data_9BQG
# 
_entry.id   9BQG 
# 
_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   9BQG         pdb_00009bqg 10.2210/pdb9bqg/pdb 
WWPDB D_1000283978 ?            ?                   
# 
_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                        9BQG 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-09 
_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 in complex with inhibitor k68' 
_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 
'benzyl (2S,4S)-4-tert-butoxy-2-({(2R)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}carbamoyl)pyrrolidine-1-carboxylate' 
461.551   1   ?         ? ? ? 
3 water       nat water 18.015    326 ?         ? ? ? 
# 
_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 'benzyl (2S,4S)-4-tert-butoxy-2-({(2R)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}carbamoyl)pyrrolidine-1-carboxylate' 
A1AQ3 
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 
A1AQ3 non-polymer         . 
'benzyl (2S,4S)-4-tert-butoxy-2-({(2R)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propan-2-yl}carbamoyl)pyrrolidine-1-carboxylate' ? 
'C24 H35 N3 O6'  461.551 
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        A1AQ3 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AQ3 
_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 A1AQ3 1   401 401 A1AQ3 k68 A . 
C 3 HOH   1   501 65  HOH   HOH A . 
C 3 HOH   2   502 136 HOH   HOH A . 
C 3 HOH   3   503 17  HOH   HOH A . 
C 3 HOH   4   504 173 HOH   HOH A . 
C 3 HOH   5   505 132 HOH   HOH A . 
C 3 HOH   6   506 324 HOH   HOH A . 
C 3 HOH   7   507 203 HOH   HOH A . 
C 3 HOH   8   508 285 HOH   HOH A . 
C 3 HOH   9   509 268 HOH   HOH A . 
C 3 HOH   10  510 229 HOH   HOH A . 
C 3 HOH   11  511 271 HOH   HOH A . 
C 3 HOH   12  512 111 HOH   HOH A . 
C 3 HOH   13  513 84  HOH   HOH A . 
C 3 HOH   14  514 85  HOH   HOH A . 
C 3 HOH   15  515 190 HOH   HOH A . 
C 3 HOH   16  516 70  HOH   HOH A . 
C 3 HOH   17  517 266 HOH   HOH A . 
C 3 HOH   18  518 295 HOH   HOH A . 
C 3 HOH   19  519 126 HOH   HOH A . 
C 3 HOH   20  520 47  HOH   HOH A . 
C 3 HOH   21  521 119 HOH   HOH A . 
C 3 HOH   22  522 60  HOH   HOH A . 
C 3 HOH   23  523 48  HOH   HOH A . 
C 3 HOH   24  524 269 HOH   HOH A . 
C 3 HOH   25  525 170 HOH   HOH A . 
C 3 HOH   26  526 202 HOH   HOH A . 
C 3 HOH   27  527 104 HOH   HOH A . 
C 3 HOH   28  528 107 HOH   HOH A . 
C 3 HOH   29  529 188 HOH   HOH A . 
C 3 HOH   30  530 54  HOH   HOH A . 
C 3 HOH   31  531 264 HOH   HOH A . 
C 3 HOH   32  532 167 HOH   HOH A . 
C 3 HOH   33  533 92  HOH   HOH A . 
C 3 HOH   34  534 102 HOH   HOH A . 
C 3 HOH   35  535 127 HOH   HOH A . 
C 3 HOH   36  536 7   HOH   HOH A . 
C 3 HOH   37  537 195 HOH   HOH A . 
C 3 HOH   38  538 186 HOH   HOH A . 
C 3 HOH   39  539 226 HOH   HOH A . 
C 3 HOH   40  540 24  HOH   HOH A . 
C 3 HOH   41  541 249 HOH   HOH A . 
C 3 HOH   42  542 185 HOH   HOH A . 
C 3 HOH   43  543 212 HOH   HOH A . 
C 3 HOH   44  544 316 HOH   HOH A . 
C 3 HOH   45  545 141 HOH   HOH A . 
C 3 HOH   46  546 165 HOH   HOH A . 
C 3 HOH   47  547 75  HOH   HOH A . 
C 3 HOH   48  548 29  HOH   HOH A . 
C 3 HOH   49  549 159 HOH   HOH A . 
C 3 HOH   50  550 309 HOH   HOH A . 
C 3 HOH   51  551 2   HOH   HOH A . 
C 3 HOH   52  552 33  HOH   HOH A . 
C 3 HOH   53  553 89  HOH   HOH A . 
C 3 HOH   54  554 43  HOH   HOH A . 
C 3 HOH   55  555 52  HOH   HOH A . 
C 3 HOH   56  556 129 HOH   HOH A . 
C 3 HOH   57  557 31  HOH   HOH A . 
C 3 HOH   58  558 164 HOH   HOH A . 
C 3 HOH   59  559 73  HOH   HOH A . 
C 3 HOH   60  560 220 HOH   HOH A . 
C 3 HOH   61  561 221 HOH   HOH A . 
C 3 HOH   62  562 171 HOH   HOH A . 
C 3 HOH   63  563 143 HOH   HOH A . 
C 3 HOH   64  564 162 HOH   HOH A . 
C 3 HOH   65  565 112 HOH   HOH A . 
C 3 HOH   66  566 323 HOH   HOH A . 
C 3 HOH   67  567 251 HOH   HOH A . 
C 3 HOH   68  568 115 HOH   HOH A . 
C 3 HOH   69  569 114 HOH   HOH A . 
C 3 HOH   70  570 206 HOH   HOH A . 
C 3 HOH   71  571 50  HOH   HOH A . 
C 3 HOH   72  572 67  HOH   HOH A . 
C 3 HOH   73  573 57  HOH   HOH A . 
C 3 HOH   74  574 138 HOH   HOH A . 
C 3 HOH   75  575 122 HOH   HOH A . 
C 3 HOH   76  576 288 HOH   HOH A . 
C 3 HOH   77  577 3   HOH   HOH A . 
C 3 HOH   78  578 287 HOH   HOH A . 
C 3 HOH   79  579 96  HOH   HOH A . 
C 3 HOH   80  580 166 HOH   HOH A . 
C 3 HOH   81  581 26  HOH   HOH A . 
C 3 HOH   82  582 216 HOH   HOH A . 
C 3 HOH   83  583 196 HOH   HOH A . 
C 3 HOH   84  584 34  HOH   HOH A . 
C 3 HOH   85  585 56  HOH   HOH A . 
C 3 HOH   86  586 108 HOH   HOH A . 
C 3 HOH   87  587 5   HOH   HOH A . 
C 3 HOH   88  588 135 HOH   HOH A . 
C 3 HOH   89  589 137 HOH   HOH A . 
C 3 HOH   90  590 161 HOH   HOH A . 
C 3 HOH   91  591 321 HOH   HOH A . 
C 3 HOH   92  592 101 HOH   HOH A . 
C 3 HOH   93  593 179 HOH   HOH A . 
C 3 HOH   94  594 23  HOH   HOH A . 
C 3 HOH   95  595 28  HOH   HOH A . 
C 3 HOH   96  596 163 HOH   HOH A . 
C 3 HOH   97  597 109 HOH   HOH A . 
C 3 HOH   98  598 61  HOH   HOH A . 
C 3 HOH   99  599 246 HOH   HOH A . 
C 3 HOH   100 600 93  HOH   HOH A . 
C 3 HOH   101 601 68  HOH   HOH A . 
C 3 HOH   102 602 139 HOH   HOH A . 
C 3 HOH   103 603 176 HOH   HOH A . 
C 3 HOH   104 604 118 HOH   HOH A . 
C 3 HOH   105 605 13  HOH   HOH A . 
C 3 HOH   106 606 281 HOH   HOH A . 
C 3 HOH   107 607 180 HOH   HOH A . 
C 3 HOH   108 608 272 HOH   HOH A . 
C 3 HOH   109 609 150 HOH   HOH A . 
C 3 HOH   110 610 175 HOH   HOH A . 
C 3 HOH   111 611 38  HOH   HOH A . 
C 3 HOH   112 612 46  HOH   HOH A . 
C 3 HOH   113 613 21  HOH   HOH A . 
C 3 HOH   114 614 20  HOH   HOH A . 
C 3 HOH   115 615 207 HOH   HOH A . 
C 3 HOH   116 616 125 HOH   HOH A . 
C 3 HOH   117 617 27  HOH   HOH A . 
C 3 HOH   118 618 128 HOH   HOH A . 
C 3 HOH   119 619 53  HOH   HOH A . 
C 3 HOH   120 620 105 HOH   HOH A . 
C 3 HOH   121 621 155 HOH   HOH A . 
C 3 HOH   122 622 63  HOH   HOH A . 
C 3 HOH   123 623 39  HOH   HOH A . 
C 3 HOH   124 624 88  HOH   HOH A . 
C 3 HOH   125 625 312 HOH   HOH A . 
C 3 HOH   126 626 253 HOH   HOH A . 
C 3 HOH   127 627 90  HOH   HOH A . 
C 3 HOH   128 628 181 HOH   HOH A . 
C 3 HOH   129 629 59  HOH   HOH A . 
C 3 HOH   130 630 255 HOH   HOH A . 
C 3 HOH   131 631 146 HOH   HOH A . 
C 3 HOH   132 632 18  HOH   HOH A . 
C 3 HOH   133 633 35  HOH   HOH A . 
C 3 HOH   134 634 42  HOH   HOH A . 
C 3 HOH   135 635 191 HOH   HOH A . 
C 3 HOH   136 636 77  HOH   HOH A . 
C 3 HOH   137 637 319 HOH   HOH A . 
C 3 HOH   138 638 1   HOH   HOH A . 
C 3 HOH   139 639 12  HOH   HOH A . 
C 3 HOH   140 640 71  HOH   HOH A . 
C 3 HOH   141 641 133 HOH   HOH A . 
C 3 HOH   142 642 10  HOH   HOH A . 
C 3 HOH   143 643 156 HOH   HOH A . 
C 3 HOH   144 644 78  HOH   HOH A . 
C 3 HOH   145 645 58  HOH   HOH A . 
C 3 HOH   146 646 148 HOH   HOH A . 
C 3 HOH   147 647 55  HOH   HOH A . 
C 3 HOH   148 648 100 HOH   HOH A . 
C 3 HOH   149 649 291 HOH   HOH A . 
C 3 HOH   150 650 325 HOH   HOH A . 
C 3 HOH   151 651 256 HOH   HOH A . 
C 3 HOH   152 652 154 HOH   HOH A . 
C 3 HOH   153 653 222 HOH   HOH A . 
C 3 HOH   154 654 209 HOH   HOH A . 
C 3 HOH   155 655 106 HOH   HOH A . 
C 3 HOH   156 656 22  HOH   HOH A . 
C 3 HOH   157 657 103 HOH   HOH A . 
C 3 HOH   158 658 145 HOH   HOH A . 
C 3 HOH   159 659 314 HOH   HOH A . 
C 3 HOH   160 660 197 HOH   HOH A . 
C 3 HOH   161 661 317 HOH   HOH A . 
C 3 HOH   162 662 64  HOH   HOH A . 
C 3 HOH   163 663 121 HOH   HOH A . 
C 3 HOH   164 664 130 HOH   HOH A . 
C 3 HOH   165 665 120 HOH   HOH A . 
C 3 HOH   166 666 217 HOH   HOH A . 
C 3 HOH   167 667 30  HOH   HOH A . 
C 3 HOH   168 668 153 HOH   HOH A . 
C 3 HOH   169 669 270 HOH   HOH A . 
C 3 HOH   170 670 124 HOH   HOH A . 
C 3 HOH   171 671 187 HOH   HOH A . 
C 3 HOH   172 672 82  HOH   HOH A . 
C 3 HOH   173 673 4   HOH   HOH A . 
C 3 HOH   174 674 9   HOH   HOH A . 
C 3 HOH   175 675 40  HOH   HOH A . 
C 3 HOH   176 676 168 HOH   HOH A . 
C 3 HOH   177 677 110 HOH   HOH A . 
C 3 HOH   178 678 144 HOH   HOH A . 
C 3 HOH   179 679 11  HOH   HOH A . 
C 3 HOH   180 680 258 HOH   HOH A . 
C 3 HOH   181 681 265 HOH   HOH A . 
C 3 HOH   182 682 219 HOH   HOH A . 
C 3 HOH   183 683 14  HOH   HOH A . 
C 3 HOH   184 684 69  HOH   HOH A . 
C 3 HOH   185 685 182 HOH   HOH A . 
C 3 HOH   186 686 178 HOH   HOH A . 
C 3 HOH   187 687 72  HOH   HOH A . 
C 3 HOH   188 688 44  HOH   HOH A . 
C 3 HOH   189 689 174 HOH   HOH A . 
C 3 HOH   190 690 151 HOH   HOH A . 
C 3 HOH   191 691 311 HOH   HOH A . 
C 3 HOH   192 692 267 HOH   HOH A . 
C 3 HOH   193 693 74  HOH   HOH A . 
C 3 HOH   194 694 45  HOH   HOH A . 
C 3 HOH   195 695 310 HOH   HOH A . 
C 3 HOH   196 696 279 HOH   HOH A . 
C 3 HOH   197 697 80  HOH   HOH A . 
C 3 HOH   198 698 302 HOH   HOH A . 
C 3 HOH   199 699 19  HOH   HOH A . 
C 3 HOH   200 700 62  HOH   HOH A . 
C 3 HOH   201 701 157 HOH   HOH A . 
C 3 HOH   202 702 6   HOH   HOH A . 
C 3 HOH   203 703 293 HOH   HOH A . 
C 3 HOH   204 704 259 HOH   HOH A . 
C 3 HOH   205 705 99  HOH   HOH A . 
C 3 HOH   206 706 87  HOH   HOH A . 
C 3 HOH   207 707 41  HOH   HOH A . 
C 3 HOH   208 708 201 HOH   HOH A . 
C 3 HOH   209 709 79  HOH   HOH A . 
C 3 HOH   210 710 15  HOH   HOH A . 
C 3 HOH   211 711 198 HOH   HOH A . 
C 3 HOH   212 712 142 HOH   HOH A . 
C 3 HOH   213 713 236 HOH   HOH A . 
C 3 HOH   214 714 241 HOH   HOH A . 
C 3 HOH   215 715 66  HOH   HOH A . 
C 3 HOH   216 716 8   HOH   HOH A . 
C 3 HOH   217 717 83  HOH   HOH A . 
C 3 HOH   218 718 16  HOH   HOH A . 
C 3 HOH   219 719 147 HOH   HOH A . 
C 3 HOH   220 720 304 HOH   HOH A . 
C 3 HOH   221 721 116 HOH   HOH A . 
C 3 HOH   222 722 233 HOH   HOH A . 
C 3 HOH   223 723 91  HOH   HOH A . 
C 3 HOH   224 724 237 HOH   HOH A . 
C 3 HOH   225 725 140 HOH   HOH A . 
C 3 HOH   226 726 51  HOH   HOH A . 
C 3 HOH   227 727 134 HOH   HOH A . 
C 3 HOH   228 728 230 HOH   HOH A . 
C 3 HOH   229 729 231 HOH   HOH A . 
C 3 HOH   230 730 299 HOH   HOH A . 
C 3 HOH   231 731 296 HOH   HOH A . 
C 3 HOH   232 732 320 HOH   HOH A . 
C 3 HOH   233 733 225 HOH   HOH A . 
C 3 HOH   234 734 213 HOH   HOH A . 
C 3 HOH   235 735 238 HOH   HOH A . 
C 3 HOH   236 736 117 HOH   HOH A . 
C 3 HOH   237 737 215 HOH   HOH A . 
C 3 HOH   238 738 326 HOH   HOH A . 
C 3 HOH   239 739 300 HOH   HOH A . 
C 3 HOH   240 740 214 HOH   HOH A . 
C 3 HOH   241 741 245 HOH   HOH A . 
C 3 HOH   242 742 262 HOH   HOH A . 
C 3 HOH   243 743 308 HOH   HOH A . 
C 3 HOH   244 744 277 HOH   HOH A . 
C 3 HOH   245 745 294 HOH   HOH A . 
C 3 HOH   246 746 274 HOH   HOH A . 
C 3 HOH   247 747 37  HOH   HOH A . 
C 3 HOH   248 748 243 HOH   HOH A . 
C 3 HOH   249 749 257 HOH   HOH A . 
C 3 HOH   250 750 283 HOH   HOH A . 
C 3 HOH   251 751 97  HOH   HOH A . 
C 3 HOH   252 752 307 HOH   HOH A . 
C 3 HOH   253 753 223 HOH   HOH A . 
C 3 HOH   254 754 95  HOH   HOH A . 
C 3 HOH   255 755 169 HOH   HOH A . 
C 3 HOH   256 756 263 HOH   HOH A . 
C 3 HOH   257 757 49  HOH   HOH A . 
C 3 HOH   258 758 123 HOH   HOH A . 
C 3 HOH   259 759 261 HOH   HOH A . 
C 3 HOH   260 760 275 HOH   HOH A . 
C 3 HOH   261 761 193 HOH   HOH A . 
C 3 HOH   262 762 284 HOH   HOH A . 
C 3 HOH   263 763 232 HOH   HOH A . 
C 3 HOH   264 764 322 HOH   HOH A . 
C 3 HOH   265 765 81  HOH   HOH A . 
C 3 HOH   266 766 280 HOH   HOH A . 
C 3 HOH   267 767 131 HOH   HOH A . 
C 3 HOH   268 768 86  HOH   HOH A . 
C 3 HOH   269 769 239 HOH   HOH A . 
C 3 HOH   270 770 313 HOH   HOH A . 
C 3 HOH   271 771 172 HOH   HOH A . 
C 3 HOH   272 772 208 HOH   HOH A . 
C 3 HOH   273 773 297 HOH   HOH A . 
C 3 HOH   274 774 306 HOH   HOH A . 
C 3 HOH   275 775 205 HOH   HOH A . 
C 3 HOH   276 776 260 HOH   HOH A . 
C 3 HOH   277 777 289 HOH   HOH A . 
C 3 HOH   278 778 252 HOH   HOH A . 
C 3 HOH   279 779 158 HOH   HOH A . 
C 3 HOH   280 780 250 HOH   HOH A . 
C 3 HOH   281 781 160 HOH   HOH A . 
C 3 HOH   282 782 218 HOH   HOH A . 
C 3 HOH   283 783 282 HOH   HOH A . 
C 3 HOH   284 784 113 HOH   HOH A . 
C 3 HOH   285 785 276 HOH   HOH A . 
C 3 HOH   286 786 210 HOH   HOH A . 
C 3 HOH   287 787 254 HOH   HOH A . 
C 3 HOH   288 788 36  HOH   HOH A . 
C 3 HOH   289 789 199 HOH   HOH A . 
C 3 HOH   290 790 273 HOH   HOH A . 
C 3 HOH   291 791 305 HOH   HOH A . 
C 3 HOH   292 792 192 HOH   HOH A . 
C 3 HOH   293 793 152 HOH   HOH A . 
C 3 HOH   294 794 189 HOH   HOH A . 
C 3 HOH   295 795 303 HOH   HOH A . 
C 3 HOH   296 796 292 HOH   HOH A . 
C 3 HOH   297 797 247 HOH   HOH A . 
C 3 HOH   298 798 318 HOH   HOH A . 
C 3 HOH   299 799 211 HOH   HOH A . 
C 3 HOH   300 800 98  HOH   HOH A . 
C 3 HOH   301 801 228 HOH   HOH A . 
C 3 HOH   302 802 177 HOH   HOH A . 
C 3 HOH   303 803 149 HOH   HOH A . 
C 3 HOH   304 804 224 HOH   HOH A . 
C 3 HOH   305 805 184 HOH   HOH A . 
C 3 HOH   306 806 234 HOH   HOH A . 
C 3 HOH   307 807 76  HOH   HOH A . 
C 3 HOH   308 808 301 HOH   HOH A . 
C 3 HOH   309 809 32  HOH   HOH A . 
C 3 HOH   310 810 278 HOH   HOH A . 
C 3 HOH   311 811 244 HOH   HOH A . 
C 3 HOH   312 812 25  HOH   HOH A . 
C 3 HOH   313 813 200 HOH   HOH A . 
C 3 HOH   314 814 240 HOH   HOH A . 
C 3 HOH   315 815 290 HOH   HOH A . 
C 3 HOH   316 816 235 HOH   HOH A . 
C 3 HOH   317 817 94  HOH   HOH A . 
C 3 HOH   318 818 248 HOH   HOH A . 
C 3 HOH   319 819 194 HOH   HOH A . 
C 3 HOH   320 820 242 HOH   HOH A . 
C 3 HOH   321 821 227 HOH   HOH A . 
C 3 HOH   322 822 286 HOH   HOH A . 
C 3 HOH   323 823 315 HOH   HOH A . 
C 3 HOH   324 824 204 HOH   HOH A . 
C 3 HOH   325 825 183 HOH   HOH A . 
C 3 HOH   326 826 298 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 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? 1.18.2_3874 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT    ? ? ? .           3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? 'PROTEUM PLUS' ? ? ? .           4 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless        ? ? ? .           5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX         ? ? ? .           6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.936 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BQG 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.415 
_cell.length_a_esd                 ? 
_cell.length_b                     80.863 
_cell.length_b_esd                 ? 
_cell.length_c                     89.869 
_cell.length_c_esd                 ? 
_cell.volume                       370903.182 
_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                         9BQG 
_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                   9BQG 
_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         2021-05-31 
_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                          14.48 
_reflns.entry_id                                       9BQG 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.65 
_reflns.d_resolution_low                               42.16 
_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                                     43276 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.42 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.29 
_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                                0.07639 
_reflns.pdbx_Rpim_I_all                                0.05402 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.05402 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.65 
_reflns_shell.d_res_low                                     1.709 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.03 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4171 
_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                               0.5867 
_reflns_shell.pdbx_Rpim_I_all                               0.4149 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.86 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          95.02 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.4149 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               23.48 
_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                                 9BQG 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.65 
_refine.ls_d_res_low                             42.16 
_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                     43197 
_refine.ls_number_reflns_R_free                  2124 
_refine.ls_number_reflns_R_work                  41073 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.43 
_refine.ls_percent_reflns_R_free                 4.92 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2383 
_refine.ls_R_factor_R_free                       0.2746 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2366 
_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                 30.7745 
_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                            0.2286 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.65 
_refine_hist.d_res_low                        42.16 
_refine_hist.number_atoms_solvent             326 
_refine_hist.number_atoms_total               2722 
_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         33 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0078  ? 2451 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1094  ? 3333 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0586  ? 376  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0075  ? 432  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.2254 ? 349  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.65 1.69  . . 148 2604 95.49 . . . . 0.3884 . . . . . . . . . . . 0.3661 
'X-RAY DIFFRACTION' 1.69 1.73  . . 145 2652 95.49 . . . . 0.3417 . . . . . . . . . . . 0.3373 
'X-RAY DIFFRACTION' 1.73 1.78  . . 131 2646 95.53 . . . . 0.3126 . . . . . . . . . . . 0.3851 
'X-RAY DIFFRACTION' 1.78 1.83  . . 167 2670 96.89 . . . . 0.2929 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 1.83 1.89  . . 158 2691 98.11 . . . . 0.2792 . . . . . . . . . . . 0.3471 
'X-RAY DIFFRACTION' 1.89 1.96  . . 135 2733 98.52 . . . . 0.2841 . . . . . . . . . . . 0.3217 
'X-RAY DIFFRACTION' 1.96 2.03  . . 150 2753 99.35 . . . . 0.2688 . . . . . . . . . . . 0.3047 
'X-RAY DIFFRACTION' 2.03 2.13  . . 149 2795 99.66 . . . . 0.2699 . . . . . . . . . . . 0.3342 
'X-RAY DIFFRACTION' 2.13 2.24  . . 131 2753 99.65 . . . . 0.2711 . . . . . . . . . . . 0.3258 
'X-RAY DIFFRACTION' 2.24 2.38  . . 130 2785 99.62 . . . . 0.2659 . . . . . . . . . . . 0.3001 
'X-RAY DIFFRACTION' 2.38 2.56  . . 146 2769 99.69 . . . . 0.2580 . . . . . . . . . . . 0.3055 
'X-RAY DIFFRACTION' 2.56 2.82  . . 142 2774 99.52 . . . . 0.2454 . . . . . . . . . . . 0.2674 
'X-RAY DIFFRACTION' 2.82 3.23  . . 143 2790 99.80 . . . . 0.2152 . . . . . . . . . . . 0.2623 
'X-RAY DIFFRACTION' 3.23 4.07  . . 126 2797 99.56 . . . . 0.1813 . . . . . . . . . . . 0.2354 
'X-RAY DIFFRACTION' 4.07 42.16 . . 123 2861 99.57 . . . . 0.1707 . . . . . . . . . . . 0.1684 
# 
_struct.entry_id                     9BQG 
_struct.title                        'Structure of the SARS-CoV-2 main protease in complex with inhibitor k68' 
_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        9BQG 
_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              9BQG 
_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)' 3280  ? 
1 MORE         -13   ? 
1 'SSA (A^2)'  24760 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_455 -x-1,y,-z -1.0000000000 0.0000000000 0.0000000000 -51.4150000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 GLU A 47  ? ASN A 51  ? GLU A 47  ASN A 51  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? TYR A 237 ? THR A 226 TYR A 237 1 ? 12 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            covale1 
_struct_conn.conn_type_id                  covale 
_struct_conn.pdbx_leaving_atom_flag        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           A1AQ3 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           C8 
_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            A1AQ3 
_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               1.812 
_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                      A1AQ3 
_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                       A1AQ3 
_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               C8 
_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                        A1AQ3 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA2 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA2 3 VAL A 148 ? ASP A 153 ? VAL A 148 ASP A 153 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 LYS A 100 ? PHE A 103 ? LYS A 100 PHE A 103 
AA3 2 CYS A 156 ? GLU A 166 ? CYS A 156 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 73  ? O VAL A 73  N ALA A 70  ? N ALA A 70  
AA1 2 3 O GLN A 69  ? O GLN A 69  N GLN A 19  ? N GLN A 19  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O LYS A 90  ? O LYS A 90  N ILE A 78  ? N ILE A 78  
AA2 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N VAL A 114 ? N VAL A 114 O TYR A 126 ? O TYR A 126 
AA3 1 2 N LYS A 100 ? N LYS A 100 O VAL A 157 ? O VAL A 157 
AA3 2 3 N MET A 162 ? N MET A 162 O THR A 175 ? O THR A 175 
# 
_pdbx_entry_details.entry_id                   9BQG 
_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 741 ? ? O A HOH 803 ? ? 1.85 
2  1 O   A HOH 649 ? ? O A HOH 750 ? ? 1.86 
3  1 O   A HOH 779 ? ? O A HOH 818 ? ? 1.88 
4  1 OD2 A ASP 33  ? ? O A HOH 501 ? ? 1.91 
5  1 O   A HOH 606 ? ? O A HOH 780 ? ? 1.94 
6  1 OH  A TYR 126 ? ? O A HOH 502 ? ? 1.99 
7  1 O   A HOH 664 ? ? O A HOH 811 ? ? 2.05 
8  1 O   A HOH 542 ? ? O A HOH 772 ? ? 2.07 
9  1 O   A HOH 779 ? ? O A HOH 788 ? ? 2.08 
10 1 O   A HOH 570 ? ? O A HOH 682 ? ? 2.11 
11 1 O   A ALA 194 ? ? O A HOH 503 ? ? 2.11 
12 1 O   A HOH 695 ? ? O A HOH 773 ? ? 2.12 
13 1 O   A HOH 560 ? ? O A HOH 775 ? ? 2.14 
14 1 O   A HOH 629 ? ? O A HOH 778 ? ? 2.17 
15 1 OE2 A GLU 166 ? ? O A HOH 504 ? ? 2.17 
16 1 O   A HOH 644 ? ? O A HOH 796 ? ? 2.17 
17 1 NZ  A LYS 102 ? ? O A HOH 505 ? ? 2.18 
# 
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 692 ? ? 1_555 O A HOH 698 ? ? 2_455 1.97 
2 1 O A HOH 685 ? ? 1_555 O A HOH 692 ? ? 2_455 2.03 
3 1 O A HOH 738 ? ? 1_555 O A HOH 787 ? ? 2_455 2.10 
4 1 O A HOH 786 ? ? 1_555 O A HOH 818 ? ? 2_555 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 33  ? ? 51.20   -131.88 
2 1 HIS A 41  ? ? -69.26  0.42    
3 1 MET A 49  ? ? -82.84  41.29   
4 1 ASN A 51  ? ? -173.07 71.57   
5 1 ASN A 72  ? ? -98.30  32.91   
6 1 ASN A 84  ? ? 53.13   -118.90 
7 1 TYR A 154 ? ? 43.99   -102.56 
8 1 ASP A 187 ? ? -94.95  55.63   
9 1 SER A 301 ? ? -147.27 -46.10  
# 
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 595 ? C HOH . 
2 1 A HOH 702 ? C HOH . 
3 1 A HOH 718 ? C HOH . 
4 1 A HOH 805 ? C HOH . 
5 1 A HOH 821 ? C HOH . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 -x,y,-z             
3 x+1/2,y+1/2,z+1/2   
4 -x+1/2,y+1/2,-z+1/2 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -12.8753811574 
_pdbx_refine_tls.origin_y         -14.9966964909 
_pdbx_refine_tls.origin_z         -1.08074887317 
_pdbx_refine_tls.T[1][1]          0.0566789147169 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.000293539666477 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0137405065465 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.0857735725738 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.000924393985887 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.0633416379631 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.88956910368 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.231096820855 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.302597611631 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.48268705895 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.652604738588 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.40051543345 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0319490201178 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.00796321221521 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0272852595452 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0279806073585 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0281195891381 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.00418821617429 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.0311687773095 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.0108756042586 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0107056701055 
_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_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 825 ? 5.82 . 
2 1 O ? A HOH 826 ? 6.71 . 
