   A CG  1 
ATOM   715  O  OD1 . ASP   A 1 92  ? -12.08461 14.16532  -11.62151 1.000 40.04178 ? 92  ASP   A OD1 1 
ATOM   716  O  OD2 . ASP   A 1 92  ? -11.37191 15.81770  -12.87584 1.000 43.65881 ? 92  ASP   A OD2 1 
ATOM   717  N  N   . THR   A 1 93  ? -11.56487 13.11434  -8.71325  1.000 31.20677 ? 93  THR   A N   1 
ATOM   718  C  CA  . THR   A 1 93  ? -12.67224 13.19237  -7.76828  1.000 31.99843 ? 93  THR   A CA  1 
ATOM   719  C  C   . THR   A 1 93  ? -12.50950 12.09654  -6.72688  1.000 27.67113 ? 93  THR   A C   1 
ATOM   720  O  O   . THR   A 1 93  ? -12.39327 10.91708  -7.07671  1.000 26.15090 ? 93  THR   A O   1 
ATOM   721  C  CB  . THR   A 1 93  ? -14.02316 13.05003  -8.47740  1.000 29.87974 ? 93  THR   A CB  1 
ATOM   722  O  OG1 . THR   A 1 93  ? -14.09842 13.98919  -9.55855  1.000 37.15362 ? 93  THR   A OG1 1 
ATOM   723  C  CG2 . THR   A 1 93  ? -15.17721 13.27447  -7.50035  1.000 34.85085 ? 93  THR   A CG2 1 
ATOM   724  N  N   . ALA   A 1 94  ? -12.50180 12.48891  -5.45484  1.000 28.40621 ? 94  ALA   A N   1 
ATOM   725  C  CA  . ALA   A 1 94  ? -12.55810 11.51459  -4.37738  1.000 24.51532 ? 94  ALA   A CA  1 
ATOM   726  C  C   . ALA   A 1 94  ? -13.97296 10.96758  -4.26973  1.000 25.34690 ? 94  ALA   A C   1 
ATOM   727  O  O   . ALA   A 1 94  ? -14.94844 11.72073  -4.34958  1.000 26.96226 ? 94  ALA   A O   1 
ATOM   728  C  CB  . ALA   A 1 94  ? -12.14293 12.15015  -3.05271  1.000 27.40487 ? 94  ALA   A CB  1 
ATOM   729  N  N   . ASN   A 1 95  ? -14.08097 9.65925   -4.11922  1.000 25.16354 ? 95  ASN   A N   1 
ATOM   730  C  CA  . ASN   A 1 95  ? -15.38916 9.02889   -3.98280  1.000 22.09138 ? 95  ASN   A CA  1 
ATOM   731  C  C   . ASN   A 1 95  ? -16.05299 9.47130   -2.68482  1.000 24.55829 ? 95  ASN   A C   1 
ATOM   732  O  O   . ASN   A 1 95  ? -15.57934 9.09375   -1.60392  1.000 25.35724 ? 95  ASN   A O   1 
ATOM   733  C  CB  . ASN   A 1 95  ? -15.23773 7.50962   -4.01703  1.000 19.15094 ? 95  ASN   A CB  1 
ATOM   734  C  CG  . ASN   A 1 95  ? -16.58057 6.77698   -3.97344  1.000 18.82835 ? 95  ASN   A CG  1 
ATOM   735  O  OD1 . ASN   A 1 95  ? -17.64344 7.39504   -3.87984  1.000 20.26287 ? 95  ASN   A OD1 1 
ATOM   736  N  ND2 . ASN   A 1 95  ? -16.52817 5.45068   -4.04614  1.000 20.21510 ? 95  ASN   A ND2 1 
ATOM   737  N  N   . PRO   A 1 96  ? -17.15358 10.22911  -2.73071  1.000 25.69348 ? 96  PRO   A N   1 
ATOM   738  C  CA  . PRO   A 1 96  ? -17.79746 10.65895  -1.47983  1.000 29.11800 ? 96  PRO   A CA  1 
ATOM   739  C  C   . PRO   A 1 96  ? -18.38146 9.50906   -0.68687  1.000 25.45339 ? 96  PRO   A C   1 
ATOM   740  O  O   . PRO   A 1 96  ? -18.71246 9.69218   0.49260   1.000 27.92717 ? 96  PRO   A O   1 
ATOM   741  C  CB  . PRO   A 1 96  ? -18.89735 11.61365  -1.95717  1.000 29.64784 ? 96  PRO   A CB  1 
ATOM   742  C  CG  . PRO   A 1 96  ? -19.20789 11.17240  -3.34705  1.000 29.96939 ? 96  PRO   A CG  1 
ATOM   743  C  CD  . PRO   A 1 96  ? -17.93857 10.59738  -3.92271  1.000 27.81601 ? 96  PRO   A CD  1 
ATOM   744  N  N   . LYS   A 1 97  ? -18.50932 8.33317   -1.29343  1.000 25.30692 ? 97  LYS   A N   1 
ATOM   745  C  CA  . LYS   A 1 97  ? -19.06982 7.17017   -0.62950  1.000 21.14510 ? 97  LYS   A CA  1 
ATOM   746  C  C   . LYS   A 1 97  ? -17.99093 6.23721   -0.09682  1.000 18.87897 ? 97  LYS   A C   1 
ATOM   747  O  O   . LYS   A 1 97  ? -18.29828 5.10925   0.28030   1.000 19.16290 ? 97  LYS   A O   1 
ATOM   748  C  CB  . LYS   A 1 97  ? -19.99413 6.42992   -1.59375  1.000 22.10619 ? 97  LYS   A CB  1 
ATOM   749  C  CG  . LYS   A 1 97  ? -21.27588 7.20450   -1.88007  1.000 23.43119 ? 97  LYS   A CG  1 
ATOM   750  C  CD  . LYS   A 1 97  ? -22.19673 6.41025   -2.77759  1.000 26.39479 ? 97  LYS   A CD  1 
ATOM   751  C  CE  . LYS   A 1 97  ? -23.22850 7.30759   -3.42680  1.000 34.37572 ? 97  LYS   A CE  1 
ATOM   752  N  NZ  . LYS   A 1 97  ? -23.50990 6.85420   -4.81520  1.000 40.34106 ? 97  LYS   A NZ  1 
ATOM   753  N  N   . THR   A 1 98  ? -16.74074 6.68889   -0.04331  1.000 21.65049 ? 98  THR   A N   1 
ATOM   754  C  CA  . THR   A 1 98  ? -15.67014 5.83247   0.44663   1.000 20.37754 ? 98  THR   A CA  1 
ATOM   755  C  C   . THR   A 1 98  ? -15.94449 5.41081   1.88808   1.000 21.17082 ? 98  THR   A C   1 
ATOM   756  O  O   . THR   A 1 98  ? -16.05562 6.28025   2.77224   1.000 20.50736 ? 98  THR   A O   1 
ATOM   757  C  CB  . THR   A 1 98  ? -14.32308 6.54887   0.36570   1.000 22.91297 ? 98  THR   A CB  1 
ATOM   758  O  OG1 . THR   A 1 98  ? -14.07749 6.96572   -0.98139  1.000 22.79523 ? 98  THR   A OG1 1 
ATOM   759  C  CG2 . THR   A 1 98  ? -13.19815 5.60704   0.79984   1.000 20.69306 ? 98  THR   A CG2 1 
ATOM   760  N  N   . PRO   A 1 99  ? -16.06231 4.11859   2.17037   1.000 19.25583 ? 99  PRO   A N   1 
ATOM   761  C  CA  . PRO   A 1 99  ? -16.20563 3.67356   3.55448   1.000 18.16714 ? 99  PRO   A CA  1 
ATOM   762  C  C   . PRO   A 1 99  ? -14.85145 3.68755   4.23595   1.000 19.62471 ? 99  PRO   A C   1 
ATOM   763  O  O   . PRO   A 1 99  ? -13.80649 3.79540   3.59387   1.000 18.76818 ? 99  PRO   A O   1 
ATOM   764  C  CB  . PRO   A 1 99  ? -16.72730 2.24474   3.40720   1.000 15.94744 ? 99  PRO   A CB  1 
ATOM   765  C  CG  . PRO   A 1 99  ? -16.07967 1.76706   2.17577   1.000 18.91300 ? 99  PRO   A CG  1 
ATOM   766  C  CD  . PRO   A 1 99  ? -15.94148 2.97448   1.25150   1.000 17.16982 ? 99  PRO   A CD  1 
ATOM   767  N  N   . LYS   A 1 100 ? -14.87879 3.55714   5.55630   1.000 18.13986 ? 100 LYS   A N   1 
ATOM   768  C  CA  . LYS   A 1 100 ? -13.65236 3.16354   6.22955   1.000 19.42363 ? 100 LYS   A CA  1 
ATOM   769  C  C   . LYS   A 1 100 ? -13.24317 1.79611   5.69633   1.000 19.38283 ? 100 LYS   A C   1 
ATOM   770  O  O   . LYS   A 1 100 ? -14.08057 0.89923   5.54689   1.000 18.11126 ? 100 LYS   A O   1 
ATOM   771  C  CB  . LYS   A 1 100 ? -13.85432 3.13609   7.74075   1.000 25.36030 ? 100 LYS   A CB  1 
ATOM   772  C  CG  . LYS   A 1 100 ? -12.55753 3.00970   8.54330   1.000 31.37150 ? 100 LYS   A CG  1 
ATOM   773  C  CD  . LYS   A 1 100 ? -12.83542 2.62967   10.00218  1.000 38.13932 ? 100 LYS   A CD  1 
ATOM   774  C  CE  . LYS   A 1 100 ? -11.55202 2.25891   10.75400  1.000 41.02159 ? 100 LYS   A CE  1 
ATOM   775  N  NZ  . LYS   A 1 100 ? -11.86450 1.49126   12.00388  1.000 41.60731 ? 100 LYS   A NZ  1 
ATOM   776  N  N   . TYR   A 1 101 ? -11.96587 1.64527   5.33940   1.000 16.89082 ? 101 TYR   A N   1 
ATOM   777  C  CA  . TYR   A 1 101 ? -11.55402 0.38437   4.74283   1.000 16.14778 ? 101 TYR   A CA  1 
ATOM   778  C  C   . TYR   A 1 101 ? -10.11298 0.05149   5.09411   1.000 15.78947 ? 101 TYR   A C   1 
ATOM   779  O  O   . TYR   A 1 101 ? -9.34257  0.88932   5.58392   1.000 16.43120 ? 101 TYR   A O   1 
ATOM   780  C  CB  . TYR   A 1 101 ? -11.70576 0.39263   3.22206   1.000 14.39450 ? 101 TYR   A CB  1 
ATOM   781  C  CG  . TYR   A 1 101 ? -10.70190 1.28571   2.51546   1.000 18.31265 ? 101 TYR   A CG  1 
ATOM   782  C  CD1 . TYR   A 1 101 ? -10.94040 2.63916   2.35132   1.000 17.38105 ? 101 TYR   A CD1 1 
ATOM   783  C  CD2 . TYR   A 1 101 ? -9.52620  0.75708   1.98298   1.000 17.89053 ? 101 TYR   A CD2 1 
ATOM   784  C  CE1 . TYR   A 1 101 ? -10.02173 3.46692   1.69876   1.000 22.12336 ? 101 TYR   A CE1 1 
ATOM   785  C  CE2 . TYR   A 1 101 ? -8.60196  1.57972   1.33048   1.000 17.91643 ? 101 TYR   A CE2 1 
ATOM   786  C  CZ  . TYR   A 1 101 ? -8.86085  2.92498   1.18952   1.000 19.79835 ? 101 TYR   A CZ  1 
ATOM   787  O  OH  . TYR   A 1 101 ? -7.94789  3.75556   0.54905   1.000 27.02573 ? 101 TYR   A OH  1 
ATOM   788  N  N   . LYS   A 1 102 ? -9.78646  -1.21576  4.83027   1.000 13.68173 ? 102 LYS   A N   1 
ATOM   789  C  CA  . LYS   A 1 102 ? -8.44382  -1.77927  4.90644   1.000 14.36265 ? 102 LYS   A CA  1 
ATOM   790  C  C   . LYS   A 1 102 ? -8.25549  -2.74782  3.74851   1.000 14.13768 ? 102 LYS   A C   1 
ATOM   791  O  O   . LYS   A 1 102 ? -9.21593  -3.32933  3.24114   1.000 12.22089 ? 102 LYS   A O   1 
ATOM   792  C  CB  . LYS   A 1 102 ? -8.20868  -2.54049  6.22083   1.000 18.16144 ? 102 LYS   A CB  1 
ATOM   793  C  CG  . LYS   A 1 102 ? -8.56684  -1.75786  7.44353   1.000 22.29024 ? 102 LYS   A CG  1 
ATOM   794  C  CD  . LYS   A 1 102 ? -8.08522  -2.42317  8.70546   1.000 31.00351 ? 102 LYS   A CD  1 
ATOM   795  C  CE  . LYS   A 1 102 ? -8.72223  -3.77063  8.87392   1.000 25.06429 ? 102 LYS   A CE  1 
ATOM   796  N  NZ  . LYS   A 1 102 ? -8.49227  -4.27995  10.26950  1.000 37.28050 ? 102 LYS   A NZ  1 
ATOM   797  N  N   . PHE   A 1 103 ? -6.99440  -2.92116  3.34792   1.000 13.36424 ? 103 PHE   A N   1 
ATOM   798  C  CA  . PHE   A 1 103 ? -6.59991  -3.97306  2.42266   1.000 11.35801 ? 103 PHE   A CA  1 
ATOM   799  C  C   . PHE   A 1 103 ? -5.92619  -5.07190  3.24043   1.000 11.08173 ? 103 PHE   A C   1 
ATOM   800  O  O   . PHE   A 1 103 ? -4.80830  -4.87978  3.74702   1.000 14.40678 ? 103 PHE   A O   1 
ATOM   801  C  CB  . PHE   A 1 103 ? -5.62979  -3.45136  1.36675   1.000 10.85231 ? 103 PHE   A CB  1 
ATOM   802  C  CG  . PHE   A 1 103 ? -6.23308  -2.53950  0.31820   1.000 12.79568 ? 103 PHE   A CG  1 
ATOM   803  C  CD1 . PHE   A 1 103 ? -7.60583  -2.37021  0.19057   1.000 11.41248 ? 103 PHE   A CD1 1 
ATOM   804  C  CD2 . PHE   A 1 103 ? -5.39356  -1.85745  -0.54542  1.000 15.25356 ? 103 PHE   A CD2 1 
ATOM   805  C  CE1 . PHE   A 1 103 ? -8.12199  -1.51584  -0.77277  1.000 13.61733 ? 103 PHE   A CE1 1 
ATOM   806  C  CE2 . PHE   A 1 103 ? -5.89552  -1.01757  -1.52677  1.000 15.66980 ? 103 PHE   A CE2 1 
ATOM   807  C  CZ  . PHE   A 1 103 ? -7.26167  -0.85069  -1.64611  1.000 12.85354 ? 103 PHE   A CZ  1 
ATOM   808  N  N   . VAL   A 1 104 ? -6.59125  -6.21655  3.35604   1.000 10.42426 ? 104 VAL   A N   1 
ATOM   809  C  CA  . VAL   A 1 104 ? -6.06694  -7.34215  4.11456   1.000 12.12760 ? 104 VAL   A CA  1 
ATOM   810  C  C   . VAL   A 1 104 ? -5.88884  -8.50668  3.15642   1.000 12.71085 ? 104 VAL   A C   1 
ATOM   811  O  O   . VAL   A 1 104 ? -6.53940  -8.57535  2.11000   1.000 18.26806 ? 104 VAL   A O   1 
ATOM   812  C  CB  . VAL   A 1 104 ? -6.97225  -7.71517  5.30132   1.000 13.27529 ? 104 VAL   A CB  1 
ATOM   813  C  CG1 . VAL   A 1 104 ? -7.33392  -6.45071  6.09534   1.000 17.92197 ? 104 VAL   A CG1 1 
ATOM   814  C  CG2 . VAL   A 1 104 ? -8.22184  -8.34104  4.79094   1.000 14.81312 ? 104 VAL   A CG2 1 
ATOM   815  N  N   . ARG   A 1 105 ? -4.95156  -9.39724  3.47609   1.000 10.66965 ? 105 ARG   A N   1 
ATOM   816  C  CA  . ARG   A 1 105 ? -4.82269  -10.64489 2.73620   1.000 9.36976  ? 105 ARG   A CA  1 
ATOM   817  C  C   . ARG   A 1 105 ? -5.30556  -11.77247 3.63696   1.000 9.19889  ? 105 ARG   A C   1 
ATOM   818  O  O   . ARG   A 1 105 ? -4.91693  -11.84337 4.80878   1.000 11.18266 ? 105 ARG   A O   1 
ATOM   819  C  CB  . ARG   A 1 105 ? -3.37516  -10.88710 2.30394   1.000 11.93711 ? 105 ARG   A CB  1 
ATOM   820  C  CG  . ARG   A 1 105 ? -3.25043  -12.04852 1.36122   1.000 9.21131  ? 105 ARG   A CG  1 
ATOM   821  C  CD  . ARG   A 1 105 ? -1.77631  -12.23793 0.98659   1.000 8.78170  ? 105 ARG   A CD  1 
ATOM   822  N  NE  . ARG   A 1 105 ? -1.60280  -13.46734 0.22025   1.000 8.73817  ? 105 ARG   A NE  1 
ATOM   823  C  CZ  . ARG   A 1 105 ? -1.60601  -13.52800 -1.10272  1.000 8.67833  ? 105 ARG   A CZ  1 
ATOM   824  N  NH1 . ARG   A 1 105 ? -1.79459  -12.45006 -1.83445  1.000 9.41814  ? 105 ARG   A NH1 1 
ATOM   825  N  NH2 . ARG   A 1 105 ? -1.44169  -14.70542 -1.70392  1.000 9.74814  ? 105 ARG   A NH2 1 
ATOM   826  N  N   . ILE   A 1 106 ? -6.18992  -12.61567 3.11495   1.000 10.54516 ? 106 ILE   A N   1 
ATOM   827  C  CA  . ILE   A 1 106 ? -6.73558  -13.69407 3.92629   1.000 12.35321 ? 106 ILE   A CA  1 
ATOM   828  C  C   . ILE   A 1 106 ? -5.92953  -14.96571 3.73342   1.000 12.10677 ? 106 ILE   A C   1 
ATOM   829  O  O   . ILE   A 1 106 ? -5.15981  -15.09360 2.77970   1.000 12.46783 ? 106 ILE   A O   1 
ATOM   830  C  CB  . ILE   A 1 106 ? -8.21647  -13.96157 3.61235   1.000 10.45331 ? 106 ILE   A CB  1 
ATOM   831  C  CG1 . ILE   A 1 106 ? -8.41735  -14.35740 2.14772   1.000 9.07420  ? 106 ILE   A CG1 1 
ATOM   832  C  CG2 . ILE   A 1 106 ? -9.05475  -12.77021 4.03376   1.000 18.63158 ? 106 ILE   A CG2 1 
ATOM   833  C  CD1 . ILE   A 1 106 ? -9.82722  -14.96008 1.89430   1.000 14.62581 ? 106 ILE   A CD1 1 
ATOM   834  N  N   . GLN   A 1 107 ? -6.12326  -15.89561 4.59928   1.000 12.92148 ? 107 GLN   A N   1 
ATOM   835  C  CA  . GLN   A 1 107 ? -5.59173  -17.24992 4.65004   1.000 12.64827 ? 107 GLN   A CA  1 
ATOM   836  C  C   . GLN   A 1 107 ? -6.54191  -18.23991 3.97194   1.000 12.21350 ? 107 GLN   A C   1 
ATOM   837  O  O   . GLN   A 1 107 ? -7.76451  -18.09438 4.04855   1.000 11.87692 ? 107 GLN   A O   1 
ATOM   838  C  CB  . GLN   A 1 107 ? -5.39854  -17.65781 6.10760   1.000 14.75552 ? 107 GLN   A CB  1 
ATOM   839  C  CG  . GLN   A 1 107 ? -4.28625  -16.93019 6.77202   1.000 14.16391 ? 107 GLN   A CG  1 
ATOM   840  C  CD  . GLN   A 1 107 ? -2.96849  -17.43095 6.26745   1.000 15.42475 ? 107 GLN   A CD  1 
ATOM   841  O  OE1 . GLN   A 1 107 ? -2.81407  -18.64419 6.11153   1.000 12.71881 ? 107 GLN   A OE1 1 
ATOM   842  N  NE2 . GLN   A 1 107 ? -2.00141  -16.52151 5.99887   1.000 15.10206 ? 107 GLN   A NE2 1 
ATOM   843  N  N   . PRO   A 1 108 ? -6.01464  -19.27920 3.32895   1.000 11.46721 ? 108 PRO   A N   1 
ATOM   844  C  CA  . PRO   A 1 108 ? -6.86980  -20.40537 2.93160   1.000 15.27661 ? 108 PRO   A CA  1 
ATOM   845  C  C   . PRO   A 1 108 ? -7.66777  -20.88698 4.13323   1.000 12.97812 ? 108 PRO   A C   1 
ATOM   846  O  O   . PRO   A 1 108 ? -7.16658  -20.92973 5.25991   1.000 15.69489 ? 108 PRO   A O   1 
ATOM   847  C  CB  . PRO   A 1 108 ? -5.87718  -21.47738 2.44992   1.000 15.29916 ? 108 PRO   A CB  1 
ATOM   848  C  CG  . PRO   A 1 108 ? -4.53640  -20.84694 2.44473   1.000 17.80904 ? 108 PRO   A CG  1 
ATOM   849  C  CD  . PRO   A 1 108 ? -4.62244  -19.40846 2.86369   1.000 12.80135 ? 108 PRO   A CD  1 
ATOM   850  N  N   . GLY   A 1 109 ? -8.93947  -21.22197 3.90062   1.000 9.01347  ? 109 GLY   A N   1 
ATOM   851  C  CA  . GLY   A 1 109 ? -9.83319  -21.60330 4.96199   1.000 15.99384 ? 109 GLY   A CA  1 
ATOM   852  C  C   . GLY   A 1 109 ? -10.69917 -20.47141 5.47548   1.000 16.08855 ? 109 GLY   A C   1 
ATOM   853  O  O   . GLY   A 1 109 ? -11.73680 -20.74073 6.09999   1.000 17.78512 ? 109 GLY   A O   1 
ATOM   854  N  N   . GLN   A 1 110 ? -10.29677 -19.21704 5.24903   1.000 11.30129 ? 110 GLN   A N   1 
ATOM   855  C  CA  . GLN   A 1 110 ? -11.12151 -18.08140 5.65231   1.000 13.78790 ? 110 GLN   A CA  1 
ATOM   856  C  C   . GLN   A 1 110 ? -12.18287 -17.74999 4.59955   1.000 10.72255 ? 110 GLN   A C   1 
ATOM   857  O  O   . GLN   A 1 110 ? -12.07408 -18.10416 3.41679   1.000 11.68580 ? 110 GLN   A O   1 
ATOM   858  C  CB  . GLN   A 1 110 ? -10.28249 -16.81867 5.95329   1.000 13.85743 ? 110 GLN   A CB  1 
ATOM   859  C  CG  . GLN   A 1 110 ? -9.30647  -16.94113 7.13135   1.000 16.07344 ? 110 GLN   A CG  1 
ATOM   860  C  CD  . GLN   A 1 110 ? -8.60784  -15.60858 7.51877   1.000 27.15277 ? 110 GLN   A CD  1 
ATOM   861  O  OE1 . GLN   A 1 110 ? -7.68809  -15.11483 6.85619   1.000 15.87008 ? 110 GLN   A OE1 1 
ATOM   862  N  NE2 . GLN   A 1 110 ? -9.07516  -15.02243 8.62281   1.000 34.72576 ? 110 GLN   A NE2 1 
ATOM   863  N  N   . THR   A 1 111 ? -13.25788 -17.12136 5.05845   1.000 12.19427 ? 111 THR   A N   1 
ATOM   864  C  CA  . THR   A 1 111 ? -14.40163 -16.81590 4.20928   1.000 10.76042 ? 111 THR   A CA  1 
ATOM   865  C  C   . THR   A 1 111 ? -14.49183 -15.31832 3.94097   1.000 13.05145 ? 111 THR   A C   1 
ATOM   866  O  O   . THR   A 1 111 ? -13.85971 -14.50223 4.61503   1.000 11.81987 ? 111 THR   A O   1 
ATOM   867  C  CB  . THR   A 1 111 ? -15.71791 -17.29637 4.85088   1.000 11.16345 ? 111 THR   A CB  1 
ATOM   868  O  OG1 . THR   A 1 111 ? -15.83354 -16.73562 6.16896   1.000 14.15840 ? 111 THR   A OG1 1 
ATOM   869  C  CG2 . THR   A 1 111 ? -15.70007 -18.80681 4.94824   1.000 10.05323 ? 111 THR   A CG2 1 
ATOM   870  N  N   . PHE   A 1 112 ? -15.28013 -14.97061 2.91869   1.000 9.93973  ? 112 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 112 ? -15.52990 -13.57745 2.57607   1.000 11.82127 ? 112 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 112 ? -16.72761 -13.50832 1.64759   1.000 10.48573 ? 112 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 112 ? -17.14291 -14.51415 1.05074   1.000 11.58471 ? 112 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 112 ? -14.31230 -12.92654 1.90063   1.000 11.33887 ? 112 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 112 ? -13.81764 -13.65183 0.65713   1.000 13.24512 ? 112 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 112 ? -13.02138 -14.79131 0.76243   1.000 12.64330 ? 112 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 112 ? -14.09548 -13.16576 -0.61375  1.000 8.43902  ? 112 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 112 ? -12.55150 -15.44534 -0.39265  1.000 12.33707 ? 112 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 112 ? -13.63277 -13.80541 -1.76644  1.000 10.62089 ? 112 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 112 ? -12.83724 -14.94486 -1.65190  1.000 13.03260 ? 112 PHE   A CZ  1 
ATOM   881  N  N   . SER   A 1 113 ? -17.27446 -12.30204 1.52888   1.000 11.12604 ? 113 SER   A N   1 
ATOM   882  C  CA  . SER   A 1 113 ? -18.39764 -12.03781 0.64815   1.000 11.21607 ? 113 SER   A CA  1 
ATOM   883  C  C   . SER   A 1 113 ? -17.88697 -11.48751 -0.66678  1.000 10.93553 ? 113 SER   A C   1 
ATOM   884  O  O   . SER   A 1 113 ? -16.93611 -10.69749 -0.69068  1.000 11.08640 ? 113 SER   A O   1 
ATOM   885  C  CB  . SER   A 1 113 ? -19.38575 -11.03700 1.26885   1.000 12.02242 ? 113 SER   A CB  1 
ATOM   886  O  OG  . SER   A 1 113 ? -19.74898 -11.42472 2.57913   1.000 13.65664 ? 113 SER   A OG  1 
ATOM   887  N  N   . VAL   A 1 114 ? -18.53477 -11.89215 -1.75389  1.000 9.99190  ? 114 VAL   A N   1 
ATOM   888  C  CA  . VAL   A 1 114 ? -18.20826 -11.44155 -3.09962  1.000 11.90153 ? 114 VAL   A CA  1 
ATOM   889  C  C   . VAL   A 1 114 ? -19.37466 -10.62851 -3.62975  1.000 11.20692 ? 114 VAL   A C   1 
ATOM   890  O  O   . VAL   A 1 114 ? -20.52523 -11.08849 -3.60535  1.000 11.42255 ? 114 VAL   A O   1 
ATOM   891  C  CB  . VAL   A 1 114 ? -17.90137 -12.62826 -4.02702  1.000 9.02048  ? 114 VAL   A CB  1 
ATOM   892  C  CG1 . VAL   A 1 114 ? -17.81360 -12.13853 -5.50222  1.000 11.90111 ? 114 VAL   A CG1 1 
ATOM   893  C  CG2 . VAL   A 1 114 ? -16.61914 -13.35096 -3.61732  1.000 14.76919 ? 114 VAL   A CG2 1 
ATOM   894  N  N   . LEU   A 1 115 ? -19.08760 -9.42773  -4.12114  1.000 10.72878 ? 115 LEU   A N   1 
ATOM   895  C  CA  . LEU   A 1 115 ? -20.07134 -8.63506  -4.84878  1.000 10.73829 ? 115 LEU   A CA  1 
ATOM   896  C  C   . LEU   A 1 115 ? -19.78265 -8.78238  -6.33919  1.000 12.70264 ? 115 LEU   A C   1 
ATOM   897  O  O   . LEU   A 1 115 ? -18.89721 -8.11887  -6.88322  1.000 12.89586 ? 115 LEU   A O   1 
ATOM   898  C  CB  . LEU   A 1 115 ? -20.04972 -7.17983  -4.39619  1.000 13.50736 ? 115 LEU   A CB  1 
ATOM   899  C  CG  . LEU   A 1 115 ? -21.07754 -6.30410  -5.11423  1.000 11.04277 ? 115 LEU   A CG  1 
ATOM   900  C  CD1 . LEU   A 1 115 ? -22.55806 -6.75134  -4.82747  1.000 13.59195 ? 115 LEU   A CD1 1 
ATOM   901  C  CD2 . LEU   A 1 115 ? -20.88963 -4.84484  -4.74780  1.000 13.01463 ? 115 LEU   A CD2 1 
ATOM   902  N  N   . ALA   A 1 116 ? -20.50468 -9.68742  -6.99539  1.000 11.34245 ? 116 ALA   A N   1 
ATOM   903  C  CA  . ALA   A 1 116 ? -20.28491 -9.90862  -8.41482  1.000 10.85729 ? 116 ALA   A CA  1 
ATOM   904  C  C   . ALA   A 1 116 ? -20.82828 -8.71693  -9.18414  1.000 16.36473 ? 116 ALA   A C   1 
ATOM   905  O  O   . ALA   A 1 116 ? -21.96629 -8.28757  -8.95398  1.000 17.95056 ? 116 ALA   A O   1 
ATOM   906  C  CB  . ALA   A 1 116 ? -20.96815 -11.19555 -8.87634  1.000 13.82816 ? 116 ALA   A CB  1 
ATOM   907  N  N   . CYS   A 1 117 ? -20.03875 -8.21607  -10.13098 1.000 11.27105 ? 117 CYS   A N   1 
ATOM   908  C  CA  . CYS   A 1 117 ? -20.36623 -6.99661  -10.84894 1.000 13.87909 ? 117 CYS   A CA  1 
ATOM   909  C  C   . CYS   A 1 117 ? -20.07303 -7.16708  -12.33120 1.000 16.67393 ? 117 CYS   A C   1 
ATOM   910  O  O   . CYS   A 1 117 ? -19.15778 -7.89612  -12.71887 1.000 16.73353 ? 117 CYS   A O   1 
ATOM   911  C  CB  . CYS   A 1 117 ? -19.54277 -5.81453  -10.35844 1.000 17.73426 ? 117 CYS   A CB  1 
ATOM   912  S  SG  . CYS   A 1 117 ? -19.92183 -5.28598  -8.71362  1.000 20.43215 ? 117 CYS   A SG  1 
ATOM   913  N  N   . TYR   A 1 118 ? -20.82794 -6.43506  -13.14743 1.000 16.15725 ? 118 TYR   A N   1 
ATOM   914  C  CA  . TYR   A 1 118 ? -20.65796 -6.37237  -14.59470 1.000 19.79021 ? 118 TYR   A CA  1 
ATOM   915  C  C   . TYR   A 1 118 ? -20.85916 -4.92915  -15.01789 1.000 22.88937 ? 118 TYR   A C   1 
ATOM   916  O  O   . TYR   A 1 118 ? -21.82925 -4.29113  -14.59395 1.000 19.88339 ? 118 TYR   A O   1 
ATOM   917  C  CB  . TYR   A 1 118 ? -21.64304 -7.30448  -15.32273 1.000 19.32370 ? 118 TYR   A CB  1 
ATOM   918  C  CG  . TYR   A 1 118 ? -21.46299 -8.72150  -14.85694 1.000 20.65428 ? 118 TYR   A CG  1 
ATOM   919  C  CD1 . TYR   A 1 118 ? -22.15511 -9.20413  -13.74703 1.000 18.38436 ? 118 TYR   A CD1 1 
ATOM   920  C  CD2 . TYR   A 1 118 ? -20.53761 -9.55240  -15.46794 1.000 19.60815 ? 118 TYR   A CD2 1 
ATOM   921  C  CE1 . TYR   A 1 118 ? -21.93777 -10.47879 -13.27864 1.000 19.75731 ? 118 TYR   A CE1 1 
ATOM   922  C  CE2 . TYR   A 1 118 ? -20.31995 -10.82876 -15.01234 1.000 20.94649 ? 118 TYR   A CE2 1 
ATOM   923  C  CZ  . TYR   A 1 118 ? -21.01965 -11.28719 -13.92318 1.000 22.67190 ? 118 TYR   A CZ  1 
ATOM   924  O  OH  . TYR   A 1 118 ? -20.78068 -12.55933 -13.47065 1.000 19.87234 ? 118 TYR   A OH  1 
ATOM   925  N  N   . ASN   A 1 119 ? -19.92796 -4.41146  -15.82415 1.000 23.64507 ? 119 ASN   A N   1 
ATOM   926  C  CA  . ASN   A 1 119 ? -20.00248 -3.03909  -16.33409 1.000 23.05381 ? 119 ASN   A CA  1 
ATOM   927  C  C   . ASN   A 1 119 ? -20.11094 -2.01351  -15.21001 1.000 25.57972 ? 119 ASN   A C   1 
ATOM   928  O  O   . ASN   A 1 119 ? -20.78065 -0.98427  -15.36432 1.000 23.92423 ? 119 ASN   A O   1 
ATOM   929  C  CB  . ASN   A 1 119 ? -21.17546 -2.86426  -17.30482 1.000 27.48934 ? 119 ASN   A CB  1 
ATOM   930  C  CG  . ASN   A 1 119 ? -21.12357 -3.83220  -18.46006 1.000 29.57044 ? 119 ASN   A CG  1 
ATOM   931  O  OD1 . ASN   A 1 119 ? -20.21698 -3.76859  -19.29131 1.000 36.14877 ? 119 ASN   A OD1 1 
ATOM   932  N  ND2 . ASN   A 1 119 ? -22.09078 -4.74472  -18.51492 1.000 31.24464 ? 119 ASN   A ND2 1 
ATOM   933  N  N   . GLY   A 1 120 ? -19.47020 -2.29603  -14.07519 1.000 20.02218 ? 120 GLY   A N   1 
ATOM   934  C  CA  . GLY   A 1 120 ? -19.53914 -1.43749  -12.90900 1.000 19.50945 ? 120 GLY   A CA  1 
ATOM   935  C  C   . GLY   A 1 120 ? -20.83579 -1.51333  -12.13118 1.000 24.05619 ? 120 GLY   A C   1 
ATOM   936  O  O   . GLY   A 1 120 ? -21.00957 -0.75190  -11.17479 1.000 22.43170 ? 120 GLY   A O   1 
ATOM   937  N  N   . SER   A 1 121 ? -21.75519 -2.40714  -12.50515 1.000 21.08210 ? 121 SER   A N   1 
ATOM   938  C  CA  . SER   A 1 121 ? -23.06182 -2.49405  -11.84896 1.000 20.71039 ? 121 SER   A CA  1 
ATOM   939  C  C   . SER   A 1 121 ? -23.18714 -3.78849  -11.05465 1.000 23.29388 ? 121 SER   A C   1 
ATOM   940  O  O   . SER   A 1 121 ? -23.02413 -4.88083  -11.62242 1.000 18.97276 ? 121 SER   A O   1 
ATOM   941  C  CB  . SER   A 1 121 ? -24.18229 -2.39874  -12.87736 1.000 26.72302 ? 121 SER   A CB  1 
ATOM   942  O  OG  . SER   A 1 121 ? -24.35043 -1.06469  -13.30051 1.000 31.76530 ? 121 SER   A OG  1 
ATOM   943  N  N   . PRO   A 1 122 ? -23.46518 -3.70864  -9.75127  1.000 20.70932 ? 122 PRO   A N   1 
ATOM   944  C  CA  . PRO   A 1 122 ? -23.56305 -4.92555  -8.92967  1.000 15.09973 ? 122 PRO   A CA  1 
ATOM   945  C  C   . PRO   A 1 122 ? -24.69764 -5.83171  -9.37675  1.000 20.55411 ? 122 PRO   A C   1 
ATOM   946  O  O   . PRO   A 1 122 ? -25.82388 -5.38482  -9.57822  1.000 25.06684 ? 122 PRO   A O   1 
ATOM   947  C  CB  . PRO   A 1 122 ? -23.83383 -4.37852  -7.52686  1.000 21.13009 ? 122 PRO   A CB  1 
ATOM   948  C  CG  . PRO   A 1 122 ? -23.34280 -2.96177  -7.53763  1.000 25.30280 ? 122 PRO   A CG  1 
ATOM   949  C  CD  . PRO   A 1 122 ? -23.18881 -2.50320  -8.95153  1.000 21.86455 ? 122 PRO   A CD  1 
ATOM   950  N  N   . SER   A 1 123 ? -24.40459 -7.12611  -9.46352  1.000 21.12013 ? 123 SER   A N   1 
ATOM   951  C  CA  . SER   A 1 123 ? -25.38266 -8.12747  -9.86414  1.000 21.54845 ? 123 SER   A CA  1 
ATOM   952  C  C   . SER   A 1 123 ? -25.87908 -9.00043  -8.71775  1.000 16.75331 ? 123 SER   A C   1 
ATOM   953  O  O   . SER   A 1 123 ? -27.08525 -9.29888  -8.65588  1.000 17.95446 ? 123 SER   A O   1 
ATOM   954  C  CB  . SER   A 1 123 ? -24.78493 -9.01756  -10.96128 1.000 26.07617 ? 123 SER   A CB  1 
ATOM   955  O  OG  . SER   A 1 123 ? -25.59454 -10.15019 -11.20890 1.000 33.44443 ? 123 SER   A OG  1 
ATOM   956  N  N   . GLY   A 1 124 ? -25.00403 -9.42680  -7.81203  1.000 15.58128 ? 124 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? -25.39223 -10.29607 -6.71456  1.000 14.81574 ? 124 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? -24.28112 -10.41350 -5.70150  1.000 13.58790 ? 124 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? -23.12980 -10.03903 -5.95786  1.000 12.91974 ? 124 GLY   A O   1 
ATOM   960  N  N   . VAL   A 1 125 ? -24.64054 -10.94064 -4.53453  1.000 11.93625 ? 125 VAL   A N   1 
ATOM   961  C  CA  . VAL   A 1 125 ? -23.72446 -11.08430 -3.41832  1.000 11.44671 ? 125 VAL   A CA  1 
ATOM   962  C  C   . VAL   A 1 125 ? -23.81467 -12.51153 -2.90915  1.000 13.35369 ? 125 VAL   A C   1 
ATOM   963  O  O   . VAL   A 1 125 ? -24.90445 -13.09380 -2.85106  1.000 13.51618 ? 125 VAL   A O   1 
ATOM   964  C  CB  . VAL   A 1 125 ? -24.00099 -10.05934 -2.29259  1.000 12.70509 ? 125 VAL   A CB  1 
ATOM   965  C  CG1 . VAL   A 1 125 ? -25.31130 -10.33533 -1.63829  1.000 18.24849 ? 125 VAL   A CG1 1 
ATOM   966  C  CG2 . VAL   A 1 125 ? -22.88009 -10.05385 -1.27920  1.000 14.91810 ? 125 VAL   A CG2 1 
ATOM   967  N  N   . TYR   A 1 126 ? -22.66016 -13.09329 -2.60031  1.000 13.14564 ? 126 TYR   A N   1 
ATOM   968  C  CA  . TYR   A 1 126 ? -22.59481 -14.44512 -2.05440  1.000 11.77348 ? 126 TYR   A CA  1 
ATOM   969  C  C   . TYR   A 1 126 ? -21.32939 -14.62643 -1.22377  1.000 13.33806 ? 126 TYR   A C   1 
ATOM   970  O  O   . TYR   A 1 126 ? -20.36968 -13.85254 -1.30147  1.000 14.17033 ? 126 TYR   A O   1 
ATOM   971  C  CB  . TYR   A 1 126 ? -22.67397 -15.52579 -3.15391  1.000 14.10723 ? 126 TYR   A CB  1 
ATOM   972  C  CG  . TYR   A 1 126 ? -21.63196 -15.41324 -4.23915  1.000 13.36044 ? 126 TYR   A CG  1 
ATOM   973  C  CD1 . TYR   A 1 126 ? -20.37246 -15.97765 -4.08660  1.000 15.87542 ? 126 TYR   A CD1 1 
ATOM   974  C  CD2 . TYR   A 1 126 ? -21.89936 -14.72857 -5.41213  1.000 15.84158 ? 126 TYR   A CD2 1 
ATOM   975  C  CE1 . TYR   A 1 126 ? -19.42212 -15.86033 -5.08445  1.000 16.19030 ? 126 TYR   A CE1 1 
ATOM   976  C  CE2 . TYR   A 1 126 ? -20.92878 -14.60616 -6.41277  1.000 16.83946 ? 126 TYR   A CE2 1 
ATOM   977  C  CZ  . TYR   A 1 126 ? -19.71240 -15.17551 -6.23460  1.000 17.38982 ? 126 TYR   A CZ  1 
ATOM   978  O  OH  . TYR   A 1 126 ? -18.75733 -15.05996 -7.22804  1.000 19.35823 ? 126 TYR   A OH  1 
ATOM   979  N  N   . GLN   A 1 127 ? -21.34740 -15.68792 -0.43334  1.000 12.26021 ? 127 GLN   A N   1 
ATOM   980  C  CA  . GLN   A 1 127 ? -20.25282 -16.03214 0.45289   1.000 14.49643 ? 127 GLN   A CA  1 
ATOM   981  C  C   . GLN   A 1 127 ? -19.37021 -17.09201 -0.19998  1.000 14.36433 ? 127 GLN   A C   1 
ATOM   982  O  O   . GLN   A 1 127 ? -19.87515 -18.01669 -0.84498  1.000 20.35362 ? 127 GLN   A O   1 
ATOM   983  C  CB  . GLN   A 1 127 ? -20.81806 -16.52242 1.78795   1.000 18.05313 ? 127 GLN   A CB  1 
ATOM   984  C  CG  . GLN   A 1 127 ? -19.82690 -16.61757 2.85237   1.000 20.84271 ? 127 GLN   A CG  1 
ATOM   985  C  CD  . GLN   A 1 127 ? -19.52291 -15.29163 3.51546   1.000 15.54402 ? 127 GLN   A CD  1 
ATOM   986  O  OE1 . GLN   A 1 127 ? -19.85883 -14.21083 3.00600   1.000 16.83772 ? 127 GLN   A OE1 1 
ATOM   987  N  NE2 . GLN   A 1 127 ? -18.86598 -15.37248 4.66062   1.000 14.72298 ? 127 GLN   A NE2 1 
ATOM   988  N  N   . CYS   A 1 128 ? -18.04526 -16.92864 -0.03807  1.000 13.19876 ? 128 CYS   A N   1 
ATOM   989  C  CA  . CYS   A 1 128 ? -16.97365 -17.73490 -0.62439  1.000 20.26376 ? 128 CYS   A CA  1 
ATOM   990  C  C   . CYS   A 1 128 ? -16.00315 -18.10331 0.48919   1.000 16.62810 ? 128 CYS   A C   1 
ATOM   991  O  O   . CYS   A 1 128 ? -15.91816 -17.39199 1.48894   1.000 13.89990 ? 128 CYS   A O   1 
ATOM   992  C  CB  . CYS   A 1 128 ? -16.17512 -16.94704 -1.74083  1.000 11.71818 ? 128 CYS   A CB  1 
ATOM   993  S  SG  . CYS   A 1 128 ? -16.87466 -17.19464 -3.34120  1.000 29.25365 ? 128 CYS   A SG  1 
ATOM   994  N  N   . ALA   A 1 129 ? -15.29392 -19.22791 0.33192   1.000 15.76295 ? 129 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 129 ? -14.11867 -19.54088 1.13898   1.000 14.57859 ? 129 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 129 ? -12.90201 -19.57583 0.22497   1.000 15.03817 ? 129 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 129 ? -12.98607 -19.98450 -0.93930  1.000 14.65502 ? 129 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 129 ? -14.24257 -20.88982 1.86537   1.000 16.43799 ? 129 ALA   A CB  1 
ATOM   999  N  N   . MET   A 1 130 ? -11.76848 -19.14888 0.75346   1.000 12.13041 ? 130 MET   A N   1 
ATOM   1000 C  CA  . MET   A 1 130 ? -10.51510 -19.34949 0.04137   1.000 10.51289 ? 130 MET   A CA  1 
ATOM   1001 C  C   . MET   A 1 130 ? -10.11630 -20.80850 0.24414   1.000 11.29643 ? 130 MET   A C   1 
ATOM   1002 O  O   . MET   A 1 130 ? -9.95903  -21.25277 1.38534   1.000 13.61159 ? 130 MET   A O   1 
ATOM   1003 C  CB  . MET   A 1 130 ? -9.44732  -18.37056 0.54446   1.000 12.80335 ? 130 MET   A CB  1 
ATOM   1004 C  CG  . MET   A 1 130 ? -8.03388  -18.59248 -0.02768  1.000 15.39099 ? 130 MET   A CG  1 
ATOM   1005 S  SD  . MET   A 1 130 ? -7.91963  -18.10597 -1.74973  1.000 18.62483 ? 130 MET   A SD  1 
ATOM   1006 C  CE  . MET   A 1 130 ? -8.34662  -16.35188 -1.73497  1.000 8.84830  ? 130 MET   A CE  1 
ATOM   1007 N  N   . ARG   A 1 131 ? -10.00160 -21.57175 -0.84564  1.000 11.06774 ? 131 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 131 ? -9.71381  -22.99591 -0.72012  1.000 11.26665 ? 131 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 131 ? -8.26281  -23.18573 -0.28093  1.000 11.92536 ? 131 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 131 ? -7.43995  -22.28243 -0.45979  1.000 13.33814 ? 131 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 131 ? -9.94047  -23.71981 -2.05493  1.000 13.87447 ? 131 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 131 ? -11.35282 -23.64748 -2.63912  1.000 14.80027 ? 131 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 131 ? -12.41265 -24.14682 -1.66446  1.000 13.86379 ? 131 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 131 ? -12.05073 -25.42476 -1.06575  1.000 13.89857 ? 131 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 131 ? -12.71575 -25.97969 -0.06003  1.000 14.14755 ? 131 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 131 ? -13.79998 -25.41141 0.43942   1.000 15.70690 ? 131 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 131 ? -12.25305 -27.10491 0.48695   1.000 15.72197 ? 131 ARG   A NH2 1 
ATOM   1018 N  N   . PRO   A 1 132 ? -7.92557  -24.35049 0.30945   1.000 12.53366 ? 132 PRO   A N   1 
ATOM   1019 C  CA  . PRO   A 1 132 ? -6.51273  -24.64634 0.57945   1.000 13.21426 ? 132 PRO   A CA  1 
ATOM   1020 C  C   . PRO   A 1 132 ? -5.62676  -24.49622 -0.63437  1.000 16.14014 ? 132 PRO   A C   1 
ATOM   1021 O  O   . PRO   A 1 132 ? -4.44835  -24.14015 -0.46838  1.000 13.90013 ? 132 PRO   A O   1 
ATOM   1022 C  CB  . PRO   A 1 132 ? -6.55480  -26.09859 1.08259   1.000 16.74440 ? 132 PRO   A CB  1 
ATOM   1023 C  CG  . PRO   A 1 132 ? -7.87767  -26.19472 1.76869   1.000 16.25922 ? 132 PRO   A CG  1 
ATOM   1024 C  CD  . PRO   A 1 132 ? -8.80106  -25.41921 0.85089   1.000 13.19463 ? 132 PRO   A CD  1 
ATOM   1025 N  N   . ASN   A 1 133 ? -6.13777  -24.71981 -1.85774  1.000 13.69088 ? 133 ASN   A N   1 
ATOM   1026 C  CA  . ASN   A 1 133 ? -5.28789  -24.56692 -3.03593  1.000 12.28335 ? 133 ASN   A CA  1 
ATOM   1027 C  C   . ASN   A 1 133 ? -5.32646  -23.15776 -3.60700  1.000 12.37154 ? 133 ASN   A C   1 
ATOM   1028 O  O   . ASN   A 1 133 ? -4.85671  -22.95610 -4.73519  1.000 13.41216 ? 133 ASN   A O   1 
ATOM   1029 C  CB  . ASN   A 1 133 ? -5.64733  -25.58611 -4.12703  1.000 15.98276 ? 133 ASN   A CB  1 
ATOM   1030 C  CG  . ASN   A 1 133 ? -7.03894  -25.37461 -4.69365  1.000 12.46407 ? 133 ASN   A CG  1 
ATOM   1031 O  OD1 . ASN   A 1 133 ? -7.71751  -24.42016 -4.35013  1.000 13.46549 ? 133 ASN   A OD1 1 
ATOM   1032 N  ND2 . ASN   A 1 133 ? -7.44618  -26.26669 -5.59140  1.000 15.02272 ? 133 ASN   A ND2 1 
ATOM   1033 N  N   . PHE   A 1 134 ? -5.88700  -22.19725 -2.86038  1.000 10.35375 ? 134 PHE   A N   1 
ATOM   1034 C  CA  . PHE   A 1 134 ? -5.87949  -20.77466 -3.19574  1.000 12.12674 ? 134 PHE   A CA  1 
ATOM   1035 C  C   . PHE   A 1 134 ? -6.76627  -20.42580 -4.38279  1.000 14.75984 ? 134 PHE   A C   1 
ATOM   1036 O  O   . PHE   A 1 134 ? -6.60253  -19.36130 -4.99355  1.000 17.01427 ? 134 PHE   A O   1 
ATOM   1037 C  CB  . PHE   A 1 134 ? -4.45676  -20.26998 -3.46327  1.000 11.15573 ? 134 PHE   A CB  1 
ATOM   1038 C  CG  . PHE   A 1 134 ? -3.61992  -20.09767 -2.23715  1.000 13.35961 ? 134 PHE   A CG  1 
ATOM   1039 C  CD1 . PHE   A 1 134 ? -3.81153  -19.00850 -1.41445  1.000 12.47199 ? 134 PHE   A CD1 1 
ATOM   1040 C  CD2 . PHE   A 1 134 ? -2.60697  -20.99507 -1.94127  1.000 14.03090 ? 134 PHE   A CD2 1 
ATOM   1041 C  CE1 . PHE   A 1 134 ? -3.00440  -18.81721 -0.28538  1.000 12.33045 ? 134 PHE   A CE1 1 
ATOM   1042 C  CE2 . PHE   A 1 134 ? -1.79824  -20.82797 -0.80333  1.000 16.73315 ? 134 PHE   A CE2 1 
ATOM   1043 C  CZ  . PHE   A 1 134 ? -1.99343  -19.73681 0.01610   1.000 13.95466 ? 134 PHE   A CZ  1 
ATOM   1044 N  N   . THR   A 1 135 ? -7.70761  -21.29041 -4.73820  1.000 12.62611 ? 135 THR   A N   1 
ATOM   1045 C  CA  . THR   A 1 135 ? -8.78382  -20.91988 -5.64429  1.000 12.81889 ? 135 THR   A CA  1 
ATOM   1046 C  C   . THR   A 1 135 ? -10.02431 -20.62640 -4.83177  1.000 13.53184 ? 135 THR   A C   1 
ATOM   1047 O  O   . THR   A 1 135 ? -10.08370 -20.89291 -3.63191  1.000 10.17274 ? 135 THR   A O   1 
ATOM   1048 C  CB  . THR   A 1 135 ? -9.07026  -22.05137 -6.64600  1.000 12.95069 ? 135 THR   A CB  1 
ATOM   1049 O  OG1 . THR   A 1 135 ? -9.57793  -23.20266 -5.94286  1.000 14.03648 ? 135 THR   A OG1 1 
ATOM   1050 C  CG2 . THR   A 1 135 ? -7.79971  -22.44270 -7.37611  1.000 13.55772 ? 135 THR   A CG2 1 
ATOM   1051 N  N   . ILE   A 1 136 ? -11.02448 -20.08779 -5.50398  1.000 11.23556 ? 136 ILE   A N   1 
ATOM   1052 C  CA  . ILE   A 1 136 ? -12.33508 -19.94132 -4.88980  1.000 12.84133 ? 136 ILE   A CA  1 
ATOM   1053 C  C   . ILE   A 1 136 ? -13.36687 -20.51414 -5.83688  1.000 11.69048 ? 136 ILE   A C   1 
ATOM   1054 O  O   . ILE   A 1 136 ? -13.20304 -20.50537 -7.05927  1.000 12.72949 ? 136 ILE   A O   1 
ATOM   1055 C  CB  . ILE   A 1 136 ? -12.68172 -18.47886 -4.50065  1.000 15.40166 ? 136 ILE   A CB  1 
ATOM   1056 C  CG1 . ILE   A 1 136 ? -12.96925 -17.61447 -5.73676  1.000 15.63534 ? 136 ILE   A CG1 1 
ATOM   1057 C  CG2 . ILE   A 1 136 ? -11.61869 -17.89227 -3.53691  1.000 13.00394 ? 136 ILE   A CG2 1 
ATOM   1058 C  CD1 . ILE   A 1 136 ? -13.69060 -16.26609 -5.44398  1.000 14.75733 ? 136 ILE   A CD1 1 
ATOM   1059 N  N   . LYS   A 1 137 ? -14.41516 -21.08014 -5.25234  1.000 14.92459 ? 137 LYS   A N   1 
ATOM   1060 C  CA  . LYS   A 1 137 ? -15.50025 -21.66298 -6.02362  1.000 17.65040 ? 137 LYS   A CA  1 
ATOM   1061 C  C   . LYS   A 1 137 ? -16.57135 -20.58106 -6.10685  1.000 13.81996 ? 137 LYS   A C   1 
ATOM   1062 O  O   . LYS   A 1 137 ? -17.49586 -20.50417 -5.30317  1.000 17.52462 ? 137 LYS   A O   1 
ATOM   1063 C  CB  . LYS   A 1 137 ? -15.99144 -22.94858 -5.37052  1.000 16.89856 ? 137 LYS   A CB  1 
ATOM   1064 C  CG  . LYS   A 1 137 ? -14.90705 -24.02132 -5.21753  1.000 17.79246 ? 137 LYS   A CG  1 
ATOM   1065 C  CD  . LYS   A 1 137 ? -15.49478 -25.30049 -4.64317  1.000 21.83612 ? 137 LYS   A CD  1 
ATOM   1066 C  CE  . LYS   A 1 137 ? -14.48455 -26.43762 -4.66682  1.000 29.31270 ? 137 LYS   A CE  1 
ATOM   1067 N  NZ  . LYS   A 1 137 ? -14.66034 -27.26173 -5.89657  1.000 33.19478 ? 137 LYS   A NZ  1 
ATOM   1068 N  N   . GLY   A 1 138 ? -16.39479 -19.68356 -7.07354  1.000 14.18475 ? 138 GLY   A N   1 
ATOM   1069 C  CA  . GLY   A 1 138 ? -17.26257 -18.54280 -7.22143  1.000 14.30320 ? 138 GLY   A CA  1 
ATOM   1070 C  C   . GLY   A 1 138 ? -18.34267 -18.77964 -8.25923  1.000 15.99018 ? 138 GLY   A C   1 
ATOM   1071 O  O   . GLY   A 1 138 ? -18.58741 -19.89490 -8.72809  1.000 15.97987 ? 138 GLY   A O   1 
ATOM   1072 N  N   . SER   A 1 139 ? -18.99487 -17.68463 -8.62171  1.000 12.97200 ? 139 SER   A N   1 
ATOM   1073 C  CA  . SER   A 1 139 ? -19.93708 -17.67193 -9.72764  1.000 14.54905 ? 139 SER   A CA  1 
ATOM   1074 C  C   . SER   A 1 139 ? -19.66531 -16.37202 -10.46901 1.000 16.31350 ? 139 SER   A C   1 
ATOM   1075 O  O   . SER   A 1 139 ? -19.98543 -15.28726 -9.97310  1.000 13.75964 ? 139 SER   A O   1 
ATOM   1076 C  CB  . SER   A 1 139 ? -21.38314 -17.76591 -9.24368  1.000 16.98756 ? 139 SER   A CB  1 
ATOM   1077 O  OG  . SER   A 1 139 ? -22.27406 -17.52604 -10.30347 1.000 18.02472 ? 139 SER   A OG  1 
ATOM   1078 N  N   . PHE   A 1 140 ? -19.04188 -16.48730 -11.63616 1.000 16.51393 ? 140 PHE   A N   1 
ATOM   1079 C  CA  . PHE   A 1 140 ? -18.48533 -15.36020 -12.37092 1.000 17.80305 ? 140 PHE   A CA  1 
ATOM   1080 C  C   . PHE   A 1 140 ? -18.65494 -15.65307 -13.85183 1.000 22.56980 ? 140 PHE   A C   1 
ATOM   1081 O  O   . PHE   A 1 140 ? -18.34497 -16.76209 -14.29734 1.000 23.33752 ? 140 PHE   A O   1 
ATOM   1082 C  CB  . PHE   A 1 140 ? -16.98816 -15.16375 -12.05906 1.000 15.62904 ? 140 PHE   A CB  1 
ATOM   1083 C  CG  . PHE   A 1 140 ? -16.67751 -14.60370 -10.69342 1.000 14.33076 ? 140 PHE   A CG  1 
ATOM   1084 C  CD1 . PHE   A 1 140 ? -17.15664 -13.36093 -10.29467 1.000 16.59905 ? 140 PHE   A CD1 1 
ATOM   1085 C  CD2 . PHE   A 1 140 ? -15.89664 -15.32053 -9.81309  1.000 15.00125 ? 140 PHE   A CD2 1 
ATOM   1086 C  CE1 . PHE   A 1 140 ? -16.83729 -12.85027 -9.04400  1.000 14.95528 ? 140 PHE   A CE1 1 
ATOM   1087 C  CE2 . PHE   A 1 140 ? -15.56328 -14.81025 -8.54224  1.000 16.02761 ? 140 PHE   A CE2 1 
ATOM   1088 C  CZ  . PHE   A 1 140 ? -16.02471 -13.57094 -8.16677  1.000 15.56542 ? 140 PHE   A CZ  1 
ATOM   1089 N  N   . LEU   A 1 141 ? -19.14435 -14.67713 -14.61275 1.000 20.09765 ? 141 LEU   A N   1 
ATOM   1090 C  CA  . LEU   A 1 141 ? -19.18355 -14.77573 -16.06639 1.000 22.09952 ? 141 LEU   A CA  1 
ATOM   1091 C  C   . LEU   A 1 141 ? -18.20666 -13.77163 -16.67082 1.000 23.26718 ? 141 LEU   A C   1 
ATOM   1092 O  O   . LEU   A 1 141 ? -17.54682 -13.01326 -15.95970 1.000 23.88662 ? 141 LEU   A O   1 
ATOM   1093 C  CB  . LEU   A 1 141 ? -20.60277 -14.55253 -16.58477 1.000 22.46515 ? 141 LEU   A CB  1 
ATOM   1094 C  CG  . LEU   A 1 141 ? -21.66292 -15.44419 -15.94284 1.000 27.55654 ? 141 LEU   A CG  1 
ATOM   1095 C  CD1 . LEU   A 1 141 ? -23.03135 -14.87801 -16.21970 1.000 27.42703 ? 141 LEU   A CD1 1 
ATOM   1096 C  CD2 . LEU   A 1 141 ? -21.57731 -16.87296 -16.44946 1.000 26.41244 ? 141 LEU   A CD2 1 
ATOM   1097 N  N   . ASN   A 1 142 ? -18.11443 -13.76994 -18.00347 1.000 26.92665 ? 142 ASN   A N   1 
ATOM   1098 C  CA  . ASN   A 1 142 ? -17.30363 -12.75766 -18.66670 1.000 26.56274 ? 142 ASN   A CA  1 
ATOM   1099 C  C   . ASN   A 1 142 ? -17.75393 -11.36408 -18.25502 1.000 24.94259 ? 142 ASN   A C   1 
ATOM   1100 O  O   . ASN   A 1 142 ? -18.95301 -11.06168 -18.20521 1.000 24.62304 ? 142 ASN   A O   1 
ATOM   1101 C  CB  . ASN   A 1 142 ? -17.37454 -12.88464 -20.18734 1.000 29.86652 ? 142 ASN   A CB  1 
ATOM   1102 C  CG  . ASN   A 1 142 ? -16.76255 -14.16751 -20.70324 1.000 36.28442 ? 142 ASN   A CG  1 
ATOM   1103 O  OD1 . ASN   A 1 142 ? -15.65829 -14.54884 -20.30818 1.000 40.00328 ? 142 ASN   A OD1 1 
ATOM   1104 N  ND2 . ASN   A 1 142 ? -17.45105 -14.81472 -21.64097 1.000 42.34563 ? 142 ASN   A ND2 1 
ATOM   1105 N  N   . GLY   A 1 143 ? -16.77640 -10.51046 -17.97336 1.000 23.41566 ? 143 GLY   A N   1 
ATOM   1106 C  CA  . GLY   A 1 143 ? -17.03660 -9.15717  -17.54072 1.000 24.32427 ? 143 GLY   A CA  1 
ATOM   1107 C  C   . GLY   A 1 143 ? -16.99276 -8.97497  -16.04920 1.000 21.22641 ? 143 GLY   A C   1 
ATOM   1108 O  O   . GLY   A 1 143 ? -17.13301 -7.84483  -15.57500 1.000 20.05592 ? 143 GLY   A O   1 
ATOM   1109 N  N   . SER   A 1 144 ? -16.81282 -10.05258 -15.29865 1.000 17.22599 ? 144 SER   A N   1 
ATOM   1110 C  CA  . SER   A 1 144 ? -16.81192 -9.96470  -13.85202 1.000 16.66868 ? 144 SER   A CA  1 
ATOM   1111 C  C   . SER   A 1 144 ? -15.45716 -9.57799  -13.28117 1.000 14.46752 ? 144 SER   A C   1 
ATOM   1112 O  O   . SER   A 1 144 ? -15.39108 -9.26854  -12.09183 1.000 14.20423 ? 144 SER   A O   1 
ATOM   1113 C  CB  . SER   A 1 144 ? -17.24412 -11.30659 -13.23489 1.000 16.97529 ? 144 SER   A CB  1 
ATOM   1114 O  OG  . SER   A 1 144 ? -16.35189 -12.34358 -13.61479 1.000 18.40849 ? 144 SER   A OG  1 
ATOM   1115 N  N   . CYS   A 1 145 ? -14.38480 -9.61076  -14.08389 1.000 16.89789 ? 145 CYS   A N   1 
ATOM   1116 C  CA  . CYS   A 1 145 ? -13.06978 -9.19970  -13.60580 1.000 17.52239 ? 145 CYS   A CA  1 
ATOM   1117 C  C   . CYS   A 1 145 ? -13.15671 -7.85386  -12.90693 1.000 13.83852 ? 145 CYS   A C   1 
ATOM   1118 O  O   . CYS   A 1 145 ? -13.84444 -6.94364  -13.37622 1.000 16.18728 ? 145 CYS   A O   1 
ATOM   1119 C  CB  . CYS   A 1 145 ? -12.06821 -9.08320  -14.76200 1.000 24.28390 ? 145 CYS   A CB  1 
ATOM   1120 S  SG  . CYS   A 1 145 ? -11.84053 -10.53769 -15.78262 1.000 34.58676 ? 145 CYS   A SG  1 
ATOM   1121 N  N   . GLY   A 1 146 ? -12.44257 -7.72977  -11.78278 1.000 12.69441 ? 146 GLY   A N   1 
ATOM   1122 C  CA  . GLY   A 1 146 ? -12.48821 -6.52481  -10.98154 1.000 14.28386 ? 146 GLY   A CA  1 
ATOM   1123 C  C   . GLY   A 1 146 ? -13.50126 -6.54405  -9.85590  1.000 13.82272 ? 146 GLY   A C   1 
ATOM   1124 O  O   . GLY   A 1 146 ? -13.44156 -5.66927  -8.97708  1.000 13.62471 ? 146 GLY   A O   1 
ATOM   1125 N  N   . SER   A 1 147 ? -14.44044 -7.49483  -9.86205  1.000 12.10671 ? 147 SER   A N   1 
ATOM   1126 C  CA  . SER   A 1 147 ? -15.32399 -7.67886  -8.71531  1.000 12.18238 ? 147 SER   A CA  1 
ATOM   1127 C  C   . SER   A 1 147 ? -14.48197 -8.01530  -7.49645  1.000 13.46513 ? 147 SER   A C   1 
ATOM   1128 O  O   . SER   A 1 147 ? -13.40876 -8.62714  -7.61118  1.000 11.06276 ? 147 SER   A O   1 
ATOM   1129 C  CB  . SER   A 1 147 ? -16.32977 -8.81106  -8.96711  1.000 14.28614 ? 147 SER   A CB  1 
ATOM   1130 O  OG  . SER   A 1 147 ? -17.05333 -8.62527  -10.17253 1.000 13.31888 ? 147 SER   A OG  1 
ATOM   1131 N  N   . VAL   A 1 148 ? -14.94038 -7.58851  -6.31792  1.000 11.81286 ? 148 VAL   A N   1 
ATOM   1132 C  CA  . VAL   A 1 148 ? -14.11308 -7.74665  -5.13400  1.000 11.78386 ? 148 VAL   A CA  1 
ATOM   1133 C  C   . VAL   A 1 148 ? -14.76816 -8.61465  -4.07195  1.000 10.52649 ? 148 VAL   A C   1 
ATOM   1134 O  O   . VAL   A 1 148 ? -15.99556 -8.77911  -4.01801  1.000 10.56477 ? 148 VAL   A O   1 
ATOM   1135 C  CB  . VAL   A 1 148 ? -13.71034 -6.38780  -4.52449  1.000 11.62350 ? 148 VAL   A CB  1 
ATOM   1136 C  CG1 . VAL   A 1 148 ? -12.88291 -5.57402  -5.55511  1.000 12.56504 ? 148 VAL   A CG1 1 
ATOM   1137 C  CG2 . VAL   A 1 148 ? -14.90053 -5.65430  -4.02809  1.000 13.77625 ? 148 VAL   A CG2 1 
ATOM   1138 N  N   . GLY   A 1 149 ? -13.90330 -9.20169  -3.24675  1.000 9.08585  ? 149 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 149 ? -14.29192 -9.91068  -2.03572  1.000 10.13320 ? 149 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 149 ? -13.92303 -9.12138  -0.78686  1.000 9.26845  ? 149 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 149 ? -12.93309 -8.37993  -0.76523  1.000 8.29164  ? 149 GLY   A O   1 
ATOM   1142 N  N   . PHE   A 1 150 ? -14.70361 -9.30732  0.28181   1.000 8.76547  ? 150 PHE   A N   1 
ATOM   1143 C  CA  . PHE   A 1 150 ? -14.54573 -8.44909  1.44211   1.000 10.20975 ? 150 PHE   A CA  1 
ATOM   1144 C  C   . PHE   A 1 150 ? -15.22347 -9.06380  2.66075   1.000 10.60996 ? 150 PHE   A C   1 
ATOM   1145 O  O   . PHE   A 1 150 ? -16.09857 -9.92561  2.54536   1.000 10.08701 ? 150 PHE   A O   1 
ATOM   1146 C  CB  . PHE   A 1 150 ? -15.14702 -7.06010  1.19071   1.000 10.85680 ? 150 PHE   A CB  1 
ATOM   1147 C  CG  . PHE   A 1 150 ? -16.61518 -7.09151  0.93041   1.000 12.47882 ? 150 PHE   A CG  1 
ATOM   1148 C  CD1 . PHE   A 1 150 ? -17.11439 -7.39989  -0.33928  1.000 13.73167 ? 150 PHE   A CD1 1 
ATOM   1149 C  CD2 . PHE   A 1 150 ? -17.50434 -6.86442  1.96177   1.000 12.93776 ? 150 PHE   A CD2 1 
ATOM   1150 C  CE1 . PHE   A 1 150 ? -18.49002 -7.46375  -0.57710  1.000 14.78252 ? 150 PHE   A CE1 1 
ATOM   1151 C  CE2 . PHE   A 1 150 ? -18.89822 -6.90809  1.73257   1.000 16.35290 ? 150 PHE   A CE2 1 
ATOM   1152 C  CZ  . PHE   A 1 150 ? -19.38638 -7.20157  0.46203   1.000 13.84213 ? 150 PHE   A CZ  1 
ATOM   1153 N  N   . ASN   A 1 151 ? -14.80200 -8.58684  3.83315   1.000 10.19443 ? 151 ASN   A N   1 
ATOM   1154 C  CA  . ASN   A 1 151 ? -15.48582 -8.79578  5.10131   1.000 12.92768 ? 151 ASN   A CA  1 
ATOM   1155 C  C   . ASN   A 1 151 ? -15.77619 -7.43347  5.71107   1.000 12.15562 ? 151 ASN   A C   1 
ATOM   1156 O  O   . ASN   A 1 151 ? -15.11675 -6.45257  5.40348   1.000 10.82846 ? 151 ASN   A O   1 
ATOM   1157 C  CB  . ASN   A 1 151 ? -14.64010 -9.60919  6.06924   1.000 12.59456 ? 151 ASN   A CB  1 
ATOM   1158 C  CG  . ASN   A 1 151 ? -14.57248 -11.06276 5.69265   1.000 14.59371 ? 151 ASN   A CG  1 
ATOM   1159 O  OD1 . ASN   A 1 151 ? -15.50932 -11.83317 5.93188   1.000 15.59516 ? 151 ASN   A OD1 1 
ATOM   1160 N  ND2 . ASN   A 1 151 ? -13.49213 -11.43967 5.03512   1.000 12.71977 ? 151 ASN   A ND2 1 
ATOM   1161 N  N   . ILE   A 1 152 ? -16.74283 -7.36115  6.61963   1.000 12.87903 ? 152 ILE   A N   1 
ATOM   1162 C  CA  . ILE   A 1 152 ? -17.03637 -6.10069  7.28869   1.000 14.13974 ? 152 ILE   A CA  1 
ATOM   1163 C  C   . ILE   A 1 152 ? -16.94448 -6.33570  8.78228   1.000 21.71692 ? 152 ILE   A C   1 
ATOM   1164 O  O   . ILE   A 1 152 ? -17.52993 -7.29291  9.29614   1.000 19.39405 ? 152 ILE   A O   1 
ATOM   1165 C  CB  . ILE   A 1 152 ? -18.41648 -5.53356  6.90411   1.000 16.46261 ? 152 ILE   A CB  1 
ATOM   1166 C  CG1 . ILE   A 1 152 ? -18.47850 -5.28054  5.39698   1.000 16.57950 ? 152 ILE   A CG1 1 
ATOM   1167 C  CG2 . ILE   A 1 152 ? -18.64275 -4.20759  7.60816   1.000 20.86989 ? 152 ILE   A CG2 1 
ATOM   1168 C  CD1 . ILE   A 1 152 ? -19.87550 -4.82055  4.91779   1.000 22.86192 ? 152 ILE   A CD1 1 
ATOM   1169 N  N   . ASP   A 1 153 ? -16.21150 -5.45817  9.46493   1.000 23.69132 ? 153 ASP   A N   1 
ATOM   1170 C  CA  . ASP   A 1 153 ? -16.01493 -5.47688  10.91139  1.000 29.91169 ? 153 ASP   A CA  1 
ATOM   1171 C  C   . ASP   A 1 153 ? -16.50288 -4.13545  11.43449  1.000 31.82327 ? 153 ASP   A C   1 
ATOM   1172 O  O   . ASP   A 1 153 ? -15.90121 -3.09485  11.14114  1.000 32.25715 ? 153 ASP   A O   1 
ATOM   1173 C  CB  . ASP   A 1 153 ? -14.54752 -5.69919  11.27263  1.000 31.87960 ? 153 ASP   A CB  1 
ATOM   1174 C  CG  . ASP   A 1 153 ? -14.35999 -6.76424  12.33377  1.000 42.37269 ? 153 ASP   A CG  1 
ATOM   1175 O  OD1 . ASP   A 1 153 ? -15.19344 -6.82607  13.26795  1.000 41.17573 ? 153 ASP   A OD1 1 
ATOM   1176 O  OD2 . ASP   A 1 153 ? -13.37115 -7.53203  12.23911  1.000 44.82606 ? 153 ASP   A OD2 1 
ATOM   1177 N  N   . TYR   A 1 154 ? -17.57312 -4.17198  12.22527  1.000 34.40275 ? 154 TYR   A N   1 
ATOM   1178 C  CA  . TYR   A 1 154 ? -18.37029 -2.99667  12.54442  1.000 39.93225 ? 154 TYR   A CA  1 
ATOM   1179 C  C   . TYR   A 1 154 ? -18.62552 -2.15796  11.29700  1.000 39.67534 ? 154 TYR   A C   1 
ATOM   1180 O  O   . TYR   A 1 154 ? -19.46339 -2.51625  10.46507  1.000 40.82684 ? 154 TYR   A O   1 
ATOM   1181 C  CB  . TYR   A 1 154 ? -17.71458 -2.14827  13.63388  1.000 43.22048 ? 154 TYR   A CB  1 
ATOM   1182 C  CG  . TYR   A 1 154 ? -18.69477 -1.14386  14.20998  1.000 50.67147 ? 154 TYR   A CG  1 
ATOM   1183 C  CD1 . TYR   A 1 154 ? -20.03994 -1.47926  14.36131  1.000 50.42633 ? 154 TYR   A CD1 1 
ATOM   1184 C  CD2 . TYR   A 1 154 ? -18.28860 0.13088   14.59468  1.000 48.82453 ? 154 TYR   A CD2 1 
ATOM   1185 C  CE1 . TYR   A 1 154 ? -20.95301 -0.57937  14.87816  1.000 53.98380 ? 154 TYR   A CE1 1 
ATOM   1186 C  CE2 . TYR   A 1 154 ? -19.19851 1.04198   15.11758  1.000 53.88613 ? 154 TYR   A CE2 1 
ATOM   1187 C  CZ  . TYR   A 1 154 ? -20.52836 0.67889   15.25643  1.000 55.82696 ? 154 TYR   A CZ  1 
ATOM   1188 O  OH  . TYR   A 1 154 ? -21.43737 1.57562   15.77265  1.000 54.62989 ? 154 TYR   A OH  1 
ATOM   1189 N  N   . ASP   A 1 155 ? -17.91130 -1.04654  11.14692  1.000 37.52073 ? 155 ASP   A N   1 
ATOM   1190 C  CA  . ASP   A 1 155 ? -18.16259 -0.12018  10.05070  1.000 36.37588 ? 155 ASP   A CA  1 
ATOM   1191 C  C   . ASP   A 1 155 ? -17.08088 -0.14998  8.97883   1.000 33.27488 ? 155 ASP   A C   1 
ATOM   1192 O  O   . ASP   A 1 155 ? -17.14666 0.63777   8.02701   1.000 28.60386 ? 155 ASP   A O   1 
ATOM   1193 C  CB  . ASP   A 1 155 ? -18.28768 1.30143   10.60048  1.000 39.93317 ? 155 ASP   A CB  1 
ATOM   1194 C  CG  . ASP   A 1 155 ? -16.97249 1.81870   11.13930  1.000 41.82934 ? 155 ASP   A CG  1 
ATOM   1195 O  OD1 . ASP   A 1 155 ? -16.31897 1.07338   11.90657  1.000 43.30441 ? 155 ASP   A OD1 1 
ATOM   1196 O  OD2 . ASP   A 1 155 ? -16.59100 2.96042   10.79457  1.000 47.57700 ? 155 ASP   A OD2 1 
ATOM   1197 N  N   . CYS   A 1 156 ? -16.09300 -1.03092  9.10269   1.000 23.47104 ? 156 CYS   A N   1 
ATOM   1198 C  CA  . CYS   A 1 156 ? -14.88956 -0.98022  8.28439   1.000 23.46309 ? 156 CYS   A CA  1 
ATOM   1199 C  C   . CYS   A 1 156 ? -14.89491 -2.15153  7.31580   1.000 18.24892 ? 156 CYS   A C   1 
ATOM   1200 O  O   . CYS   A 1 156 ? -15.09600 -3.30148  7.73098   1.000 15.29772 ? 156 CYS   A O   1 
ATOM   1201 C  CB  . CYS   A 1 156 ? -13.64967 -1.02568  9.17082   1.000 22.75676 ? 156 CYS   A CB  1 
ATOM   1202 S  SG  . CYS   A 1 156 ? -12.06721 -1.22470  8.31061   1.000 22.26435 ? 156 CYS   A SG  1 
ATOM   1203 N  N   . VAL   A 1 157 ? -14.67165 -1.85965  6.03268   1.000 15.26908 ? 157 VAL   A N   1 
ATOM   1204 C  CA  . VAL   A 1 157 ? -14.64414 -2.89053  4.99879   1.000 11.50567 ? 157 VAL   A CA  1 
ATOM   1205 C  C   . VAL   A 1 157 ? -13.21015 -3.35505  4.82632   1.000 14.00670 ? 157 VAL   A C   1 
ATOM   1206 O  O   . VAL   A 1 157 ? -12.34678 -2.56280  4.45024   1.000 13.19137 ? 157 VAL   A O   1 
ATOM   1207 C  CB  . VAL   A 1 157 ? -15.18720 -2.37080  3.66125   1.000 12.58291 ? 157 VAL   A CB  1 
ATOM   1208 C  CG1 . VAL   A 1 157 ? -15.20361 -3.49203  2.62959   1.000 12.80069 ? 157 VAL   A CG1 1 
ATOM   1209 C  CG2 . VAL   A 1 157 ? -16.58014 -1.73843  3.84842   1.000 14.26814 ? 157 VAL   A CG2 1 
ATOM   1210 N  N   . SER   A 1 158 ? -12.95983 -4.63543  5.06802   1.000 11.50197 ? 158 SER   A N   1 
ATOM   1211 C  CA  . SER   A 1 158 ? -11.63670 -5.20300  4.81936   1.000 11.69392 ? 158 SER   A CA  1 
ATOM   1212 C  C   . SER   A 1 158 ? -11.69961 -5.87310  3.46045   1.000 9.79271  ? 158 SER   A C   1 
ATOM   1213 O  O   . SER   A 1 158 ? -12.29064 -6.94191  3.31511   1.000 9.30234  ? 158 SER   A O   1 
ATOM   1214 C  CB  . SER   A 1 158 ? -11.24421 -6.18651  5.91087   1.000 13.71842 ? 158 SER   A CB  1 
ATOM   1215 O  OG  . SER   A 1 158 ? -10.96545 -5.48558  7.09737   1.000 15.38882 ? 158 SER   A OG  1 
ATOM   1216 N  N   . PHE   A 1 159 ? -11.13653 -5.22899  2.44343   1.000 11.32359 ? 159 PHE   A N   1 
ATOM   1217 C  CA  . PHE   A 1 159 ? -11.11769 -5.82431  1.11626   1.000 9.69372  ? 159 PHE   A CA  1 
ATOM   1218 C  C   . PHE   A 1 159 ? -10.02373 -6.88201  1.06849   1.000 10.49228 ? 159 PHE   A C   1 
ATOM   1219 O  O   . PHE   A 1 159 ? -8.90594  -6.62318  1.50920   1.000 11.28339 ? 159 PHE   A O   1 
ATOM   1220 C  CB  . PHE   A 1 159 ? -10.84849 -4.75868  0.04757   1.000 11.46657 ? 159 PHE   A CB  1 
ATOM   1221 C  CG  . PHE   A 1 159 ? -11.94681 -3.75020  -0.10548  1.000 11.78896 ? 159 PHE   A CG  1 
ATOM   1222 C  CD1 . PHE   A 1 159 ? -13.10720 -4.08704  -0.79879  1.000 10.74736 ? 159 PHE   A CD1 1 
ATOM   1223 C  CD2 . PHE   A 1 159 ? -11.83189 -2.47541  0.45234   1.000 12.56812 ? 159 PHE   A CD2 1 
ATOM   1224 C  CE1 . PHE   A 1 159 ? -14.11267 -3.17373  -0.95143  1.000 12.09140 ? 159 PHE   A CE1 1 
ATOM   1225 C  CE2 . PHE   A 1 159 ? -12.85546 -1.54317  0.30381   1.000 12.93702 ? 159 PHE   A CE2 1 
ATOM   1226 C  CZ  . PHE   A 1 159 ? -14.00174 -1.91208  -0.39377  1.000 12.85867 ? 159 PHE   A CZ  1 
ATOM   1227 N  N   . CYS   A 1 160 ? -10.34095 -8.06540  0.54848   1.000 9.56885  ? 160 CYS   A N   1 
ATOM   1228 C  CA  . CYS   A 1 160 ? -9.37573  -9.15319  0.50347   1.000 11.11804 ? 160 CYS   A CA  1 
ATOM   1229 C  C   . CYS   A 1 160 ? -9.19717  -9.82574  -0.83577  1.000 10.38242 ? 160 CYS   A C   1 
ATOM   1230 O  O   . CYS   A 1 160 ? -8.22446  -10.57479 -0.97601  1.000 12.24215 ? 160 CYS   A O   1 
ATOM   1231 C  CB  . CYS   A 1 160 ? -9.71573  -10.19994 1.56883   1.000 9.49341  ? 160 CYS   A CB  1 
ATOM   1232 S  SG  . CYS   A 1 160 ? -11.31244 -10.94553 1.32439   1.000 10.39427 ? 160 CYS   A SG  1 
ATOM   1233 N  N   . TYR   A 1 161 ? -10.00338 -9.51657  -1.84694  1.000 6.71707  ? 161 TYR   A N   1 
ATOM   1234 C  CA  . TYR   A 1 161 ? -9.95090  -10.26786 -3.09549  1.000 8.95753  ? 161 TYR   A CA  1 
ATOM   1235 C  C   . TYR   A 1 161 ? -10.37576 -9.38451  -4.25719  1.000 10.10197 ? 161 TYR   A C   1 
ATOM   1236 O  O   . TYR   A 1 161 ? -11.33375 -8.62113  -4.14126  1.000 11.07943 ? 161 TYR   A O   1 
ATOM   1237 C  CB  . TYR   A 1 161 ? -10.86169 -11.49992 -3.03918  1.000 10.35417 ? 161 TYR   A CB  1 
ATOM   1238 C  CG  . TYR   A 1 161 ? -10.90963 -12.33486 -4.31926  1.000 10.24380 ? 161 TYR   A CG  1 
ATOM   1239 C  CD1 . TYR   A 1 161 ? -9.90338  -13.26117 -4.58278  1.000 10.72284 ? 161 TYR   A CD1 1 
ATOM   1240 C  CD2 . TYR   A 1 161 ? -11.96430 -12.23405 -5.23743  1.000 9.69978  ? 161 TYR   A CD2 1 
ATOM   1241 C  CE1 . TYR   A 1 161 ? -9.93992  -14.04895 -5.72566  1.000 9.36664  ? 161 TYR   A CE1 1 
