data_9BQM
# 
_entry.id   9BQM 
# 
_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   9BQM         pdb_00009bqm 10.2210/pdb9bqm/pdb 
WWPDB D_1000283989 ?            ?                   
# 
_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                        9BQM 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-10 
_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 ?                   
# 
_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 
;O-tert-butyl-N-{[(propan-2-yl)oxy]carbonyl}-L-threonyl-3-cyclohexyl-N-{(2R)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-alaninamide
;
554.719   1   ?         ? ? ? 
3 water       nat water 18.015    172 ?         ? ? ? 
# 
_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 
;O-tert-butyl-N-{[(propan-2-yl)oxy]carbonyl}-L-threonyl-3-cyclohexyl-N-{(2R)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-alaninamide
;
A1ARI 
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 
A1ARI non-polymer         . 
;O-tert-butyl-N-{[(propan-2-yl)oxy]carbonyl}-L-threonyl-3-cyclohexyl-N-{(2R)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}-L-alaninamide
;
? 'C28 H50 N4 O7'  554.719 
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 ALA 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        A1ARI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ARI 
_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 A1ARI 1   401 401 A1ARI v26 A . 
C 3 HOH   1   501 5   HOH   HOH A . 
C 3 HOH   2   502 61  HOH   HOH A . 
C 3 HOH   3   503 81  HOH   HOH A . 
C 3 HOH   4   504 113 HOH   HOH A . 
C 3 HOH   5   505 145 HOH   HOH A . 
C 3 HOH   6   506 153 HOH   HOH A . 
C 3 HOH   7   507 88  HOH   HOH A . 
C 3 HOH   8   508 109 HOH   HOH A . 
C 3 HOH   9   509 29  HOH   HOH A . 
C 3 HOH   10  510 103 HOH   HOH A . 
C 3 HOH   11  511 119 HOH   HOH A . 
C 3 HOH   12  512 128 HOH   HOH A . 
C 3 HOH   13  513 165 HOH   HOH A . 
C 3 HOH   14  514 65  HOH   HOH A . 
C 3 HOH   15  515 122 HOH   HOH A . 
C 3 HOH   16  516 80  HOH   HOH A . 
C 3 HOH   17  517 76  HOH   HOH A . 
C 3 HOH   18  518 125 HOH   HOH A . 
C 3 HOH   19  519 161 HOH   HOH A . 
C 3 HOH   20  520 32  HOH   HOH A . 
C 3 HOH   21  521 71  HOH   HOH A . 
C 3 HOH   22  522 16  HOH   HOH A . 
C 3 HOH   23  523 75  HOH   HOH A . 
C 3 HOH   24  524 45  HOH   HOH A . 
C 3 HOH   25  525 87  HOH   HOH A . 
C 3 HOH   26  526 171 HOH   HOH A . 
C 3 HOH   27  527 124 HOH   HOH A . 
C 3 HOH   28  528 107 HOH   HOH A . 
C 3 HOH   29  529 118 HOH   HOH A . 
C 3 HOH   30  530 54  HOH   HOH A . 
C 3 HOH   31  531 141 HOH   HOH A . 
C 3 HOH   32  532 19  HOH   HOH A . 
C 3 HOH   33  533 7   HOH   HOH A . 
C 3 HOH   34  534 21  HOH   HOH A . 
C 3 HOH   35  535 38  HOH   HOH A . 
C 3 HOH   36  536 93  HOH   HOH A . 
C 3 HOH   37  537 18  HOH   HOH A . 
C 3 HOH   38  538 20  HOH   HOH A . 
C 3 HOH   39  539 36  HOH   HOH A . 
C 3 HOH   40  540 163 HOH   HOH A . 
C 3 HOH   41  541 50  HOH   HOH A . 
C 3 HOH   42  542 52  HOH   HOH A . 
C 3 HOH   43  543 92  HOH   HOH A . 
C 3 HOH   44  544 60  HOH   HOH A . 
C 3 HOH   45  545 9   HOH   HOH A . 
C 3 HOH   46  546 112 HOH   HOH A . 
C 3 HOH   47  547 6   HOH   HOH A . 
C 3 HOH   48  548 136 HOH   HOH A . 
C 3 HOH   49  549 130 HOH   HOH A . 
C 3 HOH   50  550 47  HOH   HOH A . 
C 3 HOH   51  551 49  HOH   HOH A . 
C 3 HOH   52  552 43  HOH   HOH A . 
C 3 HOH   53  553 66  HOH   HOH A . 
C 3 HOH   54  554 48  HOH   HOH A . 
C 3 HOH   55  555 3   HOH   HOH A . 
C 3 HOH   56  556 40  HOH   HOH A . 
C 3 HOH   57  557 17  HOH   HOH A . 
C 3 HOH   58  558 166 HOH   HOH A . 
C 3 HOH   59  559 27  HOH   HOH A . 
C 3 HOH   60  560 77  HOH   HOH A . 
C 3 HOH   61  561 74  HOH   HOH A . 
C 3 HOH   62  562 151 HOH   HOH A . 
C 3 HOH   63  563 94  HOH   HOH A . 
C 3 HOH   64  564 30  HOH   HOH A . 
C 3 HOH   65  565 104 HOH   HOH A . 
C 3 HOH   66  566 164 HOH   HOH A . 
C 3 HOH   67  567 101 HOH   HOH A . 
C 3 HOH   68  568 4   HOH   HOH A . 
C 3 HOH   69  569 110 HOH   HOH A . 
C 3 HOH   70  570 31  HOH   HOH A . 
C 3 HOH   71  571 22  HOH   HOH A . 
C 3 HOH   72  572 8   HOH   HOH A . 
C 3 HOH   73  573 35  HOH   HOH A . 
C 3 HOH   74  574 102 HOH   HOH A . 
C 3 HOH   75  575 42  HOH   HOH A . 
C 3 HOH   76  576 58  HOH   HOH A . 
C 3 HOH   77  577 79  HOH   HOH A . 
C 3 HOH   78  578 63  HOH   HOH A . 
C 3 HOH   79  579 15  HOH   HOH A . 
C 3 HOH   80  580 142 HOH   HOH A . 
C 3 HOH   81  581 25  HOH   HOH A . 
C 3 HOH   82  582 82  HOH   HOH A . 
C 3 HOH   83  583 1   HOH   HOH A . 
C 3 HOH   84  584 59  HOH   HOH A . 
C 3 HOH   85  585 2   HOH   HOH A . 
C 3 HOH   86  586 12  HOH   HOH A . 
C 3 HOH   87  587 62  HOH   HOH A . 
C 3 HOH   88  588 168 HOH   HOH A . 
C 3 HOH   89  589 162 HOH   HOH A . 
C 3 HOH   90  590 14  HOH   HOH A . 
C 3 HOH   91  591 10  HOH   HOH A . 
C 3 HOH   92  592 132 HOH   HOH A . 
C 3 HOH   93  593 123 HOH   HOH A . 
C 3 HOH   94  594 117 HOH   HOH A . 
C 3 HOH   95  595 99  HOH   HOH A . 
C 3 HOH   96  596 156 HOH   HOH A . 
C 3 HOH   97  597 167 HOH   HOH A . 
C 3 HOH   98  598 64  HOH   HOH A . 
C 3 HOH   99  599 115 HOH   HOH A . 
C 3 HOH   100 600 149 HOH   HOH A . 
C 3 HOH   101 601 51  HOH   HOH A . 
C 3 HOH   102 602 70  HOH   HOH A . 
C 3 HOH   103 603 53  HOH   HOH A . 
C 3 HOH   104 604 170 HOH   HOH A . 
C 3 HOH   105 605 28  HOH   HOH A . 
C 3 HOH   106 606 105 HOH   HOH A . 
C 3 HOH   107 607 89  HOH   HOH A . 
C 3 HOH   108 608 154 HOH   HOH A . 
C 3 HOH   109 609 131 HOH   HOH A . 
C 3 HOH   110 610 23  HOH   HOH A . 
C 3 HOH   111 611 146 HOH   HOH A . 
C 3 HOH   112 612 95  HOH   HOH A . 
C 3 HOH   113 613 37  HOH   HOH A . 
C 3 HOH   114 614 138 HOH   HOH A . 
C 3 HOH   115 615 86  HOH   HOH A . 
C 3 HOH   116 616 100 HOH   HOH A . 
C 3 HOH   117 617 126 HOH   HOH A . 
C 3 HOH   118 618 159 HOH   HOH A . 
C 3 HOH   119 619 33  HOH   HOH A . 
C 3 HOH   120 620 41  HOH   HOH A . 
C 3 HOH   121 621 121 HOH   HOH A . 
C 3 HOH   122 622 157 HOH   HOH A . 
C 3 HOH   123 623 147 HOH   HOH A . 
C 3 HOH   124 624 39  HOH   HOH A . 
C 3 HOH   125 625 85  HOH   HOH A . 
C 3 HOH   126 626 137 HOH   HOH A . 
C 3 HOH   127 627 13  HOH   HOH A . 
C 3 HOH   128 628 68  HOH   HOH A . 
C 3 HOH   129 629 135 HOH   HOH A . 
C 3 HOH   130 630 34  HOH   HOH A . 
C 3 HOH   131 631 11  HOH   HOH A . 
C 3 HOH   132 632 134 HOH   HOH A . 
C 3 HOH   133 633 169 HOH   HOH A . 
C 3 HOH   134 634 26  HOH   HOH A . 
C 3 HOH   135 635 158 HOH   HOH A . 
C 3 HOH   136 636 44  HOH   HOH A . 
C 3 HOH   137 637 57  HOH   HOH A . 
C 3 HOH   138 638 108 HOH   HOH A . 
C 3 HOH   139 639 96  HOH   HOH A . 
C 3 HOH   140 640 67  HOH   HOH A . 
C 3 HOH   141 641 140 HOH   HOH A . 
C 3 HOH   142 642 155 HOH   HOH A . 
C 3 HOH   143 643 144 HOH   HOH A . 
C 3 HOH   144 644 84  HOH   HOH A . 
C 3 HOH   145 645 98  HOH   HOH A . 
C 3 HOH   146 646 91  HOH   HOH A . 
C 3 HOH   147 647 90  HOH   HOH A . 
C 3 HOH   148 648 106 HOH   HOH A . 
C 3 HOH   149 649 111 HOH   HOH A . 
C 3 HOH   150 650 129 HOH   HOH A . 
C 3 HOH   151 651 24  HOH   HOH A . 
C 3 HOH   152 652 69  HOH   HOH A . 
C 3 HOH   153 653 143 HOH   HOH A . 
C 3 HOH   154 654 152 HOH   HOH A . 
C 3 HOH   155 655 55  HOH   HOH A . 
C 3 HOH   156 656 56  HOH   HOH A . 
C 3 HOH   157 657 150 HOH   HOH A . 
C 3 HOH   158 658 133 HOH   HOH A . 
C 3 HOH   159 659 116 HOH   HOH A . 
C 3 HOH   160 660 148 HOH   HOH A . 
C 3 HOH   161 661 72  HOH   HOH A . 
C 3 HOH   162 662 83  HOH   HOH A . 
C 3 HOH   163 663 73  HOH   HOH A . 
C 3 HOH   164 664 97  HOH   HOH A . 
C 3 HOH   165 665 127 HOH   HOH A . 
C 3 HOH   166 666 160 HOH   HOH A . 
C 3 HOH   167 667 78  HOH   HOH A . 
C 3 HOH   168 668 172 HOH   HOH A . 
C 3 HOH   169 669 114 HOH   HOH A . 
C 3 HOH   170 670 139 HOH   HOH A . 
C 3 HOH   171 671 46  HOH   HOH A . 
C 3 HOH   172 672 120 HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A GLU 178 ? CG  ? A GLU 178 CG  
2 1 Y 1 A GLU 178 ? CD  ? A GLU 178 CD  
3 1 Y 1 A GLU 178 ? OE1 ? A GLU 178 OE1 
4 1 Y 1 A GLU 178 ? OE2 ? A GLU 178 OE2 
# 
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         ? ? ? 1.18.2_3874 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                   96.628 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BQM 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     54.484 
_cell.length_a_esd                 ? 
_cell.length_b                     82.471 
_cell.length_b_esd                 ? 
_cell.length_c                     86.941 
_cell.length_c_esd                 ? 
_cell.volume                       388046.882 
_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                         9BQM 
_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                   9BQM 
_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         2021-09-25 
_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                          16.91 
_reflns.entry_id                                       9BQM 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.1 
_reflns.d_resolution_low                               24.51 
_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                                     21033 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.05 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.61 
_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                                0.07304 
_reflns.pdbx_Rpim_I_all                                0.02877 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.06665 
_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                                    2.1 
_reflns_shell.d_res_low                                     2.175 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           5.51 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1981 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.2115 
_reflns_shell.pdbx_Rpim_I_all                               0.1129 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.973 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.1772 
_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                               28.79 
_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                                 9BQM 
_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                            2.10 
_refine.ls_d_res_low                             24.51 
_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                     21023 
_refine.ls_number_reflns_R_free                  1082 
_refine.ls_number_reflns_R_work                  19941 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.11 
_refine.ls_percent_reflns_R_free                 5.15 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2275 
_refine.ls_R_factor_R_free                       0.2581 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2259 
_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                          1.35 
_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             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.3132 
_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                            0.2530 
_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                       2.10 
_refine_hist.d_res_low                        24.51 
_refine_hist.number_atoms_solvent             172 
_refine_hist.number_atoms_total               2574 
_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        2363 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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' ? 0.0083  ? 2456 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1448  ? 3339 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0572  ? 379  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0063  ? 431  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.3808 ? 356  ? 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' 2.10 2.20  . . 131 2378 89.77 . . . . 0.3104 . . . . . . . . . . . 0.3844 
'X-RAY DIFFRACTION' 2.20 2.31  . . 135 2313 89.41 . . . . 0.2891 . . . . . . . . . . . 0.3171 
'X-RAY DIFFRACTION' 2.31 2.46  . . 122 2409 90.78 . . . . 0.2831 . . . . . . . . . . . 0.3122 
'X-RAY DIFFRACTION' 2.46 2.65  . . 126 2461 92.99 . . . . 0.2674 . . . . . . . . . . . 0.3132 
'X-RAY DIFFRACTION' 2.65 2.91  . . 157 2516 95.67 . . . . 0.2519 . . . . . . . . . . . 0.2850 
'X-RAY DIFFRACTION' 2.91 3.33  . . 145 2590 98.10 . . . . 0.2235 . . . . . . . . . . . 0.2534 
'X-RAY DIFFRACTION' 3.33 4.19  . . 124 2652 99.07 . . . . 0.1808 . . . . . . . . . . . 0.1975 
'X-RAY DIFFRACTION' 4.19 24.51 . . 142 2622 97.05 . . . . 0.1766 . . . . . . . . . . . 0.1976 
# 
_struct.entry_id                     9BQM 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor VB-A-26' 
_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        9BQM 
_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              9BQM 
_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)' 5380  ? 
1 MORE         -19   ? 
1 'SSA (A^2)'  24810 ? 
# 
_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 -54.4840000000 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  ? PHE A 66  ? SER A 62  PHE A 66  5 ? 5  
HELX_P HELX_P5  AA5 ILE A 200 ? GLY A 215 ? ILE A 200 GLY A 215 1 ? 16 
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           A1ARI 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C5 
_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            A1ARI 
_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               1.798 
_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                      A1ARI 
_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                       A1ARI 
_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               C5 
_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                        A1ARI 
_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 LEU A 67  ? ALA A 70  ? LEU A 67  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 18  ? N VAL A 18  O GLY A 29  ? O GLY A 29  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N GLY A 79  ? N GLY A 79  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O TYR A 161 ? O TYR A 161 N GLY A 149 ? N GLY A 149 
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 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9BQM 
_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 635 ? ? O A HOH 644 ? ? 1.83 
2  1 O   A HOH 544 ? ? O A HOH 587 ? ? 2.04 
3  1 O   A ALA 194 ? ? O A HOH 501 ? ? 2.07 
4  1 OE1 A GLU 288 ? ? O A HOH 502 ? ? 2.10 
5  1 O   A HOH 529 ? ? O A HOH 642 ? ? 2.12 
6  1 O   A HOH 615 ? ? O A HOH 663 ? ? 2.13 
7  1 O   A HOH 510 ? ? O A HOH 561 ? ? 2.13 
8  1 O   A LEU 75  ? ? O A HOH 503 ? ? 2.15 
9  1 N   A ALA 193 ? ? O A HOH 504 ? ? 2.15 
10 1 O   A VAL 42  ? ? O A HOH 505 ? ? 2.17 
11 1 O   A CYS 300 ? ? O A HOH 506 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 561 ? ? 1_555 O A HOH 623 ? ? 2_455 1.91 
2 1 O A HOH 626 ? ? 1_555 O A HOH 655 ? ? 2_455 2.02 
3 1 O A HOH 540 ? ? 1_555 O A HOH 611 ? ? 2_455 2.07 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              128 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              128 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             SG 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             CYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              128 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                121.88 
_pdbx_validate_rmsd_angle.angle_target_value         114.20 
_pdbx_validate_rmsd_angle.angle_deviation            7.68 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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  ? ? 52.46   -128.14 
2 1 HIS A 41  ? ? -69.35  0.50    
3 1 THR A 45  ? ? -135.64 -159.25 
4 1 LEU A 50  ? ? -52.91  -73.04  
5 1 ASN A 53  ? ? -165.67 84.44   
6 1 ASN A 72  ? ? -80.83  34.57   
7 1 ASN A 84  ? ? 52.38   -121.78 
8 1 TYR A 154 ? ? 39.26   -108.71 
# 
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 591 ? C HOH . 
2 1 A HOH 627 ? C HOH . 
3 1 A HOH 643 ? 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         -14.1693853869 
_pdbx_refine_tls.origin_y         -15.1200527081 
_pdbx_refine_tls.origin_z         -0.509781947506 
_pdbx_refine_tls.T[1][1]          0.0704409135102 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0065003570098 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0945892017981 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0762646292483 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0213183104373 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          -0.031028991669 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          3.76957363736 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.789280507916 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.904688221267 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          2.3389777867 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -1.08451529499 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.82658112764 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0105478852439 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0736527847499 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0656282487181 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.112034016345 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0895646777325 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.00170773677768 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0487441806009 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0122318369042 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.00568091741073 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   A 
_pdbx_refine_tls_group.beg_label_seq_id    1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   B 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     401 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ARI N    N N N 1   
A1ARI C    C N S 2   
A1ARI O    O N N 3   
A1ARI C1   C N N 4   
A1ARI C10  C N N 5   
A1ARI C11  C N N 6   
A1ARI C12  C N N 7   
A1ARI C13  C N R 8   
A1ARI C14  C N N 9   
A1ARI C15  C N N 10  
A1ARI C16  C N N 11  
A1ARI C17  C N N 12  
A1ARI C18  C N N 13  
A1ARI C19  C N N 14  
A1ARI C2   C N S 15  
A1ARI C20  C N N 16  
A1ARI C21  C N N 17  
A1ARI C22  C N N 18  
A1ARI C23  C N N 19  
A1ARI C24  C N N 20  
A1ARI C25  C N N 21  
A1ARI C26  C N N 22  
A1ARI C27  C N N 23  
A1ARI C3   C N N 24  
A1ARI C4   C N S 25  
A1ARI C5   C N N 26  
A1ARI C6   C N N 27  
A1ARI C7   C N S 28  
A1ARI C8   C N N 29  
A1ARI C9   C N N 30  
A1ARI N1   N N N 31  
A1ARI N2   N N N 32  
A1ARI N3   N N N 33  
A1ARI O1   O N N 34  
A1ARI O2   O N N 35  
A1ARI O3   O N N 36  
A1ARI O4   O N N 37  
A1ARI O5   O N N 38  
A1ARI O6   O N N 39  
A1ARI HN   H N N 40  
A1ARI H0   H N N 41  
A1ARI H111 H N N 42  
A1ARI H112 H N N 43  
A1ARI H12  H N N 44  
A1ARI H13  H N N 45  
A1ARI H142 H N N 46  
A1ARI H141 H N N 47  
A1ARI H143 H N N 48  
A1ARI H162 H N N 49  
A1ARI H182 H N N 50  
A1ARI H183 H N N 51  
A1ARI H181 H N N 52  
A1ARI H191 H N N 53  
A1ARI H192 H N N 54  
A1ARI H193 H N N 55  
A1ARI H2   H N N 56  
A1ARI H201 H N N 57  
A1ARI H203 H N N 58  
A1ARI H202 H N N 59  
A1ARI H212 H N N 60  
A1ARI H211 H N N 61  
A1ARI H221 H N N 62  
A1ARI H222 H N N 63  
A1ARI H231 H N N 64  
A1ARI H232 H N N 65  
A1ARI H241 H N N 66  
A1ARI H242 H N N 67  
A1ARI H251 H N N 68  
A1ARI H252 H N N 69  
A1ARI H26  H N N 70  
A1ARI H261 H N N 71  
A1ARI H262 H N N 72  
A1ARI H271 H N N 73  
A1ARI H27  H N N 74  
A1ARI H272 H N N 75  
A1ARI H4   H N N 76  
A1ARI H5   H N N 77  
A1ARI H    H N N 78  
A1ARI H61  H N N 79  
A1ARI H62  H N N 80  
A1ARI H7   H N N 81  
A1ARI H82  H N N 82  
A1ARI H81  H N N 83  
A1ARI H92  H N N 84  
A1ARI H91  H N N 85  
A1ARI HN1  H N N 86  
A1ARI HN2  H N N 87  
A1ARI HN3  H N N 88  
A1ARI HO2  H N N 89  
ALA   N    N N N 90  
ALA   CA   C N S 91  
ALA   C    C N N 92  
ALA   O    O N N 93  
ALA   CB   C N N 94  
ALA   OXT  O N N 95  
ALA   H    H N N 96  
ALA   H2   H N N 97  
ALA   HA   H N N 98  
ALA   HB1  H N N 99  
ALA   HB2  H N N 100 
ALA   HB3  H N N 101 
ALA   HXT  H N N 102 
ARG   N    N N N 103 
ARG   CA   C N S 104 
ARG   C    C N N 105 
ARG   O    O N N 106 
ARG   CB   C N N 107 
ARG   CG   C N N 108 
ARG   CD   C N N 109 
ARG   NE   N N N 110 
ARG   CZ   C N N 111 
ARG   NH1  N N N 112 
ARG   NH2  N N N 113 
ARG   OXT  O N N 114 
ARG   H    H N N 115 
ARG   H2   H N N 116 
ARG   HA   H N N 117 
ARG   HB2  H N N 118 
ARG   HB3  H N N 119 
ARG   HG2  H N N 120 
ARG   HG3  H N N 121 
ARG   HD2  H N N 122 
ARG   HD3  H N N 123 
ARG   HE   H N N 124 
ARG   HH11 H N N 125 
ARG   HH12 H N N 126 
ARG   HH21 H N N 127 
ARG   HH22 H N N 128 
ARG   HXT  H N N 129 
ASN   N    N N N 130 
ASN   CA   C N S 131 
ASN   C    C N N 132 
ASN   O    O N N 133 
ASN   CB   C N N 134 
ASN   CG   C N N 135 
ASN   OD1  O N N 136 
ASN   ND2  N N N 137 
ASN   OXT  O N N 138 
ASN   H    H N N 139 
ASN   H2   H N N 140 
ASN   HA   H N N 141 
ASN   HB2  H N N 142 
ASN   HB3  H N N 143 
ASN   HD21 H N N 144 
ASN   HD22 H N N 145 
ASN   HXT  H N N 146 
ASP   N    N N N 147 
ASP   CA   C N S 148 
ASP   C    C N N 149 
ASP   O    O N N 150 
ASP   CB   C N N 151 
ASP   CG   C N N 152 
ASP   OD1  O N N 153 
ASP   OD2  O N N 154 
ASP   OXT  O N N 155 
ASP   H    H N N 156 
ASP   H2   H N N 157 
ASP   HA   H N N 158 
ASP   HB2  H N N 159 
ASP   HB3  H N N 160 
ASP   HD2  H N N 161 
ASP   HXT  H N N 162 
CYS   N    N N N 163 
CYS   CA   C N R 164 
CYS   C    C N N 165 
CYS   O    O N N 166 
CYS   CB   C N N 167 
CYS   SG   S N N 168 
CYS   OXT  O N N 169 
CYS   H    H N N 170 
CYS   H2   H N N 171 
CYS   HA   H N N 172 
CYS   HB2  H N N 173 
CYS   HB3  H N N 174 
CYS   HG   H N N 175 
CYS   HXT  H N N 176 
GLN   N    N N N 177 
GLN   CA   C N S 178 
GLN   C    C N N 179 
GLN   O    O N N 180 
GLN   CB   C N N 181 
GLN   CG   C N N 182 
GLN   CD   C N N 183 
GLN   OE1  O N N 184 
GLN   NE2  N N N 185 
GLN   OXT  O N N 186 
GLN   H    H N N 187 
GLN   H2   H N N 188 
GLN   HA   H N N 189 
GLN   HB2  H N N 190 
GLN   HB3  H N N 191 
GLN   HG2  H N N 192 
GLN   HG3  H N N 193 
GLN   HE21 H N N 194 
GLN   HE22 H N N 195 
GLN   HXT  H N N 196 
GLU   N    N N N 197 
GLU   CA   C N S 198 
GLU   C    C N N 199 
GLU   O    O N N 200 
GLU   CB   C N N 201 
GLU   CG   C N N 202 
GLU   CD   C N N 203 
GLU   OE1  O N N 204 
GLU   OE2  O N N 205 
GLU   OXT  O N N 206 
GLU   H    H N N 207 
GLU   H2   H N N 208 
GLU   HA   H N N 209 
GLU   HB2  H N N 210 
GLU   HB3  H N N 211 
GLU   HG2  H N N 212 
GLU   HG3  H N N 213 
GLU   HE2  H N N 214 
GLU   HXT  H N N 215 
GLY   N    N N N 216 
GLY   CA   C N N 217 
GLY   C    C N N 218 
GLY   O    O N N 219 
GLY   OXT  O N N 220 
GLY   H    H N N 221 
GLY   H2   H N N 222 
GLY   HA2  H N N 223 
GLY   HA3  H N N 224 
GLY   HXT  H N N 225 
HIS   N    N N N 226 
HIS   CA   C N S 227 
HIS   C    C N N 228 
HIS   O    O N N 229 
HIS   CB   C N N 230 
HIS   CG   C Y N 231 
HIS   ND1  N Y N 232 
HIS   CD2  C Y N 233 
HIS   CE1  C Y N 234 
HIS   NE2  N Y N 235 
HIS   OXT  O N N 236 
HIS   H    H N N 237 
HIS   H2   H N N 238 
HIS   HA   H N N 239 
HIS   HB2  H N N 240 
HIS   HB3  H N N 241 
HIS   HD1  H N N 242 
HIS   HD2  H N N 243 
HIS   HE1  H N N 244 
HIS   HE2  H N N 245 
HIS   HXT  H N N 246 
HOH   O    O N N 247 
HOH   H1   H N N 248 
HOH   H2   H N N 249 
ILE   N    N N N 250 
ILE   CA   C N S 251 
ILE   C    C N N 252 
ILE   O    O N N 253 
ILE   CB   C N S 254 
ILE   CG1  C N N 255 
ILE   CG2  C N N 256 
ILE   CD1  C N N 257 
ILE   OXT  O N N 258 
ILE   H    H N N 259 
ILE   H2   H N N 260 
ILE   HA   H N N 261 
ILE   HB   H N N 262 
ILE   HG12 H N N 263 
ILE   HG13 H N N 264 
ILE   HG21 H N N 265 
ILE   HG22 H N N 266 
ILE   HG23 H N N 267 
ILE   HD11 H N N 268 
ILE   HD12 H N N 269 
ILE   HD13 H N N 270 
ILE   HXT  H N N 271 
LEU   N    N N N 272 
LEU   CA   C N S 273 
LEU   C    C N N 274 
LEU   O    O N N 275 
LEU   CB   C N N 276 
LEU   CG   C N N 277 
LEU   CD1  C N N 278 
LEU   CD2  C N N 279 
LEU   OXT  O N N 280 
LEU   H    H N N 281 
LEU   H2   H N N 282 
LEU   HA   H N N 283 
LEU   HB2  H N N 284 
LEU   HB3  H N N 285 
LEU   HG   H N N 286 
LEU   HD11 H N N 287 
LEU   HD12 H N N 288 
LEU   HD13 H N N 289 
LEU   HD21 H N N 290 
LEU   HD22 H N N 291 
LEU   HD23 H N N 292 
LEU   HXT  H N N 293 
LYS   N    N N N 294 
LYS   CA   C N S 295 
LYS   C    C N N 296 
LYS   O    O N N 297 
LYS   CB   C N N 298 
LYS   CG   C N N 299 
LYS   CD   C N N 300 
LYS   CE   C N N 301 
LYS   NZ   N N N 302 
LYS   OXT  O N N 303 
LYS   H    H N N 304 
LYS   H2   H N N 305 
LYS   HA   H N N 306 
LYS   HB2  H N N 307 
LYS   HB3  H N N 308 
LYS   HG2  H N N 309 
LYS   HG3  H N N 310 
LYS   HD2  H N N 311 
LYS   HD3  H N N 312 
LYS   HE2  H N N 313 
LYS   HE3  H N N 314 
LYS   HZ1  H N N 315 
LYS   HZ2  H N N 316 
LYS   HZ3  H N N 317 
LYS   HXT  H N N 318 
MET   N    N N N 319 
MET   CA   C N S 320 
MET   C    C N N 321 
MET   O    O N N 322 
MET   CB   C N N 323 
MET   CG   C N N 324 
MET   SD   S N N 325 
MET   CE   C N N 326 
MET   OXT  O N N 327 
MET   H    H N N 328 
MET   H2   H N N 329 
MET   HA   H N N 330 
MET   HB2  H N N 331 
MET   HB3  H N N 332 
MET   HG2  H N N 333 
MET   HG3  H N N 334 
MET   HE1  H N N 335 
MET   HE2  H N N 336 
MET   HE3  H N N 337 
MET   HXT  H N N 338 
PHE   N    N N N 339 
PHE   CA   C N S 340 
PHE   C    C N N 341 
PHE   O    O N N 342 
PHE   CB   C N N 343 
PHE   CG   C Y N 344 
PHE   CD1  C Y N 345 
PHE   CD2  C Y N 346 
PHE   CE1  C Y N 347 
PHE   CE2  C Y N 348 
PHE   CZ   C Y N 349 
PHE   OXT  O N N 350 
PHE   H    H N N 351 
PHE   H2   H N N 352 
PHE   HA   H N N 353 
PHE   HB2  H N N 354 
PHE   HB3  H N N 355 
PHE   HD1  H N N 356 
PHE   HD2  H N N 357 
PHE   HE1  H N N 358 
PHE   HE2  H N N 359 
PHE   HZ   H N N 360 
PHE   HXT  H N N 361 
PRO   N    N N N 362 
PRO   CA   C N S 363 
PRO   C    C N N 364 
PRO   O    O N N 365 
PRO   CB   C N N 366 
PRO   CG   C N N 367 
PRO   CD   C N N 368 
PRO   OXT  O N N 369 
PRO   H    H N N 370 
PRO   HA   H N N 371 
PRO   HB2  H N N 372 
PRO   HB3  H N N 373 
PRO   HG2  H N N 374 
PRO   HG3  H N N 375 
PRO   HD2  H N N 376 
PRO   HD3  H N N 377 
PRO   HXT  H N N 378 
SER   N    N N N 379 
SER   CA   C N S 380 
SER   C    C N N 381 
SER   O    O N N 382 
SER   CB   C N N 383 
SER   OG   O N N 384 
SER   OXT  O N N 385 
SER   H    H N N 386 
SER   H2   H N N 387 
SER   HA   H N N 388 
SER   HB2  H N N 389 
SER   HB3  H N N 390 
SER   HG   H N N 391 
SER   HXT  H N N 392 
THR   N    N N N 393 
THR   CA   C N S 394 
THR   C    C N N 395 
THR   O    O N N 396 
THR   CB   C N R 397 
THR   OG1  O N N 398 
THR   CG2  C N N 399 
THR   OXT  O N N 400 
THR   H    H N N 401 
THR   H2   H N N 402 
THR   HA   H N N 403 
THR   HB   H N N 404 
THR   HG1  H N N 405 
THR   HG21 H N N 406 
THR   HG22 H N N 407 
THR   HG23 H N N 408 
THR   HXT  H N N 409 
TRP   N    N N N 410 
TRP   CA   C N S 411 
TRP   C    C N N 412 
TRP   O    O N N 413 
TRP   CB   C N N 414 
TRP   CG   C Y N 415 
TRP   CD1  C Y N 416 
TRP   CD2  C Y N 417 
TRP   NE1  N Y N 418 
TRP   CE2  C Y N 419 
TRP   CE3  C Y N 420 
TRP   CZ2  C Y N 421 
TRP   CZ3  C Y N 422 
TRP   CH2  C Y N 423 
TRP   OXT  O N N 424 
TRP   H    H N N 425 
TRP   H2   H N N 426 
TRP   HA   H N N 427 
TRP   HB2  H N N 428 
TRP   HB3  H N N 429 
TRP   HD1  H N N 430 
TRP   HE1  H N N 431 
TRP   HE3  H N N 432 
TRP   HZ2  H N N 433 
TRP   HZ3  H N N 434 
TRP   HH2  H N N 435 
TRP   HXT  H N N 436 
TYR   N    N N N 437 
TYR   CA   C N S 438 
TYR   C    C N N 439 
TYR   O    O N N 440 
TYR   CB   C N N 441 
TYR   CG   C Y N 442 
TYR   CD1  C Y N 443 
TYR   CD2  C Y N 444 
TYR   CE1  C Y N 445 
TYR   CE2  C Y N 446 
TYR   CZ   C Y N 447 
TYR   OH   O N N 448 
TYR   OXT  O N N 449 
TYR   H    H N N 450 
TYR   H2   H N N 451 
TYR   HA   H N N 452 
TYR   HB2  H N N 453 
TYR   HB3  H N N 454 
TYR   HD1  H N N 455 
TYR   HD2  H N N 456 
TYR   HE1  H N N 457 
TYR   HE2  H N N 458 
TYR   HH   H N N 459 
TYR   HXT  H N N 460 
VAL   N    N N N 461 
VAL   CA   C N S 462 
VAL   C    C N N 463 
VAL   O    O N N 464 
VAL   CB   C N N 465 
VAL   CG1  C N N 466 
VAL   CG2  C N N 467 
VAL   OXT  O N N 468 
VAL   H    H N N 469 
VAL   H2   H N N 470 
VAL   HA   H N N 471 
VAL   HB   H N N 472 
VAL   HG11 H N N 473 
VAL   HG12 H N N 474 
VAL   HG13 H N N 475 
VAL   HG21 H N N 476 
VAL   HG22 H N N 477 
VAL   HG23 H N N 478 
VAL   HXT  H N N 479 
# 
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 
A1ARI O3  C10  doub N N 1   
A1ARI C10 N2   sing N N 2   
A1ARI C10 C7   sing N N 3   
A1ARI N2  C9   sing N N 4   
A1ARI C9  C8   sing N N 5   
A1ARI C8  C7   sing N N 6   
A1ARI C7  C6   sing N N 7   
A1ARI C6  C4   sing N N 8   
A1ARI C5  C4   sing N N 9   
A1ARI C4  N1   sing N N 10  
A1ARI O2  C5   sing N N 11  
A1ARI N1  C3   sing N N 12  
A1ARI O1  C3   doub N N 13  
A1ARI C3  C2   sing N N 14  
A1ARI C11 C2   sing N N 15  
A1ARI C2  N    sing N N 16  
A1ARI C12 C11  sing N N 17  
A1ARI C12 C21  sing N N 18  
A1ARI C25 C12  sing N N 19  
A1ARI C21 C22  sing N N 20  
A1ARI C22 C23  sing N N 21  
A1ARI C23 C24  sing N N 22  
A1ARI C24 C25  sing N N 23  
A1ARI N   C1   sing N N 24  
A1ARI O   C1   doub N N 25  
A1ARI C1  C    sing N N 26  
A1ARI C13 C    sing N N 27  
A1ARI C   N3   sing N N 28  
A1ARI C14 C13  sing N N 29  
A1ARI O4  C13  sing N N 30  
A1ARI C17 O4   sing N N 31  
A1ARI C18 C17  sing N N 32  
A1ARI C19 C17  sing N N 33  
A1ARI C20 C17  sing N N 34  
A1ARI N3  C15  sing N N 35  
A1ARI C15 O6   doub N N 36  
A1ARI O5  C15  sing N N 37  
A1ARI C16 O5   sing N N 38  
A1ARI C26 C16  sing N N 39  
A1ARI C27 C16  sing N N 40  
A1ARI N   HN   sing N N 41  
A1ARI C   H0   sing N N 42  
A1ARI C11 H111 sing N N 43  
A1ARI C11 H112 sing N N 44  
A1ARI C12 H12  sing N N 45  
A1ARI C13 H13  sing N N 46  
A1ARI C14 H142 sing N N 47  
A1ARI C14 H141 sing N N 48  
A1ARI C14 H143 sing N N 49  
A1ARI C16 H162 sing N N 50  
A1ARI C18 H182 sing N N 51  
A1ARI C18 H183 sing N N 52  
A1ARI C18 H181 sing N N 53  
A1ARI C19 H191 sing N N 54  
A1ARI C19 H192 sing N N 55  
A1ARI C19 H193 sing N N 56  
A1ARI C2  H2   sing N N 57  
A1ARI C20 H201 sing N N 58  
A1ARI C20 H203 sing N N 59  
A1ARI C20 H202 sing N N 60  
A1ARI C21 H212 sing N N 61  
A1ARI C21 H211 sing N N 62  
A1ARI C22 H221 sing N N 63  
A1ARI C22 H222 sing N N 64  
A1ARI C23 H231 sing N N 65  
A1ARI C23 H232 sing N N 66  
A1ARI C24 H241 sing N N 67  
A1ARI C24 H242 sing N N 68  
A1ARI C25 H251 sing N N 69  
A1ARI C25 H252 sing N N 70  
A1ARI C26 H26  sing N N 71  
A1ARI C26 H261 sing N N 72  
A1ARI C26 H262 sing N N 73  
A1ARI C27 H271 sing N N 74  
A1ARI C27 H27  sing N N 75  
A1ARI C27 H272 sing N N 76  
A1ARI C4  H4   sing N N 77  
A1ARI C5  H5   sing N N 78  
A1ARI C5  H    sing N N 79  
A1ARI C6  H61  sing N N 80  
A1ARI C6  H62  sing N N 81  
A1ARI C7  H7   sing N N 82  
A1ARI C8  H82  sing N N 83  
A1ARI C8  H81  sing N N 84  
A1ARI C9  H92  sing N N 85  
A1ARI C9  H91  sing N N 86  
A1ARI N1  HN1  sing N N 87  
A1ARI N2  HN2  sing N N 88  
A1ARI N3  HN3  sing N N 89  
A1ARI O2  HO2  sing N N 90  
ALA   N   CA   sing N N 91  
ALA   N   H    sing N N 92  
ALA   N   H2   sing N N 93  
ALA   CA  C    sing N N 94  
ALA   CA  CB   sing N N 95  
ALA   CA  HA   sing N N 96  
ALA   C   O    doub N N 97  
ALA   C   OXT  sing N N 98  
ALA   CB  HB1  sing N N 99  
ALA   CB  HB2  sing N N 100 
ALA   CB  HB3  sing N N 101 
ALA   OXT HXT  sing N N 102 
ARG   N   CA   sing N N 103 
ARG   N   H    sing N N 104 
ARG   N   H2   sing N N 105 
ARG   CA  C    sing N N 106 
ARG   CA  CB   sing N N 107 
ARG   CA  HA   sing N N 108 
ARG   C   O    doub N N 109 
ARG   C   OXT  sing N N 110 
ARG   CB  CG   sing N N 111 
ARG   CB  HB2  sing N N 112 
ARG   CB  HB3  sing N N 113 
ARG   CG  CD   sing N N 114 
ARG   CG  HG2  sing N N 115 
ARG   CG  HG3  sing N N 116 
ARG   CD  NE   sing N N 117 
ARG   CD  HD2  sing N N 118 
ARG   CD  HD3  sing N N 119 
ARG   NE  CZ   sing N N 120 
ARG   NE  HE   sing N N 121 
ARG   CZ  NH1  sing N N 122 
ARG   CZ  NH2  doub N N 123 
ARG   NH1 HH11 sing N N 124 
ARG   NH1 HH12 sing N N 125 
ARG   NH2 HH21 sing N N 126 
ARG   NH2 HH22 sing N N 127 
ARG   OXT HXT  sing N N 128 
ASN   N   CA   sing N N 129 
ASN   N   H    sing N N 130 
ASN   N   H2   sing N N 131 
ASN   CA  C    sing N N 132 
ASN   CA  CB   sing N N 133 
ASN   CA  HA   sing N N 134 
ASN   C   O    doub N N 135 
ASN   C   OXT  sing N N 136 
ASN   CB  CG   sing N N 137 
ASN   CB  HB2  sing N N 138 
ASN   CB  HB3  sing N N 139 
ASN   CG  OD1  doub N N 140 
ASN   CG  ND2  sing N N 141 
ASN   ND2 HD21 sing N N 142 
ASN   ND2 HD22 sing N N 143 
ASN   OXT HXT  sing N N 144 
ASP   N   CA   sing N N 145 
ASP   N   H    sing N N 146 
ASP   N   H2   sing N N 147 
ASP   CA  C    sing N N 148 
ASP   CA  CB   sing N N 149 
ASP   CA  HA   sing N N 150 
ASP   C   O    doub N N 151 
ASP   C   OXT  sing N N 152 
ASP   CB  CG   sing N N 153 
ASP   CB  HB2  sing N N 154 
ASP   CB  HB3  sing N N 155 
ASP   CG  OD1  doub N N 156 
ASP   CG  OD2  sing N N 157 
ASP   OD2 HD2  sing N N 158 
ASP   OXT HXT  sing N N 159 
CYS   N   CA   sing N N 160 
CYS   N   H    sing N N 161 
CYS   N   H2   sing N N 162 
CYS   CA  C    sing N N 163 
CYS   CA  CB   sing N N 164 
CYS   CA  HA   sing N N 165 
CYS   C   O    doub N N 166 
CYS   C   OXT  sing N N 167 
CYS   CB  SG   sing N N 168 
CYS   CB  HB2  sing N N 169 
CYS   CB  HB3  sing N N 170 
CYS   SG  HG   sing N N 171 
CYS   OXT HXT  sing N N 172 
GLN   N   CA   sing N N 173 
GLN   N   H    sing N N 174 
GLN   N   H2   sing N N 175 
GLN   CA  C    sing N N 176 
GLN   CA  CB   sing N N 177 
GLN   CA  HA   sing N N 178 
GLN   C   O    doub N N 179 
GLN   C   OXT  sing N N 180 
GLN   CB  CG   sing N N 181 
GLN   CB  HB2  sing N N 182 
GLN   CB  HB3  sing N N 183 
GLN   CG  CD   sing N N 184 
GLN   CG  HG2  sing N N 185 
GLN   CG  HG3  sing N N 186 
GLN   CD  OE1  doub N N 187 
GLN   CD  NE2  sing N N 188 
GLN   NE2 HE21 sing N N 189 
GLN   NE2 HE22 sing N N 190 
GLN   OXT HXT  sing N N 191 
GLU   N   CA   sing N N 192 
GLU   N   H    sing N N 193 
GLU   N   H2   sing N N 194 
GLU   CA  C    sing N N 195 
GLU   CA  CB   sing N N 196 
GLU   CA  HA   sing N N 197 
GLU   C   O    doub N N 198 
GLU   C   OXT  sing N N 199 
GLU   CB  CG   sing N N 200 
GLU   CB  HB2  sing N N 201 
GLU   CB  HB3  sing N N 202 
GLU   CG  CD   sing N N 203 
GLU   CG  HG2  sing N N 204 
GLU   CG  HG3  sing N N 205 
GLU   CD  OE1  doub N N 206 
GLU   CD  OE2  sing N N 207 
GLU   OE2 HE2  sing N N 208 
GLU   OXT HXT  sing N N 209 
GLY   N   CA   sing N N 210 
GLY   N   H    sing N N 211 
GLY   N   H2   sing N N 212 
GLY   CA  C    sing N N 213 
GLY   CA  HA2  sing N N 214 
GLY   CA  HA3  sing N N 215 
GLY   C   O    doub N N 216 
GLY   C   OXT  sing N N 217 
GLY   OXT HXT  sing N N 218 
HIS   N   CA   sing N N 219 
HIS   N   H    sing N N 220 
HIS   N   H2   sing N N 221 
HIS   CA  C    sing N N 222 
HIS   CA  CB   sing N N 223 
HIS   CA  HA   sing N N 224 
HIS   C   O    doub N N 225 
HIS   C   OXT  sing N N 226 
HIS   CB  CG   sing N N 227 
HIS   CB  HB2  sing N N 228 
HIS   CB  HB3  sing N N 229 
HIS   CG  ND1  sing Y N 230 
HIS   CG  CD2  doub Y N 231 
HIS   ND1 CE1  doub Y N 232 
HIS   ND1 HD1  sing N N 233 
HIS   CD2 NE2  sing Y N 234 
HIS   CD2 HD2  sing N N 235 
HIS   CE1 NE2  sing Y N 236 
HIS   CE1 HE1  sing N N 237 
HIS   NE2 HE2  sing N N 238 
HIS   OXT HXT  sing N N 239 
HOH   O   H1   sing N N 240 
HOH   O   H2   sing N N 241 
ILE   N   CA   sing N N 242 
ILE   N   H    sing N N 243 
ILE   N   H2   sing N N 244 
ILE   CA  C    sing N N 245 
ILE   CA  CB   sing N N 246 
ILE   CA  HA   sing N N 247 
ILE   C   O    doub N N 248 
ILE   C   OXT  sing N N 249 
ILE   CB  CG1  sing N N 250 
ILE   CB  CG2  sing N N 251 
ILE   CB  HB   sing N N 252 
ILE   CG1 CD1  sing N N 253 
ILE   CG1 HG12 sing N N 254 
ILE   CG1 HG13 sing N N 255 
ILE   CG2 HG21 sing N N 256 
ILE   CG2 HG22 sing N N 257 
ILE   CG2 HG23 sing N N 258 
ILE   CD1 HD11 sing N N 259 
ILE   CD1 HD12 sing N N 260 
ILE   CD1 HD13 sing N N 261 
ILE   OXT HXT  sing N N 262 
LEU   N   CA   sing N N 263 
LEU   N   H    sing N N 264 
LEU   N   H2   sing N N 265 
LEU   CA  C    sing N N 266 
LEU   CA  CB   sing N N 267 
LEU   CA  HA   sing N N 268 
LEU   C   O    doub N N 269 
LEU   C   OXT  sing N N 270 
LEU   CB  CG   sing N N 271 
LEU   CB  HB2  sing N N 272 
LEU   CB  HB3  sing N N 273 
LEU   CG  CD1  sing N N 274 
LEU   CG  CD2  sing N N 275 
LEU   CG  HG   sing N N 276 
LEU   CD1 HD11 sing N N 277 
LEU   CD1 HD12 sing N N 278 
LEU   CD1 HD13 sing N N 279 
LEU   CD2 HD21 sing N N 280 
LEU   CD2 HD22 sing N N 281 
LEU   CD2 HD23 sing N N 282 
LEU   OXT HXT  sing N N 283 
LYS   N   CA   sing N N 284 
LYS   N   H    sing N N 285 
LYS   N   H2   sing N N 286 
LYS   CA  C    sing N N 287 
LYS   CA  CB   sing N N 288 
LYS   CA  HA   sing N N 289 
LYS   C   O    doub N N 290 
LYS   C   OXT  sing N N 291 
LYS   CB  CG   sing N N 292 
LYS   CB  HB2  sing N N 293 
LYS   CB  HB3  sing N N 294 
LYS   CG  CD   sing N N 295 
LYS   CG  HG2  sing N N 296 
LYS   CG  HG3  sing N N 297 
LYS   CD  CE   sing N N 298 
LYS   CD  HD2  sing N N 299 
LYS   CD  HD3  sing N N 300 
LYS   CE  NZ   sing N N 301 
LYS   CE  HE2  sing N N 302 
LYS   CE  HE3  sing N N 303 
LYS   NZ  HZ1  sing N N 304 
LYS   NZ  HZ2  sing N N 305 
LYS   NZ  HZ3  sing N N 306 
LYS   OXT HXT  sing N N 307 
MET   N   CA   sing N N 308 
MET   N   H    sing N N 309 
MET   N   H2   sing N N 310 
MET   CA  C    sing N N 311 
MET   CA  CB   sing N N 312 
MET   CA  HA   sing N N 313 
MET   C   O    doub N N 314 
MET   C   OXT  sing N N 315 
MET   CB  CG   sing N N 316 
MET   CB  HB2  sing N N 317 
MET   CB  HB3  sing N N 318 
MET   CG  SD   sing N N 319 
MET   CG  HG2  sing N N 320 
MET   CG  HG3  sing N N 321 
MET   SD  CE   sing N N 322 
MET   CE  HE1  sing N N 323 
MET   CE  HE2  sing N N 324 
MET   CE  HE3  sing N N 325 
MET   OXT HXT  sing N N 326 
PHE   N   CA   sing N N 327 
PHE   N   H    sing N N 328 
PHE   N   H2   sing N N 329 
PHE   CA  C    sing N N 330 
PHE   CA  CB   sing N N 331 
PHE   CA  HA   sing N N 332 
PHE   C   O    doub N N 333 
PHE   C   OXT  sing N N 334 
PHE   CB  CG   sing N N 335 
PHE   CB  HB2  sing N N 336 
PHE   CB  HB3  sing N N 337 
PHE   CG  CD1  doub Y N 338 
PHE   CG  CD2  sing Y N 339 
PHE   CD1 CE1  sing Y N 340 
PHE   CD1 HD1  sing N N 341 
PHE   CD2 CE2  doub Y N 342 
PHE   CD2 HD2  sing N N 343 
PHE   CE1 CZ   doub Y N 344 
PHE   CE1 HE1  sing N N 345 
PHE   CE2 CZ   sing Y N 346 
PHE   CE2 HE2  sing N N 347 
PHE   CZ  HZ   sing N N 348 
PHE   OXT HXT  sing N N 349 
PRO   N   CA   sing N N 350 
PRO   N   CD   sing N N 351 
PRO   N   H    sing N N 352 
PRO   CA  C    sing N N 353 
PRO   CA  CB   sing N N 354 
PRO   CA  HA   sing N N 355 
PRO   C   O    doub N N 356 
PRO   C   OXT  sing N N 357 
PRO   CB  CG   sing N N 358 
PRO   CB  HB2  sing N N 359 
PRO   CB  HB3  sing N N 360 
PRO   CG  CD   sing N N 361 
PRO   CG  HG2  sing N N 362 
PRO   CG  HG3  sing N N 363 
PRO   CD  HD2  sing N N 364 
PRO   CD  HD3  sing N N 365 
PRO   OXT HXT  sing N N 366 
SER   N   CA   sing N N 367 
SER   N   H    sing N N 368 
SER   N   H2   sing N N 369 
SER   CA  C    sing N N 370 
SER   CA  CB   sing N N 371 
SER   CA  HA   sing N N 372 
SER   C   O    doub N N 373 
SER   C   OXT  sing N N 374 
SER   CB  OG   sing N N 375 
SER   CB  HB2  sing N N 376 
SER   CB  HB3  sing N N 377 
SER   OG  HG   sing N N 378 
SER   OXT HXT  sing N N 379 
THR   N   CA   sing N N 380 
THR   N   H    sing N N 381 
THR   N   H2   sing N N 382 
THR   CA  C    sing N N 383 
THR   CA  CB   sing N N 384 
THR   CA  HA   sing N N 385 
THR   C   O    doub N N 386 
THR   C   OXT  sing N N 387 
THR   CB  OG1  sing N N 388 
THR   CB  CG2  sing N N 389 
THR   CB  HB   sing N N 390 
THR   OG1 HG1  sing N N 391 
THR   CG2 HG21 sing N N 392 
THR   CG2 HG22 sing N N 393 
THR   CG2 HG23 sing N N 394 
THR   OXT HXT  sing N N 395 
TRP   N   CA   sing N N 396 
TRP   N   H    sing N N 397 
TRP   N   H2   sing N N 398 
TRP   CA  C    sing N N 399 
TRP   CA  CB   sing N N 400 
TRP   CA  HA   sing N N 401 
TRP   C   O    doub N N 402 
TRP   C   OXT  sing N N 403 
TRP   CB  CG   sing N N 404 
TRP   CB  HB2  sing N N 405 
TRP   CB  HB3  sing N N 406 
TRP   CG  CD1  doub Y N 407 
TRP   CG  CD2  sing Y N 408 
TRP   CD1 NE1  sing Y N 409 
TRP   CD1 HD1  sing N N 410 
TRP   CD2 CE2  doub Y N 411 
TRP   CD2 CE3  sing Y N 412 
TRP   NE1 CE2  sing Y N 413 
TRP   NE1 HE1  sing N N 414 
TRP   CE2 CZ2  sing Y N 415 
TRP   CE3 CZ3  doub Y N 416 
TRP   CE3 HE3  sing N N 417 
TRP   CZ2 CH2  doub Y N 418 
TRP   CZ2 HZ2  sing N N 419 
TRP   CZ3 CH2  sing Y N 420 
TRP   CZ3 HZ3  sing N N 421 
TRP   CH2 HH2  sing N N 422 
TRP   OXT HXT  sing N N 423 
TYR   N   CA   sing N N 424 
TYR   N   H    sing N N 425 
TYR   N   H2   sing N N 426 
TYR   CA  C    sing N N 427 
TYR   CA  CB   sing N N 428 
TYR   CA  HA   sing N N 429 
TYR   C   O    doub N N 430 
TYR   C   OXT  sing N N 431 
TYR   CB  CG   sing N N 432 
TYR   CB  HB2  sing N N 433 
TYR   CB  HB3  sing N N 434 
TYR   CG  CD1  doub Y N 435 
TYR   CG  CD2  sing Y N 436 
TYR   CD1 CE1  sing Y N 437 
TYR   CD1 HD1  sing N N 438 
TYR   CD2 CE2  doub Y N 439 
TYR   CD2 HD2  sing N N 440 
TYR   CE1 CZ   doub Y N 441 
TYR   CE1 HE1  sing N N 442 
TYR   CE2 CZ   sing Y N 443 
TYR   CE2 HE2  sing N N 444 
TYR   CZ  OH   sing N N 445 
TYR   OH  HH   sing N N 446 
TYR   OXT HXT  sing N N 447 
VAL   N   CA   sing N N 448 
VAL   N   H    sing N N 449 
VAL   N   H2   sing N N 450 
VAL   CA  C    sing N N 451 
VAL   CA  CB   sing N N 452 
VAL   CA  HA   sing N N 453 
VAL   C   O    doub N N 454 
VAL   C   OXT  sing N N 455 
VAL   CB  CG1  sing N N 456 
VAL   CB  CG2  sing N N 457 
VAL   CB  HB   sing N N 458 
VAL   CG1 HG11 sing N N 459 
VAL   CG1 HG12 sing N N 460 
VAL   CG1 HG13 sing N N 461 
VAL   CG2 HG21 sing N N 462 
VAL   CG2 HG22 sing N N 463 
VAL   CG2 HG23 sing N N 464 
VAL   OXT HXT  sing N N 465 
# 
_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                    9BQM 
_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]   0.018354 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002133 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012125 
_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]   0.011579 
_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.
;
? 
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   ? -35.67047 -19.36032 14.81663  1.000 23.42701 ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? -34.73028 -20.41458 14.47327  1.000 23.99483 ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? -34.54040 -20.53046 12.95789  1.000 21.24181 ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? -35.01370 -19.67889 12.19939  1.000 20.17382 ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? -35.20264 -21.75012 15.03621  1.000 23.32754 ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? -36.27008 -22.23527 14.26842  1.000 26.82890 ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? -33.86583 -21.60138 12.53811  1.000 20.86666 ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? -33.55199 -21.86389 11.14895  1.000 21.69977 ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? -32.13757 -21.42848 10.80919  1.000 19.06487 ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? -31.49852 -20.66970 11.53251  1.000 18.13145 ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? -31.63405 -21.92183 9.68074   1.000 16.72627 ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? -30.23382 -21.69491 9.35385   1.000 19.27063 ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? -30.06133 -21.57325 7.85375   1.000 20.64970 ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? -30.52821 -22.43320 7.09918   1.000 25.95345 ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? -29.36494 -22.82336 9.89739   1.000 19.70830 ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? -27.96810 -22.41748 10.12126  1.000 20.75769 ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? -27.65107 -21.56504 11.15081  1.000 22.03988 ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? -26.95730 -22.86684 9.28820   1.000 19.45196 ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? -26.34167 -21.17488 11.35586  1.000 20.35721 ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? -25.65082 -22.48385 9.49097   1.000 17.03196 ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? -25.34360 -21.63759 10.52059  1.000 19.52536 ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? -29.40722 -20.50342 7.42681   1.000 18.10090 ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? -29.37108 -20.13834 6.02619   1.000 17.91677 ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? -27.98227 -19.63547 5.66782   1.000 17.05376 ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? -27.30572 -19.02824 6.49531   1.000 17.18309 ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? -30.40727 -19.05275 5.72834   1.000 16.16051 ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? -31.79999 -19.58992 5.48181   1.000 20.87748 ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? -31.84970 -20.24900 4.13370   1.000 19.34195 ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? -33.22030 -20.51018 3.70870   1.000 21.79140 ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? -33.53358 -21.05836 2.54366   1.000 22.23937 ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? -34.80752 -21.27610 2.22627   1.000 20.89110 ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? -32.56122 -21.39169 1.69722   1.000 20.71933 ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? -27.56254 -19.86594 4.42381   1.000 17.65758 ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? -26.35265 -19.19494 3.94910   1.000 17.92234 ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? -26.63428 -17.71626 3.84081   1.000 17.16771 ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? -27.27343 -17.24232 2.89721   1.000 19.39780 ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? -25.84587 -19.76142 2.63474   1.000 17.95885 ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? -24.64032 -20.57548 2.92637   1.000 19.96375 ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? -24.22698 -21.50756 1.83548   1.000 24.70643 ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? -22.96100 -22.24158 2.29572   1.000 20.03184 ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? -22.99105 -23.66480 1.83726   1.000 26.51721 ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? -26.14809 -16.97801 4.81130   1.000 15.59240 ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? -26.50781 -15.58344 4.95475   1.000 17.14115 ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? -25.32565 -14.74497 4.51019   1.000 16.19859 ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? -24.22633 -14.91317 5.03964   1.000 15.57784 ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? -26.84681 -15.28407 6.40622   1.000 15.92799 ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? -27.52045 -13.96364 6.61716   1.000 19.67351 ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? -28.07975 -14.01682 8.30235   1.000 28.68122 ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? -29.47671 -15.10314 8.07585   1.000 17.69086 ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? -25.54788 -13.84463 3.56695   1.000 13.66856 ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? -24.53657 -12.85153 3.23549   1.000 15.35522 ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? -24.77572 -11.57164 4.02776   1.000 16.29094 ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? -25.86773 -11.34073 4.54524   1.000 14.45310 ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? -24.53886 -12.54795 1.74281   1.000 16.73783 ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? -23.72004 -10.74840 4.14419   1.000 12.98524 ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? -23.87985 -9.44125  4.76374   1.000 16.08091 ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? -24.74494 -8.55154  3.87313   1.000 14.15273 ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? -24.70123 -8.66816  2.64907   1.000 11.67371 ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? -22.52604 -8.76434  4.98601   1.000 12.45036 ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? -21.72198 -9.39266  6.07621   1.000 15.96325 ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? -21.86347 -8.98410  7.38251   1.000 19.89865 ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? -20.85023 -10.42220 5.80058   1.000 13.39420 ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? -21.13031 -9.58150  8.39057   1.000 22.60880 ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? -20.12784 -11.02339 6.81368   1.000 16.58307 ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? -20.26330 -10.60357 8.10361   1.000 18.28612 ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? -25.49779 -7.62481  4.46366   1.000 13.63271 ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? -26.14949 -6.60235  3.63955   1.000 15.69430 ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? -25.09064 -5.88401  2.80934   1.000 17.81811 ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? -23.97930 -5.61821  3.28157   1.000 11.12180 ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? -26.80777 -5.66970  4.67361   1.000 19.19975 ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? -26.80143 -6.43090  5.98016   1.000 19.70478 ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? -25.57303 -7.30919  5.89631   1.000 17.17095 ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? -25.43204 -5.60592  1.54995   1.000 13.72992 ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? -24.46758 -5.19618  0.53816   1.000 13.18574 ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? -24.55611 -3.72521  0.18576   1.000 17.01737 ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? -23.86336 -3.27296  -0.74355  1.000 15.61685 ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? -24.64369 -6.02802  -0.73029  1.000 14.82747 ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? -25.86130 -5.71068  -1.40793  1.000 15.25172 ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? -25.37968 -2.95614  0.88829   1.000 17.11048 ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? -25.53533 -1.56375  0.49212   1.000 17.70035 ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? -24.25425 -0.74128  0.57215   1.000 18.63549 ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? -24.01812 0.13871   -0.26397  1.000 18.75443 ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? -23.44160 -0.94887  1.61572   1.000 19.40749 ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? -22.24373 -0.11335  1.69677   1.000 22.46741 ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? -21.26094 -0.38055  0.54951   1.000 18.87328 ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? -20.47851 0.51548   0.21724   1.000 20.68771 ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? -21.52452 -0.22929  3.04587   1.000 23.51997 ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? -21.94349 0.73760   4.24226   1.000 28.67880 ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? -23.01638 0.37704   5.23449   1.000 35.36795 ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? -22.50348 -0.82538  6.04876   1.000 39.43115 ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? -23.24703 -1.23000  7.32298   1.000 43.72165 ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? -21.35134 -1.53142  -0.12541  1.000 16.76188 ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? -20.47161 -1.88072  -1.25545  1.000 15.35534 ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? -21.08360 -1.50490  -2.59651  1.000 16.83369 ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? -20.37332 -1.07883  -3.51046  1.000 15.49540 ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? -20.14874 -3.38998  -1.19377  1.000 13.74089 ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? -19.37160 -3.84977  -2.42989  1.000 15.16829 ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? -19.33363 -3.68800  0.05062   1.000 16.01353 ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? -22.39758 -1.71674  -2.75272  1.000 15.39695 ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? -23.07925 -1.23784  -3.94530  1.000 17.65032 ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? -22.69274 0.20720   -4.23949  1.000 17.48713 ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? -22.41804 0.56678   -5.39370  1.000 16.85923 ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? -24.59945 -1.37469  -3.78495  1.000 16.74903 ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? -25.12521 -2.82152  -3.58793  1.000 17.30445 ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? -26.59898 -2.85527  -3.16930  1.000 17.23738 ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? -27.39193 -2.07323  -3.71824  1.000 19.26857 ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? -26.97327 -3.63869  -2.26658  1.000 17.49562 ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? -22.62433 1.04006   -3.19794  1.000 17.12091 ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? -22.28219 2.44508   -3.35996  1.000 19.93069 ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? -20.86040 2.71457   -3.83164  1.000 19.09106 ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? -20.52608 3.87753   -4.09299  1.000 19.95887 ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? -20.02316 1.68101   -3.93791  1.000 16.26206 ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? -18.63752 1.84670   -4.35939  1.000 19.62726 ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? -18.35172 1.31979   -5.75470  1.000 19.69061 ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? -17.27499 1.60352   -6.29674  1.000 19.61231 ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? -17.68465 1.13897   -3.38104  1.000 17.50433 ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? -17.82771 1.72763   -1.68831  1.000 18.63453 ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? -19.26202 0.56146   -6.34866  1.000 17.54408 ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? -18.95164 -0.11993  -7.59502  1.000 17.80207 ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? -19.04546 0.83419   -8.77594  1.000 21.04034 ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? -19.94730 1.67480   -8.84903  1.000 20.64160 ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? -19.87904 -1.31367  -7.79677  1.000 15.77466 ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? -19.78448 -2.36521  -6.70496  1.000 15.23931 ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? -18.08090 -2.86095  -6.38299  1.000 15.87140 ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? -17.67438 -3.59414  -7.97388  1.000 14.18652 ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? -18.09091 0.70022   -9.69961  1.000 17.62264 ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? -18.04618 1.48748   -10.92392 1.000 21.19584 ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? -17.60310 0.58268   -12.06408 1.000 21.03479 ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? -17.05186 -0.50323  -11.85781 1.000 19.75670 ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? -17.09357 2.69513   -10.83064 1.000 19.19202 ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? -17.55046 3.64844   -9.74403  1.000 20.28291 ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? -15.66320 2.22455   -10.58579 1.000 18.27848 ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? -17.84887 1.05655   -13.27891 1.000 23.14035 ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? -17.43947 0.38043   -14.49882 1.000 25.34377 ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? -16.15509 1.02364   -14.98277 1.000 24.98042 ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? -16.04593 2.24924   -14.97900 1.000 25.80807 ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? -18.52575 0.49432   -15.56913 1.000 29.45930 ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? -18.13879 -0.10246  -16.90150 1.000 30.74372 ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? -19.10758 0.27123   -18.00481 1.000 34.93770 ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? -20.10354 -0.41567  -18.22276 1.000 29.94235 ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? -18.80285 1.35744   -18.72960 1.000 44.85893 ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? -15.17808 0.20113   -15.37057 1.000 25.85414 ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? -13.88890 0.67669   -15.86941 1.000 28.15914 ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? -13.69631 0.10051   -17.25887 1.000 28.17030 ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? -13.77976 -1.11906  -17.44569 1.000 27.36696 ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? -12.71409 0.27938   -14.95796 1.000 26.10841 ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? -11.37352 0.59174   -15.65697 1.000 26.01550 ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? -12.79608 0.98831   -13.61596 1.000 24.33354 ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? -13.44888 0.97065   -18.23188 1.000 31.36254 ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? -13.30950 0.56185   -19.62285 1.000 35.86902 ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? -12.01166 1.11667   -20.18110 1.000 36.32330 ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? -11.75364 2.32046   -20.08545 1.000 39.59145 ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? -14.49095 1.04185   -20.47478 1.000 38.69153 ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? -15.69269 0.39016   -20.03977 1.000 36.68247 ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? -14.24261 0.72687   -21.95064 1.000 38.31699 ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? -11.19426 0.23755   -20.74981 1.000 38.92775 ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? -9.95684  0.63193   -21.40323 1.000 38.47702 ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? -9.79310  -0.24156  -22.63340 1.000 40.27265 ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? -9.81817  -1.47130  -22.52978 1.000 39.33514 ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? -8.75391  0.48799   -20.46409 1.000 40.50158 ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? -7.28715  1.43341   -20.96277 1.000 43.96632 ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? -9.65837  0.39371   -23.79171 1.000 43.48910 ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? -9.56205  -0.36366  -25.02659 1.000 43.66240 ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? -10.85200 -1.11284  -25.29029 1.000 42.97357 ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? -11.94526 -0.53713  -25.30330 1.000 40.74209 ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? -10.72563 -2.42098  -25.49595 1.000 47.97631 ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? -11.86212 -3.29588  -25.73845 1.000 47.35707 ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? -12.34257 -4.00273  -24.47518 1.000 46.58483 ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? -13.25134 -4.83507  -24.55392 1.000 46.78874 ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? -11.50636 -4.33511  -26.80501 1.000 49.36703 ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? -10.25505 -4.95588  -26.47446 1.000 52.58901 ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? -11.39293 -3.67706  -28.17636 1.000 48.44869 ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? -11.76614 -3.68993  -23.31642 1.000 44.52168 ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? -12.04601 -4.41136  -22.08223 1.000 39.21032 ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? -12.85572 -3.54849  -21.12221 1.000 39.17482 ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? -12.43975 -2.43330  -20.78132 1.000 36.22459 ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? -10.74982 -4.85012  -21.40160 1.000 40.54954 ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? -9.98645  -5.67093  -22.29637 1.000 43.40138 ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? -11.07168 -5.63538  -20.13279 1.000 36.82385 ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? -13.99992 -4.08015  -20.67786 1.000 34.15509 ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? -14.82645 -3.47991  -19.63499 1.000 31.32961 ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? -14.93047 -4.44267  -18.45929 1.000 29.28508 ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? -15.29059 -5.60742  -18.63736 1.000 29.68134 ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? -16.23389 -3.12444  -20.14534 1.000 33.58399 ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? -16.15960 -2.10877  -21.15762 1.000 40.96737 ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? -17.11506 -2.66487  -19.01887 1.000 33.85548 ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? -14.61268 -3.95299  -17.26580 1.000 26.68179 ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? -14.76903 -4.69971  -16.02113 1.000 24.78624 ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? -15.19900 -3.74438  -14.91232 1.000 21.98924 ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? -15.55721 -2.59160  -15.16522 1.000 22.67805 ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? -13.48555 -5.47152  -15.68375 1.000 23.69301 ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? -12.14457 -4.73800  -15.70422 1.000 22.13915 ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? -11.87632 -3.86861  -14.50123 1.000 23.37380 ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? -11.11987 -5.84667  -15.76198 1.000 23.15391 ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? -15.14250 -4.22766  -13.67528 1.000 18.31184 ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? -15.68664 -3.52776  -12.51920 1.000 19.03206 ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? -14.56326 -2.91562  -11.69933 1.000 17.49620 ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? -13.49210 -3.50408  -11.57429 1.000 16.61101 ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? -16.51578 -4.49616  -11.65923 1.000 15.55760 ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? -17.78669 -4.94131  -12.36724 1.000 19.10538 ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? -18.72569 -4.16089  -12.47662 1.000 17.51502 ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? -17.79584 -6.16785  -12.90478 1.000 14.92557 ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? -14.81084 -1.72480  -11.16332 1.000 18.91154 ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? -13.85585 -1.06926  -10.29075 1.000 19.32519 ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? -14.42894 -0.82739  -8.91089  1.000 17.46953 ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? -15.64565 -0.87912  -8.73112  1.000 13.67872 ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? -13.57101 -0.59245  -7.92382  1.000 18.66989 ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? -14.00636 -0.28890  -6.56187  1.000 17.93298 ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? -13.55671 1.12771   -6.24663  1.000 18.93137 ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? -12.35413 1.39271   -6.14900  1.000 15.23285 ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? -13.44425 -1.28326  -5.54818  1.000 14.10831 ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? -13.99710 -1.15883  -4.12445  1.000 15.35798 ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? -15.47954 -1.56428  -4.08487  1.000 16.61524 ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? -13.19944 -2.01817  -3.14578  1.000 11.15906 ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? -14.52799 2.02799   -6.09480  1.000 17.11289 ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? -14.29556 3.45054   -5.87328  1.000 18.56961 ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? -14.35680 3.75167   -4.37782  1.000 21.78699 ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? -15.44217 3.75411   -3.78647  1.000 19.50892 ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? -15.34742 4.24608   -6.62795  1.000 20.06293 ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? -15.16934 5.71342   -6.66196  1.000 22.73050 ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? -14.01345 6.42110   -6.47516  1.000 23.92093 ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? -16.19453 6.67554   -6.93354  1.000 24.37732 ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? -14.26170 7.77692   -6.61160  1.000 26.44147 ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? -15.59374 7.95342   -6.89090  1.000 26.03571 ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? -17.56437 6.57846   -7.21175  1.000 23.41009 ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? -16.31234 9.11298   -7.10658  1.000 27.43424 ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? -18.27932 7.73537   -7.42506  1.000 26.09979 ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? -17.65595 8.98683   -7.36785  1.000 30.76444 ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? -13.19541 4.02397   -3.77274  1.000 19.47620 ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? -13.10063 4.40658   -2.36941  1.000 20.28485 ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? -12.30767 5.69754   -2.28507  1.000 24.23050 ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? -11.18468 5.76309   -2.79645  1.000 22.78470 ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? -12.41319 3.32268   -1.53146  1.000 20.43104 ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? -13.11568 1.96742   -1.45328  1.000 21.84255 ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? -12.17503 0.89104   -0.93060  1.000 15.63351 ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? -14.40157 2.03922   -0.62334  1.000 17.51570 ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? -12.88223 6.71393   -1.63290  1.000 23.83592 ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? -12.30127 8.05901   -1.61972  1.000 27.05944 ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? -12.05686 8.44670   -3.07000  1.000 28.38755 ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? -12.97671 8.30620   -3.90086  1.000 28.34573 ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? -11.07225 8.07751   -0.70183  1.000 28.18362 ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? -11.42706 7.78997   0.75223   1.000 29.19015 ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? -12.22465 8.56418   1.33430   1.000 32.75754 ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? -10.93131 6.79091   1.30782   1.000 28.45344 ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? -10.86215 8.88606   -3.45936  1.000 28.51702 ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? -10.61269 9.30472   -4.83030  1.000 27.11973 ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? -9.76445  8.30051   -5.61929  1.000 26.81198 ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? -9.04024  8.68316   -6.53975  1.000 27.45232 ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? -9.97349  10.69049  -4.84129  1.000 29.63414 ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? -8.55758  10.69482  -4.28720  1.000 34.18266 ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? -8.19185  9.75583   -3.53591  1.000 33.81748 ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? -7.81751  11.65739  -4.58996  1.000 35.61961 ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? -9.87319  7.00866   -5.30431  1.000 24.14304 ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? -9.13151  5.96672   -6.00144  1.000 19.60817 ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? -10.08821 4.87531   -6.45403  1.000 21.43363 ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? -10.97955 4.46354   -5.69823  1.000 21.45226 ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? -8.02657  5.37258   -5.10893  1.000 21.31945 ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? -7.49768  4.07276   -5.72135  1.000 16.76958 ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? -6.90986  6.40343   -4.89949  1.000 20.62229 ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? -9.89568  4.39493   -7.68231  1.000 18.80272 ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? -10.66223 3.27485   -8.22321  1.000 19.97650 ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? -9.72098  2.08363   -8.38856  1.000 19.53405 ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? -8.74732  2.15331   -9.14990  1.000 19.80723 ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? -11.34245 3.64253   -9.55425  1.000 20.80253 ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? -11.89006 2.39847   -10.25067 1.000 16.36398 ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? -12.44567 4.67996   -9.31563  1.000 19.09306 ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? -10.01799 0.99221   -7.67997  1.000 17.09951 ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? -9.22898  -0.23558  -7.71021  1.000 17.47359 ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? -9.85613  -1.20255  -8.70308  1.000 17.31871 ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? -11.08068 -1.31985  -8.76083  1.000 20.84188 ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? -9.16491  -0.89004  -6.31900  1.000 15.59644 ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? -8.67931  0.02029   -5.20637  1.000 16.92657 ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? -9.50984  1.00237   -4.68892  1.000 15.96860 ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? -7.39686  -0.11318  -4.66129  1.000 18.13471 ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? -9.10081  1.83376   -3.68736  1.000 17.97176 ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? -6.96351  0.73971   -3.64223  1.000 18.54655 ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? -7.82711  1.71084   -3.16518  1.000 20.40900 ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? -7.45740  2.57950   -2.16935  1.000 19.66254 ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? -9.02807  -1.89136  -9.49271  1.000 17.06473 ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? -9.54035  -2.84557  -10.46244 1.000 17.49922 ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? -8.41216  -3.79359  -10.86924 1.000 19.51044 ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? -7.23639  -3.50146  -10.61894 1.000 16.11890 ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? -10.13560 -2.12614  -11.68469 1.000 15.48055 ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? -8.93100  -1.51337  -12.91687 1.000 21.03230 ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? -8.72549  -4.94061  -11.47907 1.000 17.30192 ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? -7.66037  -5.86888  -11.87695 1.000 17.11018 ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? -6.81656  -5.29622  -13.01015 1.000 20.58858 ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? -7.33688  -4.73127  -13.97484 1.000 16.74110 ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? -8.41824  -7.12591  -12.32736 1.000 15.88816 ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? -9.84283  -6.92590  -11.90422 1.000 14.36841 ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? -10.05429 -5.44808  -11.86659 1.000 16.23820 ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? -5.49483  -5.45882  -12.89157 1.000 17.87607 ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? -4.59260  -4.83379  -13.85836 1.000 20.28260 ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? -4.70619  -5.42305  -15.26503 1.000 21.88383 ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? -4.29462  -4.76432  -16.22370 1.000 24.15834 ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? -3.13667  -4.92085  -13.36579 1.000 20.13622 ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? -2.53658  -6.31750  -13.40852 1.000 20.38729 ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? -1.06372  -6.31797  -13.01907 1.000 18.79634 ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? -0.53500  -7.68151  -13.00232 1.000 19.41308 ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? 