# 
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 
A1AQ3 C1   C N N 1   
A1AQ3 C10  C N N 2   
A1AQ3 C11  C N N 3   
A1AQ3 C12  C N N 4   
A1AQ3 C13  C N N 5   
A1AQ3 C14  C N S 6   
A1AQ3 C15  C N N 7   
A1AQ3 C16  C N R 8   
A1AQ3 C17  C N S 9   
A1AQ3 C18  C N N 10  
A1AQ3 C19  C N N 11  
A1AQ3 C20  C N S 12  
A1AQ3 C21  C N N 13  
A1AQ3 C22  C N N 14  
A1AQ3 C23  C N N 15  
A1AQ3 C24  C N N 16  
A1AQ3 C3   C Y N 17  
A1AQ3 C34  C N N 18  
A1AQ3 C4   C Y N 19  
A1AQ3 C5   C Y N 20  
A1AQ3 C6   C Y N 21  
A1AQ3 C7   C Y N 22  
A1AQ3 C8   C N N 23  
A1AQ3 C9   C Y N 24  
A1AQ3 N13  N N N 25  
A1AQ3 N16  N N N 26  
A1AQ3 N23  N N N 27  
A1AQ3 O11  O N N 28  
A1AQ3 O26  O N N 29  
A1AQ3 O3   O N N 30  
A1AQ3 O33  O N N 31  
A1AQ3 O38  O N N 32  
A1AQ3 O9   O N N 33  
A1AQ3 H12  H N N 34  
A1AQ3 H1   H N N 35  
A1AQ3 H11  H N N 36  
A1AQ3 H111 H N N 37  
A1AQ3 H112 H N N 38  
A1AQ3 H13  H N N 39  
A1AQ3 H131 H N N 40  
A1AQ3 H14  H N N 41  
A1AQ3 H16  H N N 42  
A1AQ3 H17  H N N 43  
A1AQ3 H18  H N N 44  
A1AQ3 H182 H N N 45  
A1AQ3 H181 H N N 46  
A1AQ3 H191 H N N 47  
A1AQ3 H19  H N N 48  
A1AQ3 H20  H N N 49  
A1AQ3 H211 H N N 50  
A1AQ3 H21  H N N 51  
A1AQ3 H22  H N N 52  
A1AQ3 H221 H N N 53  
A1AQ3 H232 H N N 54  
A1AQ3 H23  H N N 55  
A1AQ3 H231 H N N 56  
A1AQ3 H341 H N N 57  
A1AQ3 H34  H N N 58  
A1AQ3 H4   H N N 59  
A1AQ3 H5   H N N 60  
A1AQ3 H6   H N N 61  
A1AQ3 H7   H N N 62  
A1AQ3 H81  H N N 63  
A1AQ3 H8   H N N 64  
A1AQ3 H9   H N N 65  
A1AQ3 HN16 H N N 66  
A1AQ3 HN23 H N N 67  
A1AQ3 HO9  H N N 68  
ALA   N    N N N 69  
ALA   CA   C N S 70  
ALA   C    C N N 71  
ALA   O    O N N 72  
ALA   CB   C N N 73  
ALA   OXT  O N N 74  
ALA   H    H N N 75  
ALA   H2   H N N 76  
ALA   HA   H N N 77  
ALA   HB1  H N N 78  
ALA   HB2  H N N 79  
ALA   HB3  H N N 80  
ALA   HXT  H N N 81  
ARG   N    N N N 82  
ARG   CA   C N S 83  
ARG   C    C N N 84  
ARG   O    O N N 85  
ARG   CB   C N N 86  
ARG   CG   C N N 87  
ARG   CD   C N N 88  
ARG   NE   N N N 89  
ARG   CZ   C N N 90  
ARG   NH1  N N N 91  
ARG   NH2  N N N 92  
ARG   OXT  O N N 93  
ARG   H    H N N 94  
ARG   H2   H N N 95  
ARG   HA   H N N 96  
ARG   HB2  H N N 97  
ARG   HB3  H N N 98  
ARG   HG2  H N N 99  
ARG   HG3  H N N 100 
ARG   HD2  H N N 101 
ARG   HD3  H N N 102 
ARG   HE   H N N 103 
ARG   HH11 H N N 104 
ARG   HH12 H N N 105 
ARG   HH21 H N N 106 
ARG   HH22 H N N 107 
ARG   HXT  H N N 108 
ASN   N    N N N 109 
ASN   CA   C N S 110 
ASN   C    C N N 111 
ASN   O    O N N 112 
ASN   CB   C N N 113 
ASN   CG   C N N 114 
ASN   OD1  O N N 115 
ASN   ND2  N N N 116 
ASN   OXT  O N N 117 
ASN   H    H N N 118 
ASN   H2   H N N 119 
ASN   HA   H N N 120 
ASN   HB2  H N N 121 
ASN   HB3  H N N 122 
ASN   HD21 H N N 123 
ASN   HD22 H N N 124 
ASN   HXT  H N N 125 
ASP   N    N N N 126 
ASP   CA   C N S 127 
ASP   C    C N N 128 
ASP   O    O N N 129 
ASP   CB   C N N 130 
ASP   CG   C N N 131 
ASP   OD1  O N N 132 
ASP   OD2  O N N 133 
ASP   OXT  O N N 134 
ASP   H    H N N 135 
ASP   H2   H N N 136 
ASP   HA   H N N 137 
ASP   HB2  H N N 138 
ASP   HB3  H N N 139 
ASP   HD2  H N N 140 
ASP   HXT  H N N 141 
CYS   N    N N N 142 
CYS   CA   C N R 143 
CYS   C    C N N 144 
CYS   O    O N N 145 
CYS   CB   C N N 146 
CYS   SG   S N N 147 
CYS   OXT  O N N 148 
CYS   H    H N N 149 
CYS   H2   H N N 150 
CYS   HA   H N N 151 
CYS   HB2  H N N 152 
CYS   HB3  H N N 153 
CYS   HG   H N N 154 
CYS   HXT  H N N 155 
GLN   N    N N N 156 
GLN   CA   C N S 157 
GLN   C    C N N 158 
GLN   O    O N N 159 
GLN   CB   C N N 160 
GLN   CG   C N N 161 
GLN   CD   C N N 162 
GLN   OE1  O N N 163 
GLN   NE2  N N N 164 
GLN   OXT  O N N 165 
GLN   H    H N N 166 
GLN   H2   H N N 167 
GLN   HA   H N N 168 
GLN   HB2  H N N 169 
GLN   HB3  H N N 170 
GLN   HG2  H N N 171 
GLN   HG3  H N N 172 
GLN   HE21 H N N 173 
GLN   HE22 H N N 174 
GLN   HXT  H N N 175 
GLU   N    N N N 176 
GLU   CA   C N S 177 
GLU   C    C N N 178 
GLU   O    O N N 179 
GLU   CB   C N N 180 
GLU   CG   C N N 181 
GLU   CD   C N N 182 
GLU   OE1  O N N 183 
GLU   OE2  O N N 184 
GLU   OXT  O N N 185 
GLU   H    H N N 186 
GLU   H2   H N N 187 
GLU   HA   H N N 188 
GLU   HB2  H N N 189 
GLU   HB3  H N N 190 
GLU   HG2  H N N 191 
GLU   HG3  H N N 192 
GLU   HE2  H N N 193 
GLU   HXT  H N N 194 
GLY   N    N N N 195 
GLY   CA   C N N 196 
GLY   C    C N N 197 
GLY   O    O N N 198 
GLY   OXT  O N N 199 
GLY   H    H N N 200 
GLY   H2   H N N 201 
GLY   HA2  H N N 202 
GLY   HA3  H N N 203 
GLY   HXT  H N N 204 
HIS   N    N N N 205 
HIS   CA   C N S 206 
HIS   C    C N N 207 
HIS   O    O N N 208 
HIS   CB   C N N 209 
HIS   CG   C Y N 210 
HIS   ND1  N Y N 211 
HIS   CD2  C Y N 212 
HIS   CE1  C Y N 213 
HIS   NE2  N Y N 214 
HIS   OXT  O N N 215 
HIS   H    H N N 216 
HIS   H2   H N N 217 
HIS   HA   H N N 218 
HIS   HB2  H N N 219 
HIS   HB3  H N N 220 
HIS   HD1  H N N 221 
HIS   HD2  H N N 222 
HIS   HE1  H N N 223 
HIS   HE2  H N N 224 
HIS   HXT  H N N 225 
HOH   O    O N N 226 
HOH   H1   H N N 227 
HOH   H2   H N N 228 
ILE   N    N N N 229 
ILE   CA   C N S 230 
ILE   C    C N N 231 
ILE   O    O N N 232 
ILE   CB   C N S 233 
ILE   CG1  C N N 234 
ILE   CG2  C N N 235 
ILE   CD1  C N N 236 
ILE   OXT  O N N 237 
ILE   H    H N N 238 
ILE   H2   H N N 239 
ILE   HA   H N N 240 
ILE   HB   H N N 241 
ILE   HG12 H N N 242 
ILE   HG13 H N N 243 
ILE   HG21 H N N 244 
ILE   HG22 H N N 245 
ILE   HG23 H N N 246 
ILE   HD11 H N N 247 
ILE   HD12 H N N 248 
ILE   HD13 H N N 249 
ILE   HXT  H N N 250 
LEU   N    N N N 251 
LEU   CA   C N S 252 
LEU   C    C N N 253 
LEU   O    O N N 254 
LEU   CB   C N N 255 
LEU   CG   C N N 256 
LEU   CD1  C N N 257 
LEU   CD2  C N N 258 
LEU   OXT  O N N 259 
LEU   H    H N N 260 
LEU   H2   H N N 261 
LEU   HA   H N N 262 
LEU   HB2  H N N 263 
LEU   HB3  H N N 264 
LEU   HG   H N N 265 
LEU   HD11 H N N 266 
LEU   HD12 H N N 267 
LEU   HD13 H N N 268 
LEU   HD21 H N N 269 
LEU   HD22 H N N 270 
LEU   HD23 H N N 271 
LEU   HXT  H N N 272 
LYS   N    N N N 273 
LYS   CA   C N S 274 
LYS   C    C N N 275 
LYS   O    O N N 276 
LYS   CB   C N N 277 
LYS   CG   C N N 278 
LYS   CD   C N N 279 
LYS   CE   C N N 280 
LYS   NZ   N N N 281 
LYS   OXT  O N N 282 
LYS   H    H N N 283 
LYS   H2   H N N 284 
LYS   HA   H N N 285 
LYS   HB2  H N N 286 
LYS   HB3  H N N 287 
LYS   HG2  H N N 288 
LYS   HG3  H N N 289 
LYS   HD2  H N N 290 
LYS   HD3  H N N 291 
LYS   HE2  H N N 292 
LYS   HE3  H N N 293 
LYS   HZ1  H N N 294 
LYS   HZ2  H N N 295 
LYS   HZ3  H N N 296 
LYS   HXT  H N N 297 
MET   N    N N N 298 
MET   CA   C N S 299 
MET   C    C N N 300 
MET   O    O N N 301 
MET   CB   C N N 302 
MET   CG   C N N 303 
MET   SD   S N N 304 
MET   CE   C N N 305 
MET   OXT  O N N 306 
MET   H    H N N 307 
MET   H2   H N N 308 
MET   HA   H N N 309 
MET   HB2  H N N 310 
MET   HB3  H N N 311 
MET   HG2  H N N 312 
MET   HG3  H N N 313 
MET   HE1  H N N 314 
MET   HE2  H N N 315 
MET   HE3  H N N 316 
MET   HXT  H N N 317 
PHE   N    N N N 318 
PHE   CA   C N S 319 
PHE   C    C N N 320 
PHE   O    O N N 321 
PHE   CB   C N N 322 
PHE   CG   C Y N 323 
PHE   CD1  C Y N 324 
PHE   CD2  C Y N 325 
PHE   CE1  C Y N 326 
PHE   CE2  C Y N 327 
PHE   CZ   C Y N 328 
PHE   OXT  O N N 329 
PHE   H    H N N 330 
PHE   H2   H N N 331 
PHE   HA   H N N 332 
PHE   HB2  H N N 333 
PHE   HB3  H N N 334 
PHE   HD1  H N N 335 
PHE   HD2  H N N 336 
PHE   HE1  H N N 337 
PHE   HE2  H N N 338 
PHE   HZ   H N N 339 
PHE   HXT  H N N 340 
PRO   N    N N N 341 
PRO   CA   C N S 342 
PRO   C    C N N 343 
PRO   O    O N N 344 
PRO   CB   C N N 345 
PRO   CG   C N N 346 
PRO   CD   C N N 347 
PRO   OXT  O N N 348 
PRO   H    H N N 349 
PRO   HA   H N N 350 
PRO   HB2  H N N 351 
PRO   HB3  H N N 352 
PRO   HG2  H N N 353 
PRO   HG3  H N N 354 
PRO   HD2  H N N 355 
PRO   HD3  H N N 356 
PRO   HXT  H N N 357 
SER   N    N N N 358 
SER   CA   C N S 359 
SER   C    C N N 360 
SER   O    O N N 361 
SER   CB   C N N 362 
SER   OG   O N N 363 
SER   OXT  O N N 364 
SER   H    H N N 365 
SER   H2   H N N 366 
SER   HA   H N N 367 
SER   HB2  H N N 368 
SER   HB3  H N N 369 
SER   HG   H N N 370 
SER   HXT  H N N 371 
THR   N    N N N 372 
THR   CA   C N S 373 
THR   C    C N N 374 
THR   O    O N N 375 
THR   CB   C N R 376 
THR   OG1  O N N 377 
THR   CG2  C N N 378 
THR   OXT  O N N 379 
THR   H    H N N 380 
THR   H2   H N N 381 
THR   HA   H N N 382 
THR   HB   H N N 383 
THR   HG1  H N N 384 
THR   HG21 H N N 385 
THR   HG22 H N N 386 
THR   HG23 H N N 387 
THR   HXT  H N N 388 
TRP   N    N N N 389 
TRP   CA   C N S 390 
TRP   C    C N N 391 
TRP   O    O N N 392 
TRP   CB   C N N 393 
TRP   CG   C Y N 394 
TRP   CD1  C Y N 395 
TRP   CD2  C Y N 396 
TRP   NE1  N Y N 397 
TRP   CE2  C Y N 398 
TRP   CE3  C Y N 399 
TRP   CZ2  C Y N 400 
TRP   CZ3  C Y N 401 
TRP   CH2  C Y N 402 
TRP   OXT  O N N 403 
TRP   H    H N N 404 
TRP   H2   H N N 405 
TRP   HA   H N N 406 
TRP   HB2  H N N 407 
TRP   HB3  H N N 408 
TRP   HD1  H N N 409 
TRP   HE1  H N N 410 
TRP   HE3  H N N 411 
TRP   HZ2  H N N 412 
TRP   HZ3  H N N 413 
TRP   HH2  H N N 414 
TRP   HXT  H N N 415 
TYR   N    N N N 416 
TYR   CA   C N S 417 
TYR   C    C N N 418 
TYR   O    O N N 419 
TYR   CB   C N N 420 
TYR   CG   C Y N 421 
TYR   CD1  C Y N 422 
TYR   CD2  C Y N 423 
TYR   CE1  C Y N 424 
TYR   CE2  C Y N 425 
TYR   CZ   C Y N 426 
TYR   OH   O N N 427 
TYR   OXT  O N N 428 
TYR   H    H N N 429 
TYR   H2   H N N 430 
TYR   HA   H N N 431 
TYR   HB2  H N N 432 
TYR   HB3  H N N 433 
TYR   HD1  H N N 434 
TYR   HD2  H N N 435 
TYR   HE1  H N N 436 
TYR   HE2  H N N 437 
TYR   HH   H N N 438 
TYR   HXT  H N N 439 
VAL   N    N N N 440 
VAL   CA   C N S 441 
VAL   C    C N N 442 
VAL   O    O N N 443 
VAL   CB   C N N 444 
VAL   CG1  C N N 445 
VAL   CG2  C N N 446 
VAL   OXT  O N N 447 
VAL   H    H N N 448 
VAL   H2   H N N 449 
VAL   HA   H N N 450 
VAL   HB   H N N 451 
VAL   HG11 H N N 452 
VAL   HG12 H N N 453 
VAL   HG13 H N N 454 
VAL   HG21 H N N 455 
VAL   HG22 H N N 456 
VAL   HG23 H N N 457 
VAL   HXT  H N N 458 
# 
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 
A1AQ3 C6  C5   doub Y N 1   
A1AQ3 C6  C7   sing Y N 2   
A1AQ3 C5  C4   sing Y N 3   
A1AQ3 C4  C3   doub Y N 4   
A1AQ3 C7  C9   doub Y N 5   
A1AQ3 C9  C3   sing Y N 6   
A1AQ3 C3  C1   sing N N 7   
A1AQ3 C1  O11  sing N N 8   
A1AQ3 O11 C12  sing N N 9   
A1AQ3 O33 C12  doub N N 10  
A1AQ3 C12 N13  sing N N 11  
A1AQ3 N13 C14  sing N N 12  
A1AQ3 N13 C13  sing N N 13  
A1AQ3 C34 C14  sing N N 14  
A1AQ3 C14 C15  sing N N 15  
A1AQ3 C16 C34  sing N N 16  
A1AQ3 C13 C16  sing N N 17  
A1AQ3 O3  C16  sing N N 18  
A1AQ3 O38 C15  doub N N 19  
A1AQ3 C15 N16  sing N N 20  
A1AQ3 N16 C17  sing N N 21  
A1AQ3 C8  C17  sing N N 22  
A1AQ3 C17 C19  sing N N 23  
A1AQ3 O9  C8   sing N N 24  
A1AQ3 C19 C20  sing N N 25  
A1AQ3 C20 C21  sing N N 26  
A1AQ3 C20 C24  sing N N 27  
A1AQ3 C21 C22  sing N N 28  
A1AQ3 C22 N23  sing N N 29  
A1AQ3 N23 C24  sing N N 30  
A1AQ3 C24 O26  doub N N 31  
A1AQ3 C10 O3   sing N N 32  
A1AQ3 C11 C10  sing N N 33  
A1AQ3 C18 C10  sing N N 34  
A1AQ3 C23 C10  sing N N 35  
A1AQ3 C1  H12  sing N N 36  
A1AQ3 C1  H1   sing N N 37  
A1AQ3 C11 H11  sing N N 38  
A1AQ3 C11 H111 sing N N 39  
A1AQ3 C11 H112 sing N N 40  
A1AQ3 C13 H13  sing N N 41  
A1AQ3 C13 H131 sing N N 42  
A1AQ3 C14 H14  sing N N 43  
A1AQ3 C16 H16  sing N N 44  
A1AQ3 C17 H17  sing N N 45  
A1AQ3 C18 H18  sing N N 46  
A1AQ3 C18 H182 sing N N 47  
A1AQ3 C18 H181 sing N N 48  
A1AQ3 C19 H191 sing N N 49  
A1AQ3 C19 H19  sing N N 50  
A1AQ3 C20 H20  sing N N 51  
A1AQ3 C21 H211 sing N N 52  
A1AQ3 C21 H21  sing N N 53  
A1AQ3 C22 H22  sing N N 54  
A1AQ3 C22 H221 sing N N 55  
A1AQ3 C23 H232 sing N N 56  
A1AQ3 C23 H23  sing N N 57  
A1AQ3 C23 H231 sing N N 58  
A1AQ3 C34 H341 sing N N 59  
A1AQ3 C34 H34  sing N N 60  
A1AQ3 C4  H4   sing N N 61  
A1AQ3 C5  H5   sing N N 62  
A1AQ3 C6  H6   sing N N 63  
A1AQ3 C7  H7   sing N N 64  
A1AQ3 C8  H81  sing N N 65  
A1AQ3 C8  H8   sing N N 66  
A1AQ3 C9  H9   sing N N 67  
A1AQ3 N16 HN16 sing N N 68  
A1AQ3 N23 HN23 sing N N 69  
A1AQ3 O9  HO9  sing N N 70  
ALA   N   CA   sing N N 71  
ALA   N   H    sing N N 72  
ALA   N   H2   sing N N 73  
ALA   CA  C    sing N N 74  
ALA   CA  CB   sing N N 75  
ALA   CA  HA   sing N N 76  
ALA   C   O    doub N N 77  
ALA   C   OXT  sing N N 78  
ALA   CB  HB1  sing N N 79  
ALA   CB  HB2  sing N N 80  
ALA   CB  HB3  sing N N 81  
ALA   OXT HXT  sing N N 82  
ARG   N   CA   sing N N 83  
ARG   N   H    sing N N 84  
ARG   N   H2   sing N N 85  
ARG   CA  C    sing N N 86  
ARG   CA  CB   sing N N 87  
ARG   CA  HA   sing N N 88  
ARG   C   O    doub N N 89  
ARG   C   OXT  sing N N 90  
ARG   CB  CG   sing N N 91  
ARG   CB  HB2  sing N N 92  
ARG   CB  HB3  sing N N 93  
ARG   CG  CD   sing N N 94  
ARG   CG  HG2  sing N N 95  
ARG   CG  HG3  sing N N 96  
ARG   CD  NE   sing N N 97  
ARG   CD  HD2  sing N N 98  
ARG   CD  HD3  sing N N 99  
ARG   NE  CZ   sing N N 100 
ARG   NE  HE   sing N N 101 
ARG   CZ  NH1  sing N N 102 
ARG   CZ  NH2  doub N N 103 
ARG   NH1 HH11 sing N N 104 
ARG   NH1 HH12 sing N N 105 
ARG   NH2 HH21 sing N N 106 
ARG   NH2 HH22 sing N N 107 
ARG   OXT HXT  sing N N 108 
ASN   N   CA   sing N N 109 
ASN   N   H    sing N N 110 
ASN   N   H2   sing N N 111 
ASN   CA  C    sing N N 112 
ASN   CA  CB   sing N N 113 
ASN   CA  HA   sing N N 114 
ASN   C   O    doub N N 115 
ASN   C   OXT  sing N N 116 
ASN   CB  CG   sing N N 117 
ASN   CB  HB2  sing N N 118 
ASN   CB  HB3  sing N N 119 
ASN   CG  OD1  doub N N 120 
ASN   CG  ND2  sing N N 121 
ASN   ND2 HD21 sing N N 122 
ASN   ND2 HD22 sing N N 123 
ASN   OXT HXT  sing N N 124 
ASP   N   CA   sing N N 125 
ASP   N   H    sing N N 126 
ASP   N   H2   sing N N 127 
ASP   CA  C    sing N N 128 
ASP   CA  CB   sing N N 129 
ASP   CA  HA   sing N N 130 
ASP   C   O    doub N N 131 
ASP   C   OXT  sing N N 132 
ASP   CB  CG   sing N N 133 
ASP   CB  HB2  sing N N 134 
ASP   CB  HB3  sing N N 135 
ASP   CG  OD1  doub N N 136 
ASP   CG  OD2  sing N N 137 
ASP   OD2 HD2  sing N N 138 
ASP   OXT HXT  sing N N 139 
CYS   N   CA   sing N N 140 
CYS   N   H    sing N N 141 
CYS   N   H2   sing N N 142 
CYS   CA  C    sing N N 143 
CYS   CA  CB   sing N N 144 
CYS   CA  HA   sing N N 145 
CYS   C   O    doub N N 146 
CYS   C   OXT  sing N N 147 
CYS   CB  SG   sing N N 148 
CYS   CB  HB2  sing N N 149 
CYS   CB  HB3  sing N N 150 
CYS   SG  HG   sing N N 151 
CYS   OXT HXT  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
HOH   O   H1   sing N N 220 
HOH   O   H2   sing N N 221 
ILE   N   CA   sing N N 222 
ILE   N   H    sing N N 223 
ILE   N   H2   sing N N 224 
ILE   CA  C    sing N N 225 
ILE   CA  CB   sing N N 226 
ILE   CA  HA   sing N N 227 
ILE   C   O    doub N N 228 
ILE   C   OXT  sing N N 229 
ILE   CB  CG1  sing N N 230 
ILE   CB  CG2  sing N N 231 
ILE   CB  HB   sing N N 232 
ILE   CG1 CD1  sing N N 233 
ILE   CG1 HG12 sing N N 234 
ILE   CG1 HG13 sing N N 235 
ILE   CG2 HG21 sing N N 236 
ILE   CG2 HG22 sing N N 237 
ILE   CG2 HG23 sing N N 238 
ILE   CD1 HD11 sing N N 239 
ILE   CD1 HD12 sing N N 240 
ILE   CD1 HD13 sing N N 241 
ILE   OXT HXT  sing N N 242 
LEU   N   CA   sing N N 243 
LEU   N   H    sing N N 244 
LEU   N   H2   sing N N 245 
LEU   CA  C    sing N N 246 
LEU   CA  CB   sing N N 247 
LEU   CA  HA   sing N N 248 
LEU   C   O    doub N N 249 
LEU   C   OXT  sing N N 250 
LEU   CB  CG   sing N N 251 
LEU   CB  HB2  sing N N 252 
LEU   CB  HB3  sing N N 253 
LEU   CG  CD1  sing N N 254 
LEU   CG  CD2  sing N N 255 
LEU   CG  HG   sing N N 256 
LEU   CD1 HD11 sing N N 257 
LEU   CD1 HD12 sing N N 258 
LEU   CD1 HD13 sing N N 259 
LEU   CD2 HD21 sing N N 260 
LEU   CD2 HD22 sing N N 261 
LEU   CD2 HD23 sing N N 262 
LEU   OXT HXT  sing N N 263 
LYS   N   CA   sing N N 264 
LYS   N   H    sing N N 265 
LYS   N   H2   sing N N 266 
LYS   CA  C    sing N N 267 
LYS   CA  CB   sing N N 268 
LYS   CA  HA   sing N N 269 
LYS   C   O    doub N N 270 
LYS   C   OXT  sing N N 271 
LYS   CB  CG   sing N N 272 
LYS   CB  HB2  sing N N 273 
LYS   CB  HB3  sing N N 274 
LYS   CG  CD   sing N N 275 
LYS   CG  HG2  sing N N 276 
LYS   CG  HG3  sing N N 277 
LYS   CD  CE   sing N N 278 
LYS   CD  HD2  sing N N 279 
LYS   CD  HD3  sing N N 280 
LYS   CE  NZ   sing N N 281 
LYS   CE  HE2  sing N N 282 
LYS   CE  HE3  sing N N 283 
LYS   NZ  HZ1  sing N N 284 
LYS   NZ  HZ2  sing N N 285 
LYS   NZ  HZ3  sing N N 286 
LYS   OXT HXT  sing N N 287 
MET   N   CA   sing N N 288 
MET   N   H    sing N N 289 
MET   N   H2   sing N N 290 
MET   CA  C    sing N N 291 
MET   CA  CB   sing N N 292 
MET   CA  HA   sing N N 293 
MET   C   O    doub N N 294 
MET   C   OXT  sing N N 295 
MET   CB  CG   sing N N 296 
MET   CB  HB2  sing N N 297 
MET   CB  HB3  sing N N 298 
MET   CG  SD   sing N N 299 
MET   CG  HG2  sing N N 300 
MET   CG  HG3  sing N N 301 
MET   SD  CE   sing N N 302 
MET   CE  HE1  sing N N 303 
MET   CE  HE2  sing N N 304 
MET   CE  HE3  sing N N 305 
MET   OXT HXT  sing N N 306 
PHE   N   CA   sing N N 307 
PHE   N   H    sing N N 308 
PHE   N   H2   sing N N 309 
PHE   CA  C    sing N N 310 
PHE   CA  CB   sing N N 311 
PHE   CA  HA   sing N N 312 
PHE   C   O    doub N N 313 
PHE   C   OXT  sing N N 314 
PHE   CB  CG   sing N N 315 
PHE   CB  HB2  sing N N 316 
PHE   CB  HB3  sing N N 317 
PHE   CG  CD1  doub Y N 318 
PHE   CG  CD2  sing Y N 319 
PHE   CD1 CE1  sing Y N 320 
PHE   CD1 HD1  sing N N 321 
PHE   CD2 CE2  doub Y N 322 
PHE   CD2 HD2  sing N N 323 
PHE   CE1 CZ   doub Y N 324 
PHE   CE1 HE1  sing N N 325 
PHE   CE2 CZ   sing Y N 326 
PHE   CE2 HE2  sing N N 327 
PHE   CZ  HZ   sing N N 328 
PHE   OXT HXT  sing N N 329 
PRO   N   CA   sing N N 330 
PRO   N   CD   sing N N 331 
PRO   N   H    sing N N 332 
PRO   CA  C    sing N N 333 
PRO   CA  CB   sing N N 334 
PRO   CA  HA   sing N N 335 
PRO   C   O    doub N N 336 
PRO   C   OXT  sing N N 337 
PRO   CB  CG   sing N N 338 
PRO   CB  HB2  sing N N 339 
PRO   CB  HB3  sing N N 340 
PRO   CG  CD   sing N N 341 
PRO   CG  HG2  sing N N 342 
PRO   CG  HG3  sing N N 343 
PRO   CD  HD2  sing N N 344 
PRO   CD  HD3  sing N N 345 
PRO   OXT HXT  sing N N 346 
SER   N   CA   sing N N 347 
SER   N   H    sing N N 348 
SER   N   H2   sing N N 349 
SER   CA  C    sing N N 350 
SER   CA  CB   sing N N 351 
SER   CA  HA   sing N N 352 
SER   C   O    doub N N 353 
SER   C   OXT  sing N N 354 
SER   CB  OG   sing N N 355 
SER   CB  HB2  sing N N 356 
SER   CB  HB3  sing N N 357 
SER   OG  HG   sing N N 358 
SER   OXT HXT  sing N N 359 
THR   N   CA   sing N N 360 
THR   N   H    sing N N 361 
THR   N   H2   sing N N 362 
THR   CA  C    sing N N 363 
THR   CA  CB   sing N N 364 
THR   CA  HA   sing N N 365 
THR   C   O    doub N N 366 
THR   C   OXT  sing N N 367 
THR   CB  OG1  sing N N 368 
THR   CB  CG2  sing N N 369 
THR   CB  HB   sing N N 370 
THR   OG1 HG1  sing N N 371 
THR   CG2 HG21 sing N N 372 
THR   CG2 HG22 sing N N 373 
THR   CG2 HG23 sing N N 374 
THR   OXT HXT  sing N N 375 
TRP   N   CA   sing N N 376 
TRP   N   H    sing N N 377 
TRP   N   H2   sing N N 378 
TRP   CA  C    sing N N 379 
TRP   CA  CB   sing N N 380 
TRP   CA  HA   sing N N 381 
TRP   C   O    doub N N 382 
TRP   C   OXT  sing N N 383 
TRP   CB  CG   sing N N 384 
TRP   CB  HB2  sing N N 385 
TRP   CB  HB3  sing N N 386 
TRP   CG  CD1  doub Y N 387 
TRP   CG  CD2  sing Y N 388 
TRP   CD1 NE1  sing Y N 389 
TRP   CD1 HD1  sing N N 390 
TRP   CD2 CE2  doub Y N 391 
TRP   CD2 CE3  sing Y N 392 
TRP   NE1 CE2  sing Y N 393 
TRP   NE1 HE1  sing N N 394 
TRP   CE2 CZ2  sing Y N 395 
TRP   CE3 CZ3  doub Y N 396 
TRP   CE3 HE3  sing N N 397 
TRP   CZ2 CH2  doub Y N 398 
TRP   CZ2 HZ2  sing N N 399 
TRP   CZ3 CH2  sing Y N 400 
TRP   CZ3 HZ3  sing N N 401 
TRP   CH2 HH2  sing N N 402 
TRP   OXT HXT  sing N N 403 
TYR   N   CA   sing N N 404 
TYR   N   H    sing N N 405 
TYR   N   H2   sing N N 406 
TYR   CA  C    sing N N 407 
TYR   CA  CB   sing N N 408 
TYR   CA  HA   sing N N 409 
TYR   C   O    doub N N 410 
TYR   C   OXT  sing N N 411 
TYR   CB  CG   sing N N 412 
TYR   CB  HB2  sing N N 413 
TYR   CB  HB3  sing N N 414 
TYR   CG  CD1  doub Y N 415 
TYR   CG  CD2  sing Y N 416 
TYR   CD1 CE1  sing Y N 417 
TYR   CD1 HD1  sing N N 418 
TYR   CD2 CE2  doub Y N 419 
TYR   CD2 HD2  sing N N 420 
TYR   CE1 CZ   doub Y N 421 
TYR   CE1 HE1  sing N N 422 
TYR   CE2 CZ   sing Y N 423 
TYR   CE2 HE2  sing N N 424 
TYR   CZ  OH   sing N N 425 
TYR   OH  HH   sing N N 426 
TYR   OXT HXT  sing N N 427 
VAL   N   CA   sing N N 428 
VAL   N   H    sing N N 429 
VAL   N   H2   sing N N 430 
VAL   CA  C    sing N N 431 
VAL   CA  CB   sing N N 432 
VAL   CA  HA   sing N N 433 
VAL   C   O    doub N N 434 
VAL   C   OXT  sing N N 435 
VAL   CB  CG1  sing N N 436 
VAL   CB  CG2  sing N N 437 
VAL   CB  HB   sing N N 438 
VAL   CG1 HG11 sing N N 439 
VAL   CG1 HG12 sing N N 440 
VAL   CG1 HG13 sing N N 441 
VAL   CG2 HG21 sing N N 442 
VAL   CG2 HG22 sing N N 443 
VAL   CG2 HG23 sing N N 444 
VAL   OXT HXT  sing N N 445 
# 
_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                    9BQG 
_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]   0.019450 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002366 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012367 
_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]   0.011209 
_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   ? -33.14819 -19.06413 15.29183  1.000 22.24680 ? 1   SER   A N   1 
ATOM   2    C CA  . SER   A 1 1   ? -32.39472 -20.19078 14.76238  1.000 20.63138 ? 1   SER   A CA  1 
ATOM   3    C C   . SER   A 1 1   ? -32.37758 -20.22803 13.23620  1.000 20.02102 ? 1   SER   A C   1 
ATOM   4    O O   . SER   A 1 1   ? -32.89012 -19.32545 12.56766  1.000 20.01634 ? 1   SER   A O   1 
ATOM   5    C CB  . SER   A 1 1   ? -32.95860 -21.48830 15.32514  1.000 25.59126 ? 1   SER   A CB  1 