ATOM   1242 C  CE2 . TYR   A 1 161 ? -12.00309 -13.02482 -6.41469  1.000 10.36022 ? 161 TYR   A CE2 1 
ATOM   1243 C  CZ  . TYR   A 1 161 ? -10.97110 -13.93206 -6.63684  1.000 10.40782 ? 161 TYR   A CZ  1 
ATOM   1244 O  OH  . TYR   A 1 161 ? -10.96065 -14.72118 -7.76267  1.000 11.35258 ? 161 TYR   A OH  1 
ATOM   1245 N  N   . MET   A 1 162 ? -9.62889  -9.45108  -5.35537  1.000 9.23567  ? 162 MET   A N   1 
ATOM   1246 C  CA  . MET   A 1 162 ? -10.07157 -8.90068  -6.62875  1.000 9.72491  ? 162 MET   A CA  1 
ATOM   1247 C  C   . MET   A 1 162 ? -10.04689 -10.00574 -7.66541  1.000 10.56757 ? 162 MET   A C   1 
ATOM   1248 O  O   . MET   A 1 162 ? -9.02530  -10.67423 -7.82414  1.000 8.01315  ? 162 MET   A O   1 
ATOM   1249 C  CB  . MET   A 1 162 ? -9.20299  -7.73438  -7.10725  1.000 11.24335 ? 162 MET   A CB  1 
ATOM   1250 C  CG  . MET   A 1 162 ? -9.81633  -7.09090  -8.34677  1.000 12.46848 ? 162 MET   A CG  1 
ATOM   1251 S  SD  . MET   A 1 162 ? -9.05277  -5.52079  -8.78897  1.000 16.40266 ? 162 MET   A SD  1 
ATOM   1252 C  CE  . MET   A 1 162 ? -10.16256 -4.34264  -8.00018  1.000 16.75292 ? 162 MET   A CE  1 
ATOM   1253 N  N   . HIS   A 1 163 ? -11.17957 -10.21557 -8.33525  1.000 9.71523  ? 163 HIS   A N   1 
ATOM   1254 C  CA  . HIS   A 1 163 ? -11.30557 -11.30379 -9.30237  1.000 8.79404  ? 163 HIS   A CA  1 
ATOM   1255 C  C   . HIS   A 1 163 ? -10.54737 -11.02467 -10.59936 1.000 10.17091 ? 163 HIS   A C   1 
ATOM   1256 O  O   . HIS   A 1 163 ? -10.68302 -9.95117  -11.18362 1.000 11.57181 ? 163 HIS   A O   1 
ATOM   1257 C  CB  . HIS   A 1 163 ? -12.77190 -11.53639 -9.65575  1.000 14.48451 ? 163 HIS   A CB  1 
ATOM   1258 C  CG  . HIS   A 1 163 ? -12.95653 -12.74497 -10.51120 1.000 12.42850 ? 163 HIS   A CG  1 
ATOM   1259 N  ND1 . HIS   A 1 163 ? -12.44477 -13.96779 -10.14608 1.000 12.88012 ? 163 HIS   A ND1 1 
ATOM   1260 C  CD2 . HIS   A 1 163 ? -13.51503 -12.91959 -11.73188 1.000 13.90381 ? 163 HIS   A CD2 1 
ATOM   1261 C  CE1 . HIS   A 1 163 ? -12.69740 -14.85293 -11.08777 1.000 12.62523 ? 163 HIS   A CE1 1 
ATOM   1262 N  NE2 . HIS   A 1 163 ? -13.34923 -14.24562 -12.06193 1.000 14.82412 ? 163 HIS   A NE2 1 
ATOM   1263 N  N   . HIS   A 1 164 ? -9.79670  -12.03074 -11.08113 1.000 13.47686 ? 164 HIS   A N   1 
ATOM   1264 C  CA  . HIS   A 1 164 ? -9.05200  -11.92132 -12.33938 1.000 13.32997 ? 164 HIS   A CA  1 
ATOM   1265 C  C   . HIS   A 1 164 ? -9.44939  -12.94038 -13.39821 1.000 15.35981 ? 164 HIS   A C   1 
ATOM   1266 O  O   . HIS   A 1 164 ? -9.54220  -12.57837 -14.57549 1.000 18.92522 ? 164 HIS   A O   1 
ATOM   1267 C  CB  . HIS   A 1 164 ? -7.52593  -12.04052 -12.11126 1.000 11.29526 ? 164 HIS   A CB  1 
ATOM   1268 C  CG  . HIS   A 1 164 ? -6.88826  -10.79790 -11.56203 1.000 12.77515 ? 164 HIS   A CG  1 
ATOM   1269 N  ND1 . HIS   A 1 164 ? -7.19724  -10.27763 -10.32374 1.000 14.32736 ? 164 HIS   A ND1 1 
ATOM   1270 C  CD2 . HIS   A 1 164 ? -5.96311  -9.96407  -12.09788 1.000 10.60222 ? 164 HIS   A CD2 1 
ATOM   1271 C  CE1 . HIS   A 1 164 ? -6.47377  -9.18787  -10.11088 1.000 10.97439 ? 164 HIS   A CE1 1 
ATOM   1272 N  NE2 . HIS   A 1 164 ? -5.72426  -8.97311  -11.17747 1.000 14.30726 ? 164 HIS   A NE2 1 
ATOM   1273 N  N   . MET   A 1 165 ? -9.65730  -14.21147 -13.04917 1.000 14.27467 ? 165 MET   A N   1 
ATOM   1274 C  CA  . MET   A 1 165 ? -9.76996  -15.19712 -14.12130 1.000 19.87233 ? 165 MET   A CA  1 
ATOM   1275 C  C   . MET   A 1 165 ? -10.46662 -16.46134 -13.64935 1.000 14.90388 ? 165 MET   A C   1 
ATOM   1276 O  O   . MET   A 1 165 ? -10.57793 -16.73158 -12.45045 1.000 14.69896 ? 165 MET   A O   1 
ATOM   1277 C  CB  . MET   A 1 165 ? -8.39158  -15.57238 -14.64967 1.000 20.06205 ? 165 MET   A CB  1 
ATOM   1278 C  CG  . MET   A 1 165 ? -7.38719  -15.58531 -13.53307 1.000 23.56311 ? 165 MET   A CG  1 
ATOM   1279 S  SD  . MET   A 1 165 ? -5.79813  -16.10410 -14.15966 1.000 32.12821 ? 165 MET   A SD  1 
ATOM   1280 C  CE  . MET   A 1 165 ? -5.77768  -17.78396 -13.57833 1.000 24.48869 ? 165 MET   A CE  1 
ATOM   1281 N  N   . GLU   A 1 166 ? -10.90050 -17.25666 -14.62602 1.000 16.05420 ? 166 GLU   A N   1 
ATOM   1282 C  CA  . GLU   A 1 166 ? -11.46114 -18.56651 -14.34691 1.000 14.22765 ? 166 GLU   A CA  1 
ATOM   1283 C  C   . GLU   A 1 166 ? -10.48055 -19.61916 -14.84563 1.000 16.77107 ? 166 GLU   A C   1 
ATOM   1284 O  O   . GLU   A 1 166 ? -9.91849  -19.48023 -15.93551 1.000 21.45368 ? 166 GLU   A O   1 
ATOM   1285 C  CB  . GLU   A 1 166 ? -12.83688 -18.73665 -15.00981 1.000 18.58952 ? 166 GLU   A CB  1 
ATOM   1286 C  CG  . GLU   A 1 166 ? -13.34205 -20.16962 -14.98805 1.000 21.35244 ? 166 GLU   A CG  1 
ATOM   1287 C  CD  . GLU   A 1 166 ? -14.83727 -20.27864 -15.28236 1.000 26.07785 ? 166 GLU   A CD  1 
ATOM   1288 O  OE1 . GLU   A 1 166 ? -15.63280 -19.50689 -14.71316 1.000 23.13363 ? 166 GLU   A OE1 1 
ATOM   1289 O  OE2 . GLU   A 1 166 ? -15.21187 -21.15428 -16.08097 1.000 26.22235 ? 166 GLU   A OE2 1 
ATOM   1290 N  N   . LEU   A 1 167 ? -10.24565 -20.63809 -14.03052 1.000 17.34914 ? 167 LEU   A N   1 
ATOM   1291 C  CA  . LEU   A 1 167 ? -9.36258  -21.75145 -14.36232 1.000 19.16254 ? 167 LEU   A CA  1 
ATOM   1292 C  C   . LEU   A 1 167 ? -10.14505 -22.83227 -15.09204 1.000 21.90121 ? 167 LEU   A C   1 
ATOM   1293 O  O   . LEU   A 1 167 ? -11.37870 -22.80758 -15.12577 1.000 21.94924 ? 167 LEU   A O   1 
ATOM   1294 C  CB  . LEU   A 1 167 ? -8.72433  -22.28147 -13.07717 1.000 20.04514 ? 167 LEU   A CB  1 
ATOM   1295 C  CG  . LEU   A 1 167 ? -7.73085  -21.32602 -12.42195 1.000 17.18070 ? 167 LEU   A CG  1 
ATOM   1296 C  CD1 . LEU   A 1 167 ? -7.41732  -21.79981 -11.01986 1.000 16.16061 ? 167 LEU   A CD1 1 
ATOM   1297 C  CD2 . LEU   A 1 167 ? -6.46403  -21.30508 -13.24705 1.000 21.17948 ? 167 LEU   A CD2 1 
ATOM   1298 N  N   . PRO   A 1 168 ? -9.45950  -23.81979 -15.68459 1.000 22.09243 ? 168 PRO   A N   1 
ATOM   1299 C  CA  . PRO   A 1 168 ? -10.17248 -24.77976 -16.55088 1.000 22.37766 ? 168 PRO   A CA  1 
ATOM   1300 C  C   . PRO   A 1 168 ? -11.22168 -25.63222 -15.83970 1.000 25.22548 ? 168 PRO   A C   1 
ATOM   1301 O  O   . PRO   A 1 168 ? -12.17131 -26.07909 -16.49428 1.000 29.08432 ? 168 PRO   A O   1 
ATOM   1302 C  CB  . PRO   A 1 168 ? -9.03533  -25.63792 -17.12373 1.000 23.33890 ? 168 PRO   A CB  1 
ATOM   1303 C  CG  . PRO   A 1 168 ? -7.83239  -24.77415 -17.05549 1.000 25.98731 ? 168 PRO   A CG  1 
ATOM   1304 C  CD  . PRO   A 1 168 ? -7.99271  -23.96486 -15.79920 1.000 21.20971 ? 168 PRO   A CD  1 
ATOM   1305 N  N   . THR   A 1 169 ? -11.09044 -25.88805 -14.53993 1.000 21.56971 ? 169 THR   A N   1 
ATOM   1306 C  CA  . THR   A 1 169 ? -12.10681 -26.64649 -13.80846 1.000 22.28396 ? 169 THR   A CA  1 
ATOM   1307 C  C   . THR   A 1 169 ? -13.30668 -25.79437 -13.38639 1.000 22.88125 ? 169 THR   A C   1 
ATOM   1308 O  O   . THR   A 1 169 ? -14.15650 -26.28217 -12.62926 1.000 25.05913 ? 169 THR   A O   1 
ATOM   1309 C  CB  . THR   A 1 169 ? -11.50168 -27.29159 -12.55787 1.000 25.22061 ? 169 THR   A CB  1 
ATOM   1310 O  OG1 . THR   A 1 169 ? -10.80947 -26.29067 -11.79984 1.000 25.27665 ? 169 THR   A OG1 1 
ATOM   1311 C  CG2 . THR   A 1 169 ? -10.53665 -28.39920 -12.93995 1.000 23.76518 ? 169 THR   A CG2 1 
ATOM   1312 N  N   . GLY   A 1 170 ? -13.38980 -24.54774 -13.84075 1.000 20.17601 ? 170 GLY   A N   1 
ATOM   1313 C  CA  . GLY   A 1 170 ? -14.49975 -23.69561 -13.47159 1.000 20.64036 ? 170 GLY   A CA  1 
ATOM   1314 C  C   . GLY   A 1 170 ? -14.36650 -22.99706 -12.13485 1.000 21.16880 ? 170 GLY   A C   1 
ATOM   1315 O  O   . GLY   A 1 170 ? -15.33521 -22.36346 -11.69483 1.000 21.80831 ? 170 GLY   A O   1 
ATOM   1316 N  N   . VAL   A 1 171 ? -13.21257 -23.07720 -11.47971 1.000 19.13793 ? 171 VAL   A N   1 
ATOM   1317 C  CA  . VAL   A 1 171 ? -12.96189 -22.33527 -10.25333 1.000 15.90608 ? 171 VAL   A CA  1 
ATOM   1318 C  C   . VAL   A 1 171 ? -12.19828 -21.06214 -10.59709 1.000 15.16401 ? 171 VAL   A C   1 
ATOM   1319 O  O   . VAL   A 1 171 ? -11.77618 -20.84946 -11.73226 1.000 16.01433 ? 171 VAL   A O   1 
ATOM   1320 C  CB  . VAL   A 1 171 ? -12.19374 -23.17820 -9.18779  1.000 16.17019 ? 171 VAL   A CB  1 
ATOM   1321 C  CG1 . VAL   A 1 171 ? -12.95939 -24.46154 -8.83793  1.000 17.00215 ? 171 VAL   A CG1 1 
ATOM   1322 C  CG2 . VAL   A 1 171 ? -10.78175 -23.49769 -9.65710  1.000 17.98853 ? 171 VAL   A CG2 1 
ATOM   1323 N  N   . HIS   A 1 172 ? -11.98729 -20.21042 -9.59972  1.000 12.17007 ? 172 HIS   A N   1 
ATOM   1324 C  CA  . HIS   A 1 172 ? -11.61545 -18.82946 -9.86707  1.000 11.81949 ? 172 HIS   A CA  1 
ATOM   1325 C  C   . HIS   A 1 172 ? -10.33384 -18.44159 -9.15088  1.000 13.40969 ? 172 HIS   A C   1 
ATOM   1326 O  O   . HIS   A 1 172 ? -10.00818 -18.94966 -8.07460  1.000 12.18018 ? 172 HIS   A O   1 
ATOM   1327 C  CB  . HIS   A 1 172 ? -12.78969 -17.92393 -9.50384  1.000 14.21017 ? 172 HIS   A CB  1 
ATOM   1328 C  CG  . HIS   A 1 172 ? -14.01675 -18.26145 -10.28840 1.000 15.19512 ? 172 HIS   A CG  1 
ATOM   1329 N  ND1 . HIS   A 1 172 ? -15.08972 -18.93431 -9.74504  1.000 13.93848 ? 172 HIS   A ND1 1 
ATOM   1330 C  CD2 . HIS   A 1 172 ? -14.29452 -18.10874 -11.60686 1.000 15.54905 ? 172 HIS   A CD2 1 
ATOM   1331 C  CE1 . HIS   A 1 172 ? -16.00147 -19.13127 -10.68149 1.000 17.68321 ? 172 HIS   A CE1 1 
ATOM   1332 N  NE2 . HIS   A 1 172 ? -15.54021 -18.64876 -11.82317 1.000 15.39784 ? 172 HIS   A NE2 1 
ATOM   1333 N  N   . ALA   A 1 173 ? -9.58793  -17.55300 -9.78755  1.000 13.55769 ? 173 ALA   A N   1 
ATOM   1334 C  CA  . ALA   A 1 173 ? -8.34950  -17.07593 -9.20451  1.000 11.69395 ? 173 ALA   A CA  1 
ATOM   1335 C  C   . ALA   A 1 173 ? -8.28446  -15.55518 -9.24913  1.000 12.43603 ? 173 ALA   A C   1 
ATOM   1336 O  O   . ALA   A 1 173 ? -8.83450  -14.91385 -10.15339 1.000 9.88789  ? 173 ALA   A O   1 
ATOM   1337 C  CB  . ALA   A 1 173 ? -7.15565  -17.70232 -9.91881  1.000 13.14924 ? 173 ALA   A CB  1 
ATOM   1338 N  N   . GLY   A 1 174 ? -7.60891  -14.97498 -8.25875  1.000 8.32565  ? 174 GLY   A N   1 
ATOM   1339 C  CA  . GLY   A 1 174 ? -7.48464  -13.53595 -8.22509  1.000 9.87718  ? 174 GLY   A CA  1 
ATOM   1340 C  C   . GLY   A 1 174 ? -6.39344  -13.12354 -7.26230  1.000 11.94060 ? 174 GLY   A C   1 
ATOM   1341 O  O   . GLY   A 1 174 ? -5.59419  -13.94671 -6.81030  1.000 10.05216 ? 174 GLY   A O   1 
ATOM   1342 N  N   . THR   A 1 175 ? -6.40179  -11.83587 -6.92257  1.000 8.14501  ? 175 THR   A N   1 
ATOM   1343 C  CA  . THR   A 1 175 ? -5.32777  -11.23282 -6.15567  1.000 10.15381 ? 175 THR   A CA  1 
ATOM   1344 C  C   . THR   A 1 175 ? -5.89587  -10.62934 -4.88733  1.000 8.10236  ? 175 THR   A C   1 
ATOM   1345 O  O   . THR   A 1 175 ? -7.12455  -10.47571 -4.73960  1.000 9.98324  ? 175 THR   A O   1 
ATOM   1346 C  CB  . THR   A 1 175 ? -4.62472  -10.12293 -6.95646  1.000 10.29252 ? 175 THR   A CB  1 
ATOM   1347 O  OG1 . THR   A 1 175 ? -5.54990  -9.03632  -7.14822  1.000 9.88641  ? 175 THR   A OG1 1 
ATOM   1348 C  CG2 . THR   A 1 175 ? -4.12173  -10.64711 -8.28403  1.000 11.38134 ? 175 THR   A CG2 1 
ATOM   1349 N  N   . ASP   A 1 176 ? -5.00300  -10.28471 -3.96300  1.000 10.18658 ? 176 ASP   A N   1 
ATOM   1350 C  CA  . ASP   A 1 176 ? -5.37564  -9.32790  -2.93442  1.000 9.94443  ? 176 ASP   A CA  1 
ATOM   1351 C  C   . ASP   A 1 176 ? -5.41528  -7.92732  -3.56339  1.000 8.98794  ? 176 ASP   A C   1 
ATOM   1352 O  O   . ASP   A 1 176 ? -5.16273  -7.75809  -4.75588  1.000 9.32798  ? 176 ASP   A O   1 
ATOM   1353 C  CB  . ASP   A 1 176 ? -4.43356  -9.44064  -1.73057  1.000 11.35286 ? 176 ASP   A CB  1 
ATOM   1354 C  CG  . ASP   A 1 176 ? -2.98057  -9.11599  -2.03450  1.000 10.75368 ? 176 ASP   A CG  1 
ATOM   1355 O  OD1 . ASP   A 1 176 ? -2.66963  -8.33018  -2.95612  1.000 9.69871  ? 176 ASP   A OD1 1 
ATOM   1356 O  OD2 . ASP   A 1 176 ? -2.13704  -9.63951  -1.25931  1.000 12.11675 ? 176 ASP   A OD2 1 
ATOM   1357 N  N   . LEU   A 1 177 ? -5.76522  -6.91067  -2.76985  1.000 10.83200 ? 177 LEU   A N   1 
ATOM   1358 C  CA  . LEU   A 1 177 ? -5.92143  -5.57319  -3.33656  1.000 10.67819 ? 177 LEU   A CA  1 
ATOM   1359 C  C   . LEU   A 1 177 ? -4.59559  -4.83244  -3.45083  1.000 14.40602 ? 177 LEU   A C   1 
ATOM   1360 O  O   . LEU   A 1 177 ? -4.58196  -3.67727  -3.90118  1.000 15.70165 ? 177 LEU   A O   1 
ATOM   1361 C  CB  . LEU   A 1 177 ? -6.92458  -4.73876  -2.51017  1.000 11.12942 ? 177 LEU   A CB  1 
ATOM   1362 C  CG  . LEU   A 1 177 ? -8.42131  -4.81431  -2.92663  1.000 10.87460 ? 177 LEU   A CG  1 
ATOM   1363 C  CD1 . LEU   A 1 177 ? -8.66164  -4.14514  -4.28265  1.000 11.73770 ? 177 LEU   A CD1 1 
ATOM   1364 C  CD2 . LEU   A 1 177 ? -8.95133  -6.26983  -2.96839  1.000 13.92128 ? 177 LEU   A CD2 1 
ATOM   1365 N  N   . GLU   A 1 178 ? -3.48782  -5.46404  -3.05882  1.000 12.06685 ? 178 GLU   A N   1 
ATOM   1366 C  CA  . GLU   A 1 178 ? -2.16268  -4.99758  -3.44236  1.000 13.40863 ? 178 GLU   A CA  1 
ATOM   1367 C  C   . GLU   A 1 178 ? -1.72388  -5.57616  -4.77324  1.000 12.37339 ? 178 GLU   A C   1 
ATOM   1368 O  O   . GLU   A 1 178 ? -0.62486  -5.25477  -5.24100  1.000 12.56034 ? 178 GLU   A O   1 
ATOM   1369 C  CB  . GLU   A 1 178 ? -1.11176  -5.32793  -2.37501  1.000 14.91183 ? 178 GLU   A CB  1 
ATOM   1370 C  CG  . GLU   A 1 178 ? -1.58299  -5.12321  -0.96323  1.000 19.71917 ? 178 GLU   A CG  1 
ATOM   1371 C  CD  . GLU   A 1 178 ? -1.62955  -3.66982  -0.52723  1.000 22.89503 ? 178 GLU   A CD  1 
ATOM   1372 O  OE1 . GLU   A 1 178 ? -1.36703  -2.74913  -1.35052  1.000 22.01789 ? 178 GLU   A OE1 1 
ATOM   1373 O  OE2 . GLU   A 1 178 ? -1.98512  -3.45254  0.66946   1.000 22.73662 ? 178 GLU   A OE2 1 
ATOM   1374 N  N   . GLY   A 1 179 ? -2.53199  -6.43663  -5.37222  1.000 11.81699 ? 179 GLY   A N   1 
ATOM   1375 C  CA  . GLY   A 1 179 ? -2.23805  -6.98335  -6.67744  1.000 11.28170 ? 179 GLY   A CA  1 
ATOM   1376 C  C   . GLY   A 1 179 ? -1.42822  -8.26545  -6.65227  1.000 10.39605 ? 179 GLY   A C   1 
ATOM   1377 O  O   . GLY   A 1 179 ? -0.92649  -8.68906  -7.70029  1.000 11.77106 ? 179 GLY   A O   1 
ATOM   1378 N  N   . ASN   A 1 180 ? -1.30337  -8.91256  -5.49923  1.000 9.67067  ? 180 ASN   A N   1 
ATOM   1379 C  CA  . ASN   A 1 180 ? -0.52190  -10.14244 -5.40026  1.000 11.96695 ? 180 ASN   A CA  1 
ATOM   1380 C  C   . ASN   A 1 180 ? -1.45007  -11.34273 -5.47180  1.000 10.68821 ? 180 ASN   A C   1 
ATOM   1381 O  O   . ASN   A 1 180 ? -2.35534  -11.47513 -4.65213  1.000 9.33633  ? 180 ASN   A O   1 
ATOM   1382 C  CB  . ASN   A 1 180 ? 0.27329   -10.14749 -4.10171  1.000 11.06407 ? 180 ASN   A CB  1 
ATOM   1383 C  CG  . ASN   A 1 180 ? 1.20854   -8.98482  -4.02984  1.000 11.49763 ? 180 ASN   A CG  1 
ATOM   1384 O  OD1 . ASN   A 1 180 ? 2.10976   -8.83435  -4.87260  1.000 13.11086 ? 180 ASN   A OD1 1 
ATOM   1385 N  ND2 . ASN   A 1 180 ? 0.99559   -8.11746  -3.03704  1.000 15.40796 ? 180 ASN   A ND2 1 
ATOM   1386 N  N   . PHE   A 1 181 ? -1.21255  -12.23076 -6.43466  1.000 10.65970 ? 181 PHE   A N   1 
ATOM   1387 C  CA  . PHE   A 1 181 ? -2.12790  -13.34411 -6.62154  1.000 9.44960  ? 181 PHE   A CA  1 
ATOM   1388 C  C   . PHE   A 1 181 ? -2.20081  -14.23593 -5.39037  1.000 10.72467 ? 181 PHE   A C   1 
ATOM   1389 O  O   . PHE   A 1 181 ? -1.21695  -14.45137 -4.68648  1.000 9.43859  ? 181 PHE   A O   1 
ATOM   1390 C  CB  . PHE   A 1 181 ? -1.70825  -14.19789 -7.81735  1.000 11.29637 ? 181 PHE   A CB  1 
ATOM   1391 C  CG  . PHE   A 1 181 ? -2.49252  -13.92218 -9.05198  1.000 11.73450 ? 181 PHE   A CG  1 
ATOM   1392 C  CD1 . PHE   A 1 181 ? -3.74044  -14.51605 -9.24102  1.000 12.19531 ? 181 PHE   A CD1 1 
ATOM   1393 C  CD2 . PHE   A 1 181 ? -2.01515  -13.04397 -10.00623 1.000 10.71803 ? 181 PHE   A CD2 1 
ATOM   1394 C  CE1 . PHE   A 1 181 ? -4.47106  -14.24689 -10.38914 1.000 11.61837 ? 181 PHE   A CE1 1 
ATOM   1395 C  CE2 . PHE   A 1 181 ? -2.73657  -12.76612 -11.18102 1.000 13.90099 ? 181 PHE   A CE2 1 
ATOM   1396 C  CZ  . PHE   A 1 181 ? -3.98051  -13.37432 -11.35936 1.000 13.21656 ? 181 PHE   A CZ  1 
ATOM   1397 N  N   . TYR   A 1 182 ? -3.38347  -14.77926 -5.16964  1.000 8.69429  ? 182 TYR   A N   1 
ATOM   1398 C  CA  . TYR   A 1 182 ? -3.54503  -15.89994 -4.27472  1.000 8.29394  ? 182 TYR   A CA  1 
ATOM   1399 C  C   . TYR   A 1 182 ? -3.18621  -17.17199 -5.01890  1.000 10.66618 ? 182 TYR   A C   1 
ATOM   1400 O  O   . TYR   A 1 182 ? -3.81211  -17.49091 -6.03918  1.000 10.53534 ? 182 TYR   A O   1 
ATOM   1401 C  CB  . TYR   A 1 182 ? -4.98606  -15.96575 -3.79920  1.000 7.64267  ? 182 TYR   A CB  1 
ATOM   1402 C  CG  . TYR   A 1 182 ? -5.33831  -14.92743 -2.78933  1.000 7.26784  ? 182 TYR   A CG  1 
ATOM   1403 C  CD1 . TYR   A 1 182 ? -4.99022  -15.12370 -1.46108  1.000 7.57316  ? 182 TYR   A CD1 1 
ATOM   1404 C  CD2 . TYR   A 1 182 ? -6.14924  -13.82981 -3.11914  1.000 7.38805  ? 182 TYR   A CD2 1 
ATOM   1405 C  CE1 . TYR   A 1 182 ? -5.31590  -14.19420 -0.47729  1.000 7.08656  ? 182 TYR   A CE1 1 
ATOM   1406 C  CE2 . TYR   A 1 182 ? -6.52080  -12.89540 -2.13499  1.000 8.88207  ? 182 TYR   A CE2 1 
ATOM   1407 C  CZ  . TYR   A 1 182 ? -6.12166  -13.08802 -0.83529  1.000 10.38612 ? 182 TYR   A CZ  1 
ATOM   1408 O  OH  . TYR   A 1 182 ? -6.49682  -12.13791 0.07101   1.000 9.19435  ? 182 TYR   A OH  1 
ATOM   1409 N  N   . GLY   A 1 183 ? -2.14751  -17.86009 -4.55626  1.000 9.42632  ? 183 GLY   A N   1 
ATOM   1410 C  CA  . GLY   A 1 183 ? -1.74981  -19.10735 -5.17276  1.000 10.84467 ? 183 GLY   A CA  1 
ATOM   1411 C  C   . GLY   A 1 183 ? -0.87964  -18.94075 -6.39817  1.000 10.98634 ? 183 GLY   A C   1 
ATOM   1412 O  O   . GLY   A 1 183 ? -0.55709  -17.82399 -6.82801  1.000 10.95586 ? 183 GLY   A O   1 
ATOM   1413 N  N   . PRO   A 1 184 ? -0.51001  -20.06844 -7.00385  1.000 12.86401 ? 184 PRO   A N   1 
ATOM   1414 C  CA  . PRO   A 1 184 ? 0.51118   -20.07881 -8.07033  1.000 14.77430 ? 184 PRO   A CA  1 
ATOM   1415 C  C   . PRO   A 1 184 ? -0.08240  -19.80458 -9.44618  1.000 16.90764 ? 184 PRO   A C   1 
ATOM   1416 O  O   . PRO   A 1 184 ? 0.01502   -20.63573 -10.35872 1.000 19.34391 ? 184 PRO   A O   1 
ATOM   1417 C  CB  . PRO   A 1 184 ? 1.06036   -21.50903 -7.97882  1.000 16.56828 ? 184 PRO   A CB  1 
ATOM   1418 C  CG  . PRO   A 1 184 ? -0.19321  -22.31495 -7.57120  1.000 15.61270 ? 184 PRO   A CG  1 
ATOM   1419 C  CD  . PRO   A 1 184 ? -1.01408  -21.41563 -6.68498  1.000 15.56657 ? 184 PRO   A CD  1 
ATOM   1420 N  N   . PHE   A 1 185 ? -0.72006  -18.64002 -9.59935  1.000 12.91640 ? 185 PHE   A N   1 
ATOM   1421 C  CA  . PHE   A 1 185 ? -1.40818  -18.25769 -10.83030 1.000 13.75650 ? 185 PHE   A CA  1 
ATOM   1422 C  C   . PHE   A 1 185 ? -0.86792  -16.93002 -11.33865 1.000 18.84717 ? 185 PHE   A C   1 
ATOM   1423 O  O   . PHE   A 1 185 ? -0.29515  -16.13874 -10.57828 1.000 17.78725 ? 185 PHE   A O   1 
ATOM   1424 C  CB  . PHE   A 1 185 ? -2.92521  -18.18472 -10.60295 1.000 15.20652 ? 185 PHE   A CB  1 
ATOM   1425 C  CG  . PHE   A 1 185 ? -3.46361  -19.41283 -9.96275  1.000 13.10877 ? 185 PHE   A CG  1 
ATOM   1426 C  CD1 . PHE   A 1 185 ? -3.43130  -20.62187 -10.64443 1.000 14.51186 ? 185 PHE   A CD1 1 
ATOM   1427 C  CD2 . PHE   A 1 185 ? -3.91345  -19.39510 -8.65165  1.000 12.48697 ? 185 PHE   A CD2 1 
ATOM   1428 C  CE1 . PHE   A 1 185 ? -3.89080  -21.78710 -10.04712 1.000 15.97327 ? 185 PHE   A CE1 1 
ATOM   1429 C  CE2 . PHE   A 1 185 ? -4.37387  -20.56262 -8.05410  1.000 14.22717 ? 185 PHE   A CE2 1 
ATOM   1430 C  CZ  . PHE   A 1 185 ? -4.36918  -21.75592 -8.74595  1.000 14.15965 ? 185 PHE   A CZ  1 
ATOM   1431 N  N   . VAL   A 1 186 ? -1.04976  -16.69550 -12.64353 1.000 15.24614 ? 186 VAL   A N   1 
ATOM   1432 C  CA  . VAL   A 1 186 ? -0.48033  -15.53459 -13.32102 1.000 18.60253 ? 186 VAL   A CA  1 
ATOM   1433 C  C   . VAL   A 1 186 ? -1.51600  -14.95328 -14.27325 1.000 21.43302 ? 186 VAL   A C   1 
ATOM   1434 O  O   . VAL   A 1 186 ? -2.37843  -15.66952 -14.79290 1.000 19.23405 ? 186 VAL   A O   1 
ATOM   1435 C  CB  . VAL   A 1 186 ? 0.82314   -15.88799 -14.07221 1.000 20.81002 ? 186 VAL   A CB  1 
ATOM   1436 C  CG1 . VAL   A 1 186 ? 1.91849   -16.24280 -13.06718 1.000 21.63737 ? 186 VAL   A CG1 1 
ATOM   1437 C  CG2 . VAL   A 1 186 ? 0.60081   -17.04808 -15.04311 1.000 20.86697 ? 186 VAL   A CG2 1 
ATOM   1438 N  N   . ASP   A 1 187 ? -1.43046  -13.64048 -14.50220 1.000 19.69750 ? 187 ASP   A N   1 
ATOM   1439 C  CA  . ASP   A 1 187 ? -2.36549  -12.98011 -15.42010 1.000 19.19646 ? 187 ASP   A CA  1 
ATOM   1440 C  C   . ASP   A 1 187 ? -1.81883  -12.99410 -16.85074 1.000 22.07996 ? 187 ASP   A C   1 
ATOM   1441 O  O   . ASP   A 1 187 ? -1.56398  -11.97123 -17.48888 1.000 22.87702 ? 187 ASP   A O   1 
ATOM   1442 C  CB  . ASP   A 1 187 ? -2.71756  -11.57401 -14.94382 1.000 18.05139 ? 187 ASP   A CB  1 
ATOM   1443 C  CG  . ASP   A 1 187 ? -1.52417  -10.70396 -14.63291 1.000 15.94221 ? 187 ASP   A CG  1 
ATOM   1444 O  OD1 . ASP   A 1 187 ? -0.36645  -11.17296 -14.64817 1.000 15.37392 ? 187 ASP   A OD1 1 
ATOM   1445 O  OD2 . ASP   A 1 187 ? -1.77979  -9.51123  -14.34270 1.000 15.49031 ? 187 ASP   A OD2 1 
ATOM   1446 N  N   . ARG   A 1 188 ? -1.60936  -14.21696 -17.32869 1.000 22.95825 ? 188 ARG   A N   1 
ATOM   1447 C  CA  . ARG   A 1 188 ? -1.35612  -14.49349 -18.73481 1.000 26.39179 ? 188 ARG   A CA  1 
ATOM   1448 C  C   . ARG   A 1 188 ? -2.04024  -15.81100 -19.05126 1.000 31.59385 ? 188 ARG   A C   1 
ATOM   1449 O  O   . ARG   A 1 188 ? -2.37436  -16.58498 -18.14762 1.000 28.91049 ? 188 ARG   A O   1 
ATOM   1450 C  CB  . ARG   A 1 188 ? 0.13221   -14.61951 -19.10045 1.000 30.83508 ? 188 ARG   A CB  1 
ATOM   1451 C  CG  . ARG   A 1 188 ? 1.02222   -15.12616 -17.99624 1.000 32.07368 ? 188 ARG   A CG  1 
ATOM   1452 C  CD  . ARG   A 1 188 ? 2.48806   -14.76795 -18.22624 1.000 31.51247 ? 188 ARG   A CD  1 
ATOM   1453 N  NE  . ARG   A 1 188 ? 3.30616   -15.31246 -17.15060 1.000 37.82599 ? 188 ARG   A NE  1 
ATOM   1454 C  CZ  . ARG   A 1 188 ? 3.86071   -16.51527 -17.18611 1.000 35.98353 ? 188 ARG   A CZ  1 
ATOM   1455 N  NH1 . ARG   A 1 188 ? 3.69750   -17.31690 -18.22529 1.000 40.89528 ? 188 ARG   A NH1 1 
ATOM   1456 N  NH2 . ARG   A 1 188 ? 4.57360   -16.93427 -16.14258 1.000 38.28038 ? 188 ARG   A NH2 1 
ATOM   1457 N  N   . GLN   A 1 189 ? -2.23126  -16.08548 -20.33821 1.000 34.82297 ? 189 GLN   A N   1 
ATOM   1458 C  CA  . GLN   A 1 189 ? -2.97581  -17.28303 -20.71767 1.000 37.70463 ? 189 GLN   A CA  1 
ATOM   1459 C  C   . GLN   A 1 189 ? -1.94151  -18.39294 -20.87612 1.000 35.99346 ? 189 GLN   A C   1 
ATOM   1460 O  O   . GLN   A 1 189 ? -1.16146  -18.40996 -21.83155 1.000 39.24831 ? 189 GLN   A O   1 
ATOM   1461 C  CB  . GLN   A 1 189 ? -3.81876  -17.03404 -21.96919 1.000 42.60804 ? 189 GLN   A CB  1 
ATOM   1462 C  CG  . GLN   A 1 189 ? -4.94385  -18.07982 -22.26078 1.000 45.27903 ? 189 GLN   A CG  1 
ATOM   1463 C  CD  . GLN   A 1 189 ? -4.52387  -19.52015 -22.20841 1.000 49.73196 ? 189 GLN   A CD  1 
ATOM   1464 O  OE1 . GLN   A 1 189 ? -5.22860  -20.36768 -21.65632 1.000 52.62932 ? 189 GLN   A OE1 1 
ATOM   1465 N  NE2 . GLN   A 1 189 ? -3.44745  -19.83478 -22.90967 1.000 51.36520 ? 189 GLN   A NE2 1 
ATOM   1466 N  N   . THR   A 1 190 ? -1.90770  -19.29228 -19.89942 1.000 31.86747 ? 190 THR   A N   1 
ATOM   1467 C  CA  . THR   A 1 190 ? -1.07694  -20.48703 -19.87035 1.000 34.98647 ? 190 THR   A CA  1 
ATOM   1468 C  C   . THR   A 1 190 ? -1.98429  -21.68334 -19.62224 1.000 33.75284 ? 190 THR   A C   1 
ATOM   1469 O  O   . THR   A 1 190 ? -3.20389  -21.55484 -19.50103 1.000 32.74792 ? 190 THR   A O   1 
ATOM   1470 C  CB  . THR   A 1 190 ? -0.00288  -20.41251 -18.77236 1.000 31.43854 ? 190 THR   A CB  1 
ATOM   1471 O  OG1 . THR   A 1 190 ? -0.59974  -20.66797 -17.49406 1.000 29.06119 ? 190 THR   A OG1 1 
ATOM   1472 C  CG2 . THR   A 1 190 ? 0.66842   -19.03746 -18.73676 1.000 32.01341 ? 190 THR   A CG2 1 
ATOM   1473 N  N   . ALA   A 1 191 ? -1.37884  -22.85063 -19.50585 1.000 31.68804 ? 191 ALA   A N   1 
ATOM   1474 C  CA  . ALA   A 1 191 ? -2.13335  -24.03138 -19.12252 1.000 30.69215 ? 191 ALA   A CA  1 
ATOM   1475 C  C   . ALA   A 1 191 ? -2.27997  -24.17206 -17.60680 1.000 27.59868 ? 191 ALA   A C   1 
ATOM   1476 O  O   . ALA   A 1 191 ? -2.47761  -25.29963 -17.13733 1.000 30.07800 ? 191 ALA   A O   1 
ATOM   1477 C  CB  . ALA   A 1 191 ? -1.47714  -25.28240 -19.72034 1.000 35.32227 ? 191 ALA   A CB  1 
ATOM   1478 N  N   . GLN   A 1 192 ? -2.20746  -23.07801 -16.83996 1.000 26.48499 ? 192 GLN   A N   1 
ATOM   1479 C  CA  . GLN   A 1 192 ? -2.26450  -23.19026 -15.38538 1.000 24.93188 ? 192 GLN   A CA  1 
ATOM   1480 C  C   . GLN   A 1 192 ? -3.55120  -23.87732 -14.95053 1.000 26.62189 ? 192 GLN   A C   1 
ATOM   1481 O  O   . GLN   A 1 192 ? -4.61083  -23.70933 -15.56344 1.000 28.02039 ? 192 GLN   A O   1 
ATOM   1482 C  CB  . GLN   A 1 192 ? -2.21818  -21.82729 -14.68637 1.000 25.80821 ? 192 GLN   A CB  1 
ATOM   1483 C  CG  . GLN   A 1 192 ? -2.99284  -20.72585 -15.36080 1.000 23.91616 ? 192 GLN   A CG  1 
ATOM   1484 C  CD  . GLN   A 1 192 ? -2.59284  -19.33527 -14.88846 1.000 22.42771 ? 192 GLN   A CD  1 
ATOM   1485 O  OE1 . GLN   A 1 192 ? -2.03009  -19.15569 -13.79269 1.000 19.86664 ? 192 GLN   A OE1 1 
ATOM   1486 N  NE2 . GLN   A 1 192 ? -2.88925  -18.34152 -15.70578 1.000 21.28232 ? 192 GLN   A NE2 1 
ATOM   1487 N  N   . ALA   A 1 193 ? -3.46370  -24.61178 -13.84378 1.000 24.68995 ? 193 ALA   A N   1 
ATOM   1488 C  CA  . ALA   A 1 193 ? -4.60009  -25.36018 -13.33131 1.000 22.55749 ? 193 ALA   A CA  1 
ATOM   1489 C  C   . ALA   A 1 193 ? -4.55791  -25.37773 -11.80800 1.000 22.41088 ? 193 ALA   A C   1 
ATOM   1490 O  O   . ALA   A 1 193 ? -3.50828  -25.17544 -11.19386 1.000 25.47828 ? 193 ALA   A O   1 
ATOM   1491 C  CB  . ALA   A 1 193 ? -4.62726  -26.79121 -13.88113 1.000 23.54377 ? 193 ALA   A CB  1 
ATOM   1492 N  N   . ALA   A 1 194 ? -5.71950  -25.66051 -11.21060 1.000 22.23122 ? 194 ALA   A N   1 
ATOM   1493 C  CA  . ALA   A 1 194 ? -5.86761  -25.59850 -9.75787  1.000 22.65288 ? 194 ALA   A CA  1 
ATOM   1494 C  C   . ALA   A 1 194 ? -4.90325  -26.54356 -9.04192  1.000 29.27324 ? 194 ALA   A C   1 
ATOM   1495 O  O   . ALA   A 1 194 ? -4.16515  -26.13478 -8.13917  1.000 30.44543 ? 194 ALA   A O   1 
ATOM   1496 C  CB  . ALA   A 1 194 ? -7.31506  -25.91621 -9.37529  1.000 21.77015 ? 194 ALA   A CB  1 
ATOM   1497 N  N   . GLY   A 1 195 ? -4.89786  -27.81472 -9.40531  1.000 29.66983 ? 195 GLY   A N   1 
ATOM   1498 C  CA  . GLY   A 1 195 ? -4.13537  -28.69835 -8.53670  1.000 35.24655 ? 195 GLY   A CA  1 
ATOM   1499 C  C   . GLY   A 1 195 ? -4.81886  -28.98500 -7.20746  1.000 29.10534 ? 195 GLY   A C   1 
ATOM   1500 O  O   . GLY   A 1 195 ? -5.83078  -28.36269 -6.86091  1.000 22.78781 ? 195 GLY   A O   1 
ATOM   1501 N  N   . THR   A 1 196 ? -4.26241  -29.92134 -6.44250  1.000 28.40638 ? 196 THR   A N   1 
ATOM   1502 C  CA  . THR   A 1 196 ? -5.07691  -30.68462 -5.50853  1.000 25.52622 ? 196 THR   A CA  1 
ATOM   1503 C  C   . THR   A 1 196 ? -5.54468  -29.84020 -4.32877  1.000 22.12826 ? 196 THR   A C   1 
ATOM   1504 O  O   . THR   A 1 196 ? -4.82044  -28.97832 -3.81957  1.000 24.40148 ? 196 THR   A O   1 
ATOM   1505 C  CB  . THR   A 1 196 ? -4.30785  -31.89827 -5.00352  1.000 26.88902 ? 196 THR   A CB  1 
ATOM   1506 O  OG1 . THR   A 1 196 ? -3.11256  -31.45757 -4.34400  1.000 32.08072 ? 196 THR   A OG1 1 
ATOM   1507 C  CG2 . THR   A 1 196 ? -3.92782  -32.78980 -6.18952  1.000 27.68355 ? 196 THR   A CG2 1 
ATOM   1508 N  N   . ASP   A 1 197 ? -6.77816  -30.08992 -3.91444  1.000 21.71808 ? 197 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 197 ? -7.42492  -29.42299 -2.79283  1.000 19.56739 ? 197 ASP   A CA  1 
ATOM   1510 C  C   . ASP   A 1 197 ? -7.62815  -30.40484 -1.64394  1.000 22.57710 ? 197 ASP   A C   1 
ATOM   1511 O  O   . ASP   A 1 197 ? -7.50449  -31.61885 -1.80775  1.000 24.19068 ? 197 ASP   A O   1 
ATOM   1512 C  CB  . ASP   A 1 197 ? -8.77166  -28.83570 -3.21893  1.000 18.12613 ? 197 ASP   A CB  1 
ATOM   1513 C  CG  . ASP   A 1 197 ? -9.14495  -27.59076 -2.43810  1.000 19.31980 ? 197 ASP   A CG  1 
ATOM   1514 O  OD1 . ASP   A 1 197 ? -8.24038  -26.93127 -1.86852  1.000 18.76750 ? 197 ASP   A OD1 1 
ATOM   1515 O  OD2 . ASP   A 1 197 ? -10.34728 -27.25232 -2.42771  1.000 19.69393 ? 197 ASP   A OD2 1 
ATOM   1516 N  N   . THR   A 1 198 ? -7.94708  -29.85283 -0.47260  1.000 19.58713 ? 198 THR   A N   1 
ATOM   1517 C  CA  . THR   A 1 198 ? -8.29631  -30.62127 0.71700   1.000 19.49476 ? 198 THR   A CA  1 
ATOM   1518 C  C   . THR   A 1 198 ? -9.53146  -29.99552 1.34099   1.000 18.63572 ? 198 THR   A C   1 
ATOM   1519 O  O   . THR   A 1 198 ? -9.94082  -28.89504 0.97065   1.000 17.31470 ? 198 THR   A O   1 
ATOM   1520 C  CB  . THR   A 1 198 ? -7.16967  -30.64853 1.76210   1.000 26.48085 ? 198 THR   A CB  1 
ATOM   1521 O  OG1 . THR   A 1 198 ? -6.69285  -29.31577 1.99198   1.000 23.78871 ? 198 THR   A OG1 1 
ATOM   1522 C  CG2 . THR   A 1 198 ? -6.02675  -31.48157 1.27273   1.000 27.31607 ? 198 THR   A CG2 1 
ATOM   1523 N  N   . THR   A 1 199 ? -10.12334 -30.70935 2.29913   1.000 19.93276 ? 199 THR   A N   1 
ATOM   1524 C  CA  . THR   A 1 199 ? -11.28361 -30.20372 3.02313   1.000 19.73569 ? 199 THR   A CA  1 
ATOM   1525 C  C   . THR   A 1 199 ? -10.82589 -29.49616 4.29703   1.000 17.84215 ? 199 THR   A C   1 
ATOM   1526 O  O   . THR   A 1 199 ? -9.89315  -29.94924 4.96970   1.000 18.36936 ? 199 THR   A O   1 
ATOM   1527 C  CB  . THR   A 1 199 ? -12.24390 -31.35979 3.33384   1.000 20.91849 ? 199 THR   A CB  1 
ATOM   1528 O  OG1 . THR   A 1 199 ? -12.68767 -31.95102 2.10437   1.000 20.35642 ? 199 THR   A OG1 1 
ATOM   1529 C  CG2 . THR   A 1 199 ? -13.44903 -30.88648 4.11057   1.000 17.68094 ? 199 THR   A CG2 1 
ATOM   1530 N  N   . ILE   A 1 200 ? -11.47356 -28.37378 4.61311   1.000 17.13733 ? 200 ILE   A N   1 
ATOM   1531 C  CA  . ILE   A 1 200 ? -11.06110 -27.50838 5.72220   1.000 13.02417 ? 200 ILE   A CA  1 
ATOM   1532 C  C   . ILE   A 1 200 ? -11.66065 -28.06925 7.01363   1.000 14.49025 ? 200 ILE   A C   1 
ATOM   1533 O  O   . ILE   A 1 200 ? -12.80358 -27.77081 7.36597   1.000 13.12068 ? 200 ILE   A O   1 
ATOM   1534 C  CB  . ILE   A 1 200 ? -11.46175 -26.04754 5.49020   1.000 13.48785 ? 200 ILE   A CB  1 
ATOM   1535 C  CG1 . ILE   A 1 200 ? -10.97818 -25.55666 4.11519   1.000 13.34813 ? 200 ILE   A CG1 1 
ATOM   1536 C  CG2 . ILE   A 1 200 ? -10.90004 -25.15907 6.59802   1.000 12.33957 ? 200 ILE   A CG2 1 
ATOM   1537 C  CD1 . ILE   A 1 200 ? -11.85582 -24.44939 3.53700   1.000 10.85855 ? 200 ILE   A CD1 1 
ATOM   1538 N  N   . THR   A 1 201 ? -10.86542 -28.86559 7.73532   1.000 14.99276 ? 201 THR   A N   1 
ATOM   1539 C  CA  . THR   A 1 201 ? -11.35845 -29.66855 8.86434   1.000 15.44134 ? 201 THR   A CA  1 
ATOM   1540 C  C   . THR   A 1 201 ? -11.94637 -28.80577 9.97249   1.000 14.67444 ? 201 THR   A C   1 
ATOM   1541 O  O   . THR   A 1 201 ? -13.01707 -29.11987 10.51243  1.000 15.41350 ? 201 THR   A O   1 
ATOM   1542 C  CB  . THR   A 1 201 ? -10.21834 -30.52472 9.40994   1.000 17.69920 ? 201 THR   A CB  1 
ATOM   1543 O  OG1 . THR   A 1 201 ? -9.67578  -31.30563 8.34285   1.000 17.65111 ? 201 THR   A OG1 1 
ATOM   1544 C  CG2 . THR   A 1 201 ? -10.68691 -31.44653 10.53962  1.000 17.15902 ? 201 THR   A CG2 1 
ATOM   1545 N  N   . VAL   A 1 202 ? -11.24940 -27.72936 10.34902  1.000 12.71041 ? 202 VAL   A N   1 
ATOM   1546 C  CA  . VAL   A 1 202 ? -11.72730 -26.91514 11.45882  1.000 13.15569 ? 202 VAL   A CA  1 
ATOM   1547 C  C   . VAL   A 1 202 ? -13.09691 -26.33393 11.13264  1.000 11.65598 ? 202 VAL   A C   1 
ATOM   1548 O  O   . VAL   A 1 202 ? -13.93257 -26.16896 12.03046  1.000 14.26642 ? 202 VAL   A O   1 
ATOM   1549 C  CB  . VAL   A 1 202 ? -10.71457 -25.81275 11.83408  1.000 15.09922 ? 202 VAL   A CB  1 
ATOM   1550 C  CG1 . VAL   A 1 202 ? -10.45577 -24.85548 10.66023  1.000 15.53955 ? 202 VAL   A CG1 1 
ATOM   1551 C  CG2 . VAL   A 1 202 ? -11.21112 -25.04253 13.07294  1.000 17.80261 ? 202 VAL   A CG2 1 
ATOM   1552 N  N   . ASN   A 1 203 ? -13.35092 -26.03807 9.85055   1.000 13.03709 ? 203 ASN   A N   1 
ATOM   1553 C  CA  . ASN   A 1 203 ? -14.62819 -25.46408 9.44663   1.000 11.63844 ? 203 ASN   A CA  1 
ATOM   1554 C  C   . ASN   A 1 203 ? -15.73753 -26.50818 9.51103   1.000 12.47460 ? 203 ASN   A C   1 
ATOM   1555 O  O   . ASN   A 1 203 ? -16.87943 -26.20247 9.90093   1.000 11.72669 ? 203 ASN   A O   1 
ATOM   1556 C  CB  . ASN   A 1 203 ? -14.52476 -24.89844 8.02940   1.000 10.62235 ? 203 ASN   A CB  1 
ATOM   1557 C  CG  . ASN   A 1 203 ? -13.72476 -23.57703 7.96209   1.000 9.88725  ? 203 ASN   A CG  1 
ATOM   1558 O  OD1 . ASN   A 1 203 ? -13.19610 -23.09566 8.97137   1.000 11.35855 ? 203 ASN   A OD1 1 
ATOM   1559 N  ND2 . ASN   A 1 203 ? -13.67271 -22.98804 6.77193   1.000 9.81408  ? 203 ASN   A ND2 1 
ATOM   1560 N  N   . VAL   A 1 204 ? -15.43645 -27.74107 9.10256   1.000 13.73507 ? 204 VAL   A N   1 
ATOM   1561 C  CA  . VAL   A 1 204 ? -16.42232 -28.81522 9.22650   1.000 13.47211 ? 204 VAL   A CA  1 
ATOM   1562 C  C   . VAL   A 1 204 ? -16.81819 -28.98198 10.68332  1.000 13.68592 ? 204 VAL   A C   1 
ATOM   1563 O  O   . VAL   A 1 204 ? -18.00977 -29.07558 11.00876  1.000 14.38199 ? 204 VAL   A O   1 
ATOM   1564 C  CB  . VAL   A 1 204 ? -15.88344 -30.12824 8.62958   1.000 14.02269 ? 204 VAL   A CB  1 
ATOM   1565 C  CG1 . VAL   A 1 204 ? -16.86192 -31.29899 8.87638   1.000 15.64280 ? 204 VAL   A CG1 1 
ATOM   1566 C  CG2 . VAL   A 1 204 ? -15.62689 -29.94980 7.12481   1.000 14.76768 ? 204 VAL   A CG2 1 
ATOM   1567 N  N   . LEU   A 1 205 ? -15.83079 -28.97253 11.58307  1.000 13.88462 ? 205 LEU   A N   1 
ATOM   1568 C  CA  . LEU   A 1 205 ? -16.14272 -29.07611 13.00579  1.000 15.17029 ? 205 LEU   A CA  1 
ATOM   1569 C  C   . LEU   A 1 205 ? -16.98712 -27.89196 13.45618  1.000 16.56916 ? 205 LEU   A C   1 
ATOM   1570 O  O   . LEU   A 1 205 ? -17.94653 -28.07035 14.20791  1.000 14.40086 ? 205 LEU   A O   1 
ATOM   1571 C  CB  . LEU   A 1 205 ? -14.85857 -29.17366 13.83503  1.000 14.70071 ? 205 LEU   A CB  1 
ATOM   1572 C  CG  . LEU   A 1 205 ? -14.07082 -30.45969 13.64880  1.000 15.47970 ? 205 LEU   A CG  1 
ATOM   1573 C  CD1 . LEU   A 1 205 ? -12.71427 -30.31947 14.32282  1.000 16.73187 ? 205 LEU   A CD1 1 
ATOM   1574 C  CD2 . LEU   A 1 205 ? -14.81936 -31.67758 14.20271  1.000 20.26283 ? 205 LEU   A CD2 1 
ATOM   1575 N  N   . ALA   A 1 206 ? -16.64324 -26.67723 13.00035  1.000 14.86396 ? 206 ALA   A N   1 
ATOM   1576 C  CA  . ALA   A 1 206 ? -17.46432 -25.50723 13.32077  1.000 12.53608 ? 206 ALA   A CA  1 
ATOM   1577 C  C   . ALA   A 1 206 ? -18.90438 -25.72832 12.90292  1.000 13.88833 ? 206 ALA   A C   1 
ATOM   1578 O  O   . ALA   A 1 206 ? -19.83337 -25.39726 13.64545  1.000 13.97972 ? 206 ALA   A O   1 
ATOM   1579 C  CB  . ALA   A 1 206 ? -16.90603 -24.25043 12.64321  1.000 13.41285 ? 206 ALA   A CB  1 
ATOM   1580 N  N   . TRP   A 1 207 ? -19.09874 -26.26539 11.70115  1.000 12.73945 ? 207 TRP   A N   1 
ATOM   1581 C  CA  . TRP   A 1 207 ? -20.43826 -26.44980 11.16287  1.000 12.57185 ? 207 TRP   A CA  1 
ATOM   1582 C  C   . TRP   A 1 207 ? -21.18074 -27.56111 11.89919  1.000 15.54176 ? 207 TRP   A C   1 
ATOM   1583 O  O   . TRP   A 1 207 ? -22.40035 -27.47858 12.07626  1.000 15.83693 ? 207 TRP   A O   1 
ATOM   1584 C  CB  . TRP   A 1 207 ? -20.29912 -26.72743 9.66924   1.000 13.71743 ? 207 TRP   A CB  1 
ATOM   1585 C  CG  . TRP   A 1 207 ? -21.52090 -27.20605 8.91907   1.000 14.17763 ? 207 TRP   A CG  1 
ATOM   1586 C  CD1 . TRP   A 1 207 ? -22.54018 -26.44697 8.42584   1.000 16.78412 ? 207 TRP   A CD1 1 
ATOM   1587 C  CD2 . TRP   A 1 207 ? -21.77590 -28.54475 8.50588   1.000 13.83448 ? 207 TRP   A CD2 1 
ATOM   1588 N  NE1 . TRP   A 1 207 ? -23.44855 -27.24909 7.76484   1.000 15.60839 ? 207 TRP   A NE1 1 
ATOM   1589 C  CE2 . TRP   A 1 207 ? -23.00275 -28.54145 7.80233   1.000 15.75209 ? 207 TRP   A CE2 1 
ATOM   1590 C  CE3 . TRP   A 1 207 ? -21.10366 -29.75518 8.68697   1.000 17.74604 ? 207 TRP   A CE3 1 
ATOM   1591 C  CZ2 . TRP   A 1 207 ? -23.54925 -29.69756 7.25848   1.000 19.97622 ? 207 TRP   A CZ2 1 
ATOM   1592 C  CZ3 . TRP   A 1 207 ? -21.66450 -30.91160 8.16275   1.000 19.62743 ? 207 TRP   A CZ3 1 
ATOM   1593 C  CH2 . TRP   A 1 207 ? -22.87233 -30.87132 7.45318   1.000 16.49635 ? 207 TRP   A CH2 1 
ATOM   1594 N  N   . LEU   A 1 208 ? -20.47015 -28.59159 12.35854  1.000 14.03664 ? 208 LEU   A N   1 
ATOM   1595 C  CA  . LEU   A 1 208 ? -21.13207 -29.58572 13.21323  1.000 15.12824 ? 208 LEU   A CA  1 
ATOM   1596 C  C   . LEU   A 1 208 ? -21.61847 -28.94713 14.51323  1.000 16.07348 ? 208 LEU   A C   1 
ATOM   1597 O  O   . LEU   A 1 208 ? -22.70604 -29.27391 15.00896  1.000 17.28397 ? 208 LEU   A O   1 
ATOM   1598 C  CB  . LEU   A 1 208 ? -20.18830 -30.75357 13.49918  1.000 16.46961 ? 208 LEU   A CB  1 
ATOM   1599 C  CG  . LEU   A 1 208 ? -19.92935 -31.68405 12.30816  1.000 19.59306 ? 208 LEU   A CG  1 
ATOM   1600 C  CD1 . LEU   A 1 208 ? -18.92286 -32.74566 12.69852  1.000 18.13879 ? 208 LEU   A CD1 1 
ATOM   1601 C  CD2 . LEU   A 1 208 ? -21.18852 -32.35423 11.77081  1.000 16.52596 ? 208 LEU   A CD2 1 
ATOM   1602 N  N   . TYR   A 1 209 ? -20.84608 -28.00429 15.06374  1.000 17.45348 ? 209 TYR   A N   1 
ATOM   1603 C  CA  . TYR   A 1 209 ? -21.31492 -27.27961 16.24386  1.000 17.49997 ? 209 TYR   A CA  1 
ATOM   1604 C  C   . TYR   A 1 209 ? -22.52176 -26.40862 15.91772  1.000 16.34427 ? 209 TYR   A C   1 
ATOM   1605 O  O   . TYR   A 1 209 ? -23.45829 -26.33168 16.72416  1.000 17.95802 ? 209 TYR   A O   1 
ATOM   1606 C  CB  . TYR   A 1 209 ? -20.18694 -26.43292 16.83069  1.000 15.91190 ? 209 TYR   A CB  1 
ATOM   1607 C  CG  . TYR   A 1 209 ? -19.24358 -27.20295 17.72578  1.000 16.84680 ? 209 TYR   A CG  1 
ATOM   1608 C  CD1 . TYR   A 1 209 ? -19.64133 -27.66529 18.97825  1.000 18.26141 ? 209 TYR   A CD1 1 
ATOM   1609 C  CD2 . TYR   A 1 209 ? -17.95026 -27.47667 17.31015  1.000 16.46377 ? 209 TYR   A CD2 1 
ATOM   1610 C  CE1 . TYR   A 1 209 ? -18.77115 -28.37625 19.78085  1.000 21.72232 ? 209 TYR   A CE1 1 
ATOM   1611 C  CE2 . TYR   A 1 209 ? -17.08031 -28.18217 18.09979  1.000 19.78766 ? 209 TYR   A CE2 1 
ATOM   1612 C  CZ  . TYR   A 1 209 ? -17.48286 -28.62416 19.33260  1.000 20.98708 ? 209 TYR   A CZ  1 
ATOM   1613 O  OH  . TYR   A 1 209 ? -16.59801 -29.32951 20.11735  1.000 23.51885 ? 209 TYR   A OH  1 
ATOM   1614 N  N   . ALA   A 1 210 ? -22.51605 -25.73580 14.75322  1.000 15.97740 ? 210 ALA   A N   1 
ATOM   1615 C  CA  . ALA   A 1 210 ? -23.71454 -25.02431 14.30956  1.000 17.48137 ? 210 ALA   A CA  1 
ATOM   1616 C  C   . ALA   A 1 210 ? -24.92135 -25.95005 14.26068  1.000 18.68509 ? 210 ALA   A C   1 
ATOM   1617 O  O   . ALA   A 1 210 ? -26.03391 -25.55393 14.62988  1.000 16.57545 ? 210 ALA   A O   1 
ATOM   1618 C  CB  . ALA   A 1 210 ? -23.49778 -24.40544 12.93234  1.000 16.08913 ? 210 ALA   A CB  1 
ATOM   1619 N  N   . ALA   A 1 211 ? -24.72788 -27.18445 13.78552  1.000 15.41983 ? 211 ALA   A N   1 
ATOM   1620 C  CA  . ALA   A 1 211 ? -25.84955 -28.11203 13.69319  1.000 18.36024 ? 211 ALA   A CA  1 
ATOM   1621 C  C   . ALA   A 1 211 ? -26.40653 -28.43046 15.07216  1.000 19.61142 ? 211 ALA   A C   1 
ATOM   1622 O  O   . ALA   A 1 211 ? -27.62944 -28.41915 15.27154  1.000 19.37400 ? 211 ALA   A O   1 
ATOM   1623 C  CB  . ALA   A 1 211 ? -25.41648 -29.39192 12.97957  1.000 17.44158 ? 211 ALA   A CB  1 
ATOM   1624 N  N   . VAL   A 1 212 ? -25.52210 -28.68781 16.04110  1.000 18.01189 ? 212 VAL   A N   1 
ATOM   1625 C  CA  . VAL   A 1 212 ? -25.95982 -29.00252 17.40075  1.000 22.29707 ? 212 VAL   A CA  1 
ATOM   1626 C  C   . VAL   A 1 212 ? -26.70447 -27.81661 18.00363  1.000 21.55035 ? 212 VAL   A C   1 
ATOM   1627 O  O   . VAL   A 1 212 ? -27.74964 -27.97932 18.65294  1.000 23.53960 ? 212 VAL   A O   1 
ATOM   1628 C  CB  . VAL   A 1 212 ? -24.75536 -29.40946 18.27536  1.000 24.65009 ? 212 VAL   A CB  1 
ATOM   1629 C  CG1 . VAL   A 1 212 ? -25.19817 -29.59011 19.71678  1.000 23.84064 ? 212 VAL   A CG1 1 
ATOM   1630 C  CG2 . VAL   A 1 212 ? -24.08735 -30.69045 17.75050  1.000 19.87515 ? 212 VAL   A CG2 1 
ATOM   1631 N  N   . ILE   A 1 213 ? -26.17088 -26.60458 17.80699  1.000 21.50560 ? 213 ILE   A N   1 
ATOM   1632 C  CA  . ILE   A 1 213 ? -26.84915 -25.39774 18.27609  1.000 21.22655 ? 213 ILE   A CA  1 
ATOM   1633 C  C   . ILE   A 1 213 ? -28.24784 -25.32313 17.68744  1.000 22.77804 ? 213 ILE   A C   1 
ATOM   1634 O  O   . ILE   A 1 213 ? -29.19466 -24.89327 18.36189  1.000 26.18845 ? 213 ILE   A O   1 
ATOM   1635 C  CB  . ILE   A 1 213 ? -26.01429 -24.13945 17.94203  1.000 23.19245 ? 213 ILE   A CB  1 
ATOM   1636 C  CG1 . ILE   A 1 213 ? -24.74069 -24.11275 18.80423  1.000 23.54742 ? 213 ILE   A CG1 1 
ATOM   1637 C  CG2 . ILE   A 1 213 ? -26.84515 -22.87055 18.14860  1.000 26.01211 ? 213 ILE   A CG2 1 
ATOM   1638 C  CD1 . ILE   A 1 213 ? -23.67648 -23.12617 18.36472  1.000 24.50219 ? 213 ILE   A CD1 1 
ATOM   1639 N  N   . ASN   A 1 214 ? -28.42272 -25.81360 16.46275  1.000 21.03780 ? 214 ASN   A N   1 
ATOM   1640 C  CA  . ASN   A 1 214 ? -29.69720 -25.73391 15.76084  1.000 22.23410 ? 214 ASN   A CA  1 
ATOM   1641 C  C   . ASN   A 1 214 ? -30.53037 -27.01282 15.86632  1.000 26.53817 ? 214 ASN   A C   1 
ATOM   1642 O  O   . ASN   A 1 214 ? -31.52488 -27.14820 15.14279  1.000 26.78555 ? 214 ASN   A O   1 
ATOM   1643 C  CB  . ASN   A 1 214 ? -29.44975 -25.37511 14.29972  1.000 24.33046 ? 214 ASN   A CB  1 
ATOM   1644 C  CG  . ASN   A 1 214 ? -29.18287 -23.87147 14.10480  1.000 23.63184 ? 214 ASN   A CG  1 
ATOM   1645 O  OD1 . ASN   A 1 214 ? -30.10305 -23.05989 14.18162  1.000 32.07199 ? 214 ASN   A OD1 1 
ATOM   1646 N  ND2 . ASN   A 1 214 ? -27.92519 -23.50506 13.90563  1.000 25.05322 ? 214 ASN   A ND2 1 
ATOM   1647 N  N   . GLY   A 1 215 ? -30.14731 -27.95640 16.73770  1.000 24.19705 ? 215 GLY   A N   1 
ATOM   1648 C  CA  . GLY   A 1 215 ? -30.96926 -29.11229 17.05283  1.000 26.65580 ? 215 GLY   A CA  1 
ATOM   1649 C  C   . GLY   A 1 215 ? -30.67903 -30.40401 16.30364  1.000 28.43631 ? 215 GLY   A C   1 
ATOM   1650 O  O   . GLY   A 1 215 ? -31.38625 -31.39379 16.53724  1.000 30.83560 ? 215 GLY   A O   1 
ATOM   1651 N  N   . ASP   A 1 216 ? -29.69749 -30.43167 15.39647  1.000 25.27055 ? 216 ASP   A N   1 
ATOM   1652 C  CA  . ASP   A 1 216 ? -29.26798 -31.68134 14.76619  1.000 22.66888 ? 216 ASP   A CA  1 
ATOM   1653 C  C   . ASP   A 1 216 ? -28.25026 -32.35616 15.67761  1.000 27.70091 ? 216 ASP   A C   1 
ATOM   1654 O  O   . ASP   A 1 216 ? -27.14666 -31.83114 15.87663  1.000 27.28371 ? 216 ASP   A O   1 
ATOM   1655 C  CB  . ASP   A 1 216 ? -28.63266 -31.44926 13.39599  1.000 26.98206 ? 216 ASP   A CB  1 
ATOM   1656 C  CG  . ASP   A 1 216 ? -29.64042 -31.15482 12.31990  1.000 32.30008 ? 216 ASP   A CG  1 
ATOM   1657 O  OD1 . ASP   A 1 216 ? -29.32007 -30.35067 11.41434  1.000 26.74551 ? 216 ASP   A OD1 1 
ATOM   1658 O  OD2 . ASP   A 1 216 ? -30.75549 -31.71053 12.39751  1.000 43.22897 ? 216 ASP   A OD2 1 
ATOM   1659 N  N   . ARG   A 1 217 ? -28.59697 -33.53290 16.21029  1.000 26.88563 ? 217 ARG   A N   1 
ATOM   1660 C  CA  . ARG   A 1 217 ? -27.70494 -34.23029 17.13250  1.000 26.25329 ? 217 ARG   A CA  1 
ATOM   1661 C  C   . ARG   A 1 217 ? -27.46690 -35.69043 16.78930  1.000 25.35371 ? 217 ARG   A C   1 
ATOM   1662 O  O   . ARG   A 1 217 ? -26.73133 -36.36115 17.52234  1.000 24.93234 ? 217 ARG   A O   1 
ATOM   1663 C  CB  . ARG   A 1 217 ? -28.24857 -34.15437 18.56493  1.000 28.40846 ? 217 ARG   A CB  1 
ATOM   1664 C  CG  . ARG   A 1 217 ? -28.78620 -32.79577 18.95169  1.000 29.56145 ? 217 ARG   A CG  1 
ATOM   1665 C  CD  . ARG   A 1 217 ? -29.25543 -32.80078 20.41517  1.000 30.02657 ? 217 ARG   A CD  1 
ATOM   1666 N  NE  . ARG   A 1 217 ? -28.29838 -33.45649 21.30172  1.000 26.69325 ? 217 ARG   A NE  1 
ATOM   1667 C  CZ  . ARG   A 1 217 ? -27.40655 -32.80500 22.03342  1.000 27.77978 ? 217 ARG   A CZ  1 
ATOM   1668 N  NH1 . ARG   A 1 217 ? -27.29490 -31.48635 21.97278  1.000 27.38945 ? 217 ARG   A NH1 1 
ATOM   1669 N  NH2 . ARG   A 1 217 ? -26.58498 -33.49230 22.82073  1.000 27.48022 ? 217 ARG   A NH2 1 
ATOM   1670 N  N   . TRP   A 1 218 ? -28.05450 -36.20183 15.70664  1.000 25.72723 ? 218 TRP   A N   1 
ATOM   1671 C  CA  . TRP   A 1 218 ? -28.03997 -37.63729 15.45496  1.000 25.33153 ? 218 TRP   A CA  1 
ATOM   1672 C  C   . TRP   A 1 218 ? -26.63214 -38.19123 15.28465  1.000 25.10477 ? 218 TRP   A C   1 
ATOM   1673 O  O   . TRP   A 1 218 ? -26.41795 -39.39221 15.49828  1.000 26.37886 ? 218 TRP   A O   1 
ATOM   1674 C  CB  . TRP   A 1 218 ? -28.88569 -37.95245 14.22035  1.000 27.40364 ? 218 TRP   A CB  1 
ATOM   1675 C  CG  . TRP   A 1 218 ? -28.38246 -37.34580 12.92335  1.000 26.25036 ? 218 TRP   A CG  1 
ATOM   1676 C  CD1 . TRP   A 1 218 ? -28.83035 -36.20236 12.31827  1.000 28.36309 ? 218 TRP   A CD1 1 
ATOM   1677 C  CD2 . TRP   A 1 218 ? -27.35810 -37.87242 12.06816  1.000 24.50106 ? 218 TRP   A CD2 1 
ATOM   1678 N  NE1 . TRP   A 1 218 ? -28.13905 -35.98225 11.14630  1.000 27.16072 ? 218 TRP   A NE1 1 
ATOM   1679 C  CE2 . TRP   A 1 218 ? -27.24112 -36.99910 10.96574  1.000 26.06399 ? 218 TRP   A CE2 1 
ATOM   1680 C  CE3 . TRP   A 1 218 ? -26.53757 -39.00463 12.12221  1.000 27.18222 ? 218 TRP   A CE3 1 
ATOM   1681 C  CZ2 . TRP   A 1 218 ? -26.32201 -37.20937 9.93938   1.000 25.37173 ? 218 TRP   A CZ2 1 
ATOM   1682 C  CZ3 . TRP   A 1 218 ? -25.63288 -39.21671 11.10322  1.000 27.37253 ? 218 TRP   A CZ3 1 
ATOM   1683 C  CH2 . TRP   A 1 218 ? -25.53185 -38.31860 10.02168  1.000 27.13782 ? 218 TRP   A CH2 1 
ATOM   1684 N  N   . PHE   A 1 219 ? -25.67796 -37.34457 14.89950  1.000 23.64465 ? 219 PHE   A N   1 
ATOM   1685 C  CA  . PHE   A 1 219 ? -24.30708 -37.74485 14.61868  1.000 23.66498 ? 219 PHE   A CA  1 
ATOM   1686 C  C   . PHE   A 1 219 ? -23.41461 -37.71784 15.85299  1.000 23.82595 ? 219 PHE   A C   1 
ATOM   1687 O  O   . PHE   A 1 219 ? -22.23321 -38.05904 15.75595  1.000 24.58994 ? 219 PHE   A O   1 
ATOM   1688 C  CB  . PHE   A 1 219 ? -23.73382 -36.82994 13.53033  1.000 23.16309 ? 219 PHE   A CB  1 
ATOM   1689 C  CG  . PHE   A 1 219 ? -23.91359 -35.37602 13.82694  1.000 20.56693 ? 219 PHE   A CG  1 
ATOM   1690 C  CD1 . PHE   A 1 219 ? -23.00235 -34.70526 14.62511  1.000 20.16865 ? 219 PHE   A CD1 1 
ATOM   1691 C  CD2 . PHE   A 1 219 ? -25.02106 -34.68228 13.34540  1.000 20.11124 ? 219 PHE   A CD2 1 
ATOM   1692 C  CE1 . PHE   A 1 219 ? -23.16210 -33.35387 14.91033  1.000 20.67552 ? 219 PHE   A CE1 1 
ATOM   1693 C  CE2 . PHE   A 1 219 ? -25.19250 -33.32888 13.63396  1.000 21.19875 ? 219 PHE   A CE2 1 
ATOM   1694 C  CZ  . PHE   A 1 219 ? -24.26321 -32.66428 14.42005  1.000 20.19279 ? 219 PHE   A CZ  1 
ATOM   1695 N  N   . LEU   A 1 220 ? -23.94354 -37.32389 17.00599  1.000 24.39110 ? 220 LEU   A N   1 
ATOM   1696 C  CA  . LEU   A 1 220 ? -23.15381 -37.32060 18.22280  1.000 25.08608 ? 220 LEU   A CA  1 
ATOM   1697 C  C   . LEU   A 1 220 ? -23.01861 -38.74083 18.76651  1.000 26.88536 ? 220 LEU   A C   1 
ATOM   1698 O  O   . LEU   A 1 220 ? -23.81107 -39.62852 18.45602  1.000 27.76775 ? 220 LEU   A O   1 
ATOM   1699 C  CB  . LEU   A 1 220 ? -23.79502 -36.42140 19.27228  1.000 25.31075 ? 220 LEU   A CB  1 
ATOM   1700 C  CG  . LEU   A 1 220 ? -23.86255 -34.94346 18.90660  1.000 23.76352 ? 220 LEU   A CG  1 
ATOM   1701 C  CD1 . LEU   A 1 220 ? -24.56704 -34.22101 20.02836  1.000 24.54715 ? 220 LEU   A CD1 1 
ATOM   1702 C  CD2 . LEU   A 1 220 ? -22.44971 -34.40403 18.67943  1.000 22.74582 ? 220 LEU   A CD2 1 
ATOM   1703 N  N   . ASN   A 1 221 ? -21.99344 -38.94860 19.58515  1.000 27.56337 ? 221 ASN   A N   1 
ATOM   1704 C  CA  . ASN   A 1 221 ? -21.77887 -40.25249 20.19479  1.000 29.44223 ? 221 ASN   A CA  1 
ATOM   1705 C  C   . ASN   A 1 221 ? -21.04820 -40.08239 21.51995  1.000 33.22139 ? 221 ASN   A C   1 
ATOM   1706 O  O   . ASN   A 1 221 ? -20.60784 -38.98532 21.87909  1.000 31.26086 ? 221 ASN   A O   1 
ATOM   1707 C  CB  . ASN   A 1 221 ? -21.02570 -41.18991 19.24014  1.000 35.02136 ? 221 ASN   A CB  1 
ATOM   1708 C  CG  . ASN   A 1 221 ? -19.91270 -40.48786 18.49093  1.000 36.45182 ? 221 ASN   A CG  1 
ATOM   1709 O  OD1 . ASN   A 1 221 ? -20.08244 -40.10050 17.33229  1.000 37.84583 ? 221 ASN   A OD1 1 
ATOM   1710 N  ND2 . ASN   A 1 221 ? -18.76932 -40.30354 19.14905  1.000 37.26665 ? 221 ASN   A ND2 1 
ATOM   1711 N  N   . ARG   A 1 222 ? -20.95964 -41.19332 22.26353  1.000 34.32878 ? 222 ARG   A N   1 
ATOM   1712 C  CA  . ARG   A 1 222 ? -20.26931 -41.21524 23.54585  1.000 36.02448 ? 222 ARG   A CA  1 
ATOM   1713 C  C   . ARG   A 1 222 ? -18.75801 -41.34653 23.40547  1.000 39.56216 ? 222 ARG   A C   1 
ATOM   1714 O  O   . ARG   A 1 222 ? -18.03906 -41.00225 24.34703  1.000 45.62238 ? 222 ARG   A O   1 
ATOM   1715 C  CB  . ARG   A 1 222 ? -20.79141 -42.37138 24.41133  1.000 41.12393 ? 222 ARG   A CB  1 
ATOM   1716 C  CG  . ARG   A 1 222 ? -20.17474 -43.72941 24.04182  1.000 41.18267 ? 222 ARG   A CG  1 
ATOM   1717 C  CD  . ARG   A 1 222 ? -20.88225 -44.89235 24.71247  1.000 39.41002 ? 222 ARG   A CD  1 
ATOM   1718 N  NE  . ARG   A 1 222 ? -20.48491 -45.05226 26.10675  1.000 48.73052 ? 222 ARG   A NE  1 
ATOM   1719 C  CZ  . ARG   A 1 222 ? -20.96619 -45.98285 26.92121  1.000 47.70829 ? 222 ARG   A CZ  1 
ATOM   1720 N  NH1 . ARG   A 1 222 ? -21.88808 -46.84605 26.51977  1.000 49.53695 ? 222 ARG   A NH1 1 
ATOM   1721 N  NH2 . ARG   A 1 222 ? -20.50950 -46.05298 28.17026  1.000 51.32280 ? 222 ARG   A NH2 1 
ATOM   1722 N  N   . PHE   A 1 223 ? -18.26296 -41.83577 22.26830  1.000 40.21839 ? 223 PHE   A N   1 
ATOM   1723 C  CA  . PHE   A 1 223 ? -16.83117 -42.03110 22.09826  1.000 40.62666 ? 223 PHE   A CA  1 
ATOM   1724 C  C   . PHE   A 1 223 ? -16.08888 -40.69980 22.09185  1.000 36.82750 ? 223 PHE   A C   1 
ATOM   1725 O  O   . PHE   A 1 223 ? -16.65022 -39.63026 21.82940  1.000 34.89611 ? 223 PHE   A O   1 
ATOM   1726 C  CB  . PHE   A 1 223 ? -16.50468 -42.76158 20.78978  1.000 42.68477 ? 223 PHE   A CB  1 
ATOM   1727 C  CG  . PHE   A 1 223 ? -17.60245 -43.64626 20.28039  1.000 43.29965 ? 223 PHE   A CG  1 
ATOM   1728 C  CD1 . PHE   A 1 223 ? -18.02099 -44.75060 21.00766  1.000 45.61139 ? 223 PHE   A CD1 1 
ATOM   1729 C  CD2 . PHE   A 1 223 ? -18.20396 -43.38244 19.05931  1.000 43.77207 ? 223 PHE   A CD2 1 
ATOM   1730 C  CE1 . PHE   A 1 223 ? -19.03100 -45.57303 20.53062  1.000 48.50939 ? 223 PHE   A CE1 1 
ATOM   1731 C  CE2 . PHE   A 1 223 ? -19.21753 -44.19307 18.57872  1.000 48.09702 ? 223 PHE   A CE2 1 
ATOM   1732 C  CZ  . PHE   A 1 223 ? -19.63298 -45.28725 19.31196  1.000 50.48137 ? 223 PHE   A CZ  1 
ATOM   1733 N  N   . THR   A 1 224 ? -14.79595 -40.78635 22.37585  1.000 37.63772 ? 224 THR   A N   1 
ATOM   1734 C  CA  . THR   A 1 224 ? -13.85935 -39.70197 22.14340  1.000 37.23669 ? 224 THR   A CA  1 
ATOM   1735 C  C   . THR   A 1 224 ? -12.69324 -40.24508 21.32834  1.000 35.89608 ? 224 THR   A C   1 
ATOM   1736 O  O   . THR   A 1 224 ? -12.63087 -41.43596 21.00702  1.000 38.49567 ? 224 THR   A O   1 
ATOM   1737 C  CB  . THR   A 1 224 ? -13.37956 -39.07715 23.46092  1.000 37.82933 ? 224 THR   A CB  1 
ATOM   1738 O  OG1 . THR   A 1 224 ? -12.88586 -37.75103 23.21201  1.000 35.67560 ? 224 THR   A OG1 1 
ATOM   1739 C  CG2 . THR   A 1 224 ? -12.29737 -39.93629 24.11397  1.000 36.66973 ? 224 THR   A CG2 1 
ATOM   1740 N  N   . THR   A 1 225 ? -11.76819 -39.35587 20.98839  1.000 32.74014 ? 225 THR   A N   1 
ATOM   1741 C  CA  . THR   A 1 225 ? -10.55910 -39.72910 20.27239  1.000 35.70371 ? 225 THR   A CA  1 
ATOM   1742 C  C   . THR   A 1 225 ? -9.44297  -38.78714 20.69610  1.000 32.59147 ? 225 THR   A C   1 
ATOM   1743 O  O   . THR   A 1 225 ? -9.68683  -37.72659 21.27596  1.000 36.58129 ? 225 THR   A O   1 
ATOM   1744 C  CB  . THR   A 1 225 ? -10.76621 -39.68398 18.74739  1.000 37.91475 ? 225 THR   A CB  1 
ATOM   1745 O  OG1 . THR   A 1 225 ? -9.64752  -40.29081 18.08688  1.000 40.66104 ? 225 THR   A OG1 1 
ATOM   1746 C  CG2 . THR   A 1 225 ? -10.93215 -38.25413 18.26242  1.000 32.88452 ? 225 THR   A CG2 1 
ATOM   1747 N  N   . THR   A 1 226 ? -8.20886  -39.19250 20.42568  1.000 33.03499 ? 226 THR   A N   1 
ATOM   1748 C  CA  . THR   A 1 226 ? -7.08954  -38.28674 20.62339  1.000 37.82903 ? 226 THR   A CA  1 
ATOM   1749 C  C   . THR   A 1 226 ? -6.86284  -37.46462 19.35929  1.000 30.28023 ? 226 THR   A C   1 
ATOM   1750 O  O   . THR   A 1 226 ? -7.30697  -37.82953 18.26732  1.000 31.92457 ? 226 THR   A O   1 
ATOM   1751 C  CB  . THR   A 1 226 ? -5.81508  -39.04852 20.99048  1.000 35.83917 ? 226 THR   A CB  1 
ATOM   1752 O  OG1 . THR   A 1 226 ? -5.31236  -39.72104 19.83159  1.000 41.24920 ? 226 THR   A OG1 1 
ATOM   1753 C  CG2 . THR   A 1 226 ? -6.07757  -40.06350 22.11076  1.000 37.79439 ? 226 THR   A CG2 1 
ATOM   1754 N  N   . LEU   A 1 227 ? -6.16658  -36.33589 19.52800  1.000 32.00770 ? 227 LEU   A N   1 
ATOM   1755 C  CA  . LEU   A 1 227 ? -5.82819  -35.47951 18.39409  1.000 30.63854 ? 227 LEU   A CA  1 
ATOM   1756 C  C   . LEU   A 1 227 ? -5.00879  -36.23026 17.34880  1.000 32.35635 ? 227 LEU   A C   1 
ATOM   1757 O  O   . LEU   A 1 227 ? -5.29765  -36.15372 16.14850  1.000 27.77755 ? 227 LEU   A O   1 
ATOM   1758 C  CB  . LEU   A 1 227 ? -5.08488  -34.23212 18.88239  1.000 34.26481 ? 227 LEU   A CB  1 
ATOM   1759 C  CG  . LEU   A 1 227 ? -4.96781  -33.03593 17.93325  1.000 33.14296 ? 227 LEU   A CG  1 
ATOM   1760 C  CD1 . LEU   A 1 227 ? -6.33895  -32.53978 17.46446  1.000 30.35402 ? 227 LEU   A CD1 1 
ATOM   1761 C  CD2 . LEU   A 1 227 ? -4.21605  -31.90274 18.60998  1.000 31.16595 ? 227 LEU   A CD2 1 
ATOM   1762 N  N   . ASN   A 1 228 ? -3.97269  -36.95790 17.78049  1.000 35.48132 ? 228 ASN   A N   1 
ATOM   1763 C  CA  . ASN   A 1 228 ? -3.18414  -37.73339 16.82298  1.000 37.27301 ? 228 ASN   A CA  1 
ATOM   1764 C  C   . ASN   A 1 228 ? -4.03238  -38.79161 16.12989  1.000 34.90638 ? 228 ASN   A C   1 
ATOM   1765 O  O   . ASN   A 1 228 ? -3.92349  -38.98805 14.91368  1.000 34.90248 ? 228 ASN   A O   1 
ATOM   1766 C  CB  . ASN   A 1 228 ? -1.97976  -38.37831 17.51022  1.000 36.98509 ? 228 ASN   A CB  1 
ATOM   1767 C  CG  . ASN   A 1 228 ? -1.14892  -37.37581 18.28491  1.000 41.88375 ? 228 ASN   A CG  1 
ATOM   1768 O  OD1 . ASN   A 1 228 ? -1.03246  -36.21004 17.88911  1.000 44.37480 ? 228 ASN   A OD1 1 
ATOM   1769 N  ND2 . ASN   A 1 228 ? -0.55187  -37.82360 19.38593  1.000 43.91722 ? 228 ASN   A ND2 1 
ATOM   1770 N  N   . ASP   A 1 229 ? -4.89386  -39.47543 16.87927  1.000 35.16872 ? 229 ASP   A N   1 
ATOM   1771 C  CA  . ASP   A 1 229 ? -5.70548  -40.51853 16.26299  1.000 36.05539 ? 229 ASP   A CA  1 