0.74566   -7.99022  -12.82137 1.000 19.89061 ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? 1.65920   -7.02376  -12.63935 1.000 18.85128 ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? 1.11768   -9.26523  -12.83482 1.000 18.29787 ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? -5.26753  -6.62328  -15.43451 1.000 23.98641 ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? -5.38356  -7.12778  -16.80609 1.000 26.09821 ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? -6.39942  -6.34895  -17.64130 1.000 28.38150 ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? -6.56156  -6.68018  -18.81695 1.000 28.55725 ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? -5.71275  -8.63801  -16.83022 1.000 26.58704 ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? -7.08693  -8.99198  -16.33647 1.000 28.03203 ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? -8.24101  -8.62557  -17.00011 1.000 27.80807 ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? -7.48723  -9.69600  -15.24783 1.000 25.83036 ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? -9.29425  -9.07666  -16.33500 1.000 25.14277 ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? -8.86597  -9.73158  -15.27028 1.000 26.47310 ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? -7.05559  -5.32031  -17.08558 1.000 24.23259 ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? -7.84519  -4.39237  -17.89691 1.000 29.53791 ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? -6.99352  -3.65681  -18.92333 1.000 34.20466 ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? -7.52985  -3.10225  -19.88546 1.000 36.63052 ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? -8.58906  -3.36316  -17.01711 1.000 28.65329 ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? -7.63200  -2.29549  -16.52008 1.000 25.57813 ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? -9.74737  -2.72218  -17.80126 1.000 30.17658 ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? -5.67299  -3.61169  -18.74504 1.000 32.81489 ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? -4.84137  -2.97501  -19.76390 1.000 39.13770 ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? -4.37704  -3.96038  -20.82814 1.000 39.05358 ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? -3.79939  -3.53006  -21.83625 1.000 45.43012 ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? -3.70987  -2.19719  -19.06003 1.000 34.55573 ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? -2.82972  -3.11896  -18.21829 1.000 34.43600 ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? -4.30792  -1.08454  -18.20926 1.000 38.85298 ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? -1.65133  -2.42384  -17.53896 1.000 33.16903 ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? -4.66782  -5.25438  -20.66453 1.000 43.14165 ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? -4.49717  -6.28263  -21.68144 1.000 54.57748 ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? -5.58484  -6.20537  -22.76005 1.000 60.84398 ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? -6.60244  -5.51517  -22.60436 1.000 58.89540 ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? -4.54253  -7.68662  -21.06771 1.000 55.02633 ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? -3.17577  -8.17389  -20.00518 1.000 62.34827 ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? -5.36227  -6.93102  -23.83838 1.000 70.26448 ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? -6.39317  -7.22868  -24.83998 1.000 73.32561 ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? -6.27930  -8.71097  -25.19233 1.000 78.07872 ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? -5.71670  -9.51187  -24.43535 1.000 76.40933 ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? -6.28125  -6.30813  -26.07138 1.000 76.45984 ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? -4.93869  -6.31965  -26.58199 1.000 79.58152 ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? -6.71567  -4.87394  -25.73643 1.000 69.22917 ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? -6.81141  -9.09586  -26.36013 1.000 85.00027 ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? -6.85900  -10.50882 -26.73948 1.000 86.82690 ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? -5.49088  -11.07382 -27.12223 1.000 85.82245 ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? -5.29516  -12.29308 -27.03831 1.000 84.53577 ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? -7.85534  -10.71680 -27.88797 1.000 86.45253 ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? -9.18458  -10.42876 -27.47518 1.000 82.74202 ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? -4.54312  -10.22978 -27.54448 1.000 83.97566 ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? -3.18141  -10.68523 -27.78991 1.000 82.39659 ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? -2.19523  -10.25317 -26.71282 1.000 81.06744 ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? -1.09069  -10.80707 -26.65506 1.000 77.85566 ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? -2.69082  -10.20427 -29.16469 1.000 82.49415 ? 47  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 47  ? -2.65915  -8.70019  -29.35488 1.000 80.47785 ? 47  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 47  ? -2.00037  -8.30277  -30.66466 1.000 83.43332 ? 47  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 47  ? -1.37368  -9.17271  -31.31174 1.000 83.55548 ? 47  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 47  ? -2.10897  -7.11983  -31.05052 1.000 82.94146 ? 47  GLU   A OE2 1 
ATOM   356  N N   . ASP   A 1 48  ? -2.56953  -9.29039  -25.85711 1.000 80.86206 ? 48  ASP   A N   1 
ATOM   357  C CA  . ASP   A 1 48  ? -1.79490  -9.00384  -24.65155 1.000 76.88832 ? 48  ASP   A CA  1 
ATOM   358  C C   . ASP   A 1 48  ? -1.92143  -10.11450 -23.61058 1.000 75.00968 ? 48  ASP   A C   1 
ATOM   359  O O   . ASP   A 1 48  ? -1.11061  -10.16794 -22.67828 1.000 70.96955 ? 48  ASP   A O   1 
ATOM   360  C CB  . ASP   A 1 48  ? -2.23344  -7.67813  -24.00317 1.000 69.35272 ? 48  ASP   A CB  1 
ATOM   361  C CG  . ASP   A 1 48  ? -2.24016  -6.49165  -24.97339 1.000 71.22972 ? 48  ASP   A CG  1 
ATOM   362  O OD1 . ASP   A 1 48  ? -1.56104  -6.54472  -26.02111 1.000 73.22709 ? 48  ASP   A OD1 1 
ATOM   363  O OD2 . ASP   A 1 48  ? -2.93038  -5.48954  -24.67024 1.000 66.12784 ? 48  ASP   A OD2 1 
ATOM   364  N N   . MET   A 1 49  ? -2.91300  -11.00380 -23.74955 1.000 77.30398 ? 49  MET   A N   1 
ATOM   365  C CA  . MET   A 1 49  ? -3.25518  -11.93014 -22.67388 1.000 72.11180 ? 49  MET   A CA  1 
ATOM   366  C C   . MET   A 1 49  ? -2.32391  -13.14136 -22.62434 1.000 71.86464 ? 49  MET   A C   1 
ATOM   367  O O   . MET   A 1 49  ? -2.17063  -13.74150 -21.54981 1.000 65.86034 ? 49  MET   A O   1 
ATOM   368  C CB  . MET   A 1 49  ? -4.72591  -12.35550 -22.82642 1.000 69.05935 ? 49  MET   A CB  1 
ATOM   369  C CG  . MET   A 1 49  ? -5.16346  -13.60902 -22.07724 1.000 64.39018 ? 49  MET   A CG  1 
ATOM   370  S SD  . MET   A 1 49  ? -6.96770  -13.76591 -22.01749 1.000 67.66338 ? 49  MET   A SD  1 
ATOM   371  C CE  . MET   A 1 49  ? -7.20528  -15.16520 -20.90605 1.000 47.05412 ? 49  MET   A CE  1 
ATOM   372  N N   . LEU   A 1 50  ? -1.66141  -13.47371 -23.74368 1.000 74.67748 ? 50  LEU   A N   1 
ATOM   373  C CA  . LEU   A 1 50  ? -0.81825  -14.66479 -23.85850 1.000 71.98769 ? 50  LEU   A CA  1 
ATOM   374  C C   . LEU   A 1 50  ? 0.22277   -14.73857 -22.74447 1.000 72.84766 ? 50  LEU   A C   1 
ATOM   375  O O   . LEU   A 1 50  ? 0.09620   -15.56104 -21.82814 1.000 67.66499 ? 50  LEU   A O   1 
ATOM   376  C CB  . LEU   A 1 50  ? -0.13049  -14.71132 -25.22735 1.000 74.37237 ? 50  LEU   A CB  1 
ATOM   377  C CG  . LEU   A 1 50  ? 0.86750   -15.85539 -25.44565 1.000 78.98069 ? 50  LEU   A CG  1 
ATOM   378  C CD1 . LEU   A 1 50  ? 0.26546   -17.20251 -25.04276 1.000 77.94616 ? 50  LEU   A CD1 1 
ATOM   379  C CD2 . LEU   A 1 50  ? 1.34490   -15.89403 -26.89472 1.000 81.08883 ? 50  LEU   A CD2 1 
ATOM   380  N N   . ASN   A 1 51  ? 1.25290   -13.89314 -22.80823 1.000 72.56927 ? 51  ASN   A N   1 
ATOM   381  C CA  . ASN   A 1 51  ? 2.24797   -13.78279 -21.73800 1.000 65.89609 ? 51  ASN   A CA  1 
ATOM   382  C C   . ASN   A 1 51  ? 2.57124   -12.31126 -21.52116 1.000 64.27766 ? 51  ASN   A C   1 
ATOM   383  O O   . ASN   A 1 51  ? 3.54694   -11.77762 -22.06925 1.000 62.17727 ? 51  ASN   A O   1 
ATOM   384  C CB  . ASN   A 1 51  ? 3.50438   -14.58869 -22.06345 1.000 67.03385 ? 51  ASN   A CB  1 
ATOM   385  C CG  . ASN   A 1 51  ? 4.44730   -14.68788 -20.88650 1.000 67.29683 ? 51  ASN   A CG  1 
ATOM   386  O OD1 . ASN   A 1 51  ? 4.21918   -14.08118 -19.84033 1.000 65.41680 ? 51  ASN   A OD1 1 
ATOM   387  N ND2 . ASN   A 1 51  ? 5.51891   -15.45549 -21.05094 1.000 71.55858 ? 51  ASN   A ND2 1 
ATOM   388  N N   . PRO   A 1 52  ? 1.77018   -11.61696 -20.69364 1.000 62.18095 ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 52  ? 1.89402   -10.15651 -20.58755 1.000 55.55220 ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 52  ? 3.13937   -9.71096  -19.84138 1.000 50.91225 ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 52  ? 3.98876   -10.52162 -19.46101 1.000 59.13048 ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 52  ? 0.62224   -9.75409  -19.83211 1.000 51.19985 ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 52  ? 0.29114   -10.96196 -19.01976 1.000 48.28220 ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 52  ? 0.69556   -12.14900 -19.83777 1.000 56.14105 ? 52  PRO   A CD  1 
ATOM   395  N N   . ASN   A 1 53  ? 3.23791   -8.40383  -19.63140 1.000 46.54811 ? 53  ASN   A N   1 
ATOM   396  C CA  . ASN   A 1 53  ? 4.37397   -7.75967  -18.98738 1.000 43.83583 ? 53  ASN   A CA  1 
ATOM   397  C C   . ASN   A 1 53  ? 3.92107   -6.35124  -18.63303 1.000 40.39056 ? 53  ASN   A C   1 
ATOM   398  O O   . ASN   A 1 53  ? 4.16466   -5.39585  -19.38322 1.000 37.90424 ? 53  ASN   A O   1 
ATOM   399  C CB  . ASN   A 1 53  ? 5.59227   -7.75836  -19.90995 1.000 43.61960 ? 53  ASN   A CB  1 
ATOM   400  C CG  . ASN   A 1 53  ? 6.73228   -6.90929  -19.38559 1.000 44.16441 ? 53  ASN   A CG  1 
ATOM   401  O OD1 . ASN   A 1 53  ? 6.73747   -6.46040  -18.23552 1.000 41.70684 ? 53  ASN   A OD1 1 
ATOM   402  N ND2 . ASN   A 1 53  ? 7.70763   -6.66936  -20.24726 1.000 50.38511 ? 53  ASN   A ND2 1 
ATOM   403  N N   . TYR   A 1 54  ? 3.26215   -6.22779  -17.47967 1.000 36.73316 ? 54  TYR   A N   1 
ATOM   404  C CA  . TYR   A 1 54  ? 2.31364   -5.14208  -17.27850 1.000 34.46769 ? 54  TYR   A CA  1 
ATOM   405  C C   . TYR   A 1 54  ? 2.99109   -3.79654  -17.08984 1.000 35.02847 ? 54  TYR   A C   1 
ATOM   406  O O   . TYR   A 1 54  ? 2.40334   -2.76890  -17.43289 1.000 34.09222 ? 54  TYR   A O   1 
ATOM   407  C CB  . TYR   A 1 54  ? 1.41584   -5.45913  -16.09445 1.000 30.82537 ? 54  TYR   A CB  1 
ATOM   408  C CG  . TYR   A 1 54  ? 0.46161   -6.59587  -16.35442 1.000 28.02879 ? 54  TYR   A CG  1 
ATOM   409  C CD1 . TYR   A 1 54  ? 0.82684   -7.90656  -16.09257 1.000 28.37796 ? 54  TYR   A CD1 1 
ATOM   410  C CD2 . TYR   A 1 54  ? -0.79995  -6.35402  -16.86697 1.000 26.88388 ? 54  TYR   A CD2 1 
ATOM   411  C CE1 . TYR   A 1 54  ? -0.04849  -8.94247  -16.32157 1.000 29.43698 ? 54  TYR   A CE1 1 
ATOM   412  C CE2 . TYR   A 1 54  ? -1.67842  -7.37330  -17.10073 1.000 30.00273 ? 54  TYR   A CE2 1 
ATOM   413  C CZ  . TYR   A 1 54  ? -1.30174  -8.67048  -16.83503 1.000 30.27500 ? 54  TYR   A CZ  1 
ATOM   414  O OH  . TYR   A 1 54  ? -2.18864  -9.69581  -17.07281 1.000 30.37587 ? 54  TYR   A OH  1 
ATOM   415  N N   . GLU   A 1 55  ? 4.20742   -3.77977  -16.54563 1.000 37.08404 ? 55  GLU   A N   1 
ATOM   416  C CA  . GLU   A 1 55  ? 5.00011   -2.55500  -16.49322 1.000 37.16303 ? 55  GLU   A CA  1 
ATOM   417  C C   . GLU   A 1 55  ? 5.13379   -1.91956  -17.87723 1.000 38.56320 ? 55  GLU   A C   1 
ATOM   418  O O   . GLU   A 1 55  ? 4.78004   -0.75318  -18.06984 1.000 37.61419 ? 55  GLU   A O   1 
ATOM   419  C CB  . GLU   A 1 55  ? 6.37171   -2.86653  -15.89358 1.000 39.95010 ? 55  GLU   A CB  1 
ATOM   420  C CG  . GLU   A 1 55  ? 6.26891   -3.63026  -14.57824 1.000 44.76092 ? 55  GLU   A CG  1 
ATOM   421  C CD  . GLU   A 1 55  ? 6.18879   -5.14260  -14.75882 1.000 45.34189 ? 55  GLU   A CD  1 
ATOM   422  O OE1 . GLU   A 1 55  ? 6.56547   -5.87030  -13.81839 1.000 47.82644 ? 55  GLU   A OE1 1 
ATOM   423  O OE2 . GLU   A 1 55  ? 5.74233   -5.60568  -15.83287 1.000 46.68040 ? 55  GLU   A OE2 1 
ATOM   424  N N   . ASP   A 1 56  ? 5.65007   -2.67733  -18.85547 1.000 40.91912 ? 56  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 56  ? 5.71208   -2.19612  -20.23822 1.000 41.92810 ? 56  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 56  ? 4.35137   -1.76581  -20.75589 1.000 38.71528 ? 56  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 56  ? 4.23504   -0.75037  -21.45574 1.000 36.82617 ? 56  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 56  ? 6.27787   -3.27529  -21.16364 1.000 45.38100 ? 56  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 56  ? 7.76580   -3.15255  -21.37141 1.000 49.22750 ? 56  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 56  ? 8.25457   -2.00674  -21.46623 1.000 44.00371 ? 56  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 56  ? 8.44038   -4.20289  -21.44499 1.000 53.24247 ? 56  ASP   A OD2 1 
ATOM   432  N N   . LEU   A 1 57  ? 3.31657   -2.55536  -20.46828 1.000 33.18624 ? 57  LEU   A N   1 
ATOM   433  C CA  . LEU   A 1 57  ? 1.98743   -2.20365  -20.94926 1.000 35.75572 ? 57  LEU   A CA  1 
ATOM   434  C C   . LEU   A 1 57  ? 1.48762   -0.91939  -20.30625 1.000 32.47539 ? 57  LEU   A C   1 
ATOM   435  O O   . LEU   A 1 57  ? 0.81602   -0.12145  -20.96300 1.000 33.87267 ? 57  LEU   A O   1 
ATOM   436  C CB  . LEU   A 1 57  ? 1.00330   -3.34721  -20.68321 1.000 36.42246 ? 57  LEU   A CB  1 
ATOM   437  C CG  . LEU   A 1 57  ? 1.32029   -4.70048  -21.32374 1.000 36.58766 ? 57  LEU   A CG  1 
ATOM   438  C CD1 . LEU   A 1 57  ? 0.17022   -5.67075  -21.09830 1.000 43.62498 ? 57  LEU   A CD1 1 
ATOM   439  C CD2 . LEU   A 1 57  ? 1.61019   -4.53791  -22.81733 1.000 38.95306 ? 57  LEU   A CD2 1 
ATOM   440  N N   . LEU   A 1 58  ? 1.81896   -0.68795  -19.03653 1.000 33.79895 ? 58  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 58  ? 1.22819   0.44120   -18.32878 1.000 33.12638 ? 58  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 58  ? 1.91569   1.75823   -18.66169 1.000 34.06973 ? 58  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 58  ? 1.25461   2.80486   -18.66783 1.000 30.77792 ? 58  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 58  ? 1.25281   0.18781   -16.82179 1.000 31.37007 ? 58  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 58  ? 0.52649   1.19696   -15.92859 1.000 32.55629 ? 58  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 58  ? -0.92922  1.31882   -16.32596 1.000 29.08378 ? 58  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 58  ? 0.62427   0.78179   -14.45587 1.000 31.48886 ? 58  LEU   A CD2 1 
ATOM   448  N N   . ILE   A 1 59  ? 3.22416   1.73424   -18.94489 1.000 35.58645 ? 59  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 59  ? 3.92200   2.96786   -19.30705 1.000 35.68059 ? 59  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 59  ? 3.43891   3.49152   -20.65847 1.000 35.13037 ? 59  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 59  ? 3.62481   4.67665   -20.96274 1.000 38.99561 ? 59  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 59  ? 5.45871   2.76393   -19.28250 1.000 35.61473 ? 59  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 59  ? 6.18856   4.10406   -19.29465 1.000 37.95751 ? 59  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 59  ? 5.92453   1.96815   -20.49764 1.000 37.12051 ? 59  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 59  ? 5.95260   4.94924   -18.03814 1.000 41.37948 ? 59  ILE   A CD1 1 
ATOM   456  N N   . ARG   A 1 60  ? 2.78015   2.65323   -21.46623 1.000 34.64528 ? 60  ARG   A N   1 
ATOM   457  C CA  . ARG   A 1 60  ? 2.28037   3.07432   -22.76895 1.000 34.08864 ? 60  ARG   A CA  1 
ATOM   458  C C   . ARG   A 1 60  ? 0.90792   3.72354   -22.71325 1.000 33.93214 ? 60  ARG   A C   1 
ATOM   459  O O   . ARG   A 1 60  ? 0.47811   4.26637   -23.73058 1.000 36.04595 ? 60  ARG   A O   1 
ATOM   460  C CB  . ARG   A 1 60  ? 2.23424   1.87910   -23.71511 1.000 34.64744 ? 60  ARG   A CB  1 
ATOM   461  C CG  . ARG   A 1 60  ? 3.59782   1.42220   -24.13245 1.000 35.85610 ? 60  ARG   A CG  1 
ATOM   462  C CD  . ARG   A 1 60  ? 3.67028   -0.05388  -24.41141 1.000 35.41823 ? 60  ARG   A CD  1 
ATOM   463  N NE  . ARG   A 1 60  ? 5.03833   -0.39054  -24.77824 1.000 41.64808 ? 60  ARG   A NE  1 
ATOM   464  C CZ  . ARG   A 1 60  ? 5.44388   -1.57640  -25.21034 1.000 45.16253 ? 60  ARG   A CZ  1 
ATOM   465  N NH1 . ARG   A 1 60  ? 4.57576   -2.57683  -25.31334 1.000 45.09285 ? 60  ARG   A NH1 1 
ATOM   466  N NH2 . ARG   A 1 60  ? 6.72499   -1.75530  -25.53341 1.000 43.44475 ? 60  ARG   A NH2 1 
ATOM   467  N N   . LYS   A 1 61  ? 0.22282   3.68592   -21.56816 1.000 34.78228 ? 61  LYS   A N   1 
ATOM   468  C CA  . LYS   A 1 61  ? -1.13763  4.19062   -21.43092 1.000 34.62431 ? 61  LYS   A CA  1 
ATOM   469  C C   . LYS   A 1 61  ? -1.13907  5.63468   -20.93803 1.000 37.68771 ? 61  LYS   A C   1 
ATOM   470  O O   . LYS   A 1 61  ? -0.29533  6.02015   -20.12144 1.000 36.14439 ? 61  LYS   A O   1 
ATOM   471  C CB  . LYS   A 1 61  ? -1.94786  3.33147   -20.45395 1.000 36.25546 ? 61  LYS   A CB  1 
ATOM   472  C CG  . LYS   A 1 61  ? -1.66375  1.83097   -20.48710 1.000 34.72777 ? 61  LYS   A CG  1 
ATOM   473  C CD  . LYS   A 1 61  ? -2.46294  1.12221   -21.57962 1.000 35.86860 ? 61  LYS   A CD  1 
ATOM   474  C CE  . LYS   A 1 61  ? -3.94913  1.38753   -21.45028 1.000 40.22252 ? 61  LYS   A CE  1 
ATOM   475  N NZ  . LYS   A 1 61  ? -4.77372  0.64863   -22.46455 1.000 41.06143 ? 61  LYS   A NZ  1 
ATOM   476  N N   . SER   A 1 62  ? -2.09925  6.42499   -21.43579 1.000 37.42669 ? 62  SER   A N   1 
ATOM   477  C CA  . SER   A 1 62  ? -2.40251  7.75751   -20.92309 1.000 40.65257 ? 62  SER   A CA  1 
ATOM   478  C C   . SER   A 1 62  ? -3.65973  7.71856   -20.04822 1.000 44.21291 ? 62  SER   A C   1 
ATOM   479  O O   . SER   A 1 62  ? -4.53047  6.85784   -20.21933 1.000 41.77710 ? 62  SER   A O   1 
ATOM   480  C CB  . SER   A 1 62  ? -2.60799  8.75338   -22.06577 1.000 39.84517 ? 62  SER   A CB  1 
ATOM   481  O OG  . SER   A 1 62  ? -1.61946  8.62213   -23.08055 1.000 43.00971 ? 62  SER   A OG  1 
ATOM   482  N N   . ASN   A 1 63  ? -3.74833  8.66937   -19.10718 1.000 41.92712 ? 63  ASN   A N   1 
ATOM   483  C CA  . ASN   A 1 63  ? -4.89062  8.71967   -18.19346 1.000 39.94303 ? 63  ASN   A CA  1 
ATOM   484  C C   . ASN   A 1 63  ? -6.21986  8.68116   -18.94143 1.000 41.53112 ? 63  ASN   A C   1 
ATOM   485  O O   . ASN   A 1 63  ? -7.16670  8.01159   -18.50647 1.000 38.70612 ? 63  ASN   A O   1 
ATOM   486  C CB  . ASN   A 1 63  ? -4.82558  9.97796   -17.32545 1.000 39.75738 ? 63  ASN   A CB  1 
ATOM   487  C CG  . ASN   A 1 63  ? -3.79571  9.88243   -16.20948 1.000 37.75334 ? 63  ASN   A CG  1 
ATOM   488  O OD1 . ASN   A 1 63  ? -3.30671  8.80440   -15.88194 1.000 36.22196 ? 63  ASN   A OD1 1 
ATOM   489  N ND2 . ASN   A 1 63  ? -3.45700  11.02860  -15.62397 1.000 36.34492 ? 63  ASN   A ND2 1 
ATOM   490  N N   . HIS   A 1 64  ? -6.31294  9.38469   -20.07456 1.000 41.27775 ? 64  HIS   A N   1 
ATOM   491  C CA  . HIS   A 1 64  ? -7.58413  9.42294   -20.79366 1.000 41.68039 ? 64  HIS   A CA  1 
ATOM   492  C C   . HIS   A 1 64  ? -7.92408  8.10336   -21.47511 1.000 43.46891 ? 64  HIS   A C   1 
ATOM   493  O O   . HIS   A 1 64  ? -9.01669  7.98449   -22.03795 1.000 41.38762 ? 64  HIS   A O   1 
ATOM   494  C CB  . HIS   A 1 64  ? -7.57947  10.56226  -21.81387 1.000 43.27902 ? 64  HIS   A CB  1 
ATOM   495  C CG  . HIS   A 1 64  ? -6.53429  10.42002  -22.87466 1.000 51.12184 ? 64  HIS   A CG  1 
ATOM   496  N ND1 . HIS   A 1 64  ? -6.79738  9.86959   -24.11227 1.000 51.23246 ? 64  HIS   A ND1 1 
ATOM   497  C CD2 . HIS   A 1 64  ? -5.21607  10.73566  -22.87264 1.000 45.79980 ? 64  HIS   A CD2 1 
ATOM   498  C CE1 . HIS   A 1 64  ? -5.68834  9.86744   -24.83228 1.000 49.32202 ? 64  HIS   A CE1 1 
ATOM   499  N NE2 . HIS   A 1 64  ? -4.71416  10.38236  -24.10174 1.000 47.10439 ? 64  HIS   A NE2 1 
ATOM   500  N N   . ASN   A 1 65  ? -7.03981  7.10363   -21.42648 1.000 44.27475 ? 65  ASN   A N   1 
ATOM   501  C CA  . ASN   A 1 65  ? -7.39802  5.78298   -21.93220 1.000 43.03297 ? 65  ASN   A CA  1 
ATOM   502  C C   . ASN   A 1 65  ? -8.35858  5.04582   -21.00390 1.000 40.46689 ? 65  ASN   A C   1 
ATOM   503  O O   . ASN   A 1 65  ? -9.09355  4.16338   -21.46737 1.000 40.11113 ? 65  ASN   A O   1 
ATOM   504  C CB  . ASN   A 1 65  ? -6.13780  4.94647   -22.15945 1.000 40.84886 ? 65  ASN   A CB  1 
ATOM   505  C CG  . ASN   A 1 65  ? -5.21869  5.56005   -23.18668 1.000 42.18487 ? 65  ASN   A CG  1 
ATOM   506  O OD1 . ASN   A 1 65  ? -4.01178  5.63371   -22.98798 1.000 43.52183 ? 65  ASN   A OD1 1 
ATOM   507  N ND2 . ASN   A 1 65  ? -5.79217  6.02730   -24.29034 1.000 46.15957 ? 65  ASN   A ND2 1 
ATOM   508  N N   . PHE   A 1 66  ? -8.38802  5.39243   -19.71814 1.000 37.54278 ? 66  PHE   A N   1 
ATOM   509  C CA  . PHE   A 1 66  ? -9.26227  4.71944   -18.75703 1.000 39.74033 ? 66  PHE   A CA  1 
ATOM   510  C C   . PHE   A 1 66  ? -10.59211 5.47076   -18.67518 1.000 38.54773 ? 66  PHE   A C   1 
ATOM   511  O O   . PHE   A 1 66  ? -10.64743 6.60957   -18.19523 1.000 38.25825 ? 66  PHE   A O   1 
ATOM   512  C CB  . PHE   A 1 66  ? -8.60188  4.63293   -17.38167 1.000 35.96532 ? 66  PHE   A CB  1 
ATOM   513  C CG  . PHE   A 1 66  ? -7.28293  3.90984   -17.37386 1.000 34.46707 ? 66  PHE   A CG  1 
ATOM   514  C CD1 . PHE   A 1 66  ? -7.23314  2.53298   -17.27510 1.000 31.28417 ? 66  PHE   A CD1 1 
ATOM   515  C CD2 . PHE   A 1 66  ? -6.08510  4.61706   -17.48136 1.000 35.24713 ? 66  PHE   A CD2 1 
ATOM   516  C CE1 . PHE   A 1 66  ? -6.00857  1.86741   -17.26762 1.000 35.83613 ? 66  PHE   A CE1 1 
ATOM   517  C CE2 . PHE   A 1 66  ? -4.85550  3.95769   -17.46796 1.000 32.40223 ? 66  PHE   A CE2 1 
ATOM   518  C CZ  . PHE   A 1 66  ? -4.81645  2.58649   -17.36440 1.000 32.95555 ? 66  PHE   A CZ  1 
ATOM   519  N N   . LEU   A 1 67  ? -11.66434 4.83250   -19.13391 1.000 37.78476 ? 67  LEU   A N   1 
ATOM   520  C CA  . LEU   A 1 67  ? -13.00663 5.38619   -19.01564 1.000 38.36038 ? 67  LEU   A CA  1 
ATOM   521  C C   . LEU   A 1 67  ? -13.67720 4.79663   -17.77387 1.000 38.75507 ? 67  LEU   A C   1 
ATOM   522  O O   . LEU   A 1 67  ? -13.89132 3.58061   -17.69200 1.000 36.15484 ? 67  LEU   A O   1 
ATOM   523  C CB  . LEU   A 1 67  ? -13.81509 5.09317   -20.27808 1.000 39.06258 ? 67  LEU   A CB  1 
ATOM   524  C CG  . LEU   A 1 67  ? -13.06335 5.45427   -21.56841 1.000 41.15065 ? 67  LEU   A CG  1 
ATOM   525  C CD1 . LEU   A 1 67  ? -13.90261 5.19724   -22.82569 1.000 36.78672 ? 67  LEU   A CD1 1 
ATOM   526  C CD2 . LEU   A 1 67  ? -12.53277 6.89250   -21.53389 1.000 40.58028 ? 67  LEU   A CD2 1 
ATOM   527  N N   . VAL   A 1 68  ? -13.99542 5.65791   -16.80788 1.000 39.21176 ? 68  VAL   A N   1 
ATOM   528  C CA  . VAL   A 1 68  ? -14.48882 5.25060   -15.49355 1.000 38.40099 ? 68  VAL   A CA  1 
ATOM   529  C C   . VAL   A 1 68  ? -15.85493 5.87674   -15.26833 1.000 37.49918 ? 68  VAL   A C   1 
ATOM   530  O O   . VAL   A 1 68  ? -15.98443 7.10526   -15.22481 1.000 37.80448 ? 68  VAL   A O   1 
ATOM   531  C CB  . VAL   A 1 68  ? -13.51972 5.65020   -14.37265 1.000 37.29288 ? 68  VAL   A CB  1 
ATOM   532  C CG1 . VAL   A 1 68  ? -14.08252 5.22627   -13.03467 1.000 29.93037 ? 68  VAL   A CG1 1 
ATOM   533  C CG2 . VAL   A 1 68  ? -12.15415 5.01623   -14.61416 1.000 35.75614 ? 68  VAL   A CG2 1 
ATOM   534  N N   . GLN   A 1 69  ? -16.86302 5.03767   -15.08181 1.000 35.00864 ? 69  GLN   A N   1 
ATOM   535  C CA  . GLN   A 1 69  ? -18.24184 5.49783   -15.06226 1.000 42.05732 ? 69  GLN   A CA  1 
ATOM   536  C C   . GLN   A 1 69  ? -18.90090 5.08573   -13.75241 1.000 39.70905 ? 69  GLN   A C   1 
ATOM   537  O O   . GLN   A 1 69  ? -18.96279 3.89336   -13.42912 1.000 31.73460 ? 69  GLN   A O   1 
ATOM   538  C CB  . GLN   A 1 69  ? -18.98333 4.93267   -16.27202 1.000 44.06630 ? 69  GLN   A CB  1 
ATOM   539  C CG  . GLN   A 1 69  ? -20.22781 5.65867   -16.67568 1.000 50.15150 ? 69  GLN   A CG  1 
ATOM   540  C CD  . GLN   A 1 69  ? -20.78548 5.11739   -17.97502 1.000 55.84336 ? 69  GLN   A CD  1 
ATOM   541  O OE1 . GLN   A 1 69  ? -21.92922 4.65914   -18.04289 1.000 53.19022 ? 69  GLN   A OE1 1 
ATOM   542  N NE2 . GLN   A 1 69  ? -19.96144 5.16735   -19.02961 1.000 55.88675 ? 69  GLN   A NE2 1 
ATOM   543  N N   . ALA   A 1 70  ? -19.37245 6.07583   -12.99723 1.000 41.47280 ? 70  ALA   A N   1 
ATOM   544  C CA  . ALA   A 1 70  ? -20.17174 5.87099   -11.79213 1.000 42.62803 ? 70  ALA   A CA  1 
ATOM   545  C C   . ALA   A 1 70  ? -21.57905 6.39138   -12.08293 1.000 45.58406 ? 70  ALA   A C   1 
ATOM   546  O O   . ALA   A 1 70  ? -21.81999 7.60026   -12.04088 1.000 44.22070 ? 70  ALA   A O   1 
ATOM   547  C CB  . ALA   A 1 70  ? -19.54505 6.57444   -10.59209 1.000 36.99995 ? 70  ALA   A CB  1 
ATOM   548  N N   . GLY   A 1 71  ? -22.50598 5.47306   -12.37869 1.000 49.48408 ? 71  GLY   A N   1 
ATOM   549  C CA  . GLY   A 1 71  ? -23.83097 5.84681   -12.85527 1.000 51.29150 ? 71  GLY   A CA  1 
ATOM   550  C C   . GLY   A 1 71  ? -23.75815 6.44608   -14.25385 1.000 59.46931 ? 71  GLY   A C   1 
ATOM   551  O O   . GLY   A 1 71  ? -22.85279 6.15289   -15.04199 1.000 58.00289 ? 71  GLY   A O   1 
ATOM   552  N N   . ASN   A 1 72  ? -24.72734 7.30597   -14.57271 1.000 61.94719 ? 72  ASN   A N   1 
ATOM   553  C CA  . ASN   A 1 72  ? -24.61196 8.14225   -15.77018 1.000 65.93168 ? 72  ASN   A CA  1 
ATOM   554  C C   . ASN   A 1 72  ? -23.73392 9.36943   -15.53159 1.000 63.64678 ? 72  ASN   A C   1 
ATOM   555  O O   . ASN   A 1 72  ? -23.97767 10.44925  -16.08059 1.000 64.37391 ? 72  ASN   A O   1 
ATOM   556  C CB  . ASN   A 1 72  ? -25.99647 8.54336   -16.28847 1.000 71.61036 ? 72  ASN   A CB  1 
ATOM   557  C CG  . ASN   A 1 72  ? -26.95643 8.97216   -15.18134 1.000 74.51310 ? 72  ASN   A CG  1 
ATOM   558  O OD1 . ASN   A 1 72  ? -26.60620 8.98498   -13.99734 1.000 74.15052 ? 72  ASN   A OD1 1 
ATOM   559  N ND2 . ASN   A 1 72  ? -28.17830 9.33336   -15.57140 1.000 75.67607 ? 72  ASN   A ND2 1 
ATOM   560  N N   . VAL   A 1 73  ? -22.70243 9.20985   -14.70381 1.000 59.22331 ? 73  VAL   A N   1 
ATOM   561  C CA  . VAL   A 1 73  ? -21.71675 10.24722  -14.42116 1.000 58.18693 ? 73  VAL   A CA  1 
ATOM   562  C C   . VAL   A 1 73  ? -20.35211 9.58328   -14.46742 1.000 54.47853 ? 73  VAL   A C   1 
ATOM   563  O O   . VAL   A 1 73  ? -20.05575 8.71136   -13.64473 1.000 52.87561 ? 73  VAL   A O   1 
ATOM   564  C CB  . VAL   A 1 73  ? -21.94083 10.91214  -13.05151 1.000 59.81236 ? 73  VAL   A CB  1 
ATOM   565  C CG1 . VAL   A 1 73  ? -20.67346 11.60352  -12.58123 1.000 57.07014 ? 73  VAL   A CG1 1 
ATOM   566  C CG2 . VAL   A 1 73  ? -23.09792 11.89652  -13.12640 1.000 59.04755 ? 73  VAL   A CG2 1 
ATOM   567  N N   . GLN   A 1 74  ? -19.52695 9.95751   -15.42859 1.000 54.28205 ? 74  GLN   A N   1 
ATOM   568  C CA  . GLN   A 1 74  ? -18.24930 9.28321   -15.56378 1.000 52.90848 ? 74  GLN   A CA  1 
ATOM   569  C C   . GLN   A 1 74  ? -17.12472 10.18049  -15.06868 1.000 48.18031 ? 74  GLN   A C   1 
ATOM   570  O O   . GLN   A 1 74  ? -17.13050 11.39174  -15.30360 1.000 46.65569 ? 74  GLN   A O   1 
ATOM   571  C CB  . GLN   A 1 74  ? -18.01483 8.80442   -17.00043 1.000 55.73651 ? 74  GLN   A CB  1 
ATOM   572  C CG  . GLN   A 1 74  ? -18.09175 9.81601   -18.10649 1.000 53.23890 ? 74  GLN   A CG  1 
ATOM   573  C CD  . GLN   A 1 74  ? -17.80275 9.15282   -19.44282 1.000 61.70902 ? 74  GLN   A CD  1 
ATOM   574  O OE1 . GLN   A 1 74  ? -17.49391 7.95428   -19.49490 1.000 60.44721 ? 74  GLN   A OE1 1 
ATOM   575  N NE2 . GLN   A 1 74  ? -17.89256 9.92010   -20.52676 1.000 67.62500 ? 74  GLN   A NE2 1 
ATOM   576  N N   . LEU   A 1 75  ? -16.18552 9.57039   -14.34938 1.000 44.34554 ? 75  LEU   A N   1 
ATOM   577  C CA  . LEU   A 1 75  ? -15.13465 10.26272  -13.62187 1.000 43.35975 ? 75  LEU   A CA  1 
ATOM   578  C C   . LEU   A 1 75  ? -13.91956 10.49831  -14.50902 1.000 44.95218 ? 75  LEU   A C   1 
ATOM   579  O O   . LEU   A 1 75  ? -13.73736 9.85372   -15.54603 1.000 44.84258 ? 75  LEU   A O   1 
ATOM   580  C CB  . LEU   A 1 75  ? -14.73181 9.45486   -12.38903 1.000 40.09812 ? 75  LEU   A CB  1 
ATOM   581  C CG  . LEU   A 1 75  ? -15.89215 9.20486   -11.42783 1.000 41.49157 ? 75  LEU   A CG  1 
ATOM   582  C CD1 . LEU   A 1 75  ? -15.53195 8.12387   -10.42417 1.000 37.68689 ? 75  LEU   A CD1 1 
ATOM   583  C CD2 . LEU   A 1 75  ? -16.30182 10.49327  -10.73304 1.000 42.57746 ? 75  LEU   A CD2 1 
ATOM   584  N N   . ARG   A 1 76  ? -13.07353 11.42700  -14.07289 1.000 43.52172 ? 76  ARG   A N   1 
ATOM   585  C CA  . ARG   A 1 76  ? -11.86653 11.81218  -14.79702 1.000 45.63825 ? 76  ARG   A CA  1 
ATOM   586  C C   . ARG   A 1 76  ? -10.65396 11.19757  -14.10662 1.000 40.68540 ? 76  ARG   A C   1 
ATOM   587  O O   . ARG   A 1 76  ? -10.38904 11.49436  -12.93758 1.000 39.91187 ? 76  ARG   A O   1 
ATOM   588  C CB  . ARG   A 1 76  ? -11.75354 13.33723  -14.85627 1.000 48.71762 ? 76  ARG   A CB  1 
ATOM   589  C CG  . ARG   A 1 76  ? -10.53023 13.90049  -15.57482 1.000 53.81981 ? 76  ARG   A CG  1 
ATOM   590  C CD  . ARG   A 1 76  ? -10.43100 13.41302  -17.02206 1.000 57.72765 ? 76  ARG   A CD  1 
ATOM   591  N NE  . ARG   A 1 76  ? -11.73444 13.25753  -17.67802 1.000 62.09335 ? 76  ARG   A NE  1 
ATOM   592  C CZ  . ARG   A 1 76  ? -12.46160 14.25341  -18.17391 1.000 62.90135 ? 76  ARG   A CZ  1 
ATOM   593  N NH1 . ARG   A 1 76  ? -12.02937 15.50408  -18.09269 1.000 64.98677 ? 76  ARG   A NH1 1 
ATOM   594  N NH2 . ARG   A 1 76  ? -13.62838 13.99424  -18.75180 1.000 67.97508 ? 76  ARG   A NH2 1 
ATOM   595  N N   . VAL   A 1 77  ? -9.93413  10.33444  -14.81850 1.000 37.87657 ? 77  VAL   A N   1 
ATOM   596  C CA  . VAL   A 1 77  ? -8.72708  9.72026   -14.27185 1.000 39.10393 ? 77  VAL   A CA  1 
ATOM   597  C C   . VAL   A 1 77  ? -7.58925  10.72902  -14.35332 1.000 39.17334 ? 77  VAL   A C   1 
ATOM   598  O O   . VAL   A 1 77  ? -7.25773  11.22238  -15.43663 1.000 40.23956 ? 77  VAL   A O   1 
ATOM   599  C CB  . VAL   A 1 77  ? -8.36960  8.41894   -15.00848 1.000 39.05419 ? 77  VAL   A CB  1 
ATOM   600  C CG1 . VAL   A 1 77  ? -7.03709  7.84859   -14.49104 1.000 35.21208 ? 77  VAL   A CG1 1 
ATOM   601  C CG2 . VAL   A 1 77  ? -9.47052  7.39327   -14.83053 1.000 36.41228 ? 77  VAL   A CG2 1 
ATOM   602  N N   . ILE   A 1 78  ? -6.99715  11.04413  -13.20307 1.000 35.96193 ? 78  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 78  ? -5.92959  12.02749  -13.10362 1.000 35.47981 ? 78  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 78  ? -4.61288  11.38382  -12.69382 1.000 35.79845 ? 78  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 78  ? -3.63044  12.09013  -12.44036 1.000 33.50796 ? 78  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 78  ? -6.30835  13.16501  -12.14075 1.000 38.22694 ? 78  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 78  ? -6.29508  12.67090  -10.69298 1.000 37.26483 ? 78  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 78  ? -7.69737  13.70558  -12.48396 1.000 36.71334 ? 78  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 78  ? -6.88150  13.65820  -9.70297  1.000 37.63484 ? 78  ILE   A CD1 1 
ATOM   610  N N   . GLY   A 1 79  ? -4.56911  10.05690  -12.62032 1.000 33.89775 ? 79  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 79  ? -3.34232  9.34535   -12.32414 1.000 32.78435 ? 79  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 79  ? -3.58703  7.85753   -12.15555 1.000 31.74434 ? 79  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 79  ? -4.71692  7.43202   -11.88805 1.000 28.70266 ? 79  GLY   A O   1 
ATOM   614  N N   . HIS   A 1 80  ? -2.54093  7.05231   -12.31185 1.000 27.83903 ? 80  HIS   A N   1 
ATOM   615  C CA  . HIS   A 1 80  ? -2.67965  5.61160   -12.16656 1.000 28.23475 ? 80  HIS   A CA  1 
ATOM   616  C C   . HIS   A 1 80  ? -1.39379  5.06974   -11.58157 1.000 25.58846 ? 80  HIS   A C   1 
ATOM   617  O O   . HIS   A 1 80  ? -0.33156  5.67422   -11.72034 1.000 24.08031 ? 80  HIS   A O   1 
ATOM   618  C CB  . HIS   A 1 80  ? -2.94533  4.91980   -13.49865 1.000 26.79422 ? 80  HIS   A CB  1 
ATOM   619  C CG  . HIS   A 1 80  ? -1.93745  5.25582   -14.54691 1.000 28.96960 ? 80  HIS   A CG  1 
ATOM   620  N ND1 . HIS   A 1 80  ? -1.94989  6.45227   -15.23005 1.000 31.92045 ? 80  HIS   A ND1 1 
ATOM   621  C CD2 . HIS   A 1 80  ? -0.85873  4.57539   -15.00051 1.000 30.31196 ? 80  HIS   A CD2 1 
ATOM   622  C CE1 . HIS   A 1 80  ? -0.94302  6.48041   -16.08422 1.000 31.18323 ? 80  HIS   A CE1 1 
ATOM   623  N NE2 . HIS   A 1 80  ? -0.26387  5.35340   -15.96429 1.000 28.90153 ? 80  HIS   A NE2 1 
ATOM   624  N N   . SER   A 1 81  ? -1.49790  3.90808   -10.94634 1.000 22.97662 ? 81  SER   A N   1 
ATOM   625  C CA  . SER   A 1 81  ? -0.32416  3.23381   -10.40944 1.000 24.58168 ? 81  SER   A CA  1 
ATOM   626  C C   . SER   A 1 81  ? -0.65310  1.76838   -10.19081 1.000 22.87303 ? 81  SER   A C   1 
ATOM   627  O O   . SER   A 1 81  ? -1.75656  1.42897   -9.75827  1.000 22.29390 ? 81  SER   A O   1 
ATOM   628  C CB  . SER   A 1 81  ? 0.13776   3.86463   -9.09060  1.000 22.45221 ? 81  SER   A CB  1 
ATOM   629  O OG  . SER   A 1 81  ? -0.77808  3.53768   -8.06152  1.000 25.72231 ? 81  SER   A OG  1 
ATOM   630  N N   . MET   A 1 82  ? 0.31550   0.90915   -10.44986 1.000 22.73813 ? 82  MET   A N   1 
ATOM   631  C CA  . MET   A 1 82  ? 0.11520   -0.52407  -10.30130 1.000 22.02826 ? 82  MET   A CA  1 
ATOM   632  C C   . MET   A 1 82  ? 0.65997   -1.00296  -8.95852  1.000 21.68132 ? 82  MET   A C   1 
ATOM   633  O O   . MET   A 1 82  ? 1.74706   -0.59815  -8.53935  1.000 18.63409 ? 82  MET   A O   1 
ATOM   634  C CB  . MET   A 1 82  ? 0.78358   -1.26375  -11.45700 1.000 22.12043 ? 82  MET   A CB  1 
ATOM   635  C CG  . MET   A 1 82  ? 0.66659   -2.76172  -11.36283 1.000 23.73767 ? 82  MET   A CG  1 
ATOM   636  S SD  . MET   A 1 82  ? 0.96886   -3.44509  -12.97720 1.000 29.72136 ? 82  MET   A SD  1 
ATOM   637  C CE  . MET   A 1 82  ? 2.60345   -2.78343  -13.30387 1.000 29.30606 ? 82  MET   A CE  1 
ATOM   638  N N   . GLN   A 1 83  ? -0.09831  -1.86101  -8.28083  1.000 19.66742 ? 83  GLN   A N   1 
ATOM   639  C CA  . GLN   A 1 83  ? 0.34418   -2.45682  -7.02535  1.000 18.79394 ? 83  GLN   A CA  1 
ATOM   640  C C   . GLN   A 1 83  ? 0.05720   -3.94367  -7.10810  1.000 19.42610 ? 83  GLN   A C   1 
ATOM   641  O O   . GLN   A 1 83  ? -1.10517  -4.34767  -7.02461  1.000 19.44299 ? 83  GLN   A O   1 
ATOM   642  C CB  . GLN   A 1 83  ? -0.36050  -1.84048  -5.82687  1.000 17.10824 ? 83  GLN   A CB  1 
ATOM   643  C CG  . GLN   A 1 83  ? -0.03725  -2.53861  -4.52208  1.000 19.84183 ? 83  GLN   A CG  1 
ATOM   644  C CD  . GLN   A 1 83  ? -0.75849  -1.93015  -3.31615  1.000 20.78670 ? 83  GLN   A CD  1 
ATOM   645  O OE1 . GLN   A 1 83  ? -1.72791  -1.17080  -3.45930  1.000 18.77343 ? 83  GLN   A OE1 1 
ATOM   646  N NE2 . GLN   A 1 83  ? -0.26769  -2.24958  -2.12180  1.000 18.87185 ? 83  GLN   A NE2 1 
ATOM   647  N N   . ASN   A 1 84  ? 1.11217   -4.74908  -7.26678  1.000 18.19619 ? 84  ASN   A N   1 
ATOM   648  C CA  . ASN   A 1 84  ? 0.94771   -6.17781  -7.50288  1.000 18.29646 ? 84  ASN   A CA  1 
ATOM   649  C C   . ASN   A 1 84  ? -0.00895  -6.38992  -8.67578  1.000 17.77157 ? 84  ASN   A C   1 
ATOM   650  O O   . ASN   A 1 84  ? 0.24344   -5.85507  -9.75883  1.000 18.33838 ? 84  ASN   A O   1 
ATOM   651  C CB  . ASN   A 1 84  ? 0.51628   -6.84587  -6.19769  1.000 14.16882 ? 84  ASN   A CB  1 
ATOM   652  C CG  . ASN   A 1 84  ? 1.49918   -6.51246  -5.06359  1.000 16.75617 ? 84  ASN   A CG  1 
ATOM   653  O OD1 . ASN   A 1 84  ? 2.68720   -6.79504  -5.19765  1.000 19.25397 ? 84  ASN   A OD1 1 
ATOM   654  N ND2 . ASN   A 1 84  ? 1.02296   -5.89001  -3.97824  1.000 13.42406 ? 84  ASN   A ND2 1 
ATOM   655  N N   . CYS   A 1 85  ? -1.12542  -7.09993  -8.50813  1.000 15.35992 ? 85  CYS   A N   1 
ATOM   656  C CA  . CYS   A 1 85  ? -1.97171  -7.35321  -9.66919  1.000 14.23820 ? 85  CYS   A CA  1 
ATOM   657  C C   . CYS   A 1 85  ? -3.22131  -6.46147  -9.74788  1.000 15.40835 ? 85  CYS   A C   1 
ATOM   658  O O   . CYS   A 1 85  ? -4.17718  -6.81896  -10.44949 1.000 17.57383 ? 85  CYS   A O   1 
ATOM   659  C CB  . CYS   A 1 85  ? -2.34851  -8.82355  -9.71402  1.000 15.50993 ? 85  CYS   A CB  1 
ATOM   660  S SG  . CYS   A 1 85  ? -0.88766  -9.84630  -9.78276  1.000 15.83206 ? 85  CYS   A SG  1 
ATOM   661  N N   . VAL   A 1 86  ? -3.22955  -5.29651  -9.09430  1.000 15.18090 ? 86  VAL   A N   1 
ATOM   662  C CA  . VAL   A 1 86  ? -4.36578  -4.37700  -9.18217  1.000 16.78693 ? 86  VAL   A CA  1 
ATOM   663  C C   . VAL   A 1 86  ? -3.88629  -3.03087  -9.69962  1.000 19.40478 ? 86  VAL   A C   1 
ATOM   664  O O   . VAL   A 1 86  ? -2.77007  -2.59093  -9.40441  1.000 17.25092 ? 86  VAL   A O   1 
ATOM   665  C CB  . VAL   A 1 86  ? -5.11486  -4.16063  -7.83888  1.000 17.68304 ? 86  VAL   A CB  1 
ATOM   666  C CG1 . VAL   A 1 86  ? -5.61845  -5.47475  -7.25895  1.000 14.18755 ? 86  VAL   A CG1 1 
ATOM   667  C CG2 . VAL   A 1 86  ? -4.26652  -3.40107  -6.84744  1.000 16.92070 ? 86  VAL   A CG2 1 
ATOM   668  N N   . LEU   A 1 87  ? -4.74993  -2.37462  -10.47804 1.000 18.59440 ? 87  LEU   A N   1 
ATOM   669  C CA  . LEU   A 1 87  ? -4.58495  -0.96967  -10.83601 1.000 19.35680 ? 87  LEU   A CA  1 
ATOM   670  C C   . LEU   A 1 87  ? -5.27495  -0.06907  -9.82658  1.000 20.50636 ? 87  LEU   A C   1 
ATOM   671  O O   . LEU   A 1 87  ? -6.38500  -0.35985  -9.37094  1.000 20.54375 ? 87  LEU   A O   1 
ATOM   672  C CB  . LEU   A 1 87  ? -5.17110  -0.65673  -12.20973 1.000 21.60702 ? 87  LEU   A CB  1 
ATOM   673  C CG  . LEU   A 1 87  ? -4.26790  -0.58706  -13.42769 1.000 27.55721 ? 87  LEU   A CG  1 
ATOM   674  C CD1 . LEU   A 1 87  ? -5.09233  -0.15045  -14.62143 1.000 24.18244 ? 87  LEU   A CD1 1 
ATOM   675  C CD2 . LEU   A 1 87  ? -3.10052  0.37964   -13.19692 1.000 27.79661 ? 87  LEU   A CD2 1 
ATOM   676  N N   . LYS   A 1 88  ? -4.63083  1.05075   -9.52134  1.000 21.26501 ? 88  LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 88  ? -5.21364  2.10498   -8.70280  1.000 20.00374 ? 88  LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 88  ? -5.29680  3.36048   -9.56047  1.000 23.97220 ? 88  LYS   A C   1 
ATOM   679  O O   . LYS   A 1 88  ? -4.28148  4.02225   -9.81085  1.000 23.82013 ? 88  LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 88  ? -4.39477  2.32921   -7.43272  1.000 20.70009 ? 88  LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 88  ? -4.25399  1.05270   -6.62767  1.000 19.51609 ? 88  LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 88  ? -3.67288  1.29310   -5.25946  1.000 20.45759 ? 88  LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 88  ? -2.20564  1.58453   -5.28089  1.000 22.43552 ? 88  LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 88  ? -1.74768  1.61696   -3.85413  1.000 22.36629 ? 88  LYS   A NZ  1 
ATOM   685  N N   . LEU   A 1 89  ? -6.50183  3.65854   -10.03319 1.000 22.37019 ? 89  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 89  ? -6.76074  4.83171   -10.85145 1.000 26.06230 ? 89  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 89  ? -7.13806  5.99411   -9.93927  1.000 26.58221 ? 89  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 89  ? -8.13071  5.91622   -9.20506  1.000 25.27692 ? 89  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 89  ? -7.87871  4.54437   -11.85849 1.000 24.29433 ? 89  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 89  ? -7.61730  3.38875   -12.81820 1.000 25.01424 ? 89  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 89  ? -8.85086  3.06066   -13.62698 1.000 23.94612 ? 89  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 89  ? -6.44867  3.75088   -13.72595 1.000 26.17487 ? 89  LEU   A CD2 1 
ATOM   693  N N   . LYS   A 1 90  ? -6.34293  7.06086   -9.97493  1.000 27.68426 ? 90  LYS   A N   1 
ATOM   694  C CA  . LYS   A 1 90  ? -6.68280  8.27222   -9.24536  1.000 28.65167 ? 90  LYS   A CA  1 
ATOM   695  C C   . LYS   A 1 90  ? -7.70966  9.07278   -10.03596 1.000 31.57881 ? 90  LYS   A C   1 
ATOM   696  O O   . LYS   A 1 90  ? -7.50223  9.36489   -11.21758 1.000 33.81552 ? 90  LYS   A O   1 
ATOM   697  C CB  . LYS   A 1 90  ? -5.43678  9.11043   -8.99720  1.000 30.66508 ? 90  LYS   A CB  1 
ATOM   698  C CG  . LYS   A 1 90  ? -5.65871  10.25592  -8.04301  1.000 34.82356 ? 90  LYS   A CG  1 
ATOM   699  C CD  . LYS   A 1 90  ? -5.15347  9.90228   -6.65879  1.000 36.54569 ? 90  LYS   A CD  1 
ATOM   700  C CE  . LYS   A 1 90  ? -4.78426  11.15105  -5.87693  1.000 41.33780 ? 90  LYS   A CE  1 
ATOM   701  N NZ  . LYS   A 1 90  ? -4.13442  10.80691  -4.57948  1.000 43.50133 ? 90  LYS   A NZ  1 
ATOM   702  N N   . VAL   A 1 91  ? -8.82065  9.42354   -9.38793  1.000 31.10179 ? 91  VAL   A N   1 
ATOM   703  C CA  . VAL   A 1 91  ? -9.88414  10.18080  -10.03419 1.000 35.66420 ? 91  VAL   A CA  1 
ATOM   704  C C   . VAL   A 1 91  ? -10.03255 11.51963  -9.32646  1.000 35.13516 ? 91  VAL   A C   1 
ATOM   705  O O   . VAL   A 1 91  ? -9.62061  11.69007  -8.17535  1.000 35.28929 ? 91  VAL   A O   1 
ATOM   706  C CB  . VAL   A 1 91  ? -11.22089 9.41472   -10.04286 1.000 34.34913 ? 91  VAL   A CB  1 
ATOM   707  C CG1 . VAL   A 1 91  ? -11.12067 8.22298   -10.98198 1.000 33.88502 ? 91  VAL   A CG1 1 
ATOM   708  C CG2 . VAL   A 1 91  ? -11.59246 8.97520   -8.63320  1.000 29.30704 ? 91  VAL   A CG2 1 
ATOM   709  N N   . ASP   A 1 92  ? -10.62918 12.48248  -10.03312 1.000 36.74460 ? 92  ASP   A N   1 
ATOM   710  C CA  . ASP   A 1 92  ? -10.69931 13.84135  -9.50434  1.000 38.45914 ? 92  ASP   A CA  1 
ATOM   711  C C   . ASP   A 1 92  ? -11.83771 14.04293  -8.51571  1.000 39.99852 ? 92  ASP   A C   1 
ATOM   712  O O   . ASP   A 1 92  ? -11.98988 15.15271  -7.99308  1.000 39.15529 ? 92  ASP   A O   1 
ATOM   713  C CB  . ASP   A 1 92  ? -10.81178 14.86197  -10.64721 1.000 38.97095 ? 92  ASP   A CB  1 
ATOM   714  C CG  . ASP   A 1 92  ? -12.07047 14.69299  -11.48596 1.000 41.84608 ? 92  ASP   A CG  1 
ATOM   715  O OD1 . ASP   A 1 92  ? -12.94283 13.85443  -11.16525 1.000 41.24595 ? 92  ASP   A OD1 1 
ATOM   716  O OD2 . ASP   A 1 92  ? -12.17527 15.40925  -12.49854 1.000 44.13417 ? 92  ASP   A OD2 1 
ATOM   717  N N   . THR   A 1 93  ? -12.62323 13.00498  -8.23768  1.000 37.96537 ? 93  THR   A N   1 
ATOM   718  C CA  . THR   A 1 93  ? -13.79644 13.11548  -7.38206  1.000 36.53676 ? 93  THR   A CA  1 
ATOM   719  C C   . THR   A 1 93  ? -13.72454 12.03664  -6.31830  1.000 33.73990 ? 93  THR   A C   1 
ATOM   720  O O   . THR   A 1 93  ? -13.49728 10.86570  -6.63493  1.000 30.69534 ? 93  THR   A O   1 
ATOM   721  C CB  . THR   A 1 93  ? -15.08924 12.98189  -8.20097  1.000 36.70823 ? 93  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 93  ? -15.00276 13.82346  -9.35667  1.000 42.14210 ? 93  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 93  ? -16.31912 13.37421  -7.37869  1.000 37.46303 ? 93  THR   A CG2 1 
ATOM   724  N N   . ALA   A 1 94  ? -13.89591 12.42974  -5.06024  1.000 35.52945 ? 94  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 94  ? -14.01230 11.45003  -3.99083  1.000 31.05418 ? 94  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 94  ? -15.43080 10.89484  -3.97473  1.000 30.76661 ? 94  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 94  ? -16.40061 11.62790  -4.17959  1.000 32.43397 ? 94  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 94  ? -13.66532 12.07137  -2.63843  1.000 32.47461 ? 94  ALA   A CB  1 
ATOM   729  N N   . ASN   A 1 95  ? -15.53898 9.59033   -3.78022  1.000 28.30447 ? 95  ASN   A N   1 
ATOM   730  C CA  . ASN   A 1 95  ? -16.83232 8.94904   -3.64155  1.000 26.93025 ? 95  ASN   A CA  1 
ATOM   731  C C   . ASN   A 1 95  ? -17.48028 9.42740   -2.35235  1.000 29.28820 ? 95  ASN   A C   1 
ATOM   732  O O   . ASN   A 1 95  ? -16.95367 9.14456   -1.26824  1.000 31.00617 ? 95  ASN   A O   1 
ATOM   733  C CB  . ASN   A 1 95  ? -16.64609 7.43268   -3.63774  1.000 24.68411 ? 95  ASN   A CB  1 
ATOM   734  C CG  . ASN   A 1 95  ? -17.96636 6.66130   -3.62036  1.000 24.45979 ? 95  ASN   A CG  1 
ATOM   735  O OD1 . ASN   A 1 95  ? -19.05063 7.24272   -3.57045  1.000 24.85494 ? 95  ASN   A OD1 1 
ATOM   736  N ND2 . ASN   A 1 95  ? -17.86610 5.33168   -3.67104  1.000 20.68525 ? 95  ASN   A ND2 1 
ATOM   737  N N   . PRO   A 1 96  ? -18.60770 10.14196  -2.40251  1.000 30.58846 ? 96  PRO   A N   1 
ATOM   738  C CA  . PRO   A 1 96  ? -19.25196 10.54342  -1.14519  1.000 32.16684 ? 96  PRO   A CA  1 
ATOM   739  C C   . PRO   A 1 96  ? -19.84486 9.37068   -0.37357  1.000 30.20422 ? 96  PRO   A C   1 
ATOM   740  O O   . PRO   A 1 96  ? -20.14144 9.52455   0.81806   1.000 31.19397 ? 96  PRO   A O   1 
ATOM   741  C CB  . PRO   A 1 96  ? -20.33514 11.53961  -1.59672  1.000 35.11073 ? 96  PRO   A CB  1 
ATOM   742  C CG  . PRO   A 1 96  ? -20.53250 11.29715  -3.07934  1.000 34.46779 ? 96  PRO   A CG  1 
ATOM   743  C CD  . PRO   A 1 96  ? -19.44610 10.39677  -3.58805  1.000 31.60090 ? 96  PRO   A CD  1 
ATOM   744  N N   . LYS   A 1 97  ? -20.02048 8.21125   -1.00959  1.000 27.69951 ? 97  LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 97  ? -20.57438 7.03421   -0.36158  1.000 27.20477 ? 97  LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 97  ? -19.50798 6.11684   0.20559   1.000 24.99412 ? 97  LYS   A C   1 
ATOM   747  O O   . LYS   A 1 97  ? -19.82593 4.98095   0.56623   1.000 23.43185 ? 97  LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 97  ? -21.44169 6.24070   -1.33999  1.000 26.14100 ? 97  LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 97  ? -22.65851 7.00798   -1.85399  1.000 28.82595 ? 97  LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 97  ? -23.17462 6.40284   -3.15573  1.000 27.63113 ? 97  LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 97  ? -24.45333 7.09644   -3.64941  1.000 29.23783 ? 97  LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 97  ? -25.68999 6.53200   -3.05215  1.000 29.15477 ? 97  LYS   A NZ  1 
ATOM   753  N N   . THR   A 1 98  ? -18.25525 6.57799   0.29389   1.000 26.22502 ? 98  THR   A N   1 
ATOM   754  C CA  . THR   A 1 98  ? -17.18668 5.73739   0.81706   1.000 24.31055 ? 98  THR   A CA  1 
ATOM   755  C C   . THR   A 1 98  ? -17.50010 5.34528   2.25574   1.000 23.50760 ? 98  THR   A C   1 
ATOM   756  O O   . THR   A 1 98  ? -17.55073 6.21671   3.13361   1.000 24.18494 ? 98  THR   A O   1 
ATOM   757  C CB  . THR   A 1 98  ? -15.83339 6.44790   0.77753   1.000 23.81106 ? 98  THR   A CB  1 
ATOM   758  O OG1 . THR   A 1 98  ? -15.51596 6.82513   -0.56909  1.000 22.79296 ? 98  THR   A OG1 1 
ATOM   759  C CG2 . THR   A 1 98  ? -14.75019 5.51449   1.31501   1.000 20.98501 ? 98  THR   A CG2 1 
ATOM   760  N N   . PRO   A 1 99  ? -17.69621 4.05851   2.53924   1.000 19.97767 ? 99  PRO   A N   1 
ATOM   761  C CA  . PRO   A 1 99  ? -17.90388 3.63068   3.92603   1.000 20.17775 ? 99  PRO   A CA  1 
ATOM   762  C C   . PRO   A 1 99  ? -16.59113 3.65781   4.68452   1.000 20.88234 ? 99  PRO   A C   1 
ATOM   763  O O   . PRO   A 1 99  ? -15.52280 3.80171   4.08987   1.000 23.54632 ? 99  PRO   A O   1 
ATOM   764  C CB  . PRO   A 1 99  ? -18.41561 2.20164   3.77345   1.000 21.79784 ? 99  PRO   A CB  1 
ATOM   765  C CG  . PRO   A 1 99  ? -17.72569 1.70963   2.55475   1.000 19.27226 ? 99  PRO   A CG  1 
ATOM   766  C CD  . PRO   A 1 99  ? -17.50185 2.91288   1.63911   1.000 21.62779 ? 99  PRO   A CD  1 
ATOM   767  N N   . LYS   A 1 100 ? -16.68594 3.52047   6.01227   1.000 21.18541 ? 100 LYS   A N   1 
ATOM   768  C CA  . LYS   A 1 100 ? -15.54215 3.07509   6.79063   1.000 23.82086 ? 100 LYS   A CA  1 
ATOM   769  C C   . LYS   A 1 100 ? -15.15069 1.69980   6.28417   1.000 23.35432 ? 100 LYS   A C   1 
ATOM   770  O O   . LYS   A 1 100 ? -16.01446 0.83978   6.05270   1.000 18.75328 ? 100 LYS   A O   1 
ATOM   771  C CB  . LYS   A 1 100 ? -15.84761 3.02653   8.29213   1.000 24.43483 ? 100 LYS   A CB  1 
ATOM   772  C CG  . LYS   A 1 100 ? -14.63325 2.50663   9.10800   1.000 31.09461 ? 100 LYS   A CG  1 
ATOM   773  C CD  . LYS   A 1 100 ? -14.88968 2.52504   10.64411  1.000 33.91144 ? 100 LYS   A CD  1 
ATOM   774  C CE  . LYS   A 1 100 ? -13.76463 1.75585   11.40431  1.000 40.24303 ? 100 LYS   A CE  1 
ATOM   775  N NZ  . LYS   A 1 100 ? -12.36401 2.32724   11.31433  1.000 40.60659 ? 100 LYS   A NZ  1 
ATOM   776  N N   . TYR   A 1 101 ? -13.85121 1.50961   6.05659   1.000 20.07924 ? 101 TYR   A N   1 
ATOM   777  C CA  . TYR   A 1 101 ? -13.40560 0.26904   5.45934   1.000 19.83772 ? 101 TYR   A CA  1 
ATOM   778  C C   . TYR   A 1 101 ? -11.97615 -0.04488  5.85641   1.000 22.47659 ? 101 TYR   A C   1 
ATOM   779  O O   . TYR   A 1 101 ? -11.22214 0.82211   6.31256   1.000 17.37652 ? 101 TYR   A O   1 
ATOM   780  C CB  . TYR   A 1 101 ? -13.53108 0.31333   3.93605   1.000 19.80032 ? 101 TYR   A CB  1 
ATOM   781  C CG  . TYR   A 1 101 ? -12.53019 1.19242   3.24309   1.000 19.35587 ? 101 TYR   A CG  1 
ATOM   782  C CD1 . TYR   A 1 101 ? -11.30088 0.68498   2.82275   1.000 21.36402 ? 101 TYR   A CD1 1 
ATOM   783  C CD2 . TYR   A 1 101 ? -12.82159 2.52164   2.97393   1.000 20.59486 ? 101 TYR   A CD2 1 
ATOM   784  C CE1 . TYR   A 1 101 ? -10.38063 1.48701   2.16139   1.000 17.88311 ? 101 TYR   A CE1 1 
ATOM   785  C CE2 . TYR   A 1 101 ? -11.91604 3.33488   2.30836   1.000 21.84946 ? 101 TYR   A CE2 1 
ATOM   786  C CZ  . TYR   A 1 101 ? -10.69382 2.80098   1.90214   1.000 22.90158 ? 101 TYR   A CZ  1 
ATOM   787  O OH  . TYR   A 1 101 ? -9.78511  3.60160   1.24845   1.000 28.84575 ? 101 TYR   A OH  1 
ATOM   788  N N   . LYS   A 1 102 ? -11.63172 -1.31979  5.65419   1.000 18.73810 ? 102 LYS   A N   1 
ATOM   789  C CA  . LYS   A 1 102 ? -10.28601 -1.85370  5.77808   1.000 20.92439 ? 102 LYS   A CA  1 
ATOM   790  C C   . LYS   A 1 102 ? -10.05075 -2.77802  4.59196   1.000 18.27273 ? 102 LYS   A C   1 
ATOM   791  O O   . LYS   A 1 102 ? -10.99682 -3.24136  3.95130   1.000 14.96684 ? 102 LYS   A O   1 
ATOM   792  C CB  . LYS   A 1 102 ? -10.07197 -2.64990  7.08543   1.000 20.35827 ? 102 LYS   A CB  1 
ATOM   793  C CG  . LYS   A 1 102 ? -10.17240 -1.86720  8.41373   1.000 26.04868 ? 102 LYS   A CG  1 
ATOM   794  C CD  . LYS   A 1 102 ? -10.64920 -2.79195  9.56426   1.000 28.79807 ? 102 LYS   A CD  1 
ATOM   795  C CE  . LYS   A 1 102 ? -10.72767 -2.09167  10.96201  1.000 35.08831 ? 102 LYS   A CE  1 
ATOM   796  N NZ  . LYS   A 1 102 ? -11.72633 -0.96961  11.12157  1.000 31.01264 ? 102 LYS   A NZ  1 
ATOM   797  N N   . PHE   A 1 103 ? -8.77496  -3.02559  4.29384   1.000 16.85042 ? 103 PHE   A N   1 
ATOM   798  C CA  . PHE   A 1 103 ? -8.35046  -4.09298  3.39080   1.000 14.98379 ? 103 PHE   A CA  1 
ATOM   799  C C   . PHE   A 1 103 ? -7.71937  -5.18037  4.25161   1.000 15.37799 ? 103 PHE   A C   1 
ATOM   800  O O   . PHE   A 1 103 ? -6.77090  -4.90248  4.99723   1.000 16.96987 ? 103 PHE   A O   1 
ATOM   801  C CB  . PHE   A 1 103 ? -7.32144  -3.59932  2.37119   1.000 11.95569 ? 103 PHE   A CB  1 
ATOM   802  C CG  . PHE   A 1 103 ? -7.86759  -2.70571  1.28499   1.000 13.95072 ? 103 PHE   A CG  1 
ATOM   803  C CD1 . PHE   A 1 103 ? -9.24398  -2.52069  1.10659   1.000 16.15465 ? 103 PHE   A CD1 1 
ATOM   804  C CD2 . PHE   A 1 103 ? -6.98433  -2.04864  0.42326   1.000 14.66102 ? 103 PHE   A CD2 1 
ATOM   805  C CE1 . PHE   A 1 103 ? -9.72610  -1.71047  0.09380   1.000 15.65730 ? 103 PHE   A CE1 1 
ATOM   806  C CE2 . PHE   A 1 103 ? -7.45194  -1.23021  -0.59948  1.000 14.55276 ? 103 PHE   A CE2 1 
ATOM   807  C CZ  . PHE   A 1 103 ? -8.83132  -1.06559  -0.77154  1.000 16.55568 ? 103 PHE   A CZ  1 
ATOM   808  N N   . VAL   A 1 104 ? -8.21954  -6.40826  4.15400   1.000 11.11531 ? 104 VAL   A N   1 
ATOM   809  C CA  . VAL   A 1 104 ? -7.66186  -7.51115  4.93072   1.000 12.28348 ? 104 VAL   A CA  1 
ATOM   810  C C   . VAL   A 1 104 ? -7.39567  -8.69453  4.01464   1.000 11.25457 ? 104 VAL   A C   1 
ATOM   811  O O   . VAL   A 1 104 ? -8.19721  -9.00701  3.12730   1.000 12.43083 ? 104 VAL   A O   1 
ATOM   812  C CB  . VAL   A 1 104 ? -8.57619  -7.93524  6.10805   1.000 12.60140 ? 104 VAL   A CB  1 
ATOM   813  C CG1 . VAL   A 1 104 ? -8.89489  -6.73554  6.99262   1.000 16.76856 ? 104 VAL   A CG1 1 
ATOM   814  C CG2 . VAL   A 1 104 ? -9.85471  -8.56691  5.60706   1.000 15.01964 ? 104 VAL   A CG2 1 
ATOM   815  N N   . ARG   A 1 105 ? -6.28304  -9.37280  4.25320   1.000 11.48129 ? 105 ARG   A N   1 
ATOM   816  C CA  . ARG   A 1 105 ? -5.94953  -10.60808 3.56145   1.000 13.78768 ? 105 ARG   A CA  1 
ATOM   817  C C   . ARG   A 1 105 ? -6.38538  -11.75754 4.46363   1.000 10.47344 ? 105 ARG   A C   1 
ATOM   818  O O   . ARG   A 1 105 ? -5.85718  -11.89606 5.56147   1.000 9.75859  ? 105 ARG   A O   1 
ATOM   819  C CB  . ARG   A 1 105 ? -4.44414  -10.67716 3.25599   1.000 10.99036 ? 105 ARG   A CB  1 
ATOM   820  C CG  . ARG   A 1 105 ? -4.04160  -11.95166 2.49925   1.000 10.89713 ? 105 ARG   A CG  1 
ATOM   821  C CD  . ARG   A 1 105 ? -2.62560  -11.91038 1.90651   1.000 9.17674  ? 105 ARG   A CD  1 
ATOM   822  N NE  . ARG   A 1 105 ? -2.33480  -13.15687 1.18143   1.000 8.67040  ? 105 ARG   A NE  1 
ATOM   823  C CZ  . ARG   A 1 105 ? -2.58490  -13.35600 -0.10989  1.000 8.43835  ? 105 ARG   A CZ  1 
ATOM   824  N NH1 . ARG   A 1 105 ? -3.13581  -12.40162 -0.82652  1.000 9.12361  ? 105 ARG   A NH1 1 
ATOM   825  N NH2 . ARG   A 1 105 ? -2.32420  -14.52378 -0.68477  1.000 9.85368  ? 105 ARG   A NH2 1 
ATOM   826  N N   . ILE   A 1 106 ? -7.35577  -12.57454 4.00850   1.000 9.38651  ? 106 ILE   A N   1 
ATOM   827  C CA  . ILE   A 1 106 ? -7.96282  -13.59255 4.86636   1.000 11.78064 ? 106 ILE   A CA  1 
ATOM   828  C C   . ILE   A 1 106 ? -7.22201  -14.91430 4.72710   1.000 11.86583 ? 106 ILE   A C   1 
ATOM   829  O O   . ILE   A 1 106 ? -6.59317  -15.20531 3.71365   1.000 11.59898 ? 106 ILE   A O   1 
ATOM   830  C CB  . ILE   A 1 106 ? -9.46501  -13.82867 4.56561   1.000 11.83345 ? 106 ILE   A CB  1 
ATOM   831  C CG1 . ILE   A 1 106 ? -9.61636  -14.24379 3.09971   1.000 10.15611 ? 106 ILE   A CG1 1 
ATOM   832  C CG2 . ILE   A 1 106 ? -10.29004 -12.61928 4.97028   1.000 13.48656 ? 106 ILE   A CG2 1 
ATOM   833  C CD1 . ILE   A 1 106 ? -10.99187 -14.85009 2.68680   1.000 12.47021 ? 106 ILE   A CD1 1 
ATOM   834  N N   . GLN   A 1 107 ? -7.38188  -15.74244 5.72367   1.000 12.07552 ? 107 GLN   A N   1 
ATOM   835  C CA  . GLN   A 1 107 ? -6.90313  -17.10432 5.79769   1.000 14.15033 ? 107 GLN   A CA  1 
ATOM   836  C C   . GLN   A 1 107 ? -7.84400  -18.06034 5.06364   1.000 18.43597 ? 107 GLN   A C   1 
ATOM   837  O O   . GLN   A 1 107 ? -9.04628  -17.79468 4.93399   1.000 13.11129 ? 107 GLN   A O   1 
ATOM   838  C CB  . GLN   A 1 107 ? -6.79413  -17.53755 7.26233   1.000 18.49304 ? 107 GLN   A CB  1 
ATOM   839  C CG  . GLN   A 1 107 ? -5.66473  -16.87288 8.04534   1.000 15.97123 ? 107 GLN   A CG  1 
ATOM   840  C CD  . GLN   A 1 107 ? -4.30575  -17.36500 7.59117   1.000 19.07205 ? 107 GLN   A CD  1 
ATOM   841  O OE1 . GLN   A 1 107 ? -4.21056  -18.36870 6.88367   1.000 16.82518 ? 107 GLN   A OE1 1 
ATOM   842  N NE2 . GLN   A 1 107 ? -3.24448  -16.66059 7.99150   1.000 19.12177 ? 107 GLN   A NE2 1 
ATOM   843  N N   . PRO   A 1 108 ? -7.31912  -19.18843 4.58001   1.000 18.76707 ? 108 PRO   A N   1 
ATOM   844  C CA  . PRO   A 1 108 ? -8.20256  -20.26002 4.10254   1.000 16.61118 ? 108 PRO   A CA  1 
ATOM   845  C C   . PRO   A 1 108 ? -9.13200  -20.71236 5.21678   1.000 15.32679 ? 108 PRO   A C   1 
ATOM   846  O O   . PRO   A 1 108 ? -8.76405  -20.73087 6.38998   1.000 16.16342 ? 108 PRO   A O   1 
ATOM   847  C CB  . PRO   A 1 108 ? -7.23515  -21.37599 3.69000   1.000 14.21295 ? 108 PRO   A CB  1 
ATOM   848  C CG  . PRO   A 1 108 ? -5.93240  -21.02999 4.36043   1.000 18.24025 ? 108 PRO   A CG  1 
ATOM   849  C CD  . PRO   A 1 108 ? -5.89233  -19.55024 4.52209   1.000 13.67434 ? 108 PRO   A CD  1 
ATOM   850  N N   . GLY   A 1 109 ? -10.34587 -21.08927 4.83342   1.000 14.75271 ? 109 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 109 ? -11.37176 -21.44609 5.77621   1.000 14.99471 ? 109 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 109 ? -12.28363 -20.29898 6.14322   1.000 16.19927 ? 109 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 109 ? -13.41006 -20.53494 6.58431   1.000 19.39932 ? 109 GLY   A O   1 
ATOM   854  N N   . GLN   A 1 110 ? -11.83267 -19.07052 5.95159   1.000 15.00928 ? 110 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 110 ? -12.62804 -17.90592 6.29138   1.000 17.64960 ? 110 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 110 ? -13.67340 -17.65196 5.20023   1.000 12.74931 ? 110 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 110 ? -13.45230 -17.93144 4.01502   1.000 11.48265 ? 110 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 110 ? -11.70919 -16.70104 6.45796   1.000 14.69397 ? 110 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 110 ? -12.44276 -15.39022 6.67974   1.000 21.02635 ? 110 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 110 ? -13.20268 -15.39600 7.99566   1.000 27.68390 ? 110 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 110 ? -12.57795 -15.53725 9.06440   1.000 23.65242 ? 110 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 110 ? -14.54441 -15.21072 7.94039   1.000 14.85061 ? 110 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 111 ? -14.81767 -17.13061 5.60804   1.000 12.47204 ? 111 THR   A N   1 
ATOM   864  C CA  . THR   A 1 111 ? -15.91772 -16.86341 4.69135   1.000 12.17500 ? 111 THR   A CA  1 
ATOM   865  C C   . THR   A 1 111 ? -16.03963 -15.36426 4.46121   1.000 13.33377 ? 111 THR   A C   1 
ATOM   866  O O   . THR   A 1 111 ? -15.48845 -14.54883 5.21130   1.000 10.60580 ? 111 THR   A O   1 
ATOM   867  C CB  . THR   A 1 111 ? -17.24384 -17.43536 5.22607   1.000 11.04671 ? 111 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 111 ? -17.53021 -16.87315 6.51221   1.000 9.40586  ? 111 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 111 ? -17.17187 -18.98191 5.35013   1.000 10.26096 ? 111 THR   A CG2 1 
ATOM   870  N N   . PHE   A 1 112 ? -16.76830 -15.01286 3.39729   1.000 9.50487  ? 112 PHE   A N   1 
ATOM   871  C CA  . PHE   A 1 112 ? -17.02239 -13.63322 3.00371   1.000 10.52860 ? 112 PHE   A CA  1 
ATOM   872  C C   . PHE   A 1 112 ? -18.17145 -13.64137 2.00471   1.000 12.10424 ? 112 PHE   A C   1 
ATOM   873  O O   . PHE   A 1 112 ? -18.51409 -14.68106 1.42467   1.000 11.71745 ? 112 PHE   A O   1 
ATOM   874  C CB  . PHE   A 1 112 ? -15.79803 -12.93027 2.37903   1.000 9.35593  ? 112 PHE   A CB  1 
ATOM   875  C CG  . PHE   A 1 112 ? -15.20893 -13.64474 1.17252   1.000 11.93171 ? 112 PHE   A CG  1 
ATOM   876  C CD1 . PHE   A 1 112 ? -15.66370 -13.38038 -0.11312  1.000 10.91231 ? 112 PHE   A CD1 1 
ATOM   877  C CD2 . PHE   A 1 112 ? -14.17797 -14.55520 1.32226   1.000 11.32297 ? 112 PHE   A CD2 1 
ATOM   878  C CE1 . PHE   A 1 112 ? -15.10357 -14.01840 -1.22017  1.000 10.64632 ? 112 PHE   A CE1 1 
ATOM   879  C CE2 . PHE   A 1 112 ? -13.61306 -15.20110 0.19855   1.000 12.02052 ? 112 PHE   A CE2 1 
ATOM   880  C CZ  . PHE   A 1 112 ? -14.08007 -14.93460 -1.05635  1.000 11.90879 ? 112 PHE   A CZ  1 
ATOM   881  N N   . SER   A 1 113 ? -18.75478 -12.46573 1.83199   1.000 9.01762  ? 113 SER   A N   1 
ATOM   882  C CA  . SER   A 1 113 ? -19.85404 -12.21571 0.90992   1.000 11.13202 ? 113 SER   A CA  1 
ATOM   883  C C   . SER   A 1 113 ? -19.29748 -11.59655 -0.36086  1.000 12.04367 ? 113 SER   A C   1 
ATOM   884  O O   . SER   A 1 113 ? -18.39385 -10.76130 -0.30103  1.000 8.69941  ? 113 SER   A O   1 
ATOM   885  C CB  . SER   A 1 113 ? -20.85547 -11.25402 1.55133   1.000 11.28988 ? 113 SER   A CB  1 
ATOM   886  O OG  . SER   A 1 113 ? -21.56444 -11.86799 2.59920   1.000 10.92198 ? 113 SER   A OG  1 
ATOM   887  N N   . VAL   A 1 114 ? -19.85713 -11.98812 -1.50172  1.000 12.52322 ? 114 VAL   A N   1 
ATOM   888  C CA  . VAL   A 1 114 ? -19.41898 -11.54766 -2.82084  1.000 11.01409 ? 114 VAL   A CA  1 
ATOM   889  C C   . VAL   A 1 114 ? -20.56579 -10.75980 -3.44187  1.000 11.19290 ? 114 VAL   A C   1 
ATOM   890  O O   . VAL   A 1 114 ? -21.68288 -11.28087 -3.56841  1.000 10.17077 ? 114 VAL   A O   1 
ATOM   891  C CB  . VAL   A 1 114 ? -19.04826 -12.74375 -3.72557  1.000 9.46573  ? 114 VAL   A CB  1 
ATOM   892  C CG1 . VAL   A 1 114 ? -18.96040 -12.30990 -5.19498  1.000 9.82213  ? 114 VAL   A CG1 1 