ATOM   6    O OG  . SER   A 1 1   ? -34.17618 -21.82454 14.69573  1.000 26.42442 ? 1   SER   A OG  1 
ATOM   7    N N   . GLY   A 1 2   ? -31.76150 -21.26681 12.68666  1.000 20.28296 ? 2   GLY   A N   1 
ATOM   8    C CA  . GLY   A 1 2   ? -31.48912 -21.33901 11.26881  1.000 19.94661 ? 2   GLY   A CA  1 
ATOM   9    C C   . GLY   A 1 2   ? -30.02901 -21.04942 10.97664  1.000 18.71754 ? 2   GLY   A C   1 
ATOM   10   O O   . GLY   A 1 2   ? -29.32862 -20.38684 11.74217  1.000 19.88849 ? 2   GLY   A O   1 
ATOM   11   N N   . PHE   A 1 3   ? -29.56039 -21.56690 9.84094   1.000 18.36431 ? 3   PHE   A N   1 
ATOM   12   C CA  . PHE   A 1 3   ? -28.17732 -21.36083 9.42681   1.000 20.09508 ? 3   PHE   A CA  1 
ATOM   13   C C   . PHE   A 1 3   ? -28.10525 -21.25642 7.91548   1.000 20.86589 ? 3   PHE   A C   1 
ATOM   14   O O   . PHE   A 1 3   ? -28.46167 -22.20039 7.20773   1.000 23.73002 ? 3   PHE   A O   1 
ATOM   15   C CB  . PHE   A 1 3   ? -27.26238 -22.47451 9.92849   1.000 21.08578 ? 3   PHE   A CB  1 
ATOM   16   C CG  . PHE   A 1 3   ? -25.82082 -22.05820 9.98299   1.000 16.61109 ? 3   PHE   A CG  1 
ATOM   17   C CD1 . PHE   A 1 3   ? -25.36409 -21.25335 11.01032  1.000 19.92020 ? 3   PHE   A CD1 1 
ATOM   18   C CD2 . PHE   A 1 3   ? -24.93127 -22.44444 8.99213   1.000 20.04453 ? 3   PHE   A CD2 1 
ATOM   19   C CE1 . PHE   A 1 3   ? -24.04659 -20.83899 11.05493  1.000 21.21282 ? 3   PHE   A CE1 1 
ATOM   20   C CE2 . PHE   A 1 3   ? -23.60972 -22.04161 9.03553   1.000 19.98555 ? 3   PHE   A CE2 1 
ATOM   21   C CZ  . PHE   A 1 3   ? -23.16576 -21.23793 10.07103  1.000 19.60931 ? 3   PHE   A CZ  1 
ATOM   22   N N   . ARG   A 1 4   ? -27.62259 -20.11789 7.42918   1.000 18.67032 ? 4   ARG   A N   1 
ATOM   23   C CA  . ARG   A 1 4   ? -27.58485 -19.82047 6.00917   1.000 17.37998 ? 4   ARG   A CA  1 
ATOM   24   C C   . ARG   A 1 4   ? -26.19767 -19.33227 5.64085   1.000 14.54378 ? 4   ARG   A C   1 
ATOM   25   O O   . ARG   A 1 4   ? -25.50602 -18.72641 6.45731   1.000 16.62676 ? 4   ARG   A O   1 
ATOM   26   C CB  . ARG   A 1 4   ? -28.60930 -18.75081 5.63513   1.000 19.56711 ? 4   ARG   A CB  1 
ATOM   27   C CG  . ARG   A 1 4   ? -30.00963 -19.27471 5.58650   1.000 17.26060 ? 4   ARG   A CG  1 
ATOM   28   C CD  . ARG   A 1 4   ? -30.24774 -19.85808 4.20479   1.000 23.57426 ? 4   ARG   A CD  1 
ATOM   29   N NE  . ARG   A 1 4   ? -31.67176 -20.00179 3.90298   1.000 25.59744 ? 4   ARG   A NE  1 
ATOM   30   C CZ  . ARG   A 1 4   ? -32.13562 -20.66851 2.84986   1.000 25.19097 ? 4   ARG   A CZ  1 
ATOM   31   N NH1 . ARG   A 1 4   ? -33.43835 -20.77949 2.64457   1.000 22.28169 ? 4   ARG   A NH1 1 
ATOM   32   N NH2 . ARG   A 1 4   ? -31.27974 -21.19383 1.98202   1.000 28.94211 ? 4   ARG   A NH2 1 
ATOM   33   N N   . LYS   A 1 5   ? -25.80367 -19.59292 4.39966   1.000 17.07957 ? 5   LYS   A N   1 
ATOM   34   C CA  . LYS   A 1 5   ? -24.62163 -18.93952 3.86464   1.000 15.98612 ? 5   LYS   A CA  1 
ATOM   35   C C   . LYS   A 1 5   ? -24.95319 -17.45965 3.71501   1.000 16.23261 ? 5   LYS   A C   1 
ATOM   36   O O   . LYS   A 1 5   ? -25.84062 -17.07905 2.94514   1.000 18.98265 ? 5   LYS   A O   1 
ATOM   37   C CB  . LYS   A 1 5   ? -24.18161 -19.58672 2.55426   1.000 20.72406 ? 5   LYS   A CB  1 
ATOM   38   C CG  . LYS   A 1 5   ? -22.68469 -19.51912 2.34137   1.000 21.63930 ? 5   LYS   A CG  1 
ATOM   39   C CD  . LYS   A 1 5   ? -22.16944 -20.60779 1.40943   1.000 22.72986 ? 5   LYS   A CD  1 
ATOM   40   C CE  . LYS   A 1 5   ? -21.74283 -21.84577 2.17344   1.000 23.35225 ? 5   LYS   A CE  1 
ATOM   41   N NZ  . LYS   A 1 5   ? -20.88833 -22.75880 1.35632   1.000 30.04366 ? 5   LYS   A NZ  1 
ATOM   42   N N   . MET   A 1 6   ? -24.29865 -16.64192 4.52108   1.000 11.49590 ? 6   MET   A N   1 
ATOM   43   C CA  . MET   A 1 6   ? -24.69670 -15.26537 4.74852   1.000 14.35743 ? 6   MET   A CA  1 
ATOM   44   C C   . MET   A 1 6   ? -23.56802 -14.33931 4.34386   1.000 13.54874 ? 6   MET   A C   1 
ATOM   45   O O   . MET   A 1 6   ? -22.45167 -14.47339 4.84915   1.000 15.78207 ? 6   MET   A O   1 
ATOM   46   C CB  . MET   A 1 6   ? -24.99746 -15.02010 6.22243   1.000 14.85557 ? 6   MET   A CB  1 
ATOM   47   C CG  . MET   A 1 6   ? -25.71121 -13.74529 6.43522   1.000 19.70296 ? 6   MET   A CG  1 
ATOM   48   S SD  . MET   A 1 6   ? -26.37633 -13.70647 8.09219   1.000 24.67500 ? 6   MET   A SD  1 
ATOM   49   C CE  . MET   A 1 6   ? -27.60396 -15.01296 8.04226   1.000 21.71789 ? 6   MET   A CE  1 
ATOM   50   N N   . ALA   A 1 7   ? -23.85868 -13.39490 3.46799   1.000 13.16216 ? 7   ALA   A N   1 
ATOM   51   C CA  . ALA   A 1 7   ? -22.85489 -12.41358 3.08928   1.000 10.64146 ? 7   ALA   A CA  1 
ATOM   52   C C   . ALA   A 1 7   ? -23.02555 -11.15698 3.92600   1.000 13.21479 ? 7   ALA   A C   1 
ATOM   53   O O   . ALA   A 1 7   ? -24.04478 -10.95968 4.59052   1.000 12.49044 ? 7   ALA   A O   1 
ATOM   54   C CB  . ALA   A 1 7   ? -22.94018 -12.07089 1.60546   1.000 13.06797 ? 7   ALA   A CB  1 
ATOM   55   N N   . PHE   A 1 8   ? -21.99895 -10.31053 3.90815   1.000 10.04240 ? 8   PHE   A N   1 
ATOM   56   C CA  . PHE   A 1 8   ? -22.13381 -9.01628  4.55273   1.000 10.49661 ? 8   PHE   A CA  1 
ATOM   57   C C   . PHE   A 1 8   ? -23.01932 -8.11035  3.71128   1.000 10.53909 ? 8   PHE   A C   1 
ATOM   58   O O   . PHE   A 1 8   ? -23.05812 -8.23930  2.49000   1.000 10.49391 ? 8   PHE   A O   1 
ATOM   59   C CB  . PHE   A 1 8   ? -20.76698 -8.36066  4.73328   1.000 9.94164  ? 8   PHE   A CB  1 
ATOM   60   C CG  . PHE   A 1 8   ? -19.95952 -8.99208  5.84247   1.000 12.72470 ? 8   PHE   A CG  1 
ATOM   61   C CD1 . PHE   A 1 8   ? -20.24374 -8.72679  7.16555   1.000 18.08998 ? 8   PHE   A CD1 1 
ATOM   62   C CD2 . PHE   A 1 8   ? -18.97681 -9.91115  5.54870   1.000 15.50879 ? 8   PHE   A CD2 1 
ATOM   63   C CE1 . PHE   A 1 8   ? -19.51787 -9.33415  8.18294   1.000 23.45252 ? 8   PHE   A CE1 1 
ATOM   64   C CE2 . PHE   A 1 8   ? -18.23925 -10.52467 6.56874   1.000 18.02536 ? 8   PHE   A CE2 1 
ATOM   65   C CZ  . PHE   A 1 8   ? -18.51539 -10.23320 7.88145   1.000 18.90205 ? 8   PHE   A CZ  1 
ATOM   66   N N   . PRO   A 1 9   ? -23.75172 -7.19805  4.34812   1.000 11.05061 ? 9   PRO   A N   1 
ATOM   67   C CA  . PRO   A 1 9   ? -24.45641 -6.16178  3.58614   1.000 11.82401 ? 9   PRO   A CA  1 
ATOM   68   C C   . PRO   A 1 9   ? -23.47844 -5.47467  2.64489   1.000 14.13086 ? 9   PRO   A C   1 
ATOM   69   O O   . PRO   A 1 9   ? -22.33911 -5.16691  3.01993   1.000 12.36380 ? 9   PRO   A O   1 
ATOM   70   C CB  . PRO   A 1 9   ? -24.96918 -5.20816  4.67167   1.000 15.02596 ? 9   PRO   A CB  1 
ATOM   71   C CG  . PRO   A 1 9   ? -24.94305 -6.00420  5.94067   1.000 13.21396 ? 9   PRO   A CG  1 
ATOM   72   C CD  . PRO   A 1 9   ? -23.76997 -6.94214  5.79692   1.000 12.36881 ? 9   PRO   A CD  1 
ATOM   73   N N   . SER   A 1 10  ? -23.90999 -5.26556  1.40067   1.000 11.44897 ? 10  SER   A N   1 
ATOM   74   C CA  . SER   A 1 10  ? -22.97484 -4.89378  0.34149   1.000 11.41664 ? 10  SER   A CA  1 
ATOM   75   C C   . SER   A 1 10  ? -22.95634 -3.40611  0.06096   1.000 12.31430 ? 10  SER   A C   1 
ATOM   76   O O   . SER   A 1 10  ? -22.15110 -2.96247  -0.76487  1.000 11.74209 ? 10  SER   A O   1 
ATOM   77   C CB  . SER   A 1 10  ? -23.29621 -5.64880  -0.95518  1.000 10.70550 ? 10  SER   A CB  1 
ATOM   78   O OG  . SER   A 1 10  ? -24.64249 -5.48044  -1.33721  1.000 12.94027 ? 10  SER   A OG  1 
ATOM   79   N N   . GLY   A 1 11  ? -23.81191 -2.63510  0.73026   1.000 13.21496 ? 11  GLY   A N   1 
ATOM   80   C CA  . GLY   A 1 11  ? -23.98671 -1.23154  0.37227   1.000 14.07963 ? 11  GLY   A CA  1 
ATOM   81   C C   . GLY   A 1 11  ? -22.68936 -0.44639  0.33406   1.000 14.72256 ? 11  GLY   A C   1 
ATOM   82   O O   . GLY   A 1 11  ? -22.48020 0.37962   -0.56317  1.000 17.29401 ? 11  GLY   A O   1 
ATOM   83   N N   . LYS   A 1 12  ? -21.81948 -0.66373  1.32856   1.000 13.56614 ? 12  LYS   A N   1 
ATOM   84   C CA  . LYS   A 1 12  ? -20.59328 0.12146   1.41613   1.000 14.01106 ? 12  LYS   A CA  1 
ATOM   85   C C   . LYS   A 1 12  ? -19.68159 -0.15172  0.23852   1.000 15.52804 ? 12  LYS   A C   1 
ATOM   86   O O   . LYS   A 1 12  ? -18.92598 0.73387   -0.18023  1.000 18.35722 ? 12  LYS   A O   1 
ATOM   87   C CB  . LYS   A 1 12  ? -19.85155 -0.17522  2.71703   1.000 17.90806 ? 12  LYS   A CB  1 
ATOM   88   C CG  . LYS   A 1 12  ? -20.60377 0.19213   3.98426   1.000 21.29848 ? 12  LYS   A CG  1 
ATOM   89   C CD  . LYS   A 1 12  ? -19.68550 0.07571   5.19316   1.000 25.32441 ? 12  LYS   A CD  1 
ATOM   90   C CE  . LYS   A 1 12  ? -20.12704 0.98704   6.32116   1.000 28.91548 ? 12  LYS   A CE  1 
ATOM   91   N NZ  . LYS   A 1 12  ? -21.47079 0.58405   6.82098   1.000 37.19397 ? 12  LYS   A NZ  1 
ATOM   92   N N   . VAL   A 1 13  ? -19.72325 -1.36619  -0.29565  1.000 13.91430 ? 13  VAL   A N   1 
ATOM   93   C CA  . VAL   A 1 13  ? -18.88524 -1.67742  -1.45035  1.000 13.13057 ? 13  VAL   A CA  1 
ATOM   94   C C   . VAL   A 1 13  ? -19.57175 -1.24899  -2.74084  1.000 12.28641 ? 13  VAL   A C   1 
ATOM   95   O O   . VAL   A 1 13  ? -18.90763 -0.83237  -3.68560  1.000 12.33432 ? 13  VAL   A O   1 
ATOM   96   C CB  . VAL   A 1 13  ? -18.56297 -3.17706  -1.45360  1.000 10.11500 ? 13  VAL   A CB  1 
ATOM   97   C CG1 . VAL   A 1 13  ? -17.67225 -3.54646  -2.65487  1.000 13.03752 ? 13  VAL   A CG1 1 
ATOM   98   C CG2 . VAL   A 1 13  ? -17.91622 -3.56880  -0.13994  1.000 10.45069 ? 13  VAL   A CG2 1 
ATOM   99   N N   . GLU   A 1 14  ? -20.91252 -1.34254  -2.80161  1.000 12.25446 ? 14  GLU   A N   1 
ATOM   100  C CA  . GLU   A 1 14  ? -21.63175 -0.91739  -3.99710  1.000 12.96566 ? 14  GLU   A CA  1 
ATOM   101  C C   . GLU   A 1 14  ? -21.26322 0.50380   -4.36996  1.000 13.92423 ? 14  GLU   A C   1 
ATOM   102  O O   . GLU   A 1 14  ? -21.12030 0.82211   -5.55487  1.000 15.29667 ? 14  GLU   A O   1 
ATOM   103  C CB  . GLU   A 1 14  ? -23.14371 -1.01042  -3.77709  1.000 13.66311 ? 14  GLU   A CB  1 
ATOM   104  C CG  . GLU   A 1 14  ? -23.66236 -2.43047  -3.57040  1.000 12.93072 ? 14  GLU   A CG  1 
ATOM   105  C CD  . GLU   A 1 14  ? -25.11972 -2.43067  -3.13914  1.000 14.08212 ? 14  GLU   A CD  1 
ATOM   106  O OE1 . GLU   A 1 14  ? -25.96272 -1.71391  -3.72703  1.000 16.56446 ? 14  GLU   A OE1 1 
ATOM   107  O OE2 . GLU   A 1 14  ? -25.40198 -3.10434  -2.14707  1.000 13.97884 ? 14  GLU   A OE2 1 
ATOM   108  N N   . GLY   A 1 15  ? -21.10199 1.37610   -3.36912  1.000 14.52262 ? 15  GLY   A N   1 
ATOM   109  C CA  . GLY   A 1 15  ? -20.80883 2.76456   -3.66339  1.000 15.64585 ? 15  GLY   A CA  1 
ATOM   110  C C   . GLY   A 1 15  ? -19.41750 3.00839   -4.18728  1.000 15.84741 ? 15  GLY   A C   1 
ATOM   111  O O   . GLY   A 1 15  ? -19.08321 4.13802   -4.56224  1.000 16.27311 ? 15  GLY   A O   1 
ATOM   112  N N   . CYS   A 1 16  ? -18.58930 1.97356   -4.20726  1.000 14.04428 ? 16  CYS   A N   1 
ATOM   113  C CA  . CYS   A 1 16  ? -17.23631 2.08341   -4.71671  1.000 13.73100 ? 16  CYS   A CA  1 
ATOM   114  C C   . CYS   A 1 16  ? -17.07290 1.54179   -6.12243  1.000 13.37859 ? 16  CYS   A C   1 
ATOM   115  O O   . CYS   A 1 16  ? -15.97548 1.65261   -6.68850  1.000 13.26779 ? 16  CYS   A O   1 
ATOM   116  C CB  . CYS   A 1 16  ? -16.24932 1.34703   -3.79634  1.000 12.78712 ? 16  CYS   A CB  1 
ATOM   117  S SG  . CYS   A 1 16  ? -16.27095 1.95732   -2.09996  1.000 15.96957 ? 16  CYS   A SG  1 
ATOM   118  N N   . MET   A 1 17  ? -18.09499 0.93118   -6.68993  1.000 13.30447 ? 17  MET   A N   1 
ATOM   119  C CA  . MET   A 1 17  ? -17.84113 0.15512   -7.87640  1.000 12.98571 ? 17  MET   A CA  1 
ATOM   120  C C   . MET   A 1 17  ? -18.01287 1.06146   -9.08599  1.000 14.64967 ? 17  MET   A C   1 
ATOM   121  O O   . MET   A 1 17  ? -18.96996 1.83442   -9.14526  1.000 16.45745 ? 17  MET   A O   1 
ATOM   122  C CB  . MET   A 1 17  ? -18.77181 -1.03172  -8.00948  1.000 14.73166 ? 17  MET   A CB  1 
ATOM   123  C CG  . MET   A 1 17  ? -18.60641 -2.02765  -6.85687  1.000 12.09739 ? 17  MET   A CG  1 
ATOM   124  S SD  . MET   A 1 17  ? -16.94211 -2.63036  -6.67984  1.000 11.03301 ? 17  MET   A SD  1 
ATOM   125  C CE  . MET   A 1 17  ? -16.71023 -3.57018  -8.18276  1.000 19.35665 ? 17  MET   A CE  1 
ATOM   126  N N   . VAL   A 1 18  ? -17.06819 0.98740   -10.03095 1.000 15.78290 ? 18  VAL   A N   1 
ATOM   127  C CA  . VAL   A 1 18  ? -17.07924 1.78372   -11.25458 1.000 17.83636 ? 18  VAL   A CA  1 
ATOM   128  C C   . VAL   A 1 18  ? -16.73974 0.89002   -12.44457 1.000 15.60123 ? 18  VAL   A C   1 
ATOM   129  O O   . VAL   A 1 18  ? -16.29292 -0.23976  -12.29558 1.000 15.05735 ? 18  VAL   A O   1 
ATOM   130  C CB  . VAL   A 1 18  ? -16.09445 2.97463   -11.20567 1.000 15.72975 ? 18  VAL   A CB  1 
ATOM   131  C CG1 . VAL   A 1 18  ? -16.30682 3.81394   -9.95811  1.000 17.14010 ? 18  VAL   A CG1 1 
ATOM   132  C CG2 . VAL   A 1 18  ? -14.66256 2.47918   -11.26062 1.000 16.29614 ? 18  VAL   A CG2 1 
ATOM   133  N N   . GLN   A 1 19  ? -16.93294 1.43471   -13.63811 1.000 21.97196 ? 19  GLN   A N   1 
ATOM   134  C CA  . GLN   A 1 19  ? -16.66552 0.72842   -14.87948 1.000 20.20624 ? 19  GLN   A CA  1 
ATOM   135  C C   . GLN   A 1 19  ? -15.36715 1.27182   -15.46452 1.000 18.35037 ? 19  GLN   A C   1 
ATOM   136  O O   . GLN   A 1 19  ? -15.17507 2.49020   -15.54457 1.000 19.65355 ? 19  GLN   A O   1 
ATOM   137  C CB  . GLN   A 1 19  ? -17.83745 0.90302   -15.84385 1.000 20.64379 ? 19  GLN   A CB  1 
ATOM   138  C CG  . GLN   A 1 19  ? -17.68884 0.25884   -17.20259 1.000 23.79388 ? 19  GLN   A CG  1 
ATOM   139  C CD  . GLN   A 1 19  ? -18.99644 0.29964   -17.98140 1.000 28.53665 ? 19  GLN   A CD  1 
ATOM   140  O OE1 . GLN   A 1 19  ? -19.27867 -0.58002  -18.79751 1.000 33.67153 ? 19  GLN   A OE1 1 
ATOM   141  N NE2 . GLN   A 1 19  ? -19.81096 1.31381   -17.71445 1.000 28.93835 ? 19  GLN   A NE2 1 
ATOM   142  N N   . VAL   A 1 20  ? -14.45500 0.37878   -15.82111 1.000 17.38633 ? 20  VAL   A N   1 
ATOM   143  C CA  . VAL   A 1 20  ? -13.19213 0.77477   -16.42793 1.000 19.21649 ? 20  VAL   A CA  1 
ATOM   144  C C   . VAL   A 1 20  ? -13.12869 0.15593   -17.81249 1.000 17.15826 ? 20  VAL   A C   1 
ATOM   145  O O   . VAL   A 1 20  ? -13.24086 -1.06466  -17.95549 1.000 21.28918 ? 20  VAL   A O   1 
ATOM   146  C CB  . VAL   A 1 20  ? -11.98109 0.35309   -15.58055 1.000 17.46652 ? 20  VAL   A CB  1 
ATOM   147  C CG1 . VAL   A 1 20  ? -10.68781 0.74732   -16.29937 1.000 16.57785 ? 20  VAL   A CG1 1 
ATOM   148  C CG2 . VAL   A 1 20  ? -12.02642 0.99445   -14.21176 1.000 17.81943 ? 20  VAL   A CG2 1 
ATOM   149  N N   . THR   A 1 21  ? -12.95744 0.99306   -18.83045 1.000 23.10490 ? 21  THR   A N   1 
ATOM   150  C CA  . THR   A 1 21  ? -12.84215 0.53074   -20.20532 1.000 22.46708 ? 21  THR   A CA  1 
ATOM   151  C C   . THR   A 1 21  ? -11.53277 1.03517   -20.77986 1.000 24.80908 ? 21  THR   A C   1 
ATOM   152  O O   . THR   A 1 21  ? -11.18136 2.20676   -20.60534 1.000 25.30503 ? 21  THR   A O   1 
ATOM   153  C CB  . THR   A 1 21  ? -14.00869 1.00383   -21.07725 1.000 24.29058 ? 21  THR   A CB  1 
ATOM   154  O OG1 . THR   A 1 21  ? -15.24631 0.56897   -20.49988 1.000 24.18323 ? 21  THR   A OG1 1 
ATOM   155  C CG2 . THR   A 1 21  ? -13.88301 0.43264   -22.48631 1.000 23.39585 ? 21  THR   A CG2 1 
ATOM   156  N N   . CYS   A 1 22  ? -10.81413 0.14704   -21.45166 1.000 23.46476 ? 22  CYS   A N   1 
ATOM   157  C CA  . CYS   A 1 22  ? -9.58858  0.52814   -22.13375 1.000 25.78496 ? 22  CYS   A CA  1 
ATOM   158  C C   . CYS   A 1 22  ? -9.48828  -0.32591  -23.38386 1.000 29.12436 ? 22  CYS   A C   1 
ATOM   159  O O   . CYS   A 1 22  ? -9.51768  -1.55761  -23.29182 1.000 25.65107 ? 22  CYS   A O   1 
ATOM   160  C CB  . CYS   A 1 22  ? -8.36916  0.33757   -21.23490 1.000 25.79403 ? 22  CYS   A CB  1 
ATOM   161  S SG  . CYS   A 1 22  ? -6.85456  0.79013   -22.07758 1.000 35.31008 ? 22  CYS   A SG  1 
ATOM   162  N N   . GLY   A 1 23  ? -9.38184  0.32330   -24.53595 1.000 28.04049 ? 23  GLY   A N   1 
ATOM   163  C CA  . GLY   A 1 23  ? -9.48745  -0.40172  -25.79163 1.000 27.85078 ? 23  GLY   A CA  1 
ATOM   164  C C   . GLY   A 1 23  ? -10.87160 -1.01301  -25.88965 1.000 31.30121 ? 23  GLY   A C   1 
ATOM   165  O O   . GLY   A 1 23  ? -11.88940 -0.32438  -25.75691 1.000 34.91298 ? 23  GLY   A O   1 
ATOM   166  N N   . THR   A 1 24  ? -10.93187 -2.32652  -26.09737 1.000 31.24946 ? 24  THR   A N   1 
ATOM   167  C CA  . THR   A 1 24  ? -12.20180 -3.03486  -26.19837 1.000 32.64006 ? 24  THR   A CA  1 
ATOM   168  C C   . THR   A 1 24  ? -12.50425 -3.85854  -24.95876 1.000 32.43644 ? 24  THR   A C   1 
ATOM   169  O O   . THR   A 1 24  ? -13.44792 -4.65491  -24.97032 1.000 36.12880 ? 24  THR   A O   1 
ATOM   170  C CB  . THR   A 1 24  ? -12.21135 -3.95888  -27.41138 1.000 34.50951 ? 24  THR   A CB  1 
ATOM   171  O OG1 . THR   A 1 24  ? -11.08342 -4.83689  -27.33186 1.000 35.81135 ? 24  THR   A OG1 1 
ATOM   172  C CG2 . THR   A 1 24  ? -12.13587 -3.14638  -28.69337 1.000 34.25656 ? 24  THR   A CG2 1 
ATOM   173  N N   . THR   A 1 25  ? -11.71799 -3.70966  -23.90423 1.000 28.12022 ? 25  THR   A N   1 
ATOM   174  C CA  . THR   A 1 25  ? -11.92078 -4.45674  -22.67511 1.000 29.30890 ? 25  THR   A CA  1 
ATOM   175  C C   . THR   A 1 25  ? -12.70122 -3.59146  -21.69992 1.000 27.45432 ? 25  THR   A C   1 
ATOM   176  O O   . THR   A 1 25  ? -12.31348 -2.45365  -21.42344 1.000 25.75592 ? 25  THR   A O   1 
ATOM   177  C CB  . THR   A 1 25  ? -10.58889 -4.87552  -22.05701 1.000 30.74716 ? 25  THR   A CB  1 
ATOM   178  O OG1 . THR   A 1 25  ? -9.93548  -5.80566  -22.92678 1.000 34.45975 ? 25  THR   A OG1 1 
ATOM   179  C CG2 . THR   A 1 25  ? -10.83033 -5.54853  -20.71376 1.000 27.08755 ? 25  THR   A CG2 1 
ATOM   180  N N   . THR   A 1 26  ? -13.81041 -4.11700  -21.20047 1.000 23.04677 ? 26  THR   A N   1 
ATOM   181  C CA  . THR   A 1 26  ? -14.54369 -3.46928  -20.12749 1.000 23.13614 ? 26  THR   A CA  1 
ATOM   182  C C   . THR   A 1 26  ? -14.55262 -4.39522  -18.91832 1.000 20.94184 ? 26  THR   A C   1 
ATOM   183  O O   . THR   A 1 26  ? -14.78179 -5.60112  -19.04758 1.000 20.35627 ? 26  THR   A O   1 
ATOM   184  C CB  . THR   A 1 26  ? -15.96323 -3.09513  -20.56388 1.000 23.80264 ? 26  THR   A CB  1 
ATOM   185  O OG1 . THR   A 1 26  ? -15.89056 -2.02673  -21.51073 1.000 27.39036 ? 26  THR   A OG1 1 
ATOM   186  C CG2 . THR   A 1 26  ? -16.78860 -2.63761  -19.38243 1.000 26.10232 ? 26  THR   A CG2 1 
ATOM   187  N N   . LEU   A 1 27  ? -14.24671 -3.83002  -17.76086 1.000 19.72341 ? 27  LEU   A N   1 
ATOM   188  C CA  . LEU   A 1 27  ? -14.27261 -4.53190  -16.48782 1.000 20.03032 ? 27  LEU   A CA  1 
ATOM   189  C C   . LEU   A 1 27  ? -14.57720 -3.53839  -15.37138 1.000 19.17460 ? 27  LEU   A C   1 
ATOM   190  O O   . LEU   A 1 27  ? -14.86708 -2.35885  -15.61559 1.000 18.06318 ? 27  LEU   A O   1 
ATOM   191  C CB  . LEU   A 1 27  ? -12.98251 -5.34918  -16.30646 1.000 19.84661 ? 27  LEU   A CB  1 
ATOM   192  C CG  . LEU   A 1 27  ? -11.65701 -4.56422  -16.34070 1.000 18.19668 ? 27  LEU   A CG  1 
ATOM   193  C CD1 . LEU   A 1 27  ? -11.26267 -3.88624  -15.06967 1.000 19.83810 ? 27  LEU   A CD1 1 
ATOM   194  C CD2 . LEU   A 1 27  ? -10.62094 -5.65329  -16.62596 1.000 20.35897 ? 27  LEU   A CD2 1 
ATOM   195  N N   . ASN   A 1 28  ? -14.55717 -4.03603  -14.14641 1.000 18.08740 ? 28  ASN   A N   1 
ATOM   196  C CA  . ASN   A 1 28  ? -14.93434 -3.24827  -12.98578 1.000 16.93505 ? 28  ASN   A CA  1 
ATOM   197  C C   . ASN   A 1 28  ? -13.71100 -2.66053  -12.31789 1.000 12.46476 ? 28  ASN   A C   1 
ATOM   198  O O   . ASN   A 1 28  ? -12.62271 -3.23733  -12.36098 1.000 14.02560 ? 28  ASN   A O   1 
ATOM   199  C CB  . ASN   A 1 28  ? -15.69986 -4.10473  -11.97950 1.000 15.82060 ? 28  ASN   A CB  1 
ATOM   200  C CG  . ASN   A 1 28  ? -16.88833 -4.75786  -12.60601 1.000 15.85293 ? 28  ASN   A CG  1 
ATOM   201  O OD1 . ASN   A 1 28  ? -17.90357 -4.09756  -12.83310 1.000 14.19128 ? 28  ASN   A OD1 1 
ATOM   202  N ND2 . ASN   A 1 28  ? -16.78317 -6.05707  -12.90608 1.000 15.24809 ? 28  ASN   A ND2 1 
ATOM   203  N N   . GLY   A 1 29  ? -13.89585 -1.49821  -11.69349 1.000 13.24077 ? 29  GLY   A N   1 
ATOM   204  C CA  . GLY   A 1 29  ? -12.86745 -0.92988  -10.85630 1.000 12.52299 ? 29  GLY   A CA  1 
ATOM   205  C C   . GLY   A 1 29  ? -13.42248 -0.62393  -9.47356  1.000 12.96717 ? 29  GLY   A C   1 
ATOM   206  O O   . GLY   A 1 29  ? -14.62645 -0.48068  -9.28493  1.000 12.02614 ? 29  GLY   A O   1 
ATOM   207  N N   . LEU   A 1 30  ? -12.51713 -0.52219  -8.51718  1.000 14.09641 ? 30  LEU   A N   1 
ATOM   208  C CA  . LEU   A 1 30  ? -12.86793 -0.17421  -7.14433  1.000 14.12993 ? 30  LEU   A CA  1 
ATOM   209  C C   . LEU   A 1 30  ? -12.36291 1.23655   -6.86656  1.000 12.56551 ? 30  LEU   A C   1 
ATOM   210  O O   . LEU   A 1 30  ? -11.15804 1.49342   -6.94594  1.000 13.82885 ? 30  LEU   A O   1 
ATOM   211  C CB  . LEU   A 1 30  ? -12.28359 -1.20124  -6.16685  1.000 12.40397 ? 30  LEU   A CB  1 
ATOM   212  C CG  . LEU   A 1 30  ? -12.59699 -0.95390  -4.69989  1.000 10.48825 ? 30  LEU   A CG  1 
ATOM   213  C CD1 . LEU   A 1 30  ? -14.00679 -1.46863  -4.43104  1.000 13.14667 ? 30  LEU   A CD1 1 
ATOM   214  C CD2 . LEU   A 1 30  ? -11.63613 -1.69850  -3.78465  1.000 9.88525  ? 30  LEU   A CD2 1 
ATOM   215  N N   . TRP   A 1 31  ? -13.28758 2.15380   -6.55534  1.000 13.16914 ? 31  TRP   A N   1 
ATOM   216  C CA  . TRP   A 1 31  ? -12.98986 3.58417   -6.44267  1.000 14.38136 ? 31  TRP   A CA  1 
ATOM   217  C C   . TRP   A 1 31  ? -12.96838 3.94307   -4.95821  1.000 16.36533 ? 31  TRP   A C   1 
ATOM   218  O O   . TRP   A 1 31  ? -14.01191 3.94037   -4.29880  1.000 14.69967 ? 31  TRP   A O   1 
ATOM   219  C CB  . TRP   A 1 31  ? -14.02908 4.40046   -7.20600  1.000 15.40890 ? 31  TRP   A CB  1 
ATOM   220  C CG  . TRP   A 1 31  ? -13.87011 5.91021   -7.20428  1.000 16.89085 ? 31  TRP   A CG  1 
ATOM   221  C CD1 . TRP   A 1 31  ? -12.71730 6.61865   -7.02316  1.000 17.45134 ? 31  TRP   A CD1 1 