ATOM   1772 C  C   . ASP   A 1 229 ? -6.68608  -39.92862 15.24794  1.000 37.06717 ? 229 ASP   A C   1 
ATOM   1773 O  O   . ASP   A 1 229 ? -6.86558  -40.48130 14.15375  1.000 38.32939 ? 229 ASP   A O   1 
ATOM   1774 C  CB  . ASP   A 1 229 ? -6.43127  -41.31554 17.34686  1.000 38.80038 ? 229 ASP   A CB  1 
ATOM   1775 C  CG  . ASP   A 1 229 ? -5.61720  -42.50696 17.83699  1.000 42.59883 ? 229 ASP   A CG  1 
ATOM   1776 O  OD1 . ASP   A 1 229 ? -4.48206  -42.70414 17.34899  1.000 45.96129 ? 229 ASP   A OD1 1 
ATOM   1777 O  OD2 . ASP   A 1 229 ? -6.10639  -43.24409 18.71818  1.000 47.93361 ? 229 ASP   A OD2 1 
ATOM   1778 N  N   . PHE   A 1 230 ? -7.31386  -38.79466 15.57366  1.000 31.61955 ? 230 PHE   A N   1 
ATOM   1779 C  CA  . PHE   A 1 230 ? -8.16946  -38.14062 14.58715  1.000 31.89622 ? 230 PHE   A CA  1 
ATOM   1780 C  C   . PHE   A 1 230 ? -7.38195  -37.73422 13.34687  1.000 30.45060 ? 230 PHE   A C   1 
ATOM   1781 O  O   . PHE   A 1 230 ? -7.87640  -37.86173 12.22126  1.000 31.09309 ? 230 PHE   A O   1 
ATOM   1782 C  CB  . PHE   A 1 230 ? -8.85562  -36.91248 15.17931  1.000 27.96195 ? 230 PHE   A CB  1 
ATOM   1783 C  CG  . PHE   A 1 230 ? -9.63267  -36.12838 14.16099  1.000 24.94787 ? 230 PHE   A CG  1 
ATOM   1784 C  CD1 . PHE   A 1 230 ? -10.88836 -36.55630 13.75523  1.000 24.54198 ? 230 PHE   A CD1 1 
ATOM   1785 C  CD2 . PHE   A 1 230 ? -9.09511  -34.99891 13.57089  1.000 25.15297 ? 230 PHE   A CD2 1 
ATOM   1786 C  CE1 . PHE   A 1 230 ? -11.59835 -35.85473 12.80420  1.000 24.24521 ? 230 PHE   A CE1 1 
ATOM   1787 C  CE2 . PHE   A 1 230 ? -9.81057  -34.29790 12.61355  1.000 25.76899 ? 230 PHE   A CE2 1 
ATOM   1788 C  CZ  . PHE   A 1 230 ? -11.06349 -34.72801 12.24066  1.000 24.23350 ? 230 PHE   A CZ  1 
ATOM   1789 N  N   . ASN   A 1 231 ? -6.16127  -37.22583 13.52844  1.000 31.80758 ? 231 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 231 ? -5.42717  -36.70253 12.37799  1.000 32.31065 ? 231 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 231 ? -4.98689  -37.81810 11.43774  1.000 32.82081 ? 231 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 231 ? -4.81294  -37.57894 10.23605  1.000 30.23357 ? 231 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 231 ? -4.22890  -35.87158 12.83714  1.000 28.05618 ? 231 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 231 ? -4.60874  -34.44290 13.15016  1.000 29.23663 ? 231 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 231 ? -5.37777  -33.83402 12.42145  1.000 33.05957 ? 231 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 231 ? -4.06276  -33.89607 14.22830  1.000 33.26005 ? 231 ASN   A ND2 1 
ATOM   1797 N  N   . LEU   A 1 232 ? -4.81931  -39.03829 11.95777  1.000 33.39883 ? 232 LEU   A N   1 
ATOM   1798 C  CA  . LEU   A 1 232 ? -4.60185  -40.18490 11.08244  1.000 35.34282 ? 232 LEU   A CA  1 
ATOM   1799 C  C   . LEU   A 1 232 ? -5.79006  -40.39301 10.15651  1.000 35.25561 ? 232 LEU   A C   1 
ATOM   1800 O  O   . LEU   A 1 232 ? -5.61699  -40.70022 8.97075   1.000 36.12687 ? 232 LEU   A O   1 
ATOM   1801 C  CB  . LEU   A 1 232 ? -4.34342  -41.44576 11.90979  1.000 35.69170 ? 232 LEU   A CB  1 
ATOM   1802 C  CG  . LEU   A 1 232 ? -3.08773  -41.48445 12.78745  1.000 39.92918 ? 232 LEU   A CG  1 
ATOM   1803 C  CD1 . LEU   A 1 232 ? -2.99952  -42.80548 13.53253  1.000 40.62646 ? 232 LEU   A CD1 1 
ATOM   1804 C  CD2 . LEU   A 1 232 ? -1.82920  -41.26516 11.95174  1.000 38.07821 ? 232 LEU   A CD2 1 
ATOM   1805 N  N   . VAL   A 1 233 ? -7.00830  -40.22080 10.67759  1.000 31.50622 ? 233 VAL   A N   1 
ATOM   1806 C  CA  . VAL   A 1 233 ? -8.19613  -40.40601 9.85042   1.000 35.09927 ? 233 VAL   A CA  1 
ATOM   1807 C  C   . VAL   A 1 233 ? -8.34252  -39.25990 8.85901   1.000 34.52336 ? 233 VAL   A C   1 
ATOM   1808 O  O   . VAL   A 1 233 ? -8.67752  -39.47379 7.68584   1.000 33.26683 ? 233 VAL   A O   1 
ATOM   1809 C  CB  . VAL   A 1 233 ? -9.44399  -40.55747 10.74082  1.000 36.30692 ? 233 VAL   A CB  1 
ATOM   1810 C  CG1 . VAL   A 1 233 ? -10.72176 -40.18680 9.97392   1.000 33.84361 ? 233 VAL   A CG1 1 
ATOM   1811 C  CG2 . VAL   A 1 233 ? -9.52483  -41.96820 11.29076  1.000 36.83610 ? 233 VAL   A CG2 1 
ATOM   1812 N  N   . ALA   A 1 234 ? -8.09816  -38.02595 9.31376   1.000 33.26183 ? 234 ALA   A N   1 
ATOM   1813 C  CA  . ALA   A 1 234 ? -8.21280  -36.86723 8.43639   1.000 31.34872 ? 234 ALA   A CA  1 
ATOM   1814 C  C   . ALA   A 1 234 ? -7.30653  -37.00231 7.22189   1.000 30.72763 ? 234 ALA   A C   1 
ATOM   1815 O  O   . ALA   A 1 234 ? -7.70859  -36.67993 6.09812   1.000 29.79763 ? 234 ALA   A O   1 
ATOM   1816 C  CB  . ALA   A 1 234 ? -7.88157  -35.59158 9.21266   1.000 30.30790 ? 234 ALA   A CB  1 
ATOM   1817 N  N   . MET   A 1 235 ? -6.07471  -37.46884 7.43044   1.000 32.03218 ? 235 MET   A N   1 
ATOM   1818 C  CA  . MET   A 1 235 ? -5.15758  -37.64338 6.31127   1.000 34.11800 ? 235 MET   A CA  1 
ATOM   1819 C  C   . MET   A 1 235 ? -5.72358  -38.62774 5.29170   1.000 33.47795 ? 235 MET   A C   1 
ATOM   1820 O  O   . MET   A 1 235 ? -5.64342  -38.39221 4.07868   1.000 34.18029 ? 235 MET   A O   1 
ATOM   1821 C  CB  . MET   A 1 235 ? -3.79591  -38.10516 6.83117   1.000 35.04254 ? 235 MET   A CB  1 
ATOM   1822 C  CG  . MET   A 1 235 ? -2.74931  -38.33805 5.75520   1.000 39.95576 ? 235 MET   A CG  1 
ATOM   1823 S  SD  . MET   A 1 235 ? -1.05885  -38.29472 6.40038   1.000 53.41346 ? 235 MET   A SD  1 
ATOM   1824 C  CE  . MET   A 1 235 ? -1.25276  -37.29060 7.87610   1.000 41.33166 ? 235 MET   A CE  1 
ATOM   1825 N  N   . LYS   A 1 236 ? -6.34221  -39.71419 5.76870   1.000 36.02686 ? 236 LYS   A N   1 
ATOM   1826 C  CA  . LYS   A 1 236 ? -6.85485  -40.73820 4.86531   1.000 31.24157 ? 236 LYS   A CA  1 
ATOM   1827 C  C   . LYS   A 1 236 ? -7.97635  -40.21163 3.98083   1.000 30.53384 ? 236 LYS   A C   1 
ATOM   1828 O  O   . LYS   A 1 236 ? -8.09256  -40.63340 2.82564   1.000 32.78943 ? 236 LYS   A O   1 
ATOM   1829 C  CB  . LYS   A 1 236 ? -7.32834  -41.95598 5.66391   1.000 35.30375 ? 236 LYS   A CB  1 
ATOM   1830 C  CG  . LYS   A 1 236 ? -8.11150  -42.97420 4.84347   1.000 37.26152 ? 236 LYS   A CG  1 
ATOM   1831 C  CD  . LYS   A 1 236 ? -8.43949  -44.23001 5.64838   1.000 38.75411 ? 236 LYS   A CD  1 
ATOM   1832 C  CE  . LYS   A 1 236 ? -9.55272  -45.04095 4.98118   1.000 43.74699 ? 236 LYS   A CE  1 
ATOM   1833 N  NZ  . LYS   A 1 236 ? -9.24989  -45.33908 3.54422   1.000 47.27763 ? 236 LYS   A NZ  1 
ATOM   1834 N  N   . TYR   A 1 237 ? -8.79368  -39.28037 4.48259   1.000 29.44663 ? 237 TYR   A N   1 
ATOM   1835 C  CA  . TYR   A 1 237 ? -9.92607  -38.74643 3.73356   1.000 27.45363 ? 237 TYR   A CA  1 
ATOM   1836 C  C   . TYR   A 1 237 ? -9.65389  -37.37453 3.12353   1.000 24.14655 ? 237 TYR   A C   1 
ATOM   1837 O  O   . TYR   A 1 237 ? -10.60111 -36.66418 2.76894   1.000 24.68236 ? 237 TYR   A O   1 
ATOM   1838 C  CB  . TYR   A 1 237 ? -11.16754 -38.68430 4.61899   1.000 27.77892 ? 237 TYR   A CB  1 
ATOM   1839 C  CG  . TYR   A 1 237 ? -11.69947 -40.05308 4.94296   1.000 29.49439 ? 237 TYR   A CG  1 
ATOM   1840 C  CD1 . TYR   A 1 237 ? -11.18960 -40.78173 6.00833   1.000 32.16747 ? 237 TYR   A CD1 1 
ATOM   1841 C  CD2 . TYR   A 1 237 ? -12.69709 -40.62944 4.16666   1.000 30.16719 ? 237 TYR   A CD2 1 
ATOM   1842 C  CE1 . TYR   A 1 237 ? -11.66447 -42.04586 6.29893   1.000 31.98465 ? 237 TYR   A CE1 1 
ATOM   1843 C  CE2 . TYR   A 1 237 ? -13.17435 -41.89210 4.44822   1.000 30.65286 ? 237 TYR   A CE2 1 
ATOM   1844 C  CZ  . TYR   A 1 237 ? -12.65724 -42.59204 5.51759   1.000 32.83410 ? 237 TYR   A CZ  1 
ATOM   1845 O  OH  . TYR   A 1 237 ? -13.13182 -43.84985 5.80516   1.000 37.05764 ? 237 TYR   A OH  1 
ATOM   1846 N  N   . ASN   A 1 238 ? -8.38568  -36.99723 2.97662   1.000 25.55162 ? 238 ASN   A N   1 
ATOM   1847 C  CA  . ASN   A 1 238 ? -8.02238  -35.74591 2.31391   1.000 25.16494 ? 238 ASN   A CA  1 
ATOM   1848 C  C   . ASN   A 1 238 ? -8.53704  -34.52756 3.08651   1.000 22.13654 ? 238 ASN   A C   1 
ATOM   1849 O  O   . ASN   A 1 238 ? -8.89803  -33.50450 2.50025   1.000 24.25157 ? 238 ASN   A O   1 
ATOM   1850 C  CB  . ASN   A 1 238 ? -8.53193  -35.71718 0.87085   1.000 25.75165 ? 238 ASN   A CB  1 
ATOM   1851 C  CG  . ASN   A 1 238 ? -7.79800  -34.70773 0.02546   1.000 28.26663 ? 238 ASN   A CG  1 
ATOM   1852 O  OD1 . ASN   A 1 238 ? -8.31691  -34.20716 -0.97836  1.000 32.38067 ? 238 ASN   A OD1 1 
ATOM   1853 N  ND2 . ASN   A 1 238 ? -6.57221  -34.41132 0.42069   1.000 29.48870 ? 238 ASN   A ND2 1 
ATOM   1854 N  N   . TYR   A 1 239 ? -8.56736  -34.62931 4.40853   1.000 22.87154 ? 239 TYR   A N   1 
ATOM   1855 C  CA  . TYR   A 1 239 ? -8.86319  -33.50913 5.28615   1.000 23.57669 ? 239 TYR   A CA  1 
ATOM   1856 C  C   . TYR   A 1 239 ? -7.54604  -32.94161 5.79799   1.000 23.31030 ? 239 TYR   A C   1 
ATOM   1857 O  O   . TYR   A 1 239 ? -6.56617  -33.66990 5.97836   1.000 23.86050 ? 239 TYR   A O   1 
ATOM   1858 C  CB  . TYR   A 1 239 ? -9.73562  -33.94328 6.47024   1.000 21.41298 ? 239 TYR   A CB  1 
ATOM   1859 C  CG  . TYR   A 1 239 ? -11.23123 -33.92455 6.24620   1.000 20.41896 ? 239 TYR   A CG  1 
ATOM   1860 C  CD1 . TYR   A 1 239 ? -11.81632 -34.58479 5.16625   1.000 21.94157 ? 239 TYR   A CD1 1 
ATOM   1861 C  CD2 . TYR   A 1 239 ? -12.06072 -33.25674 7.13675   1.000 18.66931 ? 239 TYR   A CD2 1 
ATOM   1862 C  CE1 . TYR   A 1 239 ? -13.20513 -34.56385 4.97259   1.000 21.81848 ? 239 TYR   A CE1 1 
ATOM   1863 C  CE2 . TYR   A 1 239 ? -13.44498 -33.23634 6.96158   1.000 18.36322 ? 239 TYR   A CE2 1 
ATOM   1864 C  CZ  . TYR   A 1 239 ? -14.00869 -33.89038 5.87942   1.000 19.74671 ? 239 TYR   A CZ  1 
ATOM   1865 O  OH  . TYR   A 1 239 ? -15.37723 -33.86594 5.71038   1.000 20.03293 ? 239 TYR   A OH  1 
ATOM   1866 N  N   . GLU   A 1 240 ? -7.52153  -31.65177 6.02525   1.000 22.67827 ? 240 GLU   A N   1 
ATOM   1867 C  CA  . GLU   A 1 240 ? -6.20960  -31.20105 6.45681   1.000 26.52125 ? 240 GLU   A CA  1 
ATOM   1868 C  C   . GLU   A 1 240 ? -6.05451  -31.37458 7.96377   1.000 25.61835 ? 240 GLU   A C   1 
ATOM   1869 O  O   . GLU   A 1 240 ? -7.02342  -31.67237 8.67055   1.000 23.04159 ? 240 GLU   A O   1 
ATOM   1870 C  CB  . GLU   A 1 240 ? -5.98538  -29.76547 6.00101   1.000 31.06860 ? 240 GLU   A CB  1 
ATOM   1871 C  CG  . GLU   A 1 240 ? -6.89245  -28.76433 6.55714   1.000 25.62824 ? 240 GLU   A CG  1 
ATOM   1872 C  CD  . GLU   A 1 240 ? -6.77131  -27.44260 5.82832   1.000 28.94314 ? 240 GLU   A CD  1 
ATOM   1873 O  OE1 . GLU   A 1 240 ? -5.77677  -27.24547 5.08377   1.000 36.49054 ? 240 GLU   A OE1 1 
ATOM   1874 O  OE2 . GLU   A 1 240 ? -7.68956  -26.60335 5.99020   1.000 29.48372 ? 240 GLU   A OE2 1 
ATOM   1875 N  N   . PRO   A 1 241 ? -4.82846  -31.33554 8.48209   1.000 26.65755 ? 241 PRO   A N   1 
ATOM   1876 C  CA  . PRO   A 1 241 ? -4.64627  -31.64449 9.90253   1.000 24.30301 ? 241 PRO   A CA  1 
ATOM   1877 C  C   . PRO   A 1 241 ? -5.32448  -30.61675 10.79583  1.000 23.66349 ? 241 PRO   A C   1 
ATOM   1878 O  O   . PRO   A 1 241 ? -5.48598  -29.44424 10.44168  1.000 27.82380 ? 241 PRO   A O   1 
ATOM   1879 C  CB  . PRO   A 1 241 ? -3.12254  -31.63738 10.09792  1.000 28.12858 ? 241 PRO   A CB  1 
ATOM   1880 C  CG  . PRO   A 1 241 ? -2.52280  -31.29203 8.78829   1.000 32.44910 ? 241 PRO   A CG  1 
ATOM   1881 C  CD  . PRO   A 1 241 ? -3.56176  -31.33018 7.73107   1.000 29.52634 ? 241 PRO   A CD  1 
ATOM   1882 N  N   . LEU   A 1 242 ? -5.77268  -31.09525 11.95412  1.000 26.26134 ? 242 LEU   A N   1 
ATOM   1883 C  CA  . LEU   A 1 242 ? -6.29732  -30.23996 13.00959  1.000 27.84476 ? 242 LEU   A CA  1 
ATOM   1884 C  C   . LEU   A 1 242 ? -5.17978  -29.95395 14.00139  1.000 26.37240 ? 242 LEU   A C   1 
ATOM   1885 O  O   . LEU   A 1 242 ? -4.46847  -30.87124 14.41224  1.000 25.92044 ? 242 LEU   A O   1 
ATOM   1886 C  CB  . LEU   A 1 242 ? -7.47001  -30.91340 13.72702  1.000 25.62663 ? 242 LEU   A CB  1 
ATOM   1887 C  CG  . LEU   A 1 242 ? -8.42926  -30.00730 14.50041  1.000 22.82734 ? 242 LEU   A CG  1 
ATOM   1888 C  CD1 . LEU   A 1 242 ? -9.25620  -29.15495 13.55133  1.000 23.34384 ? 242 LEU   A CD1 1 
ATOM   1889 C  CD2 . LEU   A 1 242 ? -9.30529  -30.85400 15.40524  1.000 22.91878 ? 242 LEU   A CD2 1 
ATOM   1890 N  N   . THR   A 1 243 ? -5.02678  -28.68937 14.37641  1.000 24.47227 ? 243 THR   A N   1 
ATOM   1891 C  CA  . THR   A 1 243 ? -3.98388  -28.28267 15.30626  1.000 27.90448 ? 243 THR   A CA  1 
ATOM   1892 C  C   . THR   A 1 243 ? -4.58035  -27.95819 16.66711  1.000 26.22529 ? 243 THR   A C   1 
ATOM   1893 O  O   . THR   A 1 243 ? -5.79796  -27.80494 16.82786  1.000 26.38197 ? 243 THR   A O   1 
ATOM   1894 C  CB  . THR   A 1 243 ? -3.22043  -27.06592 14.77690  1.000 26.54889 ? 243 THR   A CB  1 
ATOM   1895 O  OG1 . THR   A 1 243 ? -4.08083  -25.92151 14.80319  1.000 23.44731 ? 243 THR   A OG1 1 
ATOM   1896 C  CG2 . THR   A 1 243 ? -2.74531  -27.31443 13.35782  1.000 27.88614 ? 243 THR   A CG2 1 
ATOM   1897 N  N   . GLN   A 1 244 ? -3.69345  -27.82672 17.65553  1.000 25.65023 ? 244 GLN   A N   1 
ATOM   1898 C  CA  . GLN   A 1 244 ? -4.13911  -27.38612 18.97069  1.000 26.66439 ? 244 GLN   A CA  1 
ATOM   1899 C  C   . GLN   A 1 244 ? -4.70883  -25.97408 18.91916  1.000 25.43755 ? 244 GLN   A C   1 
ATOM   1900 O  O   . GLN   A 1 244 ? -5.61551  -25.64333 19.69522  1.000 27.30921 ? 244 GLN   A O   1 
ATOM   1901 C  CB  . GLN   A 1 244 ? -2.99144  -27.46448 19.97765  1.000 27.48855 ? 244 GLN   A CB  1 
ATOM   1902 C  CG  . GLN   A 1 244 ? -3.43076  -27.17677 21.40841  1.000 30.35437 ? 244 GLN   A CG  1 
ATOM   1903 C  CD  . GLN   A 1 244 ? -4.55114  -28.08926 21.86248  1.000 32.01255 ? 244 GLN   A CD  1 
ATOM   1904 O  OE1 . GLN   A 1 244 ? -4.53633  -29.29138 21.59368  1.000 33.64884 ? 244 GLN   A OE1 1 
ATOM   1905 N  NE2 . GLN   A 1 244 ? -5.54140  -27.51817 22.54194  1.000 34.44445 ? 244 GLN   A NE2 1 
ATOM   1906 N  N   . ASP   A 1 245 ? -4.20235  -25.12689 18.01426  1.000 26.13028 ? 245 ASP   A N   1 
ATOM   1907 C  CA  . ASP   A 1 245 ? -4.81237  -23.81119 17.84138  1.000 24.10867 ? 245 ASP   A CA  1 
ATOM   1908 C  C   . ASP   A 1 245 ? -6.24562  -23.93687 17.33775  1.000 23.48553 ? 245 ASP   A C   1 
ATOM   1909 O  O   . ASP   A 1 245 ? -7.13391  -23.21098 17.79681  1.000 26.53652 ? 245 ASP   A O   1 
ATOM   1910 C  CB  . ASP   A 1 245 ? -3.99548  -22.93929 16.88326  1.000 27.40094 ? 245 ASP   A CB  1 
ATOM   1911 C  CG  . ASP   A 1 245 ? -4.41146  -21.46470 16.94255  1.000 32.75607 ? 245 ASP   A CG  1 
ATOM   1912 O  OD1 . ASP   A 1 245 ? -4.73941  -20.99082 18.05317  1.000 36.21333 ? 245 ASP   A OD1 1 
ATOM   1913 O  OD2 . ASP   A 1 245 ? -4.43162  -20.78208 15.89062  1.000 38.47530 ? 245 ASP   A OD2 1 
ATOM   1914 N  N   . HIS   A 1 246 ? -6.48637  -24.84439 16.38701  1.000 23.30097 ? 246 HIS   A N   1 
ATOM   1915 C  CA  . HIS   A 1 246 ? -7.85780  -25.11819 15.95474  1.000 23.92412 ? 246 HIS   A CA  1 
ATOM   1916 C  C   . HIS   A 1 246 ? -8.72926  -25.54515 17.12723  1.000 23.73416 ? 246 HIS   A C   1 
ATOM   1917 O  O   . HIS   A 1 246 ? -9.87140  -25.08647 17.27090  1.000 23.19135 ? 246 HIS   A O   1 
ATOM   1918 C  CB  . HIS   A 1 246 ? -7.87906  -26.20784 14.88525  1.000 23.05387 ? 246 HIS   A CB  1 
ATOM   1919 C  CG  . HIS   A 1 246 ? -7.26369  -25.81015 13.58158  1.000 22.46843 ? 246 HIS   A CG  1 
ATOM   1920 N  ND1 . HIS   A 1 246 ? -6.60057  -26.70887 12.77196  1.000 23.61000 ? 246 HIS   A ND1 1 
ATOM   1921 C  CD2 . HIS   A 1 246 ? -7.22458  -24.62036 12.93744  1.000 23.96537 ? 246 HIS   A CD2 1 
ATOM   1922 C  CE1 . HIS   A 1 246 ? -6.18826  -26.09015 11.67940  1.000 25.63194 ? 246 HIS   A CE1 1 
ATOM   1923 N  NE2 . HIS   A 1 246 ? -6.55346  -24.82152 11.75447  1.000 25.50579 ? 246 HIS   A NE2 1 
ATOM   1924 N  N   . VAL   A 1 247 ? -8.22245  -26.46103 17.95188  1.000 24.33591 ? 247 VAL   A N   1 
ATOM   1925 C  CA  . VAL   A 1 247 ? -8.97462  -26.89344 19.12664  1.000 22.42680 ? 247 VAL   A CA  1 
ATOM   1926 C  C   . VAL   A 1 247 ? -9.28306  -25.69652 20.01553  1.000 23.42027 ? 247 VAL   A C   1 
ATOM   1927 O  O   . VAL   A 1 247 ? -10.42528 -25.50365 20.45883  1.000 25.06401 ? 247 VAL   A O   1 
ATOM   1928 C  CB  . VAL   A 1 247 ? -8.20308  -27.98962 19.88181  1.000 26.67282 ? 247 VAL   A CB  1 
ATOM   1929 C  CG1 . VAL   A 1 247 ? -8.84837  -28.26374 21.22824  1.000 27.88771 ? 247 VAL   A CG1 1 
ATOM   1930 C  CG2 . VAL   A 1 247 ? -8.14040  -29.25381 19.04067  1.000 26.93940 ? 247 VAL   A CG2 1 
ATOM   1931 N  N   . ASP   A 1 248 ? -8.27516  -24.85055 20.25476  1.000 23.65099 ? 248 ASP   A N   1 
ATOM   1932 C  CA  . ASP   A 1 248 ? -8.49138  -23.65643 21.06469  1.000 29.31754 ? 248 ASP   A CA  1 
ATOM   1933 C  C   . ASP   A 1 248 ? -9.54917  -22.75223 20.44000  1.000 24.16983 ? 248 ASP   A C   1 
ATOM   1934 O  O   . ASP   A 1 248 ? -10.45284 -22.27028 21.13476  1.000 27.40316 ? 248 ASP   A O   1 
ATOM   1935 C  CB  . ASP   A 1 248 ? -7.17127  -22.89658 21.25289  1.000 28.82160 ? 248 ASP   A CB  1 
ATOM   1936 C  CG  . ASP   A 1 248 ? -6.13639  -23.68677 22.05837  1.000 30.44611 ? 248 ASP   A CG  1 
ATOM   1937 O  OD1 . ASP   A 1 248 ? -6.50391  -24.64311 22.77880  1.000 32.30795 ? 248 ASP   A OD1 1 
ATOM   1938 O  OD2 . ASP   A 1 248 ? -4.93197  -23.34383 21.97254  1.000 29.39437 ? 248 ASP   A OD2 1 
ATOM   1939 N  N   . ILE   A 1 249 ? -9.46486  -22.52298 19.12452  1.000 25.63997 ? 249 ILE   A N   1 
ATOM   1940 C  CA  . ILE   A 1 249 ? -10.43331 -21.66303 18.44387  1.000 23.82881 ? 249 ILE   A CA  1 
ATOM   1941 C  C   . ILE   A 1 249 ? -11.85114 -22.21153 18.57486  1.000 23.82600 ? 249 ILE   A C   1 
ATOM   1942 O  O   . ILE   A 1 249 ? -12.81446 -21.44182 18.67246  1.000 25.89068 ? 249 ILE   A O   1 
ATOM   1943 C  CB  . ILE   A 1 249 ? -10.01814 -21.47481 16.96713  1.000 22.20875 ? 249 ILE   A CB  1 
ATOM   1944 C  CG1 . ILE   A 1 249 ? -8.79525  -20.56170 16.87716  1.000 27.99394 ? 249 ILE   A CG1 1 
ATOM   1945 C  CG2 . ILE   A 1 249 ? -11.15095 -20.93357 16.12326  1.000 24.32174 ? 249 ILE   A CG2 1 
ATOM   1946 C  CD1 . ILE   A 1 249 ? -7.96336  -20.79655 15.62437  1.000 27.47620 ? 249 ILE   A CD1 1 
ATOM   1947 N  N   . LEU   A 1 250 ? -12.00229 -23.53563 18.62678  1.000 23.08619 ? 250 LEU   A N   1 
ATOM   1948 C  CA  . LEU   A 1 250 ? -13.31455 -24.15550 18.79267  1.000 22.78699 ? 250 LEU   A CA  1 
ATOM   1949 C  C   . LEU   A 1 250 ? -13.79546 -24.15423 20.24003  1.000 23.81559 ? 250 LEU   A C   1 
ATOM   1950 O  O   . LEU   A 1 250 ? -14.90455 -24.63495 20.50784  1.000 24.79665 ? 250 LEU   A O   1 
ATOM   1951 C  CB  . LEU   A 1 250 ? -13.27852 -25.58923 18.25393  1.000 21.10680 ? 250 LEU   A CB  1 
ATOM   1952 C  CG  . LEU   A 1 250 ? -13.09257 -25.69176 16.73299  1.000 16.98942 ? 250 LEU   A CG  1 
ATOM   1953 C  CD1 . LEU   A 1 250 ? -12.77463 -27.14198 16.33046  1.000 17.61233 ? 250 LEU   A CD1 1 
ATOM   1954 C  CD2 . LEU   A 1 250 ? -14.34493 -25.19664 16.01141  1.000 20.09343 ? 250 LEU   A CD2 1 
ATOM   1955 N  N   . GLY   A 1 251 ? -12.99653 -23.62489 21.16710  1.000 27.56712 ? 251 GLY   A N   1 
ATOM   1956 C  CA  . GLY   A 1 251 ? -13.32322 -23.61980 22.57738  1.000 27.26682 ? 251 GLY   A CA  1 
ATOM   1957 C  C   . GLY   A 1 251 ? -14.68821 -23.04696 22.91995  1.000 26.29638 ? 251 GLY   A C   1 
ATOM   1958 O  O   . GLY   A 1 251 ? -15.48835 -23.68208 23.61533  1.000 28.47013 ? 251 GLY   A O   1 
ATOM   1959 N  N   . PRO   A 1 252 ? -14.96665 -21.81592 22.47679  1.000 26.63543 ? 252 PRO   A N   1 
ATOM   1960 C  CA  . PRO   A 1 252 ? -16.28855 -21.22682 22.77132  1.000 28.09626 ? 252 PRO   A CA  1 
ATOM   1961 C  C   . PRO   A 1 252 ? -17.45797 -22.06910 22.29102  1.000 26.69550 ? 252 PRO   A C   1 
ATOM   1962 O  O   . PRO   A 1 252 ? -18.43171 -22.25364 23.03654  1.000 27.28888 ? 252 PRO   A O   1 
ATOM   1963 C  CB  . PRO   A 1 252 ? -16.21920 -19.87211 22.05701  1.000 29.96859 ? 252 PRO   A CB  1 
ATOM   1964 C  CG  . PRO   A 1 252 ? -14.78002 -19.51460 22.11894  1.000 31.27380 ? 252 PRO   A CG  1 
ATOM   1965 C  CD  . PRO   A 1 252 ? -14.02643 -20.80757 21.95569  1.000 28.61859 ? 252 PRO   A CD  1 
ATOM   1966 N  N   . LEU   A 1 253 ? -17.39397 -22.58302 21.06042  1.000 26.26392 ? 253 LEU   A N   1 
ATOM   1967 C  CA  . LEU   A 1 253 ? -18.48000 -23.41981 20.55422  1.000 24.03344 ? 253 LEU   A CA  1 
ATOM   1968 C  C   . LEU   A 1 253 ? -18.60884 -24.69787 21.36883  1.000 25.31868 ? 253 LEU   A C   1 
ATOM   1969 O  O   . LEU   A 1 253 ? -19.72097 -25.16673 21.63161  1.000 22.59616 ? 253 LEU   A O   1 
ATOM   1970 C  CB  . LEU   A 1 253 ? -18.23009 -23.73861 19.08247  1.000 21.68328 ? 253 LEU   A CB  1 
ATOM   1971 C  CG  . LEU   A 1 253 ? -18.49249 -22.59962 18.09982  1.000 21.83745 ? 253 LEU   A CG  1 
ATOM   1972 C  CD1 . LEU   A 1 253 ? -18.17296 -23.04549 16.68778  1.000 19.76391 ? 253 LEU   A CD1 1 
ATOM   1973 C  CD2 . LEU   A 1 253 ? -19.93897 -22.17304 18.19191  1.000 22.30399 ? 253 LEU   A CD2 1 
ATOM   1974 N  N   . SER   A 1 254 ? -17.47462 -25.27312 21.77197  1.000 23.14349 ? 254 SER   A N   1 
ATOM   1975 C  CA  . SER   A 1 254 ? -17.47532 -26.42555 22.67051  1.000 25.03421 ? 254 SER   A CA  1 
ATOM   1976 C  C   . SER   A 1 254 ? -18.15183 -26.10109 23.99674  1.000 27.96013 ? 254 SER   A C   1 
ATOM   1977 O  O   . SER   A 1 254 ? -18.93664 -26.90099 24.51980  1.000 27.86112 ? 254 SER   A O   1 
ATOM   1978 C  CB  . SER   A 1 254 ? -16.03622 -26.88715 22.91069  1.000 26.75323 ? 254 SER   A CB  1 
ATOM   1979 O  OG  . SER   A 1 254 ? -15.99470 -28.14597 23.55377  1.000 29.12937 ? 254 SER   A OG  1 
ATOM   1980 N  N   . ALA   A 1 255 ? -17.83100 -24.94082 24.57460  1.000 28.50323 ? 255 ALA   A N   1 
ATOM   1981 C  CA  . ALA   A 1 255 ? -18.38553 -24.59384 25.87922  1.000 31.84111 ? 255 ALA   A CA  1 
ATOM   1982 C  C   . ALA   A 1 255 ? -19.87617 -24.30679 25.78721  1.000 32.11359 ? 255 ALA   A C   1 
ATOM   1983 O  O   . ALA   A 1 255 ? -20.62400 -24.59002 26.73349  1.000 32.37568 ? 255 ALA   A O   1 
ATOM   1984 C  CB  . ALA   A 1 255 ? -17.64196 -23.39282 26.46390  1.000 33.18775 ? 255 ALA   A CB  1 
ATOM   1985 N  N   . GLN   A 1 256 ? -20.32538 -23.76885 24.65264  1.000 28.55532 ? 256 GLN   A N   1 
ATOM   1986 C  CA  . GLN   A 1 256 ? -21.73905 -23.45024 24.49668  1.000 28.97521 ? 256 GLN   A CA  1 
ATOM   1987 C  C   . GLN   A 1 256 ? -22.57433 -24.71396 24.33883  1.000 28.33133 ? 256 GLN   A C   1 
ATOM   1988 O  O   . GLN   A 1 256 ? -23.65966 -24.82652 24.92425  1.000 32.80710 ? 256 GLN   A O   1 
ATOM   1989 C  CB  . GLN   A 1 256 ? -21.91770 -22.50553 23.31112  1.000 28.51127 ? 256 GLN   A CB  1 
ATOM   1990 C  CG  . GLN   A 1 256 ? -23.30394 -21.94238 23.15537  1.000 30.15110 ? 256 GLN   A CG  1 
ATOM   1991 C  CD  . GLN   A 1 256 ? -23.47563 -21.27656 21.81650  1.000 30.64527 ? 256 GLN   A CD  1 
ATOM   1992 O  OE1 . GLN   A 1 256 ? -22.49007 -20.92517 21.16205  1.000 33.40477 ? 256 GLN   A OE1 1 
ATOM   1993 N  NE2 . GLN   A 1 256 ? -24.72007 -21.10327 21.39049  1.000 35.22952 ? 256 GLN   A NE2 1 
ATOM   1994 N  N   . THR   A 1 257 ? -22.07089 -25.69483 23.58717  1.000 28.44098 ? 257 THR   A N   1 
ATOM   1995 C  CA  . THR   A 1 257 ? -22.80490 -26.93156 23.36164  1.000 26.60481 ? 257 THR   A CA  1 
ATOM   1996 C  C   . THR   A 1 257 ? -22.53458 -27.99211 24.41783  1.000 27.87649 ? 257 THR   A C   1 
ATOM   1997 O  O   . THR   A 1 257 ? -23.30153 -28.95358 24.51380  1.000 31.26148 ? 257 THR   A O   1 
ATOM   1998 C  CB  . THR   A 1 257 ? -22.46333 -27.50905 21.98626  1.000 25.61231 ? 257 THR   A CB  1 
ATOM   1999 O  OG1 . THR   A 1 257 ? -21.04245 -27.68502 21.87731  1.000 26.29273 ? 257 THR   A OG1 1 
ATOM   2000 C  CG2 . THR   A 1 257 ? -22.90961 -26.55292 20.90001  1.000 23.54502 ? 257 THR   A CG2 1 
ATOM   2001 N  N   . GLY   A 1 258 ? -21.46692 -27.84780 25.19958  1.000 27.53938 ? 258 GLY   A N   1 
ATOM   2002 C  CA  . GLY   A 1 258 ? -21.08366 -28.87897 26.14229  1.000 29.11750 ? 258 GLY   A CA  1 
ATOM   2003 C  C   . GLY   A 1 258 ? -20.46669 -30.10787 25.51609  1.000 29.07731 ? 258 GLY   A C   1 
ATOM   2004 O  O   . GLY   A 1 258 ? -20.36483 -31.14568 26.17653  1.000 30.97166 ? 258 GLY   A O   1 
ATOM   2005 N  N   . ILE   A 1 259 ? -20.05700 -30.02950 24.25436  1.000 27.37320 ? 259 ILE   A N   1 
ATOM   2006 C  CA  . ILE   A 1 259 ? -19.46836 -31.16064 23.54871  1.000 29.02009 ? 259 ILE   A CA  1 
ATOM   2007 C  C   . ILE   A 1 259 ? -17.98055 -30.88262 23.37904  1.000 27.92373 ? 259 ILE   A C   1 
ATOM   2008 O  O   . ILE   A 1 259 ? -17.59579 -29.92656 22.69362  1.000 24.92214 ? 259 ILE   A O   1 
ATOM   2009 C  CB  . ILE   A 1 259 ? -20.14659 -31.39323 22.19302  1.000 26.52830 ? 259 ILE   A CB  1 
ATOM   2010 C  CG1 . ILE   A 1 259 ? -21.59983 -31.81491 22.40765  1.000 30.76573 ? 259 ILE   A CG1 1 
ATOM   2011 C  CG2 . ILE   A 1 259 ? -19.41957 -32.47383 21.41205  1.000 23.39844 ? 259 ILE   A CG2 1 
ATOM   2012 C  CD1 . ILE   A 1 259 ? -22.44469 -31.59431 21.21634  1.000 31.44628 ? 259 ILE   A CD1 1 
ATOM   2013 N  N   . ALA   A 1 260 ? -17.14689 -31.70544 24.01726  1.000 26.91934 ? 260 ALA   A N   1 
ATOM   2014 C  CA  . ALA   A 1 260 ? -15.70558 -31.52467 23.92704  1.000 25.60597 ? 260 ALA   A CA  1 
ATOM   2015 C  C   . ALA   A 1 260 ? -15.25118 -31.57133 22.47035  1.000 23.95743 ? 260 ALA   A C   1 
ATOM   2016 O  O   . ALA   A 1 260 ? -15.81427 -32.29107 21.64380  1.000 24.27050 ? 260 ALA   A O   1 
ATOM   2017 C  CB  . ALA   A 1 260 ? -14.98426 -32.59859 24.75138  1.000 27.41907 ? 260 ALA   A CB  1 
ATOM   2018 N  N   . VAL   A 1 261 ? -14.23340 -30.77381 22.14848  1.000 23.48195 ? 261 VAL   A N   1 
ATOM   2019 C  CA  . VAL   A 1 261 ? -13.77145 -30.71126 20.76323  1.000 21.97713 ? 261 VAL   A CA  1 
ATOM   2020 C  C   . VAL   A 1 261 ? -13.37002 -32.09847 20.28109  1.000 22.22441 ? 261 VAL   A C   1 
ATOM   2021 O  O   . VAL   A 1 261 ? -13.78246 -32.54674 19.20681  1.000 24.54314 ? 261 VAL   A O   1 
ATOM   2022 C  CB  . VAL   A 1 261 ? -12.61414 -29.70713 20.61757  1.000 24.04681 ? 261 VAL   A CB  1 
ATOM   2023 C  CG1 . VAL   A 1 261 ? -12.01044 -29.80214 19.22091  1.000 20.29136 ? 261 VAL   A CG1 1 
ATOM   2024 C  CG2 . VAL   A 1 261 ? -13.07968 -28.29501 20.92681  1.000 24.58686 ? 261 VAL   A CG2 1 
ATOM   2025 N  N   . LEU   A 1 262 ? -12.59682 -32.81909 21.09469  1.000 26.07295 ? 262 LEU   A N   1 
ATOM   2026 C  CA  . LEU   A 1 262 ? -12.16202 -34.15569 20.70321  1.000 27.87426 ? 262 LEU   A CA  1 
ATOM   2027 C  C   . LEU   A 1 262 ? -13.33617 -35.12679 20.59020  1.000 25.23069 ? 262 LEU   A C   1 
ATOM   2028 O  O   . LEU   A 1 262 ? -13.25372 -36.10986 19.84227  1.000 26.61780 ? 262 LEU   A O   1 
ATOM   2029 C  CB  . LEU   A 1 262 ? -11.11566 -34.66133 21.70074  1.000 27.96066 ? 262 LEU   A CB  1 
ATOM   2030 C  CG  . LEU   A 1 262 ? -9.71718  -34.05354 21.49202  1.000 26.02833 ? 262 LEU   A CG  1 
ATOM   2031 C  CD1 . LEU   A 1 262 ? -8.70201  -34.83104 22.29493  1.000 31.76072 ? 262 LEU   A CD1 1 
ATOM   2032 C  CD2 . LEU   A 1 262 ? -9.31106  -34.03312 20.02529  1.000 30.04291 ? 262 LEU   A CD2 1 
ATOM   2033 N  N   . ASP   A 1 263 ? -14.44226 -34.86340 21.30130  1.000 25.84206 ? 263 ASP   A N   1 
ATOM   2034 C  CA  . ASP   A 1 263 ? -15.64358 -35.67548 21.11891  1.000 27.78242 ? 263 ASP   A CA  1 
ATOM   2035 C  C   . ASP   A 1 263 ? -16.27355 -35.40532 19.75758  1.000 24.33150 ? 263 ASP   A C   1 
ATOM   2036 O  O   . ASP   A 1 263 ? -16.72086 -36.33165 19.06910  1.000 24.16636 ? 263 ASP   A O   1 
ATOM   2037 C  CB  . ASP   A 1 263 ? -16.66072 -35.39914 22.23517  1.000 26.45932 ? 263 ASP   A CB  1 
ATOM   2038 C  CG  . ASP   A 1 263 ? -16.25109 -35.99633 23.58667  1.000 32.61566 ? 263 ASP   A CG  1 
ATOM   2039 O  OD1 . ASP   A 1 263 ? -15.13319 -36.53649 23.71609  1.000 31.95315 ? 263 ASP   A OD1 1 
ATOM   2040 O  OD2 . ASP   A 1 263 ? -17.07525 -35.93393 24.52516  1.000 33.02009 ? 263 ASP   A OD2 1 
ATOM   2041 N  N   . MET   A 1 264 ? -16.32165 -34.14084 19.35343  1.000 22.53710 ? 264 MET   A N   1 
ATOM   2042 C  CA  . MET   A 1 264 ? -16.85120 -33.84170 18.03190  1.000 21.10290 ? 264 MET   A CA  1 
ATOM   2043 C  C   . MET   A 1 264 ? -15.94545 -34.42789 16.95355  1.000 22.85865 ? 264 MET   A C   1 
ATOM   2044 O  O   . MET   A 1 264 ? -16.42957 -34.84680 15.89795  1.000 22.02906 ? 264 MET   A O   1 
ATOM   2045 C  CB  . MET   A 1 264 ? -17.01661 -32.32962 17.86687  1.000 19.80312 ? 264 MET   A CB  1 
ATOM   2046 C  CG  . MET   A 1 264 ? -17.76949 -31.91274 16.61871  1.000 18.50115 ? 264 MET   A CG  1 
ATOM   2047 S  SD  . MET   A 1 264 ? -19.50616 -32.45877 16.75620  1.000 20.27350 ? 264 MET   A SD  1 
ATOM   2048 C  CE  . MET   A 1 264 ? -20.22382 -31.01973 17.55861  1.000 18.91863 ? 264 MET   A CE  1 
ATOM   2049 N  N   . CYS   A 1 265 ? -14.63533 -34.50507 17.21398  1.000 22.87829 ? 265 CYS   A N   1 
ATOM   2050 C  CA  . CYS   A 1 265 ? -13.74309 -35.15638 16.25805  1.000 23.88163 ? 265 CYS   A CA  1 
ATOM   2051 C  C   . CYS   A 1 265 ? -14.10138 -36.62610 16.08434  1.000 22.30410 ? 265 CYS   A C   1 
ATOM   2052 O  O   . CYS   A 1 265 ? -14.10146 -37.13984 14.96077  1.000 23.50802 ? 265 CYS   A O   1 
ATOM   2053 C  CB  . CYS   A 1 265 ? -12.28074 -35.01410 16.69487  1.000 22.52096 ? 265 CYS   A CB  1 
ATOM   2054 S  SG  . CYS   A 1 265 ? -11.59613 -33.34773 16.58024  1.000 22.88096 ? 265 CYS   A SG  1 
ATOM   2055 N  N   . ALA   A 1 266 ? -14.40917 -37.32115 17.18735  1.000 24.73432 ? 266 ALA   A N   1 
ATOM   2056 C  CA  . ALA   A 1 266 ? -14.85356 -38.70632 17.08075  1.000 25.08882 ? 266 ALA   A CA  1 
ATOM   2057 C  C   . ALA   A 1 266 ? -16.10900 -38.81010 16.22453  1.000 25.40331 ? 266 ALA   A C   1 
ATOM   2058 O  O   . ALA   A 1 266 ? -16.24111 -39.73641 15.41454  1.000 26.20458 ? 266 ALA   A O   1 
ATOM   2059 C  CB  . ALA   A 1 266 ? -15.08588 -39.29503 18.47233  1.000 26.80704 ? 266 ALA   A CB  1 
ATOM   2060 N  N   . SER   A 1 267 ? -17.02954 -37.84895 16.36298  1.000 23.47649 ? 267 SER   A N   1 
ATOM   2061 C  CA  . SER   A 1 267 ? -18.22152 -37.86468 15.52486  1.000 23.70812 ? 267 SER   A CA  1 
ATOM   2062 C  C   . SER   A 1 267 ? -17.86441 -37.66378 14.06137  1.000 23.68707 ? 267 SER   A C   1 
ATOM   2063 O  O   . SER   A 1 267 ? -18.38042 -38.37217 13.18965  1.000 24.53127 ? 267 SER   A O   1 
ATOM   2064 C  CB  . SER   A 1 267 ? -19.21306 -36.79889 15.98973  1.000 24.84529 ? 267 SER   A CB  1 
ATOM   2065 O  OG  . SER   A 1 267 ? -19.77499 -37.18308 17.22739  1.000 29.25508 ? 267 SER   A OG  1 
ATOM   2066 N  N   . LEU   A 1 268 ? -16.98339 -36.70214 13.77222  1.000 22.88605 ? 268 LEU   A N   1 
ATOM   2067 C  CA  . LEU   A 1 268 ? -16.53400 -36.50792 12.39882  1.000 20.47047 ? 268 LEU   A CA  1 
ATOM   2068 C  C   . LEU   A 1 268 ? -15.85323 -37.76199 11.85694  1.000 24.01657 ? 268 LEU   A C   1 
ATOM   2069 O  O   . LEU   A 1 268 ? -16.06724 -38.14104 10.69857  1.000 24.07908 ? 268 LEU   A O   1 
ATOM   2070 C  CB  . LEU   A 1 268 ? -15.58988 -35.30491 12.32356  1.000 20.67189 ? 268 LEU   A CB  1 
ATOM   2071 C  CG  . LEU   A 1 268 ? -15.05143 -34.93438 10.93746  1.000 20.29013 ? 268 LEU   A CG  1 
ATOM   2072 C  CD1 . LEU   A 1 268 ? -16.17114 -34.88986 9.89175   1.000 20.51231 ? 268 LEU   A CD1 1 
ATOM   2073 C  CD2 . LEU   A 1 268 ? -14.29551 -33.60662 10.98330  1.000 22.40741 ? 268 LEU   A CD2 1 
ATOM   2074 N  N   . LYS   A 1 269 ? -15.03210 -38.41810 12.68312  1.000 22.95416 ? 269 LYS   A N   1 
ATOM   2075 C  CA  . LYS   A 1 269 ? -14.41977 -39.68623 12.29314  1.000 26.96613 ? 269 LYS   A CA  1 
ATOM   2076 C  C   . LYS   A 1 269 ? -15.46682 -40.69448 11.84294  1.000 25.71625 ? 269 LYS   A C   1 
ATOM   2077 O  O   . LYS   A 1 269 ? -15.33449 -41.31262 10.78135  1.000 27.46026 ? 269 LYS   A O   1 
ATOM   2078 C  CB  . LYS   A 1 269 ? -13.60096 -40.24926 13.45586  1.000 28.10893 ? 269 LYS   A CB  1 
ATOM   2079 C  CG  . LYS   A 1 269 ? -13.00767 -41.62661 13.19641  1.000 33.20303 ? 269 LYS   A CG  1 
ATOM   2080 C  CD  . LYS   A 1 269 ? -11.95513 -41.98787 14.23718  1.000 33.23854 ? 269 LYS   A CD  1 
ATOM   2081 C  CE  . LYS   A 1 269 ? -11.35204 -43.36166 13.95444  1.000 40.72507 ? 269 LYS   A CE  1 
ATOM   2082 N  NZ  . LYS   A 1 269 ? -11.18663 -44.18869 15.18549  1.000 42.31344 ? 269 LYS   A NZ  1 
ATOM   2083 N  N   . GLU   A 1 270 ? -16.51994 -40.87366 12.64713  1.000 27.28306 ? 270 GLU   A N   1 
ATOM   2084 C  CA  . GLU   A 1 270 ? -17.56933 -41.82604 12.29727  1.000 28.37785 ? 270 GLU   A CA  1 
ATOM   2085 C  C   . GLU   A 1 270 ? -18.27586 -41.41854 11.01101  1.000 29.44814 ? 270 GLU   A C   1 
ATOM   2086 O  O   . GLU   A 1 270 ? -18.57464 -42.26626 10.16251  1.000 31.43618 ? 270 GLU   A O   1 
ATOM   2087 C  CB  . GLU   A 1 270 ? -18.56888 -41.94567 13.44992  1.000 31.28865 ? 270 GLU   A CB  1 
ATOM   2088 C  CG  . GLU   A 1 270 ? -18.00125 -42.65940 14.66348  1.000 34.69757 ? 270 GLU   A CG  1 
ATOM   2089 C  CD  . GLU   A 1 270 ? -17.33184 -43.97311 14.31239  1.000 39.97609 ? 270 GLU   A CD  1 
ATOM   2090 O  OE1 . GLU   A 1 270 ? -17.93410 -44.76002 13.54762  1.000 44.49273 ? 270 GLU   A OE1 1 
ATOM   2091 O  OE2 . GLU   A 1 270 ? -16.19108 -44.20687 14.77374  1.000 40.90882 ? 270 GLU   A OE2 1 
ATOM   2092 N  N   . LEU   A 1 271 ? -18.53564 -40.11912 10.84052  1.000 25.76893 ? 271 LEU   A N   1 
ATOM   2093 C  CA  . LEU   A 1 271 ? -19.21372 -39.65173 9.63464   1.000 26.35094 ? 271 LEU   A CA  1 
ATOM   2094 C  C   . LEU   A 1 271 ? -18.36592 -39.89662 8.39578   1.000 29.28109 ? 271 LEU   A C   1 
ATOM   2095 O  O   . LEU   A 1 271 ? -18.89816 -40.20414 7.32232   1.000 30.05449 ? 271 LEU   A O   1 
ATOM   2096 C  CB  . LEU   A 1 271 ? -19.54944 -38.16969 9.76699   1.000 23.95585 ? 271 LEU   A CB  1 
ATOM   2097 C  CG  . LEU   A 1 271 ? -20.72242 -37.82345 10.67887  1.000 23.86491 ? 271 LEU   A CG  1 
ATOM   2098 C  CD1 . LEU   A 1 271 ? -20.79345 -36.32222 10.92530  1.000 21.43437 ? 271 LEU   A CD1 1 
ATOM   2099 C  CD2 . LEU   A 1 271 ? -22.01709 -38.33083 10.07225  1.000 29.55949 ? 271 LEU   A CD2 1 
ATOM   2100 N  N   . LEU   A 1 272 ? -17.04089 -39.76345 8.52605   1.000 26.41986 ? 272 LEU   A N   1 
ATOM   2101 C  CA  . LEU   A 1 272 ? -16.15839 -40.02556 7.39567   1.000 26.87598 ? 272 LEU   A CA  1 
ATOM   2102 C  C   . LEU   A 1 272 ? -16.14111 -41.50852 7.04447   1.000 29.57060 ? 272 LEU   A C   1 
ATOM   2103 O  O   . LEU   A 1 272 ? -16.13182 -41.86744 5.86154   1.000 32.88263 ? 272 LEU   A O   1 
ATOM   2104 C  CB  . LEU   A 1 272 ? -14.74655 -39.52787 7.70647   1.000 24.37071 ? 272 LEU   A CB  1 
ATOM   2105 C  CG  . LEU   A 1 272 ? -14.60730 -38.00449 7.73280   1.000 22.31267 ? 272 LEU   A CG  1 
ATOM   2106 C  CD1 . LEU   A 1 272 ? -13.24494 -37.60207 8.28178   1.000 27.34373 ? 272 LEU   A CD1 1 
ATOM   2107 C  CD2 . LEU   A 1 272 ? -14.84228 -37.41568 6.34848   1.000 26.41926 ? 272 LEU   A CD2 1 
ATOM   2108 N  N   . GLN   A 1 273 ? -16.16360 -42.38413 8.05676   1.000 31.94278 ? 273 GLN   A N   1 
ATOM   2109 C  CA  . GLN   A 1 273 ? -16.02275 -43.81850 7.81153   1.000 34.27365 ? 273 GLN   A CA  1 
ATOM   2110 C  C   . GLN   A 1 273 ? -17.33772 -44.48116 7.41719   1.000 36.30137 ? 273 GLN   A C   1 
ATOM   2111 O  O   . GLN   A 1 273 ? -17.32193 -45.51820 6.74399   1.000 38.22803 ? 273 GLN   A O   1 
ATOM   2112 C  CB  . GLN   A 1 273 ? -15.45577 -44.52675 9.04585   1.000 33.92280 ? 273 GLN   A CB  1 
ATOM   2113 C  CG  . GLN   A 1 273 ? -13.99117 -44.23618 9.33380   1.000 33.58110 ? 273 GLN   A CG  1 
ATOM   2114 C  CD  . GLN   A 1 273 ? -13.57750 -44.64246 10.74339  1.000 38.33005 ? 273 GLN   A CD  1 
ATOM   2115 O  OE1 . GLN   A 1 273 ? -12.39278 -44.63259 11.08313  1.000 40.32861 ? 273 GLN   A OE1 1 
ATOM   2116 N  NE2 . GLN   A 1 273 ? -14.55130 -45.02535 11.56146  1.000 42.49453 ? 273 GLN   A NE2 1 
ATOM   2117 N  N   . ASN   A 1 274 ? -18.47468 -43.91966 7.82914   1.000 34.34758 ? 274 ASN   A N   1 
ATOM   2118 C  CA  . ASN   A 1 274 ? -19.77256 -44.52808 7.56998   1.000 36.43254 ? 274 ASN   A CA  1 
ATOM   2119 C  C   . ASN   A 1 274 ? -20.65248 -43.73024 6.62292   1.000 37.32689 ? 274 ASN   A C   1 
ATOM   2120 O  O   . ASN   A 1 274 ? -21.69508 -44.24252 6.20214   1.000 40.36647 ? 274 ASN   A O   1 
ATOM   2121 C  CB  . ASN   A 1 274 ? -20.54521 -44.73609 8.88078   1.000 38.02202 ? 274 ASN   A CB  1 
ATOM   2122 C  CG  . ASN   A 1 274 ? -19.69020 -45.33347 9.97843   1.000 42.06698 ? 274 ASN   A CG  1 
ATOM   2123 O  OD1 . ASN   A 1 274 ? -18.75536 -46.09386 9.71680   1.000 40.52101 ? 274 ASN   A OD1 1 
ATOM   2124 N  ND2 . ASN   A 1 274 ? -20.01542 -44.99857 11.22312  1.000 43.76923 ? 274 ASN   A ND2 1 
ATOM   2125 N  N   . GLY   A 1 275 ? -20.27513 -42.50658 6.27650   1.000 35.78023 ? 275 GLY   A N   1 
ATOM   2126 C  CA  . GLY   A 1 275 ? -21.20314 -41.66277 5.56098   1.000 36.88778 ? 275 GLY   A CA  1 
ATOM   2127 C  C   . GLY   A 1 275 ? -22.34445 -41.24787 6.47808   1.000 38.86219 ? 275 GLY   A C   1 
ATOM   2128 O  O   . GLY   A 1 275 ? -22.28850 -41.38163 7.69890   1.000 39.04997 ? 275 GLY   A O   1 
ATOM   2129 N  N   . MET   A 1 276 ? -23.40783 -40.74504 5.85958   1.000 41.92333 ? 276 MET   A N   1 
ATOM   2130 C  CA  . MET   A 1 276 ? -24.50665 -40.16575 6.61564   1.000 39.92499 ? 276 MET   A CA  1 
ATOM   2131 C  C   . MET   A 1 276 ? -25.75886 -41.03504 6.59239   1.000 42.72297 ? 276 MET   A C   1 
ATOM   2132 O  O   . MET   A 1 276 ? -26.74888 -40.69093 7.24834   1.000 39.80694 ? 276 MET   A O   1 
ATOM   2133 C  CB  . MET   A 1 276 ? -24.78501 -38.75090 6.09316   1.000 37.94814 ? 276 MET   A CB  1 
ATOM   2134 C  CG  . MET   A 1 276 ? -23.57408 -37.82517 6.34490   1.000 37.66672 ? 276 MET   A CG  1 
ATOM   2135 S  SD  . MET   A 1 276 ? -23.73404 -36.07499 5.97248   1.000 49.53575 ? 276 MET   A SD  1 
ATOM   2136 C  CE  . MET   A 1 276 ? -25.43474 -35.84275 6.37406   1.000 30.01394 ? 276 MET   A CE  1 
ATOM   2137 N  N   . ASN   A 1 277 ? -25.71820 -42.17406 5.89002   1.000 42.74692 ? 277 ASN   A N   1 
ATOM   2138 C  CA  . ASN   A 1 277 ? -26.78449 -43.18046 5.90352   1.000 42.00874 ? 277 ASN   A CA  1 
ATOM   2139 C  C   . ASN   A 1 277 ? -28.14607 -42.57018 5.58569   1.000 40.27442 ? 277 ASN   A C   1 
ATOM   2140 O  O   . ASN   A 1 277 ? -29.15753 -42.89054 6.21689   1.000 43.01194 ? 277 ASN   A O   1 
ATOM   2141 C  CB  . ASN   A 1 277 ? -26.82401 -43.92830 7.23896   1.000 42.20671 ? 277 ASN   A CB  1 
ATOM   2142 C  CG  . ASN   A 1 277 ? -25.51750 -44.64794 7.55148   1.000 46.98777 ? 277 ASN   A CG  1 
ATOM   2143 O  OD1 . ASN   A 1 277 ? -25.04326 -45.47291 6.76733   1.000 51.82380 ? 277 ASN   A OD1 1 
ATOM   2144 N  ND2 . ASN   A 1 277 ? -24.93538 -44.34405 8.70835   1.000 46.09037 ? 277 ASN   A ND2 1 
ATOM   2145 N  N   . GLY   A 1 278 ? -28.17301 -41.68454 4.59193   1.000 38.37867 ? 278 GLY   A N   1 
ATOM   2146 C  CA  . GLY   A 1 278 ? -29.42096 -41.12051 4.12046   1.000 40.29234 ? 278 GLY   A CA  1 
ATOM   2147 C  C   . GLY   A 1 278 ? -29.98880 -39.98940 4.94799   1.000 39.50826 ? 278 GLY   A C   1 
ATOM   2148 O  O   . GLY   A 1 278 ? -31.12080 -39.56642 4.68783   1.000 43.11524 ? 278 GLY   A O   1 
ATOM   2149 N  N   . ARG   A 1 279 ? -29.25211 -39.49022 5.93409   1.000 36.40683 ? 279 ARG   A N   1 
ATOM   2150 C  CA  . ARG   A 1 279 ? -29.68827 -38.36915 6.75235   1.000 34.43329 ? 279 ARG   A CA  1 
ATOM   2151 C  C   . ARG   A 1 279 ? -28.97824 -37.09714 6.30375   1.000 31.83999 ? 279 ARG   A C   1 
ATOM   2152 O  O   . ARG   A 1 279 ? -28.09376 -37.12111 5.44993   1.000 32.32489 ? 279 ARG   A O   1 
ATOM   2153 C  CB  . ARG   A 1 279 ? -29.42814 -38.66071 8.23563   1.000 33.67375 ? 279 ARG   A CB  1 
ATOM   2154 C  CG  . ARG   A 1 279 ? -30.04857 -39.97665 8.68767   1.000 37.73429 ? 279 ARG   A CG  1 
ATOM   2155 C  CD  . ARG   A 1 279 ? -29.55156 -40.42227 10.04525  1.000 37.49404 ? 279 ARG   A CD  1 
ATOM   2156 N  NE  . ARG   A 1 279 ? -28.31738 -41.18751 9.91149   1.000 40.85530 ? 279 ARG   A NE  1 
ATOM   2157 C  CZ  . ARG   A 1 279 ? -27.75855 -41.90263 10.87798  1.000 36.66634 ? 279 ARG   A CZ  1 
ATOM   2158 N  NH1 . ARG   A 1 279 ? -28.36144 -42.08312 12.04339  1.000 39.03856 ? 279 ARG   A NH1 1 
ATOM   2159 N  NH2 . ARG   A 1 279 ? -26.56469 -42.45151 10.66886  1.000 36.29955 ? 279 ARG   A NH2 1 
ATOM   2160 N  N   . THR   A 1 280 ? -29.40495 -35.97008 6.86551   1.000 30.58009 ? 280 THR   A N   1 
ATOM   2161 C  CA  . THR   A 1 280 ? -28.84735 -34.67104 6.52458   1.000 26.43815 ? 280 THR   A CA  1 
ATOM   2162 C  C   . THR   A 1 280 ? -28.45444 -33.93012 7.79367   1.000 22.86095 ? 280 THR   A C   1 
ATOM   2163 O  O   . THR   A 1 280 ? -28.90485 -34.24562 8.89981   1.000 22.05637 ? 280 THR   A O   1 
ATOM   2164 C  CB  . THR   A 1 280 ? -29.82910 -33.81345 5.70340   1.000 26.60219 ? 280 THR   A CB  1 
ATOM   2165 O  OG1 . THR   A 1 280 ? -31.01015 -33.55810 6.47454   1.000 27.67286 ? 280 THR   A OG1 1 
ATOM   2166 C  CG2 . THR   A 1 280 ? -30.21015 -34.53035 4.41365   1.000 28.89497 ? 280 THR   A CG2 1 
ATOM   2167 N  N   . ILE   A 1 281 ? -27.57336 -32.95590 7.61744   1.000 21.31109 ? 281 ILE   A N   1 
ATOM   2168 C  CA  . ILE   A 1 281 ? -27.14933 -32.05322 8.67348   1.000 18.75913 ? 281 ILE   A CA  1 
ATOM   2169 C  C   . ILE   A 1 281 ? -27.31932 -30.64368 8.13445   1.000 21.11913 ? 281 ILE   A C   1 
ATOM   2170 O  O   . ILE   A 1 281 ? -26.72761 -30.30665 7.10641   1.000 18.48247 ? 281 ILE   A O   1 
ATOM   2171 C  CB  . ILE   A 1 281 ? -25.68277 -32.28392 9.07213   1.000 17.57437 ? 281 ILE   A CB  1 
ATOM   2172 C  CG1 . ILE   A 1 281 ? -25.43302 -33.73497 9.50875   1.000 20.95750 ? 281 ILE   A CG1 1 
ATOM   2173 C  CG2 . ILE   A 1 281 ? -25.27365 -31.25683 10.11088  1.000 16.65954 ? 281 ILE   A CG2 1 
ATOM   2174 C  CD1 . ILE   A 1 281 ? -23.97217 -34.05147 9.94970   1.000 21.64497 ? 281 ILE   A CD1 1 
ATOM   2175 N  N   . LEU   A 1 282 ? -28.11624 -29.82393 8.82137   1.000 21.42337 ? 282 LEU   A N   1 
ATOM   2176 C  CA  . LEU   A 1 282 ? -28.37180 -28.44405 8.39743   1.000 20.44503 ? 282 LEU   A CA  1 
ATOM   2177 C  C   . LEU   A 1 282 ? -28.74984 -28.39753 6.91697   1.000 22.68768 ? 282 LEU   A C   1 
ATOM   2178 O  O   . LEU   A 1 282 ? -28.26345 -27.55894 6.15461   1.000 20.37905 ? 282 LEU   A O   1 
ATOM   2179 C  CB  . LEU   A 1 282 ? -27.16147 -27.53777 8.69060   1.000 16.97652 ? 282 LEU   A CB  1 
ATOM   2180 C  CG  . LEU   A 1 282 ? -26.99726 -27.23009 10.18591  1.000 20.16502 ? 282 LEU   A CG  1 
ATOM   2181 C  CD1 . LEU   A 1 282 ? -25.72565 -26.45758 10.48452  1.000 19.16469 ? 282 LEU   A CD1 1 
ATOM   2182 C  CD2 . LEU   A 1 282 ? -28.20340 -26.51430 10.76539  1.000 21.70952 ? 282 LEU   A CD2 1 
ATOM   2183 N  N   . GLY   A 1 283 ? -29.60013 -29.34410 6.50806   1.000 22.95270 ? 283 GLY   A N   1 
ATOM   2184 C  CA  . GLY   A 1 283 ? -30.09668 -29.40381 5.14619   1.000 24.63767 ? 283 GLY   A CA  1 
ATOM   2185 C  C   . GLY   A 1 283 ? -29.08077 -29.79909 4.09784   1.000 26.41138 ? 283 GLY   A C   1 
ATOM   2186 O  O   . GLY   A 1 283 ? -29.30757 -29.55514 2.90853   1.000 28.60114 ? 283 GLY   A O   1 
ATOM   2187 N  N   . SER   A 1 284 ? -27.95790 -30.39042 4.49877   1.000 21.91127 ? 284 SER   A N   1 
ATOM   2188 C  CA  . SER   A 1 284 ? -26.92658 -30.83872 3.57122   1.000 20.50735 ? 284 SER   A CA  1 
ATOM   2189 C  C   . SER   A 1 284 ? -26.68827 -32.33197 3.74822   1.000 23.76979 ? 284 SER   A C   1 
ATOM   2190 O  O   . SER   A 1 284 ? -26.77594 -32.85795 4.86401   1.000 22.19209 ? 284 SER   A O   1 
ATOM   2191 C  CB  . SER   A 1 284 ? -25.61760 -30.06472 3.78548   1.000 21.94320 ? 284 SER   A CB  1 
ATOM   2192 O  OG  . SER   A 1 284 ? -24.59874 -30.51667 2.90267   1.000 23.25319 ? 284 SER   A OG  1 
ATOM   2193 N  N   . ALA   A 1 285 ? -26.43124 -33.02563 2.63960   1.000 22.91950 ? 285 ALA   A N   1 
ATOM   2194 C  CA  . ALA   A 1 285 ? -26.04540 -34.42626 2.67682   1.000 25.81762 ? 285 ALA   A CA  1 
ATOM   2195 C  C   . ALA   A 1 285 ? -24.54501 -34.60401 2.49906   1.000 24.75294 ? 285 ALA   A C   1 
ATOM   2196 O  O   . ALA   A 1 285 ? -24.08188 -35.73395 2.30520   1.000 29.04810 ? 285 ALA   A O   1 
ATOM   2197 C  CB  . ALA   A 1 285 ? -26.80002 -35.22493 1.61392   1.000 28.20823 ? 285 ALA   A CB  1 
ATOM   2198 N  N   . LEU   A 1 286 ? -23.78854 -33.51105 2.54859   1.000 22.65649 ? 286 LEU   A N   1 
ATOM   2199 C  CA  . LEU   A 1 286 ? -22.33314 -33.52775 2.54381   1.000 23.58766 ? 286 LEU   A CA  1 
ATOM   2200 C  C   . LEU   A 1 286 ? -21.82135 -32.76857 3.76022   1.000 22.99556 ? 286 LEU   A C   1 
ATOM   2201 O  O   . LEU   A 1 286 ? -22.51691 -31.92157 4.32808   1.000 19.86377 ? 286 LEU   A O   1 
ATOM   2202 C  CB  . LEU   A 1 286 ? -21.75517 -32.88142 1.28175   1.000 26.32850 ? 286 LEU   A CB  1 
ATOM   2203 C  CG  . LEU   A 1 286 ? -22.05755 -33.49630 -0.07338  1.000 29.76995 ? 286 LEU   A CG  1 
ATOM   2204 C  CD1 . LEU   A 1 286 ? -21.64098 -32.51445 -1.15268  1.000 26.90791 ? 286 LEU   A CD1 1 
ATOM   2205 C  CD2 . LEU   A 1 286 ? -21.33838 -34.84206 -0.22336  1.000 32.00118 ? 286 LEU   A CD2 1 
ATOM   2206 N  N   . LEU   A 1 287 ? -20.58104 -33.05501 4.13995   1.000 20.74220 ? 287 LEU   A N   1 
ATOM   2207 C  CA  . LEU   A 1 287 ? -19.93285 -32.30514 5.20908   1.000 20.75201 ? 287 LEU   A CA  1 
ATOM   2208 C  C   . LEU   A 1 287 ? -19.46045 -30.95851 4.66546   1.000 17.71613 ? 287 LEU   A C   1 
ATOM   2209 O  O   . LEU   A 1 287 ? -18.62666 -30.90580 3.75927   1.000 20.57712 ? 287 LEU   A O   1 
ATOM   2210 C  CB  . LEU   A 1 287 ? -18.77499 -33.11636 5.79290   1.000 20.22013 ? 287 LEU   A CB  1 
ATOM   2211 C  CG  . LEU   A 1 287 ? -19.24289 -34.49122 6.29505   1.000 20.00940 ? 287 LEU   A CG  1 
ATOM   2212 C  CD1 . LEU   A 1 287 ? -18.09709 -35.43158 6.69257   1.000 25.69334 ? 287 LEU   A CD1 1 
ATOM   2213 C  CD2 . LEU   A 1 287 ? -20.21410 -34.31850 7.45395   1.000 24.37073 ? 287 LEU   A CD2 1 
ATOM   2214 N  N   . GLU   A 1 288 ? -20.00064 -29.87551 5.21822   1.000 15.02240 ? 288 GLU   A N   1 
ATOM   2215 C  CA  . GLU   A 1 288 ? -19.80107 -28.51726 4.72639   1.000 16.91869 ? 288 GLU   A CA  1 
ATOM   2216 C  C   . GLU   A 1 288 ? -18.55345 -27.90056 5.34933   1.000 14.80722 ? 288 GLU   A C   1 
ATOM   2217 O  O   . GLU   A 1 288 ? -18.40891 -27.90777 6.57462   1.000 13.69389 ? 288 GLU   A O   1 
ATOM   2218 C  CB  . GLU   A 1 288 ? -21.03113 -27.68919 5.09634   1.000 16.37276 ? 288 GLU   A CB  1 
ATOM   2219 C  CG  . GLU   A 1 288 ? -21.02741 -26.22473 4.71162   1.000 23.99701 ? 288 GLU   A CG  1 
ATOM   2220 C  CD  . GLU   A 1 288 ? -20.87064 -25.99464 3.22239   1.000 26.28448 ? 288 GLU   A CD  1 
ATOM   2221 O  OE1 . GLU   A 1 288 ? -21.65415 -26.59750 2.44193   1.000 29.83252 ? 288 GLU   A OE1 1 
ATOM   2222 O  OE2 . GLU   A 1 288 ? -19.99272 -25.18542 2.84086   1.000 21.86892 ? 288 GLU   A OE2 1 
ATOM   2223 N  N   . ASP   A 1 289 ? -17.66810 -27.32339 4.52496   1.000 14.75622 ? 289 ASP   A N   1 
ATOM   2224 C  CA  . ASP   A 1 289 ? -16.43120 -26.76606 5.07312   1.000 15.25138 ? 289 ASP   A CA  1 
ATOM   2225 C  C   . ASP   A 1 289 ? -16.22434 -25.27807 4.76688   1.000 14.31277 ? 289 ASP   A C   1 
ATOM   2226 O  O   . ASP   A 1 289 ? -15.10852 -24.77654 4.93431   1.000 14.30290 ? 289 ASP   A O   1 
ATOM   2227 C  CB  . ASP   A 1 289 ? -15.22163 -27.60567 4.62241   1.000 16.39884 ? 289 ASP   A CB  1 
ATOM   2228 C  CG  . ASP   A 1 289 ? -14.74928 -27.30042 3.19295   1.000 16.77497 ? 289 ASP   A CG  1 
ATOM   2229 O  OD1 . ASP   A 1 289 ? -15.53333 -26.75020 2.38460   1.000 16.17818 ? 289 ASP   A OD1 1 
ATOM   2230 O  OD2 . ASP   A 1 289 ? -13.56200 -27.62804 2.90183   1.000 18.18344 ? 289 ASP   A OD2 1 
ATOM   2231 N  N   . GLU   A 1 290 ? -17.26351 -24.53325 4.36630   1.000 14.37059 ? 290 GLU   A N   1 
ATOM   2232 C  CA  . GLU   A 1 290 ? -17.06577 -23.12004 4.06121   1.000 13.88462 ? 290 GLU   A CA  1 
ATOM   2233 C  C   . GLU   A 1 290 ? -17.69841 -22.19517 5.10445   1.000 16.79439 ? 290 GLU   A C   1 
ATOM   2234 O  O   . GLU   A 1 290 ? -18.01769 -21.04617 4.79997   1.000 16.20765 ? 290 GLU   A O   1 
ATOM   2235 C  CB  . GLU   A 1 290 ? -17.54357 -22.80540 2.63658   1.000 17.66093 ? 290 GLU   A CB  1 
ATOM   2236 C  CG  . GLU   A 1 290 ? -16.80515 -23.65059 1.53167   1.000 20.77437 ? 290 GLU   A CG  1 
ATOM   2237 C  CD  . GLU   A 1 290 ? -16.52761 -22.90184 0.20927   1.000 20.49201 ? 290 GLU   A CD  1 
ATOM   2238 O  OE1 . GLU   A 1 290 ? -15.63738 -23.37315 -0.57961  1.000 18.46483 ? 290 GLU   A OE1 1 
ATOM   2239 O  OE2 . GLU   A 1 290 ? -17.21113 -21.86640 -0.04109  1.000 17.75312 ? 290 GLU   A OE2 1 
ATOM   2240 N  N   . PHE   A 1 291 ? -17.81879 -22.66092 6.35567   1.000 13.39324 ? 291 PHE   A N   1 
ATOM   2241 C  CA  . PHE   A 1 291 ? -18.14589 -21.82211 7.50833   1.000 14.15715 ? 291 PHE   A CA  1 
ATOM   2242 C  C   . PHE   A 1 291 ? -17.00494 -21.87750 8.52393   1.000 13.26841 ? 291 PHE   A C   1 
ATOM   2243 O  O   . PHE   A 1 291 ? -16.68836 -22.95774 9.04234   1.000 13.05202 ? 291 PHE   A O   1 
ATOM   2244 C  CB  . PHE   A 1 291 ? -19.43629 -22.28908 8.18737   1.000 16.36600 ? 291 PHE   A CB  1 
ATOM   2245 C  CG  . PHE   A 1 291 ? -20.67301 -22.17102 7.34788   1.000 16.16063 ? 291 PHE   A CG  1 
ATOM   2246 C  CD1 . PHE   A 1 291 ? -21.31288 -20.94833 7.20927   1.000 21.15520 ? 291 PHE   A CD1 1 
ATOM   2247 C  CD2 . PHE   A 1 291 ? -21.19668 -23.28269 6.70122   1.000 16.96997 ? 291 PHE   A CD2 1 
ATOM   2248 C  CE1 . PHE   A 1 291 ? -22.46791 -20.83620 6.44517   1.000 21.55086 ? 291 PHE   A CE1 1 
ATOM   2249 C  CE2 . PHE   A 1 291 ? -22.35203 -23.17091 5.93732   1.000 21.25022 ? 291 PHE   A CE2 1 
ATOM   2250 C  CZ  . PHE   A 1 291 ? -22.98418 -21.94488 5.81857   1.000 21.42294 ? 291 PHE   A CZ  1 
ATOM   2251 N  N   . THR   A 1 292 ? -16.44432 -20.71630 8.87631   1.000 12.94800 ? 292 THR   A N   1 
ATOM   2252 C  CA  . THR   A 1 292 ? -15.41326 -20.67991 9.91783   1.000 15.73078 ? 292 THR   A CA  1 
ATOM   2253 C  C   . THR   A 1 292 ? -16.04953 -20.70609 11.30253  1.000 14.90377 ? 292 THR   A C   1 
ATOM   2254 O  O   . THR   A 1 292 ? -17.25133 -20.46994 11.46249  1.000 15.30713 ? 292 THR   A O   1 
ATOM   2255 C  CB  . THR   A 1 292 ? -14.57104 -19.41782 9.80845   1.000 16.40530 ? 292 THR   A CB  1 
ATOM   2256 O  OG1 . THR   A 1 292 ? -15.39700 -18.28916 10.13273  1.000 15.99379 ? 292 THR   A OG1 1 
ATOM   2257 C  CG2 . THR   A 1 292 ? -14.01117 -19.27708 8.40179   1.000 14.09165 ? 292 THR   A CG2 1 
ATOM   2258 N  N   . PRO   A 1 293 ? -15.26308 -20.96854 12.34009  1.000 15.02605 ? 293 PRO   A N   1 
ATOM   2259 C  CA  . PRO   A 1 293 ? -15.81883 -20.83418 13.69862  1.000 14.28509 ? 293 PRO   A CA  1 
ATOM   2260 C  C   . PRO   A 1 293 ? -16.38385 -19.44167 13.94946  1.000 18.11715 ? 293 PRO   A C   1 
ATOM   2261 O  O   . PRO   A 1 293 ? -17.45881 -19.30940 14.55012  1.000 18.05761 ? 293 PRO   A O   1 
ATOM   2262 C  CB  . PRO   A 1 293 ? -14.62399 -21.18386 14.59598  1.000 17.85459 ? 293 PRO   A CB  1 
ATOM   2263 C  CG  . PRO   A 1 293 ? -13.82492 -22.14917 13.76271  1.000 16.66548 ? 293 PRO   A CG  1 
ATOM   2264 C  CD  . PRO   A 1 293 ? -13.93846 -21.62596 12.34649  1.000 15.75539 ? 293 PRO   A CD  1 
ATOM   2265 N  N   . PHE   A 1 294 ? -15.73626 -18.39927 13.41721  1.000 18.43003 ? 294 PHE   A N   1 
ATOM   2266 C  CA  . PHE   A 1 294 ? -16.27287 -17.04777 13.55863  1.000 20.93219 ? 294 PHE   A CA  1 
ATOM   2267 C  C   . PHE   A 1 294 ? -17.62993 -16.91335 12.88698  1.000 20.49697 ? 294 PHE   A C   1 
ATOM   2268 O  O   . PHE   A 1 294 ? -18.54088 -16.28130 13.44057  1.000 22.18027 ? 294 PHE   A O   1 
ATOM   2269 C  CB  . PHE   A 1 294 ? -15.29217 -16.02042 12.98369  1.000 21.71606 ? 294 PHE   A CB  1 
ATOM   2270 C  CG  . PHE   A 1 294 ? -15.89964 -14.65003 12.76666  1.000 29.72627 ? 294 PHE   A CG  1 
ATOM   2271 C  CD1 . PHE   A 1 294 ? -15.75607 -13.65987 13.72340  1.000 32.25149 ? 294 PHE   A CD1 1 
ATOM   2272 C  CD2 . PHE   A 1 294 ? -16.58060 -14.34254 11.58504  1.000 31.33845 ? 294 PHE   A CD2 1 
ATOM   2273 C  CE1 . PHE   A 1 294 ? -16.31383 -12.40212 13.53603  1.000 34.71105 ? 294 PHE   A CE1 1 
ATOM   2274 C  CE2 . PHE   A 1 294 ? -17.14419 -13.08319 11.39034  1.000 32.80234 ? 294 PHE   A CE2 1 
ATOM   2275 C  CZ  . PHE   A 1 294 ? -16.99947 -12.11167 12.37025  1.000 34.27397 ? 294 PHE   A CZ  1 
ATOM   2276 N  N   . ASP   A 1 295 ? -17.77089 -17.46315 11.67424  1.000 16.53973 ? 295 ASP   A N   1 
ATOM   2277 C  CA  . ASP   A 1 295 ? -19.04628 -17.39953 10.96687  1.000 15.92048 ? 295 ASP   A CA  1 
ATOM   2278 C  C   . ASP   A 1 295 ? -20.16012 -18.03305 11.77677  1.000 20.23480 ? 295 ASP   A C   1 
ATOM   2279 O  O   . ASP   A 1 295 ? -21.27917 -17.51599 11.80587  1.000 19.29254 ? 295 ASP   A O   1 
ATOM   2280 C  CB  . ASP   A 1 295 ? -18.95491 -18.11305 9.62551   1.000 15.63003 ? 295 ASP   A CB  1 
ATOM   2281 C  CG  . ASP   A 1 295 ? -17.96816 -17.46793 8.69213   1.000 19.37863 ? 295 ASP   A CG  1 
ATOM   2282 O  OD1 . ASP   A 1 295 ? -17.58149 -16.30500 8.94121   1.000 22.47298 ? 295 ASP   A OD1 1 
ATOM   2283 O  OD2 . ASP   A 1 295 ? -17.56478 -18.15243 7.73349   1.000 16.77159 ? 295 ASP   A OD2 1 
ATOM   2284 N  N   . VAL   A 1 296 ? -19.87667 -19.17070 12.42186  1.000 15.17053 ? 296 VAL   A N   1 
ATOM   2285 C  CA  . VAL   A 1 296 ? -20.90731 -19.85942 13.19253  1.000 16.18655 ? 296 VAL   A CA  1 
ATOM   2286 C  C   . VAL   A 1 296 ? -21.30474 -19.01963 14.39412  1.000 17.76425 ? 296 VAL   A C   1 
ATOM   2287 O  O   . VAL   A 1 296 ? -22.49150 -18.81467 14.66371  1.000 18.94775 ? 296 VAL   A O   1 
ATOM   2288 C  CB  . VAL   A 1 296 ? -20.43082 -21.26037 13.62185  1.000 16.75885 ? 296 VAL   A CB  1 
ATOM   2289 C  CG1 . VAL   A 1 296 ? -21.43234 -21.87510 14.60294  1.000 17.37054 ? 296 VAL   A CG1 1 
ATOM   2290 C  CG2 . VAL   A 1 296 ? -20.27781 -22.16435 12.41135  1.000 14.17239 ? 296 VAL   A CG2 1 
ATOM   2291 N  N   . VAL   A 1 297 ? -20.31443 -18.49372 15.11620  1.000 19.68333 ? 297 VAL   A N   1 
ATOM   2292 C  CA  . VAL   A 1 297 ? -20.60642 -17.65748 16.27561  1.000 21.58441 ? 297 VAL   A CA  1 
ATOM   2293 C  C   . VAL   A 1 297 ? -21.38067 -16.41229 15.85479  1.000 23.66007 ? 297 VAL   A C   1 
ATOM   2294 O  O   . VAL   A 1 297 ? -22.35043 -16.02190 16.50992  1.000 26.46759 ? 297 VAL   A O   1 
ATOM   2295 C  CB  . VAL   A 1 297 ? -19.30422 -17.29755 17.01700  1.000 21.94073 ? 297 VAL   A CB  1 
ATOM   2296 C  CG1 . VAL   A 1 297 ? -19.57771 -16.27443 18.10495  1.000 23.85470 ? 297 VAL   A CG1 1 
ATOM   2297 C  CG2 . VAL   A 1 297 ? -18.66281 -18.54627 17.62288  1.000 25.63816 ? 297 VAL   A CG2 1 
ATOM   2298 N  N   . ARG   A 1 298 ? -20.97931 -15.78062 14.74522  1.000 24.26280 ? 298 ARG   A N   1 
ATOM   2299 C  CA  . ARG   A 1 298 ? -21.67560 -14.57968 14.28556  1.000 29.35805 ? 298 ARG   A CA  1 
ATOM   2300 C  C   . ARG   A 1 298 ? -23.14557 -14.86869 14.02033  1.000 28.70435 ? 298 ARG   A C   1 