ATOM   893  C CG2 . VAL   A 1 114 ? -17.73928 -13.42598 -3.27319  1.000 10.57847 ? 114 VAL   A CG2 1 
ATOM   894  N N   . LEU   A 1 115 ? -20.29685 -9.52487  -3.84814  1.000 9.08548  ? 115 LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 115 ? -21.28356 -8.75290  -4.60793  1.000 12.33932 ? 115 LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 115 ? -20.91462 -8.85228  -6.09015  1.000 12.51936 ? 115 LEU   A C   1 
ATOM   897  O O   . LEU   A 1 115 ? -19.99093 -8.17954  -6.56381  1.000 10.59703 ? 115 LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 115 ? -21.32885 -7.31384  -4.11128  1.000 12.13977 ? 115 LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 115 ? -22.25586 -6.35384  -4.85571  1.000 14.11544 ? 115 LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 115 ? -23.72409 -6.63912  -4.51402  1.000 16.03588 ? 115 LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 115 ? -21.91045 -4.88239  -4.58003  1.000 15.26788 ? 115 LEU   A CD2 1 
ATOM   902  N N   . ALA   A 1 116 ? -21.63363 -9.70500  -6.82353  1.000 15.43401 ? 116 ALA   A N   1 
ATOM   903  C CA  . ALA   A 1 116 ? -21.36767 -9.90169  -8.24676  1.000 13.87908 ? 116 ALA   A CA  1 
ATOM   904  C C   . ALA   A 1 116 ? -21.89230 -8.72578  -9.07095  1.000 18.70408 ? 116 ALA   A C   1 
ATOM   905  O O   . ALA   A 1 116 ? -23.04253 -8.29762  -8.91392  1.000 19.27382 ? 116 ALA   A O   1 
ATOM   906  C CB  . ALA   A 1 116 ? -21.98388 -11.21164 -8.73703  1.000 14.35162 ? 116 ALA   A CB  1 
ATOM   907  N N   . CYS   A 1 117 ? -21.05001 -8.24047  -9.98714  1.000 17.61211 ? 117 CYS   A N   1 
ATOM   908  C CA  . CYS   A 1 117 ? -21.26481 -6.99602  -10.70653 1.000 18.36171 ? 117 CYS   A CA  1 
ATOM   909  C C   . CYS   A 1 117 ? -20.90798 -7.16310  -12.16908 1.000 19.56337 ? 117 CYS   A C   1 
ATOM   910  O O   . CYS   A 1 117 ? -19.99602 -7.90782  -12.52378 1.000 19.08998 ? 117 CYS   A O   1 
ATOM   911  C CB  . CYS   A 1 117 ? -20.41487 -5.85633  -10.15295 1.000 17.91513 ? 117 CYS   A CB  1 
ATOM   912  S SG  . CYS   A 1 117 ? -20.92671 -5.29565  -8.57342  1.000 26.99056 ? 117 CYS   A SG  1 
ATOM   913  N N   . TYR   A 1 118 ? -21.62895 -6.42941  -13.00835 1.000 21.74108 ? 118 TYR   A N   1 
ATOM   914  C CA  . TYR   A 1 118 ? -21.38870 -6.34964  -14.43889 1.000 21.57603 ? 118 TYR   A CA  1 
ATOM   915  C C   . TYR   A 1 118 ? -21.57394 -4.88633  -14.79798 1.000 25.12371 ? 118 TYR   A C   1 
ATOM   916  O O   . TYR   A 1 118 ? -22.52926 -4.26324  -14.31967 1.000 25.47260 ? 118 TYR   A O   1 
ATOM   917  C CB  . TYR   A 1 118 ? -22.36355 -7.27405  -15.20279 1.000 21.80892 ? 118 TYR   A CB  1 
ATOM   918  C CG  . TYR   A 1 118 ? -22.18901 -8.70986  -14.75160 1.000 22.41874 ? 118 TYR   A CG  1 
ATOM   919  C CD1 . TYR   A 1 118 ? -21.24046 -9.53390  -15.35405 1.000 21.70242 ? 118 TYR   A CD1 1 
ATOM   920  C CD2 . TYR   A 1 118 ? -22.90266 -9.21860  -13.66136 1.000 24.13782 ? 118 TYR   A CD2 1 
ATOM   921  C CE1 . TYR   A 1 118 ? -21.03173 -10.82581 -14.90989 1.000 21.65345 ? 118 TYR   A CE1 1 
ATOM   922  C CE2 . TYR   A 1 118 ? -22.69501 -10.52364 -13.20968 1.000 21.93204 ? 118 TYR   A CE2 1 
ATOM   923  C CZ  . TYR   A 1 118 ? -21.75412 -11.31601 -13.84370 1.000 21.85946 ? 118 TYR   A CZ  1 
ATOM   924  O OH  . TYR   A 1 118 ? -21.52205 -12.60649 -13.41433 1.000 22.47634 ? 118 TYR   A OH  1 
ATOM   925  N N   . ASN   A 1 119 ? -20.63383 -4.32128  -15.57019 1.000 25.25552 ? 119 ASN   A N   1 
ATOM   926  C CA  . ASN   A 1 119 ? -20.75584 -2.94170  -16.07157 1.000 25.46566 ? 119 ASN   A CA  1 
ATOM   927  C C   . ASN   A 1 119 ? -20.98191 -1.94401  -14.93520 1.000 26.18285 ? 119 ASN   A C   1 
ATOM   928  O O   . ASN   A 1 119 ? -21.69521 -0.94492  -15.08786 1.000 26.65201 ? 119 ASN   A O   1 
ATOM   929  C CB  . ASN   A 1 119 ? -21.88273 -2.82830  -17.10258 1.000 29.83270 ? 119 ASN   A CB  1 
ATOM   930  C CG  . ASN   A 1 119 ? -21.72118 -3.79485  -18.26052 1.000 31.39270 ? 119 ASN   A CG  1 
ATOM   931  O OD1 . ASN   A 1 119 ? -22.43879 -4.79893  -18.35408 1.000 30.05261 ? 119 ASN   A OD1 1 
ATOM   932  N ND2 . ASN   A 1 119 ? -20.78026 -3.49660  -19.15350 1.000 32.33744 ? 119 ASN   A ND2 1 
ATOM   933  N N   . GLY   A 1 120 ? -20.39865 -2.24266  -13.77036 1.000 23.69041 ? 120 GLY   A N   1 
ATOM   934  C CA  . GLY   A 1 120 ? -20.53119 -1.41636  -12.58291 1.000 23.17376 ? 120 GLY   A CA  1 
ATOM   935  C C   . GLY   A 1 120 ? -21.84437 -1.53125  -11.84266 1.000 25.63296 ? 120 GLY   A C   1 
ATOM   936  O O   . GLY   A 1 120 ? -22.07305 -0.77208  -10.89610 1.000 26.79152 ? 120 GLY   A O   1 
ATOM   937  N N   . SER   A 1 121 ? -22.73124 -2.43980  -12.24385 1.000 25.21211 ? 121 SER   A N   1 
ATOM   938  C CA  . SER   A 1 121 ? -24.02698 -2.53520  -11.60078 1.000 26.65910 ? 121 SER   A CA  1 
ATOM   939  C C   . SER   A 1 121 ? -24.12548 -3.84554  -10.84510 1.000 23.28933 ? 121 SER   A C   1 
ATOM   940  O O   . SER   A 1 121 ? -24.01674 -4.91841  -11.45809 1.000 21.75670 ? 121 SER   A O   1 
ATOM   941  C CB  . SER   A 1 121 ? -25.16159 -2.42564  -12.61670 1.000 31.39047 ? 121 SER   A CB  1 
ATOM   942  O OG  . SER   A 1 121 ? -24.96888 -1.32558  -13.47510 1.000 38.75514 ? 121 SER   A OG  1 
ATOM   943  N N   . PRO   A 1 122 ? -24.32511 -3.80208  -9.53259  1.000 22.80746 ? 122 PRO   A N   1 
ATOM   944  C CA  . PRO   A 1 122 ? -24.44754 -5.04354  -8.75788  1.000 22.00882 ? 122 PRO   A CA  1 
ATOM   945  C C   . PRO   A 1 122 ? -25.56165 -5.92683  -9.30174  1.000 25.15150 ? 122 PRO   A C   1 
ATOM   946  O O   . PRO   A 1 122 ? -26.63286 -5.44074  -9.67282  1.000 23.83202 ? 122 PRO   A O   1 
ATOM   947  C CB  . PRO   A 1 122 ? -24.77280 -4.54578  -7.34484  1.000 22.45006 ? 122 PRO   A CB  1 
ATOM   948  C CG  . PRO   A 1 122 ? -24.21159 -3.17392  -7.28716  1.000 24.71166 ? 122 PRO   A CG  1 
ATOM   949  C CD  . PRO   A 1 122 ? -24.36508 -2.60216  -8.68305  1.000 26.15828 ? 122 PRO   A CD  1 
ATOM   950  N N   . SER   A 1 123 ? -25.29634 -7.23909  -9.32695  1.000 22.36404 ? 123 SER   A N   1 
ATOM   951  C CA  . SER   A 1 123 ? -26.20798 -8.23843  -9.86593  1.000 24.78414 ? 123 SER   A CA  1 
ATOM   952  C C   . SER   A 1 123 ? -26.84792 -9.12582  -8.81147  1.000 22.24897 ? 123 SER   A C   1 
ATOM   953  O O   . SER   A 1 123 ? -27.99838 -9.54322  -8.98170  1.000 23.24728 ? 123 SER   A O   1 
ATOM   954  C CB  . SER   A 1 123 ? -25.46356 -9.12479  -10.87220 1.000 24.59897 ? 123 SER   A CB  1 
ATOM   955  O OG  . SER   A 1 123 ? -26.31809 -10.12152 -11.38929 1.000 30.20547 ? 123 SER   A OG  1 
ATOM   956  N N   . GLY   A 1 124 ? -26.13683 -9.41621  -7.73259  1.000 18.90096 ? 124 GLY   A N   1 
ATOM   957  C CA  . GLY   A 1 124 ? -26.59489 -10.37013 -6.73833  1.000 17.02353 ? 124 GLY   A CA  1 
ATOM   958  C C   . GLY   A 1 124 ? -25.51494 -10.54150 -5.69960  1.000 16.43137 ? 124 GLY   A C   1 
ATOM   959  O O   . GLY   A 1 124 ? -24.34741 -10.17204 -5.91415  1.000 12.96859 ? 124 GLY   A O   1 
ATOM   960  N N   . VAL   A 1 125 ? -25.90097 -11.09019 -4.55821  1.000 13.93120 ? 125 VAL   A N   1 
ATOM   961  C CA  . VAL   A 1 125 ? -24.99217 -11.22960 -3.43217  1.000 14.65057 ? 125 VAL   A CA  1 
ATOM   962  C C   . VAL   A 1 125 ? -25.07871 -12.65336 -2.89834  1.000 15.26303 ? 125 VAL   A C   1 
ATOM   963  O O   . VAL   A 1 125 ? -26.15683 -13.26644 -2.90795  1.000 11.31266 ? 125 VAL   A O   1 
ATOM   964  C CB  . VAL   A 1 125 ? -25.30597 -10.18499 -2.33419  1.000 14.52030 ? 125 VAL   A CB  1 
ATOM   965  C CG1 . VAL   A 1 125 ? -26.65595 -10.40709 -1.76121  1.000 15.06615 ? 125 VAL   A CG1 1 
ATOM   966  C CG2 . VAL   A 1 125 ? -24.24616 -10.15767 -1.24851  1.000 10.13806 ? 125 VAL   A CG2 1 
ATOM   967  N N   . TYR   A 1 126 ? -23.93227 -13.21271 -2.50534  1.000 11.65531 ? 126 TYR   A N   1 
ATOM   968  C CA  . TYR   A 1 126 ? -23.89845 -14.57375 -1.98277  1.000 13.30040 ? 126 TYR   A CA  1 
ATOM   969  C C   . TYR   A 1 126 ? -22.64243 -14.73850 -1.12982  1.000 13.76400 ? 126 TYR   A C   1 
ATOM   970  O O   . TYR   A 1 126 ? -21.67663 -13.96607 -1.23407  1.000 10.95674 ? 126 TYR   A O   1 
ATOM   971  C CB  . TYR   A 1 126 ? -23.95424 -15.62977 -3.11112  1.000 13.86847 ? 126 TYR   A CB  1 
ATOM   972  C CG  . TYR   A 1 126 ? -22.85850 -15.46849 -4.15332  1.000 15.13768 ? 126 TYR   A CG  1 
ATOM   973  C CD1 . TYR   A 1 126 ? -21.58672 -16.00659 -3.94986  1.000 14.87755 ? 126 TYR   A CD1 1 
ATOM   974  C CD2 . TYR   A 1 126 ? -23.07674 -14.74003 -5.31529  1.000 14.79352 ? 126 TYR   A CD2 1 
ATOM   975  C CE1 . TYR   A 1 126 ? -20.58222 -15.84992 -4.88157  1.000 13.65974 ? 126 TYR   A CE1 1 
ATOM   976  C CE2 . TYR   A 1 126 ? -22.05940 -14.56574 -6.25711  1.000 14.86260 ? 126 TYR   A CE2 1 
ATOM   977  C CZ  . TYR   A 1 126 ? -20.81589 -15.13105 -6.02398  1.000 14.85874 ? 126 TYR   A CZ  1 
ATOM   978  O OH  . TYR   A 1 126 ? -19.80256 -14.98624 -6.94937  1.000 18.06615 ? 126 TYR   A OH  1 
ATOM   979  N N   . GLN   A 1 127 ? -22.66817 -15.80731 -0.33144  1.000 12.38458 ? 127 GLN   A N   1 
ATOM   980  C CA  . GLN   A 1 127 ? -21.64481 -16.17047 0.63056   1.000 15.62695 ? 127 GLN   A CA  1 
ATOM   981  C C   . GLN   A 1 127 ? -20.73952 -17.25644 0.05474   1.000 16.09918 ? 127 GLN   A C   1 
ATOM   982  O O   . GLN   A 1 127 ? -21.23096 -18.23183 -0.52793  1.000 14.12910 ? 127 GLN   A O   1 
ATOM   983  C CB  . GLN   A 1 127 ? -22.33489 -16.66161 1.91284   1.000 16.12002 ? 127 GLN   A CB  1 
ATOM   984  C CG  . GLN   A 1 127 ? -21.47059 -16.64380 3.13784   1.000 16.55368 ? 127 GLN   A CG  1 
ATOM   985  C CD  . GLN   A 1 127 ? -21.21541 -15.23432 3.62690   1.000 13.90806 ? 127 GLN   A CD  1 
ATOM   986  O OE1 . GLN   A 1 127 ? -21.75556 -14.26823 3.07551   1.000 15.30824 ? 127 GLN   A OE1 1 
ATOM   987  N NE2 . GLN   A 1 127 ? -20.41195 -15.10832 4.66661   1.000 13.94052 ? 127 GLN   A NE2 1 
ATOM   988  N N   . CYS   A 1 128 ? -19.42327 -17.08086 0.23136   1.000 13.67866 ? 128 CYS   A N   1 
ATOM   989  C CA  . CYS   A 1 128 ? -18.36718 -18.00791 -0.19298  1.000 13.90256 ? 128 CYS   A CA  1 
ATOM   990  C C   . CYS   A 1 128 ? -17.33757 -18.18295 0.92154   1.000 13.47388 ? 128 CYS   A C   1 
ATOM   991  O O   . CYS   A 1 128 ? -17.21680 -17.34735 1.81745   1.000 11.09779 ? 128 CYS   A O   1 
ATOM   992  C CB  . CYS   A 1 128 ? -17.53601 -17.52519 -1.42303  1.000 14.77904 ? 128 CYS   A CB  1 
ATOM   993  S SG  . CYS   A 1 128 ? -18.28789 -17.16215 -2.96232  1.000 26.36506 ? 128 CYS   A SG  1 
ATOM   994  N N   . ALA   A 1 129 ? -16.53084 -19.23732 0.79659   1.000 11.87954 ? 129 ALA   A N   1 
ATOM   995  C CA  . ALA   A 1 129 ? -15.33310 -19.43084 1.60155   1.000 12.91682 ? 129 ALA   A CA  1 
ATOM   996  C C   . ALA   A 1 129 ? -14.08344 -19.51890 0.71871   1.000 11.99240 ? 129 ALA   A C   1 
ATOM   997  O O   . ALA   A 1 129 ? -14.12258 -20.00497 -0.41828  1.000 8.79920  ? 129 ALA   A O   1 
ATOM   998  C CB  . ALA   A 1 129 ? -15.43840 -20.70230 2.45817   1.000 10.88809 ? 129 ALA   A CB  1 
ATOM   999  N N   . MET   A 1 130 ? -12.97197 -19.03488 1.26026   1.000 10.98380 ? 130 MET   A N   1 
ATOM   1000 C CA  . MET   A 1 130 ? -11.65045 -19.33433 0.73116   1.000 11.01547 ? 130 MET   A CA  1 
ATOM   1001 C C   . MET   A 1 130 ? -11.38104 -20.81699 0.96905   1.000 11.32880 ? 130 MET   A C   1 
ATOM   1002 O O   . MET   A 1 130 ? -11.26032 -21.24752 2.12101   1.000 11.35183 ? 130 MET   A O   1 
ATOM   1003 C CB  . MET   A 1 130 ? -10.60997 -18.46254 1.43547   1.000 11.90299 ? 130 MET   A CB  1 
ATOM   1004 C CG  . MET   A 1 130 ? -9.19283  -18.36790 0.78430   1.000 11.61926 ? 130 MET   A CG  1 
ATOM   1005 S SD  . MET   A 1 130 ? -9.19951  -17.99029 -0.98049  1.000 11.81447 ? 130 MET   A SD  1 
ATOM   1006 C CE  . MET   A 1 130 ? -9.60740  -16.25468 -0.87177  1.000 12.56100 ? 130 MET   A CE  1 
ATOM   1007 N N   . ARG   A 1 131 ? -11.30764 -21.60865 -0.10226  1.000 11.35528 ? 131 ARG   A N   1 
ATOM   1008 C CA  . ARG   A 1 131 ? -11.04575 -23.02659 0.05883   1.000 13.32423 ? 131 ARG   A CA  1 
ATOM   1009 C C   . ARG   A 1 131 ? -9.60459  -23.23920 0.50926   1.000 13.73453 ? 131 ARG   A C   1 
ATOM   1010 O O   . ARG   A 1 131 ? -8.74413  -22.40652 0.25092   1.000 11.46039 ? 131 ARG   A O   1 
ATOM   1011 C CB  . ARG   A 1 131 ? -11.28756 -23.77347 -1.24156  1.000 14.03962 ? 131 ARG   A CB  1 
ATOM   1012 C CG  . ARG   A 1 131 ? -12.67719 -23.58201 -1.84982  1.000 14.33020 ? 131 ARG   A CG  1 
ATOM   1013 C CD  . ARG   A 1 131 ? -13.78140 -24.08410 -0.94341  1.000 12.31084 ? 131 ARG   A CD  1 
ATOM   1014 N NE  . ARG   A 1 131 ? -13.56067 -25.42088 -0.40146  1.000 14.81802 ? 131 ARG   A NE  1 
ATOM   1015 C CZ  . ARG   A 1 131 ? -14.30480 -25.95671 0.57062   1.000 18.91995 ? 131 ARG   A CZ  1 
ATOM   1016 N NH1 . ARG   A 1 131 ? -15.31203 -25.25550 1.09710   1.000 15.07149 ? 131 ARG   A NH1 1 
ATOM   1017 N NH2 . ARG   A 1 131 ? -14.05635 -27.18857 1.01744   1.000 16.76429 ? 131 ARG   A NH2 1 
ATOM   1018 N N   . PRO   A 1 132 ? -9.31557  -24.36754 1.15364   1.000 15.94472 ? 132 PRO   A N   1 
ATOM   1019 C CA  . PRO   A 1 132 ? -7.91295  -24.68848 1.47157   1.000 18.19989 ? 132 PRO   A CA  1 
ATOM   1020 C C   . PRO   A 1 132 ? -6.96568  -24.59725 0.27610   1.000 18.65711 ? 132 PRO   A C   1 
ATOM   1021 O O   . PRO   A 1 132 ? -5.76620  -24.35522 0.47439   1.000 15.80420 ? 132 PRO   A O   1 
ATOM   1022 C CB  . PRO   A 1 132 ? -8.00575  -26.12187 2.00381   1.000 18.96600 ? 132 PRO   A CB  1 
ATOM   1023 C CG  . PRO   A 1 132 ? -9.39081  -26.18589 2.59374   1.000 19.60921 ? 132 PRO   A CG  1 
ATOM   1024 C CD  . PRO   A 1 132 ? -10.25472 -25.36531 1.70054   1.000 16.50335 ? 132 PRO   A CD  1 
ATOM   1025 N N   . ASN   A 1 133 ? -7.45007  -24.78358 -0.95845  1.000 16.25428 ? 133 ASN   A N   1 
ATOM   1026 C CA  . ASN   A 1 133 ? -6.57402  -24.62395 -2.11242  1.000 16.43288 ? 133 ASN   A CA  1 
ATOM   1027 C C   . ASN   A 1 133 ? -6.57992  -23.19952 -2.63707  1.000 12.13652 ? 133 ASN   A C   1 
ATOM   1028 O O   . ASN   A 1 133 ? -6.10088  -22.95986 -3.74163  1.000 13.11615 ? 133 ASN   A O   1 
ATOM   1029 C CB  . ASN   A 1 133 ? -6.92474  -25.62570 -3.22470  1.000 17.31708 ? 133 ASN   A CB  1 
ATOM   1030 C CG  . ASN   A 1 133 ? -8.29799  -25.39248 -3.85336  1.000 17.95495 ? 133 ASN   A CG  1 
ATOM   1031 O OD1 . ASN   A 1 133 ? -8.99475  -24.41006 -3.57750  1.000 14.11821 ? 133 ASN   A OD1 1 
ATOM   1032 N ND2 . ASN   A 1 133 ? -8.68209  -26.30764 -4.71994  1.000 19.36942 ? 133 ASN   A ND2 1 
ATOM   1033 N N   . PHE   A 1 134 ? -7.08684  -22.25318 -1.85027  1.000 11.48084 ? 134 PHE   A N   1 
ATOM   1034 C CA  . PHE   A 1 134 ? -7.11626  -20.82918 -2.19971  1.000 13.72549 ? 134 PHE   A CA  1 
ATOM   1035 C C   . PHE   A 1 134 ? -7.88538  -20.53770 -3.48396  1.000 12.11901 ? 134 PHE   A C   1 
ATOM   1036 O O   . PHE   A 1 134 ? -7.63989  -19.53169 -4.13985  1.000 12.68510 ? 134 PHE   A O   1 
ATOM   1037 C CB  . PHE   A 1 134 ? -5.71617  -20.23761 -2.30447  1.000 12.38909 ? 134 PHE   A CB  1 
ATOM   1038 C CG  . PHE   A 1 134 ? -5.00110  -20.17676 -0.99996  1.000 13.45057 ? 134 PHE   A CG  1 
ATOM   1039 C CD1 . PHE   A 1 134 ? -5.35595  -19.23843 -0.04562  1.000 12.13094 ? 134 PHE   A CD1 1 
ATOM   1040 C CD2 . PHE   A 1 134 ? -4.00844  -21.08982 -0.70368  1.000 15.45697 ? 134 PHE   A CD2 1 
ATOM   1041 C CE1 . PHE   A 1 134 ? -4.69553  -19.18310 1.18926   1.000 12.99428 ? 134 PHE   A CE1 1 
ATOM   1042 C CE2 . PHE   A 1 134 ? -3.34300  -21.04639 0.52116   1.000 15.67995 ? 134 PHE   A CE2 1 
ATOM   1043 C CZ  . PHE   A 1 134 ? -3.70476  -20.08817 1.47424   1.000 13.56947 ? 134 PHE   A CZ  1 
ATOM   1044 N N   . THR   A 1 135 ? -8.82991  -21.37734 -3.86102  1.000 13.57632 ? 135 THR   A N   1 
ATOM   1045 C CA  . THR   A 1 135 ? -9.83747  -20.98440 -4.84117  1.000 12.30911 ? 135 THR   A CA  1 
ATOM   1046 C C   . THR   A 1 135 ? -11.14052 -20.66821 -4.10762  1.000 12.35368 ? 135 THR   A C   1 
ATOM   1047 O O   . THR   A 1 135 ? -11.30403 -20.96373 -2.92384  1.000 11.48997 ? 135 THR   A O   1 
ATOM   1048 C CB  . THR   A 1 135 ? -10.05905 -22.08811 -5.88966  1.000 13.51925 ? 135 THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 135 ? -10.57525 -23.26467 -5.26172  1.000 13.48399 ? 135 THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 135 ? -8.74983  -22.46433 -6.59987  1.000 14.00895 ? 135 THR   A CG2 1 
ATOM   1051 N N   . ILE   A 1 136 ? -12.09849 -20.07742 -4.81605  1.000 11.60440 ? 136 ILE   A N   1 
ATOM   1052 C CA  . ILE   A 1 136 ? -13.43646 -19.90828 -4.26555  1.000 14.78659 ? 136 ILE   A CA  1 
ATOM   1053 C C   . ILE   A 1 136 ? -14.42460 -20.47274 -5.27504  1.000 14.06247 ? 136 ILE   A C   1 
ATOM   1054 O O   . ILE   A 1 136 ? -14.23348 -20.32755 -6.48325  1.000 10.64454 ? 136 ILE   A O   1 
ATOM   1055 C CB  . ILE   A 1 136 ? -13.77594 -18.43642 -3.91934  1.000 13.51169 ? 136 ILE   A CB  1 
ATOM   1056 C CG1 . ILE   A 1 136 ? -13.92770 -17.58214 -5.18021  1.000 14.05419 ? 136 ILE   A CG1 1 
ATOM   1057 C CG2 . ILE   A 1 136 ? -12.71608 -17.82697 -2.98255  1.000 11.84734 ? 136 ILE   A CG2 1 
ATOM   1058 C CD1 . ILE   A 1 136 ? -14.78903 -16.32274 -4.97529  1.000 13.62664 ? 136 ILE   A CD1 1 
ATOM   1059 N N   . LYS   A 1 137 ? -15.45799 -21.14875 -4.77647  1.000 15.32975 ? 137 LYS   A N   1 
ATOM   1060 C CA  . LYS   A 1 137 ? -16.51934 -21.70833 -5.61988  1.000 15.89840 ? 137 LYS   A CA  1 
ATOM   1061 C C   . LYS   A 1 137 ? -17.59221 -20.63409 -5.79807  1.000 17.10321 ? 137 LYS   A C   1 
ATOM   1062 O O   . LYS   A 1 137 ? -18.60270 -20.58341 -5.09185  1.000 16.38185 ? 137 LYS   A O   1 
ATOM   1063 C CB  . LYS   A 1 137 ? -17.07131 -22.97760 -4.99422  1.000 15.72951 ? 137 LYS   A CB  1 
ATOM   1064 C CG  . LYS   A 1 137 ? -16.09546 -24.14366 -5.02458  1.000 17.01761 ? 137 LYS   A CG  1 
ATOM   1065 C CD  . LYS   A 1 137 ? -16.67932 -25.35393 -4.29570  1.000 20.24908 ? 137 LYS   A CD  1 
ATOM   1066 C CE  . LYS   A 1 137 ? -15.67150 -26.49283 -4.21905  1.000 24.34314 ? 137 LYS   A CE  1 
ATOM   1067 N NZ  . LYS   A 1 137 ? -15.17892 -26.91167 -5.57376  1.000 26.64608 ? 137 LYS   A NZ  1 
ATOM   1068 N N   . GLY   A 1 138 ? -17.33074 -19.72642 -6.73430  1.000 13.08030 ? 138 GLY   A N   1 
ATOM   1069 C CA  . GLY   A 1 138 ? -18.17396 -18.57432 -6.93572  1.000 16.71656 ? 138 GLY   A CA  1 
ATOM   1070 C C   . GLY   A 1 138 ? -19.17403 -18.80482 -8.03375  1.000 16.21173 ? 138 GLY   A C   1 
ATOM   1071 O O   . GLY   A 1 138 ? -19.36530 -19.93446 -8.51948  1.000 17.78606 ? 138 GLY   A O   1 
ATOM   1072 N N   . SER   A 1 139 ? -19.82679 -17.72645 -8.45310  1.000 14.23658 ? 139 SER   A N   1 
ATOM   1073 C CA  . SER   A 1 139 ? -20.74964 -17.72965 -9.58044  1.000 17.58410 ? 139 SER   A CA  1 
ATOM   1074 C C   . SER   A 1 139 ? -20.47602 -16.45108 -10.36522 1.000 17.16192 ? 139 SER   A C   1 
ATOM   1075 O O   . SER   A 1 139 ? -20.86214 -15.35079 -9.94699  1.000 13.86389 ? 139 SER   A O   1 
ATOM   1076 C CB  . SER   A 1 139 ? -22.20336 -17.82465 -9.12489  1.000 15.02910 ? 139 SER   A CB  1 
ATOM   1077 O OG  . SER   A 1 139 ? -23.09199 -17.52605 -10.19331 1.000 20.10553 ? 139 SER   A OG  1 
ATOM   1078 N N   . PHE   A 1 140 ? -19.77779 -16.59424 -11.48420 1.000 18.55707 ? 140 PHE   A N   1 
ATOM   1079 C CA  . PHE   A 1 140 ? -19.11430 -15.47544 -12.14607 1.000 19.57994 ? 140 PHE   A CA  1 
ATOM   1080 C C   . PHE   A 1 140 ? -19.24084 -15.69225 -13.63696 1.000 19.12871 ? 140 PHE   A C   1 
ATOM   1081 O O   . PHE   A 1 140 ? -18.94906 -16.78960 -14.11892 1.000 22.03745 ? 140 PHE   A O   1 
ATOM   1082 C CB  . PHE   A 1 140 ? -17.62530 -15.40176 -11.75479 1.000 16.25363 ? 140 PHE   A CB  1 
ATOM   1083 C CG  . PHE   A 1 140 ? -17.37080 -14.86744 -10.36408 1.000 15.40237 ? 140 PHE   A CG  1 
ATOM   1084 C CD1 . PHE   A 1 140 ? -17.80339 -13.60318 -10.00248 1.000 14.51934 ? 140 PHE   A CD1 1 
ATOM   1085 C CD2 . PHE   A 1 140 ? -16.68179 -15.62940 -9.42252  1.000 15.76940 ? 140 PHE   A CD2 1 
ATOM   1086 C CE1 . PHE   A 1 140 ? -17.55234 -13.09956 -8.74493  1.000 14.78610 ? 140 PHE   A CE1 1 
ATOM   1087 C CE2 . PHE   A 1 140 ? -16.43330 -15.13730 -8.15959  1.000 14.57704 ? 140 PHE   A CE2 1 
ATOM   1088 C CZ  . PHE   A 1 140 ? -16.85935 -13.87325 -7.81162  1.000 13.29472 ? 140 PHE   A CZ  1 
ATOM   1089 N N   . LEU   A 1 141 ? -19.68851 -14.67172 -14.36155 1.000 20.44030 ? 141 LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 141 ? -19.71629 -14.69773 -15.81693 1.000 21.83574 ? 141 LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 141 ? -18.72198 -13.67924 -16.36445 1.000 22.22450 ? 141 LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 141 ? -18.05515 -12.97630 -15.61401 1.000 21.09455 ? 141 LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 141 ? -21.12132 -14.42684 -16.33707 1.000 23.11327 ? 141 LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 141 ? -22.17093 -15.31312 -15.68876 1.000 27.90924 ? 141 LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 141 ? -23.54233 -14.80885 -16.09922 1.000 31.07022 ? 141 LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 141 ? -21.96719 -16.78962 -16.06882 1.000 24.64417 ? 141 LEU   A CD2 1 
ATOM   1097 N N   . ASN   A 1 142 ? -18.61888 -13.60526 -17.68880 1.000 23.81797 ? 142 ASN   A N   1 
ATOM   1098 C CA  . ASN   A 1 142 ? -17.68879 -12.65627 -18.27837 1.000 24.03860 ? 142 ASN   A CA  1 
ATOM   1099 C C   . ASN   A 1 142 ? -18.08965 -11.25053 -17.86386 1.000 25.46234 ? 142 ASN   A C   1 
ATOM   1100 O O   . ASN   A 1 142 ? -19.27801 -10.92549 -17.78940 1.000 24.41707 ? 142 ASN   A O   1 
ATOM   1101 C CB  . ASN   A 1 142 ? -17.66797 -12.76426 -19.80641 1.000 24.52023 ? 142 ASN   A CB  1 
ATOM   1102 C CG  . ASN   A 1 142 ? -16.64410 -11.80623 -20.44006 1.000 34.63235 ? 142 ASN   A CG  1 
ATOM   1103 O OD1 . ASN   A 1 142 ? -16.78150 -11.38269 -21.59773 1.000 35.94201 ? 142 ASN   A OD1 1 
ATOM   1104 N ND2 . ASN   A 1 142 ? -15.59095 -11.47764 -19.67440 1.000 32.13173 ? 142 ASN   A ND2 1 
ATOM   1105 N N   . GLY   A 1 143 ? -17.09147 -10.42190 -17.56229 1.000 23.38640 ? 143 GLY   A N   1 
ATOM   1106 C CA  . GLY   A 1 143 ? -17.35126 -9.06953  -17.12776 1.000 21.90834 ? 143 GLY   A CA  1 
ATOM   1107 C C   . GLY   A 1 143 ? -17.52437 -8.92348  -15.63934 1.000 19.36165 ? 143 GLY   A C   1 
ATOM   1108 O O   . GLY   A 1 143 ? -17.68997 -7.79838  -15.15700 1.000 19.50790 ? 143 GLY   A O   1 
ATOM   1109 N N   . SER   A 1 144 ? -17.49545 -10.02088 -14.89634 1.000 16.76521 ? 144 SER   A N   1 
ATOM   1110 C CA  . SER   A 1 144 ? -17.58038 -9.94456  -13.45120 1.000 17.04678 ? 144 SER   A CA  1 
ATOM   1111 C C   . SER   A 1 144 ? -16.25884 -9.57500  -12.80437 1.000 14.93937 ? 144 SER   A C   1 
ATOM   1112 O O   . SER   A 1 144 ? -16.22968 -9.37378  -11.59508 1.000 13.16404 ? 144 SER   A O   1 
ATOM   1113 C CB  . SER   A 1 144 ? -18.06832 -11.28490 -12.88877 1.000 17.84061 ? 144 SER   A CB  1 
ATOM   1114 O OG  . SER   A 1 144 ? -17.34182 -12.36435 -13.44991 1.000 16.45827 ? 144 SER   A OG  1 
ATOM   1115 N N   . CYS   A 1 145 ? -15.16915 -9.49940  -13.56439 1.000 16.16916 ? 145 CYS   A N   1 
ATOM   1116 C CA  . CYS   A 1 145 ? -13.89300 -9.10807  -12.97071 1.000 16.54989 ? 145 CYS   A CA  1 
ATOM   1117 C C   . CYS   A 1 145 ? -14.03345 -7.75629  -12.30039 1.000 15.94271 ? 145 CYS   A C   1 
ATOM   1118 O O   . CYS   A 1 145 ? -14.77263 -6.89028  -12.77421 1.000 16.81704 ? 145 CYS   A O   1 
ATOM   1119 C CB  . CYS   A 1 145 ? -12.79498 -9.08693  -14.02946 1.000 16.87961 ? 145 CYS   A CB  1 
ATOM   1120 S SG  . CYS   A 1 145 ? -12.42492 -10.78521 -14.46048 1.000 23.02445 ? 145 CYS   A SG  1 
ATOM   1121 N N   . GLY   A 1 146 ? -13.39273 -7.60936  -11.14118 1.000 14.71114 ? 146 GLY   A N   1 
ATOM   1122 C CA  . GLY   A 1 146 ? -13.55186 -6.41747  -10.33376 1.000 16.88264 ? 146 GLY   A CA  1 
ATOM   1123 C C   . GLY   A 1 146 ? -14.61030 -6.47880  -9.23918  1.000 15.82791 ? 146 GLY   A C   1 
ATOM   1124 O O   . GLY   A 1 146 ? -14.60483 -5.61110  -8.35828  1.000 15.76108 ? 146 GLY   A O   1 
ATOM   1125 N N   . SER   A 1 147 ? -15.52570 -7.45835  -9.27526  1.000 14.42073 ? 147 SER   A N   1 
ATOM   1126 C CA  . SER   A 1 147 ? -16.42016 -7.71632  -8.14689  1.000 11.42681 ? 147 SER   A CA  1 
ATOM   1127 C C   . SER   A 1 147 ? -15.59935 -8.05822  -6.91468  1.000 12.20877 ? 147 SER   A C   1 
ATOM   1128 O O   . SER   A 1 147 ? -14.56302 -8.71985  -7.01730  1.000 12.04486 ? 147 SER   A O   1 
ATOM   1129 C CB  . SER   A 1 147 ? -17.35925 -8.88903  -8.45919  1.000 12.42450 ? 147 SER   A CB  1 
ATOM   1130 O OG  . SER   A 1 147 ? -18.09482 -8.67194  -9.64998  1.000 13.84561 ? 147 SER   A OG  1 
ATOM   1131 N N   . VAL   A 1 148 ? -16.06558 -7.63479  -5.74069  1.000 10.11214 ? 148 VAL   A N   1 
ATOM   1132 C CA  . VAL   A 1 148 ? -15.28261 -7.82084  -4.53304  1.000 9.80629  ? 148 VAL   A CA  1 
ATOM   1133 C C   . VAL   A 1 148 ? -15.97313 -8.75725  -3.54845  1.000 10.24546 ? 148 VAL   A C   1 
ATOM   1134 O O   . VAL   A 1 148 ? -17.17694 -9.02280  -3.60692  1.000 10.86943 ? 148 VAL   A O   1 
ATOM   1135 C CB  . VAL   A 1 148 ? -14.93023 -6.48000  -3.84242  1.000 11.23110 ? 148 VAL   A CB  1 
ATOM   1136 C CG1 . VAL   A 1 148 ? -13.98141 -5.64668  -4.74890  1.000 9.29976  ? 148 VAL   A CG1 1 
ATOM   1137 C CG2 . VAL   A 1 148 ? -16.18392 -5.69966  -3.47937  1.000 9.82346  ? 148 VAL   A CG2 1 
ATOM   1138 N N   . GLY   A 1 149 ? -15.16209 -9.27495  -2.63688  1.000 9.57525  ? 149 GLY   A N   1 
ATOM   1139 C CA  . GLY   A 1 149 ? -15.62678 -10.04731 -1.50650  1.000 8.42001  ? 149 GLY   A CA  1 
ATOM   1140 C C   . GLY   A 1 149 ? -15.36995 -9.25715  -0.24194  1.000 10.85992 ? 149 GLY   A C   1 
ATOM   1141 O O   . GLY   A 1 149 ? -14.38962 -8.50100  -0.14874  1.000 8.47156  ? 149 GLY   A O   1 
ATOM   1142 N N   . PHE   A 1 150 ? -16.25116 -9.42111  0.73867   1.000 8.16478  ? 150 PHE   A N   1 
ATOM   1143 C CA  . PHE   A 1 150 ? -16.12412 -8.55884  1.90096   1.000 10.77070 ? 150 PHE   A CA  1 
ATOM   1144 C C   . PHE   A 1 150 ? -16.80125 -9.18534  3.10231   1.000 11.36273 ? 150 PHE   A C   1 
ATOM   1145 O O   . PHE   A 1 150 ? -17.69113 -10.03179 2.97545   1.000 9.13845  ? 150 PHE   A O   1 
ATOM   1146 C CB  . PHE   A 1 150 ? -16.72992 -7.18143  1.63903   1.000 11.87404 ? 150 PHE   A CB  1 
ATOM   1147 C CG  . PHE   A 1 150 ? -18.18241 -7.23282  1.24263   1.000 11.50547 ? 150 PHE   A CG  1 
ATOM   1148 C CD1 . PHE   A 1 150 ? -18.54633 -7.48994  -0.07408  1.000 11.21054 ? 150 PHE   A CD1 1 
ATOM   1149 C CD2 . PHE   A 1 150 ? -19.17497 -7.02498  2.19149   1.000 10.73999 ? 150 PHE   A CD2 1 
ATOM   1150 C CE1 . PHE   A 1 150 ? -19.89045 -7.53622  -0.44020  1.000 12.78650 ? 150 PHE   A CE1 1 
ATOM   1151 C CE2 . PHE   A 1 150 ? -20.51498 -7.07948  1.84001   1.000 13.76131 ? 150 PHE   A CE2 1 
ATOM   1152 C CZ  . PHE   A 1 150 ? -20.88031 -7.32507  0.51959   1.000 11.35612 ? 150 PHE   A CZ  1 
ATOM   1153 N N   . ASN   A 1 151 ? -16.36456 -8.73647  4.27564   1.000 10.65670 ? 151 ASN   A N   1 
ATOM   1154 C CA  . ASN   A 1 151 ? -17.07479 -8.92930  5.52671   1.000 13.25182 ? 151 ASN   A CA  1 
ATOM   1155 C C   . ASN   A 1 151 ? -17.44367 -7.55155  6.06320   1.000 15.00581 ? 151 ASN   A C   1 
ATOM   1156 O O   . ASN   A 1 151 ? -16.95399 -6.52800  5.57891   1.000 14.31692 ? 151 ASN   A O   1 
ATOM   1157 C CB  . ASN   A 1 151 ? -16.22530 -9.73254  6.52106   1.000 11.91133 ? 151 ASN   A CB  1 
ATOM   1158 C CG  . ASN   A 1 151 ? -16.22837 -11.22955 6.20727   1.000 13.73370 ? 151 ASN   A CG  1 
ATOM   1159 O OD1 . ASN   A 1 151 ? -15.24088 -11.78179 5.71816   1.000 13.40758 ? 151 ASN   A OD1 1 
ATOM   1160 N ND2 . ASN   A 1 151 ? -17.34976 -11.88666 6.46726   1.000 17.04952 ? 151 ASN   A ND2 1 
ATOM   1161 N N   . ILE   A 1 152 ? -18.34208 -7.52448  7.04112   1.000 13.81081 ? 152 ILE   A N   1 
ATOM   1162 C CA  . ILE   A 1 152 ? -18.78756 -6.29125  7.67568   1.000 19.55100 ? 152 ILE   A CA  1 
ATOM   1163 C C   . ILE   A 1 152 ? -18.67955 -6.46149  9.17936   1.000 26.52944 ? 152 ILE   A C   1 
ATOM   1164 O O   . ILE   A 1 152 ? -19.05342 -7.50387  9.73072   1.000 28.76479 ? 152 ILE   A O   1 
ATOM   1165 C CB  . ILE   A 1 152 ? -20.22726 -5.89840  7.28142   1.000 23.53033 ? 152 ILE   A CB  1 
ATOM   1166 C CG1 . ILE   A 1 152 ? -20.33305 -5.73302  5.76446   1.000 18.75915 ? 152 ILE   A CG1 1 
ATOM   1167 C CG2 . ILE   A 1 152 ? -20.62032 -4.59208  7.96060   1.000 28.55924 ? 152 ILE   A CG2 1 
ATOM   1168 C CD1 . ILE   A 1 152 ? -21.58338 -4.98951  5.30679   1.000 21.95352 ? 152 ILE   A CD1 1 
ATOM   1169 N N   . ASP   A 1 153 ? -18.14794 -5.44021  9.84106   1.000 30.46966 ? 153 ASP   A N   1 
ATOM   1170 C CA  . ASP   A 1 153 ? -17.86070 -5.53922  11.26534  1.000 35.87980 ? 153 ASP   A CA  1 
ATOM   1171 C C   . ASP   A 1 153 ? -18.27256 -4.19599  11.87125  1.000 37.07645 ? 153 ASP   A C   1 
ATOM   1172 O O   . ASP   A 1 153 ? -17.61049 -3.18180  11.64440  1.000 33.56426 ? 153 ASP   A O   1 
ATOM   1173 C CB  . ASP   A 1 153 ? -16.39422 -5.86116  11.49166  1.000 35.84296 ? 153 ASP   A CB  1 
ATOM   1174 C CG  . ASP   A 1 153 ? -16.15777 -6.58915  12.78645  1.000 44.21622 ? 153 ASP   A CG  1 
ATOM   1175 O OD1 . ASP   A 1 153 ? -16.75585 -6.19312  13.80795  1.000 42.11905 ? 153 ASP   A OD1 1 
ATOM   1176 O OD2 . ASP   A 1 153 ? -15.40330 -7.59416  12.77128  1.000 45.91501 ? 153 ASP   A OD2 1 
ATOM   1177 N N   . TYR   A 1 154 ? -19.36396 -4.21614  12.63448  1.000 38.83417 ? 154 TYR   A N   1 
ATOM   1178 C CA  . TYR   A 1 154 ? -20.21937 -3.05154  12.84683  1.000 42.66970 ? 154 TYR   A CA  1 
ATOM   1179 C C   . TYR   A 1 154 ? -20.38223 -2.24559  11.56293  1.000 43.35649 ? 154 TYR   A C   1 
ATOM   1180 O O   . TYR   A 1 154 ? -21.06542 -2.69047  10.63890  1.000 45.61661 ? 154 TYR   A O   1 
ATOM   1181 C CB  . TYR   A 1 154 ? -19.72392 -2.14698  13.97553  1.000 44.14060 ? 154 TYR   A CB  1 
ATOM   1182 C CG  . TYR   A 1 154 ? -20.78732 -1.12198  14.31843  1.000 54.41457 ? 154 TYR   A CG  1 
ATOM   1183 C CD1 . TYR   A 1 154 ? -22.12887 -1.49335  14.36642  1.000 53.08543 ? 154 TYR   A CD1 1 
ATOM   1184 C CD2 . TYR   A 1 154 ? -20.46574 0.21649   14.54391  1.000 53.76414 ? 154 TYR   A CD2 1 
ATOM   1185 C CE1 . TYR   A 1 154 ? -23.12369 -0.57010  14.65026  1.000 57.10437 ? 154 TYR   A CE1 1 
ATOM   1186 C CE2 . TYR   A 1 154 ? -21.45445 1.15636   14.82977  1.000 53.50902 ? 154 TYR   A CE2 1 
ATOM   1187 C CZ  . TYR   A 1 154 ? -22.78364 0.75437   14.88242  1.000 62.75501 ? 154 TYR   A CZ  1 
ATOM   1188 O OH  . TYR   A 1 154 ? -23.77950 1.66494   15.16960  1.000 63.17640 ? 154 TYR   A OH  1 
ATOM   1189 N N   . ASP   A 1 155 ? -19.78204 -1.06279  11.47550  1.000 39.62544 ? 155 ASP   A N   1 
ATOM   1190 C CA  . ASP   A 1 155 ? -19.99325 -0.21567  10.30926  1.000 41.52147 ? 155 ASP   A CA  1 
ATOM   1191 C C   . ASP   A 1 155 ? -18.79922 -0.18493  9.36622   1.000 34.93959 ? 155 ASP   A C   1 
ATOM   1192 O O   . ASP   A 1 155 ? -18.78119 0.63042   8.43439   1.000 27.36864 ? 155 ASP   A O   1 
ATOM   1193 C CB  . ASP   A 1 155 ? -20.37668 1.19823   10.74783  1.000 43.88103 ? 155 ASP   A CB  1 
ATOM   1194 C CG  . ASP   A 1 155 ? -21.82273 1.27010   11.19105  1.000 54.81261 ? 155 ASP   A CG  1 
ATOM   1195 O OD1 . ASP   A 1 155 ? -22.59566 0.45535   10.64454  1.000 53.96750 ? 155 ASP   A OD1 1 
ATOM   1196 O OD2 . ASP   A 1 155 ? -22.19291 2.11008   12.05049  1.000 57.34831 ? 155 ASP   A OD2 1 
ATOM   1197 N N   . CYS   A 1 156 ? -17.82907 -1.07640  9.56706   1.000 31.50052 ? 156 CYS   A N   1 
ATOM   1198 C CA  . CYS   A 1 156 ? -16.60750 -1.13546  8.77679   1.000 25.21044 ? 156 CYS   A CA  1 
ATOM   1199 C C   . CYS   A 1 156 ? -16.66646 -2.29045  7.78696   1.000 24.00509 ? 156 CYS   A C   1 
ATOM   1200 O O   . CYS   A 1 156 ? -16.86508 -3.44767  8.18509   1.000 21.50101 ? 156 CYS   A O   1 
ATOM   1201 C CB  . CYS   A 1 156 ? -15.39080 -1.30599  9.68169   1.000 27.29600 ? 156 CYS   A CB  1 
ATOM   1202 S SG  . CYS   A 1 156 ? -13.85118 -1.20511  8.76473   1.000 23.84713 ? 156 CYS   A SG  1 
ATOM   1203 N N   . VAL   A 1 157 ? -16.47199 -1.97284  6.50824   1.000 19.58675 ? 157 VAL   A N   1 
ATOM   1204 C CA  . VAL   A 1 157 ? -16.40182 -2.96674  5.44479   1.000 17.54091 ? 157 VAL   A CA  1 
ATOM   1205 C C   . VAL   A 1 157 ? -14.95454 -3.45334  5.33827   1.000 18.77195 ? 157 VAL   A C   1 
ATOM   1206 O O   . VAL   A 1 157 ? -14.05998 -2.70002  4.95270   1.000 16.65074 ? 157 VAL   A O   1 
ATOM   1207 C CB  . VAL   A 1 157 ? -16.89605 -2.39368  4.10926   1.000 14.55896 ? 157 VAL   A CB  1 
ATOM   1208 C CG1 . VAL   A 1 157 ? -16.74256 -3.43242  3.00917   1.000 12.14489 ? 157 VAL   A CG1 1 
ATOM   1209 C CG2 . VAL   A 1 157 ? -18.35959 -1.96124  4.23215   1.000 19.29417 ? 157 VAL   A CG2 1 
ATOM   1210 N N   . SER   A 1 158 ? -14.71460 -4.71211  5.68991   1.000 17.83142 ? 158 SER   A N   1 
ATOM   1211 C CA  . SER   A 1 158 ? -13.40035 -5.31052  5.48101   1.000 17.38372 ? 158 SER   A CA  1 
ATOM   1212 C C   . SER   A 1 158 ? -13.41445 -5.98493  4.11903   1.000 14.19551 ? 158 SER   A C   1 
ATOM   1213 O O   . SER   A 1 158 ? -13.97086 -7.07694  3.94924   1.000 11.30956 ? 158 SER   A O   1 
ATOM   1214 C CB  . SER   A 1 158 ? -13.05044 -6.29020  6.59137   1.000 15.73760 ? 158 SER   A CB  1 
ATOM   1215 O OG  . SER   A 1 158 ? -12.83185 -5.58614  7.78837   1.000 22.64913 ? 158 SER   A OG  1 
ATOM   1216 N N   . PHE   A 1 159 ? -12.81179 -5.32393  3.14356   1.000 12.98959 ? 159 PHE   A N   1 
ATOM   1217 C CA  . PHE   A 1 159 ? -12.68884 -5.88734  1.80695   1.000 11.55978 ? 159 PHE   A CA  1 
ATOM   1218 C C   . PHE   A 1 159 ? -11.59931 -6.94055  1.79853   1.000 13.50046 ? 159 PHE   A C   1 
ATOM   1219 O O   . PHE   A 1 159 ? -10.46741 -6.68097  2.24591   1.000 11.53445 ? 159 PHE   A O   1 
ATOM   1220 C CB  . PHE   A 1 159 ? -12.34418 -4.79683  0.81045   1.000 11.74724 ? 159 PHE   A CB  1 
ATOM   1221 C CG  . PHE   A 1 159 ? -13.46788 -3.88038  0.50828   1.000 12.59284 ? 159 PHE   A CG  1 
ATOM   1222 C CD1 . PHE   A 1 159 ? -14.49593 -4.28173  -0.32474  1.000 12.77293 ? 159 PHE   A CD1 1 
ATOM   1223 C CD2 . PHE   A 1 159 ? -13.48366 -2.59339  1.02221   1.000 12.01856 ? 159 PHE   A CD2 1 
ATOM   1224 C CE1 . PHE   A 1 159 ? -15.53408 -3.42150  -0.61892  1.000 10.86771 ? 159 PHE   A CE1 1 
ATOM   1225 C CE2 . PHE   A 1 159 ? -14.51015 -1.73223  0.72583   1.000 10.30064 ? 159 PHE   A CE2 1 
ATOM   1226 C CZ  . PHE   A 1 159 ? -15.53769 -2.14921  -0.09480  1.000 11.91848 ? 159 PHE   A CZ  1 
ATOM   1227 N N   . CYS   A 1 160 ? -11.91814 -8.12285  1.27399   1.000 10.16064 ? 160 CYS   A N   1 
ATOM   1228 C CA  . CYS   A 1 160 ? -10.93883 -9.19532  1.28431   1.000 10.52758 ? 160 CYS   A CA  1 
ATOM   1229 C C   . CYS   A 1 160 ? -10.68705 -9.86853  -0.06376  1.000 11.42865 ? 160 CYS   A C   1 
ATOM   1230 O O   . CYS   A 1 160 ? -9.80529  -10.73741 -0.13671  1.000 11.85681 ? 160 CYS   A O   1 
ATOM   1231 C CB  . CYS   A 1 160 ? -11.33813 -10.25364 2.31352   1.000 11.07735 ? 160 CYS   A CB  1 
ATOM   1232 S SG  . CYS   A 1 160 ? -12.86670 -11.16326 1.89112   1.000 9.41653  ? 160 CYS   A SG  1 
ATOM   1233 N N   . TYR   A 1 161 ? -11.39801 -9.50060  -1.13099  1.000 9.40724  ? 161 TYR   A N   1 
ATOM   1234 C CA  . TYR   A 1 161 ? -11.28478 -10.27878 -2.36399  1.000 10.55912 ? 161 TYR   A CA  1 
ATOM   1235 C C   . TYR   A 1 161 ? -11.69744 -9.44283  -3.55443  1.000 10.21299 ? 161 TYR   A C   1 
ATOM   1236 O O   . TYR   A 1 161 ? -12.70449 -8.74192  -3.49732  1.000 8.46279  ? 161 TYR   A O   1 
ATOM   1237 C CB  . TYR   A 1 161 ? -12.15891 -11.53702 -2.33483  1.000 8.44104  ? 161 TYR   A CB  1 
ATOM   1238 C CG  . TYR   A 1 161 ? -12.08353 -12.36746 -3.60353  1.000 9.15313  ? 161 TYR   A CG  1 
ATOM   1239 C CD1 . TYR   A 1 161 ? -10.95582 -13.12957 -3.87811  1.000 9.75370  ? 161 TYR   A CD1 1 
ATOM   1240 C CD2 . TYR   A 1 161 ? -13.15084 -12.41860 -4.51457  1.000 7.52672  ? 161 TYR   A CD2 1 
ATOM   1241 C CE1 . TYR   A 1 161 ? -10.86782 -13.92235 -5.02107  1.000 9.88607  ? 161 TYR   A CE1 1 
ATOM   1242 C CE2 . TYR   A 1 161 ? -13.07871 -13.21325 -5.65977  1.000 7.32048  ? 161 TYR   A CE2 1 
ATOM   1243 C CZ  . TYR   A 1 161 ? -11.92799 -13.96412 -5.90243  1.000 8.97146  ? 161 TYR   A CZ  1 
ATOM   1244 O OH  . TYR   A 1 161 ? -11.78191 -14.76249 -6.99400  1.000 6.87486  ? 161 TYR   A OH  1 
ATOM   1245 N N   . MET   A 1 162 ? -10.91060 -9.52780  -4.62007  1.000 8.75595  ? 162 MET   A N   1 
ATOM   1246 C CA  . MET   A 1 162 ? -11.26952 -9.00218  -5.91934  1.000 10.58946 ? 162 MET   A CA  1 
ATOM   1247 C C   . MET   A 1 162 ? -11.17215 -10.12186 -6.94623  1.000 10.27359 ? 162 MET   A C   1 
ATOM   1248 O O   . MET   A 1 162 ? -10.18521 -10.87591 -6.96966  1.000 7.93675  ? 162 MET   A O   1 
ATOM   1249 C CB  . MET   A 1 162 ? -10.37477 -7.84488  -6.31119  1.000 10.02682 ? 162 MET   A CB  1 
ATOM   1250 C CG  . MET   A 1 162 ? -10.67401 -7.35335  -7.70962  1.000 10.60011 ? 162 MET   A CG  1 
ATOM   1251 S SD  . MET   A 1 162 ? -9.96010  -5.74210  -8.08037  1.000 17.66900 ? 162 MET   A SD  1 
ATOM   1252 C CE  . MET   A 1 162 ? -11.02256 -4.61913  -7.15321  1.000 17.99666 ? 162 MET   A CE  1 
ATOM   1253 N N   . HIS   A 1 163 ? -12.19002 -10.22450 -7.80942  1.000 9.97176  ? 163 HIS   A N   1 
ATOM   1254 C CA  . HIS   A 1 163 ? -12.25765 -11.32319 -8.76804  1.000 9.82179  ? 163 HIS   A CA  1 
ATOM   1255 C C   . HIS   A 1 163 ? -11.47012 -11.04210 -10.04608 1.000 10.82113 ? 163 HIS   A C   1 
ATOM   1256 O O   . HIS   A 1 163 ? -11.61071 -9.97284  -10.64755 1.000 10.44006 ? 163 HIS   A O   1 
ATOM   1257 C CB  . HIS   A 1 163 ? -13.70560 -11.63706 -9.14225  1.000 12.87931 ? 163 HIS   A CB  1 
ATOM   1258 C CG  . HIS   A 1 163 ? -13.81747 -12.85765 -9.98654  1.000 10.91581 ? 163 HIS   A CG  1 
ATOM   1259 N ND1 . HIS   A 1 163 ? -13.20447 -14.03802 -9.63827  1.000 11.25493 ? 163 HIS   A ND1 1 
ATOM   1260 C CD2 . HIS   A 1 163 ? -14.40503 -13.07325 -11.18471 1.000 13.66639 ? 163 HIS   A CD2 1 
ATOM   1261 C CE1 . HIS   A 1 163 ? -13.43292 -14.94423 -10.57298 1.000 13.30299 ? 163 HIS   A CE1 1 
ATOM   1262 N NE2 . HIS   A 1 163 ? -14.17067 -14.38882 -11.51571 1.000 14.19753 ? 163 HIS   A NE2 1 
ATOM   1263 N N   . HIS   A 1 164 ? -10.66960 -12.03880 -10.47348 1.000 11.12279 ? 164 HIS   A N   1 
ATOM   1264 C CA  . HIS   A 1 164 ? -9.80870  -11.98399 -11.65795 1.000 14.22448 ? 164 HIS   A CA  1 
ATOM   1265 C C   . HIS   A 1 164 ? -10.13387 -13.04051 -12.70107 1.000 15.39731 ? 164 HIS   A C   1 
ATOM   1266 O O   . HIS   A 1 164 ? -10.19668 -12.71715 -13.88964 1.000 19.91027 ? 164 HIS   A O   1 
ATOM   1267 C CB  . HIS   A 1 164 ? -8.30896  -12.11527 -11.27832 1.000 14.37274 ? 164 HIS   A CB  1 
ATOM   1268 C CG  . HIS   A 1 164 ? -7.76850  -10.91409 -10.56275 1.000 12.87004 ? 164 HIS   A CG  1 
ATOM   1269 N ND1 . HIS   A 1 164 ? -6.82572  -10.07628 -11.11806 1.000 13.08106 ? 164 HIS   A ND1 1 
ATOM   1270 C CD2 . HIS   A 1 164 ? -8.05989  -10.39875 -9.34600  1.000 10.54192 ? 164 HIS   A CD2 1 
ATOM   1271 C CE1 . HIS   A 1 164 ? -6.56554  -9.09024  -10.27699 1.000 11.46659 ? 164 HIS   A CE1 1 
ATOM   1272 N NE2 . HIS   A 1 164 ? -7.30188  -9.26003  -9.19632  1.000 9.39586  ? 164 HIS   A NE2 1 
ATOM   1273 N N   . MET   A 1 165 ? -10.33166 -14.29806 -12.31356 1.000 15.01442 ? 165 MET   A N   1 
ATOM   1274 C CA  . MET   A 1 165 ? -10.32467 -15.32911 -13.34104 1.000 18.41327 ? 165 MET   A CA  1 
ATOM   1275 C C   . MET   A 1 165 ? -11.04743 -16.58346 -12.87877 1.000 16.95602 ? 165 MET   A C   1 
ATOM   1276 O O   . MET   A 1 165 ? -11.18532 -16.85089 -11.68202 1.000 14.50486 ? 165 MET   A O   1 
ATOM   1277 C CB  . MET   A 1 165 ? -8.88902  -15.67575 -13.76254 1.000 17.04475 ? 165 MET   A CB  1 
ATOM   1278 C CG  . MET   A 1 165 ? -8.05777  -16.32544 -12.67533 1.000 19.10827 ? 165 MET   A CG  1 
ATOM   1279 S SD  . MET   A 1 165 ? -6.31214  -16.31280 -13.15018 1.000 28.73214 ? 165 MET   A SD  1 
ATOM   1280 C CE  . MET   A 1 165 ? -6.41403  -17.00677 -14.79596 1.000 25.14882 ? 165 MET   A CE  1 
ATOM   1281 N N   . GLU   A 1 166 ? -11.50098 -17.34943 -13.86523 1.000 17.56665 ? 166 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 166 ? -12.03975 -18.68169 -13.66916 1.000 18.81274 ? 166 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 166 ? -11.04004 -19.70755 -14.20643 1.000 20.81269 ? 166 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 166 ? -10.38077 -19.47252 -15.22638 1.000 19.78690 ? 166 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 166 ? -13.39309 -18.81684 -14.37957 1.000 15.96021 ? 166 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 166 ? -14.02702 -20.20079 -14.28614 1.000 17.50511 ? 166 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 166 ? -15.44111 -20.25821 -14.92451 1.000 20.80720 ? 166 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 166 ? -16.32481 -19.43723 -14.57880 1.000 17.42516 ? 166 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 166 ? -15.65709 -21.13293 -15.77921 1.000 21.83588 ? 166 GLU   A OE2 1 
ATOM   1290 N N   . LEU   A 1 167 ? -10.92155 -20.83415 -13.50989 1.000 19.96499 ? 167 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 167 ? -10.03101 -21.93621 -13.83014 1.000 21.12462 ? 167 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 167 ? -10.78967 -23.02062 -14.57864 1.000 25.28055 ? 167 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 167 ? -12.01189 -23.14436 -14.42985 1.000 24.76461 ? 167 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 167 ? -9.42424  -22.51314 -12.54169 1.000 20.54946 ? 167 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 167 ? -8.59732  -21.55360 -11.68173 1.000 20.54048 ? 167 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 167 ? -8.21462  -22.17448 -10.35122 1.000 17.73835 ? 167 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 167 ? -7.34298  -21.14738 -12.44152 1.000 22.87908 ? 167 LEU   A CD2 1 
ATOM   1298 N N   . PRO   A 1 168 ? -10.09271 -23.83754 -15.39729 1.000 26.74827 ? 168 PRO   A N   1 
ATOM   1299 C CA  . PRO   A 1 168 ? -10.78275 -24.90847 -16.13760 1.000 25.99136 ? 168 PRO   A CA  1 
ATOM   1300 C C   . PRO   A 1 168 ? -11.75868 -25.72605 -15.30594 1.000 25.32052 ? 168 PRO   A C   1 
ATOM   1301 O O   . PRO   A 1 168 ? -12.74311 -26.23176 -15.86274 1.000 25.50682 ? 168 PRO   A O   1 
ATOM   1302 C CB  . PRO   A 1 168 ? -9.62352  -25.78030 -16.64809 1.000 25.86204 ? 168 PRO   A CB  1 
ATOM   1303 C CG  . PRO   A 1 168 ? -8.47956  -24.85580 -16.76585 1.000 25.08271 ? 168 PRO   A CG  1 
ATOM   1304 C CD  . PRO   A 1 168 ? -8.63760  -23.85878 -15.64520 1.000 27.10109 ? 168 PRO   A CD  1 
ATOM   1305 N N   . THR   A 1 169 ? -11.53585 -25.87566 -13.99573 1.000 24.52699 ? 169 THR   A N   1 
ATOM   1306 C CA  . THR   A 1 169 ? -12.44793 -26.71535 -13.22512 1.000 27.64787 ? 169 THR   A CA  1 
ATOM   1307 C C   . THR   A 1 169 ? -13.73407 -25.99886 -12.82905 1.000 23.68109 ? 169 THR   A C   1 
ATOM   1308 O O   . THR   A 1 169 ? -14.57059 -26.60665 -12.16000 1.000 24.19131 ? 169 THR   A O   1 
ATOM   1309 C CB  . THR   A 1 169 ? -11.76093 -27.26751 -11.96713 1.000 24.90076 ? 169 THR   A CB  1 
ATOM   1310 O OG1 . THR   A 1 169 ? -11.11845 -26.20982 -11.26101 1.000 28.55403 ? 169 THR   A OG1 1 
ATOM   1311 C CG2 . THR   A 1 169 ? -10.71616 -28.34601 -12.33470 1.000 26.97063 ? 169 THR   A CG2 1 
ATOM   1312 N N   . GLY   A 1 170 ? -13.91584 -24.73427 -13.20580 1.000 22.54960 ? 170 GLY   A N   1 
ATOM   1313 C CA  . GLY   A 1 170 ? -15.11659 -24.00852 -12.84176 1.000 22.29929 ? 170 GLY   A CA  1 
ATOM   1314 C C   . GLY   A 1 170 ? -15.03287 -23.22152 -11.55296 1.000 19.26385 ? 170 GLY   A C   1 
ATOM   1315 O O   . GLY   A 1 170 ? -15.97407 -22.48933 -11.23230 1.000 18.56980 ? 170 GLY   A O   1 
ATOM   1316 N N   . VAL   A 1 171 ? -13.93409 -23.32966 -10.81007 1.000 18.37698 ? 171 VAL   A N   1 
ATOM   1317 C CA  . VAL   A 1 171 ? -13.74160 -22.52781 -9.61144  1.000 14.56836 ? 171 VAL   A CA  1 
ATOM   1318 C C   . VAL   A 1 171 ? -13.03591 -21.23350 -9.98934  1.000 16.72120 ? 171 VAL   A C   1 
ATOM   1319 O O   . VAL   A 1 171 ? -12.73804 -20.99126 -11.16245 1.000 14.31797 ? 171 VAL   A O   1 
ATOM   1320 C CB  . VAL   A 1 171 ? -12.94486 -23.30296 -8.55504  1.000 17.05799 ? 171 VAL   A CB  1 
ATOM   1321 C CG1 . VAL   A 1 171 ? -13.71636 -24.58108 -8.14690  1.000 20.23318 ? 171 VAL   A CG1 1 
ATOM   1322 C CG2 . VAL   A 1 171 ? -11.55970 -23.64246 -9.09898  1.000 14.15800 ? 171 VAL   A CG2 1 
ATOM   1323 N N   . HIS   A 1 172 ? -12.72383 -20.41536 -8.99056  1.000 14.38199 ? 172 HIS   A N   1 
ATOM   1324 C CA  . HIS   A 1 172 ? -12.43523 -19.01570 -9.22865  1.000 11.82144 ? 172 HIS   A CA  1 
ATOM   1325 C C   . HIS   A 1 172 ? -11.24480 -18.58376 -8.39711  1.000 12.89738 ? 172 HIS   A C   1 
ATOM   1326 O O   . HIS   A 1 172 ? -11.03478 -19.06754 -7.27522  1.000 9.88176  ? 172 HIS   A O   1 
ATOM   1327 C CB  . HIS   A 1 172 ? -13.66083 -18.14662 -8.89552  1.000 12.85372 ? 172 HIS   A CB  1 
ATOM   1328 C CG  . HIS   A 1 172 ? -14.83476 -18.40835 -9.78470  1.000 16.19376 ? 172 HIS   A CG  1 
ATOM   1329 N ND1 . HIS   A 1 172 ? -15.88926 -19.21376 -9.40329  1.000 14.21931 ? 172 HIS   A ND1 1 
ATOM   1330 C CD2 . HIS   A 1 172 ? -15.10592 -18.01063 -11.05181 1.000 16.75414 ? 172 HIS   A CD2 1 
ATOM   1331 C CE1 . HIS   A 1 172 ? -16.76490 -19.28415 -10.39010 1.000 16.01037 ? 172 HIS   A CE1 1 
ATOM   1332 N NE2 . HIS   A 1 172 ? -16.31198 -18.56476 -11.40380 1.000 15.94680 ? 172 HIS   A NE2 1 
ATOM   1333 N N   . ALA   A 1 173 ? -10.50337 -17.61702 -8.93897  1.000 10.90992 ? 173 ALA   A N   1 
ATOM   1334 C CA  . ALA   A 1 173 ? -9.27523  -17.15101 -8.32677  1.000 10.15291 ? 173 ALA   A CA  1 
ATOM   1335 C C   . ALA   A 1 173 ? -9.20951  -15.63856 -8.44105  1.000 11.91869 ? 173 ALA   A C   1 
ATOM   1336 O O   . ALA   A 1 173 ? -9.72116  -15.04577 -9.39380  1.000 10.45001 ? 173 ALA   A O   1 
ATOM   1337 C CB  . ALA   A 1 173 ? -8.02159  -17.78602 -8.97819  1.000 8.62071  ? 173 ALA   A CB  1 
ATOM   1338 N N   . GLY   A 1 174 ? -8.57048  -15.02416 -7.45750  1.000 10.09338 ? 174 GLY   A N   1 
ATOM   1339 C CA  . GLY   A 1 174 ? -8.43390  -13.58780 -7.45662  1.000 11.03676 ? 174 GLY   A CA  1 
ATOM   1340 C C   . GLY   A 1 174 ? -7.47198  -13.16477 -6.38298  1.000 10.29314 ? 174 GLY   A C   1 
ATOM   1341 O O   . GLY   A 1 174 ? -6.70338  -13.98033 -5.86211  1.000 8.27390  ? 174 GLY   A O   1 
ATOM   1342 N N   . THR   A 1 175 ? -7.54257  -11.88429 -6.04211  1.000 9.33909  ? 175 THR   A N   1 
ATOM   1343 C CA  . THR   A 1 175 ? -6.55133  -11.24523 -5.18554  1.000 11.54292 ? 175 THR   A CA  1 
ATOM   1344 C C   . THR   A 1 175 ? -7.21987  -10.62655 -3.96523  1.000 12.54940 ? 175 THR   A C   1 
ATOM   1345 O O   . THR   A 1 175 ? -8.44798  -10.44527 -3.90957  1.000 8.63123  ? 175 THR   A O   1 
ATOM   1346 C CB  . THR   A 1 175 ? -5.77860  -10.15374 -5.95166  1.000 10.34375 ? 175 THR   A CB  1 
ATOM   1347 O OG1 . THR   A 1 175 ? -6.64185  -9.05188  -6.25719  1.000 7.69143  ? 175 THR   A OG1 1 
ATOM   1348 C CG2 . THR   A 1 175 ? -5.19087  -10.70220 -7.23002  1.000 9.76748  ? 175 THR   A CG2 1 
ATOM   1349 N N   . ASP   A 1 176 ? -6.38947  -10.29331 -2.98353  1.000 10.98108 ? 176 ASP   A N   1 
ATOM   1350 C CA  . ASP   A 1 176 ? -6.80801  -9.33904  -1.97068  1.000 9.14012  ? 176 ASP   A CA  1 
ATOM   1351 C C   . ASP   A 1 176 ? -6.86727  -7.95224  -2.60902  1.000 7.66924  ? 176 ASP   A C   1 
ATOM   1352 O O   . ASP   A 1 176 ? -6.51192  -7.76151  -3.76907  1.000 7.74736  ? 176 ASP   A O   1 
ATOM   1353 C CB  . ASP   A 1 176 ? -5.87948  -9.40463  -0.74684  1.000 8.82128  ? 176 ASP   A CB  1 
ATOM   1354 C CG  . ASP   A 1 176 ? -4.44898  -8.95561  -1.02729  1.000 9.57462  ? 176 ASP   A CG  1 
ATOM   1355 O OD1 . ASP   A 1 176 ? -4.20134  -8.02692  -1.83613  1.000 10.06834 ? 176 ASP   A OD1 1 
ATOM   1356 O OD2 . ASP   A 1 176 ? -3.54421  -9.52516  -0.38968  1.000 9.59852  ? 176 ASP   A OD2 1 
ATOM   1357 N N   . LEU   A 1 177 ? -7.33523  -6.96637  -1.86757  1.000 7.87283  ? 177 LEU   A N   1 
ATOM   1358 C CA  . LEU   A 1 177 ? -7.45770  -5.64253  -2.46888  1.000 9.42143  ? 177 LEU   A CA  1 
ATOM   1359 C C   . LEU   A 1 177 ? -6.11547  -4.91749  -2.60753  1.000 12.91121 ? 177 LEU   A C   1 
ATOM   1360 O O   . LEU   A 1 177 ? -6.10109  -3.74384  -3.00182  1.000 13.64634 ? 177 LEU   A O   1 
ATOM   1361 C CB  . LEU   A 1 177 ? -8.45915  -4.80056  -1.66541  1.000 9.95629  ? 177 LEU   A CB  1 
ATOM   1362 C CG  . LEU   A 1 177 ? -9.93037  -4.92594  -2.13819  1.000 12.17483 ? 177 LEU   A CG  1 
ATOM   1363 C CD1 . LEU   A 1 177 ? -10.14289 -4.30759  -3.51994  1.000 12.90368 ? 177 LEU   A CD1 1 
ATOM   1364 C CD2 . LEU   A 1 177 ? -10.34503 -6.39631  -2.17083  1.000 8.91378  ? 177 LEU   A CD2 1 
ATOM   1365 N N   . GLU   A 1 178 ? -4.99018  -5.56009  -2.27500  1.000 11.17269 ? 178 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 178 ? -3.68081  -4.99228  -2.57940  1.000 13.70285 ? 178 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 178 ? -3.04628  -5.67277  -3.78316  1.000 13.20078 ? 178 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 178 ? -1.87744  -5.41653  -4.09598  1.000 15.37876 ? 178 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 178 ? -2.75329  -5.07806  -1.36082  1.000 13.29439 ? 178 GLU   A CB  1 
ATOM   1370 N N   . GLY   A 1 179 ? -3.78962  -6.53599  -4.46461  1.000 11.77662 ? 179 GLY   A N   1 
ATOM   1371 C CA  . GLY   A 1 179 ? -3.32041  -7.13726  -5.68758  1.000 12.70720 ? 179 GLY   A CA  1 
ATOM   1372 C C   . GLY   A 1 179 ? -2.59986  -8.46224  -5.57247  1.000 14.21320 ? 179 GLY   A C   1 
ATOM   1373 O O   . GLY   A 1 179 ? -2.26766  -9.04727  -6.61549  1.000 12.38334 ? 179 GLY   A O   1 
ATOM   1374 N N   . ASN   A 1 180 ? -2.34764  -8.96325  -4.36211  1.000 10.78429 ? 180 ASN   A N   1 
ATOM   1375 C CA  . ASN   A 1 180 ? -1.73318  -10.27939 -4.21034  1.000 10.03838 ? 180 ASN   A CA  1 
ATOM   1376 C C   . ASN   A 1 180 ? -2.76403  -11.37716 -4.42113  1.000 11.33011 ? 180 ASN   A C   1 
ATOM   1377 O O   . ASN   A 1 180 ? -3.76250  -11.43702 -3.69492  1.000 9.33735  ? 180 ASN   A O   1 
ATOM   1378 C CB  . ASN   A 1 180 ? -1.11589  -10.41390 -2.83064  1.000 10.39705 ? 180 ASN   A CB  1 
ATOM   1379 C CG  . ASN   A 1 180 ? -0.28771  -9.21153  -2.47098  1.000 10.53860 ? 180 ASN   A CG  1 
ATOM   1380 O OD1 . ASN   A 1 180 ? 0.72134   -8.94998  -3.11520  1.000 10.46625 ? 180 ASN   A OD1 1 
ATOM   1381 N ND2 . ASN   A 1 180 ? -0.74717  -8.43236  -1.49563  1.000 9.13451  ? 180 ASN   A ND2 1 
ATOM   1382 N N   . PHE   A 1 181 ? -2.49043  -12.28368 -5.36620  1.000 12.01412 ? 181 PHE   A N   1 
ATOM   1383 C CA  . PHE   A 1 181 ? -3.36828  -13.43147 -5.56250  1.000 11.57433 ? 181 PHE   A CA  1 
ATOM   1384 C C   . PHE   A 1 181 ? -3.45373  -14.25525 -4.29048  1.000 10.59807 ? 181 PHE   A C   1 
ATOM   1385 O O   . PHE   A 1 181 ? -2.49811  -14.36737 -3.52147  1.000 10.42855 ? 181 PHE   A O   1 
ATOM   1386 C CB  . PHE   A 1 181 ? -2.88982  -14.31294 -6.73538  1.000 11.10169 ? 181 PHE   A CB  1 
ATOM   1387 C CG  . PHE   A 1 181 ? -3.58816  -13.98793 -8.05783  1.000 12.11245 ? 181 PHE   A CG  1 
ATOM   1388 C CD1 . PHE   A 1 181 ? -4.85004  -14.50788 -8.34540  1.000 10.82834 ? 181 PHE   A CD1 1 
ATOM   1389 C CD2 . PHE   A 1 181 ? -3.00787  -13.11576 -8.96473  1.000 9.71977  ? 181 PHE   A CD2 1 
ATOM   1390 C CE1 . PHE   A 1 181 ? -5.49987  -14.18571 -9.51604  1.000 10.35098 ? 181 PHE   A CE1 1 
ATOM   1391 C CE2 . PHE   A 1 181 ? -3.64583  -12.79149 -10.12839 1.000 14.54429 ? 181 PHE   A CE2 1 
ATOM   1392 C CZ  . PHE   A 1 181 ? -4.89441  -13.34169 -10.41547 1.000 12.63876 ? 181 PHE   A CZ  1 
ATOM   1393 N N   . TYR   A 1 182 ? -4.62063  -14.82077 -4.06143  1.000 9.62805  ? 182 TYR   A N   1 
ATOM   1394 C CA  . TYR   A 1 182 ? -4.71888  -15.96934 -3.18459  1.000 10.90167 ? 182 TYR   A CA  1 
ATOM   1395 C C   . TYR   A 1 182 ? -4.24483  -17.18334 -3.96638  1.000 13.03265 ? 182 TYR   A C   1 
ATOM   1396 O O   . TYR   A 1 182 ? -4.70300  -17.42068 -5.08625  1.000 9.47185  ? 182 TYR   A O   1 
ATOM   1397 C CB  . TYR   A 1 182 ? -6.15361  -16.16968 -2.70209  1.000 10.85399 ? 182 TYR   A CB  1 
ATOM   1398 C CG  . TYR   A 1 182 ? -6.61540  -15.09980 -1.73132  1.000 12.06676 ? 182 TYR   A CG  1 
ATOM   1399 C CD1 . TYR   A 1 182 ? -6.34521  -15.20434 -0.37548  1.000 9.65953  ? 182 TYR   A CD1 1 
ATOM   1400 C CD2 . TYR   A 1 182 ? -7.32458  -13.99511 -2.17291  1.000 9.63611  ? 182 TYR   A CD2 1 
ATOM   1401 C CE1 . TYR   A 1 182 ? -6.79275  -14.23171 0.52103   1.000 11.07914 ? 182 TYR   A CE1 1 
ATOM   1402 C CE2 . TYR   A 1 182 ? -7.74606  -13.01191 -1.29726  1.000 8.63120  ? 182 TYR   A CE2 1 
ATOM   1403 C CZ  . TYR   A 1 182 ? -7.47710  -13.13322 0.05428   1.000 9.35865  ? 182 TYR   A CZ  1 
ATOM   1404 O OH  . TYR   A 1 182 ? -7.90179  -12.16345 0.93529   1.000 8.57764  ? 182 TYR   A OH  1 
ATOM   1405 N N   . GLY   A 1 183 ? -3.30406  -17.92624 -3.39387  1.000 11.77325 ? 183 GLY   A N   1 
ATOM   1406 C CA  . GLY   A 1 183 ? -2.85495  -19.16428 -3.99374  1.000 13.40083 ? 183 GLY   A CA  1 
ATOM   1407 C C   . GLY   A 1 183 ? -1.74930  -18.93768 -4.99271  1.000 12.94031 ? 183 GLY   A C   1 
ATOM   1408 O O   . GLY   A 1 183 ? -1.15958  -17.85060 -5.07602  1.000 12.29731 ? 183 GLY   A O   1 
ATOM   1409 N N   . PRO   A 1 184 ? -1.45331  -19.94824 -5.77074  1.000 13.89019 ? 184 PRO   A N   1 
ATOM   1410 C CA  . PRO   A 1 184 ? -0.26099  -19.89094 -6.63204  1.000 16.92066 ? 184 PRO   A CA  1 
ATOM   1411 C C   . PRO   A 1 184 ? -0.56754  -19.38378 -8.02567  1.000 17.52220 ? 184 PRO   A C   1 
ATOM   1412 O O   . PRO   A 1 184 ? 0.20184   -19.58808 -8.96873  1.000 17.99631 ? 184 PRO   A O   1 
ATOM   1413 C CB  . PRO   A 1 184 ? 0.21071   -21.34729 -6.67453  1.000 15.07711 ? 184 PRO   A CB  1 
ATOM   1414 C CG  . PRO   A 1 184 ? -1.08517  -22.12718 -6.59630  1.000 18.63501 ? 184 PRO   A CG  1 
ATOM   1415 C CD  . PRO   A 1 184 ? -2.04976  -21.29197 -5.72405  1.000 16.44301 ? 184 PRO   A CD  1 
ATOM   1416 N N   . PHE   A 1 185 ? -1.71435  -18.74544 -8.16650  1.000 17.13710 ? 185 PHE   A N   1 
ATOM   1417 C CA  . PHE   A 1 185 ? -2.17674  -18.31663 -9.46419  1.000 16.19954 ? 185 PHE   A CA  1 
ATOM   1418 C C   . PHE   A 1 185 ? -1.55267  -16.97396 -9.83445  1.000 17.37690 ? 185 PHE   A C   1 
ATOM   1419 O O   . PHE   A 1 185 ? -1.17089  -16.16762 -8.97405  1.000 14.04115 ? 185 PHE   A O   1 
ATOM   1420 C CB  . PHE   A 1 185 ? -3.70771  -18.28478 -9.46988  1.000 16.26954 ? 185 PHE   A CB  1 
ATOM   1421 C CG  . PHE   A 1 185 ? -4.30362  -19.55631 -8.96946  1.000 15.93332 ? 185 PHE   A CG  1 
ATOM   1422 C CD1 . PHE   A 1 185 ? -4.08315  -20.73333 -9.66858  1.000 17.61867 ? 185 PHE   A CD1 1 
ATOM   1423 C CD2 . PHE   A 1 185 ? -5.01211  -19.59872 -7.79845  1.000 14.25562 ? 185 PHE   A CD2 1 
ATOM   1424 C CE1 . PHE   A 1 185 ? -4.58075  -21.94669 -9.23255  1.000 20.28011 ? 185 PHE   A CE1 1 
ATOM   1425 C CE2 . PHE   A 1 185 ? -5.52850  -20.82698 -7.33608  1.000 15.93689 ? 185 PHE   A CE2 1 
ATOM   1426 C CZ  . PHE   A 1 185 ? -5.30908  -21.97343 -8.03763  1.000 19.58909 ? 185 PHE   A CZ  1 
ATOM   1427 N N   . VAL   A 1 186 ? -1.38251  -16.78392 -11.13699 1.000 14.71807 ? 186 VAL   A N   1 
ATOM   1428 C CA  . VAL   A 1 186 ? -0.81914  -15.57546 -11.69888 1.000 20.40330 ? 186 VAL   A CA  1 
ATOM   1429 C C   . VAL   A 1 186 ? -1.76745  -15.11044 -12.79394 1.000 21.34649 ? 186 VAL   A C   1 
ATOM   1430 O O   . VAL   A 1 186 ? -2.54137  -15.89880 -13.34014 1.000 21.79542 ? 186 VAL   A O   1 
ATOM   1431 C CB  . VAL   A 1 186 ? 0.59241   -15.83798 -12.24440 1.000 21.51194 ? 186 VAL   A CB  1 
ATOM   1432 C CG1 . VAL   A 1 186 ? 1.52236   -16.16598 -11.09186 1.000 18.97066 ? 186 VAL   A CG1 1 
ATOM   1433 C CG2 . VAL   A 1 186 ? 0.54417   -16.97666 -13.22808 1.000 23.20488 ? 186 VAL   A CG2 1 
ATOM   1434 N N   . ASP   A 1 187 ? -1.71729  -13.81616 -13.11702 1.000 20.50996 ? 187 ASP   A N   1 
ATOM   1435 C CA  . ASP   A 1 187 ? -2.64578  -13.29076 -14.12559 1.000 22.86318 ? 187 ASP   A CA  1 
ATOM   1436 C C   . ASP   A 1 187 ? -1.99879  -13.32609 -15.51527 1.000 27.84208 ? 187 ASP   A C   1 
ATOM   1437 O O   . ASP   A 1 187 ? -1.64921  -12.30042 -16.10564 1.000 27.76295 ? 187 ASP   A O   1 
ATOM   1438 C CB  . ASP   A 1 187 ? -3.14937  -11.89579 -13.74628 1.000 20.18610 ? 187 ASP   A CB  1 
ATOM   1439 C CG  . ASP   A 1 187 ? -2.02701  -10.88342 -13.45461 1.000 22.62623 ? 187 ASP   A CG  1 
ATOM   1440 O OD1 . ASP   A 1 187 ? -0.84906  -11.29167 -13.36669 1.000 24.14493 ? 187 ASP   A OD1 1 
ATOM   1441 O OD2 . ASP   A 1 187 ? -2.33311  -9.67432  -13.28322 1.000 14.56469 ? 187 ASP   A OD2 1 
ATOM   1442 N N   . ARG   A 1 188 ? -1.84593  -14.56399 -16.02499 1.000 30.13770 ? 188 ARG   A N   1 
ATOM   1443 C CA  . ARG   A 1 188 ? -1.48901  -14.86969 -17.41163 1.000 37.26874 ? 188 ARG   A CA  1 
ATOM   1444 C C   . ARG   A 1 188 ? -2.49035  -15.88257 -17.94419 1.000 41.05015 ? 188 ARG   A C   1 
ATOM   1445 O O   . ARG   A 1 188 ? -3.17974  -16.55027 -17.17083 1.000 39.74042 ? 188 ARG   A O   1 
ATOM   1446 C CB  . ARG   A 1 188 ? -0.10004  -15.51338 -17.57836 1.000 37.16051 ? 188 ARG   A CB  1 
ATOM   1447 C CG  . ARG   A 1 188 ? 1.04170   -14.61565 -17.28812 1.000 39.85053 ? 188 ARG   A CG  1 
ATOM   1448 C CD  . ARG   A 1 188 ? 1.33519   -14.76594 -15.80910 1.000 36.21751 ? 188 ARG   A CD  1 
ATOM   1449 N NE  . ARG   A 1 188 ? 2.49678   -14.00091 -15.38113 1.000 42.85986 ? 188 ARG   A NE  1 
ATOM   1450 C CZ  . ARG   A 1 188 ? 2.37942   -12.79004 -14.83175 1.000 38.55358 ? 188 ARG   A CZ  1 
ATOM   1451 N NH1 . ARG   A 1 188 ? 1.16895   -12.25147 -14.67916 1.000 27.36627 ? 188 ARG   A NH1 1 
ATOM   1452 N NH2 . ARG   A 1 188 ? 3.46050   -12.11125 -14.44373 1.000 45.58424 ? 188 ARG   A NH2 1 
ATOM   1453 N N   . GLN   A 1 189 ? -2.54338  -16.04364 -19.27128 1.000 46.23793 ? 189 GLN   A N   1 
ATOM   1454 C CA  . GLN   A 1 189 ? -3.28628  -17.17329 -19.84191 1.000 49.39956 ? 189 GLN   A CA  1 
ATOM   1455 C C   . GLN   A 1 189 ? -2.28544  -18.28777 -20.11380 1.000 46.84390 ? 189 GLN   A C   1 
ATOM   1456 O O   . GLN   A 1 189 ? -1.83108  -18.51226 -21.23634 1.000 53.17290 ? 189 GLN   A O   1 
ATOM   1457 C CB  . GLN   A 1 189 ? -4.04954  -16.80679 -21.10826 1.000 54.78942 ? 189 GLN   A CB  1 
ATOM   1458 C CG  . GLN   A 1 189 ? -5.06667  -17.91171 -21.46492 1.000 57.29299 ? 189 GLN   A CG  1 
ATOM   1459 C CD  . GLN   A 1 189 ? -5.70399  -17.77862 -22.84927 1.000 67.40682 ? 189 GLN   A CD  1 
ATOM   1460 O OE1 . GLN   A 1 189 ? -6.06253  -16.68625 -23.29304 1.000 69.79635 ? 189 GLN   A OE1 1 
ATOM   1461 N NE2 . GLN   A 1 189 ? -5.83873  -18.91625 -23.54439 1.000 68.61996 ? 189 GLN   A NE2 1 
ATOM   1462 N N   . THR   A 1 190 ? -1.92627  -18.97735 -19.04379 1.000 42.44846 ? 190 THR   A N   1 
ATOM   1463 C CA  . THR   A 1 190 ? -1.11055  -20.17659 -19.09512 1.000 42.15902 ? 190 THR   A CA  1 
ATOM   1464 C C   . THR   A 1 190 ? -1.78576  -21.23785 -18.24431 1.000 37.52449 ? 190 THR   A C   1 
ATOM   1465 O O   . THR   A 1 190 ? -2.46588  -20.91595 -17.26495 1.000 39.27240 ? 190 THR   A O   1 
ATOM   1466 C CB  . THR   A 1 190 ? 0.31386   -19.91834 -18.57306 1.000 42.48563 ? 190 THR   A CB  1 
ATOM   1467 O OG1 . THR   A 1 190 ? 0.27487   -19.76016 -17.14578 1.000 41.95680 ? 190 THR   A OG1 1 
ATOM   1468 C CG2 . THR   A 1 190 ? 0.90698   -18.66513 -19.19879 1.000 44.25383 ? 190 THR   A CG2 1 
ATOM   1469 N N   . ALA   A 1 191 ? -1.60030  -22.50038 -18.62497 1.000 37.11149 ? 191 ALA   A N   1 
ATOM   1470 C CA  . ALA   A 1 191 ? -2.17519  -23.60517 -17.86879 1.000 33.64761 ? 191 ALA   A CA  1 
ATOM   1471 C C   . ALA   A 1 191 ? -1.87733  -23.45334 -16.38278 1.000 36.34435 ? 191 ALA   A C   1 
ATOM   1472 O O   . ALA   A 1 191 ? -0.71765  -23.35640 -15.97213 1.000 37.20190 ? 191 ALA   A O   1 
ATOM   1473 C CB  . ALA   A 1 191 ? -1.63063  -24.93478 -18.39186 1.000 33.05112 ? 191 ALA   A CB  1 
ATOM   1474 N N   . GLN   A 1 192 ? -2.93596  -23.36476 -15.59025 1.000 33.84835 ? 192 GLN   A N   1 
ATOM   1475 C CA  . GLN   A 1 192 ? -2.85445  -23.37574 -14.14087 1.000 34.04543 ? 192 GLN   A CA  1 
ATOM   1476 C C   . GLN   A 1 192 ? -3.97101  -24.26860 -13.62401 1.000 35.43957 ? 192 GLN   A C   1 
ATOM   1477 O O   . GLN   A 1 192 ? -5.05696  -24.33591 -14.21157 1.000 33.82791 ? 192 GLN   A O   1 
ATOM   1478 C CB  . GLN   A 1 192 ? -2.99331  -21.96511 -13.52843 1.000 30.78419 ? 192 GLN   A CB  1 
ATOM   1479 C CG  . GLN   A 1 192 ? -2.03589  -20.92218 -14.08690 1.000 33.76521 ? 192 GLN   A CG  1 
ATOM   1480 C CD  . GLN   A 1 192 ? -2.37007  -19.52418 -13.60251 1.000 29.76056 ? 192 GLN   A CD  1 
ATOM   1481 O OE1 . GLN   A 1 192 ? -2.27305  -19.22996 -12.41582 1.000 22.32315 ? 192 GLN   A OE1 1 
ATOM   1482 N NE2 . GLN   A 1 192 ? -2.76004  -18.65221 -14.52646 1.000 32.60892 ? 192 GLN   A NE2 1 
ATOM   1483 N N   . ALA   A 1 193 ? -3.71070  -24.94943 -12.51665 1.000 34.75319 ? 193 ALA   A N   1 
ATOM   1484 C CA  . ALA   A 1 193 ? -4.72337  -25.83295 -11.95897 1.000 35.21536 ? 193 ALA   A CA  1 
ATOM   1485 C C   . ALA   A 1 193 ? -4.77426  -25.67143 -10.44793 1.000 32.15926 ? 193 ALA   A C   1 
ATOM   1486 O O   . ALA   A 1 193 ? -3.76862  -25.35606 -9.79597  1.000 34.29163 ? 193 ALA   A O   1 
ATOM   1487 C CB  . ALA   A 1 193 ? -4.48197  -27.30464 -12.33821 1.000 31.75531 ? 193 ALA   A CB  1 
ATOM   1488 N N   . ALA   A 1 194 ? -5.96959  -25.92818 -9.90996  1.000 29.44994 ? 194 ALA   A N   1 
ATOM   1489 C CA  . ALA   A 1 194 ? -6.29822  -25.59084 -8.53165  1.000 28.12294 ? 194 ALA   A CA  1 
ATOM   1490 C C   . ALA   A 1 194 ? -5.45429  -26.35798 -7.52208  1.000 29.75826 ? 194 ALA   A C   1 
ATOM   1491 O O   . ALA   A 1 194 ? -5.09115  -25.80940 -6.47768  1.000 34.35922 ? 194 ALA   A O   1 
ATOM   1492 C CB  . ALA   A 1 194 ? -7.78404  -25.85994 -8.28003  1.000 26.88395 ? 194 ALA   A CB  1 
ATOM   1493 N N   . GLY   A 1 195 ? -5.14478  -27.60477 -7.78433  1.000 28.40992 ? 195 GLY   A N   1 
ATOM   1494 C CA  . GLY   A 1 195 ? -4.58147  -28.26282 -6.62043  1.000 29.55388 ? 195 GLY   A CA  1 
ATOM   1495 C C   . GLY   A 1 195 ? -5.66034  -28.86859 -5.75050  1.000 28.93151 ? 195 GLY   A C   1 
ATOM   1496 O O   . GLY   A 1 195 ? -6.77284  -28.35284 -5.62953  1.000 27.46147 ? 195 GLY   A O   1 
ATOM   1497 N N   . THR   A 1 196 ? -5.32567  -30.00484 -5.14675  1.000 29.58633 ? 196 THR   A N   1 
ATOM   1498 C CA  . THR   A 1 196 ? -6.31649  -30.81250 -4.44423  1.000 29.79979 ? 196 THR   A CA  1 
ATOM   1499 C C   . THR   A 1 196 ? -6.96681  -30.02438 -3.31647  1.000 26.68066 ? 196 THR   A C   1 
ATOM   1500 O O   . THR   A 1 196 ? -6.28737  -29.34423 -2.54367  1.000 28.88356 ? 196 THR   A O   1 
ATOM   1501 C CB  . THR   A 1 196 ? -5.64609  -32.06162 -3.89421  1.000 29.63404 ? 196 THR   A CB  1 
ATOM   1502 O OG1 . THR   A 1 196 ? -5.31296  -32.92145 -4.98974  1.000 35.87592 ? 196 THR   A OG1 1 
ATOM   1503 C CG2 . THR   A 1 196 ? -6.57138  -32.79338 -2.91641  1.000 31.16568 ? 196 THR   A CG2 1 
ATOM   1504 N N   . ASP   A 1 197 ? -8.28397  -30.08929 -3.23357  1.000 23.86921 ? 197 ASP   A N   1 
ATOM   1505 C CA  . ASP   A 1 197 ? -8.96874  -29.40100 -2.15250  1.000 24.57892 ? 197 ASP   A CA  1 
ATOM   1506 C C   . ASP   A 1 197 ? -9.25754  -30.35063 -0.99507  1.000 26.76567 ? 197 ASP   A C   1 
ATOM   1507 O O   . ASP   A 1 197 ? -9.19035  -31.57527 -1.12015  1.000 25.73227 ? 197 ASP   A O   1 
ATOM   1508 C CB  . ASP   A 1 197 ? -10.26870 -28.76272 -2.62752  1.000 23.61626 ? 197 ASP   A CB  1 
ATOM   1509 C CG  . ASP   A 1 197 ? -10.68318 -27.60629 -1.74452  1.000 22.03716 ? 197 ASP   A CG  1 
ATOM   1510 O OD1 . ASP   A 1 197 ? -9.85602  -27.15888 -0.91222  1.000 22.86795 ? 197 ASP   A OD1 1 
ATOM   1511 O OD2 . ASP   A 1 197 ? -11.81637 -27.13817 -1.88140  1.000 19.66211 ? 197 ASP   A OD2 1 
ATOM   1512 N N   . THR   A 1 198 ? -9.55673  -29.75209 0.15319   1.000 24.82992 ? 198 THR   A N   1 
ATOM   1513 C CA  . THR   A 1 198 ? -9.85550  -30.47608 1.37629   1.000 24.31218 ? 198 THR   A CA  1 
ATOM   1514 C C   . THR   A 1 198 ? -11.02173 -29.78201 2.05413   1.000 23.39512 ? 198 THR   A C   1 
ATOM   1515 O O   . THR   A 1 198 ? -11.32275 -28.60845 1.78264   1.000 20.14253 ? 198 THR   A O   1 
ATOM   1516 C CB  . THR   A 1 198 ? -8.63598  -30.54944 2.32078   1.000 25.60063 ? 198 THR   A CB  1 
ATOM   1517 O OG1 . THR   A 1 198 ? -8.27345  -29.22980 2.75860   1.000 23.12729 ? 198 THR   A OG1 1 
ATOM   1518 C CG2 . THR   A 1 198 ? -7.43817  -31.17207 1.59875   1.000 27.47950 ? 198 THR   A CG2 1 
ATOM   1519 N N   . THR   A 1 199 ? -11.68863 -30.52620 2.93103   1.000 22.79577 ? 199 THR   A N   1 
ATOM   1520 C CA  . THR   A 1 199 ? -12.85650 -30.01378 3.63250   1.000 22.27736 ? 199 THR   A CA  1 
ATOM   1521 C C   . THR   A 1 199 ? -12.43358 -29.25696 4.88944   1.000 21.08757 ? 199 THR   A C   1 
ATOM   1522 O O   . THR   A 1 199 ? -11.49570 -29.65779 5.58618   1.000 21.25958 ? 199 THR   A O   1 
ATOM   1523 C CB  . THR   A 1 199 ? -13.79678 -31.17023 3.96336   1.000 23.55352 ? 199 THR   A CB  1 
ATOM   1524 O OG1 . THR   A 1 199 ? -14.15941 -31.82705 2.73949   1.000 22.62390 ? 199 THR   A OG1 1 
ATOM   1525 C CG2 . THR   A 1 199 ? -15.04945 -30.67274 4.66986   1.000 22.30654 ? 199 THR   A CG2 1 
ATOM   1526 N N   . ILE   A 1 200 ? -13.09995 -28.13242 5.15824   1.000 16.55329 ? 200 ILE   A N   1 
ATOM   1527 C CA  . ILE   A 1 200 ? -12.68682 -27.29454 6.27864   1.000 18.16200 ? 200 ILE   A CA  1 
ATOM   1528 C C   . ILE   A 1 200 ? -13.27474 -27.84775 7.57181   1.000 19.19294 ? 200 ILE   A C   1 
ATOM   1529 O O   . ILE   A 1 200 ? -14.40642 -27.52838 7.93959   1.000 15.46147 ? 200 ILE   A O   1 
ATOM   1530 C CB  . ILE   A 1 200 ? -13.07930 -25.82452 6.06497   1.000 18.12656 ? 200 ILE   A CB  1 
ATOM   1531 C CG1 . ILE   A 1 200 ? -12.51975 -25.32046 4.73050   1.000 17.97453 ? 200 ILE   A CG1 1 
ATOM   1532 C CG2 . ILE   A 1 200 ? -12.58933 -24.95945 7.23521   1.000 16.25317 ? 200 ILE   A CG2 1 
ATOM   1533 C CD1 . ILE   A 1 200 ? -13.45905 -24.35172 4.00170   1.000 18.43096 ? 200 ILE   A CD1 1 
ATOM   1534 N N   . THR   A 1 201 ? -12.48776 -28.65648 8.29485   1.000 21.69584 ? 201 THR   A N   1 
ATOM   1535 C CA  . THR   A 1 201 ? -13.05879 -29.44604 9.38256   1.000 20.37668 ? 201 THR   A CA  1 
ATOM   1536 C C   . THR   A 1 201 ? -13.65832 -28.57313 10.47866  1.000 18.47951 ? 201 THR   A C   1 
ATOM   1537 O O   . THR   A 1 201 ? -14.74258 -28.87631 10.97957  1.000 19.75313 ? 201 THR   A O   1 
ATOM   1538 C CB  . THR   A 1 201 ? -12.01301 -30.38339 9.98154   1.000 24.04162 ? 201 THR   A CB  1 
ATOM   1539 O OG1 . THR   A 1 201 ? -11.25308 -31.00029 8.93241   1.000 24.08512 ? 201 THR   A OG1 1 
ATOM   1540 C CG2 . THR   A 1 201 ? -12.71926 -31.45579 10.79217  1.000 23.01265 ? 201 THR   A CG2 1 
ATOM   1541 N N   . VAL   A 1 202 ? -12.97474 -27.49730 10.88032  1.000 16.51217 ? 202 VAL   A N   1 
ATOM   1542 C CA  . VAL   A 1 202 ? -13.49466 -26.68630 11.98063  1.000 16.77996 ? 202 VAL   A CA  1 
ATOM   1543 C C   . VAL   A 1 202 ? -14.88474 -26.15654 11.63561  1.000 15.61516 ? 202 VAL   A C   1 