ATOM   222  C CD2 . TRP   A 1 31  ? -14.90590 6.87982   -7.42609  1.000 20.64457 ? 31  TRP   A CD2 1 
ATOM   223  N NE1 . TRP   A 1 31  ? -12.96950 7.96734   -7.11802  1.000 18.99073 ? 31  TRP   A NE1 1 
ATOM   224  C CE2 . TRP   A 1 31  ? -14.30539 8.15464   -7.36385  1.000 20.83223 ? 31  TRP   A CE2 1 
ATOM   225  C CE3 . TRP   A 1 31  ? -16.28231 6.79103   -7.66301  1.000 20.40748 ? 31  TRP   A CE3 1 
ATOM   226  C CZ2 . TRP   A 1 31  ? -15.03536 9.33204   -7.52809  1.000 22.25144 ? 31  TRP   A CZ2 1 
ATOM   227  C CZ3 . TRP   A 1 31  ? -17.00449 7.94712   -7.82158  1.000 22.66184 ? 31  TRP   A CZ3 1 
ATOM   228  C CH2 . TRP   A 1 31  ? -16.38332 9.20818   -7.74919  1.000 22.70799 ? 31  TRP   A CH2 1 
ATOM   229  N N   . LEU   A 1 32  ? -11.77955 4.23189   -4.43122  1.000 14.75715 ? 32  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 32  ? -11.60405 4.60008   -3.03414  1.000 15.15871 ? 32  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 32  ? -10.77080 5.86053   -3.00914  1.000 19.49662 ? 32  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 32  ? -9.69191  5.89012   -3.60786  1.000 17.68609 ? 32  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 32  ? -10.90893 3.48957   -2.23616  1.000 15.05939 ? 32  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 32  ? -11.55064 2.11320   -2.22040  1.000 12.97068 ? 32  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 32  ? -10.57711 1.06172   -1.73157  1.000 12.64314 ? 32  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 32  ? -12.77295 2.15010   -1.32892  1.000 15.06911 ? 32  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 33  ? -11.27484 6.89734   -2.34020  1.000 18.29561 ? 33  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 33  ? -10.67575 8.22815   -2.39179  1.000 21.53829 ? 33  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 33  ? -10.50421 8.56699   -3.87541  1.000 23.51479 ? 33  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 33  ? -11.44259 8.36265   -4.65656  1.000 21.20651 ? 33  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 33  ? -9.41801  8.22995   -1.53980  1.000 24.01739 ? 33  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 33  ? -9.71931  7.93199   -0.07642  1.000 25.85435 ? 33  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 33  ? -10.67090 8.52939   0.46507   1.000 28.56474 ? 33  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 33  ? -9.03941  7.07606   0.52052   1.000 25.84169 ? 33  ASP   A OD2 1 
ATOM   245  N N   . ASP   A 1 34  ? -9.34048  9.04436   -4.32106  1.000 20.65763 ? 34  ASP   A N   1 
ATOM   246  C CA  . ASP   A 1 34  ? -9.20383  9.41079   -5.72530  1.000 20.82744 ? 34  ASP   A CA  1 
ATOM   247  C C   . ASP   A 1 34  ? -8.44523  8.36553   -6.54138  1.000 20.35049 ? 34  ASP   A C   1 
ATOM   248  O O   . ASP   A 1 34  ? -7.77695  8.71486   -7.51884  1.000 22.05526 ? 34  ASP   A O   1 
ATOM   249  C CB  . ASP   A 1 34  ? -8.53137  10.77895  -5.85739  1.000 22.19579 ? 34  ASP   A CB  1 
ATOM   250  C CG  . ASP   A 1 34  ? -7.11440  10.79378  -5.31939  1.000 28.71299 ? 34  ASP   A CG  1 
ATOM   251  O OD1 . ASP   A 1 34  ? -6.74522  9.88382   -4.54074  1.000 25.58557 ? 34  ASP   A OD1 1 
ATOM   252  O OD2 . ASP   A 1 34  ? -6.37060  11.74086  -5.66478  1.000 28.01640 ? 34  ASP   A OD2 1 
ATOM   253  N N   . VAL   A 1 35  ? -8.55358  7.08682   -6.18978  1.000 17.84603 ? 35  VAL   A N   1 
ATOM   254  C CA  . VAL   A 1 35  ? -7.88137  6.02935   -6.93205  1.000 16.81059 ? 35  VAL   A CA  1 
ATOM   255  C C   . VAL   A 1 35  ? -8.91181  4.99240   -7.35903  1.000 17.12492 ? 35  VAL   A C   1 
ATOM   256  O O   . VAL   A 1 35  ? -9.80654  4.62957   -6.58313  1.000 16.90196 ? 35  VAL   A O   1 
ATOM   257  C CB  . VAL   A 1 35  ? -6.75713  5.37892   -6.09912  1.000 16.24091 ? 35  VAL   A CB  1 
ATOM   258  C CG1 . VAL   A 1 35  ? -6.17090  4.17808   -6.82306  1.000 17.12451 ? 35  VAL   A CG1 1 
ATOM   259  C CG2 . VAL   A 1 35  ? -5.66704  6.39684   -5.79386  1.000 20.27661 ? 35  VAL   A CG2 1 
ATOM   260  N N   . VAL   A 1 36  ? -8.78328  4.51274   -8.59191  1.000 15.51186 ? 36  VAL   A N   1 
ATOM   261  C CA  . VAL   A 1 36  ? -9.57124  3.39123   -9.09020  1.000 14.58020 ? 36  VAL   A CA  1 
ATOM   262  C C   . VAL   A 1 36  ? -8.62552  2.22262   -9.28725  1.000 15.71082 ? 36  VAL   A C   1 
ATOM   263  O O   . VAL   A 1 36  ? -7.60740  2.34301   -9.98338  1.000 15.06805 ? 36  VAL   A O   1 
ATOM   264  C CB  . VAL   A 1 36  ? -10.31143 3.73283   -10.39174 1.000 15.25177 ? 36  VAL   A CB  1 
ATOM   265  C CG1 . VAL   A 1 36  ? -10.98292 2.48278   -10.94301 1.000 17.36700 ? 36  VAL   A CG1 1 
ATOM   266  C CG2 . VAL   A 1 36  ? -11.35473 4.81915   -10.12670 1.000 17.20124 ? 36  VAL   A CG2 1 
ATOM   267  N N   . TYR   A 1 37  ? -8.94789  1.10291   -8.65294  1.000 12.64402 ? 37  TYR   A N   1 
ATOM   268  C CA  . TYR   A 1 37  ? -8.11870  -0.09115  -8.68626  1.000 15.35814 ? 37  TYR   A CA  1 
ATOM   269  C C   . TYR   A 1 37  ? -8.78370  -1.09142  -9.61669  1.000 11.42680 ? 37  TYR   A C   1 
ATOM   270  O O   . TYR   A 1 37  ? -10.00014 -1.29021  -9.55193  1.000 12.71288 ? 37  TYR   A O   1 
ATOM   271  C CB  . TYR   A 1 37  ? -7.99644  -0.71752  -7.29225  1.000 11.62506 ? 37  TYR   A CB  1 
ATOM   272  C CG  . TYR   A 1 37  ? -7.37718  0.16361   -6.25002  1.000 13.07407 ? 37  TYR   A CG  1 
ATOM   273  C CD1 . TYR   A 1 37  ? -8.12285  1.14653   -5.61526  1.000 12.56961 ? 37  TYR   A CD1 1 
ATOM   274  C CD2 . TYR   A 1 37  ? -6.02137  0.04106   -5.91025  1.000 14.82171 ? 37  TYR   A CD2 1 
ATOM   275  C CE1 . TYR   A 1 37  ? -7.55024  1.96002   -4.64822  1.000 15.02579 ? 37  TYR   A CE1 1 
ATOM   276  C CE2 . TYR   A 1 37  ? -5.45268  0.85044   -4.95170  1.000 12.47059 ? 37  TYR   A CE2 1 
ATOM   277  C CZ  . TYR   A 1 37  ? -6.22002  1.80394   -4.32018  1.000 17.06217 ? 37  TYR   A CZ  1 
ATOM   278  O OH  . TYR   A 1 37  ? -5.65745  2.62963   -3.36951  1.000 19.20803 ? 37  TYR   A OH  1 
ATOM   279  N N   . CYS   A 1 38  ? -7.99846  -1.74103  -10.46533 1.000 11.41382 ? 38  CYS   A N   1 
ATOM   280  C CA  . CYS   A 1 38  ? -8.59127  -2.71742  -11.36687 1.000 11.61311 ? 38  CYS   A CA  1 
ATOM   281  C C   . CYS   A 1 38  ? -7.50225  -3.67292  -11.82533 1.000 13.84323 ? 38  CYS   A C   1 
ATOM   282  O O   . CYS   A 1 38  ? -6.31441  -3.37794  -11.66935 1.000 13.74747 ? 38  CYS   A O   1 
ATOM   283  C CB  . CYS   A 1 38  ? -9.26576  -2.04021  -12.57226 1.000 12.06648 ? 38  CYS   A CB  1 
ATOM   284  S SG  . CYS   A 1 38  ? -8.14149  -1.31100  -13.79189 1.000 18.24288 ? 38  CYS   A SG  1 
ATOM   285  N N   . PRO   A 1 39  ? -7.87860  -4.82966  -12.37886 1.000 11.06666 ? 39  PRO   A N   1 
ATOM   286  C CA  . PRO   A 1 39  ? -6.87091  -5.78821  -12.85488 1.000 13.73330 ? 39  PRO   A CA  1 
ATOM   287  C C   . PRO   A 1 39  ? -6.03616  -5.18163  -13.97367 1.000 14.79453 ? 39  PRO   A C   1 
ATOM   288  O O   . PRO   A 1 39  ? -6.55562  -4.50022  -14.85805 1.000 14.69458 ? 39  PRO   A O   1 
ATOM   289  C CB  . PRO   A 1 39  ? -7.72191  -6.96320  -13.35696 1.000 13.19781 ? 39  PRO   A CB  1 
ATOM   290  C CG  . PRO   A 1 39  ? -8.99681  -6.85223  -12.59059 1.000 11.66676 ? 39  PRO   A CG  1 
ATOM   291  C CD  . PRO   A 1 39  ? -9.23560  -5.39174  -12.43140 1.000 12.20559 ? 39  PRO   A CD  1 
ATOM   292  N N   . ARG   A 1 40  ? -4.72174  -5.41555  -13.93039 1.000 13.84815 ? 40  ARG   A N   1 
ATOM   293  C CA  . ARG   A 1 40  ? -3.89542  -4.79595  -14.95936 1.000 14.32470 ? 40  ARG   A CA  1 
ATOM   294  C C   . ARG   A 1 40  ? -4.09761  -5.42690  -16.33374 1.000 15.87553 ? 40  ARG   A C   1 
ATOM   295  O O   . ARG   A 1 40  ? -3.72347  -4.80926  -17.33620 1.000 17.31440 ? 40  ARG   A O   1 
ATOM   296  C CB  . ARG   A 1 40  ? -2.41482  -4.84815  -14.57658 1.000 13.89975 ? 40  ARG   A CB  1 
ATOM   297  C CG  . ARG   A 1 40  ? -1.83793  -6.24184  -14.57719 1.000 15.71409 ? 40  ARG   A CG  1 
ATOM   298  C CD  . ARG   A 1 40  ? -0.34563  -6.22180  -14.25081 1.000 14.86176 ? 40  ARG   A CD  1 
ATOM   299  N NE  . ARG   A 1 40  ? 0.20004   -7.57519  -14.26559 1.000 16.31080 ? 40  ARG   A NE  1 
ATOM   300  C CZ  . ARG   A 1 40  ? 1.49723   -7.85401  -14.15661 1.000 20.77168 ? 40  ARG   A CZ  1 
ATOM   301  N NH1 . ARG   A 1 40  ? 2.38087   -6.87858  -13.98579 1.000 18.15574 ? 40  ARG   A NH1 1 
ATOM   302  N NH2 . ARG   A 1 40  ? 1.90843   -9.10808  -14.20867 1.000 16.56937 ? 40  ARG   A NH2 1 
ATOM   303  N N   . HIS   A 1 41  ? -4.67773  -6.63560  -16.41425 1.000 17.58942 ? 41  HIS   A N   1 
ATOM   304  C CA  . HIS   A 1 41  ? -4.86148  -7.20727  -17.74560 1.000 20.65430 ? 41  HIS   A CA  1 
ATOM   305  C C   . HIS   A 1 41  ? -5.90645  -6.46062  -18.56475 1.000 20.57364 ? 41  HIS   A C   1 
ATOM   306  O O   . HIS   A 1 41  ? -6.11293  -6.82807  -19.72049 1.000 21.22788 ? 41  HIS   A O   1 
ATOM   307  C CB  . HIS   A 1 41  ? -5.17208  -8.72249  -17.67580 1.000 17.86792 ? 41  HIS   A CB  1 
ATOM   308  C CG  . HIS   A 1 41  ? -6.51913  -9.09391  -17.11074 1.000 16.41036 ? 41  HIS   A CG  1 
ATOM   309  N ND1 . HIS   A 1 41  ? -7.71541  -8.76327  -17.71788 1.000 20.86892 ? 41  HIS   A ND1 1 
ATOM   310  C CD2 . HIS   A 1 41  ? -6.84453  -9.85556  -16.03934 1.000 19.72581 ? 41  HIS   A CD2 1 
ATOM   311  C CE1 . HIS   A 1 41  ? -8.71930  -9.26605  -17.01635 1.000 20.81709 ? 41  HIS   A CE1 1 
ATOM   312  N NE2 . HIS   A 1 41  ? -8.21809  -9.93145  -15.99146 1.000 17.34546 ? 41  HIS   A NE2 1 
ATOM   313  N N   . VAL   A 1 42  ? -6.51885  -5.40107  -18.01828 1.000 19.03697 ? 42  VAL   A N   1 
ATOM   314  C CA  . VAL   A 1 42  ? -7.35163  -4.51026  -18.82317 1.000 19.97196 ? 42  VAL   A CA  1 
ATOM   315  C C   . VAL   A 1 42  ? -6.56094  -3.83976  -19.94078 1.000 24.58057 ? 42  VAL   A C   1 
ATOM   316  O O   . VAL   A 1 42  ? -7.14880  -3.41704  -20.94174 1.000 27.95279 ? 42  VAL   A O   1 
ATOM   317  C CB  . VAL   A 1 42  ? -8.02122  -3.43525  -17.94125 1.000 20.50963 ? 42  VAL   A CB  1 
ATOM   318  C CG1 . VAL   A 1 42  ? -6.99426  -2.42144  -17.44495 1.000 17.70833 ? 42  VAL   A CG1 1 
ATOM   319  C CG2 . VAL   A 1 42  ? -9.16191  -2.74118  -18.69872 1.000 22.16331 ? 42  VAL   A CG2 1 
ATOM   320  N N   . ILE   A 1 43  ? -5.23574  -3.71764  -19.80966 1.000 22.79755 ? 43  ILE   A N   1 
ATOM   321  C CA  . ILE   A 1 43  ? -4.48790  -3.01890  -20.85185 1.000 27.82454 ? 43  ILE   A CA  1 
ATOM   322  C C   . ILE   A 1 43  ? -4.11851  -3.94377  -21.99583 1.000 28.10405 ? 43  ILE   A C   1 
ATOM   323  O O   . ILE   A 1 43  ? -3.51451  -3.49695  -22.98022 1.000 33.90380 ? 43  ILE   A O   1 
ATOM   324  C CB  . ILE   A 1 43  ? -3.25028  -2.31537  -20.26554 1.000 31.35139 ? 43  ILE   A CB  1 
ATOM   325  C CG1 . ILE   A 1 43  ? -2.29080  -3.30985  -19.62091 1.000 30.65298 ? 43  ILE   A CG1 1 
ATOM   326  C CG2 . ILE   A 1 43  ? -3.69206  -1.29235  -19.23311 1.000 30.08730 ? 43  ILE   A CG2 1 
ATOM   327  C CD1 . ILE   A 1 43  ? -1.06317  -2.63758  -19.01536 1.000 28.45345 ? 43  ILE   A CD1 1 
ATOM   328  N N   . CYS   A 1 44  ? -4.54368  -5.19375  -21.92978 1.000 34.04952 ? 44  CYS   A N   1 
ATOM   329  C CA  . CYS   A 1 44  ? -4.15549  -6.25274  -22.83978 1.000 39.89927 ? 44  CYS   A CA  1 
ATOM   330  C C   . CYS   A 1 44  ? -5.18778  -6.45585  -23.93688 1.000 46.05231 ? 44  CYS   A C   1 
ATOM   331  O O   . CYS   A 1 44  ? -6.39526  -6.42602  -23.68515 1.000 46.78184 ? 44  CYS   A O   1 
ATOM   332  C CB  . CYS   A 1 44  ? -4.00354  -7.55117  -22.06271 1.000 41.05363 ? 44  CYS   A CB  1 
ATOM   333  S SG  . CYS   A 1 44  ? -2.60751  -7.52167  -20.93355 1.000 44.28756 ? 44  CYS   A SG  1 
ATOM   334  N N   . THR   A 1 45  ? -4.70128  -6.68740  -25.14704 1.000 52.85498 ? 45  THR   A N   1 
ATOM   335  C CA  . THR   A 1 45  ? -5.52264  -7.20374  -26.22669 1.000 57.30020 ? 45  THR   A CA  1 
ATOM   336  C C   . THR   A 1 45  ? -5.44135  -8.73145  -26.24080 1.000 62.05154 ? 45  THR   A C   1 
ATOM   337  O O   . THR   A 1 45  ? -4.63298  -9.33984  -25.53522 1.000 61.42304 ? 45  THR   A O   1 
ATOM   338  C CB  . THR   A 1 45  ? -5.07418  -6.60334  -27.55886 1.000 59.21946 ? 45  THR   A CB  1 
ATOM   339  O OG1 . THR   A 1 45  ? -3.79414  -7.13862  -27.92205 1.000 61.36681 ? 45  THR   A OG1 1 
ATOM   340  C CG2 . THR   A 1 45  ? -4.96765  -5.08581  -27.43928 1.000 52.31663 ? 45  THR   A CG2 1 
ATOM   341  N N   . SER   A 1 46  ? -6.29917  -9.35678  -27.05587 1.000 65.29728 ? 46  SER   A N   1 
ATOM   342  C CA  . SER   A 1 46  ? -6.35966  -10.81760 -27.09541 1.000 67.31761 ? 46  SER   A CA  1 
ATOM   343  C C   . SER   A 1 46  ? -5.06672  -11.45328 -27.60238 1.000 68.55862 ? 46  SER   A C   1 
ATOM   344  O O   . SER   A 1 46  ? -4.82188  -12.63461 -27.33322 1.000 67.57131 ? 46  SER   A O   1 
ATOM   345  C CB  . SER   A 1 46  ? -7.54237  -11.27993 -27.94653 1.000 66.46830 ? 46  SER   A CB  1 
ATOM   346  O OG  . SER   A 1 46  ? -8.76021  -11.10961 -27.24357 1.000 68.57778 ? 46  SER   A OG  1 
ATOM   347  N N   . GLU   A 1 47  ? -4.23280  -10.70664 -28.32241 1.000 66.59404 ? 47  GLU   A N   1 
ATOM   348  C CA  . GLU   A 1 47  ? -2.89799  -11.17704 -28.65752 1.000 65.07740 ? 47  GLU   A CA  1 
ATOM   349  C C   . GLU   A 1 47  ? -1.82351  -10.65261 -27.71331 1.000 65.13186 ? 47  GLU   A C   1 
ATOM   350  O O   . GLU   A 1 47  ? -0.74514  -11.25270 -27.64684 1.000 64.28083 ? 47  GLU   A O   1 
ATOM   351  C CB  . GLU   A 1 47  ? -2.53264  -10.78611 -30.08897 1.000 67.40544 ? 47  GLU   A CB  1 
ATOM   352  C CG  . GLU   A 1 47  ? -2.32520  -9.29991  -30.26687 1.000 68.20034 ? 47  GLU   A CG  1 
ATOM   353  C CD  . GLU   A 1 47  ? -3.58015  -8.62249  -30.77496 1.000 69.48561 ? 47  GLU   A CD  1 
ATOM   354  O OE1 . GLU   A 1 47  ? -4.53238  -9.35006  -31.14605 1.000 69.13627 ? 47  GLU   A OE1 1 
ATOM   355  O OE2 . GLU   A 1 47  ? -3.61208  -7.37410  -30.81419 1.000 67.69456 ? 47  GLU   A OE2 1 
ATOM   356  N N   . ASP   A 1 48  ? -2.08591  -9.55563  -26.98833 1.000 64.66595 ? 48  ASP   A N   1 
ATOM   357  C CA  . ASP   A 1 48  ? -1.23954  -9.19569  -25.85573 1.000 62.29020 ? 48  ASP   A CA  1 
ATOM   358  C C   . ASP   A 1 48  ? -1.25229  -10.29718 -24.82240 1.000 62.89949 ? 48  ASP   A C   1 
ATOM   359  O O   . ASP   A 1 48  ? -0.27506  -10.48697 -24.09280 1.000 59.08580 ? 48  ASP   A O   1 
ATOM   360  C CB  . ASP   A 1 48  ? -1.73804  -7.91674  -25.19385 1.000 57.06447 ? 48  ASP   A CB  1 
ATOM   361  C CG  . ASP   A 1 48  ? -1.37293  -6.70212  -25.96129 1.000 54.31778 ? 48  ASP   A CG  1 
ATOM   362  O OD1 . ASP   A 1 48  ? -0.25173  -6.68424  -26.54088 1.000 55.32576 ? 48  ASP   A OD1 1 
ATOM   363  O OD2 . ASP   A 1 48  ? -2.20019  -5.76221  -25.96775 1.000 51.34217 ? 48  ASP   A OD2 1 
ATOM   364  N N   . MET   A 1 49  ? -2.37898  -11.00052 -24.70674 1.000 65.26773 ? 49  MET   A N   1 
ATOM   365  C CA  . MET   A 1 49  ? -2.62336  -11.87604 -23.56652 1.000 62.56156 ? 49  MET   A CA  1 
ATOM   366  C C   . MET   A 1 49  ? -1.97249  -13.24393 -23.73246 1.000 61.46798 ? 49  MET   A C   1 
ATOM   367  O O   . MET   A 1 49  ? -2.49447  -14.25111 -23.25395 1.000 61.72045 ? 49  MET   A O   1 
ATOM   368  C CB  . MET   A 1 49  ? -4.13599  -11.87478 -23.30790 1.000 62.88322 ? 49  MET   A CB  1 
ATOM   369  C CG  . MET   A 1 49  ? -5.02207  -12.42760 -24.39769 1.000 68.09681 ? 49  MET   A CG  1 
ATOM   370  S SD  . MET   A 1 49  ? -6.74574  -12.31638 -23.88022 1.000 79.23213 ? 49  MET   A SD  1 
ATOM   371  C CE  . MET   A 1 49  ? -6.65457  -13.64441 -22.67370 1.000 56.17503 ? 49  MET   A CE  1 
ATOM   372  N N   . LEU   A 1 50  ? -0.73483  -13.24688 -24.25424 1.000 56.76640 ? 50  LEU   A N   1 
ATOM   373  C CA  . LEU   A 1 50  ? -0.04071  -14.46317 -24.69184 1.000 56.98632 ? 50  LEU   A CA  1 
ATOM   374  C C   . LEU   A 1 50  ? 1.38744   -14.56747 -24.12799 1.000 53.30178 ? 50  LEU   A C   1 
ATOM   375  O O   . LEU   A 1 50  ? 1.90534   -15.67901 -23.98302 1.000 52.11848 ? 50  LEU   A O   1 
ATOM   376  C CB  . LEU   A 1 50  ? -0.03165  -14.48506 -26.23267 1.000 63.10019 ? 50  LEU   A CB  1 
ATOM   377  C CG  . LEU   A 1 50  ? -1.45429  -14.60946 -26.83261 1.000 61.27637 ? 50  LEU   A CG  1 
ATOM   378  C CD1 . LEU   A 1 50  ? -1.38153  -14.51005 -28.35523 1.000 62.62469 ? 50  LEU   A CD1 1 
ATOM   379  C CD2 . LEU   A 1 50  ? -2.20862  -15.83815 -26.34275 1.000 56.24647 ? 50  LEU   A CD2 1 
ATOM   380  N N   . ASN   A 1 51  ? 2.04045   -13.42787 -23.80784 1.000 52.59722 ? 51  ASN   A N   1 
ATOM   381  C CA  . ASN   A 1 51  ? 3.20153   -13.41354 -22.91422 1.000 45.44645 ? 51  ASN   A CA  1 
ATOM   382  C C   . ASN   A 1 51  ? 3.59939   -11.96679 -22.61892 1.000 42.32513 ? 51  ASN   A C   1 
ATOM   383  O O   . ASN   A 1 51  ? 4.64602   -11.49621 -23.07820 1.000 44.80571 ? 51  ASN   A O   1 
ATOM   384  C CB  . ASN   A 1 51  ? 4.37611   -14.17693 -23.51790 1.000 49.58106 ? 51  ASN   A CB  1 
ATOM   385  C CG  . ASN   A 1 51  ? 5.27657   -14.80290 -22.44063 1.000 50.21405 ? 51  ASN   A CG  1 
ATOM   386  O OD1 . ASN   A 1 51  ? 5.42768   -14.26122 -21.33716 1.000 46.08019 ? 51  ASN   A OD1 1 
ATOM   387  N ND2 . ASN   A 1 51  ? 5.85184   -15.96327 -22.75128 1.000 47.53579 ? 51  ASN   A ND2 1 
ATOM   388  N N   . PRO   A 1 52  ? 2.80611   -11.24830 -21.83112 1.000 42.72081 ? 52  PRO   A N   1 
ATOM   389  C CA  . PRO   A 1 52  ? 2.87395   -9.78170  -21.84247 1.000 37.79880 ? 52  PRO   A CA  1 
ATOM   390  C C   . PRO   A 1 52  ? 4.07336   -9.26249  -21.07420 1.000 36.79881 ? 52  PRO   A C   1 
ATOM   391  O O   . PRO   A 1 52  ? 4.42468   -9.78494  -20.01533 1.000 34.77893 ? 52  PRO   A O   1 
ATOM   392  C CB  . PRO   A 1 52  ? 1.60369   -9.38218  -21.09764 1.000 38.04263 ? 52  PRO   A CB  1 
ATOM   393  C CG  . PRO   A 1 52  ? 0.70133   -10.52085 -21.26174 1.000 41.65268 ? 52  PRO   A CG  1 
ATOM   394  C CD  . PRO   A 1 52  ? 1.53886   -11.74303 -21.27223 1.000 39.78893 ? 52  PRO   A CD  1 
ATOM   395  N N   . ASN   A 1 53  ? 4.66992   -8.19469  -21.59063 1.000 33.37148 ? 53  ASN   A N   1 
ATOM   396  C CA  . ASN   A 1 53  ? 5.52374   -7.34505  -20.77345 1.000 33.22457 ? 53  ASN   A CA  1 
ATOM   397  C C   . ASN   A 1 53  ? 4.64709   -6.16818  -20.35520 1.000 30.42025 ? 53  ASN   A C   1 
ATOM   398  O O   . ASN   A 1 53  ? 4.48685   -5.19819  -21.10434 1.000 27.12347 ? 53  ASN   A O   1 
ATOM   399  C CB  . ASN   A 1 53  ? 6.76675   -6.89664  -21.52651 1.000 32.09410 ? 53  ASN   A CB  1 
ATOM   400  C CG  . ASN   A 1 53  ? 7.74750   -6.18900  -20.62261 1.000 33.24073 ? 53  ASN   A CG  1 
ATOM   401  O OD1 . ASN   A 1 53  ? 7.37856   -5.28512  -19.87085 1.000 32.00246 ? 53  ASN   A OD1 1 
ATOM   402  N ND2 . ASN   A 1 53  ? 9.00515   -6.60156  -20.67988 1.000 36.02196 ? 53  ASN   A ND2 1 
ATOM   403  N N   . TYR   A 1 54  ? 4.05352   -6.27027  -19.16296 1.000 28.27195 ? 54  TYR   A N   1 
ATOM   404  C CA  . TYR   A 1 54  ? 3.07690   -5.27077  -18.73960 1.000 25.33166 ? 54  TYR   A CA  1 
ATOM   405  C C   . TYR   A 1 54  ? 3.68593   -3.88822  -18.59571 1.000 25.18815 ? 54  TYR   A C   1 
ATOM   406  O O   . TYR   A 1 54  ? 3.00507   -2.88251  -18.82422 1.000 23.90231 ? 54  TYR   A O   1 
ATOM   407  C CB  . TYR   A 1 54  ? 2.42358   -5.68065  -17.42450 1.000 22.48767 ? 54  TYR   A CB  1 
ATOM   408  C CG  . TYR   A 1 54  ? 1.34481   -6.69230  -17.60830 1.000 24.40297 ? 54  TYR   A CG  1 
ATOM   409  C CD1 . TYR   A 1 54  ? 0.06777   -6.28825  -17.96962 1.000 22.83111 ? 54  TYR   A CD1 1 
ATOM   410  C CD2 . TYR   A 1 54  ? 1.57903   -8.04922  -17.39165 1.000 23.78628 ? 54  TYR   A CD2 1 
ATOM   411  C CE1 . TYR   A 1 54  ? -0.94021  -7.19227  -18.12891 1.000 23.10158 ? 54  TYR   A CE1 1 
ATOM   412  C CE2 . TYR   A 1 54  ? 0.56759   -8.97185  -17.55212 1.000 21.05670 ? 54  TYR   A CE2 1 
ATOM   413  C CZ  . TYR   A 1 54  ? -0.69636  -8.52753  -17.92043 1.000 24.25858 ? 54  TYR   A CZ  1 
ATOM   414  O OH  . TYR   A 1 54  ? -1.72233  -9.41676  -18.09242 1.000 22.53629 ? 54  TYR   A OH  1 
ATOM   415  N N   . GLU   A 1 55  ? 4.95035   -3.80937  -18.20287 1.000 28.08338 ? 55  GLU   A N   1 
ATOM   416  C CA  . GLU   A 1 55  ? 5.58234   -2.50428  -18.09824 1.000 27.00426 ? 55  GLU   A CA  1 
ATOM   417  C C   . GLU   A 1 55  ? 5.67701   -1.84629  -19.46771 1.000 27.12529 ? 55  GLU   A C   1 
ATOM   418  O O   . GLU   A 1 55  ? 5.38462   -0.65280  -19.60961 1.000 25.21597 ? 55  GLU   A O   1 
ATOM   419  C CB  . GLU   A 1 55  ? 6.94230   -2.66346  -17.42858 1.000 28.93416 ? 55  GLU   A CB  1 
ATOM   420  C CG  . GLU   A 1 55  ? 6.77926   -3.00571  -15.95274 1.000 33.94224 ? 55  GLU   A CG  1 
ATOM   421  C CD  . GLU   A 1 55  ? 6.81370   -4.50768  -15.70083 1.000 40.14783 ? 55  GLU   A CD  1 
ATOM   422  O OE1 . GLU   A 1 55  ? 7.05686   -4.92069  -14.54423 1.000 41.57922 ? 55  GLU   A OE1 1 
ATOM   423  O OE2 . GLU   A 1 55  ? 6.57605   -5.27927  -16.66053 1.000 37.55074 ? 55  GLU   A OE2 1 
ATOM   424  N N   . ASP   A 1 56  ? 6.04918   -2.61550  -20.49614 1.000 29.47459 ? 56  ASP   A N   1 
ATOM   425  C CA  . ASP   A 1 56  ? 6.03627   -2.07262  -21.85324 1.000 29.73014 ? 56  ASP   A CA  1 
ATOM   426  C C   . ASP   A 1 56  ? 4.62249   -1.70785  -22.28664 1.000 28.17855 ? 56  ASP   A C   1 
ATOM   427  O O   . ASP   A 1 56  ? 4.40195   -0.65468  -22.89528 1.000 25.01714 ? 56  ASP   A O   1 
ATOM   428  C CB  . ASP   A 1 56  ? 6.64776   -3.06290  -22.84885 1.000 33.63502 ? 56  ASP   A CB  1 
ATOM   429  C CG  . ASP   A 1 56  ? 8.13757   -3.23563  -22.66996 1.000 35.26475 ? 56  ASP   A CG  1 
ATOM   430  O OD1 . ASP   A 1 56  ? 8.79663   -2.28947  -22.20035 1.000 34.81530 ? 56  ASP   A OD1 1 
ATOM   431  O OD2 . ASP   A 1 56  ? 8.65586   -4.31502  -23.02423 1.000 42.67503 ? 56  ASP   A OD2 1 
ATOM   432  N N   . LEU   A 1 57  ? 3.64735   -2.56526  -21.98267 1.000 25.82692 ? 57  LEU   A N   1 
ATOM   433  C CA  . LEU   A 1 57  ? 2.27834   -2.26433  -22.37319 1.000 25.68362 ? 57  LEU   A CA  1 
ATOM   434  C C   . LEU   A 1 57  ? 1.79479   -0.97731  -21.72315 1.000 25.62359 ? 57  LEU   A C   1 
ATOM   435  O O   . LEU   A 1 57  ? 1.09002   -0.18427  -22.35680 1.000 23.47242 ? 57  LEU   A O   1 
ATOM   436  C CB  . LEU   A 1 57  ? 1.35830   -3.43057  -22.01414 1.000 26.86350 ? 57  LEU   A CB  1 
ATOM   437  C CG  . LEU   A 1 57  ? 1.66803   -4.71496  -22.78447 1.000 31.43097 ? 57  LEU   A CG  1 