ATOM   2301 O  O   . ARG   A 1 298 ? -24.02693 -14.11152 14.44435  1.000 31.26271 ? 298 ARG   A O   1 
ATOM   2302 C  CB  . ARG   A 1 298 ? -21.01379 -14.01869 13.01857  1.000 27.23164 ? 298 ARG   A CB  1 
ATOM   2303 C  CG  . ARG   A 1 298 ? -21.98858 -13.18788 12.14651  1.000 34.70557 ? 298 ARG   A CG  1 
ATOM   2304 C  CD  . ARG   A 1 298 ? -21.33229 -12.37256 11.01123  1.000 36.91021 ? 298 ARG   A CD  1 
ATOM   2305 N  NE  . ARG   A 1 298 ? -21.10898 -13.13451 9.78472   1.000 37.99679 ? 298 ARG   A NE  1 
ATOM   2306 C  CZ  . ARG   A 1 298 ? -21.65450 -12.85648 8.60306   1.000 29.55664 ? 298 ARG   A CZ  1 
ATOM   2307 N  NH1 . ARG   A 1 298 ? -22.49797 -11.84333 8.44081   1.000 30.86003 ? 298 ARG   A NH1 1 
ATOM   2308 N  NH2 . ARG   A 1 298 ? -21.35588 -13.61935 7.55785   1.000 29.06022 ? 298 ARG   A NH2 1 
ATOM   2309 N  N   . GLN   A 1 299 ? -23.42815 -15.97750 13.33527  1.000 23.60284 ? 299 GLN   A N   1 
ATOM   2310 C  CA  . GLN   A 1 299 ? -24.78960 -16.26903 12.90015  1.000 24.40018 ? 299 GLN   A CA  1 
ATOM   2311 C  C   . GLN   A 1 299 ? -25.65048 -16.85338 14.00881  1.000 28.94056 ? 299 GLN   A C   1 
ATOM   2312 O  O   . GLN   A 1 299 ? -26.83851 -16.52155 14.10566  1.000 29.72842 ? 299 GLN   A O   1 
ATOM   2313 C  CB  . GLN   A 1 299 ? -24.77394 -17.22040 11.70319  1.000 24.47185 ? 299 GLN   A CB  1 
ATOM   2314 C  CG  . GLN   A 1 299 ? -26.10981 -17.25833 10.99666  1.000 21.78271 ? 299 GLN   A CG  1 
ATOM   2315 C  CD  . GLN   A 1 299 ? -26.05727 -18.00170 9.68917   1.000 18.09606 ? 299 GLN   A CD  1 
ATOM   2316 O  OE1 . GLN   A 1 299 ? -27.08313 -18.50176 9.20778   1.000 21.09012 ? 299 GLN   A OE1 1 
ATOM   2317 N  NE2 . GLN   A 1 299 ? -24.86050 -18.10203 9.10802   1.000 18.92297 ? 299 GLN   A NE2 1 
ATOM   2318 N  N   . CYS   A 1 300 ? -25.09159 -17.74249 14.82893  1.000 26.42397 ? 300 CYS   A N   1 
ATOM   2319 C  CA  . CYS   A 1 300 ? -25.82295 -18.36422 15.92560  1.000 27.05664 ? 300 CYS   A CA  1 
ATOM   2320 C  C   . CYS   A 1 300 ? -25.83074 -17.50408 17.21037  1.000 33.82357 ? 300 CYS   A C   1 
ATOM   2321 O  O   . CYS   A 1 300 ? -26.30688 -17.97595 18.25151  1.000 44.79973 ? 300 CYS   A O   1 
ATOM   2322 C  CB  . CYS   A 1 300 ? -25.25346 -19.76864 16.20868  1.000 21.17348 ? 300 CYS   A CB  1 
ATOM   2323 S  SG  . CYS   A 1 300 ? -25.20928 -20.96526 14.80142  1.000 28.99433 ? 300 CYS   A SG  1 
ATOM   2324 N  N   . SER   A 1 301 ? -25.33294 -16.24340 17.14650  1.000 37.52130 ? 301 SER   A N   1 
ATOM   2325 C  CA  . SER   A 1 301 ? -25.33390 -15.24486 18.22365  1.000 40.99712 ? 301 SER   A CA  1 
ATOM   2326 C  C   . SER   A 1 301 ? -25.83922 -13.87556 17.77639  1.000 42.13356 ? 301 SER   A C   1 
ATOM   2327 O  O   . SER   A 1 301 ? -26.53451 -13.20706 18.54815  1.000 45.34783 ? 301 SER   A O   1 
ATOM   2328 C  CB  . SER   A 1 301 ? -23.92608 -15.09692 18.84690  1.000 44.61452 ? 301 SER   A CB  1 
ATOM   2329 O  OG  . SER   A 1 301 ? -23.81460 -13.89518 19.59763  1.000 53.40918 ? 301 SER   A OG  1 
ATOM   2330 N  N   . GLY   A 1 302 ? -25.49071 -13.42686 16.56769  1.000 41.57168 ? 302 GLY   A N   1 
ATOM   2331 C  CA  . GLY   A 1 302 ? -26.22769 -12.34225 15.93157  1.000 44.30805 ? 302 GLY   A CA  1 
ATOM   2332 C  C   . GLY   A 1 302 ? -25.58950 -10.96792 15.86718  1.000 45.36445 ? 302 GLY   A C   1 
ATOM   2333 O  O   . GLY   A 1 302 ? -26.25245 -9.95904  16.13449  1.000 47.97861 ? 302 GLY   A O   1 
ATOM   2334 N  N   . VAL   A 1 303 ? -24.32229 -10.90393 15.48977  1.000 46.58055 ? 303 VAL   A N   1 
ATOM   2335 C  CA  . VAL   A 1 303 ? -23.60349 -9.63336  15.45659  1.000 49.66795 ? 303 VAL   A CA  1 
ATOM   2336 C  C   . VAL   A 1 303 ? -23.98902 -8.85673  14.20052  1.000 46.72027 ? 303 VAL   A C   1 
ATOM   2337 O  O   . VAL   A 1 303 ? -24.10377 -9.42729  13.10682  1.000 46.13600 ? 303 VAL   A O   1 
ATOM   2338 C  CB  . VAL   A 1 303 ? -22.08486 -9.88328  15.53218  1.000 45.99549 ? 303 VAL   A CB  1 
ATOM   2339 C  CG1 . VAL   A 1 303 ? -21.30363 -8.58955  15.33057  1.000 50.81636 ? 303 VAL   A CG1 1 
ATOM   2340 C  CG2 . VAL   A 1 303 ? -21.72795 -10.53731 16.86333  1.000 46.76615 ? 303 VAL   A CG2 1 
ATOM   2341 N  N   . THR   A 1 304 ? -24.19884 -7.54642  14.35624  1.000 46.05860 ? 304 THR   A N   1 
ATOM   2342 C  CA  . THR   A 1 304 ? -24.52379 -6.63642  13.26245  1.000 43.72051 ? 304 THR   A CA  1 
ATOM   2343 C  C   . THR   A 1 304 ? -23.31006 -5.77463  12.92448  1.000 48.12227 ? 304 THR   A C   1 
ATOM   2344 O  O   . THR   A 1 304 ? -22.22323 -5.93839  13.49004  1.000 51.34747 ? 304 THR   A O   1 
ATOM   2345 C  CB  . THR   A 1 304 ? -25.72445 -5.75453  13.61868  1.000 38.97867 ? 304 THR   A CB  1 
ATOM   2346 O  OG1 . THR   A 1 304 ? -25.52480 -5.16148  14.90990  1.000 46.48818 ? 304 THR   A OG1 1 
ATOM   2347 C  CG2 . THR   A 1 304 ? -26.99207 -6.57501  13.65027  1.000 30.21989 ? 304 THR   A CG2 1 
ATOM   2348 N  N   . PHE   A 1 305 ? -23.50495 -4.84529  11.98511  1.000 45.71284 ? 305 PHE   A N   1 
ATOM   2349 C  CA  . PHE   A 1 305 ? -22.42440 -3.98911  11.50099  1.000 49.56706 ? 305 PHE   A CA  1 
ATOM   2350 C  C   . PHE   A 1 305 ? -22.99713 -2.62546  11.13739  1.000 49.99090 ? 305 PHE   A C   1 
ATOM   2351 O  O   . PHE   A 1 305 ? -24.03788 -2.54278  10.47507  1.000 47.66955 ? 305 PHE   A O   1 
ATOM   2352 C  CB  . PHE   A 1 305 ? -21.72617 -4.62657  10.28832  1.000 44.77173 ? 305 PHE   A CB  1 
ATOM   2353 C  CG  . PHE   A 1 305 ? -21.42829 -6.08428  10.47579  1.000 44.92926 ? 305 PHE   A CG  1 
ATOM   2354 C  CD1 . PHE   A 1 305 ? -20.27811 -6.49357  11.13091  1.000 40.92278 ? 305 PHE   A CD1 1 
ATOM   2355 C  CD2 . PHE   A 1 305 ? -22.34423 -7.04883  10.05840  1.000 42.19638 ? 305 PHE   A CD2 1 
ATOM   2356 C  CE1 . PHE   A 1 305 ? -20.02755 -7.83824  11.33084  1.000 43.06069 ? 305 PHE   A CE1 1 
ATOM   2357 C  CE2 . PHE   A 1 305 ? -22.10433 -8.39559  10.26426  1.000 36.99652 ? 305 PHE   A CE2 1 
ATOM   2358 C  CZ  . PHE   A 1 305 ? -20.94696 -8.78980  10.90529  1.000 42.84176 ? 305 PHE   A CZ  1 
ATOM   2359 N  N   . GLN   A 1 306 ? -22.32195 -1.56455  11.56988  1.000 50.74786 ? 306 GLN   A N   1 
ATOM   2360 C  CA  . GLN   A 1 306 ? -22.80489 -0.21340  11.31474  1.000 51.27662 ? 306 GLN   A CA  1 
ATOM   2361 C  C   . GLN   A 1 306 ? -21.65880 0.73103   10.96410  1.000 50.44135 ? 306 GLN   A C   1 
ATOM   2362 O  O   . GLN   A 1 306 ? -21.43035 1.04086   9.78982   1.000 49.98808 ? 306 GLN   A O   1 
ATOM   2363 C  CB  . GLN   A 1 306 ? -23.57577 0.30823   12.53011  1.000 52.49689 ? 306 GLN   A CB  1 
ATOM   2364 C  CG  . GLN   A 1 306 ? -24.52091 1.46819   12.23080  1.000 55.92658 ? 306 GLN   A CG  1 
ATOM   2365 C  CD  . GLN   A 1 306 ? -25.45355 1.75940   13.38937  1.000 57.20222 ? 306 GLN   A CD  1 
ATOM   2366 O  OE1 . GLN   A 1 306 ? -25.25484 1.25458   14.49601  1.000 62.77146 ? 306 GLN   A OE1 1 
ATOM   2367 N  NE2 . GLN   A 1 306 ? -26.47600 2.58002   13.14516  1.000 53.16582 ? 306 GLN   A NE2 1 
HETATM 2368 N  N1  . A1ARX B 2 .   ? -12.92291 -12.89079 -17.33412 1.000 33.52272 ? 401 A1ARX A N1  1 
HETATM 2369 C  C4  . A1ARX B 2 .   ? -12.58697 -10.32151 -17.42471 1.000 34.31956 ? 401 A1ARX A C4  1 
HETATM 2370 C  C5  . A1ARX B 2 .   ? -10.54635 -13.43540 -17.89614 1.000 32.29696 ? 401 A1ARX A C5  1 
HETATM 2371 C  C6  . A1ARX B 2 .   ? -9.55565  -13.75330 -18.84586 1.000 35.63735 ? 401 A1ARX A C6  1 
HETATM 2372 C  C7  . A1ARX B 2 .   ? -9.90238  -13.86736 -20.19622 1.000 35.53914 ? 401 A1ARX A C7  1 
HETATM 2373 C  C8  . A1ARX B 2 .   ? -11.21342 -13.65626 -20.59931 1.000 36.97128 ? 401 A1ARX A C8  1 
HETATM 2374 C  C10 . A1ARX B 2 .   ? -8.15507  -13.98390 -18.40374 1.000 34.04496 ? 401 A1ARX A C10 1 
HETATM 2375 C  C13 . A1ARX B 2 .   ? -5.51479  -14.42120 -17.53084 1.000 34.88265 ? 401 A1ARX A C13 1 
HETATM 2376 C  C15 . A1ARX B 2 .   ? -7.30826  -14.86322 -19.08507 1.000 37.97441 ? 401 A1ARX A C15 1 
HETATM 2377 C  C17 . A1ARX B 2 .   ? -15.04114 -15.92189 -16.73593 1.000 28.80377 ? 401 A1ARX A C17 1 
HETATM 2378 C  C20 . A1ARX B 2 .   ? -12.43006 -10.07784 -18.94216 1.000 36.18095 ? 401 A1ARX A C20 1 
HETATM 2379 C  C21 . A1ARX B 2 .   ? -12.33417 -8.66231  -19.41956 1.000 40.35260 ? 401 A1ARX A C21 1 
HETATM 2380 C  C22 . A1ARX B 2 .   ? -14.57616 -9.10739  -20.20935 1.000 41.70786 ? 401 A1ARX A C22 1 
HETATM 2381 C  C1  . A1ARX B 2 .   ? -13.65593 -13.99103 -16.72668 1.000 28.77846 ? 401 A1ARX A C1  1 
HETATM 2382 C  C11 . A1ARX B 2 .   ? -7.65408  -13.32838 -17.27334 1.000 31.50284 ? 401 A1ARX A C11 1 
HETATM 2383 C  C12 . A1ARX B 2 .   ? -6.35712  -13.55153 -16.85231 1.000 31.23729 ? 401 A1ARX A C12 1 
HETATM 2384 C  C14 . A1ARX B 2 .   ? -6.00424  -15.07596 -18.64987 1.000 36.13127 ? 401 A1ARX A C14 1 
HETATM 2385 C  C16 . A1ARX B 2 .   ? -14.38660 -14.92624 -17.44274 1.000 33.24266 ? 401 A1ARX A C16 1 
HETATM 2386 C  C18 . A1ARX B 2 .   ? -14.96625 -15.96909 -15.36038 1.000 25.39084 ? 401 A1ARX A C18 1 
HETATM 2387 C  C19 . A1ARX B 2 .   ? -13.62710 -14.12054 -15.33683 1.000 27.60644 ? 401 A1ARX A C19 1 
HETATM 2388 C  C2  . A1ARX B 2 .   ? -11.86323 -13.22073 -18.29491 1.000 35.49538 ? 401 A1ARX A C2  1 
HETATM 2389 C  C3  . A1ARX B 2 .   ? -13.28764 -11.59556 -16.95259 1.000 32.44514 ? 401 A1ARX A C3  1 
HETATM 2390 C  C9  . A1ARX B 2 .   ? -12.18014 -13.34096 -19.65850 1.000 34.99359 ? 401 A1ARX A C9  1 
HETATM 2391 N  N2  . A1ARX B 2 .   ? -14.25928 -15.08362 -14.65107 1.000 21.11190 ? 401 A1ARX A N2  1 
HETATM 2392 O  O1  . A1ARX B 2 .   ? -14.17595 -11.44359 -16.12708 1.000 33.51558 ? 401 A1ARX A O1  1 
HETATM 2393 O  O2  . A1ARX B 2 .   ? -13.35153 -8.31755  -20.22449 1.000 44.42891 ? 401 A1ARX A O2  1 
HETATM 2394 O  O3  . A1ARX B 2 .   ? -11.42200 -7.93427  -19.10902 1.000 43.48825 ? 401 A1ARX A O3  1 
HETATM 2395 CL CL1 . A1ARX B 2 .   ? -5.80134  -12.70551 -15.43528 1.000 37.29728 ? 401 A1ARX A CL1 1 
HETATM 2396 CL CL2 . A1ARX B 2 .   ? -15.96350 -17.12138 -17.57325 1.000 39.77301 ? 401 A1ARX A CL2 1 
HETATM 2397 O  O   . HOH   C 3 .   ? -16.76459 -16.69577 -21.67626 1.000 39.54712 ? 501 HOH   A O   1 
HETATM 2398 O  O   . HOH   C 3 .   ? 0.66748   0.85254   -3.03875  1.000 39.01212 ? 502 HOH   A O   1 
HETATM 2399 O  O   . HOH   C 3 .   ? -24.81478 -2.78404  8.51106   1.000 38.98270 ? 503 HOH   A O   1 
HETATM 2400 O  O   . HOH   C 3 .   ? -24.14638 -42.46959 9.40914   1.000 39.85641 ? 504 HOH   A O   1 
HETATM 2401 O  O   . HOH   C 3 .   ? -1.68842  8.49734   -25.85368 1.000 37.20759 ? 505 HOH   A O   1 
HETATM 2402 O  O   . HOH   C 3 .   ? -2.15479  -4.04311  -27.33179 1.000 52.13188 ? 506 HOH   A O   1 
HETATM 2403 O  O   . HOH   C 3 .   ? -13.70045 -22.53038 -17.21119 1.000 29.76566 ? 507 HOH   A O   1 
HETATM 2404 O  O   . HOH   C 3 .   ? -27.19789 -4.82556  16.54472  1.000 33.70424 ? 508 HOH   A O   1 
HETATM 2405 O  O   . HOH   C 3 .   ? -18.79643 -19.57109 3.10431   1.000 46.51184 ? 509 HOH   A O   1 
HETATM 2406 O  O   . HOH   C 3 .   ? -12.93024 -28.89777 -5.66289  1.000 35.21167 ? 510 HOH   A O   1 
HETATM 2407 O  O   . HOH   C 3 .   ? -23.08845 -28.49454 2.09113   1.000 29.65616 ? 511 HOH   A O   1 
HETATM 2408 O  O   . HOH   C 3 .   ? -1.82209  -34.62171 16.25859  1.000 36.45880 ? 512 HOH   A O   1 
HETATM 2409 O  O   . HOH   C 3 .   ? -25.04399 8.78109   -11.29524 1.000 41.88505 ? 513 HOH   A O   1 
HETATM 2410 O  O   . HOH   C 3 .   ? -7.34337  -25.40827 8.06403   1.000 28.03709 ? 514 HOH   A O   1 
HETATM 2411 O  O   . HOH   C 3 .   ? -7.40647  -24.25076 5.41341   1.000 22.99800 ? 515 HOH   A O   1 
HETATM 2412 O  O   . HOH   C 3 .   ? -3.43170  -24.48594 -6.49340  1.000 22.06296 ? 516 HOH   A O   1 
HETATM 2413 O  O   . HOH   C 3 .   ? -14.30948 -0.05372  12.74384  1.000 40.56525 ? 517 HOH   A O   1 
HETATM 2414 O  O   . HOH   C 3 .   ? -5.58709  2.46204   -25.70495 1.000 35.65631 ? 518 HOH   A O   1 
HETATM 2415 O  O   . HOH   C 3 .   ? -4.84187  -21.63079 13.60332  1.000 32.26185 ? 519 HOH   A O   1 
HETATM 2416 O  O   . HOH   C 3 .   ? 4.87624   -14.84649 -14.82645 1.000 47.18679 ? 520 HOH   A O   1 
HETATM 2417 O  O   . HOH   C 3 .   ? 3.08727   -10.41432 -6.52513  1.000 20.92676 ? 521 HOH   A O   1 
HETATM 2418 O  O   . HOH   C 3 .   ? -3.32104  -24.12788 23.71637  1.000 40.74866 ? 522 HOH   A O   1 
HETATM 2419 O  O   . HOH   C 3 .   ? -16.79914 -13.97966 6.19044   1.000 17.84140 ? 523 HOH   A O   1 
HETATM 2420 O  O   . HOH   C 3 .   ? -12.95485 8.64554   -17.81442 1.000 34.39674 ? 524 HOH   A O   1 
HETATM 2421 O  O   . HOH   C 3 .   ? -19.30925 -20.67413 0.71577   1.000 25.40094 ? 525 HOH   A O   1 
HETATM 2422 O  O   . HOH   C 3 .   ? -19.61174 -24.34413 0.12990   1.000 29.32958 ? 526 HOH   A O   1 
HETATM 2423 O  O   . HOH   C 3 .   ? -21.06421 -12.02004 -19.25621 1.000 34.20862 ? 527 HOH   A O   1 
HETATM 2424 O  O   . HOH   C 3 .   ? -6.13174  -11.08468 6.92224   1.000 29.78771 ? 528 HOH   A O   1 
HETATM 2425 O  O   . HOH   C 3 .   ? -11.19645 -33.44838 0.66612   1.000 26.55814 ? 529 HOH   A O   1 
HETATM 2426 O  O   . HOH   C 3 .   ? -12.98280 -5.07470  8.61512   1.000 23.10219 ? 530 HOH   A O   1 
HETATM 2427 O  O   . HOH   C 3 .   ? -17.35542 -8.92274  11.28720  1.000 35.70916 ? 531 HOH   A O   1 
HETATM 2428 O  O   . HOH   C 3 .   ? -3.71455  -42.03065 7.83764   1.000 39.92450 ? 532 HOH   A O   1 
HETATM 2429 O  O   . HOH   C 3 .   ? -28.75000 -29.53469 20.45757  1.000 26.82479 ? 533 HOH   A O   1 
HETATM 2430 O  O   . HOH   C 3 .   ? -18.46235 -26.82372 1.53855   1.000 26.28992 ? 534 HOH   A O   1 
HETATM 2431 O  O   . HOH   C 3 .   ? -0.05792  -1.00696  -24.89586 1.000 31.63747 ? 535 HOH   A O   1 
HETATM 2432 O  O   . HOH   C 3 .   ? -19.93330 -26.26768 28.59722  1.000 37.76179 ? 536 HOH   A O   1 
HETATM 2433 O  O   . HOH   C 3 .   ? -8.46283  3.03419   -24.82955 1.000 38.95670 ? 537 HOH   A O   1 
HETATM 2434 O  O   . HOH   C 3 .   ? -17.49774 2.98771   6.95262   1.000 26.98089 ? 538 HOH   A O   1 
HETATM 2435 O  O   . HOH   C 3 .   ? -18.31100 -33.84335 25.48566  1.000 29.39321 ? 539 HOH   A O   1 
HETATM 2436 O  O   . HOH   C 3 .   ? -31.15124 -31.24147 7.67683   1.000 27.62188 ? 540 HOH   A O   1 
HETATM 2437 O  O   . HOH   C 3 .   ? -21.95088 -13.53832 -11.34648 1.000 22.94341 ? 541 HOH   A O   1 
HETATM 2438 O  O   . HOH   C 3 .   ? -19.99771 -36.68809 19.78939  1.000 29.38489 ? 542 HOH   A O   1 
HETATM 2439 O  O   . HOH   C 3 .   ? -8.43854  -25.79917 24.11373  1.000 33.88910 ? 543 HOH   A O   1 
HETATM 2440 O  O   . HOH   C 3 .   ? -4.20860  -34.35428 6.89338   1.000 30.13131 ? 544 HOH   A O   1 
HETATM 2441 O  O   . HOH   C 3 .   ? -25.08733 -38.13686 1.97061   1.000 38.21043 ? 545 HOH   A O   1 
HETATM 2442 O  O   . HOH   C 3 .   ? -31.61298 -28.71344 1.97072   1.000 36.87383 ? 546 HOH   A O   1 
HETATM 2443 O  O   . HOH   C 3 .   ? -15.87789 2.62259   -18.83282 1.000 28.67045 ? 547 HOH   A O   1 
HETATM 2444 O  O   . HOH   C 3 .   ? -11.02689 -21.59099 9.12017   1.000 19.12579 ? 548 HOH   A O   1 
HETATM 2445 O  O   . HOH   C 3 .   ? -2.49339  -5.43634  2.34395   1.000 16.25748 ? 549 HOH   A O   1 
HETATM 2446 O  O   . HOH   C 3 .   ? -16.20366 -34.92675 3.43042   1.000 26.00572 ? 550 HOH   A O   1 
HETATM 2447 O  O   . HOH   C 3 .   ? -20.81276 -39.52107 14.06444  1.000 28.71241 ? 551 HOH   A O   1 
HETATM 2448 O  O   . HOH   C 3 .   ? -2.39597  -28.00225 -4.27792  1.000 27.63550 ? 552 HOH   A O   1 
HETATM 2449 O  O   . HOH   C 3 .   ? -7.41417  13.63760  -7.01405  1.000 31.42927 ? 553 HOH   A O   1 
HETATM 2450 O  O   . HOH   C 3 .   ? -12.86248 -37.54742 1.69477   1.000 29.71393 ? 554 HOH   A O   1 
HETATM 2451 O  O   . HOH   C 3 .   ? -6.04794  -6.90642  0.09595   1.000 16.71501 ? 555 HOH   A O   1 
HETATM 2452 O  O   . HOH   C 3 .   ? -3.06158  -1.47473  -4.27179  1.000 24.45989 ? 556 HOH   A O   1 
HETATM 2453 O  O   . HOH   C 3 .   ? -29.71083 -19.20133 13.85187  1.000 26.80488 ? 557 HOH   A O   1 
HETATM 2454 O  O   . HOH   C 3 .   ? -15.62842 -2.13209  -24.15828 1.000 40.81776 ? 558 HOH   A O   1 
HETATM 2455 O  O   . HOH   C 3 .   ? -1.94644  -24.93564 -9.01318  1.000 27.88176 ? 559 HOH   A O   1 
HETATM 2456 O  O   . HOH   C 3 .   ? -0.00000  -8.63695  0.00000   0.50  14.59097 ? 560 HOH   A O   1 
HETATM 2457 O  O   . HOH   C 3 .   ? -1.95422  -24.58710 -1.33815  1.000 24.71553 ? 561 HOH   A O   1 
HETATM 2458 O  O   . HOH   C 3 .   ? -2.04128  -2.99344  -25.06262 1.000 36.30455 ? 562 HOH   A O   1 
HETATM 2459 O  O   . HOH   C 3 .   ? -9.77293  -7.17050  8.81471   1.000 28.90307 ? 563 HOH   A O   1 
HETATM 2460 O  O   . HOH   C 3 .   ? 1.18816   -21.06589 -15.52802 1.000 31.39283 ? 564 HOH   A O   1 
HETATM 2461 O  O   . HOH   C 3 .   ? -7.69871  -41.83918 20.44121  1.000 40.00843 ? 565 HOH   A O   1 
HETATM 2462 O  O   . HOH   C 3 .   ? -14.80110 -21.36700 -2.38418  1.000 15.54715 ? 566 HOH   A O   1 
HETATM 2463 O  O   . HOH   C 3 .   ? -29.73880 -24.84933 7.03688   1.000 31.24457 ? 567 HOH   A O   1 
HETATM 2464 O  O   . HOH   C 3 .   ? -15.50651 -21.58060 18.90314  1.000 26.12347 ? 568 HOH   A O   1 
HETATM 2465 O  O   . HOH   C 3 .   ? -17.60916 -5.51706  -16.86995 1.000 23.52371 ? 569 HOH   A O   1 
HETATM 2466 O  O   . HOH   C 3 .   ? -21.55588 3.51077   8.68602   1.000 41.46877 ? 570 HOH   A O   1 
HETATM 2467 O  O   . HOH   C 3 .   ? -2.52718  14.63818  -15.01904 1.000 39.43185 ? 571 HOH   A O   1 
HETATM 2468 O  O   . HOH   C 3 .   ? 3.33388   -11.18131 -17.97624 1.000 33.08734 ? 572 HOH   A O   1 
HETATM 2469 O  O   . HOH   C 3 .   ? -6.51712  -17.20669 -6.64046  1.000 11.54797 ? 573 HOH   A O   1 
HETATM 2470 O  O   . HOH   C 3 .   ? -22.295   -16.553   -12.845   1.000 26.14334 ? 574 HOH   A O   1 
HETATM 2471 O  O   . HOH   C 3 .   ? -17.33548 -5.93112  -6.44703  1.000 14.08040 ? 575 HOH   A O   1 
HETATM 2472 O  O   . HOH   C 3 .   ? -10.06496 9.52540   -18.45252 1.000 34.23593 ? 576 HOH   A O   1 
HETATM 2473 O  O   . HOH   C 3 .   ? -18.69915 -13.93145 8.08198   1.000 39.02791 ? 577 HOH   A O   1 
HETATM 2474 O  O   . HOH   C 3 .   ? -18.08354 -25.35622 7.50273   1.000 12.42881 ? 578 HOH   A O   1 
HETATM 2475 O  O   . HOH   C 3 .   ? -5.46225  -22.47455 -17.86093 1.000 29.13103 ? 579 HOH   A O   1 
HETATM 2476 O  O   . HOH   C 3 .   ? -3.34098  -21.76564 20.38262  1.000 31.34041 ? 580 HOH   A O   1 
HETATM 2477 O  O   . HOH   C 3 .   ? 2.27456   5.12190   -19.36449 1.000 29.56739 ? 581 HOH   A O   1 
HETATM 2478 O  O   . HOH   C 3 .   ? 4.82340   -8.70656  -8.15938  1.000 24.69678 ? 582 HOH   A O   1 
HETATM 2479 O  O   . HOH   C 3 .   ? -3.51020  -23.84252 13.09241  1.000 27.27747 ? 583 HOH   A O   1 
HETATM 2480 O  O   . HOH   C 3 .   ? -3.08322  -24.08809 1.92607   1.000 24.82977 ? 584 HOH   A O   1 
HETATM 2481 O  O   . HOH   C 3 .   ? -19.59501 -43.76542 29.40981  1.000 43.30197 ? 585 HOH   A O   1 
HETATM 2482 O  O   . HOH   C 3 .   ? -19.34136 -18.17558 5.62385   1.000 17.08785 ? 586 HOH   A O   1 
HETATM 2483 O  O   . HOH   C 3 .   ? -25.85406 -1.25372  -6.49420  1.000 27.80258 ? 587 HOH   A O   1 
HETATM 2484 O  O   . HOH   C 3 .   ? -6.69400  -22.28379 10.66779  1.000 40.71697 ? 588 HOH   A O   1 
HETATM 2485 O  O   . HOH   C 3 .   ? -20.16279 3.14674   -0.29588  1.000 20.77547 ? 589 HOH   A O   1 
HETATM 2486 O  O   . HOH   C 3 .   ? -24.10026 -43.97478 4.54653   1.000 41.46960 ? 590 HOH   A O   1 
HETATM 2487 O  O   . HOH   C 3 .   ? 1.96874   -8.06969  -26.49226 1.000 45.02972 ? 591 HOH   A O   1 
HETATM 2488 O  O   . HOH   C 3 .   ? 1.11274   -12.64867 -12.82627 1.000 19.43582 ? 592 HOH   A O   1 
HETATM 2489 O  O   . HOH   C 3 .   ? -3.74574  -35.08915 9.64022   1.000 33.31196 ? 593 HOH   A O   1 
HETATM 2490 O  O   . HOH   C 3 .   ? -25.45016 -23.16990 26.24439  1.000 39.84353 ? 594 HOH   A O   1 
HETATM 2491 O  O   . HOH   C 3 .   ? -3.68015  -27.60982 9.40826   1.000 32.80177 ? 595 HOH   A O   1 
HETATM 2492 O  O   . HOH   C 3 .   ? -15.93566 -28.41938 0.19819   1.000 33.60138 ? 596 HOH   A O   1 
HETATM 2493 O  O   . HOH   C 3 .   ? -14.88564 -15.69741 9.24569   1.000 22.43787 ? 597 HOH   A O   1 
HETATM 2494 O  O   . HOH   C 3 .   ? -28.80438 -2.52106  -3.65245  1.000 18.94567 ? 598 HOH   A O   1 
HETATM 2495 O  O   . HOH   C 3 .   ? -10.67997 -27.15409 -9.15853  1.000 24.14469 ? 599 HOH   A O   1 
HETATM 2496 O  O   . HOH   C 3 .   ? -11.31549 -27.34677 -5.03584  1.000 25.32398 ? 600 HOH   A O   1 
HETATM 2497 O  O   . HOH   C 3 .   ? -20.70642 2.49500   -11.61366 1.000 29.36490 ? 601 HOH   A O   1 
HETATM 2498 O  O   . HOH   C 3 .   ? -1.55149  6.58922   -25.73458 1.000 41.64042 ? 602 HOH   A O   1 
HETATM 2499 O  O   . HOH   C 3 .   ? 1.13523   8.16427   -20.08015 1.000 34.38785 ? 603 HOH   A O   1 
HETATM 2500 O  O   . HOH   C 3 .   ? -7.29055  -6.79106  10.07483  1.000 41.77174 ? 604 HOH   A O   1 
HETATM 2501 O  O   . HOH   C 3 .   ? -7.66716  -20.25944 7.93498   1.000 24.42849 ? 605 HOH   A O   1 
HETATM 2502 O  O   . HOH   C 3 .   ? -11.36179 -7.02478  -25.23683 1.000 41.19221 ? 606 HOH   A O   1 
HETATM 2503 O  O   . HOH   C 3 .   ? -15.14137 -33.25832 1.73529   1.000 31.47696 ? 607 HOH   A O   1 
HETATM 2504 O  O   . HOH   C 3 .   ? -10.87773 -16.41588 -17.30156 1.000 29.58134 ? 608 HOH   A O   1 
HETATM 2505 O  O   . HOH   C 3 .   ? -1.66349  5.87920   -9.87584  1.000 26.75454 ? 609 HOH   A O   1 
HETATM 2506 O  O   . HOH   C 3 .   ? -11.46264 -9.58683  4.45950   1.000 13.87395 ? 610 HOH   A O   1 
HETATM 2507 O  O   . HOH   C 3 .   ? -9.14701  -42.37082 15.83376  1.000 44.57548 ? 611 HOH   A O   1 
HETATM 2508 O  O   . HOH   C 3 .   ? 5.25578   1.05866   -17.78511 1.000 29.34640 ? 612 HOH   A O   1 
HETATM 2509 O  O   . HOH   C 3 .   ? -20.07034 7.34542   -5.31269  1.000 28.20881 ? 613 HOH   A O   1 
HETATM 2510 O  O   . HOH   C 3 .   ? -9.35939  1.51685   8.33241   1.000 30.18700 ? 614 HOH   A O   1 
HETATM 2511 O  O   . HOH   C 3 .   ? -6.99391  -43.20944 14.87149  1.000 41.96726 ? 615 HOH   A O   1 
HETATM 2512 O  O   . HOH   C 3 .   ? 1.40139   -13.44786 -4.33252  1.000 12.08381 ? 616 HOH   A O   1 
HETATM 2513 O  O   . HOH   C 3 .   ? -16.52730 -22.34282 -9.12943  1.000 20.38052 ? 617 HOH   A O   1 
HETATM 2514 O  O   . HOH   C 3 .   ? -12.90459 15.22080  -4.81487  1.000 34.32545 ? 618 HOH   A O   1 
HETATM 2515 O  O   . HOH   C 3 .   ? -12.61597 -18.66302 19.19838  1.000 33.59050 ? 619 HOH   A O   1 
HETATM 2516 O  O   . HOH   C 3 .   ? 0.70214   -20.29705 -13.08985 1.000 26.36681 ? 620 HOH   A O   1 
HETATM 2517 O  O   . HOH   C 3 .   ? -6.88140  2.22333   5.05554   1.000 36.24837 ? 621 HOH   A O   1 
HETATM 2518 O  O   . HOH   C 3 .   ? -12.12366 -29.47629 -2.22325  1.000 26.17821 ? 622 HOH   A O   1 
HETATM 2519 O  O   . HOH   C 3 .   ? -32.94124 -18.82324 17.96939  1.000 29.56536 ? 623 HOH   A O   1 
HETATM 2520 O  O   . HOH   C 3 .   ? -26.05008 -29.30448 23.34825  1.000 34.46723 ? 624 HOH   A O   1 
HETATM 2521 O  O   . HOH   C 3 .   ? 0.29652   -23.43960 -10.87987 1.000 27.14932 ? 625 HOH   A O   1 
HETATM 2522 O  O   . HOH   C 3 .   ? -0.74909  -24.99885 -13.01079 1.000 28.70518 ? 626 HOH   A O   1 
HETATM 2523 O  O   . HOH   C 3 .   ? -14.92882 -42.08357 16.41707  1.000 34.38548 ? 627 HOH   A O   1 
HETATM 2524 O  O   . HOH   C 3 .   ? 1.36025   -23.70149 -19.68766 1.000 33.21631 ? 628 HOH   A O   1 
HETATM 2525 O  O   . HOH   C 3 .   ? 1.09342   -11.98675 -8.13489  1.000 10.63309 ? 629 HOH   A O   1 
HETATM 2526 O  O   . HOH   C 3 .   ? -3.27099  -28.97761 -11.47935 1.000 31.03366 ? 630 HOH   A O   1 
HETATM 2527 O  O   . HOH   C 3 .   ? -16.16355 -40.09710 3.58848   1.000 30.34383 ? 631 HOH   A O   1 
HETATM 2528 O  O   . HOH   C 3 .   ? -10.14258 -25.88966 -6.82156  1.000 18.33908 ? 632 HOH   A O   1 
HETATM 2529 O  O   . HOH   C 3 .   ? -4.53227  -8.65243  -14.29862 1.000 17.10485 ? 633 HOH   A O   1 
HETATM 2530 O  O   . HOH   C 3 .   ? -8.17566  -25.91194 -12.92404 1.000 24.16324 ? 634 HOH   A O   1 
HETATM 2531 O  O   . HOH   C 3 .   ? 1.72126   -12.30091 -16.29923 1.000 25.57324 ? 635 HOH   A O   1 
HETATM 2532 O  O   . HOH   C 3 .   ? 3.85126   -5.15281  -11.86505 1.000 22.98665 ? 636 HOH   A O   1 
HETATM 2533 O  O   . HOH   C 3 .   ? -0.10318  -4.58408  -27.98699 1.000 41.55293 ? 637 HOH   A O   1 
HETATM 2534 O  O   . HOH   C 3 .   ? -22.26863 -2.37622  6.19466   1.000 29.94585 ? 638 HOH   A O   1 
HETATM 2535 O  O   . HOH   C 3 .   ? -22.451   -19.332   -1.111    1.000 45.08063 ? 639 HOH   A O   1 
HETATM 2536 O  O   . HOH   C 3 .   ? -7.42375  4.73684   -2.31884  1.000 24.64595 ? 640 HOH   A O   1 
HETATM 2537 O  O   . HOH   C 3 .   ? 0.55690   8.77167   -14.53563 1.000 30.42077 ? 641 HOH   A O   1 
HETATM 2538 O  O   . HOH   C 3 .   ? -31.21446 -24.22168 9.34714   1.000 30.75074 ? 642 HOH   A O   1 
HETATM 2539 O  O   . HOH   C 3 .   ? -25.61686 -26.37756 5.90264   1.000 22.00300 ? 643 HOH   A O   1 
HETATM 2540 O  O   . HOH   C 3 .   ? 5.05112   -8.17863  -17.48022 1.000 29.41444 ? 644 HOH   A O   1 
HETATM 2541 O  O   . HOH   C 3 .   ? -12.97800 -14.93349 7.35996   1.000 22.04557 ? 645 HOH   A O   1 
HETATM 2542 O  O   . HOH   C 3 .   ? 3.71966   -7.45079  -24.60128 1.000 34.79050 ? 646 HOH   A O   1 
HETATM 2543 O  O   . HOH   C 3 .   ? -24.42147 -26.49034 3.36563   1.000 32.80823 ? 647 HOH   A O   1 
HETATM 2544 O  O   . HOH   C 3 .   ? -8.22047  -29.86754 -7.60843  1.000 31.15232 ? 648 HOH   A O   1 
HETATM 2545 O  O   . HOH   C 3 .   ? -14.17631 -24.95964 25.89606  1.000 34.16709 ? 649 HOH   A O   1 
HETATM 2546 O  O   . HOH   C 3 .   ? 1.36093   -13.75284 -10.22687 1.000 15.42409 ? 650 HOH   A O   1 
HETATM 2547 O  O   . HOH   C 3 .   ? -17.42472 -6.25036  -19.98584 1.000 31.08333 ? 651 HOH   A O   1 
HETATM 2548 O  O   . HOH   C 3 .   ? 3.67579   2.16435   -13.03032 1.000 25.79528 ? 652 HOH   A O   1 
HETATM 2549 O  O   . HOH   C 3 .   ? -0.00000  -16.60279 0.00000   0.50  11.05053 ? 653 HOH   A O   1 
HETATM 2550 O  O   . HOH   C 3 .   ? -22.28023 -16.71063 9.14998   1.000 16.73026 ? 654 HOH   A O   1 
HETATM 2551 O  O   . HOH   C 3 .   ? -10.87718 -25.86214 23.33592  1.000 31.09414 ? 655 HOH   A O   1 
HETATM 2552 O  O   . HOH   C 3 .   ? -4.37215  -21.11008 6.49385   1.000 22.55166 ? 656 HOH   A O   1 
HETATM 2553 O  O   . HOH   C 3 .   ? -21.62367 8.22566   -9.35515  1.000 45.79697 ? 657 HOH   A O   1 
HETATM 2554 O  O   . HOH   C 3 .   ? -11.92615 5.88465   4.47372   1.000 28.06798 ? 658 HOH   A O   1 
HETATM 2555 O  O   . HOH   C 3 .   ? -2.24461  -15.40229 2.45132   1.000 10.85157 ? 659 HOH   A O   1 
HETATM 2556 O  O   . HOH   C 3 .   ? -18.92261 -35.14301 2.87684   1.000 26.48332 ? 660 HOH   A O   1 
HETATM 2557 O  O   . HOH   C 3 .   ? -1.10463  -19.72362 3.96093   1.000 13.53022 ? 661 HOH   A O   1 
HETATM 2558 O  O   . HOH   C 3 .   ? -23.94330 -17.08370 -0.23051  1.000 22.97761 ? 662 HOH   A O   1 
HETATM 2559 O  O   . HOH   C 3 .   ? -18.95586 -16.25334 -19.37963 1.000 32.26624 ? 663 HOH   A O   1 
HETATM 2560 O  O   . HOH   C 3 .   ? -22.65926 -43.66404 11.27081  1.000 41.68274 ? 664 HOH   A O   1 
HETATM 2561 O  O   . HOH   C 3 .   ? -5.15473  -1.98323  -25.51544 1.000 35.47596 ? 665 HOH   A O   1 
HETATM 2562 O  O   . HOH   C 3 .   ? -4.99316  -24.57623 4.06214   1.000 26.65510 ? 666 HOH   A O   1 
HETATM 2563 O  O   . HOH   C 3 .   ? 2.02632   -16.97391 -21.30174 1.000 42.43195 ? 667 HOH   A O   1 
HETATM 2564 O  O   . HOH   C 3 .   ? -11.12549 -36.28754 25.10427  1.000 45.60209 ? 668 HOH   A O   1 
HETATM 2565 O  O   . HOH   C 3 .   ? -28.64014 -25.89340 3.71857   1.000 36.34516 ? 669 HOH   A O   1 
HETATM 2566 O  O   . HOH   C 3 .   ? -23.62368 1.85532   4.63354   1.000 38.53732 ? 670 HOH   A O   1 
HETATM 2567 O  O   . HOH   C 3 .   ? -6.50242  -31.52496 21.81555  1.000 32.17572 ? 671 HOH   A O   1 
HETATM 2568 O  O   . HOH   C 3 .   ? -22.00642 -17.32621 6.29197   1.000 17.14433 ? 672 HOH   A O   1 
HETATM 2569 O  O   . HOH   C 3 .   ? -3.04248  -13.77503 6.54204   1.000 15.75109 ? 673 HOH   A O   1 
HETATM 2570 O  O   . HOH   C 3 .   ? -12.86365 -29.49091 24.47282  1.000 30.82293 ? 674 HOH   A O   1 
HETATM 2571 O  O   . HOH   C 3 .   ? -11.37785 -31.68809 23.57671  1.000 30.08046 ? 675 HOH   A O   1 
HETATM 2572 O  O   . HOH   C 3 .   ? -4.47614  -19.10874 -18.32558 1.000 32.39427 ? 676 HOH   A O   1 
HETATM 2573 O  O   . HOH   C 3 .   ? -19.41038 -19.98408 24.73307  1.000 33.43120 ? 677 HOH   A O   1 
HETATM 2574 O  O   . HOH   C 3 .   ? -14.26384 10.48460  0.71302   1.000 45.27966 ? 678 HOH   A O   1 
HETATM 2575 O  O   . HOH   C 3 .   ? -8.24320  10.98034  -18.87322 1.000 42.86072 ? 679 HOH   A O   1 
HETATM 2576 O  O   . HOH   C 3 .   ? -24.64129 -12.96792 -11.68913 1.000 32.73294 ? 680 HOH   A O   1 
HETATM 2577 O  O   . HOH   C 3 .   ? -0.42499  3.15835   -27.99183 1.000 32.57951 ? 681 HOH   A O   1 
HETATM 2578 O  O   . HOH   C 3 .   ? -8.33935  -27.50378 9.59236   1.000 19.33548 ? 682 HOH   A O   1 
HETATM 2579 O  O   . HOH   C 3 .   ? -0.72852  -28.10885 17.18341  1.000 30.94497 ? 683 HOH   A O   1 
HETATM 2580 O  O   . HOH   C 3 .   ? 1.15794   -2.23164  -27.27271 1.000 31.66902 ? 684 HOH   A O   1 
HETATM 2581 O  O   . HOH   C 3 .   ? -10.18627 3.99066   6.01091   1.000 24.43566 ? 685 HOH   A O   1 
HETATM 2582 O  O   . HOH   C 3 .   ? -4.94567  -1.36470  4.93406   1.000 23.23136 ? 686 HOH   A O   1 
HETATM 2583 O  O   . HOH   C 3 .   ? -3.90647  11.67822  -21.52248 1.000 33.33270 ? 687 HOH   A O   1 
HETATM 2584 O  O   . HOH   C 3 .   ? -13.60280 -30.10624 -0.11598  1.000 29.05889 ? 688 HOH   A O   1 
HETATM 2585 O  O   . HOH   C 3 .   ? -1.25436  -25.05406 17.31357  1.000 27.71469 ? 689 HOH   A O   1 
HETATM 2586 O  O   . HOH   C 3 .   ? 2.35439   -17.08203 -9.43728  1.000 22.36482 ? 690 HOH   A O   1 
HETATM 2587 O  O   . HOH   C 3 .   ? -4.21339  12.66858  -3.50598  1.000 40.52304 ? 691 HOH   A O   1 
HETATM 2588 O  O   . HOH   C 3 .   ? 0.22863   -17.39427 -2.70826  1.000 12.48261 ? 692 HOH   A O   1 
HETATM 2589 O  O   . HOH   C 3 .   ? -7.67533  -32.80747 -4.96418  1.000 36.55014 ? 693 HOH   A O   1 
HETATM 2590 O  O   . HOH   C 3 .   ? 5.52167   -17.34236 -13.27405 1.000 37.79566 ? 694 HOH   A O   1 
HETATM 2591 O  O   . HOH   C 3 .   ? -12.76559 -18.28787 12.71322  1.000 24.21660 ? 695 HOH   A O   1 
HETATM 2592 O  O   . HOH   C 3 .   ? 5.12993   -5.42594  -26.01142 1.000 36.48577 ? 696 HOH   A O   1 
HETATM 2593 O  O   . HOH   C 3 .   ? -21.24371 3.88648   -8.91701  1.000 38.91441 ? 697 HOH   A O   1 
HETATM 2594 O  O   . HOH   C 3 .   ? 4.77012   -3.52056  -6.72264  1.000 23.98759 ? 698 HOH   A O   1 
HETATM 2595 O  O   . HOH   C 3 .   ? -25.82950 -31.54321 0.00000   0.50  22.23547 ? 699 HOH   A O   1 
HETATM 2596 O  O   . HOH   C 3 .   ? -7.63247  -28.68608 24.50217  1.000 34.88525 ? 700 HOH   A O   1 
HETATM 2597 O  O   . HOH   C 3 .   ? -2.12374  -31.23360 21.49792  1.000 37.92551 ? 701 HOH   A O   1 
HETATM 2598 O  O   . HOH   C 3 .   ? -24.93031 -31.72648 24.75795  1.000 39.10673 ? 702 HOH   A O   1 
HETATM 2599 O  O   . HOH   C 3 .   ? -23.58191 -39.88121 2.87356   1.000 44.26003 ? 703 HOH   A O   1 
HETATM 2600 O  O   . HOH   C 3 .   ? -25.99762 -17.44127 21.31400  1.000 40.28965 ? 704 HOH   A O   1 
HETATM 2601 O  O   . HOH   C 3 .   ? -22.30963 1.28274   -13.60026 1.000 45.25055 ? 705 HOH   A O   1 
HETATM 2602 O  O   . HOH   C 3 .   ? -0.78461  10.33203  -19.19642 1.000 36.02295 ? 706 HOH   A O   1 
HETATM 2603 O  O   . HOH   C 3 .   ? -8.29013  -18.13436 -18.24248 1.000 35.26975 ? 707 HOH   A O   1 
HETATM 2604 O  O   . HOH   C 3 .   ? -31.080   -35.044   15.049    1.000 30.58589 ? 708 HOH   A O   1 
HETATM 2605 O  O   . HOH   C 3 .   ? -20.14594 -36.12088 23.05759  1.000 34.21997 ? 709 HOH   A O   1 
HETATM 2606 O  O   . HOH   C 3 .   ? 8.14903   -4.52078  -28.00472 1.000 45.76893 ? 710 HOH   A O   1 
HETATM 2607 O  O   . HOH   C 3 .   ? -1.24507  -30.18283 -7.27227  1.000 36.76653 ? 711 HOH   A O   1 
HETATM 2608 O  O   . HOH   C 3 .   ? -4.52037  -28.50893 -0.72722  1.000 27.68692 ? 712 HOH   A O   1 
HETATM 2609 O  O   . HOH   C 3 .   ? -31.65666 -34.54771 10.40102  1.000 35.86204 ? 713 HOH   A O   1 
HETATM 2610 O  O   . HOH   C 3 .   ? -15.40357 -5.99068  -22.85299 1.000 39.06835 ? 714 HOH   A O   1 
HETATM 2611 O  O   . HOH   C 3 .   ? -3.74675  13.77205  -18.56567 1.000 39.56341 ? 715 HOH   A O   1 
HETATM 2612 O  O   . HOH   C 3 .   ? -8.13597  3.70343   4.76695   1.000 33.90843 ? 716 HOH   A O   1 
HETATM 2613 O  O   . HOH   C 3 .   ? -15.05385 -11.89506 9.07398   1.000 25.38429 ? 717 HOH   A O   1 
HETATM 2614 O  O   . HOH   C 3 .   ? -2.25802  -39.15282 21.71890  1.000 40.79467 ? 718 HOH   A O   1 
HETATM 2615 O  O   . HOH   C 3 .   ? -3.76154  6.92147   -27.73231 1.000 42.71017 ? 719 HOH   A O   1 
HETATM 2616 O  O   . HOH   C 3 .   ? -5.17082  -13.68673 8.18642   1.000 24.40315 ? 720 HOH   A O   1 
HETATM 2617 O  O   . HOH   C 3 .   ? -31.80209 -36.40237 8.92093   1.000 34.07052 ? 721 HOH   A O   1 
HETATM 2618 O  O   . HOH   C 3 .   ? -8.26475  6.95539   -26.69439 1.000 44.95295 ? 722 HOH   A O   1 
HETATM 2619 O  O   . HOH   C 3 .   ? -6.67605  8.22597   -28.59806 1.000 45.36424 ? 723 HOH   A O   1 
HETATM 2620 O  O   . HOH   C 3 .   ? -22.64668 -3.86557  7.88680   1.000 38.65162 ? 724 HOH   A O   1 
HETATM 2621 O  O   . HOH   C 3 .   ? -11.66826 -4.11992  10.82444  1.000 33.72123 ? 725 HOH   A O   1 
HETATM 2622 O  O   . HOH   C 3 .   ? 0.16825   11.04328  -15.92579 1.000 34.58346 ? 726 HOH   A O   1 
HETATM 2623 O  O   . HOH   C 3 .   ? -4.18645  8.47977   -3.17333  1.000 39.26330 ? 727 HOH   A O   1 
HETATM 2624 O  O   . HOH   C 3 .   ? -27.56264 -29.36784 0.15579   1.000 32.13383 ? 728 HOH   A O   1 
HETATM 2625 O  O   . HOH   C 3 .   ? 2.71206   0.90283   -2.67818  1.000 51.98550 ? 729 HOH   A O   1 
HETATM 2626 O  O   . HOH   C 3 .   ? -27.92607 -21.00368 2.03218   1.000 23.74442 ? 730 HOH   A O   1 
HETATM 2627 O  O   . HOH   C 3 .   ? -29.03562 -20.54140 16.05981  1.000 29.54659 ? 731 HOH   A O   1 
HETATM 2628 O  O   . HOH   C 3 .   ? -3.45323  -7.33612  0.74304   1.000 20.38745 ? 732 HOH   A O   1 
HETATM 2629 O  O   . HOH   C 3 .   ? -12.91889 -42.67796 17.59690  1.000 38.15353 ? 733 HOH   A O   1 
HETATM 2630 O  O   . HOH   C 3 .   ? -13.65806 -7.72649  8.91457   1.000 26.97381 ? 734 HOH   A O   1 
HETATM 2631 O  O   . HOH   C 3 .   ? -1.72652  -0.11841  0.70420   1.000 38.03409 ? 735 HOH   A O   1 
HETATM 2632 O  O   . HOH   C 3 .   ? 2.72958   3.90646   -15.14852 1.000 30.89349 ? 736 HOH   A O   1 
HETATM 2633 O  O   . HOH   C 3 .   ? -21.26058 -21.15014 26.60833  1.000 40.84023 ? 737 HOH   A O   1 
HETATM 2634 O  O   . HOH   C 3 .   ? -15.19054 -9.71115  9.82878   1.000 30.14331 ? 738 HOH   A O   1 
HETATM 2635 O  O   . HOH   C 3 .   ? -11.42751 -17.00426 10.18637  1.000 28.74035 ? 739 HOH   A O   1 
HETATM 2636 O  O   . HOH   C 3 .   ? -21.44076 4.28988   -7.00336  1.000 32.79151 ? 740 HOH   A O   1 
HETATM 2637 O  O   . HOH   C 3 .   ? -3.709    -19.443   12.770    1.000 41.25746 ? 741 HOH   A O   1 
HETATM 2638 O  O   . HOH   C 3 .   ? -0.92266  8.31064   -10.41504 1.000 35.70970 ? 742 HOH   A O   1 
HETATM 2639 O  O   . HOH   C 3 .   ? -33.60051 -24.82829 12.38610  1.000 48.88476 ? 743 HOH   A O   1 
HETATM 2640 O  O   . HOH   C 3 .   ? 4.24324   -10.35695 -16.51695 1.000 32.50422 ? 744 HOH   A O   1 
HETATM 2641 O  O   . HOH   C 3 .   ? -8.58870  -11.72178 7.52222   1.000 31.35592 ? 745 HOH   A O   1 
HETATM 2642 O  O   . HOH   C 3 .   ? -3.37917  -28.39756 1.19703   1.000 41.51447 ? 746 HOH   A O   1 
HETATM 2643 O  O   . HOH   C 3 .   ? -1.18605  -23.90003 14.64418  1.000 27.43980 ? 747 HOH   A O   1 
HETATM 2644 O  O   . HOH   C 3 .   ? -22.62068 3.61502   0.36382   1.000 28.94706 ? 748 HOH   A O   1 
HETATM 2645 O  O   . HOH   C 3 .   ? -0.67712  -22.34662 -23.01226 1.000 41.89879 ? 749 HOH   A O   1 
HETATM 2646 O  O   . HOH   C 3 .   ? -15.23808 -16.86801 16.65159  1.000 39.60733 ? 750 HOH   A O   1 
HETATM 2647 O  O   . HOH   C 3 .   ? 0.88970   4.91185   -2.55997  1.000 49.92986 ? 751 HOH   A O   1 
HETATM 2648 O  O   . HOH   C 3 .   ? -20.10170 -7.73682  -19.12236 1.000 35.17239 ? 752 HOH   A O   1 
HETATM 2649 O  O   . HOH   C 3 .   ? -4.67614  -23.95623 -22.09702 1.000 45.17128 ? 753 HOH   A O   1 
HETATM 2650 O  O   . HOH   C 3 .   ? -31.89360 -28.30153 9.80591   1.000 35.93122 ? 754 HOH   A O   1 
HETATM 2651 O  O   . HOH   C 3 .   ? -1.03446  -27.57711 -12.46255 1.000 32.82743 ? 755 HOH   A O   1 
HETATM 2652 O  O   . HOH   C 3 .   ? -27.581   -33.118   26.362    1.000 36.09529 ? 756 HOH   A O   1 
HETATM 2653 O  O   . HOH   C 3 .   ? -11.87349 -12.24591 8.26274   1.000 33.59090 ? 757 HOH   A O   1 
HETATM 2654 O  O   . HOH   C 3 .   ? -12.99828 -28.41638 -9.02507  1.000 31.91398 ? 758 HOH   A O   1 
HETATM 2655 O  O   . HOH   C 3 .   ? -10.18920 -19.22763 9.13668   1.000 37.30012 ? 759 HOH   A O   1 
HETATM 2656 O  O   . HOH   C 3 .   ? -12.71220 -26.94986 24.89261  1.000 34.73550 ? 760 HOH   A O   1 
HETATM 2657 O  O   . HOH   C 3 .   ? -7.59631  -21.23877 12.09695  1.000 31.11055 ? 761 HOH   A O   1 
HETATM 2658 O  O   . HOH   C 3 .   ? 1.698     -20.793   -22.374   1.000 36.58521 ? 762 HOH   A O   1 
HETATM 2659 O  O   . HOH   C 3 .   ? 4.04199   3.65767   -17.58132 1.000 30.87698 ? 763 HOH   A O   1 
HETATM 2660 O  O   . HOH   C 3 .   ? 3.42567   -12.79992 -14.29159 1.000 33.18794 ? 764 HOH   A O   1 
HETATM 2661 O  O   . HOH   C 3 .   ? -0.43789  -26.91522 -7.98929  1.000 37.12457 ? 765 HOH   A O   1 
HETATM 2662 O  O   . HOH   C 3 .   ? -1.13815  -37.47127 11.27272  1.000 39.40282 ? 766 HOH   A O   1 
HETATM 2663 O  O   . HOH   C 3 .   ? -10.73032 -9.87583  7.18114   1.000 27.18163 ? 767 HOH   A O   1 
HETATM 2664 O  O   . HOH   C 3 .   ? 3.61024   -19.26949 -10.48238 1.000 30.40912 ? 768 HOH   A O   1 
HETATM 2665 O  O   . HOH   C 3 .   ? -8.45545  -11.52142 10.11995  1.000 38.47173 ? 769 HOH   A O   1 
HETATM 2666 O  O   . HOH   C 3 .   ? -1.45854  -25.48414 -5.44219  1.000 27.67428 ? 770 HOH   A O   1 
HETATM 2667 O  O   . HOH   C 3 .   ? -20.91574 -34.88994 25.17915  1.000 35.74971 ? 771 HOH   A O   1 
HETATM 2668 O  O   . HOH   C 3 .   ? -2.91788  -24.03599 10.52888  1.000 29.93199 ? 772 HOH   A O   1 
HETATM 2669 O  O   . HOH   C 3 .   ? -33.42757 -30.51826 5.93936   1.000 37.83617 ? 773 HOH   A O   1 
HETATM 2670 O  O   . HOH   C 3 .   ? 6.74173   -13.57689 -16.30486 1.000 42.14639 ? 774 HOH   A O   1 
HETATM 2671 O  O   . HOH   C 3 .   ? -1.76659  6.16856   -7.46223  1.000 31.83115 ? 775 HOH   A O   1 
HETATM 2672 O  O   . HOH   C 3 .   ? -12.30550 -9.41348  8.90964   1.000 45.81745 ? 776 HOH   A O   1 
HETATM 2673 O  O   . HOH   C 3 .   ? 0.89481   -24.55756 -22.27892 1.000 37.72248 ? 777 HOH   A O   1 
HETATM 2674 O  O   . HOH   C 3 .   ? -8.38767  -22.34385 8.78356   1.000 25.52430 ? 778 HOH   A O   1 
HETATM 2675 O  O   . HOH   C 3 .   ? 1.09461   2.42069   -1.36992  1.000 42.10845 ? 779 HOH   A O   1 
HETATM 2676 O  O   . HOH   C 3 .   ? -5.52640  6.32935   -1.96923  1.000 42.19175 ? 780 HOH   A O   1 
HETATM 2677 O  O   . HOH   C 3 .   ? -7.73539  -28.12466 -14.67107 1.000 30.57513 ? 781 HOH   A O   1 
HETATM 2678 O  O   . HOH   C 3 .   ? -21.29398 -15.34195 -20.37782 1.000 37.11487 ? 782 HOH   A O   1 
HETATM 2679 O  O   . HOH   C 3 .   ? -17.97878 14.38990  -5.25470  1.000 39.49946 ? 783 HOH   A O   1 
HETATM 2680 O  O   . HOH   C 3 .   ? -4.426    -21.137   8.996     1.000 29.49099 ? 784 HOH   A O   1 
HETATM 2681 O  O   . HOH   C 3 .   ? -5.26182  0.74174   6.35949   1.000 38.31590 ? 785 HOH   A O   1 
HETATM 2682 O  O   . HOH   C 3 .   ? -25.82950 -38.77039 0.00000   0.50  46.86354 ? 786 HOH   A O   1 
HETATM 2683 O  O   . HOH   C 3 .   ? -6.67033  -18.32803 9.59218   1.000 28.67250 ? 787 HOH   A O   1 
HETATM 2684 O  O   . HOH   C 3 .   ? -23.891   -25.031   -0.954    1.000 48.05579 ? 788 HOH   A O   1 
HETATM 2685 O  O   . HOH   C 3 .   ? -0.77701  -23.84463 -3.70380  1.000 26.08513 ? 789 HOH   A O   1 
HETATM 2686 O  O   . HOH   C 3 .   ? -1.32333  -28.35182 10.16515  1.000 42.29048 ? 790 HOH   A O   1 
HETATM 2687 O  O   . HOH   C 3 .   ? -25.035   1.120     18.838    1.000 41.72811 ? 791 HOH   A O   1 
HETATM 2688 O  O   . HOH   C 3 .   ? -2.02563  -26.44545 2.32462   1.000 32.86054 ? 792 HOH   A O   1 
HETATM 2689 O  O   . HOH   C 3 .   ? -32.04004 -25.61262 10.98418  1.000 34.72154 ? 793 HOH   A O   1 
HETATM 2690 O  O   . HOH   C 3 .   ? -22.89581 -41.21955 12.70011  1.000 34.55112 ? 794 HOH   A O   1 
HETATM 2691 O  O   . HOH   C 3 .   ? 3.856     -14.790   -9.865    1.000 26.30935 ? 795 HOH   A O   1 
HETATM 2692 O  O   . HOH   C 3 .   ? -12.52056 -17.58933 -19.50414 1.000 36.21704 ? 796 HOH   A O   1 
HETATM 2693 O  O   . HOH   C 3 .   ? -15.30783 -17.74189 18.76974  1.000 34.60688 ? 797 HOH   A O   1 
HETATM 2694 O  O   . HOH   C 3 .   ? -0.00000  -24.04244 0.00000   0.50  28.49141 ? 798 HOH   A O   1 
HETATM 2695 O  O   . HOH   C 3 .   ? -1.15030  -34.95326 10.52632  1.000 37.42508 ? 799 HOH   A O   1 
HETATM 2696 O  O   . HOH   C 3 .   ? -11.36616 -17.89973 21.81860  1.000 42.19076 ? 800 HOH   A O   1 
HETATM 2697 O  O   . HOH   C 3 .   ? -3.31597  -23.36515 5.67685   1.000 23.91344 ? 801 HOH   A O   1 
HETATM 2698 O  O   . HOH   C 3 .   ? -4.48070  1.46513   2.47710   1.000 43.73558 ? 802 HOH   A O   1 
HETATM 2699 O  O   . HOH   C 3 .   ? 5.263     -15.036   -12.029   1.000 36.11469 ? 803 HOH   A O   1 
HETATM 2700 O  O   . HOH   C 3 .   ? -25.82950 -21.48853 0.00000   0.50  31.72875 ? 804 HOH   A O   1 
HETATM 2701 O  O   . HOH   C 3 .   ? -10.88964 -19.69560 11.35095  1.000 30.54114 ? 805 HOH   A O   1 
HETATM 2702 O  O   . HOH   C 3 .   ? 1.527     -22.369   -3.458    1.000 20.71240 ? 806 HOH   A O   1 
HETATM 2703 O  O   . HOH   C 3 .   ? -18.91353 12.25867  -6.82627  1.000 40.96655 ? 807 HOH   A O   1 
HETATM 2704 O  O   . HOH   C 3 .   ? -3.52511  1.60672   0.84726   1.000 47.37959 ? 808 HOH   A O   1 
HETATM 2705 O  O   . HOH   C 3 .   ? -11.27042 -33.59379 25.64214  1.000 32.84668 ? 809 HOH   A O   1 
HETATM 2706 O  O   . HOH   C 3 .   ? -0.88564  -30.37109 -10.05338 1.000 39.91179 ? 810 HOH   A O   1 
HETATM 2707 O  O   . HOH   C 3 .   ? -15.37962 -37.83426 2.62452   1.000 31.97786 ? 811 HOH   A O   1 
HETATM 2708 O  O   . HOH   C 3 .   ? -8.54289  -31.23432 23.74320  1.000 32.36133 ? 812 HOH   A O   1 
HETATM 2709 O  O   . HOH   C 3 .   ? -6.34616  -28.35084 -17.12007 1.000 34.55285 ? 813 HOH   A O   1 
HETATM 2710 O  O   . HOH   C 3 .   ? -21.21190 -35.97526 27.87066  1.000 45.90393 ? 814 HOH   A O   1 
HETATM 2711 O  O   . HOH   C 3 .   ? -0.261    -29.486   11.418    1.000 36.94040 ? 815 HOH   A O   1 
HETATM 2712 O  O   . HOH   C 3 .   ? -5.43449  -41.74201 25.05600  1.000 41.47210 ? 816 HOH   A O   1 
HETATM 2713 O  O   . HOH   C 3 .   ? -17.26130 -16.63560 21.03680  1.000 37.54470 ? 817 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   ? 0.21783 0.37950 0.36550 0.00262  0.10144  0.06359  1   SER   A N   
2    C  CA  . SER   A 1   ? 0.19808 0.35315 0.34117 -0.00325 0.09054  0.06947  1   SER   A CA  
3    C  C   . SER   A 1   ? 0.19168 0.34167 0.34946 -0.00480 0.07716  0.07009  1   SER   A C   
4    O  O   . SER   A 1   ? 0.17785 0.32906 0.34719 -0.00086 0.07547  0.06612  1   SER   A O   
5    C  CB  . SER   A 1   ? 0.29702 0.45650 0.44350 -0.00898 0.09195  0.07999  1   SER   A CB  
6    O  OG  . SER   A 1   ? 0.31552 0.48010 0.48629 -0.01176 0.08742  0.08594  1   SER   A OG  
7    N  N   . GLY   A 2   ? 0.15354 0.29689 0.30948 -0.01061 0.06764  0.07489  2   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.18729 0.32368 0.35062 -0.01310 0.05491  0.07361  2   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.17144 0.29905 0.31885 -0.01151 0.05119  0.06799  2   GLY   A C   
10   O  O   . GLY   A 2   ? 0.18792 0.31585 0.31995 -0.00728 0.05828  0.06351  2   GLY   A O   
11   N  N   . PHE   A 3   ? 0.13590 0.25562 0.28637 -0.01539 0.03976  0.06765  3   PHE   A N   
12   C  CA  . PHE   A 3   ? 0.13852 0.24852 0.27377 -0.01421 0.03497  0.06226  3   PHE   A CA  
13   C  C   . PHE   A 3   ? 0.17837 0.28088 0.31874 -0.01646 0.02311  0.05842  3   PHE   A C   
14   O  O   . PHE   A 3   ? 0.20383 0.30295 0.35259 -0.02312 0.01589  0.06196  3   PHE   A O   
15   C  CB  . PHE   A 3   ? 0.18996 0.29172 0.31102 -0.01696 0.03397  0.06586  3   PHE   A CB  
16   C  CG  . PHE   A 3   ? 0.18279 0.27574 0.28184 -0.01296 0.03199  0.05905  3   PHE   A CG  
17   C  CD1 . PHE   A 3   ? 0.23924 0.33746 0.32446 -0.00876 0.03956  0.05577  3   PHE   A CD1 
18   C  CD2 . PHE   A 3   ? 0.23153 0.31170 0.32408 -0.01385 0.02298  0.05552  3   PHE   A CD2 
19   C  CE1 . PHE   A 3   ? 0.22798 0.31992 0.29457 -0.00637 0.03669  0.04979  3   PHE   A CE1 
20   C  CE2 . PHE   A 3   ? 0.19184 0.26653 0.26738 -0.01032 0.02136  0.05026  3   PHE   A CE2 
21   C  CZ  . PHE   A 3   ? 0.20581 0.28698 0.26907 -0.00703 0.02750  0.04781  3   PHE   A CZ  
22   N  N   . ARG   A 4   ? 0.15632 0.25575 0.29067 -0.01154 0.02133  0.05109  4   ARG   A N   
23   C  CA  . ARG   A 4   ? 0.15032 0.24464 0.28813 -0.01307 0.01099  0.04808  4   ARG   A CA  
24   C  C   . ARG   A 4   ? 0.13686 0.21877 0.25478 -0.01023 0.00761  0.04025  4   ARG   A C   
25   O  O   . ARG   A 4   ? 0.17523 0.25557 0.28088 -0.00581 0.01352  0.03626  4   ARG   A O   
26   C  CB  . ARG   A 4   ? 0.14186 0.24688 0.29738 -0.00971 0.01195  0.04949  4   ARG   A CB  
27   C  CG  . ARG   A 4   ? 0.15275 0.26533 0.32353 -0.01294 0.01125  0.05578  4   ARG   A CG  
28   C  CD  . ARG   A 4   ? 0.17025 0.27814 0.34326 -0.02017 -0.00192 0.05691  4   ARG   A CD  
29   N  NE  . ARG   A 4   ? 0.20227 0.31798 0.39011 -0.02352 -0.00442 0.06266  4   ARG   A NE  
30   C  CZ  . ARG   A 4   ? 0.18548 0.29881 0.37540 -0.03078 -0.01536 0.06383  4   ARG   A CZ  
31   N  NH1 . ARG   A 4   ? 0.20192 0.30422 0.37888 -0.03524 -0.02396 0.05899  4   ARG   A NH1 
32   N  NH2 . ARG   A 4   ? 0.11467 0.23687 0.31918 -0.03407 -0.01735 0.06956  4   ARG   A NH2 
33   N  N   . LYS   A 5   ? 0.16130 0.23521 0.27597 -0.01340 -0.00190 0.03793  5   LYS   A N   
34   C  CA  . LYS   A 5   ? 0.18372 0.24821 0.28307 -0.01056 -0.00475 0.03127  5   LYS   A CA  
35   C  C   . LYS   A 5   ? 0.17127 0.24033 0.27600 -0.00573 -0.00300 0.02944  5   LYS   A C   
36   O  O   . LYS   A 5   ? 0.24317 0.31539 0.35796 -0.00672 -0.00859 0.03167  5   LYS   A O   
37   C  CB  . LYS   A 5   ? 0.23997 0.29494 0.33335 -0.01527 -0.01382 0.02918  5   LYS   A CB  
38   C  CG  . LYS   A 5   ? 0.30055 0.34477 0.37650 -0.01310 -0.01433 0.02355  5   LYS   A CG  
39   C  CD  . LYS   A 5   ? 0.30850 0.34179 0.37795 -0.01747 -0.01844 0.02205  5   LYS   A CD  
40   C  CE  . LYS   A 5   ? 0.32375 0.35316 0.39021 -0.01643 -0.01370 0.02431  5   LYS   A CE  
41   N  NZ  . LYS   A 5   ? 0.35882 0.37498 0.42033 -0.01959 -0.01643 0.02213  5   LYS   A NZ  
42   N  N   . MET   A 6   ? 0.11123 0.18033 0.20933 -0.00083 0.00454  0.02567  6   MET   A N   
43   C  CA  . MET   A 6   ? 0.12092 0.19297 0.22612 0.00434  0.00923  0.02362  6   MET   A CA  
44   C  C   . MET   A 6   ? 0.15146 0.21399 0.24410 0.00634  0.00749  0.01726  6   MET   A C   
45   O  O   . MET   A 6   ? 0.15418 0.21139 0.23116 0.00560  0.00817  0.01297  6   MET   A O   
46   C  CB  . MET   A 6   ? 0.14141 0.22003 0.24870 0.00761  0.02086  0.02294  6   MET   A CB  
47   C  CG  . MET   A 6   ? 0.20547 0.28499 0.32018 0.01366  0.02828  0.01937  6   MET   A CG  
48   S  SD  . MET   A 6   ? 0.34058 0.42667 0.45181 0.01644  0.04333  0.01685  6   MET   A SD  
49   C  CE  . MET   A 6   ? 0.18462 0.28437 0.31291 0.01291  0.04334  0.02803  6   MET   A CE  
50   N  N   . ALA   A 7   ? 0.10623 0.16749 0.20700 0.00841  0.00458  0.01797  7   ALA   A N   
51   C  CA  . ALA   A 7   ? 0.08843 0.14064 0.17971 0.00980  0.00329  0.01312  7   ALA   A CA  
52   C  C   . ALA   A 7   ? 0.12339 0.17351 0.21831 0.01484  0.01223  0.00856  7   ALA   A C   
53   O  O   . ALA   A 7   ? 0.12290 0.17908 0.22969 0.01826  0.01938  0.00977  7   ALA   A O   
54   C  CB  . ALA   A 7   ? 0.11684 0.16740 0.21285 0.00855  -0.00528 0.01741  7   ALA   A CB  
55   N  N   . PHE   A 8   ? 0.08720 0.12820 0.17207 0.01503  0.01259  0.00277  8   PHE   A N   
56   C  CA  . PHE   A 8   ? 0.09667 0.13213 0.18507 0.01912  0.02067  -0.00274 8   PHE   A CA  
57   C  C   . PHE   A 8   ? 0.08432 0.11921 0.19215 0.02362  0.02019  0.00290  8   PHE   A C   
58   O  O   . PHE   A 8   ? 0.10983 0.14649 0.22248 0.02209  0.01140  0.01002  8   PHE   A O   
59   C  CB  . PHE   A 8   ? 0.11953 0.14501 0.19270 0.01649  0.02020  -0.01034 8   PHE   A CB  
60   C  CG  . PHE   A 8   ? 0.13917 0.16671 0.19514 0.01292  0.02191  -0.01585 8   PHE   A CG  
61   C  CD1 . PHE   A 8   ? 0.19821 0.22584 0.24829 0.01382  0.03074  -0.02257 8   PHE   A CD1 
62   C  CD2 . PHE   A 8   ? 0.17650 0.20611 0.22205 0.00885  0.01500  -0.01398 8   PHE   A CD2 
63   C  CE1 . PHE   A 8   ? 0.29939 0.33058 0.33257 0.00996  0.03110  -0.02612 8   PHE   A CE1 
64   C  CE2 . PHE   A 8   ? 0.19082 0.22402 0.22266 0.00602  0.01578  -0.01689 8   PHE   A CE2 
65   C  CZ  . PHE   A 8   ? 0.20306 0.23756 0.22815 0.00616  0.02299  -0.02247 8   PHE   A CZ  
66   N  N   . PRO   A 9   ? 0.10413 0.13675 0.22334 0.02936  0.02982  0.00023  9   PRO   A N   
67   C  CA  . PRO   A 9   ? 0.13642 0.16764 0.27655 0.03484  0.02979  0.00672  9   PRO   A CA  
68   C  C   . PRO   A 9   ? 0.12606 0.14628 0.26031 0.03277  0.02345  0.00712  9   PRO   A C   
69   O  O   . PRO   A 9   ? 0.15820 0.16816 0.27683 0.02968  0.02514  -0.00144 9   PRO   A O   
70   C  CB  . PRO   A 9   ? 0.13452 0.16105 0.28368 0.04158  0.04404  0.00024  9   PRO   A CB  
71   C  CG  . PRO   A 9   ? 0.14197 0.17288 0.27609 0.03911  0.05091  -0.00736 9   PRO   A CG  
72   C  CD  . PRO   A 9   ? 0.10940 0.13944 0.22135 0.03113  0.04164  -0.00929 9   PRO   A CD  
73   N  N   . SER   A 10  ? 0.12636 0.15023 0.27256 0.03351  0.01538  0.01796  10  SER   A N   
74   C  CA  . SER   A 10  ? 0.12823 0.14471 0.26630 0.03004  0.00788  0.02074  10  SER   A CA  
75   C  C   . SER   A 10  ? 0.11136 0.11658 0.26151 0.03462  0.01133  0.02313  10  SER   A C   
76   O  O   . SER   A 10  ? 0.12266 0.12108 0.26626 0.03148  0.00623  0.02591  10  SER   A O   
77   C  CB  . SER   A 10  ? 0.08726 0.11376 0.22558 0.02634  -0.00401 0.03110  10  SER   A CB  
78   O  OG  . SER   A 10  ? 0.11719 0.15410 0.27723 0.03035  -0.00620 0.04124  10  SER   A OG  
79   N  N   . GLY   A 11  ? 0.11471 0.11714 0.28277 0.04208  0.02073  0.02231  11  GLY   A N   
80   C  CA  . GLY   A 11  ? 0.12901 0.12028 0.30741 0.04544  0.02358  0.02581  11  GLY   A CA  
81   C  C   . GLY   A 11  ? 0.13698 0.11076 0.30620 0.04284  0.02508  0.01931  11  GLY   A C   
82   O  O   . GLY   A 11  ? 0.16674 0.13474 0.33972 0.04196  0.02080  0.02707  11  GLY   A O   
83   N  N   . LYS   A 12  ? 0.13818 0.10517 0.29017 0.03881  0.03039  0.00497  12  LYS   A N   
84   C  CA  . LYS   A 12  ? 0.16036 0.11183 0.30103 0.03358  0.03136  -0.00251 12  LYS   A CA  
85   C  C   . LYS   A 12  ? 0.19634 0.15098 0.32812 0.02734  0.02057  0.00532  12  LYS   A C   
86   O  O   . LYS   A 12  ? 0.20716 0.15017 0.33862 0.02438  0.02005  0.00598  12  LYS   A O   
87   C  CB  . LYS   A 12  ? 0.20322 0.15158 0.32460 0.02861  0.03652  -0.01830 12  LYS   A CB  
88   C  CG  . LYS   A 12  ? 0.22754 0.16494 0.35307 0.03307  0.04967  -0.02984 12  LYS   A CG  
89   C  CD  . LYS   A 12  ? 0.30145 0.23964 0.40424 0.02702  0.05303  -0.04416 12  LYS   A CD  
90   C  CE  . LYS   A 12  ? 0.38034 0.30792 0.48203 0.03023  0.06624  -0.05645 12  LYS   A CE  
91   N  NZ  . LYS   A 12  ? 0.43777 0.37551 0.55307 0.03860  0.07199  -0.05003 12  LYS   A NZ  
92   N  N   . VAL   A 13  ? 0.14758 0.11707 0.27199 0.02495  0.01271  0.01096  13  VAL   A N   
93   C  CA  . VAL   A 13  ? 0.15269 0.12534 0.26746 0.01952  0.00389  0.01785  13  VAL   A CA  
94   C  C   . VAL   A 13  ? 0.12165 0.09695 0.24939 0.02241  -0.00178 0.03282  13  VAL   A C   
95   O  O   . VAL   A 13  ? 0.14986 0.12140 0.27383 0.01915  -0.00584 0.03927  13  VAL   A O   
96   C  CB  . VAL   A 13  ? 0.13214 0.11693 0.23168 0.01542  -0.00107 0.01574  13  VAL   A CB  
97   C  CG1 . VAL   A 13  ? 0.15594 0.14358 0.24429 0.01027  -0.00841 0.02160  13  VAL   A CG1 
98   C  CG2 . VAL   A 13  ? 0.16162 0.14475 0.24908 0.01263  0.00379  0.00308  13  VAL   A CG2 
99   N  N   . GLU   A 14  ? 0.12054 0.10366 0.26446 0.02831  -0.00226 0.03966  14  GLU   A N   
100  C  CA  . GLU   A 14  ? 0.12481 0.11266 0.28206 0.03081  -0.00909 0.05558  14  GLU   A CA  
101  C  C   . GLU   A 14  ? 0.13950 0.11415 0.30260 0.03156  -0.00587 0.05923  14  GLU   A C   
102  O  O   . GLU   A 14  ? 0.17668 0.15380 0.33765 0.02888  -0.01230 0.07016  14  GLU   A O   
103  C  CB  . GLU   A 14  ? 0.12589 0.12530 0.29779 0.03500  -0.00809 0.05980  14  GLU   A CB  
104  C  CG  . GLU   A 14  ? 0.11325 0.12721 0.28085 0.03286  -0.01241 0.05848  14  GLU   A CG  
105  C  CD  . GLU   A 14  ? 0.11614 0.13943 0.29923 0.03662  -0.00872 0.06090  14  GLU   A CD  
106  O  OE1 . GLU   A 14  ? 0.16385 0.19044 0.35974 0.03864  -0.01014 0.07023  14  GLU   A OE1 
107  O  OE2 . GLU   A 14  ? 0.11472 0.14229 0.29765 0.03756  -0.00392 0.05381  14  GLU   A OE2 
108  N  N   . GLY   A 15  ? 0.15753 0.11823 0.32610 0.03428  0.00434  0.04946  15  GLY   A N   
109  C  CA  . GLY   A 15  ? 0.19655 0.14413 0.37146 0.03456  0.00797  0.05195  15  GLY   A CA  
110  C  C   . GLY   A 15  ? 0.20095 0.13894 0.36444 0.02784  0.00536  0.05215  15  GLY   A C   
111  O  O   . GLY   A 15  ? 0.20734 0.13450 0.37555 0.02699  0.00791  0.05478  15  GLY   A O   
112  N  N   . CYS   A 16  ? 0.15483 0.09774 0.30266 0.02238  0.00080  0.04897  16  CYS   A N   
113  C  CA  . CYS   A 16  ? 0.15922 0.09859 0.29302 0.01438  -0.00158 0.04877  16  CYS   A CA  
114  C  C   . CYS   A 16  ? 0.17616 0.12742 0.30056 0.01113  -0.01046 0.06147  16  CYS   A C   
115  O  O   . CYS   A 16  ? 0.19031 0.13956 0.30489 0.00513  -0.01155 0.06376  16  CYS   A O   
116  C  CB  . CYS   A 16  ? 0.15307 0.09406 0.27019 0.00871  0.00075  0.03339  16  CYS   A CB  
117  S  SG  . CYS   A 16  ? 0.21069 0.13766 0.33224 0.01004  0.01079  0.01667  16  CYS   A SG  
118  N  N   . MET   A 17  ? 0.17565 0.13977 0.30183 0.01412  -0.01661 0.06926  17  MET   A N   
119  C  CA  . MET   A 17  ? 0.14398 0.11943 0.25556 0.00951  -0.02499 0.07789  17  MET   A CA  
120  C  C   . MET   A 17  ? 0.17669 0.15149 0.29354 0.00936  -0.02847 0.09305  17  MET   A C   
121  O  O   . MET   A 17  ? 0.20126 0.17647 0.33373 0.01405  -0.02738 0.09777  17  MET   A O   
122  C  CB  . MET   A 17  ? 0.14746 0.13728 0.25637 0.01057  -0.03107 0.07857  17  MET   A CB  
123  C  CG  . MET   A 17  ? 0.12251 0.11487 0.22348 0.00980  -0.02733 0.06353  17  MET   A CG  
124  S  SD  . MET   A 17  ? 0.14953 0.13860 0.22928 0.00332  -0.02395 0.05209  17  MET   A SD  