ATOM   1544 O O   . VAL   A 1 202 ? -15.76192 -26.06888 12.50552  1.000 16.10279 ? 202 VAL   A O   1 
ATOM   1545 C CB  . VAL   A 1 202 ? -12.51643 -25.55065 12.33938  1.000 16.90077 ? 202 VAL   A CB  1 
ATOM   1546 C CG1 . VAL   A 1 202 ? -12.20452 -24.67692 11.13473  1.000 16.94702 ? 202 VAL   A CG1 1 
ATOM   1547 C CG2 . VAL   A 1 202 ? -13.03519 -24.72407 13.51234  1.000 19.22387 ? 202 VAL   A CG2 1 
ATOM   1548 N N   . ASN   A 1 203 ? -15.10581 -25.83799 10.35297  1.000 15.07664 ? 203 ASN   A N   1 
ATOM   1549 C CA  . ASN   A 1 203 ? -16.38557 -25.31005 9.88295   1.000 15.51632 ? 203 ASN   A CA  1 
ATOM   1550 C C   . ASN   A 1 203 ? -17.49444 -26.35939 9.95105   1.000 16.54904 ? 203 ASN   A C   1 
ATOM   1551 O O   . ASN   A 1 203 ? -18.63059 -26.04067 10.32293  1.000 16.92677 ? 203 ASN   A O   1 
ATOM   1552 C CB  . ASN   A 1 203 ? -16.23249 -24.79979 8.45476   1.000 13.41301 ? 203 ASN   A CB  1 
ATOM   1553 C CG  . ASN   A 1 203 ? -15.49122 -23.45745 8.37434   1.000 15.54508 ? 203 ASN   A CG  1 
ATOM   1554 O OD1 . ASN   A 1 203 ? -15.04657 -22.89600 9.38451   1.000 18.11453 ? 203 ASN   A OD1 1 
ATOM   1555 N ND2 . ASN   A 1 203 ? -15.34735 -22.95447 7.17373   1.000 15.48370 ? 203 ASN   A ND2 1 
ATOM   1556 N N   . VAL   A 1 204 ? -17.20435 -27.59628 9.53022   1.000 18.14377 ? 204 VAL   A N   1 
ATOM   1557 C CA  . VAL   A 1 204 ? -18.14937 -28.70066 9.70514   1.000 17.06038 ? 204 VAL   A CA  1 
ATOM   1558 C C   . VAL   A 1 204 ? -18.57004 -28.80364 11.16140  1.000 17.31584 ? 204 VAL   A C   1 
ATOM   1559 O O   . VAL   A 1 204 ? -19.76243 -28.84732 11.48574  1.000 17.86171 ? 204 VAL   A O   1 
ATOM   1560 C CB  . VAL   A 1 204 ? -17.53190 -30.02860 9.23260   1.000 17.45652 ? 204 VAL   A CB  1 
ATOM   1561 C CG1 . VAL   A 1 204 ? -18.48947 -31.18209 9.52139   1.000 19.08881 ? 204 VAL   A CG1 1 
ATOM   1562 C CG2 . VAL   A 1 204 ? -17.17724 -29.96818 7.76870   1.000 16.70698 ? 204 VAL   A CG2 1 
ATOM   1563 N N   . LEU   A 1 205 ? -17.58487 -28.87343 12.05919  1.000 17.46544 ? 205 LEU   A N   1 
ATOM   1564 C CA  . LEU   A 1 205 ? -17.87357 -28.93514 13.48612  1.000 18.96345 ? 205 LEU   A CA  1 
ATOM   1565 C C   . LEU   A 1 205 ? -18.77740 -27.78496 13.90928  1.000 18.26441 ? 205 LEU   A C   1 
ATOM   1566 O O   . LEU   A 1 205 ? -19.72642 -27.97666 14.67537  1.000 19.15417 ? 205 LEU   A O   1 
ATOM   1567 C CB  . LEU   A 1 205 ? -16.56059 -28.92330 14.28769  1.000 20.22367 ? 205 LEU   A CB  1 
ATOM   1568 C CG  . LEU   A 1 205 ? -15.70564 -30.19140 14.19412  1.000 21.64729 ? 205 LEU   A CG  1 
ATOM   1569 C CD1 . LEU   A 1 205 ? -14.41785 -30.07028 15.02925  1.000 23.09610 ? 205 LEU   A CD1 1 
ATOM   1570 C CD2 . LEU   A 1 205 ? -16.49960 -31.40861 14.65811  1.000 23.25015 ? 205 LEU   A CD2 1 
ATOM   1571 N N   . ALA   A 1 206 ? -18.49428 -26.58358 13.40486  1.000 16.82716 ? 206 ALA   A N   1 
ATOM   1572 C CA  . ALA   A 1 206 ? -19.27493 -25.40722 13.76241  1.000 18.29209 ? 206 ALA   A CA  1 
ATOM   1573 C C   . ALA   A 1 206 ? -20.71648 -25.52991 13.27490  1.000 17.32776 ? 206 ALA   A C   1 
ATOM   1574 O O   . ALA   A 1 206 ? -21.64880 -25.07286 13.94306  1.000 17.25178 ? 206 ALA   A O   1 
ATOM   1575 C CB  . ALA   A 1 206 ? -18.60547 -24.16372 13.17348  1.000 16.18407 ? 206 ALA   A CB  1 
ATOM   1576 N N   . TRP   A 1 207 ? -20.91499 -26.14409 12.10844  1.000 17.18556 ? 207 TRP   A N   1 
ATOM   1577 C CA  . TRP   A 1 207 ? -22.25195 -26.31022 11.53862  1.000 17.08195 ? 207 TRP   A CA  1 
ATOM   1578 C C   . TRP   A 1 207 ? -23.03991 -27.41674 12.24950  1.000 16.88049 ? 207 TRP   A C   1 
ATOM   1579 O O   . TRP   A 1 207 ? -24.26728 -27.32042 12.36595  1.000 18.06869 ? 207 TRP   A O   1 
ATOM   1580 C CB  . TRP   A 1 207 ? -22.10615 -26.56824 10.03425  1.000 15.63122 ? 207 TRP   A CB  1 
ATOM   1581 C CG  . TRP   A 1 207 ? -23.30680 -27.05283 9.23965   1.000 15.33405 ? 207 TRP   A CG  1 
ATOM   1582 C CD1 . TRP   A 1 207 ? -24.32566 -26.29430 8.70603   1.000 17.96037 ? 207 TRP   A CD1 1 
ATOM   1583 C CD2 . TRP   A 1 207 ? -23.56712 -28.40314 8.83615   1.000 16.47650 ? 207 TRP   A CD2 1 
ATOM   1584 N NE1 . TRP   A 1 207 ? -25.20971 -27.10861 8.01273   1.000 13.88268 ? 207 TRP   A NE1 1 
ATOM   1585 C CE2 . TRP   A 1 207 ? -24.75688 -28.40006 8.07821   1.000 14.99420 ? 207 TRP   A CE2 1 
ATOM   1586 C CE3 . TRP   A 1 207 ? -22.91074 -29.61717 9.04987   1.000 17.02806 ? 207 TRP   A CE3 1 
ATOM   1587 C CZ2 . TRP   A 1 207 ? -25.28745 -29.55715 7.53925   1.000 18.46306 ? 207 TRP   A CZ2 1 
ATOM   1588 C CZ3 . TRP   A 1 207 ? -23.43962 -30.76009 8.51459   1.000 17.53985 ? 207 TRP   A CZ3 1 
ATOM   1589 C CH2 . TRP   A 1 207 ? -24.61846 -30.72739 7.76728   1.000 18.81039 ? 207 TRP   A CH2 1 
ATOM   1590 N N   . LEU   A 1 208 ? -22.36511 -28.45396 12.75374  1.000 17.69206 ? 208 LEU   A N   1 
ATOM   1591 C CA  . LEU   A 1 208 ? -23.05066 -29.42360 13.60954  1.000 20.72752 ? 208 LEU   A CA  1 
ATOM   1592 C C   . LEU   A 1 208 ? -23.55866 -28.75780 14.88741  1.000 22.05769 ? 208 LEU   A C   1 
ATOM   1593 O O   . LEU   A 1 208 ? -24.68093 -29.02521 15.32957  1.000 23.86184 ? 208 LEU   A O   1 
ATOM   1594 C CB  . LEU   A 1 208 ? -22.11794 -30.59602 13.93902  1.000 22.20021 ? 208 LEU   A CB  1 
ATOM   1595 C CG  . LEU   A 1 208 ? -21.68523 -31.40172 12.70402  1.000 21.65427 ? 208 LEU   A CG  1 
ATOM   1596 C CD1 . LEU   A 1 208 ? -20.56711 -32.40467 13.01895  1.000 21.68398 ? 208 LEU   A CD1 1 
ATOM   1597 C CD2 . LEU   A 1 208 ? -22.88931 -32.08982 12.01256  1.000 22.39104 ? 208 LEU   A CD2 1 
ATOM   1598 N N   . TYR   A 1 209 ? -22.75077 -27.86984 15.48465  1.000 20.46175 ? 209 TYR   A N   1 
ATOM   1599 C CA  . TYR   A 1 209 ? -23.22657 -27.07390 16.61338  1.000 21.07123 ? 209 TYR   A CA  1 
ATOM   1600 C C   . TYR   A 1 209 ? -24.42082 -26.21775 16.22250  1.000 22.80585 ? 209 TYR   A C   1 
ATOM   1601 O O   . TYR   A 1 209 ? -25.36472 -26.06487 17.00717  1.000 20.57931 ? 209 TYR   A O   1 
ATOM   1602 C CB  . TYR   A 1 209 ? -22.10532 -26.19387 17.15018  1.000 21.07040 ? 209 TYR   A CB  1 
ATOM   1603 C CG  . TYR   A 1 209 ? -21.13139 -26.93806 18.02851  1.000 22.52726 ? 209 TYR   A CG  1 
ATOM   1604 C CD1 . TYR   A 1 209 ? -21.51959 -27.43127 19.26895  1.000 24.70249 ? 209 TYR   A CD1 1 
ATOM   1605 C CD2 . TYR   A 1 209 ? -19.82121 -27.15640 17.60856  1.000 22.69629 ? 209 TYR   A CD2 1 
ATOM   1606 C CE1 . TYR   A 1 209 ? -20.62187 -28.12528 20.06921  1.000 28.46513 ? 209 TYR   A CE1 1 
ATOM   1607 C CE2 . TYR   A 1 209 ? -18.92607 -27.85088 18.39134  1.000 24.17358 ? 209 TYR   A CE2 1 
ATOM   1608 C CZ  . TYR   A 1 209 ? -19.32974 -28.32814 19.62050  1.000 26.38399 ? 209 TYR   A CZ  1 
ATOM   1609 O OH  . TYR   A 1 209 ? -18.43924 -29.00635 20.40506  1.000 29.10690 ? 209 TYR   A OH  1 
ATOM   1610 N N   . ALA   A 1 210 ? -24.37758 -25.61480 15.02815  1.000 20.61863 ? 210 ALA   A N   1 
ATOM   1611 C CA  . ALA   A 1 210 ? -25.55558 -24.92220 14.51883  1.000 20.85130 ? 210 ALA   A CA  1 
ATOM   1612 C C   . ALA   A 1 210 ? -26.76032 -25.85616 14.47787  1.000 23.46493 ? 210 ALA   A C   1 
ATOM   1613 O O   . ALA   A 1 210 ? -27.86568 -25.48188 14.87752  1.000 21.85892 ? 210 ALA   A O   1 
ATOM   1614 C CB  . ALA   A 1 210 ? -25.26751 -24.36087 13.13557  1.000 18.50667 ? 210 ALA   A CB  1 
ATOM   1615 N N   . ALA   A 1 211 ? -26.55538 -27.08687 14.01719  1.000 24.00065 ? 211 ALA   A N   1 
ATOM   1616 C CA  . ALA   A 1 211 ? -27.63831 -28.05726 13.98031  1.000 23.61450 ? 211 ALA   A CA  1 
ATOM   1617 C C   . ALA   A 1 211 ? -28.20317 -28.31067 15.37363  1.000 27.71541 ? 211 ALA   A C   1 
ATOM   1618 O O   . ALA   A 1 211 ? -29.42584 -28.35867 15.56065  1.000 27.95820 ? 211 ALA   A O   1 
ATOM   1619 C CB  . ALA   A 1 211 ? -27.12696 -29.35509 13.35804  1.000 25.56872 ? 211 ALA   A CB  1 
ATOM   1620 N N   . VAL   A 1 212 ? -27.32874 -28.47708 16.36668  1.000 25.02730 ? 212 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 212 ? -27.80648 -28.73967 17.71877  1.000 27.85747 ? 212 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 212 ? -28.52892 -27.51843 18.27458  1.000 26.11329 ? 212 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 212 ? -29.55377 -27.64867 18.95785  1.000 26.00755 ? 212 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 212 ? -26.64575 -29.19264 18.63344  1.000 25.84010 ? 212 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 212 ? -27.15930 -29.41829 20.06062  1.000 27.88488 ? 212 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 212 ? -26.00911 -30.47448 18.09531  1.000 25.69484 ? 212 VAL   A CG2 1 
ATOM   1627 N N   . ILE   A 1 213 ? -28.01261 -26.31368 17.99347  1.000 22.94449 ? 213 ILE   A N   1 
ATOM   1628 C CA  . ILE   A 1 213 ? -28.65744 -25.09949 18.49348  1.000 24.37993 ? 213 ILE   A CA  1 
ATOM   1629 C C   . ILE   A 1 213 ? -30.07023 -24.98771 17.92591  1.000 26.85693 ? 213 ILE   A C   1 
ATOM   1630 O O   . ILE   A 1 213 ? -30.98143 -24.47271 18.58955  1.000 24.66567 ? 213 ILE   A O   1 
ATOM   1631 C CB  . ILE   A 1 213 ? -27.79885 -23.85675 18.16623  1.000 22.58862 ? 213 ILE   A CB  1 
ATOM   1632 C CG1 . ILE   A 1 213 ? -26.51843 -23.84768 19.01032  1.000 27.33178 ? 213 ILE   A CG1 1 
ATOM   1633 C CG2 . ILE   A 1 213 ? -28.58034 -22.57152 18.38291  1.000 27.16561 ? 213 ILE   A CG2 1 
ATOM   1634 C CD1 . ILE   A 1 213 ? -25.44182 -22.88044 18.52075  1.000 20.97468 ? 213 ILE   A CD1 1 
ATOM   1635 N N   . ASN   A 1 214 ? -30.29068 -25.53316 16.72999  1.000 26.48639 ? 214 ASN   A N   1 
ATOM   1636 C CA  . ASN   A 1 214 ? -31.57996 -25.45932 16.05288  1.000 30.11377 ? 214 ASN   A CA  1 
ATOM   1637 C C   . ASN   A 1 214 ? -32.47574 -26.68563 16.27018  1.000 30.95521 ? 214 ASN   A C   1 
ATOM   1638 O O   . ASN   A 1 214 ? -33.60203 -26.70155 15.76416  1.000 32.49836 ? 214 ASN   A O   1 
ATOM   1639 C CB  . ASN   A 1 214 ? -31.35040 -25.22170 14.55894  1.000 24.99196 ? 214 ASN   A CB  1 
ATOM   1640 C CG  . ASN   A 1 214 ? -31.10607 -23.75026 14.23874  1.000 26.53219 ? 214 ASN   A CG  1 
ATOM   1641 O OD1 . ASN   A 1 214 ? -32.05108 -23.00909 13.96918  1.000 29.33629 ? 214 ASN   A OD1 1 
ATOM   1642 N ND2 . ASN   A 1 214 ? -29.83953 -23.31716 14.28087  1.000 24.19305 ? 214 ASN   A ND2 1 
ATOM   1643 N N   . GLY   A 1 215 ? -32.02286 -27.71067 16.99438  1.000 31.39585 ? 215 GLY   A N   1 
ATOM   1644 C CA  . GLY   A 1 215 ? -32.88864 -28.82932 17.34175  1.000 31.11358 ? 215 GLY   A CA  1 
ATOM   1645 C C   . GLY   A 1 215 ? -32.52564 -30.18215 16.75522  1.000 34.58512 ? 215 GLY   A C   1 
ATOM   1646 O O   . GLY   A 1 215 ? -33.12928 -31.18347 17.16319  1.000 38.08272 ? 215 GLY   A O   1 
ATOM   1647 N N   . ASP   A 1 216 ? -31.61233 -30.27884 15.79338  1.000 33.50416 ? 216 ASP   A N   1 
ATOM   1648 C CA  . ASP   A 1 216 ? -31.10860 -31.58032 15.35101  1.000 37.82218 ? 216 ASP   A CA  1 
ATOM   1649 C C   . ASP   A 1 216 ? -30.18344 -32.16950 16.41949  1.000 35.91297 ? 216 ASP   A C   1 
ATOM   1650 O O   . ASP   A 1 216 ? -29.20676 -31.53034 16.81704  1.000 32.89412 ? 216 ASP   A O   1 
ATOM   1651 C CB  . ASP   A 1 216 ? -30.33367 -31.45495 14.03476  1.000 37.51756 ? 216 ASP   A CB  1 
ATOM   1652 C CG  . ASP   A 1 216 ? -31.19831 -31.65463 12.79995  1.000 40.97161 ? 216 ASP   A CG  1 
ATOM   1653 O OD1 . ASP   A 1 216 ? -31.24955 -30.72891 11.93111  1.000 37.00401 ? 216 ASP   A OD1 1 
ATOM   1654 O OD2 . ASP   A 1 216 ? -31.80871 -32.74268 12.70499  1.000 40.13253 ? 216 ASP   A OD2 1 
ATOM   1655 N N   . ARG   A 1 217 ? -30.47024 -33.38994 16.87925  1.000 36.69971 ? 217 ARG   A N   1 
ATOM   1656 C CA  . ARG   A 1 217 ? -29.55357 -34.07886 17.77860  1.000 35.66830 ? 217 ARG   A CA  1 
ATOM   1657 C C   . ARG   A 1 217 ? -29.24795 -35.50813 17.33889  1.000 34.31339 ? 217 ARG   A C   1 
ATOM   1658 O O   . ARG   A 1 217 ? -28.55250 -36.22373 18.06857  1.000 33.72601 ? 217 ARG   A O   1 
ATOM   1659 C CB  . ARG   A 1 217 ? -30.10271 -34.09274 19.21714  1.000 37.12839 ? 217 ARG   A CB  1 
ATOM   1660 C CG  . ARG   A 1 217 ? -29.68853 -32.89920 20.08938  1.000 36.05082 ? 217 ARG   A CG  1 
ATOM   1661 C CD  . ARG   A 1 217 ? -30.24333 -32.98825 21.52690  1.000 35.10444 ? 217 ARG   A CD  1 
ATOM   1662 N NE  . ARG   A 1 217 ? -29.30608 -33.64444 22.43911  1.000 36.89473 ? 217 ARG   A NE  1 
ATOM   1663 C CZ  . ARG   A 1 217 ? -28.43044 -32.99651 23.20399  1.000 39.02308 ? 217 ARG   A CZ  1 
ATOM   1664 N NH1 . ARG   A 1 217 ? -28.38029 -31.66897 23.16894  1.000 42.15306 ? 217 ARG   A NH1 1 
ATOM   1665 N NH2 . ARG   A 1 217 ? -27.60076 -33.66815 23.99653  1.000 39.03897 ? 217 ARG   A NH2 1 
ATOM   1666 N N   . TRP   A 1 218 ? -29.73241 -35.94330 16.16829  1.000 32.56709 ? 218 TRP   A N   1 
ATOM   1667 C CA  . TRP   A 1 218 ? -29.76787 -37.37504 15.87535  1.000 33.70740 ? 218 TRP   A CA  1 
ATOM   1668 C C   . TRP   A 1 218 ? -28.38739 -37.98508 15.68553  1.000 34.53345 ? 218 TRP   A C   1 
ATOM   1669 O O   . TRP   A 1 218 ? -28.24130 -39.20303 15.84067  1.000 36.11558 ? 218 TRP   A O   1 
ATOM   1670 C CB  . TRP   A 1 218 ? -30.61051 -37.65726 14.63282  1.000 33.52956 ? 218 TRP   A CB  1 
ATOM   1671 C CG  . TRP   A 1 218 ? -30.08256 -37.10454 13.30468  1.000 36.01055 ? 218 TRP   A CG  1 
ATOM   1672 C CD1 . TRP   A 1 218 ? -30.50635 -35.97298 12.66688  1.000 35.30935 ? 218 TRP   A CD1 1 
ATOM   1673 C CD2 . TRP   A 1 218 ? -29.07592 -37.68396 12.45165  1.000 34.65249 ? 218 TRP   A CD2 1 
ATOM   1674 N NE1 . TRP   A 1 218 ? -29.82250 -35.80399 11.48645  1.000 34.08960 ? 218 TRP   A NE1 1 
ATOM   1675 C CE2 . TRP   A 1 218 ? -28.94275 -36.84147 11.32894  1.000 35.35667 ? 218 TRP   A CE2 1 
ATOM   1676 C CE3 . TRP   A 1 218 ? -28.27247 -38.82825 12.53092  1.000 36.90831 ? 218 TRP   A CE3 1 
ATOM   1677 C CZ2 . TRP   A 1 218 ? -28.03924 -37.10793 10.29765  1.000 35.42609 ? 218 TRP   A CZ2 1 
ATOM   1678 C CZ3 . TRP   A 1 218 ? -27.37423 -39.08680 11.50691  1.000 33.61542 ? 218 TRP   A CZ3 1 
ATOM   1679 C CH2 . TRP   A 1 218 ? -27.26423 -38.23379 10.40885  1.000 32.89762 ? 218 TRP   A CH2 1 
ATOM   1680 N N   . PHE   A 1 219 ? -27.38614 -37.17598 15.34912  1.000 32.21908 ? 219 PHE   A N   1 
ATOM   1681 C CA  . PHE   A 1 219 ? -26.05924 -37.64822 14.98314  1.000 31.86536 ? 219 PHE   A CA  1 
ATOM   1682 C C   . PHE   A 1 219 ? -25.10727 -37.71103 16.16524  1.000 32.91095 ? 219 PHE   A C   1 
ATOM   1683 O O   . PHE   A 1 219 ? -23.97287 -38.16652 16.00265  1.000 33.35653 ? 219 PHE   A O   1 
ATOM   1684 C CB  . PHE   A 1 219 ? -25.46740 -36.73012 13.91181  1.000 29.31692 ? 219 PHE   A CB  1 
ATOM   1685 C CG  . PHE   A 1 219 ? -25.64541 -35.27158 14.22101  1.000 29.87669 ? 219 PHE   A CG  1 
ATOM   1686 C CD1 . PHE   A 1 219 ? -24.76993 -34.61295 15.07444  1.000 27.08426 ? 219 PHE   A CD1 1 
ATOM   1687 C CD2 . PHE   A 1 219 ? -26.71860 -34.56973 13.69873  1.000 29.93230 ? 219 PHE   A CD2 1 
ATOM   1688 C CE1 . PHE   A 1 219 ? -24.94004 -33.27231 15.37688  1.000 26.86798 ? 219 PHE   A CE1 1 
ATOM   1689 C CE2 . PHE   A 1 219 ? -26.90522 -33.22346 13.99555  1.000 28.88502 ? 219 PHE   A CE2 1 
ATOM   1690 C CZ  . PHE   A 1 219 ? -26.01813 -32.57488 14.83240  1.000 27.73403 ? 219 PHE   A CZ  1 
ATOM   1691 N N   . LEU   A 1 220 ? -25.52007 -37.23869 17.33472  1.000 33.49750 ? 220 LEU   A N   1 
ATOM   1692 C CA  . LEU   A 1 220 ? -24.63651 -37.26355 18.48537  1.000 34.79687 ? 220 LEU   A CA  1 
ATOM   1693 C C   . LEU   A 1 220 ? -24.48508 -38.69370 19.00631  1.000 37.87461 ? 220 LEU   A C   1 
ATOM   1694 O O   . LEU   A 1 220 ? -25.26353 -39.59370 18.67608  1.000 39.15333 ? 220 LEU   A O   1 
ATOM   1695 C CB  . LEU   A 1 220 ? -25.16905 -36.34107 19.58239  1.000 34.90038 ? 220 LEU   A CB  1 
ATOM   1696 C CG  . LEU   A 1 220 ? -25.33693 -34.86665 19.20963  1.000 33.48103 ? 220 LEU   A CG  1 
ATOM   1697 C CD1 . LEU   A 1 220 ? -26.07781 -34.11122 20.30565  1.000 36.98424 ? 220 LEU   A CD1 1 
ATOM   1698 C CD2 . LEU   A 1 220 ? -23.99862 -34.19778 18.91353  1.000 30.89133 ? 220 LEU   A CD2 1 
ATOM   1699 N N   . ASN   A 1 221 ? -23.45551 -38.90646 19.82122  1.000 39.30111 ? 221 ASN   A N   1 
ATOM   1700 C CA  . ASN   A 1 221 ? -23.25347 -40.20890 20.43358  1.000 42.55051 ? 221 ASN   A CA  1 
ATOM   1701 C C   . ASN   A 1 221 ? -22.73062 -40.01799 21.85142  1.000 44.44370 ? 221 ASN   A C   1 
ATOM   1702 O O   . ASN   A 1 221 ? -22.46451 -38.89834 22.30091  1.000 43.32082 ? 221 ASN   A O   1 
ATOM   1703 C CB  . ASN   A 1 221 ? -22.31003 -41.09161 19.59549  1.000 44.98740 ? 221 ASN   A CB  1 
ATOM   1704 C CG  . ASN   A 1 221 ? -20.99502 -40.39949 19.24813  1.000 44.54921 ? 221 ASN   A CG  1 
ATOM   1705 O OD1 . ASN   A 1 221 ? -20.24940 -39.98902 20.13140  1.000 44.90749 ? 221 ASN   A OD1 1 
ATOM   1706 N ND2 . ASN   A 1 221 ? -20.69398 -40.30151 17.95768  1.000 44.16343 ? 221 ASN   A ND2 1 
ATOM   1707 N N   . ARG   A 1 222 ? -22.60772 -41.13336 22.56637  1.000 47.69932 ? 222 ARG   A N   1 
ATOM   1708 C CA  . ARG   A 1 222 ? -22.00415 -41.11457 23.88967  1.000 50.15152 ? 222 ARG   A CA  1 
ATOM   1709 C C   . ARG   A 1 222 ? -20.48412 -41.13716 23.80516  1.000 52.06786 ? 222 ARG   A C   1 
ATOM   1710 O O   . ARG   A 1 222 ? -19.80720 -40.64217 24.71229  1.000 53.85203 ? 222 ARG   A O   1 
ATOM   1711 C CB  . ARG   A 1 222 ? -22.50925 -42.30505 24.71139  1.000 53.81217 ? 222 ARG   A CB  1 
ATOM   1712 C CG  . ARG   A 1 222 ? -21.68137 -43.57944 24.50063  1.000 56.38458 ? 222 ARG   A CG  1 
ATOM   1713 C CD  . ARG   A 1 222 ? -22.38961 -44.83735 24.99135  1.000 59.60383 ? 222 ARG   A CD  1 
ATOM   1714 N NE  . ARG   A 1 222 ? -21.53023 -46.02254 24.93266  1.000 63.67634 ? 222 ARG   A NE  1 
ATOM   1715 C CZ  . ARG   A 1 222 ? -20.39306 -46.18563 25.61038  1.000 70.98384 ? 222 ARG   A CZ  1 
ATOM   1716 N NH1 . ARG   A 1 222 ? -19.94359 -45.24873 26.44044  1.000 70.94215 ? 222 ARG   A NH1 1 
ATOM   1717 N NH2 . ARG   A 1 222 ? -19.70477 -47.30796 25.46967  1.000 70.85071 ? 222 ARG   A NH2 1 
ATOM   1718 N N   . PHE   A 1 223 ? -19.93723 -41.67733 22.71802  1.000 53.69346 ? 223 PHE   A N   1 
ATOM   1719 C CA  . PHE   A 1 223 ? -18.50160 -41.86548 22.60023  1.000 53.05775 ? 223 PHE   A CA  1 
ATOM   1720 C C   . PHE   A 1 223 ? -17.76771 -40.53244 22.62672  1.000 49.60521 ? 223 PHE   A C   1 
ATOM   1721 O O   . PHE   A 1 223 ? -18.35174 -39.45854 22.45919  1.000 47.76192 ? 223 PHE   A O   1 
ATOM   1722 C CB  . PHE   A 1 223 ? -18.16075 -42.60999 21.30939  1.000 51.82879 ? 223 PHE   A CB  1 
ATOM   1723 C CG  . PHE   A 1 223 ? -18.83207 -43.94120 21.18837  1.000 56.23889 ? 223 PHE   A CG  1 
ATOM   1724 C CD1 . PHE   A 1 223 ? -18.42914 -45.00407 21.98462  1.000 60.37429 ? 223 PHE   A CD1 1 
ATOM   1725 C CD2 . PHE   A 1 223 ? -19.85386 -44.14026 20.27326  1.000 58.61846 ? 223 PHE   A CD2 1 
ATOM   1726 C CE1 . PHE   A 1 223 ? -19.03839 -46.24455 21.88342  1.000 64.85895 ? 223 PHE   A CE1 1 
ATOM   1727 C CE2 . PHE   A 1 223 ? -20.47212 -45.37900 20.16416  1.000 62.89747 ? 223 PHE   A CE2 1 
ATOM   1728 C CZ  . PHE   A 1 223 ? -20.06075 -46.43432 20.97093  1.000 65.95280 ? 223 PHE   A CZ  1 
ATOM   1729 N N   . THR   A 1 224 ? -16.46401 -40.61574 22.85661  1.000 49.67826 ? 224 THR   A N   1 
ATOM   1730 C CA  . THR   A 1 224 ? -15.60747 -39.46686 22.63164  1.000 48.03250 ? 224 THR   A CA  1 
ATOM   1731 C C   . THR   A 1 224 ? -14.35040 -39.94432 21.91805  1.000 48.20225 ? 224 THR   A C   1 
ATOM   1732 O O   . THR   A 1 224 ? -14.25006 -41.11625 21.53853  1.000 49.70601 ? 224 THR   A O   1 
ATOM   1733 C CB  . THR   A 1 224 ? -15.27534 -38.75974 23.94373  1.000 49.17067 ? 224 THR   A CB  1 
ATOM   1734 O OG1 . THR   A 1 224 ? -14.56484 -37.54757 23.65582  1.000 47.06605 ? 224 THR   A OG1 1 
ATOM   1735 C CG2 . THR   A 1 224 ? -14.42004 -39.65681 24.83332  1.000 53.13037 ? 224 THR   A CG2 1 
ATOM   1736 N N   . THR   A 1 225 ? -13.39153 -39.05060 21.72200  1.000 48.32574 ? 225 THR   A N   1 
ATOM   1737 C CA  . THR   A 1 225 ? -12.17769 -39.40422 21.00758  1.000 47.09268 ? 225 THR   A CA  1 
ATOM   1738 C C   . THR   A 1 225 ? -11.12205 -38.38722 21.39014  1.000 46.83393 ? 225 THR   A C   1 
ATOM   1739 O O   . THR   A 1 225 ? -11.45137 -37.28886 21.83584  1.000 45.51058 ? 225 THR   A O   1 
ATOM   1740 C CB  . THR   A 1 225 ? -12.41708 -39.42777 19.48929  1.000 44.38601 ? 225 THR   A CB  1 
ATOM   1741 O OG1 . THR   A 1 225 ? -11.19069 -39.67589 18.80188  1.000 44.73888 ? 225 THR   A OG1 1 
ATOM   1742 C CG2 . THR   A 1 225 ? -12.98397 -38.11232 19.02652  1.000 40.86300 ? 225 THR   A CG2 1 
ATOM   1743 N N   . THR   A 1 226 ? -9.85297  -38.77513 21.26435  1.000 51.20906 ? 226 THR   A N   1 
ATOM   1744 C CA  . THR   A 1 226 ? -8.77764  -37.80971 21.42301  1.000 48.07683 ? 226 THR   A CA  1 
ATOM   1745 C C   . THR   A 1 226 ? -8.56635  -37.03264 20.12376  1.000 44.68544 ? 226 THR   A C   1 
ATOM   1746 O O   . THR   A 1 226 ? -9.10075  -37.37252 19.06288  1.000 42.84019 ? 226 THR   A O   1 
ATOM   1747 C CB  . THR   A 1 226 ? -7.47920  -38.50099 21.85632  1.000 51.67892 ? 226 THR   A CB  1 
ATOM   1748 O OG1 . THR   A 1 226 ? -7.10129  -39.48406 20.87447  1.000 51.88784 ? 226 THR   A OG1 1 
ATOM   1749 C CG2 . THR   A 1 226 ? -7.61797  -39.14489 23.24466  1.000 55.25191 ? 226 THR   A CG2 1 
ATOM   1750 N N   . LEU   A 1 227 ? -7.76285  -35.97050 20.22267  1.000 44.89715 ? 227 LEU   A N   1 
ATOM   1751 C CA  . LEU   A 1 227 ? -7.47531  -35.14814 19.05251  1.000 45.54714 ? 227 LEU   A CA  1 
ATOM   1752 C C   . LEU   A 1 227 ? -6.63484  -35.90586 18.03344  1.000 43.26668 ? 227 LEU   A C   1 
ATOM   1753 O O   . LEU   A 1 227 ? -6.91492  -35.84894 16.83165  1.000 41.84845 ? 227 LEU   A O   1 
ATOM   1754 C CB  . LEU   A 1 227 ? -6.77965  -33.85462 19.47195  1.000 42.04777 ? 227 LEU   A CB  1 
ATOM   1755 C CG  . LEU   A 1 227 ? -6.66723  -32.77863 18.39337  1.000 40.70577 ? 227 LEU   A CG  1 
ATOM   1756 C CD1 . LEU   A 1 227 ? -7.99817  -32.61111 17.68018  1.000 38.54722 ? 227 LEU   A CD1 1 
ATOM   1757 C CD2 . LEU   A 1 227 ? -6.22107  -31.46467 18.99930  1.000 37.04015 ? 227 LEU   A CD2 1 
ATOM   1758 N N   . ASN   A 1 228 ? -5.59958  -36.61223 18.48823  1.000 47.05605 ? 228 ASN   A N   1 
ATOM   1759 C CA  . ASN   A 1 228 ? -4.84676  -37.46867 17.57946  1.000 49.77923 ? 228 ASN   A CA  1 
ATOM   1760 C C   . ASN   A 1 228 ? -5.77395  -38.45429 16.88012  1.000 47.22922 ? 228 ASN   A C   1 
ATOM   1761 O O   . ASN   A 1 228 ? -5.76319  -38.57043 15.64972  1.000 46.70758 ? 228 ASN   A O   1 
ATOM   1762 C CB  . ASN   A 1 228 ? -3.74091  -38.21751 18.33232  1.000 54.11811 ? 228 ASN   A CB  1 
ATOM   1763 C CG  . ASN   A 1 228 ? -2.53789  -37.34069 18.64493  1.000 58.12982 ? 228 ASN   A CG  1 
ATOM   1764 O OD1 . ASN   A 1 228 ? -2.22390  -37.09147 19.80858  1.000 62.07011 ? 228 ASN   A OD1 1 
ATOM   1765 N ND2 . ASN   A 1 228 ? -1.86301  -36.86391 17.60300  1.000 58.98901 ? 228 ASN   A ND2 1 
ATOM   1766 N N   . ASP   A 1 229 ? -6.59626  -39.16735 17.65047  1.000 46.39552 ? 229 ASP   A N   1 
ATOM   1767 C CA  . ASP   A 1 229 ? -7.44445  -40.18612 17.04752  1.000 47.06694 ? 229 ASP   A CA  1 
ATOM   1768 C C   . ASP   A 1 229 ? -8.48879  -39.56906 16.11566  1.000 44.89740 ? 229 ASP   A C   1 
ATOM   1769 O O   . ASP   A 1 229 ? -8.85929  -40.18418 15.10781  1.000 42.54904 ? 229 ASP   A O   1 
ATOM   1770 C CB  . ASP   A 1 229 ? -8.11091  -41.03438 18.13682  1.000 49.28909 ? 229 ASP   A CB  1 
ATOM   1771 C CG  . ASP   A 1 229 ? -7.18495  -42.10368 18.69581  1.000 53.43987 ? 229 ASP   A CG  1 
ATOM   1772 O OD1 . ASP   A 1 229 ? -6.03943  -42.21692 18.20976  1.000 54.24044 ? 229 ASP   A OD1 1 
ATOM   1773 O OD2 . ASP   A 1 229 ? -7.60688  -42.84564 19.61276  1.000 56.09378 ? 229 ASP   A OD2 1 
ATOM   1774 N N   . PHE   A 1 230 ? -8.96614  -38.35902 16.40718  1.000 43.00070 ? 230 PHE   A N   1 
ATOM   1775 C CA  . PHE   A 1 230 ? -9.84975  -37.71573 15.43794  1.000 42.18945 ? 230 PHE   A CA  1 
ATOM   1776 C C   . PHE   A 1 230 ? -9.08887  -37.38445 14.16110  1.000 38.80739 ? 230 PHE   A C   1 
ATOM   1777 O O   . PHE   A 1 230 ? -9.55372  -37.68154 13.05677  1.000 39.20926 ? 230 PHE   A O   1 
ATOM   1778 C CB  . PHE   A 1 230 ? -10.50739 -36.46150 16.01854  1.000 35.45305 ? 230 PHE   A CB  1 
ATOM   1779 C CG  . PHE   A 1 230 ? -11.33024 -35.70711 15.00975  1.000 35.89306 ? 230 PHE   A CG  1 
ATOM   1780 C CD1 . PHE   A 1 230 ? -12.53958 -36.21179 14.57197  1.000 31.86445 ? 230 PHE   A CD1 1 
ATOM   1781 C CD2 . PHE   A 1 230 ? -10.87082 -34.52022 14.46192  1.000 35.37317 ? 230 PHE   A CD2 1 
ATOM   1782 C CE1 . PHE   A 1 230 ? -13.29155 -35.53704 13.62739  1.000 33.91761 ? 230 PHE   A CE1 1 
ATOM   1783 C CE2 . PHE   A 1 230 ? -11.61690 -33.84534 13.52267  1.000 33.31585 ? 230 PHE   A CE2 1 
ATOM   1784 C CZ  . PHE   A 1 230 ? -12.83430 -34.35724 13.10256  1.000 30.47746 ? 230 PHE   A CZ  1 
ATOM   1785 N N   . ASN   A 1 231 ? -7.89402  -36.80803 14.29530  1.000 42.46872 ? 231 ASN   A N   1 
ATOM   1786 C CA  . ASN   A 1 231 ? -7.12251  -36.40753 13.11919  1.000 43.30402 ? 231 ASN   A CA  1 
ATOM   1787 C C   . ASN   A 1 231 ? -6.73732  -37.60178 12.24875  1.000 43.63391 ? 231 ASN   A C   1 
ATOM   1788 O O   . ASN   A 1 231 ? -6.65616  -37.46988 11.02168  1.000 43.65582 ? 231 ASN   A O   1 
ATOM   1789 C CB  . ASN   A 1 231 ? -5.88763  -35.62539 13.56183  1.000 39.20449 ? 231 ASN   A CB  1 
ATOM   1790 C CG  . ASN   A 1 231 ? -6.23659  -34.24048 14.06650  1.000 37.13385 ? 231 ASN   A CG  1 
ATOM   1791 O OD1 . ASN   A 1 231 ? -7.18827  -33.61547 13.58675  1.000 35.25379 ? 231 ASN   A OD1 1 
ATOM   1792 N ND2 . ASN   A 1 231 ? -5.48180  -33.75653 15.04517  1.000 36.33700 ? 231 ASN   A ND2 1 
ATOM   1793 N N   . LEU   A 1 232 ? -6.53146  -38.77646 12.85475  1.000 45.00325 ? 232 LEU   A N   1 
ATOM   1794 C CA  . LEU   A 1 232 ? -6.23024  -39.97789 12.07917  1.000 44.55277 ? 232 LEU   A CA  1 
ATOM   1795 C C   . LEU   A 1 232 ? -7.39870  -40.39279 11.19688  1.000 47.33349 ? 232 LEU   A C   1 
ATOM   1796 O O   . LEU   A 1 232 ? -7.18755  -40.98115 10.12814  1.000 47.07971 ? 232 LEU   A O   1 
ATOM   1797 C CB  . LEU   A 1 232 ? -5.84965  -41.13201 13.01111  1.000 45.25777 ? 232 LEU   A CB  1 
ATOM   1798 C CG  . LEU   A 1 232 ? -4.36744  -41.22713 13.39364  1.000 49.21947 ? 232 LEU   A CG  1 
ATOM   1799 C CD1 . LEU   A 1 232 ? -4.08264  -42.47470 14.25399  1.000 51.76940 ? 232 LEU   A CD1 1 
ATOM   1800 C CD2 . LEU   A 1 232 ? -3.48849  -41.20094 12.14444  1.000 47.35910 ? 232 LEU   A CD2 1 
ATOM   1801 N N   . VAL   A 1 233 ? -8.63271  -40.12069 11.63477  1.000 44.27313 ? 233 VAL   A N   1 
ATOM   1802 C CA  . VAL   A 1 233 ? -9.80462  -40.45668 10.83361  1.000 43.60715 ? 233 VAL   A CA  1 
ATOM   1803 C C   . VAL   A 1 233 ? -10.09233 -39.36237 9.81552   1.000 44.66788 ? 233 VAL   A C   1 
ATOM   1804 O O   . VAL   A 1 233 ? -10.53153 -39.64099 8.69380   1.000 43.25513 ? 233 VAL   A O   1 
ATOM   1805 C CB  . VAL   A 1 233 ? -11.01460 -40.71364 11.75012  1.000 45.89424 ? 233 VAL   A CB  1 
ATOM   1806 C CG1 . VAL   A 1 233 ? -12.26186 -40.99575 10.92497  1.000 41.65839 ? 233 VAL   A CG1 1 
ATOM   1807 C CG2 . VAL   A 1 233 ? -10.72171 -41.87679 12.69545  1.000 43.42288 ? 233 VAL   A CG2 1 
ATOM   1808 N N   . ALA   A 1 234 ? -9.84841  -38.10516 10.19141  1.000 43.49396 ? 234 ALA   A N   1 
ATOM   1809 C CA  . ALA   A 1 234 ? -10.08413 -36.99451 9.27842   1.000 44.30670 ? 234 ALA   A CA  1 
ATOM   1810 C C   . ALA   A 1 234 ? -9.16842  -37.07615 8.06625   1.000 45.01669 ? 234 ALA   A C   1 
ATOM   1811 O O   . ALA   A 1 234 ? -9.59728  -36.81947 6.93277   1.000 44.91723 ? 234 ALA   A O   1 
ATOM   1812 C CB  . ALA   A 1 234 ? -9.87719  -35.66533 10.00591  1.000 41.90273 ? 234 ALA   A CB  1 
ATOM   1813 N N   . MET   A 1 235 ? -7.89582  -37.40241 8.29303   1.000 44.02499 ? 235 MET   A N   1 
ATOM   1814 C CA  . MET   A 1 235 ? -6.95857  -37.56021 7.19181   1.000 45.83234 ? 235 MET   A CA  1 
ATOM   1815 C C   . MET   A 1 235 ? -7.50982  -38.52258 6.14530   1.000 44.85299 ? 235 MET   A C   1 
ATOM   1816 O O   . MET   A 1 235 ? -7.49738  -38.21902 4.94817   1.000 44.04034 ? 235 MET   A O   1 
ATOM   1817 C CB  . MET   A 1 235 ? -5.61098  -38.04354 7.73889   1.000 48.03264 ? 235 MET   A CB  1 
ATOM   1818 C CG  . MET   A 1 235 ? -4.58189  -38.43733 6.68579   1.000 51.96744 ? 235 MET   A CG  1 
ATOM   1819 S SD  . MET   A 1 235 ? -2.88347  -38.10734 7.22499   1.000 67.64966 ? 235 MET   A SD  1 
ATOM   1820 C CE  . MET   A 1 235 ? -2.93847  -38.76689 8.90215   1.000 53.17239 ? 235 MET   A CE  1 
ATOM   1821 N N   . LYS   A 1 236 ? -8.04794  -39.66642 6.58579   1.000 43.20604 ? 236 LYS   A N   1 
ATOM   1822 C CA  . LYS   A 1 236 ? -8.52972  -40.67828 5.64747   1.000 44.47159 ? 236 LYS   A CA  1 
ATOM   1823 C C   . LYS   A 1 236 ? -9.64814  -40.15371 4.75018   1.000 42.68198 ? 236 LYS   A C   1 
ATOM   1824 O O   . LYS   A 1 236 ? -9.77521  -40.59645 3.60200   1.000 42.16747 ? 236 LYS   A O   1 
ATOM   1825 C CB  . LYS   A 1 236 ? -8.99693  -41.92643 6.40668   1.000 47.64188 ? 236 LYS   A CB  1 
ATOM   1826 C CG  . LYS   A 1 236 ? -9.67581  -42.96702 5.51883   1.000 48.63759 ? 236 LYS   A CG  1 
ATOM   1827 C CD  . LYS   A 1 236 ? -10.00085 -44.26836 6.25135   1.000 57.49484 ? 236 LYS   A CD  1 
ATOM   1828 C CE  . LYS   A 1 236 ? -11.19066 -44.98214 5.58548   1.000 61.52847 ? 236 LYS   A CE  1 
ATOM   1829 N NZ  . LYS   A 1 236 ? -11.25091 -44.72887 4.10315   1.000 60.23518 ? 236 LYS   A NZ  1 
ATOM   1830 N N   . TYR   A 1 237 ? -10.45500 -39.20634 5.23510   1.000 43.06284 ? 237 TYR   A N   1 
ATOM   1831 C CA  . TYR   A 1 237 ? -11.57712 -38.67161 4.46874   1.000 38.85974 ? 237 TYR   A CA  1 
ATOM   1832 C C   . TYR   A 1 237 ? -11.29065 -37.29839 3.87355   1.000 36.65796 ? 237 TYR   A C   1 
ATOM   1833 O O   . TYR   A 1 237 ? -12.23375 -36.58305 3.51383   1.000 33.31478 ? 237 TYR   A O   1 
ATOM   1834 C CB  . TYR   A 1 237 ? -12.83185 -38.61523 5.33604   1.000 36.91370 ? 237 TYR   A CB  1 
ATOM   1835 C CG  . TYR   A 1 237 ? -13.37307 -39.98486 5.66582   1.000 41.81777 ? 237 TYR   A CG  1 
ATOM   1836 C CD1 . TYR   A 1 237 ? -14.24773 -40.63188 4.80103   1.000 43.28161 ? 237 TYR   A CD1 1 
ATOM   1837 C CD2 . TYR   A 1 237 ? -12.99339 -40.64190 6.82451   1.000 40.51944 ? 237 TYR   A CD2 1 
ATOM   1838 C CE1 . TYR   A 1 237 ? -14.74106 -41.88429 5.08888   1.000 45.06000 ? 237 TYR   A CE1 1 
ATOM   1839 C CE2 . TYR   A 1 237 ? -13.48006 -41.89546 7.11816   1.000 45.06953 ? 237 TYR   A CE2 1 
ATOM   1840 C CZ  . TYR   A 1 237 ? -14.35490 -42.51537 6.24657   1.000 46.70197 ? 237 TYR   A CZ  1 
ATOM   1841 O OH  . TYR   A 1 237 ? -14.85239 -43.77281 6.52999   1.000 49.81970 ? 237 TYR   A OH  1 
ATOM   1842 N N   . ASN   A 1 238 ? -10.01129 -36.91812 3.76592   1.000 37.63568 ? 238 ASN   A N   1 
ATOM   1843 C CA  . ASN   A 1 238 ? -9.60846  -35.68648 3.08096   1.000 34.48461 ? 238 ASN   A CA  1 
ATOM   1844 C C   . ASN   A 1 238 ? -10.09983 -34.44202 3.82257   1.000 31.73791 ? 238 ASN   A C   1 
ATOM   1845 O O   . ASN   A 1 238 ? -10.45354 -33.43516 3.21004   1.000 31.67114 ? 238 ASN   A O   1 
ATOM   1846 C CB  . ASN   A 1 238 ? -10.09470 -35.68055 1.62805   1.000 34.02737 ? 238 ASN   A CB  1 
ATOM   1847 C CG  . ASN   A 1 238 ? -9.36707  -34.67005 0.78003   1.000 35.16717 ? 238 ASN   A CG  1 
ATOM   1848 O OD1 . ASN   A 1 238 ? -8.14415  -34.52264 0.88420   1.000 31.00958 ? 238 ASN   A OD1 1 
ATOM   1849 N ND2 . ASN   A 1 238 ? -10.12152 -33.93402 -0.04888  1.000 33.30261 ? 238 ASN   A ND2 1 
ATOM   1850 N N   . TYR   A 1 239 ? -10.13622 -34.51547 5.14996   1.000 32.69714 ? 239 TYR   A N   1 
ATOM   1851 C CA  . TYR   A 1 239 ? -10.44097 -33.37551 5.99921   1.000 29.93496 ? 239 TYR   A CA  1 
ATOM   1852 C C   . TYR   A 1 239 ? -9.13527  -32.76110 6.49323   1.000 31.20283 ? 239 TYR   A C   1 
ATOM   1853 O O   . TYR   A 1 239 ? -8.09954  -33.43066 6.55528   1.000 30.15669 ? 239 TYR   A O   1 
ATOM   1854 C CB  . TYR   A 1 239 ? -11.31025 -33.80471 7.18609   1.000 28.25587 ? 239 TYR   A CB  1 
ATOM   1855 C CG  . TYR   A 1 239 ? -12.79890 -33.80360 6.91711   1.000 28.10399 ? 239 TYR   A CG  1 
ATOM   1856 C CD1 . TYR   A 1 239 ? -13.31253 -34.34385 5.75071   1.000 29.04992 ? 239 TYR   A CD1 1 
ATOM   1857 C CD2 . TYR   A 1 239 ? -13.68972 -33.25438 7.83209   1.000 26.43647 ? 239 TYR   A CD2 1 
ATOM   1858 C CE1 . TYR   A 1 239 ? -14.68115 -34.34842 5.49438   1.000 29.44254 ? 239 TYR   A CE1 1 
ATOM   1859 C CE2 . TYR   A 1 239 ? -15.05780 -33.25902 7.59460   1.000 26.61367 ? 239 TYR   A CE2 1 
ATOM   1860 C CZ  . TYR   A 1 239 ? -15.54803 -33.81721 6.42650   1.000 28.46736 ? 239 TYR   A CZ  1 
ATOM   1861 O OH  . TYR   A 1 239 ? -16.89998 -33.81719 6.18251   1.000 26.87189 ? 239 TYR   A OH  1 
ATOM   1862 N N   . GLU   A 1 240 ? -9.18125  -31.47934 6.84532   1.000 30.07193 ? 240 GLU   A N   1 
ATOM   1863 C CA  . GLU   A 1 240 ? -7.93833  -30.85699 7.26849   1.000 30.16467 ? 240 GLU   A CA  1 
ATOM   1864 C C   . GLU   A 1 240 ? -7.70667  -31.22654 8.71793   1.000 29.55563 ? 240 GLU   A C   1 
ATOM   1865 O O   . GLU   A 1 240 ? -8.65756  -31.55784 9.42984   1.000 29.42893 ? 240 GLU   A O   1 
ATOM   1866 C CB  . GLU   A 1 240 ? -7.99239  -29.34083 7.21342   1.000 29.47599 ? 240 GLU   A CB  1 
ATOM   1867 C CG  . GLU   A 1 240 ? -8.50480  -28.74131 6.00510   1.000 27.01522 ? 240 GLU   A CG  1 
ATOM   1868 C CD  . GLU   A 1 240 ? -8.16759  -27.27157 6.00912   1.000 32.54705 ? 240 GLU   A CD  1 
ATOM   1869 O OE1 . GLU   A 1 240 ? -7.29237  -26.88311 6.83357   1.000 40.42856 ? 240 GLU   A OE1 1 
ATOM   1870 O OE2 . GLU   A 1 240 ? -8.98037  -26.49073 5.46365   1.000 31.51219 ? 240 GLU   A OE2 1 
ATOM   1871 N N   . PRO   A 1 241 ? -6.46612  -31.15561 9.20162   1.000 33.14045 ? 241 PRO   A N   1 
ATOM   1872 C CA  . PRO   A 1 241 ? -6.25215  -31.39124 10.63141  1.000 33.67432 ? 241 PRO   A CA  1 
ATOM   1873 C C   . PRO   A 1 241 ? -6.98291  -30.33946 11.45288  1.000 29.60447 ? 241 PRO   A C   1 
ATOM   1874 O O   . PRO   A 1 241 ? -7.11855  -29.18479 11.04543  1.000 30.00343 ? 241 PRO   A O   1 
ATOM   1875 C CB  . PRO   A 1 241 ? -4.72871  -31.30019 10.78873  1.000 28.84252 ? 241 PRO   A CB  1 
ATOM   1876 C CG  . PRO   A 1 241 ? -4.19328  -31.64860 9.42852   1.000 30.81715 ? 241 PRO   A CG  1 
ATOM   1877 C CD  . PRO   A 1 241 ? -5.18682  -31.00986 8.48035   1.000 28.59559 ? 241 PRO   A CD  1 
ATOM   1878 N N   . LEU   A 1 242 ? -7.50272  -30.76944 12.59324  1.000 29.89752 ? 242 LEU   A N   1 
ATOM   1879 C CA  . LEU   A 1 242 ? -8.08511  -29.87241 13.58139  1.000 28.57616 ? 242 LEU   A CA  1 
ATOM   1880 C C   . LEU   A 1 242 ? -7.01731  -29.57480 14.62577  1.000 32.07898 ? 242 LEU   A C   1 
ATOM   1881 O O   . LEU   A 1 242 ? -6.45012  -30.49998 15.23116  1.000 29.78732 ? 242 LEU   A O   1 
ATOM   1882 C CB  . LEU   A 1 242 ? -9.32010  -30.49768 14.22776  1.000 27.13924 ? 242 LEU   A CB  1 
ATOM   1883 C CG  . LEU   A 1 242 ? -10.19686 -29.54960 15.03794  1.000 25.62090 ? 242 LEU   A CG  1 
ATOM   1884 C CD1 . LEU   A 1 242 ? -11.05804 -28.75182 14.08550  1.000 26.97471 ? 242 LEU   A CD1 1 
ATOM   1885 C CD2 . LEU   A 1 242 ? -11.04906 -30.33402 16.01472  1.000 26.62768 ? 242 LEU   A CD2 1 
ATOM   1886 N N   . THR   A 1 243 ? -6.70694  -28.29968 14.80038  1.000 30.22400 ? 243 THR   A N   1 
ATOM   1887 C CA  . THR   A 1 243 ? -5.69235  -27.92076 15.76996  1.000 31.62964 ? 243 THR   A CA  1 
ATOM   1888 C C   . THR   A 1 243 ? -6.35434  -27.56811 17.09795  1.000 35.08085 ? 243 THR   A C   1 
ATOM   1889 O O   . THR   A 1 243 ? -7.57142  -27.35084 17.17842  1.000 33.86717 ? 243 THR   A O   1 
ATOM   1890 C CB  . THR   A 1 243 ? -4.86690  -26.74066 15.26198  1.000 31.58112 ? 243 THR   A CB  1 
ATOM   1891 O OG1 . THR   A 1 243 ? -5.71232  -25.59068 15.12266  1.000 28.34761 ? 243 THR   A OG1 1 
ATOM   1892 C CG2 . THR   A 1 243 ? -4.20148  -27.07314 13.90909  1.000 31.31890 ? 243 THR   A CG2 1 
ATOM   1893 N N   . GLN   A 1 244 ? -5.53806  -27.51900 18.15273  1.000 31.82396 ? 244 GLN   A N   1 
ATOM   1894 C CA  . GLN   A 1 244 ? -6.05682  -27.05256 19.43276  1.000 34.39141 ? 244 GLN   A CA  1 
ATOM   1895 C C   . GLN   A 1 244 ? -6.61376  -25.64324 19.31742  1.000 33.82884 ? 244 GLN   A C   1 
ATOM   1896 O O   . GLN   A 1 244 ? -7.57927  -25.29904 20.01096  1.000 35.43232 ? 244 GLN   A O   1 
ATOM   1897 C CB  . GLN   A 1 244 ? -4.97272  -27.10353 20.50623  1.000 36.45080 ? 244 GLN   A CB  1 
ATOM   1898 C CG  . GLN   A 1 244 ? -5.42948  -26.55931 21.84485  1.000 38.24827 ? 244 GLN   A CG  1 
ATOM   1899 C CD  . GLN   A 1 244 ? -6.49076  -27.42134 22.50989  1.000 39.25096 ? 244 GLN   A CD  1 
ATOM   1900 O OE1 . GLN   A 1 244 ? -6.34358  -28.64312 22.61915  1.000 40.73374 ? 244 GLN   A OE1 1 
ATOM   1901 N NE2 . GLN   A 1 244 ? -7.56225  -26.78391 22.97136  1.000 38.65524 ? 244 GLN   A NE2 1 
ATOM   1902 N N   . ASP   A 1 245 ? -6.03162  -24.82058 18.44181  1.000 29.71012 ? 245 ASP   A N   1 
ATOM   1903 C CA  . ASP   A 1 245 ? -6.57893  -23.48935 18.22150  1.000 32.51058 ? 245 ASP   A CA  1 
ATOM   1904 C C   . ASP   A 1 245 ? -8.00983  -23.57125 17.70251  1.000 33.14935 ? 245 ASP   A C   1 
ATOM   1905 O O   . ASP   A 1 245 ? -8.88152  -22.79287 18.11390  1.000 31.57370 ? 245 ASP   A O   1 
ATOM   1906 C CB  . ASP   A 1 245 ? -5.69596  -22.72094 17.24287  1.000 33.90103 ? 245 ASP   A CB  1 
ATOM   1907 C CG  . ASP   A 1 245 ? -5.96608  -21.23736 17.26921  1.000 34.62037 ? 245 ASP   A CG  1 
ATOM   1908 O OD1 . ASP   A 1 245 ? -5.79906  -20.64643 18.35542  1.000 36.70059 ? 245 ASP   A OD1 1 
ATOM   1909 O OD2 . ASP   A 1 245 ? -6.36406  -20.67513 16.22218  1.000 36.78816 ? 245 ASP   A OD2 1 
ATOM   1910 N N   . HIS   A 1 246 ? -8.26473  -24.51211 16.79246  1.000 33.35579 ? 246 HIS   A N   1 
ATOM   1911 C CA  . HIS   A 1 246 ? -9.62284  -24.73891 16.32013  1.000 30.85205 ? 246 HIS   A CA  1 
ATOM   1912 C C   . HIS   A 1 246 ? -10.53293 -25.13174 17.46781  1.000 31.36170 ? 246 HIS   A C   1 
ATOM   1913 O O   . HIS   A 1 246 ? -11.65047 -24.62048 17.58327  1.000 27.75347 ? 246 HIS   A O   1 
ATOM   1914 C CB  . HIS   A 1 246 ? -9.62222  -25.82528 15.25628  1.000 28.60555 ? 246 HIS   A CB  1 
ATOM   1915 C CG  . HIS   A 1 246 ? -8.92041  -25.43454 14.00109  1.000 25.65801 ? 246 HIS   A CG  1 
ATOM   1916 N ND1 . HIS   A 1 246 ? -8.27887  -26.34857 13.19216  1.000 26.83453 ? 246 HIS   A ND1 1 
ATOM   1917 C CD2 . HIS   A 1 246 ? -8.75238  -24.22862 13.41196  1.000 25.97487 ? 246 HIS   A CD2 1 
ATOM   1918 C CE1 . HIS   A 1 246 ? -7.76679  -25.72519 12.14655  1.000 25.73890 ? 246 HIS   A CE1 1 
ATOM   1919 N NE2 . HIS   A 1 246 ? -8.03396  -24.43634 12.25934  1.000 26.42045 ? 246 HIS   A NE2 1 
ATOM   1920 N N   . VAL   A 1 247 ? -10.06091 -26.03607 18.33041  1.000 31.78103 ? 247 VAL   A N   1 
ATOM   1921 C CA  . VAL   A 1 247 ? -10.83434 -26.43832 19.50105  1.000 31.08039 ? 247 VAL   A CA  1 
ATOM   1922 C C   . VAL   A 1 247 ? -11.18788 -25.21989 20.34321  1.000 32.16695 ? 247 VAL   A C   1 
ATOM   1923 O O   . VAL   A 1 247 ? -12.34241 -25.03274 20.74118  1.000 34.36480 ? 247 VAL   A O   1 
ATOM   1924 C CB  . VAL   A 1 247 ? -10.06084 -27.49158 20.31812  1.000 32.59657 ? 247 VAL   A CB  1 
ATOM   1925 C CG1 . VAL   A 1 247 ? -10.76688 -27.78865 21.66243  1.000 33.97538 ? 247 VAL   A CG1 1 
ATOM   1926 C CG2 . VAL   A 1 247 ? -9.88492  -28.76595 19.49763  1.000 31.47926 ? 247 VAL   A CG2 1 
ATOM   1927 N N   . ASP   A 1 248 ? -10.20155 -24.36459 20.61646  1.000 34.07553 ? 248 ASP   A N   1 
ATOM   1928 C CA  . ASP   A 1 248 ? -10.46280 -23.18784 21.44145  1.000 33.26695 ? 248 ASP   A CA  1 
ATOM   1929 C C   . ASP   A 1 248 ? -11.49354 -22.27909 20.78967  1.000 32.10980 ? 248 ASP   A C   1 
ATOM   1930 O O   . ASP   A 1 248 ? -12.42489 -21.80824 21.45466  1.000 33.63056 ? 248 ASP   A O   1 
ATOM   1931 C CB  . ASP   A 1 248 ? -9.16580  -22.42594 21.70084  1.000 33.85812 ? 248 ASP   A CB  1 
ATOM   1932 C CG  . ASP   A 1 248 ? -8.18634  -23.22049 22.54487  1.000 37.19967 ? 248 ASP   A CG  1 
ATOM   1933 O OD1 . ASP   A 1 248 ? -8.65411  -23.99679 23.41176  1.000 36.78795 ? 248 ASP   A OD1 1 
ATOM   1934 O OD2 . ASP   A 1 248 ? -6.95992  -23.06360 22.34654  1.000 37.84000 ? 248 ASP   A OD2 1 
ATOM   1935 N N   . ILE   A 1 249 ? -11.34598 -22.02820 19.48747  1.000 29.50814 ? 249 ILE   A N   1 
ATOM   1936 C CA  . ILE   A 1 249 ? -12.27095 -21.15103 18.77636  1.000 30.69150 ? 249 ILE   A CA  1 
ATOM   1937 C C   . ILE   A 1 249 ? -13.69761 -21.66210 18.90800  1.000 27.84486 ? 249 ILE   A C   1 
ATOM   1938 O O   . ILE   A 1 249 ? -14.63101 -20.86842 19.06861  1.000 31.79605 ? 249 ILE   A O   1 
ATOM   1939 C CB  . ILE   A 1 249 ? -11.82665 -21.01190 17.30468  1.000 30.62342 ? 249 ILE   A CB  1 
ATOM   1940 C CG1 . ILE   A 1 249 ? -10.66001 -20.03375 17.20898  1.000 27.36140 ? 249 ILE   A CG1 1 
ATOM   1941 C CG2 . ILE   A 1 249 ? -12.95769 -20.53872 16.42380  1.000 23.48635 ? 249 ILE   A CG2 1 
ATOM   1942 C CD1 . ILE   A 1 249 ? -9.85880  -20.18627 15.95091  1.000 29.10751 ? 249 ILE   A CD1 1 
ATOM   1943 N N   . LEU   A 1 250 ? -13.88138 -22.99165 18.91824  1.000 27.23337 ? 250 LEU   A N   1 
ATOM   1944 C CA  . LEU   A 1 250 ? -15.16934 -23.64882 19.11547  1.000 27.76625 ? 250 LEU   A CA  1 
ATOM   1945 C C   . LEU   A 1 250 ? -15.58240 -23.73075 20.57996  1.000 30.36689 ? 250 LEU   A C   1 
ATOM   1946 O O   . LEU   A 1 250 ? -16.42165 -24.57487 20.94343  1.000 27.04314 ? 250 LEU   A O   1 
ATOM   1947 C CB  . LEU   A 1 250 ? -15.14479 -25.05410 18.51235  1.000 24.10122 ? 250 LEU   A CB  1 
ATOM   1948 C CG  . LEU   A 1 250 ? -15.10554 -25.21978 16.99518  1.000 23.12430 ? 250 LEU   A CG  1 
ATOM   1949 C CD1 . LEU   A 1 250 ? -14.64764 -26.63321 16.66905  1.000 23.74969 ? 250 LEU   A CD1 1 
ATOM   1950 C CD2 . LEU   A 1 250 ? -16.44365 -24.90975 16.32124  1.000 19.80784 ? 250 LEU   A CD2 1 
ATOM   1951 N N   . GLY   A 1 251 ? -15.02161 -22.88285 21.43362  1.000 32.37876 ? 251 GLY   A N   1 
ATOM   1952 C CA  . GLY   A 1 251 ? -15.35521 -22.89141 22.83814  1.000 30.41573 ? 251 GLY   A CA  1 
ATOM   1953 C C   . GLY   A 1 251 ? -16.76969 -22.42274 23.11230  1.000 30.15360 ? 251 GLY   A C   1 
ATOM   1954 O O   . GLY   A 1 251 ? -17.58657 -23.15709 23.67500  1.000 31.26569 ? 251 GLY   A O   1 
ATOM   1955 N N   . PRO   A 1 252 ? -17.06975 -21.16850 22.76013  1.000 29.41131 ? 252 PRO   A N   1 
ATOM   1956 C CA  . PRO   A 1 252 ? -18.43593 -20.66027 22.94202  1.000 29.76553 ? 252 PRO   A CA  1 
ATOM   1957 C C   . PRO   A 1 252 ? -19.51019 -21.59729 22.41722  1.000 29.39594 ? 252 PRO   A C   1 
ATOM   1958 O O   . PRO   A 1 252 ? -20.50489 -21.82887 23.11309  1.000 31.65013 ? 252 PRO   A O   1 
ATOM   1959 C CB  . PRO   A 1 252 ? -18.41062 -19.33980 22.16421  1.000 30.45929 ? 252 PRO   A CB  1 
ATOM   1960 C CG  . PRO   A 1 252 ? -17.00743 -18.88366 22.27425  1.000 32.34800 ? 252 PRO   A CG  1 
ATOM   1961 C CD  . PRO   A 1 252 ? -16.15788 -20.12215 22.26300  1.000 32.05447 ? 252 PRO   A CD  1 
ATOM   1962 N N   . LEU   A 1 253 ? -19.32600 -22.16650 21.22231  1.000 27.32270 ? 253 LEU   A N   1 
ATOM   1963 C CA  . LEU   A 1 253 ? -20.33952 -23.06570 20.67560  1.000 27.93692 ? 253 LEU   A CA  1 
ATOM   1964 C C   . LEU   A 1 253 ? -20.48143 -24.30504 21.53342  1.000 28.54960 ? 253 LEU   A C   1 
ATOM   1965 O O   . LEU   A 1 253 ? -21.59104 -24.80766 21.72503  1.000 30.98745 ? 253 LEU   A O   1 
ATOM   1966 C CB  . LEU   A 1 253 ? -19.98923 -23.46505 19.24754  1.000 23.14034 ? 253 LEU   A CB  1 
ATOM   1967 C CG  . LEU   A 1 253 ? -20.18633 -22.36868 18.22386  1.000 24.20109 ? 253 LEU   A CG  1 
ATOM   1968 C CD1 . LEU   A 1 253 ? -19.49093 -22.78501 16.94135  1.000 21.17280 ? 253 LEU   A CD1 1 
ATOM   1969 C CD2 . LEU   A 1 253 ? -21.67821 -22.10246 18.01184  1.000 21.50710 ? 253 LEU   A CD2 1 
ATOM   1970 N N   . SER   A 1 254 ? -19.35847 -24.82340 22.03358  1.000 28.22503 ? 254 SER   A N   1 
ATOM   1971 C CA  . SER   A 1 254 ? -19.38163 -25.94225 22.96710  1.000 30.82370 ? 254 SER   A CA  1 
ATOM   1972 C C   . SER   A 1 254 ? -20.12539 -25.56371 24.24238  1.000 33.76560 ? 254 SER   A C   1 
ATOM   1973 O O   . SER   A 1 254 ? -21.03665 -26.27575 24.68592  1.000 33.88313 ? 254 SER   A O   1 
ATOM   1974 C CB  . SER   A 1 254 ? -17.93958 -26.35475 23.28009  1.000 31.98493 ? 254 SER   A CB  1 
ATOM   1975 O OG  . SER   A 1 254 ? -17.86363 -27.56794 24.00193  1.000 34.32999 ? 254 SER   A OG  1 
ATOM   1976 N N   . ALA   A 1 255 ? -19.75038 -24.42153 24.83292  1.000 33.53926 ? 255 ALA   A N   1 
ATOM   1977 C CA  . ALA   A 1 255 ? -20.29842 -23.99114 26.11345  1.000 36.06079 ? 255 ALA   A CA  1 
ATOM   1978 C C   . ALA   A 1 255 ? -21.79624 -23.72958 26.03299  1.000 35.44083 ? 255 ALA   A C   1 
ATOM   1979 O O   . ALA   A 1 255 ? -22.52404 -23.97073 27.00456  1.000 37.66982 ? 255 ALA   A O   1 
ATOM   1980 C CB  . ALA   A 1 255 ? -19.55701 -22.73857 26.58490  1.000 36.94469 ? 255 ALA   A CB  1 
ATOM   1981 N N   . GLN   A 1 256 ? -22.27795 -23.24862 24.88796  1.000 33.14809 ? 256 GLN   A N   1 
ATOM   1982 C CA  . GLN   A 1 256 ? -23.69492 -22.95613 24.74324  1.000 33.48978 ? 256 GLN   A CA  1 
ATOM   1983 C C   . GLN   A 1 256 ? -24.53520 -24.21041 24.56678  1.000 35.90537 ? 256 GLN   A C   1 
ATOM   1984 O O   . GLN   A 1 256 ? -25.73550 -24.18975 24.86266  1.000 36.16597 ? 256 GLN   A O   1 
ATOM   1985 C CB  . GLN   A 1 256 ? -23.90079 -22.02247 23.55619  1.000 33.69586 ? 256 GLN   A CB  1 
ATOM   1986 C CG  . GLN   A 1 256 ? -25.31342 -21.55672 23.35747  1.000 35.22422 ? 256 GLN   A CG  1 
ATOM   1987 C CD  . GLN   A 1 256 ? -25.52697 -21.00291 21.97125  1.000 34.98078 ? 256 GLN   A CD  1 
ATOM   1988 O OE1 . GLN   A 1 256 ? -24.58438 -20.53702 21.32377  1.000 39.80048 ? 256 GLN   A OE1 1 
ATOM   1989 N NE2 . GLN   A 1 256 ? -26.76485 -21.05391 21.49811  1.000 35.10900 ? 256 GLN   A NE2 1 
ATOM   1990 N N   . THR   A 1 257 ? -23.94637 -25.29716 24.07851  1.000 33.53292 ? 257 THR   A N   1 
ATOM   1991 C CA  . THR   A 1 257 ? -24.71605 -26.49833 23.80750  1.000 32.78370 ? 257 THR   A CA  1 
ATOM   1992 C C   . THR   A 1 257 ? -24.48592 -27.60443 24.81978  1.000 34.59284 ? 257 THR   A C   1 
ATOM   1993 O O   . THR   A 1 257 ? -25.29484 -28.53130 24.88330  1.000 35.39277 ? 257 THR   A O   1 
ATOM   1994 C CB  . THR   A 1 257 ? -24.39258 -27.03433 22.40250  1.000 33.77877 ? 257 THR   A CB  1 
ATOM   1995 O OG1 . THR   A 1 257 ? -22.97208 -27.09785 22.23131  1.000 29.30015 ? 257 THR   A OG1 1 
ATOM   1996 C CG2 . THR   A 1 257 ? -24.97797 -26.12256 21.31368  1.000 27.01163 ? 257 THR   A CG2 1 
ATOM   1997 N N   . GLY   A 1 258 ? -23.41665 -27.53532 25.61029  1.000 36.27402 ? 258 GLY   A N   1 
ATOM   1998 C CA  . GLY   A 1 258 ? -23.12724 -28.59705 26.54983  1.000 39.12580 ? 258 GLY   A CA  1 
ATOM   1999 C C   . GLY   A 1 258 ? -22.47210 -29.81179 25.94015  1.000 38.87091 ? 258 GLY   A C   1 
ATOM   2000 O O   . GLY   A 1 258 ? -22.35858 -30.84317 26.61229  1.000 41.29486 ? 258 GLY   A O   1 
ATOM   2001 N N   . ILE   A 1 259 ? -22.04428 -29.72263 24.68956  1.000 36.23997 ? 259 ILE   A N   1 
ATOM   2002 C CA  . ILE   A 1 259 ? -21.35826 -30.79902 23.98738  1.000 35.96800 ? 259 ILE   A CA  1 
ATOM   2003 C C   . ILE   A 1 259 ? -19.89183 -30.40348 23.89691  1.000 35.79534 ? 259 ILE   A C   1 
ATOM   2004 O O   . ILE   A 1 259 ? -19.54302 -29.42473 23.22372  1.000 33.67621 ? 259 ILE   A O   1 
ATOM   2005 C CB  . ILE   A 1 259 ? -21.96133 -31.04476 22.59443  1.000 33.44611 ? 259 ILE   A CB  1 
ATOM   2006 C CG1 . ILE   A 1 259 ? -23.46432 -31.32045 22.72136  1.000 33.76980 ? 259 ILE   A CG1 1 
ATOM   2007 C CG2 . ILE   A 1 259 ? -21.24390 -32.18458 21.87529  1.000 33.49911 ? 259 ILE   A CG2 1 
ATOM   2008 C CD1 . ILE   A 1 259 ? -24.22677 -31.07332 21.46275  1.000 31.28645 ? 259 ILE   A CD1 1 
ATOM   2009 N N   . ALA   A 1 260 ? -19.03519 -31.15769 24.58128  1.000 38.21824 ? 260 ALA   A N   1 
ATOM   2010 C CA  . ALA   A 1 260 ? -17.60150 -30.95383 24.47509  1.000 38.38586 ? 260 ALA   A CA  1 
ATOM   2011 C C   . ALA   A 1 260 ? -17.15496 -31.08727 23.02085  1.000 37.25688 ? 260 ALA   A C   1 
ATOM   2012 O O   . ALA   A 1 260 ? -17.71507 -31.87073 22.24626  1.000 35.98077 ? 260 ALA   A O   1 
ATOM   2013 C CB  . ALA   A 1 260 ? -16.86689 -31.95968 25.35792  1.000 41.67335 ? 260 ALA   A CB  1 
ATOM   2014 N N   . VAL   A 1 261 ? -16.14264 -30.29472 22.64750  1.000 34.75865 ? 261 VAL   A N   1 
ATOM   2015 C CA  . VAL   A 1 261 ? -15.68831 -30.27338 21.26043  1.000 32.36384 ? 261 VAL   A CA  1 
ATOM   2016 C C   . VAL   A 1 261 ? -15.21615 -31.65677 20.83255  1.000 33.79960 ? 261 VAL   A C   1 
ATOM   2017 O O   . VAL   A 1 261 ? -15.53680 -32.12546 19.73232  1.000 31.79354 ? 261 VAL   A O   1 
ATOM   2018 C CB  . VAL   A 1 261 ? -14.57992 -29.21949 21.08161  1.000 34.14244 ? 261 VAL   A CB  1 
ATOM   2019 C CG1 . VAL   A 1 261 ? -13.95399 -29.32144 19.68276  1.000 29.57711 ? 261 VAL   A CG1 1 
ATOM   2020 C CG2 . VAL   A 1 261 ? -15.12050 -27.82461 21.36491  1.000 30.62968 ? 261 VAL   A CG2 1 
ATOM   2021 N N   . LEU   A 1 262 ? -14.44523 -32.33152 21.69673  1.000 36.23756 ? 262 LEU   A N   1 
ATOM   2022 C CA  . LEU   A 1 262 ? -13.98287 -33.68220 21.39235  1.000 38.27628 ? 262 LEU   A CA  1 
ATOM   2023 C C   . LEU   A 1 262 ? -15.15215 -34.65189 21.25383  1.000 38.14115 ? 262 LEU   A C   1 
ATOM   2024 O O   . LEU   A 1 262 ? -15.04528 -35.66132 20.54613  1.000 38.10992 ? 262 LEU   A O   1 
ATOM   2025 C CB  . LEU   A 1 262 ? -13.04118 -34.19179 22.48227  1.000 40.87354 ? 262 LEU   A CB  1 
ATOM   2026 C CG  . LEU   A 1 262 ? -11.58603 -33.70795 22.52384  1.000 43.93833 ? 262 LEU   A CG  1 
ATOM   2027 C CD1 . LEU   A 1 262 ? -10.86978 -33.99114 21.20390  1.000 39.92295 ? 262 LEU   A CD1 1 
ATOM   2028 C CD2 . LEU   A 1 262 ? -11.44258 -32.25307 22.98342  1.000 45.14110 ? 262 LEU   A CD2 1 
ATOM   2029 N N   . ASP   A 1 263 ? -16.26380 -34.38034 21.94296  1.000 38.11385 ? 263 ASP   A N   1 
ATOM   2030 C CA  . ASP   A 1 263 ? -17.45349 -35.20307 21.76192  1.000 38.56901 ? 263 ASP   A CA  1 
ATOM   2031 C C   . ASP   A 1 263 ? -18.08817 -34.95842 20.40400  1.000 35.38610 ? 263 ASP   A C   1 
ATOM   2032 O O   . ASP   A 1 263 ? -18.48646 -35.91062 19.72379  1.000 35.49352 ? 263 ASP   A O   1 
ATOM   2033 C CB  . ASP   A 1 263 ? -18.46011 -34.94029 22.88088  1.000 43.16712 ? 263 ASP   A CB  1 
ATOM   2034 C CG  . ASP   A 1 263 ? -17.99535 -35.49085 24.20079  1.000 43.09537 ? 263 ASP   A CG  1 
ATOM   2035 O OD1 . ASP   A 1 263 ? -16.95190 -36.16237 24.19670  1.000 44.56584 ? 263 ASP   A OD1 1 
ATOM   2036 O OD2 . ASP   A 1 263 ? -18.65314 -35.25351 25.23168  1.000 44.57514 ? 263 ASP   A OD2 1 
ATOM   2037 N N   . MET   A 1 264 ? -18.18374 -33.69421 19.98362  1.000 32.97687 ? 264 MET   A N   1 
ATOM   2038 C CA  . MET   A 1 264 ? -18.67676 -33.42541 18.63977  1.000 30.87704 ? 264 MET   A CA  1 
ATOM   2039 C C   . MET   A 1 264 ? -17.76800 -34.04521 17.59296  1.000 33.10587 ? 264 MET   A C   1 
ATOM   2040 O O   . MET   A 1 264 ? -18.24785 -34.44883 16.52644  1.000 30.37306 ? 264 MET   A O   1 
ATOM   2041 C CB  . MET   A 1 264 ? -18.81960 -31.92134 18.40552  1.000 29.68172 ? 264 MET   A CB  1 
ATOM   2042 C CG  . MET   A 1 264 ? -19.61551 -31.57396 17.14187  1.000 29.16470 ? 264 MET   A CG  1 
ATOM   2043 S SD  . MET   A 1 264 ? -21.36204 -32.08205 17.17333  1.000 26.09094 ? 264 MET   A SD  1 
ATOM   2044 C CE  . MET   A 1 264 ? -22.11969 -30.70591 18.03144  1.000 25.71392 ? 264 MET   A CE  1 
ATOM   2045 N N   . CYS   A 1 265 ? -16.45801 -34.14592 17.88496  1.000 32.22177 ? 265 CYS   A N   1 
ATOM   2046 C CA  . CYS   A 1 265 ? -15.53066 -34.79282 16.95893  1.000 31.00638 ? 265 CYS   A CA  1 
ATOM   2047 C C   . CYS   A 1 265 ? -15.85000 -36.27276 16.80491  1.000 32.85187 ? 265 CYS   A C   1 
ATOM   2048 O O   . CYS   A 1 265 ? -15.76577 -36.82118 15.69894  1.000 32.30977 ? 265 CYS   A O   1 
ATOM   2049 C CB  . CYS   A 1 265 ? -14.08794 -34.62023 17.43807  1.000 32.21394 ? 265 CYS   A CB  1 
ATOM   2050 S SG  . CYS   A 1 265 ? -13.36402 -32.97586 17.18904  1.000 30.03249 ? 265 CYS   A SG  1 
ATOM   2051 N N   . ALA   A 1 266 ? -16.19371 -36.93997 17.91188  1.000 35.30199 ? 266 ALA   A N   1 
ATOM   2052 C CA  . ALA   A 1 266 ? -16.63538 -38.32918 17.83902  1.000 37.30332 ? 266 ALA   A CA  1 
ATOM   2053 C C   . ALA   A 1 266 ? -17.89308 -38.46886 16.99290  1.000 37.92051 ? 266 ALA   A C   1 
ATOM   2054 O O   . ALA   A 1 266 ? -18.05965 -39.47965 16.30087  1.000 40.86131 ? 266 ALA   A O   1 
ATOM   2055 C CB  . ALA   A 1 266 ? -16.88123 -38.87965 19.23947  1.000 40.21044 ? 266 ALA   A CB  1 
ATOM   2056 N N   . SER   A 1 267 ? -18.78499 -37.46819 17.03092  1.000 35.76864 ? 267 SER   A N   1 
ATOM   2057 C CA  . SER   A 1 267 ? -19.96880 -37.49101 16.17331  1.000 34.40939 ? 267 SER   A CA  1 
ATOM   2058 C C   . SER   A 1 267 ? -19.57525 -37.42435 14.70855  1.000 34.15871 ? 267 SER   A C   1 
ATOM   2059 O O   . SER   A 1 267 ? -20.02350 -38.23951 13.89558  1.000 33.08167 ? 267 SER   A O   1 
ATOM   2060 C CB  . SER   A 1 267 ? -20.90043 -36.32934 16.51000  1.000 32.19734 ? 267 SER   A CB  1 
ATOM   2061 O OG  . SER   A 1 267 ? -21.12490 -36.24566 17.89708  1.000 38.60562 ? 267 SER   A OG  1 
ATOM   2062 N N   . LEU   A 1 268 ? -18.74023 -36.44163 14.35293  1.000 32.49988 ? 268 LEU   A N   1 
ATOM   2063 C CA  . LEU   A 1 268 ? -18.26364 -36.33318 12.98045  1.000 32.00812 ? 268 LEU   A CA  1 
ATOM   2064 C C   . LEU   A 1 268 ? -17.55731 -37.60815 12.53185  1.000 33.89341 ? 268 LEU   A C   1 
ATOM   2065 O O   . LEU   A 1 268 ? -17.77593 -38.07860 11.41064  1.000 33.58949 ? 268 LEU   A O   1 
ATOM   2066 C CB  . LEU   A 1 268 ? -17.33689 -35.12773 12.84232  1.000 30.51688 ? 268 LEU   A CB  1 
ATOM   2067 C CG  . LEU   A 1 268 ? -16.72877 -34.86953 11.46721  1.000 29.67855 ? 268 LEU   A CG  1 
ATOM   2068 C CD1 . LEU   A 1 268 ? -17.82448 -34.74386 10.40109  1.000 27.80633 ? 268 LEU   A CD1 1 
ATOM   2069 C CD2 . LEU   A 1 268 ? -15.91058 -33.60022 11.51938  1.000 26.71496 ? 268 LEU   A CD2 1 
ATOM   2070 N N   . LYS   A 1 269 ? -16.70052 -38.17935 13.38310  1.000 32.74604 ? 269 LYS   A N   1 
ATOM   2071 C CA  . LYS   A 1 269 ? -16.05858 -39.44749 13.03261  1.000 37.42673 ? 269 LYS   A CA  1 
ATOM   2072 C C   . LYS   A 1 269 ? -17.07995 -40.49970 12.59500  1.000 38.09626 ? 269 LYS   A C   1 
ATOM   2073 O O   . LYS   A 1 269 ? -16.94901 -41.10459 11.52368  1.000 37.01137 ? 269 LYS   A O   1 
ATOM   2074 C CB  . LYS   A 1 269 ? -15.23513 -39.97363 14.20954  1.000 38.90294 ? 269 LYS   A CB  1 
ATOM   2075 C CG  . LYS   A 1 269 ? -14.55311 -41.31131 13.93554  1.000 44.00961 ? 269 LYS   A CG  1 
ATOM   2076 C CD  . LYS   A 1 269 ? -13.93247 -41.92671 15.19637  1.000 44.71255 ? 269 LYS   A CD  1 
ATOM   2077 C CE  . LYS   A 1 269 ? -12.65271 -41.23255 15.62961  1.000 48.05528 ? 269 LYS   A CE  1 
ATOM   2078 N NZ  . LYS   A 1 269 ? -12.02952 -41.97588 16.76008  1.000 48.63499 ? 269 LYS   A NZ  1 
ATOM   2079 N N   . GLU   A 1 270 ? -18.11169 -40.73435 13.40820  1.000 39.22810 ? 270 GLU   A N   1 
ATOM   2080 C CA  . GLU   A 1 270 ? -19.10171 -41.73337 13.01241  1.000 41.63370 ? 270 GLU   A CA  1 
ATOM   2081 C C   . GLU   A 1 270 ? -19.87941 -41.27471 11.78470  1.000 38.26142 ? 270 GLU   A C   1 
ATOM   2082 O O   . GLU   A 1 270 ? -20.23595 -42.09580 10.93280  1.000 41.21335 ? 270 GLU   A O   1 
ATOM   2083 C CB  . GLU   A 1 270 ? -20.04001 -42.05200 14.17685  1.000 41.82880 ? 270 GLU   A CB  1 
ATOM   2084 C CG  . GLU   A 1 270 ? -19.29258 -42.46899 15.43317  1.000 46.73151 ? 270 GLU   A CG  1 
ATOM   2085 C CD  . GLU   A 1 270 ? -18.37667 -43.69029 15.21766  1.000 54.41397 ? 270 GLU   A CD  1 
ATOM   2086 O OE1 . GLU   A 1 270 ? -18.73972 -44.58463 14.41886  1.000 57.80421 ? 270 GLU   A OE1 1 
ATOM   2087 O OE2 . GLU   A 1 270 ? -17.27651 -43.74333 15.82634  1.000 52.48651 ? 270 GLU   A OE2 1 
ATOM   2088 N N   . LEU   A 1 271 ? -20.11039 -39.96360 11.65072  1.000 34.28846 ? 271 LEU   A N   1 
ATOM   2089 C CA  . LEU   A 1 271 ? -20.78192 -39.45402 10.45588  1.000 37.54824 ? 271 LEU   A CA  1 
ATOM   2090 C C   . LEU   A 1 271 ? -19.96051 -39.73950 9.20333   1.000 38.55479 ? 271 LEU   A C   1 
ATOM   2091 O O   . LEU   A 1 271 ? -20.51427 -40.07849 8.14845   1.000 36.71973 ? 271 LEU   A O   1 
ATOM   2092 C CB  . LEU   A 1 271 ? -21.04059 -37.95453 10.59182  1.000 33.32268 ? 271 LEU   A CB  1 
ATOM   2093 C CG  . LEU   A 1 271 ? -22.31047 -37.48380 11.29720  1.000 33.89050 ? 271 LEU   A CG  1 
ATOM   2094 C CD1 . LEU   A 1 271 ? -22.33845 -35.96290 11.34915  1.000 25.48577 ? 271 LEU   A CD1 1 
ATOM   2095 C CD2 . LEU   A 1 271 ? -23.54865 -38.02245 10.59825  1.000 36.01341 ? 271 LEU   A CD2 1 
ATOM   2096 N N   . LEU   A 1 272 ? -18.63486 -39.61064 9.30392   1.000 36.20067 ? 272 LEU   A N   1 
ATOM   2097 C CA  . LEU   A 1 272 ? -17.76958 -39.87808 8.15843   1.000 41.11283 ? 272 LEU   A CA  1 
ATOM   2098 C C   . LEU   A 1 272 ? -17.65212 -41.36937 7.88055   1.000 42.69061 ? 272 LEU   A C   1 
ATOM   2099 O O   . LEU   A 1 272 ? -17.43339 -41.76511 6.73048   1.000 46.56123 ? 272 LEU   A O   1 
ATOM   2100 C CB  . LEU   A 1 272 ? -16.37598 -39.28975 8.39270   1.000 35.36475 ? 272 LEU   A CB  1 
ATOM   2101 C CG  . LEU   A 1 272 ? -16.24225 -37.77036 8.43543   1.000 35.31465 ? 272 LEU   A CG  1 
ATOM   2102 C CD1 . LEU   A 1 272 ? -14.81610 -37.39320 8.75412   1.000 36.30599 ? 272 LEU   A CD1 1 
ATOM   2103 C CD2 . LEU   A 1 272 ? -16.68357 -37.13643 7.12785   1.000 34.03229 ? 272 LEU   A CD2 1 
ATOM   2104 N N   . GLN   A 1 273 ? -17.78146 -42.20624 8.91369   1.000 42.67629 ? 273 GLN   A N   1 
ATOM   2105 C CA  . GLN   A 1 273 ? -17.57837 -43.64035 8.74434   1.000 43.95544 ? 273 GLN   A CA  1 
ATOM   2106 C C   . GLN   A 1 273 ? -18.82806 -44.35242 8.24685   1.000 47.55979 ? 273 GLN   A C   1 
ATOM   2107 O O   . GLN   A 1 273 ? -18.71837 -45.37944 7.56876   1.000 50.91110 ? 273 GLN   A O   1 
ATOM   2108 C CB  . GLN   A 1 273 ? -17.11975 -44.26775 10.06191  1.000 45.20136 ? 273 GLN   A CB  1 
ATOM   2109 C CG  . GLN   A 1 273 ? -15.64578 -44.04479 10.37516  1.000 46.01321 ? 273 GLN   A CG  1 
ATOM   2110 C CD  . GLN   A 1 273 ? -15.28353 -44.45009 11.79122  1.000 47.53001 ? 273 GLN   A CD  1 
ATOM   2111 O OE1 . GLN   A 1 273 ? -16.13070 -44.91696 12.55285  1.000 50.01860 ? 273 GLN   A OE1 1 
ATOM   2112 N NE2 . GLN   A 1 273 ? -14.02183 -44.26670 12.15340  1.000 45.29370 ? 273 GLN   A NE2 1 
ATOM   2113 N N   . ASN   A 1 274 ? -20.01510 -43.84204 8.57282   1.000 46.24874 ? 274 ASN   A N   1 
ATOM   2114 C CA  . ASN   A 1 274 ? -21.25482 -44.52681 8.24634   1.000 47.16550 ? 274 ASN   A CA  1 
ATOM   2115 C C   . ASN   A 1 274 ? -22.14611 -43.74938 7.29299   1.000 45.97026 ? 274 ASN   A C   1 
ATOM   2116 O O   . ASN   A 1 274 ? -23.22266 -44.24140 6.94011   1.000 42.34691 ? 274 ASN   A O   1 
ATOM   2117 C CB  . ASN   A 1 274 ? -22.03842 -44.84623 9.52750   1.000 49.47236 ? 274 ASN   A CB  1 
ATOM   2118 C CG  . ASN   A 1 274 ? -21.15406 -45.41669 10.62705  1.000 51.94051 ? 274 ASN   A CG  1 
ATOM   2119 O OD1 . ASN   A 1 274 ? -21.22021 -44.98389 11.77925  1.000 54.14271 ? 274 ASN   A OD1 1 
ATOM   2120 N ND2 . ASN   A 1 274 ? -20.31289 -46.38669 10.27217  1.000 52.73315 ? 274 ASN   A ND2 1 
ATOM   2121 N N   . GLY   A 1 275 ? -21.73142 -42.56415 6.85611   1.000 47.54624 ? 275 GLY   A N   1 
ATOM   2122 C CA  . GLY   A 1 275 ? -22.60896 -41.73588 6.05955   1.000 44.36432 ? 275 GLY   A CA  1 
ATOM   2123 C C   . GLY   A 1 275 ? -23.76110 -41.23047 6.91003   1.000 46.49718 ? 275 GLY   A C   1 
ATOM   2124 O O   . GLY   A 1 275 ? -23.83710 -41.46504 8.11521   1.000 45.63870 ? 275 GLY   A O   1 
ATOM   2125 N N   . MET   A 1 276 ? -24.67663 -40.52216 6.25277   1.000 47.32011 ? 276 MET   A N   1 
ATOM   2126 C CA  . MET   A 1 276 ? -25.81970 -39.97259 6.96540   1.000 45.45005 ? 276 MET   A CA  1 
ATOM   2127 C C   . MET   A 1 276 ? -27.03063 -40.89007 6.92063   1.000 46.65116 ? 276 MET   A C   1 
ATOM   2128 O O   . MET   A 1 276 ? -28.01035 -40.62912 7.62582   1.000 48.79791 ? 276 MET   A O   1 
ATOM   2129 C CB  . MET   A 1 276 ? -26.16565 -38.58028 6.41672   1.000 44.85328 ? 276 MET   A CB  1 
ATOM   2130 C CG  . MET   A 1 276 ? -25.39370 -37.46429 7.13507   1.000 39.92943 ? 276 MET   A CG  1 
ATOM   2131 S SD  . MET   A 1 276 ? -25.16565 -35.92638 6.20883   1.000 48.73607 ? 276 MET   A SD  1 
ATOM   2132 C CE  . MET   A 1 276 ? -26.85132 -35.38852 6.03719   1.000 30.30694 ? 276 MET   A CE  1 
ATOM   2133 N N   . ASN   A 1 277 ? -26.96766 -41.96204 6.12859   1.000 51.38387 ? 277 ASN   A N   1 
ATOM   2134 C CA  . ASN   A 1 277 ? -27.99178 -43.00794 6.09339   1.000 51.93807 ? 277 ASN   A CA  1 
ATOM   2135 C C   . ASN   A 1 277 ? -29.35447 -42.44206 5.70240   1.000 51.85255 ? 277 ASN   A C   1 
ATOM   2136 O O   . ASN   A 1 277 ? -30.38505 -42.78554 6.28776   1.000 47.97298 ? 277 ASN   A O   1 
ATOM   2137 C CB  . ASN   A 1 277 ? -28.06594 -43.75530 7.42679   1.000 57.63996 ? 277 ASN   A CB  1 
ATOM   2138 C CG  . ASN   A 1 277 ? -28.61738 -45.16393 7.27571   1.000 63.29174 ? 277 ASN   A CG  1 
ATOM   2139 O OD1 . ASN   A 1 277 ? -29.34619 -45.46401 6.32524   1.000 66.36236 ? 277 ASN   A OD1 1 
ATOM   2140 N ND2 . ASN   A 1 277 ? -28.26469 -46.03900 8.21078   1.000 69.76487 ? 277 ASN   A ND2 1 
ATOM   2141 N N   . GLY   A 1 278 ? -29.35749 -41.55944 4.70436   1.000 51.50834 ? 278 GLY   A N   1 
ATOM   2142 C CA  . GLY   A 1 278 ? -30.60716 -41.02423 4.20296   1.000 46.91823 ? 278 GLY   A CA  1 
ATOM   2143 C C   . GLY   A 1 278 ? -31.26612 -39.98458 5.08106   1.000 46.14566 ? 278 GLY   A C   1 
ATOM   2144 O O   . GLY   A 1 278 ? -32.44427 -39.68080 4.88465   1.000 44.97026 ? 278 GLY   A O   1 
ATOM   2145 N N   . ARG   A 1 279 ? -30.55260 -39.43586 6.05540   1.000 44.09723 ? 279 ARG   A N   1 
ATOM   2146 C CA  . ARG   A 1 279 ? -31.04680 -38.28888 6.79722   1.000 38.84514 ? 279 ARG   A CA  1 
ATOM   2147 C C   . ARG   A 1 279 ? -30.34624 -37.01783 6.35251   1.000 35.86029 ? 279 ARG   A C   1 
ATOM   2148 O O   . ARG   A 1 279 ? -29.34445 -37.03407 5.63466   1.000 34.57438 ? 279 ARG   A O   1 
ATOM   2149 C CB  . ARG   A 1 279 ? -30.84549 -38.43940 8.30187   1.000 41.68576 ? 279 ARG   A CB  1 
ATOM   2150 C CG  . ARG   A 1 279 ? -31.36259 -39.67455 8.96222   1.000 42.69470 ? 279 ARG   A CG  1 
ATOM   2151 C CD  . ARG   A 1 279 ? -31.69435 -39.23390 10.36847  1.000 43.60497 ? 279 ARG   A CD  1 
ATOM   2152 N NE  . ARG   A 1 279 ? -31.73879 -40.30717 11.35348  1.000 47.52222 ? 279 ARG   A NE  1 
ATOM   2153 C CZ  . ARG   A 1 279 ? -32.27742 -40.15698 12.55923  1.000 45.44216 ? 279 ARG   A CZ  1 
ATOM   2154 N NH1 . ARG   A 1 279 ? -32.81399 -38.98592 12.89409  1.000 41.90097 ? 279 ARG   A NH1 1 
ATOM   2155 N NH2 . ARG   A 1 279 ? -32.28224 -41.16647 13.42201  1.000 48.07906 ? 279 ARG   A NH2 1 
ATOM   2156 N N   . THR   A 1 280 ? -30.87938 -35.90000 6.83143   1.000 37.59918 ? 280 THR   A N   1 
ATOM   2157 C CA  . THR   A 1 280 ? -30.36518 -34.58141 6.51087   1.000 32.05490 ? 280 THR   A CA  1 
ATOM   2158 C C   . THR   A 1 280 ? -30.00241 -33.85190 7.79823   1.000 28.45103 ? 280 THR   A C   1 
ATOM   2159 O O   . THR   A 1 280 ? -30.44841 -34.19698 8.89252   1.000 29.92657 ? 280 THR   A O   1 
ATOM   2160 C CB  . THR   A 1 280 ? -31.38523 -33.77449 5.68906   1.000 29.48026 ? 280 THR   A CB  1 
ATOM   2161 O OG1 . THR   A 1 280 ? -32.59993 -33.62781 6.42918   1.000 30.14645 ? 280 THR   A OG1 1 
ATOM   2162 C CG2 . THR   A 1 280 ? -31.69171 -34.49322 4.39078   1.000 27.57544 ? 280 THR   A CG2 1 
ATOM   2163 N N   . ILE   A 1 281 ? -29.14755 -32.85309 7.66359   1.000 25.90264 ? 281 ILE   A N   1 
ATOM   2164 C CA  . ILE   A 1 281 ? -28.79900 -31.98316 8.77269   1.000 23.22341 ? 281 ILE   A CA  1 
ATOM   2165 C C   . ILE   A 1 281 ? -28.98158 -30.56290 8.28758   1.000 22.41600 ? 281 ILE   A C   1 
ATOM   2166 O O   . ILE   A 1 281 ? -28.35800 -30.16349 7.29401   1.000 20.31399 ? 281 ILE   A O   1 
ATOM   2167 C CB  . ILE   A 1 281 ? -27.35965 -32.20291 9.25862   1.000 22.84481 ? 281 ILE   A CB  1 
ATOM   2168 C CG1 . ILE   A 1 281 ? -27.18264 -33.60075 9.85572   1.000 23.64443 ? 281 ILE   A CG1 1 
ATOM   2169 C CG2 . ILE   A 1 281 ? -26.99361 -31.13632 10.24174  1.000 22.85305 ? 281 ILE   A CG2 1 
ATOM   2170 C CD1 . ILE   A 1 281 ? -25.73484 -33.92266 10.17061  1.000 26.71480 ? 281 ILE   A CD1 1 
ATOM   2171 N N   . LEU   A 1 282 ? -29.83282 -29.80335 8.97605   1.000 24.35439 ? 282 LEU   A N   1 
ATOM   2172 C CA  . LEU   A 1 282 ? -30.11886 -28.42357 8.59178   1.000 24.05156 ? 282 LEU   A CA  1 
ATOM   2173 C C   . LEU   A 1 282 ? -30.43767 -28.33922 7.10290   1.000 20.65655 ? 282 LEU   A C   1 
ATOM   2174 O O   . LEU   A 1 282 ? -29.94448 -27.46474 6.39118   1.000 17.95265 ? 282 LEU   A O   1 
ATOM   2175 C CB  . LEU   A 1 282 ? -28.94551 -27.50162 8.96133   1.000 19.72431 ? 282 LEU   A CB  1 
ATOM   2176 C CG  . LEU   A 1 282 ? -28.75163 -27.29894 10.45682  1.000 21.25731 ? 282 LEU   A CG  1 
ATOM   2177 C CD1 . LEU   A 1 282 ? -27.56633 -26.40766 10.72899  1.000 21.03524 ? 282 LEU   A CD1 1 
ATOM   2178 C CD2 . LEU   A 1 282 ? -30.01257 -26.73686 11.09907  1.000 22.79346 ? 282 LEU   A CD2 1 
ATOM   2179 N N   . GLY   A 1 283 ? -31.23025 -29.29878 6.62017   1.000 23.77275 ? 283 GLY   A N   1 
ATOM   2180 C CA  . GLY   A 1 283 ? -31.67144 -29.33237 5.23743   1.000 22.74454 ? 283 GLY   A CA  1 
ATOM   2181 C C   . GLY   A 1 283 ? -30.64652 -29.80636 4.22666   1.000 27.19492 ? 283 GLY   A C   1 
ATOM   2182 O O   . GLY   A 1 283 ? -30.91993 -29.74111 3.01990   1.000 28.08264 ? 283 GLY   A O   1 
ATOM   2183 N N   . SER   A 1 284 ? -29.47436 -30.26964 4.66745   1.000 26.97604 ? 284 SER   A N   1 
ATOM   2184 C CA  . SER   A 1 284 ? -28.39626 -30.67963 3.77299   1.000 25.11289 ? 284 SER   A CA  1 
ATOM   2185 C C   . SER   A 1 284 ? -28.15476 -32.17751 3.90335   1.000 26.46377 ? 284 SER   A C   1 
ATOM   2186 O O   . SER   A 1 284 ? -28.16381 -32.72052 5.00869   1.000 27.72917 ? 284 SER   A O   1 
ATOM   2187 C CB  . SER   A 1 284 ? -27.10398 -29.91708 4.08619   1.000 24.67429 ? 284 SER   A CB  1 
ATOM   2188 O OG  . SER   A 1 284 ? -25.99855 -30.43023 3.34714   1.000 24.87070 ? 284 SER   A OG  1 
ATOM   2189 N N   . ALA   A 1 285 ? -27.94932 -32.85123 2.77407   1.000 26.14371 ? 285 ALA   A N   1 
ATOM   2190 C CA  . ALA   A 1 285 ? -27.56471 -34.25462 2.79401   1.000 25.44141 ? 285 ALA   A CA  1 
ATOM   2191 C C   . ALA   A 1 285 ? -26.05317 -34.45395 2.71677   1.000 27.73712 ? 285 ALA   A C   1 
ATOM   2192 O O   . ALA   A 1 285 ? -25.59767 -35.59869 2.66189   1.000 27.78046 ? 285 ALA   A O   1 
ATOM   2193 C CB  . ALA   A 1 285 ? -28.24913 -35.01693 1.65919   1.000 26.99801 ? 285 ALA   A CB  1 
ATOM   2194 N N   . LEU   A 1 286 ? -25.27216 -33.37449 2.71721   1.000 24.87780 ? 286 LEU   A N   1 
ATOM   2195 C CA  . LEU   A 1 286 ? -23.81854 -33.43484 2.80298   1.000 26.55544 ? 286 LEU   A CA  1 
ATOM   2196 C C   . LEU   A 1 286 ? -23.33949 -32.62929 4.00576   1.000 23.67248 ? 286 LEU   A C   1 