ATOM   438  C CD1 . LEU   A 1 57  ? 0.60329   -5.75291  -22.52211 1.000 29.99681 ? 57  LEU   A CD1 1 
ATOM   439  C CD2 . LEU   A 1 57  ? 1.76184   -4.42838  -24.27627 1.000 29.87234 ? 57  LEU   A CD2 1 
ATOM   440  N N   . LEU   A 1 58  ? 2.19090   -0.73560  -20.47036 1.000 24.41612 ? 58  LEU   A N   1 
ATOM   441  C CA  . LEU   A 1 58  ? 1.62870   0.38870   -19.73263 1.000 23.09967 ? 58  LEU   A CA  1 
ATOM   442  C C   . LEU   A 1 58  ? 2.27604   1.70988   -20.14338 1.000 22.59778 ? 58  LEU   A C   1 
ATOM   443  O O   . LEU   A 1 58  ? 1.60183   2.74466   -20.18005 1.000 22.95375 ? 58  LEU   A O   1 
ATOM   444  C CB  . LEU   A 1 58  ? 1.77565   0.16435   -18.22506 1.000 23.93424 ? 58  LEU   A CB  1 
ATOM   445  C CG  . LEU   A 1 58  ? 1.06250   1.23154   -17.37868 1.000 26.88632 ? 58  LEU   A CG  1 
ATOM   446  C CD1 . LEU   A 1 58  ? -0.39778  1.31568   -17.77802 1.000 23.26368 ? 58  LEU   A CD1 1 
ATOM   447  C CD2 . LEU   A 1 58  ? 1.19750   0.97886   -15.88796 1.000 25.70758 ? 58  LEU   A CD2 1 
ATOM   448  N N   . ILE   A 1 59  ? 3.57635   1.70165   -20.45456 1.000 23.57827 ? 59  ILE   A N   1 
ATOM   449  C CA  . ILE   A 1 59  ? 4.22499   2.93291   -20.89859 1.000 25.12885 ? 59  ILE   A CA  1 
ATOM   450  C C   . ILE   A 1 59  ? 3.64431   3.43377   -22.21833 1.000 26.26867 ? 59  ILE   A C   1 
ATOM   451  O O   . ILE   A 1 59  ? 3.71854   4.63433   -22.51218 1.000 27.43732 ? 59  ILE   A O   1 
ATOM   452  C CB  . ILE   A 1 59  ? 5.76271   2.74870   -20.99562 1.000 26.49723 ? 59  ILE   A CB  1 
ATOM   453  C CG1 . ILE   A 1 59  ? 6.44179   4.10237   -21.17542 1.000 27.64225 ? 59  ILE   A CG1 1 
ATOM   454  C CG2 . ILE   A 1 59  ? 6.14808   1.86327   -22.15322 1.000 26.80612 ? 59  ILE   A CG2 1 
ATOM   455  C CD1 . ILE   A 1 59  ? 6.22525   5.02967   -20.02213 1.000 29.86577 ? 59  ILE   A CD1 1 
ATOM   456  N N   . ARG   A 1 60  ? 3.05494   2.55006   -23.02030 1.000 26.09885 ? 60  ARG   A N   1 
ATOM   457  C CA  . ARG   A 1 60  ? 2.41086   2.96103   -24.26240 1.000 27.24995 ? 60  ARG   A CA  1 
ATOM   458  C C   . ARG   A 1 60  ? 0.99965   3.49003   -24.06586 1.000 26.72143 ? 60  ARG   A C   1 
ATOM   459  O O   . ARG   A 1 60  ? 0.38589   3.93075   -25.04316 1.000 27.77744 ? 60  ARG   A O   1 
ATOM   460  C CB  . ARG   A 1 60  ? 2.41700   1.79672   -25.25352 1.000 27.59235 ? 60  ARG   A CB  1 
ATOM   461  C CG  . ARG   A 1 60  ? 3.79460   1.17633   -25.40446 1.000 28.16691 ? 60  ARG   A CG  1 
ATOM   462  C CD  . ARG   A 1 60  ? 3.76831   -0.09659  -26.20514 1.000 28.42279 ? 60  ARG   A CD  1 
ATOM   463  N NE  . ARG   A 1 60  ? 5.09899   -0.68840  -26.24286 1.000 29.01826 ? 60  ARG   A NE  1 
ATOM   464  C CZ  . ARG   A 1 60  ? 5.35612   -1.93469  -26.61812 1.000 35.56188 ? 60  ARG   A CZ  1 
ATOM   465  N NH1 . ARG   A 1 60  ? 4.35576   -2.75540  -26.92046 1.000 33.48873 ? 60  ARG   A NH1 1 
ATOM   466  N NH2 . ARG   A 1 60  ? 6.61218   -2.37835  -26.62584 1.000 35.43848 ? 60  ARG   A NH2 1 
ATOM   467  N N   . LYS   A 1 61  ? 0.48845   3.48382   -22.84026 1.000 25.66173 ? 61  LYS   A N   1 
ATOM   468  C CA  . LYS   A 1 61  ? -0.85434  3.95329   -22.55327 1.000 26.51411 ? 61  LYS   A CA  1 
ATOM   469  C C   . LYS   A 1 61  ? -0.82077  5.42996   -22.17542 1.000 28.31092 ? 61  LYS   A C   1 
ATOM   470  O O   . LYS   A 1 61  ? 0.21609   5.97427   -21.78713 1.000 27.36366 ? 61  LYS   A O   1 
ATOM   471  C CB  . LYS   A 1 61  ? -1.48002  3.13930   -21.41802 1.000 24.56811 ? 61  LYS   A CB  1 
ATOM   472  C CG  . LYS   A 1 61  ? -1.39972  1.65206   -21.64500 1.000 24.79590 ? 61  LYS   A CG  1 
ATOM   473  C CD  . LYS   A 1 61  ? -2.26669  1.20566   -22.77257 1.000 28.14871 ? 61  LYS   A CD  1 
ATOM   474  C CE  . LYS   A 1 61  ? -3.69593  1.50605   -22.49132 1.000 32.39765 ? 61  LYS   A CE  1 
ATOM   475  N NZ  . LYS   A 1 61  ? -4.58574  0.67546   -23.35231 1.000 34.06726 ? 61  LYS   A NZ  1 
ATOM   476  N N   . SER   A 1 62  ? -1.97927  6.07321   -22.30329 1.000 33.01420 ? 62  SER   A N   1 
ATOM   477  C CA  . SER   A 1 62  ? -2.20653  7.45402   -21.90167 1.000 31.17209 ? 62  SER   A CA  1 
ATOM   478  C C   . SER   A 1 62  ? -3.35662  7.47952   -20.90239 1.000 27.70263 ? 62  SER   A C   1 
ATOM   479  O O   . SER   A 1 62  ? -4.19322  6.57658   -20.89985 1.000 30.28995 ? 62  SER   A O   1 
ATOM   480  C CB  . SER   A 1 62  ? -2.56682  8.33890   -23.10887 1.000 31.74559 ? 62  SER   A CB  1 
ATOM   481  O OG  . SER   A 1 62  ? -1.70687  8.11910   -24.22317 1.000 39.31480 ? 62  SER   A OG  1 
ATOM   482  N N   . ASN   A 1 63  ? -3.40212  8.51585   -20.05424 1.000 28.04029 ? 63  ASN   A N   1 
ATOM   483  C CA  . ASN   A 1 63  ? -4.54676  8.68083   -19.15236 1.000 27.69041 ? 63  ASN   A CA  1 
ATOM   484  C C   . ASN   A 1 63  ? -5.86782  8.58243   -19.90809 1.000 28.21755 ? 63  ASN   A C   1 
ATOM   485  O O   . ASN   A 1 63  ? -6.80663  7.90833   -19.46265 1.000 25.76454 ? 63  ASN   A O   1 
ATOM   486  C CB  . ASN   A 1 63  ? -4.45914  10.02177  -18.41576 1.000 27.91463 ? 63  ASN   A CB  1 
ATOM   487  C CG  . ASN   A 1 63  ? -3.37272  10.03717  -17.34591 1.000 27.47655 ? 63  ASN   A CG  1 
ATOM   488  O OD1 . ASN   A 1 63  ? -2.98518  8.99320   -16.83435 1.000 27.88947 ? 63  ASN   A OD1 1 
ATOM   489  N ND2 . ASN   A 1 63  ? -2.86246  11.22806  -17.02410 1.000 26.91843 ? 63  ASN   A ND2 1 
ATOM   490  N N   . HIS   A 1 64  ? -5.95405  9.24489   -21.06444 1.000 29.16471 ? 64  HIS   A N   1 
ATOM   491  C CA  . HIS   A 1 64  ? -7.19403  9.27387   -21.82724 1.000 30.25982 ? 64  HIS   A CA  1 
ATOM   492  C C   . HIS   A 1 64  ? -7.54498  7.92943   -22.44967 1.000 27.74604 ? 64  HIS   A C   1 
ATOM   493  O O   . HIS   A 1 64  ? -8.69158  7.75015   -22.87290 1.000 28.57499 ? 64  HIS   A O   1 
ATOM   494  C CB  . HIS   A 1 64  ? -7.12319  10.36948  -22.89640 1.000 31.47299 ? 64  HIS   A CB  1 
ATOM   495  C CG  . HIS   A 1 64  ? -6.40954  9.96535   -24.15074 1.000 34.12218 ? 64  HIS   A CG  1 
ATOM   496  N ND1 . HIS   A 1 64  ? -5.05977  10.18606  -24.34188 1.000 36.42500 ? 64  HIS   A ND1 1 
ATOM   497  C CD2 . HIS   A 1 64  ? -6.86424  9.40308   -25.29719 1.000 33.86303 ? 64  HIS   A CD2 1 
ATOM   498  C CE1 . HIS   A 1 64  ? -4.70876  9.74961   -25.53978 1.000 34.17668 ? 64  HIS   A CE1 1 
ATOM   499  N NE2 . HIS   A 1 64  ? -5.78556  9.27325   -26.14168 1.000 37.69382 ? 64  HIS   A NE2 1 
ATOM   500  N N   . ASN   A 1 65  ? -6.61490  6.97265   -22.48890 1.000 27.30700 ? 65  ASN   A N   1 
ATOM   501  C CA  . ASN   A 1 65  ? -6.98478  5.63224   -22.93077 1.000 25.69669 ? 65  ASN   A CA  1 
ATOM   502  C C   . ASN   A 1 65  ? -7.90617  4.92503   -21.94479 1.000 28.09541 ? 65  ASN   A C   1 
ATOM   503  O O   . ASN   A 1 65  ? -8.49916  3.90569   -22.30351 1.000 29.49528 ? 65  ASN   A O   1 
ATOM   504  C CB  . ASN   A 1 65  ? -5.74705  4.76450   -23.15397 1.000 28.59340 ? 65  ASN   A CB  1 
ATOM   505  C CG  . ASN   A 1 65  ? -4.84417  5.29776   -24.22772 1.000 32.50447 ? 65  ASN   A CG  1 
ATOM   506  O OD1 . ASN   A 1 65  ? -3.62365  5.15992   -24.15223 1.000 30.79872 ? 65  ASN   A OD1 1 
ATOM   507  N ND2 . ASN   A 1 65  ? -5.43796  5.89318   -25.25603 1.000 31.44015 ? 65  ASN   A ND2 1 
ATOM   508  N N   . PHE   A 1 66  ? -8.02659  5.42628   -20.71711 1.000 27.00878 ? 66  PHE   A N   1 
ATOM   509  C CA  . PHE   A 1 66  ? -8.81239  4.77880   -19.67081 1.000 25.86772 ? 66  PHE   A CA  1 
ATOM   510  C C   . PHE   A 1 66  ? -10.11920 5.53957   -19.48224 1.000 27.29178 ? 66  PHE   A C   1 
ATOM   511  O O   . PHE   A 1 66  ? -10.12480 6.65977   -18.96249 1.000 26.20102 ? 66  PHE   A O   1 
ATOM   512  C CB  . PHE   A 1 66  ? -8.03049  4.72498   -18.36293 1.000 22.23605 ? 66  PHE   A CB  1 
ATOM   513  C CG  . PHE   A 1 66  ? -6.77412  3.91008   -18.43907 1.000 21.72651 ? 66  PHE   A CG  1 
ATOM   514  C CD1 . PHE   A 1 66  ? -6.81440  2.53869   -18.27450 1.000 24.10502 ? 66  PHE   A CD1 1 
ATOM   515  C CD2 . PHE   A 1 66  ? -5.55930  4.51685   -18.69339 1.000 25.20176 ? 66  PHE   A CD2 1 
ATOM   516  C CE1 . PHE   A 1 66  ? -5.66894  1.78758   -18.34690 1.000 24.71566 ? 66  PHE   A CE1 1 
ATOM   517  C CE2 . PHE   A 1 66  ? -4.40523  3.76770   -18.76581 1.000 26.94026 ? 66  PHE   A CE2 1 
ATOM   518  C CZ  . PHE   A 1 66  ? -4.46255  2.40169   -18.58854 1.000 24.45339 ? 66  PHE   A CZ  1 
ATOM   519  N N   . LEU   A 1 67  ? -11.22080 4.92607   -19.90032 1.000 25.37898 ? 67  LEU   A N   1 
ATOM   520  C CA  . LEU   A 1 67  ? -12.55116 5.47617   -19.67803 1.000 28.21235 ? 67  LEU   A CA  1 
ATOM   521  C C   . LEU   A 1 67  ? -13.07673 4.90997   -18.36695 1.000 23.35328 ? 67  LEU   A C   1 
ATOM   522  O O   . LEU   A 1 67  ? -13.28006 3.69905   -18.25574 1.000 24.61554 ? 67  LEU   A O   1 
ATOM   523  C CB  . LEU   A 1 67  ? -13.49291 5.11555   -20.82824 1.000 28.92296 ? 67  LEU   A CB  1 
ATOM   524  C CG  . LEU   A 1 67  ? -13.54682 5.98222   -22.09285 1.000 34.06690 ? 67  LEU   A CG  1 
ATOM   525  C CD1 . LEU   A 1 67  ? -14.14158 7.36677   -21.81027 1.000 34.57658 ? 67  LEU   A CD1 1 
ATOM   526  C CD2 . LEU   A 1 67  ? -12.18054 6.08966   -22.73872 1.000 32.81226 ? 67  LEU   A CD2 1 
ATOM   527  N N   . VAL   A 1 68  ? -13.27359 5.77081   -17.37325 1.000 25.47971 ? 68  VAL   A N   1 
ATOM   528  C CA  . VAL   A 1 68  ? -13.79755 5.36522   -16.07151 1.000 22.83665 ? 68  VAL   A CA  1 
ATOM   529  C C   . VAL   A 1 68  ? -15.17375 5.99585   -15.89100 1.000 24.68729 ? 68  VAL   A C   1 
ATOM   530  O O   . VAL   A 1 68  ? -15.31276 7.22595   -15.93624 1.000 23.31268 ? 68  VAL   A O   1 
ATOM   531  C CB  . VAL   A 1 68  ? -12.85006 5.75885   -14.92662 1.000 24.88694 ? 68  VAL   A CB  1 
ATOM   532  C CG1 . VAL   A 1 68  ? -13.43353 5.32846   -13.59263 1.000 24.69875 ? 68  VAL   A CG1 1 
ATOM   533  C CG2 . VAL   A 1 68  ? -11.48346 5.11246   -15.12376 1.000 22.25665 ? 68  VAL   A CG2 1 
ATOM   534  N N   . GLN   A 1 69  ? -16.18156 5.14750   -15.67649 1.000 22.63911 ? 69  GLN   A N   1 
ATOM   535  C CA  . GLN   A 1 69  ? -17.58565 5.52811   -15.55247 1.000 27.40122 ? 69  GLN   A CA  1 
ATOM   536  C C   . GLN   A 1 69  ? -18.04238 5.19148   -14.13770 1.000 24.89543 ? 69  GLN   A C   1 
ATOM   537  O O   . GLN   A 1 69  ? -18.00673 4.02251   -13.74023 1.000 22.46319 ? 69  GLN   A O   1 
ATOM   538  C CB  . GLN   A 1 69  ? -18.44309 4.75433   -16.55873 1.000 28.33405 ? 69  GLN   A CB  1 
ATOM   539  C CG  . GLN   A 1 69  ? -18.25352 5.01922   -18.04740 1.000 32.30296 ? 69  GLN   A CG  1 
ATOM   540  C CD  . GLN   A 1 69  ? -19.21147 6.07002   -18.57700 1.000 38.10243 ? 69  GLN   A CD  1 
ATOM   541  O OE1 . GLN   A 1 69  ? -19.07668 7.26103   -18.29648 1.000 41.40317 ? 69  GLN   A OE1 1 
ATOM   542  N NE2 . GLN   A 1 69  ? -20.22266 5.61679   -19.31933 1.000 44.17042 ? 69  GLN   A NE2 1 
ATOM   543  N N   . ALA   A 1 70  ? -18.46850 6.19686   -13.38124 1.000 26.16798 ? 70  ALA   A N   1 
ATOM   544  C CA  . ALA   A 1 70  ? -19.06380 5.97073   -12.06281 1.000 27.55283 ? 70  ALA   A CA  1 
ATOM   545  C C   . ALA   A 1 70  ? -20.55462 6.25515   -12.20199 1.000 32.26203 ? 70  ALA   A C   1 
ATOM   546  O O   . ALA   A 1 70  ? -20.98142 7.41200   -12.17043 1.000 30.12141 ? 70  ALA   A O   1 
ATOM   547  C CB  . ALA   A 1 70  ? -18.41536 6.83715   -10.98617 1.000 26.09182 ? 70  ALA   A CB  1 
ATOM   548  N N   . GLY   A 1 71  ? -21.34331 5.19676   -12.35108 1.000 32.54552 ? 71  GLY   A N   1 
ATOM   549  C CA  . GLY   A 1 71  ? -22.72423 5.39407   -12.74983 1.000 35.93305 ? 71  GLY   A CA  1 
ATOM   550  C C   . GLY   A 1 71  ? -22.74446 6.03492   -14.11993 1.000 39.01256 ? 71  GLY   A C   1 
ATOM   551  O O   . GLY   A 1 71  ? -22.03008 5.61455   -15.03796 1.000 40.27310 ? 71  GLY   A O   1 
ATOM   552  N N   . ASN   A 1 72  ? -23.54752 7.08750   -14.26508 1.000 41.15340 ? 72  ASN   A N   1 
ATOM   553  C CA  . ASN   A 1 72  ? -23.60287 7.85479   -15.50155 1.000 43.95274 ? 72  ASN   A CA  1 
ATOM   554  C C   . ASN   A 1 72  ? -22.75090 9.11814   -15.42840 1.000 43.63896 ? 72  ASN   A C   1 
ATOM   555  O O   . ASN   A 1 72  ? -23.09726 10.14071  -16.03338 1.000 43.09344 ? 72  ASN   A O   1 
ATOM   556  C CB  . ASN   A 1 72  ? -25.05416 8.18963   -15.85593 1.000 44.12333 ? 72  ASN   A CB  1 
ATOM   557  C CG  . ASN   A 1 72  ? -25.80301 8.85849   -14.71127 1.000 51.09133 ? 72  ASN   A CG  1 
ATOM   558  O OD1 . ASN   A 1 72  ? -25.19432 9.40373   -13.78911 1.000 55.31387 ? 72  ASN   A OD1 1 
ATOM   559  N ND2 . ASN   A 1 72  ? -27.13345 8.82449   -14.77076 1.000 47.57454 ? 72  ASN   A ND2 1 
ATOM   560  N N   . VAL   A 1 73  ? -21.63972 9.06285   -14.69536 1.000 38.82499 ? 73  VAL   A N   1 
ATOM   561  C CA  . VAL   A 1 73  ? -20.72674 10.19176  -14.53477 1.000 39.34119 ? 73  VAL   A CA  1 
ATOM   562  C C   . VAL   A 1 73  ? -19.32935 9.71734   -14.91483 1.000 34.70525 ? 73  VAL   A C   1 
ATOM   563  O O   . VAL   A 1 73  ? -18.84127 8.72174   -14.36921 1.000 32.91404 ? 73  VAL   A O   1 
ATOM   564  C CB  . VAL   A 1 73  ? -20.75251 10.74156  -13.09763 1.000 39.53460 ? 73  VAL   A CB  1 
ATOM   565  C CG1 . VAL   A 1 73  ? -19.61854 11.72741  -12.87237 1.000 37.63638 ? 73  VAL   A CG1 1 
ATOM   566  C CG2 . VAL   A 1 73  ? -22.09339 11.38624  -12.79946 1.000 42.49521 ? 73  VAL   A CG2 1 
ATOM   567  N N   . GLN   A 1 74  ? -18.69099 10.41574  -15.85092 1.000 36.89841 ? 74  GLN   A N   1 
ATOM   568  C CA  . GLN   A 1 74  ? -17.33771 10.05399  -16.25462 1.000 35.90286 ? 74  GLN   A CA  1 
ATOM   569  C C   . GLN   A 1 74  ? -16.30883 10.62974  -15.29092 1.000 34.24786 ? 74  GLN   A C   1 
ATOM   570  O O   . GLN   A 1 74  ? -16.39256 11.79541  -14.89519 1.000 35.99215 ? 74  GLN   A O   1 
ATOM   571  C CB  . GLN   A 1 74  ? -17.01547 10.55130  -17.66396 1.000 39.38744 ? 74  GLN   A CB  1 
ATOM   572  C CG  . GLN   A 1 74  ? -15.62228 10.09628  -18.08377 1.000 39.29591 ? 74  GLN   A CG  1 
ATOM   573  C CD  . GLN   A 1 74  ? -15.22055 10.51745  -19.47965 1.000 44.25311 ? 74  GLN   A CD  1 
ATOM   574  O OE1 . GLN   A 1 74  ? -15.96506 11.20745  -20.18168 1.000 48.20161 ? 74  GLN   A OE1 1 
ATOM   575  N NE2 . GLN   A 1 74  ? -14.00791 10.14430  -19.87296 1.000 41.42126 ? 74  GLN   A NE2 1 
ATOM   576  N N   . LEU   A 1 75  ? -15.31213 9.81589   -14.95069 1.000 28.34101 ? 75  LEU   A N   1 
ATOM   577  C CA  . LEU   A 1 75  ? -14.21922 10.21801  -14.07600 1.000 27.72740 ? 75  LEU   A CA  1 
ATOM   578  C C   . LEU   A 1 75  ? -12.96691 10.45029  -14.91435 1.000 31.28616 ? 75  LEU   A C   1 
ATOM   579  O O   . LEU   A 1 75  ? -12.47953 9.52635   -15.57534 1.000 33.17004 ? 75  LEU   A O   1 
ATOM   580  C CB  . LEU   A 1 75  ? -13.95215 9.14608   -13.02122 1.000 28.00297 ? 75  LEU   A CB  1 
ATOM   581  C CG  . LEU   A 1 75  ? -14.94978 9.02620   -11.87125 1.000 27.97532 ? 75  LEU   A CG  1 
ATOM   582  C CD1 . LEU   A 1 75  ? -14.41052 8.04292   -10.85162 1.000 27.43214 ? 75  LEU   A CD1 1 
ATOM   583  C CD2 . LEU   A 1 75  ? -15.23077 10.37535  -11.22585 1.000 32.96619 ? 75  LEU   A CD2 1 
ATOM   584  N N   . ARG   A 1 76  ? -12.43888 11.67004  -14.87237 1.000 28.14359 ? 76  ARG   A N   1 
ATOM   585  C CA  . ARG   A 1 76  ? -11.20409 11.97869  -15.58440 1.000 31.26012 ? 76  ARG   A CA  1 
ATOM   586  C C   . ARG   A 1 76  ? -10.01570 11.31795  -14.89665 1.000 28.78452 ? 76  ARG   A C   1 
ATOM   587  O O   . ARG   A 1 76  ? -9.73921  11.59487  -13.72467 1.000 26.45320 ? 76  ARG   A O   1 
ATOM   588  C CB  . ARG   A 1 76  ? -10.98420 13.48758  -15.65344 1.000 32.83643 ? 76  ARG   A CB  1 
ATOM   589  C CG  . ARG   A 1 76  ? -9.89759  13.89701  -16.63608 1.000 33.78318 ? 76  ARG   A CG  1 
ATOM   590  C CD  . ARG   A 1 76  ? -9.90109  15.39046  -16.85731 1.000 40.32859 ? 76  ARG   A CD  1 
ATOM   591  N NE  . ARG   A 1 76  ? -9.55636  16.09646  -15.62599 1.000 42.72452 ? 76  ARG   A NE  1 
ATOM   592  C CZ  . ARG   A 1 76  ? -8.41798  16.76039  -15.44183 1.000 46.57944 ? 76  ARG   A CZ  1 
ATOM   593  N NH1 . ARG   A 1 76  ? -7.51536  16.81804  -16.41636 1.000 47.61514 ? 76  ARG   A NH1 1 
ATOM   594  N NH2 . ARG   A 1 76  ? -8.18147  17.37329  -14.28557 1.000 48.69506 ? 76  ARG   A NH2 1 
ATOM   595  N N   . VAL   A 1 77  ? -9.30443  10.46715  -15.63153 1.000 29.02483 ? 77  VAL   A N   1 
ATOM   596  C CA  . VAL   A 1 77  ? -8.07345  9.85515   -15.13877 1.000 25.67760 ? 77  VAL   A CA  1 
ATOM   597  C C   . VAL   A 1 77  ? -6.93420  10.85746  -15.28892 1.000 26.83336 ? 77  VAL   A C   1 
ATOM   598  O O   . VAL   A 1 77  ? -6.73419  11.42997  -16.36730 1.000 26.06839 ? 77  VAL   A O   1 
ATOM   599  C CB  . VAL   A 1 77  ? -7.77166  8.55458   -15.89817 1.000 24.46764 ? 77  VAL   A CB  1 
ATOM   600  C CG1 . VAL   A 1 77  ? -6.47394  7.93216   -15.40146 1.000 24.30949 ? 77  VAL   A CG1 1 
ATOM   601  C CG2 . VAL   A 1 77  ? -8.92252  7.55653   -15.73461 1.000 24.89434 ? 77  VAL   A CG2 1 
ATOM   602  N N   . ILE   A 1 78  ? -6.18797  11.07855  -14.20752 1.000 26.40860 ? 78  ILE   A N   1 
ATOM   603  C CA  . ILE   A 1 78  ? -5.10000  12.05061  -14.18910 1.000 26.00083 ? 78  ILE   A CA  1 
ATOM   604  C C   . ILE   A 1 78  ? -3.75056  11.41075  -13.90931 1.000 26.95311 ? 78  ILE   A C   1 
ATOM   605  O O   . ILE   A 1 78  ? -2.72960  12.10620  -13.92107 1.000 30.38462 ? 78  ILE   A O   1 
ATOM   606  C CB  . ILE   A 1 78  ? -5.38073  13.18313  -13.18087 1.000 27.02410 ? 78  ILE   A CB  1 
ATOM   607  C CG1 . ILE   A 1 78  ? -5.48663  12.62586  -11.75464 1.000 26.90472 ? 78  ILE   A CG1 1 
ATOM   608  C CG2 . ILE   A 1 78  ? -6.63624  13.94873  -13.57971 1.000 29.62972 ? 78  ILE   A CG2 1 
ATOM   609  C CD1 . ILE   A 1 78  ? -5.29195  13.69150  -10.68358 1.000 32.34061 ? 78  ILE   A CD1 1 
ATOM   610  N N   . GLY   A 1 79  ? -3.71591  10.10649  -13.67088 1.000 25.62199 ? 79  GLY   A N   1 
ATOM   611  C CA  . GLY   A 1 79  ? -2.47053  9.39055   -13.49152 1.000 23.21561 ? 79  GLY   A CA  1 
ATOM   612  C C   . GLY   A 1 79  ? -2.75786  7.90989   -13.53491 1.000 22.80418 ? 79  GLY   A C   1 
ATOM   613  O O   . GLY   A 1 79  ? -3.90196  7.47878   -13.35922 1.000 23.79755 ? 79  GLY   A O   1 
ATOM   614  N N   . HIS   A 1 80  ? -1.70990  7.13541   -13.79796 1.000 21.96296 ? 80  HIS   A N   1 
ATOM   615  C CA  . HIS   A 1 80  ? -1.84871  5.68619   -13.81727 1.000 20.81662 ? 80  HIS   A CA  1 
ATOM   616  C C   . HIS   A 1 80  ? -0.51324  5.07238   -13.42491 1.000 21.36045 ? 80  HIS   A C   1 
ATOM   617  O O   . HIS   A 1 80  ? 0.54693   5.58895   -13.80014 1.000 21.01283 ? 80  HIS   A O   1 
ATOM   618  C CB  . HIS   A 1 80  ? -2.27890  5.19734   -15.20669 1.000 21.74773 ? 80  HIS   A CB  1 
ATOM   619  C CG  . HIS   A 1 80  ? -1.34249  5.61293   -16.30256 1.000 22.96301 ? 80  HIS   A CG  1 
ATOM   620  N ND1 . HIS   A 1 80  ? -1.49667  6.78054   -17.02042 1.000 26.09607 ? 80  HIS   A ND1 1 
ATOM   621  C CD2 . HIS   A 1 80  ? -0.24129  5.00622   -16.80450 1.000 24.03587 ? 80  HIS   A CD2 1 
ATOM   622  C CE1 . HIS   A 1 80  ? -0.52483  6.87878   -17.91137 1.000 29.52083 ? 80  HIS   A CE1 1 
ATOM   623  N NE2 . HIS   A 1 80  ? 0.25219   5.81596   -17.79909 1.000 27.18267 ? 80  HIS   A NE2 1 
ATOM   624  N N   . SER   A 1 81  ? -0.56622  3.98051   -12.66367 1.000 18.94469 ? 81  SER   A N   1 
ATOM   625  C CA  . SER   A 1 81  ? 0.62955   3.22722   -12.30340 1.000 19.12904 ? 81  SER   A CA  1 
ATOM   626  C C   . SER   A 1 81  ? 0.21280   1.78834   -12.06761 1.000 19.16650 ? 81  SER   A C   1 
ATOM   627  O O   . SER   A 1 81  ? -0.96476  1.50250   -11.86240 1.000 21.75624 ? 81  SER   A O   1 
ATOM   628  C CB  . SER   A 1 81  ? 1.30899   3.76677   -11.03757 1.000 18.47309 ? 81  SER   A CB  1 
ATOM   629  O OG  . SER   A 1 81  ? 0.34575   3.98108   -10.01488 1.000 22.83698 ? 81  SER   A OG  1 
ATOM   630  N N   . MET   A 1 82  ? 1.18089   0.87857   -12.08712 1.000 16.61269 ? 82  MET   A N   1 
ATOM   631  C CA  . MET   A 1 82  ? 0.91613   -0.48774  -11.64977 1.000 18.12768 ? 82  MET   A CA  1 
ATOM   632  C C   . MET   A 1 82  ? 1.43644   -0.72951  -10.24885 1.000 17.01823 ? 82  MET   A C   1 
ATOM   633  O O   . MET   A 1 82  ? 2.53907   -0.29367  -9.89577  1.000 17.00805 ? 82  MET   A O   1 
ATOM   634  C CB  . MET   A 1 82  ? 1.54899   -1.54945  -12.54540 1.000 23.94730 ? 82  MET   A CB  1 
ATOM   635  C CG  . MET   A 1 82  ? 0.69952   -2.04777  -13.64994 1.000 28.73882 ? 82  MET   A CG  1 
ATOM   636  S SD  . MET   A 1 82  ? 1.68211   -3.21622  -14.56865 1.000 24.16039 ? 82  MET   A SD  1 
ATOM   637  C CE  . MET   A 1 82  ? 3.24864   -2.35725  -14.73753 1.000 26.67539 ? 82  MET   A CE  1 
ATOM   638  N N   . GLN   A 1 83  ? 0.66988   -1.49500  -9.48461  1.000 16.41529 ? 83  GLN   A N   1 
ATOM   639  C CA  . GLN   A 1 83  ? 1.16184   -2.14093  -8.27124  1.000 21.32753 ? 83  GLN   A CA  1 
ATOM   640  C C   . GLN   A 1 83  ? 0.94448   -3.63550  -8.47843  1.000 14.66956 ? 83  GLN   A C   1 
ATOM   641  O O   . GLN   A 1 83  ? -0.19137  -4.11361  -8.40506  1.000 13.83276 ? 83  GLN   A O   1 
ATOM   642  C CB  . GLN   A 1 83  ? 0.45459   -1.64231  -7.02189  1.000 21.49846 ? 83  GLN   A CB  1 
ATOM   643  C CG  . GLN   A 1 83  ? 0.86870   -2.42165  -5.78982  1.000 24.22223 ? 83  GLN   A CG  1 
ATOM   644  C CD  . GLN   A 1 83  ? 0.69336   -1.64417  -4.49554  1.000 34.30680 ? 83  GLN   A CD  1 
ATOM   645  O OE1 . GLN   A 1 83  ? 0.10729   -0.55409  -4.47770  1.000 37.21566 ? 83  GLN   A OE1 1 
ATOM   646  N NE2 . GLN   A 1 83  ? 1.19873   -2.20826  -3.39619  1.000 33.22363 ? 83  GLN   A NE2 1 
ATOM   647  N N   . ASN   A 1 84  ? 2.03305   -4.35806  -8.76639  1.000 14.24505 ? 84  ASN   A N   1 
ATOM   648  C CA  . ASN   A 1 84  ? 1.95403   -5.79211  -9.03257  1.000 16.20340 ? 84  ASN   A CA  1 
ATOM   649  C C   . ASN   A 1 84  ? 0.93068   -6.09197  -10.11806 1.000 13.28965 ? 84  ASN   A C   1 
ATOM   650  O O   . ASN   A 1 84  ? 1.06769   -5.58641  -11.23261 1.000 14.38522 ? 84  ASN   A O   1 
ATOM   651  C CB  . ASN   A 1 84  ? 1.68261   -6.52485  -7.73375  1.000 13.25084 ? 84  ASN   A CB  1 
ATOM   652  C CG  . ASN   A 1 84  ? 2.72310   -6.17938  -6.69020  1.000 14.93385 ? 84  ASN   A CG  1 
ATOM   653  O OD1 . ASN   A 1 84  ? 3.93887   -6.30789  -6.94570  1.000 13.76123 ? 84  ASN   A OD1 1 