125  C  CE  . MET   A 17  ? 0.14789 0.14415 0.20984 -0.00222 -0.03100 0.06075  17  MET   A CE  
126  N  N   . VAL   A 18  ? 0.17396 0.15003 0.27537 0.00331  -0.03119 0.09841  18  VAL   A N   
127  C  CA  . VAL   A 18  ? 0.20983 0.18804 0.30994 0.00145  -0.03363 0.11030  18  VAL   A CA  
128  C  C   . VAL   A 18  ? 0.19535 0.18502 0.27276 -0.00446 -0.03992 0.11492  18  VAL   A C   
129  O  O   . VAL   A 18  ? 0.18833 0.18172 0.25091 -0.00745 -0.04108 0.10835  18  VAL   A O   
130  C  CB  . VAL   A 18  ? 0.21130 0.17600 0.31602 -0.00060 -0.02716 0.11110  18  VAL   A CB  
131  C  CG1 . VAL   A 18  ? 0.24154 0.19276 0.36569 0.00436  -0.02011 0.10366  18  VAL   A CG1 
132  C  CG2 . VAL   A 18  ? 0.22040 0.18280 0.30984 -0.00739 -0.02460 0.10592  18  VAL   A CG2 
133  N  N   . GLN   A 19  ? 0.23591 0.23058 0.31014 -0.00615 -0.04345 0.12593  19  GLN   A N   
134  C  CA  . GLN   A 19  ? 0.27776 0.28185 0.32892 -0.01213 -0.04813 0.13015  19  GLN   A CA  
135  C  C   . GLN   A 19  ? 0.22761 0.22610 0.26973 -0.01627 -0.04285 0.13371  19  GLN   A C   
136  O  O   . GLN   A 19  ? 0.24578 0.23688 0.30115 -0.01484 -0.03957 0.14009  19  GLN   A O   
137  C  CB  . GLN   A 19  ? 0.30196 0.31617 0.35520 -0.01197 -0.05560 0.14038  19  GLN   A CB  
138  C  CG  . GLN   A 19  ? 0.36422 0.38850 0.39231 -0.01838 -0.06131 0.14227  19  GLN   A CG  
139  C  CD  . GLN   A 19  ? 0.36970 0.40481 0.40168 -0.01884 -0.06988 0.15150  19  GLN   A CD  
140  O  OE1 . GLN   A 19  ? 0.47821 0.51351 0.53121 -0.01454 -0.07080 0.16073  19  GLN   A OE1 
141  N  NE2 . GLN   A 19  ? 0.44777 0.49162 0.45973 -0.02436 -0.07594 0.14892  19  GLN   A NE2 
142  N  N   . VAL   A 20  ? 0.22570 0.22754 0.24626 -0.02140 -0.04111 0.12919  20  VAL   A N   
143  C  CA  . VAL   A 20  ? 0.28845 0.28782 0.29975 -0.02585 -0.03509 0.13258  20  VAL   A CA  
144  C  C   . VAL   A 20  ? 0.25985 0.26883 0.24700 -0.03017 -0.03769 0.13654  20  VAL   A C   
145  O  O   . VAL   A 20  ? 0.28061 0.29557 0.25043 -0.03203 -0.03996 0.12933  20  VAL   A O   
146  C  CB  . VAL   A 20  ? 0.28293 0.27811 0.29186 -0.02826 -0.02785 0.12326  20  VAL   A CB  
147  C  CG1 . VAL   A 20  ? 0.28849 0.28383 0.28999 -0.03321 -0.02097 0.12715  20  VAL   A CG1 
148  C  CG2 . VAL   A 20  ? 0.25283 0.23716 0.28433 -0.02500 -0.02522 0.11822  20  VAL   A CG2 
149  N  N   . THR   A 21  ? 0.27895 0.28838 0.26426 -0.03195 -0.03697 0.14731  21  THR   A N   
150  C  CA  . THR   A 21  ? 0.31940 0.33697 0.28078 -0.03624 -0.03869 0.15133  21  THR   A CA  
151  C  C   . THR   A 21  ? 0.33341 0.34903 0.28678 -0.03988 -0.03005 0.15529  21  THR   A C   
152  O  O   . THR   A 21  ? 0.36108 0.37052 0.33032 -0.03936 -0.02694 0.16296  21  THR   A O   
153  C  CB  . THR   A 21  ? 0.34952 0.37252 0.31416 -0.03548 -0.04729 0.16281  21  THR   A CB  
154  O  OG1 . THR   A 21  ? 0.34296 0.36998 0.31574 -0.03273 -0.05487 0.15900  21  THR   A OG1 
155  C  CG2 . THR   A 21  ? 0.37277 0.40342 0.31051 -0.04069 -0.04889 0.16652  21  THR   A CG2 
156  N  N   . CYS   A 22  ? 0.36457 0.38504 0.29406 -0.04351 -0.02547 0.14956  22  CYS   A N   
157  C  CA  . CYS   A 22  ? 0.37251 0.39354 0.29235 -0.04703 -0.01655 0.15368  22  CYS   A CA  
158  C  C   . CYS   A 22  ? 0.42312 0.45097 0.31368 -0.05006 -0.01702 0.15333  22  CYS   A C   
159  O  O   . CYS   A 22  ? 0.42795 0.45831 0.30189 -0.05052 -0.01647 0.14187  22  CYS   A O   
160  C  CB  . CYS   A 22  ? 0.36168 0.38099 0.28557 -0.04788 -0.00645 0.14477  22  CYS   A CB  
161  S  SG  . CYS   A 22  ? 0.44441 0.46691 0.35821 -0.05218 0.00611  0.14864  22  CYS   A SG  
162  N  N   . GLY   A 23  ? 0.43682 0.46681 0.32097 -0.05216 -0.01834 0.16562  23  GLY   A N   
163  C  CA  . GLY   A 23  ? 0.43820 0.47421 0.29387 -0.05538 -0.01999 0.16627  23  GLY   A CA  
164  C  C   . GLY   A 23  ? 0.45198 0.49207 0.30193 -0.05514 -0.03186 0.16274  23  GLY   A C   
165  O  O   . GLY   A 23  ? 0.49308 0.53444 0.36057 -0.05321 -0.04112 0.17086  23  GLY   A O   
166  N  N   . THR   A 24  ? 0.45399 0.49604 0.28115 -0.05708 -0.03131 0.15044  24  THR   A N   
167  C  CA  . THR   A 24  ? 0.50065 0.54639 0.32303 -0.05803 -0.04248 0.14554  24  THR   A CA  
168  C  C   . THR   A 24  ? 0.46782 0.51021 0.30091 -0.05536 -0.04321 0.13246  24  THR   A C   
169  O  O   . THR   A 24  ? 0.51781 0.56282 0.34876 -0.05646 -0.05179 0.12719  24  THR   A O   
170  C  CB  . THR   A 24  ? 0.52142 0.57050 0.31082 -0.06291 -0.04305 0.14011  24  THR   A CB  
171  O  OG1 . THR   A 24  ? 0.57284 0.61724 0.34582 -0.06276 -0.03179 0.12556  24  THR   A OG1 
172  C  CG2 . THR   A 24  ? 0.50652 0.55959 0.28318 -0.06586 -0.04258 0.15382  24  THR   A CG2 
173  N  N   . THR   A 25  ? 0.45585 0.49308 0.30108 -0.05239 -0.03469 0.12774  25  THR   A N   
174  C  CA  . THR   A 25  ? 0.45321 0.48733 0.30802 -0.04987 -0.03472 0.11612  25  THR   A CA  
175  C  C   . THR   A 25  ? 0.39066 0.42313 0.27521 -0.04592 -0.04034 0.12239  25  THR   A C   
176  O  O   . THR   A 25  ? 0.38518 0.41452 0.28611 -0.04412 -0.03683 0.13072  25  THR   A O   
177  C  CB  . THR   A 25  ? 0.44774 0.47852 0.29882 -0.04905 -0.02216 0.10742  25  THR   A CB  
178  O  OG1 . THR   A 25  ? 0.51767 0.54909 0.34187 -0.05142 -0.01572 0.09946  25  THR   A OG1 
179  C  CG2 . THR   A 25  ? 0.43613 0.46408 0.29900 -0.04637 -0.02262 0.09729  25  THR   A CG2 
180  N  N   . THR   A 26  ? 0.37266 0.40658 0.26487 -0.04459 -0.04838 0.11806  26  THR   A N   
181  C  CA  . THR   A 26  ? 0.36732 0.39929 0.28758 -0.03988 -0.05223 0.12184  26  THR   A CA  
182  C  C   . THR   A 26  ? 0.32964 0.35885 0.25411 -0.03799 -0.05125 0.10947  26  THR   A C   
183  O  O   . THR   A 26  ? 0.34181 0.37303 0.25197 -0.04038 -0.05378 0.10012  26  THR   A O   
184  C  CB  . THR   A 26  ? 0.37762 0.41575 0.30787 -0.03934 -0.06251 0.13045  26  THR   A CB  
185  O  OG1 . THR   A 26  ? 0.44272 0.48273 0.37399 -0.04011 -0.06322 0.14403  26  THR   A OG1 
186  C  CG2 . THR   A 26  ? 0.37269 0.40900 0.33113 -0.03371 -0.06494 0.13138  26  THR   A CG2 
187  N  N   . LEU   A 27  ? 0.26060 0.28432 0.20408 -0.03411 -0.04735 0.10909  27  LEU   A N   
188  C  CA  . LEU   A 27  ? 0.25642 0.27797 0.20632 -0.03182 -0.04739 0.09917  27  LEU   A CA  
189  C  C   . LEU   A 27  ? 0.20749 0.22368 0.18482 -0.02648 -0.04696 0.10282  27  LEU   A C   
190  O  O   . LEU   A 27  ? 0.22798 0.24232 0.21975 -0.02435 -0.04771 0.11211  27  LEU   A O   
191  C  CB  . LEU   A 27  ? 0.24639 0.26586 0.18205 -0.03362 -0.03911 0.08860  27  LEU   A CB  
192  C  CG  . LEU   A 27  ? 0.23086 0.24839 0.16536 -0.03484 -0.02936 0.09100  27  LEU   A CG  
193  C  CD1 . LEU   A 27  ? 0.22496 0.23665 0.18483 -0.03169 -0.02630 0.09328  27  LEU   A CD1 
194  C  CD2 . LEU   A 27  ? 0.28477 0.30293 0.20728 -0.03519 -0.02060 0.07772  27  LEU   A CD2 
195  N  N   . ASN   A 28  ? 0.21531 0.22840 0.20111 -0.02348 -0.04372 0.09110  28  ASN   A N   
196  C  CA  . ASN   A 28  ? 0.19316 0.20049 0.20311 -0.01815 -0.04168 0.08951  28  ASN   A CA  
197  C  C   . ASN   A 28  ? 0.16453 0.16440 0.18024 -0.01828 -0.03278 0.08381  28  ASN   A C   
198  O  O   . ASN   A 28  ? 0.17774 0.17916 0.18165 -0.02108 -0.02789 0.07676  28  ASN   A O   
199  C  CB  . ASN   A 28  ? 0.17770 0.18733 0.19324 -0.01521 -0.04311 0.07912  28  ASN   A CB  
200  C  CG  . ASN   A 28  ? 0.21257 0.23077 0.22354 -0.01658 -0.05257 0.08395  28  ASN   A CG  
201  O  OD1 . ASN   A 28  ? 0.20668 0.22837 0.23162 -0.01422 -0.05781 0.09364  28  ASN   A OD1 
202  N  ND2 . ASN   A 28  ? 0.19998 0.22160 0.19194 -0.02078 -0.05425 0.07654  28  ASN   A ND2 
203  N  N   . GLY   A 29  ? 0.17379 0.16553 0.20894 -0.01531 -0.03060 0.08666  29  GLY   A N   
204  C  CA  . GLY   A 29  ? 0.19275 0.17672 0.23520 -0.01642 -0.02334 0.07947  29  GLY   A CA  
205  C  C   . GLY   A 29  ? 0.16897 0.14579 0.22782 -0.01199 -0.02113 0.07149  29  GLY   A C   
206  O  O   . GLY   A 29  ? 0.16142 0.13848 0.22999 -0.00713 -0.02411 0.07435  29  GLY   A O   
207  N  N   . LEU   A 30  ? 0.16410 0.13548 0.22587 -0.01410 -0.01569 0.06164  30  LEU   A N   
208  C  CA  . LEU   A 30  ? 0.19252 0.15669 0.26513 -0.01126 -0.01239 0.05143  30  LEU   A CA  
209  C  C   . LEU   A 30  ? 0.16986 0.12004 0.25440 -0.01353 -0.00805 0.05187  30  LEU   A C   
210  O  O   . LEU   A 30  ? 0.18732 0.13614 0.26879 -0.01972 -0.00592 0.05003  30  LEU   A O   
211  C  CB  . LEU   A 30  ? 0.15666 0.12685 0.22038 -0.01279 -0.01078 0.03824  30  LEU   A CB  
212  C  CG  . LEU   A 30  ? 0.12530 0.09009 0.19518 -0.01078 -0.00734 0.02676  30  LEU   A CG  
213  C  CD1 . LEU   A 30  ? 0.15026 0.11730 0.22560 -0.00420 -0.00821 0.02691  30  LEU   A CD1 
214  C  CD2 . LEU   A 30  ? 0.14151 0.11314 0.20174 -0.01407 -0.00649 0.01638  30  LEU   A CD2 
215  N  N   . TRP   A 31  ? 0.17470 0.11435 0.27432 -0.00863 -0.00637 0.05436  31  TRP   A N   
216  C  CA  . TRP   A 31  ? 0.17569 0.09862 0.28873 -0.01014 -0.00209 0.05667  31  TRP   A CA  
217  C  C   . TRP   A 31  ? 0.20443 0.11644 0.32205 -0.01007 0.00370  0.04056  31  TRP   A C   
218  O  O   . TRP   A 31  ? 0.19996 0.10908 0.32463 -0.00335 0.00623  0.03612  31  TRP   A O   
219  C  CB  . TRP   A 31  ? 0.18669 0.10553 0.31336 -0.00384 -0.00341 0.07052  31  TRP   A CB  
220  C  CG  . TRP   A 31  ? 0.23427 0.13969 0.37155 -0.00386 0.00119  0.07165  31  TRP   A CG  
221  C  CD1 . TRP   A 31  ? 0.21595 0.11111 0.35223 -0.01096 0.00464  0.06736  31  TRP   A CD1 
222  C  CD2 . TRP   A 31  ? 0.23513 0.13633 0.38667 0.00323  0.00268  0.07788  31  TRP   A CD2 
223  N  NE1 . TRP   A 31  ? 0.23577 0.11865 0.38370 -0.00864 0.00812  0.07033  31  TRP   A NE1 
224  C  CE2 . TRP   A 31  ? 0.27035 0.15658 0.42827 0.00038  0.00730  0.07703  31  TRP   A CE2 
225  C  CE3 . TRP   A 31  ? 0.30990 0.21951 0.47063 0.01120  0.00047  0.08438  31  TRP   A CE3 
226  C  CZ2 . TRP   A 31  ? 0.30182 0.17976 0.47497 0.00600  0.01024  0.08263  31  TRP   A CZ2 
227  C  CZ3 . TRP   A 31  ? 0.28086 0.18429 0.45759 0.01652  0.00336  0.09022  31  TRP   A CZ3 
228  C  CH2 . TRP   A 31  ? 0.27554 0.16251 0.45842 0.01433  0.00846  0.08933  31  TRP   A CH2 
229  N  N   . LEU   A 32  ? 0.18821 0.09558 0.30122 -0.01803 0.00580  0.03174  32  LEU   A N   
230  C  CA  . LEU   A 32  ? 0.20320 0.09994 0.31687 -0.02039 0.01052  0.01557  32  LEU   A CA  
231  C  C   . LEU   A 32  ? 0.23409 0.11528 0.35437 -0.02740 0.01335  0.01419  32  LEU   A C   
232  O  O   . LEU   A 32  ? 0.25242 0.13810 0.37033 -0.03496 0.01096  0.01936  32  LEU   A O   
233  C  CB  . LEU   A 32  ? 0.19370 0.10392 0.29204 -0.02490 0.00840  0.00437  32  LEU   A CB  
234  C  CG  . LEU   A 32  ? 0.18370 0.11017 0.27321 -0.01921 0.00545  0.00504  32  LEU   A CG  
235  C  CD1 . LEU   A 32  ? 0.18615 0.12641 0.26238 -0.02416 0.00273  -0.00166 32  LEU   A CD1 
236  C  CD2 . LEU   A 32  ? 0.19663 0.11782 0.29064 -0.01231 0.00951  -0.00148 32  LEU   A CD2 
237  N  N   . ASP   A 33  ? 0.27536 0.14191 0.40044 -0.02456 0.01850  0.00669  33  ASP   A N   
238  C  CA  . ASP   A 33  ? 0.29787 0.15024 0.42666 -0.02991 0.02079  0.00573  33  ASP   A CA  
239  C  C   . ASP   A 33  ? 0.30474 0.16017 0.44014 -0.02950 0.01814  0.02409  33  ASP   A C   
240  O  O   . ASP   A 33  ? 0.30513 0.16637 0.44594 -0.02130 0.01672  0.03582  33  ASP   A O   
241  C  CB  . ASP   A 33  ? 0.32109 0.17275 0.44013 -0.04162 0.01957  -0.00695 33  ASP   A CB  
242  C  CG  . ASP   A 33  ? 0.36351 0.21446 0.47279 -0.04167 0.02156  -0.02430 33  ASP   A CG  
243  O  OD1 . ASP   A 33  ? 0.43090 0.27026 0.54224 -0.03551 0.02712  -0.03090 33  ASP   A OD1 
244  O  OD2 . ASP   A 33  ? 0.38611 0.24945 0.48556 -0.04762 0.01786  -0.03077 33  ASP   A OD2 
245  N  N   . ASP   A 34  ? 0.28196 0.13604 0.41622 -0.03848 0.01697  0.02770  34  ASP   A N   
246  C  CA  . ASP   A 34  ? 0.29572 0.15299 0.43444 -0.03829 0.01538  0.04515  34  ASP   A CA  
247  C  C   . ASP   A 34  ? 0.29701 0.17265 0.42735 -0.04267 0.01150  0.05335  34  ASP   A C   
248  O  O   . ASP   A 34  ? 0.28004 0.15891 0.41039 -0.04705 0.01124  0.06407  34  ASP   A O   
249  C  CB  . ASP   A 34  ? 0.31786 0.16019 0.46278 -0.04438 0.01806  0.04612  34  ASP   A CB  
250  C  CG  . ASP   A 34  ? 0.35418 0.19686 0.49341 -0.05683 0.01750  0.03673  34  ASP   A CG  
251  O  OD1 . ASP   A 34  ? 0.32159 0.17466 0.45282 -0.06006 0.01545  0.02712  34  ASP   A OD1 
252  O  OD2 . ASP   A 34  ? 0.38690 0.22047 0.53052 -0.06374 0.01873  0.03963  34  ASP   A OD2 
253  N  N   . VAL   A 35  ? 0.25990 0.14781 0.38305 -0.04124 0.00914  0.04895  35  VAL   A N   
254  C  CA  . VAL   A 35  ? 0.22092 0.12634 0.33564 -0.04461 0.00630  0.05607  35  VAL   A CA  
255  C  C   . VAL   A 35  ? 0.24211 0.15741 0.35083 -0.03683 0.00298  0.06101  35  VAL   A C   
256  O  O   . VAL   A 35  ? 0.20449 0.11880 0.31284 -0.03099 0.00267  0.05219  35  VAL   A O   
257  C  CB  . VAL   A 35  ? 0.25846 0.17223 0.36934 -0.05283 0.00602  0.04499  35  VAL   A CB  
258  C  CG1 . VAL   A 35  ? 0.22675 0.16174 0.32578 -0.05310 0.00433  0.05053  35  VAL   A CG1 
259  C  CG2 . VAL   A 35  ? 0.28665 0.19313 0.40200 -0.06167 0.00793  0.04037  35  VAL   A CG2 
260  N  N   . VAL   A 36  ? 0.19239 0.11970 0.29238 -0.03664 0.00064  0.07326  36  VAL   A N   
261  C  CA  . VAL   A 36  ? 0.18966 0.12993 0.27765 -0.03074 -0.00343 0.07561  36  VAL   A CA  
262  C  C   . VAL   A 36  ? 0.21830 0.17407 0.29112 -0.03419 -0.00323 0.07099  36  VAL   A C   
263  O  O   . VAL   A 36  ? 0.21851 0.17895 0.28822 -0.03970 -0.00081 0.07690  36  VAL   A O   
264  C  CB  . VAL   A 36  ? 0.22269 0.16377 0.31073 -0.02780 -0.00677 0.09322  36  VAL   A CB  
265  C  CG1 . VAL   A 36  ? 0.20634 0.16211 0.27870 -0.02471 -0.01170 0.09480  36  VAL   A CG1 
266  C  CG2 . VAL   A 36  ? 0.22575 0.15561 0.32912 -0.02129 -0.00673 0.09523  36  VAL   A CG2 
267  N  N   . TYR   A 37  ? 0.15642 0.11998 0.22137 -0.03066 -0.00492 0.06105  37  TYR   A N   
268  C  CA  . TYR   A 37  ? 0.17990 0.15683 0.23251 -0.03216 -0.00420 0.05565  37  TYR   A CA  
269  C  C   . TYR   A 37  ? 0.15492 0.13967 0.19383 -0.02853 -0.00719 0.06017  37  TYR   A C   
270  O  O   . TYR   A 37  ? 0.19514 0.17833 0.23450 -0.02393 -0.01116 0.06023  37  TYR   A O   
271  C  CB  . TYR   A 37  ? 0.14815 0.12767 0.20139 -0.03127 -0.00409 0.04172  37  TYR   A CB  
272  C  CG  . TYR   A 37  ? 0.14836 0.12060 0.21197 -0.03604 -0.00228 0.03489  37  TYR   A CG  
273  C  CD1 . TYR   A 37  ? 0.16534 0.12350 0.23809 -0.03472 -0.00182 0.03142  37  TYR   A CD1 
274  C  CD2 . TYR   A 37  ? 0.15542 0.13495 0.22040 -0.04241 -0.00082 0.03185  37  TYR   A CD2 
275  C  CE1 . TYR   A 37  ? 0.20931 0.15879 0.28914 -0.04031 -0.00003 0.02331  37  TYR   A CE1 
276  C  CE2 . TYR   A 37  ? 0.18617 0.15944 0.25957 -0.04849 -0.00052 0.02505  37  TYR   A CE2 
277  C  CZ  . TYR   A 37  ? 0.22086 0.17808 0.30022 -0.04791 -0.00013 0.02008  37  TYR   A CZ  
278  O  OH  . TYR   A 37  ? 0.27152 0.22053 0.35703 -0.05520 0.00034  0.01159  37  TYR   A OH  
279  N  N   . CYS   A 38  ? 0.16022 0.15371 0.18707 -0.03089 -0.00499 0.06314  38  CYS   A N   
280  C  CA  . CYS   A 38  ? 0.16496 0.16435 0.17582 -0.02880 -0.00765 0.06553  38  CYS   A CA  
281  C  C   . CYS   A 38  ? 0.17503 0.18322 0.17350 -0.03043 -0.00244 0.06185  38  CYS   A C   
282  O  O   . CYS   A 38  ? 0.17554 0.18695 0.17977 -0.03335 0.00296  0.06144  38  CYS   A O   
283  C  CB  . CYS   A 38  ? 0.19257 0.18993 0.19953 -0.02971 -0.01116 0.07955  38  CYS   A CB  
284  S  SG  . CYS   A 38  ? 0.23854 0.23860 0.23912 -0.03564 -0.00567 0.09161  38  CYS   A SG  
285  N  N   . PRO   A 39  ? 0.15504 0.16716 0.13766 -0.02879 -0.00349 0.05899  39  PRO   A N   
286  C  CA  . PRO   A 39  ? 0.18113 0.19990 0.15231 -0.02933 0.00335  0.05489  39  PRO   A CA  
287  C  C   . PRO   A 39  ? 0.19192 0.21415 0.15676 -0.03341 0.00889  0.06435  39  PRO   A C   
288  O  O   . PRO   A 39  ? 0.20246 0.22258 0.16062 -0.03578 0.00582  0.07448  39  PRO   A O   
289  C  CB  . PRO   A 39  ? 0.20299 0.22142 0.15734 -0.02756 0.00035  0.04993  39  PRO   A CB  
290  C  CG  . PRO   A 39  ? 0.17059 0.18467 0.13357 -0.02533 -0.00796 0.04844  39  PRO   A CG  
291  C  CD  . PRO   A 39  ? 0.18038 0.19091 0.15655 -0.02641 -0.01049 0.05782  39  PRO   A CD  
292  N  N   . ARG   A 40  ? 0.18300 0.21189 0.15147 -0.03425 0.01723  0.06233  40  ARG   A N   
293  C  CA  . ARG   A 40  ? 0.20267 0.23616 0.16648 -0.03839 0.02388  0.07191  40  ARG   A CA  
294  C  C   . ARG   A 40  ? 0.22205 0.25714 0.16018 -0.03898 0.02643  0.07439  40  ARG   A C   
295  O  O   . ARG   A 40  ? 0.24209 0.27977 0.17245 -0.04298 0.03007  0.08498  40  ARG   A O   
296  C  CB  . ARG   A 40  ? 0.17801 0.22073 0.15419 -0.03916 0.03263  0.06977  40  ARG   A CB  
297  C  CG  . ARG   A 40  ? 0.17480 0.22410 0.14321 -0.03468 0.03966  0.06098  40  ARG   A CG  
298  C  CD  . ARG   A 40  ? 0.17005 0.23129 0.15510 -0.03515 0.04809  0.06150  40  ARG   A CD  
299  N  NE  . ARG   A 40  ? 0.16899 0.23569 0.15028 -0.02921 0.05508  0.05341  40  ARG   A NE  
300  C  CZ  . ARG   A 40  ? 0.18977 0.26902 0.18345 -0.02770 0.06449  0.05408  40  ARG   A CZ  
301  N  NH1 . ARG   A 40  ? 0.19692 0.28576 0.20769 -0.03276 0.06719  0.06208  40  ARG   A NH1 
302  N  NH2 . ARG   A 40  ? 0.19115 0.27336 0.18139 -0.02103 0.07168  0.04704  40  ARG   A NH2 
303  N  N   . HIS   A 41  ? 0.21508 0.24816 0.13881 -0.03593 0.02453  0.06504  41  HIS   A N   
304  C  CA  . HIS   A 41  ? 0.28236 0.31593 0.17885 -0.03805 0.02670  0.06612  41  HIS   A CA  
305  C  C   . HIS   A 41  ? 0.29782 0.32888 0.18425 -0.04198 0.01723  0.07744  41  HIS   A C   
306  O  O   . HIS   A 41  ? 0.30881 0.33967 0.17321 -0.04372 0.01721  0.07758  41  HIS   A O   
307  C  CB  . HIS   A 41  ? 0.30253 0.33275 0.18571 -0.03492 0.02748  0.05231  41  HIS   A CB  
308  C  CG  . HIS   A 41  ? 0.29708 0.32124 0.18201 -0.03393 0.01570  0.04809  41  HIS   A CG  
309  N  ND1 . HIS   A 41  ? 0.32457 0.34622 0.22430 -0.02955 0.01394  0.03928  41  HIS   A ND1 
310  C  CD2 . HIS   A 41  ? 0.34486 0.36652 0.21875 -0.03699 0.00533  0.05207  41  HIS   A CD2 
311  C  CE1 . HIS   A 41  ? 0.30751 0.32501 0.20594 -0.02994 0.00388  0.03790  41  HIS   A CE1 
312  N  NE2 . HIS   A 41  ? 0.34594 0.36387 0.22991 -0.03439 -0.00179 0.04553  41  HIS   A NE2 
313  N  N   . VAL   A 42  ? 0.27271 0.30051 0.17773 -0.04195 0.00965  0.08532  42  VAL   A N   
314  C  CA  . VAL   A 42  ? 0.28050 0.30640 0.18232 -0.04394 0.00172  0.09748  42  VAL   A CA  
315  C  C   . VAL   A 42  ? 0.30749 0.33565 0.20095 -0.04640 0.00786  0.10524  42  VAL   A C   
316  O  O   . VAL   A 42  ? 0.32317 0.35108 0.20680 -0.04751 0.00252  0.11226  42  VAL   A O   
317  C  CB  . VAL   A 42  ? 0.28271 0.30328 0.20961 -0.04245 -0.00478 0.10458  42  VAL   A CB  
318  C  CG1 . VAL   A 42  ? 0.22259 0.24144 0.16707 -0.04414 0.00211  0.10968  42  VAL   A CG1 
319  C  CG2 . VAL   A 42  ? 0.29036 0.30923 0.21787 -0.04165 -0.01408 0.11364  42  VAL   A CG2 
320  N  N   . ILE   A 43  ? 0.28767 0.31923 0.18570 -0.04742 0.01900  0.10468  43  ILE   A N   
321  C  CA  . ILE   A 43  ? 0.27925 0.31294 0.17021 -0.04992 0.02564  0.11257  43  ILE   A CA  
322  C  C   . ILE   A 43  ? 0.34212 0.37877 0.20594 -0.04989 0.03268  0.10644  43  ILE   A C   
323  O  O   . ILE   A 43  ? 0.39692 0.43542 0.25131 -0.05186 0.03938  0.11242  43  ILE   A O   
324  C  CB  . ILE   A 43  ? 0.30505 0.34150 0.21578 -0.05171 0.03451  0.11593  43  ILE   A CB  
325  C  CG1 . ILE   A 43  ? 0.31876 0.36243 0.23021 -0.05017 0.04501  0.10551  43  ILE   A CG1 
326  C  CG2 . ILE   A 43  ? 0.33003 0.36083 0.26725 -0.05221 0.02825  0.12008  43  ILE   A CG2 
327  C  CD1 . ILE   A 43  ? 0.32661 0.37502 0.26387 -0.05214 0.05081  0.10744  43  ILE   A CD1 
328  N  N   . CYS   A 44  ? 0.36575 0.40163 0.21657 -0.04775 0.03192  0.09431  44  CYS   A N   
329  C  CA  . CYS   A 44  ? 0.35931 0.39528 0.18499 -0.04700 0.03972  0.08586  44  CYS   A CA  
330  C  C   . CYS   A 44  ? 0.48662 0.51955 0.29041 -0.04885 0.03022  0.08592  44  CYS   A C   
331  O  O   . CYS   A 44  ? 0.50693 0.53799 0.31516 -0.04936 0.01763  0.08618  44  CYS   A O   
332  C  CB  . CYS   A 44  ? 0.45160 0.48714 0.27694 -0.04333 0.04562  0.07112  44  CYS   A CB  
333  S  SG  . CYS   A 44  ? 0.38153 0.42442 0.23291 -0.04088 0.05745  0.07001  44  CYS   A SG  
334  N  N   . THR   A 45  ? 0.58219 0.61547 0.36306 -0.04991 0.03657  0.08545  45  THR   A N   
335  C  CA  . THR   A 45  ? 0.66575 0.69734 0.42320 -0.05228 0.02853  0.08305  45  THR   A CA  
336  C  C   . THR   A 45  ? 0.71464 0.74207 0.45668 -0.05035 0.03259  0.06562  45  THR   A C   
337  O  O   . THR   A 45  ? 0.70010 0.72600 0.45171 -0.04648 0.04062  0.05645  45  THR   A O   
338  C  CB  . THR   A 45  ? 0.68518 0.71922 0.42429 -0.05501 0.03241  0.09234  45  THR   A CB  
339  O  OG1 . THR   A 45  ? 0.65967 0.69455 0.39409 -0.05278 0.04955  0.08977  45  THR   A OG1 
340  C  CG2 . THR   A 45  ? 0.70285 0.73964 0.45762 -0.05736 0.02510  0.10998  45  THR   A CG2 
341  N  N   . SER   A 46  ? 0.80101 0.82665 0.51977 -0.05333 0.02686  0.06108  46  SER   A N   
342  C  CA  . SER   A 46  ? 0.82806 0.84802 0.53141 -0.05241 0.02999  0.04394  46  SER   A CA  
343  C  C   . SER   A 46  ? 0.78596 0.80495 0.48432 -0.04722 0.04852  0.03586  46  SER   A C   
344  O  O   . SER   A 46  ? 0.75442 0.77009 0.46243 -0.04292 0.05474  0.02486  46  SER   A O   
345  C  CB  . SER   A 46  ? 0.83347 0.85267 0.51098 -0.05787 0.02166  0.04186  46  SER   A CB  
346  O  OG  . SER   A 46  ? 0.90660 0.92813 0.59257 -0.06199 0.00449  0.04818  46  SER   A OG  
347  N  N   . GLU   A 47  ? 0.81957 0.84224 0.50453 -0.04713 0.05797  0.04210  47  GLU   A N   
348  C  CA  . GLU   A 47  ? 0.79290 0.81705 0.47492 -0.04139 0.07661  0.03589  47  GLU   A CA  
349  C  C   . GLU   A 47  ? 0.76508 0.79378 0.47630 -0.03682 0.08544  0.04029  47  GLU   A C   
350  O  O   . GLU   A 47  ? 0.72327 0.75470 0.44076 -0.03069 0.09908  0.03264  47  GLU   A O   
351  C  CB  . GLU   A 47  ? 0.80899 0.83654 0.46862 -0.04271 0.08462  0.04263  47  GLU   A CB  
352  C  CG  . GLU   A 47  ? 0.86416 0.89605 0.53116 -0.04631 0.08218  0.06170  47  GLU   A CG  
353  C  CD  . GLU   A 47  ? 0.89881 0.93055 0.55316 -0.05312 0.06540  0.07009  47  GLU   A CD  
354  O  OE1 . GLU   A 47  ? 0.88589 0.91505 0.54195 -0.05535 0.05147  0.06475  47  GLU   A OE1 
355  O  OE2 . GLU   A 47  ? 0.86887 0.90373 0.51272 -0.05625 0.06634  0.08262  47  GLU   A OE2 
356  N  N   . ASP   A 48  ? 0.71672 0.74755 0.44775 -0.03977 0.07769  0.05230  48  ASP   A N   
357  C  CA  . ASP   A 48  ? 0.69172 0.72686 0.45106 -0.03715 0.08463  0.05561  48  ASP   A CA  
358  C  C   . ASP   A 48  ? 0.63470 0.66829 0.40689 -0.03276 0.08485  0.04319  48  ASP   A C   
359  O  O   . ASP   A 48  ? 0.55667 0.59505 0.34408 -0.02768 0.09669  0.03972  48  ASP   A O   
360  C  CB  . ASP   A 48  ? 0.63226 0.66957 0.41038 -0.04197 0.07441  0.06949  48  ASP   A CB  
361  C  CG  . ASP   A 48  ? 0.60596 0.64647 0.38278 -0.04539 0.07948  0.08303  48  ASP   A CG  
362  O  OD1 . ASP   A 48  ? 0.61176 0.65374 0.37720 -0.04388 0.09353  0.08202  48  ASP   A OD1 
363  O  OD2 . ASP   A 48  ? 0.59952 0.64069 0.38743 -0.04927 0.06978  0.09490  48  ASP   A OD2 
364  N  N   . MET   A 49  ? 0.68548 0.71293 0.45283 -0.03465 0.07191  0.03685  49  MET   A N   
365  C  CA  . MET   A 49  ? 0.68745 0.71187 0.46850 -0.03175 0.06998  0.02695  49  MET   A CA  
366  C  C   . MET   A 49  ? 0.66577 0.68775 0.44130 -0.02580 0.08211  0.01294  49  MET   A C   
367  O  O   . MET   A 49  ? 0.69872 0.71648 0.48470 -0.02262 0.08234  0.00363  49  MET   A O   
368  C  CB  . MET   A 49  ? 0.65616 0.67402 0.43251 -0.03570 0.05354  0.02428  49  MET   A CB  
369  C  CG  . MET   A 49  ? 0.68871 0.70993 0.48496 -0.03814 0.04283  0.03458  49  MET   A CG  
370  S  SD  . MET   A 49  ? 0.78638 0.81542 0.61115 -0.03498 0.05205  0.03812  49  MET   A SD  
371  C  CE  . MET   A 49  ? 0.50878 0.53246 0.34204 -0.03068 0.05174  0.02382  49  MET   A CE  
372  N  N   . LEU   A 50  ? 0.69508 0.71961 0.45508 -0.02401 0.09241  0.01151  50  LEU   A N   
373  C  CA  . LEU   A 50  ? 0.67293 0.69712 0.43097 -0.01791 0.10498  -0.00136 50  LEU   A CA  
374  C  C   . LEU   A 50  ? 0.68284 0.71857 0.47043 -0.01210 0.11557  0.00103  50  LEU   A C   
375  O  O   . LEU   A 50  ? 0.70979 0.74232 0.51470 -0.00918 0.11415  -0.00483 50  LEU   A O   
376  C  CB  . LEU   A 50  ? 0.72971 0.75566 0.46331 -0.01793 0.11337  -0.00320 50  LEU   A CB  
377  C  CG  . LEU   A 50  ? 0.78897 0.80411 0.49253 -0.02405 0.10299  -0.00861 50  LEU   A CG  
378  C  CD1 . LEU   A 50  ? 0.76274 0.78099 0.44075 -0.02468 0.11142  -0.00817 50  LEU   A CD1 
379  C  CD2 . LEU   A 50  ? 0.75105 0.75303 0.45077 -0.02391 0.09887  -0.02508 50  LEU   A CD2 
380  N  N   . ASN   A 51  ? 0.63288 0.68328 0.42831 -0.01106 0.12526  0.01063  51  ASN   A N   
381  C  CA  . ASN   A 51  ? 0.60432 0.67110 0.43159 -0.00897 0.13293  0.01399  51  ASN   A CA  
382  C  C   . ASN   A 51  ? 0.56895 0.64630 0.41036 -0.01442 0.13012  0.03025  51  ASN   A C   
383  O  O   . ASN   A 51  ? 0.60184 0.69217 0.44429 -0.01959 0.13702  0.03483  51  ASN   A O   
384  C  CB  . ASN   A 51  ? 0.67714 0.75178 0.50773 -0.00466 0.14800  0.00579  51  ASN   A CB  
385  C  CG  . ASN   A 51  ? 0.67927 0.76001 0.54312 -0.00040 0.15392  0.00350  51  ASN   A CG  
386  O  OD1 . ASN   A 51  ? 0.67615 0.75929 0.56120 -0.00239 0.14741  0.00974  51  ASN   A OD1 
387  N  ND2 . ASN   A 51  ? 0.66990 0.75172 0.53875 0.00678  0.16610  -0.00482 51  ASN   A ND2 
388  N  N   . PRO   A 52  ? 0.52072 0.58187 0.37115 -0.01510 0.12259  0.03696  52  PRO   A N   
389  C  CA  . PRO   A 52  ? 0.47264 0.53073 0.32857 -0.02701 0.12087  0.04754  52  PRO   A CA  
390  C  C   . PRO   A 52  ? 0.41704 0.49219 0.30727 -0.02909 0.12403  0.05156  52  PRO   A C   
391  O  O   . PRO   A 52  ? 0.44241 0.52561 0.35433 -0.02426 0.12388  0.04665  52  PRO   A O   
392  C  CB  . PRO   A 52  ? 0.43324 0.48857 0.29064 -0.02884 0.10297  0.05114  52  PRO   A CB  
393  C  CG  . PRO   A 52  ? 0.47215 0.52617 0.33599 -0.02350 0.10107  0.03997  52  PRO   A CG  
394  C  CD  . PRO   A 52  ? 0.49689 0.55328 0.35026 -0.01532 0.11201  0.03030  52  PRO   A CD  
395  N  N   . ASN   A 53  ? 0.40202 0.48227 0.29819 -0.03415 0.12611  0.06252  53  ASN   A N   
396  C  CA  . ASN   A 53  ? 0.34133 0.43515 0.27045 -0.03578 0.12570  0.06971  53  ASN   A CA  
397  C  C   . ASN   A 53  ? 0.36239 0.45186 0.29898 -0.04059 0.11232  0.07976  53  ASN   A C   
398  O  O   . ASN   A 53  ? 0.34051 0.42687 0.27054 -0.04585 0.11125  0.08924  53  ASN   A O   
399  C  CB  . ASN   A 53  ? 0.40383 0.50734 0.33708 -0.03873 0.13803  0.07401  53  ASN   A CB  
400  C  CG  . ASN   A 53  ? 0.42326 0.54085 0.39127 -0.04043 0.13720  0.08069  53  ASN   A CG  
401  O  OD1 . ASN   A 53  ? 0.37690 0.49323 0.35955 -0.04413 0.12668  0.08728  53  ASN   A OD1 
402  N  ND2 . ASN   A 53  ? 0.47501 0.60624 0.45685 -0.03797 0.14797  0.07852  53  ASN   A ND2 
403  N  N   . TYR   A 54  ? 0.29778 0.38685 0.24853 -0.03883 0.10232  0.07750  54  TYR   A N   
404  C  CA  . TYR   A 54  ? 0.28822 0.37111 0.24455 -0.04331 0.08944  0.08470  54  TYR   A CA  
405  C  C   . TYR   A 54  ? 0.28973 0.37624 0.26588 -0.04952 0.08868  0.09451  54  TYR   A C   
406  O  O   . TYR   A 54  ? 0.28702 0.36541 0.26121 -0.05387 0.08168  0.10248  54  TYR   A O   
407  C  CB  . TYR   A 54  ? 0.22976 0.31239 0.19826 -0.04066 0.08082  0.07916  54  TYR   A CB  
408  C  CG  . TYR   A 54  ? 0.24625 0.32143 0.19326 -0.03679 0.07706  0.07186  54  TYR   A CG  
409  C  CD1 . TYR   A 54  ? 0.24769 0.31274 0.18054 -0.03958 0.06668  0.07529  54  TYR   A CD1 
410  C  CD2 . TYR   A 54  ? 0.25255 0.32939 0.19503 -0.03016 0.08300  0.06089  54  TYR   A CD2 
411  C  CE1 . TYR   A 54  ? 0.23993 0.29629 0.15512 -0.03660 0.06077  0.06670  54  TYR   A CE1 
412  C  CE2 . TYR   A 54  ? 0.26159 0.32711 0.18522 -0.02718 0.07769  0.05155  54  TYR   A CE2 
413  C  CZ  . TYR   A 54  ? 0.27044 0.32653 0.18035 -0.03098 0.06631  0.05444  54  TYR   A CZ  
414  O  OH  . TYR   A 54  ? 0.27574 0.32238 0.16879 -0.02919 0.06061  0.04571  54  TYR   A OH  
415  N  N   . GLU   A 55  ? 0.29333 0.39158 0.29013 -0.05005 0.09500  0.09408  55  GLU   A N   
416  C  CA  . GLU   A 55  ? 0.28291 0.38402 0.29772 -0.05696 0.09405  0.10271  55  GLU   A CA  
417  C  C   . GLU   A 55  ? 0.26859 0.36561 0.26733 -0.06054 0.09944  0.11136  55  GLU   A C   
418  O  O   . GLU   A 55  ? 0.29512 0.38533 0.29797 -0.06593 0.09417  0.12009  55  GLU   A O   
419  C  CB  . GLU   A 55  ? 0.28702 0.40346 0.32601 -0.05707 0.09938  0.10068  55  GLU   A CB  
420  C  CG  . GLU   A 55  ? 0.34178 0.46206 0.40023 -0.05575 0.09099  0.09466  55  GLU   A CG  
421  C  CD  . GLU   A 55  ? 0.49087 0.61547 0.54464 -0.04687 0.09377  0.08543  55  GLU   A CD  
422  O  OE1 . GLU   A 55  ? 0.43618 0.55696 0.46855 -0.04199 0.10105  0.08217  55  GLU   A OE1 
423  O  OE2 . GLU   A 55  ? 0.46157 0.59206 0.53197 -0.04507 0.08814  0.08102  55  GLU   A OE2 
424  N  N   . ASP   A 56  ? 0.31041 0.41007 0.28951 -0.05749 0.10996  0.10861  56  ASP   A N   
425  C  CA  . ASP   A 56  ? 0.37436 0.47023 0.33411 -0.06088 0.11572  0.11633  56  ASP   A CA  
426  C  C   . ASP   A 56  ? 0.36384 0.44608 0.30459 -0.06182 0.10564  0.12139  56  ASP   A C   
427  O  O   . ASP   A 56  ? 0.35941 0.43735 0.29702 -0.06636 0.10368  0.13232  56  ASP   A O   
428  C  CB  . ASP   A 56  ? 0.46249 0.56193 0.40209 -0.05738 0.12920  0.10953  56  ASP   A CB  
429  C  CG  . ASP   A 56  ? 0.47485 0.58850 0.42988 -0.05894 0.14152  0.11086  56  ASP   A CG  
430  O  OD1 . ASP   A 56  ? 0.49926 0.61930 0.47780 -0.06368 0.13927  0.11881  56  ASP   A OD1 
431  O  OD2 . ASP   A 56  ? 0.54580 0.66418 0.48961 -0.05577 0.15349  0.10365  56  ASP   A OD2 
432  N  N   . LEU   A 57  ? 0.32152 0.39764 0.24983 -0.05737 0.09910  0.11392  57  LEU   A N   
433  C  CA  . LEU   A 57  ? 0.34760 0.41301 0.25908 -0.05776 0.08838  0.11829  57  LEU   A CA  
434  C  C   . LEU   A 57  ? 0.32237 0.38271 0.25361 -0.06133 0.07781  0.12724  57  LEU   A C   
435  O  O   . LEU   A 57  ? 0.34067 0.39433 0.26422 -0.06342 0.07208  0.13665  57  LEU   A O   
436  C  CB  . LEU   A 57  ? 0.30997 0.37145 0.20886 -0.05280 0.08290  0.10755  57  LEU   A CB  
437  C  CG  . LEU   A 57  ? 0.35626 0.41743 0.23028 -0.04899 0.09228  0.09774  57  LEU   A CG  
438  C  CD1 . LEU   A 57  ? 0.40707 0.46193 0.26726 -0.04539 0.08385  0.08850  57  LEU   A CD1 
439  C  CD2 . LEU   A 57  ? 0.39981 0.45812 0.25008 -0.05145 0.09745  0.10407  57  LEU   A CD2 
440  N  N   . LEU   A 58  ? 0.28593 0.34876 0.24305 -0.06196 0.07529  0.12423  58  LEU   A N   
441  C  CA  . LEU   A 58  ? 0.27714 0.33162 0.25213 -0.06484 0.06543  0.12963  58  LEU   A CA  
442  C  C   . LEU   A 58  ? 0.29170 0.34465 0.27856 -0.07063 0.06802  0.14017  58  LEU   A C   
443  O  O   . LEU   A 58  ? 0.29989 0.34245 0.29200 -0.07252 0.06108  0.14763  58  LEU   A O   
444  C  CB  . LEU   A 58  ? 0.26631 0.32246 0.26218 -0.06419 0.06161  0.12128  58  LEU   A CB  
445  C  CG  . LEU   A 58  ? 0.29006 0.33459 0.30237 -0.06645 0.05169  0.12309  58  LEU   A CG  
446  C  CD1 . LEU   A 58  ? 0.30237 0.33610 0.30177 -0.06352 0.04348  0.12701  58  LEU   A CD1 
447  C  CD2 . LEU   A 58  ? 0.26816 0.31517 0.29627 -0.06591 0.04849  0.11301  58  LEU   A CD2 
448  N  N   . ILE   A 59  ? 0.29912 0.36216 0.29150 -0.07333 0.07818  0.14113  59  ILE   A N   
449  C  CA  . ILE   A 59  ? 0.31452 0.37655 0.31849 -0.07960 0.08087  0.15143  59  ILE   A CA  
450  C  C   . ILE   A 59  ? 0.33996 0.39563 0.32474 -0.08040 0.08077  0.16263  59  ILE   A C   
451  O  O   . ILE   A 59  ? 0.35360 0.40380 0.34725 -0.08500 0.07963  0.17301  59  ILE   A O   
452  C  CB  . ILE   A 59  ? 0.31794 0.39433 0.33256 -0.08233 0.09205  0.15032  59  ILE   A CB  
453  C  CG1 . ILE   A 59  ? 0.33062 0.40597 0.36273 -0.09000 0.09331  0.15997  59  ILE   A CG1 
454  C  CG2 . ILE   A 59  ? 0.33620 0.41988 0.32795 -0.07978 0.10325  0.15052  59  ILE   A CG2 
455  C  CD1 . ILE   A 59  ? 0.37714 0.44198 0.43022 -0.09368 0.08333  0.15910  59  ILE   A CD1 
456  N  N   . ARG   A 60  ? 0.34837 0.40415 0.30681 -0.07623 0.08126  0.16065  60  ARG   A N   
457  C  CA  . ARG   A 60  ? 0.37409 0.42511 0.31182 -0.07689 0.07972  0.17083  60  ARG   A CA  
458  C  C   . ARG   A 60  ? 0.37106 0.41130 0.31040 -0.07520 0.06632  0.17580  60  ARG   A C   
459  O  O   . ARG   A 60  ? 0.39208 0.42918 0.31670 -0.07548 0.06290  0.18535  60  ARG   A O   
460  C  CB  . ARG   A 60  ? 0.38788 0.44308 0.29527 -0.07375 0.08564  0.16513  60  ARG   A CB  
461  C  CG  . ARG   A 60  ? 0.40127 0.46567 0.30406 -0.07541 0.10079  0.16324  60  ARG   A CG  
462  C  CD  . ARG   A 60  ? 0.40714 0.47369 0.28586 -0.07085 0.10758  0.15154  60  ARG   A CD  
463  N  NE  . ARG   A 60  ? 0.41094 0.48716 0.29475 -0.07105 0.12259  0.14615  60  ARG   A NE  
464  C  CZ  . ARG   A 60  ? 0.45797 0.53597 0.32499 -0.06709 0.13221  0.13495  60  ARG   A CZ  
465  N  NH1 . ARG   A 60  ? 0.47922 0.54940 0.32362 -0.06258 0.12783  0.12688  60  ARG   A NH1 
466  N  NH2 . ARG   A 60  ? 0.48400 0.57190 0.35854 -0.06768 0.14645  0.13142  60  ARG   A NH2 
467  N  N   . LYS   A 61  ? 0.36089 0.39603 0.31803 -0.07334 0.05894  0.16973  61  LYS   A N   
468  C  CA  . LYS   A 61  ? 0.38085 0.40594 0.34222 -0.07073 0.04713  0.17295  61  LYS   A CA  
469  C  C   . LYS   A 61  ? 0.36215 0.37753 0.34788 -0.07376 0.04449  0.18025  61  LYS   A C   
470  O  O   . LYS   A 61  ? 0.37151 0.38755 0.37389 -0.07801 0.04972  0.17857  61  LYS   A O   
471  C  CB  . LYS   A 61  ? 0.36549 0.38962 0.33002 -0.06648 0.04153  0.16083  61  LYS   A CB  
472  C  CG  . LYS   A 61  ? 0.33923 0.36908 0.27871 -0.06292 0.04108  0.15375  61  LYS   A CG  
473  C  CD  . LYS   A 61  ? 0.41378 0.44336 0.33105 -0.06276 0.03749  0.16187  61  LYS   A CD  
474  C  CE  . LYS   A 61  ? 0.38087 0.41360 0.27449 -0.05983 0.03474  0.15281  61  LYS   A CE  
475  N  NZ  . LYS   A 61  ? 0.46260 0.49667 0.33203 -0.06098 0.03222  0.15987  61  LYS   A NZ  
476  N  N   . SER   A 62  ? 0.43474 0.44101 0.42331 -0.07147 0.03612  0.18779  62  SER   A N   
477  C  CA  . SER   A 62  ? 0.42669 0.42026 0.43838 -0.07270 0.03288  0.19298  62  SER   A CA  
478  C  C   . SER   A 62  ? 0.41317 0.39783 0.43499 -0.06734 0.02426  0.18705  62  SER   A C   
479  O  O   . SER   A 62  ? 0.38826 0.37726 0.39793 -0.06282 0.01923  0.18313  62  SER   A O   
480  C  CB  . SER   A 62  ? 0.40337 0.39324 0.41280 -0.07395 0.03187  0.20919  62  SER   A CB  
481  O  OG  . SER   A 62  ? 0.50043 0.49772 0.50126 -0.07924 0.04054  0.21557  62  SER   A OG  
482  N  N   . ASN   A 63  ? 0.39322 0.36469 0.43724 -0.06808 0.02296  0.18605  63  ASN   A N   
483  C  CA  . ASN   A 63  ? 0.34548 0.30685 0.40040 -0.06242 0.01614  0.18116  63  ASN   A CA  
484  C  C   . ASN   A 63  ? 0.38595 0.34979 0.43196 -0.05662 0.00912  0.19005  63  ASN   A C   
485  O  O   . ASN   A 63  ? 0.39423 0.35967 0.43810 -0.05149 0.00359  0.18432  63  ASN   A O   
486  C  CB  . ASN   A 63  ? 0.40043 0.34497 0.47804 -0.06406 0.01690  0.18089  63  ASN   A CB  
487  C  CG  . ASN   A 63  ? 0.39964 0.34087 0.48769 -0.06981 0.02119  0.16840  63  ASN   A CG  
488  O  OD1 . ASN   A 63  ? 0.39978 0.35077 0.48172 -0.07069 0.02234  0.15871  63  ASN   A OD1 
489  N  ND2 . ASN   A 63  ? 0.38051 0.30832 0.48441 -0.07433 0.02338  0.16886  63  ASN   A ND2 
490  N  N   . HIS   A 64  ? 0.40328 0.36874 0.44420 -0.05783 0.00894  0.20445  64  HIS   A N   
491  C  CA  . HIS   A 64  ? 0.41786 0.38681 0.45272 -0.05312 0.00129  0.21420  64  HIS   A CA  
492  C  C   . HIS   A 64  ? 0.39935 0.38228 0.40957 -0.05218 -0.00221 0.21087  64  HIS   A C   
493  O  O   . HIS   A 64  ? 0.42769 0.41504 0.43317 -0.04864 -0.01008 0.21625  64  HIS   A O   
494  C  CB  . HIS   A 64  ? 0.45598 0.42340 0.49180 -0.05535 0.00194  0.23132  64  HIS   A CB  
495  C  CG  . HIS   A 64  ? 0.46905 0.44760 0.48209 -0.06057 0.00648  0.23735  64  HIS   A CG  
496  N  ND1 . HIS   A 64  ? 0.52660 0.50406 0.54095 -0.06670 0.01538  0.23952  64  HIS   A ND1 
497  C  CD2 . HIS   A 64  ? 0.49096 0.48155 0.47924 -0.06081 0.00378  0.24172  64  HIS   A CD2 
498  C  CE1 . HIS   A 64  ? 0.50880 0.49727 0.50028 -0.06983 0.01895  0.24488  64  HIS   A CE1 
499  N  NE2 . HIS   A 64  ? 0.55290 0.54869 0.52704 -0.06644 0.01205  0.24580  64  HIS   A NE2 
500  N  N   . ASN   A 65  ? 0.38845 0.37844 0.38391 -0.05535 0.00344  0.20171  65  ASN   A N   
501  C  CA  . ASN   A 65  ? 0.39047 0.39115 0.36238 -0.05446 0.00100  0.19565  65  ASN   A CA  
502  C  C   . ASN   A 65  ? 0.38922 0.38903 0.36625 -0.04998 -0.00487 0.18466  65  ASN   A C   
503  O  O   . ASN   A 65  ? 0.41518 0.42253 0.37431 -0.04911 -0.00858 0.17962  65  ASN   A O   
504  C  CB  . ASN   A 65  ? 0.41667 0.42435 0.37274 -0.05852 0.01072  0.18902  65  ASN   A CB  
505  C  CG  . ASN   A 65  ? 0.47565 0.48651 0.42175 -0.06293 0.01709  0.19975  65  ASN   A CG  
506  O  OD1 . ASN   A 65  ? 0.42800 0.44221 0.37208 -0.06647 0.02690  0.19694  65  ASN   A OD1 
507  N  ND2 . ASN   A 65  ? 0.47352 0.48455 0.41372 -0.06277 0.01168  0.21262  65  ASN   A ND2 
508  N  N   . PHE   A 66  ? 0.36835 0.35851 0.36852 -0.04749 -0.00544 0.18022  66  PHE   A N   
509  C  CA  . PHE   A 66  ? 0.40183 0.39040 0.40847 -0.04318 -0.01002 0.17002  66  PHE   A CA  
510  C  C   . PHE   A 66  ? 0.37707 0.35967 0.40096 -0.03782 -0.01680 0.17595  66  PHE   A C   
511  O  O   . PHE   A 66  ? 0.38296 0.35429 0.42693 -0.03659 -0.01462 0.17855  66  PHE   A O   
512  C  CB  . PHE   A 66  ? 0.33401 0.31651 0.35295 -0.04440 -0.00453 0.15866  66  PHE   A CB  
513  C  CG  . PHE   A 66  ? 0.33865 0.32895 0.34526 -0.04909 0.00279  0.15292  66  PHE   A CG  
514  C  CD1 . PHE   A 66  ? 0.29354 0.29219 0.28504 -0.04835 0.00285  0.14412  66  PHE   A CD1 
515  C  CD2 . PHE   A 66  ? 0.33668 0.32629 0.34841 -0.05409 0.01011  0.15624  66  PHE   A CD2 
516  C  CE1 . PHE   A 66  ? 0.30976 0.31623 0.29215 -0.05155 0.01084  0.13868  66  PHE   A CE1 
517  C  CE2 . PHE   A 66  ? 0.34250 0.34129 0.34601 -0.05767 0.01765  0.15113  66  PHE   A CE2 
518  C  CZ  . PHE   A 66  ? 0.31096 0.31830 0.30029 -0.05589 0.01837  0.14228  66  PHE   A CZ  
519  N  N   . LEU   A 67  ? 0.33469 0.32489 0.35166 -0.03480 -0.02456 0.17733  67  LEU   A N   
520  C  CA  . LEU   A 67  ? 0.37309 0.36077 0.40824 -0.02906 -0.03070 0.18218  67  LEU   A CA  
521  C  C   . LEU   A 67  ? 0.32003 0.30533 0.36432 -0.02500 -0.03185 0.16988  67  LEU   A C   
522  O  O   . LEU   A 67  ? 0.35365 0.34668 0.38354 -0.02596 -0.03447 0.16244  67  LEU   A O   
523  C  CB  . LEU   A 67  ? 0.40119 0.40067 0.42577 -0.02900 -0.03904 0.19211  67  LEU   A CB  
524  C  CG  . LEU   A 67  ? 0.45079 0.45642 0.45533 -0.03436 -0.03839 0.20191  67  LEU   A CG  
525  C  CD1 . LEU   A 67  ? 0.48024 0.49823 0.47229 -0.03508 -0.04785 0.20923  67  LEU   A CD1 
526  C  CD2 . LEU   A 67  ? 0.50396 0.50128 0.52133 -0.03501 -0.03373 0.21313  67  LEU   A CD2 
527  N  N   . VAL   A 68  ? 0.34846 0.32223 0.41576 -0.02067 -0.02921 0.16713  68  VAL   A N   
528  C  CA  . VAL   A 68  ? 0.30340 0.27367 0.38115 -0.01626 -0.02921 0.15578  68  VAL   A CA  
529  C  C   . VAL   A 68  ? 0.32684 0.29678 0.42376 -0.00939 -0.03275 0.16093  68  VAL   A C   
530  O  O   . VAL   A 68  ? 0.33801 0.29935 0.45097 -0.00690 -0.03022 0.16750  68  VAL   A O   
531  C  CB  . VAL   A 68  ? 0.31529 0.27178 0.40261 -0.01738 -0.02152 0.14505  68  VAL   A CB  
532  C  CG1 . VAL   A 68  ? 0.28900 0.24261 0.38424 -0.01305 -0.02131 0.13303  68  VAL   A CG1 
533  C  CG2 . VAL   A 68  ? 0.34070 0.29978 0.41255 -0.02459 -0.01752 0.14145  68  VAL   A CG2 
534  N  N   . GLN   A 69  ? 0.28613 0.26552 0.38253 -0.00648 -0.03804 0.15788  69  GLN   A N   
535  C  CA  . GLN   A 69  ? 0.32907 0.31123 0.44496 -0.00005 -0.04092 0.16241  69  GLN   A CA  
536  C  C   . GLN   A 69  ? 0.29455 0.27301 0.42091 0.00454  -0.03778 0.14976  69  GLN   A C   
537  O  O   . GLN   A 69  ? 0.26954 0.25414 0.38392 0.00270  -0.03997 0.14171  69  GLN   A O   
538  C  CB  . GLN   A 69  ? 0.37735 0.37639 0.48510 -0.00156 -0.05042 0.17159  69  GLN   A CB  
539  C  CG  . GLN   A 69  ? 0.41741 0.42255 0.50398 -0.00810 -0.05383 0.18014  69  GLN   A CG  
540  C  CD  . GLN   A 69  ? 0.51198 0.53254 0.59186 -0.01002 -0.06351 0.18965  69  GLN   A CD  
541  O  OE1 . GLN   A 69  ? 0.57485 0.60071 0.67318 -0.00581 -0.06742 0.19602  69  GLN   A OE1 
542  N  NE2 . GLN   A 69  ? 0.53027 0.55822 0.58355 -0.01673 -0.06699 0.19041  69  GLN   A NE2 
543  N  N   . ALA   A 70  ? 0.28298 0.25088 0.43091 0.01043  -0.03203 0.14774  70  ALA   A N   
544  C  CA  . ALA   A 70  ? 0.34440 0.30906 0.50386 0.01568  -0.02789 0.13649  70  ALA   A CA  
545  C  C   . ALA   A 70  ? 0.39951 0.37342 0.57648 0.02149  -0.03072 0.14454  70  ALA   A C   
546  O  O   . ALA   A 70  ? 0.36449 0.33172 0.55974 0.02613  -0.02692 0.15026  70  ALA   A O   
547  C  CB  . ALA   A 70  ? 0.36828 0.31372 0.53706 0.01740  -0.01802 0.12613  70  ALA   A CB  
548  N  N   . GLY   A 71  ? 0.40260 0.39194 0.57451 0.02072  -0.03733 0.14526  71  GLY   A N   
549  C  CA  . GLY   A 71  ? 0.43578 0.43716 0.62298 0.02417  -0.04178 0.15543  71  GLY   A CA  
550  C  C   . GLY   A 71  ? 0.44774 0.45409 0.63385 0.02171  -0.04764 0.17119  71  GLY   A C   
551  O  O   . GLY   A 71  ? 0.46874 0.47886 0.63399 0.01511  -0.05272 0.17445  71  GLY   A O   
552  N  N   . ASN   A 72  ? 0.46655 0.47271 0.67520 0.02719  -0.04625 0.18132  72  ASN   A N   
553  C  CA  . ASN   A 72  ? 0.49863 0.50875 0.70989 0.02583  -0.05118 0.19782  72  ASN   A CA  
554  C  C   . ASN   A 72  ? 0.47873 0.47105 0.69672 0.02765  -0.04375 0.19976  72  ASN   A C   
555  O  O   . ASN   A 72  ? 0.53114 0.52272 0.76370 0.03036  -0.04430 0.21327  72  ASN   A O   
556  C  CB  . ASN   A 72  ? 0.50699 0.52984 0.73995 0.03020  -0.05549 0.21037  72  ASN   A CB  
557  C  CG  . ASN   A 72  ? 0.59851 0.61480 0.85737 0.03900  -0.04650 0.20481  72  ASN   A CG  
558  O  OD1 . ASN   A 72  ? 0.66117 0.66007 0.92426 0.04246  -0.03635 0.19394  72  ASN   A OD1 
559  N  ND2 . ASN   A 72  ? 0.56387 0.59413 0.83960 0.04219  -0.04990 0.21198  72  ASN   A ND2 
560  N  N   . VAL   A 73  ? 0.45876 0.43665 0.66691 0.02571  -0.03701 0.18691  73  VAL   A N   
561  C  CA  . VAL   A 73  ? 0.44698 0.40655 0.66024 0.02583  -0.02979 0.18675  73  VAL   A CA  
562  C  C   . VAL   A 73  ? 0.40849 0.36484 0.59777 0.01773  -0.03023 0.18264  73  VAL   A C   
563  O  O   . VAL   A 73  ? 0.38837 0.34590 0.56346 0.01476  -0.02975 0.17061  73  VAL   A O   
564  C  CB  . VAL   A 73  ? 0.46392 0.40629 0.69265 0.03134  -0.01913 0.17337  73  VAL   A CB  
565  C  CG1 . VAL   A 73  ? 0.47063 0.39275 0.70025 0.02898  -0.01221 0.17046  73  VAL   A CG1 
566  C  CG2 . VAL   A 73  ? 0.50171 0.44642 0.75575 0.03987  -0.01679 0.17849  73  VAL   A CG2 
567  N  N   . GLN   A 74  ? 0.43227 0.38507 0.61781 0.01419  -0.03070 0.19322  74  GLN   A N   
568  C  CA  . GLN   A 74  ? 0.41695 0.36847 0.58064 0.00627  -0.03035 0.19121  74  GLN   A CA  
569  C  C   . GLN   A 74  ? 0.43250 0.36464 0.60044 0.00444  -0.02129 0.18096  74  GLN   A C   
570  O  O   . GLN   A 74  ? 0.44989 0.36805 0.63505 0.00726  -0.01629 0.18315  74  GLN   A O   
571  C  CB  . GLN   A 74  ? 0.48795 0.44679 0.64336 0.00239  -0.03503 0.20799  74  GLN   A CB  
572  C  CG  . GLN   A 74  ? 0.48144 0.44362 0.61131 -0.00589 -0.03479 0.20668  74  GLN   A CG  
573  C  CD  . GLN   A 74  ? 0.57662 0.53870 0.70204 -0.00971 -0.03497 0.22162  74  GLN   A CD  
574  O  OE1 . GLN   A 74  ? 0.59383 0.55583 0.73357 -0.00637 -0.03731 0.23490  74  GLN   A OE1 
575  N  NE2 . GLN   A 74  ? 0.59765 0.56008 0.70414 -0.01667 -0.03188 0.22003  74  GLN   A NE2 
576  N  N   . LEU   A 75  ? 0.36665 0.29806 0.51888 -0.00086 -0.01933 0.16970  75  LEU   A N   
577  C  CA  . LEU   A 75  ? 0.38546 0.30095 0.53939 -0.00467 -0.01182 0.15874  75  LEU   A CA  
578  C  C   . LEU   A 75  ? 0.42959 0.34529 0.57164 -0.01264 -0.01073 0.16525  75  LEU   A C   
579  O  O   . LEU   A 75  ? 0.45311 0.38181 0.57651 -0.01688 -0.01378 0.16785  75  LEU   A O   
580  C  CB  . LEU   A 75  ? 0.34952 0.26532 0.49596 -0.00579 -0.01013 0.14240  75  LEU   A CB  
581  C  CG  . LEU   A 75  ? 0.36827 0.28368 0.52509 0.00149  -0.00965 0.13378  75  LEU   A CG  
582  C  CD1 . LEU   A 75  ? 0.33096 0.24454 0.47954 -0.00097 -0.00714 0.11778  75  LEU   A CD1 
583  C  CD2 . LEU   A 75  ? 0.40906 0.30959 0.58660 0.00693  -0.00400 0.13236  75  LEU   A CD2 
584  N  N   . ARG   A 76  ? 0.39317 0.29428 0.54573 -0.01493 -0.00572 0.16727  76  ARG   A N   
585  C  CA  . ARG   A 76  ? 0.39992 0.30116 0.54378 -0.02276 -0.00377 0.17416  76  ARG   A CA  
586  C  C   . ARG   A 76  ? 0.39454 0.29508 0.52882 -0.02990 0.00008  0.16111  76  ARG   A C   
587  O  O   . ARG   A 76  ? 0.37868 0.26696 0.52112 -0.03101 0.00392  0.14789  76  ARG   A O   
588  C  CB  . ARG   A 76  ? 0.42881 0.31434 0.58857 -0.02330 0.00004  0.18139  76  ARG   A CB  
589  C  CG  . ARG   A 76  ? 0.45828 0.34387 0.61079 -0.03183 0.00265  0.18922  76  ARG   A CG  
590  C  CD  . ARG   A 76  ? 0.52529 0.39652 0.69372 -0.03179 0.00526  0.19984  76  ARG   A CD  
591  N  NE  . ARG   A 76  ? 0.60276 0.45343 0.78390 -0.03475 0.01114  0.18794  76  ARG   A NE  
592  C  CZ  . ARG   A 76  ? 0.61847 0.46118 0.79937 -0.04394 0.01542  0.18607  76  ARG   A CZ  
593  N  NH1 . ARG   A 76  ? 0.60018 0.45357 0.77067 -0.05031 0.01565  0.19629  76  ARG   A NH1 
594  N  NH2 . ARG   A 76  ? 0.60397 0.42779 0.79496 -0.04729 0.01977  0.17343  76  ARG   A NH2 
595  N  N   . VAL   A 77  ? 0.38676 0.30111 0.50353 -0.03488 -0.00075 0.16450  77  VAL   A N   
596  C  CA  . VAL   A 77  ? 0.34749 0.26464 0.45653 -0.04185 0.00316  0.15436  77  VAL   A CA  
597  C  C   . VAL   A 77  ? 0.38652 0.29565 0.50190 -0.04922 0.00836  0.15745  77  VAL   A C   
598  O  O   . VAL   A 77  ? 0.35720 0.26889 0.47003 -0.05103 0.00887  0.17096  77  VAL   A O   
599  C  CB  . VAL   A 77  ? 0.37879 0.31428 0.46704 -0.04352 0.00148  0.15665  77  VAL   A CB  
600  C  CG1 . VAL   A 77  ? 0.34004 0.28061 0.42279 -0.05077 0.00674  0.14912  77  VAL   A CG1 
601  C  CG2 . VAL   A 77  ? 0.36634 0.30882 0.44843 -0.03753 -0.00391 0.15167  77  VAL   A CG2 
602  N  N   . ILE   A 78  ? 0.34849 0.24845 0.47169 -0.05420 0.01190  0.14500  78  ILE   A N   
603  C  CA  . ILE   A 78  ? 0.35813 0.24996 0.48880 -0.06246 0.01633  0.14629  78  ILE   A CA  
604  C  C   . ILE   A 78  ? 0.34250 0.24477 0.46788 -0.07087 0.01923  0.13901  78  ILE   A C   
605  O  O   . ILE   A 78  ? 0.36035 0.25926 0.49183 -0.07890 0.02273  0.14015  78  ILE   A O   
606  C  CB  . ILE   A 78  ? 0.38536 0.25530 0.53184 -0.06273 0.01790  0.13856  78  ILE   A CB  
607  C  CG1 . ILE   A 78  ? 0.38389 0.24978 0.53084 -0.06289 0.01762  0.11982  78  ILE   A CG1 
608  C  CG2 . ILE   A 78  ? 0.40369 0.26414 0.55906 -0.05401 0.01627  0.14792  78  ILE   A CG2 
609  C  CD1 . ILE   A 78  ? 0.43647 0.28038 0.59537 -0.06174 0.01951  0.11042  78  ILE   A CD1 
610  N  N   . GLY   A 79  ? 0.34454 0.26018 0.46008 -0.06937 0.01792  0.13210  79  GLY   A N   
611  C  CA  . GLY   A 79  ? 0.32783 0.25687 0.43958 -0.07613 0.02085  0.12678  79  GLY   A CA  
612  C  C   . GLY   A 79  ? 0.32199 0.26603 0.42095 -0.07181 0.01924  0.12316  79  GLY   A C   
613  O  O   . GLY   A 79  ? 0.31253 0.25422 0.40747 -0.06485 0.01522  0.12142  79  GLY   A O   
614  N  N   . HIS   A 80  ? 0.29818 0.25806 0.39154 -0.07581 0.02283  0.12230  80  HIS   A N   
615  C  CA  . HIS   A 80  ? 0.29655 0.27038 0.37776 -0.07206 0.02236  0.11821  80  HIS   A CA  
616  C  C   . HIS   A 80  ? 0.29795 0.28613 0.38232 -0.07707 0.02649  0.11193  80  HIS   A C   
617  O  O   . HIS   A 80  ? 0.29138 0.28350 0.38254 -0.08301 0.03070  0.11521  80  HIS   A O   
618  C  CB  . HIS   A 80  ? 0.30907 0.29092 0.37227 -0.06791 0.02302  0.12850  80  HIS   A CB  
619  C  CG  . HIS   A 80  ? 0.32839 0.31757 0.38697 -0.07205 0.02913  0.13767  80  HIS   A CG  
620  N  ND1 . HIS   A 80  ? 0.38207 0.36261 0.44692 -0.07479 0.02990  0.14755  80  HIS   A ND1 
621  C  CD2 . HIS   A 80  ? 0.35944 0.36360 0.40841 -0.07369 0.03562  0.13828  80  HIS   A CD2 
622  C  CE1 . HIS   A 80  ? 0.42352 0.41380 0.48220 -0.07849 0.03625  0.15435  80  HIS   A CE1 
623  N  NE2 . HIS   A 80  ? 0.39043 0.39505 0.43946 -0.07763 0.04019  0.14847  80  HIS   A NE2 
624  N  N   . SER   A 81  ? 0.25355 0.25054 0.33419 -0.07443 0.02517  0.10347  81  SER   A N   
625  C  CA  . SER   A 81  ? 0.24882 0.26250 0.33296 -0.07726 0.02888  0.09825  81  SER   A CA  
626  C  C   . SER   A 81  ? 0.23908 0.26289 0.31308 -0.07161 0.02842  0.09312  81  SER   A C   
627  O  O   . SER   A 81  ? 0.24647 0.26260 0.31346 -0.06670 0.02358  0.08989  81  SER   A O   
628  C  CB  . SER   A 81  ? 0.25209 0.26380 0.35282 -0.08370 0.02625  0.08914  81  SER   A CB  
629  O  OG  . SER   A 81  ? 0.31164 0.31160 0.41455 -0.08221 0.02021  0.08004  81  SER   A OG  
630  N  N   . MET   A 82  ? 0.18137 0.22216 0.25496 -0.07131 0.03373  0.09129  82  MET   A N   
631  C  CA  . MET   A 82  ? 0.21856 0.26905 0.28418 -0.06503 0.03409  0.08355  82  MET   A CA  
632  C  C   . MET   A 82  ? 0.19151 0.24783 0.27042 -0.06607 0.03008  0.07325  82  MET   A C   
633  O  O   . MET   A 82  ? 0.18979 0.25439 0.28505 -0.07291 0.03106  0.07456  82  MET   A O   
634  C  CB  . MET   A 82  ? 0.27442 0.34004 0.33238 -0.06266 0.04369  0.08745  82  MET   A CB  
635  C  CG  . MET   A 82  ? 0.23695 0.30400 0.27761 -0.05399 0.04445  0.07994  82  MET   A CG  
636  S  SD  . MET   A 82  ? 0.27951 0.35526 0.30243 -0.05200 0.05651  0.08628  82  MET   A SD  
637  C  CE  . MET   A 82  ? 0.31401 0.40465 0.35677 -0.05472 0.06494  0.08800  82  MET   A CE  
638  N  N   . GLN   A 83  ? 0.19101 0.24478 0.26223 -0.05951 0.02549  0.06361  83  GLN   A N   
639  C  CA  . GLN   A 83  ? 0.18220 0.24414 0.26213 -0.05922 0.02182  0.05473  83  GLN   A CA  
640  C  C   . GLN   A 83  ? 0.12769 0.19576 0.19651 -0.05005 0.02364  0.05012  83  GLN   A C   
641  O  O   . GLN   A 83  ? 0.13410 0.19239 0.19079 -0.04487 0.02021  0.04561  83  GLN   A O   
642  C  CB  . GLN   A 83  ? 0.25674 0.30603 0.33970 -0.06171 0.01394  0.04712  83  GLN   A CB  
643  C  CG  . GLN   A 83  ? 0.28017 0.33724 0.36613 -0.06053 0.00927  0.03795  83  GLN   A CG  
644  C  CD  . GLN   A 83  ? 0.35586 0.40134 0.44463 -0.06534 0.00295  0.03009  83  GLN   A CD  
645  O  OE1 . GLN   A 83  ? 0.36936 0.40714 0.46667 -0.07350 0.00224  0.03108  83  GLN   A OE1 
646  N  NE2 . GLN   A 83  ? 0.30772 0.35076 0.38885 -0.06054 -0.00089 0.02196  83  GLN   A NE2 
647  N  N   . ASN   A 84  ? 0.16026 0.24417 0.23483 -0.04808 0.02955  0.05173  84  ASN   A N   
648  C  CA  . ASN   A 84  ? 0.12599 0.21395 0.19117 -0.03918 0.03327  0.04780  84  ASN   A CA  
649  C  C   . ASN   A 84  ? 0.15225 0.22827 0.19627 -0.03545 0.03543  0.04812  84  ASN   A C   
650  O  O   . ASN   A 84  ? 0.14221 0.21764 0.18026 -0.03813 0.04062  0.05508  84  ASN   A O   
651  C  CB  . ASN   A 84  ? 0.11048 0.19914 0.17897 -0.03591 0.02636  0.04012  84  ASN   A CB  
652  C  CG  . ASN   A 84  ? 0.13095 0.23309 0.21875 -0.04123 0.02274  0.04073  84  ASN   A CG  
653  O  OD1 . ASN   A 84  ? 0.13424 0.25238 0.23528 -0.04196 0.02792  0.04587  84  ASN   A OD1 
654  N  ND2 . ASN   A 84  ? 0.13854 0.23488 0.22824 -0.04573 0.01408  0.03576  84  ASN   A ND2 
655  N  N   . CYS   A 85  ? 0.13173 0.19884 0.16422 -0.03041 0.03094  0.04162  85  CYS   A N   
656  C  CA  . CYS   A 85  ? 0.12894 0.18697 0.14157 -0.02803 0.03193  0.04196  85  CYS   A CA  
657  C  C   . CYS   A 85  ? 0.15299 0.19891 0.16095 -0.03064 0.02418  0.04439  85  CYS   A C   
658  O  O   . CYS   A 85  ? 0.17314 0.21251 0.16578 -0.02897 0.02218  0.04472  85  CYS   A O   
659  C  CB  . CYS   A 85  ? 0.13424 0.19005 0.13699 -0.02138 0.03256  0.03409  85  CYS   A CB  
660  S  SG  . CYS   A 85  ? 0.15892 0.22634 0.16574 -0.01629 0.04415  0.03228  85  CYS   A SG  
661  N  N   . VAL   A 86  ? 0.13827 0.18103 0.15955 -0.03485 0.01993  0.04619  86  VAL   A N   
662  C  CA  . VAL   A 86  ? 0.18078 0.21156 0.20090 -0.03638 0.01433  0.04972  86  VAL   A CA  
663  C  C   . VAL   A 86  ? 0.16797 0.19672 0.19524 -0.04250 0.01663  0.05958  86  VAL   A C   
664  O  O   . VAL   A 86  ? 0.18348 0.21973 0.22105 -0.04699 0.02099  0.06188  86  VAL   A O   
665  C  CB  . VAL   A 86  ? 0.20763 0.23147 0.23599 -0.03529 0.00808  0.04268  86  VAL   A CB  
666  C  CG1 . VAL   A 86  ? 0.21501 0.24013 0.23606 -0.02952 0.00572  0.03491  86  VAL   A CG1 
667  C  CG2 . VAL   A 86  ? 0.16506 0.19256 0.20762 -0.03978 0.00816  0.03920  86  VAL   A CG2 
668  N  N   . LEU   A 87  ? 0.16630 0.18571 0.18911 -0.04278 0.01358  0.06676  87  LEU   A N   
669  C  CA  . LEU   A 87  ? 0.19351 0.20684 0.22482 -0.04803 0.01441  0.07726  87  LEU   A CA  
670  C  C   . LEU   A 87  ? 0.18986 0.19029 0.23540 -0.04866 0.00967  0.07408  87  LEU   A C   
671  O  O   . LEU   A 87  ? 0.20915 0.20395 0.25308 -0.04370 0.00508  0.06853  87  LEU   A O   
672  C  CB  . LEU   A 87  ? 0.23310 0.24405 0.25142 -0.04756 0.01375  0.08914  87  LEU   A CB  
673  C  CG  . LEU   A 87  ? 0.30213 0.32110 0.30838 -0.05071 0.02007  0.09910  87  LEU   A CG  
674  C  CD1 . LEU   A 87  ? 0.27830 0.29251 0.27229 -0.05024 0.01553  0.11075  87  LEU   A CD1 
675  C  CD2 . LEU   A 87  ? 0.30072 0.32127 0.32197 -0.05742 0.02565  0.10622  87  LEU   A CD2 
676  N  N   . LYS   A 88  ? 0.18446 0.17984 0.24419 -0.05504 0.01149  0.07720  88  LYS   A N   
677  C  CA  . LYS   A 88  ? 0.19139 0.17116 0.26430 -0.05649 0.00866  0.07413  88  LYS   A CA  
678  C  C   . LYS   A 88  ? 0.23364 0.20281 0.31288 -0.05922 0.00985  0.08840  88  LYS   A C   
679  O  O   . LYS   A 88  ? 0.24701 0.21882 0.32958 -0.06455 0.01358  0.09354  88  LYS   A O   
680  C  CB  . LYS   A 88  ? 0.21188 0.19220 0.29619 -0.06292 0.00906  0.06436  88  LYS   A CB  
681  C  CG  . LYS   A 88  ? 0.20445 0.19518 0.28361 -0.06010 0.00699  0.05187  88  LYS   A CG  
682  C  CD  . LYS   A 88  ? 0.25021 0.24565 0.33961 -0.06786 0.00624  0.04453  88  LYS   A CD  
683  C  CE  . LYS   A 88  ? 0.33249 0.31204 0.42817 -0.07121 0.00338  0.03514  88  LYS   A CE  
684  N  NZ  . LYS   A 88  ? 0.44262 0.42772 0.54662 -0.08104 0.00135  0.02803  88  LYS   A NZ  
685  N  N   . LEU   A 89  ? 0.22294 0.18195 0.30223 -0.05359 0.00655  0.09312  89  LEU   A N   
686  C  CA  . LEU   A 89  ? 0.23245 0.18320 0.31448 -0.05216 0.00656  0.10376  89  LEU   A CA  
687  C  C   . LEU   A 89  ? 0.25277 0.18579 0.35041 -0.05193 0.00686  0.09779  89  LEU   A C   
688  O  O   . LEU   A 89  ? 0.27520 0.20057 0.37756 -0.04661 0.00486  0.09125  89  LEU   A O   
689  C  CB  . LEU   A 89  ? 0.25973 0.21396 0.33192 -0.04544 0.00214  0.11255  89  LEU   A CB  
690  C  CG  . LEU   A 89  ? 0.26287 0.23285 0.31513 -0.04608 0.00209  0.11711  89  LEU   A CG  
691  C  CD1 . LEU   A 89  ? 0.28965 0.26249 0.33204 -0.04088 -0.00383 0.12498  89  LEU   A CD1 
692  C  CD2 . LEU   A 89  ? 0.27369 0.24992 0.32095 -0.05166 0.00782  0.12319  89  LEU   A CD2 