ATOM   2197 O O   . LEU   A 1 286 ? -23.99314 -31.67547 4.43015   1.000 21.77431 ? 286 LEU   A O   1 
ATOM   2198 C CB  . LEU   A 1 286 ? -23.15766 -32.88661 1.52592   1.000 28.60836 ? 286 LEU   A CB  1 
ATOM   2199 C CG  . LEU   A 1 286 ? -23.46726 -33.60183 0.20984   1.000 28.07105 ? 286 LEU   A CG  1 
ATOM   2200 C CD1 . LEU   A 1 286 ? -22.81558 -32.87789 -0.96300  1.000 27.77288 ? 286 LEU   A CD1 1 
ATOM   2201 C CD2 . LEU   A 1 286 ? -23.04815 -35.07768 0.26895   1.000 27.69586 ? 286 LEU   A CD2 1 
ATOM   2202 N N   . LEU   A 1 287 ? -22.19622 -33.01646 4.56386   1.000 22.25962 ? 287 LEU   A N   1 
ATOM   2203 C CA  . LEU   A 1 287 ? -21.61869 -32.23109 5.64474   1.000 21.01818 ? 287 LEU   A CA  1 
ATOM   2204 C C   . LEU   A 1 287 ? -21.09328 -30.91110 5.09090   1.000 18.67003 ? 287 LEU   A C   1 
ATOM   2205 O O   . LEU   A 1 287 ? -20.28570 -30.89319 4.16284   1.000 25.33626 ? 287 LEU   A O   1 
ATOM   2206 C CB  . LEU   A 1 287 ? -20.51007 -33.01500 6.34896   1.000 19.69574 ? 287 LEU   A CB  1 
ATOM   2207 C CG  . LEU   A 1 287 ? -21.00003 -34.29919 7.01890   1.000 22.90336 ? 287 LEU   A CG  1 
ATOM   2208 C CD1 . LEU   A 1 287 ? -19.82336 -35.18188 7.42328   1.000 27.00683 ? 287 LEU   A CD1 1 
ATOM   2209 C CD2 . LEU   A 1 287 ? -21.90910 -34.01930 8.21219   1.000 21.23644 ? 287 LEU   A CD2 1 
ATOM   2210 N N   . GLU   A 1 288 ? -21.54091 -29.80687 5.67045   1.000 17.22997 ? 288 GLU   A N   1 
ATOM   2211 C CA  . GLU   A 1 288 ? -21.35940 -28.47630 5.10205   1.000 18.84025 ? 288 GLU   A CA  1 
ATOM   2212 C C   . GLU   A 1 288 ? -20.17988 -27.77192 5.76531   1.000 17.64365 ? 288 GLU   A C   1 
ATOM   2213 O O   . GLU   A 1 288 ? -20.07700 -27.76027 6.99443   1.000 15.01542 ? 288 GLU   A O   1 
ATOM   2214 C CB  . GLU   A 1 288 ? -22.65540 -27.66892 5.27366   1.000 18.44990 ? 288 GLU   A CB  1 
ATOM   2215 C CG  . GLU   A 1 288 ? -22.53299 -26.20024 4.99232   1.000 21.67301 ? 288 GLU   A CG  1 
ATOM   2216 C CD  . GLU   A 1 288 ? -22.47370 -25.89337 3.48959   1.000 25.60096 ? 288 GLU   A CD  1 
ATOM   2217 O OE1 . GLU   A 1 288 ? -23.40892 -26.31711 2.74717   1.000 29.07884 ? 288 GLU   A OE1 1 
ATOM   2218 O OE2 . GLU   A 1 288 ? -21.52130 -25.18217 3.06351   1.000 15.84254 ? 288 GLU   A OE2 1 
ATOM   2219 N N   . ASP   A 1 289 ? -19.28772 -27.18272 4.95988   1.000 16.81942 ? 289 ASP   A N   1 
ATOM   2220 C CA  . ASP   A 1 289 ? -18.07684 -26.58887 5.52228   1.000 15.59841 ? 289 ASP   A CA  1 
ATOM   2221 C C   . ASP   A 1 289 ? -17.90271 -25.11221 5.20336   1.000 15.58722 ? 289 ASP   A C   1 
ATOM   2222 O O   . ASP   A 1 289 ? -16.80516 -24.58374 5.40911   1.000 12.43452 ? 289 ASP   A O   1 
ATOM   2223 C CB  . ASP   A 1 289 ? -16.81415 -27.35538 5.09044   1.000 17.04392 ? 289 ASP   A CB  1 
ATOM   2224 C CG  . ASP   A 1 289 ? -16.41753 -27.12582 3.61594   1.000 18.66001 ? 289 ASP   A CG  1 
ATOM   2225 O OD1 . ASP   A 1 289 ? -17.19422 -26.56353 2.82076   1.000 15.88201 ? 289 ASP   A OD1 1 
ATOM   2226 O OD2 . ASP   A 1 289 ? -15.29500 -27.53958 3.24193   1.000 19.21813 ? 289 ASP   A OD2 1 
ATOM   2227 N N   . GLU   A 1 290 ? -18.93143 -24.41301 4.71875   1.000 11.98652 ? 290 GLU   A N   1 
ATOM   2228 C CA  . GLU   A 1 290 ? -18.74955 -22.99214 4.45468   1.000 13.96495 ? 290 GLU   A CA  1 
ATOM   2229 C C   . GLU   A 1 290 ? -19.43846 -22.09899 5.48916   1.000 14.95847 ? 290 GLU   A C   1 
ATOM   2230 O O   . GLU   A 1 290 ? -19.81009 -20.96282 5.17767   1.000 13.66574 ? 290 GLU   A O   1 
ATOM   2231 C CB  . GLU   A 1 290 ? -19.18263 -22.65338 3.02606   1.000 16.40159 ? 290 GLU   A CB  1 
ATOM   2232 C CG  . GLU   A 1 290 ? -18.36727 -23.46356 1.99182   1.000 15.44023 ? 290 GLU   A CG  1 
ATOM   2233 C CD  . GLU   A 1 290 ? -18.02620 -22.71074 0.70722   1.000 16.25983 ? 290 GLU   A CD  1 
ATOM   2234 O OE1 . GLU   A 1 290 ? -17.11273 -23.16818 -0.03443  1.000 16.99550 ? 290 GLU   A OE1 1 
ATOM   2235 O OE2 . GLU   A 1 290 ? -18.65020 -21.66631 0.43300   1.000 15.59359 ? 290 GLU   A OE2 1 
ATOM   2236 N N   . PHE   A 1 291 ? -19.58372 -22.58660 6.72890   1.000 12.08921 ? 291 PHE   A N   1 
ATOM   2237 C CA  . PHE   A 1 291 ? -19.89813 -21.75756 7.89405   1.000 12.49110 ? 291 PHE   A CA  1 
ATOM   2238 C C   . PHE   A 1 291 ? -18.73692 -21.80882 8.89609   1.000 15.21283 ? 291 PHE   A C   1 
ATOM   2239 O O   . PHE   A 1 291 ? -18.38634 -22.88869 9.37745   1.000 13.43953 ? 291 PHE   A O   1 
ATOM   2240 C CB  . PHE   A 1 291 ? -21.18451 -22.24265 8.56740   1.000 14.14789 ? 291 PHE   A CB  1 
ATOM   2241 C CG  . PHE   A 1 291 ? -22.42964 -22.08034 7.71762   1.000 14.89969 ? 291 PHE   A CG  1 
ATOM   2242 C CD1 . PHE   A 1 291 ? -23.03784 -20.84357 7.58613   1.000 17.58710 ? 291 PHE   A CD1 1 
ATOM   2243 C CD2 . PHE   A 1 291 ? -22.98220 -23.17478 7.03903   1.000 14.58023 ? 291 PHE   A CD2 1 
ATOM   2244 C CE1 . PHE   A 1 291 ? -24.20856 -20.68946 6.80568   1.000 15.82200 ? 291 PHE   A CE1 1 
ATOM   2245 C CE2 . PHE   A 1 291 ? -24.12453 -23.03051 6.25964   1.000 16.83580 ? 291 PHE   A CE2 1 
ATOM   2246 C CZ  . PHE   A 1 291 ? -24.73963 -21.78329 6.14886   1.000 14.95318 ? 291 PHE   A CZ  1 
ATOM   2247 N N   . THR   A 1 292 ? -18.17377 -20.64457 9.24350   1.000 13.57151 ? 292 THR   A N   1 
ATOM   2248 C CA  . THR   A 1 292 ? -17.18314 -20.53473 10.30968  1.000 15.95554 ? 292 THR   A CA  1 
ATOM   2249 C C   . THR   A 1 292 ? -17.85004 -20.53373 11.68987  1.000 17.84262 ? 292 THR   A C   1 
ATOM   2250 O O   . THR   A 1 292 ? -19.06142 -20.31299 11.80821  1.000 14.22211 ? 292 THR   A O   1 
ATOM   2251 C CB  . THR   A 1 292 ? -16.36787 -19.25193 10.14673  1.000 17.88456 ? 292 THR   A CB  1 
ATOM   2252 O OG1 . THR   A 1 292 ? -17.24493 -18.11750 10.20013  1.000 16.98332 ? 292 THR   A OG1 1 
ATOM   2253 C CG2 . THR   A 1 292 ? -15.63667 -19.24757 8.82982   1.000 15.71456 ? 292 THR   A CG2 1 
ATOM   2254 N N   . PRO   A 1 293 ? -17.07673 -20.77912 12.76154  1.000 16.37354 ? 293 PRO   A N   1 
ATOM   2255 C CA  . PRO   A 1 293 ? -17.65680 -20.64093 14.10960  1.000 17.83813 ? 293 PRO   A CA  1 
ATOM   2256 C C   . PRO   A 1 293 ? -18.24303 -19.26334 14.35824  1.000 18.65017 ? 293 PRO   A C   1 
ATOM   2257 O O   . PRO   A 1 293 ? -19.26589 -19.13821 15.05458  1.000 17.65230 ? 293 PRO   A O   1 
ATOM   2258 C CB  . PRO   A 1 293 ? -16.46312 -20.93243 15.03683  1.000 17.11393 ? 293 PRO   A CB  1 
ATOM   2259 C CG  . PRO   A 1 293 ? -15.60936 -21.82439 14.23544  1.000 17.85076 ? 293 PRO   A CG  1 
ATOM   2260 C CD  . PRO   A 1 293 ? -15.68109 -21.24236 12.83385  1.000 17.05311 ? 293 PRO   A CD  1 
ATOM   2261 N N   . PHE   A 1 294 ? -17.63638 -18.22296 13.77926  1.000 18.43430 ? 294 PHE   A N   1 
ATOM   2262 C CA  . PHE   A 1 294 ? -18.20026 -16.88532 13.91519  1.000 19.51116 ? 294 PHE   A CA  1 
ATOM   2263 C C   . PHE   A 1 294 ? -19.51703 -16.76339 13.16463  1.000 18.76177 ? 294 PHE   A C   1 
ATOM   2264 O O   . PHE   A 1 294 ? -20.43093 -16.07616 13.62907  1.000 21.14324 ? 294 PHE   A O   1 
ATOM   2265 C CB  . PHE   A 1 294 ? -17.20108 -15.84462 13.42488  1.000 19.47461 ? 294 PHE   A CB  1 
ATOM   2266 C CG  . PHE   A 1 294 ? -17.76775 -14.45780 13.33090  1.000 24.99776 ? 294 PHE   A CG  1 
ATOM   2267 C CD1 . PHE   A 1 294 ? -17.70966 -13.59573 14.41941  1.000 26.01565 ? 294 PHE   A CD1 1 
ATOM   2268 C CD2 . PHE   A 1 294 ? -18.34517 -14.00159 12.14602  1.000 26.80115 ? 294 PHE   A CD2 1 
ATOM   2269 C CE1 . PHE   A 1 294 ? -18.23028 -12.31038 14.34076  1.000 24.70116 ? 294 PHE   A CE1 1 
ATOM   2270 C CE2 . PHE   A 1 294 ? -18.86923 -12.70243 12.05774  1.000 29.65961 ? 294 PHE   A CE2 1 
ATOM   2271 C CZ  . PHE   A 1 294 ? -18.80103 -11.86228 13.15973  1.000 26.89169 ? 294 PHE   A CZ  1 
ATOM   2272 N N   . ASP   A 1 295 ? -19.63558 -17.41754 12.00305  1.000 17.05157 ? 295 ASP   A N   1 
ATOM   2273 C CA  . ASP   A 1 295 ? -20.87234 -17.32921 11.22559  1.000 17.25506 ? 295 ASP   A CA  1 
ATOM   2274 C C   . ASP   A 1 295 ? -22.05122 -17.86504 12.02020  1.000 21.11698 ? 295 ASP   A C   1 
ATOM   2275 O O   . ASP   A 1 295 ? -23.13866 -17.27610 12.02682  1.000 18.54370 ? 295 ASP   A O   1 
ATOM   2276 C CB  . ASP   A 1 295 ? -20.74440 -18.11166 9.92785   1.000 15.02057 ? 295 ASP   A CB  1 
ATOM   2277 C CG  . ASP   A 1 295 ? -19.77338 -17.48253 8.96544   1.000 16.49640 ? 295 ASP   A CG  1 
ATOM   2278 O OD1 . ASP   A 1 295 ? -19.44209 -16.28922 9.17041   1.000 16.31423 ? 295 ASP   A OD1 1 
ATOM   2279 O OD2 . ASP   A 1 295 ? -19.34993 -18.18222 8.00636   1.000 13.47373 ? 295 ASP   A OD2 1 
ATOM   2280 N N   . VAL   A 1 296 ? -21.84171 -18.99728 12.69060  1.000 17.88892 ? 296 VAL   A N   1 
ATOM   2281 C CA  . VAL   A 1 296 ? -22.90079 -19.65395 13.43728  1.000 20.30198 ? 296 VAL   A CA  1 
ATOM   2282 C C   . VAL   A 1 296 ? -23.35200 -18.78999 14.61620  1.000 21.28081 ? 296 VAL   A C   1 
ATOM   2283 O O   . VAL   A 1 296 ? -24.54899 -18.58113 14.82490  1.000 23.50219 ? 296 VAL   A O   1 
ATOM   2284 C CB  . VAL   A 1 296 ? -22.42868 -21.04576 13.89103  1.000 15.52980 ? 296 VAL   A CB  1 
ATOM   2285 C CG1 . VAL   A 1 296 ? -23.49060 -21.68801 14.75221  1.000 17.60324 ? 296 VAL   A CG1 1 
ATOM   2286 C CG2 . VAL   A 1 296 ? -22.12815 -21.90424 12.66769  1.000 13.48541 ? 296 VAL   A CG2 1 
ATOM   2287 N N   . VAL   A 1 297 ? -22.39982 -18.29221 15.41419  1.000 22.69864 ? 297 VAL   A N   1 
ATOM   2288 C CA  . VAL   A 1 297 ? -22.73873 -17.39783 16.52127  1.000 22.39314 ? 297 VAL   A CA  1 
ATOM   2289 C C   . VAL   A 1 297 ? -23.53447 -16.18781 16.02185  1.000 25.60910 ? 297 VAL   A C   1 
ATOM   2290 O O   . VAL   A 1 297 ? -24.54288 -15.80126 16.62624  1.000 26.13280 ? 297 VAL   A O   1 
ATOM   2291 C CB  . VAL   A 1 297 ? -21.46195 -16.96726 17.26254  1.000 20.95010 ? 297 VAL   A CB  1 
ATOM   2292 C CG1 . VAL   A 1 297 ? -21.75924 -15.81260 18.19085  1.000 22.01765 ? 297 VAL   A CG1 1 
ATOM   2293 C CG2 . VAL   A 1 297 ? -20.87539 -18.13654 18.04136  1.000 24.58811 ? 297 VAL   A CG2 1 
ATOM   2294 N N   . ARG   A 1 298 ? -23.09705 -15.57926 14.90949  1.000 21.96286 ? 298 ARG   A N   1 
ATOM   2295 C CA  . ARG   A 1 298 ? -23.76617 -14.39434 14.37576  1.000 24.50737 ? 298 ARG   A CA  1 
ATOM   2296 C C   . ARG   A 1 298 ? -25.21442 -14.69592 14.02527  1.000 28.11151 ? 298 ARG   A C   1 
ATOM   2297 O O   . ARG   A 1 298 ? -26.12304 -13.93292 14.37528  1.000 31.94181 ? 298 ARG   A O   1 
ATOM   2298 C CB  . ARG   A 1 298 ? -23.03169 -13.86347 13.12806  1.000 24.03867 ? 298 ARG   A CB  1 
ATOM   2299 C CG  . ARG   A 1 298 ? -23.96015 -13.04066 12.17662  1.000 26.14086 ? 298 ARG   A CG  1 
ATOM   2300 C CD  . ARG   A 1 298 ? -23.26436 -12.36421 10.92355  1.000 32.94085 ? 298 ARG   A CD  1 
ATOM   2301 N NE  . ARG   A 1 298 ? -22.98069 -13.28437 9.80984   1.000 32.90090 ? 298 ARG   A NE  1 
ATOM   2302 C CZ  . ARG   A 1 298 ? -23.48833 -13.18231 8.57660   1.000 25.73140 ? 298 ARG   A CZ  1 
ATOM   2303 N NH1 . ARG   A 1 298 ? -24.29809 -12.19198 8.25803   1.000 24.95353 ? 298 ARG   A NH1 1 
ATOM   2304 N NH2 . ARG   A 1 298 ? -23.16582 -14.07208 7.64727   1.000 24.81739 ? 298 ARG   A NH2 1 
ATOM   2305 N N   . GLN   A 1 299 ? -25.44811 -15.80048 13.31574  1.000 24.54387 ? 299 GLN   A N   1 
ATOM   2306 C CA  . GLN   A 1 299 ? -26.78779 -16.06874 12.81069  1.000 28.10426 ? 299 GLN   A CA  1 
ATOM   2307 C C   . GLN   A 1 299 ? -27.68053 -16.64963 13.89969  1.000 30.96854 ? 299 GLN   A C   1 
ATOM   2308 O O   . GLN   A 1 299 ? -28.85384 -16.27069 14.00761  1.000 30.39543 ? 299 GLN   A O   1 
ATOM   2309 C CB  . GLN   A 1 299 ? -26.71843 -16.99627 11.58732  1.000 25.65838 ? 299 GLN   A CB  1 
ATOM   2310 C CG  . GLN   A 1 299 ? -28.09826 -17.50145 11.11699  1.000 23.68560 ? 299 GLN   A CG  1 
ATOM   2311 C CD  . GLN   A 1 299 ? -28.08535 -18.16732 9.74756   1.000 22.33844 ? 299 GLN   A CD  1 
ATOM   2312 O OE1 . GLN   A 1 299 ? -29.13433 -18.59056 9.25138   1.000 22.68352 ? 299 GLN   A OE1 1 
ATOM   2313 N NE2 . GLN   A 1 299 ? -26.91024 -18.26071 9.12867   1.000 17.22883 ? 299 GLN   A NE2 1 
ATOM   2314 N N   . CYS   A 1 300 ? -27.15412 -17.57089 14.71454  1.000 28.14111 ? 300 CYS   A N   1 
ATOM   2315 C CA  . CYS   A 1 300 ? -27.97538 -18.21241 15.73337  1.000 27.94706 ? 300 CYS   A CA  1 
ATOM   2316 C C   . CYS   A 1 300 ? -28.24886 -17.30591 16.93244  1.000 33.14247 ? 300 CYS   A C   1 
ATOM   2317 O O   . CYS   A 1 300 ? -29.10223 -17.64986 17.76415  1.000 31.78218 ? 300 CYS   A O   1 
ATOM   2318 C CB  . CYS   A 1 300 ? -27.32080 -19.52601 16.18077  1.000 30.56762 ? 300 CYS   A CB  1 
ATOM   2319 S SG  . CYS   A 1 300 ? -27.27875 -20.80596 14.85245  1.000 25.46220 ? 300 CYS   A SG  1 
ATOM   2320 N N   . SER   A 1 301 ? -27.58223 -16.14353 17.01706  1.000 32.91730 ? 301 SER   A N   1 
ATOM   2321 C CA  . SER   A 1 301 ? -27.71383 -15.19230 18.12439  1.000 35.52068 ? 301 SER   A CA  1 
ATOM   2322 C C   . SER   A 1 301 ? -28.14540 -13.80014 17.68490  1.000 35.44047 ? 301 SER   A C   1 
ATOM   2323 O O   . SER   A 1 301 ? -28.87349 -13.12568 18.41973  1.000 36.85150 ? 301 SER   A O   1 
ATOM   2324 C CB  . SER   A 1 301 ? -26.38903 -15.09089 18.90470  1.000 39.47115 ? 301 SER   A CB  1 
ATOM   2325 O OG  . SER   A 1 301 ? -26.39051 -13.97306 19.78085  1.000 45.56997 ? 301 SER   A OG  1 
ATOM   2326 N N   . GLY   A 1 302 ? -27.70637 -13.33532 16.51520  1.000 38.01158 ? 302 GLY   A N   1 
ATOM   2327 C CA  . GLY   A 1 302 ? -28.37551 -12.20862 15.87898  1.000 40.03655 ? 302 GLY   A CA  1 
ATOM   2328 C C   . GLY   A 1 302 ? -27.65508 -10.87399 15.86816  1.000 42.99763 ? 302 GLY   A C   1 
ATOM   2329 O O   . GLY   A 1 302 ? -28.25616 -9.84119  16.18989  1.000 41.28214 ? 302 GLY   A O   1 
ATOM   2330 N N   . VAL   A 1 303 ? -26.37891 -10.87774 15.47547  1.000 42.85443 ? 303 VAL   A N   1 
ATOM   2331 C CA  . VAL   A 1 303 ? -25.57826 -9.65642  15.43217  1.000 46.29772 ? 303 VAL   A CA  1 
ATOM   2332 C C   . VAL   A 1 303 ? -25.91988 -8.87958  14.16248  1.000 44.73961 ? 303 VAL   A C   1 
ATOM   2333 O O   . VAL   A 1 303 ? -26.15668 -9.47124  13.10071  1.000 43.70090 ? 303 VAL   A O   1 
ATOM   2334 C CB  . VAL   A 1 303 ? -24.07489 -10.00202 15.51691  1.000 44.15707 ? 303 VAL   A CB  1 
ATOM   2335 C CG1 . VAL   A 1 303 ? -23.19829 -8.76713  15.26622  1.000 47.46576 ? 303 VAL   A CG1 1 
ATOM   2336 C CG2 . VAL   A 1 303 ? -23.74346 -10.63856 16.87079  1.000 37.50337 ? 303 VAL   A CG2 1 
ATOM   2337 N N   . THR   A 1 304 ? -25.96541 -7.54745  14.26693  1.000 45.69024 ? 304 THR   A N   1 
ATOM   2338 C CA  . THR   A 1 304 ? -26.29826 -6.67271  13.14377  1.000 44.33362 ? 304 THR   A CA  1 
ATOM   2339 C C   . THR   A 1 304 ? -25.17248 -5.66559  12.88451  1.000 51.37252 ? 304 THR   A C   1 
ATOM   2340 O O   . THR   A 1 304 ? -24.07545 -5.75102  13.45489  1.000 51.86094 ? 304 THR   A O   1 
ATOM   2341 C CB  . THR   A 1 304 ? -27.60637 -5.91564  13.39501  1.000 42.82864 ? 304 THR   A CB  1 
ATOM   2342 O OG1 . THR   A 1 304 ? -27.36918 -4.88208  14.36304  1.000 47.05162 ? 304 THR   A OG1 1 
ATOM   2343 C CG2 . THR   A 1 304 ? -28.70539 -6.85960  13.90282  1.000 35.19993 ? 304 THR   A CG2 1 
ATOM   2344 N N   . PHE   A 1 305 ? -25.47941 -4.69770  12.01403  1.000 52.18760 ? 305 PHE   A N   1 
ATOM   2345 C CA  . PHE   A 1 305 ? -24.59452 -3.61719  11.58141  1.000 53.63608 ? 305 PHE   A CA  1 
ATOM   2346 C C   . PHE   A 1 305 ? -25.47675 -2.43274  11.20257  1.000 56.75139 ? 305 PHE   A C   1 
ATOM   2347 O O   . PHE   A 1 305 ? -26.66450 -2.59960  10.90606  1.000 53.91758 ? 305 PHE   A O   1 
ATOM   2348 C CB  . PHE   A 1 305 ? -23.71586 -4.05873  10.39957  1.000 49.97252 ? 305 PHE   A CB  1 
ATOM   2349 C CG  . PHE   A 1 305 ? -23.19587 -5.45300  10.54818  1.000 47.40559 ? 305 PHE   A CG  1 
ATOM   2350 C CD1 . PHE   A 1 305 ? -22.04197 -5.69515  11.27576  1.000 46.66111 ? 305 PHE   A CD1 1 
ATOM   2351 C CD2 . PHE   A 1 305 ? -23.90985 -6.53175  10.03525  1.000 42.79414 ? 305 PHE   A CD2 1 
ATOM   2352 C CE1 . PHE   A 1 305 ? -21.58048 -6.98253  11.45692  1.000 44.90943 ? 305 PHE   A CE1 1 
ATOM   2353 C CE2 . PHE   A 1 305 ? -23.45973 -7.81591  10.21303  1.000 42.77588 ? 305 PHE   A CE2 1 
ATOM   2354 C CZ  . PHE   A 1 305 ? -22.28651 -8.04208  10.92682  1.000 45.06974 ? 305 PHE   A CZ  1 
ATOM   2355 N N   . GLN   A 1 306 ? -24.90989 -1.22921  11.21614  1.000 58.50097 ? 306 GLN   A N   1 
ATOM   2356 C CA  . GLN   A 1 306 ? -25.77845 -0.06534  10.99779  1.000 64.01152 ? 306 GLN   A CA  1 
ATOM   2357 C C   . GLN   A 1 306 ? -25.19606 1.02232   10.08694  1.000 62.13219 ? 306 GLN   A C   1 
ATOM   2358 O O   . GLN   A 1 306 ? -25.02798 0.81754   8.88071   1.000 58.87714 ? 306 GLN   A O   1 
ATOM   2359 C CB  . GLN   A 1 306 ? -26.16841 0.54870   12.34744  1.000 63.84855 ? 306 GLN   A CB  1 
ATOM   2360 C CG  . GLN   A 1 306 ? -27.31386 1.54310   12.24753  1.000 66.03781 ? 306 GLN   A CG  1 
ATOM   2361 C CD  . GLN   A 1 306 ? -27.91405 1.86658   13.59115  1.000 67.72981 ? 306 GLN   A CD  1 
ATOM   2362 O OE1 . GLN   A 1 306 ? -27.48463 1.33507   14.61515  1.000 72.22949 ? 306 GLN   A OE1 1 
ATOM   2363 N NE2 . GLN   A 1 306 ? -28.90992 2.74633   13.60107  1.000 67.56165 ? 306 GLN   A NE2 1 
HETATM 2364 N N   . A1ARI B 2 .   ? -9.79863  -15.28972 -18.18185 1.000 26.02118 ? 401 A1ARI A N   1 
HETATM 2365 C C   . A1ARI B 2 .   ? -10.14716 -17.64672 -18.34013 1.000 25.29493 ? 401 A1ARI A C   1 
HETATM 2366 O O   . A1ARI B 2 .   ? -10.83639 -16.30529 -16.46602 1.000 24.19731 ? 401 A1ARI A O   1 
HETATM 2367 C C1  . A1ARI B 2 .   ? -10.29608 -16.36148 -17.57731 1.000 26.05718 ? 401 A1ARI A C1  1 
HETATM 2368 C C10 . A1ARI B 2 .   ? -14.98200 -15.67786 -14.96955 1.000 18.52782 ? 401 A1ARI A C10 1 
HETATM 2369 C C11 . A1ARI B 2 .   ? -9.09826  -12.97914 -18.35508 1.000 28.80495 ? 401 A1ARI A C11 1 
HETATM 2370 C C12 . A1ARI B 2 .   ? -7.74882  -12.59588 -17.73374 1.000 32.08520 ? 401 A1ARI A C12 1 
HETATM 2371 C C13 . A1ARI B 2 .   ? -11.52618 -18.23027 -18.67177 1.000 26.63372 ? 401 A1ARI A C13 1 
HETATM 2372 C C14 . A1ARI B 2 .   ? -12.43871 -17.16263 -19.28894 1.000 26.73320 ? 401 A1ARI A C14 1 
HETATM 2373 C C15 . A1ARI B 2 .   ? -8.06635  -18.83927 -17.77079 1.000 30.44693 ? 401 A1ARI A C15 1 
HETATM 2374 C C16 . A1ARI B 2 .   ? -6.16254  -20.23925 -17.16243 1.000 31.49640 ? 401 A1ARI A C16 1 
HETATM 2375 C C17 . A1ARI B 2 .   ? -12.03712 -20.55431 -19.29261 1.000 29.85633 ? 401 A1ARI A C17 1 
HETATM 2376 C C18 . A1ARI B 2 .   ? -11.17531 -21.28144 -18.26558 1.000 29.70326 ? 401 A1ARI A C18 1 
HETATM 2377 C C19 . A1ARI B 2 .   ? -12.12901 -21.37360 -20.57421 1.000 29.39405 ? 401 A1ARI A C19 1 
HETATM 2378 C C2  . A1ARI B 2 .   ? -9.91179  -13.99354 -17.55018 1.000 25.42591 ? 401 A1ARI A C2  1 
HETATM 2379 C C20 . A1ARI B 2 .   ? -13.46009 -20.40500 -18.75406 1.000 25.16573 ? 401 A1ARI A C20 1 
HETATM 2380 C C21 . A1ARI B 2 .   ? -6.71473  -12.42856 -18.84835 1.000 37.62189 ? 401 A1ARI A C21 1 
HETATM 2381 C C22 . A1ARI B 2 .   ? -5.30727  -12.07025 -18.37171 1.000 35.82003 ? 401 A1ARI A C22 1 
HETATM 2382 C C23 . A1ARI B 2 .   ? -5.04087  -12.54037 -16.94970 1.000 33.77313 ? 401 A1ARI A C23 1 
HETATM 2383 C C24 . A1ARI B 2 .   ? -5.76796  -13.84809 -16.68959 1.000 34.28661 ? 401 A1ARI A C24 1 
HETATM 2384 C C25 . A1ARI B 2 .   ? -7.28282  -13.64738 -16.72372 1.000 29.92794 ? 401 A1ARI A C25 1 
HETATM 2385 C C26 . A1ARI B 2 .   ? -6.37306  -21.68441 -17.58841 1.000 30.58542 ? 401 A1ARI A C26 1 
HETATM 2386 C C27 . A1ARI B 2 .   ? -5.24994  -20.21818 -15.94996 1.000 32.85521 ? 401 A1ARI A C27 1 
HETATM 2387 C C3  . A1ARI B 2 .   ? -11.35959 -13.60178 -17.47010 1.000 25.04342 ? 401 A1ARI A C3  1 
HETATM 2388 C C4  . A1ARI B 2 .   ? -13.16257 -12.56789 -16.39701 1.000 23.89880 ? 401 A1ARI A C4  1 
HETATM 2389 C C5  . A1ARI B 2 .   ? -13.10777 -11.06910 -16.09956 1.000 22.04001 ? 401 A1ARI A C5  1 
HETATM 2390 C C6  . A1ARI B 2 .   ? -14.05371 -13.38206 -15.45657 1.000 20.55335 ? 401 A1ARI A C6  1 
HETATM 2391 C C7  . A1ARI B 2 .   ? -14.15720 -14.84575 -15.90638 1.000 19.61504 ? 401 A1ARI A C7  1 
HETATM 2392 C C8  . A1ARI B 2 .   ? -14.90274 -14.99841 -17.23753 1.000 20.43973 ? 401 A1ARI A C8  1 
HETATM 2393 C C9  . A1ARI B 2 .   ? -15.78831 -16.23180 -17.06507 1.000 19.61281 ? 401 A1ARI A C9  1 
HETATM 2394 N N1  . A1ARI B 2 .   ? -11.80765 -13.06932 -16.34295 1.000 23.48396 ? 401 A1ARI A N1  1 
HETATM 2395 N N2  . A1ARI B 2 .   ? -15.85346 -16.42801 -15.63441 1.000 20.35261 ? 401 A1ARI A N2  1 
HETATM 2396 N N3  . A1ARI B 2 .   ? -9.35454  -18.56713 -17.55032 1.000 27.24380 ? 401 A1ARI A N3  1 
HETATM 2397 O O1  . A1ARI B 2 .   ? -12.11976 -13.77890 -18.40847 1.000 26.98220 ? 401 A1ARI A O1  1 
HETATM 2398 O O2  . A1ARI B 2 .   ? -14.40511 -10.47177 -16.00318 1.000 23.41006 ? 401 A1ARI A O2  1 
HETATM 2399 O O3  . A1ARI B 2 .   ? -14.85424 -15.65593 -13.75476 1.000 16.82104 ? 401 A1ARI A O3  1 
HETATM 2400 O O4  . A1ARI B 2 .   ? -11.40864 -19.30147 -19.61280 1.000 28.91316 ? 401 A1ARI A O4  1 
HETATM 2401 O O5  . A1ARI B 2 .   ? -7.39763  -19.64651 -16.76557 1.000 30.04206 ? 401 A1ARI A O5  1 
HETATM 2402 O O6  . A1ARI B 2 .   ? -7.43019  -18.45014 -18.73733 1.000 34.80743 ? 401 A1ARI A O6  1 
HETATM 2403 O O   . HOH   C 3 .   ? -4.31621  -24.38127 -5.19083  1.000 18.36916 ? 501 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? -24.10375 -28.25343 2.30209   1.000 32.02842 ? 502 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? -13.22964 8.45148   -17.09201 1.000 37.62068 ? 503 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? -1.63318  -24.74130 -11.99444 1.000 42.76093 ? 504 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? -7.24519  -3.46105  -22.00753 1.000 42.87243 ? 505 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? -30.29712 -18.74455 19.23479  1.000 34.34817 ? 506 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? -4.51721  8.64650   -3.97821  1.000 46.02131 ? 507 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? 5.13086   -5.74674  -11.98101 1.000 32.58254 ? 508 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? -18.78746 -14.32937 6.15371   1.000 14.87895 ? 509 HOH   A O   1 
HETATM 2412 O O   . HOH   C 3 .   ? -27.43551 -12.14897 -11.05493 1.000 39.98638 ? 510 HOH   A O   1 
HETATM 2413 O O   . HOH   C 3 .   ? -31.88402 -34.14745 15.14786  1.000 46.25805 ? 511 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? -5.97991  -33.74134 7.55016   1.000 34.61677 ? 512 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? -6.24723  -26.11955 8.81041   1.000 36.91605 ? 513 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? -27.02403 -3.11586  8.60274   1.000 37.28327 ? 514 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? -6.85486  -21.23233 7.76879   1.000 33.33363 ? 515 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? -3.54294  -12.31119 6.18653   1.000 15.00337 ? 516 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? -7.73346  13.34193  -6.36562  1.000 37.48347 ? 517 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? -24.28532 -18.57769 19.86646  1.000 38.71700 ? 518 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? -27.36526 -1.41369  -6.09685  1.000 45.81605 ? 519 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? -5.96476  -0.80439  -24.07464 1.000 34.36820 ? 520 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? -8.76570  4.57209   -1.50124  1.000 22.82780 ? 521 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? 4.15590   -8.53514  -6.19318  1.000 13.38241 ? 522 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? -27.95326 -19.17404 19.36570  1.000 37.47377 ? 523 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? -12.87589 -27.44547 -4.12044  1.000 23.41971 ? 524 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? -17.80979 -34.84490 4.07970   1.000 27.12340 ? 525 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? -16.58725 2.43732   -18.22436 1.000 41.96003 ? 526 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? -17.06349 -41.72099 17.37916  1.000 44.11864 ? 527 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? -22.58155 -13.66797 -11.33954 1.000 23.54440 ? 528 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? -3.00455  2.21852   -1.67734  1.000 41.56043 ? 529 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? -17.20646 -21.16471 19.07392  1.000 25.96977 ? 530 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? -21.68861 -3.12653  1.89654   1.000 46.86326 ? 531 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? 1.56752   -10.05629 -5.30996  1.000 14.11474 ? 532 HOH   A O   1 
HETATM 2435 O O   . HOH   C 3 .   ? -19.60206 -24.96044 7.79711   1.000 16.73208 ? 533 HOH   A O   1 
HETATM 2436 O O   . HOH   C 3 .   ? -16.50962 -15.66304 9.71801   1.000 19.31372 ? 534 HOH   A O   1 
HETATM 2437 O O   . HOH   C 3 .   ? -31.94392 -19.05621 13.53376  1.000 22.85182 ? 535 HOH   A O   1 
HETATM 2438 O O   . HOH   C 3 .   ? -20.84081 -37.14159 20.33394  1.000 39.43197 ? 536 HOH   A O   1 
HETATM 2439 O O   . HOH   C 3 .   ? -0.43380  -11.79513 -6.90697  1.000 15.30801 ? 537 HOH   A O   1 
HETATM 2440 O O   . HOH   C 3 .   ? 0.25829   -16.32423 -6.66085  1.000 13.18418 ? 538 HOH   A O   1 
HETATM 2441 O O   . HOH   C 3 .   ? -9.69983  -19.95110 8.71755   1.000 21.11848 ? 539 HOH   A O   1 
HETATM 2442 O O   . HOH   C 3 .   ? -28.86705 -18.04053 0.95955   1.000 31.92777 ? 540 HOH   A O   1 
HETATM 2443 O O   . HOH   C 3 .   ? -20.00996 -26.87555 1.71301   1.000 30.76184 ? 541 HOH   A O   1 
HETATM 2444 O O   . HOH   C 3 .   ? -12.82165 -21.53722 9.81650   1.000 25.18932 ? 542 HOH   A O   1 
HETATM 2445 O O   . HOH   C 3 .   ? -18.45847 8.70674   3.08271   1.000 33.70784 ? 543 HOH   A O   1 
HETATM 2446 O O   . HOH   C 3 .   ? -4.90542  -23.55431 13.62430  1.000 28.35497 ? 544 HOH   A O   1 
HETATM 2447 O O   . HOH   C 3 .   ? -18.38678 -6.09445  -6.06688  1.000 11.89720 ? 545 HOH   A O   1 
HETATM 2448 O O   . HOH   C 3 .   ? -31.30626 -28.38565 13.64939  1.000 45.11316 ? 546 HOH   A O   1 
HETATM 2449 O O   . HOH   C 3 .   ? 0.13626   -14.05630 -3.12958  1.000 11.05158 ? 547 HOH   A O   1 
HETATM 2450 O O   . HOH   C 3 .   ? -31.33822 -16.34905 13.00099  1.000 29.42445 ? 548 HOH   A O   1 
HETATM 2451 O O   . HOH   C 3 .   ? -11.28814 -14.16307 -20.92920 1.000 30.74108 ? 549 HOH   A O   1 
HETATM 2452 O O   . HOH   C 3 .   ? -20.62860 -13.92508 8.50482   1.000 34.56862 ? 550 HOH   A O   1 
HETATM 2453 O O   . HOH   C 3 .   ? -21.56965 3.02730   -0.01941  1.000 27.42286 ? 551 HOH   A O   1 
HETATM 2454 O O   . HOH   C 3 .   ? -18.32524 -5.61304  -16.58840 1.000 25.53188 ? 552 HOH   A O   1 
HETATM 2455 O O   . HOH   C 3 .   ? 0.54832   -20.83805 -11.32414 1.000 25.34798 ? 553 HOH   A O   1 
HETATM 2456 O O   . HOH   C 3 .   ? -2.94035  -20.10344 8.50277   1.000 23.74563 ? 554 HOH   A O   1 
HETATM 2457 O O   . HOH   C 3 .   ? -16.05366 -21.28267 -1.80507  1.000 12.93957 ? 555 HOH   A O   1 
HETATM 2458 O O   . HOH   C 3 .   ? -20.99404 -20.50998 1.12127   1.000 15.60115 ? 556 HOH   A O   1 
HETATM 2459 O O   . HOH   C 3 .   ? -30.06276 -2.60705  -3.68611  1.000 19.92682 ? 557 HOH   A O   1 
HETATM 2460 O O   . HOH   C 3 .   ? -27.54211 0.61161   -3.25447  1.000 41.44117 ? 558 HOH   A O   1 
HETATM 2461 O O   . HOH   C 3 .   ? -4.56590  -1.50346  -2.69628  1.000 16.59812 ? 559 HOH   A O   1 
HETATM 2462 O O   . HOH   C 3 .   ? -17.40473 -28.22426 0.65630   1.000 36.05431 ? 560 HOH   A O   1 
HETATM 2463 O O   . HOH   C 3 .   ? -25.37462 -12.68646 -11.18551 1.000 29.12018 ? 561 HOH   A O   1 
HETATM 2464 O O   . HOH   C 3 .   ? -4.89777  -24.34503 3.07640   1.000 23.55834 ? 562 HOH   A O   1 
HETATM 2465 O O   . HOH   C 3 .   ? -8.59505  -25.89666 -12.31284 1.000 29.33818 ? 563 HOH   A O   1 
HETATM 2466 O O   . HOH   C 3 .   ? 0.61823   -12.53968 -11.37439 1.000 18.60690 ? 564 HOH   A O   1 
HETATM 2467 O O   . HOH   C 3 .   ? -6.63144  -28.62042 -10.05271 1.000 39.05764 ? 565 HOH   A O   1 
HETATM 2468 O O   . HOH   C 3 .   ? -35.17280 -24.56420 16.58504  1.000 35.97558 ? 566 HOH   A O   1 
HETATM 2469 O O   . HOH   C 3 .   ? -31.67678 -24.94527 6.75534   1.000 25.28769 ? 567 HOH   A O   1 
HETATM 2470 O O   . HOH   C 3 .   ? -7.45178  -7.21004  0.90983   1.000 8.38605  ? 568 HOH   A O   1 
HETATM 2471 O O   . HOH   C 3 .   ? -3.26565  -24.53785 18.14981  1.000 32.06221 ? 569 HOH   A O   1 
HETATM 2472 O O   . HOH   C 3 .   ? -20.73202 -23.88540 0.19016   1.000 21.55346 ? 570 HOH   A O   1 
HETATM 2473 O O   . HOH   C 3 .   ? -17.44810 -22.35038 -8.84762  1.000 16.14638 ? 571 HOH   A O   1 
HETATM 2474 O O   . HOH   C 3 .   ? -4.98843  -8.75711  -13.41527 1.000 16.74027 ? 572 HOH   A O   1 
HETATM 2475 O O   . HOH   C 3 .   ? -3.52286  -13.93443 8.63487   1.000 19.00828 ? 573 HOH   A O   1 
HETATM 2476 O O   . HOH   C 3 .   ? -17.83293 -6.25403  -19.67112 1.000 37.93589 ? 574 HOH   A O   1 
HETATM 2477 O O   . HOH   C 3 .   ? -3.00156  -24.68247 -0.00412  1.000 18.86319 ? 575 HOH   A O   1 
HETATM 2478 O O   . HOH   C 3 .   ? -30.78487 -29.57628 20.61892  1.000 29.60065 ? 576 HOH   A O   1 
HETATM 2479 O O   . HOH   C 3 .   ? -26.04541 -31.20751 25.39889  1.000 35.61159 ? 577 HOH   A O   1 
HETATM 2480 O O   . HOH   C 3 .   ? 3.97844   -4.48648  -4.19588  1.000 25.30954 ? 578 HOH   A O   1 
HETATM 2481 O O   . HOH   C 3 .   ? -0.03314  -16.76215 -2.72008  1.000 11.75693 ? 579 HOH   A O   1 
HETATM 2482 O O   . HOH   C 3 .   ? -16.65606 -33.03047 2.17113   1.000 29.28701 ? 580 HOH   A O   1 
HETATM 2483 O O   . HOH   C 3 .   ? -2.27557  -18.13206 4.83198   1.000 13.98639 ? 581 HOH   A O   1 
HETATM 2484 O O   . HOH   C 3 .   ? -32.71739 -31.13540 8.18507   1.000 26.27820 ? 582 HOH   A O   1 
HETATM 2485 O O   . HOH   C 3 .   ? -13.08161 -9.52327  5.07799   1.000 12.14393 ? 583 HOH   A O   1 
HETATM 2486 O O   . HOH   C 3 .   ? -14.09922 -16.34331 11.32204  1.000 23.14449 ? 584 HOH   A O   1 
HETATM 2487 O O   . HOH   C 3 .   ? -7.43852  -17.04564 -5.81176  1.000 10.09828 ? 585 HOH   A O   1 
HETATM 2488 O O   . HOH   C 3 .   ? -20.92623 -18.22484 5.64079   1.000 13.19016 ? 586 HOH   A O   1 
HETATM 2489 O O   . HOH   C 3 .   ? -6.08069  -21.88202 13.65112  1.000 32.05008 ? 587 HOH   A O   1 
HETATM 2490 O O   . HOH   C 3 .   ? -20.38264 2.80637   -20.62395 1.000 48.52307 ? 588 HOH   A O   1 
HETATM 2491 O O   . HOH   C 3 .   ? -19.64640 3.01563   7.09951   1.000 26.57558 ? 589 HOH   A O   1 
HETATM 2492 O O   . HOH   C 3 .   ? -3.92432  -16.26659 3.68890   1.000 12.40795 ? 590 HOH   A O   1 
HETATM 2493 O O   . HOH   C 3 .   ? -0.00000  -6.09536  0.00000   0.50  12.13125 ? 591 HOH   A O   1 
HETATM 2494 O O   . HOH   C 3 .   ? -4.74731  -21.83266 20.98644  1.000 38.51034 ? 592 HOH   A O   1 
HETATM 2495 O O   . HOH   C 3 .   ? -8.22006  -30.81919 22.70928  1.000 36.58289 ? 593 HOH   A O   1 
HETATM 2496 O O   . HOH   C 3 .   ? -25.69396 1.90606   -1.79649  1.000 25.44910 ? 594 HOH   A O   1 
HETATM 2497 O O   . HOH   C 3 .   ? -8.95265  -23.76896 6.43486   1.000 22.80086 ? 595 HOH   A O   1 
HETATM 2498 O O   . HOH   C 3 .   ? -14.08787 -8.44597  -18.07230 1.000 20.99006 ? 596 HOH   A O   1 
HETATM 2499 O O   . HOH   C 3 .   ? -21.57028 -19.64101 24.71740  1.000 36.15193 ? 597 HOH   A O   1 
HETATM 2500 O O   . HOH   C 3 .   ? 3.13010   -5.36201  -10.02390 1.000 21.47133 ? 598 HOH   A O   1 
HETATM 2501 O O   . HOH   C 3 .   ? -6.57933  -1.14331  4.83164   1.000 20.78519 ? 599 HOH   A O   1 
HETATM 2502 O O   . HOH   C 3 .   ? -9.54999  -18.82866 -21.84692 1.000 35.29459 ? 600 HOH   A O   1 
HETATM 2503 O O   . HOH   C 3 .   ? 3.83795   -3.82791  -7.89904  1.000 21.70652 ? 601 HOH   A O   1 
HETATM 2504 O O   . HOH   C 3 .   ? -13.98054 -29.10913 -2.22111  1.000 26.86157 ? 602 HOH   A O   1 
HETATM 2505 O O   . HOH   C 3 .   ? -14.43606 -43.53330 23.21506  1.000 38.44892 ? 603 HOH   A O   1 
HETATM 2506 O O   . HOH   C 3 .   ? -29.21928 -46.71026 3.65221   1.000 40.34209 ? 604 HOH   A O   1 
HETATM 2507 O O   . HOH   C 3 .   ? -24.19240 -17.10663 9.13221   1.000 18.40671 ? 605 HOH   A O   1 
HETATM 2508 O O   . HOH   C 3 .   ? -26.97123 -26.21940 5.81527   1.000 29.16264 ? 606 HOH   A O   1 
HETATM 2509 O O   . HOH   C 3 .   ? -30.21262 -9.51345  18.38250  1.000 35.27111 ? 607 HOH   A O   1 
HETATM 2510 O O   . HOH   C 3 .   ? -14.52301 -29.32678 24.94109  1.000 37.48907 ? 608 HOH   A O   1 
HETATM 2511 O O   . HOH   C 3 .   ? 2.97902   2.08190   -11.06219 1.000 24.48529 ? 609 HOH   A O   1 
HETATM 2512 O O   . HOH   C 3 .   ? -1.93133  -18.01636 -0.75300  1.000 12.75136 ? 610 HOH   A O   1 
HETATM 2513 O O   . HOH   C 3 .   ? -25.80846 -16.50401 0.40868   1.000 31.40063 ? 611 HOH   A O   1 
HETATM 2514 O O   . HOH   C 3 .   ? -20.52662 -35.11680 3.23472   1.000 26.61469 ? 612 HOH   A O   1 
HETATM 2515 O O   . HOH   C 3 .   ? -10.02234 -27.39820 10.31385  1.000 22.97515 ? 613 HOH   A O   1 
HETATM 2516 O O   . HOH   C 3 .   ? -12.95941 -34.18818 1.30142   1.000 30.55525 ? 614 HOH   A O   1 
HETATM 2517 O O   . HOH   C 3 .   ? -5.77556  2.16669   0.29767   1.000 38.99059 ? 615 HOH   A O   1 
HETATM 2518 O O   . HOH   C 3 .   ? -11.32255 -26.04749 -6.16383  1.000 22.99588 ? 616 HOH   A O   1 
HETATM 2519 O O   . HOH   C 3 .   ? -7.83853  -21.82974 10.72242  1.000 32.44660 ? 617 HOH   A O   1 
HETATM 2520 O O   . HOH   C 3 .   ? -2.37478  -30.63195 -5.55784  1.000 30.22430 ? 618 HOH   A O   1 
HETATM 2521 O O   . HOH   C 3 .   ? -23.64345 -17.35542 6.76549   1.000 16.55085 ? 619 HOH   A O   1 
HETATM 2522 O O   . HOH   C 3 .   ? 0.79103   -20.39914 -3.75803  1.000 17.51020 ? 620 HOH   A O   1 
HETATM 2523 O O   . HOH   C 3 .   ? -18.81315 -30.02591 1.63354   1.000 34.49975 ? 621 HOH   A O   1 
HETATM 2524 O O   . HOH   C 3 .   ? -4.24268  -40.54944 21.10446  1.000 42.57933 ? 622 HOH   A O   1 
HETATM 2525 O O   . HOH   C 3 .   ? -29.724   -13.608   12.746    1.000 49.26800 ? 623 HOH   A O   1 
HETATM 2526 O O   . HOH   C 3 .   ? 0.71206   -13.76198 -8.62993  1.000 18.60118 ? 624 HOH   A O   1 
HETATM 2527 O O   . HOH   C 3 .   ? -33.11947 -24.49988 8.90137   1.000 24.12949 ? 625 HOH   A O   1 
HETATM 2528 O O   . HOH   C 3 .   ? -20.521   -22.494   -7.250    1.000 43.61879 ? 626 HOH   A O   1 
HETATM 2529 O O   . HOH   C 3 .   ? -27.24210 -31.68407 0.00000   0.50  24.66675 ? 627 HOH   A O   1 
HETATM 2530 O O   . HOH   C 3 .   ? -11.83691 -18.46961 9.72455   1.000 28.09075 ? 628 HOH   A O   1 
HETATM 2531 O O   . HOH   C 3 .   ? -31.22510 -20.53392 15.64664  1.000 27.25278 ? 629 HOH   A O   1 
HETATM 2532 O O   . HOH   C 3 .   ? -34.93574 -19.04925 17.81481  1.000 22.51347 ? 630 HOH   A O   1 
HETATM 2533 O O   . HOH   C 3 .   ? -2.12181  -16.62083 1.62521   1.000 10.88701 ? 631 HOH   A O   1 
HETATM 2534 O O   . HOH   C 3 .   ? -12.14765 4.13187   6.30090   1.000 28.11921 ? 632 HOH   A O   1 
HETATM 2535 O O   . HOH   C 3 .   ? 2.238     -22.475   -16.657   1.000 35.43686 ? 633 HOH   A O   1 
HETATM 2536 O O   . HOH   C 3 .   ? -29.45056 -20.85029 1.91729   1.000 18.26275 ? 634 HOH   A O   1 
HETATM 2537 O O   . HOH   C 3 .   ? -5.24482  -28.34812 2.44162   1.000 30.21446 ? 635 HOH   A O   1 
HETATM 2538 O O   . HOH   C 3 .   ? -9.34434  -25.33950 8.70695   1.000 25.74959 ? 636 HOH   A O   1 
HETATM 2539 O O   . HOH   C 3 .   ? -21.80146 2.36585   -12.12259 1.000 29.28280 ? 637 HOH   A O   1 
HETATM 2540 O O   . HOH   C 3 .   ? -1.60275  -27.16770 -11.29711 1.000 35.57657 ? 638 HOH   A O   1 
HETATM 2541 O O   . HOH   C 3 .   ? -34.83224 -33.72796 12.32280  1.000 41.11027 ? 639 HOH   A O   1 
HETATM 2542 O O   . HOH   C 3 .   ? -6.42528  -24.50442 4.84475   1.000 23.04235 ? 640 HOH   A O   1 
HETATM 2543 O O   . HOH   C 3 .   ? -11.74896 -27.68706 -8.45883  1.000 39.33585 ? 641 HOH   A O   1 
HETATM 2544 O O   . HOH   C 3 .   ? -4.41820  3.71069   -2.17889  1.000 29.54410 ? 642 HOH   A O   1 
HETATM 2545 O O   . HOH   C 3 .   ? -27.24210 -14.32450 0.00000   0.50  26.99393 ? 643 HOH   A O   1 
HETATM 2546 O O   . HOH   C 3 .   ? -5.66724  -28.39774 0.66499   1.000 29.09967 ? 644 HOH   A O   1 
HETATM 2547 O O   . HOH   C 3 .   ? -4.88073  -24.20822 10.96917  1.000 27.49158 ? 645 HOH   A O   1 
HETATM 2548 O O   . HOH   C 3 .   ? -3.60308  -29.14509 -0.40167  1.000 41.15288 ? 646 HOH   A O   1 
HETATM 2549 O O   . HOH   C 3 .   ? -25.38067 -29.17202 0.18596   1.000 27.41101 ? 647 HOH   A O   1 
HETATM 2550 O O   . HOH   C 3 .   ? -14.17621 -18.12160 13.44317  1.000 27.54429 ? 648 HOH   A O   1 
HETATM 2551 O O   . HOH   C 3 .   ? -9.54076  -21.22564 12.51547  1.000 31.78459 ? 649 HOH   A O   1 
HETATM 2552 O O   . HOH   C 3 .   ? -9.93645  -22.79124 9.13552   1.000 26.68450 ? 650 HOH   A O   1 
HETATM 2553 O O   . HOH   C 3 .   ? -2.00202  -14.67734 5.19309   1.000 18.72070 ? 651 HOH   A O   1 
HETATM 2554 O O   . HOH   C 3 .   ? -5.16859  -6.61466  2.10255   1.000 11.34209 ? 652 HOH   A O   1 
HETATM 2555 O O   . HOH   C 3 .   ? -22.06461 4.58791   3.55555   1.000 27.70209 ? 653 HOH   A O   1 
HETATM 2556 O O   . HOH   C 3 .   ? -0.28547  -23.10440 -10.29020 1.000 35.54765 ? 654 HOH   A O   1 
HETATM 2557 O O   . HOH   C 3 .   ? -33.83244 -23.87505 5.77617   1.000 22.13094 ? 655 HOH   A O   1 
HETATM 2558 O O   . HOH   C 3 .   ? -34.58416 -25.36329 11.58935  1.000 24.85449 ? 656 HOH   A O   1 
HETATM 2559 O O   . HOH   C 3 .   ? -23.95200 3.71496   1.46741   1.000 27.99405 ? 657 HOH   A O   1 
HETATM 2560 O O   . HOH   C 3 .   ? -35.56818 -31.54603 13.61488  1.000 37.97967 ? 658 HOH   A O   1 
HETATM 2561 O O   . HOH   C 3 .   ? -3.89246  0.25365   -0.32106  1.000 23.98510 ? 659 HOH   A O   1 
HETATM 2562 O O   . HOH   C 3 .   ? -12.24286 -9.92678  7.88912   1.000 36.08776 ? 660 HOH   A O   1 
HETATM 2563 O O   . HOH   C 3 .   ? -1.36703  -25.29803 -4.67314  1.000 27.81860 ? 661 HOH   A O   1 
HETATM 2564 O O   . HOH   C 3 .   ? -0.64720  -20.46221 -1.26646  1.000 19.46032 ? 662 HOH   A O   1 
HETATM 2565 O O   . HOH   C 3 .   ? -6.13523  1.68386   2.34313   1.000 29.01574 ? 663 HOH   A O   1 
HETATM 2566 O O   . HOH   C 3 .   ? 5.924     -1.124    -7.820    1.000 30.97350 ? 664 HOH   A O   1 
HETATM 2567 O O   . HOH   C 3 .   ? -21.17650 -37.18840 4.28018   1.000 30.34770 ? 665 HOH   A O   1 
HETATM 2568 O O   . HOH   C 3 .   ? -16.53882 -37.43670 3.65819   1.000 36.28835 ? 666 HOH   A O   1 
HETATM 2569 O O   . HOH   C 3 .   ? -8.47997  -18.56894 10.36768  1.000 30.83190 ? 667 HOH   A O   1 
HETATM 2570 O O   . HOH   C 3 .   ? -8.18981  -15.92693 10.91473  1.000 42.03492 ? 668 HOH   A O   1 
HETATM 2571 O O   . HOH   C 3 .   ? -12.12931 -20.37663 12.27052  1.000 30.10580 ? 669 HOH   A O   1 
HETATM 2572 O O   . HOH   C 3 .   ? -2.770    -22.757   4.027     1.000 27.67877 ? 670 HOH   A O   1 
HETATM 2573 O O   . HOH   C 3 .   ? -1.29790  -22.60976 -1.34769  1.000 22.32450 ? 671 HOH   A O   1 
HETATM 2574 O O   . HOH   C 3 .   ? 0.78501   -24.13177 -3.12080  1.000 26.87684 ? 672 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   ? 0.16479 0.43243 0.29290 0.02898  0.03391  0.19884  1   SER   A N   
2    C CA  . SER   A 1   ? 0.17434 0.43677 0.30058 0.01834  0.01768  0.19306  1   SER   A CA  
3    C C   . SER   A 1   ? 0.14020 0.38660 0.28029 0.00766  0.00565  0.18493  1   SER   A C   
4    O O   . SER   A 1   ? 0.12768 0.36582 0.27301 0.00951  0.00736  0.18363  1   SER   A O   
5    C CB  . SER   A 1   ? 0.15697 0.43104 0.29834 0.01349  0.01441  0.20672  1   SER   A CB  
6    O OG  . SER   A 1   ? 0.18950 0.46683 0.36304 0.00949  0.00709  0.21906  1   SER   A OG  
7    N N   . GLY   A 2   ? 0.14115 0.37308 0.27860 -0.00501 -0.00375 0.17780  2   GLY   A N   
8    C CA  . GLY   A 2   ? 0.16149 0.36638 0.29662 -0.01688 -0.01330 0.16686  2   GLY   A CA  
9    C C   . GLY   A 2   ? 0.14511 0.32706 0.25221 -0.01627 -0.01593 0.14734  2   GLY   A C   
10   O O   . GLY   A 2   ? 0.13927 0.32278 0.22686 -0.00737 -0.01058 0.14064  2   GLY   A O   
11   N N   . PHE   A 3   ? 0.12614 0.28242 0.22697 -0.02441 -0.02518 0.13667  3   PHE   A N   
12   C CA  . PHE   A 3   ? 0.17576 0.30660 0.24984 -0.02149 -0.02811 0.11743  3   PHE   A CA  
13   C C   . PHE   A 3   ? 0.20162 0.31143 0.27154 -0.02634 -0.03511 0.10738  3   PHE   A C   
14   O O   . PHE   A 3   ? 0.26618 0.37221 0.34772 -0.03571 -0.04163 0.11263  3   PHE   A O   
15   C CB  . PHE   A 3   ? 0.18489 0.31034 0.25360 -0.02295 -0.03008 0.11675  3   PHE   A CB  
16   C CG  . PHE   A 3   ? 0.20924 0.32302 0.25644 -0.01817 -0.02947 0.10439  3   PHE   A CG  
17   C CD1 . PHE   A 3   ? 0.22750 0.34947 0.26044 -0.01100 -0.02386 0.10153  3   PHE   A CD1 
18   C CD2 . PHE   A 3   ? 0.20017 0.29654 0.24237 -0.02153 -0.03484 0.09680  3   PHE   A CD2 
19   C CE1 . PHE   A 3   ? 0.21443 0.32858 0.23048 -0.00874 -0.02456 0.09170  3   PHE   A CE1 
20   C CE2 . PHE   A 3   ? 0.17693 0.26636 0.20384 -0.01765 -0.03417 0.08797  3   PHE   A CE2 
21   C CZ  . PHE   A 3   ? 0.20938 0.30818 0.22431 -0.01196 -0.02953 0.08563  3   PHE   A CZ  
22   N N   . ARG   A 4   ? 0.17716 0.27745 0.23314 -0.02154 -0.03436 0.09634  4   ARG   A N   
23   C CA  . ARG   A 4   ? 0.17916 0.26752 0.23407 -0.02583 -0.03970 0.09113  4   ARG   A CA  
24   C C   . ARG   A 4   ? 0.17916 0.25258 0.21623 -0.02236 -0.04007 0.07762  4   ARG   A C   
25   O O   . ARG   A 4   ? 0.18401 0.25839 0.21047 -0.01512 -0.03565 0.07239  4   ARG   A O   
26   C CB  . ARG   A 4   ? 0.15049 0.24833 0.21521 -0.02272 -0.03745 0.09654  4   ARG   A CB  
27   C CG  . ARG   A 4   ? 0.19945 0.30905 0.28475 -0.02952 -0.03974 0.11094  4   ARG   A CG  
28   C CD  . ARG   A 4   ? 0.18396 0.28181 0.26914 -0.04087 -0.04968 0.11074  4   ARG   A CD  
29   N NE  . ARG   A 4   ? 0.20570 0.31363 0.30864 -0.04782 -0.05366 0.12522  4   ARG   A NE  
30   C CZ  . ARG   A 4   ? 0.21449 0.31407 0.31643 -0.05801 -0.06373 0.12802  4   ARG   A CZ  
31   N NH1 . ARG   A 4   ? 0.18844 0.29880 0.30653 -0.06462 -0.06868 0.14382  4   ARG   A NH1 
32   N NH2 . ARG   A 4   ? 0.20736 0.28840 0.29147 -0.06144 -0.06929 0.11663  4   ARG   A NH2 
33   N N   . LYS   A 5   ? 0.19257 0.25248 0.22586 -0.02784 -0.04549 0.07262  5   LYS   A N   
34   C CA  . LYS   A 5   ? 0.20445 0.25257 0.22394 -0.02404 -0.04476 0.06148  5   LYS   A CA  
35   C C   . LYS   A 5   ? 0.19363 0.24604 0.21263 -0.01816 -0.04192 0.06000  5   LYS   A C   
36   O O   . LYS   A 5   ? 0.21940 0.27305 0.24459 -0.02087 -0.04449 0.06339  5   LYS   A O   
37   C CB  . LYS   A 5   ? 0.21133 0.24498 0.22604 -0.03030 -0.05018 0.05745  5   LYS   A CB  
38   C CG  . LYS   A 5   ? 0.24199 0.26680 0.24974 -0.02917 -0.04999 0.05250  5   LYS   A CG  
39   C CD  . LYS   A 5   ? 0.30831 0.31847 0.31195 -0.03477 -0.05556 0.05010  5   LYS   A CD  
40   C CE  . LYS   A 5   ? 0.25239 0.25662 0.25210 -0.03137 -0.05462 0.04660  5   LYS   A CE  
41   N NZ  . LYS   A 5   ? 0.33716 0.33104 0.33933 -0.03667 -0.06111 0.04898  5   LYS   A NZ  
42   N N   . MET   A 6   ? 0.17550 0.22999 0.18696 -0.01026 -0.03740 0.05582  6   MET   A N   
43   C CA  . MET   A 6   ? 0.19392 0.25168 0.20568 -0.00323 -0.03475 0.05564  6   MET   A CA  
44   C C   . MET   A 6   ? 0.18992 0.23569 0.18987 -0.00030 -0.03535 0.04572  6   MET   A C   
45   O O   . MET   A 6   ? 0.18761 0.22783 0.17644 0.00084  -0.03473 0.03890  6   MET   A O   
46   C CB  . MET   A 6   ? 0.17632 0.24332 0.18555 0.00334  -0.02984 0.05837  6   MET   A CB  
47   C CG  . MET   A 6   ? 0.21841 0.29418 0.23491 0.01095  -0.02579 0.06433  6   MET   A CG  
48   S SD  . MET   A 6   ? 0.32212 0.42671 0.34092 0.01730  -0.01584 0.07752  6   MET   A SD  
49   C CE  . MET   A 6   ? 0.17103 0.28701 0.21414 0.01136  -0.01605 0.09107  6   MET   A CE  
50   N N   . ALA   A 7   ? 0.15713 0.20077 0.16144 0.00058  -0.03653 0.04662  7   ALA   A N   
51   C CA  . ALA   A 7   ? 0.18465 0.21889 0.17988 0.00436  -0.03651 0.03920  7   ALA   A CA  
52   C C   . ALA   A 7   ? 0.19715 0.23076 0.19107 0.01320  -0.03461 0.03937  7   ALA   A C   
53   O O   . ALA   A 7   ? 0.16583 0.21099 0.17233 0.01667  -0.03168 0.04901  7   ALA   A O   
54   C CB  . ALA   A 7   ? 0.20124 0.23317 0.20155 -0.00002 -0.03910 0.04148  7   ALA   A CB  
55   N N   . PHE   A 8   ? 0.16268 0.18578 0.14492 0.01617  -0.03567 0.03163  8   PHE   A N   
56   C CA  . PHE   A 8   ? 0.19531 0.23090 0.18479 0.02289  -0.03236 0.04112  8   PHE   A CA  
57   C C   . PHE   A 8   ? 0.16232 0.19820 0.17722 0.02850  -0.02910 0.05241  8   PHE   A C   
58   O O   . PHE   A 8   ? 0.13433 0.16189 0.14733 0.02288  -0.03329 0.04886  8   PHE   A O   
59   C CB  . PHE   A 8   ? 0.15728 0.18712 0.12866 0.02247  -0.03337 0.03059  8   PHE   A CB  
60   C CG  . PHE   A 8   ? 0.20872 0.24017 0.15765 0.01549  -0.03308 0.01821  8   PHE   A CG  
61   C CD1 . PHE   A 8   ? 0.26041 0.29821 0.19743 0.01744  -0.02119 0.00747  8   PHE   A CD1 
62   C CD2 . PHE   A 8   ? 0.18341 0.19253 0.13298 0.00663  -0.03632 0.01292  8   PHE   A CD2 
63   C CE1 . PHE   A 8   ? 0.29960 0.34197 0.21746 0.00993  -0.02272 0.00012  8   PHE   A CE1 
64   C CE2 . PHE   A 8   ? 0.22607 0.23802 0.16599 0.00401  -0.03505 0.00873  8   PHE   A CE2 
65   C CZ  . PHE   A 8   ? 0.24883 0.27164 0.17432 0.00289  -0.03041 0.00435  8   PHE   A CZ  
66   N N   . PRO   A 9   ? 0.14642 0.18764 0.18392 0.04059  -0.01500 0.06016  9   PRO   A N   
67   C CA  . PRO   A 9   ? 0.16384 0.20126 0.23121 0.04677  -0.00976 0.07151  9   PRO   A CA  
68   C C   . PRO   A 9   ? 0.19843 0.21955 0.25903 0.04368  -0.01437 0.06651  9   PRO   A C   
69   O O   . PRO   A 9   ? 0.12460 0.13225 0.16572 0.04052  -0.01147 0.04948  9   PRO   A O   
70   C CB  . PRO   A 9   ? 0.20347 0.23599 0.29004 0.05793  0.01467  0.06598  9   PRO   A CB  
71   C CG  . PRO   A 9   ? 0.21510 0.25506 0.27853 0.05473  0.02033  0.05325  9   PRO   A CG  
72   C CD  . PRO   A 9   ? 0.19491 0.23365 0.22386 0.04336  0.00296  0.04466  9   PRO   A CD  
73   N N   . SER   A 10  ? 0.14462 0.16652 0.21053 0.03750  -0.01906 0.07133  10  SER   A N   
74   C CA  . SER   A 10  ? 0.14463 0.15693 0.19944 0.03241  -0.02462 0.06766  10  SER   A CA  
75   C C   . SER   A 10  ? 0.18748 0.19135 0.26775 0.03881  -0.01503 0.07594  10  SER   A C   
76   O O   . SER   A 10  ? 0.17315 0.17194 0.24828 0.03468  -0.01875 0.07647  10  SER   A O   
77   C CB  . SER   A 10  ? 0.16764 0.18741 0.20833 0.02260  -0.03289 0.06558  10  SER   A CB  
78   O OG  . SER   A 10  ? 0.16195 0.19390 0.22365 0.02217  -0.03201 0.07902  10  SER   A OG  
79   N N   . GLY   A 11  ? 0.18016 0.18127 0.28869 0.04897  0.00029  0.08097  11  GLY   A N   
80   C CA  . GLY   A 11  ? 0.18231 0.17362 0.31660 0.05371  0.01204  0.08692  11  GLY   A CA  
81   C C   . GLY   A 11  ? 0.20379 0.17020 0.33407 0.05379  0.01778  0.07553  11  GLY   A C   
82   O O   . GLY   A 11  ? 0.20286 0.16559 0.34413 0.05204  0.01886  0.08225  11  GLY   A O   
83   N N   . LYS   A 12  ? 0.22405 0.17229 0.34106 0.05534  0.02392  0.05700  12  LYS   A N   
84   C CA  . LYS   A 12  ? 0.27287 0.19647 0.38432 0.05029  0.03037  0.04094  12  LYS   A CA  
85   C C   . LYS   A 12  ? 0.23042 0.15829 0.32839 0.04224  0.01270  0.05013  12  LYS   A C   
86   O O   . LYS   A 12  ? 0.25680 0.16913 0.36010 0.03852  0.01743  0.04598  12  LYS   A O   
87   C CB  . LYS   A 12  ? 0.29906 0.21297 0.38162 0.04222  0.03758  0.00886  12  LYS   A CB  
88   C CG  . LYS   A 12  ? 0.36748 0.26117 0.46101 0.04641  0.06377  -0.01222 12  LYS   A CG  
89   C CD  . LYS   A 12  ? 0.44893 0.35206 0.54283 0.05331  0.07589  -0.01679 12  LYS   A CD  
90   C CE  . LYS   A 12  ? 0.50870 0.42943 0.56008 0.04298  0.06355  -0.03004 12  LYS   A CE  
91   N NZ  . LYS   A 12  ? 0.56375 0.49427 0.60321 0.04541  0.07614  -0.04091 12  LYS   A NZ  
92   N N   . VAL   A 13  ? 0.20238 0.15342 0.28107 0.03757  -0.00587 0.06041  13  VAL   A N   
93   C CA  . VAL   A 13  ? 0.18877 0.14742 0.24724 0.02855  -0.01888 0.06309  13  VAL   A CA  
94   C C   . VAL   A 13  ? 0.20001 0.17297 0.26662 0.02705  -0.02046 0.07590  13  VAL   A C   
95   O O   . VAL   A 13  ? 0.18434 0.15616 0.24826 0.02327  -0.02229 0.07933  13  VAL   A O   
96   C CB  . VAL   A 13  ? 0.17371 0.14643 0.20195 0.02219  -0.03111 0.05558  13  VAL   A CB  
97   C CG1 . VAL   A 13  ? 0.19481 0.17581 0.20571 0.01489  -0.03572 0.05276  13  VAL   A CG1 
98   C CG2 . VAL   A 13  ? 0.21024 0.17338 0.22482 0.01961  -0.03189 0.03949  13  VAL   A CG2 
99   N N   . GLU   A 14  ? 0.17314 0.16103 0.25084 0.02913  -0.02033 0.08386  14  GLU   A N   
100  C CA  . GLU   A 14  ? 0.19225 0.19376 0.28462 0.02770  -0.02147 0.09826  14  GLU   A CA  
101  C C   . GLU   A 14  ? 0.18600 0.17719 0.30123 0.03164  -0.01257 0.10649  14  GLU   A C   
102  O O   . GLU   A 14  ? 0.17534 0.17372 0.29151 0.02800  -0.01636 0.11550  14  GLU   A O   
103  C CB  . GLU   A 14  ? 0.16929 0.18583 0.28127 0.03059  -0.01925 0.10819  14  GLU   A CB  
104  C CG  . GLU   A 14  ? 0.17917 0.20608 0.27224 0.02536  -0.02718 0.10117  14  GLU   A CG  
105  C CD  . GLU   A 14  ? 0.16588 0.20616 0.28290 0.02889  -0.02283 0.11207  14  GLU   A CD  
106  O OE1 . GLU   A 14  ? 0.17908 0.22990 0.32314 0.03114  -0.01903 0.12845  14  GLU   A OE1 
107  O OE2 . GLU   A 14  ? 0.17058 0.21218 0.28199 0.02971  -0.02232 0.10602  14  GLU   A OE2 
108  N N   . GLY   A 15  ? 0.18146 0.15369 0.31536 0.03869  0.00119  0.10147  15  GLY   A N   
109  C CA  . GLY   A 15  ? 0.21373 0.17157 0.37198 0.04184  0.01327  0.10543  15  GLY   A CA  
110  C C   . GLY   A 15  ? 0.21153 0.15776 0.35608 0.03573  0.00979  0.10047  15  GLY   A C   
111  O O   . GLY   A 15  ? 0.21933 0.15478 0.38424 0.03688  0.01908  0.10454  15  GLY   A O   
112  N N   . CYS   A 16  ? 0.18540 0.13410 0.29838 0.02913  -0.00214 0.09233  16  CYS   A N   
113  C CA  . CYS   A 16  ? 0.23512 0.17473 0.33589 0.02275  -0.00484 0.08838  16  CYS   A CA  
114  C C   . CYS   A 16  ? 0.23504 0.19432 0.31880 0.01744  -0.01585 0.09741  16  CYS   A C   
115  O O   . CYS   A 16  ? 0.23731 0.19223 0.31564 0.01298  -0.01633 0.09810  16  CYS   A O   
116  C CB  . CYS   A 16  ? 0.21939 0.14519 0.30051 0.01824  -0.00751 0.07093  16  CYS   A CB  
117  S SG  . CYS   A 16  ? 0.23796 0.13627 0.33379 0.02117  0.00839  0.05046  16  CYS   A SG  
118  N N   . MET   A 17  ? 0.20382 0.18308 0.27969 0.01678  -0.02302 0.10223  17  MET   A N   
119  C CA  . MET   A 17  ? 0.20894 0.20242 0.26504 0.01056  -0.03111 0.10383  17  MET   A CA  
120  C C   . MET   A 17  ? 0.24171 0.24374 0.31399 0.01022  -0.03000 0.12128  17  MET   A C   
121  O O   . MET   A 17  ? 0.22575 0.23306 0.32547 0.01474  -0.02573 0.13501  17  MET   A O   
122  C CB  . MET   A 17  ? 0.18158 0.19039 0.22740 0.00761  -0.03765 0.10086  17  MET   A CB  
123  C CG  . MET   A 17  ? 0.18191 0.18487 0.21224 0.00770  -0.03850 0.08474  17  MET   A CG  
124  S SD  . MET   A 17  ? 0.20109 0.19293 0.20902 0.00510  -0.03821 0.06955  17  MET   A SD  
125  C CE  . MET   A 17  ? 0.17865 0.18415 0.17622 -0.00350 -0.04349 0.07248  17  MET   A CE  
126  N N   . VAL   A 18  ? 0.20257 0.20729 0.25972 0.00522  -0.03293 0.12182  18  VAL   A N   
127  C CA  . VAL   A 18  ? 0.24061 0.25581 0.30893 0.00392  -0.03288 0.13922  18  VAL   A CA  
128  C C   . VAL   A 18  ? 0.24158 0.27107 0.28658 -0.00371 -0.04016 0.13869  18  VAL   A C   
129  O O   . VAL   A 18  ? 0.23411 0.26019 0.25637 -0.00713 -0.04269 0.12327  18  VAL   A O   
130  C CB  . VAL   A 18  ? 0.21410 0.21585 0.29926 0.00556  -0.02485 0.14534  18  VAL   A CB  
131  C CG1 . VAL   A 18  ? 0.22310 0.20970 0.33785 0.01233  -0.01513 0.14593  18  VAL   A CG1 
132  C CG2 . VAL   A 18  ? 0.21350 0.20380 0.27720 0.00096  -0.02487 0.13199  18  VAL   A CG2 
133  N N   . GLN   A 19  ? 0.26007 0.30624 0.31292 -0.00633 -0.04263 0.15662  19  GLN   A N   
134  C CA  . GLN   A 19  ? 0.29064 0.35047 0.32184 -0.01394 -0.04833 0.15853  19  GLN   A CA  
135  C C   . GLN   A 19  ? 0.29022 0.34261 0.31631 -0.01397 -0.04332 0.16192  19  GLN   A C   
136  O O   . GLN   A 19  ? 0.29484 0.34288 0.34287 -0.00994 -0.03787 0.17462  19  GLN   A O   
137  C CB  . GLN   A 19  ? 0.33094 0.41653 0.37185 -0.01817 -0.05492 0.17795  19  GLN   A CB  
138  C CG  . GLN   A 19  ? 0.35060 0.45037 0.36715 -0.02681 -0.06049 0.18095  19  GLN   A CG  
139  C CD  . GLN   A 19  ? 0.39074 0.51809 0.41865 -0.03165 -0.06716 0.20423  19  GLN   A CD  
140  O OE1 . GLN   A 19  ? 0.32351 0.46510 0.34906 -0.03747 -0.07441 0.20589  19  GLN   A OE1 
141  N NE2 . GLN   A 19  ? 0.50908 0.64529 0.55006 -0.03007 -0.06487 0.22372  19  GLN   A NE2 
142  N N   . VAL   A 20  ? 0.31093 0.36095 0.31046 -0.01836 -0.04381 0.15077  20  VAL   A N   
143  C CA  . VAL   A 20  ? 0.34440 0.38861 0.33691 -0.01930 -0.03831 0.15376  20  VAL   A CA  
144  C C   . VAL   A 20  ? 0.34632 0.40699 0.31703 -0.02568 -0.04191 0.15882  20  VAL   A C   
145  O O   . VAL   A 20  ? 0.34215 0.40606 0.29161 -0.02948 -0.04566 0.14636  20  VAL   A O   
146  C CB  . VAL   A 20  ? 0.32772 0.35388 0.31040 -0.01844 -0.03328 0.13640  20  VAL   A CB  
147  C CG1 . VAL   A 20  ? 0.32842 0.35550 0.30455 -0.02207 -0.02802 0.14221  20  VAL   A CG1 
148  C CG2 . VAL   A 20  ? 0.30239 0.31438 0.30779 -0.01457 -0.02984 0.13432  20  VAL   A CG2 
149  N N   . THR   A 21  ? 0.38172 0.45213 0.35778 -0.02708 -0.04014 0.17717  21  THR   A N   
150  C CA  . THR   A 21  ? 0.44041 0.52813 0.39433 -0.03365 -0.04320 0.18440  21  THR   A CA  
151  C C   . THR   A 21  ? 0.44980 0.53321 0.39711 -0.03420 -0.03501 0.19035  21  THR   A C   
152  O O   . THR   A 21  ? 0.48450 0.56450 0.45530 -0.03120 -0.03011 0.20434  21  THR   A O   
153  C CB  . THR   A 21  ? 0.46386 0.57601 0.43023 -0.03662 -0.05055 0.20609  21  THR   A CB  
154  O OG1 . THR   A 21  ? 0.43506 0.55300 0.40570 -0.03788 -0.05784 0.20055  21  THR   A OG1 
155  C CG2 . THR   A 21  ? 0.46155 0.59227 0.40205 -0.04456 -0.05341 0.21466  21  THR   A CG2 
156  N N   . CYS   A 22  ? 0.49295 0.57593 0.41020 -0.03807 -0.03231 0.17990  22  CYS   A N   
157  C CA  . CYS   A 22  ? 0.49053 0.57265 0.39877 -0.03981 -0.02345 0.18615  22  CYS   A CA  
158  C C   . CYS   A 22  ? 0.52105 0.61499 0.39413 -0.04568 -0.02387 0.18357  22  CYS   A C   
159  O O   . CYS   A 22  ? 0.51766 0.60737 0.36953 -0.04698 -0.02530 0.16524  22  CYS   A O   
160  C CB  . CYS   A 22  ? 0.52010 0.58622 0.43256 -0.03804 -0.01533 0.17353  22  CYS   A CB  
161  S SG  . CYS   A 22  ? 0.56046 0.62866 0.48140 -0.04079 -0.00337 0.18798  22  CYS   A SG  
162  N N   . GLY   A 23  ? 0.55840 0.66782 0.42616 -0.04950 -0.02241 0.20246  23  GLY   A N   
163  C CA  . GLY   A 23  ? 0.56817 0.69077 0.40003 -0.05629 -0.02263 0.20109  23  GLY   A CA  
164  C C   . GLY   A 23  ? 0.55827 0.69423 0.38030 -0.06129 -0.03514 0.19747  23  GLY   A C   
165  O O   . GLY   A 23  ? 0.51811 0.66861 0.36129 -0.06224 -0.04438 0.21271  23  GLY   A O   
166  N N   . THR   A 24  ? 0.63336 0.76447 0.42506 -0.06477 -0.03468 0.17746  24  THR   A N   
167  C CA  . THR   A 24  ? 0.62597 0.76740 0.40599 -0.07144 -0.04571 0.17083  24  THR   A CA  
168  C C   . THR   A 24  ? 0.61652 0.74262 0.41088 -0.06729 -0.04908 0.15340  24  THR   A C   
169  O O   . THR   A 24  ? 0.61991 0.75155 0.40629 -0.07310 -0.05716 0.14601  24  THR   A O   
170  C CB  . THR   A 24  ? 0.66442 0.80970 0.40159 -0.07908 -0.04284 0.15904  24  THR   A CB  
171  O OG1 . THR   A 24  ? 0.71686 0.84096 0.44032 -0.07331 -0.02952 0.14077  24  THR   A OG1 
172  C CG2 . THR   A 24  ? 0.65108 0.81835 0.37140 -0.08591 -0.04260 0.17885  24  THR   A CG2 
173  N N   . THR   A 25  ? 0.58954 0.69747 0.40461 -0.05842 -0.04313 0.14737  25  THR   A N   
174  C CA  . THR   A 25  ? 0.52360 0.61678 0.34944 -0.05424 -0.04473 0.13025  25  THR   A CA  
175  C C   . THR   A 25  ? 0.51176 0.60481 0.37190 -0.04983 -0.04927 0.13941  25  THR   A C   
176  O O   . THR   A 25  ? 0.46927 0.55834 0.34877 -0.04494 -0.04491 0.14989  25  THR   A O   
177  C CB  . THR   A 25  ? 0.54855 0.62238 0.36977 -0.04806 -0.03439 0.11474  25  THR   A CB  
178  O OG1 . THR   A 25  ? 0.59528 0.66849 0.38529 -0.05093 -0.02783 0.10600  25  THR   A OG1 
179  C CG2 . THR   A 25  ? 0.50168 0.56325 0.33420 -0.04417 -0.03680 0.09873  25  THR   A CG2 
180  N N   . THR   A 26  ? 0.44463 0.54087 0.31224 -0.05177 -0.05682 0.13512  26  THR   A N   
181  C CA  . THR   A 26  ? 0.39950 0.49352 0.29737 -0.04697 -0.05944 0.14007  26  THR   A CA  
182  C C   . THR   A 26  ? 0.37833 0.45707 0.27730 -0.04411 -0.05870 0.12042  26  THR   A C   
183  O O   . THR   A 26  ? 0.38817 0.46749 0.27209 -0.04895 -0.06202 0.10980  26  THR   A O   
184  C CB  . THR   A 26  ? 0.41673 0.53201 0.32731 -0.05186 -0.06840 0.15730  26  THR   A CB  
185  O OG1 . THR   A 26  ? 0.50326 0.63510 0.41821 -0.05368 -0.06911 0.17902  26  THR   A OG1 
186  C CG2 . THR   A 26  ? 0.41139 0.52312 0.35185 -0.04621 -0.06927 0.16026  26  THR   A CG2 
187  N N   . LEU   A 27  ? 0.34400 0.40924 0.26054 -0.03680 -0.05422 0.11622  27  LEU   A N   
188  C CA  . LEU   A 27  ? 0.32259 0.37553 0.24364 -0.03367 -0.05349 0.10052  27  LEU   A CA  
189  C C   . LEU   A 27  ? 0.28085 0.32803 0.22661 -0.02762 -0.05205 0.10505  27  LEU   A C   
190  O O   . LEU   A 27  ? 0.28233 0.33530 0.24403 -0.02585 -0.05203 0.12077  27  LEU   A O   
191  C CB  . LEU   A 27  ? 0.31756 0.35799 0.22468 -0.03158 -0.04771 0.08477  27  LEU   A CB  
192  C CG  . LEU   A 27  ? 0.30014 0.33435 0.20670 -0.02834 -0.04086 0.08712  27  LEU   A CG  
193  C CD1 . LEU   A 27  ? 0.31275 0.33689 0.23846 -0.02327 -0.03797 0.08739  27  LEU   A CD1 
194  C CD2 . LEU   A 27  ? 0.32068 0.34909 0.20997 -0.02806 -0.03649 0.07327  27  LEU   A CD2 
195  N N   . ASN   A 28  ? 0.23699 0.27259 0.18619 -0.02420 -0.05012 0.09165  28  ASN   A N   
196  C CA  . ASN   A 28  ? 0.24191 0.27109 0.21013 -0.01879 -0.04865 0.09297  28  ASN   A CA  
197  C C   . ASN   A 28  ? 0.22642 0.24114 0.19722 -0.01437 -0.04280 0.08762  28  ASN   A C   
198  O O   . ASN   A 28  ? 0.22075 0.23079 0.17960 -0.01535 -0.04069 0.07755  28  ASN   A O   
199  C CB  . ASN   A 28  ? 0.19813 0.22596 0.16703 -0.01901 -0.05075 0.08300  28  ASN   A CB  
200  C CG  . ASN   A 28  ? 0.23784 0.27973 0.20835 -0.02422 -0.05675 0.09091  28  ASN   A CG  
201  O OD1 . ASN   A 28  ? 0.20908 0.26006 0.19635 -0.02304 -0.05858 0.10454  28  ASN   A OD1 
202  N ND2 . ASN   A 28  ? 0.18952 0.23372 0.14387 -0.03021 -0.05961 0.08378  28  ASN   A ND2 
203  N N   . GLY   A 29  ? 0.24104 0.24848 0.22903 -0.00985 -0.03968 0.09527  29  GLY   A N   
204  C CA  . GLY   A 29  ? 0.24890 0.24200 0.24337 -0.00854 -0.03496 0.09248  29  GLY   A CA  
205  C C   . GLY   A 29  ? 0.22459 0.20772 0.23145 -0.00494 -0.03384 0.08804  29  GLY   A C   
206  O O   . GLY   A 29  ? 0.17307 0.16023 0.18643 -0.00142 -0.03481 0.09006  29  GLY   A O   
207  N N   . LEU   A 30  ? 0.24291 0.21287 0.25359 -0.00672 -0.03200 0.08222  30  LEU   A N   
208  C CA  . LEU   A 30  ? 0.23434 0.19015 0.25688 -0.00413 -0.02998 0.07696  30  LEU   A CA  
209  C C   . LEU   A 30  ? 0.24552 0.18132 0.29247 -0.00505 -0.02057 0.08023  30  LEU   A C   
210  O O   . LEU   A 30  ? 0.20127 0.12802 0.24949 -0.01205 -0.01882 0.07597  30  LEU   A O   
211  C CB  . LEU   A 30  ? 0.19200 0.14518 0.19887 -0.00795 -0.03631 0.06286  30  LEU   A CB  
212  C CG  . LEU   A 30  ? 0.21068 0.14790 0.22495 -0.00596 -0.03604 0.05523  30  LEU   A CG  
213  C CD1 . LEU   A 30  ? 0.22177 0.17195 0.23759 0.00176  -0.03500 0.05848  30  LEU   A CD1 
214  C CD2 . LEU   A 30  ? 0.16288 0.10377 0.15735 -0.01146 -0.04049 0.03445  30  LEU   A CD2 
215  N N   . TRP   A 31  ? 0.21728 0.14714 0.28579 0.00115  -0.01321 0.08571  31  TRP   A N   
216  C CA  . TRP   A 31  ? 0.23298 0.14455 0.32803 0.00134  -0.00114 0.08609  31  TRP   A CA  
217  C C   . TRP   A 31  ? 0.27847 0.16752 0.38181 0.00067  0.00738  0.06631  31  TRP   A C   
218  O O   . TRP   A 31  ? 0.24750 0.13526 0.35849 0.00768  0.01153  0.06427  31  TRP   A O   
219  C CB  . TRP   A 31  ? 0.24148 0.16282 0.35800 0.00859  0.00277  0.10336  31  TRP   A CB  
220  C CG  . TRP   A 31  ? 0.27005 0.17702 0.41658 0.00987  0.01516  0.10769  31  TRP   A CG  
221  C CD1 . TRP   A 31  ? 0.28874 0.17844 0.44170 0.00331  0.02156  0.09997  31  TRP   A CD1 
222  C CD2 . TRP   A 31  ? 0.27954 0.18974 0.45694 0.01764  0.02325  0.12140  31  TRP   A CD2 
223  N NE1 . TRP   A 31  ? 0.31317 0.19334 0.49814 0.00688  0.03340  0.10717  31  TRP   A NE1 
224  C CE2 . TRP   A 31  ? 0.29838 0.19093 0.49993 0.01631  0.03509  0.12116  31  TRP   A CE2 
225  C CE3 . TRP   A 31  ? 0.25747 0.18510 0.44691 0.02481  0.02193  0.13439  31  TRP   A CE3 
226  C CZ2 . TRP   A 31  ? 0.30459 0.19540 0.54238 0.02318  0.04636  0.13396  31  TRP   A CZ2 
227  C CZ3 . TRP   A 31  ? 0.27913 0.20686 0.50568 0.03130  0.03285  0.14822  31  TRP   A CZ3 
228  C CH2 . TRP   A 31  ? 0.33638 0.24532 0.58721 0.03111  0.04539  0.14817  31  TRP   A CH2 
229  N N   . LEU   A 32  ? 0.25495 0.12864 0.35641 -0.00907 0.01065  0.04961  32  LEU   A N   
230  C CA  . LEU   A 32  ? 0.27068 0.12564 0.37442 -0.01349 0.01913  0.02406  32  LEU   A CA  
231  C C   . LEU   A 32  ? 0.32052 0.16077 0.43935 -0.02039 0.02852  0.01642  32  LEU   A C   
232  O O   . LEU   A 32  ? 0.30203 0.14546 0.41822 -0.02876 0.02433  0.01894  32  LEU   A O   
233  C CB  . LEU   A 32  ? 0.27915 0.13778 0.35935 -0.02275 0.01026  0.00447  32  LEU   A CB  
234  C CG  . LEU   A 32  ? 0.29745 0.17534 0.35713 -0.01636 -0.00079 0.00885  32  LEU   A CG  
235  C CD1 . LEU   A 32  ? 0.22277 0.11760 0.25363 -0.02463 -0.01249 -0.00556 32  LEU   A CD1 
236  C CD2 . LEU   A 32  ? 0.24278 0.11447 0.30827 -0.00782 0.00743  0.00317  32  LEU   A CD2 
237  N N   . ASP   A 33  ? 0.31494 0.13989 0.45083 -0.01712 0.04184  0.00725  33  ASP   A N   
238  C CA  . ASP   A 33  ? 0.35446 0.16399 0.50969 -0.02238 0.05204  0.00237  33  ASP   A CA  
239  C C   . ASP   A 33  ? 0.36328 0.18134 0.53398 -0.01919 0.04983  0.02914  33  ASP   A C   
240  O O   . ASP   A 33  ? 0.35546 0.18681 0.53474 -0.00830 0.04814  0.05122  33  ASP   A O   
241  C CB  . ASP   A 33  ? 0.37637 0.17975 0.51474 -0.03806 0.04906  -0.02317 33  ASP   A CB  
242  C CG  . ASP   A 33  ? 0.39625 0.19599 0.51686 -0.04083 0.05152  -0.04883 33  ASP   A CG  
243  O OD1 . ASP   A 33  ? 0.44169 0.22768 0.57527 -0.03585 0.06556  -0.05681 33  ASP   A OD1 
244  O OD2 . ASP   A 33  ? 0.39135 0.20428 0.48548 -0.04762 0.04006  -0.05993 33  ASP   A OD2 
245  N N   . ASP   A 34  ? 0.36499 0.18024 0.53829 -0.02878 0.04873  0.02931  34  ASP   A N   
246  C CA  . ASP   A 34  ? 0.33952 0.16422 0.52669 -0.02590 0.04800  0.05462  34  ASP   A CA  
247  C C   . ASP   A 34  ? 0.33651 0.18010 0.50212 -0.03094 0.03579  0.06381  34  ASP   A C   
248  O O   . ASP   A 34  ? 0.34035 0.18983 0.51288 -0.03399 0.03602  0.07732  34  ASP   A O   
249  C CB  . ASP   A 34  ? 0.36865 0.17648 0.58083 -0.03153 0.05876  0.05215  34  ASP   A CB  
250  C CG  . ASP   A 34  ? 0.43208 0.23350 0.63320 -0.04765 0.05561  0.03327  34  ASP   A CG  
251  O OD1 . ASP   A 34  ? 0.43392 0.24089 0.61009 -0.05444 0.04718  0.01638  34  ASP   A OD1 
252  O OD2 . ASP   A 34  ? 0.44715 0.23985 0.66638 -0.05396 0.06125  0.03603  34  ASP   A OD2 
253  N N   . VAL   A 35  ? 0.30745 0.16150 0.44837 -0.03129 0.02624  0.05758  35  VAL   A N   
254  C CA  . VAL   A 35  ? 0.25035 0.12282 0.37185 -0.03523 0.01629  0.06520  35  VAL   A CA  
255  C C   . VAL   A 35  ? 0.27362 0.16298 0.37778 -0.02623 0.00771  0.07606  35  VAL   A C   
256  O O   . VAL   A 35  ? 0.27640 0.16237 0.37632 -0.02152 0.00634  0.06823  35  VAL   A O   
257  C CB  . VAL   A 35  ? 0.27624 0.14807 0.38574 -0.04784 0.01176  0.04423  35  VAL   A CB  
258  C CG1 . VAL   A 35  ? 0.21761 0.11082 0.30874 -0.04925 0.00152  0.05227  35  VAL   A CG1 
259  C CG2 . VAL   A 35  ? 0.26582 0.12807 0.38967 -0.05897 0.01766  0.03582  35  VAL   A CG2 
260  N N   . VAL   A 36  ? 0.23772 0.14655 0.33014 -0.02460 0.00213  0.09239  36  VAL   A N   
261  C CA  . VAL   A 36  ? 0.25337 0.18161 0.32404 -0.01882 -0.00724 0.09882  36  VAL   A CA  
262  C C   . VAL   A 36  ? 0.25181 0.19163 0.29876 -0.02451 -0.01440 0.09364  36  VAL   A C   
263  O O   . VAL   A 36  ? 0.25383 0.20062 0.29814 -0.02895 -0.01259 0.09949  36  VAL   A O   
264  C CB  . VAL   A 36  ? 0.25761 0.20153 0.33127 -0.01349 -0.00783 0.11732  36  VAL   A CB  
265  C CG1 . VAL   A 36  ? 0.20321 0.16794 0.25061 -0.01189 -0.01731 0.11787  36  VAL   A CG1 
266  C CG2 . VAL   A 36  ? 0.22941 0.16620 0.32984 -0.00667 -0.00180 0.12408  36  VAL   A CG2 
267  N N   . TYR   A 37  ? 0.22536 0.16823 0.25612 -0.02405 -0.02203 0.08319  37  TYR   A N   
268  C CA  . TYR   A 37  ? 0.23384 0.18800 0.24207 -0.02843 -0.02936 0.07671  37  TYR   A CA  
269  C C   . TYR   A 37  ? 0.23223 0.20516 0.22064 -0.02249 -0.03227 0.07714  37  TYR   A C   
270  O O   . TYR   A 37  ? 0.27578 0.25175 0.26437 -0.01693 -0.03327 0.07716  37  TYR   A O   
271  C CB  . TYR   A 37  ? 0.21412 0.16321 0.21527 -0.03078 -0.03486 0.05823  37  TYR   A CB  
272  C CG  . TYR   A 37  ? 0.22956 0.16466 0.24892 -0.03671 -0.02891 0.04283  37  TYR   A CG  
273  C CD1 . TYR   A 37  ? 0.21735 0.13436 0.25502 -0.03428 -0.02185 0.04125  37  TYR   A CD1 
274  C CD2 . TYR   A 37  ? 0.24309 0.18382 0.26212 -0.04543 -0.03000 0.02927  37  TYR   A CD2 
275  C CE1 . TYR   A 37  ? 0.24327 0.14499 0.29458 -0.04143 -0.01517 0.02377  37  TYR   A CE1 
276  C CE2 . TYR   A 37  ? 0.24742 0.17660 0.28067 -0.05403 -0.02594 0.01342  37  TYR   A CE2 
277  C CZ  . TYR   A 37  ? 0.27335 0.18139 0.32070 -0.05255 -0.01810 0.00912  37  TYR   A CZ  
278  O OH  . TYR   A 37  ? 0.26492 0.15820 0.32397 -0.06246 -0.01240 -0.00989 37  TYR   A OH  
279  N N   . CYS   A 38  ? 0.23032 0.21371 0.20435 -0.02464 -0.03168 0.07548  38  CYS   A N   
280  C CA  . CYS   A 38  ? 0.23778 0.23158 0.19553 -0.02069 -0.03171 0.07108  38  CYS   A CA  
281  C C   . CYS   A 38  ? 0.26614 0.26526 0.20991 -0.02254 -0.02952 0.06425  38  CYS   A C   
282  O O   . CYS   A 38  ? 0.22191 0.22112 0.16942 -0.02759 -0.02777 0.06734  38  CYS   A O   
283  C CB  . CYS   A 38  ? 0.21000 0.20837 0.16982 -0.01973 -0.03010 0.08477  38  CYS   A CB  
284  S SG  . CYS   A 38  ? 0.27937 0.28314 0.23662 -0.02425 -0.02425 0.09780  38  CYS   A SG  
285  N N   . PRO   A 39  ? 0.24164 0.24421 0.17154 -0.01885 -0.02884 0.05585  39  PRO   A N   
286  C CA  . PRO   A 39  ? 0.24235 0.24763 0.16014 -0.01926 -0.02521 0.05001  39  PRO   A CA  
287  C C   . PRO   A 39  ? 0.28712 0.29756 0.19760 -0.02359 -0.01986 0.06130  39  PRO   A C   
288  O O   . PRO   A 39  ? 0.23882 0.25174 0.14552 -0.02430 -0.01953 0.07058  39  PRO   A O   
289  C CB  . PRO   A 39  ? 0.23017 0.23610 0.13740 -0.01663 -0.02661 0.04164  39  PRO   A CB  
290  C CG  . PRO   A 39  ? 0.20774 0.21385 0.12434 -0.01756 -0.03207 0.04312  39  PRO   A CG  
291  C CD  . PRO   A 39  ? 0.22835 0.23361 0.15502 -0.01752 -0.03230 0.05435  39  PRO   A CD  
292  N N   . ARG   A 40  ? 0.25172 0.26608 0.16141 -0.02677 -0.01478 0.06162  40  ARG   A N   
293  C CA  . ARG   A 40  ? 0.28066 0.30189 0.18810 -0.03092 -0.00639 0.07351  40  ARG   A CA  
294  C C   . ARG   A 40  ? 0.30792 0.33148 0.19210 -0.02956 -0.00147 0.07251  40  ARG   A C   
295  O O   . ARG   A 40  ? 0.33603 0.36515 0.21673 -0.03254 0.00482  0.08375  40  ARG   A O   