ATOM   654  N ND2 . ASN   A 1 84  ? 2.27687   -5.64187  -5.55828  1.000 14.15138 ? 84  ASN   A ND2 1 
ATOM   655  N N   . CYS   A 1 85  ? -0.12035  -6.86287  -9.82406  1.000 12.96578 ? 85  CYS   A N   1 
ATOM   656  C CA  . CYS   A 1 85  ? -1.05830  -7.21183  -10.87242 1.000 12.10141 ? 85  CYS   A CA  1 
ATOM   657  C C   . CYS   A 1 85  ? -2.30393  -6.32508  -10.89409 1.000 14.91622 ? 85  CYS   A C   1 
ATOM   658  O O   . CYS   A 1 85  ? -3.23614  -6.60758  -11.65844 1.000 12.34249 ? 85  CYS   A O   1 
ATOM   659  C CB  . CYS   A 1 85  ? -1.45585  -8.68017  -10.74904 1.000 12.22677 ? 85  CYS   A CB  1 
ATOM   660  S SG  . CYS   A 1 85  ? -0.05199  -9.73743  -11.09684 1.000 13.76741 ? 85  CYS   A SG  1 
ATOM   661  N N   . VAL   A 1 86  ? -2.32945  -5.23996  -10.11951 1.000 11.05807 ? 86  VAL   A N   1 
ATOM   662  C CA  . VAL   A 1 86  ? -3.41780  -4.28331  -10.24194 1.000 13.19586 ? 86  VAL   A CA  1 
ATOM   663  C C   . VAL   A 1 86  ? -2.89539  -2.97672  -10.80773 1.000 12.90148 ? 86  VAL   A C   1 
ATOM   664  O O   . VAL   A 1 86  ? -1.70130  -2.63730  -10.73274 1.000 13.46244 ? 86  VAL   A O   1 
ATOM   665  C CB  . VAL   A 1 86  ? -4.19193  -4.04856  -8.92651  1.000 15.91693 ? 86  VAL   A CB  1 
ATOM   666  C CG1 . VAL   A 1 86  ? -4.74116  -5.38199  -8.40261  1.000 14.53794 ? 86  VAL   A CG1 1 
ATOM   667  C CG2 . VAL   A 1 86  ? -3.32542  -3.40665  -7.90476  1.000 16.08656 ? 86  VAL   A CG2 1 
ATOM   668  N N   . LEU   A 1 87  ? -3.81579  -2.27979  -11.44050 1.000 12.39141 ? 87  LEU   A N   1 
ATOM   669  C CA  . LEU   A 1 87  ? -3.62578  -0.93957  -11.96185 1.000 13.41770 ? 87  LEU   A CA  1 
ATOM   670  C C   . LEU   A 1 87  ? -4.24462  0.05025   -10.99339 1.000 13.46399 ? 87  LEU   A C   1 
ATOM   671  O O   . LEU   A 1 87  ? -5.30505  -0.21381  -10.42008 1.000 15.50929 ? 87  LEU   A O   1 
ATOM   672  C CB  . LEU   A 1 87  ? -4.28166  -0.82305  -13.33322 1.000 14.31584 ? 87  LEU   A CB  1 
ATOM   673  C CG  . LEU   A 1 87  ? -3.82289  0.20599   -14.33971 1.000 21.01019 ? 87  LEU   A CG  1 
ATOM   674  C CD1 . LEU   A 1 87  ? -2.35312  0.03160   -14.66405 1.000 22.12701 ? 87  LEU   A CD1 1 
ATOM   675  C CD2 . LEU   A 1 87  ? -4.70682  0.06105   -15.58641 1.000 21.15169 ? 87  LEU   A CD2 1 
ATOM   676  N N   . LYS   A 1 88  ? -3.56922  1.17867   -10.79087 1.000 15.81414 ? 88  LYS   A N   1 
ATOM   677  C CA  . LYS   A 1 88  ? -4.08100  2.26986   -9.96901  1.000 20.44990 ? 88  LYS   A CA  1 
ATOM   678  C C   . LYS   A 1 88  ? -4.25422  3.49367   -10.85818 1.000 17.84783 ? 88  LYS   A C   1 
ATOM   679  O O   . LYS   A 1 88  ? -3.27589  4.11702   -11.29074 1.000 20.35942 ? 88  LYS   A O   1 
ATOM   680  C CB  . LYS   A 1 88  ? -3.17404  2.55529   -8.76786  1.000 14.96789 ? 88  LYS   A CB  1 
ATOM   681  C CG  . LYS   A 1 88  ? -2.98011  1.35089   -7.86862  1.000 16.32870 ? 88  LYS   A CG  1 
ATOM   682  C CD  . LYS   A 1 88  ? -2.01354  1.59868   -6.72525  1.000 17.26140 ? 88  LYS   A CD  1 
ATOM   683  C CE  . LYS   A 1 88  ? -2.23130  2.93816   -6.04698  1.000 23.24125 ? 88  LYS   A CE  1 
ATOM   684  N NZ  . LYS   A 1 88  ? -1.46588  2.99951   -4.75527  1.000 31.73067 ? 88  LYS   A NZ  1 
ATOM   685  N N   . LEU   A 1 89  ? -5.49972  3.81872   -11.14646 1.000 16.05810 ? 89  LEU   A N   1 
ATOM   686  C CA  . LEU   A 1 89  ? -5.83634  4.97030   -11.97267 1.000 17.30769 ? 89  LEU   A CA  1 
ATOM   687  C C   . LEU   A 1 89  ? -6.16498  6.12652   -11.04751 1.000 18.57933 ? 89  LEU   A C   1 
ATOM   688  O O   . LEU   A 1 89  ? -7.15672  6.08099   -10.32004 1.000 19.35297 ? 89  LEU   A O   1 
ATOM   689  C CB  . LEU   A 1 89  ? -7.03110  4.67201   -12.86990 1.000 17.55607 ? 89  LEU   A CB  1 
ATOM   690  C CG  . LEU   A 1 89  ? -6.87780  3.43641   -13.74123 1.000 18.39317 ? 89  LEU   A CG  1 
ATOM   691  C CD1 . LEU   A 1 89  ? -8.12877  3.14917   -14.56313 1.000 20.62839 ? 89  LEU   A CD1 1 
ATOM   692  C CD2 . LEU   A 1 89  ? -5.66977  3.61939   -14.64277 1.000 19.39041 ? 89  LEU   A CD2 1 
ATOM   693  N N   . LYS   A 1 90  ? -5.33806  7.15130   -11.03582 1.000 19.20346 ? 90  LYS   A N   1 
ATOM   694  C CA  . LYS   A 1 90  ? -5.71038  8.31976   -10.25533 1.000 20.48024 ? 90  LYS   A CA  1 
ATOM   695  C C   . LYS   A 1 90  ? -6.70139  9.17782   -11.00811 1.000 23.10450 ? 90  LYS   A C   1 
ATOM   696  O O   . LYS   A 1 90  ? -6.49546  9.49983   -12.17617 1.000 27.15389 ? 90  LYS   A O   1 
ATOM   697  C CB  . LYS   A 1 90  ? -4.49848  9.14960   -9.82833  1.000 25.17716 ? 90  LYS   A CB  1 
ATOM   698  C CG  . LYS   A 1 90  ? -4.98051  10.26930  -8.92968  1.000 28.79010 ? 90  LYS   A CG  1 
ATOM   699  C CD  . LYS   A 1 90  ? -3.91405  11.14549  -8.41252  1.000 32.88259 ? 90  LYS   A CD  1 
ATOM   700  C CE  . LYS   A 1 90  ? -3.13201  10.34607  -7.40509  1.000 39.23900 ? 90  LYS   A CE  1 
ATOM   701  N NZ  . LYS   A 1 90  ? -3.96229  10.01289  -6.19586  1.000 40.90512 ? 90  LYS   A NZ  1 
ATOM   702  N N   . VAL   A 1 91  ? -7.79650  9.50707   -10.33958 1.000 21.28150 ? 91  VAL   A N   1 
ATOM   703  C CA  . VAL   A 1 91  ? -8.85286  10.30423  -10.92713 1.000 24.54921 ? 91  VAL   A CA  1 
ATOM   704  C C   . VAL   A 1 91  ? -8.90224  11.65154  -10.21963 1.000 25.92084 ? 91  VAL   A C   1 
ATOM   705  O O   . VAL   A 1 91  ? -8.34782  11.83850  -9.13276  1.000 27.19554 ? 91  VAL   A O   1 
ATOM   706  C CB  . VAL   A 1 91  ? -10.20131 9.57075   -10.86537 1.000 23.65419 ? 91  VAL   A CB  1 
ATOM   707  C CG1 . VAL   A 1 91  ? -10.06040 8.25553   -11.60581 1.000 24.19461 ? 91  VAL   A CG1 1 
ATOM   708  C CG2 . VAL   A 1 91  ? -10.60706 9.31688   -9.42521  1.000 22.27914 ? 91  VAL   A CG2 1 
ATOM   709  N N   . ASP   A 1 92  ? -9.54058  12.60913  -10.87498 1.000 27.51850 ? 92  ASP   A N   1 
ATOM   710  C CA  . ASP   A 1 92  ? -9.56931  13.96612  -10.35052 1.000 30.66297 ? 92  ASP   A CA  1 
ATOM   711  C C   . ASP   A 1 92  ? -10.60331 14.15259  -9.25148  1.000 31.28307 ? 92  ASP   A C   1 
ATOM   712  O O   . ASP   A 1 92  ? -10.75856 15.26990  -8.75135  1.000 33.21772 ? 92  ASP   A O   1 
ATOM   713  C CB  . ASP   A 1 92  ? -9.82168  14.96591  -11.48620 1.000 33.19166 ? 92  ASP   A CB  1 
ATOM   714  C CG  . ASP   A 1 92  ? -11.19007 14.79116  -12.14242 1.000 35.30419 ? 92  ASP   A CG  1 
ATOM   715  O OD1 . ASP   A 1 92  ? -12.03674 14.02054  -11.63686 1.000 33.77196 ? 92  ASP   A OD1 1 
ATOM   716  O OD2 . ASP   A 1 92  ? -11.42798 15.45574  -13.16925 1.000 40.32329 ? 92  ASP   A OD2 1 
ATOM   717  N N   . THR   A 1 93  ? -11.32064 13.09837  -8.87552  1.000 28.84200 ? 93  THR   A N   1 
ATOM   718  C CA  . THR   A 1 93  ? -12.40139 13.19262  -7.90280  1.000 29.99850 ? 93  THR   A CA  1 
ATOM   719  C C   . THR   A 1 93  ? -12.26918 12.08980  -6.86459  1.000 25.72252 ? 93  THR   A C   1 
ATOM   720  O O   . THR   A 1 93  ? -12.19799 10.90946  -7.21573  1.000 23.45626 ? 93  THR   A O   1 
ATOM   721  C CB  . THR   A 1 93  ? -13.77026 13.09276  -8.58659  1.000 28.82108 ? 93  THR   A CB  1 
ATOM   722  O OG1 . THR   A 1 93  ? -13.80400 13.96434  -9.72456  1.000 33.99664 ? 93  THR   A OG1 1 
ATOM   723  C CG2 . THR   A 1 93  ? -14.88856 13.45192  -7.61457  1.000 29.85799 ? 93  THR   A CG2 1 
ATOM   724  N N   . ALA   A 1 94  ? -12.23813 12.47333  -5.59066  1.000 26.01061 ? 94  ALA   A N   1 
ATOM   725  C CA  . ALA   A 1 94  ? -12.31252 11.48396  -4.52693  1.000 23.23316 ? 94  ALA   A CA  1 
ATOM   726  C C   . ALA   A 1 94  ? -13.74778 10.97944  -4.39101  1.000 25.20806 ? 94  ALA   A C   1 
ATOM   727  O O   . ALA   A 1 94  ? -14.70318 11.75892  -4.46446  1.000 25.47558 ? 94  ALA   A O   1 
ATOM   728  C CB  . ALA   A 1 94  ? -11.83099 12.08249  -3.20970  1.000 24.14651 ? 94  ALA   A CB  1 
ATOM   729  N N   . ASN   A 1 95  ? -13.89482 9.67372   -4.21088  1.000 23.43603 ? 95  ASN   A N   1 
ATOM   730  C CA  . ASN   A 1 95  ? -15.21657 9.05295   -4.07549  1.000 22.28090 ? 95  ASN   A CA  1 
ATOM   731  C C   . ASN   A 1 95  ? -15.88457 9.53392   -2.79496  1.000 23.01953 ? 95  ASN   A C   1 
ATOM   732  O O   . ASN   A 1 95  ? -15.41876 9.18424   -1.70335  1.000 24.06242 ? 95  ASN   A O   1 
ATOM   733  C CB  . ASN   A 1 95  ? -15.08770 7.52928   -4.05788  1.000 18.71691 ? 95  ASN   A CB  1 
ATOM   734  C CG  . ASN   A 1 95  ? -16.44306 6.81141   -4.04128  1.000 18.22569 ? 95  ASN   A CG  1 
ATOM   735  O OD1 . ASN   A 1 95  ? -17.50553 7.43486   -3.92357  1.000 19.26216 ? 95  ASN   A OD1 1 
ATOM   736  N ND2 . ASN   A 1 95  ? -16.40169 5.47896   -4.13764  1.000 17.16442 ? 95  ASN   A ND2 1 
ATOM   737  N N   . PRO   A 1 96  ? -16.97275 10.30565  -2.86483  1.000 26.00752 ? 96  PRO   A N   1 
ATOM   738  C CA  . PRO   A 1 96  ? -17.61053 10.77467  -1.62572  1.000 25.11036 ? 96  PRO   A CA  1 
ATOM   739  C C   . PRO   A 1 96  ? -18.22206 9.65149   -0.81465  1.000 22.63148 ? 96  PRO   A C   1 
ATOM   740  O O   . PRO   A 1 96  ? -18.53004 9.85012   0.36557   1.000 26.35620 ? 96  PRO   A O   1 
ATOM   741  C CB  . PRO   A 1 96  ? -18.67260 11.75846  -2.13128  1.000 25.43458 ? 96  PRO   A CB  1 
ATOM   742  C CG  . PRO   A 1 96  ? -19.00380 11.26661  -3.50456  1.000 26.16526 ? 96  PRO   A CG  1 
ATOM   743  C CD  . PRO   A 1 96  ? -17.70285 10.74727  -4.06862  1.000 23.47723 ? 96  PRO   A CD  1 
ATOM   744  N N   . LYS   A 1 97  ? -18.37009 8.46563   -1.39279  1.000 21.04914 ? 97  LYS   A N   1 
ATOM   745  C CA  . LYS   A 1 97  ? -18.90087 7.32229   -0.67593  1.000 23.04182 ? 97  LYS   A CA  1 
ATOM   746  C C   . LYS   A 1 97  ? -17.81067 6.39346   -0.15893  1.000 19.99945 ? 97  LYS   A C   1 
ATOM   747  O O   . LYS   A 1 97  ? -18.11509 5.25879   0.21662   1.000 19.20016 ? 97  LYS   A O   1 
ATOM   748  C CB  . LYS   A 1 97  ? -19.87348 6.54971   -1.56452  1.000 19.59754 ? 97  LYS   A CB  1 
ATOM   749  C CG  . LYS   A 1 97  ? -21.16043 7.30041   -1.86424  1.000 22.45352 ? 97  LYS   A CG  1 
ATOM   750  C CD  . LYS   A 1 97  ? -22.03654 6.49067   -2.81081  1.000 27.02781 ? 97  LYS   A CD  1 
ATOM   751  C CE  . LYS   A 1 97  ? -22.70180 7.34817   -3.86646  1.000 28.73817 ? 97  LYS   A CE  1 
ATOM   752  N NZ  . LYS   A 1 97  ? -23.29187 6.47707   -4.93038  1.000 33.95520 ? 97  LYS   A NZ  1 
ATOM   753  N N   . THR   A 1 98  ? -16.55694 6.84670   -0.11393  1.000 19.67413 ? 98  THR   A N   1 
ATOM   754  C CA  . THR   A 1 98  ? -15.48541 5.96490   0.34643   1.000 17.72976 ? 98  THR   A CA  1 
ATOM   755  C C   . THR   A 1 98  ? -15.74540 5.53449   1.78714   1.000 20.90773 ? 98  THR   A C   1 
ATOM   756  O O   . THR   A 1 98  ? -15.83567 6.39587   2.68147   1.000 20.38176 ? 98  THR   A O   1 
ATOM   757  C CB  . THR   A 1 98  ? -14.12138 6.64265   0.23577   1.000 18.33072 ? 98  THR   A CB  1 
ATOM   758  O OG1 . THR   A 1 98  ? -13.91366 7.05919   -1.11329  1.000 18.28713 ? 98  THR   A OG1 1 
ATOM   759  C CG2 . THR   A 1 98  ? -12.99864 5.66779   0.60840   1.000 17.00340 ? 98  THR   A CG2 1 
ATOM   760  N N   . PRO   A 1 99  ? -15.90972 4.24550   2.05422   1.000 20.11330 ? 99  PRO   A N   1 
ATOM   761  C CA  . PRO   A 1 99  ? -16.07695 3.79833   3.43335   1.000 19.43279 ? 99  PRO   A CA  1 
ATOM   762  C C   . PRO   A 1 99  ? -14.72253 3.79469   4.11164   1.000 20.15101 ? 99  PRO   A C   1 
ATOM   763  O O   . PRO   A 1 99  ? -13.67226 3.86389   3.46097   1.000 17.94524 ? 99  PRO   A O   1 
ATOM   764  C CB  . PRO   A 1 99  ? -16.59828 2.36693   3.27553   1.000 17.09429 ? 99  PRO   A CB  1 
ATOM   765  C CG  . PRO   A 1 99  ? -15.83853 1.88805   2.09390   1.000 17.71913 ? 99  PRO   A CG  1 
ATOM   766  C CD  . PRO   A 1 99  ? -15.75296 3.09629   1.14363   1.000 18.89043 ? 99  PRO   A CD  1 
ATOM   767  N N   . LYS   A 1 100 ? -14.74801 3.67884   5.43142   1.000 17.90248 ? 100 LYS   A N   1 
ATOM   768  C CA  . LYS   A 1 100 ? -13.50858 3.34271   6.10469   1.000 18.79623 ? 100 LYS   A CA  1 
ATOM   769  C C   . LYS   A 1 100 ? -13.07405 1.96996   5.61335   1.000 20.01239 ? 100 LYS   A C   1 
ATOM   770  O O   . LYS   A 1 100 ? -13.88959 1.05443   5.52167   1.000 16.12182 ? 100 LYS   A O   1 
ATOM   771  C CB  . LYS   A 1 100 ? -13.70214 3.35380   7.61498   1.000 25.47479 ? 100 LYS   A CB  1 
ATOM   772  C CG  . LYS   A 1 100 ? -12.39744 3.10506   8.34513   1.000 28.80880 ? 100 LYS   A CG  1 
ATOM   773  C CD  . LYS   A 1 100 ? -12.52474 3.15954   9.86428   1.000 36.55408 ? 100 LYS   A CD  1 
ATOM   774  C CE  . LYS   A 1 100 ? -11.13046 3.00468   10.48779  1.000 31.27078 ? 100 LYS   A CE  1 
ATOM   775  N NZ  . LYS   A 1 100 ? -10.56611 1.64013   10.25130  1.000 34.28922 ? 100 LYS   A NZ  1 
ATOM   776  N N   . TYR   A 1 101 ? -11.80921 1.82669   5.22190   1.000 14.77484 ? 101 TYR   A N   1 
ATOM   777  C CA  . TYR   A 1 101 ? -11.44408 0.55357   4.62241   1.000 14.42379 ? 101 TYR   A CA  1 
ATOM   778  C C   . TYR   A 1 101 ? -10.01417 0.18490   4.97673   1.000 15.73682 ? 101 TYR   A C   1 
ATOM   779  O O   . TYR   A 1 101 ? -9.21540  1.01324   5.42582   1.000 14.61770 ? 101 TYR   A O   1 
ATOM   780  C CB  . TYR   A 1 101 ? -11.58544 0.56757   3.09141   1.000 13.45469 ? 101 TYR   A CB  1 
ATOM   781  C CG  . TYR   A 1 101 ? -10.55886 1.42256   2.38831   1.000 15.96550 ? 101 TYR   A CG  1 
ATOM   782  C CD1 . TYR   A 1 101 ? -10.78519 2.76999   2.15167   1.000 16.32185 ? 101 TYR   A CD1 1 
ATOM   783  C CD2 . TYR   A 1 101 ? -9.37429  0.85841   1.91098   1.000 17.42242 ? 101 TYR   A CD2 1 
ATOM   784  C CE1 . TYR   A 1 101 ? -9.84281  3.54468   1.49848   1.000 18.46394 ? 101 TYR   A CE1 1 
ATOM   785  C CE2 . TYR   A 1 101 ? -8.43589  1.62911   1.25298   1.000 15.50542 ? 101 TYR   A CE2 1 
ATOM   786  C CZ  . TYR   A 1 101 ? -8.67647  2.96442   1.05533   1.000 17.21915 ? 101 TYR   A CZ  1 
ATOM   787  O OH  . TYR   A 1 101 ? -7.73595  3.74216   0.40713   1.000 21.20348 ? 101 TYR   A OH  1 
ATOM   788  N N   . LYS   A 1 102 ? -9.70534  -1.08744  4.72263   1.000 16.18291 ? 102 LYS   A N   1 
ATOM   789  C CA  . LYS   A 1 102 ? -8.36217  -1.64518  4.81449   1.000 13.55442 ? 102 LYS   A CA  1 
ATOM   790  C C   . LYS   A 1 102 ? -8.17768  -2.64457  3.68514   1.000 12.98879 ? 102 LYS   A C   1 
ATOM   791  O O   . LYS   A 1 102 ? -9.12642  -3.29658  3.25845   1.000 11.90767 ? 102 LYS   A O   1 
ATOM   792  C CB  . LYS   A 1 102 ? -8.13584  -2.38650  6.12831   1.000 15.69553 ? 102 LYS   A CB  1 
ATOM   793  C CG  . LYS   A 1 102 ? -8.30144  -1.54998  7.37317   1.000 22.28197 ? 102 LYS   A CG  1 
ATOM   794  C CD  . LYS   A 1 102 ? -7.86766  -2.37056  8.56547   1.000 24.92089 ? 102 LYS   A CD  1 
ATOM   795  C CE  . LYS   A 1 102 ? -8.86140  -3.47550  8.80812   1.000 24.63157 ? 102 LYS   A CE  1 
ATOM   796  N NZ  . LYS   A 1 102 ? -8.24854  -4.59110  9.58883   1.000 33.53041 ? 102 LYS   A NZ  1 
ATOM   797  N N   . PHE   A 1 103 ? -6.93950  -2.78587  3.23249   1.000 12.82270 ? 103 PHE   A N   1 
ATOM   798  C CA  . PHE   A 1 103 ? -6.55169  -3.86498  2.33123   1.000 9.92539  ? 103 PHE   A CA  1 
ATOM   799  C C   . PHE   A 1 103 ? -5.90708  -4.97148  3.16760   1.000 11.56916 ? 103 PHE   A C   1 
ATOM   800  O O   . PHE   A 1 103 ? -4.81530  -4.78402  3.72295   1.000 11.97100 ? 103 PHE   A O   1 
ATOM   801  C CB  . PHE   A 1 103 ? -5.55315  -3.37401  1.28326   1.000 10.33841 ? 103 PHE   A CB  1 
ATOM   802  C CG  . PHE   A 1 103 ? -6.12226  -2.43939  0.27680   1.000 10.80321 ? 103 PHE   A CG  1 
ATOM   803  C CD1 . PHE   A 1 103 ? -7.49010  -2.31836  0.11568   1.000 10.14305 ? 103 PHE   A CD1 1 
ATOM   804  C CD2 . PHE   A 1 103 ? -5.28565  -1.71859  -0.55958  1.000 11.25829 ? 103 PHE   A CD2 1 
ATOM   805  C CE1 . PHE   A 1 103 ? -8.01182  -1.47417  -0.83456  1.000 11.69926 ? 103 PHE   A CE1 1 
ATOM   806  C CE2 . PHE   A 1 103 ? -5.80967  -0.87178  -1.52247  1.000 12.06029 ? 103 PHE   A CE2 1 
ATOM   807  C CZ  . PHE   A 1 103 ? -7.16818  -0.74349  -1.65540  1.000 11.02295 ? 103 PHE   A CZ  1 
ATOM   808  N N   . VAL   A 1 104 ? -6.56316  -6.11767  3.24325   1.000 8.98705  ? 104 VAL   A N   1 
ATOM   809  C CA  . VAL   A 1 104 ? -6.08353  -7.22577  4.05573   1.000 11.11446 ? 104 VAL   A CA  1 
ATOM   810  C C   . VAL   A 1 104 ? -5.95072  -8.40494  3.11652   1.000 12.25284 ? 104 VAL   A C   1 
ATOM   811  O O   . VAL   A 1 104 ? -6.71094  -8.54048  2.15603   1.000 18.80800 ? 104 VAL   A O   1 
ATOM   812  C CB  . VAL   A 1 104 ? -7.03013  -7.57466  5.22525   1.000 9.76491  ? 104 VAL   A CB  1 
ATOM   813  C CG1 . VAL   A 1 104 ? -7.25718  -6.33325  6.12508   1.000 13.64681 ? 104 VAL   A CG1 1 
ATOM   814  C CG2 . VAL   A 1 104 ? -8.31803  -8.12044  4.71347   1.000 15.67964 ? 104 VAL   A CG2 1 
ATOM   815  N N   . ARG   A 1 105 ? -4.97702  -9.25905  3.38097   1.000 9.85022  ? 105 ARG   A N   1 
ATOM   816  C CA  . ARG   A 1 105 ? -4.86623  -10.50558 2.64277   1.000 7.74258  ? 105 ARG   A CA  1 
ATOM   817  C C   . ARG   A 1 105 ? -5.36209  -11.60940 3.55587   1.000 8.94786  ? 105 ARG   A C   1 
ATOM   818  O O   . ARG   A 1 105 ? -4.96248  -11.66022 4.71559   1.000 11.07419 ? 105 ARG   A O   1 
ATOM   819  C CB  . ARG   A 1 105 ? -3.41245  -10.76576 2.24115   1.000 8.45942  ? 105 ARG   A CB  1 
ATOM   820  C CG  . ARG   A 1 105 ? -3.26555  -11.96766 1.31554   1.000 7.80518  ? 105 ARG   A CG  1 
ATOM   821  C CD  . ARG   A 1 105 ? -1.78607  -12.07499 0.89566   1.000 8.40724  ? 105 ARG   A CD  1 
ATOM   822  N NE  . ARG   A 1 105 ? -1.54206  -13.31056 0.16015   1.000 9.31080  ? 105 ARG   A NE  1 
ATOM   823  C CZ  . ARG   A 1 105 ? -1.55622  -13.39909 -1.15857  1.000 8.21309  ? 105 ARG   A CZ  1 
ATOM   824  N NH1 . ARG   A 1 105 ? -1.80079  -12.31167 -1.87091  1.000 8.14682  ? 105 ARG   A NH1 1 
ATOM   825  N NH2 . ARG   A 1 105 ? -1.32647  -14.56283 -1.77157  1.000 8.31830  ? 105 ARG   A NH2 1 
ATOM   826  N N   . ILE   A 1 106 ? -6.24205  -12.47260 3.04645   1.000 10.26662 ? 106 ILE   A N   1 
ATOM   827  C CA  . ILE   A 1 106 ? -6.72943  -13.56296 3.88025   1.000 11.47187 ? 106 ILE   A CA  1 
ATOM   828  C C   . ILE   A 1 106 ? -5.92603  -14.83455 3.65933   1.000 9.80035  ? 106 ILE   A C   1 
ATOM   829  O O   . ILE   A 1 106 ? -5.14855  -14.95070 2.70595   1.000 12.47052 ? 106 ILE   A O   1 
ATOM   830  C CB  . ILE   A 1 106 ? -8.22795  -13.81980 3.64424   1.000 10.96495 ? 106 ILE   A CB  1 
ATOM   831  C CG1 . ILE   A 1 106 ? -8.46794  -14.19709 2.18302   1.000 8.91826  ? 106 ILE   A CG1 1 
ATOM   832  C CG2 . ILE   A 1 106 ? -9.07120  -12.64525 4.14286   1.000 15.35561 ? 106 ILE   A CG2 1 
ATOM   833  C CD1 . ILE   A 1 106 ? -9.89489  -14.69823 1.89433   1.000 14.29958 ? 106 ILE   A CD1 1 
ATOM   834  N N   . GLN   A 1 107 ? -6.09987  -15.78605 4.55664   1.000 9.06244  ? 107 GLN   A N   1 
ATOM   835  C CA  . GLN   A 1 107 ? -5.60107  -17.14922 4.65563   1.000 11.37500 ? 107 GLN   A CA  1 
ATOM   836  C C   . GLN   A 1 107 ? -6.57673  -18.10350 3.98933   1.000 10.45846 ? 107 GLN   A C   1 
ATOM   837  O O   . GLN   A 1 107 ? -7.78444  -17.93820 4.12830   1.000 11.90774 ? 107 GLN   A O   1 
ATOM   838  C CB  . GLN   A 1 107 ? -5.43859  -17.55609 6.11571   1.000 12.81325 ? 107 GLN   A CB  1 
ATOM   839  C CG  . GLN   A 1 107 ? -4.29837  -16.86698 6.80322   1.000 12.70026 ? 107 GLN   A CG  1 
ATOM   840  C CD  . GLN   A 1 107 ? -2.99226  -17.31142 6.23604   1.000 15.69125 ? 107 GLN   A CD  1 
ATOM   841  O OE1 . GLN   A 1 107 ? -2.81953  -18.49197 5.94370   1.000 13.40016 ? 107 GLN   A OE1 1 
ATOM   842  N NE2 . GLN   A 1 107 ? -2.07437  -16.37192 6.01634   1.000 13.25544 ? 107 GLN   A NE2 1 
ATOM   843  N N   . PRO   A 1 108 ? -6.07569  -19.11154 3.27488   1.000 11.22798 ? 108 PRO   A N   1 
ATOM   844  C CA  . PRO   A 1 108 ? -6.93440  -20.23707 2.90348   1.000 12.16846 ? 108 PRO   A CA  1 
ATOM   845  C C   . PRO   A 1 108 ? -7.68481  -20.70911 4.13655   1.000 11.95139 ? 108 PRO   A C   1 
ATOM   846  O O   . PRO   A 1 108 ? -7.15797  -20.69120 5.25081   1.000 15.44783 ? 108 PRO   A O   1 
ATOM   847  C CB  . PRO   A 1 108 ? -5.95113  -21.29865 2.38281   1.000 11.58275 ? 108 PRO   A CB  1 
ATOM   848  C CG  . PRO   A 1 108 ? -4.59412  -20.77158 2.64981   1.000 14.95470 ? 108 PRO   A CG  1 
ATOM   849  C CD  . PRO   A 1 108 ? -4.66476  -19.30909 2.90041   1.000 10.63121 ? 108 PRO   A CD  1 
ATOM   850  N N   . GLY   A 1 109 ? -8.93130  -21.09227 3.93638   1.000 9.60370  ? 109 GLY   A N   1 
ATOM   851  C CA  . GLY   A 1 109 ? -9.81610  -21.43253 5.02249   1.000 14.01732 ? 109 GLY   A CA  1 
ATOM   852  C C   . GLY   A 1 109 ? -10.70540 -20.30532 5.49135   1.000 16.47849 ? 109 GLY   A C   1 
ATOM   853  O O   . GLY   A 1 109 ? -11.75816 -20.57921 6.07999   1.000 17.19573 ? 109 GLY   A O   1 
ATOM   854  N N   . GLN   A 1 110 ? -10.31884 -19.05213 5.25772   1.000 12.94520 ? 110 GLN   A N   1 
ATOM   855  C CA  . GLN   A 1 110 ? -11.14988 -17.91351 5.63902   1.000 12.82478 ? 110 GLN   A CA  1 
ATOM   856  C C   . GLN   A 1 110 ? -12.19849 -17.58982 4.57854   1.000 10.99709 ? 110 GLN   A C   1 
ATOM   857  O O   . GLN   A 1 110 ? -12.07734 -17.93244 3.39746   1.000 9.60398  ? 110 GLN   A O   1 
ATOM   858  C CB  . GLN   A 1 110 ? -10.32694 -16.64255 5.90566   1.000 12.30964 ? 110 GLN   A CB  1 
ATOM   859  C CG  . GLN   A 1 110 ? -9.30366  -16.71880 7.00949   1.000 16.67204 ? 110 GLN   A CG  1 
ATOM   860  C CD  . GLN   A 1 110 ? -8.73199  -15.32624 7.31562   1.000 23.58803 ? 110 GLN   A CD  1 
ATOM   861  O OE1 . GLN   A 1 110 ? -7.70097  -14.91090 6.78453   1.000 13.13862 ? 110 GLN   A OE1 1 
ATOM   862  N NE2 . GLN   A 1 110 ? -9.44619  -14.58093 8.16793   1.000 26.47852 ? 110 GLN   A NE2 1 
ATOM   863  N N   . THR   A 1 111 ? -13.26041 -16.93678 5.02483   1.000 9.13012  ? 111 THR   A N   1 
ATOM   864  C CA  . THR   A 1 111 ? -14.36790 -16.62583 4.13685   1.000 8.91726  ? 111 THR   A CA  1 
ATOM   865  C C   . THR   A 1 111 ? -14.41986 -15.13008 3.88739   1.000 11.47856 ? 111 THR   A C   1 
ATOM   866  O O   . THR   A 1 111 ? -13.84259 -14.33262 4.63520   1.000 10.32091 ? 111 THR   A O   1 
ATOM   867  C CB  . THR   A 1 111 ? -15.70506 -17.07408 4.73742   1.000 10.45095 ? 111 THR   A CB  1 
ATOM   868  O OG1 . THR   A 1 111 ? -15.82771 -16.48103 6.03326   1.000 11.87554 ? 111 THR   A OG1 1 
ATOM   869  C CG2 . THR   A 1 111 ? -15.73297 -18.57579 4.86339   1.000 12.01956 ? 111 THR   A CG2 1 