693  N  N   . LYS   A 90  ? 0.25716 0.18353 0.36225 -0.05787 0.01003  0.09911  90  LYS   A N   
694  C  CA  . LYS   A 90  ? 0.27236 0.18000 0.39001 -0.05814 0.01102  0.09364  90  LYS   A CA  
695  C  C   . LYS   A 90  ? 0.30375 0.20295 0.42602 -0.05112 0.00998  0.10477  90  LYS   A C   
696  O  O   . LYS   A 90  ? 0.35592 0.26001 0.47499 -0.05143 0.00987  0.11851  90  LYS   A O   
697  C  CB  . LYS   A 90  ? 0.30099 0.20434 0.42463 -0.06797 0.01419  0.09159  90  LYS   A CB  
698  C  CG  . LYS   A 90  ? 0.37605 0.26263 0.50800 -0.07154 0.01495  0.07803  90  LYS   A CG  
699  C  CD  . LYS   A 90  ? 0.44405 0.33823 0.57234 -0.07609 0.01346  0.06320  90  LYS   A CD  
700  C  CE  . LYS   A 90  ? 0.46877 0.34615 0.60105 -0.08045 0.01376  0.04865  90  LYS   A CE  
701  N  NZ  . LYS   A 90  ? 0.51421 0.37628 0.65416 -0.08562 0.01619  0.05313  90  LYS   A NZ  
702  N  N   . VAL   A 91  ? 0.32387 0.21207 0.45377 -0.04448 0.00938  0.09910  91  VAL   A N   
703  C  CA  . VAL   A 91  ? 0.31217 0.19375 0.45028 -0.03715 0.00850  0.10936  91  VAL   A CA  
704  C  C   . VAL   A 91  ? 0.33290 0.19380 0.48478 -0.03734 0.01262  0.10312  91  VAL   A C   
705  O  O   . VAL   A 91  ? 0.33797 0.18962 0.49072 -0.04217 0.01530  0.08856  91  VAL   A O   
706  C  CB  . VAL   A 91  ? 0.33296 0.22232 0.46990 -0.02781 0.00459  0.11074  91  VAL   A CB  
707  C  CG1 . VAL   A 91  ? 0.32653 0.23481 0.44753 -0.02876 0.00025  0.11697  91  VAL   A CG1 
708  C  CG2 . VAL   A 91  ? 0.29785 0.18128 0.43799 -0.02510 0.00637  0.09438  91  VAL   A CG2 
709  N  N   . ASP   A 92  ? 0.36967 0.22351 0.53166 -0.03258 0.01296  0.11440  92  ASP   A N   
710  C  CA  . ASP   A 92  ? 0.42899 0.26189 0.60431 -0.03298 0.01751  0.11060  92  ASP   A CA  
711  C  C   . ASP   A 92  ? 0.41138 0.23418 0.59569 -0.02472 0.02010  0.10038  92  ASP   A C   
712  O  O   . ASP   A 92  ? 0.42937 0.23402 0.62525 -0.02334 0.02455  0.09737  92  ASP   A O   
713  C  CB  . ASP   A 92  ? 0.44709 0.27619 0.63096 -0.03196 0.01746  0.12826  92  ASP   A CB  
714  C  CG  . ASP   A 92  ? 0.47467 0.31173 0.66514 -0.02143 0.01409  0.14105  92  ASP   A CG  
715  O  OD1 . ASP   A 92  ? 0.49550 0.34153 0.68437 -0.01497 0.01178  0.13669  92  ASP   A OD1 
716  O  OD2 . ASP   A 92  ? 0.54191 0.37684 0.74009 -0.02012 0.01352  0.15618  92  ASP   A OD2 
717  N  N   . THR   A 93  ? 0.39080 0.22475 0.57017 -0.01929 0.01806  0.09498  93  THR   A N   
718  C  CA  . THR   A 93  ? 0.40030 0.22777 0.58773 -0.01107 0.02135  0.08552  93  THR   A CA  
719  C  C   . THR   A 93  ? 0.34743 0.18020 0.52375 -0.01287 0.02143  0.06976  93  THR   A C   
720  O  O   . THR   A 93  ? 0.32602 0.17514 0.49246 -0.01364 0.01677  0.07252  93  THR   A O   
721  C  CB  . THR   A 93  ? 0.36673 0.20524 0.56332 -0.00076 0.01848  0.09855  93  THR   A CB  
722  O  OG1 . THR   A 93  ? 0.45656 0.29286 0.66225 0.00011  0.01727  0.11502  93  THR   A OG1 
723  C  CG2 . THR   A 93  ? 0.42806 0.26002 0.63610 0.00792  0.02358  0.08959  93  THR   A CG2 
724  N  N   . ALA   A 94  ? 0.36118 0.17991 0.53822 -0.01379 0.02676  0.05328  94  ALA   A N   
725  C  CA  . ALA   A 94  ? 0.31350 0.13717 0.48080 -0.01416 0.02737  0.03829  94  ALA   A CA  
726  C  C   . ALA   A 94  ? 0.31921 0.15140 0.49246 -0.00299 0.02807  0.04036  94  ALA   A C   
727  O  O   . ALA   A 94  ? 0.33708 0.16343 0.52393 0.00479  0.03162  0.04489  94  ALA   A O   
728  C  CB  . ALA   A 94  ? 0.35694 0.16372 0.52060 -0.01920 0.03261  0.01989  94  ALA   A CB  
729  N  N   . ASN   A 95  ? 0.31498 0.16172 0.47940 -0.00245 0.02467  0.03790  95  ASN   A N   
730  C  CA  . ASN   A 95  ? 0.27098 0.12763 0.44076 0.00701  0.02483  0.03974  95  ASN   A CA  
731  C  C   . ASN   A 95  ? 0.30438 0.15028 0.47844 0.01151  0.03320  0.02546  95  ASN   A C   
732  O  O   . ASN   A 95  ? 0.31951 0.16180 0.48216 0.00713  0.03587  0.00986  95  ASN   A O   
733  C  CB  . ASN   A 95  ? 0.23226 0.10481 0.39058 0.00537  0.01956  0.03888  95  ASN   A CB  
734  C  CG  . ASN   A 95  ? 0.22222 0.10696 0.38622 0.01417  0.01857  0.04228  95  ASN   A CG  
735  O  OD1 . ASN   A 95  ? 0.23654 0.11947 0.41388 0.02147  0.02219  0.04515  95  ASN   A OD1 
736  N  ND2 . ASN   A 95  ? 0.23851 0.13624 0.39334 0.01307  0.01366  0.04233  95  ASN   A ND2 
737  N  N   . PRO   A 96  ? 0.31495 0.15686 0.50443 0.01995  0.03764  0.03019  96  PRO   A N   
738  C  CA  . PRO   A 96  ? 0.36065 0.19234 0.55336 0.02436  0.04702  0.01632  96  PRO   A CA  
739  C  C   . PRO   A 96  ? 0.31249 0.15606 0.49856 0.02745  0.04845  0.00826  96  PRO   A C   
740  O  O   . PRO   A 96  ? 0.34732 0.18352 0.53026 0.02920  0.05647  -0.00565 96  PRO   A O   
741  C  CB  . PRO   A 96  ? 0.36139 0.19000 0.57510 0.03331  0.05063  0.02725  96  PRO   A CB  
742  C  CG  . PRO   A 96  ? 0.35771 0.20337 0.57763 0.03523  0.04152  0.04680  96  PRO   A CG  
743  C  CD  . PRO   A 96  ? 0.33437 0.18392 0.53859 0.02595  0.03404  0.04888  96  PRO   A CD  
744  N  N   . LYS   A 97  ? 0.30575 0.16718 0.48862 0.02782  0.04108  0.01652  97  LYS   A N   
745  C  CA  . LYS   A 97  ? 0.25077 0.12433 0.42832 0.03060  0.04180  0.01056  97  LYS   A CA  
746  C  C   . LYS   A 97  ? 0.22776 0.10308 0.38648 0.02264  0.03911  -0.00017 97  LYS   A C   
747  O  O   . LYS   A 97  ? 0.22934 0.11615 0.38261 0.02406  0.03805  -0.00319 97  LYS   A O   
748  C  CB  . LYS   A 97  ? 0.25361 0.14605 0.44027 0.03580  0.03499  0.02623  97  LYS   A CB  
749  C  CG  . LYS   A 97  ? 0.26309 0.15747 0.46972 0.04400  0.03827  0.03545  97  LYS   A CG  
750  C  CD  . LYS   A 97  ? 0.29125 0.20640 0.50523 0.04716  0.03024  0.05002  97  LYS   A CD  
751  C  CE  . LYS   A 97  ? 0.38460 0.30247 0.61905 0.05316  0.03067  0.06310  97  LYS   A CE  
752  N  NZ  . LYS   A 97  ? 0.45407 0.38856 0.69014 0.05151  0.01889  0.08006  97  LYS   A NZ  
753  N  N   . THR   A 98  ? 0.26931 0.13431 0.41900 0.01394  0.03793  -0.00566 98  THR   A N   
754  C  CA  . THR   A 98  ? 0.25744 0.12611 0.39071 0.00542  0.03476  -0.01518 98  THR   A CA  
755  C  C   . THR   A 98  ? 0.27091 0.13966 0.39382 0.00578  0.04060  -0.03144 98  THR   A C   
756  O  O   . THR   A 98  ? 0.26738 0.12403 0.38777 0.00542  0.04740  -0.04206 98  THR   A O   
757  C  CB  . THR   A 98  ? 0.29486 0.15366 0.42207 -0.00484 0.03288  -0.01857 98  THR   A CB  
758  O  OG1 . THR   A 98  ? 0.29030 0.14980 0.42602 -0.00522 0.02842  -0.00264 98  THR   A OG1 
759  C  CG2 . THR   A 98  ? 0.26898 0.13600 0.38126 -0.01425 0.02842  -0.02663 98  THR   A CG2 
760  N  N   . PRO   A 99  ? 0.24469 0.12647 0.36048 0.00627  0.03839  -0.03370 99  PRO   A N   
761  C  CA  . PRO   A 99  ? 0.23464 0.11831 0.33733 0.00537  0.04365  -0.04862 99  PRO   A CA  
762  C  C   . PRO   A 99  ? 0.25990 0.14082 0.34493 -0.00638 0.04085  -0.06038 99  PRO   A C   
763  O  O   . PRO   A 99  ? 0.24923 0.13042 0.33346 -0.01354 0.03442  -0.05611 99  PRO   A O   
764  C  CB  . PRO   A 99  ? 0.20076 0.10518 0.29999 0.00912  0.03938  -0.04231 99  PRO   A CB  
765  C  CG  . PRO   A 99  ? 0.23531 0.14953 0.33378 0.00578  0.02924  -0.02986 99  PRO   A CG  
766  C  CD  . PRO   A 99  ? 0.21317 0.11334 0.32587 0.00613  0.02937  -0.02203 99  PRO   A CD  
767  N  N   . LYS   A 100 ? 0.24595 0.12724 0.31605 -0.00871 0.04511  -0.07382 100 LYS   A N   
768  C  CA  . LYS   A 100 ? 0.26650 0.15334 0.31818 -0.01989 0.03968  -0.08262 100 LYS   A CA  
769  C  C   . LYS   A 100 ? 0.26021 0.16844 0.30780 -0.02058 0.03092  -0.07293 100 LYS   A C   
770  O  O   . LYS   A 100 ? 0.23958 0.15947 0.28909 -0.01325 0.03116  -0.06640 100 LYS   A O   
771  C  CB  . LYS   A 100 ? 0.34745 0.23468 0.38144 -0.02161 0.04454  -0.09583 100 LYS   A CB  
772  C  CG  . LYS   A 100 ? 0.42815 0.32076 0.44306 -0.03378 0.03773  -0.10380 100 LYS   A CG  
773  C  CD  . LYS   A 100 ? 0.51856 0.41669 0.51388 -0.03486 0.04109  -0.11377 100 LYS   A CD  
774  C  CE  . LYS   A 100 ? 0.55745 0.46647 0.53472 -0.04633 0.03188  -0.11791 100 LYS   A CE  
775  N  NZ  . LYS   A 100 ? 0.56742 0.48749 0.52597 -0.04638 0.03351  -0.12282 100 LYS   A NZ  
776  N  N   . TYR   A 101 ? 0.22797 0.14258 0.27123 -0.02897 0.02303  -0.07021 101 TYR   A N   
777  C  CA  . TYR   A 101 ? 0.21289 0.14742 0.25323 -0.02828 0.01559  -0.05978 101 TYR   A CA  
778  C  C   . TYR   A 101 ? 0.20814 0.15279 0.23899 -0.03815 0.00885  -0.06234 101 TYR   A C   
779  O  O   . TYR   A 101 ? 0.21979 0.15654 0.24798 -0.04697 0.00825  -0.07049 101 TYR   A O   
780  C  CB  . TYR   A 101 ? 0.18607 0.12175 0.23910 -0.02403 0.01301  -0.04559 101 TYR   A CB  
781  C  CG  . TYR   A 101 ? 0.23607 0.16445 0.29527 -0.03076 0.01078  -0.04227 101 TYR   A CG  
782  C  CD1 . TYR   A 101 ? 0.22721 0.13620 0.29699 -0.03122 0.01539  -0.04379 101 TYR   A CD1 
783  C  CD2 . TYR   A 101 ? 0.22753 0.16850 0.28373 -0.03625 0.00486  -0.03667 101 TYR   A CD2 
784  C  CE1 . TYR   A 101 ? 0.28740 0.18928 0.36391 -0.03814 0.01361  -0.03960 101 TYR   A CE1 
785  C  CE2 . TYR   A 101 ? 0.22729 0.16302 0.29044 -0.04289 0.00360  -0.03265 101 TYR   A CE2 
786  C  CZ  . TYR   A 101 ? 0.25436 0.17057 0.32732 -0.04423 0.00768  -0.03385 101 TYR   A CZ  
787  O  OH  . TYR   A 101 ? 0.34518 0.25563 0.42604 -0.05157 0.00671  -0.02889 101 TYR   A OH  
788  N  N   . LYS   A 102 ? 0.17674 0.13926 0.20384 -0.03649 0.00376  -0.05491 102 LYS   A N   
789  C  CA  . LYS   A 102 ? 0.18207 0.15875 0.20490 -0.04322 -0.00296 -0.05277 102 LYS   A CA  
790  C  C   . LYS   A 102 ? 0.17369 0.16178 0.20170 -0.03839 -0.00571 -0.04047 102 LYS   A C   
791  O  O   . LYS   A 102 ? 0.14877 0.13724 0.17833 -0.03071 -0.00391 -0.03545 102 LYS   A O   
792  C  CB  . LYS   A 102 ? 0.23091 0.21893 0.24021 -0.04601 -0.00545 -0.05869 102 LYS   A CB  
793  C  CG  . LYS   A 102 ? 0.29013 0.26741 0.28939 -0.05024 -0.00169 -0.07220 102 LYS   A CG  
794  C  CD  . LYS   A 102 ? 0.40127 0.39172 0.38500 -0.05548 -0.00586 -0.07691 102 LYS   A CD  
795  C  CE  . LYS   A 102 ? 0.32318 0.32597 0.30318 -0.04761 -0.00539 -0.06994 102 LYS   A CE  
796  N  NZ  . LYS   A 102 ? 0.48012 0.49335 0.44302 -0.05229 -0.00790 -0.07477 102 LYS   A NZ  
797  N  N   . PHE   A 103 ? 0.15976 0.15748 0.19054 -0.04345 -0.00982 -0.03611 103 PHE   A N   
798  C  CA  . PHE   A 103 ? 0.12950 0.13931 0.16275 -0.03949 -0.01150 -0.02645 103 PHE   A CA  
799  C  C   . PHE   A 103 ? 0.12240 0.14810 0.15055 -0.04035 -0.01524 -0.02662 103 PHE   A C   
800  O  O   . PHE   A 103 ? 0.16120 0.19539 0.19080 -0.04737 -0.01900 -0.02795 103 PHE   A O   
801  C  CB  . PHE   A 103 ? 0.11986 0.13093 0.16155 -0.04346 -0.01179 -0.02015 103 PHE   A CB  
802  C  CG  . PHE   A 103 ? 0.14712 0.14467 0.19439 -0.04176 -0.00859 -0.01582 103 PHE   A CG  
803  C  CD1 . PHE   A 103 ? 0.13325 0.12045 0.17993 -0.03549 -0.00620 -0.01607 103 PHE   A CD1 
804  C  CD2 . PHE   A 103 ? 0.17602 0.17291 0.23064 -0.04655 -0.00808 -0.00997 103 PHE   A CD2 
805  C  CE1 . PHE   A 103 ? 0.16251 0.13889 0.21599 -0.03380 -0.00422 -0.01002 103 PHE   A CE1 
806  C  CE2 . PHE   A 103 ? 0.18347 0.16873 0.24318 -0.04525 -0.00557 -0.00387 103 PHE   A CE2 
807  C  CZ  . PHE   A 103 ? 0.15138 0.12647 0.21053 -0.03867 -0.00409 -0.00355 103 PHE   A CZ  
808  N  N   . VAL   A 104 ? 0.11405 0.14430 0.13773 -0.03365 -0.01468 -0.02425 104 VAL   A N   
809  C  CA  . VAL   A 104 ? 0.13216 0.17648 0.15216 -0.03314 -0.01786 -0.02243 104 VAL   A CA  
810  C  C   . VAL   A 104 ? 0.13615 0.18654 0.16026 -0.02700 -0.01700 -0.01435 104 VAL   A C   
811  O  O   . VAL   A 104 ? 0.20865 0.25159 0.23386 -0.02290 -0.01414 -0.01191 104 VAL   A O   
812  C  CB  . VAL   A 104 ? 0.15018 0.19372 0.16050 -0.03147 -0.01723 -0.02706 104 VAL   A CB  
813  C  CG1 . VAL   A 104 ? 0.21431 0.24752 0.21912 -0.03673 -0.01557 -0.03712 104 VAL   A CG1 
814  C  CG2 . VAL   A 104 ? 0.17145 0.20937 0.18202 -0.02390 -0.01357 -0.02430 104 VAL   A CG2 
815  N  N   . ARG   A 105 ? 0.10491 0.16887 0.13162 -0.02664 -0.01951 -0.01005 105 ARG   A N   
816  C  CA  . ARG   A 105 ? 0.08604 0.15396 0.11602 -0.02000 -0.01744 -0.00377 105 ARG   A CA  
817  C  C   . ARG   A 105 ? 0.08407 0.15578 0.10967 -0.01621 -0.01858 -0.00234 105 ARG   A C   
818  O  O   . ARG   A 105 ? 0.10692 0.18760 0.13037 -0.01919 -0.02241 -0.00232 105 ARG   A O   
819  C  CB  . ARG   A 105 ? 0.11113 0.19130 0.15113 -0.02069 -0.01764 0.00169  105 ARG   A CB  
820  C  CG  . ARG   A 105 ? 0.07546 0.15608 0.11845 -0.01344 -0.01319 0.00645  105 ARG   A CG  
821  C  CD  . ARG   A 105 ? 0.06143 0.15555 0.11668 -0.01333 -0.01176 0.01202  105 ARG   A CD  
822  N  NE  . ARG   A 105 ? 0.06006 0.15388 0.11807 -0.00548 -0.00611 0.01553  105 ARG   A NE  
823  C  CZ  . ARG   A 105 ? 0.06224 0.14942 0.11808 -0.00310 0.00019  0.01520  105 ARG   A CZ  
824  N  NH1 . ARG   A 105 ? 0.07491 0.15627 0.12666 -0.00758 0.00112  0.01343  105 ARG   A NH1 
825  N  NH2 . ARG   A 105 ? 0.07606 0.16141 0.13291 0.00381  0.00595  0.01665  105 ARG   A NH2 
826  N  N   . ILE   A 106 ? 0.10411 0.16892 0.12764 -0.01064 -0.01569 -0.00093 106 ILE   A N   
827  C  CA  . ILE   A 106 ? 0.12732 0.19426 0.14779 -0.00743 -0.01616 0.00134  106 ILE   A CA  
828  C  C   . ILE   A 106 ? 0.11974 0.19344 0.14682 -0.00287 -0.01566 0.00807  106 ILE   A C   
829  O  O   . ILE   A 106 ? 0.12194 0.19665 0.15513 -0.00105 -0.01338 0.00988  106 ILE   A O   
830  C  CB  . ILE   A 106 ? 0.10818 0.16432 0.12467 -0.00482 -0.01364 -0.00052 106 ILE   A CB  
831  C  CG1 . ILE   A 106 ? 0.09254 0.14125 0.11099 -0.00199 -0.01133 0.00050  106 ILE   A CG1 
832  C  CG2 . ILE   A 106 ? 0.21490 0.26564 0.22738 -0.00787 -0.01317 -0.00628 106 ILE   A CG2 
833  C  CD1 . ILE   A 106 ? 0.16623 0.20711 0.18237 -0.00005 -0.01046 0.00021  106 ILE   A CD1 
834  N  N   . GLN   A 107 ? 0.12898 0.20666 0.15532 -0.00063 -0.01681 0.01211  107 GLN   A N   
835  C  CA  . GLN   A 107 ? 0.12167 0.20371 0.15520 0.00479  -0.01595 0.01959  107 GLN   A CA  
836  C  C   . GLN   A 107 ? 0.12089 0.18980 0.15337 0.00908  -0.01179 0.01929  107 GLN   A C   
837  O  O   . GLN   A 107 ? 0.12135 0.18257 0.14735 0.00746  -0.01147 0.01584  107 GLN   A O   
838  C  CB  . GLN   A 107 ? 0.14501 0.23837 0.17726 0.00384  -0.02030 0.02542  107 GLN   A CB  
839  C  CG  . GLN   A 107 ? 0.13184 0.24024 0.16608 -0.00097 -0.02575 0.02687  107 GLN   A CG  
840  C  CD  . GLN   A 107 ? 0.13950 0.25769 0.18888 0.00284  -0.02561 0.03385  107 GLN   A CD  
841  O  OE1 . GLN   A 107 ? 0.10272 0.22042 0.16012 0.00981  -0.02293 0.04079  107 GLN   A OE1 
842  N  NE2 . GLN   A 107 ? 0.13060 0.25747 0.18573 -0.00150 -0.02773 0.03241  107 GLN   A NE2 
843  N  N   . PRO   A 108 ? 0.10999 0.17610 0.14961 0.01437  -0.00832 0.02275  108 PRO   A N   
844  C  CA  . PRO   A 108 ? 0.16285 0.21614 0.20146 0.01741  -0.00514 0.02269  108 PRO   A CA  
845  C  C   . PRO   A 108 ? 0.13389 0.18872 0.17049 0.01653  -0.00754 0.02700  108 PRO   A C   
846  O  O   . PRO   A 108 ? 0.16375 0.23037 0.20221 0.01643  -0.01062 0.03316  108 PRO   A O   
847  C  CB  . PRO   A 108 ? 0.16015 0.21237 0.20878 0.02384  -0.00067 0.02688  108 PRO   A CB  
848  C  CG  . PRO   A 108 ? 0.18487 0.25093 0.24087 0.02440  -0.00118 0.02939  108 PRO   A CG  
849  C  CD  . PRO   A 108 ? 0.12094 0.19477 0.17068 0.01751  -0.00629 0.02607  108 PRO   A CD  
850  N  N   . GLY   A 109 ? 0.08861 0.13280 0.12105 0.01515  -0.00640 0.02426  109 GLY   A N   
851  C  CA  . GLY   A 109 ? 0.17711 0.22286 0.20772 0.01370  -0.00743 0.02828  109 GLY   A CA  
852  C  C   . GLY   A 109 ? 0.17953 0.22897 0.20279 0.00922  -0.00881 0.02386  109 GLY   A C   
853  O  O   . GLY   A 109 ? 0.20175 0.25058 0.22342 0.00781  -0.00791 0.02567  109 GLY   A O   
854  N  N   . GLN   A 110 ? 0.11885 0.17175 0.13879 0.00710  -0.01011 0.01842  110 GLN   A N   
855  C  CA  . GLN   A 110 ? 0.15198 0.20559 0.16631 0.00367  -0.01008 0.01323  110 GLN   A CA  
856  C  C   . GLN   A 110 ? 0.11580 0.16001 0.13160 0.00320  -0.00882 0.00898  110 GLN   A C   
857  O  O   . GLN   A 110 ? 0.12951 0.16708 0.14742 0.00414  -0.00891 0.00821  110 GLN   A O   
858  C  CB  . GLN   A 110 ? 0.15203 0.21167 0.16282 0.00078  -0.01203 0.00911  110 GLN   A CB  
859  C  CG  . GLN   A 110 ? 0.17694 0.24881 0.18497 -0.00072 -0.01512 0.01304  110 GLN   A CG  
860  C  CD  . GLN   A 110 ? 0.31705 0.39413 0.32051 -0.00585 -0.01777 0.00741  110 GLN   A CD  
861  O  OE1 . GLN   A 110 ? 0.17202 0.25052 0.18045 -0.00696 -0.01932 0.00629  110 GLN   A OE1 
862  N  NE2 . GLN   A 110 ? 0.41551 0.49491 0.40900 -0.00957 -0.01763 0.00343  110 GLN   A NE2 
863  N  N   . THR   A 111 ? 0.13477 0.17914 0.14942 0.00177  -0.00745 0.00667  111 THR   A N   
864  C  CA  . THR   A 111 ? 0.11723 0.15572 0.13590 0.00142  -0.00707 0.00475  111 THR   A CA  
865  C  C   . THR   A 111 ? 0.14673 0.18393 0.16524 0.00065  -0.00680 -0.00003 111 THR   A C   
866  O  O   . THR   A 111 ? 0.13156 0.17143 0.14610 -0.00039 -0.00610 -0.00316 111 THR   A O   
867  C  CB  . THR   A 111 ? 0.12047 0.16081 0.14288 0.00120  -0.00477 0.00744  111 THR   A CB  
868  O  OG1 . THR   A 111 ? 0.15774 0.20434 0.17587 0.00102  -0.00147 0.00627  111 THR   A OG1 
869  C  CG2 . THR   A 111 ? 0.10625 0.14517 0.13056 0.00138  -0.00512 0.01289  111 THR   A CG2 
870  N  N   . PHE   A 112 ? 0.10726 0.13996 0.13045 0.00068  -0.00786 -0.00014 112 PHE   A N   
871  C  CA  . PHE   A 112 ? 0.13103 0.16124 0.15688 0.00069  -0.00741 -0.00273 112 PHE   A CA  
872  C  C   . PHE   A 112 ? 0.11224 0.14067 0.14550 0.00108  -0.00931 0.00018  112 PHE   A C   
873  O  O   . PHE   A 112 ? 0.12599 0.15419 0.15998 -0.00004 -0.01206 0.00292  112 PHE   A O   
874  C  CB  . PHE   A 112 ? 0.12698 0.15459 0.14926 -0.00053 -0.00901 -0.00428 112 PHE   A CB  
875  C  CG  . PHE   A 112 ? 0.15270 0.17806 0.17249 -0.00088 -0.01153 -0.00195 112 PHE   A CG  
876  C  CD1 . PHE   A 112 ? 0.14557 0.17257 0.16225 -0.00026 -0.01127 -0.00106 112 PHE   A CD1 
877  C  CD2 . PHE   A 112 ? 0.09304 0.11448 0.11312 -0.00168 -0.01358 -0.00050 112 PHE   A CD2 
878  C  CE1 . PHE   A 112 ? 0.14399 0.16723 0.15754 -0.00014 -0.01170 -0.00050 112 PHE   A CE1 
879  C  CE2 . PHE   A 112 ? 0.12339 0.14230 0.13785 -0.00255 -0.01491 0.00041  112 PHE   A CE2 
880  C  CZ  . PHE   A 112 ? 0.15504 0.17417 0.16597 -0.00164 -0.01325 -0.00051 112 PHE   A CZ  
881  N  N   . SER   A 113 ? 0.11877 0.14575 0.15822 0.00234  -0.00810 -0.00027 113 SER   A N   
882  C  CA  . SER   A 113 ? 0.11659 0.14407 0.16550 0.00300  -0.01081 0.00422  113 SER   A CA  
883  C  C   . SER   A 113 ? 0.11538 0.13872 0.16140 0.00168  -0.01506 0.00630  113 SER   A C   
884  O  O   . SER   A 113 ? 0.11993 0.13930 0.16200 0.00145  -0.01361 0.00402  113 SER   A O   
885  C  CB  . SER   A 113 ? 0.12246 0.15126 0.18307 0.00648  -0.00617 0.00428  113 SER   A CB  
886  O  OG  . SER   A 113 ? 0.14180 0.17459 0.20250 0.00759  -0.00047 0.00165  113 SER   A OG  
887  N  N   . VAL   A 114 ? 0.10239 0.12724 0.15002 -0.00002 -0.02049 0.01097  114 VAL   A N   
888  C  CA  . VAL   A 114 ? 0.12901 0.15126 0.17194 -0.00189 -0.02494 0.01430  114 VAL   A CA  
889  C  C   . VAL   A 114 ? 0.11499 0.14054 0.17028 -0.00061 -0.02840 0.02131  114 VAL   A C   
890  O  O   . VAL   A 114 ? 0.11266 0.14444 0.17690 -0.00087 -0.03122 0.02465  114 VAL   A O   
891  C  CB  . VAL   A 114 ? 0.09685 0.11798 0.12791 -0.00585 -0.02894 0.01362  114 VAL   A CB  
892  C  CG1 . VAL   A 114 ? 0.13591 0.15591 0.16037 -0.00847 -0.03386 0.01801  114 VAL   A CG1 
893  C  CG2 . VAL   A 114 ? 0.17395 0.19176 0.19545 -0.00574 -0.02482 0.00813  114 VAL   A CG2 
894  N  N   . LEU   A 115 ? 0.10929 0.13138 0.16698 0.00065  -0.02838 0.02471  115 LEU   A N   
895  C  CA  . LEU   A 115 ? 0.10432 0.12966 0.17403 0.00213  -0.03274 0.03387  115 LEU   A CA  
896  C  C   . LEU   A 115 ? 0.13287 0.15893 0.19083 -0.00244 -0.04001 0.03932  115 LEU   A C   
897  O  O   . LEU   A 115 ? 0.13939 0.16035 0.19025 -0.00325 -0.03903 0.04078  115 LEU   A O   
898  C  CB  . LEU   A 115 ? 0.13730 0.15695 0.21896 0.00687  -0.02743 0.03522  115 LEU   A CB  
899  C  CG  . LEU   A 115 ? 0.09959 0.12260 0.19739 0.00987  -0.03145 0.04665  115 LEU   A CG  
900  C  CD1 . LEU   A 115 ? 0.12269 0.15682 0.23693 0.01237  -0.03347 0.05097  115 LEU   A CD1 
901  C  CD2 . LEU   A 115 ? 0.12400 0.13745 0.23304 0.01456  -0.02519 0.04749  115 LEU   A CD2 
902  N  N   . ALA   A 116 ? 0.11464 0.14705 0.16928 -0.00632 -0.04711 0.04193  116 ALA   A N   
903  C  CA  . ALA   A 116 ? 0.11322 0.14639 0.15291 -0.01172 -0.05410 0.04587  116 ALA   A CA  
904  C  C   . ALA   A 116 ? 0.17863 0.21571 0.22745 -0.01045 -0.05914 0.05813  116 ALA   A C   
905  O  O   . ALA   A 116 ? 0.19031 0.23381 0.25791 -0.00741 -0.06128 0.06457  116 ALA   A O   
906  C  CB  . ALA   A 116 ? 0.15153 0.18940 0.18448 -0.01756 -0.06097 0.04423  116 ALA   A CB  
907  N  N   . CYS   A 117 ? 0.11961 0.15315 0.15548 -0.01271 -0.06007 0.06182  117 CYS   A N   
908  C  CA  . CYS   A 117 ? 0.14936 0.18480 0.19318 -0.01126 -0.06349 0.07441  117 CYS   A CA  
909  C  C   . CYS   A 117 ? 0.19116 0.22826 0.21412 -0.01773 -0.06801 0.07786  117 CYS   A C   
910  O  O   . CYS   A 117 ? 0.19995 0.23390 0.20195 -0.02195 -0.06712 0.07187  117 CYS   A O   
911  C  CB  . CYS   A 117 ? 0.19876 0.22498 0.25008 -0.00680 -0.05565 0.07510  117 CYS   A CB  
912  S  SG  . CYS   A 117 ? 0.22701 0.24846 0.30085 0.00065  -0.04720 0.06894  117 CYS   A SG  
913  N  N   . TYR   A 118 ? 0.18090 0.22297 0.21004 -0.01812 -0.07197 0.08762  118 TYR   A N   
914  C  CA  . TYR   A 118 ? 0.23191 0.27671 0.24332 -0.02375 -0.07628 0.09273  118 TYR   A CA  
915  C  C   . TYR   A 118 ? 0.26654 0.31218 0.29098 -0.02065 -0.07632 0.10532  118 TYR   A C   
916  O  O   . TYR   A 118 ? 0.21983 0.26879 0.26686 -0.01610 -0.07697 0.11101  118 TYR   A O   
917  C  CB  . TYR   A 118 ? 0.22602 0.27858 0.22961 -0.02957 -0.08387 0.09142  118 TYR   A CB  
918  C  CG  . TYR   A 118 ? 0.24747 0.29706 0.24025 -0.03251 -0.08300 0.07863  118 TYR   A CG  
919  C  CD1 . TYR   A 118 ? 0.21274 0.26398 0.22180 -0.02979 -0.08226 0.07451  118 TYR   A CD1 
920  C  CD2 . TYR   A 118 ? 0.24456 0.28885 0.21161 -0.03745 -0.08142 0.07047  118 TYR   A CD2 
921  C  CE1 . TYR   A 118 ? 0.23420 0.28184 0.23464 -0.03237 -0.08096 0.06345  118 TYR   A CE1 
922  C  CE2 . TYR   A 118 ? 0.26587 0.30561 0.22439 -0.03962 -0.07963 0.05860  118 TYR   A CE2 
923  C  CZ  . TYR   A 118 ? 0.28152 0.32288 0.25703 -0.03727 -0.07989 0.05553  118 TYR   A CZ  
924  O  OH  . TYR   A 118 ? 0.25037 0.28646 0.21823 -0.03959 -0.07793 0.04447  118 TYR   A OH  
925  N  N   . ASN   A 119 ? 0.28170 0.32400 0.29270 -0.02288 -0.07455 0.10960  119 ASN   A N   
926  C  CA  . ASN   A 119 ? 0.27066 0.31276 0.29252 -0.02061 -0.07434 0.12210  119 ASN   A CA  
927  C  C   . ASN   A 119 ? 0.29625 0.33139 0.34428 -0.01304 -0.06857 0.12404  119 ASN   A C   
928  O  O   . ASN   A 119 ? 0.26892 0.30537 0.33472 -0.00950 -0.06927 0.13356  119 ASN   A O   
929  C  CB  . ASN   A 119 ? 0.32218 0.37504 0.34726 -0.02288 -0.08273 0.13168  119 ASN   A CB  
930  C  CG  . ASN   A 119 ? 0.35559 0.41405 0.35390 -0.03091 -0.08844 0.12897  119 ASN   A CG  
931  O  OD1 . ASN   A 119 ? 0.44633 0.50245 0.42470 -0.03447 -0.08661 0.12984  119 ASN   A OD1 
932  N  ND2 . ASN   A 119 ? 0.37476 0.44009 0.37231 -0.03405 -0.09464 0.12517  119 ASN   A ND2 
933  N  N   . GLY   A 120 ? 0.22765 0.25498 0.27812 -0.01056 -0.06260 0.11470  120 GLY   A N   
934  C  CA  . GLY   A 120 ? 0.21653 0.23529 0.28946 -0.00382 -0.05614 0.11340  120 GLY   A CA  
935  C  C   . GLY   A 120 ? 0.26603 0.28932 0.35868 0.00126  -0.05643 0.11173  120 GLY   A C   
936  O  O   . GLY   A 120 ? 0.24178 0.25759 0.35294 0.00730  -0.04984 0.10971  120 GLY   A O   
937  N  N   . SER   A 121 ? 0.22576 0.26051 0.31476 -0.00146 -0.06297 0.11184  121 SER   A N   
938  C  CA  . SER   A 121 ? 0.21244 0.25345 0.32101 0.00261  -0.06290 0.11178  121 SER   A CA  
939  C  C   . SER   A 121 ? 0.24598 0.28958 0.34950 0.00137  -0.06266 0.10102  121 SER   A C   
940  O  O   . SER   A 121 ? 0.19598 0.24385 0.28105 -0.00503 -0.06812 0.09749  121 SER   A O   
941  C  CB  . SER   A 121 ? 0.28313 0.33609 0.39613 0.00006  -0.07072 0.12234  121 SER   A CB  
942  O  OG  . SER   A 121 ? 0.34314 0.39440 0.46940 0.00355  -0.06959 0.13318  121 SER   A OG  
943  N  N   . PRO   A 122 ? 0.20921 0.24968 0.32797 0.00719  -0.05578 0.09511  122 PRO   A N   
944  C  CA  . PRO   A 122 ? 0.13847 0.18185 0.25340 0.00615  -0.05494 0.08548  122 PRO   A CA  
945  C  C   . PRO   A 122 ? 0.20363 0.25872 0.31861 0.00178  -0.06152 0.08762  122 PRO   A C   
946  O  O   . PRO   A 122 ? 0.25330 0.31542 0.38371 0.00349  -0.06303 0.09520  122 PRO   A O   
947  C  CB  . PRO   A 122 ? 0.21019 0.24881 0.34385 0.01387  -0.04521 0.08072  122 PRO   A CB  
948  C  CG  . PRO   A 122 ? 0.26415 0.29194 0.40530 0.01806  -0.04006 0.08404  122 PRO   A CG  
949  C  CD  . PRO   A 122 ? 0.22236 0.25216 0.35623 0.01407  -0.04690 0.09441  122 PRO   A CD  
950  N  N   . SER   A 123 ? 0.21569 0.27219 0.31459 -0.00390 -0.06492 0.08062  123 SER   A N   
951  C  CA  . SER   A 123 ? 0.21882 0.28399 0.31593 -0.00937 -0.07107 0.08096  123 SER   A CA  
952  C  C   . SER   A 123 ? 0.15442 0.22207 0.26005 -0.00828 -0.06728 0.07441  123 SER   A C   
953  O  O   . SER   A 123 ? 0.16279 0.23890 0.28050 -0.00928 -0.06942 0.07813  123 SER   A O   
954  C  CB  . SER   A 123 ? 0.28530 0.34877 0.35670 -0.01773 -0.07751 0.07748  123 SER   A CB  
955  O  OG  . SER   A 123 ? 0.37789 0.44677 0.44607 -0.02368 -0.08270 0.07504  123 SER   A OG  
956  N  N   . GLY   A 124 ? 0.14338 0.20490 0.24374 -0.00656 -0.06182 0.06565  124 GLY   A N   
957  C  CA  . GLY   A 124 ? 0.13056 0.19469 0.23768 -0.00597 -0.05778 0.05991  124 GLY   A CA  
958  C  C   . GLY   A 124 ? 0.11852 0.17620 0.22155 -0.00282 -0.05120 0.05187  124 GLY   A C   
959  O  O   . GLY   A 124 ? 0.11698 0.16653 0.20738 -0.00266 -0.04993 0.04896  124 GLY   A O   
960  N  N   . VAL   A 125 ? 0.09364 0.15434 0.20554 -0.00082 -0.04556 0.04787  125 VAL   A N   
961  C  CA  . VAL   A 125 ? 0.09283 0.14561 0.19649 0.00166  -0.03633 0.03853  125 VAL   A CA  
962  C  C   . VAL   A 125 ? 0.11821 0.17265 0.21652 -0.00238 -0.03597 0.03424  125 VAL   A C   
963  O  O   . VAL   A 125 ? 0.11320 0.17670 0.22365 -0.00454 -0.03885 0.03849  125 VAL   A O   
964  C  CB  . VAL   A 125 ? 0.10439 0.15647 0.22188 0.00912  -0.02649 0.03727  125 VAL   A CB  
965  C  CG1 . VAL   A 125 ? 0.16458 0.22765 0.30112 0.01140  -0.02368 0.04098  125 VAL   A CG1 
966  C  CG2 . VAL   A 125 ? 0.13989 0.18303 0.24390 0.01007  -0.01855 0.02731  125 VAL   A CG2 
967  N  N   . TYR   A 126 ? 0.12392 0.17002 0.20553 -0.00371 -0.03288 0.02693  126 TYR   A N   
968  C  CA  . TYR   A 126 ? 0.10844 0.15384 0.18506 -0.00676 -0.03161 0.02349  126 TYR   A CA  
969  C  C   . TYR   A 126 ? 0.13454 0.17310 0.19914 -0.00467 -0.02519 0.01707  126 TYR   A C   
970  O  O   . TYR   A 126 ? 0.14899 0.18288 0.20654 -0.00264 -0.02326 0.01436  126 TYR   A O   
971  C  CB  . TYR   A 126 ? 0.14159 0.18468 0.20974 -0.01375 -0.03959 0.02350  126 TYR   A CB  
972  C  CG  . TYR   A 126 ? 0.14051 0.17569 0.19144 -0.01561 -0.04251 0.02049  126 TYR   A CG  
973  C  CD1 . TYR   A 126 ? 0.17982 0.20637 0.21701 -0.01508 -0.03820 0.01426  126 TYR   A CD1 
974  C  CD2 . TYR   A 126 ? 0.17170 0.20929 0.22092 -0.01760 -0.04913 0.02499  126 TYR   A CD2 
975  C  CE1 . TYR   A 126 ? 0.19064 0.21121 0.21331 -0.01637 -0.03926 0.01178  126 TYR   A CE1 
976  C  CE2 . TYR   A 126 ? 0.19226 0.22328 0.22428 -0.01949 -0.05058 0.02270  126 TYR   A CE2 
977  C  CZ  . TYR   A 126 ? 0.20628 0.22892 0.22553 -0.01878 -0.04504 0.01571  126 TYR   A CZ  
978  O  OH  . TYR   A 126 ? 0.23826 0.25559 0.24167 -0.02031 -0.04495 0.01366  126 TYR   A OH  
979  N  N   . GLN   A 127 ? 0.12113 0.16006 0.18465 -0.00575 -0.02246 0.01579  127 GLN   A N   
980  C  CA  . GLN   A 127 ? 0.15387 0.18904 0.20789 -0.00404 -0.01746 0.01183  127 GLN   A CA  
981  C  C   . GLN   A 127 ? 0.15824 0.18616 0.20138 -0.00663 -0.02008 0.00972  127 GLN   A C   
982  O  O   . GLN   A 127 ? 0.23482 0.26019 0.27833 -0.01058 -0.02393 0.01057  127 GLN   A O   
983  C  CB  . GLN   A 127 ? 0.19517 0.23580 0.25497 -0.00308 -0.01216 0.01345  127 GLN   A CB  
984  C  CG  . GLN   A 127 ? 0.23377 0.27356 0.28460 -0.00118 -0.00753 0.01086  127 GLN   A CG  
985  C  CD  . GLN   A 127 ? 0.16688 0.20800 0.21572 0.00178  -0.00323 0.00709  127 GLN   A CD  
986  O  OE1 . GLN   A 127 ? 0.18186 0.22187 0.23603 0.00322  -0.00354 0.00616  127 GLN   A OE1 
987  N  NE2 . GLN   A 127 ? 0.15853 0.20147 0.19941 0.00230  0.00054  0.00508  127 GLN   A NE2 
988  N  N   . CYS   A 128 ? 0.14754 0.17211 0.18185 -0.00457 -0.01768 0.00668  128 CYS   A N   
989  C  CA  . CYS   A 128 ? 0.24219 0.26026 0.26749 -0.00509 -0.01796 0.00443  128 CYS   A CA  
990  C  C   . CYS   A 128 ? 0.19606 0.21594 0.21980 -0.00223 -0.01390 0.00454  128 CYS   A C   
991  O  O   . CYS   A 128 ? 0.15908 0.18470 0.18436 -0.00073 -0.01174 0.00477  128 CYS   A O   
992  C  CB  . CYS   A 128 ? 0.13729 0.15255 0.15540 -0.00519 -0.01926 0.00238  128 CYS   A CB  
993  S  SG  . CYS   A 128 ? 0.36255 0.37348 0.37547 -0.00977 -0.02495 0.00233  128 CYS   A SG  
994  N  N   . ALA   A 129 ? 0.18774 0.20266 0.20852 -0.00158 -0.01286 0.00451  129 ALA   A N   
995  C  CA  . ALA   A 129 ? 0.17197 0.18984 0.19211 0.00162  -0.01011 0.00609  129 ALA   A CA  
996  C  C   . ALA   A 129 ? 0.18029 0.19471 0.19639 0.00323  -0.00899 0.00374  129 ALA   A C   
997  O  O   . ALA   A 129 ? 0.17946 0.18591 0.19146 0.00205  -0.00907 0.00082  129 ALA   A O   
998  C  CB  . ALA   A 129 ? 0.19491 0.21088 0.21877 0.00254  -0.00855 0.01037  129 ALA   A CB  
999  N  N   . MET   A 130 ? 0.14091 0.16211 0.15788 0.00542  -0.00779 0.00494  130 MET   A N   
1000 C  CA  . MET   A 130 ? 0.12088 0.14119 0.13737 0.00776  -0.00533 0.00424  130 MET   A CA  
1001 C  C   . MET   A 130 ? 0.13079 0.14696 0.15147 0.01143  -0.00250 0.00705  130 MET   A C   
1002 O  O   . MET   A 130 ? 0.15653 0.17832 0.18233 0.01317  -0.00295 0.01236  130 MET   A O   
1003 C  CB  . MET   A 130 ? 0.14564 0.17641 0.16442 0.00793  -0.00571 0.00542  130 MET   A CB  
1004 C  CG  . MET   A 130 ? 0.17627 0.21003 0.19848 0.01078  -0.00245 0.00647  130 MET   A CG  
1005 S  SD  . MET   A 130 ? 0.22188 0.24858 0.23720 0.00939  0.00036  0.00203  130 MET   A SD  
1006 C  CE  . MET   A 130 ? 0.09777 0.12773 0.11070 0.00436  -0.00355 0.00101  130 MET   A CE  
1007 N  N   . ARG   A 131 ? 0.13238 0.13786 0.15028 0.01242  0.00065  0.00363  131 ARG   A N   
1008 C  CA  . ARG   A 131 ? 0.13577 0.13356 0.15875 0.01620  0.00439  0.00555  131 ARG   A CA  
1009 C  C   . ARG   A 131 ? 0.13836 0.14448 0.17028 0.02224  0.00775  0.01060  131 ARG   A C   
1010 O  O   . ARG   A 131 ? 0.15293 0.16856 0.18529 0.02255  0.00788  0.01047  131 ARG   A O   
1011 C  CB  . ARG   A 131 ? 0.17639 0.15854 0.19224 0.01515  0.00776  -0.00156 131 ARG   A CB  
1012 C  CG  . ARG   A 131 ? 0.19327 0.16811 0.20096 0.00819  0.00317  -0.00610 131 ARG   A CG  
1013 C  CD  . ARG   A 131 ? 0.17920 0.15410 0.19346 0.00583  -0.00017 -0.00171 131 ARG   A CD  
1014 N  NE  . ARG   A 131 ? 0.17922 0.14744 0.20142 0.00961  0.00367  0.00213  131 ARG   A NE  
1015 C  CZ  . ARG   A 131 ? 0.17964 0.14884 0.20907 0.00861  0.00224  0.00832  131 ARG   A CZ  
1016 N  NH1 . ARG   A 131 ? 0.19678 0.17348 0.22653 0.00410  -0.00207 0.01031  131 ARG   A NH1 
1017 N  NH2 . ARG   A 131 ? 0.19880 0.16211 0.23646 0.01277  0.00594  0.01364  131 ARG   A NH2 
1018 N  N   . PRO   A 132 ? 0.14389 0.14741 0.18493 0.02696  0.01024  0.01627  132 PRO   A N   
1019 C  CA  . PRO   A 132 ? 0.14584 0.15785 0.19839 0.03366  0.01365  0.02224  132 PRO   A CA  
1020 C  C   . PRO   A 132 ? 0.18392 0.19332 0.23600 0.03654  0.02006  0.01689  132 PRO   A C   
1021 O  O   . PRO   A 132 ? 0.14797 0.17079 0.20938 0.04008  0.02149  0.02144  132 PRO   A O   
1022 C  CB  . PRO   A 132 ? 0.19021 0.19374 0.25226 0.03849  0.01645  0.02842  132 PRO   A CB  
1023 C  CG  . PRO   A 132 ? 0.18689 0.18727 0.24361 0.03298  0.01155  0.02970  132 PRO   A CG  
1024 C  CD  . PRO   A 132 ? 0.15442 0.14878 0.19814 0.02641  0.00976  0.01943  132 PRO   A CD  
1025 N  N   . ASN   A 133 ? 0.16170 0.15571 0.20278 0.03447  0.02386  0.00760  133 ASN   A N   
1026 C  CA  . ASN   A 133 ? 0.14561 0.13748 0.18362 0.03699  0.03125  0.00235  133 ASN   A CA  
1027 C  C   . ASN   A 133 ? 0.14729 0.14719 0.17558 0.03145  0.02822  -0.00066 133 ASN   A C   
1028 O  O   . ASN   A 133 ? 0.16376 0.16062 0.18522 0.03174  0.03416  -0.00556 133 ASN   A O   
1029 C  CB  . ASN   A 133 ? 0.20261 0.17321 0.23146 0.03753  0.03809  -0.00674 133 ASN   A CB  
1030 C  CG  . ASN   A 133 ? 0.16708 0.12732 0.17918 0.02869  0.03235  -0.01392 133 ASN   A CG  
1031 O  OD1 . ASN   A 133 ? 0.17797 0.14703 0.18663 0.02335  0.02442  -0.01181 133 ASN   A OD1 
1032 N  ND2 . ASN   A 133 ? 0.20905 0.15049 0.21125 0.02705  0.03659  -0.02264 133 ASN   A ND2 
1033 N  N   . PHE   A 134 ? 0.11902 0.12806 0.14631 0.02653  0.01996  0.00224  134 PHE   A N   
1034 C  CA  . PHE   A 134 ? 0.14080 0.15752 0.16244 0.02168  0.01677  0.00114  134 PHE   A CA  
1035 C  C   . PHE   A 134 ? 0.18265 0.18906 0.18909 0.01680  0.01608  -0.00524 134 PHE   A C   
1036 O  O   . PHE   A 134 ? 0.21150 0.22208 0.21288 0.01371  0.01551  -0.00565 134 PHE   A O   
1037 C  CB  . PHE   A 134 ? 0.12211 0.15035 0.15141 0.02423  0.02133  0.00392  134 PHE   A CB  
1038 C  CG  . PHE   A 134 ? 0.13985 0.18386 0.18390 0.02610  0.01832  0.01143  134 PHE   A CG  
1039 C  CD1 . PHE   A 134 ? 0.12557 0.17871 0.16960 0.02078  0.01103  0.01317  134 PHE   A CD1 
1040 C  CD2 . PHE   A 134 ? 0.14170 0.19163 0.19978 0.03302  0.02286  0.01674  134 PHE   A CD2 
1041 C  CE1 . PHE   A 134 ? 0.11490 0.18347 0.17013 0.02087  0.00716  0.01945  134 PHE   A CE1 
1042 C  CE2 . PHE   A 134 ? 0.16547 0.23279 0.23753 0.03398  0.01845  0.02512  134 PHE   A CE2 
1043 C  CZ  . PHE   A 134 ? 0.12803 0.20490 0.19728 0.02719  0.01012  0.02607  134 PHE   A CZ  
1044 N  N   . THR   A 135 ? 0.16233 0.15576 0.16164 0.01533  0.01552  -0.00947 135 THR   A N   
1045 C  CA  . THR   A 135 ? 0.17156 0.15809 0.15740 0.00916  0.01149  -0.01390 135 THR   A CA  
1046 C  C   . THR   A 135 ? 0.17869 0.16750 0.16795 0.00565  0.00374  -0.01130 135 THR   A C   
1047 O  O   . THR   A 135 ? 0.13141 0.12462 0.13048 0.00777  0.00260  -0.00732 135 THR   A O   
1048 C  CB  . THR   A 135 ? 0.18210 0.15305 0.15692 0.00805  0.01521  -0.02122 135 THR   A CB  
1049 O  OG1 . THR   A 135 ? 0.19629 0.15928 0.17776 0.00909  0.01465  -0.02124 135 THR   A OG1 
1050 C  CG2 . THR   A 135 ? 0.19158 0.15963 0.16393 0.01294  0.02546  -0.02443 135 THR   A CG2 
1051 N  N   . ILE   A 136 ? 0.15294 0.13971 0.13425 0.00033  -0.00132 -0.01286 136 ILE   A N   
1052 C  CA  . ILE   A 136 ? 0.17113 0.15971 0.15707 -0.00279 -0.00764 -0.01059 136 ILE   A CA  
1053 C  C   . ILE   A 136 ? 0.16227 0.14232 0.13960 -0.00835 -0.01151 -0.01430 136 ILE   A C   
1054 O  O   . ILE   A 136 ? 0.18137 0.15636 0.14594 -0.01106 -0.01118 -0.01822 136 ILE   A O   
1055 C  CB  . ILE   A 136 ? 0.19885 0.19709 0.18926 -0.00366 -0.01135 -0.00667 136 ILE   A CB  
1056 C  CG1 . ILE   A 136 ? 0.20473 0.20259 0.18675 -0.00717 -0.01431 -0.00665 136 ILE   A CG1 
1057 C  CG2 . ILE   A 136 ? 0.16346 0.16970 0.16092 0.00004  -0.00834 -0.00428 136 ILE   A CG2 
1058 C  CD1 . ILE   A 136 ? 0.18921 0.19357 0.17792 -0.00810 -0.01855 -0.00218 136 ILE   A CD1 
1059 N  N   . LYS   A 137 ? 0.20146 0.18030 0.18531 -0.01074 -0.01509 -0.01299 137 LYS   A N   
1060 C  CA  . LYS   A 137 ? 0.24002 0.21234 0.21828 -0.01756 -0.02031 -0.01596 137 LYS   A CA  
1061 C  C   . LYS   A 137 ? 0.18658 0.16928 0.16923 -0.02079 -0.02755 -0.01108 137 LYS   A C   
1062 O  O   . LYS   A 137 ? 0.22741 0.21627 0.22218 -0.02139 -0.03021 -0.00681 137 LYS   A O   
1063 C  CB  . LYS   A 137 ? 0.23049 0.19568 0.21590 -0.01882 -0.01962 -0.01640 137 LYS   A CB  
1064 C  CG  . LYS   A 137 ? 0.24580 0.20001 0.23023 -0.01411 -0.01175 -0.01968 137 LYS   A CG  
1065 C  CD  . LYS   A 137 ? 0.29743 0.24263 0.28961 -0.01616 -0.01144 -0.01907 137 LYS   A CD  
1066 C  CE  . LYS   A 137 ? 0.39675 0.32816 0.38884 -0.01127 -0.00337 -0.02232 137 LYS   A CE  
1067 N  NZ  . LYS   A 137 ? 0.45608 0.36974 0.43543 -0.01671 -0.00243 -0.03265 137 LYS   A NZ  
1068 N  N   . GLY   A 138 ? 0.19326 0.17862 0.16708 -0.02215 -0.02982 -0.01075 138 GLY   A N   
1069 C  CA  . GLY   A 138 ? 0.18961 0.18463 0.16922 -0.02375 -0.03602 -0.00467 138 GLY   A CA  
1070 C  C   . GLY   A 138 ? 0.21285 0.20812 0.18658 -0.03147 -0.04476 -0.00424 138 GLY   A C   
1071 O  O   . GLY   A 138 ? 0.21808 0.20535 0.18373 -0.03681 -0.04658 -0.00970 138 GLY   A O   
1072 N  N   . SER   A 139 ? 0.16994 0.17451 0.14843 -0.03234 -0.05060 0.00269  139 SER   A N   
1073 C  CA  . SER   A 139 ? 0.19066 0.19894 0.16320 -0.03986 -0.06060 0.00543  139 SER   A CA  
1074 C  C   . SER   A 139 ? 0.21276 0.22641 0.18067 -0.03845 -0.06262 0.01187  139 SER   A C   
1075 O  O   . SER   A 139 ? 0.17274 0.19400 0.15607 -0.03381 -0.06281 0.01941  139 SER   A O   
1076 C  CB  . SER   A 139 ? 0.21221 0.22997 0.20327 -0.04250 -0.06735 0.01109  139 SER   A CB  
1077 O  OG  . SER   A 139 ? 0.22418 0.24796 0.21272 -0.04730 -0.07484 0.01558  139 SER   A OG  
1078 N  N   . PHE   A 140 ? 0.22413 0.23272 0.17060 -0.04228 -0.06299 0.00875  140 PHE   A N   
1079 C  CA  . PHE   A 140 ? 0.24194 0.25362 0.18087 -0.04096 -0.06259 0.01465  140 PHE   A CA  
1080 C  C   . PHE   A 140 ? 0.30960 0.32005 0.22789 -0.04782 -0.06689 0.01346  140 PHE   A C   
1081 O  O   . PHE   A 140 ? 0.32761 0.32911 0.22999 -0.05161 -0.06430 0.00345  140 PHE   A O   
1082 C  CB  . PHE   A 140 ? 0.21779 0.22350 0.15254 -0.03516 -0.05104 0.01046  140 PHE   A CB  
1083 C  CG  . PHE   A 140 ? 0.19407 0.20189 0.14854 -0.02788 -0.04548 0.01210  140 PHE   A CG  
1084 C  CD1 . PHE   A 140 ? 0.21554 0.22980 0.18535 -0.02493 -0.04779 0.02043  140 PHE   A CD1 
1085 C  CD2 . PHE   A 140 ? 0.20327 0.20625 0.16046 -0.02414 -0.03786 0.00531  140 PHE   A CD2 
1086 C  CE1 . PHE   A 140 ? 0.18969 0.20430 0.17424 -0.01926 -0.04217 0.01991  140 PHE   A CE1 
1087 C  CE2 . PHE   A 140 ? 0.21033 0.21603 0.18261 -0.01864 -0.03347 0.00643  140 PHE   A CE2 
1088 C  CZ  . PHE   A 140 ? 0.19867 0.20962 0.18312 -0.01668 -0.03547 0.01276  140 PHE   A CZ  
1089 N  N   . LEU   A 141 ? 0.27504 0.29343 0.19515 -0.04846 -0.07168 0.02312  141 LEU   A N   
1090 C  CA  . LEU   A 141 ? 0.30695 0.32524 0.20749 -0.05393 -0.07429 0.02296  141 LEU   A CA  
1091 C  C   . LEU   A 141 ? 0.32481 0.34374 0.21549 -0.05186 -0.06997 0.02849  141 LEU   A C   
1092 O  O   . LEU   A 141 ? 0.32950 0.34868 0.22940 -0.04671 -0.06552 0.03250  141 LEU   A O   
1093 C  CB  . LEU   A 141 ? 0.30546 0.33325 0.21486 -0.05763 -0.08415 0.03058  141 LEU   A CB  
1094 C  CG  . LEU   A 141 ? 0.36510 0.39428 0.28764 -0.05991 -0.08828 0.02722  141 LEU   A CG  
1095 C  CD1 . LEU   A 141 ? 0.35424 0.39575 0.29211 -0.06152 -0.09692 0.03807  141 LEU   A CD1 
1096 C  CD2 . LEU   A 141 ? 0.35973 0.37966 0.26416 -0.06653 -0.08811 0.01485  141 LEU   A CD2 
1097 N  N   . ASN   A 142 ? 0.37737 0.39672 0.24901 -0.05638 -0.07124 0.02896  142 ASN   A N   
1098 C  CA  . ASN   A 142 ? 0.37482 0.39617 0.23827 -0.05496 -0.06740 0.03620  142 ASN   A CA  
1099 C  C   . ASN   A 142 ? 0.34442 0.37349 0.22980 -0.05093 -0.07127 0.05041  142 ASN   A C   
1100 O  O   . ASN   A 142 ? 0.33311 0.36906 0.23339 -0.05132 -0.07923 0.05713  142 ASN   A O   
1101 C  CB  . ASN   A 142 ? 0.42362 0.44629 0.26488 -0.06070 -0.06976 0.03642  142 ASN   A CB  
1102 C  CG  . ASN   A 142 ? 0.51583 0.52889 0.33392 -0.06388 -0.06360 0.02169  142 ASN   A CG  
1103 O  OD1 . ASN   A 142 ? 0.56717 0.57282 0.37995 -0.06049 -0.05312 0.01410  142 ASN   A OD1 
1104 N  ND2 . ASN   A 142 ? 0.59723 0.61031 0.40140 -0.07040 -0.06957 0.01772  142 ASN   A ND2 
1105 N  N   . GLY   A 143 ? 0.32460 0.35218 0.21291 -0.04703 -0.06481 0.05504  143 GLY   A N   
1106 C  CA  . GLY   A 143 ? 0.32768 0.35934 0.23718 -0.04270 -0.06658 0.06749  143 GLY   A CA  
1107 C  C   . GLY   A 143 ? 0.28235 0.31178 0.21238 -0.03723 -0.06423 0.06616  143 GLY   A C   
1108 O  O   . GLY   A 143 ? 0.26100 0.29131 0.20973 -0.03294 -0.06411 0.07498  143 GLY   A O   
1109 N  N   . SER   A 144 ? 0.23382 0.25957 0.16112 -0.03719 -0.06210 0.05520  144 SER   A N   
1110 C  CA  . SER   A 144 ? 0.22059 0.24431 0.16843 -0.03139 -0.05837 0.05177  144 SER   A CA  
1111 C  C   . SER   A 144 ? 0.19366 0.21193 0.14411 -0.02751 -0.04741 0.04760  144 SER   A C   
1112 O  O   . SER   A 144 ? 0.18515 0.20172 0.15282 -0.02281 -0.04366 0.04503  144 SER   A O   
1113 C  CB  . SER   A 144 ? 0.22503 0.24700 0.17296 -0.03224 -0.05892 0.04111  144 SER   A CB  
1114 O  OG  . SER   A 144 ? 0.25184 0.26735 0.18025 -0.03471 -0.05331 0.03084  144 SER   A OG  
1115 N  N   . CYS   A 145 ? 0.23064 0.24709 0.16431 -0.02985 -0.04211 0.04675  145 CYS   A N   
1116 C  CA  . CYS   A 145 ? 0.23780 0.25167 0.17631 -0.02703 -0.03235 0.04433  145 CYS   A CA  
1117 C  C   . CYS   A 145 ? 0.18447 0.19776 0.14357 -0.02399 -0.03233 0.05136  145 CYS   A C   
1118 O  O   . CYS   A 145 ? 0.21204 0.22665 0.17635 -0.02452 -0.03773 0.06210  145 CYS   A O   
1119 C  CB  . CYS   A 145 ? 0.32926 0.34377 0.24965 -0.03031 -0.02707 0.04689  145 CYS   A CB  
1120 S  SG  . CYS   A 145 ? 0.46982 0.48240 0.36192 -0.03423 -0.02463 0.03755  145 CYS   A SG  
1121 N  N   . GLY   A 146 ? 0.16685 0.17782 0.13766 -0.02102 -0.02627 0.04534  146 GLY   A N   
1122 C  CA  . GLY   A 146 ? 0.18190 0.18981 0.17101 -0.01880 -0.02535 0.04876  146 GLY   A CA  
1123 C  C   . GLY   A 146 ? 0.17171 0.17844 0.17505 -0.01504 -0.02784 0.04526  146 GLY   A C   
1124 O  O   . GLY   A 146 ? 0.16599 0.16849 0.18320 -0.01298 -0.02517 0.04448  146 GLY   A O   
1125 N  N   . SER   A 147 ? 0.14992 0.15995 0.15014 -0.01462 -0.03237 0.04291  147 SER   A N   
1126 C  CA  . SER   A 147 ? 0.14632 0.15678 0.15978 -0.01114 -0.03302 0.03904  147 SER   A CA  
1127 C  C   . SER   A 147 ? 0.16258 0.17107 0.17796 -0.00968 -0.02673 0.02955  147 SER   A C   
1128 O  O   . SER   A 147 ? 0.13522 0.14413 0.14098 -0.01122 -0.02347 0.02523  147 SER   A O   
1129 C  CB  . SER   A 147 ? 0.17280 0.18796 0.18205 -0.01243 -0.03866 0.03798  147 SER   A CB  
1130 O  OG  . SER   A 147 ? 0.16072 0.17982 0.16551 -0.01533 -0.04619 0.04680  147 SER   A OG  
1131 N  N   . VAL   A 148 ? 0.13797 0.14494 0.16593 -0.00661 -0.02468 0.02667  148 VAL   A N   
1132 C  CA  . VAL   A 148 ? 0.13776 0.14375 0.16623 -0.00621 -0.01971 0.01864  148 VAL   A CA  
1133 C  C   . VAL   A 148 ? 0.12000 0.12896 0.15100 -0.00408 -0.01912 0.01354  148 VAL   A C   
1134 O  O   . VAL   A 148 ? 0.11766 0.12867 0.15509 -0.00228 -0.02132 0.01592  148 VAL   A O   
1135 C  CB  . VAL   A 148 ? 0.13479 0.13491 0.17194 -0.00616 -0.01621 0.01766  148 VAL   A CB  
1136 C  CG1 . VAL   A 148 ? 0.14835 0.14562 0.18344 -0.00922 -0.01612 0.02362  148 VAL   A CG1 
1137 C  CG2 . VAL   A 148 ? 0.15909 0.15560 0.20874 -0.00251 -0.01560 0.01889  148 VAL   A CG2 
1138 N  N   . GLY   A 149 ? 0.10265 0.11325 0.12932 -0.00455 -0.01625 0.00770  149 GLY   A N   
1139 C  CA  . GLY   A 149 ? 0.11443 0.12791 0.14268 -0.00294 -0.01468 0.00341  149 GLY   A CA  
1140 C  C   . GLY   A 149 ? 0.10291 0.11509 0.13415 -0.00293 -0.01101 -0.00155 149 GLY   A C   
1141 O  O   . GLY   A 149 ? 0.09157 0.10162 0.12186 -0.00531 -0.01007 -0.00312 149 GLY   A O   
1142 N  N   . PHE   A 150 ? 0.09507 0.10884 0.12913 -0.00104 -0.00874 -0.00435 150 PHE   A N   
1143 C  CA  . PHE   A 150 ? 0.11406 0.12512 0.14874 -0.00146 -0.00471 -0.01031 150 PHE   A CA  
1144 C  C   . PHE   A 150 ? 0.11816 0.13363 0.15134 0.00014  -0.00162 -0.01322 150 PHE   A C   
1145 O  O   . PHE   A 150 ? 0.10914 0.12874 0.14538 0.00215  -0.00217 -0.00953 150 PHE   A O   
1146 C  CB  . PHE   A 150 ? 0.12195 0.12480 0.16576 0.00015  -0.00231 -0.01015 150 PHE   A CB  
1147 C  CG  . PHE   A 150 ? 0.13867 0.14268 0.19278 0.00464  -0.00163 -0.00566 150 PHE   A CG  
1148 C  CD1 . PHE   A 150 ? 0.15229 0.15898 0.21047 0.00526  -0.00681 0.00253  150 PHE   A CD1 
1149 C  CD2 . PHE   A 150 ? 0.14271 0.14666 0.20221 0.00783  0.00416  -0.00940 150 PHE   A CD2 
1150 C  CE1 . PHE   A 150 ? 0.16044 0.17102 0.23021 0.00863  -0.00760 0.00785  150 PHE   A CE1 
1151 C  CE2 . PHE   A 150 ? 0.18034 0.18796 0.25304 0.01230  0.00514  -0.00404 150 PHE   A CE2 
1152 C  CZ  . PHE   A 150 ? 0.14513 0.15674 0.22407 0.01251  -0.00146 0.00506  150 PHE   A CZ  
1153 N  N   . ASN   A 151 ? 0.11498 0.12964 0.14272 -0.00167 0.00162  -0.01986 151 ASN   A N   
1154 C  CA  . ASN   A 151 ? 0.14967 0.16721 0.17431 -0.00046 0.00647  -0.02365 151 ASN   A CA  
1155 C  C   . ASN   A 151 ? 0.14238 0.15128 0.16820 -0.00028 0.01242  -0.03130 151 ASN   A C   
1156 O  O   . ASN   A 151 ? 0.12794 0.12912 0.15437 -0.00280 0.01168  -0.03447 151 ASN   A O   
1157 C  CB  . ASN   A 151 ? 0.14684 0.17197 0.15972 -0.00365 0.00488  -0.02505 151 ASN   A CB  
1158 C  CG  . ASN   A 151 ? 0.16975 0.20170 0.18304 -0.00252 0.00125  -0.01777 151 ASN   A CG  
1159 O  OD1 . ASN   A 151 ? 0.18049 0.21563 0.19642 -0.00031 0.00313  -0.01445 151 ASN   A OD1 
1160 N  ND2 . ASN   A 151 ? 0.14588 0.17933 0.15808 -0.00397 -0.00327 -0.01514 151 ASN   A ND2 
1161 N  N   . ILE   A 152 ? 0.15124 0.16067 0.17743 0.00250  0.01932  -0.03474 152 ILE   A N   
1162 C  CA  . ILE   A 152 ? 0.17054 0.16992 0.19679 0.00317  0.02694  -0.04383 152 ILE   A CA  
1163 C  C   . ILE   A 152 ? 0.27051 0.27354 0.28110 0.00045  0.03175  -0.05160 152 ILE   A C   
1164 O  O   . ILE   A 152 ? 0.23866 0.25139 0.24683 0.00221  0.03373  -0.04790 152 ILE   A O   
1165 C  CB  . ILE   A 152 ? 0.19552 0.19077 0.23922 0.01037  0.03320  -0.04107 152 ILE   A CB  
1166 C  CG1 . ILE   A 152 ? 0.19324 0.18616 0.25055 0.01219  0.02699  -0.03199 152 ILE   A CG1 
1167 C  CG2 . ILE   A 152 ? 0.25552 0.23765 0.29979 0.01177  0.04266  -0.05158 152 ILE   A CG2 
1168 C  CD1 . ILE   A 152 ? 0.26623 0.25864 0.34378 0.01950  0.03105  -0.02603 152 ILE   A CD1 
1169 N  N   . ASP   A 153 ? 0.30185 0.29707 0.30124 -0.00465 0.03337  -0.06209 153 ASP   A N   
1170 C  CA  . ASP   A 153 ? 0.38619 0.38365 0.36666 -0.00898 0.03743  -0.07129 153 ASP   A CA  
1171 C  C   . ASP   A 153 ? 0.41588 0.39784 0.39542 -0.00811 0.04774  -0.08392 153 ASP   A C   
1172 O  O   . ASP   A 153 ? 0.42512 0.39429 0.40621 -0.01167 0.04658  -0.09016 153 ASP   A O   
1173 C  CB  . ASP   A 153 ? 0.41406 0.41712 0.38010 -0.01781 0.02835  -0.07306 153 ASP   A CB  
1174 C  CG  . ASP   A 153 ? 0.54747 0.56478 0.49773 -0.02053 0.02654  -0.07077 153 ASP   A CG  
1175 O  OD1 . ASP   A 153 ? 0.53485 0.55311 0.47653 -0.01883 0.03491  -0.07497 153 ASP   A OD1 
1176 O  OD2 . ASP   A 153 ? 0.57604 0.60399 0.52315 -0.02410 0.01729  -0.06403 153 ASP   A OD2 
1177 N  N   . TYR   A 154 ? 0.44902 0.43167 0.42646 -0.00352 0.05859  -0.08772 154 TYR   A N   
1178 C  CA  . TYR   A 154 ? 0.52223 0.48984 0.50517 0.00096  0.07136  -0.09789 154 TYR   A CA  
1179 C  C   . TYR   A 154 ? 0.51492 0.47106 0.52151 0.00616  0.07067  -0.09325 154 TYR   A C   
1180 O  O   . TYR   A 154 ? 0.52089 0.48325 0.54709 0.01343  0.07020  -0.08161 154 TYR   A O   
1181 C  CB  . TYR   A 154 ? 0.57395 0.53186 0.53637 -0.00621 0.07182  -0.10953 154 TYR   A CB  
1182 C  CG  . TYR   A 154 ? 0.67110 0.61698 0.63720 -0.00040 0.08352  -0.11561 154 TYR   A CG  
1183 C  CD1 . TYR   A 154 ? 0.66226 0.61440 0.63931 0.00876  0.09300  -0.11075 154 TYR   A CD1 
1184 C  CD2 . TYR   A 154 ? 0.65532 0.58443 0.61536 -0.00407 0.08517  -0.12575 154 TYR   A CD2 
1185 C  CE1 . TYR   A 154 ? 0.70887 0.65154 0.69073 0.01463  0.10398  -0.11586 154 TYR   A CE1 
1186 C  CE2 . TYR   A 154 ? 0.72195 0.63978 0.68570 0.00175  0.09658  -0.13182 154 TYR   A CE2 
1187 C  CZ  . TYR   A 154 ? 0.74049 0.66548 0.71520 0.01136  0.10608  -0.12683 154 TYR   A CZ  
1188 O  OH  . TYR   A 154 ? 0.72701 0.64197 0.70671 0.01757  0.11781  -0.13258 154 TYR   A OH  
1189 N  N   . ASP   A 155 ? 0.49329 0.43399 0.49834 0.00178  0.06903  -0.10003 155 ASP   A N   
1190 C  CA  . ASP   A 155 ? 0.47565 0.40413 0.50234 0.00652  0.06925  -0.09494 155 ASP   A CA  
1191 C  C   . ASP   A 155 ? 0.43523 0.36350 0.46556 0.00114  0.05773  -0.08872 155 ASP   A C   
1192 O  O   . ASP   A 155 ? 0.37407 0.29199 0.42076 0.00384  0.05711  -0.08358 155 ASP   A O   
1193 C  CB  . ASP   A 155 ? 0.52695 0.43814 0.55219 0.00632  0.07568  -0.10316 155 ASP   A CB  
1194 C  CG  . ASP   A 155 ? 0.55967 0.46331 0.56634 -0.00503 0.07029  -0.11296 155 ASP   A CG  
1195 O  OD1 . ASP   A 155 ? 0.58149 0.49562 0.56826 -0.01202 0.06577  -0.11714 155 ASP   A OD1 
1196 O  OD2 . ASP   A 155 ? 0.63547 0.52395 0.64829 -0.00716 0.06992  -0.11517 155 ASP   A OD2 
1197 N  N   . CYS   A 156 ? 0.31155 0.25259 0.32765 -0.00608 0.04816  -0.08663 156 CYS   A N   
1198 C  CA  . CYS   A 156 ? 0.31084 0.25292 0.32773 -0.01242 0.03785  -0.08160 156 CYS   A CA  
1199 C  C   . CYS   A 156 ? 0.23754 0.19524 0.26060 -0.00934 0.03009  -0.06711 156 CYS   A C   
1200 O  O   . CYS   A 156 ? 0.19799 0.16924 0.21401 -0.00827 0.02853  -0.06411 156 CYS   A O   
1201 C  CB  . CYS   A 156 ? 0.30727 0.25234 0.30504 -0.02332 0.03301  -0.09053 156 CYS   A CB  
1202 S  SG  . CYS   A 156 ? 0.29784 0.25071 0.29739 -0.03135 0.02047  -0.08301 156 CYS   A SG  
1203 N  N   . VAL   A 157 ? 0.19667 0.15157 0.23192 -0.00834 0.02563  -0.05829 157 VAL   A N   
1204 C  CA  . VAL   A 157 ? 0.14352 0.11083 0.18282 -0.00615 0.01874  -0.04598 157 VAL   A CA  
1205 C  C   . VAL   A 157 ? 0.17567 0.15032 0.20620 -0.01319 0.01147  -0.04484 157 VAL   A C   
1206 O  O   . VAL   A 157 ? 0.16680 0.13510 0.19932 -0.01816 0.00958  -0.04575 157 VAL   A O   
1207 C  CB  . VAL   A 157 ? 0.15365 0.11574 0.20870 -0.00158 0.01774  -0.03622 157 VAL   A CB  
1208 C  CG1 . VAL   A 157 ? 0.15219 0.12658 0.20760 -0.00035 0.01084  -0.02542 157 VAL   A CG1 
1209 C  CG2 . VAL   A 157 ? 0.17294 0.12798 0.24121 0.00605  0.02531  -0.03641 157 VAL   A CG2 
1210 N  N   . SER   A 158 ? 0.14192 0.13010 0.16500 -0.01338 0.00780  -0.04183 158 SER   A N   
1211 C  CA  . SER   A 158 ? 0.14294 0.14009 0.16128 -0.01826 0.00148  -0.03879 158 SER   A CA  
1212 C  C   . SER   A 158 ? 0.11541 0.11666 0.14001 -0.01471 -0.00155 -0.02871 158 SER   A C   
1213 O  O   . SER   A 158 ? 0.10735 0.11479 0.13130 -0.01076 -0.00219 -0.02450 158 SER   A O   
1214 C  CB  . SER   A 158 ? 0.16837 0.17715 0.17571 -0.02027 -0.00051 -0.04076 158 SER   A CB  
1215 O  OG  . SER   A 158 ? 0.19363 0.19919 0.19189 -0.02569 0.00108  -0.05063 158 SER   A OG  
1216 N  N   . PHE   A 159 ? 0.13440 0.13143 0.16441 -0.01665 -0.00304 -0.02496 159 PHE   A N   
1217 C  CA  . PHE   A 159 ? 0.11170 0.11245 0.14417 -0.01425 -0.00550 -0.01624 159 PHE   A CA  
1218 C  C   . PHE   A 159 ? 0.11985 0.13161 0.14720 -0.01599 -0.00818 -0.01441 159 PHE   A C   
1219 O  O   . PHE   A 159 ? 0.12878 0.14450 0.15544 -0.02073 -0.00930 -0.01671 159 PHE   A O   
1220 C  CB  . PHE   A 159 ? 0.13453 0.12781 0.17333 -0.01597 -0.00546 -0.01170 159 PHE   A CB  
1221 C  CG  . PHE   A 159 ? 0.13951 0.12176 0.18665 -0.01282 -0.00286 -0.01075 159 PHE   A CG  
1222 C  CD1 . PHE   A 159 ? 0.12454 0.10796 0.17585 -0.00747 -0.00384 -0.00427 159 PHE   A CD1 
1223 C  CD2 . PHE   A 159 ? 0.15161 0.12228 0.20363 -0.01530 0.00049  -0.01622 159 PHE   A CD2 
1224 C  CE1 . PHE   A 159 ? 0.14062 0.11592 0.20287 -0.00366 -0.00162 -0.00157 159 PHE   A CE1 
1225 C  CE2 . PHE   A 159 ? 0.15656 0.11602 0.21897 -0.01100 0.00402  -0.01469 159 PHE   A CE2 
1226 C  CZ  . PHE   A 159 ? 0.15236 0.11534 0.22087 -0.00461 0.00292  -0.00656 159 PHE   A CZ  
1227 N  N   . CYS   A 160 ? 0.10731 0.12391 0.13235 -0.01235 -0.00916 -0.01026 160 CYS   A N   
1228 C  CA  . CYS   A 160 ? 0.12491 0.15048 0.14704 -0.01239 -0.01032 -0.00833 160 CYS   A CA  
1229 C  C   . CYS   A 160 ? 0.11588 0.14193 0.13667 -0.01044 -0.01009 -0.00346 160 CYS   A C   
1230 O  O   . CYS   A 160 ? 0.13744 0.16992 0.15779 -0.01003 -0.00946 -0.00201 160 CYS   A O   
1231 C  CB  . CYS   A 160 ? 0.10370 0.13453 0.12247 -0.01029 -0.01069 -0.00974 160 CYS   A CB  
1232 S  SG  . CYS   A 160 ? 0.11648 0.14337 0.13508 -0.00597 -0.01000 -0.00807 160 CYS   A SG  
1233 N  N   . TYR   A 161 ? 0.07167 0.09167 0.09187 -0.00950 -0.01039 -0.00071 161 TYR   A N   
1234 C  CA  . TYR   A 161 ? 0.10184 0.12185 0.11666 -0.00844 -0.01034 0.00259  161 TYR   A CA  
1235 C  C   . TYR   A 161 ? 0.11824 0.13340 0.13219 -0.00979 -0.01135 0.00710  161 TYR   A C   
1236 O  O   . TYR   A 161 ? 0.13039 0.14137 0.14920 -0.00933 -0.01304 0.00851  161 TYR   A O   
1237 C  CB  . TYR   A 161 ? 0.12085 0.14026 0.13230 -0.00590 -0.01162 0.00173  161 TYR   A CB  
1238 C  CG  . TYR   A 161 ? 0.12290 0.14004 0.12627 -0.00586 -0.01170 0.00302  161 TYR   A CG  
1239 C  CD1 . TYR   A 161 ? 0.12970 0.14846 0.12926 -0.00466 -0.00822 0.00164  161 TYR   A CD1 
1240 C  CD2 . TYR   A 161 ? 0.11847 0.13208 0.11800 -0.00712 -0.01515 0.00540  161 TYR   A CD2 
1241 C  CE1 . TYR   A 161 ? 0.11708 0.13169 0.10712 -0.00482 -0.00696 0.00077  161 TYR   A CE1 
1242 C  CE2 . TYR   A 161 ? 0.13137 0.14231 0.11996 -0.00853 -0.01565 0.00512  161 TYR   A CE2 
1243 C  CZ  . TYR   A 161 ? 0.13408 0.14440 0.11698 -0.00737 -0.01084 0.00183  161 TYR   A CZ  
1244 O  OH  . TYR   A 161 ? 0.15177 0.15747 0.12210 -0.00880 -0.00977 -0.00043 161 TYR   A OH  
1245 N  N   . MET   A 162 ? 0.10872 0.12500 0.11719 -0.01119 -0.00971 0.01013  162 MET   A N   
1246 C  CA  . MET   A 162 ? 0.11757 0.13057 0.12137 -0.01265 -0.01121 0.01591  162 MET   A CA  
1247 C  C   . MET   A 162 ? 0.13226 0.14604 0.12322 -0.01260 -0.01071 0.01563  162 MET   A C   
1248 O  O   . MET   A 162 ? 0.10028 0.11687 0.08731 -0.01207 -0.00606 0.01316  162 MET   A O   
1249 C  CB  . MET   A 162 ? 0.13589 0.14852 0.14278 -0.01572 -0.00885 0.02062  162 MET   A CB  
1250 C  CG  . MET   A 162 ? 0.15401 0.16339 0.15634 -0.01710 -0.01122 0.02868  162 MET   A CG  
1251 S  SD  . MET   A 162 ? 0.20244 0.20902 0.21176 -0.02091 -0.00877 0.03638  162 MET   A SD  
1252 C  CE  . MET   A 162 ? 0.20497 0.20262 0.22895 -0.01916 -0.01191 0.03766  162 MET   A CE  
1253 N  N   . HIS   A 163 ? 0.12419 0.13561 0.10933 -0.01326 -0.01538 0.01784  163 HIS   A N   
1254 C  CA  . HIS   A 163 ? 0.11778 0.12806 0.08829 -0.01457 -0.01571 0.01572  163 HIS   A CA  
1255 C  C   . HIS   A 163 ? 0.13925 0.15000 0.09721 -0.01718 -0.01247 0.01905  163 HIS   A C   
1256 O  O   . HIS   A 163 ? 0.15670 0.16820 0.11478 -0.01926 -0.01450 0.02664  163 HIS   A O   
1257 C  CB  . HIS   A 163 ? 0.19095 0.20023 0.15917 -0.01623 -0.02324 0.01766  163 HIS   A CB  
1258 C  CG  . HIS   A 163 ? 0.17111 0.17762 0.12349 -0.01898 -0.02426 0.01329  163 HIS   A CG  
1259 N  ND1 . HIS   A 163 ? 0.17909 0.18203 0.12826 -0.01736 -0.01952 0.00546  163 HIS   A ND1 
1260 C  CD2 . HIS   A 163 ? 0.19485 0.20074 0.13269 -0.02365 -0.02912 0.01522  163 HIS   A CD2 