296  C CB  . ARG   A 40  ? 0.27323 0.30210 0.18975 -0.03506 0.00026  0.07491  40  ARG   A CB  
297  C CG  . ARG   A 40  ? 0.27968 0.31265 0.18230 -0.03223 0.00534  0.06362  40  ARG   A CG  
298  C CD  . ARG   A 40  ? 0.24935 0.29724 0.16758 -0.03609 0.01468  0.06855  40  ARG   A CD  
299  N NE  . ARG   A 40  ? 0.25833 0.30984 0.16944 -0.03039 0.02135  0.05655  40  ARG   A NE  
300  C CZ  . ARG   A 40  ? 0.25338 0.31624 0.18613 -0.02760 0.03134  0.05500  40  ARG   A CZ  
301  N NH1 . ARG   A 40  ? 0.22710 0.30095 0.18822 -0.03214 0.03459  0.06450  40  ARG   A NH1 
302  N NH2 . ARG   A 40  ? 0.23422 0.29763 0.16339 -0.02047 0.03870  0.04479  40  ARG   A NH2 
303  N N   . HIS   A 41  ? 0.34109 0.36026 0.21002 -0.02573 -0.00394 0.06000  41  HIS   A N   
304  C CA  . HIS   A 41  ? 0.37514 0.39621 0.22027 -0.02632 0.00041  0.05928  41  HIS   A CA  
305  C C   . HIS   A 41  ? 0.40375 0.42853 0.24609 -0.02844 -0.00513 0.06997  41  HIS   A C   
306  O O   . HIS   A 41  ? 0.41171 0.44048 0.23286 -0.03062 -0.00311 0.07078  41  HIS   A O   
307  C CB  . HIS   A 41  ? 0.38775 0.40346 0.21897 -0.02276 -0.00046 0.04375  41  HIS   A CB  
308  C CG  . HIS   A 41  ? 0.40449 0.41680 0.24380 -0.02048 -0.01139 0.03878  41  HIS   A CG  
309  N ND1 . HIS   A 41  ? 0.40068 0.41927 0.23663 -0.02573 -0.01838 0.04544  41  HIS   A ND1 
310  C CD2 . HIS   A 41  ? 0.37369 0.38241 0.22534 -0.01809 -0.01614 0.03013  41  HIS   A CD2 
311  C CE1 . HIS   A 41  ? 0.36372 0.38159 0.21000 -0.02655 -0.02592 0.04095  41  HIS   A CE1 
312  N NE2 . HIS   A 41  ? 0.37966 0.39095 0.23525 -0.02198 -0.02430 0.03155  41  HIS   A NE2 
313  N N   . VAL   A 42  ? 0.34441 0.36926 0.20707 -0.02838 -0.01132 0.07874  42  VAL   A N   
314  C CA  . VAL   A 42  ? 0.40876 0.44033 0.27321 -0.03073 -0.01496 0.09323  42  VAL   A CA  
315  C C   . VAL   A 42  ? 0.46723 0.50672 0.32567 -0.03479 -0.00736 0.10714  42  VAL   A C   
316  O O   . VAL   A 42  ? 0.49655 0.54484 0.35040 -0.03735 -0.00969 0.11980  42  VAL   A O   
317  C CB  . VAL   A 42  ? 0.38953 0.41876 0.28040 -0.02900 -0.02027 0.10077  42  VAL   A CB  
318  C CG1 . VAL   A 42  ? 0.34497 0.37210 0.25478 -0.03042 -0.01480 0.11006  42  VAL   A CG1 
319  C CG2 . VAL   A 42  ? 0.40437 0.44340 0.29881 -0.03063 -0.02603 0.11468  42  VAL   A CG2 
320  N N   . ILE   A 43  ? 0.44915 0.48806 0.30961 -0.03585 0.00214  0.10674  43  ILE   A N   
321  C CA  . ILE   A 43  ? 0.52816 0.57539 0.38351 -0.03968 0.01149  0.11993  43  ILE   A CA  
322  C C   . ILE   A 43  ? 0.53669 0.58718 0.35999 -0.04102 0.01949  0.11262  43  ILE   A C   
323  O O   . ILE   A 43  ? 0.61804 0.67648 0.43161 -0.04441 0.02799  0.12309  43  ILE   A O   
324  C CB  . ILE   A 43  ? 0.46176 0.50877 0.34243 -0.04117 0.01875  0.12643  43  ILE   A CB  
325  C CG1 . ILE   A 43  ? 0.46081 0.50543 0.34217 -0.04018 0.02361  0.11233  43  ILE   A CG1 
326  C CG2 . ILE   A 43  ? 0.50814 0.54981 0.41829 -0.04041 0.01167  0.13479  43  ILE   A CG2 
327  C CD1 . ILE   A 43  ? 0.43422 0.48261 0.34344 -0.04340 0.03060  0.11893  43  ILE   A CD1 
328  N N   . CYS   A 44  ? 0.59599 0.64025 0.40295 -0.03836 0.01758  0.09529  44  CYS   A N   
329  C CA  . CYS   A 44  ? 0.75114 0.79625 0.52631 -0.03914 0.02420  0.08598  44  CYS   A CA  
330  C C   . CYS   A 44  ? 0.83417 0.88650 0.59113 -0.04308 0.01598  0.09152  44  CYS   A C   
331  O O   . CYS   A 44  ? 0.80335 0.85969 0.57471 -0.04404 0.00437  0.10119  44  CYS   A O   
332  C CB  . CYS   A 44  ? 0.76187 0.79787 0.53101 -0.03479 0.02394  0.06608  44  CYS   A CB  
333  S SG  . CYS   A 44  ? 0.85101 0.88320 0.63474 -0.03090 0.03553  0.05782  44  CYS   A SG  
334  N N   . THR   A 45  ? 0.96279 1.01829 0.68865 -0.04568 0.02275  0.08528  45  THR   A N   
335  C CA  . THR   A 45  ? 1.00633 1.07001 0.70970 -0.05116 0.01419  0.08572  45  THR   A CA  
336  C C   . THR   A 45  ? 1.07731 1.13523 0.75410 -0.05135 0.01918  0.06466  45  THR   A C   
337  O O   . THR   A 45  ? 1.05765 1.10482 0.74074 -0.04578 0.02544  0.05040  45  THR   A O   
338  C CB  . THR   A 45  ? 1.04551 1.12432 0.73529 -0.05724 0.01691  0.10422  45  THR   A CB  
339  O OG1 . THR   A 45  ? 1.08988 1.16830 0.76556 -0.05678 0.03498  0.10407  45  THR   A OG1 
340  C CG2 . THR   A 45  ? 0.94125 1.02745 0.66170 -0.05736 0.00893  0.12579  45  THR   A CG2 
341  N N   . SER   A 46  ? 1.17140 1.23952 0.81870 -0.05976 0.01630  0.06275  46  SER   A N   
342  C CA  . SER   A 46  ? 1.20475 1.26760 0.82668 -0.06236 0.01985  0.04109  46  SER   A CA  
343  C C   . SER   A 46  ? 1.20012 1.25657 0.80417 -0.05728 0.04093  0.02989  46  SER   A C   
344  O O   . SER   A 46  ? 1.19000 1.23791 0.78407 -0.05608 0.04696  0.00934  46  SER   A O   
345  C CB  . SER   A 46  ? 1.20419 1.28208 0.79853 -0.07610 0.01003  0.04189  46  SER   A CB  
346  O OG  . SER   A 46  ? 1.14798 1.23440 0.76144 -0.08190 -0.00838 0.05030  46  SER   A OG  
347  N N   . GLU   A 47  ? 1.17551 1.23766 0.77753 -0.05569 0.05349  0.04306  47  GLU   A N   
348  C CA  . GLU   A 47  ? 1.15987 1.21895 0.75188 -0.05041 0.07617  0.03450  47  GLU   A CA  
349  C C   . GLU   A 47  ? 1.13364 1.18774 0.75880 -0.04234 0.08513  0.04026  47  GLU   A C   
350  O O   . GLU   A 47  ? 1.09320 1.14588 0.71908 -0.03620 0.10399  0.03152  47  GLU   A O   
351  C CB  . GLU   A 47  ? 1.16712 1.23746 0.72981 -0.05514 0.08836  0.04387  47  GLU   A CB  
352  C CG  . GLU   A 47  ? 1.13409 1.21395 0.70975 -0.05848 0.08474  0.07045  47  GLU   A CG  
353  C CD  . GLU   A 47  ? 1.17723 1.26810 0.72476 -0.06265 0.09993  0.07985  47  GLU   A CD  
354  O OE1 . GLU   A 47  ? 1.18835 1.27790 0.70847 -0.06077 0.11688  0.06485  47  GLU   A OE1 
355  O OE2 . GLU   A 47  ? 1.16513 1.26710 0.71917 -0.06758 0.09558  0.10240  47  GLU   A OE2 
356  N N   . ASP   A 48  ? 1.12156 1.17496 0.77586 -0.04267 0.07261  0.05424  48  ASP   A N   
357  C CA  . ASP   A 48  ? 1.06205 1.11067 0.74869 -0.03752 0.07740  0.05651  48  ASP   A CA  
358  C C   . ASP   A 48  ? 1.03745 1.07742 0.73516 -0.03187 0.07388  0.03909  48  ASP   A C   
359  O O   . ASP   A 48  ? 0.97927 1.01774 0.69951 -0.02757 0.08097  0.03788  48  ASP   A O   
360  C CB  . ASP   A 48  ? 0.95650 1.00754 0.67106 -0.04049 0.06416  0.07400  48  ASP   A CB  
361  C CG  . ASP   A 48  ? 0.97825 1.04021 0.68794 -0.04645 0.06501  0.09381  48  ASP   A CG  
362  O OD1 . ASP   A 48  ? 1.00901 1.07644 0.69684 -0.04852 0.07945  0.09617  48  ASP   A OD1 
363  O OD2 . ASP   A 48  ? 0.90575 0.97158 0.63522 -0.04855 0.05200  0.10764  48  ASP   A OD2 
364  N N   . MET   A 49  ? 1.07242 1.10828 0.75650 -0.03321 0.06315  0.02627  49  MET   A N   
365  C CA  . MET   A 49  ? 1.00455 1.03190 0.70347 -0.02954 0.05627  0.01259  49  MET   A CA  
366  C C   . MET   A 49  ? 1.00369 1.02823 0.69861 -0.02495 0.07279  -0.00491 49  MET   A C   
367  O O   . MET   A 49  ? 0.92295 0.94201 0.63743 -0.02104 0.07183  -0.01280 49  MET   A O   
368  C CB  . MET   A 49  ? 0.96947 0.99390 0.66057 -0.03432 0.03889  0.00735  49  MET   A CB  
369  C CG  . MET   A 49  ? 0.91118 0.92595 0.60941 -0.03273 0.03408  -0.00952 49  MET   A CG  
370  S SD  . MET   A 49  ? 0.95202 0.96644 0.65244 -0.03888 0.01310  -0.00895 49  MET   A SD  
371  C CE  . MET   A 49  ? 0.69030 0.69196 0.40558 -0.03572 0.01089  -0.02588 49  MET   A CE  
372  N N   . LEU   A 50  ? 1.04541 1.07452 0.71748 -0.02526 0.08921  -0.01071 50  LEU   A N   
373  C CA  . LEU   A 50  ? 1.01304 1.03971 0.68245 -0.02105 0.10730  -0.02969 50  LEU   A CA  
374  C C   . LEU   A 50  ? 1.01135 1.04156 0.71497 -0.01343 0.11755  -0.02866 50  LEU   A C   
375  O O   . LEU   A 50  ? 0.94382 0.96403 0.66311 -0.01148 0.11465  -0.04007 50  LEU   A O   
376  C CB  . LEU   A 50  ? 1.04944 1.08399 0.69238 -0.02150 0.12577  -0.03238 50  LEU   A CB  
377  C CG  . LEU   A 50  ? 1.10818 1.14081 0.75191 -0.01638 0.14852  -0.05230 50  LEU   A CG  
378  C CD1 . LEU   A 50  ? 1.10217 1.11442 0.74500 -0.01870 0.14391  -0.07507 50  LEU   A CD1 
379  C CD2 . LEU   A 50  ? 1.14292 1.18323 0.75486 -0.01784 0.16536  -0.05604 50  LEU   A CD2 
380  N N   . ASN   A 51  ? 0.99839 1.04325 0.71566 -0.00989 0.12998  -0.01408 51  ASN   A N   
381  C CA  . ASN   A 51  ? 0.89799 0.95285 0.65292 -0.00501 0.13818  -0.00965 51  ASN   A CA  
382  C C   . ASN   A 51  ? 0.87011 0.93270 0.63945 -0.00648 0.13635  0.01443  51  ASN   A C   
383  O O   . ASN   A 51  ? 0.83606 0.91150 0.61489 -0.00568 0.15072  0.02442  51  ASN   A O   
384  C CB  . ASN   A 51  ? 0.90509 0.96959 0.67231 0.00000  0.16245  -0.02139 51  ASN   A CB  
385  C CG  . ASN   A 51  ? 0.89182 0.96212 0.70303 0.00376  0.16994  -0.01951 51  ASN   A CG  
386  O OD1 . ASN   A 51  ? 0.86145 0.93284 0.69125 0.00131  0.15728  -0.00910 51  ASN   A OD1 
387  N ND2 . ASN   A 51  ? 0.93943 1.01047 0.76900 0.01104  0.19128  -0.02854 51  ASN   A ND2 
388  N N   . PRO   A 52  ? 0.84568 0.89541 0.62150 -0.01161 0.11780  0.02227  52  PRO   A N   
389  C CA  . PRO   A 52  ? 0.75808 0.80723 0.54542 -0.02026 0.11365  0.04020  52  PRO   A CA  
390  C C   . PRO   A 52  ? 0.68303 0.74480 0.50661 -0.02406 0.12434  0.04610  52  PRO   A C   
391  O O   . PRO   A 52  ? 0.77863 0.84848 0.61958 -0.02180 0.13713  0.03586  52  PRO   A O   
392  C CB  . PRO   A 52  ? 0.70381 0.74642 0.49512 -0.02370 0.08822  0.04250  52  PRO   A CB  
393  C CG  . PRO   A 52  ? 0.66815 0.70491 0.46144 -0.01818 0.08357  0.02707  52  PRO   A CG  
394  C CD  . PRO   A 52  ? 0.77255 0.81156 0.54900 -0.01254 0.09858  0.01297  52  PRO   A CD  
395  N N   . ASN   A 53  ? 0.61751 0.68990 0.46121 -0.03041 0.11555  0.06247  53  ASN   A N   
396  C CA  . ASN   A 53  ? 0.56222 0.65497 0.44837 -0.03144 0.12029  0.07319  53  ASN   A CA  
397  C C   . ASN   A 53  ? 0.51334 0.60642 0.41490 -0.03701 0.10452  0.08901  53  ASN   A C   
398  O O   . ASN   A 53  ? 0.48029 0.57659 0.38330 -0.04177 0.10816  0.10128  53  ASN   A O   
399  C CB  . ASN   A 53  ? 0.55364 0.65893 0.44477 -0.03258 0.14186  0.07531  53  ASN   A CB  
400  C CG  . ASN   A 53  ? 0.53829 0.66355 0.47621 -0.03320 0.14431  0.08965  53  ASN   A CG  
401  O OD1 . ASN   A 53  ? 0.49553 0.62516 0.46398 -0.03320 0.13153  0.09559  53  ASN   A OD1 
402  N ND2 . ASN   A 53  ? 0.61137 0.74832 0.55471 -0.03514 0.16054  0.09474  53  ASN   A ND2 
403  N N   . TYR   A 54  ? 0.46421 0.55333 0.37816 -0.03664 0.08805  0.08825  54  TYR   A N   
404  C CA  . TYR   A 54  ? 0.43787 0.51793 0.35381 -0.04093 0.07224  0.09718  54  TYR   A CA  
405  C C   . TYR   A 54  ? 0.43146 0.51875 0.38072 -0.04660 0.07338  0.11220  54  TYR   A C   
406  O O   . TYR   A 54  ? 0.42197 0.50197 0.37140 -0.04965 0.06730  0.12205  54  TYR   A O   
407  C CB  . TYR   A 54  ? 0.39367 0.46570 0.31186 -0.03942 0.05618  0.08979  54  TYR   A CB  
408  C CG  . TYR   A 54  ? 0.37300 0.43286 0.25911 -0.03470 0.05129  0.07547  54  TYR   A CG  
409  C CD1 . TYR   A 54  ? 0.37924 0.44054 0.25845 -0.03004 0.05805  0.06235  54  TYR   A CD1 
410  C CD2 . TYR   A 54  ? 0.36845 0.41637 0.23664 -0.03445 0.04059  0.07551  54  TYR   A CD2 
411  C CE1 . TYR   A 54  ? 0.40606 0.45287 0.25953 -0.02635 0.05349  0.04856  54  TYR   A CE1 
412  C CE2 . TYR   A 54  ? 0.41881 0.45656 0.26460 -0.03058 0.03527  0.06282  54  TYR   A CE2 
413  C CZ  . TYR   A 54  ? 0.42569 0.46119 0.26344 -0.02681 0.04133  0.04903  54  TYR   A CZ  
414  O OH  . TYR   A 54  ? 0.43645 0.46160 0.25610 -0.02314 0.03580  0.03671  54  TYR   A OH  
415  N N   . GLU   A 55  ? 0.44223 0.54363 0.42317 -0.04783 0.08078  0.11388  55  GLU   A N   
416  C CA  . GLU   A 55  ? 0.43045 0.53769 0.44389 -0.05441 0.08307  0.12594  55  GLU   A CA  
417  C C   . GLU   A 55  ? 0.45283 0.56006 0.45234 -0.05609 0.09255  0.13675  55  GLU   A C   
418  O O   . GLU   A 55  ? 0.44054 0.54063 0.44800 -0.06034 0.08753  0.14776  55  GLU   A O   
419  C CB  . GLU   A 55  ? 0.44820 0.57377 0.49595 -0.05479 0.09001  0.12422  55  GLU   A CB  
420  C CG  . GLU   A 55  ? 0.50332 0.63319 0.56420 -0.05287 0.08033  0.11444  55  GLU   A CG  
421  C CD  . GLU   A 55  ? 0.51610 0.65007 0.55661 -0.04244 0.08811  0.10451  55  GLU   A CD  
422  O OE1 . GLU   A 55  ? 0.53844 0.68063 0.59812 -0.03830 0.08385  0.09736  55  GLU   A OE1 
423  O OE2 . GLU   A 55  ? 0.54791 0.67312 0.55261 -0.03828 0.09652  0.10080  55  GLU   A OE2 
424  N N   . ASP   A 56  ? 0.48680 0.60185 0.46609 -0.05292 0.10728  0.13358  56  ASP   A N   
425  C CA  . ASP   A 56  ? 0.50574 0.62186 0.46547 -0.05548 0.11643  0.14317  56  ASP   A CA  
426  C C   . ASP   A 56  ? 0.47834 0.58111 0.41155 -0.05611 0.10484  0.14781  56  ASP   A C   
427  O O   . ASP   A 56  ? 0.45351 0.55717 0.38855 -0.05961 0.10491  0.16279  56  ASP   A O   
428  C CB  . ASP   A 56  ? 0.55580 0.67830 0.49017 -0.05259 0.13425  0.13401  56  ASP   A CB  
429  C CG  . ASP   A 56  ? 0.58940 0.73014 0.55087 -0.05348 0.15061  0.13902  56  ASP   A CG  
430  O OD1 . ASP   A 56  ? 0.51300 0.66002 0.49892 -0.05853 0.15035  0.15415  56  ASP   A OD1 
431  O OD2 . ASP   A 56  ? 0.63793 0.78663 0.59841 -0.04876 0.16395  0.12774  56  ASP   A OD2 
432  N N   . LEU   A 57  ? 0.41953 0.51163 0.32976 -0.05229 0.09493  0.13589  57  LEU   A N   
433  C CA  . LEU   A 57  ? 0.46214 0.54475 0.35167 -0.05215 0.08270  0.14020  57  LEU   A CA  
434  C C   . LEU   A 57  ? 0.41240 0.49052 0.33099 -0.05398 0.07108  0.15241  57  LEU   A C   
435  O O   . LEU   A 57  ? 0.43160 0.50871 0.34669 -0.05495 0.06645  0.16490  57  LEU   A O   
436  C CB  . LEU   A 57  ? 0.48237 0.55486 0.34666 -0.04769 0.07373  0.12381  57  LEU   A CB  
437  C CG  . LEU   A 57  ? 0.49527 0.56618 0.32871 -0.04507 0.08550  0.10891  57  LEU   A CG  
438  C CD1 . LEU   A 57  ? 0.59538 0.65448 0.40769 -0.04092 0.07374  0.09457  57  LEU   A CD1 
439  C CD2 . LEU   A 57  ? 0.53197 0.60752 0.34055 -0.04801 0.09760  0.11561  57  LEU   A CD2 
440  N N   . LEU   A 58  ? 0.42000 0.49554 0.36867 -0.05472 0.06714  0.14916  58  LEU   A N   
441  C CA  . LEU   A 58  ? 0.40642 0.47204 0.38020 -0.05640 0.05715  0.15640  58  LEU   A CA  
442  C C   . LEU   A 58  ? 0.40867 0.47647 0.40935 -0.06127 0.06359  0.17204  58  LEU   A C   
443  O O   . LEU   A 58  ? 0.36554 0.42463 0.37925 -0.06157 0.05830  0.18200  58  LEU   A O   
444  C CB  . LEU   A 58  ? 0.37983 0.43948 0.37261 -0.05705 0.05012  0.14512  58  LEU   A CB  
445  C CG  . LEU   A 58  ? 0.39244 0.43699 0.40755 -0.05878 0.04071  0.14707  58  LEU   A CG  
446  C CD1 . LEU   A 58  ? 0.35673 0.39369 0.35463 -0.05340 0.03243  0.15008  58  LEU   A CD1 
447  C CD2 . LEU   A 58  ? 0.37587 0.41595 0.40461 -0.06125 0.03415  0.13371  58  LEU   A CD2 
448  N N   . ILE   A 59  ? 0.42033 0.49984 0.43195 -0.06465 0.07559  0.17462  59  ILE   A N   
449  C CA  . ILE   A 59  ? 0.41198 0.49393 0.44979 -0.06981 0.08190  0.18960  59  ILE   A CA  
450  C C   . ILE   A 59  ? 0.40986 0.49512 0.42981 -0.06874 0.08463  0.20571  59  ILE   A C   
451  O O   . ILE   A 59  ? 0.45198 0.53608 0.49360 -0.07181 0.08691  0.22117  59  ILE   A O   
452  C CB  . ILE   A 59  ? 0.40017 0.49675 0.45628 -0.07364 0.09387  0.18848  59  ILE   A CB  
453  C CG1 . ILE   A 59  ? 0.41833 0.51457 0.50931 -0.08055 0.09762  0.20125  59  ILE   A CG1 
454  C CG2 . ILE   A 59  ? 0.42390 0.53473 0.45178 -0.07095 0.10702  0.18997  59  ILE   A CG2 
455  C CD1 . ILE   A 59  ? 0.45703 0.53676 0.57845 -0.08554 0.08754  0.19596  59  ILE   A CD1 
456  N N   . ARG   A 60  ? 0.41523 0.50436 0.39678 -0.06505 0.08374  0.20244  60  ARG   A N   
457  C CA  . ARG   A 60  ? 0.41256 0.50784 0.37481 -0.06521 0.08481  0.21754  60  ARG   A CA  
458  C C   . ARG   A 60  ? 0.41181 0.49984 0.37762 -0.06244 0.07126  0.22572  60  ARG   A C   
459  O O   . ARG   A 60  ? 0.43857 0.53452 0.39649 -0.06287 0.07078  0.24211  60  ARG   A O   
460  C CB  . ARG   A 60  ? 0.43191 0.53427 0.35026 -0.06429 0.09060  0.20865  60  ARG   A CB  
461  C CG  . ARG   A 60  ? 0.44503 0.55741 0.35993 -0.06668 0.10824  0.20541  60  ARG   A CG  
462  C CD  . ARG   A 60  ? 0.45145 0.56311 0.33117 -0.06431 0.11513  0.18629  60  ARG   A CD  
463  N NE  . ARG   A 60  ? 0.52563 0.64806 0.40875 -0.06606 0.13452  0.18411  60  ARG   A NE  
464  C CZ  . ARG   A 60  ? 0.57875 0.70189 0.43533 -0.06448 0.14784  0.16890  60  ARG   A CZ  
465  N NH1 . ARG   A 60  ? 0.59303 0.70434 0.41596 -0.06119 0.14293  0.15378  60  ARG   A NH1 
466  N NH2 . ARG   A 60  ? 0.54968 0.68502 0.41600 -0.06597 0.16679  0.16850  60  ARG   A NH2 
467  N N   . LYS   A 61  ? 0.42251 0.49772 0.40134 -0.05962 0.06103  0.21571  61  LYS   A N   
468  C CA  . LYS   A 61  ? 0.42081 0.48989 0.40487 -0.05590 0.04936  0.22145  61  LYS   A CA  
469  C C   . LYS   A 61  ? 0.44918 0.50877 0.47401 -0.05636 0.04977  0.23409  61  LYS   A C   
470  O O   . LYS   A 61  ? 0.42435 0.47504 0.47394 -0.05978 0.05458  0.22900  61  LYS   A O   
471  C CB  . LYS   A 61  ? 0.44756 0.50720 0.42278 -0.05221 0.03947  0.20289  61  LYS   A CB  
472  C CG  . LYS   A 61  ? 0.43751 0.50048 0.38151 -0.05182 0.04093  0.18495  61  LYS   A CG  
473  C CD  . LYS   A 61  ? 0.46134 0.53167 0.36984 -0.05078 0.03705  0.18400  61  LYS   A CD  
474  C CE  . LYS   A 61  ? 0.51601 0.58426 0.42801 -0.04774 0.02376  0.18733  61  LYS   A CE  
475  N NZ  . LYS   A 61  ? 0.53445 0.61138 0.41432 -0.04839 0.01834  0.18538  61  LYS   A NZ  
476  N N   . SER   A 62  ? 0.44231 0.50407 0.47566 -0.05330 0.04491  0.25015  62  SER   A N   
477  C CA  . SER   A 62  ? 0.47409 0.52371 0.54682 -0.05167 0.04509  0.26077  62  SER   A CA  
478  C C   . SER   A 62  ? 0.52061 0.55898 0.60030 -0.04610 0.03590  0.25219  62  SER   A C   
479  O O   . SER   A 62  ? 0.49550 0.54122 0.55062 -0.04319 0.02773  0.24609  62  SER   A O   
480  C CB  . SER   A 62  ? 0.45593 0.51760 0.54041 -0.05093 0.04770  0.28769  62  SER   A CB  
481  O OG  . SER   A 62  ? 0.49611 0.57238 0.56568 -0.05573 0.05581  0.29676  62  SER   A OG  
482  N N   . ASN   A 63  ? 0.48645 0.50616 0.60043 -0.04517 0.03823  0.25078  63  ASN   A N   
483  C CA  . ASN   A 63  ? 0.46227 0.46974 0.58564 -0.03969 0.03226  0.24205  63  ASN   A CA  
484  C C   . ASN   A 63  ? 0.47946 0.50206 0.59647 -0.03353 0.02500  0.25556  63  ASN   A C   
485  O O   . ASN   A 63  ? 0.44749 0.47038 0.55278 -0.02998 0.01745  0.24539  63  ASN   A O   
486  C CB  . ASN   A 63  ? 0.45411 0.43923 0.61726 -0.03965 0.03873  0.24163  63  ASN   A CB  
487  C CG  . ASN   A 63  ? 0.43252 0.40038 0.60155 -0.04720 0.04268  0.22115  63  ASN   A CG  
488  O OD1 . ASN   A 63  ? 0.41919 0.39180 0.56528 -0.05065 0.03947  0.20683  63  ASN   A OD1 
489  N ND2 . ASN   A 63  ? 0.41026 0.35881 0.61187 -0.05053 0.04978  0.21956  63  ASN   A ND2 
490  N N   . HIS   A 64  ? 0.46835 0.50573 0.59428 -0.03293 0.02688  0.27938  64  HIS   A N   
491  C CA  . HIS   A 64  ? 0.46793 0.52330 0.59243 -0.02845 0.01933  0.29446  64  HIS   A CA  
492  C C   . HIS   A 64  ? 0.49903 0.57213 0.58045 -0.03121 0.01065  0.28731  64  HIS   A C   
493  O O   . HIS   A 64  ? 0.46850 0.55802 0.54603 -0.02946 0.00281  0.29720  64  HIS   A O   
494  C CB  . HIS   A 64  ? 0.47584 0.54449 0.62407 -0.02756 0.02347  0.32415  64  HIS   A CB  
495  C CG  . HIS   A 64  ? 0.57744 0.65944 0.70551 -0.03379 0.02764  0.33338  64  HIS   A CG  
496  N ND1 . HIS   A 64  ? 0.58046 0.68772 0.67843 -0.03667 0.02232  0.34408  64  HIS   A ND1 
497  C CD2 . HIS   A 64  ? 0.51097 0.58498 0.64423 -0.03843 0.03738  0.33270  64  HIS   A CD2 
498  C CE1 . HIS   A 64  ? 0.55870 0.67224 0.64307 -0.04197 0.02970  0.34980  64  HIS   A CE1 
499  N NE2 . HIS   A 64  ? 0.52950 0.62405 0.63620 -0.04294 0.03889  0.34367  64  HIS   A NE2 
500  N N   . ASN   A 65  ? 0.52028 0.59055 0.57141 -0.03584 0.01235  0.27005  65  ASN   A N   
501  C CA  . ASN   A 65  ? 0.51406 0.59563 0.52537 -0.03811 0.00547  0.25867  65  ASN   A CA  
502  C C   . ASN   A 65  ? 0.48560 0.55927 0.49269 -0.03477 -0.00267 0.24100  65  ASN   A C   
503  O O   . ASN   A 65  ? 0.48568 0.56979 0.46857 -0.03597 -0.01030 0.23560  65  ASN   A O   
504  C CB  . ASN   A 65  ? 0.49599 0.57625 0.47983 -0.04291 0.01227  0.24595  65  ASN   A CB  
505  C CG  . ASN   A 65  ? 0.50934 0.60013 0.49336 -0.04676 0.02116  0.26344  65  ASN   A CG  
506  O OD1 . ASN   A 65  ? 0.52678 0.61176 0.51509 -0.04947 0.03076  0.25976  65  ASN   A OD1 
507  N ND2 . ASN   A 65  ? 0.55462 0.66312 0.53611 -0.04748 0.01806  0.28404  65  ASN   A ND2 
508  N N   . PHE   A 66  ? 0.44699 0.50237 0.47709 -0.03131 -0.00087 0.23184  66  PHE   A N   
509  C CA  . PHE   A 66  ? 0.47848 0.52621 0.50527 -0.02805 -0.00738 0.21550  66  PHE   A CA  
510  C C   . PHE   A 66  ? 0.45329 0.50549 0.50586 -0.02290 -0.01114 0.22850  66  PHE   A C   
511  O O   . PHE   A 66  ? 0.44174 0.48396 0.52795 -0.01919 -0.00538 0.23743  66  PHE   A O   
512  C CB  . PHE   A 66  ? 0.43467 0.46173 0.47012 -0.02781 -0.00320 0.19847  66  PHE   A CB  
513  C CG  . PHE   A 66  ? 0.42251 0.44810 0.43898 -0.03276 0.00107  0.18750  66  PHE   A CG  
514  C CD1 . PHE   A 66  ? 0.39076 0.41935 0.37854 -0.03349 -0.00286 0.17106  66  PHE   A CD1 
515  C CD2 . PHE   A 66  ? 0.42887 0.45085 0.45951 -0.03665 0.01001  0.19419  66  PHE   A CD2 
516  C CE1 . PHE   A 66  ? 0.45276 0.48187 0.42698 -0.03711 0.00258  0.16236  66  PHE   A CE1 
517  C CE2 . PHE   A 66  ? 0.39664 0.42051 0.41400 -0.04128 0.01507  0.18547  66  PHE   A CE2 
518  C CZ  . PHE   A 66  ? 0.41150 0.43964 0.40103 -0.04107 0.01168  0.17019  66  PHE   A CZ  
519  N N   . LEU   A 67  ? 0.44320 0.51010 0.48234 -0.02295 -0.01983 0.22926  67  LEU   A N   
520  C CA  . LEU   A 67  ? 0.43947 0.51417 0.50388 -0.01837 -0.02357 0.24137  67  LEU   A CA  
521  C C   . LEU   A 67  ? 0.44838 0.51057 0.51357 -0.01498 -0.02592 0.22266  67  LEU   A C   
522  O O   . LEU   A 67  ? 0.42392 0.48775 0.46205 -0.01770 -0.03181 0.20671  67  LEU   A O   
523  C CB  . LEU   A 67  ? 0.44336 0.54484 0.49600 -0.02214 -0.03196 0.25591  67  LEU   A CB  
524  C CG  . LEU   A 67  ? 0.46857 0.58399 0.51097 -0.02680 -0.03001 0.27244  67  LEU   A CG  
525  C CD1 . LEU   A 67  ? 0.40596 0.55333 0.43844 -0.03244 -0.03947 0.28986  67  LEU   A CD1 
526  C CD2 . LEU   A 67  ? 0.45127 0.56161 0.52899 -0.02282 -0.02092 0.29113  67  LEU   A CD2 
527  N N   . VAL   A 68  ? 0.44815 0.49681 0.54491 -0.00899 -0.02013 0.22429  68  VAL   A N   
528  C CA  . VAL   A 68  ? 0.44192 0.47613 0.54101 -0.00550 -0.01996 0.20685  68  VAL   A CA  
529  C C   . VAL   A 68  ? 0.41815 0.45898 0.54767 0.00067  -0.01922 0.21902  68  VAL   A C   
530  O O   . VAL   A 68  ? 0.41182 0.44871 0.57587 0.00549  -0.01128 0.23350  68  VAL   A O   
531  C CB  . VAL   A 68  ? 0.43370 0.44222 0.54104 -0.00484 -0.01159 0.19390  68  VAL   A CB  
532  C CG1 . VAL   A 68  ? 0.34458 0.33997 0.45267 -0.00157 -0.01155 0.17714  68  VAL   A CG1 
533  C CG2 . VAL   A 68  ? 0.42387 0.42961 0.50509 -0.01133 -0.01183 0.18436  68  VAL   A CG2 
534  N N   . GLN   A 69  ? 0.38682 0.43689 0.50646 0.00064  -0.02608 0.21295  69  GLN   A N   
535  C CA  . GLN   A 69  ? 0.46236 0.52527 0.61035 0.00532  -0.02620 0.22747  69  GLN   A CA  
536  C C   . GLN   A 69  ? 0.43553 0.48634 0.58690 0.00948  -0.02413 0.21199  69  GLN   A C   
537  O O   . GLN   A 69  ? 0.34370 0.39413 0.46794 0.00582  -0.03045 0.19552  69  GLN   A O   
538  C CB  . GLN   A 69  ? 0.47959 0.57454 0.62018 -0.00095 -0.03704 0.24240  69  GLN   A CB  
539  C CG  . GLN   A 69  ? 0.53718 0.65435 0.71401 0.00216  -0.03738 0.26787  69  GLN   A CG  
540  C CD  . GLN   A 69  ? 0.60180 0.75213 0.76787 -0.00688 -0.04924 0.28363  69  GLN   A CD  
541  O OE1 . GLN   A 69  ? 0.55974 0.72854 0.73271 -0.00978 -0.05557 0.28993  69  GLN   A OE1 
542  N NE2 . GLN   A 69  ? 0.60572 0.76398 0.75375 -0.01233 -0.05206 0.29036  69  GLN   A NE2 
543  N N   . ALA   A 70  ? 0.44940 0.49028 0.63610 0.01724  -0.01386 0.21765  70  ALA   A N   
544  C CA  . ALA   A 70  ? 0.46399 0.49573 0.65995 0.02232  -0.00961 0.20706  70  ALA   A CA  
545  C C   . ALA   A 70  ? 0.48353 0.53468 0.71377 0.02717  -0.00744 0.22794  70  ALA   A C   
546  O O   . ALA   A 70  ? 0.45455 0.50249 0.72315 0.03378  0.00378  0.24226  70  ALA   A O   
547  C CB  . ALA   A 70  ? 0.39835 0.40005 0.60743 0.02692  0.00333  0.19384  70  ALA   A CB  
548  N N   . GLY   A 71  ? 0.53003 0.60125 0.74889 0.02342  -0.01730 0.23005  71  GLY   A N   
549  C CA  . GLY   A 71  ? 0.53315 0.63027 0.78543 0.02541  -0.01754 0.25432  71  GLY   A CA  
550  C C   . GLY   A 71  ? 0.62449 0.74472 0.89036 0.02209  -0.02180 0.27994  71  GLY   A C   
551  O O   . GLY   A 71  ? 0.61371 0.73655 0.85358 0.01543  -0.02861 0.27783  71  GLY   A O   
552  N N   . ASN   A 72  ? 0.63563 0.77403 0.94405 0.02696  -0.01696 0.30588  72  ASN   A N   
553  C CA  . ASN   A 72  ? 0.67250 0.83100 1.00161 0.02598  -0.01816 0.33321  72  ASN   A CA  
554  C C   . ASN   A 72  ? 0.64508 0.77933 0.99388 0.03365  -0.00445 0.33394  72  ASN   A C   
555  O O   . ASN   A 72  ? 0.63772 0.78325 1.02495 0.03825  0.00195  0.35951  72  ASN   A O   
556  C CB  . ASN   A 72  ? 0.71994 0.91155 1.08938 0.02726  -0.01917 0.36422  72  ASN   A CB  
557  C CG  . ASN   A 72  ? 0.74812 0.93004 1.15300 0.03740  -0.00585 0.36435  72  ASN   A CG  
558  O OD1 . ASN   A 72  ? 0.75670 0.90639 1.15429 0.04333  0.00417  0.34012  72  ASN   A OD1 
559  N ND2 . ASN   A 72  ? 0.74023 0.95109 1.18403 0.03901  -0.00522 0.39271  72  ASN   A ND2 
560  N N   . VAL   A 73  ? 0.60723 0.70958 0.93341 0.03427  0.00049  0.30763  73  VAL   A N   
561  C CA  . VAL   A 73  ? 0.59666 0.67474 0.93944 0.03859  0.01311  0.30556  73  VAL   A CA  
562  C C   . VAL   A 73  ? 0.56923 0.63270 0.86801 0.03119  0.00684  0.28529  73  VAL   A C   
563  O O   . VAL   A 73  ? 0.56362 0.61207 0.83335 0.02881  0.00415  0.26064  73  VAL   A O   
564  C CB  . VAL   A 73  ? 0.61733 0.66731 0.98795 0.04730  0.03037  0.29322  73  VAL   A CB  
565  C CG1 . VAL   A 73  ? 0.59285 0.61119 0.96437 0.04741  0.04085  0.27948  73  VAL   A CG1 
566  C CG2 . VAL   A 73  ? 0.58578 0.64775 1.01001 0.05599  0.04171  0.31752  73  VAL   A CG2 
567  N N   . GLN   A 74  ? 0.56615 0.63556 0.86076 0.02747  0.00484  0.29686  74  GLN   A N   
568  C CA  . GLN   A 74  ? 0.56574 0.62457 0.81997 0.02011  -0.00033 0.27991  74  GLN   A CA  
569  C C   . GLN   A 74  ? 0.51033 0.54187 0.77843 0.02164  0.01174  0.27378  74  GLN   A C   
570  O O   . GLN   A 74  ? 0.47944 0.50848 0.78479 0.02615  0.02144  0.29086  74  GLN   A O   
571  C CB  . GLN   A 74  ? 0.60102 0.68570 0.83102 0.01257  -0.01161 0.29298  74  GLN   A CB  
572  C CG  . GLN   A 74  ? 0.55397 0.65782 0.81105 0.01366  -0.00977 0.32350  74  GLN   A CG  
573  C CD  . GLN   A 74  ? 0.66423 0.79225 0.88819 0.00462  -0.02123 0.33170  74  GLN   A CD  
574  O OE1 . GLN   A 74  ? 0.66176 0.78971 0.84525 -0.00207 -0.02881 0.31310  74  GLN   A OE1 
575  N NE2 . GLN   A 74  ? 0.72528 0.87555 0.96861 0.00418  -0.02163 0.36063  74  GLN   A NE2 
576  N N   . LEU   A 75  ? 0.47783 0.48906 0.71804 0.01730  0.01146  0.24941  75  LEU   A N   
577  C CA  . LEU   A 75  ? 0.47147 0.45399 0.72201 0.01641  0.02235  0.23766  75  LEU   A CA  
578  C C   . LEU   A 75  ? 0.49363 0.47896 0.73539 0.01030  0.02189  0.24571  75  LEU   A C   
579  O O   . LEU   A 75  ? 0.49334 0.50009 0.71039 0.00604  0.01264  0.25407  75  LEU   A O   
580  C CB  . LEU   A 75  ? 0.44486 0.40754 0.67115 0.01342  0.02158  0.20908  75  LEU   A CB  
581  C CG  . LEU   A 75  ? 0.46127 0.42014 0.69508 0.01939  0.02330  0.20026  75  LEU   A CG  
582  C CD1 . LEU   A 75  ? 0.42737 0.37452 0.63004 0.01555  0.01873  0.17528  75  LEU   A CD1 
583  C CD2 . LEU   A 75  ? 0.46738 0.40739 0.74299 0.02590  0.03935  0.20148  75  LEU   A CD2 
584  N N   . ARG   A 76  ? 0.47633 0.43896 0.73834 0.00902  0.03296  0.24167  76  ARG   A N   
585  C CA  . ARG   A 76  ? 0.50370 0.46647 0.76387 0.00304  0.03509  0.24969  76  ARG   A CA  
586  C C   . ARG   A 76  ? 0.45482 0.40117 0.68987 -0.00539 0.03472  0.22616  76  ARG   A C   
587  O O   . ARG   A 76  ? 0.45011 0.37163 0.69473 -0.00720 0.04135  0.20728  76  ARG   A O   
588  C CB  . ARG   A 76  ? 0.53192 0.48210 0.83703 0.00623  0.04817  0.26338  76  ARG   A CB  
589  C CG  . ARG   A 76  ? 0.59526 0.54458 0.90507 0.00010  0.05209  0.27380  76  ARG   A CG  
590  C CD  . ARG   A 76  ? 0.64122 0.62224 0.92993 -0.00171 0.04291  0.29474  76  ARG   A CD  
591  N NE  . ARG   A 76  ? 0.68669 0.69324 0.97934 0.00451  0.03593  0.31268  76  ARG   A NE  
592  C CZ  . ARG   A 76  ? 0.68074 0.69763 1.01159 0.01096  0.04052  0.33769  76  ARG   A CZ  
593  N NH1 . ARG   A 76  ? 0.69957 0.70098 1.06865 0.01298  0.05307  0.34734  76  ARG   A NH1 
594  N NH2 . ARG   A 76  ? 0.73543 0.77895 1.06837 0.01477  0.03276  0.35353  76  ARG   A NH2 
595  N N   . VAL   A 77  ? 0.42474 0.38597 0.62843 -0.01112 0.02760  0.22683  77  VAL   A N   
596  C CA  . VAL   A 77  ? 0.45050 0.40124 0.63404 -0.01931 0.02769  0.20800  77  VAL   A CA  
597  C C   . VAL   A 77  ? 0.44814 0.38682 0.65345 -0.02515 0.03717  0.21194  77  VAL   A C   
598  O O   . VAL   A 77  ? 0.45508 0.40616 0.66768 -0.02554 0.03939  0.23188  77  VAL   A O   
599  C CB  . VAL   A 77  ? 0.45592 0.42709 0.60087 -0.02267 0.01910  0.20688  77  VAL   A CB  
600  C CG1 . VAL   A 77  ? 0.41445 0.37802 0.54542 -0.03080 0.02095  0.19074  77  VAL   A CG1 
601  C CG2 . VAL   A 77  ? 0.42624 0.40678 0.55048 -0.01844 0.00976  0.19971  77  VAL   A CG2 
602  N N   . ILE   A 78  ? 0.41180 0.32704 0.62755 -0.03077 0.04260  0.19252  78  ILE   A N   
603  C CA  . ILE   A 78  ? 0.40279 0.30408 0.64121 -0.03844 0.05142  0.19206  78  ILE   A CA  
604  C C   . ILE   A 78  ? 0.41249 0.31337 0.63432 -0.04997 0.04963  0.17619  78  ILE   A C   
605  O O   . ILE   A 78  ? 0.38136 0.27129 0.62050 -0.05901 0.05569  0.17152  78  ILE   A O   
606  C CB  . ILE   A 78  ? 0.43601 0.31025 0.70620 -0.03768 0.06070  0.18206  78  ILE   A CB  
607  C CG1 . ILE   A 78  ? 0.43356 0.29103 0.69131 -0.04270 0.05906  0.15213  78  ILE   A CG1 
608  C CG2 . ILE   A 78  ? 0.40891 0.28685 0.69918 -0.02497 0.06340  0.19832  78  ILE   A CG2 
609  C CD1 . ILE   A 78  ? 0.43840 0.27005 0.72149 -0.04094 0.06883  0.13906  78  ILE   A CD1 
610  N N   . GLY   A 79  ? 0.39429 0.30831 0.58536 -0.05026 0.04157  0.16816  79  GLY   A N   
611  C CA  . GLY   A 79  ? 0.38262 0.30211 0.56093 -0.06004 0.04007  0.15614  79  GLY   A CA  
612  C C   . GLY   A 79  ? 0.37537 0.30783 0.52295 -0.05762 0.03166  0.14772  79  GLY   A C   
613  O O   . GLY   A 79  ? 0.34078 0.27179 0.47800 -0.05025 0.02653  0.14496  79  GLY   A O   
614  N N   . HIS   A 80  ? 0.32547 0.27170 0.46058 -0.06347 0.03079  0.14416  80  HIS   A N   
615  C CA  . HIS   A 80  ? 0.33524 0.29397 0.44358 -0.06116 0.02387  0.13657  80  HIS   A CA  
616  C C   . HIS   A 80  ? 0.29833 0.26419 0.40973 -0.07054 0.02426  0.12474  80  HIS   A C   
617  O O   . HIS   A 80  ? 0.27270 0.24078 0.40146 -0.07795 0.03007  0.12691  80  HIS   A O   
618  C CB  . HIS   A 80  ? 0.31888 0.29692 0.40225 -0.05488 0.02252  0.15020  80  HIS   A CB  
619  C CG  . HIS   A 80  ? 0.34146 0.33142 0.42784 -0.05836 0.03010  0.16298  80  HIS   A CG  
620  N ND1 . HIS   A 80  ? 0.37375 0.36099 0.47809 -0.05822 0.03535  0.17884  80  HIS   A ND1 
621  C CD2 . HIS   A 80  ? 0.35682 0.36197 0.43292 -0.06189 0.03448  0.16269  80  HIS   A CD2 
622  C CE1 . HIS   A 80  ? 0.36059 0.36092 0.46331 -0.06194 0.04198  0.18810  80  HIS   A CE1 
623  N NE2 . HIS   A 80  ? 0.33374 0.34499 0.41939 -0.06402 0.04223  0.17798  80  HIS   A NE2 
624  N N   . SER   A 81  ? 0.26820 0.24037 0.36444 -0.07022 0.01741  0.11331  81  SER   A N   
625  C CA  . SER   A 81  ? 0.28263 0.26816 0.38320 -0.07806 0.01607  0.10350  81  SER   A CA  
626  C C   . SER   A 81  ? 0.26494 0.26207 0.34207 -0.07396 0.00869  0.09851  81  SER   A C   
627  O O   . SER   A 81  ? 0.26502 0.25295 0.32909 -0.06930 0.00181  0.09385  81  SER   A O   
628  C CB  . SER   A 81  ? 0.25206 0.22708 0.37394 -0.08864 0.01351  0.08550  81  SER   A CB  
629  O OG  . SER   A 81  ? 0.29994 0.26405 0.41334 -0.08715 0.00579  0.07117  81  SER   A OG  
630  N N   . MET   A 82  ? 0.25779 0.27514 0.33102 -0.07555 0.01089  0.09917  82  MET   A N   
631  C CA  . MET   A 82  ? 0.25381 0.28122 0.30194 -0.06804 0.00562  0.08974  82  MET   A CA  
632  C C   . MET   A 82  ? 0.24395 0.27769 0.30215 -0.07105 -0.00262 0.07165  82  MET   A C   
633  O O   . MET   A 82  ? 0.19384 0.23744 0.27674 -0.07984 -0.00157 0.06978  82  MET   A O   
634  C CB  . MET   A 82  ? 0.25368 0.29831 0.28849 -0.06408 0.01550  0.09856  82  MET   A CB  
635  C CG  . MET   A 82  ? 0.27957 0.33111 0.29124 -0.05566 0.01286  0.08684  82  MET   A CG  
636  S SD  . MET   A 82  ? 0.36000 0.42290 0.34638 -0.05114 0.02724  0.09625  82  MET   A SD  
637  C CE  . MET   A 82  ? 0.33812 0.41836 0.35702 -0.05732 0.04110  0.10702  82  MET   A CE  
638  N N   . GLN   A 83  ? 0.22561 0.25611 0.26556 -0.06475 -0.01151 0.05999  83  GLN   A N   
639  C CA  . GLN   A 83  ? 0.20942 0.24963 0.25503 -0.06673 -0.02026 0.04582  83  GLN   A CA  
640  C C   . GLN   A 83  ? 0.22207 0.26929 0.24675 -0.05592 -0.02256 0.04269  83  GLN   A C   
641  O O   . GLN   A 83  ? 0.23274 0.26860 0.23741 -0.05012 -0.02711 0.03929  83  GLN   A O   
642  C CB  . GLN   A 83  ? 0.19202 0.21835 0.23967 -0.07199 -0.02852 0.03341  83  GLN   A CB  
643  C CG  . GLN   A 83  ? 0.22251 0.26193 0.26946 -0.07433 -0.03889 0.02028  83  GLN   A CG  
644  C CD  . GLN   A 83  ? 0.24023 0.26605 0.28352 -0.07903 -0.04440 0.00557  83  GLN   A CD  
645  O OE1 . GLN   A 83  ? 0.22264 0.22700 0.26366 -0.07924 -0.04114 0.00513  83  GLN   A OE1 
646  N NE2 . GLN   A 83  ? 0.21241 0.24965 0.25499 -0.07709 -0.04819 -0.00598 83  GLN   A NE2 
647  N N   . ASN   A 84  ? 0.19770 0.26328 0.23039 -0.05326 -0.01851 0.04440  84  ASN   A N   
648  C CA  . ASN   A 84  ? 0.20312 0.27231 0.21975 -0.04258 -0.01689 0.04197  84  ASN   A CA  
649  C C   . ASN   A 84  ? 0.21037 0.26576 0.19910 -0.03756 -0.01130 0.04531  84  ASN   A C   
650  O O   . ASN   A 84  ? 0.21814 0.27418 0.20445 -0.03959 -0.00169 0.05458  84  ASN   A O   
651  C CB  . ASN   A 84  ? 0.15122 0.22158 0.16555 -0.04053 -0.02923 0.03268  84  ASN   A CB  
652  C CG  . ASN   A 84  ? 0.16942 0.25805 0.20918 -0.04862 -0.03652 0.03073  84  ASN   A CG  
653  O OD1 . ASN   A 84  ? 0.18767 0.29582 0.24808 -0.04863 -0.03216 0.03666  84  ASN   A OD1 
654  N ND2 . ASN   A 84  ? 0.12917 0.21307 0.16781 -0.05629 -0.04696 0.02248  84  ASN   A ND2 
655  N N   . CYS   A 85  ? 0.19041 0.23525 0.15795 -0.03254 -0.01766 0.03942  85  CYS   A N   
656  C CA  . CYS   A 85  ? 0.18804 0.22412 0.12883 -0.03015 -0.01391 0.04282  85  CYS   A CA  
657  C C   . CYS   A 85  ? 0.20931 0.23394 0.14219 -0.03298 -0.02094 0.04840  85  CYS   A C   
658  O O   . CYS   A 85  ? 0.24290 0.26001 0.16481 -0.02724 -0.01988 0.04420  85  CYS   A O   
659  C CB  . CYS   A 85  ? 0.21106 0.24391 0.13434 -0.02374 -0.01430 0.03394  85  CYS   A CB  
660  S SG  . CYS   A 85  ? 0.20624 0.25118 0.14412 -0.01801 -0.00207 0.03036  85  CYS   A SG  
661  N N   . VAL   A 86  ? 0.20128 0.22181 0.15372 -0.03754 -0.02399 0.05085  86  VAL   A N   
662  C CA  . VAL   A 86  ? 0.22573 0.23454 0.17755 -0.03853 -0.02765 0.05800  86  VAL   A CA  
663  C C   . VAL   A 86  ? 0.25343 0.26029 0.22358 -0.04403 -0.02048 0.07052  86  VAL   A C   
664  O O   . VAL   A 86  ? 0.21805 0.22959 0.20781 -0.04930 -0.01607 0.06864  86  VAL   A O   
665  C CB  . VAL   A 86  ? 0.23763 0.23716 0.19709 -0.03801 -0.03572 0.04821  86  VAL   A CB  
666  C CG1 . VAL   A 86  ? 0.19577 0.19757 0.14572 -0.03085 -0.03874 0.03492  86  VAL   A CG1 
667  C CG2 . VAL   A 86  ? 0.22060 0.21965 0.20266 -0.04468 -0.03504 0.04047  86  VAL   A CG2 
668  N N   . LEU   A 87  ? 0.24563 0.24739 0.21349 -0.04182 -0.01924 0.08214  87  LEU   A N   
669  C CA  . LEU   A 87  ? 0.24999 0.24594 0.23954 -0.04498 -0.01296 0.09451  87  LEU   A CA  
670  C C   . LEU   A 87  ? 0.26369 0.24233 0.27313 -0.04616 -0.01555 0.09222  87  LEU   A C   
671  O O   . LEU   A 87  ? 0.26824 0.24181 0.27053 -0.04071 -0.02145 0.08726  87  LEU   A O   
672  C CB  . LEU   A 87  ? 0.27974 0.28068 0.26054 -0.03941 -0.00960 0.10430  87  LEU   A CB  
673  C CG  . LEU   A 87  ? 0.35355 0.36525 0.32825 -0.04137 -0.00125 0.11290  87  LEU   A CG  
674  C CD1 . LEU   A 87  ? 0.31234 0.32732 0.27916 -0.03791 -0.00131 0.12315  87  LEU   A CD1 
675  C CD2 . LEU   A 87  ? 0.34837 0.35839 0.34938 -0.04828 0.00653  0.11998  87  LEU   A CD2 
676  N N   . LYS   A 88  ? 0.26753 0.23698 0.30346 -0.05269 -0.00930 0.09338  88  LYS   A N   
677  C CA  . LYS   A 88  ? 0.25120 0.20084 0.30801 -0.05317 -0.00711 0.08753  88  LYS   A CA  
678  C C   . LYS   A 88  ? 0.29792 0.24247 0.37045 -0.05046 0.00168  0.10098  88  LYS   A C   
679  O O   . LYS   A 88  ? 0.29119 0.23554 0.37833 -0.05699 0.00789  0.10362  88  LYS   A O   
680  C CB  . LYS   A 88  ? 0.25742 0.19973 0.32936 -0.06434 -0.00799 0.06868  88  LYS   A CB  
681  C CG  . LYS   A 88  ? 0.24508 0.20042 0.29602 -0.06312 -0.01752 0.05166  88  LYS   A CG  
682  C CD  . LYS   A 88  ? 0.25479 0.20751 0.31499 -0.07270 -0.02049 0.03035  88  LYS   A CD  
683  C CE  . LYS   A 88  ? 0.27058 0.23450 0.34737 -0.08407 -0.01899 0.02918  88  LYS   A CE  
684  N NZ  . LYS   A 88  ? 0.26801 0.23555 0.34625 -0.09291 -0.02475 0.00680  88  LYS   A NZ  
685  N N   . LEU   A 89  ? 0.27867 0.22206 0.34923 -0.04136 0.00117  0.11019  89  LEU   A N   
686  C CA  . LEU   A 89  ? 0.32060 0.26189 0.40777 -0.03826 0.00731  0.12523  89  LEU   A CA  
687  C C   . LEU   A 89  ? 0.32580 0.24467 0.43954 -0.03831 0.01360  0.11856  89  LEU   A C   
688  O O   . LEU   A 89  ? 0.31163 0.22234 0.42644 -0.03324 0.01224  0.11120  89  LEU   A O   
689  C CB  . LEU   A 89  ? 0.29737 0.25385 0.37186 -0.02994 0.00245  0.13828  89  LEU   A CB  
690  C CG  . LEU   A 89  ? 0.30976 0.28632 0.35435 -0.03049 -0.00271 0.14010  89  LEU   A CG  
691  C CD1 . LEU   A 89  ? 0.29584 0.28558 0.32843 -0.02504 -0.00873 0.14693  89  LEU   A CD1 
692  C CD2 . LEU   A 89  ? 0.32164 0.30529 0.36759 -0.03542 0.00356  0.14986  89  LEU   A CD2 
693  N N   . LYS   A 90  ? 0.33598 0.24493 0.47096 -0.04420 0.02133  0.11991  90  LYS   A N   
694  C CA  . LYS   A 90  ? 0.34707 0.23393 0.50763 -0.04429 0.02905  0.11305  90  LYS   A CA  
695  C C   . LYS   A 90  ? 0.37758 0.26695 0.55532 -0.03383 0.03285  0.13299  90  LYS   A C   
696  O O   . LYS   A 90  ? 0.40013 0.30299 0.58172 -0.03229 0.03333  0.15278  90  LYS   A O   
697  C CB  . LYS   A 90  ? 0.37058 0.24668 0.54787 -0.05576 0.03526  0.10617  90  LYS   A CB  
698  C CG  . LYS   A 90  ? 0.42425 0.27523 0.62366 -0.05844 0.04324  0.09225  90  LYS   A CG  
699  C CD  . LYS   A 90  ? 0.45276 0.29459 0.64122 -0.06934 0.04010  0.06369  90  LYS   A CD  
700  C CE  . LYS   A 90  ? 0.51436 0.33376 0.72253 -0.07802 0.04807  0.04843  90  LYS   A CE  
701  N NZ  . LYS   A 90  ? 0.54772 0.36425 0.74089 -0.09130 0.04233  0.02079  90  LYS   A NZ  
702  N N   . VAL   A 91  ? 0.37117 0.24991 0.56064 -0.02683 0.03594  0.12830  91  VAL   A N   
703  C CA  . VAL   A 91  ? 0.41980 0.30387 0.63140 -0.01667 0.03994  0.14760  91  VAL   A CA  
704  C C   . VAL   A 91  ? 0.40995 0.26966 0.65536 -0.01591 0.05334  0.14103  91  VAL   A C   
705  O O   . VAL   A 91  ? 0.41888 0.25781 0.66414 -0.02248 0.05795  0.11741  91  VAL   A O   
706  C CB  . VAL   A 91  ? 0.40214 0.30029 0.60268 -0.00785 0.03315  0.15142  91  VAL   A CB  
707  C CG1 . VAL   A 91  ? 0.39837 0.32167 0.56744 -0.00907 0.02086  0.15948  91  VAL   A CG1 
708  C CG2 . VAL   A 91  ? 0.34584 0.22858 0.53911 -0.00786 0.03421  0.12831  91  VAL   A CG2 
709  N N   . ASP   A 92  ? 0.41920 0.28273 0.69420 -0.00850 0.05988  0.16174  92  ASP   A N   
710  C CA  . ASP   A 92  ? 0.43664 0.27662 0.74802 -0.00762 0.07484  0.15754  92  ASP   A CA  
711  C C   . ASP   A 92  ? 0.45593 0.28368 0.78016 -0.00034 0.08276  0.14571  92  ASP   A C   
712  O O   . ASP   A 92  ? 0.44220 0.24879 0.79673 0.00078  0.09738  0.13954  92  ASP   A O   
713  C CB  . ASP   A 92  ? 0.42949 0.27822 0.77301 -0.00257 0.08055  0.18619  92  ASP   A CB  
714  C CG  . ASP   A 92  ? 0.45443 0.32934 0.80619 0.00876  0.07612  0.21098  92  ASP   A CG  
715  O OD1 . ASP   A 92  ? 0.44898 0.33381 0.78437 0.01312  0.06961  0.20587  92  ASP   A OD1 
716  O OD2 . ASP   A 92  ? 0.47121 0.35874 0.84695 0.01241  0.07871  0.23677  92  ASP   A OD2 
717  N N   . THR   A 93  ? 0.43326 0.27332 0.73593 0.00422  0.07467  0.14187  93  THR   A N   
718  C CA  . THR   A 93  ? 0.41350 0.24628 0.72845 0.01199  0.08251  0.13362  93  THR   A CA  
719  C C   . THR   A 93  ? 0.39092 0.21842 0.67262 0.00756  0.07628  0.10865  93  THR   A C   
720  O O   . THR   A 93  ? 0.35707 0.20091 0.60830 0.00507  0.06205  0.11032  93  THR   A O   
721  C CB  . THR   A 93  ? 0.40242 0.26106 0.73126 0.02325  0.07920  0.15961  93  THR   A CB  
722  O OG1 . THR   A 93  ? 0.45883 0.32844 0.81394 0.02580  0.08157  0.18571  93  THR   A OG1 
723  C CG2 . THR   A 93  ? 0.40659 0.25741 0.75942 0.03195  0.09169  0.15499  93  THR   A CG2 
724  N N   . ALA   A 94  ? 0.41919 0.22429 0.70647 0.00605  0.08756  0.08510  94  ALA   A N   
725  C CA  . ALA   A 94  ? 0.37309 0.17538 0.63145 0.00304  0.08283  0.06266  94  ALA   A CA  
726  C C   . ALA   A 94  ? 0.36370 0.18070 0.62460 0.01476  0.08193  0.07295  94  ALA   A C   
727  O O   . ALA   A 94  ? 0.37400 0.19256 0.66578 0.02402  0.09248  0.08618  94  ALA   A O   
728  C CB  . ALA   A 94  ? 0.39957 0.17554 0.65878 -0.00456 0.09498  0.03197  94  ALA   A CB  
729  N N   . ASN   A 95  ? 0.33838 0.16787 0.56919 0.01394  0.06924  0.06863  95  ASN   A N   
730  C CA  . ASN   A 95  ? 0.31635 0.16003 0.54686 0.02321  0.06728  0.07588  95  ASN   A CA  
731  C C   . ASN   A 95  ? 0.34835 0.17378 0.59069 0.02639  0.08358  0.05689  95  ASN   A C   
732  O O   . ASN   A 95  ? 0.38173 0.19285 0.60351 0.01918  0.08544  0.03051  95  ASN   A O   
733  C CB  . ASN   A 95  ? 0.29500 0.15298 0.48990 0.02004  0.05062  0.07283  95  ASN   A CB  
734  C CG  . ASN   A 95  ? 0.28658 0.16290 0.47988 0.02835  0.04604  0.08237  95  ASN   A CG  
735  O OD1 . ASN   A 95  ? 0.28176 0.16138 0.50124 0.03638  0.05557  0.09142  95  ASN   A OD1 
736  N ND2 . ASN   A 95  ? 0.24415 0.13351 0.40829 0.02574  0.03167  0.08087  95  ASN   A ND2 
737  N N   . PRO   A 96  ? 0.35362 0.18065 0.62795 0.03612  0.09620  0.06863  96  PRO   A N   
738  C CA  . PRO   A 96  ? 0.37632 0.18606 0.65982 0.03904  0.11376  0.04939  96  PRO   A CA  
739  C C   . PRO   A 96  ? 0.35676 0.17476 0.61611 0.04112  0.10862  0.03957  96  PRO   A C   
740  O O   . PRO   A 96  ? 0.37537 0.17871 0.63115 0.04081  0.12182  0.01783  96  PRO   A O   
741  C CB  . PRO   A 96  ? 0.39751 0.21097 0.72557 0.04964  0.12813  0.07032  96  PRO   A CB  
742  C CG  . PRO   A 96  ? 0.37712 0.21904 0.71345 0.05303  0.11331  0.10272  96  PRO   A CG  
743  C CD  . PRO   A 96  ? 0.35034 0.20020 0.65014 0.04436  0.09343  0.10037  96  PRO   A CD  
744  N N   . LYS   A 97  ? 0.32309 0.16445 0.56491 0.04256  0.09037  0.05424  97  LYS   A N   
745  C CA  . LYS   A 97  ? 0.32066 0.17135 0.54164 0.04476  0.08448  0.04764  97  LYS   A CA  
746  C C   . LYS   A 97  ? 0.30706 0.15158 0.49103 0.03530  0.07417  0.02697  97  LYS   A C   
747  O O   . LYS   A 97  ? 0.29005 0.14492 0.45533 0.03676  0.06617  0.02461  97  LYS   A O   
748  C CB  . LYS   A 97  ? 0.29630 0.17762 0.51932 0.05010  0.07011  0.07433  97  LYS   A CB  
749  C CG  . LYS   A 97  ? 0.31365 0.20727 0.57434 0.05850  0.07915  0.09612  97  LYS   A CG  
750  C CD  . LYS   A 97  ? 0.28800 0.21435 0.54751 0.05812  0.06160  0.12176  97  LYS   A CD  
751  C CE  . LYS   A 97  ? 0.28979 0.23239 0.58872 0.06522  0.06970  0.14489  97  LYS   A CE  
752  N NZ  . LYS   A 97  ? 0.28268 0.23687 0.58820 0.07011  0.07272  0.14751  97  LYS   A NZ  
753  N N   . THR   A 98  ? 0.33057 0.16027 0.50559 0.02506  0.07413  0.01283  98  THR   A N   
754  C CA  . THR   A 98  ? 0.31800 0.14557 0.46012 0.01408  0.06380  -0.00619 98  THR   A CA  
755  C C   . THR   A 98  ? 0.31540 0.13804 0.43975 0.01226  0.07074  -0.03141 98  THR   A C   
756  O O   . THR   A 98  ? 0.32735 0.13592 0.45565 0.00929  0.08522  -0.04982 98  THR   A O   
757  C CB  . THR   A 98  ? 0.31678 0.13231 0.45562 0.00183  0.06374  -0.01782 98  THR   A CB  
758  O OG1 . THR   A 98  ? 0.29681 0.11828 0.45093 0.00349  0.05866  0.00589  98  THR   A OG1 
759  C CG2 . THR   A 98  ? 0.29020 0.11087 0.39626 -0.01060 0.05128  -0.03560 98  THR   A CG2 
760  N N   . PRO   A 99  ? 0.27357 0.10852 0.37697 0.01321  0.06115  -0.03318 99  PRO   A N   
761  C CA  . PRO   A 99  ? 0.28343 0.11870 0.36453 0.01000  0.06694  -0.05751 99  PRO   A CA  
762  C C   . PRO   A 99  ? 0.30187 0.13711 0.35446 -0.00649 0.06080  -0.08143 99  PRO   A C   
763  O O   . PRO   A 99  ? 0.33607 0.17124 0.38735 -0.01448 0.05130  -0.07848 99  PRO   A O   
764  C CB  . PRO   A 99  ? 0.30197 0.15525 0.37100 0.01575  0.05572  -0.04689 99  PRO   A CB  
765  C CG  . PRO   A 99  ? 0.26684 0.13310 0.33232 0.01267  0.03665  -0.02751 99  PRO   A CG  
766  C CD  . PRO   A 99  ? 0.29235 0.14256 0.38684 0.01426  0.04330  -0.01522 99  PRO   A CD  
767  N N   . LYS   A 100 ? 0.31166 0.15147 0.34181 -0.01145 0.06530  -0.10199 100 LYS   A N   
768  C CA  . LYS   A 100 ? 0.35094 0.20507 0.34908 -0.02547 0.05223  -0.11639 100 LYS   A CA  
769  C C   . LYS   A 100 ? 0.34332 0.21794 0.32610 -0.02619 0.03372  -0.10518 100 LYS   A C   
770  O O   . LYS   A 100 ? 0.28305 0.16413 0.26536 -0.01795 0.03322  -0.09700 100 LYS   A O   
771  C CB  . LYS   A 100 ? 0.36384 0.22471 0.33986 -0.02906 0.05835  -0.13397 100 LYS   A CB  
772  C CG  . LYS   A 100 ? 0.45127 0.33217 0.39801 -0.04172 0.04195  -0.14109 100 LYS   A CG  
773  C CD  . LYS   A 100 ? 0.49207 0.37985 0.41656 -0.04619 0.04773  -0.15672 100 LYS   A CD  
774  C CE  . LYS   A 100 ? 0.57235 0.48453 0.47217 -0.05546 0.02937  -0.15556 100 LYS   A CE  
775  N NZ  . LYS   A 100 ? 0.57663 0.48772 0.47851 -0.06677 0.02068  -0.15971 100 LYS   A NZ  
776  N N   . TYR   A 101 ? 0.30157 0.18628 0.27507 -0.03547 0.01935  -0.10358 101 TYR   A N   
777  C CA  . TYR   A 101 ? 0.29548 0.19969 0.25858 -0.03533 0.00263  -0.09077 101 TYR   A CA  
778  C C   . TYR   A 101 ? 0.32715 0.24893 0.27793 -0.04285 -0.01124 -0.09031 101 TYR   A C   
779  O O   . TYR   A 101 ? 0.26392 0.17978 0.21653 -0.05074 -0.00890 -0.10002 101 TYR   A O   
780  C CB  . TYR   A 101 ? 0.29157 0.18528 0.27547 -0.03156 0.00210  -0.07599 101 TYR   A CB  
781  C CG  . TYR   A 101 ? 0.28439 0.16806 0.28299 -0.03786 0.00216  -0.07298 101 TYR   A CG  
782  C CD1 . TYR   A 101 ? 0.30735 0.20662 0.29776 -0.04485 -0.01128 -0.06804 101 TYR   A CD1 
783  C CD2 . TYR   A 101 ? 0.29940 0.16076 0.32235 -0.03516 0.01615  -0.07167 101 TYR   A CD2 
784  C CE1 . TYR   A 101 ? 0.26102 0.15232 0.26613 -0.05106 -0.01007 -0.06428 101 TYR   A CE1 
785  C CE2 . TYR   A 101 ? 0.31315 0.16715 0.34987 -0.04094 0.01636  -0.06654 101 TYR   A CE2 
786  C CZ  . TYR   A 101 ? 0.32483 0.19330 0.35203 -0.04961 0.00340  -0.06346 101 TYR   A CZ  
787  O OH  . TYR   A 101 ? 0.39736 0.25951 0.43914 -0.05579 0.00478  -0.05791 101 TYR   A OH  
788  N N   . LYS   A 102 ? 0.27537 0.21815 0.21844 -0.03844 -0.02455 -0.07746 102 LYS   A N   
789  C CA  . LYS   A 102 ? 0.29768 0.25702 0.24034 -0.03948 -0.03571 -0.07141 102 LYS   A CA  
790  C C   . LYS   A 102 ? 0.25503 0.22920 0.21005 -0.03144 -0.04038 -0.05771 102 LYS   A C   
791  O O   . LYS   A 102 ? 0.21003 0.19026 0.16838 -0.02731 -0.03614 -0.05256 102 LYS   A O   
792  C CB  . LYS   A 102 ? 0.29029 0.26375 0.21947 -0.03748 -0.04012 -0.07066 102 LYS   A CB  
793  C CG  . LYS   A 102 ? 0.36778 0.33734 0.28461 -0.04613 -0.03420 -0.08649 102 LYS   A CG  
794  C CD  . LYS   A 102 ? 0.40305 0.38605 0.30509 -0.04336 -0.03490 -0.08420 102 LYS   A CD  
795  C CE  . LYS   A 102 ? 0.48801 0.47046 0.37473 -0.05213 -0.02922 -0.10099 102 LYS   A CE  
796  N NZ  . LYS   A 102 ? 0.44303 0.40702 0.32828 -0.05434 -0.01405 -0.11765 102 LYS   A NZ  
797  N N   . PHE   A 103 ? 0.23077 0.21613 0.19334 -0.03223 -0.04436 -0.05380 103 PHE   A N   
798  C CA  . PHE   A 103 ? 0.19934 0.20206 0.16791 -0.02663 -0.04319 -0.04289 103 PHE   A CA  
799  C C   . PHE   A 103 ? 0.20418 0.21580 0.16432 -0.02555 -0.04814 -0.03849 103 PHE   A C   
800  O O   . PHE   A 103 ? 0.22410 0.23869 0.18198 -0.03271 -0.05235 -0.04223 103 PHE   A O   
801  C CB  . PHE   A 103 ? 0.15805 0.16063 0.13558 -0.03298 -0.04369 -0.04143 103 PHE   A CB  
802  C CG  . PHE   A 103 ? 0.18962 0.17291 0.16754 -0.04064 -0.04082 -0.03766 103 PHE   A CG  
803  C CD1 . PHE   A 103 ? 0.22506 0.19189 0.19685 -0.03867 -0.03965 -0.03498 103 PHE   A CD1 
804  C CD2 . PHE   A 103 ? 0.19826 0.17416 0.18463 -0.04894 -0.04167 -0.03392 103 PHE   A CD2 
805  C CE1 . PHE   A 103 ? 0.22476 0.16643 0.20372 -0.04088 -0.03995 -0.02685 103 PHE   A CE1 
806  C CE2 . PHE   A 103 ? 0.20272 0.15474 0.19547 -0.05354 -0.04080 -0.02554 103 PHE   A CE2 
807  C CZ  . PHE   A 103 ? 0.23289 0.17084 0.22531 -0.04570 -0.03760 -0.02013 103 PHE   A CZ  
808  N N   . VAL   A 104 ? 0.14917 0.16628 0.10688 -0.01911 -0.04610 -0.02995 104 VAL   A N   
809  C CA  . VAL   A 104 ? 0.16271 0.18731 0.11670 -0.01940 -0.04886 -0.02465 104 VAL   A CA  
810  C C   . VAL   A 104 ? 0.14676 0.17433 0.10653 -0.01454 -0.04641 -0.01573 104 VAL   A C   
811  O O   . VAL   A 104 ? 0.16238 0.18594 0.12400 -0.01046 -0.04189 -0.01250 104 VAL   A O   
812  C CB  . VAL   A 104 ? 0.16979 0.19463 0.11438 -0.01892 -0.04900 -0.02501 104 VAL   A CB  
813  C CG1 . VAL   A 104 ? 0.22736 0.24708 0.16269 -0.02494 -0.04962 -0.03583 104 VAL   A CG1 
814  C CG2 . VAL   A 104 ? 0.20142 0.22161 0.14764 -0.01143 -0.04514 -0.02057 104 VAL   A CG2 
815  N N   . ARG   A 105 ? 0.14595 0.18178 0.10850 -0.01649 -0.04927 -0.01173 105 ARG   A N   
816  C CA  . ARG   A 105 ? 0.17308 0.21041 0.14037 -0.01229 -0.04763 -0.00491 105 ARG   A CA  
817  C C   . ARG   A 105 ? 0.13050 0.17165 0.09579 -0.01067 -0.04839 -0.00073 105 ARG   A C   
818  O O   . ARG   A 105 ? 0.11796 0.17054 0.08229 -0.01472 -0.05219 0.00112  105 ARG   A O   
819  C CB  . ARG   A 105 ? 0.13221 0.17875 0.10662 -0.01493 -0.05057 -0.00219 105 ARG   A CB  
820  C CG  . ARG   A 105 ? 0.12895 0.17659 0.10850 -0.00991 -0.04918 0.00373  105 ARG   A CG  
821  C CD  . ARG   A 105 ? 0.10081 0.15796 0.08990 -0.01110 -0.05126 0.00673  105 ARG   A CD  
822  N NE  . ARG   A 105 ? 0.09271 0.15010 0.08662 -0.00492 -0.04995 0.01146  105 ARG   A NE  
823  C CZ  . ARG   A 105 ? 0.09402 0.14210 0.08450 -0.00096 -0.04671 0.00982  105 ARG   A CZ  
824  N NH1 . ARG   A 105 ? 0.10779 0.14762 0.09124 -0.00288 -0.04391 0.00567  105 ARG   A NH1 
825  N NH2 . ARG   A 105 ? 0.11109 0.15848 0.10482 0.00509  -0.04658 0.01295  105 ARG   A NH2 
826  N N   . ILE   A 106 ? 0.11916 0.15330 0.08418 -0.00587 -0.04493 0.00115  106 ILE   A N   
827  C CA  . ILE   A 106 ? 0.14902 0.18594 0.11265 -0.00499 -0.04553 0.00507  106 ILE   A CA  
828  C C   . ILE   A 106 ? 0.14630 0.18848 0.11606 -0.00310 -0.04687 0.01155  106 ILE   A C   
829  O O   . ILE   A 106 ? 0.14243 0.18202 0.11626 -0.00056 -0.04618 0.01186  106 ILE   A O   
830  C CB  . ILE   A 106 ? 0.15308 0.18180 0.11474 -0.00186 -0.04191 0.00406  106 ILE   A CB  
831  C CG1 . ILE   A 106 ? 0.13223 0.15593 0.09772 0.00045  -0.03816 0.00445  106 ILE   A CG1 
832  C CG2 . ILE   A 106 ? 0.17657 0.20262 0.13323 -0.00279 -0.04137 -0.00079 106 ILE   A CG2 
833  C CD1 . ILE   A 106 ? 0.16299 0.18183 0.12899 0.00056  -0.03539 0.00617  106 ILE   A CD1 
834  N N   . GLN   A 107 ? 0.14599 0.19624 0.11659 -0.00389 -0.04864 0.01731  107 GLN   A N   
835  C CA  . GLN   A 107 ? 0.16768 0.22400 0.14597 -0.00142 -0.05007 0.02569  107 GLN   A CA  
836  C C   . GLN   A 107 ? 0.22595 0.27007 0.20445 0.00299  -0.04746 0.02541  107 GLN   A C   
837  O O   . GLN   A 107 ? 0.16294 0.19919 0.13604 0.00273  -0.04497 0.02113  107 GLN   A O   
838  C CB  . GLN   A 107 ? 0.21660 0.28985 0.19620 -0.00479 -0.05297 0.03399  107 GLN   A CB  
839  C CG  . GLN   A 107 ? 0.17864 0.26944 0.15876 -0.01008 -0.05716 0.03636  107 GLN   A CG  
840  C CD  . GLN   A 107 ? 0.21079 0.31020 0.20366 -0.00812 -0.05944 0.04354  107 GLN   A CD  
841  O OE1 . GLN   A 107 ? 0.18129 0.27493 0.18306 -0.00212 -0.05772 0.04805  107 GLN   A OE1 
842  N NE2 . GLN   A 107 ? 0.20594 0.31986 0.20074 -0.01313 -0.06355 0.04468  107 GLN   A NE2 
843  N N   . PRO   A 108 ? 0.22781 0.27155 0.21371 0.00717  -0.04822 0.03059  108 PRO   A N   
844  C CA  . PRO   A 108 ? 0.20354 0.23788 0.18973 0.01050  -0.04677 0.03164  108 PRO   A CA  
845  C C   . PRO   A 108 ? 0.18565 0.22436 0.17234 0.00771  -0.04729 0.03707  108 PRO   A C   
846  O O   . PRO   A 108 ? 0.19045 0.24317 0.18052 0.00511  -0.04914 0.04420  108 PRO   A O   
847  C CB  . PRO   A 108 ? 0.16925 0.20428 0.16650 0.01651  -0.04793 0.03867  108 PRO   A CB  
848  C CG  . PRO   A 108 ? 0.21191 0.26287 0.21827 0.01506  -0.05019 0.04499  108 PRO   A CG  
849  C CD  . PRO   A 108 ? 0.15643 0.21001 0.15312 0.00934  -0.05045 0.03713  108 PRO   A CD  
850  N N   . GLY   A 109 ? 0.18238 0.21201 0.16615 0.00761  -0.04560 0.03482  109 GLY   A N   
851  C CA  . GLY   A 109 ? 0.18391 0.21750 0.16832 0.00486  -0.04575 0.03966  109 GLY   A CA  
852  C C   . GLY   A 109 ? 0.20160 0.23567 0.17822 0.00176  -0.04390 0.03376  109 GLY   A C   
853  O O   . GLY   A 109 ? 0.24185 0.27683 0.21840 0.00010  -0.04321 0.03614  109 GLY   A O   
854  N N   . GLN   A 110 ? 0.18838 0.22188 0.16003 0.00143  -0.04310 0.02703  110 GLN   A N   
855  C CA  . GLN   A 110 ? 0.22399 0.25689 0.18972 -0.00006 -0.04151 0.02204  110 GLN   A CA  
856  C C   . GLN   A 110 ? 0.16500 0.18837 0.13105 0.00071  -0.03872 0.01803  110 GLN   A C   
857  O O   . GLN   A 110 ? 0.15009 0.16763 0.11857 0.00074  -0.03773 0.01671  110 GLN   A O   
858  C CB  . GLN   A 110 ? 0.18691 0.22246 0.14893 -0.00115 -0.04236 0.01744  110 GLN   A CB  
859  C CG  . GLN   A 110 ? 0.27014 0.30265 0.22611 -0.00178 -0.04118 0.01164  110 GLN   A CG  
860  C CD  . GLN   A 110 ? 0.35338 0.39427 0.30421 -0.00397 -0.04150 0.01389  110 GLN   A CD  
861  O OE1 . GLN   A 110 ? 0.29883 0.35304 0.24681 -0.00720 -0.04348 0.01682  110 GLN   A OE1 
862  N NE2 . GLN   A 110 ? 0.19285 0.22915 0.14225 -0.00253 -0.03953 0.01309  110 GLN   A NE2 
863  N N   . THR   A 111 ? 0.16211 0.18585 0.12592 0.00021  -0.03775 0.01735  111 THR   A N   
864  C CA  . THR   A 111 ? 0.15948 0.17773 0.12538 -0.00042 -0.03597 0.01614  111 THR   A CA  
865  C C   . THR   A 111 ? 0.17527 0.19277 0.13858 0.00097  -0.03455 0.01149  111 THR   A C   
866  O O   . THR   A 111 ? 0.14165 0.16137 0.09996 0.00236  -0.03545 0.00820  111 THR   A O   
867  C CB  . THR   A 111 ? 0.14371 0.16455 0.11146 -0.00168 -0.03643 0.02077  111 THR   A CB  
868  O OG1 . THR   A 111 ? 0.12223 0.15004 0.08510 -0.00061 -0.03634 0.02122  111 THR   A OG1 
869  C CG2 . THR   A 111 ? 0.13200 0.15347 0.10440 -0.00369 -0.03829 0.02674  111 THR   A CG2 
870  N N   . PHE   A 112 ? 0.12736 0.14020 0.09358 -0.00064 -0.03361 0.01188  112 PHE   A N   
871  C CA  . PHE   A 112 ? 0.14073 0.15293 0.10638 0.00022  -0.03272 0.00983  112 PHE   A CA  
872  C C   . PHE   A 112 ? 0.16097 0.16884 0.13009 -0.00194 -0.03371 0.01325  112 PHE   A C   
873  O O   . PHE   A 112 ? 0.15662 0.16088 0.12771 -0.00541 -0.03524 0.01574  112 PHE   A O   
874  C CB  . PHE   A 112 ? 0.12707 0.13623 0.09218 -0.00098 -0.03213 0.00725  112 PHE   A CB  
875  C CG  . PHE   A 112 ? 0.16179 0.16353 0.12803 -0.00342 -0.03249 0.00829  112 PHE   A CG  
876  C CD1 . PHE   A 112 ? 0.15102 0.14635 0.11726 -0.00548 -0.03327 0.00960  112 PHE   A CD1 
877  C CD2 . PHE   A 112 ? 0.15364 0.15674 0.11984 -0.00310 -0.03273 0.00802  112 PHE   A CD2 
878  C CE1 . PHE   A 112 ? 0.15004 0.14024 0.11423 -0.00721 -0.03399 0.00952  112 PHE   A CE1 
879  C CE2 . PHE   A 112 ? 0.16471 0.16176 0.13025 -0.00417 -0.03322 0.00804  112 PHE   A CE2 
880  C CZ  . PHE   A 112 ? 0.16619 0.15659 0.12970 -0.00616 -0.03371 0.00821  112 PHE   A CZ  
881  N N   . SER   A 113 ? 0.12124 0.13043 0.09096 0.00000  -0.03375 0.01377  113 SER   A N   
882  C CA  . SER   A 113 ? 0.14680 0.15515 0.12101 -0.00151 -0.03576 0.01864  113 SER   A CA  
883  C C   . SER   A 113 ? 0.16012 0.16341 0.13408 -0.00393 -0.03672 0.01898  113 SER   A C   
884  O O   . SER   A 113 ? 0.11924 0.12048 0.09082 -0.00239 -0.03550 0.01613  113 SER   A O   
885  C CB  . SER   A 113 ? 0.14640 0.16000 0.12256 0.00427  -0.03574 0.02129  113 SER   A CB  
886  O OG  . SER   A 113 ? 0.14054 0.15818 0.11626 0.00622  -0.03561 0.02234  113 SER   A OG  
887  N N   . VAL   A 114 ? 0.16576 0.16838 0.14169 -0.00838 -0.03957 0.02314  114 VAL   A N   
888  C CA  . VAL   A 114 ? 0.14810 0.14840 0.12199 -0.01110 -0.04124 0.02469  114 VAL   A CA  
889  C C   . VAL   A 114 ? 0.14578 0.15310 0.12640 -0.01174 -0.04437 0.03300  114 VAL   A C   
890  O O   . VAL   A 114 ? 0.12934 0.14219 0.11491 -0.01478 -0.04709 0.03822  114 VAL   A O   
891  C CB  . VAL   A 114 ? 0.13184 0.12778 0.10003 -0.01592 -0.04292 0.02350  114 VAL   A CB  
892  C CG1 . VAL   A 114 ? 0.13708 0.13472 0.10139 -0.01929 -0.04576 0.02690  114 VAL   A CG1 
893  C CG2 . VAL   A 114 ? 0.14922 0.13933 0.11338 -0.01395 -0.03988 0.01754  114 VAL   A CG2 
894  N N   . LEU   A 115 ? 0.11812 0.12623 0.10085 -0.00921 -0.04433 0.03606  115 LEU   A N   
895  C CA  . LEU   A 115 ? 0.15343 0.16968 0.14572 -0.00965 -0.04737 0.04718  115 LEU   A CA  
896  C C   . LEU   A 115 ? 0.15662 0.17530 0.14376 -0.01566 -0.05079 0.05071  115 LEU   A C   
897  O O   . LEU   A 115 ? 0.13450 0.15024 0.11790 -0.01452 -0.04976 0.05030  115 LEU   A O   
898  C CB  . LEU   A 115 ? 0.14876 0.16345 0.14905 -0.00176 -0.04475 0.05127  115 LEU   A CB  
899  C CG  . LEU   A 115 ? 0.16566 0.18867 0.18199 -0.00053 -0.04609 0.06583  115 LEU   A CG  
900  C CD1 . LEU   A 115 ? 0.18187 0.21535 0.21207 -0.00022 -0.04667 0.07363  115 LEU   A CD1 
901  C CD2 . LEU   A 115 ? 0.18030 0.19484 0.20497 0.00764  -0.04154 0.06983  115 LEU   A CD2 
902  N N   . ALA   A 116 ? 0.19207 0.21661 0.17774 -0.02240 -0.05520 0.05463  116 ALA   A N   
903  C CA  . ALA   A 116 ? 0.17406 0.20230 0.15098 -0.02860 -0.05922 0.05786  116 ALA   A CA  
904  C C   . ALA   A 116 ? 0.22786 0.26856 0.21425 -0.02920 -0.06238 0.07165  116 ALA   A C   
905  O O   . ALA   A 116 ? 0.22652 0.27761 0.22819 -0.02881 -0.06431 0.08225  116 ALA   A O   
906  C CB  . ALA   A 116 ? 0.18182 0.21180 0.15168 -0.03625 -0.06381 0.05750  116 ALA   A CB  
907  N N   . CYS   A 117 ? 0.21636 0.25758 0.19524 -0.03009 -0.06268 0.07327  117 CYS   A N   
908  C CA  . CYS   A 117 ? 0.21894 0.27083 0.20789 -0.02921 -0.06434 0.08746  117 CYS   A CA  
909  C C   . CYS   A 117 ? 0.23598 0.29588 0.21146 -0.03620 -0.06870 0.09208  117 CYS   A C   
910  O O   . CYS   A 117 ? 0.23857 0.29089 0.19587 -0.03847 -0.06759 0.08159  117 CYS   A O   
911  C CB  . CYS   A 117 ? 0.21429 0.25725 0.20916 -0.02111 -0.05863 0.08650  117 CYS   A CB  
912  S SG  . CYS   A 117 ? 0.32661 0.36218 0.33673 -0.01229 -0.05368 0.08435  117 CYS   A SG  
913  N N   . TYR   A 118 ? 0.25459 0.33132 0.24015 -0.03914 -0.07322 0.10910  118 TYR   A N   
914  C CA  . TYR   A 118 ? 0.25253 0.34120 0.22606 -0.04596 -0.07791 0.11719  118 TYR   A CA  
915  C C   . TYR   A 118 ? 0.28703 0.38739 0.28016 -0.04207 -0.07748 0.13598  118 TYR   A C   
916  O O   . TYR   A 118 ? 0.28088 0.38865 0.29832 -0.03839 -0.07728 0.14727  118 TYR   A O   
917  C CB  . TYR   A 118 ? 0.25380 0.35607 0.21877 -0.05698 -0.08637 0.12127  118 TYR   A CB  
918  C CG  . TYR   A 118 ? 0.27166 0.35950 0.22065 -0.05958 -0.08553 0.10338  118 TYR   A CG  
919  C CD1 . TYR   A 118 ? 0.27365 0.35301 0.19793 -0.06287 -0.08449 0.09109  118 TYR   A CD1 
920  C CD2 . TYR   A 118 ? 0.29170 0.37371 0.25171 -0.05750 -0.08449 0.09923  118 TYR   A CD2 
921  C CE1 . TYR   A 118 ? 0.28130 0.34690 0.19454 -0.06379 -0.08270 0.07612  118 TYR   A CE1 
922  C CE2 . TYR   A 118 ? 0.27237 0.34084 0.22011 -0.05907 -0.08314 0.08473  118 TYR   A CE2 
923  C CZ  . TYR   A 118 ? 0.28164 0.34181 0.20711 -0.06195 -0.08228 0.07362  118 TYR   A CZ  
924  O OH  . TYR   A 118 ? 0.29702 0.34401 0.21297 -0.06254 -0.08048 0.06077  118 TYR   A OH  
925  N N   . ASN   A 119 ? 0.29123 0.39231 0.27605 -0.04183 -0.07599 0.13992  119 ASN   A N   
926  C CA  . ASN   A 119 ? 0.28343 0.39638 0.28776 -0.03862 -0.07533 0.16047  119 ASN   A CA  
927  C C   . ASN   A 119 ? 0.28656 0.38993 0.31834 -0.02804 -0.06855 0.16388  119 ASN   A C   
928  O O   . ASN   A 119 ? 0.27962 0.39489 0.33814 -0.02465 -0.06786 0.18297  119 ASN   A O   
929  C CB  . ASN   A 119 ? 0.32688 0.46720 0.33942 -0.04632 -0.08380 0.18078  119 ASN   A CB  
930  C CG  . ASN   A 119 ? 0.35348 0.50337 0.33593 -0.05801 -0.09082 0.17711  119 ASN   A CG  
931  O OD1 . ASN   A 119 ? 0.33803 0.49288 0.31095 -0.06575 -0.09672 0.17201  119 ASN   A OD1 
932  N ND2 . ASN   A 119 ? 0.37000 0.52202 0.33665 -0.05963 -0.08970 0.17978  119 ASN   A ND2 
933  N N   . GLY   A 120 ? 0.26402 0.34623 0.28988 -0.02282 -0.06309 0.14566  120 GLY   A N   
934  C CA  . GLY   A 120 ? 0.25504 0.32457 0.30089 -0.01336 -0.05611 0.14489  120 GLY   A CA  
935  C C   . GLY   A 120 ? 0.27849 0.35339 0.34206 -0.01076 -0.05616 0.14810  120 GLY   A C   
936  O O   . GLY   A 120 ? 0.29050 0.35537 0.37209 -0.00229 -0.04919 0.14875  120 GLY   A O   
937  N N   . SER   A 121 ? 0.26958 0.35925 0.32912 -0.01797 -0.06305 0.15055  121 SER   A N   
938  C CA  . SER   A 121 ? 0.27904 0.37628 0.35760 -0.01601 -0.06287 0.15627  121 SER   A CA  
939  C C   . SER   A 121 ? 0.24489 0.33353 0.30647 -0.01904 -0.06429 0.13877  121 SER   A C   
940  O O   . SER   A 121 ? 0.23091 0.32262 0.27312 -0.02800 -0.07021 0.13281  121 SER   A O   
941  C CB  . SER   A 121 ? 0.32483 0.44889 0.41897 -0.02241 -0.06969 0.17791  121 SER   A CB  
942  O OG  . SER   A 121 ? 0.40992 0.54448 0.51812 -0.02083 -0.06916 0.19561  121 SER   A OG  
943  N N   . PRO   A 122 ? 0.24030 0.31768 0.30860 -0.01174 -0.05841 0.13078  122 PRO   A N   
944  C CA  . PRO   A 122 ? 0.23701 0.30772 0.29151 -0.01428 -0.05931 0.11627  122 PRO   A CA  
945  C C   . PRO   A 122 ? 0.27069 0.35727 0.32768 -0.02324 -0.06624 0.12391  122 PRO   A C   
946  O O   . PRO   A 122 ? 0.24119 0.34507 0.31924 -0.02410 -0.06833 0.14144  122 PRO   A O   
947  C CB  . PRO   A 122 ? 0.24136 0.30320 0.30844 -0.00412 -0.05182 0.11303  122 PRO   A CB  
948  C CG  . PRO   A 122 ? 0.26944 0.32262 0.34688 0.00372  -0.04581 0.11738  122 PRO   A CG  
949  C CD  . PRO   A 122 ? 0.27927 0.34751 0.36711 -0.00056 -0.04967 0.13427  122 PRO   A CD  
950  N N   . SER   A 123 ? 0.24415 0.32439 0.28119 -0.02992 -0.06937 0.11161  123 SER   A N   
951  C CA  . SER   A 123 ? 0.27204 0.36306 0.30659 -0.03990 -0.07650 0.11651  123 SER   A CA  
952  C C   . SER   A 123 ? 0.24039 0.32718 0.27779 -0.03962 -0.07505 0.11081  123 SER   A C   
953  O O   . SER   A 123 ? 0.24551 0.34523 0.29255 -0.04551 -0.07992 0.12096  123 SER   A O   
954  C CB  . SER   A 123 ? 0.27966 0.36587 0.28911 -0.04837 -0.08108 0.10840  123 SER   A CB  
955  O OG  . SER   A 123 ? 0.34963 0.44410 0.35394 -0.05866 -0.08848 0.11205  123 SER   A OG  
956  N N   . GLY   A 124 ? 0.20584 0.27664 0.23568 -0.03341 -0.06888 0.09638  124 GLY   A N   
957  C CA  . GLY   A 124 ? 0.18336 0.25009 0.21336 -0.03350 -0.06742 0.09075  124 GLY   A CA  
958  C C   . GLY   A 124 ? 0.18480 0.23542 0.20409 -0.02677 -0.06099 0.07568  124 GLY   A C   
959  O O   . GLY   A 124 ? 0.14732 0.18897 0.15646 -0.02424 -0.05878 0.06849  124 GLY   A O   
960  N N   . VAL   A 125 ? 0.15271 0.20161 0.17500 -0.02416 -0.05816 0.07228  125 VAL   A N   
961  C CA  . VAL   A 125 ? 0.16856 0.20609 0.18200 -0.01790 -0.05264 0.06031  125 VAL   A CA  
962  C C   . VAL   A 125 ? 0.17928 0.21310 0.18755 -0.02181 -0.05305 0.05572  125 VAL   A C   
963  O O   . VAL   A 125 ? 0.12408 0.16552 0.14023 -0.02649 -0.05611 0.06288  125 VAL   A O   
964  C CB  . VAL   A 125 ? 0.16317 0.20296 0.18558 -0.00783 -0.04766 0.06206  125 VAL   A CB  
965  C CG1 . VAL   A 125 ? 0.16151 0.21248 0.19846 -0.00700 -0.04703 0.07080  125 VAL   A CG1 
966  C CG2 . VAL   A 125 ? 0.11539 0.14457 0.12524 -0.00187 -0.04349 0.05020  125 VAL   A CG2 
967  N N   . TYR   A 126 ? 0.14106 0.16390 0.13789 -0.02044 -0.05034 0.04559  126 TYR   A N   
968  C CA  . TYR   A 126 ? 0.16436 0.18299 0.15801 -0.02330 -0.05050 0.04270  126 TYR   A CA  
969  C C   . TYR   A 126 ? 0.17509 0.18639 0.16149 -0.01827 -0.04588 0.03407  126 TYR   A C   
970  O O   . TYR   A 126 ? 0.14222 0.14992 0.12417 -0.01469 -0.04348 0.02957  126 TYR   A O   
971  C CB  . TYR   A 126 ? 0.17521 0.18871 0.16302 -0.03153 -0.05580 0.04371  126 TYR   A CB  
972  C CG  . TYR   A 126 ? 0.19738 0.20344 0.17434 -0.03201 -0.05595 0.03874  126 TYR   A CG  
973  C CD1 . TYR   A 126 ? 0.19996 0.19603 0.16928 -0.02909 -0.05273 0.03106  126 TYR   A CD1 
974  C CD2 . TYR   A 126 ? 0.19162 0.20316 0.16730 -0.03505 -0.05925 0.04319  126 TYR   A CD2 
975  C CE1 . TYR   A 126 ? 0.18896 0.18043 0.14962 -0.02892 -0.05228 0.02734  126 TYR   A CE1 
976  C CE2 . TYR   A 126 ? 0.19751 0.20445 0.16275 -0.03533 -0.05900 0.03920  126 TYR   A CE2 
977  C CZ  . TYR   A 126 ? 0.20334 0.20007 0.16116 -0.03204 -0.05516 0.03089  126 TYR   A CZ  
978  O OH  . TYR   A 126 ? 0.24802 0.24207 0.19634 -0.03197 -0.05447 0.02744  126 TYR   A OH  
979  N N   . GLN   A 127 ? 0.15786 0.16838 0.14432 -0.01897 -0.04541 0.03343  127 GLN   A N   
980  C CA  . GLN   A 127 ? 0.20128 0.20913 0.18334 -0.01504 -0.04209 0.02833  127 GLN   A CA  
981  C C   . GLN   A 127 ? 0.21202 0.21029 0.18939 -0.01794 -0.04355 0.02560  127 GLN   A C   
982  O O   . GLN   A 127 ? 0.18848 0.18245 0.16591 -0.02315 -0.04754 0.02815  127 GLN   A O   
983  C CB  . GLN   A 127 ? 0.20348 0.21935 0.18965 -0.01362 -0.04121 0.03189  127 GLN   A CB  
984  C CG  . GLN   A 127 ? 0.20985 0.22808 0.19104 -0.00852 -0.03818 0.02845  127 GLN   A CG  
985  C CD  . GLN   A 127 ? 0.17725 0.19759 0.15360 -0.00244 -0.03595 0.02449  127 GLN   A CD  
986  O OE1 . GLN   A 127 ? 0.19429 0.21465 0.17270 -0.00110 -0.03623 0.02525  127 GLN   A OE1 
987  N NE2 . GLN   A 127 ? 0.17939 0.20111 0.14918 0.00076  -0.03487 0.02105  127 GLN   A NE2 
988  N N   . CYS   A 128 ? 0.18369 0.17902 0.15702 -0.01436 -0.04090 0.02092  128 CYS   A N   
989  C CA  . CYS   A 128 ? 0.19026 0.17812 0.15985 -0.01476 -0.04168 0.01848  128 CYS   A CA  
990  C C   . CYS   A 128 ? 0.18295 0.17572 0.15328 -0.01055 -0.03936 0.01731  128 CYS   A C   
991  O O   . CYS   A 128 ? 0.15018 0.15060 0.12088 -0.00745 -0.03700 0.01670  128 CYS   A O   
992  C CB  . CYS   A 128 ? 0.20499 0.18729 0.16926 -0.01464 -0.04132 0.01528  128 CYS   A CB  
993  S SG  . CYS   A 128 ? 0.35396 0.33394 0.31385 -0.01934 -0.04450 0.01692  128 CYS   A SG  
994  N N   . ALA   A 129 ? 0.16431 0.15320 0.13386 -0.01019 -0.04083 0.01712  129 ALA   A N   
995  C CA  . ALA   A 129 ? 0.17490 0.17034 0.14554 -0.00623 -0.03969 0.01741  129 ALA   A CA  
996  C C   . ALA   A 129 ? 0.16540 0.15665 0.13361 -0.00462 -0.03963 0.01447  129 ALA   A C   
997  O O   . ALA   A 129 ? 0.12956 0.11095 0.09382 -0.00620 -0.04138 0.01243  129 ALA   A O   
998  C CB  . ALA   A 129 ? 0.14667 0.14565 0.12138 -0.00561 -0.04199 0.02292  129 ALA   A CB  