ATOM   870  N N   . PHE   A 1 112 ? -15.15743 -14.76998 2.83679   1.000 9.62622  ? 112 PHE   A N   1 
ATOM   871  C CA  . PHE   A 1 112 ? -15.42698 -13.37643 2.53055   1.000 10.31319 ? 112 PHE   A CA  1 
ATOM   872  C C   . PHE   A 1 112 ? -16.64357 -13.30182 1.62502   1.000 10.67353 ? 112 PHE   A C   1 
ATOM   873  O O   . PHE   A 1 112 ? -17.03795 -14.28413 0.98540   1.000 11.81705 ? 112 PHE   A O   1 
ATOM   874  C CB  . PHE   A 1 112 ? -14.24902 -12.70711 1.84035   1.000 9.95764  ? 112 PHE   A CB  1 
ATOM   875  C CG  . PHE   A 1 112 ? -13.74447 -13.44583 0.62995   1.000 12.21119 ? 112 PHE   A CG  1 
ATOM   876  C CD1 . PHE   A 1 112 ? -12.97487 -14.59458 0.75797   1.000 12.16623 ? 112 PHE   A CD1 1 
ATOM   877  C CD2 . PHE   A 1 112 ? -14.01254 -12.96899 -0.64440  1.000 7.33401  ? 112 PHE   A CD2 1 
ATOM   878  C CE1 . PHE   A 1 112 ? -12.49750 -15.25464 -0.38525  1.000 13.61487 ? 112 PHE   A CE1 1 
ATOM   879  C CE2 . PHE   A 1 112 ? -13.52729 -13.61428 -1.78848  1.000 9.49140  ? 112 PHE   A CE2 1 
ATOM   880  C CZ  . PHE   A 1 112 ? -12.74262 -14.74379 -1.65474  1.000 10.07073 ? 112 PHE   A CZ  1 
ATOM   881  N N   . SER   A 1 113 ? -17.22084 -12.10757 1.56732   1.000 9.88269  ? 113 SER   A N   1 
ATOM   882  C CA  . SER   A 1 113 ? -18.33469 -11.83506 0.69030   1.000 10.04675 ? 113 SER   A CA  1 
ATOM   883  C C   . SER   A 1 113 ? -17.81307 -11.30879 -0.63402  1.000 9.22682  ? 113 SER   A C   1 
ATOM   884  O O   . SER   A 1 113 ? -16.86665 -10.52047 -0.66916  1.000 12.32235 ? 113 SER   A O   1 
ATOM   885  C CB  . SER   A 1 113 ? -19.27331 -10.80546 1.32681   1.000 10.41451 ? 113 SER   A CB  1 
ATOM   886  O OG  . SER   A 1 113 ? -19.68989 -11.20524 2.62714   1.000 11.18686 ? 113 SER   A OG  1 
ATOM   887  N N   . VAL   A 1 114 ? -18.44974 -11.72136 -1.72075  1.000 8.42022  ? 114 VAL   A N   1 
ATOM   888  C CA  . VAL   A 1 114 ? -18.10583 -11.24951 -3.05650  1.000 11.35145 ? 114 VAL   A CA  1 
ATOM   889  C C   . VAL   A 1 114 ? -19.28444 -10.45422 -3.58707  1.000 11.87212 ? 114 VAL   A C   1 
ATOM   890  O O   . VAL   A 1 114 ? -20.42438 -10.93359 -3.54815  1.000 10.50430 ? 114 VAL   A O   1 
ATOM   891  C CB  . VAL   A 1 114 ? -17.76309 -12.41718 -3.99724  1.000 10.04419 ? 114 VAL   A CB  1 
ATOM   892  C CG1 . VAL   A 1 114 ? -17.63078 -11.90042 -5.45285  1.000 12.46022 ? 114 VAL   A CG1 1 
ATOM   893  C CG2 . VAL   A 1 114 ? -16.51228 -13.15937 -3.52800  1.000 13.58859 ? 114 VAL   A CG2 1 
ATOM   894  N N   . LEU   A 1 115 ? -19.01870 -9.23804  -4.07416  1.000 9.93482  ? 115 LEU   A N   1 
ATOM   895  C CA  . LEU   A 1 115 ? -20.02759 -8.44316  -4.77194  1.000 11.21857 ? 115 LEU   A CA  1 
ATOM   896  C C   . LEU   A 1 115 ? -19.74783 -8.57320  -6.26384  1.000 11.50834 ? 115 LEU   A C   1 
ATOM   897  O O   . LEU   A 1 115 ? -18.89129 -7.88281  -6.82082  1.000 11.93250 ? 115 LEU   A O   1 
ATOM   898  C CB  . LEU   A 1 115 ? -20.01353 -6.98972  -4.31264  1.000 8.81251  ? 115 LEU   A CB  1 
ATOM   899  C CG  . LEU   A 1 115 ? -20.97600 -6.07571  -5.06035  1.000 10.21508 ? 115 LEU   A CG  1 
ATOM   900  C CD1 . LEU   A 1 115 ? -22.44126 -6.47320  -4.77650  1.000 14.48814 ? 115 LEU   A CD1 1 
ATOM   901  C CD2 . LEU   A 1 115 ? -20.72635 -4.63115  -4.63499  1.000 11.10708 ? 115 LEU   A CD2 1 
ATOM   902  N N   . ALA   A 1 116 ? -20.42504 -9.51565  -6.90066  1.000 11.01924 ? 116 ALA   A N   1 
ATOM   903  C CA  . ALA   A 1 116 ? -20.24569 -9.72174  -8.32785  1.000 10.72534 ? 116 ALA   A CA  1 
ATOM   904  C C   . ALA   A 1 116 ? -20.78057 -8.51746  -9.08332  1.000 14.68702 ? 116 ALA   A C   1 
ATOM   905  O O   . ALA   A 1 116 ? -21.89924 -8.05371  -8.82696  1.000 15.38598 ? 116 ALA   A O   1 
ATOM   906  C CB  . ALA   A 1 116 ? -20.95728 -10.99294 -8.78987  1.000 13.56658 ? 116 ALA   A CB  1 
ATOM   907  N N   . CYS   A 1 117 ? -19.98947 -8.02249  -10.02588 1.000 10.24127 ? 117 CYS   A N   1 
ATOM   908  C CA  . CYS   A 1 117 ? -20.30308 -6.80299  -10.74045 1.000 11.89587 ? 117 CYS   A CA  1 
ATOM   909  C C   . CYS   A 1 117 ? -20.06034 -6.98652  -12.22970 1.000 14.86530 ? 117 CYS   A C   1 
ATOM   910  O O   . CYS   A 1 117 ? -19.18429 -7.74267  -12.65197 1.000 14.51486 ? 117 CYS   A O   1 
ATOM   911  C CB  . CYS   A 1 117 ? -19.45783 -5.65015  -10.27017 1.000 15.63796 ? 117 CYS   A CB  1 
ATOM   912  S SG  . CYS   A 1 117 ? -19.83524 -5.07945  -8.63746  1.000 20.41568 ? 117 CYS   A SG  1 
ATOM   913  N N   . TYR   A 1 118 ? -20.83561 -6.25696  -13.01602 1.000 17.47475 ? 118 TYR   A N   1 
ATOM   914  C CA  . TYR   A 1 118 ? -20.67288 -6.19666  -14.46031 1.000 17.29270 ? 118 TYR   A CA  1 
ATOM   915  C C   . TYR   A 1 118 ? -20.88769 -4.75344  -14.88135 1.000 20.65903 ? 118 TYR   A C   1 
ATOM   916  O O   . TYR   A 1 118 ? -21.84210 -4.11145  -14.42961 1.000 18.99699 ? 118 TYR   A O   1 
ATOM   917  C CB  . TYR   A 1 118 ? -21.64609 -7.14883  -15.17628 1.000 17.88204 ? 118 TYR   A CB  1 
ATOM   918  C CG  . TYR   A 1 118 ? -21.40406 -8.57435  -14.73966 1.000 18.90491 ? 118 TYR   A CG  1 
ATOM   919  C CD1 . TYR   A 1 118 ? -22.06144 -9.10712  -13.63604 1.000 18.41289 ? 118 TYR   A CD1 1 
ATOM   920  C CD2 . TYR   A 1 118 ? -20.45815 -9.36865  -15.38720 1.000 18.50735 ? 118 TYR   A CD2 1 
ATOM   921  C CE1 . TYR   A 1 118 ? -21.79315 -10.39429 -13.19481 1.000 16.67177 ? 118 TYR   A CE1 1 
ATOM   922  C CE2 . TYR   A 1 118 ? -20.19092 -10.65138 -14.96374 1.000 18.19705 ? 118 TYR   A CE2 1 
ATOM   923  C CZ  . TYR   A 1 118 ? -20.85970 -11.16410 -13.87451 1.000 20.53748 ? 118 TYR   A CZ  1 
ATOM   924  O OH  . TYR   A 1 118 ? -20.57913 -12.44045 -13.44613 1.000 16.82628 ? 118 TYR   A OH  1 
ATOM   925  N N   . ASN   A 1 119 ? -19.97131 -4.23870  -15.70561 1.000 23.13663 ? 119 ASN   A N   1 
ATOM   926  C CA  . ASN   A 1 119 ? -20.07086 -2.88027  -16.24579 1.000 22.04078 ? 119 ASN   A CA  1 
ATOM   927  C C   . ASN   A 1 119 ? -20.16025 -1.83975  -15.13340 1.000 22.00768 ? 119 ASN   A C   1 
ATOM   928  O O   . ASN   A 1 119 ? -20.84990 -0.82407  -15.26687 1.000 20.71118 ? 119 ASN   A O   1 
ATOM   929  C CB  . ASN   A 1 119 ? -21.25920 -2.75717  -17.19771 1.000 25.07909 ? 119 ASN   A CB  1 
ATOM   930  C CG  . ASN   A 1 119 ? -21.23407 -3.80806  -18.26927 1.000 25.38160 ? 119 ASN   A CG  1 
ATOM   931  O OD1 . ASN   A 1 119 ? -22.10354 -4.67123  -18.32636 1.000 27.41397 ? 119 ASN   A OD1 1 
ATOM   932  N ND2 . ASN   A 1 119 ? -20.22925 -3.74885  -19.12406 1.000 25.28512 ? 119 ASN   A ND2 1 
ATOM   933  N N   . GLY   A 1 120 ? -19.46840 -2.10638  -14.02282 1.000 17.41903 ? 120 GLY   A N   1 
ATOM   934  C CA  . GLY   A 1 120 ? -19.53204 -1.25702  -12.85077 1.000 18.02995 ? 120 GLY   A CA  1 
ATOM   935  C C   . GLY   A 1 120 ? -20.83248 -1.31215  -12.07274 1.000 23.43281 ? 120 GLY   A C   1 
ATOM   936  O O   . GLY   A 1 120 ? -20.99760 -0.53883  -11.12502 1.000 21.88483 ? 120 GLY   A O   1 
ATOM   937  N N   . SER   A 1 121 ? -21.75853 -2.20763  -12.42343 1.000 21.65388 ? 121 SER   A N   1 
ATOM   938  C CA  . SER   A 1 121 ? -23.04725 -2.28822  -11.72797 1.000 16.81593 ? 121 SER   A CA  1 
ATOM   939  C C   . SER   A 1 121 ? -23.14864 -3.56551  -10.90218 1.000 22.09822 ? 121 SER   A C   1 
ATOM   940  O O   . SER   A 1 121 ? -23.07814 -4.66581  -11.47321 1.000 18.94227 ? 121 SER   A O   1 
ATOM   941  C CB  . SER   A 1 121 ? -24.19108 -2.22427  -12.73154 1.000 27.36161 ? 121 SER   A CB  1 
ATOM   942  O OG  . SER   A 1 121 ? -24.23697 -0.95642  -13.34802 1.000 30.82230 ? 121 SER   A OG  1 
ATOM   943  N N   . PRO   A 1 122 ? -23.31829 -3.47351  -9.57982  1.000 21.00598 ? 122 PRO   A N   1 
ATOM   944  C CA  . PRO   A 1 122 ? -23.46406 -4.68597  -8.75538  1.000 17.61060 ? 122 PRO   A CA  1 
ATOM   945  C C   . PRO   A 1 122 ? -24.62307 -5.55964  -9.20499  1.000 18.56485 ? 122 PRO   A C   1 
ATOM   946  O O   . PRO   A 1 122 ? -25.73484 -5.08160  -9.43422  1.000 21.65973 ? 122 PRO   A O   1 
ATOM   947  C CB  . PRO   A 1 122 ? -23.69911 -4.11928  -7.35251  1.000 20.84922 ? 122 PRO   A CB  1 
ATOM   948  C CG  . PRO   A 1 122 ? -22.85108 -2.85975  -7.35849  1.000 24.57574 ? 122 PRO   A CG  1 
ATOM   949  C CD  . PRO   A 1 122 ? -23.07580 -2.27939  -8.74661  1.000 20.57299 ? 122 PRO   A CD  1 
ATOM   950  N N   . SER   A 1 123 ? -24.35110 -6.85718  -9.29965  1.000 19.78780 ? 123 SER   A N   1 
ATOM   951  C CA  . SER   A 1 123 ? -25.29665 -7.87680  -9.73183  1.000 18.37131 ? 123 SER   A CA  1 
ATOM   952  C C   . SER   A 1 123 ? -25.77637 -8.78733  -8.60745  1.000 17.79086 ? 123 SER   A C   1 
ATOM   953  O O   . SER   A 1 123 ? -26.96199 -9.13170  -8.55868  1.000 16.70413 ? 123 SER   A O   1 
ATOM   954  C CB  . SER   A 1 123 ? -24.64707 -8.73073  -10.82694 1.000 23.84473 ? 123 SER   A CB  1 
ATOM   955  O OG  . SER   A 1 123 ? -25.46765 -9.82118  -11.19044 1.000 32.33722 ? 123 SER   A OG  1 
ATOM   956  N N   . GLY   A 1 124 ? -24.89036 -9.20460  -7.71149  1.000 13.82253 ? 124 GLY   A N   1 
ATOM   957  C CA  . GLY   A 1 124 ? -25.26765 -10.12912 -6.66185  1.000 12.13468 ? 124 GLY   A CA  1 
ATOM   958  C C   . GLY   A 1 124 ? -24.17735 -10.20142 -5.62589  1.000 15.46612 ? 124 GLY   A C   1 
ATOM   959  O O   . GLY   A 1 124 ? -23.04020 -9.77080  -5.85118  1.000 13.11727 ? 124 GLY   A O   1 
ATOM   960  N N   . VAL   A 1 125 ? -24.53564 -10.75371 -4.47721  1.000 11.93003 ? 125 VAL   A N   1 
ATOM   961  C CA  . VAL   A 1 125 ? -23.58426 -10.88936 -3.38991  1.000 12.62205 ? 125 VAL   A CA  1 
ATOM   962  C C   . VAL   A 1 125 ? -23.68705 -12.30722 -2.85347  1.000 13.38959 ? 125 VAL   A C   1 
ATOM   963  O O   . VAL   A 1 125 ? -24.78450 -12.87884 -2.75622  1.000 13.74352 ? 125 VAL   A O   1 
ATOM   964  C CB  . VAL   A 1 125 ? -23.81252 -9.82737  -2.28908  1.000 12.72187 ? 125 VAL   A CB  1 
ATOM   965  C CG1 . VAL   A 1 125 ? -25.15297 -9.99781  -1.67324  1.000 19.37355 ? 125 VAL   A CG1 1 
ATOM   966  C CG2 . VAL   A 1 125 ? -22.73254 -9.88335  -1.24113  1.000 13.57575 ? 125 VAL   A CG2 1 
ATOM   967  N N   . TYR   A 1 126 ? -22.53615 -12.89750 -2.56181  1.000 12.64091 ? 126 TYR   A N   1 
ATOM   968  C CA  . TYR   A 1 126 ? -22.50978 -14.24421 -2.01212  1.000 11.84365 ? 126 TYR   A CA  1 
ATOM   969  C C   . TYR   A 1 126 ? -21.21934 -14.47699 -1.23928  1.000 14.10898 ? 126 TYR   A C   1 
ATOM   970  O O   . TYR   A 1 126 ? -20.22545 -13.75173 -1.38087  1.000 10.41037 ? 126 TYR   A O   1 
ATOM   971  C CB  . TYR   A 1 126 ? -22.66780 -15.29762 -3.10877  1.000 9.63960  ? 126 TYR   A CB  1 
ATOM   972  C CG  . TYR   A 1 126 ? -21.60590 -15.21180 -4.17694  1.000 11.66334 ? 126 TYR   A CG  1 
ATOM   973  C CD1 . TYR   A 1 126 ? -20.41165 -15.89878 -4.06271  1.000 16.16054 ? 126 TYR   A CD1 1 
ATOM   974  C CD2 . TYR   A 1 126 ? -21.81341 -14.44100 -5.30628  1.000 14.37219 ? 126 TYR   A CD2 1 
ATOM   975  C CE1 . TYR   A 1 126 ? -19.45076 -15.79771 -5.04612  1.000 15.96192 ? 126 TYR   A CE1 1 
ATOM   976  C CE2 . TYR   A 1 126 ? -20.85373 -14.33432 -6.29322  1.000 17.92726 ? 126 TYR   A CE2 1 
ATOM   977  C CZ  . TYR   A 1 126 ? -19.68356 -15.01606 -6.16165  1.000 16.28732 ? 126 TYR   A CZ  1 
ATOM   978  O OH  . TYR   A 1 126 ? -18.72629 -14.92884 -7.15683  1.000 17.08949 ? 126 TYR   A OH  1 
ATOM   979  N N   . GLN   A 1 127 ? -21.24744 -15.53400 -0.44387  1.000 11.76306 ? 127 GLN   A N   1 
ATOM   980  C CA  . GLN   A 1 127 ? -20.14832 -15.88612 0.43582   1.000 15.08541 ? 127 GLN   A CA  1 
ATOM   981  C C   . GLN   A 1 127 ? -19.26510 -16.91992 -0.25131  1.000 14.50630 ? 127 GLN   A C   1 
ATOM   982  O O   . GLN   A 1 127 ? -19.76975 -17.82959 -0.91957  1.000 16.81252 ? 127 GLN   A O   1 
ATOM   983  C CB  . GLN   A 1 127 ? -20.72308 -16.41191 1.75716   1.000 16.43590 ? 127 GLN   A CB  1 
ATOM   984  C CG  . GLN   A 1 127 ? -19.77269 -16.45635 2.85591   1.000 19.12154 ? 127 GLN   A CG  1 
ATOM   985  C CD  . GLN   A 1 127 ? -19.54996 -15.09544 3.47919   1.000 16.13207 ? 127 GLN   A CD  1 
ATOM   986  O OE1 . GLN   A 1 127 ? -19.89114 -14.05407 2.89274   1.000 16.66905 ? 127 GLN   A OE1 1 
ATOM   987  N NE2 . GLN   A 1 127 ? -18.96806 -15.09349 4.67371   1.000 16.85400 ? 127 GLN   A NE2 1 
ATOM   988  N N   . CYS   A 1 128 ? -17.94640 -16.72448 -0.14988  1.000 11.51454 ? 128 CYS   A N   1 
ATOM   989  C CA  . CYS   A 1 128 ? -16.90611 -17.61224 -0.66397  1.000 13.26500 ? 128 CYS   A CA  1 
ATOM   990  C C   . CYS   A 1 128 ? -15.89610 -17.92835 0.42889   1.000 13.32183 ? 128 CYS   A C   1 
ATOM   991  O O   . CYS   A 1 128 ? -15.70752 -17.15944 1.36479   1.000 12.27264 ? 128 CYS   A O   1 
ATOM   992  C CB  . CYS   A 1 128 ? -16.11177 -17.00040 -1.84923  1.000 12.75322 ? 128 CYS   A CB  1 
ATOM   993  S SG  . CYS   A 1 128 ? -16.90785 -16.91700 -3.41469  1.000 24.12208 ? 128 CYS   A SG  1 
ATOM   994  N N   . ALA   A 1 129 ? -15.19544 -19.05009 0.27067   1.000 14.58001 ? 129 ALA   A N   1 
ATOM   995  C CA  . ALA   A 1 129 ? -14.03272 -19.35446 1.08652   1.000 12.99586 ? 129 ALA   A CA  1 
ATOM   996  C C   . ALA   A 1 129 ? -12.81384 -19.43078 0.18119   1.000 12.17680 ? 129 ALA   A C   1 
ATOM   997  O O   . ALA   A 1 129 ? -12.90652 -19.92798 -0.94724  1.000 12.27465 ? 129 ALA   A O   1 
ATOM   998  C CB  . ALA   A 1 129 ? -14.19471 -20.67273 1.83690   1.000 12.90837 ? 129 ALA   A CB  1 
ATOM   999  N N   . MET   A 1 130 ? -11.68087 -18.94131 0.67855   1.000 11.53450 ? 130 MET   A N   1 
ATOM   1000 C CA  . MET   A 1 130 ? -10.38802 -19.21578 0.04829   1.000 7.77412  ? 130 MET   A CA  1 
ATOM   1001 C C   . MET   A 1 130 ? -10.05713 -20.68659 0.25132   1.000 11.03909 ? 130 MET   A C   1 
ATOM   1002 O O   . MET   A 1 130 ? -9.82927  -21.13147 1.38012   1.000 11.79178 ? 130 MET   A O   1 
ATOM   1003 C CB  . MET   A 1 130 ? -9.31351  -18.30002 0.63886   1.000 10.89970 ? 130 MET   A CB  1 
ATOM   1004 C CG  . MET   A 1 130 ? -7.92347  -18.24561 -0.04972  1.000 14.90631 ? 130 MET   A CG  1 
ATOM   1005 S SD  . MET   A 1 130 ? -7.90717  -17.96380 -1.80595  1.000 16.16888 ? 130 MET   A SD  1 
ATOM   1006 C CE  . MET   A 1 130 ? -8.40609  -16.24919 -1.90256  1.000 8.06136  ? 130 MET   A CE  1 
ATOM   1007 N N   . ARG   A 1 131 ? -10.07082 -21.45340 -0.83533  1.000 9.81381  ? 131 ARG   A N   1 
ATOM   1008 C CA  . ARG   A 1 131 ? -9.72408  -22.86091 -0.76011  1.000 11.99063 ? 131 ARG   A CA  1 
ATOM   1009 C C   . ARG   A 1 131 ? -8.26953  -23.02092 -0.31331  1.000 11.46575 ? 131 ARG   A C   1 
ATOM   1010 O O   . ARG   A 1 131 ? -7.44780  -22.11032 -0.48804  1.000 10.94980 ? 131 ARG   A O   1 
ATOM   1011 C CB  . ARG   A 1 131 ? -9.93596  -23.52233 -2.12392  1.000 11.04087 ? 131 ARG   A CB  1 
ATOM   1012 C CG  . ARG   A 1 131 ? -11.38590 -23.57384 -2.66694  1.000 13.95573 ? 131 ARG   A CG  1 
ATOM   1013 C CD  . ARG   A 1 131 ? -12.37721 -23.99711 -1.61008  1.000 11.91909 ? 131 ARG   A CD  1 
ATOM   1014 N NE  . ARG   A 1 131 ? -12.01135 -25.27317 -1.00846  1.000 12.79407 ? 131 ARG   A NE  1 
ATOM   1015 C CZ  . ARG   A 1 131 ? -12.67987 -25.82480 -0.00325  1.000 14.29223 ? 131 ARG   A CZ  1 
ATOM   1016 N NH1 . ARG   A 1 131 ? -13.75149 -25.21150 0.46965   1.000 12.49168 ? 131 ARG   A NH1 1 
ATOM   1017 N NH2 . ARG   A 1 131 ? -12.28304 -26.98024 0.51944   1.000 15.33808 ? 131 ARG   A NH2 1 
ATOM   1018 N N   . PRO   A 1 132 ? -7.92904  -24.16851 0.28555   1.000 10.15739 ? 132 PRO   A N   1 
ATOM   1019 C CA  . PRO   A 1 132 ? -6.51630  -24.46716 0.55682   1.000 11.84101 ? 132 PRO   A CA  1 
ATOM   1020 C C   . PRO   A 1 132 ? -5.61722  -24.34412 -0.65913  1.000 12.23950 ? 132 PRO   A C   1 
ATOM   1021 O O   . PRO   A 1 132 ? -4.43274  -24.01639 -0.49167  1.000 11.49358 ? 132 PRO   A O   1 
ATOM   1022 C CB  . PRO   A 1 132 ? -6.57615  -25.90525 1.08887   1.000 13.76562 ? 132 PRO   A CB  1 
ATOM   1023 C CG  . PRO   A 1 132 ? -7.90394  -25.93263 1.82497   1.000 13.56065 ? 132 PRO   A CG  1 
ATOM   1024 C CD  . PRO   A 1 132 ? -8.82106  -25.18891 0.87820   1.000 12.56268 ? 132 PRO   A CD  1 
ATOM   1025 N N   . ASN   A 1 133 ? -6.13101  -24.54758 -1.88342  1.000 10.81682 ? 133 ASN   A N   1 
ATOM   1026 C CA  . ASN   A 1 133 ? -5.28705  -24.37665 -3.06178  1.000 10.03455 ? 133 ASN   A CA  1 
ATOM   1027 C C   . ASN   A 1 133 ? -5.32703  -22.96251 -3.62535  1.000 9.15233  ? 133 ASN   A C   1 
ATOM   1028 O O   . ASN   A 1 133 ? -4.90961  -22.76666 -4.77214  1.000 11.04395 ? 133 ASN   A O   1 
ATOM   1029 C CB  . ASN   A 1 133 ? -5.65184  -25.39142 -4.14952  1.000 14.20426 ? 133 ASN   A CB  1 
ATOM   1030 C CG  . ASN   A 1 133 ? -7.07011  -25.24069 -4.65100  1.000 10.99149 ? 133 ASN   A CG  1 
ATOM   1031 O OD1 . ASN   A 1 133 ? -7.79323  -24.31995 -4.27146  1.000 12.34791 ? 133 ASN   A OD1 1 
ATOM   1032 N ND2 . ASN   A 1 133 ? -7.48315  -26.17088 -5.50187  1.000 15.14086 ? 133 ASN   A ND2 1 
ATOM   1033 N N   . PHE   A 1 134 ? -5.82918  -21.98915 -2.85381  1.000 10.57222 ? 134 PHE   A N   1 
ATOM   1034 C CA  . PHE   A 1 134 ? -5.80883  -20.56886 -3.22328  1.000 9.88193  ? 134 PHE   A CA  1 
ATOM   1035 C C   . PHE   A 1 134 ? -6.69614  -20.25001 -4.41606  1.000 12.29646 ? 134 PHE   A C   1 
ATOM   1036 O O   . PHE   A 1 134 ? -6.46557  -19.26187 -5.12142  1.000 13.52709 ? 134 PHE   A O   1 
ATOM   1037 C CB  . PHE   A 1 134 ? -4.39062  -20.08377 -3.50926  1.000 9.83890  ? 134 PHE   A CB  1 
ATOM   1038 C CG  . PHE   A 1 134 ? -3.55781  -19.94726 -2.30313  1.000 9.26838  ? 134 PHE   A CG  1 
ATOM   1039 C CD1 . PHE   A 1 134 ? -3.72335  -18.87355 -1.46622  1.000 10.24187 ? 134 PHE   A CD1 1 
ATOM   1040 C CD2 . PHE   A 1 134 ? -2.58867  -20.89635 -1.99689  1.000 12.86256 ? 134 PHE   A CD2 1 
ATOM   1041 C CE1 . PHE   A 1 134 ? -2.91193  -18.74297 -0.31655  1.000 12.35807 ? 134 PHE   A CE1 1 
ATOM   1042 C CE2 . PHE   A 1 134 ? -1.79470  -20.77235 -0.85805  1.000 16.72674 ? 134 PHE   A CE2 1 
ATOM   1043 C CZ  . PHE   A 1 134 ? -1.96340  -19.69055 -0.02431  1.000 14.17685 ? 134 PHE   A CZ  1 
ATOM   1044 N N   . THR   A 1 135 ? -7.69789  -21.07967 -4.67076  1.000 12.76901 ? 135 THR   A N   1 
ATOM   1045 C CA  . THR   A 1 135 ? -8.75861  -20.74175 -5.59935  1.000 9.60922  ? 135 THR   A CA  1 
ATOM   1046 C C   . THR   A 1 135 ? -10.00693 -20.47948 -4.78214  1.000 12.17721 ? 135 THR   A C   1 
ATOM   1047 O O   . THR   A 1 135 ? -10.06847 -20.79517 -3.59309  1.000 10.60168 ? 135 THR   A O   1 
ATOM   1048 C CB  . THR   A 1 135 ? -9.01252  -21.87009 -6.60650  1.000 9.38402  ? 135 THR   A CB  1 
ATOM   1049 O OG1 . THR   A 1 135 ? -9.48288  -23.03971 -5.92362  1.000 13.45893 ? 135 THR   A OG1 1 
ATOM   1050 C CG2 . THR   A 1 135 ? -7.73012  -22.24502 -7.32268  1.000 10.53057 ? 135 THR   A CG2 1 
ATOM   1051 N N   . ILE   A 1 136 ? -10.99551 -19.89907 -5.43440  1.000 9.48684  ? 136 ILE   A N   1 
ATOM   1052 C CA  . ILE   A 1 136 ? -12.31101 -19.73360 -4.83665  1.000 11.67654 ? 136 ILE   A CA  1 
ATOM   1053 C C   . ILE   A 1 136 ? -13.35725 -20.29878 -5.78530  1.000 11.39121 ? 136 ILE   A C   1 
ATOM   1054 O O   . ILE   A 1 136 ? -13.24186 -20.19591 -7.01169  1.000 12.25203 ? 136 ILE   A O   1 
ATOM   1055 C CB  . ILE   A 1 136 ? -12.61006 -18.26357 -4.46977  1.000 12.94489 ? 136 ILE   A CB  1 
ATOM   1056 C CG1 . ILE   A 1 136 ? -12.84096 -17.41897 -5.71389  1.000 12.30168 ? 136 ILE   A CG1 1 
ATOM   1057 C CG2 . ILE   A 1 136 ? -11.49953 -17.67221 -3.55703  1.000 10.95230 ? 136 ILE   A CG2 1 
ATOM   1058 C CD1 . ILE   A 1 136 ? -13.41360 -16.05545 -5.41409  1.000 12.43304 ? 136 ILE   A CD1 1 
ATOM   1059 N N   . LYS   A 1 137 ? -14.36476 -20.94040 -5.21030  1.000 13.30486 ? 137 LYS   A N   1 
ATOM   1060 C CA  . LYS   A 1 137 ? -15.44162 -21.51911 -6.00004  1.000 17.05424 ? 137 LYS   A CA  1 
ATOM   1061 C C   . LYS   A 1 137 ? -16.48628 -20.41491 -6.11596  1.000 14.90995 ? 137 LYS   A C   1 
ATOM   1062 O O   . LYS   A 1 137 ? -17.40637 -20.30294 -5.30414  1.000 17.73880 ? 137 LYS   A O   1 
ATOM   1063 C CB  . LYS   A 1 137 ? -15.95121 -22.78642 -5.32804  1.000 16.40988 ? 137 LYS   A CB  1 
ATOM   1064 C CG  . LYS   A 1 137 ? -14.89928 -23.89698 -5.26127  1.000 16.90408 ? 137 LYS   A CG  1 
ATOM   1065 C CD  . LYS   A 1 137 ? -15.42283 -25.13865 -4.52482  1.000 19.87240 ? 137 LYS   A CD  1 
ATOM   1066 C CE  . LYS   A 1 137 ? -14.46322 -26.32519 -4.65352  1.000 23.31375 ? 137 LYS   A CE  1 
ATOM   1067 N NZ  . LYS   A 1 137 ? -14.51156 -26.95243 -6.00631  1.000 28.87122 ? 137 LYS   A NZ  1 
ATOM   1068 N N   . GLY   A 1 138 ? -16.29214 -19.53810 -7.10121  1.000 15.01523 ? 138 GLY   A N   1 
ATOM   1069 C CA  . GLY   A 1 138 ? -17.12536 -18.37172 -7.26598  1.000 14.26352 ? 138 GLY   A CA  1 
ATOM   1070 C C   . GLY   A 1 138 ? -18.18362 -18.56093 -8.33218  1.000 17.28946 ? 138 GLY   A C   1 
ATOM   1071 O O   . GLY   A 1 138 ? -18.40542 -19.65510 -8.85429  1.000 17.04187 ? 138 GLY   A O   1 
ATOM   1072 N N   . SER   A 1 139 ? -18.84477 -17.45384 -8.66290  1.000 12.28371 ? 139 SER   A N   1 
ATOM   1073 C CA  . SER   A 1 139 ? -19.80555 -17.39956 -9.75571  1.000 14.40935 ? 139 SER   A CA  1 
ATOM   1074 C C   . SER   A 1 139 ? -19.48604 -16.12965 -10.52993 1.000 14.43304 ? 139 SER   A C   1 
ATOM   1075 O O   . SER   A 1 139 ? -19.86867 -15.03521 -10.11311 1.000 14.19521 ? 139 SER   A O   1 
ATOM   1076 C CB  . SER   A 1 139 ? -21.24218 -17.40469 -9.24777  1.000 16.46047 ? 139 SER   A CB  1 
ATOM   1077 O OG  . SER   A 1 139 ? -22.16981 -17.36130 -10.31420 1.000 17.04650 ? 139 SER   A OG  1 
ATOM   1078 N N   . PHE   A 1 140 ? -18.80353 -16.28845 -11.65837 1.000 16.03901 ? 140 PHE   A N   1 
ATOM   1079 C CA  . PHE   A 1 140 ? -18.22037 -15.18047 -12.40253 1.000 15.61208 ? 140 PHE   A CA  1 
ATOM   1080 C C   . PHE   A 1 140 ? -18.39648 -15.43754 -13.89322 1.000 17.94064 ? 140 PHE   A C   1 
ATOM   1081 O O   . PHE   A 1 140 ? -18.11516 -16.53887 -14.36930 1.000 18.20578 ? 140 PHE   A O   1 
ATOM   1082 C CB  . PHE   A 1 140 ? -16.72932 -15.03306 -12.06106 1.000 15.41129 ? 140 PHE   A CB  1 
ATOM   1083 C CG  . PHE   A 1 140 ? -16.43580 -14.45751 -10.68931 1.000 11.80755 ? 140 PHE   A CG  1 
ATOM   1084 C CD1 . PHE   A 1 140 ? -16.78280 -13.15401 -10.36373 1.000 14.64562 ? 140 PHE   A CD1 1 
ATOM   1085 C CD2 . PHE   A 1 140 ? -15.78413 -15.21470 -9.73017  1.000 14.70994 ? 140 PHE   A CD2 1 
ATOM   1086 C CE1 . PHE   A 1 140 ? -16.47498 -12.62665 -9.11628  1.000 14.11147 ? 140 PHE   A CE1 1 