1261 C  CE1 . HIS   A 163 ? 0.18263 0.18086 0.11621 -0.02082 -0.02058 0.00141  163 HIS   A CE1 
1262 N  NE2 . HIS   A 163 ? 0.21257 0.21300 0.13768 -0.02527 -0.02680 0.00677  163 HIS   A NE2 
1263 N  N   . HIS   A 164 ? 0.18510 0.19494 0.13202 -0.01683 -0.00679 0.01375  164 HIS   A N   
1264 C  CA  . HIS   A 164 ? 0.18780 0.19839 0.12029 -0.01912 -0.00164 0.01573  164 HIS   A CA  
1265 C  C   . HIS   A 164 ? 0.22219 0.22785 0.13357 -0.02168 -0.00177 0.01072  164 HIS   A C   
1266 O  O   . HIS   A 164 ? 0.27243 0.27859 0.16806 -0.02578 -0.00254 0.01471  164 HIS   A O   
1267 C  CB  . HIS   A 164 ? 0.15873 0.17355 0.09688 -0.01638 0.00832  0.01399  164 HIS   A CB  
1268 C  CG  . HIS   A 164 ? 0.17049 0.19084 0.12407 -0.01697 0.00901  0.02018  164 HIS   A CG  
1269 N  ND1 . HIS   A 164 ? 0.18479 0.20551 0.15408 -0.01610 0.00446  0.02024  164 HIS   A ND1 
1270 C  CD2 . HIS   A 164 ? 0.14091 0.16593 0.09600 -0.01920 0.01401  0.02615  164 HIS   A CD2 
1271 C  CE1 . HIS   A 164 ? 0.13777 0.16196 0.11724 -0.01816 0.00619  0.02491  164 HIS   A CE1 
1272 N  NE2 . HIS   A 164 ? 0.18137 0.20854 0.15369 -0.02017 0.01174  0.02923  164 HIS   A NE2 
1273 N  N   . MET   A 165 ? 0.21095 0.21120 0.12022 -0.02004 -0.00083 0.00206  165 MET   A N   
1274 C  CA  . MET   A 165 ? 0.29145 0.28477 0.17884 -0.02309 0.00135  -0.00484 165 MET   A CA  
1275 C  C   . MET   A 165 ? 0.23101 0.21637 0.11889 -0.02300 -0.00139 -0.01301 165 MET   A C   
1276 O  O   . MET   A 165 ? 0.22244 0.20834 0.12771 -0.01914 -0.00220 -0.01342 165 MET   A O   
1277 C  CB  . MET   A 165 ? 0.29662 0.28923 0.17642 -0.02028 0.01433  -0.00886 165 MET   A CB  
1278 C  CG  . MET   A 165 ? 0.33211 0.32966 0.23352 -0.01368 0.02062  -0.00824 165 MET   A CG  
1279 S  SD  . MET   A 165 ? 0.44163 0.44059 0.33851 -0.00940 0.03661  -0.01198 165 MET   A SD  
1280 C  CE  . MET   A 165 ? 0.34701 0.33561 0.24783 -0.00389 0.04098  -0.02233 165 MET   A CE  
1281 N  N   . GLU   A 166 ? 0.25508 0.23257 0.12233 -0.02801 -0.00247 -0.01968 166 GLU   A N   
1282 C  CA  . GLU   A 166 ? 0.23587 0.20311 0.10160 -0.02915 -0.00381 -0.02860 166 GLU   A CA  
1283 C  C   . GLU   A 166 ? 0.27574 0.23221 0.12927 -0.02656 0.00861  -0.03905 166 GLU   A C   
1284 O  O   . GLU   A 166 ? 0.34181 0.29705 0.17629 -0.02843 0.01463  -0.04156 166 GLU   A O   
1285 C  CB  . GLU   A 166 ? 0.29595 0.26125 0.14912 -0.03820 -0.01576 -0.02927 166 GLU   A CB  
1286 C  CG  . GLU   A 166 ? 0.33722 0.28950 0.18458 -0.04165 -0.01642 -0.04005 166 GLU   A CG  
1287 C  CD  . GLU   A 166 ? 0.39716 0.35159 0.24209 -0.05054 -0.03042 -0.03838 166 GLU   A CD  
1288 O  OE1 . GLU   A 166 ? 0.35092 0.31642 0.21162 -0.05079 -0.03918 -0.02865 166 GLU   A OE1 
1289 O  OE2 . GLU   A 166 ? 0.40496 0.35231 0.23906 -0.05510 -0.03136 -0.04565 166 GLU   A OE2 
1290 N  N   . LEU   A 167 ? 0.28161 0.23059 0.14699 -0.02168 0.01337  -0.04432 167 LEU   A N   
1291 C  CA  . LEU   A 167 ? 0.31087 0.24774 0.16949 -0.01757 0.02607  -0.05419 167 LEU   A CA  
1292 C  C   . LEU   A 167 ? 0.35758 0.27783 0.19674 -0.02466 0.02391  -0.06568 167 LEU   A C   
1293 O  O   . LEU   A 167 ? 0.35940 0.27946 0.19512 -0.03247 0.01153  -0.06483 167 LEU   A O   
1294 C  CB  . LEU   A 167 ? 0.31356 0.25108 0.19698 -0.00852 0.03149  -0.05205 167 LEU   A CB  
1295 C  CG  . LEU   A 167 ? 0.26614 0.21960 0.16705 -0.00227 0.03480  -0.04254 167 LEU   A CG  
1296 C  CD1 . LEU   A 167 ? 0.24441 0.20071 0.16890 0.00443  0.03547  -0.03875 167 LEU   A CD1 
1297 C  CD2 . LEU   A 167 ? 0.31869 0.27334 0.21268 0.00162  0.04789  -0.04499 167 LEU   A CD2 
1298 N  N   . PRO   A 168 ? 0.36751 0.27482 0.19708 -0.02189 0.03545  -0.07601 168 PRO   A N   
1299 C  CA  . PRO   A 168 ? 0.37926 0.27531 0.19568 -0.02822 0.03153  -0.08489 168 PRO   A CA  
1300 C  C   . PRO   A 168 ? 0.41539 0.30192 0.24114 -0.03228 0.02347  -0.08751 168 PRO   A C   
1301 O  O   . PRO   A 168 ? 0.46891 0.35128 0.28488 -0.04056 0.01519  -0.09177 168 PRO   A O   
1302 C  CB  . PRO   A 168 ? 0.39578 0.28243 0.20856 -0.02136 0.04667  -0.09323 168 PRO   A CB  
1303 C  CG  . PRO   A 168 ? 0.42341 0.32232 0.24167 -0.01402 0.05621  -0.08678 168 PRO   A CG  
1304 C  CD  . PRO   A 168 ? 0.35428 0.26257 0.18902 -0.01231 0.05113  -0.07720 168 PRO   A CD  
1305 N  N   . THR   A 169 ? 0.36372 0.24726 0.20857 -0.02700 0.02568  -0.08459 169 THR   A N   
1306 C  CA  . THR   A 169 ? 0.37194 0.24750 0.22725 -0.03127 0.01811  -0.08529 169 THR   A CA  
1307 C  C   . THR   A 169 ? 0.37295 0.26231 0.23412 -0.03815 0.00303  -0.07626 169 THR   A C   
1308 O  O   . THR   A 169 ? 0.39659 0.28414 0.27141 -0.04088 -0.00326 -0.07386 169 THR   A O   
1309 C  CB  . THR   A 169 ? 0.40300 0.27378 0.28149 -0.02150 0.02578  -0.08209 169 THR   A CB  
1310 O  OG1 . THR   A 169 ? 0.39187 0.28199 0.28654 -0.01347 0.02683  -0.07038 169 THR   A OG1 
1311 C  CG2 . THR   A 169 ? 0.39022 0.24534 0.26741 -0.01482 0.03966  -0.09066 169 THR   A CG2 
1312 N  N   . GLY   A 170 ? 0.33576 0.24034 0.19050 -0.04002 -0.00234 -0.06963 170 GLY   A N   
1313 C  CA  . GLY   A 170 ? 0.33347 0.25275 0.19802 -0.04453 -0.01566 -0.05964 170 GLY   A CA  
1314 C  C   . GLY   A 170 ? 0.32729 0.25972 0.21731 -0.03663 -0.01574 -0.04868 170 GLY   A C   
1315 O  O   . GLY   A 170 ? 0.32812 0.27151 0.22898 -0.03928 -0.02515 -0.04096 170 GLY   A O   
1316 N  N   . VAL   A 171 ? 0.29826 0.23068 0.19821 -0.02728 -0.00563 -0.04774 171 VAL   A N   
1317 C  CA  . VAL   A 171 ? 0.24619 0.19154 0.16663 -0.02080 -0.00580 -0.03827 171 VAL   A CA  
1318 C  C   . VAL   A 171 ? 0.23398 0.19024 0.15195 -0.01815 -0.00367 -0.03340 171 VAL   A C   
1319 O  O   . VAL   A 171 ? 0.25100 0.20510 0.15237 -0.02031 -0.00071 -0.03655 171 VAL   A O   
1320 C  CB  . VAL   A 171 ? 0.24597 0.18730 0.18112 -0.01303 0.00197  -0.03812 171 VAL   A CB  
1321 C  CG1 . VAL   A 171 ? 0.25940 0.18838 0.19823 -0.01599 0.00033  -0.04176 171 VAL   A CG1 
1322 C  CG2 . VAL   A 171 ? 0.27207 0.20876 0.20265 -0.00690 0.01355  -0.04225 171 VAL   A CG2 
1323 N  N   . HIS   A 172 ? 0.18697 0.15455 0.12089 -0.01393 -0.00464 -0.02583 172 HIS   A N   
1324 C  CA  . HIS   A 172 ? 0.17923 0.15682 0.11303 -0.01366 -0.00546 -0.02004 172 HIS   A CA  
1325 C  C   . HIS   A 172 ? 0.19332 0.17760 0.13859 -0.00737 0.00141  -0.01718 172 HIS   A C   
1326 O  O   . HIS   A 172 ? 0.17319 0.15871 0.13089 -0.00308 0.00355  -0.01668 172 HIS   A O   
1327 C  CB  . HIS   A 172 ? 0.20462 0.18929 0.14601 -0.01665 -0.01488 -0.01373 172 HIS   A CB  
1328 C  CG  . HIS   A 172 ? 0.22134 0.20270 0.15330 -0.02352 -0.02280 -0.01499 172 HIS   A CG  
1329 N  ND1 . HIS   A 172 ? 0.20341 0.18323 0.14296 -0.02599 -0.02801 -0.01563 172 HIS   A ND1 
1330 C  CD2 . HIS   A 172 ? 0.23210 0.21194 0.14675 -0.02931 -0.02653 -0.01572 172 HIS   A CD2 
1331 C  CE1 . HIS   A 172 ? 0.25475 0.23312 0.18401 -0.03334 -0.03551 -0.01657 172 HIS   A CE1 
1332 N  NE2 . HIS   A 172 ? 0.23132 0.20958 0.14415 -0.03558 -0.03513 -0.01679 172 HIS   A NE2 
1333 N  N   . ALA   A 173 ? 0.19492 0.18434 0.13586 -0.00751 0.00452  -0.01452 173 ALA   A N   
1334 C  CA  . ALA   A 173 ? 0.16464 0.16230 0.11737 -0.00313 0.01011  -0.01119 173 ALA   A CA  
1335 C  C   . ALA   A 173 ? 0.17023 0.17563 0.12665 -0.00565 0.00693  -0.00474 173 ALA   A C   
1336 O  O   . ALA   A 173 ? 0.14169 0.14585 0.08815 -0.00976 0.00353  -0.00231 173 ALA   A O   
1337 C  CB  . ALA   A 173 ? 0.18545 0.18135 0.13281 0.00011  0.02064  -0.01463 173 ALA   A CB  
1338 N  N   . GLY   A 174 ? 0.11076 0.12388 0.08169 -0.00362 0.00765  -0.00156 174 GLY   A N   
1339 C  CA  . GLY   A 174 ? 0.12711 0.14519 0.10299 -0.00641 0.00532  0.00368  174 GLY   A CA  
1340 C  C   . GLY   A 174 ? 0.14568 0.17230 0.13571 -0.00514 0.00760  0.00538  174 GLY   A C   
1341 O  O   . GLY   A 174 ? 0.11844 0.14929 0.11421 -0.00161 0.01149  0.00398  174 GLY   A O   
1342 N  N   . THR   A 175 ? 0.09468 0.12361 0.09118 -0.00831 0.00462  0.00868  175 THR   A N   
1343 C  CA  . THR   A 175 ? 0.11333 0.15049 0.12197 -0.00958 0.00576  0.01023  175 THR   A CA  
1344 C  C   . THR   A 175 ? 0.08551 0.12168 0.10066 -0.01110 0.00030  0.00842  175 THR   A C   
1345 O  O   . THR   A 175 ? 0.11272 0.14201 0.12458 -0.01078 -0.00322 0.00717  175 THR   A O   
1346 C  CB  . THR   A 175 ? 0.11375 0.15329 0.12403 -0.01362 0.00851  0.01517  175 THR   A CB  
1347 O  OG1 . THR   A 175 ? 0.11170 0.14370 0.12023 -0.01662 0.00423  0.01750  175 THR   A OG1 
1348 C  CG2 . THR   A 175 ? 0.13031 0.17084 0.13129 -0.01241 0.01523  0.01685  175 THR   A CG2 
1349 N  N   . ASP   A 176 ? 0.10625 0.15007 0.13072 -0.01305 -0.00023 0.00820  176 ASP   A N   
1350 C  CA  . ASP   A 176 ? 0.10265 0.14412 0.13107 -0.01654 -0.00428 0.00569  176 ASP   A CA  
1351 C  C   . ASP   A 176 ? 0.09191 0.12721 0.12239 -0.02089 -0.00396 0.00811  176 ASP   A C   
1352 O  O   . ASP   A 176 ? 0.09725 0.13182 0.12535 -0.02129 -0.00113 0.01279  176 ASP   A O   
1353 C  CB  . ASP   A 176 ? 0.11469 0.16658 0.15009 -0.01864 -0.00621 0.00426  176 ASP   A CB  
1354 C  CG  . ASP   A 176 ? 0.10060 0.16295 0.14504 -0.02205 -0.00443 0.00803  176 ASP   A CG  
1355 O  OD1 . ASP   A 176 ? 0.08743 0.14741 0.13366 -0.02498 -0.00178 0.01102  176 ASP   A OD1 
1356 O  OD2 . ASP   A 176 ? 0.11160 0.18610 0.16268 -0.02211 -0.00609 0.00896  176 ASP   A OD2 
1357 N  N   . LEU   A 177 ? 0.11586 0.14558 0.15013 -0.02418 -0.00630 0.00502  177 LEU   A N   
1358 C  CA  . LEU   A 177 ? 0.11561 0.13659 0.15352 -0.02768 -0.00568 0.00787  177 LEU   A CA  
1359 C  C   . LEU   A 177 ? 0.15867 0.18437 0.20432 -0.03415 -0.00445 0.01020  177 LEU   A C   
1360 O  O   . LEU   A 177 ? 0.17616 0.19404 0.22639 -0.03800 -0.00359 0.01339  177 LEU   A O   
1361 C  CB  . LEU   A 177 ? 0.12424 0.13433 0.16429 -0.02785 -0.00709 0.00304  177 LEU   A CB  
1362 C  CG  . LEU   A 177 ? 0.12422 0.12697 0.16199 -0.02239 -0.00750 0.00505  177 LEU   A CG  
1363 C  CD1 . LEU   A 177 ? 0.13638 0.13402 0.17558 -0.02250 -0.00720 0.01378  177 LEU   A CD1 
1364 C  CD2 . LEU   A 177 ? 0.16306 0.17212 0.19376 -0.01766 -0.00862 0.00457  177 LEU   A CD2 
1365 N  N   . GLU   A 178 ? 0.12352 0.16232 0.17265 -0.03550 -0.00441 0.00976  178 GLU   A N   
1366 C  CA  . GLU   A 178 ? 0.13459 0.18198 0.19289 -0.04105 -0.00249 0.01428  178 GLU   A CA  
1367 C  C   . GLU   A 178 ? 0.12029 0.17348 0.17637 -0.03768 0.00316  0.02113  178 GLU   A C   
1368 O  O   . GLU   A 178 ? 0.11703 0.17887 0.18134 -0.04156 0.00649  0.02619  178 GLU   A O   
1369 C  CB  . GLU   A 178 ? 0.14631 0.20786 0.21242 -0.04456 -0.00556 0.01189  178 GLU   A CB  
1370 C  CG  . GLU   A 178 ? 0.20950 0.26732 0.27242 -0.04705 -0.01102 0.00388  178 GLU   A CG  
1371 C  CD  . GLU   A 178 ? 0.25236 0.29929 0.31826 -0.05549 -0.01294 -0.00066 178 GLU   A CD  
1372 O  OE1 . GLU   A 178 ? 0.24125 0.28211 0.31323 -0.05941 -0.01036 0.00356  178 GLU   A OE1 
1373 O  OE2 . GLU   A 178 ? 0.25322 0.29630 0.31436 -0.05821 -0.01652 -0.00882 178 GLU   A OE2 
1374 N  N   . GLY   A 179 ? 0.11829 0.16738 0.16332 -0.03116 0.00466  0.02099  179 GLY   A N   
1375 C  CA  . GLY   A 179 ? 0.11267 0.16472 0.15127 -0.02839 0.01055  0.02564  179 GLY   A CA  
1376 C  C   . GLY   A 179 ? 0.09716 0.16033 0.13751 -0.02373 0.01483  0.02462  179 GLY   A C   
1377 O  O   . GLY   A 179 ? 0.11476 0.18148 0.15101 -0.02170 0.02181  0.02762  179 GLY   A O   
1378 N  N   . ASN   A 180 ? 0.08435 0.15276 0.13033 -0.02160 0.01149  0.02082  180 ASN   A N   
1379 C  CA  . ASN   A 180 ? 0.10833 0.18711 0.15926 -0.01619 0.01553  0.02126  180 ASN   A CA  
1380 C  C   . ASN   A 180 ? 0.09867 0.16891 0.13852 -0.00973 0.01583  0.01712  180 ASN   A C   
1381 O  O   . ASN   A 180 ? 0.08456 0.14911 0.12107 -0.00940 0.01007  0.01373  180 ASN   A O   
1382 C  CB  . ASN   A 180 ? 0.08786 0.17951 0.15302 -0.01822 0.01095  0.02187  180 ASN   A CB  
1383 C  CG  . ASN   A 180 ? 0.08657 0.18674 0.16354 -0.02618 0.00994  0.02544  180 ASN   A CG  
1384 O  OD1 . ASN   A 180 ? 0.10194 0.21012 0.18610 -0.02694 0.01631  0.03067  180 ASN   A OD1 
1385 N  ND2 . ASN   A 180 ? 0.13624 0.23412 0.21507 -0.03284 0.00256  0.02227  180 ASN   A ND2 
1386 N  N   . PHE   A 181 ? 0.10056 0.16964 0.13481 -0.00500 0.02317  0.01700  181 PHE   A N   
1387 C  CA  . PHE   A 181 ? 0.09253 0.15110 0.11541 -0.00037 0.02342  0.01230  181 PHE   A CA  
1388 C  C   . PHE   A 181 ? 0.10527 0.16644 0.13579 0.00346  0.02005  0.01108  181 PHE   A C   
1389 O  O   . PHE   A 181 ? 0.08032 0.15356 0.12474 0.00519  0.02058  0.01442  181 PHE   A O   
1390 C  CB  . PHE   A 181 ? 0.11938 0.17526 0.13457 0.00371  0.03308  0.01080  181 PHE   A CB  
1391 C  CG  . PHE   A 181 ? 0.13468 0.18020 0.13097 0.00074  0.03388  0.00900  181 PHE   A CG  
1392 C  CD1 . PHE   A 181 ? 0.14898 0.18242 0.13197 0.00075  0.02964  0.00417  181 PHE   A CD1 
1393 C  CD2 . PHE   A 181 ? 0.12205 0.17099 0.11420 -0.00291 0.03800  0.01324  181 PHE   A CD2 
1394 C  CE1 . PHE   A 181 ? 0.15002 0.17605 0.11538 -0.00293 0.02870  0.00351  181 PHE   A CE1 
1395 C  CE2 . PHE   A 181 ? 0.17142 0.21222 0.14453 -0.00617 0.03787  0.01321  181 PHE   A CE2 
1396 C  CZ  . PHE   A 181 ? 0.17098 0.20072 0.13047 -0.00626 0.03253  0.00824  181 PHE   A CZ  
1397 N  N   . TYR   A 182 ? 0.08591 0.13668 0.10775 0.00452  0.01641  0.00740  182 TYR   A N   
1398 C  CA  . TYR   A 182 ? 0.07941 0.12999 0.10573 0.00888  0.01517  0.00685  182 TYR   A CA  
1399 C  C   . TYR   A 182 ? 0.11182 0.15715 0.13630 0.01472  0.02305  0.00507  182 TYR   A C   
1400 O  O   . TYR   A 182 ? 0.11855 0.15225 0.12949 0.01418  0.02569  0.00048  182 TYR   A O   
1401 C  CB  . TYR   A 182 ? 0.07664 0.11824 0.09551 0.00711  0.00914  0.00406  182 TYR   A CB  
1402 C  CG  . TYR   A 182 ? 0.06940 0.11529 0.09145 0.00302  0.00292  0.00479  182 TYR   A CG  
1403 C  CD1 . TYR   A 182 ? 0.06802 0.12225 0.09747 0.00351  -0.00008 0.00670  182 TYR   A CD1 
1404 C  CD2 . TYR   A 182 ? 0.07451 0.11494 0.09126 -0.00109 0.00008  0.00346  182 TYR   A CD2 
1405 C  CE1 . TYR   A 182 ? 0.06088 0.11787 0.09050 -0.00077 -0.00499 0.00558  182 TYR   A CE1 
1406 C  CE2 . TYR   A 182 ? 0.09194 0.13387 0.11167 -0.00425 -0.00413 0.00265  182 TYR   A CE2 
1407 C  CZ  . TYR   A 182 ? 0.10684 0.15628 0.13151 -0.00436 -0.00628 0.00270  182 TYR   A CZ  
1408 O  OH  . TYR   A 182 ? 0.09184 0.14108 0.11642 -0.00806 -0.00940 0.00014  182 TYR   A OH  
1409 N  N   . GLY   A 183 ? 0.08868 0.14266 0.12682 0.02005  0.02698  0.00871  183 GLY   A N   
1410 C  CA  . GLY   A 183 ? 0.10849 0.15607 0.14749 0.02689  0.03600  0.00676  183 GLY   A CA  
1411 C  C   . GLY   A 183 ? 0.11024 0.15980 0.14739 0.02840  0.04606  0.00559  183 GLY   A C   
1412 O  O   . GLY   A 183 ? 0.10801 0.16471 0.14355 0.02363  0.04578  0.00749  183 GLY   A O   
1413 N  N   . PRO   A 184 ? 0.13664 0.17861 0.17353 0.03506  0.05611  0.00224  184 PRO   A N   
1414 C  CA  . PRO   A 184 ? 0.15931 0.20502 0.19702 0.03837  0.06862  0.00145  184 PRO   A CA  
1415 C  C   . PRO   A 184 ? 0.19883 0.23206 0.21152 0.03362  0.07243  -0.00605 184 PRO   A C   
1416 O  O   . PRO   A 184 ? 0.23709 0.25883 0.23905 0.03715  0.08277  -0.01307 184 PRO   A O   
1417 C  CB  . PRO   A 184 ? 0.18002 0.22064 0.22886 0.04850  0.07813  0.00042  184 PRO   A CB  
1418 C  CG  . PRO   A 184 ? 0.17720 0.20003 0.21598 0.04745  0.07168  -0.00464 184 PRO   A CG  
1419 C  CD  . PRO   A 184 ? 0.17533 0.20400 0.21213 0.03997  0.05732  -0.00098 184 PRO   A CD  
1420 N  N   . PHE   A 185 ? 0.15107 0.18596 0.15374 0.02543  0.06405  -0.00456 185 PHE   A N   
1421 C  CA  . PHE   A 185 ? 0.17296 0.19809 0.15164 0.01980  0.06464  -0.00922 185 PHE   A CA  
1422 C  C   . PHE   A 185 ? 0.23359 0.27011 0.21241 0.01509  0.06563  -0.00290 185 PHE   A C   
1423 O  O   . PHE   A 185 ? 0.20988 0.25963 0.20633 0.01393  0.06206  0.00413  185 PHE   A O   
1424 C  CB  . PHE   A 185 ? 0.19881 0.21331 0.16566 0.01445  0.05273  -0.01207 185 PHE   A CB  
1425 C  CG  . PHE   A 185 ? 0.17460 0.17912 0.14435 0.01798  0.05101  -0.01660 185 PHE   A CG  
1426 C  CD1 . PHE   A 185 ? 0.20010 0.19116 0.16012 0.02119  0.05930  -0.02464 185 PHE   A CD1 
1427 C  CD2 . PHE   A 185 ? 0.16121 0.16935 0.14389 0.01824  0.04237  -0.01281 185 PHE   A CD2 
1428 C  CE1 . PHE   A 185 ? 0.22068 0.20097 0.18526 0.02424  0.05826  -0.02814 185 PHE   A CE1 
1429 C  CE2 . PHE   A 185 ? 0.18502 0.18426 0.17128 0.02139  0.04148  -0.01543 185 PHE   A CE2 
1430 C  CZ  . PHE   A 185 ? 0.19157 0.17656 0.16987 0.02431  0.04912  -0.02264 185 PHE   A CZ  
1431 N  N   . VAL   A 186 ? 0.19671 0.22769 0.15488 0.01159  0.07038  -0.00529 186 VAL   A N   
1432 C  CA  . VAL   A 186 ? 0.23654 0.27720 0.19308 0.00723  0.07357  0.00157  186 VAL   A CA  
1433 C  C   . VAL   A 186 ? 0.28323 0.31550 0.21562 0.00011  0.06793  0.00144  186 VAL   A C   
1434 O  O   . VAL   A 186 ? 0.26593 0.28579 0.17908 -0.00096 0.06606  -0.00581 186 VAL   A O   
1435 C  CB  . VAL   A 186 ? 0.26128 0.30920 0.22021 0.01175  0.08989  0.00166  186 VAL   A CB  
1436 C  CG1 . VAL   A 186 ? 0.25753 0.31858 0.24601 0.01844  0.09374  0.00541  186 VAL   A CG1 
1437 C  CG2 . VAL   A 186 ? 0.27407 0.30784 0.21094 0.01487  0.09948  -0.00898 186 VAL   A CG2 
1438 N  N   . ASP   A 187 ? 0.25826 0.29755 0.19260 -0.00528 0.06464  0.01024  187 ASP   A N   
1439 C  CA  . ASP   A 187 ? 0.26070 0.29417 0.17451 -0.01178 0.05871  0.01321  187 ASP   A CA  
1440 C  C   . ASP   A 187 ? 0.30354 0.33827 0.19712 -0.01366 0.06976  0.01395  187 ASP   A C   
1441 O  O   . ASP   A 187 ? 0.31295 0.35354 0.20274 -0.01826 0.07106  0.02310  187 ASP   A O   
1442 C  CB  . ASP   A 187 ? 0.24092 0.27830 0.16665 -0.01633 0.04918  0.02275  187 ASP   A CB  
1443 C  CG  . ASP   A 187 ? 0.20392 0.25297 0.14884 -0.01722 0.05430  0.03017  187 ASP   A CG  
1444 O  OD1 . ASP   A 187 ? 0.19119 0.24853 0.14441 -0.01374 0.06471  0.02912  187 ASP   A OD1 
1445 O  OD2 . ASP   A 187 ? 0.19511 0.24485 0.14860 -0.02164 0.04757  0.03739  187 ASP   A OD2 
1446 N  N   . ARG   A 188 ? 0.32116 0.34948 0.20167 -0.00987 0.07884  0.00386  188 ARG   A N   
1447 C  CA  . ARG   A 188 ? 0.37455 0.39999 0.22823 -0.01192 0.08935  0.00059  188 ARG   A CA  
1448 C  C   . ARG   A 188 ? 0.45067 0.46178 0.28797 -0.01010 0.08775  -0.01275 188 ARG   A C   
1449 O  O   . ARG   A 188 ? 0.41623 0.41984 0.26240 -0.00697 0.08547  -0.01925 188 ARG   A O   
1450 C  CB  . ARG   A 188 ? 0.42307 0.46011 0.28841 -0.00637 0.10421  0.00200  188 ARG   A CB  
1451 C  CG  . ARG   A 188 ? 0.42703 0.47021 0.32141 0.00105  0.11019  0.00065  188 ARG   A CG  
1452 C  CD  . ARG   A 188 ? 0.40809 0.46823 0.32101 0.00291  0.12038  0.00651  188 ARG   A CD  
1453 N  NE  . ARG   A 188 ? 0.47584 0.54302 0.41836 0.01025  0.12322  0.00623  188 ARG   A NE  
1454 C  CZ  . ARG   A 188 ? 0.45130 0.51617 0.39974 0.01804  0.13078  -0.00144 188 ARG   A CZ  
1455 N  NH1 . ARG   A 188 ? 0.52407 0.57883 0.45093 0.01957  0.13705  -0.01087 188 ARG   A NH1 
1456 N  NH2 . ARG   A 188 ? 0.46834 0.54098 0.44516 0.02442  0.13113  0.00090  188 ARG   A NH2 
1457 N  N   . GLN   A 189 ? 0.50048 0.50768 0.31496 -0.01211 0.08882  -0.01659 189 GLN   A N   
1458 C  CA  . GLN   A 189 ? 0.54708 0.53995 0.34557 -0.01254 0.08564  -0.02940 189 GLN   A CA  
1459 C  C   . GLN   A 189 ? 0.52443 0.51470 0.32846 -0.00462 0.10016  -0.03886 189 GLN   A C   
1460 O  O   . GLN   A 189 ? 0.56660 0.56210 0.36257 -0.00284 0.11008  -0.03953 189 GLN   A O   
1461 C  CB  . GLN   A 189 ? 0.61912 0.60892 0.39087 -0.01964 0.07771  -0.02894 189 GLN   A CB  
1462 C  CG  . GLN   A 189 ? 0.66276 0.63848 0.41916 -0.02355 0.06916  -0.04043 189 GLN   A CG  
1463 C  CD  . GLN   A 189 ? 0.72278 0.68703 0.47978 -0.01838 0.07864  -0.05465 189 GLN   A CD  
1464 O  OE1 . GLN   A 189 ? 0.76217 0.71516 0.52235 -0.01925 0.07305  -0.06214 189 GLN   A OE1 
1465 N  NE2 . GLN   A 189 ? 0.74421 0.71063 0.49681 -0.01352 0.09272  -0.05839 189 GLN   A NE2 
1466 N  N   . THR   A 190 ? 0.46938 0.45228 0.28916 0.00059  0.10160  -0.04506 190 THR   A N   
1467 C  CA  . THR   A 190 ? 0.50751 0.48515 0.33667 0.00883  0.11348  -0.05365 190 THR   A CA  
1468 C  C   . THR   A 190 ? 0.50025 0.45898 0.32323 0.00821  0.10821  -0.06466 190 THR   A C   
1469 O  O   . THR   A 190 ? 0.49333 0.44542 0.30553 0.00110  0.09550  -0.06544 190 THR   A O   
1470 C  CB  . THR   A 190 ? 0.44796 0.43692 0.30965 0.01698  0.12025  -0.04715 190 THR   A CB  
1471 O  OG1 . THR   A 190 ? 0.41497 0.39853 0.29069 0.01835  0.11260  -0.04647 190 THR   A OG1 
1472 C  CG2 . THR   A 190 ? 0.44544 0.45373 0.31719 0.01492  0.12146  -0.03433 190 THR   A CG2 
1473 N  N   . ALA   A 191 ? 0.47364 0.42426 0.30610 0.01559  0.11772  -0.07220 191 ALA   A N   
1474 C  CA  . ALA   A 191 ? 0.46742 0.39971 0.29903 0.01554  0.11368  -0.08133 191 ALA   A CA  
1475 C  C   . ALA   A 191 ? 0.41981 0.35243 0.27639 0.01977  0.10933  -0.07608 191 ALA   A C   
1476 O  O   . ALA   A 191 ? 0.45307 0.37230 0.31746 0.02318  0.11018  -0.08173 191 ALA   A O   
1477 C  CB  . ALA   A 191 ? 0.53049 0.45132 0.36027 0.02141  0.12591  -0.09173 191 ALA   A CB  
1478 N  N   . GLN   A 192 ? 0.39685 0.34381 0.26565 0.01941  0.10479  -0.06529 192 GLN   A N   
1479 C  CA  . GLN   A 192 ? 0.36861 0.31764 0.26105 0.02408  0.10146  -0.05995 192 GLN   A CA  
1480 C  C   . GLN   A 192 ? 0.39763 0.33051 0.28337 0.01971  0.09195  -0.06586 192 GLN   A C   
1481 O  O   . GLN   A 192 ? 0.42472 0.35088 0.28905 0.01038  0.08307  -0.07011 192 GLN   A O   
1482 C  CB  . GLN   A 192 ? 0.37051 0.33650 0.27358 0.02211  0.09545  -0.04826 192 GLN   A CB  
1483 C  CG  . GLN   A 192 ? 0.35181 0.32145 0.23545 0.01205  0.08580  -0.04530 192 GLN   A CG  
1484 C  CD  . GLN   A 192 ? 0.32147 0.31001 0.22067 0.01077  0.08059  -0.03244 192 GLN   A CD  
1485 O  OE1 . GLN   A 192 ? 0.27701 0.27605 0.20178 0.01546  0.07930  -0.02595 192 GLN   A OE1 
1486 N  NE2 . GLN   A 192 ? 0.31084 0.30339 0.19440 0.00380  0.07709  -0.02843 192 GLN   A NE2 
1487 N  N   . ALA   A 193 ? 0.36758 0.29648 0.27405 0.02616  0.09265  -0.06430 193 ALA   A N   
1488 C  CA  . ALA   A 193 ? 0.34627 0.26020 0.25061 0.02252  0.08452  -0.06878 193 ALA   A CA  
1489 C  C   . ALA   A 193 ? 0.33168 0.25550 0.26434 0.02753  0.07799  -0.05796 193 ALA   A C   
1490 O  O   . ALA   A 193 ? 0.35917 0.29651 0.31238 0.03541  0.08299  -0.04994 193 ALA   A O   
1491 C  CB  . ALA   A 193 ? 0.36633 0.26225 0.26597 0.02369  0.08944  -0.07862 193 ALA   A CB  
1492 N  N   . ALA   A 194 ? 0.33128 0.24891 0.26449 0.02236  0.06677  -0.05764 194 ALA   A N   
1493 C  CA  . ALA   A 194 ? 0.32587 0.25333 0.28150 0.02533  0.05944  -0.04729 194 ALA   A CA  
1494 C  C   . ALA   A 194 ? 0.40322 0.32911 0.37992 0.03607  0.06835  -0.04361 194 ALA   A C   
1495 O  O   . ALA   A 194 ? 0.40601 0.34888 0.40190 0.04146  0.06745  -0.03319 194 ALA   A O   
1496 C  CB  . ALA   A 194 ? 0.31883 0.23801 0.27033 0.01790  0.04834  -0.04857 194 ALA   A CB  
1497 N  N   . GLY   A 195 ? 0.41578 0.32141 0.39012 0.03911  0.07658  -0.05156 195 GLY   A N   
1498 C  CA  . GLY   A 195 ? 0.47863 0.38353 0.47704 0.04967  0.08298  -0.04497 195 GLY   A CA  
1499 C  C   . GLY   A 195 ? 0.39533 0.30294 0.40760 0.04864  0.07270  -0.03572 195 GLY   A C   
1500 O  O   . GLY   A 195 ? 0.31579 0.22890 0.32114 0.04029  0.06091  -0.03385 195 GLY   A O   
1501 N  N   . THR   A 196 ? 0.38062 0.28524 0.41344 0.05754  0.07767  -0.02889 196 THR   A N   
1502 C  CA  . THR   A 196 ? 0.34424 0.24057 0.38507 0.05589  0.07148  -0.02374 196 THR   A CA  
1503 C  C   . THR   A 196 ? 0.29248 0.20938 0.33891 0.05181  0.05859  -0.01235 196 THR   A C   
1504 O  O   . THR   A 196 ? 0.31137 0.24989 0.36589 0.05455  0.05600  -0.00436 196 THR   A O   
1505 C  CB  . THR   A 196 ? 0.35636 0.24941 0.41589 0.06410  0.07667  -0.01671 196 THR   A CB  
1506 O  OG1 . THR   A 196 ? 0.40847 0.32485 0.48560 0.07143  0.07699  -0.00459 196 THR   A OG1 
1507 C  CG2 . THR   A 196 ? 0.37515 0.25063 0.42607 0.06525  0.08644  -0.02844 196 THR   A CG2 
1508 N  N   . ASP   A 197 ? 0.29124 0.20098 0.33297 0.04458  0.05093  -0.01233 197 ASP   A N   
1509 C  CA  . ASP   A 197 ? 0.25751 0.18331 0.30265 0.04025  0.04020  -0.00312 197 ASP   A CA  
1510 C  C   . ASP   A 197 ? 0.29177 0.21427 0.35179 0.04330  0.03927  0.00725  197 ASP   A C   
1511 O  O   . ASP   A 197 ? 0.31594 0.22034 0.38286 0.04723  0.04587  0.00634  197 ASP   A O   
1512 C  CB  . ASP   A 197 ? 0.24543 0.16862 0.27466 0.02930  0.03243  -0.00986 197 ASP   A CB  
1513 C  CG  . ASP   A 197 ? 0.25376 0.19733 0.28297 0.02584  0.02381  -0.00354 197 ASP   A CG  
1514 O  OD1 . ASP   A 197 ? 0.23904 0.19882 0.27521 0.03030  0.02371  0.00280  197 ASP   A OD1 
1515 O  OD2 . ASP   A 197 ? 0.26081 0.20405 0.28342 0.01836  0.01734  -0.00539 197 ASP   A OD2 
1516 N  N   . THR   A 198 ? 0.24683 0.18632 0.31107 0.04127  0.03148  0.01719  198 THR   A N   
1517 C  CA  . THR   A 198 ? 0.24189 0.18154 0.31728 0.04242  0.02924  0.02868  198 THR   A CA  
1518 C  C   . THR   A 198 ? 0.23086 0.17855 0.29866 0.03380  0.02113  0.03016  198 THR   A C   
1519 O  O   . THR   A 198 ? 0.21521 0.17057 0.27210 0.02863  0.01709  0.02386  198 THR   A O   
1520 C  CB  . THR   A 198 ? 0.31968 0.27651 0.40996 0.05051  0.02906  0.04267  198 THR   A CB  
1521 O  OG1 . THR   A 198 ? 0.27997 0.25830 0.36559 0.04902  0.02417  0.04314  198 THR   A OG1 
1522 C  CG2 . THR   A 198 ? 0.32864 0.27720 0.43204 0.06049  0.03817  0.04381  198 THR   A CG2 
1523 N  N   . THR   A 199 ? 0.24551 0.19147 0.32037 0.03269  0.01955  0.03938  199 THR   A N   
1524 C  CA  . THR   A 199 ? 0.24167 0.19659 0.31161 0.02546  0.01365  0.04225  199 THR   A CA  
1525 C  C   . THR   A 199 ? 0.20983 0.18703 0.28106 0.02767  0.01000  0.05246  199 THR   A C   
1526 O  O   . THR   A 199 ? 0.21144 0.19479 0.29172 0.03394  0.01099  0.06267  199 THR   A O   
1527 C  CB  . THR   A 199 ? 0.25918 0.20030 0.33532 0.02173  0.01460  0.04664  199 THR   A CB  
1528 O  OG1 . THR   A 199 ? 0.26027 0.18017 0.33301 0.01781  0.01700  0.03515  199 THR   A OG1 
1529 C  CG2 . THR   A 199 ? 0.21553 0.16752 0.28875 0.01476  0.01006  0.05061  199 THR   A CG2 
1530 N  N   . ILE   A 200 ? 0.19989 0.18915 0.26209 0.02242  0.00573  0.04959  200 ILE   A N   
1531 C  CA  . ILE   A 200 ? 0.14216 0.15140 0.20130 0.02291  0.00228  0.05560  200 ILE   A CA  
1532 C  C   . ILE   A 200 ? 0.15826 0.17278 0.21952 0.02140  0.00162  0.06699  200 ILE   A C   
1533 O  O   . ILE   A 200 ? 0.14184 0.15833 0.19836 0.01609  0.00115  0.06586  200 ILE   A O   
1534 C  CB  . ILE   A 200 ? 0.14881 0.16608 0.19759 0.01845  -0.00051 0.04671  200 ILE   A CB  
1535 C  CG1 . ILE   A 200 ? 0.15005 0.16096 0.19616 0.01918  0.00048  0.03668  200 ILE   A CG1 
1536 C  CG2 . ILE   A 200 ? 0.12968 0.16514 0.17403 0.01835  -0.00366 0.05086  200 ILE   A CG2 
1537 C  CD1 . ILE   A 200 ? 0.12114 0.13236 0.15907 0.01392  -0.00169 0.02812  200 ILE   A CD1 
1538 N  N   . THR   A 201 ? 0.16073 0.17895 0.22998 0.02639  0.00190  0.07915  201 THR   A N   
1539 C  CA  . THR   A 201 ? 0.16449 0.18517 0.23704 0.02552  0.00209  0.09245  201 THR   A CA  
1540 C  C   . THR   A 201 ? 0.15320 0.19061 0.21375 0.02046  -0.00052 0.09470  201 THR   A C   
1541 O  O   . THR   A 201 ? 0.16334 0.19983 0.22248 0.01637  0.00135  0.09886  201 THR   A O   
1542 C  CB  . THR   A 201 ? 0.18828 0.21279 0.27141 0.03214  0.00202  0.10514  201 THR   A CB  
1543 O  OG1 . THR   A 201 ? 0.18966 0.19736 0.28364 0.03723  0.00646  0.10068  201 THR   A OG1 
1544 C  CG2 . THR   A 201 ? 0.17993 0.20677 0.26526 0.02992  0.00273  0.11630  201 THR   A CG2 
1545 N  N   . VAL   A 202 ? 0.12611 0.17874 0.17809 0.02033  -0.00422 0.09190  202 VAL   A N   
1546 C  CA  . VAL   A 202 ? 0.13139 0.19850 0.16996 0.01554  -0.00576 0.09275  202 VAL   A CA  
1547 C  C   . VAL   A 202 ? 0.11588 0.17754 0.14945 0.01075  -0.00243 0.08286  202 VAL   A C   
1548 O  O   . VAL   A 202 ? 0.14894 0.21743 0.17568 0.00726  -0.00027 0.08588  202 VAL   A O   
1549 C  CB  . VAL   A 202 ? 0.15389 0.23602 0.18379 0.01494  -0.01065 0.08928  202 VAL   A CB  
1550 C  CG1 . VAL   A 202 ? 0.16126 0.23789 0.19128 0.01480  -0.01078 0.07504  202 VAL   A CG1 
1551 C  CG2 . VAL   A 202 ? 0.18927 0.28449 0.20266 0.00948  -0.01138 0.08918  202 VAL   A CG2 
1552 N  N   . ASN   A 203 ? 0.13586 0.18624 0.17325 0.01064  -0.00173 0.07187  203 ASN   A N   
1553 C  CA  . ASN   A 203 ? 0.11994 0.16678 0.15549 0.00650  0.00033  0.06377  203 ASN   A CA  
1554 C  C   . ASN   A 203 ? 0.13029 0.16980 0.17388 0.00396  0.00327  0.06966  203 ASN   A C   
1555 O  O   . ASN   A 203 ? 0.11951 0.16360 0.16244 0.00029  0.00583  0.06941  203 ASN   A O   
1556 C  CB  . ASN   A 203 ? 0.10953 0.14766 0.14640 0.00667  -0.00099 0.05231  203 ASN   A CB  
1557 C  CG  . ASN   A 203 ? 0.10014 0.14612 0.12941 0.00737  -0.00322 0.04547  203 ASN   A CG  
1558 O  OD1 . ASN   A 203 ? 0.11713 0.17464 0.13981 0.00722  -0.00438 0.04815  203 ASN   A OD1 
1559 N  ND2 . ASN   A 203 ? 0.10125 0.14085 0.13079 0.00717  -0.00406 0.03681  203 ASN   A ND2 
1560 N  N   . VAL   A 204 ? 0.14719 0.17475 0.19993 0.00573  0.00358  0.07479  204 VAL   A N   
1561 C  CA  . VAL   A 204 ? 0.14364 0.16303 0.20521 0.00229  0.00616  0.08134  204 VAL   A CA  
1562 C  C   . VAL   A 204 ? 0.14303 0.17502 0.20195 0.00094  0.00855  0.09342  204 VAL   A C   
1563 O  O   . VAL   A 204 ? 0.15006 0.18452 0.21186 -0.00374 0.01155  0.09581  204 VAL   A O   
1564 C  CB  . VAL   A 204 ? 0.15303 0.15511 0.22465 0.00490  0.00685  0.08471  204 VAL   A CB  
1565 C  CG1 . VAL   A 204 ? 0.17336 0.16581 0.25518 0.00037  0.00949  0.09276  204 VAL   A CG1 
1566 C  CG2 . VAL   A 204 ? 0.16694 0.15607 0.23810 0.00517  0.00570  0.07113  204 VAL   A CG2 
1567 N  N   . LEU   A 205 ? 0.14419 0.18616 0.19721 0.00461  0.00719  0.10149  205 LEU   A N   
1568 C  CA  . LEU   A 205 ? 0.15818 0.21363 0.20459 0.00279  0.00921  0.11317  205 LEU   A CA  
1569 C  C   . LEU   A 205 ? 0.17581 0.24271 0.21103 -0.00097 0.01196  0.10553  205 LEU   A C   
1570 O  O   . LEU   A 205 ? 0.14673 0.21955 0.18089 -0.00434 0.01683  0.11158  205 LEU   A O   
1571 C  CB  . LEU   A 205 ? 0.15063 0.21669 0.19124 0.00665  0.00536  0.12163  205 LEU   A CB  
1572 C  CG  . LEU   A 205 ? 0.15901 0.21571 0.21343 0.01116  0.00419  0.12835  205 LEU   A CG  
1573 C  CD1 . LEU   A 205 ? 0.17168 0.24156 0.22249 0.01449  -0.00047 0.13222  205 LEU   A CD1 
1574 C  CD2 . LEU   A 205 ? 0.21872 0.26999 0.28118 0.00919  0.00765  0.13754  205 LEU   A CD2 
1575 N  N   . ALA   A 206 ? 0.15573 0.22538 0.18366 -0.00021 0.00981  0.09253  206 ALA   A N   
1576 C  CA  . ALA   A 206 ? 0.12639 0.20392 0.14600 -0.00282 0.01348  0.08403  206 ALA   A CA  
1577 C  C   . ALA   A 206 ? 0.14120 0.21439 0.17210 -0.00570 0.01798  0.08305  206 ALA   A C   
1578 O  O   . ALA   A 206 ? 0.14031 0.22231 0.16855 -0.00784 0.02396  0.08446  206 ALA   A O   
1579 C  CB  . ALA   A 206 ? 0.13953 0.21626 0.15384 -0.00153 0.01039  0.07041  206 ALA   A CB  
1580 N  N   . TRP   A 207 ? 0.12673 0.18709 0.17023 -0.00614 0.01528  0.08028  207 TRP   A N   
1581 C  CA  . TRP   A 207 ? 0.12158 0.17879 0.17730 -0.01009 0.01743  0.07895  207 TRP   A CA  
1582 C  C   . TRP   A 207 ? 0.15605 0.21475 0.21971 -0.01353 0.02164  0.09179  207 TRP   A C   
1583 O  O   . TRP   A 207 ? 0.15513 0.21991 0.22669 -0.01714 0.02593  0.09348  207 TRP   A O   
1584 C  CB  . TRP   A 207 ? 0.13836 0.18124 0.20160 -0.01076 0.01217  0.07177  207 TRP   A CB  
1585 C  CG  . TRP   A 207 ? 0.14148 0.17889 0.21831 -0.01636 0.01151  0.07115  207 TRP   A CG  
1586 C  CD1 . TRP   A 207 ? 0.17058 0.21371 0.25343 -0.01894 0.01107  0.06586  207 TRP   A CD1 
1587 C  CD2 . TRP   A 207 ? 0.13805 0.16268 0.22492 -0.02045 0.01027  0.07579  207 TRP   A CD2 
1588 N  NE1 . TRP   A 207 ? 0.15329 0.19039 0.24936 -0.02525 0.00873  0.06761  207 TRP   A NE1 
1589 C  CE2 . TRP   A 207 ? 0.15869 0.18322 0.25660 -0.02679 0.00837  0.07284  207 TRP   A CE2 
1590 C  CE3 . TRP   A 207 ? 0.19078 0.20380 0.27970 -0.01947 0.01067  0.08269  207 TRP   A CE3 
1591 C  CZ2 . TRP   A 207 ? 0.21253 0.22499 0.32148 -0.03349 0.00626  0.07507  207 TRP   A CZ2 
1592 C  CZ3 . TRP   A 207 ? 0.21542 0.21439 0.31595 -0.02516 0.00991  0.08490  207 TRP   A CZ3 
1593 C  CH2 . TRP   A 207 ? 0.17292 0.17143 0.28244 -0.03277 0.00747  0.08041  207 TRP   A CH2 
1594 N  N   . LEU   A 208 ? 0.13860 0.19277 0.20196 -0.01231 0.02090  0.10214  208 LEU   A N   
1595 C  CA  . LEU   A 208 ? 0.14944 0.20608 0.21929 -0.01568 0.02553  0.11641  208 LEU   A CA  
1596 C  C   . LEU   A 208 ? 0.15932 0.23354 0.21786 -0.01594 0.03126  0.11904  208 LEU   A C   
1597 O  O   . LEU   A 208 ? 0.17132 0.24979 0.23561 -0.01897 0.03589  0.12256  208 LEU   A O   
1598 C  CB  . LEU   A 208 ? 0.16882 0.21686 0.24009 -0.01254 0.02276  0.12509  208 LEU   A CB  
1599 C  CG  . LEU   A 208 ? 0.21097 0.23829 0.29518 -0.01265 0.01964  0.12252  208 LEU   A CG  
1600 C  CD1 . LEU   A 208 ? 0.19400 0.21485 0.28034 -0.00778 0.01825  0.13007  208 LEU   A CD1 
1601 C  CD2 . LEU   A 208 ? 0.17063 0.18895 0.26833 -0.01938 0.02080  0.12086  208 LEU   A CD2 
1602 N  N   . TYR   A 209 ? 0.17925 0.26312 0.22078 -0.01300 0.03098  0.11559  209 TYR   A N   
1603 C  CA  . TYR   A 209 ? 0.17974 0.27763 0.20755 -0.01354 0.03681  0.11397  209 TYR   A CA  
1604 C  C   . TYR   A 209 ? 0.16143 0.26401 0.19557 -0.01507 0.04320  0.10588  209 TYR   A C   
1605 O  O   . TYR   A 209 ? 0.17983 0.28970 0.21279 -0.01634 0.05011  0.10713  209 TYR   A O   
1606 C  CB  . TYR   A 209 ? 0.16393 0.26920 0.17145 -0.01127 0.03391  0.10949  209 TYR   A CB  
1607 C  CG  . TYR   A 209 ? 0.17752 0.28519 0.17739 -0.01021 0.02907  0.11879  209 TYR   A CG  
1608 C  CD1 . TYR   A 209 ? 0.19550 0.31008 0.18827 -0.01202 0.03253  0.12610  209 TYR   A CD1 
1609 C  CD2 . TYR   A 209 ? 0.17344 0.27726 0.17485 -0.00720 0.02123  0.12071  209 TYR   A CD2 
1610 C  CE1 . TYR   A 209 ? 0.23989 0.35796 0.22750 -0.01119 0.02763  0.13554  209 TYR   A CE1 
1611 C  CE2 . TYR   A 209 ? 0.21519 0.32296 0.21369 -0.00584 0.01671  0.12964  209 TYR   A CE2 
1612 C  CZ  . TYR   A 209 ? 0.23024 0.34540 0.22178 -0.00800 0.01953  0.13728  209 TYR   A CZ  
1613 O  OH  . TYR   A 209 ? 0.26120 0.38150 0.25091 -0.00685 0.01464  0.14725  209 TYR   A OH  
1614 N  N   . ALA   A 210 ? 0.15651 0.25293 0.19763 -0.01389 0.03962  0.09489  210 ALA   A N   
1615 C  CA  . ALA   A 210 ? 0.17056 0.27068 0.22296 -0.01464 0.04403  0.08820  210 ALA   A CA  
1616 C  C   . ALA   A 210 ? 0.17905 0.28084 0.25005 -0.01911 0.04744  0.09753  210 ALA   A C   
1617 O  O   . ALA   A 210 ? 0.14771 0.25755 0.22453 -0.01935 0.05376  0.09602  210 ALA   A O   
1618 C  CB  . ALA   A 210 ? 0.15394 0.24487 0.21251 -0.01307 0.03699  0.07680  210 ALA   A CB  
1619 N  N   . ALA   A 211 ? 0.13849 0.22913 0.21826 -0.02196 0.04192  0.10407  211 ALA   A N   
1620 C  CA  . ALA   A 211 ? 0.17122 0.25945 0.26693 -0.02648 0.04251  0.10933  211 ALA   A CA  
1621 C  C   . ALA   A 211 ? 0.18574 0.28323 0.27617 -0.02661 0.04981  0.11682  211 ALA   A C   
1622 O  O   . ALA   A 211 ? 0.17696 0.28133 0.27783 -0.02888 0.05452  0.11791  211 ALA   A O   
1623 C  CB  . ALA   A 211 ? 0.16247 0.23416 0.26607 -0.02937 0.03579  0.11322  211 ALA   A CB  
1624 N  N   . VAL   A 212 ? 0.17047 0.26921 0.24468 -0.02429 0.05055  0.12217  212 VAL   A N   
1625 C  CA  . VAL   A 212 ? 0.22441 0.33189 0.29089 -0.02496 0.05711  0.12956  212 VAL   A CA  
1626 C  C   . VAL   A 212 ? 0.21315 0.33317 0.27249 -0.02376 0.06596  0.12264  212 VAL   A C   
1627 O  O   . VAL   A 212 ? 0.23448 0.36157 0.29834 -0.02567 0.07327  0.12630  212 VAL   A O   
1628 C  CB  . VAL   A 212 ? 0.25997 0.36729 0.30933 -0.02276 0.05429  0.13600  212 VAL   A CB  
1629 C  CG1 . VAL   A 212 ? 0.25004 0.36744 0.28835 -0.02400 0.06115  0.14282  212 VAL   A CG1 
1630 C  CG2 . VAL   A 212 ? 0.20051 0.29454 0.26011 -0.02286 0.04713  0.14357  212 VAL   A CG2 
1631 N  N   . ILE   A 213 ? 0.21542 0.33777 0.26393 -0.02047 0.06610  0.11219  213 ILE   A N   
1632 C  CA  . ILE   A 213 ? 0.21075 0.34206 0.25370 -0.01857 0.07523  0.10339  213 ILE   A CA  
1633 C  C   . ILE   A 213 ? 0.22162 0.35604 0.28780 -0.01960 0.07886  0.10249  213 ILE   A C   
1634 O  O   . ILE   A 213 ? 0.26160 0.40446 0.32898 -0.01909 0.08847  0.10098  213 ILE   A O   
1635 C  CB  . ILE   A 213 ? 0.24000 0.37049 0.27072 -0.01502 0.07368  0.09148  213 ILE   A CB  
1636 C  CG1 . ILE   A 213 ? 0.25289 0.38355 0.25826 -0.01480 0.07053  0.09201  213 ILE   A CG1 
1637 C  CG2 . ILE   A 213 ? 0.27361 0.40992 0.30481 -0.01236 0.08340  0.08092  213 ILE   A CG2 
1638 C  CD1 . ILE   A 213 ? 0.26952 0.39799 0.26346 -0.01255 0.06578  0.08190  213 ILE   A CD1 
1639 N  N   . ASN   A 214 ? 0.19555 0.32333 0.28046 -0.02161 0.07103  0.10385  214 ASN   A N   
1640 C  CA  . ASN   A 214 ? 0.20204 0.33318 0.30957 -0.02325 0.07141  0.10288  214 ASN   A CA  
1641 C  C   . ASN   A 214 ? 0.25197 0.38272 0.37364 -0.02870 0.07070  0.11306  214 ASN   A C   
1642 O  O   . ASN   A 214 ? 0.24789 0.38054 0.38931 -0.03149 0.06820  0.11324  214 ASN   A O   
1643 C  CB  . ASN   A 214 ? 0.22734 0.35183 0.34528 -0.02318 0.06232  0.09662  214 ASN   A CB  
1644 C  CG  . ASN   A 214 ? 0.21924 0.34730 0.33136 -0.01755 0.06501  0.08595  214 ASN   A CG  
1645 O  OD1 . ASN   A 214 ? 0.32077 0.45633 0.44149 -0.01487 0.07071  0.08205  214 ASN   A OD1 
1646 N  ND2 . ASN   A 214 ? 0.24375 0.36636 0.34179 -0.01550 0.06144  0.08158  214 ASN   A ND2 
1647 N  N   . GLY   A 215 ? 0.22618 0.35468 0.33852 -0.03051 0.07217  0.12184  215 GLY   A N   
1648 C  CA  . GLY   A 215 ? 0.25305 0.38211 0.37764 -0.03550 0.07351  0.13193  215 GLY   A CA  
1649 C  C   . GLY   A 215 ? 0.27687 0.39199 0.41159 -0.04014 0.06445  0.13717  215 GLY   A C   
1650 O  O   . GLY   A 215 ? 0.30372 0.41830 0.44960 -0.04488 0.06550  0.14527  215 GLY   A O   
1651 N  N   . ASP   A 216 ? 0.24174 0.34493 0.37350 -0.03921 0.05624  0.13230  216 ASP   A N   
1652 C  CA  . ASP   A 216 ? 0.21192 0.29901 0.35038 -0.04295 0.04901  0.13593  216 ASP   A CA  
1653 C  C   . ASP   A 216 ? 0.28154 0.36416 0.40681 -0.04018 0.05004  0.14409  216 ASP   A C   
1654 O  O   . ASP   A 216 ? 0.28127 0.36389 0.39150 -0.03521 0.04884  0.14171  216 ASP   A O   
1655 C  CB  . ASP   A 216 ? 0.26985 0.34514 0.41020 -0.04306 0.04060  0.12677  216 ASP   A CB  
1656 C  CG  . ASP   A 216 ? 0.33167 0.40842 0.48716 -0.04757 0.03646  0.12027  216 ASP   A CG  
1657 O  OD1 . ASP   A 216 ? 0.26231 0.33754 0.41636 -0.04615 0.03186  0.11152  216 ASP   A OD1 
1658 O  OD2 . ASP   A 216 ? 0.46440 0.54490 0.63320 -0.05264 0.03748  0.12445  216 ASP   A OD2 
1659 N  N   . ARG   A 217 ? 0.27025 0.34939 0.40189 -0.04350 0.05160  0.15416  217 ARG   A N   
1660 C  CA  . ARG   A 217 ? 0.26672 0.34303 0.38775 -0.04070 0.05221  0.16364  217 ARG   A CA  
1661 C  C   . ARG   A 217 ? 0.25721 0.31677 0.38935 -0.04340 0.04826  0.17000  217 ARG   A C   
1662 O  O   . ARG   A 217 ? 0.25470 0.31166 0.38095 -0.04067 0.04836  0.17905  217 ARG   A O   
1663 C  CB  . ARG   A 217 ? 0.29173 0.38300 0.40466 -0.04083 0.06043  0.17199  217 ARG   A CB  
1664 C  CG  . ARG   A 217 ? 0.30414 0.41076 0.40831 -0.03908 0.06685  0.16480  217 ARG   A CG  
1665 C  CD  . ARG   A 217 ? 0.30931 0.42878 0.40279 -0.03954 0.07594  0.17251  217 ARG   A CD  
1666 N  NE  . ARG   A 217 ? 0.27230 0.38996 0.35196 -0.03799 0.07417  0.18201  217 ARG   A NE  
1667 C  CZ  . ARG   A 217 ? 0.29151 0.41510 0.34890 -0.03438 0.07425  0.18011  217 ARG   A CZ  
1668 N  NH1 . ARG   A 217 ? 0.28851 0.41818 0.33399 -0.03194 0.07654  0.16822  217 ARG   A NH1 
1669 N  NH2 . ARG   A 217 ? 0.29118 0.41436 0.33859 -0.03342 0.07141  0.19017  217 ARG   A NH2 
1670 N  N   . TRP   A 218 ? 0.26064 0.30861 0.40826 -0.04883 0.04464  0.16520  218 TRP   A N   
1671 C  CA  . TRP   A 218 ? 0.25763 0.28874 0.41612 -0.05267 0.04252  0.17051  218 TRP   A CA  
1672 C  C   . TRP   A 218 ? 0.26156 0.27791 0.41439 -0.04725 0.03907  0.17144  218 TRP   A C   
1673 O  O   . TRP   A 218 ? 0.27957 0.28403 0.43868 -0.04805 0.03930  0.17907  218 TRP   A O   
1674 C  CB  . TRP   A 218 ? 0.28246 0.30337 0.45538 -0.06040 0.03839  0.16225  218 TRP   A CB  
1675 C  CG  . TRP   A 218 ? 0.27178 0.28389 0.44172 -0.05957 0.03221  0.14858  218 TRP   A CG  
1676 C  CD1 . TRP   A 218 ? 0.29525 0.31743 0.46499 -0.06020 0.03020  0.13966  218 TRP   A CD1 
1677 C  CD2 . TRP   A 218 ? 0.25754 0.24880 0.42459 -0.05791 0.02775  0.14254  218 TRP   A CD2 
1678 N  NE1 . TRP   A 218 ? 0.28558 0.29486 0.45154 -0.05965 0.02421  0.12891  218 TRP   A NE1 
1679 C  CE2 . TRP   A 218 ? 0.27886 0.26874 0.44271 -0.05828 0.02304  0.12995  218 TRP   A CE2 
1680 C  CE3 . TRP   A 218 ? 0.29732 0.27075 0.46473 -0.05575 0.02781  0.14658  218 TRP   A CE3 
1681 C  CZ2 . TRP   A 218 ? 0.27783 0.24911 0.43707 -0.05681 0.01888  0.12089  218 TRP   A CZ2 
1682 C  CZ3 . TRP   A 218 ? 0.30707 0.26185 0.47111 -0.05357 0.02422  0.13726  218 TRP   A CZ3 
1683 C  CH2 . TRP   A 218 ? 0.30607 0.25977 0.46527 -0.05427 0.02000  0.12423  218 TRP   A CH2 
1684 N  N   . PHE   A 219 ? 0.24633 0.26337 0.38870 -0.04158 0.03624  0.16414  219 PHE   A N   
1685 C  CA  . PHE   A 219 ? 0.25208 0.25656 0.39051 -0.03565 0.03301  0.16381  219 PHE   A CA  
1686 C  C   . PHE   A 219 ? 0.25399 0.26957 0.38172 -0.02924 0.03438  0.17431  219 PHE   A C   
1687 O  O   . PHE   A 219 ? 0.26663 0.27503 0.39265 -0.02356 0.03174  0.17583  219 PHE   A O   
1688 C  CB  . PHE   A 219 ? 0.24880 0.24918 0.38211 -0.03330 0.02908  0.15077  219 PHE   A CB  
1689 C  CG  . PHE   A 219 ? 0.21312 0.23220 0.33613 -0.03184 0.03020  0.14688  219 PHE   A CG  
1690 C  CD1 . PHE   A 219 ? 0.20892 0.23972 0.31768 -0.02570 0.03073  0.14994  219 PHE   A CD1 
1691 C  CD2 . PHE   A 219 ? 0.20353 0.22920 0.33141 -0.03683 0.03074  0.14011  219 PHE   A CD2 
1692 C  CE1 . PHE   A 219 ? 0.21382 0.26016 0.31160 -0.02470 0.03250  0.14501  219 PHE   A CE1 
1693 C  CE2 . PHE   A 219 ? 0.21470 0.25680 0.33395 -0.03477 0.03297  0.13611  219 PHE   A CE2 
1694 C  CZ  . PHE   A 219 ? 0.20416 0.25555 0.30753 -0.02883 0.03434  0.13803  219 PHE   A CZ  
1695 N  N   . LEU   A 220 ? 0.25771 0.29104 0.37800 -0.03014 0.03842  0.18128  220 LEU   A N   
1696 C  CA  . LEU   A 220 ? 0.26681 0.31143 0.37492 -0.02553 0.03889  0.19109  220 LEU   A CA  
1697 C  C   . LEU   A 220 ? 0.28908 0.32612 0.40632 -0.02570 0.03952  0.20453  220 LEU   A C   
1698 O  O   . LEU   A 220 ? 0.29925 0.32541 0.43039 -0.03059 0.04136  0.20703  220 LEU   A O   
1699 C  CB  . LEU   A 220 ? 0.26755 0.33214 0.36200 -0.02708 0.04380  0.19258  220 LEU   A CB  
1700 C  CG  . LEU   A 220 ? 0.24855 0.32171 0.33265 -0.02614 0.04416  0.17989  220 LEU   A CG  
1701 C  CD1 . LEU   A 220 ? 0.25707 0.34747 0.32814 -0.02771 0.05092  0.18128  220 LEU   A CD1 
1702 C  CD2 . LEU   A 220 ? 0.23927 0.31206 0.31291 -0.02052 0.03850  0.17542  220 LEU   A CD2 
1703 N  N   . ASN   A 221 ? 0.29809 0.34133 0.40787 -0.02065 0.03759  0.21342  221 ASN   A N   
1704 C  CA  . ASN   A 221 ? 0.32080 0.35858 0.43929 -0.02001 0.03815  0.22782  221 ASN   A CA  
1705 C  C   . ASN   A 221 ? 0.36752 0.42261 0.47213 -0.01665 0.03693  0.23886  221 ASN   A C   
1706 O  O   . ASN   A 221 ? 0.34353 0.41273 0.43151 -0.01491 0.03509  0.23381  221 ASN   A O   
1707 C  CB  . ASN   A 221 ? 0.39359 0.41021 0.52686 -0.01655 0.03535  0.22619  221 ASN   A CB  
1708 C  CG  . ASN   A 221 ? 0.41386 0.42873 0.54242 -0.01071 0.03107  0.21589  221 ASN   A CG  
1709 O  OD1 . ASN   A 221 ? 0.43416 0.43850 0.56531 -0.01187 0.03034  0.20263  221 ASN   A OD1 
1710 N  ND2 . ASN   A 221 ? 0.42274 0.44886 0.54436 -0.00489 0.02794  0.22214  221 ASN   A ND2 
1711 N  N   . ARG   A 222 ? 0.37978 0.43349 0.49106 -0.01652 0.03783  0.25416  222 ARG   A N   
1712 C  CA  . ARG   A 222 ? 0.39987 0.46960 0.49929 -0.01408 0.03593  0.26676  222 ARG   A CA  
1713 C  C   . ARG   A 222 ? 0.44394 0.51351 0.54574 -0.00704 0.02951  0.26888  222 ARG   A C   
1714 O  O   . ARG   A 222 ? 0.51950 0.60554 0.60840 -0.00529 0.02603  0.27558  222 ARG   A O   
1715 C  CB  . ARG   A 222 ? 0.46228 0.53138 0.56886 -0.01687 0.03947  0.28394  222 ARG   A CB  
1716 C  CG  . ARG   A 222 ? 0.46177 0.51411 0.58887 -0.01318 0.03769  0.29305  222 ARG   A CG  
1717 C  CD  . ARG   A 222 ? 0.43744 0.48566 0.57430 -0.01699 0.04196  0.30886  222 ARG   A CD  
1718 N  NE  . ARG   A 222 ? 0.55326 0.61882 0.67945 -0.01598 0.04098  0.32546  222 ARG   A NE  
1719 C  CZ  . ARG   A 222 ? 0.53840 0.60452 0.66978 -0.01889 0.04436  0.34205  222 ARG   A CZ  
1720 N  NH1 . ARG   A 222 ? 0.56134 0.61174 0.70910 -0.02335 0.04912  0.34435  222 ARG   A NH1 
1721 N  NH2 . ARG   A 222 ? 0.58250 0.66545 0.70208 -0.01791 0.04264  0.35690  222 ARG   A NH2 
1722 N  N   . PHE   A 223 ? 0.45287 0.50466 0.57058 -0.00334 0.02809  0.26317  223 PHE   A N   
1723 C  CA  . PHE   A 223 ? 0.45634 0.50797 0.57932 0.00385  0.02325  0.26566  223 PHE   A CA  
1724 C  C   . PHE   A 223 ? 0.40851 0.47496 0.51581 0.00576  0.01866  0.25627  223 PHE   A C   
1725 O  O   . PHE   A 223 ? 0.38670 0.45743 0.48176 0.00242  0.01957  0.24422  223 PHE   A O   
1726 C  CB  . PHE   A 223 ? 0.48411 0.51188 0.62583 0.00743  0.02429  0.25895  223 PHE   A CB  
1727 C  CG  . PHE   A 223 ? 0.49437 0.50256 0.64825 0.00258  0.02918  0.25805  223 PHE   A CG  
1728 C  CD1 . PHE   A 223 ? 0.52182 0.52671 0.68450 0.00061  0.03184  0.27306  223 PHE   A CD1 
1729 C  CD2 . PHE   A 223 ? 0.50449 0.49752 0.66113 -0.00064 0.03069  0.24237  223 PHE   A CD2 
1730 C  CE1 . PHE   A 223 ? 0.56077 0.54725 0.73511 -0.00487 0.03601  0.27192  223 PHE   A CE1 
1731 C  CE2 . PHE   A 223 ? 0.56152 0.53691 0.72904 -0.00649 0.03426  0.24085  223 PHE   A CE2 
1732 C  CZ  . PHE   A 223 ? 0.58987 0.56177 0.76643 -0.00877 0.03696  0.25533  223 PHE   A CZ  
1733 N  N   . THR   A 224 ? 0.41552 0.48988 0.52466 0.01106  0.01372  0.26226  224 THR   A N   
1734 C  CA  . THR   A 224 ? 0.41010 0.49502 0.50971 0.01346  0.00875  0.25316  224 THR   A CA  
1735 C  C   . THR   A 224 ? 0.39047 0.46577 0.50764 0.02066  0.00700  0.25306  224 THR   A C   
1736 O  O   . THR   A 224 ? 0.42240 0.48271 0.55755 0.02385  0.00993  0.25969  224 THR   A O   
1737 C  CB  . THR   A 224 ? 0.41563 0.52458 0.49713 0.01146  0.00387  0.26018  224 THR   A CB  
1738 O  OG1 . THR   A 224 ? 0.38986 0.50803 0.45762 0.01087  0.00009  0.24721  224 THR   A OG1 
1739 C  CG2 . THR   A 224 ? 0.39505 0.51150 0.48673 0.01570  -0.00037 0.27659  224 THR   A CG2 
1740 N  N   . THR   A 225 ? 0.34949 0.43301 0.46148 0.02311  0.00282  0.24510  225 THR   A N   
1741 C  CA  . THR   A 225 ? 0.38376 0.46152 0.51130 0.03017  0.00161  0.24481  225 THR   A CA  
1742 C  C   . THR   A 225 ? 0.34043 0.43894 0.45895 0.03094  -0.00509 0.24431  225 THR   A C   
1743 O  O   . THR   A 225 ? 0.39272 0.50556 0.49164 0.02572  -0.00835 0.23968  225 THR   A O   
1744 C  CB  . THR   A 225 ? 0.41639 0.47271 0.55149 0.03218  0.00579  0.22968  225 THR   A CB  
1745 O  OG1 . THR   A 225 ? 0.44828 0.49651 0.60015 0.03965  0.00666  0.23073  225 THR   A OG1 
1746 C  CG2 . THR   A 225 ? 0.35594 0.41792 0.47561 0.02918  0.00388  0.21468  225 THR   A CG2 
1747 N  N   . THR   A 226 ? 0.34066 0.44059 0.47394 0.03716  -0.00686 0.24908  226 THR   A N   
1748 C  CA  . THR   A 226 ? 0.39723 0.51535 0.52475 0.03752  -0.01319 0.24714  226 THR   A CA  
1749 C  C   . THR   A 226 ? 0.30469 0.41434 0.43148 0.03903  -0.01176 0.23010  226 THR   A C   
1750 O  O   . THR   A 226 ? 0.32969 0.41871 0.46458 0.04161  -0.00591 0.22188  226 THR   A O   
1751 C  CB  . THR   A 226 ? 0.36331 0.49027 0.50814 0.04321  -0.01599 0.26172  226 THR   A CB  
1752 O  OG1 . THR   A 226 ? 0.43080 0.54033 0.59615 0.05077  -0.01056 0.25841  226 THR   A OG1 
1753 C  CG2 . THR   A 226 ? 0.38498 0.51702 0.53401 0.04270  -0.01655 0.28021  226 THR   A CG2 
1754 N  N   . LEU   A 227 ? 0.32477 0.45042 0.44096 0.03676  -0.01741 0.22473  227 LEU   A N   
1755 C  CA  . LEU   A 227 ? 0.30956 0.42968 0.42488 0.03805  -0.01669 0.20983  227 LEU   A CA  
1756 C  C   . LEU   A 227 ? 0.32837 0.43588 0.46515 0.04621  -0.01241 0.20986  227 LEU   A C   
1757 O  O   . LEU   A 227 ? 0.27511 0.36550 0.41482 0.04844  -0.00744 0.19808  227 LEU   A O   
1758 C  CB  . LEU   A 227 ? 0.35310 0.49353 0.45528 0.03381  -0.02398 0.20606  227 LEU   A CB  
1759 C  CG  . LEU   A 227 ? 0.34220 0.47982 0.43726 0.03259  -0.02417 0.18981  227 LEU   A CG  
1760 C  CD1 . LEU   A 227 ? 0.31513 0.44032 0.39787 0.02922  -0.02019 0.17834  227 LEU   A CD1 
1761 C  CD2 . LEU   A 227 ? 0.31460 0.47244 0.39712 0.02726  -0.03187 0.18758  227 LEU   A CD2 
1762 N  N   . ASN   A 228 ? 0.36015 0.47599 0.51199 0.05081  -0.01395 0.22300  228 ASN   A N   
1763 C  CA  . ASN   A 228 ? 0.37989 0.48336 0.55295 0.05926  -0.00846 0.22332  228 ASN   A CA  
1764 C  C   . ASN   A 228 ? 0.35580 0.43306 0.53741 0.06229  -0.00028 0.22063  228 ASN   A C   
1765 O  O   . ASN   A 228 ? 0.35923 0.41877 0.54813 0.06659  0.00577  0.21031  228 ASN   A O   
1766 C  CB  . ASN   A 228 ? 0.36592 0.48409 0.55526 0.06376  -0.01136 0.23993  228 ASN   A CB  
1767 C  CG  . ASN   A 228 ? 0.42207 0.56671 0.60261 0.05928  -0.02054 0.24329  228 ASN   A CG  
1768 O  OD1 . ASN   A 228 ? 0.45604 0.60531 0.62469 0.05565  -0.02303 0.23094  228 ASN   A OD1 
1769 N  ND2 . ASN   A 228 ? 0.44007 0.60200 0.62658 0.05914  -0.02589 0.26013  228 ASN   A ND2 
1770 N  N   . ASP   A 229 ? 0.36074 0.43476 0.54075 0.05949  0.00011  0.22929  229 ASP   A N   
1771 C  CA  . ASP   A 229 ? 0.37757 0.42612 0.56625 0.06120  0.00741  0.22696  229 ASP   A CA  
1772 C  C   . ASP   A 229 ? 0.39951 0.43209 0.57678 0.05728  0.01040  0.20925  229 ASP   A C   
1773 O  O   . ASP   A 229 ? 0.42048 0.43042 0.60544 0.06010  0.01655  0.20045  229 ASP   A O   
1774 C  CB  . ASP   A 229 ? 0.41158 0.46185 0.60081 0.05814  0.00680  0.24094  229 ASP   A CB  
1775 C  CG  . ASP   A 229 ? 0.45252 0.50416 0.66189 0.06453  0.00785  0.25777  229 ASP   A CG  
1776 O  OD1 . ASP   A 229 ? 0.49032 0.54223 0.71377 0.07150  0.00932  0.25852  229 ASP   A OD1 
1777 O  OD2 . ASP   A 229 ? 0.51881 0.57180 0.73065 0.06273  0.00752  0.27094  229 ASP   A OD2 
1778 N  N   . PHE   A 230 ? 0.33296 0.37679 0.49165 0.05065  0.00621  0.20349  230 PHE   A N   
1779 C  CA  . PHE   A 230 ? 0.34398 0.37481 0.49312 0.04720  0.00848  0.18762  230 PHE   A CA  
1780 C  C   . PHE   A 230 ? 0.32680 0.35033 0.47986 0.05188  0.01050  0.17583  230 PHE   A C   
1781 O  O   . PHE   A 230 ? 0.34140 0.34499 0.49501 0.05192  0.01500  0.16421  230 PHE   A O   
1782 C  CB  . PHE   A 230 ? 0.29564 0.34158 0.42521 0.04016  0.00401  0.18401  230 PHE   A CB  
1783 C  CG  . PHE   A 230 ? 0.26388 0.29903 0.38500 0.03706  0.00575  0.16883  230 PHE   A CG  
1784 C  CD1 . PHE   A 230 ? 0.26407 0.28288 0.38553 0.03313  0.00957  0.16497  230 PHE   A CD1 
1785 C  CD2 . PHE   A 230 ? 0.26677 0.30791 0.38103 0.03775  0.00341  0.15892  230 PHE   A CD2 
1786 C  CE1 . PHE   A 230 ? 0.26554 0.27514 0.38052 0.02987  0.01062  0.15200  230 PHE   A CE1 
1787 C  CE2 . PHE   A 230 ? 0.28015 0.31137 0.38758 0.03514  0.00482  0.14614  230 PHE   A CE2 
1788 C  CZ  . PHE   A 230 ? 0.26572 0.28147 0.37357 0.03119  0.00827  0.14299  230 PHE   A CZ  
1789 N  N   . ASN   A 231 ? 0.33780 0.37765 0.49309 0.05520  0.00717  0.17848  231 ASN   A N   
1790 C  CA  . ASN   A 231 ? 0.34485 0.38019 0.50261 0.05910  0.00929  0.16725  231 ASN   A CA  
1791 C  C   . ASN   A 231 ? 0.35260 0.36773 0.52671 0.06624  0.01711  0.16513  231 ASN   A C   
1792 O  O   . ASN   A 231 ? 0.32395 0.32693 0.49786 0.06864  0.02140  0.15253  231 ASN   A O   
1793 C  CB  . ASN   A 231 ? 0.28342 0.34217 0.44041 0.05986  0.00366  0.17100  231 ASN   A CB  
1794 C  CG  . ASN   A 231 ? 0.30018 0.37249 0.43819 0.05292  -0.00234 0.16428  231 ASN   A CG  
1795 O  OD1 . ASN   A 231 ? 0.35493 0.41760 0.48358 0.05036  -0.00081 0.15252  231 ASN   A OD1 
1796 N  ND2 . ASN   A 231 ? 0.34573 0.44009 0.47790 0.04961  -0.00921 0.17146  231 ASN   A ND2 
1797 N  N   . LEU   A 232 ? 0.35688 0.36757 0.54455 0.06962  0.01949  0.17694  232 LEU   A N   
1798 C  CA  . LEU   A 232 ? 0.38442 0.37207 0.58638 0.07573  0.02790  0.17374  232 LEU   A CA  
1799 C  C   . LEU   A 232 ? 0.39433 0.35680 0.58843 0.07163  0.03212  0.15995  232 LEU   A C   
1800 O  O   . LEU   A 232 ? 0.41079 0.35424 0.60763 0.07483  0.03852  0.14814  232 LEU   A O   
1801 C  CB  . LEU   A 232 ? 0.38371 0.37084 0.60157 0.07941  0.02928  0.18998  232 LEU   A CB  
1802 C  CG  . LEU   A 232 ? 0.42575 0.43618 0.65520 0.08404  0.02548  0.20549  232 LEU   A CG  
1803 C  CD1 . LEU   A 232 ? 0.43033 0.43734 0.67595 0.08758  0.02734  0.22176  232 LEU   A CD1 
1804 C  CD2 . LEU   A 232 ? 0.39829 0.41081 0.63770 0.09106  0.02915  0.20049  232 LEU   A CD2 
1805 N  N   . VAL   A 233 ? 0.35028 0.31275 0.53406 0.06399  0.02869  0.16103  233 VAL   A N   
1806 C  CA  . VAL   A 233 ? 0.40548 0.34560 0.58253 0.05859  0.03164  0.14888  233 VAL   A CA  
1807 C  C   . VAL   A 233 ? 0.40281 0.34160 0.56732 0.05636  0.03088  0.13346  233 VAL   A C   
1808 O  O   . VAL   A 233 ? 0.39472 0.31247 0.55679 0.05539  0.03517  0.12003  233 VAL   A O   
1809 C  CB  . VAL   A 233 ? 0.42163 0.36444 0.59343 0.05090  0.02859  0.15600  233 VAL   A CB  
1810 C  CG1 . VAL   A 233 ? 0.39858 0.32746 0.55986 0.04302  0.02888  0.14296  233 VAL   A CG1 
1811 C  CG2 . VAL   A 233 ? 0.42702 0.36023 0.61235 0.05256  0.03161  0.16761  233 VAL   A CG2 
1812 N  N   . ALA   A 234 ? 0.38248 0.34331 0.53801 0.05500  0.02526  0.13487  234 ALA   A N   
1813 C  CA  . ALA   A 234 ? 0.36186 0.32296 0.50629 0.05312  0.02421  0.12171  234 ALA   A CA  
1814 C  C   . ALA   A 234 ? 0.35606 0.30595 0.50549 0.05932  0.02981  0.11181  234 ALA   A C   
1815 O  O   . ALA   A 234 ? 0.35141 0.28721 0.49356 0.05740  0.03235  0.09799  234 ALA   A O   
1816 C  CB  . ALA   A 234 ? 0.34290 0.33016 0.47851 0.05144  0.01746  0.12589  234 ALA   A CB  
1817 N  N   . MET   A 235 ? 0.36620 0.32295 0.52793 0.06653  0.03206  0.11888  235 MET   A N   
1818 C  CA  . MET   A 235 ? 0.39384 0.34124 0.56125 0.07292  0.03881  0.11014  235 MET   A CA  
1819 C  C   . MET   A 235 ? 0.39569 0.31316 0.56316 0.07272  0.04621  0.09915  235 MET   A C   
1820 O  O   . MET   A 235 ? 0.41090 0.31599 0.57180 0.07325  0.05087  0.08480  235 MET   A O   
1821 C  CB  . MET   A 235 ? 0.39579 0.35632 0.57934 0.08046  0.04019  0.12196  235 MET   A CB  
1822 C  CG  . MET   A 235 ? 0.45780 0.41089 0.64945 0.08781  0.04837  0.11463  235 MET   A CG  
1823 S  SD  . MET   A 235 ? 0.61401 0.59207 0.82339 0.09507  0.04741  0.12894  235 MET   A SD  
1824 C  CE  . MET   A 235 ? 0.45416 0.46095 0.65530 0.08799  0.03426  0.14067  235 MET   A CE  
1825 N  N   . LYS   A 236 ? 0.43003 0.33552 0.60331 0.07094  0.04712  0.10518  236 LYS   A N   
1826 C  CA  . LYS   A 236 ? 0.37919 0.25534 0.55251 0.06974  0.05359  0.09475  236 LYS   A CA  
1827 C  C   . LYS   A 236 ? 0.38024 0.24302 0.53688 0.06110  0.05209  0.07940  236 LYS   A C   
1828 O  O   . LYS   A 236 ? 0.41784 0.25894 0.56907 0.06015  0.05739  0.06514  236 LYS   A O   