999  N N   . MET   A 130 ? 0.14936 0.14923 0.11875 -0.00146 -0.03811 0.01435  130 MET   A N   
1000 C CA  . MET   A 130 ? 0.14931 0.15036 0.11887 0.00117  -0.03842 0.01388  130 MET   A CA  
1001 C C   . MET   A 130 ? 0.15204 0.15295 0.12545 0.00423  -0.04108 0.01884  130 MET   A C   
1002 O O   . MET   A 130 ? 0.14824 0.15685 0.12623 0.00689  -0.04206 0.02434  130 MET   A O   
1003 C CB  . MET   A 130 ? 0.15628 0.16862 0.12737 0.00353  -0.03751 0.01382  130 MET   A CB  
1004 C CG  . MET   A 130 ? 0.15090 0.16745 0.12313 0.00615  -0.03751 0.01342  130 MET   A CG  
1005 S SD  . MET   A 130 ? 0.15855 0.16512 0.12522 0.00331  -0.03574 0.00911  130 MET   A SD  
1006 C CE  . MET   A 130 ? 0.16828 0.17493 0.13405 0.00043  -0.03373 0.00655  130 MET   A CE  
1007 N N   . ARG   A 131 ? 0.15679 0.14708 0.12758 0.00452  -0.04284 0.01744  131 ARG   A N   
1008 C CA  . ARG   A 131 ? 0.18077 0.16722 0.15827 0.00979  -0.04497 0.02442  131 ARG   A CA  
1009 C C   . ARG   A 131 ? 0.17995 0.17462 0.16728 0.01840  -0.04370 0.03191  131 ARG   A C   
1010 O O   . ARG   A 131 ? 0.14876 0.15248 0.13419 0.01961  -0.04158 0.02918  131 ARG   A O   
1011 C CB  . ARG   A 131 ? 0.20502 0.15803 0.17039 0.00692  -0.05622 0.01999  131 ARG   A CB  
1012 C CG  . ARG   A 131 ? 0.21558 0.16065 0.16825 -0.00262 -0.05808 0.01235  131 ARG   A CG  
1013 C CD  . ARG   A 131 ? 0.18418 0.13568 0.14789 -0.00536 -0.05817 0.01864  131 ARG   A CD  
1014 N NE  . ARG   A 131 ? 0.21531 0.15555 0.19216 -0.00175 -0.06375 0.02900  131 ARG   A NE  
1015 C CZ  . ARG   A 131 ? 0.25957 0.20999 0.24931 -0.00265 -0.06149 0.03706  131 ARG   A CZ  
1016 N NH1 . ARG   A 131 ? 0.20639 0.17346 0.19279 -0.00608 -0.05673 0.03430  131 ARG   A NH1 
1017 N NH2 . ARG   A 131 ? 0.22892 0.17057 0.23747 0.00184  -0.05979 0.04778  131 ARG   A NH2 
1018 N N   . PRO   A 132 ? 0.20481 0.19566 0.20536 0.02442  -0.04439 0.04190  132 PRO   A N   
1019 C CA  . PRO   A 132 ? 0.22673 0.22285 0.24193 0.03217  -0.04328 0.04914  132 PRO   A CA  
1020 C C   . PRO   A 132 ? 0.23275 0.21925 0.25688 0.03752  -0.04158 0.04894  132 PRO   A C   
1021 O O   . PRO   A 132 ? 0.18823 0.18820 0.22406 0.04159  -0.03980 0.05268  132 PRO   A O   
1022 C CB  . PRO   A 132 ? 0.23189 0.22111 0.26762 0.03554  -0.04133 0.06072  132 PRO   A CB  
1023 C CG  . PRO   A 132 ? 0.24369 0.23342 0.26795 0.02908  -0.04362 0.05878  132 PRO   A CG  
1024 C CD  . PRO   A 132 ? 0.21205 0.19598 0.21902 0.02282  -0.04542 0.04763  132 PRO   A CD  
1025 N N   . ASN   A 133 ? 0.21393 0.17200 0.23166 0.03638  -0.04264 0.04056  133 ASN   A N   
1026 C CA  . ASN   A 133 ? 0.22030 0.16899 0.23509 0.03856  -0.03007 0.02789  133 ASN   A CA  
1027 C C   . ASN   A 133 ? 0.17102 0.12999 0.16012 0.03159  -0.03559 0.01925  133 ASN   A C   
1028 O O   . ASN   A 133 ? 0.18963 0.14007 0.16865 0.03071  -0.02577 0.00753  133 ASN   A O   
1029 C CB  . ASN   A 133 ? 0.24477 0.15954 0.25366 0.03638  -0.01663 0.01123  133 ASN   A CB  
1030 C CG  . ASN   A 133 ? 0.26823 0.16923 0.24475 0.02274  -0.02423 -0.00273 133 ASN   A CG  
1031 O OD1 . ASN   A 133 ? 0.22042 0.13616 0.17985 0.01640  -0.03784 0.00007  133 ASN   A OD1 
1032 N ND2 . ASN   A 133 ? 0.29783 0.17065 0.26746 0.01775  -0.01480 -0.01804 133 ASN   A ND2 
1033 N N   . PHE   A 134 ? 0.15976 0.13689 0.13956 0.02671  -0.04913 0.02521  134 PHE   A N   
1034 C CA  . PHE   A 134 ? 0.18764 0.17880 0.15507 0.01766  -0.04549 0.01747  134 PHE   A CA  
1035 C C   . PHE   A 134 ? 0.18133 0.15440 0.12474 0.01155  -0.04533 0.00511  134 PHE   A C   
1036 O O   . PHE   A 134 ? 0.18707 0.16802 0.12689 0.00747  -0.04001 0.00151  134 PHE   A O   
1037 C CB  . PHE   A 134 ? 0.16383 0.16731 0.13959 0.02244  -0.04531 0.02147  134 PHE   A CB  
1038 C CG  . PHE   A 134 ? 0.16498 0.18926 0.15682 0.02692  -0.04261 0.02724  134 PHE   A CG  
1039 C CD1 . PHE   A 134 ? 0.14957 0.17653 0.13483 0.02163  -0.04148 0.01921  134 PHE   A CD1 
1040 C CD2 . PHE   A 134 ? 0.18141 0.20821 0.19768 0.03443  -0.04419 0.03822  134 PHE   A CD2 
1041 C CE1 . PHE   A 134 ? 0.15444 0.18991 0.14938 0.01970  -0.04711 0.02501  134 PHE   A CE1 
1042 C CE2 . PHE   A 134 ? 0.17608 0.21724 0.20244 0.03235  -0.04534 0.04207  134 PHE   A CE2 
1043 C CZ  . PHE   A 134 ? 0.15312 0.19714 0.16532 0.02450  -0.04820 0.03467  134 PHE   A CZ  
1044 N N   . THR   A 135 ? 0.21074 0.16376 0.14134 0.00905  -0.04918 -0.00004 135 THR   A N   
1045 C CA  . THR   A 135 ? 0.19668 0.15061 0.12041 -0.00009 -0.04291 -0.00700 135 THR   A CA  
1046 C C   . THR   A 135 ? 0.18708 0.15524 0.12706 -0.00277 -0.04047 -0.00134 135 THR   A C   
1047 O O   . THR   A 135 ? 0.17167 0.14345 0.12144 -0.00065 -0.04204 0.00399  135 THR   A O   
1048 C CB  . THR   A 135 ? 0.22890 0.15476 0.13002 -0.00430 -0.04285 -0.02025 135 THR   A CB  
1049 O OG1 . THR   A 135 ? 0.23303 0.14086 0.13844 -0.00417 -0.04801 -0.02044 135 THR   A OG1 
1050 C CG2 . THR   A 135 ? 0.24221 0.15313 0.13694 0.00084  -0.03067 -0.03079 135 THR   A CG2 
1051 N N   . ILE   A 136 ? 0.17985 0.14582 0.11524 -0.00722 -0.04015 -0.00222 136 ILE   A N   
1052 C CA  . ILE   A 136 ? 0.21882 0.18363 0.15937 -0.00989 -0.04212 0.00205  136 ILE   A CA  
1053 C C   . ILE   A 136 ? 0.21480 0.17366 0.14585 -0.01568 -0.04524 -0.00019 136 ILE   A C   
1054 O O   . ILE   A 136 ? 0.17481 0.13414 0.09549 -0.01848 -0.04454 -0.00489 136 ILE   A O   
1055 C CB  . ILE   A 136 ? 0.19832 0.17001 0.14505 -0.00996 -0.03979 0.00499  136 ILE   A CB  
1056 C CG1 . ILE   A 136 ? 0.20684 0.17994 0.14722 -0.01258 -0.03956 0.00436  136 ILE   A CG1 
1057 C CG2 . ILE   A 136 ? 0.17250 0.15170 0.12594 -0.00601 -0.03700 0.00531  136 ILE   A CG2 
1058 C CD1 . ILE   A 136 ? 0.19831 0.17543 0.14401 -0.01398 -0.03945 0.00806  136 ILE   A CD1 
1059 N N   . LYS   A 137 ? 0.23109 0.18622 0.16515 -0.01845 -0.04883 0.00262  137 LYS   A N   
1060 C CA  . LYS   A 137 ? 0.24204 0.19379 0.16824 -0.02564 -0.05303 0.00077  137 LYS   A CA  
1061 C C   . LYS   A 137 ? 0.25382 0.21267 0.18335 -0.02878 -0.05405 0.00683  137 LYS   A C   
1062 O O   . LYS   A 137 ? 0.24125 0.20228 0.17891 -0.03044 -0.05589 0.01245  137 LYS   A O   
1063 C CB  . LYS   A 137 ? 0.24090 0.18618 0.17056 -0.02790 -0.05729 0.00118  137 LYS   A CB  
1064 C CG  . LYS   A 137 ? 0.26518 0.19363 0.18778 -0.02853 -0.05980 -0.00639 137 LYS   A CG  
1065 C CD  . LYS   A 137 ? 0.31047 0.22190 0.23700 -0.03357 -0.06916 -0.00313 137 LYS   A CD  
1066 C CE  . LYS   A 137 ? 0.37136 0.25373 0.29983 -0.03408 -0.06915 -0.01205 137 LYS   A CE  
1067 N NZ  . LYS   A 137 ? 0.40819 0.27842 0.32581 -0.03840 -0.05699 -0.03117 137 LYS   A NZ  
1068 N N   . GLY   A 138 ? 0.20306 0.16684 0.12709 -0.02962 -0.05276 0.00578  138 GLY   A N   
1069 C CA  . GLY   A 138 ? 0.24508 0.21655 0.17352 -0.03189 -0.05389 0.01169  138 GLY   A CA  
1070 C C   . GLY   A 138 ? 0.24042 0.21535 0.16020 -0.04034 -0.05988 0.01303  138 GLY   A C   
1071 O O   . GLY   A 138 ? 0.26505 0.23552 0.17522 -0.04539 -0.06330 0.00800  138 GLY   A O   
1072 N N   . SER   A 139 ? 0.21130 0.19533 0.13430 -0.04280 -0.06182 0.01936  139 SER   A N   
1073 C CA  . SER   A 139 ? 0.25379 0.24540 0.16892 -0.05181 -0.06862 0.02287  139 SER   A CA  
1074 C C   . SER   A 139 ? 0.24604 0.24639 0.15964 -0.05163 -0.06834 0.02706  139 SER   A C   
1075 O O   . SER   A 139 ? 0.19779 0.20470 0.12427 -0.04880 -0.06754 0.03436  139 SER   A O   
1076 C CB  . SER   A 139 ? 0.21597 0.21359 0.14148 -0.05630 -0.07355 0.03107  139 SER   A CB  
1077 O OG  . SER   A 139 ? 0.27778 0.28730 0.19884 -0.06519 -0.08079 0.03750  139 SER   A OG  
1078 N N   . PHE   A 140 ? 0.26899 0.26959 0.16651 -0.05449 -0.06871 0.02203  140 PHE   A N   
1079 C CA  . PHE   A 140 ? 0.28090 0.28751 0.17554 -0.05257 -0.06686 0.02492  140 PHE   A CA  
1080 C C   . PHE   A 140 ? 0.27944 0.29297 0.15439 -0.06166 -0.07180 0.02414  140 PHE   A C   
1081 O O   . PHE   A 140 ? 0.32366 0.33103 0.18264 -0.06563 -0.07194 0.01385  140 PHE   A O   
1082 C CB  . PHE   A 140 ? 0.24150 0.24020 0.13586 -0.04426 -0.05931 0.01786  140 PHE   A CB  
1083 C CG  . PHE   A 140 ? 0.22604 0.22121 0.13797 -0.03646 -0.05481 0.01939  140 PHE   A CG  
1084 C CD1 . PHE   A 140 ? 0.20897 0.20996 0.13274 -0.03465 -0.05491 0.02666  140 PHE   A CD1 
1085 C CD2 . PHE   A 140 ? 0.23219 0.21919 0.14779 -0.03146 -0.05075 0.01337  140 PHE   A CD2 
1086 C CE1 . PHE   A 140 ? 0.20934 0.20707 0.14539 -0.02862 -0.05077 0.02579  140 PHE   A CE1 
1087 C CE2 . PHE   A 140 ? 0.21321 0.19866 0.14199 -0.02585 -0.04719 0.01436  140 PHE   A CE2 
1088 C CZ  . PHE   A 140 ? 0.19239 0.18269 0.13007 -0.02470 -0.04698 0.01940  140 PHE   A CZ  
1089 N N   . LEU   A 141 ? 0.29139 0.31834 0.16691 -0.06552 -0.07588 0.03469  141 LEU   A N   
1090 C CA  . LEU   A 141 ? 0.31264 0.34925 0.16777 -0.07470 -0.08058 0.03563  141 LEU   A CA  
1091 C C   . LEU   A 141 ? 0.31768 0.35809 0.16866 -0.07051 -0.07653 0.03895  141 LEU   A C   
1092 O O   . LEU   A 141 ? 0.30058 0.33579 0.16513 -0.06117 -0.07079 0.04005  141 LEU   A O   
1093 C CB  . LEU   A 141 ? 0.32213 0.37561 0.18046 -0.08459 -0.09033 0.04824  141 LEU   A CB  
1094 C CG  . LEU   A 141 ? 0.38132 0.43209 0.24701 -0.08844 -0.09447 0.04727  141 LEU   A CG  
1095 C CD1 . LEU   A 141 ? 0.41167 0.48257 0.28628 -0.09700 -0.10392 0.06331  141 LEU   A CD1 
1096 C CD2 . LEU   A 141 ? 0.35039 0.39079 0.19518 -0.09487 -0.09546 0.03194  141 LEU   A CD2 
1097 N N   . ASN   A 142 ? 0.34138 0.39152 0.17207 -0.07832 -0.07970 0.04060  142 ASN   A N   
1098 C CA  . ASN   A 142 ? 0.34449 0.39912 0.16976 -0.07484 -0.07578 0.04534  142 ASN   A CA  
1099 C C   . ASN   A 142 ? 0.35155 0.41544 0.20046 -0.07033 -0.07727 0.06147  142 ASN   A C   
1100 O O   . ASN   A 142 ? 0.33018 0.40551 0.19204 -0.07435 -0.08387 0.07261  142 ASN   A O   
1101 C CB  . ASN   A 142 ? 0.35567 0.42225 0.15374 -0.08530 -0.07944 0.04660  142 ASN   A CB  
1102 C CG  . ASN   A 142 ? 0.48461 0.55576 0.27550 -0.08141 -0.07432 0.05265  142 ASN   A CG  
1103 O OD1 . ASN   A 142 ? 0.50119 0.58775 0.27669 -0.08895 -0.07806 0.06148  142 ASN   A OD1 
1104 N ND2 . ASN   A 142 ? 0.45355 0.51227 0.25504 -0.07019 -0.06579 0.04867  142 ASN   A ND2 
1105 N N   . GLY   A 143 ? 0.32469 0.38360 0.18029 -0.06193 -0.07079 0.06278  143 GLY   A N   
1106 C CA  . GLY   A 143 ? 0.29659 0.36147 0.17436 -0.05705 -0.07095 0.07630  143 GLY   A CA  
1107 C C   . GLY   A 143 ? 0.26080 0.31505 0.15981 -0.04947 -0.06769 0.07232  143 GLY   A C   
1108 O O   . GLY   A 143 ? 0.25586 0.31242 0.17293 -0.04464 -0.06663 0.08130  143 GLY   A O   
1109 N N   . SER   A 144 ? 0.23237 0.27529 0.12934 -0.04833 -0.06578 0.05960  144 SER   A N   
1110 C CA  . SER   A 144 ? 0.23335 0.26702 0.14733 -0.04164 -0.06221 0.05540  144 SER   A CA  
1111 C C   . SER   A 144 ? 0.20916 0.23308 0.12539 -0.03437 -0.05531 0.04890  144 SER   A C   
1112 O O   . SER   A 144 ? 0.18466 0.20232 0.11319 -0.02947 -0.05247 0.04563  144 SER   A O   
1113 C CB  . SER   A 144 ? 0.24640 0.27324 0.15822 -0.04353 -0.06297 0.04678  144 SER   A CB  
1114 O OG  . SER   A 144 ? 0.23682 0.25782 0.13070 -0.04568 -0.06159 0.03695  144 SER   A OG  
1115 N N   . CYS   A 145 ? 0.22903 0.25261 0.13271 -0.03419 -0.05264 0.04720  145 CYS   A N   
1116 C CA  . CYS   A 145 ? 0.23506 0.25163 0.14214 -0.02826 -0.04670 0.04277  145 CYS   A CA  
1117 C C   . CYS   A 145 ? 0.22193 0.23868 0.14513 -0.02485 -0.04623 0.05016  145 CYS   A C   
1118 O O   . CYS   A 145 ? 0.22858 0.25268 0.15771 -0.02626 -0.04933 0.06179  145 CYS   A O   
1119 C CB  . CYS   A 145 ? 0.24405 0.26229 0.13501 -0.02892 -0.04360 0.04276  145 CYS   A CB  
1120 S SG  . CYS   A 145 ? 0.32953 0.34325 0.20205 -0.03060 -0.04188 0.02985  145 CYS   A SG  
1121 N N   . GLY   A 146 ? 0.20618 0.21546 0.13731 -0.02057 -0.04269 0.04392  146 GLY   A N   
1122 C CA  . GLY   A 146 ? 0.23010 0.23684 0.17452 -0.01741 -0.04211 0.04852  146 GLY   A CA  
1123 C C   . GLY   A 146 ? 0.21405 0.21877 0.16857 -0.01560 -0.04331 0.04649  146 GLY   A C   
1124 O O   . GLY   A 146 ? 0.21187 0.21200 0.17498 -0.01196 -0.04192 0.04743  146 GLY   A O   
1125 N N   . SER   A 147 ? 0.19591 0.20328 0.14873 -0.01800 -0.04562 0.04438  147 SER   A N   
1126 C CA  . SER   A 147 ? 0.15601 0.16142 0.11674 -0.01616 -0.04566 0.04169  147 SER   A CA  
1127 C C   . SER   A 147 ? 0.16846 0.16639 0.12902 -0.01347 -0.04188 0.03187  147 SER   A C   
1128 O O   . SER   A 147 ? 0.16924 0.16454 0.12387 -0.01415 -0.03992 0.02630  147 SER   A O   
1129 C CB  . SER   A 147 ? 0.16859 0.17727 0.12621 -0.02034 -0.04864 0.04134  147 SER   A CB  
1130 O OG  . SER   A 147 ? 0.18374 0.20210 0.14023 -0.02486 -0.05344 0.05101  147 SER   A OG  
1131 N N   . VAL   A 148 ? 0.14039 0.13639 0.10744 -0.01016 -0.04101 0.03066  148 VAL   A N   
1132 C CA  . VAL   A 148 ? 0.13843 0.12971 0.10446 -0.00860 -0.03839 0.02282  148 VAL   A CA  
1133 C C   . VAL   A 148 ? 0.14351 0.13519 0.11057 -0.00768 -0.03755 0.01931  148 VAL   A C   
1134 O O   . VAL   A 148 ? 0.14927 0.14436 0.11936 -0.00764 -0.03905 0.02289  148 VAL   A O   
1135 C CB  . VAL   A 148 ? 0.15648 0.14474 0.12550 -0.00580 -0.03832 0.02334  148 VAL   A CB  
1136 C CG1 . VAL   A 148 ? 0.13278 0.11947 0.10110 -0.00698 -0.03864 0.02766  148 VAL   A CG1 
1137 C CG2 . VAL   A 148 ? 0.13615 0.12489 0.11221 -0.00065 -0.03868 0.02968  148 VAL   A CG2 
1138 N N   . GLY   A 149 ? 0.13622 0.12611 0.10149 -0.00702 -0.03540 0.01370  149 GLY   A N   
1139 C CA  . GLY   A 149 ? 0.12060 0.11263 0.08670 -0.00553 -0.03438 0.01144  149 GLY   A CA  
1140 C C   . GLY   A 149 ? 0.15089 0.14542 0.11631 -0.00338 -0.03373 0.00813  149 GLY   A C   
1141 O O   . GLY   A 149 ? 0.12159 0.11485 0.08544 -0.00425 -0.03395 0.00558  149 GLY   A O   
1142 N N   . PHE   A 150 ? 0.11494 0.11469 0.08060 -0.00124 -0.03341 0.00777  150 PHE   A N   
1143 C CA  . PHE   A 150 ? 0.14751 0.15197 0.10975 -0.00052 -0.03335 0.00326  150 PHE   A CA  
1144 C C   . PHE   A 150 ? 0.15228 0.16691 0.11254 0.00081  -0.03223 0.00227  150 PHE   A C   
1145 O O   . PHE   A 150 ? 0.12265 0.13872 0.08585 0.00330  -0.03209 0.00658  150 PHE   A O   
1146 C CB  . PHE   A 150 ? 0.16286 0.16286 0.12544 0.00122  -0.03580 0.00516  150 PHE   A CB  
1147 C CG  . PHE   A 150 ? 0.15561 0.15673 0.12481 0.00639  -0.03675 0.01492  150 PHE   A CG  
1148 C CD1 . PHE   A 150 ? 0.14990 0.15089 0.12516 0.00651  -0.03594 0.02068  150 PHE   A CD1 
1149 C CD2 . PHE   A 150 ? 0.14785 0.14553 0.11468 0.01048  -0.04103 0.01765  150 PHE   A CD2 
1150 C CE1 . PHE   A 150 ? 0.16675 0.17019 0.14888 0.00981  -0.03653 0.02816  150 PHE   A CE1 
1151 C CE2 . PHE   A 150 ? 0.17971 0.18268 0.16047 0.01688  -0.03874 0.02911  150 PHE   A CE2 
1152 C CZ  . PHE   A 150 ? 0.14709 0.15202 0.13237 0.01690  -0.03548 0.03108  150 PHE   A CZ  
1153 N N   . ASN   A 151 ? 0.14315 0.16395 0.09781 -0.00222 -0.03095 -0.00462 151 ASN   A N   
1154 C CA  . ASN   A 151 ? 0.17606 0.20236 0.12509 -0.00706 -0.02882 -0.00454 151 ASN   A CA  
1155 C C   . ASN   A 151 ? 0.21136 0.22007 0.13873 -0.00776 -0.03108 -0.01680 151 ASN   A C   
1156 O O   . ASN   A 151 ? 0.20681 0.20456 0.13261 -0.00610 -0.03213 -0.02657 151 ASN   A O   
1157 C CB  . ASN   A 151 ? 0.17224 0.17376 0.10658 -0.00022 -0.03640 -0.00847 151 ASN   A CB  
1158 C CG  . ASN   A 151 ? 0.18902 0.19989 0.13290 0.00328  -0.03597 -0.00283 151 ASN   A CG  
1159 O OD1 . ASN   A 151 ? 0.18114 0.19740 0.13089 0.00326  -0.03552 -0.00211 151 ASN   A OD1 
1160 N ND2 . ASN   A 151 ? 0.23067 0.24264 0.17449 0.00350  -0.03593 0.00198  151 ASN   A ND2 
1161 N N   . ILE   A 152 ? 0.20075 0.20953 0.11447 -0.00219 -0.02800 -0.02309 152 ILE   A N   
1162 C CA  . ILE   A 152 ? 0.27692 0.27796 0.18798 0.00114  -0.01357 -0.04086 152 ILE   A CA  
1163 C C   . ILE   A 152 ? 0.36956 0.37828 0.26015 -0.00443 -0.00768 -0.05159 152 ILE   A C   
1164 O O   . ILE   A 152 ? 0.39507 0.41510 0.28276 -0.00343 -0.01102 -0.03956 152 ILE   A O   
1165 C CB  . ILE   A 152 ? 0.32067 0.31617 0.25721 0.01227  -0.00239 -0.03012 152 ILE   A CB  
1166 C CG1 . ILE   A 152 ? 0.25530 0.24417 0.21329 0.01649  -0.01012 -0.01386 152 ILE   A CG1 
1167 C CG2 . ILE   A 152 ? 0.38727 0.36687 0.33098 0.01458  0.01898  -0.04660 152 ILE   A CG2 
1168 C CD1 . ILE   A 152 ? 0.28743 0.27055 0.27616 0.02686  0.00118  -0.00240 152 ILE   A CD1 
1169 N N   . ASP   A 153 ? 0.42560 0.42193 0.31017 -0.00937 0.00047  -0.06813 153 ASP   A N   
1170 C CA  . ASP   A 153 ? 0.49740 0.49895 0.36692 -0.01327 0.00214  -0.07255 153 ASP   A CA  
1171 C C   . ASP   A 153 ? 0.51766 0.50644 0.38463 -0.01473 0.02050  -0.09443 153 ASP   A C   
1172 O O   . ASP   A 153 ? 0.47604 0.45011 0.34914 -0.01927 0.02234  -0.10518 153 ASP   A O   
1173 C CB  . ASP   A 153 ? 0.49683 0.50006 0.36498 -0.01801 -0.01186 -0.06658 153 ASP   A CB  
1174 C CG  . ASP   A 153 ? 0.60264 0.61883 0.45855 -0.02055 -0.01472 -0.06321 153 ASP   A CG  
1175 O OD1 . ASP   A 153 ? 0.57952 0.59974 0.42107 -0.02307 -0.00470 -0.07429 153 ASP   A OD1 
1176 O OD2 . ASP   A 153 ? 0.61798 0.64549 0.48109 -0.02155 -0.02434 -0.05105 153 ASP   A OD2 
1177 N N   . TYR   A 154 ? 0.54044 0.53354 0.40155 -0.01045 0.03524  -0.09933 154 TYR   A N   
1178 C CA  . TYR   A 154 ? 0.59113 0.56725 0.46287 -0.00564 0.05869  -0.11532 154 TYR   A CA  
1179 C C   . TYR   A 154 ? 0.59723 0.55160 0.49852 -0.00013 0.06618  -0.11608 154 TYR   A C   
1180 O O   . TYR   A 154 ? 0.61819 0.57521 0.53983 0.00948  0.06610  -0.09987 154 TYR   A O   
1181 C CB  . TYR   A 154 ? 0.61722 0.58512 0.47480 -0.01377 0.06440  -0.13338 154 TYR   A CB  
1182 C CG  . TYR   A 154 ? 0.74866 0.69982 0.61902 -0.00698 0.09002  -0.14682 154 TYR   A CG  
1183 C CD1 . TYR   A 154 ? 0.72593 0.68377 0.60731 0.00528  0.10482  -0.13945 154 TYR   A CD1 
1184 C CD2 . TYR   A 154 ? 0.74579 0.67465 0.62235 -0.01205 0.10034  -0.16446 154 TYR   A CD2 
1185 C CE1 . TYR   A 154 ? 0.77539 0.71860 0.67571 0.01375  0.12874  -0.14761 154 TYR   A CE1 
1186 C CE2 . TYR   A 154 ? 0.74280 0.65435 0.63595 -0.00473 0.12458  -0.17445 154 TYR   A CE2 
1187 C CZ  . TYR   A 154 ? 0.85319 0.77214 0.75907 0.00886  0.13848  -0.16520 154 TYR   A CZ  
1188 O OH  . TYR   A 154 ? 0.85670 0.76010 0.78362 0.01749  0.16264  -0.17193 154 TYR   A OH  
1189 N N   . ASP   A 155 ? 0.55401 0.48779 0.46379 -0.00486 0.07002  -0.12749 155 ASP   A N   
1190 C CA  . ASP   A 155 ? 0.57460 0.48524 0.51778 0.00190  0.07840  -0.12340 155 ASP   A CA  
1191 C C   . ASP   A 155 ? 0.49190 0.39879 0.43685 -0.00547 0.06159  -0.11864 155 ASP   A C   
1192 O O   . ASP   A 155 ? 0.39350 0.28073 0.36565 -0.00154 0.06692  -0.11357 155 ASP   A O   
1193 C CB  . ASP   A 155 ? 0.60630 0.49489 0.56609 0.00371  0.09813  -0.13550 155 ASP   A CB  
1194 C CG  . ASP   A 155 ? 0.73982 0.62868 0.71413 0.01649  0.11792  -0.13278 155 ASP   A CG  
1195 O OD1 . ASP   A 155 ? 0.72072 0.62146 0.70833 0.02747  0.11751  -0.11513 155 ASP   A OD1 
1196 O OD2 . ASP   A 155 ? 0.77539 0.65379 0.74980 0.01585  0.13400  -0.14683 155 ASP   A OD2 
1197 N N   . CYS   A 156 ? 0.44960 0.37684 0.37044 -0.01431 0.04126  -0.11518 156 CYS   A N   
1198 C CA  . CYS   A 156 ? 0.36900 0.29746 0.29142 -0.02074 0.02509  -0.10861 156 CYS   A CA  
1199 C C   . CYS   A 156 ? 0.34937 0.29062 0.27209 -0.01716 0.01165  -0.09223 156 CYS   A C   
1200 O O   . CYS   A 156 ? 0.31545 0.27750 0.22399 -0.01533 0.00250  -0.08282 156 CYS   A O   
1201 C CB  . CYS   A 156 ? 0.39699 0.33934 0.30080 -0.03012 0.01270  -0.11115 156 CYS   A CB  
1202 S SG  . CYS   A 156 ? 0.35026 0.29345 0.26237 -0.03582 -0.00228 -0.10310 156 CYS   A SG  
1203 N N   . VAL   A 157 ? 0.29006 0.22113 0.23301 -0.01409 0.00816  -0.08051 157 VAL   A N   
1204 C CA  . VAL   A 157 ? 0.25857 0.20361 0.20429 -0.00957 -0.00772 -0.05809 157 VAL   A CA  
1205 C C   . VAL   A 157 ? 0.27586 0.23100 0.20639 -0.01985 -0.02180 -0.06139 157 VAL   A C   
1206 O O   . VAL   A 157 ? 0.24926 0.19536 0.18803 -0.02512 -0.02158 -0.06544 157 VAL   A O   
1207 C CB  . VAL   A 157 ? 0.21544 0.14923 0.18850 -0.00133 -0.00537 -0.04024 157 VAL   A CB  
1208 C CG1 . VAL   A 157 ? 0.18118 0.12951 0.15077 0.00038  -0.02163 -0.02103 157 VAL   A CG1 
1209 C CG2 . VAL   A 157 ? 0.27035 0.19856 0.26418 0.01005  0.00818  -0.03327 157 VAL   A CG2 
1210 N N   . SER   A 158 ? 0.25352 0.23848 0.18552 -0.01471 -0.02898 -0.05036 158 SER   A N   
1211 C CA  . SER   A 158 ? 0.23925 0.23814 0.18311 -0.01041 -0.03404 -0.04245 158 SER   A CA  
1212 C C   . SER   A 158 ? 0.19214 0.20259 0.14463 -0.01295 -0.03139 -0.02838 158 SER   A C   
1213 O O   . SER   A 158 ? 0.15428 0.16862 0.10681 -0.00886 -0.03225 -0.01832 158 SER   A O   
1214 C CB  . SER   A 158 ? 0.22484 0.21932 0.15379 -0.01020 -0.03885 -0.03630 158 SER   A CB  
1215 O OG  . SER   A 158 ? 0.31894 0.30895 0.23267 -0.01738 -0.03821 -0.04789 158 SER   A OG  
1216 N N   . PHE   A 159 ? 0.18070 0.17881 0.13403 -0.01590 -0.03452 -0.02756 159 PHE   A N   
1217 C CA  . PHE   A 159 ? 0.16086 0.15875 0.11961 -0.01148 -0.03530 -0.01441 159 PHE   A CA  
1218 C C   . PHE   A 159 ? 0.18292 0.18743 0.14260 -0.01066 -0.03525 -0.01153 159 PHE   A C   
1219 O O   . PHE   A 159 ? 0.15595 0.16590 0.11640 -0.01335 -0.03661 -0.01744 159 PHE   A O   
1220 C CB  . PHE   A 159 ? 0.17119 0.14777 0.12737 -0.01591 -0.04211 -0.01221 159 PHE   A CB  
1221 C CG  . PHE   A 159 ? 0.18816 0.14327 0.14704 -0.01455 -0.04530 -0.00901 159 PHE   A CG  
1222 C CD1 . PHE   A 159 ? 0.18793 0.14661 0.15077 -0.00734 -0.04820 0.00725  159 PHE   A CD1 
1223 C CD2 . PHE   A 159 ? 0.18186 0.12110 0.15369 -0.01689 -0.03396 -0.01904 159 PHE   A CD2 
1224 C CE1 . PHE   A 159 ? 0.16018 0.11044 0.14231 -0.00117 -0.04070 0.01669  159 PHE   A CE1 
1225 C CE2 . PHE   A 159 ? 0.15775 0.08405 0.14958 -0.00974 -0.02404 -0.01127 159 PHE   A CE2 
1226 C CZ  . PHE   A 159 ? 0.17362 0.10725 0.17198 -0.00117 -0.02783 0.00834  159 PHE   A CZ  
1227 N N   . CYS   A 160 ? 0.14064 0.14381 0.10161 -0.00758 -0.03415 -0.00448 160 CYS   A N   
1228 C CA  . CYS   A 160 ? 0.14318 0.15129 0.10553 -0.00705 -0.03398 -0.00346 160 CYS   A CA  
1229 C C   . CYS   A 160 ? 0.15595 0.15864 0.11965 -0.00665 -0.03294 0.00092  160 CYS   A C   
1230 O O   . CYS   A 160 ? 0.15960 0.16654 0.12436 -0.00587 -0.03296 0.00111  160 CYS   A O   
1231 C CB  . CYS   A 160 ? 0.14819 0.16280 0.10990 -0.00475 -0.03399 -0.00353 160 CYS   A CB  
1232 S SG  . CYS   A 160 ? 0.12855 0.13766 0.09158 -0.00322 -0.03229 0.00123  160 CYS   A SG  
1233 N N   . TYR   A 161 ? 0.13300 0.12841 0.09602 -0.00712 -0.03272 0.00381  161 TYR   A N   
1234 C CA  . TYR   A 161 ? 0.14871 0.14200 0.11049 -0.00734 -0.03216 0.00601  161 TYR   A CA  
1235 C C   . TYR   A 161 ? 0.14604 0.13606 0.10595 -0.00899 -0.03311 0.00932  161 TYR   A C   
1236 O O   . TYR   A 161 ? 0.12401 0.11226 0.08528 -0.00904 -0.03434 0.01158  161 TYR   A O   
1237 C CB  . TYR   A 161 ? 0.12238 0.11434 0.08400 -0.00665 -0.03201 0.00657  161 TYR   A CB  
1238 C CG  . TYR   A 161 ? 0.13340 0.12329 0.09109 -0.00751 -0.03237 0.00722  161 TYR   A CG  
1239 C CD1 . TYR   A 161 ? 0.14078 0.13315 0.09667 -0.00615 -0.03172 0.00548  161 TYR   A CD1 
1240 C CD2 . TYR   A 161 ? 0.11462 0.10207 0.06930 -0.00977 -0.03406 0.00952  161 TYR   A CD2 
1241 C CE1 . TYR   A 161 ? 0.14520 0.13595 0.09448 -0.00663 -0.03209 0.00470  161 TYR   A CE1 
1242 C CE2 . TYR   A 161 ? 0.11463 0.10119 0.06233 -0.01131 -0.03512 0.00917  161 TYR   A CE2 
1243 C CZ  . TYR   A 161 ? 0.13650 0.12381 0.08056 -0.00951 -0.03377 0.00602  161 TYR   A CZ  
1244 O OH  . TYR   A 161 ? 0.11356 0.09989 0.04777 -0.01077 -0.03439 0.00386  161 TYR   A OH  
1245 N N   . MET   A 162 ? 0.12817 0.11970 0.08482 -0.00982 -0.03285 0.01035  162 MET   A N   
1246 C CA  . MET   A 162 ? 0.15261 0.14432 0.10542 -0.01146 -0.03396 0.01488  162 MET   A CA  
1247 C C   . MET   A 162 ? 0.15052 0.14387 0.09596 -0.01172 -0.03361 0.01410  162 MET   A C   
1248 O O   . MET   A 162 ? 0.12121 0.11620 0.06415 -0.01003 -0.03197 0.01066  162 MET   A O   
1249 C CB  . MET   A 162 ? 0.14522 0.13803 0.09772 -0.01244 -0.03415 0.01786  162 MET   A CB  
1250 C CG  . MET   A 162 ? 0.15342 0.14839 0.10094 -0.01353 -0.03488 0.02507  162 MET   A CG  
1251 S SD  . MET   A 162 ? 0.24255 0.23651 0.19229 -0.01402 -0.03457 0.03368  162 MET   A SD  
1252 C CE  . MET   A 162 ? 0.24555 0.23249 0.20575 -0.01408 -0.03791 0.03877  162 MET   A CE  
1253 N N   . HIS   A 163 ? 0.14791 0.14192 0.08905 -0.01391 -0.03580 0.01744  163 HIS   A N   
1254 C CA  . HIS   A 163 ? 0.14922 0.14382 0.08014 -0.01541 -0.03648 0.01560  163 HIS   A CA  
1255 C C   . HIS   A 163 ? 0.16460 0.16257 0.08398 -0.01623 -0.03560 0.01708  163 HIS   A C   
1256 O O   . HIS   A 163 ? 0.15904 0.16027 0.07736 -0.01779 -0.03667 0.02378  163 HIS   A O   
1257 C CB  . HIS   A 163 ? 0.18826 0.18354 0.11756 -0.01911 -0.04036 0.01864  163 HIS   A CB  
1258 C CG  . HIS   A 163 ? 0.16779 0.16221 0.08476 -0.02203 -0.04180 0.01514  163 HIS   A CG  
1259 N ND1 . HIS   A 163 ? 0.17447 0.16434 0.08883 -0.01991 -0.03964 0.00842  163 HIS   A ND1 
1260 C CD2 . HIS   A 163 ? 0.20544 0.20342 0.11040 -0.02747 -0.04543 0.01706  163 HIS   A CD2 
1261 C CE1 . HIS   A 163 ? 0.20535 0.19404 0.10606 -0.02373 -0.04135 0.00476  163 HIS   A CE1 
1262 N NE2 . HIS   A 163 ? 0.21730 0.21097 0.11117 -0.02890 -0.04503 0.00954  163 HIS   A NE2 
1263 N N   . HIS   A 164 ? 0.17183 0.16920 0.08158 -0.01491 -0.03328 0.01144  164 HIS   A N   
1264 C CA  . HIS   A 164 ? 0.21544 0.21500 0.11002 -0.01498 -0.03047 0.01117  164 HIS   A CA  
1265 C C   . HIS   A 164 ? 0.23660 0.23494 0.11348 -0.01817 -0.03060 0.00607  164 HIS   A C   
1266 O O   . HIS   A 164 ? 0.29777 0.29905 0.15968 -0.02177 -0.03043 0.00882  164 HIS   A O   
1267 C CB  . HIS   A 164 ? 0.21687 0.21695 0.11228 -0.00994 -0.02557 0.00793  164 HIS   A CB  
1268 C CG  . HIS   A 164 ? 0.19333 0.19496 0.10071 -0.00907 -0.02559 0.01295  164 HIS   A CG  
1269 N ND1 . HIS   A 164 ? 0.19735 0.20033 0.09935 -0.00909 -0.02208 0.01801  164 HIS   A ND1 
1270 C CD2 . HIS   A 164 ? 0.15889 0.16011 0.08155 -0.00930 -0.02809 0.01358  164 HIS   A CD2 
1271 C CE1 . HIS   A 164 ? 0.17235 0.17605 0.08727 -0.00997 -0.02375 0.02142  164 HIS   A CE1 
1272 N NE2 . HIS   A 164 ? 0.14264 0.14524 0.06913 -0.01005 -0.02744 0.01780  164 HIS   A NE2 
1273 N N   . MET   A 165 ? 0.23326 0.22731 0.10991 -0.01790 -0.03074 -0.00135 165 MET   A N   
1274 C CA  . MET   A 165 ? 0.28400 0.27478 0.14084 -0.02123 -0.02909 -0.00956 165 MET   A CA  
1275 C C   . MET   A 165 ? 0.26696 0.25146 0.12584 -0.02349 -0.03161 -0.01593 165 MET   A C   
1276 O O   . MET   A 165 ? 0.23114 0.21397 0.10601 -0.02050 -0.03266 -0.01445 165 MET   A O   
1277 C CB  . MET   A 165 ? 0.27061 0.26035 0.11666 -0.01663 -0.02047 -0.01646 165 MET   A CB  
1278 C CG  . MET   A 165 ? 0.29275 0.28165 0.15162 -0.01047 -0.01693 -0.02123 165 MET   A CG  
1279 S SD  . MET   A 165 ? 0.42086 0.40650 0.26433 -0.00911 -0.00379 -0.02519 165 MET   A SD  
1280 C CE  . MET   A 165 ? 0.38692 0.36594 0.20269 -0.01389 0.00397  -0.03592 165 MET   A CE  
1281 N N   . GLU   A 166 ? 0.28204 0.26269 0.12272 -0.02975 -0.03239 -0.02306 166 GLU   A N   
1282 C CA  . GLU   A 166 ? 0.30153 0.27358 0.13969 -0.03306 -0.03371 -0.03205 166 GLU   A CA  
1283 C C   . GLU   A 166 ? 0.33469 0.29714 0.15896 -0.03155 -0.02520 -0.04753 166 GLU   A C   
1284 O O   . GLU   A 166 ? 0.32718 0.29024 0.13439 -0.03205 -0.01949 -0.05165 166 GLU   A O   
1285 C CB  . GLU   A 166 ? 0.26827 0.24197 0.09618 -0.04315 -0.04102 -0.03051 166 GLU   A CB  
1286 C CG  . GLU   A 166 ? 0.29245 0.25648 0.11619 -0.04844 -0.04308 -0.04067 166 GLU   A CG  
1287 C CD  . GLU   A 166 ? 0.33557 0.30446 0.15055 -0.05982 -0.05190 -0.03749 166 GLU   A CD  
1288 O OE1 . GLU   A 166 ? 0.28567 0.26396 0.11245 -0.06079 -0.05774 -0.02381 166 GLU   A OE1 
1289 O OE2 . GLU   A 166 ? 0.35674 0.31986 0.15306 -0.06835 -0.05255 -0.04954 166 GLU   A OE2 
1290 N N   . LEU   A 167 ? 0.32462 0.27705 0.15691 -0.02943 -0.02293 -0.05618 167 LEU   A N   
1291 C CA  . LEU   A 167 ? 0.34971 0.28291 0.17002 -0.02985 -0.01175 -0.07221 167 LEU   A CA  
1292 C C   . LEU   A 167 ? 0.41126 0.33174 0.21755 -0.03844 -0.01231 -0.08541 167 LEU   A C   
1293 O O   . LEU   A 167 ? 0.40097 0.32725 0.21273 -0.04305 -0.02288 -0.08150 167 LEU   A O   
1294 C CB  . LEU   A 167 ? 0.34207 0.26178 0.17694 -0.02497 -0.00702 -0.07299 167 LEU   A CB  
1295 C CG  . LEU   A 167 ? 0.33506 0.26444 0.18094 -0.01810 -0.00678 -0.06136 167 LEU   A CG  
1296 C CD1 . LEU   A 167 ? 0.30207 0.21414 0.15777 -0.01307 -0.00524 -0.06021 167 LEU   A CD1 
1297 C CD2 . LEU   A 167 ? 0.36891 0.29754 0.20286 -0.01499 0.00582  -0.06550 167 LEU   A CD2 
1298 N N   . PRO   A 168 ? 0.44164 0.34423 0.23044 -0.04108 0.00061  -0.10194 168 PRO   A N   
1299 C CA  . PRO   A 168 ? 0.44160 0.33008 0.21587 -0.05088 0.00084  -0.11695 168 PRO   A CA  
1300 C C   . PRO   A 168 ? 0.43082 0.31073 0.22051 -0.05436 -0.00733 -0.11760 168 PRO   A C   
1301 O O   . PRO   A 168 ? 0.43712 0.31494 0.21708 -0.06440 -0.01402 -0.12415 168 PRO   A O   
1302 C CB  . PRO   A 168 ? 0.45075 0.31643 0.21546 -0.04904 0.02134  -0.13476 168 PRO   A CB  
1303 C CG  . PRO   A 168 ? 0.43754 0.31409 0.20140 -0.04102 0.03000  -0.12783 168 PRO   A CG  
1304 C CD  . PRO   A 168 ? 0.45061 0.34455 0.23456 -0.03500 0.01794  -0.10841 168 PRO   A CD  
1305 N N   . THR   A 169 ? 0.41477 0.28980 0.22735 -0.04743 -0.00710 -0.11077 169 THR   A N   
1306 C CA  . THR   A 169 ? 0.45262 0.31818 0.27969 -0.05142 -0.01365 -0.11118 169 THR   A CA  
1307 C C   . THR   A 169 ? 0.39157 0.28141 0.22679 -0.05462 -0.02919 -0.09585 169 THR   A C   
1308 O O   . THR   A 169 ? 0.39555 0.28075 0.24286 -0.05862 -0.03464 -0.09414 169 THR   A O   
1309 C CB  . THR   A 169 ? 0.41667 0.26430 0.26514 -0.04319 -0.00636 -0.10896 169 THR   A CB  
1310 O OG1 . THR   A 169 ? 0.45602 0.31822 0.31068 -0.03499 -0.00733 -0.09507 169 THR   A OG1 
1311 C CG2 . THR   A 169 ? 0.45251 0.27024 0.30201 -0.03868 0.01273  -0.12450 169 THR   A CG2 
1312 N N   . GLY   A 170 ? 0.37040 0.28419 0.20219 -0.05210 -0.03448 -0.08399 170 GLY   A N   
1313 C CA  . GLY   A 170 ? 0.35978 0.28941 0.19809 -0.05536 -0.04473 -0.06807 170 GLY   A CA  
1314 C C   . GLY   A 170 ? 0.31168 0.25067 0.16959 -0.04694 -0.04580 -0.05184 170 GLY   A C   
1315 O O   . GLY   A 170 ? 0.29787 0.24626 0.16144 -0.04843 -0.05189 -0.03818 170 GLY   A O   
1316 N N   . VAL   A 171 ? 0.29807 0.23376 0.16641 -0.03854 -0.03955 -0.05330 171 VAL   A N   
1317 C CA  . VAL   A 171 ? 0.24209 0.18615 0.12529 -0.03158 -0.04068 -0.03854 171 VAL   A CA  
1318 C C   . VAL   A 171 ? 0.26669 0.22098 0.14766 -0.02757 -0.03825 -0.03272 171 VAL   A C   
1319 O O   . VAL   A 171 ? 0.24055 0.19611 0.10736 -0.02998 -0.03612 -0.03843 171 VAL   A O   
1320 C CB  . VAL   A 171 ? 0.27785 0.20492 0.16535 -0.02808 -0.03849 -0.04019 171 VAL   A CB  
1321 C CG1 . VAL   A 171 ? 0.32381 0.23238 0.21258 -0.03388 -0.04201 -0.04439 171 VAL   A CG1 
1322 C CG2 . VAL   A 171 ? 0.25059 0.16096 0.12639 -0.02582 -0.02896 -0.05245 171 VAL   A CG2 
1323 N N   . HIS   A 172 ? 0.23050 0.19090 0.12505 -0.02180 -0.03830 -0.02219 172 HIS   A N   
1324 C CA  . HIS   A 172 ? 0.19425 0.16366 0.09125 -0.01979 -0.03742 -0.01560 172 HIS   A CA  
1325 C C   . HIS   A 172 ? 0.20310 0.17674 0.11021 -0.01346 -0.03401 -0.01325 172 HIS   A C   
1326 O O   . HIS   A 172 ? 0.16250 0.13411 0.07886 -0.01034 -0.03458 -0.01122 172 HIS   A O   
1327 C CB  . HIS   A 172 ? 0.20355 0.17614 0.10869 -0.02193 -0.04149 -0.00622 172 HIS   A CB  
1328 C CG  . HIS   A 172 ? 0.24917 0.22158 0.14454 -0.02944 -0.04622 -0.00639 172 HIS   A CG  
1329 N ND1 . HIS   A 172 ? 0.22485 0.19326 0.12216 -0.03322 -0.05025 -0.00560 172 HIS   A ND1 
1330 C CD2 . HIS   A 172 ? 0.25906 0.23595 0.14158 -0.03486 -0.04834 -0.00681 172 HIS   A CD2 
1331 C CE1 . HIS   A 172 ? 0.25003 0.22129 0.13700 -0.04112 -0.05497 -0.00587 172 HIS   A CE1 
1332 N NE2 . HIS   A 172 ? 0.25067 0.22730 0.12793 -0.04242 -0.05405 -0.00644 172 HIS   A NE2 
1333 N N   . ALA   A 173 ? 0.17639 0.15689 0.08125 -0.01203 -0.03144 -0.01235 173 ALA   A N   
1334 C CA  . ALA   A 173 ? 0.16202 0.14905 0.07470 -0.00756 -0.02865 -0.01062 173 ALA   A CA  
1335 C C   . ALA   A 173 ? 0.18096 0.17378 0.09812 -0.00711 -0.02893 -0.00489 173 ALA   A C   
1336 O O   . ALA   A 173 ? 0.16515 0.15744 0.07446 -0.00979 -0.02979 -0.00334 173 ALA   A O   
1337 C CB  . ALA   A 173 ? 0.14758 0.13256 0.04741 -0.00655 -0.02303 -0.01875 173 ALA   A CB  
1338 N N   . GLY   A 174 ? 0.15235 0.15012 0.08103 -0.00449 -0.02864 -0.00184 174 GLY   A N   
1339 C CA  . GLY   A 174 ? 0.16231 0.16230 0.09474 -0.00471 -0.02877 0.00188  174 GLY   A CA  
1340 C C   . GLY   A 174 ? 0.14782 0.15334 0.08994 -0.00235 -0.02876 0.00252  174 GLY   A C   
1341 O O   . GLY   A 174 ? 0.11924 0.13074 0.06439 0.00031  -0.02864 0.00138  174 GLY   A O   
1342 N N   . THR   A 175 ? 0.13457 0.13904 0.08123 -0.00429 -0.02959 0.00486  175 THR   A N   
1343 C CA  . THR   A 175 ? 0.15868 0.16784 0.11206 -0.00414 -0.03077 0.00473  175 THR   A CA  
1344 C C   . THR   A 175 ? 0.17000 0.17725 0.12958 -0.00636 -0.03190 0.00445  175 THR   A C   
1345 O O   . THR   A 175 ? 0.12260 0.12393 0.08141 -0.00738 -0.03160 0.00542  175 THR   A O   
1346 C CB  . THR   A 175 ? 0.14420 0.15416 0.09465 -0.00630 -0.03082 0.00746  175 THR   A CB  
1347 O OG1 . THR   A 175 ? 0.11240 0.11753 0.06231 -0.00982 -0.03111 0.01083  175 THR   A OG1 
1348 C CG2 . THR   A 175 ? 0.14115 0.15064 0.07933 -0.00399 -0.02820 0.00851  175 THR   A CG2 
1349 N N   . ASP   A 176 ? 0.14654 0.15952 0.11117 -0.00703 -0.03386 0.00285  176 ASP   A N   
1350 C CA  . ASP   A 176 ? 0.12288 0.13483 0.08957 -0.00979 -0.03520 0.00108  176 ASP   A CA  
1351 C C   . ASP   A 176 ? 0.10603 0.11336 0.07200 -0.01347 -0.03594 0.00218  176 ASP   A C   
1352 O O   . ASP   A 176 ? 0.10799 0.11454 0.07183 -0.01406 -0.03546 0.00564  176 ASP   A O   
1353 C CB  . ASP   A 176 ? 0.11449 0.13536 0.08532 -0.01070 -0.03843 -0.00194 176 ASP   A CB  
1354 C CG  . ASP   A 176 ? 0.11988 0.14771 0.09621 -0.01391 -0.04130 -0.00198 176 ASP   A CG  
1355 O OD1 . ASP   A 176 ? 0.12634 0.15233 0.10388 -0.01726 -0.04117 -0.00153 176 ASP   A OD1 
1356 O OD2 . ASP   A 176 ? 0.11547 0.15232 0.09691 -0.01401 -0.04440 -0.00128 176 ASP   A OD2 
1357 N N   . LEU   A 177 ? 0.10910 0.11388 0.07616 -0.01593 -0.03743 -0.00091 177 LEU   A N   
1358 C CA  . LEU   A 177 ? 0.13155 0.12825 0.09817 -0.02153 -0.04057 0.00139  177 LEU   A CA  
1359 C C   . LEU   A 177 ? 0.17368 0.17186 0.14502 -0.03170 -0.04515 0.00124  177 LEU   A C   
1360 O O   . LEU   A 177 ? 0.18516 0.17244 0.16090 -0.04241 -0.04984 0.00416  177 LEU   A O   
1361 C CB  . LEU   A 177 ? 0.14197 0.12896 0.10737 -0.02437 -0.04324 -0.00253 177 LEU   A CB  
1362 C CG  . LEU   A 177 ? 0.17394 0.15320 0.13545 -0.01960 -0.04371 0.00466  177 LEU   A CG  
1363 C CD1 . LEU   A 177 ? 0.18648 0.15693 0.14687 -0.02228 -0.04884 0.01807  177 LEU   A CD1 
1364 C CD2 . LEU   A 177 ? 0.12875 0.11831 0.09162 -0.01238 -0.03674 0.00476  177 LEU   A CD2 
1365 N N   . GLU   A 178 ? 0.14550 0.15690 0.12211 -0.03027 -0.04413 -0.00168 178 GLU   A N   
1366 C CA  . GLU   A 178 ? 0.17210 0.19030 0.15825 -0.04094 -0.04758 0.00049  178 GLU   A CA  
1367 C C   . GLU   A 178 ? 0.16369 0.18978 0.14809 -0.04057 -0.04731 0.01051  178 GLU   A C   
1368 O O   . GLU   A 178 ? 0.18223 0.22200 0.18010 -0.04911 -0.04885 0.01487  178 GLU   A O   
1369 C CB  . GLU   A 178 ? 0.15957 0.19028 0.15527 -0.04207 -0.04889 -0.00773 178 GLU   A CB  
1370 N N   . GLY   A 179 ? 0.15179 0.17213 0.12354 -0.03114 -0.04339 0.01321  179 GLY   A N   
1371 C CA  . GLY   A 179 ? 0.16409 0.19005 0.12868 -0.03029 -0.04091 0.02052  179 GLY   A CA  
1372 C C   . GLY   A 179 ? 0.17912 0.21514 0.14577 -0.02450 -0.03913 0.01842  179 GLY   A C   
1373 O O   . GLY   A 179 ? 0.15785 0.19841 0.11425 -0.02324 -0.03501 0.02343  179 GLY   A O   
1374 N N   . ASN   A 180 ? 0.13097 0.17091 0.10788 -0.02084 -0.04112 0.01271  180 ASN   A N   
1375 C CA  . ASN   A 180 ? 0.11685 0.16636 0.09820 -0.01558 -0.04127 0.01430  180 ASN   A CA  
1376 C C   . ASN   A 180 ? 0.14280 0.17636 0.11133 -0.00658 -0.03830 0.00963  180 ASN   A C   
1377 O O   . ASN   A 180 ? 0.12049 0.14580 0.08849 -0.00243 -0.03708 0.00418  180 ASN   A O   
1378 C CB  . ASN   A 180 ? 0.11353 0.17229 0.10922 -0.01547 -0.04494 0.01248  180 ASN   A CB  
1379 C CG  . ASN   A 180 ? 0.10727 0.17776 0.11539 -0.02530 -0.04804 0.01330  180 ASN   A CG  
1380 O OD1 . ASN   A 180 ? 0.09523 0.18418 0.11825 -0.03127 -0.04817 0.02102  180 ASN   A OD1 
1381 N ND2 . ASN   A 180 ? 0.09338 0.15541 0.09828 -0.02721 -0.04964 0.00534  180 ASN   A ND2 
1382 N N   . PHE   A 181 ? 0.15334 0.19024 0.11291 -0.00521 -0.03615 0.01331  181 PHE   A N   
1383 C CA  . PHE   A 181 ? 0.15685 0.17856 0.10436 0.00058  -0.03490 0.00852  181 PHE   A CA  
1384 C C   . PHE   A 181 ? 0.14022 0.16251 0.09994 0.00515  -0.03893 0.00798  181 PHE   A C   
1385 O O   . PHE   A 181 ? 0.12686 0.16578 0.10359 0.00478  -0.04186 0.01367  181 PHE   A O   
1386 C CB  . PHE   A 181 ? 0.15427 0.17787 0.08967 0.00224  -0.02576 0.00837  181 PHE   A CB  
1387 C CG  . PHE   A 181 ? 0.18041 0.19159 0.08821 -0.00247 -0.02146 0.00434  181 PHE   A CG  
1388 C CD1 . PHE   A 181 ? 0.16600 0.17136 0.07407 -0.00003 -0.02161 -0.00162 181 PHE   A CD1 
1389 C CD2 . PHE   A 181 ? 0.14948 0.16609 0.05374 -0.00599 -0.01374 0.00798  181 PHE   A CD2 
1390 C CE1 . PHE   A 181 ? 0.16370 0.16663 0.06296 -0.00084 -0.01869 -0.00314 181 PHE   A CE1 
1391 C CE2 . PHE   A 181 ? 0.21932 0.22646 0.10684 -0.00778 -0.01038 0.00666  181 PHE   A CE2 
1392 C CZ  . PHE   A 181 ? 0.19757 0.19829 0.08436 -0.00363 -0.01401 0.00101  181 PHE   A CZ  
1393 N N   . TYR   A 182 ? 0.12690 0.15046 0.08846 0.00878  -0.03185 0.00349  182 TYR   A N   
1394 C CA  . TYR   A 182 ? 0.13775 0.16931 0.10715 0.00931  -0.03220 0.00798  182 TYR   A CA  
1395 C C   . TYR   A 182 ? 0.17264 0.19110 0.13144 0.01202  -0.04060 0.01269  182 TYR   A C   
1396 O O   . TYR   A 182 ? 0.14046 0.14196 0.07746 0.01254  -0.03691 0.00428  182 TYR   A O   
1397 C CB  . TYR   A 182 ? 0.14068 0.16443 0.10730 0.00513  -0.03278 0.00724  182 TYR   A CB  
1398 C CG  . TYR   A 182 ? 0.15596 0.17833 0.12419 0.00399  -0.03385 0.00517  182 TYR   A CG  
1399 C CD1 . TYR   A 182 ? 0.12302 0.14886 0.09514 0.00548  -0.03701 0.00599  182 TYR   A CD1 
1400 C CD2 . TYR   A 182 ? 0.12848 0.14420 0.09346 0.00042  -0.03259 0.00357  182 TYR   A CD2 
1401 C CE1 . TYR   A 182 ? 0.14140 0.16697 0.11259 0.00223  -0.03806 0.00444  182 TYR   A CE1 
1402 C CE2 . TYR   A 182 ? 0.11552 0.13036 0.08206 -0.00167 -0.03318 0.00289  182 TYR   A CE2 
1403 C CZ  . TYR   A 182 ? 0.12199 0.14274 0.09086 -0.00087 -0.03553 0.00253  182 TYR   A CZ  
1404 O OH  . TYR   A 182 ? 0.11236 0.13339 0.08017 -0.00307 -0.03641 0.00052  182 TYR   A OH  
1405 N N   . GLY   A 183 ? 0.14587 0.17517 0.12629 0.02139  -0.04027 0.02023  183 GLY   A N   
1406 C CA  . GLY   A 183 ? 0.16668 0.18426 0.15823 0.02958  -0.02630 0.01848  183 GLY   A CA  
1407 C C   . GLY   A 183 ? 0.15780 0.17786 0.15602 0.03228  -0.01153 0.01554  183 GLY   A C   
1408 O O   . GLY   A 183 ? 0.14382 0.17909 0.14433 0.02811  -0.01343 0.01842  183 GLY   A O   
1409 N N   . PRO   A 184 ? 0.17378 0.17813 0.17585 0.03876  0.00483  0.00917  184 PRO   A N   
1410 C CA  . PRO   A 184 ? 0.20670 0.21573 0.22047 0.04364  0.02261  0.00770  184 PRO   A CA  
1411 C C   . PRO   A 184 ? 0.23010 0.22568 0.20998 0.03648  0.03140  -0.00610 184 PRO   A C   
1412 O O   . PRO   A 184 ? 0.23671 0.22925 0.21782 0.04017  0.05034  -0.01161 184 PRO   A O   
1413 C CB  . PRO   A 184 ? 0.17917 0.17639 0.21730 0.05569  0.03857  0.00755  184 PRO   A CB  
1414 C CG  . PRO   A 184 ? 0.23913 0.21117 0.25775 0.05215  0.03326  -0.00144 184 PRO   A CG  
1415 C CD  . PRO   A 184 ? 0.21273 0.19572 0.21632 0.04311  0.00955  0.00461  184 PRO   A CD  
1416 N N   . PHE   A 185 ? 0.23742 0.22641 0.18731 0.02638  0.01836  -0.01055 185 PHE   A N   
1417 C CA  . PHE   A 185 ? 0.24042 0.21907 0.15602 0.01838  0.02365  -0.02072 185 PHE   A CA  
1418 C C   . PHE   A 185 ? 0.24954 0.24544 0.16527 0.01455  0.02424  -0.01320 185 PHE   A C   
1419 O O   . PHE   A 185 ? 0.19490 0.20775 0.13085 0.01425  0.01465  -0.00234 185 PHE   A O   
1420 C CB  . PHE   A 185 ? 0.25427 0.22101 0.14289 0.00969  0.00912  -0.02547 185 PHE   A CB  
1421 C CG  . PHE   A 185 ? 0.25347 0.20472 0.14720 0.01243  0.00752  -0.03064 185 PHE   A CG  
1422 C CD1 . PHE   A 185 ? 0.28248 0.21443 0.17252 0.01496  0.02372  -0.04367 185 PHE   A CD1 
1423 C CD2 . PHE   A 185 ? 0.22748 0.18264 0.13152 0.01261  -0.00777 -0.02274 185 PHE   A CD2 
1424 C CE1 . PHE   A 185 ? 0.31899 0.23369 0.21787 0.01722  0.02412  -0.04818 185 PHE   A CE1 
1425 C CE2 . PHE   A 185 ? 0.25085 0.19189 0.16278 0.01513  -0.00806 -0.02525 185 PHE   A CE2 
1426 C CZ  . PHE   A 185 ? 0.30423 0.22477 0.21530 0.01733  0.00725  -0.03717 185 PHE   A CZ  
1427 N N   . VAL   A 186 ? 0.22473 0.21637 0.11813 0.01087  0.03697  -0.01944 186 VAL   A N   
1428 C CA  . VAL   A 186 ? 0.29246 0.29860 0.18417 0.00663  0.04036  -0.01140 186 VAL   A CA  
1429 C C   . VAL   A 186 ? 0.32009 0.31905 0.17193 -0.00340 0.03779  -0.01497 186 VAL   A C   
1430 O O   . VAL   A 186 ? 0.33646 0.32303 0.16864 -0.00542 0.03698  -0.02574 186 VAL   A O   
1431 C CB  . VAL   A 186 ? 0.29781 0.31258 0.20697 0.01340  0.06216  -0.01105 186 VAL   A CB  
1432 C CG1 . VAL   A 186 ? 0.24619 0.27471 0.19990 0.02260  0.06122  -0.00239 186 VAL   A CG1 
1433 C CG2 . VAL   A 186 ? 0.33243 0.32923 0.22001 0.01581  0.08056  -0.02721 186 VAL   A CG2 
1434 N N   . ASP   A 187 ? 0.30657 0.31714 0.15558 -0.00907 0.03395  -0.00355 187 ASP   A N   
1435 C CA  . ASP   A 187 ? 0.34269 0.34913 0.17688 -0.01140 0.02637  -0.00064 187 ASP   A CA  
1436 C C   . ASP   A 187 ? 0.40985 0.42035 0.22767 -0.01200 0.04233  -0.00209 187 ASP   A C   
1437 O O   . ASP   A 187 ? 0.40687 0.42451 0.22348 -0.01477 0.04585  0.00902  187 ASP   A O   
1438 C CB  . ASP   A 187 ? 0.30330 0.31306 0.15062 -0.01404 0.01361  0.01217  187 ASP   A CB  
1439 C CG  . ASP   A 187 ? 0.32481 0.34899 0.18590 -0.01838 0.01968  0.02339  187 ASP   A CG  
1440 O OD1 . ASP   A 187 ? 0.33715 0.37258 0.20767 -0.01643 0.03303  0.02239  187 ASP   A OD1 
1441 O OD2 . ASP   A 187 ? 0.21832 0.24460 0.09047 -0.02165 0.01199  0.03334  187 ASP   A OD2 
1442 N N   . ARG   A 188 ? 0.44454 0.44927 0.25128 -0.00974 0.05271  -0.01679 188 ARG   A N   
1443 C CA  . ARG   A 188 ? 0.54058 0.54721 0.32826 -0.01014 0.06594  -0.02274 188 ARG   A CA  
1444 C C   . ARG   A 188 ? 0.59803 0.59297 0.36873 -0.01273 0.05933  -0.03633 188 ARG   A C   
1445 O O   . ARG   A 188 ? 0.58196 0.56737 0.36063 -0.01274 0.04975  -0.04230 188 ARG   A O   
1446 C CB  . ARG   A 188 ? 0.53542 0.54502 0.33149 -0.00507 0.09066  -0.03084 188 ARG   A CB  
1447 C CG  . ARG   A 188 ? 0.55698 0.58324 0.37392 -0.00337 0.10169  -0.01731 188 ARG   A CG  
1448 C CD  . ARG   A 188 ? 0.50317 0.52592 0.34702 0.00051  0.10112  -0.01509 188 ARG   A CD  
1449 N NE  . ARG   A 188 ? 0.56786 0.61093 0.44968 0.00437  0.10567  -0.00005 188 ARG   A NE  
1450 C CZ  . ARG   A 188 ? 0.50494 0.55912 0.40080 -0.00122 0.08973  0.01441  188 ARG   A CZ  
1451 N NH1 . ARG   A 188 ? 0.37261 0.41891 0.24827 -0.00857 0.07122  0.01629  188 ARG   A NH1 
1452 N NH2 . ARG   A 188 ? 0.57571 0.64868 0.50760 0.00002  0.09298  0.02676  188 ARG   A NH2 
1453 N N   . GLN   A 189 ? 0.67130 0.66726 0.41827 -0.01578 0.06554  -0.04128 189 GLN   A N   
1454 C CA  . GLN   A 189 ? 0.72111 0.70513 0.45071 -0.02009 0.06349  -0.05731 189 GLN   A CA  
1455 C C   . GLN   A 189 ? 0.69286 0.66673 0.42026 -0.01667 0.08557  -0.07475 189 GLN   A C   
1456 O O   . GLN   A 189 ? 0.77925 0.75422 0.48685 -0.01798 0.09906  -0.08237 189 GLN   A O   
1457 C CB  . GLN   A 189 ? 0.79646 0.78580 0.49949 -0.02709 0.05675  -0.05455 189 GLN   A CB  
1458 C CG  . GLN   A 189 ? 0.83669 0.81466 0.52552 -0.03404 0.04991  -0.06959 189 GLN   A CG  
1459 C CD  . GLN   A 189 ? 0.97331 0.95685 0.63099 -0.04309 0.04629  -0.07071 189 GLN   A CD  
1460 O OE1 . GLN   A 189 ? 1.00093 0.99728 0.65373 -0.04503 0.03831  -0.05464 189 GLN   A OE1 
1461 N NE2 . GLN   A 189 ? 0.99949 0.97214 0.63562 -0.04955 0.05299  -0.09035 189 GLN   A NE2 
1462 N N   . THR   A 190 ? 0.63320 0.59623 0.38342 -0.01123 0.09057  -0.08041 190 THR   A N   
1463 C CA  . THR   A 190 ? 0.63200 0.57960 0.39025 -0.00547 0.11168  -0.09642 190 THR   A CA  
1464 C C   . THR   A 190 ? 0.57625 0.50360 0.34591 -0.00517 0.10523  -0.10516 190 THR   A C   
1465 O O   . THR   A 190 ? 0.59425 0.52362 0.37429 -0.00617 0.08837  -0.09603 190 THR   A O   
1466 C CB  . THR   A 190 ? 0.62390 0.57968 0.41069 0.00509  0.12997  -0.08967 190 THR   A CB  
1467 O OG1 . THR   A 190 ? 0.60866 0.56368 0.42183 0.00971  0.12225  -0.08054 190 THR   A OG1 
1468 C CG2 . THR   A 190 ? 0.64045 0.61993 0.42106 0.00367  0.13330  -0.07608 190 THR   A CG2 
1469 N N   . ALA   A 191 ? 0.57803 0.48555 0.34649 -0.00379 0.11937  -0.12238 191 ALA   A N   
1470 C CA  . ALA   A 191 ? 0.53675 0.42304 0.31866 -0.00313 0.11588  -0.13013 191 ALA   A CA  
1471 C C   . ALA   A 191 ? 0.55963 0.44683 0.37446 0.00628  0.11317  -0.11779 191 ALA   A C   
1472 O O   . ALA   A 191 ? 0.56038 0.45224 0.40088 0.01779  0.12851  -0.11173 191 ALA   A O   
1473 C CB  . ALA   A 191 ? 0.53536 0.39935 0.32108 0.00045  0.13763  -0.14825 191 ALA   A CB  
1474 N N   . GLN   A 192 ? 0.52821 0.41424 0.34364 0.00162  0.09320  -0.11221 192 GLN   A N   
1475 C CA  . GLN   A 192 ? 0.52266 0.40606 0.36485 0.00953  0.08926  -0.10226 192 GLN   A CA  
1476 C C   . GLN   A 192 ? 0.54506 0.41229 0.38920 0.00496  0.07752  -0.10685 192 GLN   A C   
1477 O O   . GLN   A 192 ? 0.53103 0.39957 0.35471 -0.00646 0.06416  -0.11153 192 GLN   A O   
1478 C CB  . GLN   A 192 ? 0.47543 0.37935 0.31489 0.00786  0.07445  -0.08616 192 GLN   A CB  
1479 C CG  . GLN   A 192 ? 0.50796 0.43060 0.34436 0.00957  0.08340  -0.07925 192 GLN   A CG  
1480 C CD  . GLN   A 192 ? 0.45267 0.39357 0.28453 0.00498  0.06617  -0.06359 192 GLN   A CD  
1481 O OE1 . GLN   A 192 ? 0.34867 0.29614 0.20337 0.01012  0.05689  -0.05205 192 GLN   A OE1 
1482 N NE2 . GLN   A 192 ? 0.48928 0.44485 0.30486 -0.00265 0.05731  -0.05859 192 GLN   A NE2 
1483 N N   . ALA   A 193 ? 0.53072 0.38534 0.40440 0.01500  0.08258  -0.10277 193 ALA   A N   
1484 C CA  . ALA   A 193 ? 0.53996 0.37888 0.41918 0.01102  0.07258  -0.10516 193 ALA   A CA  
1485 C C   . ALA   A 193 ? 0.49326 0.33210 0.39655 0.01966  0.06516  -0.08969 193 ALA   A C   
1486 O O   . ALA   A 193 ? 0.50439 0.36048 0.43805 0.03252  0.06895  -0.07406 193 ALA   A O   
1487 C CB  . ALA   A 193 ? 0.49912 0.31517 0.39226 0.01408  0.08847  -0.11728 193 ALA   A CB  
1488 N N   . ALA   A 194 ? 0.46266 0.29545 0.36085 0.01190  0.04853  -0.08766 194 ALA   A N   
1489 C CA  . ALA   A 194 ? 0.43259 0.28318 0.35277 0.01651  0.03067  -0.06602 194 ALA   A CA  
1490 C C   . ALA   A 194 ? 0.43732 0.28996 0.40339 0.03220  0.03846  -0.05101 194 ALA   A C   
1491 O O   . ALA   A 194 ? 0.48015 0.35877 0.46658 0.03883  0.02770  -0.03080 194 ALA   A O   
1492 C CB  . ALA   A 194 ? 0.42433 0.26658 0.33056 0.00468  0.01469  -0.06795 194 ALA   A CB  
1493 N N   . GLY   A 195 ? 0.42302 0.24976 0.40667 0.03776  0.05671  -0.05963 195 GLY   A N   
1494 C CA  . GLY   A 195 ? 0.41951 0.25342 0.44998 0.05214  0.05856  -0.03821 195 GLY   A CA  
1495 C C   . GLY   A 195 ? 0.41137 0.23836 0.44954 0.04788  0.04530  -0.02935 195 GLY   A C   
1496 O O   . GLY   A 195 ? 0.39974 0.23182 0.41185 0.03567  0.02777  -0.03115 195 GLY   A O   
1497 N N   . THR   A 196 ? 0.40929 0.23193 0.48293 0.05662  0.05204  -0.01737 196 THR   A N   
1498 C CA  . THR   A 196 ? 0.41220 0.22692 0.49313 0.05163  0.04288  -0.00976 196 THR   A CA  
1499 C C   . THR   A 196 ? 0.36522 0.20359 0.44494 0.04992  0.02182  0.00955  196 THR   A C   
1500 O O   . THR   A 196 ? 0.37868 0.24894 0.46982 0.05720  0.01428  0.02761  196 THR   A O   
1501 C CB  . THR   A 196 ? 0.39695 0.21362 0.51538 0.06119  0.05302  0.00404  196 THR   A CB  
1502 O OG1 . THR   A 196 ? 0.48517 0.27500 0.60296 0.06043  0.07240  -0.01618 196 THR   A OG1 
1503 C CG2 . THR   A 196 ? 0.41265 0.22950 0.54200 0.05746  0.04307  0.01794  196 THR   A CG2 
1504 N N   . ASP   A 197 ? 0.33862 0.16589 0.40241 0.03824  0.01103  0.00517  197 ASP   A N   
1505 C CA  . ASP   A 197 ? 0.33992 0.19556 0.39841 0.03514  -0.00907 0.02290  197 ASP   A CA  
1506 C C   . ASP   A 197 ? 0.35700 0.22238 0.43760 0.03806  -0.01025 0.04188  197 ASP   A C   
1507 O O   . ASP   A 197 ? 0.34444 0.19135 0.44191 0.03964  0.00102  0.04003  197 ASP   A O   
1508 C CB  . ASP   A 197 ? 0.34039 0.19416 0.36276 0.01933  -0.02162 0.00948  197 ASP   A CB  
1509 C CG  . ASP   A 197 ? 0.31323 0.19941 0.32467 0.01800  -0.03861 0.02297  197 ASP   A CG  
1510 O OD1 . ASP   A 197 ? 0.31140 0.22159 0.33588 0.02713  -0.04106 0.03812  197 ASP   A OD1 
1511 O OD2 . ASP   A 197 ? 0.28927 0.17762 0.28018 0.00748  -0.04898 0.01819  197 ASP   A OD2 
1512 N N   . THR   A 198 ? 0.32294 0.22163 0.39886 0.03708  -0.02296 0.05713  198 THR   A N   
1513 C CA  . THR   A 198 ? 0.30615 0.22150 0.39610 0.03734  -0.02444 0.07237  198 THR   A CA  
1514 C C   . THR   A 198 ? 0.29511 0.22850 0.36530 0.02873  -0.03570 0.07379  198 THR   A C   
1515 O O   . THR   A 198 ? 0.25841 0.20064 0.30627 0.02426  -0.04228 0.06556  198 THR   A O   
1516 C CB  . THR   A 198 ? 0.30744 0.25079 0.41447 0.04460  -0.02261 0.08630  198 THR   A CB  
1517 O OG1 . THR   A 198 ? 0.27404 0.24338 0.36132 0.04232  -0.03079 0.08444  198 THR   A OG1 
1518 C CG2 . THR   A 198 ? 0.32788 0.25771 0.45850 0.05381  -0.00940 0.08524  198 THR   A CG2 
1519 N N   . THR   A 199 ? 0.28195 0.22148 0.36270 0.02633  -0.03602 0.08361  199 THR   A N   
1520 C CA  . THR   A 199 ? 0.27475 0.23051 0.34118 0.01881  -0.04280 0.08401  199 THR   A CA  
1521 C C   . THR   A 199 ? 0.25301 0.23834 0.30988 0.01995  -0.04390 0.08702  199 THR   A C   
1522 O O   . THR   A 199 ? 0.24695 0.24339 0.31742 0.02435  -0.04171 0.09704  199 THR   A O   
1523 C CB  . THR   A 199 ? 0.28822 0.23482 0.37189 0.01513  -0.04163 0.09254  199 THR   A CB  
1524 O OG1 . THR   A 199 ? 0.28634 0.19787 0.37540 0.01143  -0.03897 0.08358  199 THR   A OG1 
1525 C CG2 . THR   A 199 ? 0.27041 0.23427 0.34287 0.00781  -0.04712 0.09339  199 THR   A CG2 
1526 N N   . ILE   A 200 ? 0.19852 0.19485 0.23558 0.01481  -0.04658 0.07807  200 ILE   A N   
1527 C CA  . ILE   A 200 ? 0.21221 0.23149 0.24637 0.01226  -0.04750 0.08106  200 ILE   A CA  
1528 C C   . ILE   A 200 ? 0.21683 0.25096 0.26145 0.00906  -0.04733 0.09457  200 ILE   A C   
1529 O O   . ILE   A 200 ? 0.17024 0.20834 0.20889 0.00411  -0.04766 0.09297  200 ILE   A O   
1530 C CB  . ILE   A 200 ? 0.21697 0.23912 0.23264 0.00792  -0.04806 0.06781  200 ILE   A CB  
1531 C CG1 . ILE   A 200 ? 0.22173 0.23214 0.22908 0.01072  -0.04764 0.05668  200 ILE   A CG1 
1532 C CG2 . ILE   A 200 ? 0.18819 0.22914 0.20022 0.00564  -0.04789 0.07015  200 ILE   A CG2 
1533 C CD1 . ILE   A 200 ? 0.23315 0.23866 0.22848 0.00551  -0.04733 0.04544  200 ILE   A CD1 
1534 N N   . THR   A 201 ? 0.23903 0.28409 0.30122 0.01210  -0.04616 0.10959  201 THR   A N   
1535 C CA  . THR   A 201 ? 0.21320 0.27177 0.28925 0.00996  -0.04528 0.12545  201 THR   A CA  
1536 C C   . THR   A 201 ? 0.18655 0.26565 0.24993 0.00409  -0.04610 0.12591  201 THR   A C   
1537 O O   . THR   A 201 ? 0.20022 0.28403 0.26628 0.00106  -0.04536 0.13123  201 THR   A O   
1538 C CB  . THR   A 201 ? 0.24781 0.31832 0.34734 0.01438  -0.04335 0.14373  201 THR   A CB  
1539 O OG1 . THR   A 201 ? 0.25115 0.30171 0.36227 0.02139  -0.04064 0.14121  201 THR   A OG1 
1540 C CG2 . THR   A 201 ? 0.22578 0.30447 0.34413 0.01331  -0.04153 0.16093  201 THR   A CG2 
1541 N N   . VAL   A 202 ? 0.16188 0.25314 0.21236 0.00263  -0.04712 0.12063  202 VAL   A N   
1542 C CA  . VAL   A 202 ? 0.16318 0.27282 0.20156 -0.00203 -0.04697 0.12069  202 VAL   A CA  
1543 C C   . VAL   A 202 ? 0.15554 0.25444 0.18332 -0.00432 -0.04544 0.10978  202 VAL   A C   
1544 O O   . VAL   A 202 ? 0.15814 0.26986 0.18383 -0.00681 -0.04399 0.11469  202 VAL   A O   
1545 C CB  . VAL   A 202 ? 0.16522 0.28579 0.19114 -0.00356 -0.04862 0.11444  202 VAL   A CB  
1546 C CG1 . VAL   A 202 ? 0.17572 0.27658 0.19161 -0.00209 -0.04870 0.09707  202 VAL   A CG1 
1547 C CG2 . VAL   A 202 ? 0.19306 0.33187 0.20549 -0.00800 -0.04842 0.11355  202 VAL   A CG2 
1548 N N   . ASN   A 203 ? 0.15771 0.23505 0.18008 -0.00331 -0.04572 0.09643  203 ASN   A N   
1549 C CA  . ASN   A 203 ? 0.16873 0.23706 0.18376 -0.00565 -0.04468 0.08743  203 ASN   A CA  
1550 C C   . ASN   A 203 ? 0.17807 0.24532 0.20540 -0.00754 -0.04474 0.09669  203 ASN   A C   
1551 O O   . ASN   A 203 ? 0.18144 0.25478 0.20692 -0.01019 -0.04324 0.09719  203 ASN   A O   
1552 C CB  . ASN   A 203 ? 0.15085 0.19994 0.15885 -0.00460 -0.04555 0.07359  203 ASN   A CB  
1553 C CG  . ASN   A 203 ? 0.18154 0.23164 0.17746 -0.00361 -0.04464 0.06329  203 ASN   A CG  
1554 O OD1 . ASN   A 203 ? 0.21080 0.27485 0.20262 -0.00422 -0.04416 0.06537  203 ASN   A OD1 
1555 N ND2 . ASN   A 203 ? 0.18696 0.22351 0.17784 -0.00262 -0.04462 0.05299  203 ASN   A ND2 
1556 N N   . VAL   A 204 ? 0.19652 0.25484 0.23802 -0.00581 -0.04622 0.10403  204 VAL   A N   
1557 C CA  . VAL   A 204 ? 0.17789 0.23535 0.23498 -0.00774 -0.04636 0.11500  204 VAL   A CA  
1558 C C   . VAL   A 204 ? 0.17129 0.25292 0.23371 -0.00921 -0.04393 0.12860  204 VAL   A C   
1559 O O   . VAL   A 204 ? 0.17516 0.26286 0.24064 -0.01234 -0.04296 0.13230  204 VAL   A O   
1560 C CB  . VAL   A 204 ? 0.18176 0.22552 0.25599 -0.00393 -0.04673 0.12250  204 VAL   A CB  
1561 C CG1 . VAL   A 204 ? 0.19661 0.23887 0.28981 -0.00613 -0.04620 0.13502  204 VAL   A CG1 
1562 C CG2 . VAL   A 204 ? 0.18286 0.20217 0.24976 -0.00187 -0.04836 0.10897  204 VAL   A CG2 
1563 N N   . LEU   A 205 ? 0.16706 0.26498 0.23157 -0.00707 -0.04310 0.13757  205 LEU   A N   
1564 C CA  . LEU   A 205 ? 0.17643 0.30072 0.24337 -0.00850 -0.04125 0.15119  205 LEU   A CA  
1565 C C   . LEU   A 205 ? 0.17061 0.30311 0.22024 -0.01089 -0.03945 0.14236  205 LEU   A C   
1566 O O   . LEU   A 205 ? 0.17596 0.32256 0.22925 -0.01225 -0.03728 0.15120  205 LEU   A O   
1567 C CB  . LEU   A 205 ? 0.18607 0.32860 0.25373 -0.00698 -0.04211 0.16003  205 LEU   A CB  
1568 C CG  . LEU   A 205 ? 0.19654 0.33814 0.28782 -0.00345 -0.04241 0.17533  205 LEU   A CG  
1569 C CD1 . LEU   A 205 ? 0.20665 0.37125 0.29965 -0.00281 -0.04390 0.18593  205 LEU   A CD1 
1570 C CD2 . LEU   A 205 ? 0.20774 0.35476 0.32090 -0.00351 -0.04041 0.19304  205 LEU   A CD2 
1571 N N   . ALA   A 206 ? 0.16110 0.28476 0.19350 -0.01063 -0.03977 0.12564  206 ALA   A N   
1572 C CA  . ALA   A 206 ? 0.18275 0.31197 0.20029 -0.01142 -0.03735 0.11679  206 ALA   A CA  
1573 C C   . ALA   A 206 ? 0.17092 0.29305 0.19441 -0.01267 -0.03579 0.11615  206 ALA   A C   
1574 O O   . ALA   A 206 ? 0.16722 0.30153 0.18673 -0.01265 -0.03267 0.11807  206 ALA   A O   
1575 C CB  . ALA   A 206 ? 0.16478 0.28287 0.16727 -0.01042 -0.03804 0.10015  206 ALA   A CB  
1576 N N   . TRP   A 207 ? 0.17214 0.27570 0.20513 -0.01392 -0.03830 0.11381  207 TRP   A N   
1577 C CA  . TRP   A 207 ? 0.17014 0.26807 0.21083 -0.01686 -0.03854 0.11399  207 TRP   A CA  
1578 C C   . TRP   A 207 ? 0.15755 0.26790 0.21593 -0.01866 -0.03773 0.13087  207 TRP   A C   
1579 O O   . TRP   A 207 ? 0.16836 0.28556 0.23260 -0.02065 -0.03625 0.13455  207 TRP   A O   
1580 C CB  . TRP   A 207 ? 0.15879 0.23378 0.20135 -0.01875 -0.04299 0.10509  207 TRP   A CB  
1581 C CG  . TRP   A 207 ? 0.15381 0.22137 0.20744 -0.02395 -0.04629 0.10664  207 TRP   A CG  
1582 C CD1 . TRP   A 207 ? 0.18781 0.25527 0.23933 -0.02706 -0.04665 0.10147  207 TRP   A CD1 
1583 C CD2 . TRP   A 207 ? 0.16578 0.22449 0.23576 -0.02695 -0.05054 0.11431  207 TRP   A CD2 
1584 N NE1 . TRP   A 207 ? 0.13352 0.19503 0.19893 -0.03332 -0.05201 0.10594  207 TRP   A NE1 
1585 C CE2 . TRP   A 207 ? 0.14585 0.20115 0.22271 -0.03360 -0.05494 0.11339  207 TRP   A CE2 
1586 C CE3 . TRP   A 207 ? 0.17064 0.22392 0.25243 -0.02463 -0.05107 0.12318  207 TRP   A CE3 
1587 C CZ2 . TRP   A 207 ? 0.18410 0.23394 0.28347 -0.04130 -0.06328 0.12331  207 TRP   A CZ2 
1588 C CZ3 . TRP   A 207 ? 0.17293 0.21712 0.27639 -0.02980 -0.05628 0.13197  207 TRP   A CZ3 
1589 C CH2 . TRP   A 207 ? 0.18700 0.22895 0.29876 -0.03852 -0.06328 0.13153  207 TRP   A CH2 
1590 N N   . LEU   A 208 ? 0.16261 0.27762 0.23199 -0.01755 -0.03830 0.14287  208 LEU   A N   
1591 C CA  . LEU   A 208 ? 0.19015 0.32024 0.27717 -0.01849 -0.03662 0.16101  208 LEU   A CA  
1592 C C   . LEU   A 208 ? 0.20151 0.35702 0.27956 -0.01728 -0.03208 0.16649  208 LEU   A C   
1593 O O   . LEU   A 208 ? 0.21743 0.38421 0.30500 -0.01831 -0.02974 0.17593  208 LEU   A O   
1594 C CB  . LEU   A 208 ? 0.20333 0.33463 0.30554 -0.01644 -0.03741 0.17444  208 LEU   A CB  
1595 C CG  . LEU   A 208 ? 0.20194 0.30612 0.31471 -0.01610 -0.04084 0.16998  208 LEU   A CG  
1596 C CD1 . LEU   A 208 ? 0.19693 0.30163 0.32533 -0.01194 -0.04003 0.18268  208 LEU   A CD1 
1597 C CD2 . LEU   A 208 ? 0.21108 0.30169 0.33799 -0.02025 -0.04300 0.17126  208 LEU   A CD2 
1598 N N   . TYR   A 209 ? 0.18450 0.34921 0.24374 -0.01504 -0.03104 0.16037  209 TYR   A N   
1599 C CA  . TYR   A 209 ? 0.18996 0.37556 0.23509 -0.01368 -0.02717 0.16165  209 TYR   A CA  
1600 C C   . TYR   A 209 ? 0.21542 0.39597 0.25513 -0.01308 -0.02418 0.15264  209 TYR   A C   
1601 O O   . TYR   A 209 ? 0.18238 0.37861 0.22093 -0.01176 -0.01987 0.15969  209 TYR   A O   
1602 C CB  . TYR   A 209 ? 0.19455 0.38686 0.21917 -0.01273 -0.02816 0.15350  209 TYR   A CB  
1603 C CG  . TYR   A 209 ? 0.20538 0.41567 0.23489 -0.01344 -0.03034 0.16794  209 TYR   A CG  
1604 C CD1 . TYR   A 209 ? 0.22356 0.45950 0.25552 -0.01387 -0.02855 0.18471  209 TYR   A CD1 
1605 C CD2 . TYR   A 209 ? 0.20877 0.41207 0.24151 -0.01345 -0.03410 0.16653  209 TYR   A CD2 
1606 C CE1 . TYR   A 209 ? 0.26255 0.51805 0.30094 -0.01483 -0.03110 0.20054  209 TYR   A CE1 
1607 C CE2 . TYR   A 209 ? 0.21855 0.44077 0.25917 -0.01393 -0.03625 0.18233  209 TYR   A CE2 
1608 C CZ  . TYR   A 209 ? 0.23659 0.48552 0.28036 -0.01487 -0.03504 0.19964  209 TYR   A CZ  
1609 O OH  . TYR   A 209 ? 0.26072 0.53151 0.31370 -0.01565 -0.03765 0.21759  209 TYR   A OH  
1610 N N   . ALA   A 210 ? 0.19574 0.35578 0.23190 -0.01354 -0.02608 0.13810  210 ALA   A N   
1611 C CA  . ALA   A 210 ? 0.19974 0.35599 0.23652 -0.01317 -0.02385 0.13278  210 ALA   A CA  
1612 C C   . ALA   A 210 ? 0.22336 0.38618 0.28202 -0.01592 -0.02349 0.14643  210 ALA   A C   
1613 O O   . ALA   A 210 ? 0.19594 0.37463 0.25998 -0.01463 -0.01923 0.15312  210 ALA   A O   
1614 C CB  . ALA   A 210 ? 0.17859 0.31277 0.21181 -0.01432 -0.02723 0.11833  210 ALA   A CB  
1615 N N   . ALA   A 211 ? 0.22729 0.38209 0.30253 -0.01986 -0.02791 0.15342  211 ALA   A N   
1616 C CA  . ALA   A 211 ? 0.21139 0.37397 0.31188 -0.02383 -0.02901 0.16829  211 ALA   A CA  
1617 C C   . ALA   A 211 ? 0.25173 0.44232 0.35900 -0.02115 -0.02351 0.18557  211 ALA   A C   
1618 O O   . ALA   A 211 ? 0.24408 0.45073 0.36748 -0.02194 -0.02137 0.19661  211 ALA   A O   
1619 C CB  . ALA   A 211 ? 0.23623 0.38327 0.35199 -0.02748 -0.03487 0.17271  211 ALA   A CB  
1620 N N   . VAL   A 212 ? 0.21887 0.41751 0.31455 -0.01794 -0.02155 0.18939  212 VAL   A N   
1621 C CA  . VAL   A 212 ? 0.24448 0.47077 0.34321 -0.01572 -0.01665 0.20651  212 VAL   A CA  
1622 C C   . VAL   A 212 ? 0.22285 0.46416 0.30518 -0.01195 -0.01046 0.20250  212 VAL   A C   
1623 O O   . VAL   A 212 ? 0.21181 0.47365 0.30270 -0.01027 -0.00532 0.21656  212 VAL   A O   
1624 C CB  . VAL   A 212 ? 0.21933 0.45325 0.30923 -0.01438 -0.01734 0.21278  212 VAL   A CB  
1625 C CG1 . VAL   A 212 ? 0.23525 0.49962 0.32463 -0.01276 -0.01245 0.23101  212 VAL   A CG1 
1626 C CG2 . VAL   A 212 ? 0.21428 0.43592 0.32609 -0.01657 -0.02190 0.22086  212 VAL   A CG2 
1627 N N   . ILE   A 213 ? 0.19411 0.42468 0.25300 -0.00993 -0.01013 0.18401  213 ILE   A N   
1628 C CA  . ILE   A 213 ? 0.21383 0.45637 0.25612 -0.00561 -0.00315 0.17970  213 ILE   A CA  
1629 C C   . ILE   A 213 ? 0.23609 0.48451 0.29984 -0.00443 -0.00007 0.18687  213 ILE   A C   
1630 O O   . ILE   A 213 ? 0.20379 0.46935 0.26404 0.00014  0.00851  0.19376  213 ILE   A O   
1631 C CB  . ILE   A 213 ? 0.20489 0.43176 0.22162 -0.00417 -0.00410 0.15868  213 ILE   A CB  
1632 C CG1 . ILE   A 213 ? 0.27156 0.49981 0.26711 -0.00551 -0.00655 0.15425  213 ILE   A CG1 
1633 C CG2 . ILE   A 213 ? 0.26489 0.49927 0.26801 0.00048  0.00429  0.15339  213 ILE   A CG2 
1634 C CD1 . ILE   A 213 ? 0.20381 0.41246 0.18068 -0.00560 -0.01012 0.13435  213 ILE   A CD1 
1635 N N   . ASN   A 214 ? 0.22845 0.46320 0.31470 -0.00917 -0.00650 0.18647  214 ASN   A N   
1636 C CA  . ASN   A 214 ? 0.26406 0.50535 0.37478 -0.01009 -0.00639 0.19382  214 ASN   A CA  
1637 C C   . ASN   A 214 ? 0.26027 0.51493 0.40096 -0.01339 -0.00813 0.21396  214 ASN   A C   
1638 O O   . ASN   A 214 ? 0.26923 0.53184 0.43372 -0.01462 -0.00966 0.22238  214 ASN   A O   
1639 C CB  . ASN   A 214 ? 0.20536 0.42405 0.32017 -0.01571 -0.01348 0.18048  214 ASN   A CB  
1640 C CG  . ASN   A 214 ? 0.23373 0.44560 0.32878 -0.01066 -0.01006 0.16600  214 ASN   A CG  
1641 O OD1 . ASN   A 214 ? 0.26180 0.48486 0.36798 -0.00743 -0.00644 0.17051  214 ASN   A OD1 
1642 N ND2 . ASN   A 214 ? 0.21862 0.41328 0.28732 -0.00917 -0.01127 0.15035  214 ASN   A ND2 
1643 N N   . GLY   A 215 ? 0.26409 0.52213 0.40668 -0.01473 -0.00864 0.22343  215 GLY   A N   
1644 C CA  . GLY   A 215 ? 0.24682 0.51798 0.41737 -0.01682 -0.00915 0.24421  215 GLY   A CA  
1645 C C   . GLY   A 215 ? 0.28895 0.54506 0.48006 -0.02395 -0.01757 0.24913  215 GLY   A C   
1646 O O   . GLY   A 215 ? 0.32249 0.58800 0.53647 -0.02539 -0.01770 0.26742  215 GLY   A O   
1647 N N   . ASP   A 216 ? 0.28574 0.51713 0.47013 -0.02804 -0.02404 0.23439  216 ASP   A N   
1648 C CA  . ASP   A 216 ? 0.34077 0.55534 0.54096 -0.03269 -0.03035 0.23912  216 ASP   A CA  
1649 C C   . ASP   A 216 ? 0.31640 0.53741 0.51071 -0.02849 -0.02604 0.24811  216 ASP   A C   
1650 O O   . ASP   A 216 ? 0.28667 0.50743 0.45572 -0.02467 -0.02347 0.23843  216 ASP   A O   
1651 C CB  . ASP   A 216 ? 0.34959 0.53541 0.54049 -0.03666 -0.03746 0.22073  216 ASP   A CB  
1652 C CG  . ASP   A 216 ? 0.39085 0.56643 0.59946 -0.04440 -0.04700 0.21890  216 ASP   A CG  
1653 O OD1 . ASP   A 216 ? 0.34676 0.51552 0.54371 -0.04693 -0.05032 0.20471  216 ASP   A OD1 
1654 O OD2 . ASP   A 216 ? 0.37258 0.54607 0.60620 -0.04827 -0.05164 0.23220  216 ASP   A OD2 
1655 N N   . ARG   A 217 ? 0.31613 0.54324 0.53505 -0.02948 -0.02593 0.26762  217 ARG   A N   
1656 C CA  . ARG   A 217 ? 0.30081 0.53468 0.51974 -0.02614 -0.02311 0.27910  217 ARG   A CA  
1657 C C   . ARG   A 217 ? 0.28016 0.49672 0.52687 -0.02854 -0.02660 0.28946  217 ARG   A C   
1658 O O   . ARG   A 217 ? 0.26779 0.49162 0.52203 -0.02549 -0.02411 0.30322  217 ARG   A O   
1659 C CB  . ARG   A 217 ? 0.30857 0.57442 0.52772 -0.02263 -0.01631 0.29776  217 ARG   A CB  
1660 C CG  . ARG   A 217 ? 0.30088 0.58338 0.48550 -0.01819 -0.01166 0.28963  217 ARG   A CG  
1661 C CD  . ARG   A 217 ? 0.27933 0.59325 0.46123 -0.01523 -0.00492 0.30890  217 ARG   A CD  
1662 N NE  . ARG   A 217 ? 0.29817 0.62496 0.47870 -0.01427 -0.00519 0.32260  217 ARG   A NE  
1663 C CZ  . ARG   A 217 ? 0.33097 0.66935 0.48238 -0.01268 -0.00475 0.31734  217 ARG   A CZ  
1664 N NH1 . ARG   A 217 ? 0.38191 0.71740 0.50232 -0.01161 -0.00319 0.29729  217 ARG   A NH1 
1665 N NH2 . ARG   A 217 ? 0.32519 0.67840 0.47971 -0.01252 -0.00624 0.33281  217 ARG   A NH2 
1666 N N   . TRP   A 218 ? 0.26048 0.45398 0.52294 -0.03392 -0.03240 0.28374  218 TRP   A N   
1667 C CA  . TRP   A 218 ? 0.27053 0.44707 0.56313 -0.03649 -0.03400 0.29598  218 TRP   A CA  
1668 C C   . TRP   A 218 ? 0.28670 0.44529 0.58013 -0.03290 -0.03325 0.29407  218 TRP   A C   
1669 O O   . TRP   A 218 ? 0.30063 0.45089 0.62070 -0.03241 -0.03104 0.30885  218 TRP   A O   
1670 C CB  . TRP   A 218 ? 0.27194 0.42482 0.57721 -0.04448 -0.04105 0.28808  218 TRP   A CB  
1671 C CG  . TRP   A 218 ? 0.31834 0.44501 0.60488 -0.04729 -0.04757 0.26441  218 TRP   A CG  
1672 C CD1 . TRP   A 218 ? 0.31436 0.44391 0.58333 -0.05004 -0.05263 0.24995  218 TRP   A CD1 
1673 C CD2 . TRP   A 218 ? 0.31230 0.40661 0.59772 -0.04738 -0.04899 0.25416  218 TRP   A CD2 
1674 N NE1 . TRP   A 218 ? 0.31246 0.41489 0.56790 -0.05237 -0.05813 0.23195  218 TRP   A NE1 
1675 C CE2 . TRP   A 218 ? 0.33319 0.41280 0.59740 -0.05062 -0.05548 0.23347  218 TRP   A CE2 
1676 C CE3 . TRP   A 218 ? 0.34126 0.41797 0.64311 -0.04444 -0.04444 0.26129  218 TRP   A CE3 
1677 C CZ2 . TRP   A 218 ? 0.34737 0.39495 0.60371 -0.05116 -0.05718 0.21902  218 TRP   A CZ2 
1678 C CZ3 . TRP   A 218 ? 0.31247 0.35653 0.60823 -0.04434 -0.04508 0.24635  218 TRP   A CZ3 
1679 C CH2 . TRP   A 218 ? 0.31616 0.34567 0.58813 -0.04778 -0.05116 0.22506  218 TRP   A CH2 
1680 N N   . PHE   A 219 ? 0.26826 0.42043 0.53549 -0.03004 -0.03429 0.27711  219 PHE   A N   
1681 C CA  . PHE   A 219 ? 0.26972 0.40338 0.53764 -0.02614 -0.03387 0.27343  219 PHE   A CA  
1682 C C   . PHE   A 219 ? 0.27630 0.43284 0.54133 -0.02004 -0.02952 0.28654  219 PHE   A C   
1683 O O   . PHE   A 219 ? 0.28348 0.42982 0.55410 -0.01595 -0.02860 0.28784  219 PHE   A O   
1684 C CB  . PHE   A 219 ? 0.25260 0.36696 0.49436 -0.02651 -0.03785 0.24864  219 PHE   A CB  
1685 C CG  . PHE   A 219 ? 0.26389 0.39561 0.47567 -0.02647 -0.03789 0.23671  219 PHE   A CG  
1686 C CD1 . PHE   A 219 ? 0.22996 0.37766 0.42145 -0.02170 -0.03461 0.23542  219 PHE   A CD1 
1687 C CD2 . PHE   A 219 ? 0.26637 0.39859 0.47233 -0.03140 -0.04094 0.22781  219 PHE   A CD2 
1688 C CE1 . PHE   A 219 ? 0.23258 0.39154 0.39674 -0.02138 -0.03334 0.22313  219 PHE   A CE1 
1689 C CE2 . PHE   A 219 ? 0.25670 0.40275 0.43804 -0.03033 -0.03883 0.21725  219 PHE   A CE2 
1690 C CZ  . PHE   A 219 ? 0.24566 0.40280 0.40531 -0.02507 -0.03451 0.21395  219 PHE   A CZ  
1691 N N   . LEU   A 220 ? 0.27625 0.46408 0.53242 -0.01938 -0.02690 0.29645  220 LEU   A N   
1692 C CA  . LEU   A 220 ? 0.28635 0.49823 0.53755 -0.01508 -0.02430 0.30949  220 LEU   A CA  
1693 C C   . LEU   A 220 ? 0.31117 0.52933 0.59856 -0.01292 -0.02158 0.33616  220 LEU   A C   
1694 O O   . LEU   A 220 ? 0.32208 0.52859 0.63698 -0.01498 -0.02063 0.34519  220 LEU   A O   
1695 C CB  . LEU   A 220 ? 0.28492 0.52720 0.51393 -0.01527 -0.02211 0.31174  220 LEU   A CB  
1696 C CG  . LEU   A 220 ? 0.27979 0.51724 0.47510 -0.01634 -0.02304 0.28699  220 LEU   A CG  
1697 C CD1 . LEU   A 220 ? 0.32029 0.58591 0.49903 -0.01580 -0.01914 0.29153  220 LEU   A CD1 
1698 C CD2 . LEU   A 220 ? 0.25587 0.48632 0.43154 -0.01475 -0.02559 0.27272  220 LEU   A CD2 
1699 N N   . ASN   A 221 ? 0.32252 0.55922 0.61153 -0.00903 -0.02045 0.34961  221 ASN   A N   
1700 C CA  . ASN   A 221 ? 0.34799 0.59551 0.67322 -0.00624 -0.01725 0.37813  221 ASN   A CA  