1829 C  CB  . LYS   A 236 ? 0.43007 0.29764 0.61367 0.06867  0.05397  0.10578  236 LYS   A CB  
1830 C  CG  . LYS   A 236 ? 0.46592 0.30245 0.64740 0.06452  0.05882  0.09483  236 LYS   A CG  
1831 C  CD  . LYS   A 236 ? 0.48346 0.31142 0.67760 0.06434  0.05988  0.10705  236 LYS   A CD  
1832 C  CE  . LYS   A 236 ? 0.55809 0.35732 0.74677 0.05626  0.06183  0.09630  236 LYS   A CE  
1833 N  NZ  . LYS   A 236 ? 0.61257 0.38876 0.79501 0.05766  0.06835  0.07778  236 LYS   A NZ  
1834 N  N   . TYR   A 237 ? 0.36510 0.24081 0.51293 0.05443  0.04495  0.08178  237 TYR   A N   
1835 C  CA  . TYR   A 237 ? 0.34793 0.21323 0.48195 0.04548  0.04263  0.06919  237 TYR   A CA  
1836 C  C   . TYR   A 237 ? 0.30601 0.18173 0.42972 0.04572  0.04081  0.06091  237 TYR   A C   
1837 O  O   . TYR   A 237 ? 0.31679 0.19085 0.43018 0.03814  0.03705  0.05403  237 TYR   A O   
1838 C  CB  . TYR   A 237 ? 0.35064 0.22158 0.48325 0.03720  0.03693  0.07701  237 TYR   A CB  
1839 C  CG  . TYR   A 237 ? 0.37478 0.23040 0.51547 0.03457  0.03908  0.08188  237 TYR   A CG  
1840 C  CD1 . TYR   A 237 ? 0.40192 0.26529 0.55500 0.03986  0.04005  0.09721  237 TYR   A CD1 
1841 C  CD2 . TYR   A 237 ? 0.39228 0.22575 0.52818 0.02617  0.03974  0.07122  237 TYR   A CD2 
1842 C  CE1 . TYR   A 237 ? 0.40180 0.25029 0.56319 0.03765  0.04238  0.10230  237 TYR   A CE1 
1843 C  CE2 . TYR   A 237 ? 0.40084 0.21939 0.54444 0.02330  0.04165  0.07561  237 TYR   A CE2 
1844 C  CZ  . TYR   A 237 ? 0.42170 0.24738 0.57847 0.02944  0.04334  0.09137  237 TYR   A CZ  
1845 O  OH  . TYR   A 237 ? 0.47753 0.28769 0.64280 0.02666  0.04552  0.09645  237 TYR   A OH  
1846 N  N   . ASN   A 238 ? 0.31888 0.20561 0.44636 0.05389  0.04348  0.06182  238 ASN   A N   
1847 C  CA  . ASN   A 238 ? 0.31392 0.20968 0.43255 0.05459  0.04278  0.05378  238 ASN   A CA  
1848 C  C   . ASN   A 238 ? 0.27071 0.18630 0.38408 0.05047  0.03467  0.05994  238 ASN   A C   
1849 O  O   . ASN   A 238 ? 0.30024 0.21732 0.40388 0.04723  0.03277  0.05181  238 ASN   A O   
1850 C  CB  . ASN   A 238 ? 0.33262 0.20740 0.43843 0.05003  0.04651  0.03571  238 ASN   A CB  
1851 C  CG  . ASN   A 238 ? 0.36449 0.24643 0.46309 0.05321  0.04906  0.02730  238 ASN   A CG  
1852 O  OD1 . ASN   A 238 ? 0.42450 0.29682 0.50900 0.04784  0.04956  0.01408  238 ASN   A OD1 
1853 N  ND2 . ASN   A 238 ? 0.37081 0.27071 0.47891 0.06109  0.05044  0.03520  238 ASN   A ND2 
1854 N  N   . TYR   A 239 ? 0.27302 0.20399 0.39200 0.05042  0.03015  0.07417  239 TYR   A N   
1855 C  CA  . TYR   A 239 ? 0.27682 0.22918 0.38981 0.04719  0.02298  0.08063  239 TYR   A CA  
1856 C  C   . TYR   A 239 ? 0.26489 0.23925 0.38155 0.05254  0.02076  0.08691  239 TYR   A C   
1857 O  O   . TYR   A 239 ? 0.26765 0.24392 0.39502 0.05810  0.02362  0.09253  239 TYR   A O   
1858 C  CB  . TYR   A 239 ? 0.24765 0.20475 0.36120 0.04233  0.01968  0.09145  239 TYR   A CB  
1859 C  CG  . TYR   A 239 ? 0.24070 0.18654 0.34859 0.03394  0.01880  0.08698  239 TYR   A CG  
1860 C  CD1 . TYR   A 239 ? 0.26783 0.18975 0.37610 0.03051  0.02238  0.07633  239 TYR   A CD1 
1861 C  CD2 . TYR   A 239 ? 0.21579 0.17599 0.31757 0.02851  0.01443  0.09304  239 TYR   A CD2 
1862 C  CE1 . TYR   A 239 ? 0.27009 0.18415 0.37477 0.02100  0.02039  0.07249  239 TYR   A CE1 
1863 C  CE2 . TYR   A 239 ? 0.21528 0.16872 0.31372 0.02000  0.01383  0.08902  239 TYR   A CE2 
1864 C  CZ  . TYR   A 239 ? 0.23933 0.17076 0.34019 0.01596  0.01613  0.07914  239 TYR   A CZ  
1865 O  OH  . TYR   A 239 ? 0.24469 0.17295 0.34352 0.00638  0.01424  0.07512  239 TYR   A OH  
1866 N  N   . GLU   A 240 ? 0.25407 0.24503 0.36257 0.05023  0.01551  0.08591  240 GLU   A N   
1867 C  CA  . GLU   A 240 ? 0.29477 0.30546 0.40746 0.05372  0.01315  0.09088  240 GLU   A CA  
1868 C  C   . GLU   A 240 ? 0.27755 0.30499 0.39084 0.05162  0.00783  0.10397  240 GLU   A C   
1869 O  O   . GLU   A 240 ? 0.24705 0.27268 0.35575 0.04750  0.00625  0.10866  240 GLU   A O   
1870 C  CB  . GLU   A 240 ? 0.35123 0.37315 0.45609 0.05203  0.01008  0.08336  240 GLU   A CB  
1871 C  CG  . GLU   A 240 ? 0.28380 0.31471 0.37525 0.04484  0.00409  0.08151  240 GLU   A CG  
1872 C  CD  . GLU   A 240 ? 0.32747 0.36330 0.40894 0.04095  0.00282  0.06897  240 GLU   A CD  
1873 O  OE1 . GLU   A 240 ? 0.42048 0.45818 0.50781 0.04501  0.00553  0.06589  240 GLU   A OE1 
1874 O  OE2 . GLU   A 240 ? 0.33790 0.37555 0.40680 0.03409  -0.00018 0.06278  240 GLU   A OE2 
1875 N  N   . PRO   A 241 ? 0.28325 0.32637 0.40325 0.05426  0.00570  0.11079  241 PRO   A N   
1876 C  CA  . PRO   A 241 ? 0.24835 0.30609 0.36897 0.05217  0.00096  0.12358  241 PRO   A CA  
1877 C  C   . PRO   A 241 ? 0.24127 0.31247 0.34536 0.04459  -0.00553 0.12320  241 PRO   A C   
1878 O  O   . PRO   A 241 ? 0.29581 0.37143 0.38995 0.04137  -0.00793 0.11426  241 PRO   A O   
1879 C  CB  . PRO   A 241 ? 0.28838 0.36062 0.41976 0.05593  -0.00050 0.12953  241 PRO   A CB  
1880 C  CG  . PRO   A 241 ? 0.34363 0.40941 0.47987 0.05998  0.00416  0.11972  241 PRO   A CG  
1881 C  CD  . PRO   A 241 ? 0.31552 0.36059 0.44575 0.05993  0.00918  0.10833  241 PRO   A CD  
1882 N  N   . LEU   A 242 ? 0.27328 0.35019 0.37434 0.04176  -0.00759 0.13275  242 LEU   A N   
1883 C  CA  . LEU   A 242 ? 0.29402 0.38524 0.37872 0.03474  -0.01280 0.13341  242 LEU   A CA  
1884 C  C   . LEU   A 242 ? 0.26887 0.38041 0.35275 0.03318  -0.01877 0.14045  242 LEU   A C   
1885 O  O   . LEU   A 242 ? 0.25786 0.37310 0.35390 0.03676  -0.01886 0.15137  242 LEU   A O   
1886 C  CB  . LEU   A 242 ? 0.26884 0.35531 0.34955 0.03198  -0.01089 0.13966  242 LEU   A CB  
1887 C  CG  . LEU   A 242 ? 0.23667 0.33192 0.29875 0.02494  -0.01298 0.13661  242 LEU   A CG  
1888 C  CD1 . LEU   A 242 ? 0.24841 0.33471 0.30384 0.02318  -0.01099 0.12448  242 LEU   A CD1 
1889 C  CD2 . LEU   A 242 ? 0.23852 0.33282 0.29946 0.02281  -0.01076 0.14610  242 LEU   A CD2 
1890 N  N   . THR   A 243 ? 0.24521 0.36933 0.31529 0.02752  -0.02379 0.13415  243 THR   A N   
1891 C  CA  . THR   A 243 ? 0.28324 0.42627 0.35073 0.02426  -0.03035 0.13916  243 THR   A CA  
1892 C  C   . THR   A 243 ? 0.26433 0.41781 0.31430 0.01733  -0.03403 0.14180  243 THR   A C   
1893 O  O   . THR   A 243 ? 0.27220 0.41940 0.31080 0.01475  -0.03111 0.13784  243 THR   A O   
1894 C  CB  . THR   A 243 ? 0.26491 0.41414 0.32969 0.02184  -0.03356 0.12934  243 THR   A CB  
1895 O  OG1 . THR   A 243 ? 0.23200 0.37986 0.27903 0.01587  -0.03436 0.11780  243 THR   A OG1 
1896 C  CG2 . THR   A 243 ? 0.28040 0.41875 0.36040 0.02862  -0.02869 0.12541  243 THR   A CG2 
1897 N  N   . GLN   A 244 ? 0.25230 0.42244 0.29985 0.01405  -0.04032 0.14848  244 GLN   A N   
1898 C  CA  . GLN   A 244 ? 0.26810 0.44886 0.29616 0.00670  -0.04409 0.14930  244 GLN   A CA  
1899 C  C   . GLN   A 244 ? 0.25938 0.43889 0.26824 0.00036  -0.04442 0.13376  244 GLN   A C   
1900 O  O   . GLN   A 244 ? 0.28863 0.46905 0.27994 -0.00435 -0.04326 0.13071  244 GLN   A O   
1901 C  CB  . GLN   A 244 ? 0.27216 0.47125 0.30103 0.00379  -0.05172 0.15902  244 GLN   A CB  
1902 C  CG  . GLN   A 244 ? 0.31198 0.52163 0.31972 -0.00366 -0.05543 0.16109  244 GLN   A CG  
1903 C  CD  . GLN   A 244 ? 0.33602 0.53939 0.34093 -0.00182 -0.05025 0.16846  244 GLN   A CD  
1904 O  OE1 . GLN   A 244 ? 0.35273 0.55067 0.37510 0.00456  -0.04722 0.17953  244 GLN   A OE1 
1905 N  NE2 . GLN   A 244 ? 0.37412 0.57725 0.35737 -0.00743 -0.04846 0.16199  244 GLN   A NE2 
1906 N  N   . ASP   A 245 ? 0.26790 0.44491 0.28002 0.00027  -0.04527 0.12378  245 ASP   A N   
1907 C  CA  . ASP   A 245 ? 0.24890 0.42220 0.24492 -0.00509 -0.04462 0.10877  245 ASP   A CA  
1908 C  C   . ASP   A 245 ? 0.24678 0.40672 0.23884 -0.00289 -0.03758 0.10427  245 ASP   A C   
1909 O  O   . ASP   A 245 ? 0.29141 0.45035 0.26651 -0.00757 -0.03559 0.09647  245 ASP   A O   
1910 C  CB  . ASP   A 245 ? 0.28870 0.46115 0.29126 -0.00535 -0.04656 0.10005  245 ASP   A CB  
1911 C  CG  . ASP   A 245 ? 0.36282 0.53342 0.34834 -0.01239 -0.04720 0.08497  245 ASP   A CG  
1912 O  OD1 . ASP   A 245 ? 0.41082 0.58640 0.37872 -0.01872 -0.04890 0.08193  245 ASP   A OD1 
1913 O  OD2 . ASP   A 245 ? 0.43638 0.59974 0.42577 -0.01159 -0.04549 0.07590  245 ASP   A OD2 
1914 N  N   . HIS   A 246 ? 0.24285 0.39190 0.25058 0.00406  -0.03331 0.10877  246 HIS   A N   
1915 C  CA  . HIS   A 246 ? 0.25546 0.39227 0.26128 0.00566  -0.02714 0.10677  246 HIS   A CA  
1916 C  C   . HIS   A 246 ? 0.25535 0.39570 0.25074 0.00268  -0.02503 0.11296  246 HIS   A C   
1917 O  O   . HIS   A 246 ? 0.25339 0.39041 0.23736 -0.00013 -0.02077 0.10736  246 HIS   A O   
1918 C  CB  . HIS   A 246 ? 0.24260 0.36605 0.26728 0.01289  -0.02332 0.11170  246 HIS   A CB  
1919 C  CG  . HIS   A 246 ? 0.23415 0.35157 0.26798 0.01636  -0.02330 0.10435  246 HIS   A CG  
1920 N  ND1 . HIS   A 246 ? 0.24546 0.35495 0.29666 0.02295  -0.02096 0.10837  246 HIS   A ND1 
1921 C  CD2 . HIS   A 246 ? 0.25493 0.37268 0.28296 0.01418  -0.02455 0.09297  246 HIS   A CD2 
1922 C  CE1 . HIS   A 246 ? 0.27104 0.37684 0.32602 0.02474  -0.02049 0.09979  246 HIS   A CE1 
1923 N  NE2 . HIS   A 246 ? 0.27209 0.38319 0.31382 0.01936  -0.02309 0.09087  246 HIS   A NE2 
1924 N  N   . VAL   A 247 ? 0.25905 0.40631 0.25929 0.00356  -0.02725 0.12518  247 VAL   A N   
1925 C  CA  . VAL   A 247 ? 0.23674 0.38857 0.22681 0.00057  -0.02543 0.13209  247 VAL   A CA  
1926 C  C   . VAL   A 247 ? 0.25436 0.41455 0.22096 -0.00657 -0.02643 0.12287  247 VAL   A C   
1927 O  O   . VAL   A 247 ? 0.27996 0.43782 0.23454 -0.00911 -0.02095 0.11996  247 VAL   A O   
1928 C  CB  . VAL   A 247 ? 0.28484 0.44458 0.28402 0.00251  -0.02888 0.14732  247 VAL   A CB  
1929 C  CG1 . VAL   A 247 ? 0.30237 0.46960 0.28765 -0.00165 -0.02809 0.15424  247 VAL   A CG1 
1930 C  CG2 . VAL   A 247 ? 0.28478 0.43231 0.30649 0.00970  -0.02543 0.15528  247 VAL   A CG2 
1931 N  N   . ASP   A 248 ? 0.25647 0.42540 0.21675 -0.01009 -0.03264 0.11729  248 ASP   A N   
1932 C  CA  . ASP   A 248 ? 0.33413 0.50816 0.27164 -0.01735 -0.03339 0.10641  248 ASP   A CA  
1933 C  C   . ASP   A 248 ? 0.27495 0.43858 0.20482 -0.01806 -0.02676 0.09260  248 ASP   A C   
1934 O  O   . ASP   A 248 ? 0.32177 0.48460 0.23482 -0.02158 -0.02163 0.08674  248 ASP   A O   
1935 C  CB  . ASP   A 248 ? 0.32564 0.50867 0.26077 -0.02147 -0.04150 0.10219  248 ASP   A CB  
1936 C  CG  . ASP   A 248 ? 0.33989 0.53625 0.28067 -0.02181 -0.04833 0.11634  248 ASP   A CG  
1937 O  OD1 . ASP   A 248 ? 0.36252 0.56227 0.30276 -0.02051 -0.04709 0.12805  248 ASP   A OD1 
1938 O  OD2 . ASP   A 248 ? 0.32201 0.52616 0.26868 -0.02356 -0.05500 0.11640  248 ASP   A OD2 
1939 N  N   . ILE   A 249 ? 0.29210 0.44771 0.23439 -0.01446 -0.02611 0.08754  249 ILE   A N   
1940 C  CA  . ILE   A 249 ? 0.27393 0.42061 0.21084 -0.01485 -0.02021 0.07541  249 ILE   A CA  
1941 C  C   . ILE   A 249 ? 0.27597 0.41756 0.21175 -0.01324 -0.01181 0.07913  249 ILE   A C   
1942 O  O   . ILE   A 249 ? 0.30661 0.44510 0.23202 -0.01531 -0.00517 0.06975  249 ILE   A O   
1943 C  CB  . ILE   A 249 ? 0.25080 0.39066 0.20237 -0.01094 -0.02187 0.07173  249 ILE   A CB  
1944 C  CG1 . ILE   A 249 ? 0.32282 0.46757 0.27325 -0.01426 -0.02835 0.06460  249 ILE   A CG1 
1945 C  CG2 . ILE   A 249 ? 0.28110 0.41179 0.23123 -0.00992 -0.01553 0.06345  249 ILE   A CG2 
1946 C  CD1 . ILE   A 249 ? 0.31117 0.45275 0.28005 -0.00950 -0.03105 0.06641  249 ILE   A CD1 
1947 N  N   . LEU   A 250 ? 0.26303 0.40348 0.21066 -0.00976 -0.01116 0.09270  250 LEU   A N   
1948 C  CA  . LEU   A 250 ? 0.26021 0.39606 0.20953 -0.00911 -0.00335 0.09768  250 LEU   A CA  
1949 C  C   . LEU   A 250 ? 0.27606 0.41952 0.20931 -0.01309 -0.00018 0.09999  250 LEU   A C   
1950 O  O   . LEU   A 250 ? 0.28888 0.42994 0.22334 -0.01311 0.00701  0.10429  250 LEU   A O   
1951 C  CB  . LEU   A 250 ? 0.23456 0.36347 0.20393 -0.00448 -0.00373 0.11045  250 LEU   A CB  
1952 C  CG  . LEU   A 250 ? 0.18112 0.29861 0.16580 -0.00034 -0.00447 0.10759  250 LEU   A CG  
1953 C  CD1 . LEU   A 250 ? 0.18556 0.29448 0.18915 0.00420  -0.00514 0.11873  250 LEU   A CD1 
1954 C  CD2 . LEU   A 250 ? 0.22287 0.33290 0.20769 -0.00151 0.00206  0.10061  250 LEU   A CD2 
1955 N  N   . GLY   A 251 ? 0.32552 0.47785 0.24406 -0.01690 -0.00522 0.09724  251 GLY   A N   
1956 C  CA  . GLY   A 251 ? 0.32532 0.48468 0.22602 -0.02099 -0.00289 0.09948  251 GLY   A CA  
1957 C  C   . GLY   A 251 ? 0.31833 0.47374 0.20707 -0.02266 0.00816  0.09139  251 GLY   A C   
1958 O  O   . GLY   A 251 ? 0.34630 0.50332 0.23212 -0.02301 0.01405  0.09898  251 GLY   A O   
1959 N  N   . PRO   A 252 ? 0.32644 0.47677 0.20882 -0.02363 0.01186  0.07587  252 PRO   A N   
1960 C  CA  . PRO   A 252 ? 0.34906 0.49539 0.22308 -0.02411 0.02413  0.06762  252 PRO   A CA  
1961 C  C   . PRO   A 252 ? 0.32669 0.47010 0.21752 -0.02079 0.03167  0.07595  252 PRO   A C   
1962 O  O   . PRO   A 252 ? 0.33552 0.48042 0.22092 -0.02166 0.04059  0.07822  252 PRO   A O   
1963 C  CB  . PRO   A 252 ? 0.37563 0.51559 0.24746 -0.02426 0.02553  0.05084  252 PRO   A CB  
1964 C  CG  . PRO   A 252 ? 0.39293 0.53597 0.25936 -0.02718 0.01396  0.04829  252 PRO   A CG  
1965 C  CD  . PRO   A 252 ? 0.35280 0.50174 0.23284 -0.02512 0.00551  0.06465  252 PRO   A CD  
1966 N  N   . LEU   A 253 ? 0.31588 0.45472 0.22731 -0.01742 0.02855  0.08044  253 LEU   A N   
1967 C  CA  . LEU   A 253 ? 0.28292 0.41796 0.21227 -0.01541 0.03454  0.08829  253 LEU   A CA  
1968 C  C   . LEU   A 253 ? 0.29748 0.43552 0.22899 -0.01615 0.03418  0.10324  253 LEU   A C   
1969 O  O   . LEU   A 253 ? 0.26112 0.39893 0.19851 -0.01679 0.04189  0.10802  253 LEU   A O   
1970 C  CB  . LEU   A 253 ? 0.24909 0.37681 0.19796 -0.01246 0.03009  0.08979  253 LEU   A CB  
1971 C  CG  . LEU   A 253 ? 0.25116 0.37562 0.20295 -0.01151 0.03278  0.07687  253 LEU   A CG  
1972 C  CD1 . LEU   A 253 ? 0.22221 0.33517 0.19356 -0.00868 0.02650  0.07679  253 LEU   A CD1 
1973 C  CD2 . LEU   A 253 ? 0.25520 0.38045 0.21180 -0.01163 0.04389  0.07213  253 LEU   A CD2 
1974 N  N   . SER   A 254 ? 0.26970 0.41124 0.19840 -0.01606 0.02536  0.11111  254 SER   A N   
1975 C  CA  . SER   A 254 ? 0.29208 0.43765 0.22146 -0.01671 0.02464  0.12564  254 SER   A CA  
1976 C  C   . SER   A 254 ? 0.33346 0.48586 0.24304 -0.02045 0.03179  0.12469  254 SER   A C   
1977 O  O   . SER   A 254 ? 0.33075 0.48411 0.24374 -0.02125 0.03728  0.13433  254 SER   A O   
1978 C  CB  . SER   A 254 ? 0.31209 0.46240 0.24201 -0.01571 0.01395  0.13291  254 SER   A CB  
1979 O  OG  . SER   A 254 ? 0.33927 0.49208 0.27543 -0.01520 0.01291  0.14859  254 SER   A OG  
1980 N  N   . ALA   A 255 ? 0.34615 0.50243 0.23441 -0.02308 0.03205  0.11293  255 ALA   A N   
1981 C  CA  . ALA   A 255 ? 0.39409 0.55524 0.26049 -0.02665 0.03941  0.11089  255 ALA   A CA  
1982 C  C   . ALA   A 255 ? 0.39772 0.55497 0.26748 -0.02610 0.05328  0.10584  255 ALA   A C   
1983 O  O   . ALA   A 255 ? 0.40293 0.56356 0.26364 -0.02801 0.06146  0.11053  255 ALA   A O   
1984 C  CB  . ALA   A 255 ? 0.41817 0.58170 0.26111 -0.02992 0.03623  0.09790  255 ALA   A CB  
1985 N  N   . GLN   A 256 ? 0.34994 0.50100 0.23403 -0.02350 0.05627  0.09713  256 GLN   A N   
1986 C  CA  . GLN   A 256 ? 0.35338 0.50241 0.24513 -0.02263 0.06924  0.09246  256 GLN   A CA  
1987 C  C   . GLN   A 256 ? 0.33839 0.48812 0.24995 -0.02251 0.07197  0.10664  256 GLN   A C   
1988 O  O   . GLN   A 256 ? 0.39408 0.54672 0.30572 -0.02377 0.08260  0.10865  256 GLN   A O   
1989 C  CB  . GLN   A 256 ? 0.34554 0.48908 0.24868 -0.01984 0.07046  0.07997  256 GLN   A CB  
1990 C  CG  . GLN   A 256 ? 0.36343 0.50622 0.27595 -0.01832 0.08375  0.07330  256 GLN   A CG  
1991 C  CD  . GLN   A 256 ? 0.36524 0.50372 0.29542 -0.01506 0.08290  0.06501  256 GLN   A CD  
1992 O  OE1 . GLN   A 256 ? 0.40191 0.53717 0.33015 -0.01436 0.07403  0.06055  256 GLN   A OE1 
1993 N  NE2 . GLN   A 256 ? 0.41684 0.55615 0.36557 -0.01317 0.09167  0.06347  256 GLN   A NE2 
1994 N  N   . THR   A 257 ? 0.33522 0.48156 0.26384 -0.02126 0.06287  0.11646  257 THR   A N   
1995 C  CA  . THR   A 257 ? 0.30603 0.45021 0.25463 -0.02167 0.06448  0.12910  257 THR   A CA  
1996 C  C   . THR   A 257 ? 0.32292 0.47118 0.26508 -0.02347 0.06262  0.14349  257 THR   A C   
1997 O  O   . THR   A 257 ? 0.36169 0.50895 0.31716 -0.02475 0.06622  0.15377  257 THR   A O   
1998 C  CB  . THR   A 257 ? 0.28909 0.42423 0.25983 -0.01954 0.05682  0.13164  257 THR   A CB  
1999 O  OG1 . THR   A 257 ? 0.29997 0.43365 0.26538 -0.01774 0.04654  0.13381  257 THR   A OG1 
2000 C  CG2 . THR   A 257 ? 0.26107 0.39289 0.24064 -0.01821 0.05917  0.11928  257 THR   A CG2 
2001 N  N   . GLY   A 258 ? 0.32329 0.47651 0.24657 -0.02394 0.05664  0.14483  258 GLY   A N   
2002 C  CA  . GLY   A 258 ? 0.34315 0.50114 0.26204 -0.02524 0.05337  0.15980  258 GLY   A CA  
2003 C  C   . GLY   A 258 ? 0.33750 0.48984 0.27747 -0.02263 0.04503  0.17190  258 GLY   A C   
2004 O  O   . GLY   A 258 ? 0.35982 0.51455 0.30241 -0.02323 0.04375  0.18615  258 GLY   A O   
2005 N  N   . ILE   A 259 ? 0.31362 0.45764 0.26880 -0.01961 0.04005  0.16656  259 ILE   A N   
2006 C  CA  . ILE   A 259 ? 0.33044 0.46605 0.30614 -0.01660 0.03363  0.17582  259 ILE   A CA  
2007 C  C   . ILE   A 259 ? 0.31703 0.45514 0.28880 -0.01376 0.02409  0.17393  259 ILE   A C   
2008 O  O   . ILE   A 259 ? 0.28054 0.41739 0.24900 -0.01279 0.02180  0.16193  259 ILE   A O   
2009 C  CB  . ILE   A 259 ? 0.29615 0.41888 0.29293 -0.01575 0.03577  0.17139  259 ILE   A CB  
2010 C  CG1 . ILE   A 259 ? 0.34756 0.46942 0.35198 -0.01926 0.04433  0.17513  259 ILE   A CG1 
2011 C  CG2 . ILE   A 259 ? 0.25410 0.36527 0.26966 -0.01247 0.02975  0.17805  259 ILE   A CG2 
2012 C  CD1 . ILE   A 259 ? 0.35367 0.46727 0.37388 -0.02012 0.04697  0.16712  259 ILE   A CD1 
2013 N  N   . ALA   A 260 ? 0.30233 0.44493 0.27556 -0.01256 0.01870  0.18624  260 ALA   A N   
2014 C  CA  . ALA   A 260 ? 0.28438 0.43158 0.25695 -0.01001 0.00967  0.18609  260 ALA   A CA  
2015 C  C   . ALA   A 260 ? 0.26145 0.39683 0.25199 -0.00569 0.00713  0.18013  260 ALA   A C   
2016 O  O   . ALA   A 260 ? 0.26411 0.38628 0.27178 -0.00399 0.01048  0.18183  260 ALA   A O   
2017 C  CB  . ALA   A 260 ? 0.30372 0.45721 0.28087 -0.00881 0.00511  0.20263  260 ALA   A CB  
2018 N  N   . VAL   A 261 ? 0.25556 0.39521 0.24144 -0.00452 0.00130  0.17246  261 VAL   A N   
2019 C  CA  . VAL   A 261 ? 0.23519 0.36405 0.23579 -0.00048 -0.00049 0.16605  261 VAL   A CA  
2020 C  C   . VAL   A 261 ? 0.23440 0.35308 0.25695 0.00429  -0.00106 0.17649  261 VAL   A C   
2021 O  O   . VAL   A 261 ? 0.26427 0.36743 0.30082 0.00635  0.00209  0.17354  261 VAL   A O   
2022 C  CB  . VAL   A 261 ? 0.26128 0.39809 0.25430 -0.00025 -0.00694 0.15796  261 VAL   A CB  
2023 C  CG1 . VAL   A 261 ? 0.21189 0.33787 0.22122 0.00460  -0.00847 0.15345  261 VAL   A CG1 
2024 C  CG2 . VAL   A 261 ? 0.27311 0.41576 0.24532 -0.00502 -0.00533 0.14501  261 VAL   A CG2 
2025 N  N   . LEU   A 262 ? 0.27946 0.40608 0.30511 0.00573  -0.00473 0.18876  262 LEU   A N   
2026 C  CA  . LEU   A 262 ? 0.29846 0.41507 0.34556 0.01078  -0.00442 0.19885  262 LEU   A CA  
2027 C  C   . LEU   A 262 ? 0.26631 0.36970 0.32264 0.00970  0.00188  0.20395  262 LEU   A C   
2028 O  O   . LEU   A 262 ? 0.28294 0.37085 0.35757 0.01328  0.00392  0.20663  262 LEU   A O   
2029 C  CB  . LEU   A 262 ? 0.29451 0.42481 0.34305 0.01226  -0.00971 0.21224  262 LEU   A CB  
2030 C  CG  . LEU   A 262 ? 0.26660 0.40639 0.31596 0.01452  -0.01615 0.20880  262 LEU   A CG  
2031 C  CD1 . LEU   A 262 ? 0.33265 0.48377 0.39035 0.01685  -0.02082 0.22437  262 LEU   A CD1 
2032 C  CD2 . LEU   A 262 ? 0.31734 0.44295 0.38120 0.01954  -0.01439 0.19977  262 LEU   A CD2 
2033 N  N   . ASP   A 263 ? 0.27644 0.38492 0.32053 0.00448  0.00557  0.20455  263 ASP   A N   
2034 C  CA  . ASP   A 263 ? 0.30177 0.39832 0.35552 0.00232  0.01173  0.20814  263 ASP   A CA  
2035 C  C   . ASP   A 263 ? 0.26046 0.34173 0.32230 0.00181  0.01463  0.19567  263 ASP   A C   
2036 O  O   . ASP   A 263 ? 0.25851 0.32351 0.33620 0.00187  0.01728  0.19695  263 ASP   A O   
2037 C  CB  . ASP   A 263 ? 0.28635 0.39380 0.32519 -0.00314 0.01588  0.21177  263 ASP   A CB  
2038 C  CG  . ASP   A 263 ? 0.36232 0.48187 0.39505 -0.00352 0.01388  0.22692  263 ASP   A CG  
2039 O  OD1 . ASP   A 263 ? 0.35071 0.47250 0.39086 0.00042  0.00854  0.23491  263 ASP   A OD1 
2040 O  OD2 . ASP   A 263 ? 0.36885 0.49604 0.38972 -0.00784 0.01814  0.23128  263 ASP   A OD2 
2041 N  N   . MET   A 264 ? 0.23989 0.32574 0.29068 0.00076  0.01397  0.18335  264 MET   A N   
2042 C  CA  . MET   A 264 ? 0.22367 0.29610 0.28205 0.00016  0.01589  0.17224  264 MET   A CA  
2043 C  C   . MET   A 264 ? 0.24611 0.30393 0.31849 0.00510  0.01326  0.17009  264 MET   A C   
2044 O  O   . MET   A 264 ? 0.23754 0.27850 0.32096 0.00428  0.01533  0.16469  264 MET   A O   
2045 C  CB  . MET   A 264 ? 0.20916 0.29037 0.25290 -0.00155 0.01583  0.16050  264 MET   A CB  
2046 C  CG  . MET   A 264 ? 0.19405 0.26427 0.24464 -0.00332 0.01815  0.15017  264 MET   A CG  
2047 S  SD  . MET   A 264 ? 0.21477 0.28142 0.27411 -0.00932 0.02485  0.15307  264 MET   A SD  
2048 C  CE  . MET   A 264 ? 0.19754 0.28219 0.23910 -0.01198 0.02958  0.14700  264 MET   A CE  
2049 N  N   . CYS   A 265 ? 0.24428 0.30826 0.31673 0.00989  0.00901  0.17402  265 CYS   A N   
2050 C  CA  . CYS   A 265 ? 0.25670 0.30707 0.34363 0.01543  0.00821  0.17255  265 CYS   A CA  
2051 C  C   . CYS   A 265 ? 0.23691 0.27088 0.33967 0.01611  0.01181  0.17943  265 CYS   A C   
2052 O  O   . CYS   A 265 ? 0.25504 0.26982 0.36834 0.01772  0.01399  0.17286  265 CYS   A O   
2053 C  CB  . CYS   A 265 ? 0.23541 0.29837 0.32191 0.02018  0.00346  0.17723  265 CYS   A CB  
2054 S  SG  . CYS   A 265 ? 0.24013 0.31799 0.31124 0.01951  -0.00141 0.16656  265 CYS   A SG  
2055 N  N   . ALA   A 266 ? 0.26521 0.30569 0.36890 0.01453  0.01261  0.19223  266 ALA   A N   
2056 C  CA  . ALA   A 266 ? 0.27005 0.29459 0.38862 0.01428  0.01622  0.19915  266 ALA   A CA  
2057 C  C   . ALA   A 266 ? 0.27816 0.28686 0.40019 0.00867  0.01982  0.19008  266 ALA   A C   
2058 O  O   . ALA   A 266 ? 0.29100 0.27908 0.42557 0.00882  0.02211  0.18730  266 ALA   A O   
2059 C  CB  . ALA   A 266 ? 0.28841 0.32461 0.40553 0.01264  0.01645  0.21497  266 ALA   A CB  
2060 N  N   . SER   A 267 ? 0.25430 0.27230 0.36540 0.00335  0.02036  0.18466  267 SER   A N   
2061 C  CA  . SER   A 267 ? 0.25974 0.26548 0.37558 -0.00265 0.02294  0.17615  267 SER   A CA  
2062 C  C   . SER   A 267 ? 0.26353 0.25328 0.38319 -0.00120 0.02167  0.16273  267 SER   A C   
2063 O  O   . SER   A 267 ? 0.27742 0.24827 0.40639 -0.00454 0.02305  0.15729  267 SER   A O   
2064 C  CB  . SER   A 267 ? 0.27265 0.29390 0.37747 -0.00770 0.02441  0.17342  267 SER   A CB  
2065 O  OG  . SER   A 267 ? 0.32573 0.35777 0.42806 -0.01017 0.02717  0.18495  267 SER   A OG  
2066 N  N   . LEU   A 268 ? 0.25371 0.25055 0.36530 0.00317  0.01894  0.15682  268 LEU   A N   
2067 C  CA  . LEU   A 268 ? 0.22717 0.20921 0.34141 0.00523  0.01813  0.14459  268 LEU   A CA  
2068 C  C   . LEU   A 268 ? 0.27448 0.23745 0.40058 0.00952  0.01991  0.14511  268 LEU   A C   
2069 O  O   . LEU   A 268 ? 0.28047 0.22354 0.41088 0.00778  0.02128  0.13485  268 LEU   A O   
2070 C  CB  . LEU   A 268 ? 0.22882 0.22358 0.33304 0.00972  0.01505  0.14024  268 LEU   A CB  
2071 C  CG  . LEU   A 268 ? 0.22791 0.20992 0.33310 0.01240  0.01446  0.12781  268 LEU   A CG  
2072 C  CD1 . LEU   A 268 ? 0.23507 0.20226 0.34204 0.00563  0.01542  0.11757  268 LEU   A CD1 
2073 C  CD2 . LEU   A 268 ? 0.25309 0.25051 0.34778 0.01550  0.01118  0.12436  268 LEU   A CD2 
2074 N  N   . LYS   A 269 ? 0.25744 0.22622 0.38850 0.01485  0.02006  0.15665  269 LYS   A N   
2075 C  CA  . LYS   A 269 ? 0.30976 0.26095 0.45388 0.01943  0.02288  0.15880  269 LYS   A CA  
2076 C  C   . LYS   A 269 ? 0.29848 0.22875 0.44988 0.01338  0.02597  0.15629  269 LYS   A C   
2077 O  O   . LYS   A 269 ? 0.32620 0.23440 0.48277 0.01393  0.02841  0.14697  269 LYS   A O   
2078 C  CB  . LYS   A 269 ? 0.31815 0.28194 0.46792 0.02468  0.02218  0.17462  269 LYS   A CB  
2079 C  CG  . LYS   A 269 ? 0.38316 0.32975 0.54865 0.02986  0.02584  0.17923  269 LYS   A CG  
2080 C  CD  . LYS   A 269 ? 0.37622 0.33841 0.54828 0.03616  0.02421  0.19474  269 LYS   A CD  
2081 C  CE  . LYS   A 269 ? 0.47097 0.41564 0.66076 0.04211  0.02865  0.19988  269 LYS   A CE  
2082 N  NZ  . LYS   A 269 ? 0.48514 0.43892 0.68366 0.04368  0.02802  0.21904  269 LYS   A NZ  
2083 N  N   . GLU   A 270 ? 0.31614 0.25320 0.46730 0.00706  0.02609  0.16406  270 GLU   A N   
2084 C  CA  . GLU   A 270 ? 0.33343 0.25254 0.49226 0.00001  0.02848  0.16255  270 GLU   A CA  
2085 C  C   . GLU   A 270 ? 0.35252 0.25862 0.50776 -0.00642 0.02764  0.14608  270 GLU   A C   
2086 O  O   . GLU   A 270 ? 0.38350 0.26693 0.54401 -0.01012 0.02907  0.13875  270 GLU   A O   
2087 C  CB  . GLU   A 270 ? 0.36570 0.29840 0.52472 -0.00559 0.02906  0.17442  270 GLU   A CB  
2088 C  CG  . GLU   A 270 ? 0.40448 0.34561 0.56826 -0.00082 0.02996  0.19148  270 GLU   A CG  
2089 C  CD  . GLU   A 270 ? 0.47371 0.39429 0.65091 0.00368  0.03228  0.19461  270 GLU   A CD  
2090 O  OE1 . GLU   A 270 ? 0.53601 0.43425 0.72026 -0.00111 0.03453  0.18823  270 GLU   A OE1 
2091 O  OE2 . GLU   A 270 ? 0.48227 0.40897 0.66311 0.01175  0.03182  0.20295  270 GLU   A OE2 
2092 N  N   . LEU   A 271 ? 0.30448 0.22447 0.45014 -0.00822 0.02506  0.13987  271 LEU   A N   
2093 C  CA  . LEU   A 271 ? 0.31615 0.22643 0.45864 -0.01473 0.02334  0.12512  271 LEU   A CA  
2094 C  C   . LEU   A 271 ? 0.36036 0.25070 0.50149 -0.01098 0.02379  0.11287  271 LEU   A C   
2095 O  O   . LEU   A 271 ? 0.37627 0.24904 0.51662 -0.01738 0.02317  0.10100  271 LEU   A O   
2096 C  CB  . LEU   A 271 ? 0.28208 0.21235 0.41578 -0.01614 0.02086  0.12242  271 LEU   A CB  
2097 C  CG  . LEU   A 271 ? 0.27496 0.22269 0.40911 -0.02195 0.02146  0.12977  271 LEU   A CG  
2098 C  CD1 . LEU   A 271 ? 0.24077 0.20845 0.36519 -0.02098 0.02029  0.12757  271 LEU   A CD1 
2099 C  CD2 . LEU   A 271 ? 0.34773 0.28573 0.48966 -0.03195 0.02096  0.12473  271 LEU   A CD2 
2100 N  N   . LEU   A 272 ? 0.32328 0.21706 0.46349 -0.00100 0.02489  0.11524  272 LEU   A N   
2101 C  CA  . LEU   A 272 ? 0.33522 0.21129 0.47466 0.00382  0.02693  0.10400  272 LEU   A CA  
2102 C  C   . LEU   A 272 ? 0.37467 0.22670 0.52218 0.00342  0.03080  0.10281  272 LEU   A C   
2103 O  O   . LEU   A 272 ? 0.42478 0.25577 0.56884 0.00127  0.03236  0.08900  272 LEU   A O   
2104 C  CB  . LEU   A 272 ? 0.29931 0.18835 0.43832 0.01460  0.02742  0.10831  272 LEU   A CB  
2105 C  CG  . LEU   A 272 ? 0.27026 0.17817 0.39935 0.01507  0.02375  0.10554  272 LEU   A CG  
2106 C  CD1 . LEU   A 272 ? 0.32840 0.25241 0.45813 0.02438  0.02326  0.11237  272 LEU   A CD1 
2107 C  CD2 . LEU   A 272 ? 0.32869 0.22453 0.45059 0.01171  0.02329  0.08912  272 LEU   A CD2 
2108 N  N   . GLN   A 273 ? 0.40073 0.25501 0.55795 0.00496  0.03242  0.11689  273 GLN   A N   
2109 C  CA  . GLN   A 273 ? 0.43488 0.26600 0.60137 0.00580  0.03660  0.11738  273 GLN   A CA  
2110 C  C   . GLN   A 273 ? 0.46609 0.28028 0.63293 -0.00606 0.03603  0.11211  273 GLN   A C   
2111 O  O   . GLN   A 273 ? 0.49790 0.28681 0.66778 -0.00769 0.03897  0.10548  273 GLN   A O   
2112 C  CB  . GLN   A 273 ? 0.42355 0.26367 0.60168 0.01241  0.03842  0.13573  273 GLN   A CB  
2113 C  CG  . GLN   A 273 ? 0.41395 0.26674 0.59524 0.02414  0.03929  0.14118  273 GLN   A CG  
2114 C  CD  . GLN   A 273 ? 0.46550 0.33513 0.65574 0.02863  0.03867  0.16111  273 GLN   A CD  
2115 O  OE1 . GLN   A 273 ? 0.48548 0.36545 0.68138 0.03743  0.03901  0.16803  273 GLN   A OE1 
2116 N  NE2 . GLN   A 273 ? 0.51654 0.38959 0.70846 0.02219  0.03773  0.17076  273 GLN   A NE2 
2117 N  N   . ASN   A 274 ? 0.43765 0.26556 0.60184 -0.01461 0.03246  0.11491  274 ASN   A N   
2118 C  CA  . ASN   A 274 ? 0.46716 0.28331 0.63380 -0.02672 0.03142  0.11186  274 ASN   A CA  
2119 C  C   . ASN   A 274 ? 0.48125 0.29805 0.63895 -0.03635 0.02700  0.09793  274 ASN   A C   
2120 O  O   . ASN   A 274 ? 0.52282 0.32891 0.68202 -0.04748 0.02532  0.09316  274 ASN   A O   
2121 C  CB  . ASN   A 274 ? 0.47927 0.31162 0.65377 -0.03002 0.03160  0.12830  274 ASN   A CB  
2122 C  CG  . ASN   A 274 ? 0.52605 0.36405 0.70825 -0.02070 0.03473  0.14436  274 ASN   A CG  
2123 O  OD1 . ASN   A 274 ? 0.50998 0.33257 0.69707 -0.01382 0.03763  0.14418  274 ASN   A OD1 
2124 N  ND2 . ASN   A 274 ? 0.53963 0.40050 0.72290 -0.02051 0.03431  0.15850  274 ASN   A ND2 
2125 N  N   . GLY   A 275 ? 0.46026 0.28983 0.60939 -0.03295 0.02470  0.09181  275 GLY   A N   
2126 C  CA  . GLY   A 275 ? 0.47450 0.30977 0.61730 -0.04214 0.01987  0.08170  275 GLY   A CA  
2127 C  C   . GLY   A 275 ? 0.49018 0.34724 0.63917 -0.04793 0.01817  0.09186  275 GLY   A C   
2128 O  O   . GLY   A 275 ? 0.48633 0.35644 0.64095 -0.04378 0.02080  0.10616  275 GLY   A O   
2129 N  N   . MET   A 276 ? 0.52774 0.38969 0.67546 -0.05773 0.01375  0.08422  276 MET   A N   
2130 C  CA  . MET   A 276 ? 0.49251 0.37781 0.64664 -0.06229 0.01261  0.09234  276 MET   A CA  
2131 C  C   . MET   A 276 ? 0.52642 0.40687 0.68999 -0.07358 0.01179  0.09402  276 MET   A C   
2132 O  O   . MET   A 276 ? 0.48057 0.38030 0.65161 -0.07735 0.01183  0.10146  276 MET   A O   
2133 C  CB  . MET   A 276 ? 0.46399 0.36515 0.61271 -0.06336 0.00826  0.08499  276 MET   A CB  
2134 C  CG  . MET   A 276 ? 0.46061 0.36945 0.60110 -0.05234 0.00968  0.08588  276 MET   A CG  
2135 S  SD  . MET   A 276 ? 0.60636 0.53478 0.74099 -0.05178 0.00574  0.08004  276 MET   A SD  
2136 C  CE  . MET   A 276 ? 0.34946 0.29643 0.49451 -0.06041 0.00441  0.08466  276 MET   A CE  
2137 N  N   . ASN   A 277 ? 0.53531 0.39018 0.69869 -0.07887 0.01173  0.08747  277 ASN   A N   
2138 C  CA  . ASN   A 277 ? 0.52565 0.37231 0.69818 -0.09003 0.01143  0.08965  277 ASN   A CA  
2139 C  C   . ASN   A 277 ? 0.49625 0.36021 0.67378 -0.10041 0.00639  0.08667  277 ASN   A C   
2140 O  O   . ASN   A 277 ? 0.52345 0.39787 0.71293 -0.10629 0.00728  0.09555  277 ASN   A O   
2141 C  CB  . ASN   A 277 ? 0.52334 0.37389 0.70643 -0.08663 0.01686  0.10660  277 ASN   A CB  
2142 C  CG  . ASN   A 277 ? 0.58995 0.42436 0.77101 -0.07636 0.02129  0.11092  277 ASN   A CG  
2143 O  OD1 . ASN   A 277 ? 0.66100 0.46915 0.83892 -0.07731 0.02184  0.10244  277 ASN   A OD1 
2144 N  ND2 . ASN   A 277 ? 0.57262 0.42334 0.75527 -0.06651 0.02451  0.12419  277 ASN   A ND2 
2145 N  N   . GLY   A 278 ? 0.47366 0.34168 0.64288 -0.10237 0.00104  0.07463  278 GLY   A N   
2146 C  CA  . GLY   A 278 ? 0.49065 0.37500 0.66528 -0.11183 -0.00485 0.07101  278 GLY   A CA  
2147 C  C   . GLY   A 278 ? 0.46772 0.38316 0.65025 -0.10731 -0.00443 0.08044  278 GLY   A C   
2148 O  O   . GLY   A 278 ? 0.50544 0.43672 0.69603 -0.11407 -0.00868 0.07982  278 GLY   A O   
2149 N  N   . ARG   A 279 ? 0.42605 0.35091 0.60633 -0.09612 0.00080  0.08903  279 ARG   A N   
2150 C  CA  . ARG   A 279 ? 0.39052 0.34283 0.57496 -0.09125 0.00273  0.09664  279 ARG   A CA  
2151 C  C   . ARG   A 279 ? 0.35888 0.31799 0.53291 -0.08451 0.00034  0.08969  279 ARG   A C   
2152 O  O   . ARG   A 279 ? 0.37367 0.31698 0.53755 -0.08301 -0.00237 0.08025  279 ARG   A O   
2153 C  CB  . ARG   A 279 ? 0.37766 0.33723 0.56456 -0.08473 0.01051  0.11103  279 ARG   A CB  
2154 C  CG  . ARG   A 279 ? 0.42839 0.37963 0.62571 -0.09127 0.01309  0.11884  279 ARG   A CG  
2155 C  CD  . ARG   A 279 ? 0.42445 0.37873 0.62141 -0.08447 0.02004  0.13279  279 ARG   A CD  
2156 N  NE  . ARG   A 279 ? 0.47629 0.40912 0.66690 -0.07941 0.02073  0.13211  279 ARG   A NE  
2157 C  CZ  . ARG   A 279 ? 0.42411 0.35362 0.61542 -0.07427 0.02531  0.14380  279 ARG   A CZ  
2158 N  NH1 . ARG   A 279 ? 0.44747 0.39146 0.64436 -0.07492 0.02969  0.15702  279 ARG   A NH1 
2159 N  NH2 . ARG   A 279 ? 0.42694 0.33884 0.61343 -0.06806 0.02565  0.14249  279 ARG   A NH2 
2160 N  N   . THR   A 280 ? 0.33431 0.31666 0.51094 -0.08062 0.00194  0.09402  280 THR   A N   
2161 C  CA  . THR   A 280 ? 0.28185 0.27252 0.45016 -0.07468 0.00012  0.08841  280 THR   A CA  
2162 C  C   . THR   A 280 ? 0.23255 0.23876 0.39730 -0.06584 0.00730  0.09697  280 THR   A C   
2163 O  O   . THR   A 280 ? 0.21782 0.23305 0.38717 -0.06505 0.01318  0.10689  280 THR   A O   
2164 C  CB  . THR   A 280 ? 0.27781 0.28153 0.45143 -0.07915 -0.00600 0.08243  280 THR   A CB  
2165 O  OG1 . THR   A 280 ? 0.28063 0.30398 0.46683 -0.08002 -0.00245 0.09058  280 THR   A OG1 
2166 C  CG2 . THR   A 280 ? 0.31161 0.30097 0.48530 -0.08896 -0.01388 0.07326  280 THR   A CG2 
2167 N  N   . ILE   A 281 ? 0.21536 0.22407 0.37029 -0.05967 0.00689  0.09264  281 ILE   A N   
2168 C  CA  . ILE   A 281 ? 0.18027 0.20399 0.32851 -0.05203 0.01301  0.09801  281 ILE   A CA  
2169 C  C   . ILE   A 281 ? 0.20669 0.24203 0.35371 -0.05031 0.01084  0.09087  281 ILE   A C   
2170 O  O   . ILE   A 281 ? 0.17765 0.20443 0.32017 -0.05057 0.00522  0.08267  281 ILE   A O   
2171 C  CB  . ILE   A 281 ? 0.17226 0.18675 0.30873 -0.04550 0.01490  0.10065  281 ILE   A CB  
2172 C  CG1 . ILE   A 281 ? 0.21865 0.21995 0.35769 -0.04612 0.01651  0.10774  281 ILE   A CG1 
2173 C  CG2 . ILE   A 281 ? 0.15836 0.18969 0.28493 -0.03893 0.02020  0.10472  281 ILE   A CG2 
2174 C  CD1 . ILE   A 281 ? 0.23300 0.22677 0.36264 -0.03834 0.01793  0.11190  281 ILE   A CD1 
2175 N  N   . LEU   A 282 ? 0.20306 0.25705 0.35388 -0.04813 0.01578  0.09367  282 LEU   A N   
2176 C  CA  . LEU   A 282 ? 0.18657 0.25210 0.33815 -0.04524 0.01484  0.08737  282 LEU   A CA  
2177 C  C   . LEU   A 282 ? 0.21497 0.27448 0.37258 -0.05045 0.00487  0.07980  282 LEU   A C   
2178 O  O   . LEU   A 282 ? 0.18756 0.24641 0.34034 -0.04846 0.00061  0.07294  282 LEU   A O   
2179 C  CB  . LEU   A 282 ? 0.14682 0.21387 0.28434 -0.03841 0.01760  0.08437  282 LEU   A CB  
2180 C  CG  . LEU   A 282 ? 0.18645 0.26457 0.31516 -0.03335 0.02739  0.09030  282 LEU   A CG  
2181 C  CD1 . LEU   A 282 ? 0.18117 0.25732 0.28968 -0.02618 0.02758  0.08409  282 LEU   A CD1 
2182 C  CD2 . LEU   A 282 ? 0.19865 0.29213 0.33408 -0.03174 0.03379  0.09050  282 LEU   A CD2 
2183 N  N   . GLY   A 283 ? 0.21679 0.27173 0.38358 -0.05769 0.00083  0.08106  283 GLY   A N   
2184 C  CA  . GLY   A 283 ? 0.23849 0.28893 0.40870 -0.06395 -0.00906 0.07418  283 GLY   A CA  
2185 C  C   . GLY   A 283 ? 0.27138 0.30250 0.42963 -0.06652 -0.01548 0.06563  283 GLY   A C   
2186 O  O   . GLY   A 283 ? 0.30081 0.32947 0.45644 -0.07053 -0.02369 0.05839  283 GLY   A O   
2187 N  N   . SER   A 284 ? 0.22174 0.23909 0.37169 -0.06379 -0.01166 0.06647  284 SER   A N   
2188 C  CA  . SER   A 284 ? 0.21459 0.21134 0.35325 -0.06494 -0.01577 0.05813  284 SER   A CA  
2189 C  C   . SER   A 284 ? 0.26204 0.24025 0.40085 -0.06781 -0.01336 0.05981  284 SER   A C   
2190 O  O   . SER   A 284 ? 0.23925 0.22051 0.38344 -0.06557 -0.00713 0.06951  284 SER   A O   
2191 C  CB  . SER   A 284 ? 0.23735 0.23335 0.36304 -0.05529 -0.01271 0.05571  284 SER   A CB  
2192 O  OG  . SER   A 284 ? 0.26465 0.24111 0.37776 -0.05412 -0.01509 0.04677  284 SER   A OG  
2193 N  N   . ALA   A 285 ? 0.25998 0.21885 0.39200 -0.07287 -0.01789 0.05010  285 ALA   A N   
2194 C  CA  . ALA   A 285 ? 0.30421 0.24166 0.43508 -0.07461 -0.01472 0.04969  285 ALA   A CA  
2195 C  C   . ALA   A 285 ? 0.29986 0.22033 0.42031 -0.06691 -0.01134 0.04575  285 ALA   A C   
2196 O  O   . ALA   A 285 ? 0.36197 0.26173 0.48000 -0.06707 -0.00845 0.04316  285 ALA   A O   
2197 C  CB  . ALA   A 285 ? 0.33890 0.26418 0.46870 -0.08575 -0.02006 0.04080  285 ALA   A CB  
2198 N  N   . LEU   A 286 ? 0.27231 0.20114 0.38739 -0.05996 -0.01122 0.04530  286 LEU   A N   
2199 C  CA  . LEU   A 286 ? 0.29064 0.20952 0.39606 -0.05003 -0.00704 0.04291  286 LEU   A CA  
2200 C  C   . LEU   A 286 ? 0.27725 0.21494 0.38154 -0.04054 -0.00287 0.05245  286 LEU   A C   
2201 O  O   . LEU   A 286 ? 0.23016 0.18749 0.33709 -0.04123 -0.00342 0.05675  286 LEU   A O   
2202 C  CB  . LEU   A 286 ? 0.33200 0.24612 0.42224 -0.04849 -0.01051 0.02894  286 LEU   A CB  
2203 C  CG  . LEU   A 286 ? 0.38389 0.27899 0.46825 -0.05764 -0.01489 0.01653  286 LEU   A CG  
2204 C  CD1 . LEU   A 286 ? 0.35180 0.25066 0.41992 -0.05599 -0.01858 0.00571  286 LEU   A CD1 
2205 C  CD2 . LEU   A 286 ? 0.42100 0.28948 0.50542 -0.05609 -0.00898 0.01353  286 LEU   A CD2 
2206 N  N   . LEU   A 287 ? 0.25199 0.18382 0.35230 -0.03168 0.00138  0.05533  287 LEU   A N   
2207 C  CA  . LEU   A 287 ? 0.24761 0.19702 0.34385 -0.02349 0.00389  0.06289  287 LEU   A CA  
2208 C  C   . LEU   A 287 ? 0.20974 0.16914 0.29425 -0.01979 0.00121  0.05341  287 LEU   A C   
2209 O  O   . LEU   A 287 ? 0.25143 0.20121 0.32919 -0.01675 0.00063  0.04490  287 LEU   A O   
2210 C  CB  . LEU   A 287 ? 0.24270 0.18435 0.34122 -0.01590 0.00803  0.07104  287 LEU   A CB  
2211 C  CG  . LEU   A 287 ? 0.23984 0.16948 0.35095 -0.01950 0.01095  0.08133  287 LEU   A CG  
2212 C  CD1 . LEU   A 287 ? 0.31383 0.23540 0.42701 -0.01101 0.01449  0.08704  287 LEU   A CD1 
2213 C  CD2 . LEU   A 287 ? 0.28792 0.23571 0.40235 -0.02316 0.01182  0.09175  287 LEU   A CD2 
2214 N  N   . GLU   A 288 ? 0.17007 0.14803 0.25269 -0.02002 0.00052  0.05499  288 GLU   A N   
2215 C  CA  . GLU   A 288 ? 0.19393 0.18106 0.26785 -0.01783 -0.00203 0.04679  288 GLU   A CA  
2216 C  C   . GLU   A 288 ? 0.16738 0.16209 0.23314 -0.01010 -0.00017 0.04820  288 GLU   A C   
2217 O  O   . GLU   A 288 ? 0.15004 0.15451 0.21575 -0.00780 0.00251  0.05668  288 GLU   A O   
2218 C  CB  . GLU   A 288 ? 0.18046 0.18260 0.25903 -0.02136 -0.00246 0.04831  288 GLU   A CB  
2219 C  CG  . GLU   A 288 ? 0.27582 0.28750 0.34846 -0.01912 -0.00442 0.04156  288 GLU   A CG  
2220 C  CD  . GLU   A 288 ? 0.30923 0.31211 0.37735 -0.02117 -0.00976 0.03242  288 GLU   A CD  
2221 O  OE1 . GLU   A 288 ? 0.35467 0.35092 0.42792 -0.02790 -0.01359 0.03062  288 GLU   A OE1 
2222 O  OE2 . GLU   A 288 ? 0.25616 0.25959 0.31517 -0.01689 -0.01033 0.02730  288 GLU   A OE2 
2223 N  N   . ASP   A 289 ? 0.17018 0.16193 0.22856 -0.00690 -0.00183 0.04026  289 ASP   A N   
2224 C  CA  . ASP   A 289 ? 0.17568 0.17543 0.22838 -0.00066 -0.00083 0.04185  289 ASP   A CA  
2225 C  C   . ASP   A 289 ? 0.16329 0.17201 0.20853 0.00004  -0.00276 0.03482  289 ASP   A C   
2226 O  O   . ASP   A 289 ? 0.16299 0.17666 0.20380 0.00397  -0.00280 0.03419  289 ASP   A O   
2227 C  CB  . ASP   A 289 ? 0.19333 0.18222 0.24753 0.00411  0.00073  0.04209  289 ASP   A CB  
2228 C  CG  . ASP   A 289 ? 0.20281 0.18285 0.25171 0.00450  0.00014  0.03128  289 ASP   A CG  
2229 O  OD1 . ASP   A 289 ? 0.19717 0.17568 0.24184 -0.00035 -0.00258 0.02424  289 ASP   A OD1 
2230 O  OD2 . ASP   A 289 ? 0.22185 0.19763 0.27140 0.00996  0.00271  0.03091  289 ASP   A OD2 
2231 N  N   . GLU   A 290 ? 0.16294 0.17464 0.20843 -0.00372 -0.00442 0.03054  290 GLU   A N   
2232 C  CA  . GLU   A 290 ? 0.15645 0.17461 0.19649 -0.00268 -0.00579 0.02481  290 GLU   A CA  
2233 C  C   . GLU   A 290 ? 0.18925 0.21940 0.22946 -0.00270 -0.00369 0.02642  290 GLU   A C   
2234 O  O   . GLU   A 290 ? 0.18094 0.21452 0.22035 -0.00275 -0.00429 0.02189  290 GLU   A O   
2235 C  CB  . GLU   A 290 ? 0.20655 0.21842 0.24606 -0.00571 -0.00932 0.01856  290 GLU   A CB  
2236 C  CG  . GLU   A 290 ? 0.25180 0.25041 0.28713 -0.00575 -0.00999 0.01460  290 GLU   A CG  
2237 C  CD  . GLU   A 290 ? 0.25174 0.24733 0.27953 -0.00669 -0.01256 0.00781  290 GLU   A CD  
2238 O  OE1 . GLU   A 290 ? 0.23100 0.21766 0.25292 -0.00528 -0.01099 0.00388  290 GLU   A OE1 
2239 O  OE2 . GLU   A 290 ? 0.21472 0.21684 0.24298 -0.00854 -0.01545 0.00707  290 GLU   A OE2 
2240 N  N   . PHE   A 291 ? 0.14407 0.18020 0.18461 -0.00232 -0.00053 0.03297  291 PHE   A N   
2241 C  CA  . PHE   A 291 ? 0.15142 0.19864 0.18784 -0.00187 0.00304  0.03355  291 PHE   A CA  
2242 C  C   . PHE   A 291 ? 0.14136 0.19427 0.16851 0.00004  0.00328  0.03680  291 PHE   A C   
2243 O  O   . PHE   A 291 ? 0.13822 0.19119 0.16650 0.00051  0.00342  0.04500  291 PHE   A O   
2244 C  CB  . PHE   A 291 ? 0.17544 0.22761 0.21877 -0.00420 0.00720  0.03933  291 PHE   A CB  
2245 C  CG  . PHE   A 291 ? 0.16945 0.22024 0.22434 -0.00681 0.00638  0.03761  291 PHE   A CG  
2246 C  CD1 . PHE   A 291 ? 0.22995 0.28618 0.28768 -0.00577 0.00795  0.03294  291 PHE   A CD1 
2247 C  CD2 . PHE   A 291 ? 0.17896 0.22299 0.24284 -0.01060 0.00371  0.04100  291 PHE   A CD2 
2248 C  CE1 . PHE   A 291 ? 0.23013 0.28781 0.30090 -0.00800 0.00620  0.03332  291 PHE   A CE1 
2249 C  CE2 . PHE   A 291 ? 0.22909 0.27422 0.30410 -0.01428 0.00137  0.04010  291 PHE   A CE2 
2250 C  CZ  . PHE   A 291 ? 0.22720 0.28052 0.30625 -0.01271 0.00230  0.03707  291 PHE   A CZ  
2251 N  N   . THR   A 292 ? 0.13836 0.19658 0.15702 0.00058  0.00309  0.03122  292 THR   A N   
2252 C  CA  . THR   A 292 ? 0.17416 0.24037 0.18317 0.00080  0.00198  0.03426  292 THR   A CA  
2253 C  C   . THR   A 292 ? 0.16320 0.23826 0.16481 -0.00093 0.00643  0.03824  292 THR   A C   
2254 O  O   . THR   A 292 ? 0.16723 0.24278 0.17159 -0.00173 0.01161  0.03673  292 THR   A O   
2255 C  CB  . THR   A 292 ? 0.18431 0.25258 0.18644 0.00026  -0.00032 0.02612  292 THR   A CB  
2256 O  OG1 . THR   A 292 ? 0.18024 0.24918 0.17827 -0.00112 0.00378  0.01887  292 THR   A OG1 
2257 C  CG2 . THR   A 292 ? 0.15544 0.21586 0.16412 0.00172  -0.00342 0.02237  292 THR   A CG2 
2258 N  N   . PRO   A 293 ? 0.16508 0.24869 0.15715 -0.00164 0.00471  0.04390  293 PRO   A N   
2259 C  CA  . PRO   A 293 ? 0.15650 0.24942 0.13686 -0.00406 0.00944  0.04651  293 PRO   A CA  
2260 C  C   . PRO   A 293 ? 0.20755 0.30096 0.17986 -0.00552 0.01437  0.03445  293 PRO   A C   
2261 O  O   . PRO   A 293 ? 0.20655 0.30290 0.17666 -0.00606 0.02197  0.03412  293 PRO   A O   
2262 C  CB  . PRO   A 293 ? 0.20189 0.30463 0.17187 -0.00518 0.00414  0.05386  293 PRO   A CB  
2263 C  CG  . PRO   A 293 ? 0.18398 0.28157 0.16766 -0.00165 -0.00104 0.06091  293 PRO   A CG  
2264 C  CD  . PRO   A 293 ? 0.17307 0.25932 0.16624 -0.00006 -0.00117 0.05073  293 PRO   A CD  
2265 N  N   . PHE   A 294 ? 0.21350 0.30299 0.18377 -0.00580 0.01120  0.02465  294 PHE   A N   
2266 C  CA  . PHE   A 294 ? 0.24786 0.33451 0.21296 -0.00659 0.01647  0.01288  294 PHE   A CA  
2267 C  C   . PHE   A 294 ? 0.23943 0.32066 0.21870 -0.00369 0.02232  0.01145  294 PHE   A C   
2268 O  O   . PHE   A 294 ? 0.26102 0.34357 0.23816 -0.00318 0.03048  0.00679  294 PHE   A O   
2269 C  CB  . PHE   A 294 ? 0.25999 0.34183 0.22329 -0.00781 0.01147  0.00416  294 PHE   A CB  
2270 C  CG  . PHE   A 294 ? 0.36376 0.43804 0.32766 -0.00746 0.01688  -0.00736 294 PHE   A CG  
2271 C  CD1 . PHE   A 294 ? 0.40068 0.47521 0.34952 -0.01078 0.02050  -0.01677 294 PHE   A CD1 
2272 C  CD2 . PHE   A 294 ? 0.38164 0.44798 0.36109 -0.00400 0.01805  -0.00865 294 PHE   A CD2 
2273 C  CE1 . PHE   A 294 ? 0.43418 0.49942 0.38526 -0.00969 0.02662  -0.02743 294 PHE   A CE1 
2274 C  CE2 . PHE   A 294 ? 0.40146 0.46081 0.38407 -0.00272 0.02314  -0.01737 294 PHE   A CE2 
2275 C  CZ  . PHE   A 294 ? 0.42504 0.48289 0.39432 -0.00512 0.02799  -0.02691 294 PHE   A CZ  
2276 N  N   . ASP   A 295 ? 0.18631 0.26185 0.18027 -0.00190 0.01834  0.01507  295 ASP   A N   
2277 C  CA  . ASP   A 295 ? 0.17457 0.24710 0.18324 -0.00018 0.02169  0.01514  295 ASP   A CA  
2278 C  C   . ASP   A 295 ? 0.22572 0.30529 0.23782 -0.00055 0.02858  0.02147  295 ASP   A C   
2279 O  O   . ASP   A 295 ? 0.21023 0.29199 0.23081 0.00091  0.03497  0.01947  295 ASP   A O   
2280 C  CB  . ASP   A 295 ? 0.16924 0.23530 0.18933 0.00004  0.01526  0.01861  295 ASP   A CB  
2281 C  CG  . ASP   A 295 ? 0.21949 0.27925 0.23757 0.00055  0.00982  0.01304  295 ASP   A CG  
2282 O  OD1 . ASP   A 295 ? 0.26087 0.32029 0.27271 0.00062  0.01099  0.00618  295 ASP   A OD1 
2283 O  OD2 . ASP   A 295 ? 0.18675 0.24138 0.20912 0.00052  0.00501  0.01541  295 ASP   A OD2 
2284 N  N   . VAL   A 296 ? 0.16170 0.24546 0.16925 -0.00222 0.02774  0.03036  296 VAL   A N   
2285 C  CA  . VAL   A 296 ? 0.17095 0.26181 0.18225 -0.00328 0.03458  0.03819  296 VAL   A CA  
2286 C  C   . VAL   A 296 ? 0.19257 0.29100 0.19139 -0.00314 0.04391  0.03351  296 VAL   A C   
2287 O  O   . VAL   A 296 ? 0.20334 0.30650 0.21008 -0.00218 0.05261  0.03383  296 VAL   A O   
2288 C  CB  . VAL   A 296 ? 0.17838 0.27078 0.18760 -0.00506 0.03150  0.05011  296 VAL   A CB  
2289 C  CG1 . VAL   A 296 ? 0.18278 0.28380 0.19342 -0.00687 0.03961  0.05912  296 VAL   A CG1 
2290 C  CG2 . VAL   A 296 ? 0.14423 0.22681 0.16745 -0.00513 0.02482  0.05356  296 VAL   A CG2 
2291 N  N   . VAL   A 297 ? 0.22288 0.32280 0.20220 -0.00438 0.04248  0.02854  297 VAL   A N   
2292 C  CA  . VAL   A 297 ? 0.25058 0.35578 0.21375 -0.00519 0.05154  0.02172  297 VAL   A CA  
2293 C  C   . VAL   A 297 ? 0.27588 0.37564 0.24745 -0.00190 0.05845  0.01047  297 VAL   A C   
2294 O  O   . VAL   A 297 ? 0.31015 0.41413 0.28136 -0.00036 0.07005  0.00786  297 VAL   A O   
2295 C  CB  . VAL   A 297 ? 0.26207 0.36934 0.20223 -0.00875 0.04631  0.01752  297 VAL   A CB  
2296 C  CG1 . VAL   A 297 ? 0.29198 0.40159 0.21280 -0.01053 0.05563  0.00675  297 VAL   A CG1 
2297 C  CG2 . VAL   A 297 ? 0.30855 0.42404 0.24154 -0.01123 0.04068  0.03127  297 VAL   A CG2 
2298 N  N   . ARG   A 298 ? 0.28362 0.37418 0.26407 -0.00031 0.05215  0.00458  298 ARG   A N   
2299 C  CA  . ARG   A 298 ? 0.34673 0.43140 0.33735 0.00341  0.05800  -0.00430 298 ARG   A CA  
2300 C  C   . ARG   A 298 ? 0.32976 0.41970 0.34118 0.00675  0.06485  0.00170  298 ARG   A C   
2301 O  O   . ARG   A 298 ? 0.36006 0.45167 0.37611 0.01017  0.07595  -0.00310 298 ARG   A O   
2302 C  CB  . ARG   A 298 ? 0.32049 0.39538 0.31881 0.00415  0.04902  -0.00815 298 ARG   A CB  
2303 C  CG  . ARG   A 298 ? 0.41008 0.48042 0.42815 0.00881  0.05256  -0.01062 298 ARG   A CG  
2304 C  CD  . ARG   A 298 ? 0.43984 0.50003 0.46255 0.00938  0.04532  -0.01498 298 ARG   A CD  
2305 N  NE  . ARG   A 298 ? 0.45067 0.51029 0.48275 0.00845  0.03533  -0.00763 298 ARG   A NE  
2306 C  CZ  . ARG   A 298 ? 0.33936 0.39636 0.38730 0.01052  0.03197  -0.00497 298 ARG   A CZ  
2307 N  NH1 . ARG   A 298 ? 0.35229 0.40777 0.41248 0.01463  0.03742  -0.00718 298 ARG   A NH1 
2308 N  NH2 . ARG   A 298 ? 0.33224 0.38816 0.38375 0.00851  0.02312  0.00030  298 ARG   A NH2 
2309 N  N   . GLN   A 299 ? 0.25968 0.35243 0.28470 0.00557  0.05869  0.01214  299 GLN   A N   
2310 C  CA  . GLN   A 299 ? 0.26019 0.35884 0.30807 0.00729  0.06253  0.01850  299 GLN   A CA  
2311 C  C   . GLN   A 299 ? 0.31376 0.42383 0.36202 0.00656  0.07312  0.02492  299 GLN   A C   
2312 O  O   . GLN   A 299 ? 0.31605 0.43319 0.38031 0.00950  0.08211  0.02620  299 GLN   A O   
2313 C  CB  . GLN   A 299 ? 0.25758 0.35357 0.31867 0.00470  0.05142  0.02586  299 GLN   A CB  
2314 C  CG  . GLN   A 299 ? 0.21326 0.31501 0.29937 0.00554  0.05234  0.03082  299 GLN   A CG  
2315 C  CD  . GLN   A 299 ? 0.16478 0.26195 0.26084 0.00196  0.04043  0.03515  299 GLN   A CD  
2316 O  OE1 . GLN   A 299 ? 0.19441 0.29772 0.30919 -0.00034 0.03884  0.04169  299 GLN   A OE1 
2317 N  NE2 . GLN   A 299 ? 0.18289 0.26971 0.26639 0.00090  0.03217  0.03136  299 GLN   A NE2 
2318 N  N   . CYS   A 300 ? 0.28606 0.39922 0.31871 0.00286  0.07241  0.03045  300 CYS   A N   
2319 C  CA  . CYS   A 300 ? 0.29102 0.41542 0.32159 0.00139  0.08251  0.03821  300 CYS   A CA  
2320 C  C   . CYS   A 300 ? 0.38257 0.51013 0.39244 0.00265  0.09437  0.02977  300 CYS   A C   
2321 O  O   . CYS   A 300 ? 0.52275 0.65443 0.52500 0.00024  0.10075  0.03376  300 CYS   A O   
2322 C  CB  . CYS   A 300 ? 0.21826 0.34388 0.24235 -0.00325 0.07609  0.04999  300 CYS   A CB  
2323 S  SG  . CYS   A 300 ? 0.31288 0.43076 0.35802 -0.00588 0.06318  0.05840  300 CYS   A SG  
2324 N  N   . SER   A 301 ? 0.43516 0.55533 0.43515 0.00519  0.09549  0.01617  301 SER   A N   
2325 C  CA  . SER   A 301 ? 0.48652 0.60451 0.46668 0.00589  0.10644  0.00432  301 SER   A CA  
2326 C  C   . SER   A 301 ? 0.49926 0.61069 0.49093 0.01182  0.11380  -0.00757 301 SER   A C   
2327 O  O   . SER   A 301 ? 0.54006 0.65433 0.52861 0.01429  0.12363  -0.01450 301 SER   A O   
2328 C  CB  . SER   A 301 ? 0.54386 0.65722 0.49407 0.00115  0.09925  -0.00128 301 SER   A CB  
2329 O  OG  . SER   A 301 ? 0.66427 0.76820 0.59684 0.00206  0.10634  -0.01526 301 SER   A OG  
2330 N  N   . GLY   A 302 ? 0.49062 0.59319 0.49572 0.01383  0.10431  -0.00992 302 GLY   A N   
2331 C  CA  . GLY   A 302 ? 0.52039 0.61751 0.54560 0.02033  0.11008  -0.01573 302 GLY   A CA  
2332 C  C   . GLY   A 302 ? 0.54192 0.62426 0.55746 0.02193  0.11102  -0.03029 302 GLY   A C   
2333 O  O   . GLY   A 302 ? 0.57500 0.65235 0.59562 0.02723  0.11804  -0.03669 302 GLY   A O   
2334 N  N   . VAL   A 303 ? 0.56437 0.63867 0.56681 0.01733  0.09872  -0.03353 303 VAL   A N   
2335 C  CA  . VAL   A 303 ? 0.61159 0.67141 0.60416 0.01699  0.09875  -0.04709 303 VAL   A CA  
2336 C  C   . VAL   A 303 ? 0.56861 0.62021 0.58634 0.02255  0.09646  -0.04647 303 VAL   A C   
2337 O  O   . VAL   A 303 ? 0.55437 0.60980 0.58879 0.02312  0.08669  -0.03603 303 VAL   A O   
2338 C  CB  . VAL   A 303 ? 0.57304 0.63007 0.54451 0.00937  0.08605  -0.04913 303 VAL   A CB  
2339 C  CG1 . VAL   A 303 ? 0.64131 0.68330 0.60618 0.00769  0.08430  -0.06198 303 VAL   A CG1 
2340 C  CG2 . VAL   A 303 ? 0.58829 0.65442 0.53418 0.00395  0.08830  -0.04902 303 VAL   A CG2 
2341 N  N   . THR   A 304 ? 0.56368 0.60313 0.58320 0.02639  0.10430  -0.05684 304 THR   A N   
2342 C  CA  . THR   A 304 ? 0.52961 0.55982 0.57175 0.03183  0.10242  -0.05580 304 THR   A CA  
2343 C  C   . THR   A 304 ? 0.59407 0.60870 0.62565 0.02781  0.09687  -0.06530 304 THR   A C   
2344 O  O   . THR   A 304 ? 0.64351 0.65623 0.65123 0.02028  0.09232  -0.07174 304 THR   A O   
2345 C  CB  . THR   A 304 ? 0.46647 0.49347 0.52108 0.03915  0.11216  -0.05705 304 THR   A CB  
2346 O  OG1 . THR   A 304 ? 0.57161 0.59115 0.60358 0.03751  0.12020  -0.06918 304 THR   A OG1 
2347 C  CG2 . THR   A 304 ? 0.34412 0.38812 0.41598 0.04286  0.11547  -0.04565 304 THR   A CG2 
2348 N  N   . PHE   A 305 ? 0.56082 0.56526 0.61081 0.03222  0.09521  -0.06402 305 PHE   A N   
2349 C  CA  . PHE   A 305 ? 0.61646 0.60585 0.66102 0.02846  0.08966  -0.07089 305 PHE   A CA  
2350 C  C   . PHE   A 305 ? 0.62120 0.59678 0.68145 0.03423  0.09386  -0.07165 305 PHE   A C   
2351 O  O   . PHE   A 305 ? 0.58240 0.56283 0.66599 0.04127  0.09483  -0.06152 305 PHE   A O   
2352 C  CB  . PHE   A 305 ? 0.55254 0.54710 0.60148 0.02490  0.07383  -0.05994 305 PHE   A CB  
2353 C  CG  . PHE   A 305 ? 0.55310 0.56261 0.59140 0.02050  0.06659  -0.05309 305 PHE   A CG  
2354 C  CD1 . PHE   A 305 ? 0.50946 0.52050 0.52492 0.01302  0.06163  -0.05779 305 PHE   A CD1 
2355 C  CD2 . PHE   A 305 ? 0.50952 0.53178 0.56197 0.02372  0.06507  -0.04156 305 PHE   A CD2 
2356 C  CE1 . PHE   A 305 ? 0.53475 0.55869 0.54267 0.01002  0.05575  -0.05025 305 PHE   A CE1 
2357 C  CE2 . PHE   A 305 ? 0.44277 0.47632 0.48661 0.01974  0.05945  -0.03533 305 PHE   A CE2 
2358 C  CZ  . PHE   A 305 ? 0.52399 0.55788 0.54592 0.01352  0.05522  -0.03936 305 PHE   A CZ  
2359 N  N   . GLN   A 306 ? 0.64034 0.59966 0.68819 0.03050  0.09551  -0.08274 306 GLN   A N   
2360 C  CA  . GLN   A 306 ? 0.64723 0.59201 0.70904 0.03544  0.10046  -0.08403 306 GLN   A CA  
2361 C  C   . GLN   A 306 ? 0.64426 0.57228 0.70001 0.02942  0.09534  -0.09036 306 GLN   A C   
2362 O  O   . GLN   A 306 ? 0.63476 0.55885 0.70571 0.03051  0.08917  -0.08261 306 GLN   A O   
2363 C  CB  . GLN   A 306 ? 0.66614 0.60715 0.72136 0.03870  0.11264  -0.09219 306 GLN   A CB  
2364 C  CG  . GLN   A 306 ? 0.70575 0.63689 0.78231 0.04687  0.11996  -0.09005 306 GLN   A CG  
2365 C  CD  . GLN   A 306 ? 0.72318 0.65428 0.79597 0.05153  0.13310  -0.09675 306 GLN   A CD  
2366 O  OE1 . GLN   A 306 ? 0.79963 0.73535 0.85004 0.04759  0.13662  -0.10471 306 GLN   A OE1 
2367 N  NE2 . GLN   A 306 ? 0.66632 0.59282 0.76092 0.05998  0.14049  -0.09300 306 GLN   A NE2 
2368 N  N1  . A1ARX B .   ? 0.47328 0.47899 0.32145 -0.04435 -0.03177 0.02210  401 A1ARX A N1  
2369 C  C4  . A1ARX B .   ? 0.47339 0.48947 0.34112 -0.04179 -0.03306 0.04606  401 A1ARX A C4  
2370 C  C5  . A1ARX B .   ? 0.46526 0.46581 0.29607 -0.04048 -0.00831 0.01211  401 A1ARX A C5  
2371 C  C6  . A1ARX B .   ? 0.51443 0.51323 0.32641 -0.04094 0.00275  0.00782  401 A1ARX A C6  
2372 C  C7  . A1ARX B .   ? 0.51955 0.51770 0.31308 -0.04450 0.00026  0.00745  401 A1ARX A C7  
2373 C  C8  . A1ARX B .   ? 0.53743 0.53776 0.32956 -0.04899 -0.01343 0.01206  401 A1ARX A C8  
2374 C  C10 . A1ARX B .   ? 0.49134 0.49037 0.31184 -0.03495 0.01719  0.00367  401 A1ARX A C10 
2375 C  C13 . A1ARX B .   ? 0.49156 0.49622 0.33761 -0.02245 0.04285  -0.00142 401 A1ARX A C13 
2376 C  C15 . A1ARX B .   ? 0.54799 0.54220 0.35266 -0.03346 0.02974  -0.00578 401 A1ARX A C15 
2377 C  C17 . A1ARX B .   ? 0.41794 0.41030 0.26617 -0.05020 -0.04345 -0.00105 401 A1ARX A C17 
2378 C  C20 . A1ARX B .   ? 0.50257 0.52067 0.35147 -0.04544 -0.03225 0.05007  401 A1ARX A C20 
2379 C  C21 . A1ARX B .   ? 0.55156 0.57412 0.40754 -0.04532 -0.03337 0.06458  401 A1ARX A C21 
2380 C  C22 . A1ARX B .   ? 0.56766 0.59521 0.42183 -0.04962 -0.05170 0.06619  401 A1ARX A C22 
2381 C  C1  . A1ARX B .   ? 0.41331 0.41418 0.26595 -0.04476 -0.03573 0.01302  401 A1ARX A C1  
2382 C  C11 . A1ARX B .   ? 0.44798 0.45265 0.29633 -0.02979 0.01841  0.00903  401 A1ARX A C11 
2383 C  C12 . A1ARX B .   ? 0.43986 0.44743 0.29958 -0.02438 0.03029  0.00633  401 A1ARX A C12 
2384 C  C14 . A1ARX B .   ? 0.51966 0.51640 0.33677 -0.02697 0.04335  -0.00820 401 A1ARX A C14 
2385 C  C16 . A1ARX B .   ? 0.47496 0.47215 0.31596 -0.04942 -0.04021 0.00629  401 A1ARX A C16 
2386 C  C18 . A1ARX B .   ? 0.36846 0.36036 0.23591 -0.04529 -0.04170 -0.00143 401 A1ARX A C18 
2387 C  C19 . A1ARX B .   ? 0.39090 0.39089 0.26713 -0.03860 -0.03333 0.01067  401 A1ARX A C19 
2388 C  C2  . A1ARX B .   ? 0.50586 0.50855 0.33425 -0.04501 -0.02137 0.01705  401 A1ARX A C2  
2389 C  C3  . A1ARX B .   ? 0.45126 0.46341 0.31810 -0.04221 -0.03676 0.03473  401 A1ARX A C3  
2390 C  C9  . A1ARX B .   ? 0.50525 0.50825 0.31610 -0.04897 -0.02378 0.01700  401 A1ARX A C9  
2391 N  N2  . A1ARX B .   ? 0.30767 0.30372 0.19077 -0.03853 -0.03599 0.00399  401 A1ARX A N2  
2392 O  O1  . A1ARX B .   ? 0.45800 0.47194 0.34350 -0.04013 -0.04322 0.03687  401 A1ARX A O1  
2393 O  O2  . A1ARX B .   ? 0.60251 0.62893 0.45666 -0.04764 -0.04249 0.07133  401 A1ARX A O2  
2394 O  O3  . A1ARX B .   ? 0.58869 0.61142 0.45224 -0.04367 -0.02651 0.06968  401 A1ARX A O3  
2395 CL CL1 . A1ARX B .   ? 0.50320 0.51863 0.39529 -0.02033 0.02926  0.01264  401 A1ARX A CL1 
2396 CL CL2 . A1ARX B .   ? 0.56246 0.54964 0.39909 -0.05685 -0.04886 -0.00945 401 A1ARX A CL2 
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