1701 C C   . ASN   A 221 ? 0.36066 0.64921 0.67879 -0.00453 -0.01686 0.39746  221 ASN   A C   
1702 O O   . ASN   A 221 ? 0.35134 0.65761 0.63704 -0.00585 -0.01913 0.38736  221 ASN   A O   
1703 C CB  . ASN   A 221 ? 0.37957 0.59998 0.72976 -0.00249 -0.01610 0.37864  221 ASN   A CB  
1704 C CG  . ASN   A 221 ? 0.38263 0.59842 0.71161 0.00027  -0.01849 0.36393  221 ASN   A CG  
1705 O OD1 . ASN   A 221 ? 0.38000 0.62604 0.70024 0.00143  -0.01965 0.37398  221 ASN   A OD1 
1706 N ND2 . ASN   A 221 ? 0.39066 0.57189 0.71545 0.00077  -0.01936 0.34297  221 ASN   A ND2 
1707 N N   . ARG   A 222 ? 0.38558 0.69057 0.73621 -0.00202 -0.01398 0.42686  222 ARG   A N   
1708 C CA  . ARG   A 222 ? 0.40297 0.75031 0.75225 -0.00084 -0.01449 0.45001  222 ARG   A CA  
1709 C C   . ARG   A 222 ? 0.42441 0.77580 0.77813 0.00208  -0.01665 0.45292  222 ARG   A C   
1710 O O   . ARG   A 222 ? 0.44107 0.82581 0.77925 0.00107  -0.01973 0.46189  222 ARG   A O   
1711 C CB  . ARG   A 222 ? 0.43115 0.79761 0.81585 0.00071  -0.01050 0.48349  222 ARG   A CB  
1712 C CG  . ARG   A 222 ? 0.45169 0.80976 0.88091 0.00566  -0.00762 0.50397  222 ARG   A CG  
1713 C CD  . ARG   A 222 ? 0.47649 0.84148 0.94671 0.00712  -0.00248 0.53354  222 ARG   A CD  
1714 N NE  . ARG   A 222 ? 0.51438 0.87530 1.02973 0.01278  0.00155  0.55606  222 ARG   A NE  
1715 C CZ  . ARG   A 222 ? 0.59359 0.98379 1.11968 0.01618  0.00071  0.57688  222 ARG   A CZ  
1716 N NH1 . ARG   A 222 ? 0.59175 1.01878 1.08494 0.01341  -0.00498 0.57819  222 ARG   A NH1 
1717 N NH2 . ARG   A 222 ? 0.57881 0.96226 1.15093 0.02212  0.00594  0.59762  222 ARG   A NH2 
1718 N N   . PHE   A 223 ? 0.44955 0.76748 0.82307 0.00537  -0.01511 0.44491  223 PHE   A N   
1719 C CA  . PHE   A 223 ? 0.43654 0.75752 0.82189 0.00937  -0.01559 0.45116  223 PHE   A CA  
1720 C C   . PHE   A 223 ? 0.40260 0.73356 0.74861 0.00670  -0.02108 0.43224  223 PHE   A C   
1721 O O   . PHE   A 223 ? 0.39291 0.71855 0.70327 0.00256  -0.02363 0.40916  223 PHE   A O   
1722 C CB  . PHE   A 223 ? 0.42713 0.70503 0.83710 0.01391  -0.01154 0.44137  223 PHE   A CB  
1723 C CG  . PHE   A 223 ? 0.47490 0.73704 0.92488 0.01618  -0.00550 0.45740  223 PHE   A CG  
1724 C CD1 . PHE   A 223 ? 0.50650 0.79054 0.99691 0.02053  -0.00117 0.49163  223 PHE   A CD1 
1725 C CD2 . PHE   A 223 ? 0.51617 0.74364 0.96742 0.01340  -0.00412 0.44051  223 PHE   A CD2 
1726 C CE1 . PHE   A 223 ? 0.55449 0.82365 1.08621 0.02262  0.00536  0.50781  223 PHE   A CE1 
1727 C CE2 . PHE   A 223 ? 0.56174 0.77466 1.05342 0.01437  0.00166  0.45614  223 PHE   A CE2 
1728 C CZ  . PHE   A 223 ? 0.58033 0.81288 1.11270 0.01927  0.00691  0.48940  223 PHE   A CZ  
1729 N N   . THR   A 224 ? 0.39534 0.74158 0.75062 0.00914  -0.02251 0.44354  224 THR   A N   
1730 C CA  . THR   A 224 ? 0.38449 0.73232 0.70820 0.00699  -0.02738 0.42419  224 THR   A CA  
1731 C C   . THR   A 224 ? 0.38362 0.71686 0.73099 0.01260  -0.02561 0.42717  224 THR   A C   
1732 O O   . THR   A 224 ? 0.39477 0.71292 0.78091 0.01834  -0.01979 0.44090  224 THR   A O   
1733 C CB  . THR   A 224 ? 0.39142 0.78426 0.69258 0.00197  -0.03277 0.43509  224 THR   A CB  
1734 O OG1 . THR   A 224 ? 0.37668 0.76656 0.64506 -0.00104 -0.03750 0.41240  224 THR   A OG1 
1735 C CG2 . THR   A 224 ? 0.41905 0.84693 0.75273 0.00400  -0.03316 0.47152  224 THR   A CG2 
1736 N N   . THR   A 225 ? 0.39123 0.72783 0.71709 0.01132  -0.02978 0.41434  225 THR   A N   
1737 C CA  . THR   A 225 ? 0.37313 0.69632 0.71986 0.01705  -0.02765 0.41604  225 THR   A CA  
1738 C C   . THR   A 225 ? 0.36975 0.71650 0.69322 0.01335  -0.03418 0.41254  225 THR   A C   
1739 O O   . THR   A 225 ? 0.36132 0.72045 0.64742 0.00663  -0.03956 0.39842  225 THR   A O   
1740 C CB  . THR   A 225 ? 0.35621 0.62991 0.70035 0.02078  -0.02383 0.38893  225 THR   A CB  
1741 O OG1 . THR   A 225 ? 0.35885 0.62051 0.72052 0.02691  -0.02101 0.38913  225 THR   A OG1 
1742 C CG2 . THR   A 225 ? 0.33124 0.59103 0.63034 0.01534  -0.02845 0.35736  225 THR   A CG2 
1743 N N   . THR   A 226 ? 0.41457 0.76868 0.76246 0.01770  -0.03325 0.42672  226 THR   A N   
1744 C CA  . THR   A 226 ? 0.37584 0.74735 0.70351 0.01412  -0.03963 0.42125  226 THR   A CA  
1745 C C   . THR   A 226 ? 0.35259 0.68646 0.65879 0.01586  -0.03915 0.38830  226 THR   A C   
1746 O O   . THR   A 226 ? 0.34038 0.63601 0.65134 0.02053  -0.03375 0.37249  226 THR   A O   
1747 C CB  . THR   A 226 ? 0.40013 0.79911 0.76433 0.01767  -0.03926 0.45244  226 THR   A CB  
1748 O OG1 . THR   A 226 ? 0.40003 0.76927 0.80220 0.02786  -0.02997 0.45621  226 THR   A OG1 
1749 C CG2 . THR   A 226 ? 0.42433 0.86779 0.80720 0.01474  -0.04138 0.48747  226 THR   A CG2 
1750 N N   . LEU   A 227 ? 0.35908 0.70543 0.64138 0.01152  -0.04533 0.37852  227 LEU   A N   
1751 C CA  . LEU   A 227 ? 0.38451 0.69957 0.64651 0.01296  -0.04539 0.34927  227 LEU   A CA  
1752 C C   . LEU   A 227 ? 0.35253 0.64551 0.64590 0.02242  -0.03905 0.35288  227 LEU   A C   
1753 O O   . LEU   A 227 ? 0.34895 0.60449 0.63661 0.02663  -0.03509 0.33089  227 LEU   A O   
1754 C CB  . LEU   A 227 ? 0.34329 0.67864 0.57569 0.00579  -0.05332 0.33989  227 LEU   A CB  
1755 C CG  . LEU   A 227 ? 0.34493 0.65089 0.55081 0.00573  -0.05411 0.30814  227 LEU   A CG  
1756 C CD1 . LEU   A 227 ? 0.33411 0.60718 0.52332 0.00651  -0.05057 0.28564  227 LEU   A CD1 
1757 C CD2 . LEU   A 227 ? 0.30155 0.62862 0.47719 -0.00285 -0.06177 0.29862  227 LEU   A CD2 
1758 N N   . ASN   A 228 ? 0.38136 0.69796 0.70860 0.02597  -0.03761 0.38081  228 ASN   A N   
1759 C CA  . ASN   A 228 ? 0.41083 0.70658 0.77397 0.03638  -0.02893 0.38662  228 ASN   A CA  
1760 C C   . ASN   A 228 ? 0.38432 0.64507 0.76510 0.04249  -0.01993 0.38095  228 ASN   A C   
1761 O O   . ASN   A 228 ? 0.38983 0.61338 0.77147 0.04828  -0.01408 0.36120  228 ASN   A O   
1762 C CB  . ASN   A 228 ? 0.44080 0.77107 0.84437 0.03948  -0.02751 0.42304  228 ASN   A CB  
1763 C CG  . ASN   A 228 ? 0.48608 0.84372 0.87887 0.03514  -0.03525 0.42701  228 ASN   A CG  
1764 O OD1 . ASN   A 228 ? 0.52335 0.92269 0.91235 0.02773  -0.04327 0.44638  228 ASN   A OD1 
1765 N ND2 . ASN   A 228 ? 0.50619 0.84143 0.89369 0.03927  -0.03318 0.40871  228 ASN   A ND2 
1766 N N   . ASP   A 229 ? 0.36526 0.63785 0.75971 0.04084  -0.01885 0.39789  229 ASP   A N   
1767 C CA  . ASP   A 229 ? 0.37750 0.61795 0.79287 0.04602  -0.01037 0.39489  229 ASP   A CA  
1768 C C   . ASP   A 229 ? 0.37383 0.57851 0.75356 0.04291  -0.01212 0.36044  229 ASP   A C   
1769 O O   . ASP   A 229 ? 0.35288 0.52029 0.74350 0.04775  -0.00524 0.34796  229 ASP   A O   
1770 C CB  . ASP   A 229 ? 0.39015 0.65407 0.82853 0.04438  -0.00941 0.42224  229 ASP   A CB  
1771 C CG  . ASP   A 229 ? 0.41813 0.70513 0.90721 0.05083  -0.00337 0.45830  229 ASP   A CG  
1772 O OD1 . ASP   A 229 ? 0.42329 0.70654 0.93107 0.05690  0.00089  0.46161  229 ASP   A OD1 
1773 O OD2 . ASP   A 229 ? 0.43636 0.74602 0.94894 0.05019  -0.00228 0.48467  229 ASP   A OD2 
1774 N N   . PHE   A 230 ? 0.36039 0.57512 0.69832 0.03475  -0.02070 0.34462  230 PHE   A N   
1775 C CA  . PHE   A 230 ? 0.37135 0.55345 0.67821 0.03229  -0.02216 0.31339  230 PHE   A CA  
1776 C C   . PHE   A 230 ? 0.33963 0.49431 0.64057 0.03733  -0.01995 0.29361  230 PHE   A C   
1777 O O   . PHE   A 230 ? 0.35713 0.47596 0.65668 0.04027  -0.01595 0.27642  230 PHE   A O   
1778 C CB  . PHE   A 230 ? 0.29396 0.49225 0.56084 0.02335  -0.02990 0.30107  230 PHE   A CB  
1779 C CG  . PHE   A 230 ? 0.31954 0.48748 0.55676 0.02099  -0.03140 0.27101  230 PHE   A CG  
1780 C CD1 . PHE   A 230 ? 0.27497 0.42108 0.51466 0.02024  -0.02922 0.26478  230 PHE   A CD1 
1781 C CD2 . PHE   A 230 ? 0.32432 0.48598 0.53371 0.01941  -0.03505 0.25041  230 PHE   A CD2 
1782 C CE1 . PHE   A 230 ? 0.31786 0.43873 0.53212 0.01758  -0.03121 0.23960  230 PHE   A CE1 
1783 C CE2 . PHE   A 230 ? 0.31495 0.45093 0.49997 0.01748  -0.03631 0.22546  230 PHE   A CE2 
1784 C CZ  . PHE   A 230 ? 0.28477 0.40116 0.47207 0.01646  -0.03463 0.22051  230 PHE   A CZ  
1785 N N   . ASN   A 231 ? 0.38107 0.55302 0.67952 0.03822  -0.02234 0.29682  231 ASN   A N   
1786 C CA  . ASN   A 231 ? 0.40116 0.55062 0.69358 0.04312  -0.02015 0.27887  231 ASN   A CA  
1787 C C   . ASN   A 231 ? 0.40276 0.52534 0.72978 0.05315  -0.00894 0.28216  231 ASN   A C   
1788 O O   . ASN   A 231 ? 0.41562 0.50777 0.73534 0.05698  -0.00489 0.26171  231 ASN   A O   
1789 C CB  . ASN   A 231 ? 0.34159 0.51875 0.62925 0.04161  -0.02489 0.28553  231 ASN   A CB  
1790 C CG  . ASN   A 231 ? 0.32375 0.51602 0.57115 0.03195  -0.03432 0.27211  231 ASN   A CG  
1791 O OD1 . ASN   A 231 ? 0.31555 0.48864 0.53529 0.02855  -0.03620 0.25000  231 ASN   A OD1 
1792 N ND2 . ASN   A 231 ? 0.30290 0.52978 0.54797 0.02725  -0.03987 0.28573  231 ASN   A ND2 
1793 N N   . LEU   A 232 ? 0.40319 0.53672 0.77001 0.05734  -0.00258 0.30824  232 LEU   A N   
1794 C CA  . LEU   A 232 ? 0.39301 0.50033 0.79946 0.06675  0.01112  0.31270  232 LEU   A CA  
1795 C C   . LEU   A 232 ? 0.44302 0.51165 0.84379 0.06588  0.01550  0.29349  232 LEU   A C   
1796 O O   . LEU   A 232 ? 0.44487 0.48095 0.86299 0.07202  0.02680  0.28289  232 LEU   A O   
1797 C CB  . LEU   A 232 ? 0.37906 0.50833 0.83220 0.07097  0.01732  0.34702  232 LEU   A CB  
1798 C CG  . LEU   A 232 ? 0.41128 0.56724 0.89159 0.07631  0.02006  0.36901  232 LEU   A CG  
1799 C CD1 . LEU   A 232 ? 0.41955 0.59612 0.95133 0.08103  0.02741  0.40544  232 LEU   A CD1 
1800 C CD2 . LEU   A 232 ? 0.39278 0.52328 0.88337 0.08440  0.03000  0.35451  232 LEU   A CD2 
1801 N N   . VAL   A 233 ? 0.41105 0.48246 0.78867 0.05788  0.00763  0.28884  233 VAL   A N   
1802 C CA  . VAL   A 233 ? 0.41634 0.45325 0.78728 0.05518  0.01003  0.27169  233 VAL   A CA  
1803 C C   . VAL   A 233 ? 0.44989 0.46720 0.78009 0.05148  0.00453  0.24195  233 VAL   A C   
1804 O O   . VAL   A 233 ? 0.44471 0.42624 0.77255 0.05150  0.00953  0.22410  233 VAL   A O   
1805 C CB  . VAL   A 233 ? 0.44129 0.49165 0.81083 0.04849  0.00503  0.28279  233 VAL   A CB  
1806 C CG1 . VAL   A 233 ? 0.40160 0.41777 0.76347 0.04399  0.00612  0.26549  233 VAL   A CG1 
1807 C CG2 . VAL   A 233 ? 0.38893 0.45817 0.80277 0.05275  0.01139  0.31429  233 VAL   A CG2 
1808 N N   . ALA   A 234 ? 0.43840 0.47802 0.73616 0.04760  -0.00528 0.23600  234 ALA   A N   
1809 C CA  . ALA   A 234 ? 0.46600 0.49034 0.72711 0.04443  -0.01049 0.21012  234 ALA   A CA  
1810 C C   . ALA   A 234 ? 0.48007 0.48126 0.74910 0.05147  -0.00287 0.19865  234 ALA   A C   
1811 O O   . ALA   A 234 ? 0.49375 0.46650 0.74640 0.05019  -0.00175 0.17803  234 ALA   A O   
1812 C CB  . ALA   A 234 ? 0.43688 0.48922 0.66602 0.03940  -0.02035 0.20657  234 ALA   A CB  
1813 N N   . MET   A 235 ? 0.45474 0.46905 0.74896 0.05853  0.00292  0.21231  235 MET   A N   
1814 C CA  . MET   A 235 ? 0.48021 0.47426 0.78695 0.06626  0.01304  0.20297  235 MET   A CA  
1815 C C   . MET   A 235 ? 0.47737 0.42952 0.79731 0.06837  0.02488  0.19009  235 MET   A C   
1816 O O   . MET   A 235 ? 0.48136 0.40630 0.78566 0.06878  0.02920  0.16786  235 MET   A O   
1817 C CB  . MET   A 235 ? 0.48894 0.50510 0.83098 0.07366  0.01959  0.22528  235 MET   A CB  
1818 C CG  . MET   A 235 ? 0.53781 0.53406 0.90265 0.08319  0.03427  0.21922  235 MET   A CG  
1819 S SD  . MET   A 235 ? 0.71741 0.74944 1.10353 0.08875  0.03491  0.23975  235 MET   A SD  
1820 C CE  . MET   A 235 ? 0.51383 0.58200 0.92448 0.08602  0.02949  0.27403  235 MET   A CE  
1821 N N   . LYS   A 236 ? 0.44977 0.39537 0.79650 0.06834  0.03033  0.20260  236 LYS   A N   
1822 C CA  . LYS   A 236 ? 0.47515 0.37847 0.83609 0.06883  0.04293  0.18931  236 LYS   A CA  
1823 C C   . LYS   A 236 ? 0.47419 0.35004 0.79750 0.05940  0.03700  0.16308  236 LYS   A C   
1824 O O   . LYS   A 236 ? 0.48122 0.31872 0.80223 0.05798  0.04708  0.14224  236 LYS   A O   
1825 C CB  . LYS   A 236 ? 0.50326 0.40728 0.89964 0.06919  0.04823  0.20914  236 LYS   A CB  
1826 C CG  . LYS   A 236 ? 0.52730 0.38559 0.93512 0.06658  0.06010  0.19342  236 LYS   A CG  
1827 C CD  . LYS   A 236 ? 0.62563 0.48378 1.07514 0.06819  0.06741  0.21472  236 LYS   A CD  
1828 C CE  . LYS   A 236 ? 0.69163 0.50883 1.13735 0.05913  0.07140  0.19717  236 LYS   A CE  
1829 N NZ  . LYS   A 236 ? 0.69814 0.47511 1.11540 0.05418  0.07664  0.16215  236 LYS   A NZ  
1830 N N   . TYR   A 237 ? 0.48276 0.37761 0.77583 0.05186  0.02163  0.16286  237 TYR   A N   
1831 C CA  . TYR   A 237 ? 0.44761 0.32098 0.70790 0.04200  0.01509  0.14195  237 TYR   A CA  
1832 C C   . TYR   A 237 ? 0.42956 0.30760 0.65568 0.04096  0.00796  0.12687  237 TYR   A C   
1833 O O   . TYR   A 237 ? 0.39847 0.27099 0.59635 0.03234  -0.00069 0.11502  237 TYR   A O   
1834 C CB  . TYR   A 237 ? 0.41974 0.30900 0.67381 0.03397  0.00497  0.15195  237 TYR   A CB  
1835 C CG  . TYR   A 237 ? 0.47562 0.35217 0.76110 0.03273  0.01210  0.16293  237 TYR   A CG  
1836 C CD1 . TYR   A 237 ? 0.50717 0.34601 0.79132 0.02450  0.01637  0.14728  237 TYR   A CD1 
1837 C CD2 . TYR   A 237 ? 0.44037 0.34223 0.75696 0.03842  0.01481  0.18872  237 TYR   A CD2 
1838 C CE1 . TYR   A 237 ? 0.52428 0.34985 0.83795 0.02258  0.02323  0.15655  237 TYR   A CE1 
1839 C CE2 . TYR   A 237 ? 0.49132 0.38157 0.83955 0.03775  0.02193  0.20015  237 TYR   A CE2 
1840 C CZ  . TYR   A 237 ? 0.52535 0.37652 0.87258 0.03015  0.02632  0.18369  237 TYR   A CZ  
1841 O OH  . TYR   A 237 ? 0.55855 0.39623 0.93814 0.02859  0.03377  0.19432  237 TYR   A OH  
1842 N N   . ASN   A 238 ? 0.43656 0.32596 0.66747 0.04926  0.01173  0.12849  238 ASN   A N   
1843 C CA  . ASN   A 238 ? 0.40542 0.29646 0.60837 0.04924  0.00716  0.11400  238 ASN   A CA  
1844 C C   . ASN   A 238 ? 0.36988 0.29073 0.54529 0.04366  -0.00829 0.11742  238 ASN   A C   
1845 O O   . ASN   A 238 ? 0.37985 0.29611 0.52740 0.03942  -0.01438 0.10345  238 ASN   A O   
1846 C CB  . ASN   A 238 ? 0.41897 0.27033 0.60358 0.04386  0.01238  0.08833  238 ASN   A CB  
1847 C CG  . ASN   A 238 ? 0.44027 0.29002 0.60590 0.04650  0.01310  0.07452  238 ASN   A CG  
1848 O OD1 . ASN   A 238 ? 0.37794 0.24261 0.55768 0.05572  0.01840  0.08106  238 ASN   A OD1 
1849 N ND2 . ASN   A 238 ? 0.43220 0.26612 0.56703 0.03741  0.00749  0.05652  238 ASN   A ND2 
1850 N N   . TYR   A 239 ? 0.36947 0.32031 0.55256 0.04292  -0.01325 0.13500  239 TYR   A N   
1851 C CA  . TYR   A 239 ? 0.33365 0.31283 0.49092 0.03741  -0.02415 0.13555  239 TYR   A CA  
1852 C C   . TYR   A 239 ? 0.34170 0.34492 0.49895 0.04108  -0.02542 0.14084  239 TYR   A C   
1853 O O   . TYR   A 239 ? 0.31817 0.32507 0.50258 0.04775  -0.01881 0.15235  239 TYR   A O   
1854 C CB  . TYR   A 239 ? 0.30511 0.30054 0.46795 0.03257  -0.02704 0.14881  239 TYR   A CB  
1855 C CG  . TYR   A 239 ? 0.31134 0.29393 0.46256 0.02536  -0.03032 0.14142  239 TYR   A CG  
1856 C CD1 . TYR   A 239 ? 0.33280 0.28245 0.48851 0.02387  -0.02699 0.13150  239 TYR   A CD1 
1857 C CD2 . TYR   A 239 ? 0.28854 0.29107 0.42486 0.01915  -0.03574 0.14350  239 TYR   A CD2 
1858 C CE1 . TYR   A 239 ? 0.34395 0.28348 0.49125 0.01535  -0.03113 0.12603  239 TYR   A CE1 
1859 C CE2 . TYR   A 239 ? 0.29560 0.28980 0.42580 0.01248  -0.03846 0.13881  239 TYR   A CE2 
1860 C CZ  . TYR   A 239 ? 0.32682 0.29109 0.46372 0.01022  -0.03730 0.13141  239 TYR   A CZ  
1861 O OH  . TYR   A 239 ? 0.31001 0.26801 0.44299 0.00183  -0.04147 0.12793  239 TYR   A OH  
1862 N N   . GLU   A 240 ? 0.33177 0.35053 0.46030 0.03626  -0.03294 0.13206  240 GLU   A N   
1863 C CA  . GLU   A 240 ? 0.32583 0.36530 0.45499 0.03783  -0.03448 0.13598  240 GLU   A CA  
1864 C C   . GLU   A 240 ? 0.30293 0.37154 0.44851 0.03499  -0.03564 0.15730  240 GLU   A C   
1865 O O   . GLU   A 240 ? 0.29938 0.37375 0.44503 0.03066  -0.03679 0.16384  240 GLU   A O   
1866 C CB  . GLU   A 240 ? 0.32376 0.37139 0.42480 0.03207  -0.04032 0.12198  240 GLU   A CB  
1867 C CG  . GLU   A 240 ? 0.30677 0.33262 0.38706 0.03230  -0.04089 0.10283  240 GLU   A CG  
1868 C CD  . GLU   A 240 ? 0.37945 0.41643 0.44076 0.02798  -0.04469 0.09257  240 GLU   A CD  
1869 O OE1 . GLU   A 240 ? 0.47025 0.52856 0.53728 0.02606  -0.04623 0.10046  240 GLU   A OE1 
1870 O OE2 . GLU   A 240 ? 0.37606 0.40374 0.41752 0.02448  -0.04613 0.07889  240 GLU   A OE2 
1871 N N   . PRO   A 241 ? 0.33667 0.42621 0.49631 0.03691  -0.03556 0.16968  241 PRO   A N   
1872 C CA  . PRO   A 241 ? 0.32902 0.45001 0.50045 0.03293  -0.03794 0.19106  241 PRO   A CA  
1873 C C   . PRO   A 241 ? 0.28195 0.41776 0.42513 0.02332  -0.04421 0.18426  241 PRO   A C   
1874 O O   . PRO   A 241 ? 0.29754 0.42670 0.41575 0.01988  -0.04706 0.16572  241 PRO   A O   
1875 C CB  . PRO   A 241 ? 0.25609 0.39568 0.44412 0.03602  -0.03777 0.20288  241 PRO   A CB  
1876 C CG  . PRO   A 241 ? 0.28596 0.39966 0.48530 0.04519  -0.03100 0.19334  241 PRO   A CG  
1877 C CD  . PRO   A 241 ? 0.27664 0.36367 0.44619 0.04320  -0.03260 0.16780  241 PRO   A CD  
1878 N N   . LEU   A 242 ? 0.27732 0.43237 0.42628 0.01954  -0.04509 0.19948  242 LEU   A N   
1879 C CA  . LEU   A 242 ? 0.26204 0.43575 0.38797 0.01119  -0.04943 0.19626  242 LEU   A CA  
1880 C C   . LEU   A 242 ? 0.29402 0.50135 0.42349 0.00761  -0.05362 0.21118  242 LEU   A C   
1881 O O   . LEU   A 242 ? 0.25008 0.47676 0.40495 0.00971  -0.05304 0.23496  242 LEU   A O   
1882 C CB  . LEU   A 242 ? 0.24151 0.41895 0.37071 0.00906  -0.04787 0.20438  242 LEU   A CB  
1883 C CG  . LEU   A 242 ? 0.22656 0.41658 0.33033 0.00186  -0.05024 0.19650  242 LEU   A CG  
1884 C CD1 . LEU   A 242 ? 0.25945 0.42274 0.34272 0.00118  -0.04927 0.17217  242 LEU   A CD1 
1885 C CD2 . LEU   A 242 ? 0.23045 0.43675 0.34453 0.00020  -0.04889 0.21353  242 LEU   A CD2 
1886 N N   . THR   A 243 ? 0.27592 0.49037 0.38209 0.00210  -0.05784 0.19814  243 THR   A N   
1887 C CA  . THR   A 243 ? 0.28276 0.52965 0.38936 -0.00303 -0.06330 0.21049  243 THR   A CA  
1888 C C   . THR   A 243 ? 0.32372 0.59490 0.41429 -0.01090 -0.06651 0.21467  243 THR   A C   
1889 O O   . THR   A 243 ? 0.31672 0.57722 0.39286 -0.01213 -0.06406 0.20404  243 THR   A O   
1890 C CB  . THR   A 243 ? 0.28830 0.53103 0.38061 -0.00536 -0.06650 0.19483  243 THR   A CB  
1891 O OG1 . THR   A 243 ? 0.26141 0.49027 0.32540 -0.00963 -0.06653 0.17179  243 THR   A OG1 
1892 C CG2 . THR   A 243 ? 0.28736 0.50756 0.39505 0.00301  -0.06286 0.19052  243 THR   A CG2 
1893 N N   . GLN   A 244 ? 0.26985 0.57585 0.36346 -0.01640 -0.07218 0.23110  244 GLN   A N   
1894 C CA  . GLN   A 244 ? 0.30028 0.63188 0.37456 -0.02485 -0.07602 0.23309  244 GLN   A CA  
1895 C C   . GLN   A 244 ? 0.30850 0.62622 0.35062 -0.02964 -0.07644 0.20542  244 GLN   A C   
1896 O O   . GLN   A 244 ? 0.33270 0.65610 0.35747 -0.03340 -0.07570 0.19983  244 GLN   A O   
1897 C CB  . GLN   A 244 ? 0.31080 0.68356 0.39060 -0.03162 -0.08367 0.25363  244 GLN   A CB  
1898 C CG  . GLN   A 244 ? 0.33197 0.73331 0.38798 -0.04162 -0.08850 0.25416  244 GLN   A CG  
1899 C CD  . GLN   A 244 ? 0.33955 0.75042 0.40139 -0.03991 -0.08499 0.26795  244 GLN   A CD  
1900 O OE1 . GLN   A 244 ? 0.34528 0.76620 0.43621 -0.03505 -0.08318 0.29252  244 GLN   A OE1 
1901 N NE2 . GLN   A 244 ? 0.34152 0.74975 0.37746 -0.04362 -0.08357 0.25309  244 GLN   A NE2 
1902 N N   . ASP   A 245 ? 0.26454 0.56416 0.30015 -0.02901 -0.07699 0.18877  245 ASP   A N   
1903 C CA  . ASP   A 245 ? 0.31410 0.59747 0.32369 -0.03242 -0.07619 0.16336  245 ASP   A CA  
1904 C C   . ASP   A 245 ? 0.33252 0.59006 0.33695 -0.02760 -0.06947 0.15198  245 ASP   A C   
1905 O O   . ASP   A 245 ? 0.31970 0.57513 0.30484 -0.03082 -0.06812 0.13954  245 ASP   A O   
1906 C CB  . ASP   A 245 ? 0.33728 0.60484 0.34596 -0.03147 -0.07729 0.15032  245 ASP   A CB  
1907 C CG  . ASP   A 245 ? 0.35742 0.61627 0.34172 -0.03693 -0.07793 0.12806  245 ASP   A CG  
1908 O OD1 . ASP   A 245 ? 0.38119 0.66257 0.35069 -0.04576 -0.08269 0.12764  245 ASP   A OD1 
1909 O OD2 . ASP   A 245 ? 0.39578 0.62603 0.37597 -0.03273 -0.07369 0.11157  245 ASP   A OD2 
1910 N N   . HIS   A 246 ? 0.33571 0.57387 0.35779 -0.02012 -0.06534 0.15629  246 HIS   A N   
1911 C CA  . HIS   A 246 ? 0.31188 0.52880 0.33156 -0.01668 -0.06010 0.14849  246 HIS   A CA  
1912 C C   . HIS   A 246 ? 0.31281 0.54884 0.32995 -0.01940 -0.05941 0.15912  246 HIS   A C   
1913 O O   . HIS   A 246 ? 0.27405 0.50284 0.27761 -0.02024 -0.05662 0.14846  246 HIS   A O   
1914 C CB  . HIS   A 246 ? 0.28347 0.48003 0.32338 -0.00970 -0.05710 0.15340  246 HIS   A CB  
1915 C CG  . HIS   A 246 ? 0.25310 0.42860 0.29319 -0.00622 -0.05692 0.14095  246 HIS   A CG  
1916 N ND1 . HIS   A 246 ? 0.26491 0.43013 0.32455 -0.00010 -0.05565 0.14790  246 HIS   A ND1 
1917 C CD2 . HIS   A 246 ? 0.26637 0.42986 0.29070 -0.00758 -0.05738 0.12268  246 HIS   A CD2 
1918 C CE1 . HIS   A 246 ? 0.25842 0.40719 0.31235 0.00208  -0.05559 0.13391  246 HIS   A CE1 
1919 N NE2 . HIS   A 246 ? 0.27428 0.42213 0.30745 -0.00263 -0.05677 0.11917  246 HIS   A NE2 
1920 N N   . VAL   A 247 ? 0.30459 0.56684 0.33611 -0.02050 -0.06177 0.18166  247 VAL   A N   
1921 C CA  . VAL   A 247 ? 0.28876 0.57386 0.31830 -0.02336 -0.06151 0.19445  247 VAL   A CA  
1922 C C   . VAL   A 247 ? 0.30796 0.60564 0.30860 -0.02996 -0.06336 0.18156  247 VAL   A C   
1923 O O   . VAL   A 247 ? 0.33961 0.63683 0.32927 -0.03030 -0.06011 0.17702  247 VAL   A O   
1924 C CB  . VAL   A 247 ? 0.29087 0.60639 0.34126 -0.02412 -0.06467 0.22273  247 VAL   A CB  
1925 C CG1 . VAL   A 247 ? 0.30019 0.64527 0.34546 -0.02822 -0.06535 0.23712  247 VAL   A CG1 
1926 C CG2 . VAL   A 247 ? 0.27160 0.57135 0.35312 -0.01649 -0.06107 0.23542  247 VAL   A CG2 
1927 N N   . ASP   A 248 ? 0.33264 0.64125 0.32082 -0.03544 -0.06846 0.17522  248 ASP   A N   
1928 C CA  . ASP   A 248 ? 0.32826 0.64776 0.28796 -0.04272 -0.07034 0.16163  248 ASP   A CA  
1929 C C   . ASP   A 248 ? 0.32813 0.61816 0.27373 -0.03975 -0.06469 0.13863  248 ASP   A C   
1930 O O   . ASP   A 248 ? 0.35180 0.64609 0.27992 -0.04184 -0.06216 0.13213  248 ASP   A O   
1931 C CB  . ASP   A 248 ? 0.33412 0.66748 0.28484 -0.05002 -0.07722 0.15767  248 ASP   A CB  
1932 C CG  . ASP   A 248 ? 0.36035 0.72985 0.32322 -0.05457 -0.08389 0.18255  248 ASP   A CG  
1933 O OD1 . ASP   A 248 ? 0.34647 0.73811 0.31320 -0.05541 -0.08392 0.19993  248 ASP   A OD1 
1934 O OD2 . ASP   A 248 ? 0.36361 0.74087 0.33327 -0.05730 -0.08916 0.18615  248 ASP   A OD2 
1935 N N   . ILE   A 249 ? 0.30234 0.56338 0.25546 -0.03471 -0.06246 0.12723  249 ILE   A N   
1936 C CA  . ILE   A 249 ? 0.32966 0.56403 0.27245 -0.03175 -0.05758 0.10772  249 ILE   A CA  
1937 C C   . ILE   A 249 ? 0.29415 0.52473 0.23910 -0.02817 -0.05250 0.11150  249 ILE   A C   
1938 O O   . ILE   A 249 ? 0.35135 0.57513 0.28162 -0.02814 -0.04901 0.09986  249 ILE   A O   
1939 C CB  . ILE   A 249 ? 0.33443 0.54158 0.28754 -0.02696 -0.05657 0.09904  249 ILE   A CB  
1940 C CG1 . ILE   A 249 ? 0.29520 0.50394 0.24047 -0.03110 -0.06057 0.08996  249 ILE   A CG1 
1941 C CG2 . ILE   A 249 ? 0.25377 0.43482 0.20378 -0.02261 -0.05141 0.08569  249 ILE   A CG2 
1942 C CD1 . ILE   A 249 ? 0.31877 0.51010 0.27708 -0.02685 -0.06080 0.08807  249 ILE   A CD1 
1943 N N   . LEU   A 250 ? 0.27811 0.51464 0.24200 -0.02540 -0.05192 0.12906  250 LEU   A N   
1944 C CA  . LEU   A 250 ? 0.28284 0.51958 0.25257 -0.02284 -0.04770 0.13643  250 LEU   A CA  
1945 C C   . LEU   A 250 ? 0.30967 0.57559 0.26854 -0.02662 -0.04789 0.14673  250 LEU   A C   
1946 O O   . LEU   A 250 ? 0.26166 0.53556 0.23030 -0.02484 -0.04517 0.16007  250 LEU   A O   
1947 C CB  . LEU   A 250 ? 0.23003 0.45994 0.22576 -0.01907 -0.04708 0.15113  250 LEU   A CB  
1948 C CG  . LEU   A 250 ? 0.22475 0.42356 0.23031 -0.01515 -0.04587 0.14161  250 LEU   A CG  
1949 C CD1 . LEU   A 250 ? 0.22512 0.42232 0.25494 -0.01250 -0.04650 0.15785  250 LEU   A CD1 
1950 C CD2 . LEU   A 250 ? 0.19031 0.36994 0.19235 -0.01359 -0.04206 0.13063  250 LEU   A CD2 
1951 N N   . GLY   A 251 ? 0.33658 0.61901 0.27466 -0.03249 -0.05108 0.14097  251 GLY   A N   
1952 C CA  . GLY   A 251 ? 0.30748 0.61828 0.22991 -0.03732 -0.05152 0.14914  251 GLY   A CA  
1953 C C   . GLY   A 251 ? 0.31157 0.61542 0.21870 -0.03534 -0.04473 0.14067  251 GLY   A C   
1954 O O   . GLY   A 251 ? 0.31987 0.63642 0.23166 -0.03380 -0.04168 0.15465  251 GLY   A O   
1955 N N   . PRO   A 252 ? 0.31474 0.59917 0.20358 -0.03532 -0.04171 0.11879  252 PRO   A N   
1956 C CA  . PRO   A 252 ? 0.32695 0.60236 0.20164 -0.03248 -0.03372 0.11082  252 PRO   A CA  
1957 C C   . PRO   A 252 ? 0.31711 0.58582 0.21398 -0.02592 -0.02969 0.12268  252 PRO   A C   
1958 O O   . PRO   A 252 ? 0.34435 0.62339 0.23482 -0.02503 -0.02425 0.12991  252 PRO   A O   
1959 C CB  . PRO   A 252 ? 0.34826 0.59724 0.21181 -0.03147 -0.03155 0.08795  252 PRO   A CB  
1960 C CG  . PRO   A 252 ? 0.37221 0.62696 0.22991 -0.03765 -0.03844 0.08202  252 PRO   A CG  
1961 C CD  . PRO   A 252 ? 0.35550 0.62687 0.23555 -0.03816 -0.04480 0.10160  252 PRO   A CD  
1962 N N   . LEU   A 253 ? 0.28810 0.54007 0.20997 -0.02214 -0.03177 0.12500  253 LEU   A N   
1963 C CA  . LEU   A 253 ? 0.29114 0.53609 0.23425 -0.01781 -0.02853 0.13508  253 LEU   A CA  
1964 C C   . LEU   A 253 ? 0.28686 0.55543 0.24246 -0.01876 -0.02890 0.15777  253 LEU   A C   
1965 O O   . LEU   A 253 ? 0.31378 0.58630 0.27730 -0.01670 -0.02452 0.16712  253 LEU   A O   
1966 C CB  . LEU   A 253 ? 0.23135 0.45321 0.19467 -0.01558 -0.03084 0.13177  253 LEU   A CB  
1967 C CG  . LEU   A 253 ? 0.25532 0.45303 0.21118 -0.01365 -0.02960 0.11256  253 LEU   A CG  
1968 C CD1 . LEU   A 253 ? 0.21853 0.39677 0.18917 -0.01287 -0.03276 0.10967  253 LEU   A CD1 
1969 C CD2 . LEU   A 253 ? 0.22302 0.41477 0.17938 -0.01077 -0.02420 0.11077  253 LEU   A CD2 
1970 N N   . SER   A 254 ? 0.27570 0.56118 0.23554 -0.02183 -0.03409 0.16859  254 SER   A N   
1971 C CA  . SER   A 254 ? 0.29589 0.60776 0.26751 -0.02298 -0.03486 0.19256  254 SER   A CA  
1972 C C   . SER   A 254 ? 0.33356 0.66703 0.28235 -0.02528 -0.03127 0.19573  254 SER   A C   
1973 O O   . SER   A 254 ? 0.32855 0.67250 0.28636 -0.02353 -0.02728 0.21066  254 SER   A O   
1974 C CB  . SER   A 254 ? 0.30297 0.63104 0.28127 -0.02617 -0.04141 0.20313  254 SER   A CB  
1975 O OG  . SER   A 254 ? 0.31845 0.67074 0.31520 -0.02643 -0.04245 0.22948  254 SER   A OG  
1976 N N   . ALA   A 255 ? 0.33923 0.67817 0.25695 -0.02973 -0.03195 0.18104  255 ALA   A N   
1977 C CA  . ALA   A 255 ? 0.37418 0.73285 0.26312 -0.03349 -0.02774 0.18163  255 ALA   A CA  
1978 C C   . ALA   A 255 ? 0.37262 0.71859 0.25539 -0.02885 -0.01751 0.17687  255 ALA   A C   
1979 O O   . ALA   A 255 ? 0.39884 0.76239 0.27005 -0.02979 -0.01168 0.18717  255 ALA   A O   
1980 C CB  . ALA   A 255 ? 0.39573 0.75630 0.25170 -0.04032 -0.02987 0.16243  255 ALA   A CB  
1981 N N   . GLN   A 256 ? 0.35054 0.66767 0.24128 -0.02404 -0.01468 0.16288  256 GLN   A N   
1982 C CA  . GLN   A 256 ? 0.35964 0.66570 0.24712 -0.01972 -0.00461 0.15958  256 GLN   A CA  
1983 C C   . GLN   A 256 ? 0.37802 0.69052 0.29570 -0.01622 -0.00328 0.18047  256 GLN   A C   
1984 O O   . GLN   A 256 ? 0.37863 0.69933 0.29618 -0.01407 0.00557  0.18658  256 GLN   A O   
1985 C CB  . GLN   A 256 ? 0.37197 0.64829 0.26003 -0.01631 -0.00294 0.14006  256 GLN   A CB  
1986 C CG  . GLN   A 256 ? 0.39195 0.66646 0.27996 -0.01228 0.00811  0.13842  256 GLN   A CG  
1987 C CD  . GLN   A 256 ? 0.39214 0.64348 0.29349 -0.00843 0.00710  0.12712  256 GLN   A CD  
1988 O OE1 . GLN   A 256 ? 0.46001 0.69373 0.35850 -0.00945 0.00055  0.11409  256 GLN   A OE1 
1989 N NE2 . GLN   A 256 ? 0.38794 0.64071 0.30533 -0.00406 0.01354  0.13353  256 GLN   A NE2 
1990 N N   . THR   A 257 ? 0.33756 0.65207 0.28447 -0.01610 -0.01066 0.19339  257 THR   A N   
1991 C CA  . THR   A 257 ? 0.31709 0.63375 0.29480 -0.01375 -0.00938 0.21168  257 THR   A CA  
1992 C C   . THR   A 257 ? 0.32731 0.67157 0.31549 -0.01559 -0.01087 0.23637  257 THR   A C   
1993 O O   . THR   A 257 ? 0.32822 0.67792 0.33862 -0.01402 -0.00804 0.25329  257 THR   A O   
1994 C CB  . THR   A 257 ? 0.32820 0.62202 0.33322 -0.01270 -0.01428 0.20854  257 THR   A CB  
1995 O OG1 . THR   A 257 ? 0.27203 0.56458 0.27667 -0.01467 -0.02068 0.20571  257 THR   A OG1 
1996 C CG2 . THR   A 257 ? 0.25220 0.52105 0.25307 -0.01064 -0.01220 0.18917  257 THR   A CG2 
1997 N N   . GLY   A 258 ? 0.34686 0.71007 0.32132 -0.01931 -0.01551 0.24019  258 GLY   A N   
1998 C CA  . GLY   A 258 ? 0.36925 0.76147 0.35588 -0.02112 -0.01764 0.26627  258 GLY   A CA  
1999 C C   . GLY   A 258 ? 0.35478 0.74352 0.37861 -0.01976 -0.02258 0.28176  258 GLY   A C   
2000 O O   . GLY   A 258 ? 0.37210 0.78309 0.41383 -0.02012 -0.02343 0.30686  258 GLY   A O   
2001 N N   . ILE   A 259 ? 0.32691 0.68772 0.36233 -0.01820 -0.02497 0.26806  259 ILE   A N   
2002 C CA  . ILE   A 259 ? 0.31611 0.66725 0.38326 -0.01690 -0.02813 0.27902  259 ILE   A CA  
2003 C C   . ILE   A 259 ? 0.31600 0.66910 0.37497 -0.01873 -0.03375 0.27284  259 ILE   A C   
2004 O O   . ILE   A 259 ? 0.30092 0.63533 0.34330 -0.01914 -0.03496 0.25029  259 ILE   A O   
2005 C CB  . ILE   A 259 ? 0.28985 0.60696 0.37399 -0.01470 -0.02632 0.26810  259 ILE   A CB  
2006 C CG1 . ILE   A 259 ? 0.29110 0.60900 0.38300 -0.01388 -0.02124 0.27415  259 ILE   A CG1 
2007 C CG2 . ILE   A 259 ? 0.28498 0.58877 0.39906 -0.01345 -0.02865 0.27810  259 ILE   A CG2 
2008 C CD1 . ILE   A 259 ? 0.26754 0.55628 0.36493 -0.01354 -0.02016 0.25818  259 ILE   A CD1 
2009 N N   . ALA   A 260 ? 0.33417 0.71139 0.40656 -0.01986 -0.03712 0.29445  260 ALA   A N   
2010 C CA  . ALA   A 260 ? 0.33527 0.71684 0.40638 -0.02157 -0.04258 0.29308  260 ALA   A CA  
2011 C C   . ALA   A 260 ? 0.32792 0.67427 0.41341 -0.01808 -0.04232 0.28032  260 ALA   A C   
2012 O O   . ALA   A 260 ? 0.31157 0.63678 0.41875 -0.01467 -0.03907 0.28291  260 ALA   A O   
2013 C CB  . ALA   A 260 ? 0.35924 0.77321 0.45094 -0.02249 -0.04563 0.32357  260 ALA   A CB  
2014 N N   . VAL   A 261 ? 0.30292 0.64292 0.37484 -0.01954 -0.04595 0.26597  261 VAL   A N   
2015 C CA  . VAL   A 261 ? 0.28086 0.58777 0.36105 -0.01630 -0.04558 0.25197  261 VAL   A CA  
2016 C C   . VAL   A 261 ? 0.28941 0.59053 0.40429 -0.01213 -0.04466 0.27068  261 VAL   A C   
2017 O O   . VAL   A 261 ? 0.26962 0.54089 0.39750 -0.00872 -0.04204 0.26375  261 VAL   A O   
2018 C CB  . VAL   A 261 ? 0.30982 0.61601 0.37143 -0.01869 -0.04975 0.23714  261 VAL   A CB  
2019 C CG1 . VAL   A 261 ? 0.25882 0.53417 0.33081 -0.01472 -0.04940 0.22640  261 VAL   A CG1 
2020 C CG2 . VAL   A 261 ? 0.27636 0.58170 0.30573 -0.02216 -0.04957 0.21615  261 VAL   A CG2 
2021 N N   . LEU   A 262 ? 0.30529 0.63531 0.43626 -0.01248 -0.04683 0.29512  262 LEU   A N   
2022 C CA  . LEU   A 262 ? 0.31994 0.64616 0.48822 -0.00754 -0.04478 0.31574  262 LEU   A CA  
2023 C C   . LEU   A 262 ? 0.31525 0.63020 0.50374 -0.00510 -0.03993 0.32451  262 LEU   A C   
2024 O O   . LEU   A 262 ? 0.31189 0.60699 0.52912 -0.00042 -0.03677 0.33141  262 LEU   A O   
2025 C CB  . LEU   A 262 ? 0.33478 0.69969 0.51854 -0.00868 -0.04794 0.34397  262 LEU   A CB  
2026 C CG  . LEU   A 262 ? 0.37065 0.74839 0.55041 -0.01024 -0.05297 0.34465  262 LEU   A CG  
2027 C CD1 . LEU   A 262 ? 0.32497 0.67057 0.52135 -0.00407 -0.05039 0.33600  262 LEU   A CD1 
2028 C CD2 . LEU   A 262 ? 0.39513 0.78486 0.53517 -0.01746 -0.05832 0.32568  262 LEU   A CD2 
2029 N N   . ASP   A 263 ? 0.31518 0.64274 0.49023 -0.00813 -0.03898 0.32485  263 ASP   A N   
2030 C CA  . ASP   A 263 ? 0.31862 0.63481 0.51201 -0.00658 -0.03468 0.33174  263 ASP   A CA  
2031 C C   . ASP   A 263 ? 0.29323 0.56968 0.48160 -0.00592 -0.03317 0.30766  263 ASP   A C   
2032 O O   . ASP   A 263 ? 0.29358 0.54877 0.50624 -0.00373 -0.03077 0.31171  263 ASP   A O   
2033 C CB  . ASP   A 263 ? 0.37256 0.71490 0.55269 -0.00957 -0.03368 0.33953  263 ASP   A CB  
2034 C CG  . ASP   A 263 ? 0.35474 0.73728 0.54541 -0.01037 -0.03519 0.36848  263 ASP   A CG  
2035 O OD1 . ASP   A 263 ? 0.36353 0.75280 0.57696 -0.00827 -0.03663 0.38422  263 ASP   A OD1 
2036 O OD2 . ASP   A 263 ? 0.36962 0.77783 0.54620 -0.01293 -0.03478 0.37635  263 ASP   A OD2 
2037 N N   . MET   A 264 ? 0.27639 0.54243 0.43415 -0.00808 -0.03474 0.28287  264 MET   A N   
2038 C CA  . MET   A 264 ? 0.26316 0.49394 0.41609 -0.00783 -0.03428 0.26133  264 MET   A CA  
2039 C C   . MET   A 264 ? 0.29415 0.50060 0.46312 -0.00428 -0.03491 0.25871  264 MET   A C   
2040 O O   . MET   A 264 ? 0.26651 0.44426 0.44326 -0.00361 -0.03428 0.24952  264 MET   A O   
2041 C CB  . MET   A 264 ? 0.26061 0.48659 0.38057 -0.01005 -0.03544 0.23748  264 MET   A CB  
2042 C CG  . MET   A 264 ? 0.26599 0.46159 0.38055 -0.01070 -0.03508 0.21802  264 MET   A CG  
2043 S SD  . MET   A 264 ? 0.22337 0.41776 0.35021 -0.01283 -0.03241 0.22428  264 MET   A SD  
2044 C CE  . MET   A 264 ? 0.22099 0.43526 0.32075 -0.01396 -0.02984 0.21622  264 MET   A CE  
2045 N N   . CYS   A 265 ? 0.27713 0.49549 0.45167 -0.00199 -0.03618 0.26727  265 CYS   A N   
2046 C CA  . CYS   A 265 ? 0.26269 0.45990 0.45551 0.00293  -0.03536 0.26703  265 CYS   A CA  
2047 C C   . CYS   A 265 ? 0.27772 0.46458 0.50592 0.00644  -0.03133 0.28383  265 CYS   A C   
2048 O O   . CYS   A 265 ? 0.27744 0.43296 0.51723 0.00983  -0.02922 0.27540  265 CYS   A O   
2049 C CB  . CYS   A 265 ? 0.27030 0.48780 0.46588 0.00461  -0.03721 0.27670  265 CYS   A CB  
2050 S SG  . CYS   A 265 ? 0.25454 0.47261 0.41396 0.00161  -0.04168 0.25336  265 CYS   A SG  
2051 N N   . ALA   A 266 ? 0.29423 0.50684 0.54025 0.00583  -0.02982 0.30784  266 ALA   A N   
2052 C CA  . ALA   A 266 ? 0.31100 0.51374 0.59262 0.00878  -0.02534 0.32464  266 ALA   A CA  
2053 C C   . ALA   A 266 ? 0.32982 0.50298 0.60801 0.00617  -0.02471 0.30937  266 ALA   A C   
2054 O O   . ALA   A 266 ? 0.36781 0.51466 0.67007 0.00867  -0.02122 0.31112  266 ALA   A O   
2055 C CB  . ALA   A 266 ? 0.32999 0.56925 0.62858 0.00799  -0.02430 0.35368  266 ALA   A CB  
2056 N N   . SER   A 267 ? 0.31091 0.48761 0.56053 0.00096  -0.02765 0.29451  267 SER   A N   
2057 C CA  . SER   A 267 ? 0.30346 0.45471 0.54923 -0.00245 -0.02818 0.28020  267 SER   A CA  
2058 C C   . SER   A 267 ? 0.31435 0.42933 0.55420 -0.00120 -0.02936 0.25939  267 SER   A C   
2059 O O   . SER   A 267 ? 0.30241 0.39264 0.56190 -0.00205 -0.02809 0.25857  267 SER   A O   
2060 C CB  . SER   A 267 ? 0.27998 0.44504 0.49833 -0.00731 -0.03019 0.26944  267 SER   A CB  
2061 O OG  . SER   A 267 ? 0.34946 0.54953 0.56785 -0.00781 -0.02860 0.28690  267 SER   A OG  
2062 N N   . LEU   A 268 ? 0.30167 0.41536 0.51781 0.00007  -0.03168 0.24418  268 LEU   A N   
2063 C CA  . LEU   A 268 ? 0.30854 0.39025 0.51736 0.00209  -0.03248 0.22533  268 LEU   A CA  
2064 C C   . LEU   A 268 ? 0.32739 0.39154 0.56886 0.00755  -0.02753 0.23556  268 LEU   A C   
2065 O O   . LEU   A 268 ? 0.33129 0.36423 0.58073 0.00721  -0.02596 0.22564  268 LEU   A O   
2066 C CB  . LEU   A 268 ? 0.29594 0.38428 0.47928 0.00330  -0.03503 0.21205  268 LEU   A CB  
2067 C CG  . LEU   A 268 ? 0.29855 0.35782 0.47128 0.00621  -0.03572 0.19296  268 LEU   A CG  
2068 C CD1 . LEU   A 268 ? 0.28508 0.32129 0.45015 0.00132  -0.03813 0.17867  268 LEU   A CD1 
2069 C CD2 . LEU   A 268 ? 0.26482 0.33590 0.41433 0.00652  -0.03831 0.18250  268 LEU   A CD2 
2070 N N   . LYS   A 269 ? 0.29992 0.38283 0.56146 0.01241  -0.02422 0.25526  269 LYS   A N   
2071 C CA  . LYS   A 269 ? 0.35215 0.41917 0.65073 0.01861  -0.01717 0.26710  269 LYS   A CA  
2072 C C   . LYS   A 269 ? 0.36072 0.40367 0.68310 0.01614  -0.01330 0.26984  269 LYS   A C   
2073 O O   . LYS   A 269 ? 0.35456 0.36254 0.68916 0.01779  -0.00824 0.25948  269 LYS   A O   
2074 C CB  . LYS   A 269 ? 0.35283 0.45041 0.67489 0.02304  -0.01446 0.29380  269 LYS   A CB  
2075 C CG  . LYS   A 269 ? 0.40743 0.49095 0.77379 0.03052  -0.00521 0.30889  269 LYS   A CG  
2076 C CD  . LYS   A 269 ? 0.39518 0.51345 0.79025 0.03409  -0.00282 0.34072  269 LYS   A CD  
2077 C CE  . LYS   A 269 ? 0.43206 0.57645 0.81737 0.03628  -0.00598 0.34569  269 LYS   A CE  
2078 N NZ  . LYS   A 269 ? 0.41625 0.59502 0.83664 0.03943  -0.00322 0.38036  269 LYS   A NZ  
2079 N N   . GLU   A 270 ? 0.36724 0.42710 0.69615 0.01156  -0.01486 0.28285  270 GLU   A N   
2080 C CA  . GLU   A 270 ? 0.39754 0.43428 0.75008 0.00804  -0.01155 0.28578  270 GLU   A CA  
2081 C C   . GLU   A 270 ? 0.37205 0.37867 0.70304 0.00110  -0.01545 0.26035  270 GLU   A C   
2082 O O   . GLU   A 270 ? 0.41588 0.38796 0.76209 -0.00197 -0.01137 0.25327  270 GLU   A O   
2083 C CB  . GLU   A 270 ? 0.38653 0.45086 0.75191 0.00477  -0.01235 0.30693  270 GLU   A CB  
2084 C CG  . GLU   A 270 ? 0.43097 0.52856 0.81605 0.01044  -0.00924 0.33390  270 GLU   A CG  
2085 C CD  . GLU   A 270 ? 0.51993 0.60236 0.94519 0.01791  -0.00062 0.34735  270 GLU   A CD  
2086 O OE1 . GLU   A 270 ? 0.56716 0.61454 1.01460 0.01745  0.00505  0.34239  270 GLU   A OE1 
2087 O OE2 . GLU   A 270 ? 0.48482 0.58946 0.91997 0.02379  0.00111  0.36225  270 GLU   A OE2 
2088 N N   . LEU   A 271 ? 0.32980 0.34770 0.62531 -0.00221 -0.02269 0.24568  271 LEU   A N   
2089 C CA  . LEU   A 271 ? 0.38599 0.37886 0.66181 -0.00899 -0.02719 0.22342  271 LEU   A CA  
2090 C C   . LEU   A 271 ? 0.41117 0.36767 0.68606 -0.00661 -0.02318 0.20716  271 LEU   A C   
2091 O O   . LEU   A 271 ? 0.39918 0.32311 0.67290 -0.01371 -0.02268 0.19273  271 LEU   A O   
2092 C CB  . LEU   A 271 ? 0.33697 0.35083 0.57831 -0.01144 -0.03424 0.21239  271 LEU   A CB  
2093 C CG  . LEU   A 271 ? 0.33788 0.37568 0.57413 -0.01728 -0.03782 0.21818  271 LEU   A CG  
2094 C CD1 . LEU   A 271 ? 0.23747 0.29069 0.44019 -0.01823 -0.04159 0.20414  271 LEU   A CD1 
2095 C CD2 . LEU   A 271 ? 0.36670 0.38579 0.61586 -0.02562 -0.04054 0.21596  271 LEU   A CD2 
2096 N N   . LEU   A 272 ? 0.37959 0.34130 0.65457 0.00221  -0.01964 0.20864  272 LEU   A N   
2097 C CA  . LEU   A 272 ? 0.45239 0.38148 0.72823 0.00585  -0.01373 0.19377  272 LEU   A CA  
2098 C C   . LEU   A 272 ? 0.47016 0.37104 0.78084 0.00744  -0.00269 0.19888  272 LEU   A C   
2099 O O   . LEU   A 272 ? 0.53205 0.39522 0.84184 0.00567  0.00380  0.18068  272 LEU   A O   
2100 C CB  . LEU   A 272 ? 0.37604 0.32241 0.64525 0.01494  -0.01288 0.19566  272 LEU   A CB  
2101 C CG  . LEU   A 272 ? 0.38107 0.34698 0.61375 0.01345  -0.02159 0.18490  272 LEU   A CG  
2102 C CD1 . LEU   A 272 ? 0.38844 0.37066 0.62036 0.02129  -0.01992 0.18908  272 LEU   A CD1 
2103 C CD2 . LEU   A 272 ? 0.38151 0.32160 0.58996 0.00813  -0.02497 0.16169  272 LEU   A CD2 
2104 N N   . GLN   A 273 ? 0.45413 0.37204 0.79533 0.01019  0.00068  0.22252  273 GLN   A N   
2105 C CA  . GLN   A 273 ? 0.46603 0.35884 0.84524 0.01293  0.01264  0.22963  273 GLN   A CA  
2106 C C   . GLN   A 273 ? 0.51956 0.38259 0.90491 0.00161  0.01389  0.22155  273 GLN   A C   
2107 O O   . GLN   A 273 ? 0.56779 0.39390 0.97270 0.00008  0.02446  0.21345  273 GLN   A O   
2108 C CB  . GLN   A 273 ? 0.45977 0.38481 0.87287 0.02069  0.01623  0.26103  273 GLN   A CB  
2109 C CG  . GLN   A 273 ? 0.46109 0.40573 0.88146 0.03131  0.01948  0.27006  273 GLN   A CG  
2110 C CD  . GLN   A 273 ? 0.45800 0.44253 0.90539 0.03609  0.02003  0.30257  273 GLN   A CD  
2111 O OE1 . GLN   A 273 ? 0.48056 0.47813 0.94179 0.03245  0.01871  0.31875  273 GLN   A OE1 
2112 N NE2 . GLN   A 273 ? 0.42006 0.42557 0.87532 0.04353  0.02191  0.31323  273 GLN   A NE2 
2113 N N   . ASN   A 274 ? 0.50295 0.38129 0.87300 -0.00720 0.00407  0.22303  274 ASN   A N   
2114 C CA  . ASN   A 274 ? 0.51898 0.37508 0.89802 -0.01939 0.00425  0.21902  274 ASN   A CA  
2115 C C   . ASN   A 274 ? 0.51967 0.36168 0.86531 -0.03261 -0.00424 0.19558  274 ASN   A C   
2116 O O   . ASN   A 274 ? 0.47798 0.30269 0.82831 -0.04560 -0.00535 0.19028  274 ASN   A O   
2117 C CB  . ASN   A 274 ? 0.53031 0.41869 0.93073 -0.01952 0.00156  0.24592  274 ASN   A CB  
2118 C CG  . ASN   A 274 ? 0.54321 0.45647 0.97382 -0.00718 0.00790  0.27261  274 ASN   A CG  
2119 O OD1 . ASN   A 274 ? 0.55748 0.51248 0.98722 -0.00371 0.00326  0.29177  274 ASN   A OD1 
2120 N ND2 . ASN   A 274 ? 0.55252 0.44096 1.01014 -0.00122 0.01930  0.27367  274 ASN   A ND2 
2121 N N   . GLY   A 275 ? 0.54759 0.39750 0.86145 -0.03066 -0.01027 0.18213  275 GLY   A N   
2122 C CA  . GLY   A 275 ? 0.51868 0.36306 0.80390 -0.04288 -0.01929 0.16397  275 GLY   A CA  
2123 C C   . GLY   A 275 ? 0.53385 0.41290 0.81992 -0.04653 -0.02844 0.17864  275 GLY   A C   
2124 O O   . GLY   A 275 ? 0.50760 0.41458 0.81189 -0.03994 -0.02737 0.20105  275 GLY   A O   
2125 N N   . MET   A 276 ? 0.55088 0.42962 0.81745 -0.05770 -0.03715 0.16569  276 MET   A N   
2126 C CA  . MET   A 276 ? 0.51558 0.42750 0.78382 -0.06083 -0.04534 0.17843  276 MET   A CA  
2127 C C   . MET   A 276 ? 0.52702 0.42909 0.81643 -0.07317 -0.04536 0.18340  276 MET   A C   
2128 O O   . MET   A 276 ? 0.54211 0.47238 0.83961 -0.07478 -0.05028 0.19758  276 MET   A O   
2129 C CB  . MET   A 276 ? 0.51302 0.43832 0.75288 -0.06434 -0.05567 0.16601  276 MET   A CB  
2130 C CG  . MET   A 276 ? 0.44608 0.40117 0.66988 -0.05191 -0.05681 0.17065  276 MET   A CG  
2131 S SD  . MET   A 276 ? 0.56815 0.52572 0.75788 -0.05331 -0.06545 0.15150  276 MET   A SD  
2132 C CE  . MET   A 276 ? 0.32876 0.30360 0.51917 -0.06447 -0.07609 0.15373  276 MET   A CE  
2133 N N   . ASN   A 277 ? 0.59704 0.45973 0.89558 -0.08234 -0.03887 0.17135  277 ASN   A N   
2134 C CA  . ASN   A 277 ? 0.60118 0.44997 0.92226 -0.09548 -0.03703 0.17511  277 ASN   A CA  
2135 C C   . ASN   A 277 ? 0.59834 0.46083 0.91100 -0.10984 -0.04807 0.17008  277 ASN   A C   
2136 O O   . ASN   A 277 ? 0.53715 0.41540 0.87020 -0.11470 -0.05034 0.18548  277 ASN   A O   
2137 C CB  . ASN   A 277 ? 0.65616 0.52376 1.01014 -0.08618 -0.03162 0.20377  277 ASN   A CB  
2138 C CG  . ASN   A 277 ? 0.72778 0.56722 1.10979 -0.09740 -0.02492 0.20588  277 ASN   A CG  
2139 O OD1 . ASN   A 277 ? 0.77693 0.59145 1.15308 -0.11564 -0.02700 0.18775  277 ASN   A OD1 
2140 N ND2 . ASN   A 277 ? 0.79777 0.64227 1.21071 -0.08779 -0.01683 0.22787  277 ASN   A ND2 
2141 N N   . GLY   A 278 ? 0.60462 0.46362 0.88884 -0.11633 -0.05505 0.14964  278 GLY   A N   
2142 C CA  . GLY   A 278 ? 0.54387 0.41741 0.82140 -0.13019 -0.06629 0.14438  278 GLY   A CA  
2143 C C   . GLY   A 278 ? 0.51873 0.43664 0.79796 -0.12107 -0.07495 0.16406  278 GLY   A C   
2144 O O   . GLY   A 278 ? 0.49746 0.43140 0.77980 -0.13067 -0.08345 0.16643  278 GLY   A O   
2145 N N   . ARG   A 279 ? 0.48628 0.42568 0.76353 -0.10348 -0.07219 0.17771  279 ARG   A N   
2146 C CA  . ARG   A 279 ? 0.40808 0.38769 0.68017 -0.09555 -0.07824 0.19056  279 ARG   A CA  
2147 C C   . ARG   A 279 ? 0.37796 0.36356 0.62101 -0.08944 -0.08300 0.17819  279 ARG   A C   
2148 O O   . ARG   A 279 ? 0.37473 0.33641 0.60254 -0.08866 -0.08095 0.16268  279 ARG   A O   
2149 C CB  . ARG   A 279 ? 0.43011 0.43634 0.71741 -0.08280 -0.07092 0.21249  279 ARG   A CB  
2150 C CG  . ARG   A 279 ? 0.43333 0.43772 0.75116 -0.08553 -0.06499 0.22925  279 ARG   A CG  
2151 C CD  . ARG   A 279 ? 0.42868 0.47448 0.75363 -0.07583 -0.06200 0.24996  279 ARG   A CD  
2152 N NE  . ARG   A 279 ? 0.46743 0.51905 0.81914 -0.07275 -0.05411 0.27037  279 ARG   A NE  
2153 C CZ  . ARG   A 279 ? 0.42621 0.51252 0.78787 -0.06761 -0.05060 0.28988  279 ARG   A CZ  
2154 N NH1 . ARG   A 279 ? 0.37661 0.49180 0.72363 -0.06499 -0.05292 0.28945  279 ARG   A NH1 
2155 N NH2 . ARG   A 279 ? 0.44948 0.54131 0.83599 -0.06510 -0.04376 0.30978  279 ARG   A NH2 
2156 N N   . THR   A 280 ? 0.39108 0.40951 0.62801 -0.08473 -0.08790 0.18558  280 THR   A N   
2157 C CA  . THR   A 280 ? 0.32587 0.35410 0.53797 -0.07955 -0.09220 0.17555  280 THR   A CA  
2158 C C   . THR   A 280 ? 0.27024 0.33005 0.48072 -0.06811 -0.08442 0.18390  280 THR   A C   
2159 O O   . THR   A 280 ? 0.27705 0.35639 0.50363 -0.06491 -0.07802 0.19900  280 THR   A O   
2160 C CB  . THR   A 280 ? 0.29366 0.32939 0.49707 -0.08722 -0.10357 0.17176  280 THR   A CB  
2161 O OG1 . THR   A 280 ? 0.28670 0.35030 0.50842 -0.08685 -0.10398 0.18858  280 THR   A OG1 
2162 C CG2 . THR   A 280 ? 0.28085 0.28652 0.48037 -0.10205 -0.10855 0.15789  280 THR   A CG2 
2163 N N   . ILE   A 281 ? 0.24433 0.30700 0.43285 -0.06338 -0.08284 0.17183  281 ILE   A N   
2164 C CA  . ILE   A 281 ? 0.20607 0.29228 0.38404 -0.05581 -0.07196 0.17246  281 ILE   A CA  
2165 C C   . ILE   A 281 ? 0.19976 0.29218 0.35976 -0.05762 -0.07241 0.15974  281 ILE   A C   
2166 O O   . ILE   A 281 ? 0.18429 0.25905 0.32849 -0.05957 -0.07708 0.14590  281 ILE   A O   
2167 C CB  . ILE   A 281 ? 0.20843 0.28567 0.37390 -0.04753 -0.06425 0.16893  281 ILE   A CB  
2168 C CG1 . ILE   A 281 ? 0.21256 0.28592 0.39989 -0.04543 -0.06117 0.18430  281 ILE   A CG1 
2169 C CG2 . ILE   A 281 ? 0.20938 0.30431 0.35463 -0.04086 -0.05489 0.16510  281 ILE   A CG2 
2170 C CD1 . ILE   A 281 ? 0.25663 0.32147 0.43694 -0.03773 -0.05561 0.18310  281 ILE   A CD1 
2171 N N   . LEU   A 282 ? 0.21567 0.33131 0.37838 -0.05645 -0.06598 0.16504  282 LEU   A N   
2172 C CA  . LEU   A 282 ? 0.21618 0.33429 0.36338 -0.05668 -0.06223 0.15470  282 LEU   A CA  
2173 C C   . LEU   A 282 ? 0.18318 0.27959 0.32208 -0.06311 -0.07205 0.14525  282 LEU   A C   
2174 O O   . LEU   A 282 ? 0.15992 0.24342 0.27878 -0.06264 -0.07052 0.13207  282 LEU   A O   
2175 C CB  . LEU   A 282 ? 0.17510 0.28345 0.29088 -0.04639 -0.05282 0.13973  282 LEU   A CB  
2176 C CG  . LEU   A 282 ? 0.19090 0.31596 0.30082 -0.03768 -0.04313 0.14550  282 LEU   A CG  
2177 C CD1 . LEU   A 282 ? 0.20084 0.31605 0.28235 -0.02959 -0.03840 0.13065  282 LEU   A CD1 
2178 C CD2 . LEU   A 282 ? 0.19797 0.34835 0.31973 -0.03669 -0.03794 0.15625  282 LEU   A CD2 
2179 N N   . GLY   A 283 ? 0.21849 0.31160 0.37317 -0.06884 -0.08351 0.15368  283 GLY   A N   
2180 C CA  . GLY   A 283 ? 0.21430 0.29044 0.35944 -0.07454 -0.09617 0.14850  283 GLY   A CA  
2181 C C   . GLY   A 283 ? 0.28514 0.33357 0.41457 -0.07697 -0.10615 0.13976  283 GLY   A C   
2182 O O   . GLY   A 283 ? 0.30780 0.33743 0.42178 -0.08378 -0.11555 0.13771  283 GLY   A O   
2183 N N   . SER   A 284 ? 0.28171 0.32679 0.41647 -0.07438 -0.10366 0.13694  284 SER   A N   
2184 C CA  . SER   A 284 ? 0.27043 0.28999 0.39375 -0.07583 -0.11202 0.12812  284 SER   A CA  
2185 C C   . SER   A 284 ? 0.29049 0.28706 0.42794 -0.07765 -0.10525 0.12965  284 SER   A C   
2186 O O   . SER   A 284 ? 0.29641 0.30464 0.45252 -0.07250 -0.09728 0.14161  284 SER   A O   
2187 C CB  . SER   A 284 ? 0.26920 0.28980 0.37850 -0.06934 -0.10067 0.11627  284 SER   A CB  
2188 O OG  . SER   A 284 ? 0.28479 0.27777 0.38242 -0.06701 -0.10333 0.10780  284 SER   A OG  
2189 N N   . ALA   A 285 ? 0.29951 0.26485 0.42898 -0.08639 -0.10576 0.11507  285 ALA   A N   
2190 C CA  . ALA   A 285 ? 0.29384 0.23391 0.43891 -0.08926 -0.09617 0.11190  285 ALA   A CA  
2191 C C   . ALA   A 285 ? 0.33163 0.25247 0.46978 -0.08039 -0.08710 0.10397  285 ALA   A C   
2192 O O   . ALA   A 285 ? 0.33610 0.23258 0.48685 -0.08112 -0.07708 0.10089  285 ALA   A O   
2193 C CB  . ALA   A 285 ? 0.32106 0.23930 0.46543 -0.10649 -0.09762 0.09634  285 ALA   A CB  
2194 N N   . LEU   A 286 ? 0.29809 0.22916 0.41800 -0.07192 -0.08952 0.10119  286 LEU   A N   
2195 C CA  . LEU   A 286 ? 0.32469 0.24435 0.43994 -0.06137 -0.08099 0.09718  286 LEU   A CA  
2196 C C   . LEU   A 286 ? 0.27819 0.22939 0.39187 -0.04916 -0.07887 0.10870  286 LEU   A C   
2197 O O   . LEU   A 286 ? 0.24755 0.22463 0.35515 -0.05030 -0.08315 0.11144  286 LEU   A O   
2198 C CB  . LEU   A 286 ? 0.36514 0.26597 0.45588 -0.06462 -0.08316 0.07705  286 LEU   A CB  
2199 C CG  . LEU   A 286 ? 0.37002 0.24255 0.45400 -0.07880 -0.08069 0.05624  286 LEU   A CG  
2200 C CD1 . LEU   A 286 ? 0.37840 0.24254 0.43431 -0.08073 -0.08171 0.03627  286 LEU   A CD1 
2201 C CD2 . LEU   A 286 ? 0.36838 0.21220 0.47174 -0.07945 -0.06620 0.05338  286 LEU   A CD2 
2202 N N   . LEU   A 287 ? 0.25926 0.20868 0.37783 -0.03872 -0.06938 0.11262  287 LEU   A N   
2203 C CA  . LEU   A 287 ? 0.23717 0.21438 0.34705 -0.02987 -0.06483 0.11711  287 LEU   A CA  
2204 C C   . LEU   A 287 ? 0.21501 0.19497 0.29939 -0.02835 -0.06697 0.10266  287 LEU   A C   
2205 O O   . LEU   A 287 ? 0.30818 0.26916 0.38533 -0.02680 -0.06823 0.09397  287 LEU   A O   
2206 C CB  . LEU   A 287 ? 0.21667 0.19323 0.33845 -0.02056 -0.05626 0.12622  287 LEU   A CB  
2207 C CG  . LEU   A 287 ? 0.24823 0.22459 0.39740 -0.02146 -0.05262 0.14224  287 LEU   A CG  
2208 C CD1 . LEU   A 287 ? 0.29653 0.26774 0.46187 -0.01282 -0.04482 0.15127  287 LEU   A CD1 
2209 C CD2 . LEU   A 287 ? 0.21619 0.22262 0.36809 -0.02352 -0.05301 0.15358  287 LEU   A CD2 
2210 N N   . GLU   A 288 ? 0.19438 0.19482 0.26546 -0.02822 -0.06457 0.09903  288 GLU   A N   
2211 C CA  . GLU   A 288 ? 0.22199 0.22279 0.27106 -0.02760 -0.06377 0.08416  288 GLU   A CA  
2212 C C   . GLU   A 288 ? 0.20839 0.21694 0.24505 -0.01836 -0.05612 0.07953  288 GLU   A C   
2213 O O   . GLU   A 288 ? 0.16850 0.19259 0.20943 -0.01630 -0.05253 0.08795  288 GLU   A O   
2214 C CB  . GLU   A 288 ? 0.21416 0.22662 0.26023 -0.03218 -0.06282 0.08262  288 GLU   A CB  
2215 C CG  . GLU   A 288 ? 0.25958 0.27443 0.28947 -0.03017 -0.05877 0.07150  288 GLU   A CG  
2216 C CD  . GLU   A 288 ? 0.31771 0.31693 0.33808 -0.03404 -0.06331 0.06144  288 GLU   A CD  
2217 O OE1 . GLU   A 288 ? 0.36230 0.35456 0.38800 -0.04420 -0.07176 0.06493  288 GLU   A OE1 
2218 O OE2 . GLU   A 288 ? 0.19954 0.19387 0.20853 -0.03003 -0.06064 0.05304  288 GLU   A OE2 
2219 N N   . ASP   A 289 ? 0.20464 0.20485 0.22957 -0.01573 -0.05615 0.06906  289 ASP   A N   
2220 C CA  . ASP   A 289 ? 0.18845 0.19665 0.20757 -0.00999 -0.05232 0.06769  289 ASP   A CA  
2221 C C   . ASP   A 289 ? 0.19210 0.20259 0.19755 -0.01029 -0.05028 0.05657  289 ASP   A C   
2222 O O   . ASP   A 289 ? 0.15263 0.16672 0.15311 -0.00622 -0.04830 0.05376  289 ASP   A O   
2223 C CB  . ASP   A 289 ? 0.20878 0.20683 0.23198 -0.00375 -0.05212 0.06929  289 ASP   A CB  
2224 C CG  . ASP   A 289 ? 0.23749 0.21940 0.25210 -0.00357 -0.05412 0.05878  289 ASP   A CG  
2225 O OD1 . ASP   A 289 ? 0.20666 0.18372 0.21306 -0.01026 -0.05781 0.05097  289 ASP   A OD1 
2226 O OD2 . ASP   A 289 ? 0.24568 0.21914 0.26538 0.00134  -0.05384 0.06094  289 ASP   A OD2 
2227 N N   . GLU   A 290 ? 0.14844 0.15709 0.14991 -0.01476 -0.05052 0.05158  290 GLU   A N   
2228 C CA  . GLU   A 290 ? 0.17626 0.18599 0.16835 -0.01349 -0.04729 0.04325  290 GLU   A CA  
2229 C C   . GLU   A 290 ? 0.18514 0.20720 0.17601 -0.01251 -0.04388 0.04501  290 GLU   A C   
2230 O O   . GLU   A 290 ? 0.17034 0.19204 0.15686 -0.01195 -0.04197 0.03982  290 GLU   A O   
2231 C CB  . GLU   A 290 ? 0.21236 0.21031 0.20051 -0.01749 -0.04931 0.03700  290 GLU   A CB  
2232 C CG  . GLU   A 290 ? 0.20556 0.19025 0.19084 -0.01769 -0.05288 0.03367  290 GLU   A CG  
2233 C CD  . GLU   A 290 ? 0.22209 0.19777 0.19794 -0.01842 -0.05233 0.02599  290 GLU   A CD  
2234 O OE1 . GLU   A 290 ? 0.23589 0.20305 0.20681 -0.01666 -0.05382 0.02231  290 GLU   A OE1 
2235 O OE2 . GLU   A 290 ? 0.21338 0.19175 0.18736 -0.01991 -0.05031 0.02476  290 GLU   A OE2 
2236 N N   . PHE   A 291 ? 0.14364 0.17718 0.13852 -0.01182 -0.04308 0.05314  291 PHE   A N   
2237 C CA  . PHE   A 291 ? 0.14583 0.19245 0.13633 -0.00999 -0.03984 0.05444  291 PHE   A CA  
2238 C C   . PHE   A 291 ? 0.17847 0.23424 0.16531 -0.00796 -0.03952 0.05706  291 PHE   A C   
2239 O O   . PHE   A 291 ? 0.15166 0.21329 0.14570 -0.00848 -0.04077 0.06637  291 PHE   A O   
2240 C CB  . PHE   A 291 ? 0.16068 0.21795 0.15893 -0.01222 -0.03893 0.06378  291 PHE   A CB  
2241 C CG  . PHE   A 291 ? 0.16986 0.22266 0.17360 -0.01529 -0.03986 0.06320  291 PHE   A CG  
2242 C CD1 . PHE   A 291 ? 0.20469 0.25936 0.20418 -0.01323 -0.03756 0.05864  291 PHE   A CD1 
2243 C CD2 . PHE   A 291 ? 0.16418 0.21126 0.17854 -0.02064 -0.04398 0.06821  291 PHE   A CD2 
2244 C CE1 . PHE   A 291 ? 0.18007 0.23391 0.18718 -0.01644 -0.03892 0.06073  291 PHE   A CE1 
2245 C CE2 . PHE   A 291 ? 0.19145 0.23658 0.21165 -0.02531 -0.04624 0.06900  291 PHE   A CE2 
2246 C CZ  . PHE   A 291 ? 0.16703 0.21689 0.18423 -0.02318 -0.04344 0.06604  291 PHE   A CZ  
2247 N N   . THR   A 292 ? 0.16004 0.21840 0.13722 -0.00627 -0.03836 0.05030  292 THR   A N   
2248 C CA  . THR   A 292 ? 0.18738 0.25853 0.16032 -0.00640 -0.03893 0.05316  292 THR   A CA  
2249 C C   . THR   A 292 ? 0.20624 0.29560 0.17610 -0.00761 -0.03726 0.05991  292 THR   A C   
2250 O O   . THR   A 292 ? 0.16005 0.25073 0.12960 -0.00722 -0.03487 0.06027  292 THR   A O   
2251 C CB  . THR   A 292 ? 0.21617 0.28336 0.18000 -0.00569 -0.03917 0.04310  292 THR   A CB  
2252 O OG1 . THR   A 292 ? 0.20801 0.27237 0.16490 -0.00492 -0.03706 0.03655  292 THR   A OG1 
2253 C CG2 . THR   A 292 ? 0.19260 0.24515 0.15933 -0.00409 -0.04021 0.03772  292 THR   A CG2 
2254 N N   . PRO   A 293 ? 0.18286 0.28891 0.15035 -0.00916 -0.03856 0.06635  293 PRO   A N   
2255 C CA  . PRO   A 293 ? 0.19726 0.32280 0.15771 -0.01061 -0.03695 0.07164  293 PRO   A CA  
2256 C C   . PRO   A 293 ? 0.21326 0.33652 0.15884 -0.01009 -0.03444 0.06031  293 PRO   A C   
2257 O O   . PRO   A 293 ? 0.19950 0.33154 0.13967 -0.00959 -0.03120 0.06283  293 PRO   A O   
2258 C CB  . PRO   A 293 ? 0.18272 0.32654 0.14099 -0.01343 -0.04017 0.07873  293 PRO   A CB  
2259 C CG  . PRO   A 293 ? 0.19017 0.32580 0.16228 -0.01219 -0.04250 0.08399  293 PRO   A CG  
2260 C CD  . PRO   A 293 ? 0.18854 0.29948 0.15992 -0.00986 -0.04173 0.07083  293 PRO   A CD  
2261 N N   . PHE   A 294 ? 0.21676 0.32774 0.15591 -0.00987 -0.03538 0.04848  294 PHE   A N   
2262 C CA  . PHE   A 294 ? 0.23670 0.34211 0.16252 -0.00914 -0.03272 0.03775  294 PHE   A CA  
2263 C C   . PHE   A 294 ? 0.22875 0.32361 0.16050 -0.00536 -0.02969 0.03769  294 PHE   A C   
2264 O O   . PHE   A 294 ? 0.26158 0.35823 0.18353 -0.00396 -0.02560 0.03498  294 PHE   A O   
2265 C CB  . PHE   A 294 ? 0.24163 0.33635 0.16197 -0.01025 -0.03474 0.02688  294 PHE   A CB  
2266 C CG  . PHE   A 294 ? 0.31914 0.40314 0.22752 -0.00930 -0.03166 0.01572  294 PHE   A CG  
2267 C CD1 . PHE   A 294 ? 0.33658 0.42649 0.22541 -0.01286 -0.02916 0.00753  294 PHE   A CD1 
2268 C CD2 . PHE   A 294 ? 0.34525 0.41280 0.26027 -0.00552 -0.03077 0.01306  294 PHE   A CD2 
2269 C CE1 . PHE   A 294 ? 0.32885 0.40522 0.20446 -0.01203 -0.02389 -0.00426 294 PHE   A CE1 
2270 C CE2 . PHE   A 294 ? 0.38866 0.44589 0.29239 -0.00458 -0.02727 0.00414  294 PHE   A CE2 
2271 C CZ  . PHE   A 294 ? 0.35945 0.41931 0.24301 -0.00756 -0.02269 -0.00528 294 PHE   A CZ  
2272 N N   . ASP   A 295 ? 0.20588 0.29005 0.15195 -0.00420 -0.03121 0.04061  295 ASP   A N   
2273 C CA  . ASP   A 295 ? 0.20847 0.28552 0.16163 -0.00208 -0.02962 0.04164  295 ASP   A CA  
2274 C C   . ASP   A 295 ? 0.25165 0.34272 0.20799 -0.00173 -0.02650 0.05107  295 ASP   A C   
2275 O O   . ASP   A 295 ? 0.21894 0.31129 0.17434 0.00086  -0.02327 0.05163  295 ASP   A O   
2276 C CB  . ASP   A 295 ? 0.18006 0.24542 0.14524 -0.00314 -0.03219 0.04291  295 ASP   A CB  
2277 C CG  . ASP   A 295 ? 0.20426 0.25598 0.16654 -0.00233 -0.03398 0.03422  295 ASP   A CG  
2278 O OD1 . ASP   A 295 ? 0.20561 0.25506 0.15919 -0.00096 -0.03355 0.02754  295 ASP   A OD1 
2279 O OD2 . ASP   A 295 ? 0.16671 0.21032 0.13491 -0.00333 -0.03563 0.03431  295 ASP   A OD2 
2280 N N   . VAL   A 296 ? 0.20522 0.30789 0.16659 -0.00393 -0.02711 0.06033  296 VAL   A N   
2281 C CA  . VAL   A 296 ? 0.22901 0.34639 0.19599 -0.00389 -0.02412 0.07166  296 VAL   A CA  
2282 C C   . VAL   A 296 ? 0.24333 0.37220 0.19304 -0.00188 -0.01904 0.06986  296 VAL   A C   
2283 O O   . VAL   A 296 ? 0.26869 0.40454 0.21974 0.00052  -0.01383 0.07470  296 VAL   A O   
2284 C CB  . VAL   A 296 ? 0.16218 0.28907 0.13882 -0.00674 -0.02627 0.08323  296 VAL   A CB  
2285 C CG1 . VAL   A 296 ? 0.18061 0.32450 0.16374 -0.00671 -0.02294 0.09638  296 VAL   A CG1 
2286 C CG2 . VAL   A 296 ? 0.13688 0.24835 0.12716 -0.00883 -0.03000 0.08387  296 VAL   A CG2 
2287 N N   . VAL   A 297 ? 0.26541 0.39883 0.19820 -0.00368 -0.01959 0.06368  297 VAL   A N   
2288 C CA  . VAL   A 297 ? 0.26716 0.40720 0.17647 -0.00381 -0.01330 0.05818  297 VAL   A CA  
2289 C C   . VAL   A 297 ? 0.31109 0.44703 0.21491 -0.00056 -0.00645 0.05043  297 VAL   A C   
2290 O O   . VAL   A 297 ? 0.31529 0.46618 0.21146 0.00165  0.00423  0.05274  297 VAL   A O   
2291 C CB  . VAL   A 297 ? 0.25274 0.39789 0.14538 -0.00850 -0.01627 0.05046  297 VAL   A CB  
2292 C CG1 . VAL   A 297 ? 0.27592 0.42075 0.13990 -0.01021 -0.00793 0.03872  297 VAL   A CG1 
2293 C CG2 . VAL   A 297 ? 0.28991 0.45570 0.18862 -0.01179 -0.02057 0.06352  297 VAL   A CG2 
2294 N N   . ARG   A 298 ? 0.26960 0.38698 0.17791 0.00046  -0.01047 0.04213  298 ARG   A N   
2295 C CA  . ARG   A 298 ? 0.30301 0.42032 0.20784 0.00433  -0.00355 0.03632  298 ARG   A CA  
2296 C C   . ARG   A 298 ? 0.33793 0.47009 0.26009 0.01011  0.00184  0.05067  298 ARG   A C   
2297 O O   . ARG   A 298 ? 0.38416 0.52867 0.30081 0.01565  0.01651  0.05113  298 ARG   A O   
2298 C CB  . ARG   A 298 ? 0.30218 0.39835 0.21284 0.00429  -0.01077 0.02880  298 ARG   A CB  
2299 C CG  . ARG   A 298 ? 0.32487 0.42484 0.24352 0.01078  -0.00629 0.03128  298 ARG   A CG  
2300 C CD  . ARG   A 298 ? 0.41596 0.49674 0.33891 0.01064  -0.01336 0.02450  298 ARG   A CD  
2301 N NE  . ARG   A 298 ? 0.41620 0.47687 0.35702 0.00793  -0.02341 0.02848  298 ARG   A NE  
2302 C CZ  . ARG   A 298 ? 0.32338 0.37591 0.27838 0.00966  -0.02676 0.03196  298 ARG   A CZ  
2303 N NH1 . ARG   A 298 ? 0.30686 0.37270 0.26856 0.01584  -0.02333 0.03874  298 ARG   A NH1 
2304 N NH2 . ARG   A 298 ? 0.31169 0.35518 0.27607 0.00689  -0.03067 0.03153  298 ARG   A NH2 
2305 N N   . GLN   A 299 ? 0.28652 0.41447 0.23156 0.00883  -0.00646 0.06107  299 GLN   A N   
2306 C CA  . GLN   A 299 ? 0.32024 0.46001 0.28759 0.01239  -0.00367 0.07549  299 GLN   A CA  
2307 C C   . GLN   A 299 ? 0.34751 0.51065 0.31850 0.01388  0.00439  0.08865  299 GLN   A C   
2308 O O   . GLN   A 299 ? 0.33149 0.51043 0.31297 0.02007  0.01500  0.09977  299 GLN   A O   
2309 C CB  . GLN   A 299 ? 0.28941 0.41003 0.27546 0.00702  -0.01359 0.07559  299 GLN   A CB  
2310 C CG  . GLN   A 299 ? 0.25215 0.38429 0.26350 0.00613  -0.01249 0.08986  299 GLN   A CG  
2311 C CD  . GLN   A 299 ? 0.23919 0.34963 0.25995 -0.00053 -0.02067 0.08469  299 GLN   A CD  
2312 O OE1 . GLN   A 299 ? 0.23487 0.35245 0.27455 -0.00434 -0.02153 0.09443  299 GLN   A OE1 
2313 N NE2 . GLN   A 299 ? 0.18449 0.27590 0.19423 -0.00265 -0.02549 0.07270  299 GLN   A NE2 
2314 N N   . CYS   A 300 ? 0.31298 0.47825 0.27801 0.00912  0.00120  0.08946  300 CYS   A N   
2315 C CA  . CYS   A 300 ? 0.30191 0.48877 0.27118 0.00992  0.00789  0.10316  300 CYS   A CA  
2316 C C   . CYS   A 300 ? 0.37255 0.57064 0.31608 0.01275  0.02270  0.09771  300 CYS   A C   
2317 O O   . CYS   A 300 ? 0.34908 0.56375 0.29475 0.01424  0.03211  0.10817  300 CYS   A O   
2318 C CB  . CYS   A 300 ? 0.33398 0.52039 0.30706 0.00435  0.00047  0.10805  300 CYS   A CB  
2319 S SG  . CYS   A 300 ? 0.26556 0.43501 0.26687 -0.00061 -0.00935 0.11228  300 CYS   A SG  
2320 N N   . SER   A 301 ? 0.38147 0.56815 0.30110 0.01241  0.02714  0.07936  301 SER   A N   
2321 C CA  . SER   A 301 ? 0.42284 0.61198 0.31480 0.01199  0.04441  0.06574  301 SER   A CA  
2322 C C   . SER   A 301 ? 0.42526 0.60571 0.31561 0.01783  0.06091  0.05202  301 SER   A C   
2323 O O   . SER   A 301 ? 0.44450 0.62776 0.32792 0.02062  0.08274  0.04399  301 SER   A O   
2324 C CB  . SER   A 301 ? 0.48453 0.66590 0.34930 0.00379  0.03723  0.05248  301 SER   A CB  
2325 O OG  . SER   A 301 ? 0.57304 0.74928 0.40913 0.00167  0.05342  0.03385  301 SER   A OG  
2326 N N   . GLY   A 302 ? 0.45885 0.62743 0.35798 0.02017  0.05325  0.04805  302 GLY   A N   
2327 C CA  . GLY   A 302 ? 0.48098 0.64578 0.39445 0.02969  0.07018  0.04262  302 GLY   A CA  
2328 C C   . GLY   A 302 ? 0.53066 0.67637 0.42669 0.02913  0.07920  0.01622  302 GLY   A C   
2329 O O   . GLY   A 302 ? 0.50935 0.64866 0.41052 0.03542  0.10282  0.00287  302 GLY   A O   
2330 N N   . VAL   A 303 ? 0.53803 0.67109 0.41915 0.02155  0.06096  0.00815  303 VAL   A N   
2331 C CA  . VAL   A 303 ? 0.59338 0.70572 0.46001 0.01857  0.06627  -0.01651 303 VAL   A CA  
2332 C C   . VAL   A 303 ? 0.56806 0.66804 0.46380 0.02857  0.07014  -0.01609 303 VAL   A C   
2333 O O   . VAL   A 303 ? 0.54650 0.64724 0.46669 0.03173  0.05502  0.00354  303 VAL   A O   
2334 C CB  . VAL   A 303 ? 0.57547 0.67665 0.42565 0.00701  0.04393  -0.02038 303 VAL   A CB  
2335 C CG1 . VAL   A 303 ? 0.62762 0.70672 0.46914 0.00377  0.04589  -0.04150 303 VAL   A CG1 
2336 C CG2 . VAL   A 303 ? 0.49500 0.60315 0.32681 0.00001  0.04073  -0.01841 303 VAL   A CG2 
2337 N N   . THR   A 304 ? 0.58561 0.66572 0.48469 0.03162  0.08824  -0.03660 304 THR   A N   
2338 C CA  . THR   A 304 ? 0.56336 0.62279 0.49832 0.04035  0.09143  -0.03363 304 THR   A CA  
2339 C C   . THR   A 304 ? 0.66443 0.69937 0.58812 0.03406  0.09005  -0.05530 304 THR   A C   
2340 O O   . THR   A 304 ? 0.68169 0.71779 0.57101 0.02187  0.08252  -0.07108 304 THR   A O   
2341 C CB  . THR   A 304 ? 0.53572 0.59163 0.49994 0.05318  0.11865  -0.03320 304 THR   A CB  
2342 O OG1 . THR   A 304 ? 0.60104 0.64126 0.54544 0.05097  0.14229  -0.06321 304 THR   A OG1 
2343 C CG2 . THR   A 304 ? 0.42715 0.51023 0.40005 0.05782  0.12365  -0.01421 304 THR   A CG2 
2344 N N   . PHE   A 305 ? 0.67069 0.68536 0.62684 0.04224  0.09730  -0.05365 305 PHE   A N   
2345 C CA  . PHE   A 305 ? 0.69747 0.68598 0.65448 0.03819  0.09846  -0.07001 305 PHE   A CA  
2346 C C   . PHE   A 305 ? 0.73022 0.69890 0.72718 0.05128  0.12065  -0.06900 305 PHE   A C   
2347 O O   . PHE   A 305 ? 0.68032 0.65949 0.70882 0.06359  0.12716  -0.04866 305 PHE   A O   
2348 C CB  . PHE   A 305 ? 0.65041 0.63906 0.60926 0.03337  0.07211  -0.05671 305 PHE   A CB  
2349 C CG  . PHE   A 305 ? 0.61865 0.62972 0.55283 0.02575  0.05104  -0.04767 305 PHE   A CG  
2350 C CD1 . PHE   A 305 ? 0.61912 0.63507 0.51871 0.01331  0.04344  -0.06307 305 PHE   A CD1 
2351 C CD2 . PHE   A 305 ? 0.54996 0.57835 0.49767 0.03059  0.03986  -0.02327 305 PHE   A CD2 
2352 C CE1 . PHE   A 305 ? 0.59582 0.63279 0.47775 0.00796  0.02577  -0.05201 305 PHE   A CE1 
2353 C CE2 . PHE   A 305 ? 0.55032 0.59590 0.47907 0.02421  0.02322  -0.01512 305 PHE   A CE2 
2354 C CZ  . PHE   A 305 ? 0.58856 0.63822 0.48567 0.01395  0.01673  -0.02847 305 PHE   A CZ  
2355 N N   . GLN   A 306 ? 0.76089 0.70162 0.76027 0.04849  0.13244  -0.08943 306 GLN   A N   
2356 C CA  . GLN   A 306 ? 0.82313 0.74766 0.86135 0.05910  0.14879  -0.08415 306 GLN   A CA  
2357 C C   . GLN   A 306 ? 0.80044 0.70037 0.85993 0.05775  0.14605  -0.08306 306 GLN   A C   
2358 O O   . GLN   A 306 ? 0.75234 0.65340 0.83132 0.06194  0.13356  -0.06332 306 GLN   A O   
2359 C CB  . GLN   A 306 ? 0.82744 0.74719 0.85133 0.05646  0.16656  -0.10456 306 GLN   A CB  
2360 C CG  . GLN   A 306 ? 0.84581 0.75319 0.91014 0.06867  0.18654  -0.09683 306 GLN   A CG  
2361 C CD  . GLN   A 306 ? 0.87174 0.77934 0.92234 0.06878  0.20589  -0.11420 306 GLN   A CD  
2362 O OE1 . GLN   A 306 ? 0.93851 0.85790 0.94798 0.05962  0.20290  -0.13047 306 GLN   A OE1 
2363 N NE2 . GLN   A 306 ? 0.86210 0.75795 0.94698 0.07900  0.22550  -0.10923 306 GLN   A NE2 
2364 N N   . A1ARI B .   ? 0.40587 0.40370 0.17911 -0.03807 -0.01940 -0.01735 401 A1ARI A N   
2365 C C   . A1ARI B .   ? 0.40765 0.38872 0.16472 -0.04357 -0.01643 -0.04307 401 A1ARI A C   
2366 O O   . A1ARI B .   ? 0.37628 0.36569 0.17742 -0.03656 -0.02752 -0.02185 401 A1ARI A O   
2367 C C1  . A1ARI B .   ? 0.40690 0.39697 0.18618 -0.03900 -0.02201 -0.02638 401 A1ARI A C1  
2368 C C10 . A1ARI B .   ? 0.28757 0.28799 0.12841 -0.04875 -0.05270 0.00195  401 A1ARI A C10 
2369 C C11 . A1ARI B .   ? 0.43369 0.44374 0.21703 -0.03362 -0.01777 0.00552  401 A1ARI A C11 
2370 C C12 . A1ARI B .   ? 0.47293 0.47988 0.26628 -0.02469 -0.00890 0.00680  401 A1ARI A C12 
2371 C C13 . A1ARI B .   ? 0.42734 0.40785 0.17677 -0.05476 -0.02587 -0.04598 401 A1ARI A C13 
2372 C C14 . A1ARI B .   ? 0.42479 0.42035 0.17060 -0.06215 -0.03518 -0.03136 401 A1ARI A C14 
2373 C C15 . A1ARI B .   ? 0.47713 0.44237 0.23735 -0.03103 0.00479  -0.06145 401 A1ARI A C15 
2374 C C16 . A1ARI B .   ? 0.49667 0.43903 0.26101 -0.02459 0.03136  -0.08116 401 A1ARI A C16 
2375 C C17 . A1ARI B .   ? 0.48331 0.44285 0.20824 -0.06641 -0.02279 -0.07513 401 A1ARI A C17 
2376 C C18 . A1ARI B .   ? 0.47992 0.42596 0.22271 -0.05539 -0.01441 -0.08299 401 A1ARI A C18 
2377 C C19 . A1ARI B .   ? 0.49028 0.44315 0.18341 -0.07767 -0.01873 -0.09182 401 A1ARI A C19 
2378 C C2  . A1ARI B .   ? 0.38947 0.39359 0.18301 -0.03470 -0.02356 -0.00287 401 A1ARI A C2  
2379 C C20 . A1ARI B .   ? 0.41696 0.38338 0.15585 -0.07216 -0.03635 -0.06465 401 A1ARI A C20 
2380 C C21 . A1ARI B .   ? 0.54943 0.55856 0.32147 -0.02399 0.00299  0.00764  401 A1ARI A C21 
2381 C C22 . A1ARI B .   ? 0.52393 0.53362 0.30345 -0.02102 0.01426  0.01046  401 A1ARI A C22 
2382 C C23 . A1ARI B .   ? 0.49268 0.49790 0.29265 -0.01673 0.01233  0.00511  401 A1ARI A C23 
2383 C C24 . A1ARI B .   ? 0.50158 0.50081 0.30035 -0.01592 0.00746  -0.00790 401 A1ARI A C24 
2384 C C25 . A1ARI B .   ? 0.44442 0.44451 0.24820 -0.01872 -0.00601 -0.00434 401 A1ARI A C25 
2385 C C26 . A1ARI B .   ? 0.49535 0.41762 0.24913 -0.02889 0.03910  -0.10024 401 A1ARI A C26 
2386 C C27 . A1ARI B .   ? 0.50786 0.44682 0.29366 -0.01664 0.03830  -0.07779 401 A1ARI A C27 
2387 C C3  . A1ARI B .   ? 0.37977 0.38982 0.18195 -0.04105 -0.03422 0.00538  401 A1ARI A C3  
2388 C C4  . A1ARI B .   ? 0.35214 0.36944 0.18647 -0.04305 -0.04608 0.02093  401 A1ARI A C4  
2389 C C5  . A1ARI B .   ? 0.32152 0.34428 0.17162 -0.03973 -0.04639 0.03346  401 A1ARI A C5  
2390 C C6  . A1ARI B .   ? 0.30754 0.31958 0.15382 -0.04352 -0.04957 0.01674  401 A1ARI A C6  
2391 C C7  . A1ARI B .   ? 0.30332 0.30948 0.13248 -0.04832 -0.04969 0.00475  401 A1ARI A C7  
2392 C C8  . A1ARI B .   ? 0.31793 0.33237 0.12632 -0.05957 -0.05531 0.00600  401 A1ARI A C8  
2393 C C9  . A1ARI B .   ? 0.31032 0.31952 0.11536 -0.06576 -0.05965 -0.00167 401 A1ARI A C9  
2394 N N1  . A1ARI B .   ? 0.35190 0.36183 0.17855 -0.03747 -0.03790 0.01159  401 A1ARI A N1  
2395 N N2  . A1ARI B .   ? 0.31461 0.31628 0.14242 -0.05801 -0.05799 -0.00127 401 A1ARI A N2  
2396 N N3  . A1ARI B .   ? 0.43257 0.40279 0.19978 -0.03587 -0.00881 -0.05371 401 A1ARI A N3  
2397 O O1  . A1ARI B .   ? 0.40758 0.42338 0.19424 -0.04972 -0.03889 0.00624  401 A1ARI A O1  
2398 O O2  . A1ARI B .   ? 0.33219 0.36292 0.19437 -0.04336 -0.05324 0.04373  401 A1ARI A O2  
2399 O O3  . A1ARI B .   ? 0.26150 0.25736 0.12027 -0.04219 -0.05059 0.00280  401 A1ARI A O3  
2400 O O4  . A1ARI B .   ? 0.46767 0.43941 0.19149 -0.06168 -0.02046 -0.06291 401 A1ARI A O4  
2401 O O5  . A1ARI B .   ? 0.47147 0.42467 0.24532 -0.02665 0.01225  -0.06902 401 A1ARI A O5  
2402 O O6  . A1ARI B .   ? 0.53712 0.50611 0.27929 -0.03233 0.01309  -0.06191 401 A1ARI A O6  
# 