ATOM   1087 C CE2 . PHE   A 1 140 ? -15.49264 -14.69183 -8.46741  1.000 14.23804 ? 140 PHE   A CE2 1 
ATOM   1088 C CZ  . PHE   A 1 140 ? -15.83591 -13.38846 -8.16717  1.000 10.92328 ? 140 PHE   A CZ  1 
ATOM   1089 N N   . LEU   A 1 141 ? -18.87783 -14.43905 -14.62479 1.000 15.42881 ? 141 LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 141 ? -18.96820 -14.49688 -16.07549 1.000 19.88494 ? 141 LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 141 ? -18.03145 -13.45811 -16.67474 1.000 17.54605 ? 141 LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 141 ? -17.39204 -12.68577 -15.96211 1.000 16.68897 ? 141 LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 141 ? -20.41341 -14.27719 -16.53325 1.000 16.12951 ? 141 LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 141 ? -21.37335 -15.20851 -15.79338 1.000 21.73974 ? 141 LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 141 ? -22.80874 -14.74108 -15.94287 1.000 25.80684 ? 141 LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 141 ? -21.22133 -16.65181 -16.26385 1.000 21.27501 ? 141 LEU   A CD2 1 
ATOM   1097 N N   . ASN   A 1 142 ? -17.95869 -13.42928 -18.00224 1.000 21.34179 ? 142 ASN   A N   1 
ATOM   1098 C CA  . ASN   A 1 142 ? -17.12637 -12.41832 -18.62761 1.000 20.79145 ? 142 ASN   A CA  1 
ATOM   1099 C C   . ASN   A 1 142 ? -17.60325 -11.04086 -18.18659 1.000 20.50938 ? 142 ASN   A C   1 
ATOM   1100 O O   . ASN   A 1 142 ? -18.80622 -10.78923 -18.04637 1.000 19.32134 ? 142 ASN   A O   1 
ATOM   1101 C CB  . ASN   A 1 142 ? -17.14841 -12.53973 -20.14646 1.000 23.53305 ? 142 ASN   A CB  1 
ATOM   1102 C CG  . ASN   A 1 142 ? -16.06656 -11.69217 -20.79966 1.000 33.76766 ? 142 ASN   A CG  1 
ATOM   1103 O OD1 . ASN   A 1 142 ? -15.06890 -11.31731 -20.14845 1.000 33.34775 ? 142 ASN   A OD1 1 
ATOM   1104 N ND2 . ASN   A 1 142 ? -16.25092 -11.37719 -22.08210 1.000 35.09902 ? 142 ASN   A ND2 1 
ATOM   1105 N N   . GLY   A 1 143 ? -16.65112 -10.15853 -17.92915 1.000 18.93925 ? 143 GLY   A N   1 
ATOM   1106 C CA  . GLY   A 1 143 ? -16.95821 -8.83159  -17.44956 1.000 20.79224 ? 143 GLY   A CA  1 
ATOM   1107 C C   . GLY   A 1 143 ? -16.92522 -8.68760  -15.94502 1.000 17.10257 ? 143 GLY   A C   1 
ATOM   1108 O O   . GLY   A 1 143 ? -17.02547 -7.56340  -15.44512 1.000 17.67630 ? 143 GLY   A O   1 
ATOM   1109 N N   . SER   A 1 144 ? -16.78531 -9.78726  -15.21039 1.000 13.71616 ? 144 SER   A N   1 
ATOM   1110 C CA  . SER   A 1 144 ? -16.79769 -9.73458  -13.75847 1.000 15.52672 ? 144 SER   A CA  1 
ATOM   1111 C C   . SER   A 1 144 ? -15.45234 -9.33190  -13.17122 1.000 13.87100 ? 144 SER   A C   1 
ATOM   1112 O O   . SER   A 1 144 ? -15.37264 -9.10733  -11.96216 1.000 14.45876 ? 144 SER   A O   1 
ATOM   1113 C CB  . SER   A 1 144 ? -17.19663 -11.10019 -13.19063 1.000 14.36642 ? 144 SER   A CB  1 
ATOM   1114 O OG  . SER   A 1 144 ? -16.23055 -12.07677 -13.57620 1.000 14.88366 ? 144 SER   A OG  1 
ATOM   1115 N N   . CYS   A 1 145 ? -14.38663 -9.26118  -13.97900 1.000 12.65702 ? 145 CYS   A N   1 
ATOM   1116 C CA  . CYS   A 1 145 ? -13.09093 -8.91116  -13.41996 1.000 14.10165 ? 145 CYS   A CA  1 
ATOM   1117 C C   . CYS   A 1 145 ? -13.15551 -7.56259  -12.72218 1.000 11.53907 ? 145 CYS   A C   1 
ATOM   1118 O O   . CYS   A 1 145 ? -13.85503 -6.64335  -13.15896 1.000 14.37231 ? 145 CYS   A O   1 
ATOM   1119 C CB  . CYS   A 1 145 ? -12.01194 -8.90894  -14.49463 1.000 16.29321 ? 145 CYS   A CB  1 
ATOM   1120 S SG  . CYS   A 1 145 ? -11.71121 -10.58590 -15.08775 1.000 19.54539 ? 145 CYS   A SG  1 
ATOM   1121 N N   . GLY   A 1 146 ? -12.41847 -7.45598  -11.62236 1.000 13.57640 ? 146 GLY   A N   1 
ATOM   1122 C CA  . GLY   A 1 146 ? -12.46133 -6.27887  -10.80036 1.000 12.66399 ? 146 GLY   A CA  1 
ATOM   1123 C C   . GLY   A 1 146 ? -13.50138 -6.29967  -9.71864  1.000 12.57830 ? 146 GLY   A C   1 
ATOM   1124 O O   . GLY   A 1 146 ? -13.46560 -5.42070  -8.84883  1.000 12.46170 ? 146 GLY   A O   1 
ATOM   1125 N N   . SER   A 1 147 ? -14.42799 -7.26530  -9.74785  1.000 10.82002 ? 147 SER   A N   1 
ATOM   1126 C CA  . SER   A 1 147 ? -15.29012 -7.52099  -8.60241  1.000 10.83552 ? 147 SER   A CA  1 
ATOM   1127 C C   . SER   A 1 147 ? -14.41690 -7.87883  -7.41036  1.000 11.23513 ? 147 SER   A C   1 
ATOM   1128 O O   . SER   A 1 147 ? -13.36627 -8.53182  -7.55601  1.000 8.88980  ? 147 SER   A O   1 
ATOM   1129 C CB  . SER   A 1 147 ? -16.24629 -8.67225  -8.90383  1.000 9.27748  ? 147 SER   A CB  1 
ATOM   1130 O OG  . SER   A 1 147 ? -17.04796 -8.39444  -10.04759 1.000 12.50811 ? 147 SER   A OG  1 
ATOM   1131 N N   . VAL   A 1 148 ? -14.82016 -7.42087  -6.22904  1.000 9.00233  ? 148 VAL   A N   1 
ATOM   1132 C CA  . VAL   A 1 148 ? -13.98404 -7.57835  -5.05471  1.000 8.07754  ? 148 VAL   A CA  1 
ATOM   1133 C C   . VAL   A 1 148 ? -14.67270 -8.47013  -4.03725  1.000 10.40536 ? 148 VAL   A C   1 
ATOM   1134 O O   . VAL   A 1 148 ? -15.90164 -8.62637  -4.00901  1.000 10.24313 ? 148 VAL   A O   1 
ATOM   1135 C CB  . VAL   A 1 148 ? -13.60106 -6.23019  -4.40483  1.000 9.06353  ? 148 VAL   A CB  1 
ATOM   1136 C CG1 . VAL   A 1 148 ? -12.68281 -5.42882  -5.34251  1.000 9.10880  ? 148 VAL   A CG1 1 
ATOM   1137 C CG2 . VAL   A 1 148 ? -14.84264 -5.43722  -4.06720  1.000 10.35083 ? 148 VAL   A CG2 1 
ATOM   1138 N N   . GLY   A 1 149 ? -13.83733 -9.06241  -3.19869  1.000 10.50153 ? 149 GLY   A N   1 
ATOM   1139 C CA  . GLY   A 1 149 ? -14.27765 -9.79701  -2.03636  1.000 8.00392  ? 149 GLY   A CA  1 
ATOM   1140 C C   . GLY   A 1 149 ? -13.87197 -9.01137  -0.80637  1.000 8.83514  ? 149 GLY   A C   1 
ATOM   1141 O O   . GLY   A 1 149 ? -12.88528 -8.28027  -0.81813  1.000 8.07250  ? 149 GLY   A O   1 
ATOM   1142 N N   . PHE   A 1 150 ? -14.63294 -9.17057  0.27077   1.000 8.36818  ? 150 PHE   A N   1 
ATOM   1143 C CA  . PHE   A 1 150 ? -14.45638 -8.28735  1.40368   1.000 8.16642  ? 150 PHE   A CA  1 
ATOM   1144 C C   . PHE   A 1 150 ? -15.12118 -8.88031  2.63259   1.000 11.29702 ? 150 PHE   A C   1 
ATOM   1145 O O   . PHE   A 1 150 ? -16.01626 -9.72017  2.53660   1.000 10.26536 ? 150 PHE   A O   1 
ATOM   1146 C CB  . PHE   A 1 150 ? -15.05848 -6.91088  1.10530   1.000 11.04835 ? 150 PHE   A CB  1 
ATOM   1147 C CG  . PHE   A 1 150 ? -16.55045 -6.94224  0.93814   1.000 10.75747 ? 150 PHE   A CG  1 
ATOM   1148 C CD1 . PHE   A 1 150 ? -17.11109 -7.22930  -0.31089  1.000 9.41922  ? 150 PHE   A CD1 1 
ATOM   1149 C CD2 . PHE   A 1 150 ? -17.39764 -6.69282  2.01929   1.000 9.55835  ? 150 PHE   A CD2 1 
ATOM   1150 C CE1 . PHE   A 1 150 ? -18.50963 -7.27442  -0.49125  1.000 11.27849 ? 150 PHE   A CE1 1 
ATOM   1151 C CE2 . PHE   A 1 150 ? -18.79043 -6.73546  1.85177   1.000 11.40762 ? 150 PHE   A CE2 1 
ATOM   1152 C CZ  . PHE   A 1 150 ? -19.34606 -7.02033  0.59481   1.000 13.15660 ? 150 PHE   A CZ  1 
ATOM   1153 N N   . ASN   A 1 151 ? -14.70935 -8.36674  3.78106   1.000 10.87208 ? 151 ASN   A N   1 
ATOM   1154 C CA  . ASN   A 1 151 ? -15.37830 -8.58535  5.05361   1.000 13.93486 ? 151 ASN   A CA  1 
ATOM   1155 C C   . ASN   A 1 151 ? -15.66656 -7.21588  5.64733   1.000 13.38066 ? 151 ASN   A C   1 
ATOM   1156 O O   . ASN   A 1 151 ? -15.05713 -6.22402  5.26423   1.000 13.21881 ? 151 ASN   A O   1 
ATOM   1157 C CB  . ASN   A 1 151 ? -14.50156 -9.41342  5.98651   1.000 12.94208 ? 151 ASN   A CB  1 
ATOM   1158 C CG  . ASN   A 1 151 ? -14.45048 -10.87017 5.60582   1.000 14.79309 ? 151 ASN   A CG  1 
ATOM   1159 O OD1 . ASN   A 1 151 ? -13.45859 -11.34598 5.06029   1.000 14.35430 ? 151 ASN   A OD1 1 
ATOM   1160 N ND2 . ASN   A 1 151 ? -15.46300 -11.61669 6.01138   1.000 15.10814 ? 151 ASN   A ND2 1 
ATOM   1161 N N   . ILE   A 1 152 ? -16.61592 -7.14478  6.57063   1.000 12.66618 ? 152 ILE   A N   1 
ATOM   1162 C CA  . ILE   A 1 152 ? -16.93688 -5.88713  7.23201   1.000 16.53815 ? 152 ILE   A CA  1 
ATOM   1163 C C   . ILE   A 1 152 ? -16.78434 -6.09456  8.72571   1.000 24.40192 ? 152 ILE   A C   1 
ATOM   1164 O O   . ILE   A 1 152 ? -17.28810 -7.08099  9.27252   1.000 21.47872 ? 152 ILE   A O   1 
ATOM   1165 C CB  . ILE   A 1 152 ? -18.34823 -5.38304  6.88190   1.000 17.72398 ? 152 ILE   A CB  1 
ATOM   1166 C CG1 . ILE   A 1 152 ? -18.46199 -5.10093  5.37684   1.000 13.83973 ? 152 ILE   A CG1 1 
ATOM   1167 C CG2 . ILE   A 1 152 ? -18.63994 -4.10957  7.66248   1.000 20.75149 ? 152 ILE   A CG2 1 
ATOM   1168 C CD1 . ILE   A 1 152 ? -19.74626 -4.34645  4.97843   1.000 20.28098 ? 152 ILE   A CD1 1 
ATOM   1169 N N   . ASP   A 1 153 ? -16.07056 -5.17699  9.37488   1.000 26.71625 ? 153 ASP   A N   1 
ATOM   1170 C CA  . ASP   A 1 153 ? -15.77279 -5.24596  10.80270  1.000 32.38715 ? 153 ASP   A CA  1 
ATOM   1171 C C   . ASP   A 1 153 ? -16.19405 -3.91125  11.39471  1.000 35.96584 ? 153 ASP   A C   1 
ATOM   1172 O O   . ASP   A 1 153 ? -15.56828 -2.88193  11.12024  1.000 33.75226 ? 153 ASP   A O   1 
ATOM   1173 C CB  . ASP   A 1 153 ? -14.28942 -5.52146  11.04685  1.000 32.49226 ? 153 ASP   A CB  1 
ATOM   1174 C CG  . ASP   A 1 153 ? -14.00623 -6.02304  12.44425  1.000 44.68540 ? 153 ASP   A CG  1 
ATOM   1175 O OD1 . ASP   A 1 153 ? -14.96118 -6.44494  13.13184  1.000 43.96039 ? 153 ASP   A OD1 1 
ATOM   1176 O OD2 . ASP   A 1 153 ? -12.81861 -6.00397  12.85204  1.000 48.66528 ? 153 ASP   A OD2 1 
ATOM   1177 N N   . TYR   A 1 154 ? -17.24651 -3.94337  12.20830  1.000 38.49952 ? 154 TYR   A N   1 
ATOM   1178 C CA  . TYR   A 1 154 ? -18.05826 -2.77997  12.53838  1.000 44.41953 ? 154 TYR   A CA  1 
ATOM   1179 C C   . TYR   A 1 154 ? -18.36429 -1.94802  11.29618  1.000 43.65299 ? 154 TYR   A C   1 
ATOM   1180 O O   . TYR   A 1 154 ? -19.24012 -2.31452  10.50877  1.000 44.79060 ? 154 TYR   A O   1 
ATOM   1181 C CB  . TYR   A 1 154 ? -17.40741 -1.90687  13.60872  1.000 44.41872 ? 154 TYR   A CB  1 
ATOM   1182 C CG  . TYR   A 1 154 ? -18.38766 -0.85069  14.07641  1.000 54.15346 ? 154 TYR   A CG  1 
ATOM   1183 C CD1 . TYR   A 1 154 ? -19.71474 -1.18865  14.32592  1.000 53.59534 ? 154 TYR   A CD1 1 
ATOM   1184 C CD2 . TYR   A 1 154 ? -18.01020 0.47997   14.22761  1.000 52.40908 ? 154 TYR   A CD2 1 
ATOM   1185 C CE1 . TYR   A 1 154 ? -20.63174 -0.24353  14.73319  1.000 58.19250 ? 154 TYR   A CE1 1 
ATOM   1186 C CE2 . TYR   A 1 154 ? -18.92818 1.44062   14.63716  1.000 54.64856 ? 154 TYR   A CE2 1 
ATOM   1187 C CZ  . TYR   A 1 154 ? -20.23826 1.07090   14.88805  1.000 60.28411 ? 154 TYR   A CZ  1 
ATOM   1188 O OH  . TYR   A 1 154 ? -21.15920 2.01273   15.29885  1.000 60.81571 ? 154 TYR   A OH  1 
ATOM   1189 N N   . ASP   A 1 155 ? -17.66635 -0.82730  11.11155  1.000 39.16456 ? 155 ASP   A N   1 
ATOM   1190 C CA  . ASP   A 1 155 ? -17.93897 0.08399   10.00577  1.000 38.41291 ? 155 ASP   A CA  1 
ATOM   1191 C C   . ASP   A 1 155 ? -16.88461 0.01100   8.91230   1.000 32.73357 ? 155 ASP   A C   1 
ATOM   1192 O O   . ASP   A 1 155 ? -16.96071 0.76982   7.93702   1.000 27.08117 ? 155 ASP   A O   1 
ATOM   1193 C CB  . ASP   A 1 155 ? -18.01110 1.52540   10.51442  1.000 42.35273 ? 155 ASP   A CB  1 
ATOM   1194 C CG  . ASP   A 1 155 ? -16.79304 1.90514   11.33928  1.000 43.21750 ? 155 ASP   A CG  1 
ATOM   1195 O OD1 . ASP   A 1 155 ? -16.03045 0.98773   11.72623  1.000 43.19169 ? 155 ASP   A OD1 1 
ATOM   1196 O OD2 . ASP   A 1 155 ? -16.59192 3.11442   11.59146  1.000 46.72163 ? 155 ASP   A OD2 1 
ATOM   1197 N N   . CYS   A 1 156 ? -15.89128 -0.85344  9.06593   1.000 29.53927 ? 156 CYS   A N   1 
ATOM   1198 C CA  . CYS   A 1 156 ? -14.69829 -0.81829  8.23530   1.000 24.29968 ? 156 CYS   A CA  1 
ATOM   1199 C C   . CYS   A 1 156 ? -14.72793 -1.98256  7.26004   1.000 19.78691 ? 156 CYS   A C   1 
ATOM   1200 O O   . CYS   A 1 156 ? -14.93244 -3.13656  7.66232   1.000 18.99155 ? 156 CYS   A O   1 
ATOM   1201 C CB  . CYS   A 1 156 ? -13.44342 -0.87098  9.10134   1.000 24.77800 ? 156 CYS   A CB  1 
ATOM   1202 S SG  . CYS   A 1 156 ? -11.92831 -1.03639  8.16532   1.000 22.22619 ? 156 CYS   A SG  1 
ATOM   1203 N N   . VAL   A 1 157 ? -14.54188 -1.67827  5.97979   1.000 16.21614 ? 157 VAL   A N   1 
ATOM   1204 C CA  . VAL   A 1 157 ? -14.54650 -2.70039  4.94164   1.000 11.19729 ? 157 VAL   A CA  1 
ATOM   1205 C C   . VAL   A 1 157 ? -13.12360 -3.19178  4.75210   1.000 14.33755 ? 157 VAL   A C   1 
ATOM   1206 O O   . VAL   A 1 157 ? -12.25926 -2.41313  4.35962   1.000 11.59886 ? 157 VAL   A O   1 
ATOM   1207 C CB  . VAL   A 1 157 ? -15.10195 -2.15188  3.61920   1.000 12.39421 ? 157 VAL   A CB  1 
ATOM   1208 C CG1 . VAL   A 1 157 ? -15.04955 -3.23549  2.55959   1.000 9.90486  ? 157 VAL   A CG1 1 
ATOM   1209 C CG2 . VAL   A 1 157 ? -16.52584 -1.60745  3.80572   1.000 14.04780 ? 157 VAL   A CG2 1 
ATOM   1210 N N   . SER   A 1 158 ? -12.87886 -4.48161  5.00031   1.000 14.23711 ? 158 SER   A N   1 
ATOM   1211 C CA  . SER   A 1 158 ? -11.56455 -5.08230  4.74210   1.000 10.02426 ? 158 SER   A CA  1 
ATOM   1212 C C   . SER   A 1 158 ? -11.64159 -5.78480  3.39696   1.000 9.99340  ? 158 SER   A C   1 
ATOM   1213 O O   . SER   A 1 158 ? -12.21342 -6.86944  3.29294   1.000 10.95491 ? 158 SER   A O   1 
ATOM   1214 C CB  . SER   A 1 158 ? -11.16796 -6.06276  5.84158   1.000 11.54422 ? 158 SER   A CB  1 
ATOM   1215 O OG  . SER   A 1 158 ? -10.97544 -5.38240  7.08447   1.000 15.84603 ? 158 SER   A OG  1 
ATOM   1216 N N   . PHE   A 1 159 ? -11.08298 -5.15321  2.36360   1.000 9.69506  ? 159 PHE   A N   1 
ATOM   1217 C CA  . PHE   A 1 159 ? -11.05778 -5.74795  1.03080   1.000 9.06480  ? 159 PHE   A CA  1 
ATOM   1218 C C   . PHE   A 1 159 ? -9.95889  -6.79018  1.00254   1.000 9.07177  ? 159 PHE   A C   1 
ATOM   1219 O O   . PHE   A 1 159 ? -8.82996  -6.51034  1.40928   1.000 9.71033  ? 159 PHE   A O   1 
ATOM   1220 C CB  . PHE   A 1 159 ? -10.78300 -4.69368  -0.04531  1.000 9.32899  ? 159 PHE   A CB  1 
ATOM   1221 C CG  . PHE   A 1 159 ? -11.87442 -3.66408  -0.18063  1.000 8.83409  ? 159 PHE   A CG  1 
ATOM   1222 C CD1 . PHE   A 1 159 ? -13.04932 -3.96581  -0.86856  1.000 9.14530  ? 159 PHE   A CD1 1 
ATOM   1223 C CD2 . PHE   A 1 159 ? -11.72494 -2.39561  0.38392   1.000 11.91181 ? 159 PHE   A CD2 1 
ATOM   1224 C CE1 . PHE   A 1 159 ? -14.05455 -3.02595  -0.99597  1.000 9.26178  ? 159 PHE   A CE1 1 
ATOM   1225 C CE2 . PHE   A 1 159 ? -12.72710 -1.44928  0.26728   1.000 10.39682 ? 159 PHE   A CE2 1 
ATOM   1226 C CZ  . PHE   A 1 159 ? -13.90377 -1.76595  -0.42361  1.000 13.88226 ? 159 PHE   A CZ  1 
ATOM   1227 N N   . CYS   A 1 160 ? -10.27698 -7.98937  0.53615   1.000 8.93977  ? 160 CYS   A N   1 
ATOM   1228 C CA  . CYS   A 1 160 ? -9.26551  -9.01397  0.48679   1.000 8.21798  ? 160 CYS   A CA  1 
ATOM   1229 C C   . CYS   A 1 160 ? -9.05871  -9.62631  -0.87922  1.000 8.04572  ? 160 CYS   A C   1 
ATOM   1230 O O   . CYS   A 1 160 ? -8.07698  -10.35468 -1.04117  1.000 10.91377 ? 160 CYS   A O   1 
ATOM   1231 C CB  . CYS   A 1 160 ? -9.57092  -10.15288 1.46459   1.000 6.42626  ? 160 CYS   A CB  1 
ATOM   1232 S SG  . CYS   A 1 160 ? -11.25048 -10.85013 1.25328   1.000 12.53460 ? 160 CYS   A SG  1 
ATOM   1233 N N   . TYR   A 1 161 ? -9.90403  -9.34693  -1.86477  1.000 7.22307  ? 161 TYR   A N   1 
ATOM   1234 C CA  . TYR   A 1 161 ? -9.84262  -10.11618 -3.10477  1.000 6.74916  ? 161 TYR   A CA  1 
ATOM   1235 C C   . TYR   A 1 161 ? -10.27301 -9.24260  -4.25832  1.000 8.96286  ? 161 TYR   A C   1 
ATOM   1236 O O   . TYR   A 1 161 ? -11.23902 -8.49021  -4.14650  1.000 9.75864  ? 161 TYR   A O   1 
ATOM   1237 C CB  . TYR   A 1 161 ? -10.73733 -11.34449 -3.06834  1.000 7.75648  ? 161 TYR   A CB  1 
ATOM   1238 C CG  . TYR   A 1 161 ? -10.78713 -12.15522 -4.34700  1.000 5.96526  ? 161 TYR   A CG  1 
ATOM   1239 C CD1 . TYR   A 1 161 ? -9.78029  -13.06442 -4.62421  1.000 9.22995  ? 161 TYR   A CD1 1 
ATOM   1240 C CD2 . TYR   A 1 161 ? -11.87276 -12.05598 -5.24094  1.000 6.08945  ? 161 TYR   A CD2 1 
ATOM   1241 C CE1 . TYR   A 1 161 ? -9.81976  -13.83097 -5.76037  1.000 8.79442  ? 161 TYR   A CE1 1 
ATOM   1242 C CE2 . TYR   A 1 161 ? -11.92820 -12.82709 -6.40043  1.000 7.27924  ? 161 TYR   A CE2 1 
ATOM   1243 C CZ  . TYR   A 1 161 ? -10.86255 -13.69554 -6.64441  1.000 6.40299  ? 161 TYR   A CZ  1 
ATOM   1244 O OH  . TYR   A 1 161 ? -10.89036 -14.47460 -7.75415  1.000 9.38991  ? 161 TYR   A OH  1 
ATOM   1245 N N   . MET   A 1 162 ? -9.54080  -9.33966  -5.35600  1.000 7.82575  ? 162 MET   A N   1 
ATOM   1246 C CA  . MET   A 1 162 ? -9.97952  -8.78009  -6.61743  1.000 7.07428  ? 162 MET   A CA  1 
ATOM   1247 C C   . MET   A 1 162 ? -9.96034  -9.89683  -7.64387  1.000 9.07508  ? 162 MET   A C   1 
ATOM   1248 O O   . MET   A 1 162 ? -8.95153  -10.60159 -7.77486  1.000 7.14516  ? 162 MET   A O   1 
ATOM   1249 C CB  . MET   A 1 162 ? -9.09160  -7.61373  -7.08369  1.000 9.66247  ? 162 MET   A CB  1 
ATOM   1250 C CG  . MET   A 1 162 ? -9.68841  -6.92637  -8.29581  1.000 10.40649 ? 162 MET   A CG  1 
ATOM   1251 S SD  . MET   A 1 162 ? -9.01092  -5.29795  -8.73762  1.000 15.01575 ? 162 MET   A SD  1 
ATOM   1252 C CE  . MET   A 1 162 ? -10.01158 -4.21514  -7.70398  1.000 17.79774 ? 162 MET   A CE  1 
ATOM   1253 N N   . HIS   A 1 163 ? -11.05438 -10.02570 -8.38173  1.000 10.31793 ? 163 HIS   A N   1 
ATOM   1254 C CA  . HIS   A 1 163 ? -11.18997 -11.09432 -9.36147  1.000 12.24384 ? 163 HIS   A CA  1 
ATOM   1255 C C   . HIS   A 1 163 ? -10.44400 -10.80815 -10.65662 1.000 9.47547  ? 163 HIS   A C   1 
ATOM   1256 O O   . HIS   A 1 163 ? -10.58748 -9.73372  -11.24672 1.000 10.09820 ? 163 HIS   A O   1 
ATOM   1257 C CB  . HIS   A 1 163 ? -12.64808 -11.33029 -9.71406  1.000 13.07664 ? 163 HIS   A CB  1 
ATOM   1258 C CG  . HIS   A 1 163 ? -12.82582 -12.56009 -10.52790 1.000 9.33744  ? 163 HIS   A CG  1 
ATOM   1259 N ND1 . HIS   A 1 163 ? -12.25941 -13.75827 -10.15429 1.000 10.74578 ? 163 HIS   A ND1 1 
ATOM   1260 C CD2 . HIS   A 1 163 ? -13.39066 -12.76304 -11.73684 1.000 13.66136 ? 163 HIS   A CD2 1 
ATOM   1261 C CE1 . HIS   A 1 163 ? -12.52828 -14.66649 -11.07360 1.000 11.19629 ? 163 HIS   A CE1 1 
ATOM   1262 N NE2 . HIS   A 1 163 ? -13.21376 -14.08981 -12.04232 1.000 11.55684 ? 163 HIS   A NE2 1 
ATOM   1263 N N   . HIS   A 1 164 ? -9.72224  -11.83224 -11.14857 1.000 13.38428 ? 164 HIS   A N   1 
ATOM   1264 C CA  . HIS   A 1 164 ? -8.96688  -11.75801 -12.38979 1.000 9.70512  ? 164 HIS   A CA  1 
ATOM   1265 C C   . HIS   A 1 164 ? -9.33285  -12.80039 -13.42900 1.000 13.11736 ? 164 HIS   A C   1 
ATOM   1266 O O   . HIS   A 1 164 ? -9.30184  -12.48020 -14.61044 1.000 12.29156 ? 164 HIS   A O   1 
ATOM   1267 C CB  . HIS   A 1 164 ? -7.45100  -11.87566 -12.11253 1.000 9.20846  ? 164 HIS   A CB  1 
ATOM   1268 C CG  . HIS   A 1 164 ? -6.86817  -10.65821 -11.46431 1.000 10.05691 ? 164 HIS   A CG  1 
ATOM   1269 N ND1 . HIS   A 1 164 ? -5.91113  -9.86720  -12.06775 1.000 11.02057 ? 164 HIS   A ND1 1 
ATOM   1270 C CD2 . HIS   A 1 164 ? -7.07937  -10.12565 -10.23716 1.000 11.19185 ? 164 HIS   A CD2 1 
ATOM   1271 C CE1 . HIS   A 1 164 ? -5.57617  -8.88676  -11.24594 1.000 11.16504 ? 164 HIS   A CE1 1 
ATOM   1272 N NE2 . HIS   A 1 164 ? -6.26256  -9.02782  -10.12567 1.000 11.40251 ? 164 HIS   A NE2 1 
ATOM   1273 N N   . MET   A 1 165 ? -9.65164  -14.04002 -13.04549 1.000 12.18099 ? 165 MET   A N   1 
ATOM   1274 C CA  . MET   A 1 165 ? -9.70930  -15.02901 -14.11791 1.000 12.83341 ? 165 MET   A CA  1 
ATOM   1275 C C   . MET   A 1 165 ? -10.36534 -16.31822 -13.62826 1.000 12.18430 ? 165 MET   A C   1 
ATOM   1276 O O   . MET   A 1 165 ? -10.49025 -16.56155 -12.42202 1.000 12.13341 ? 165 MET   A O   1 
ATOM   1277 C CB  . MET   A 1 165 ? -8.29126  -15.29797 -14.63917 1.000 13.43866 ? 165 MET   A CB  1 
ATOM   1278 C CG  . MET   A 1 165 ? -7.41962  -15.95178 -13.58615 1.000 14.71520 ? 165 MET   A CG  1 
ATOM   1279 S SD  . MET   A 1 165 ? -5.76443  -16.16758 -14.26163 1.000 25.14463 ? 165 MET   A SD  1 
ATOM   1280 C CE  . MET   A 1 165 ? -4.93506  -16.91372 -12.89108 1.000 21.20138 ? 165 MET   A CE  1 
ATOM   1281 N N   . GLU   A 1 166 ? -10.77594 -17.15317 -14.58603 1.000 14.92222 ? 166 GLU   A N   1 
ATOM   1282 C CA  . GLU   A 1 166 ? -11.36198 -18.45016 -14.28687 1.000 14.15122 ? 166 GLU   A CA  1 
ATOM   1283 C C   . GLU   A 1 166 ? -10.41188 -19.53791 -14.78124 1.000 16.34598 ? 166 GLU   A C   1 
ATOM   1284 O O   . GLU   A 1 166 ? -9.80486  -19.40641 -15.84840 1.000 17.83644 ? 166 GLU   A O   1 
ATOM   1285 C CB  . GLU   A 1 166 ? -12.76065 -18.57348 -14.91673 1.000 13.34718 ? 166 GLU   A CB  1 
ATOM   1286 C CG  . GLU   A 1 166 ? -13.28983 -20.00240 -14.90318 1.000 20.00084 ? 166 GLU   A CG  1 
ATOM   1287 C CD  . GLU   A 1 166 ? -14.75260 -20.06593 -15.27483 1.000 19.60182 ? 166 GLU   A CD  1 
ATOM   1288 O OE1 . GLU   A 1 166 ? -15.52835 -19.21486 -14.78945 1.000 18.98001 ? 166 GLU   A OE1 1 
ATOM   1289 O OE2 . GLU   A 1 166 ? -15.12546 -20.97333 -16.03176 1.000 22.75719 ? 166 GLU   A OE2 1 
ATOM   1290 N N   . LEU   A 1 167 ? -10.22077 -20.56227 -13.95872 1.000 17.30888 ? 167 LEU   A N   1 
ATOM   1291 C CA  . LEU   A 1 167 ? -9.33052  -21.67095 -14.27171 1.000 17.72034 ? 167 LEU   A CA  1 
ATOM   1292 C C   . LEU   A 1 167 ? -10.12023 -22.76144 -14.97001 1.000 18.87883 ? 167 LEU   A C   1 
ATOM   1293 O O   . LEU   A 1 167 ? -11.35059 -22.75489 -14.94132 1.000 22.82121 ? 167 LEU   A O   1 
ATOM   1294 C CB  . LEU   A 1 167 ? -8.68760  -22.17612 -12.98323 1.000 18.08631 ? 167 LEU   A CB  1 
ATOM   1295 C CG  . LEU   A 1 167 ? -7.75556  -21.19230 -12.26088 1.000 14.02944 ? 167 LEU   A CG  1 
ATOM   1296 C CD1 . LEU   A 1 167 ? -7.38347  -21.74833 -10.91288 1.000 17.53720 ? 167 LEU   A CD1 1 
ATOM   1297 C CD2 . LEU   A 1 167 ? -6.49407  -20.97350 -13.08779 1.000 17.51109 ? 167 LEU   A CD2 1 
ATOM   1298 N N   . PRO   A 1 168 ? -9.44769  -23.73072 -15.59758 1.000 20.25434 ? 168 PRO   A N   1 
ATOM   1299 C CA  . PRO   A 1 168 ? -10.17640 -24.69503 -16.43926 1.000 20.95253 ? 168 PRO   A CA  1 
ATOM   1300 C C   . PRO   A 1 168 ? -11.18552 -25.55927 -15.69673 1.000 22.92693 ? 168 PRO   A C   1 
ATOM   1301 O O   . PRO   A 1 168 ? -12.10281 -26.07420 -16.34657 1.000 24.91514 ? 168 PRO   A O   1 
ATOM   1302 C CB  . PRO   A 1 168 ? -9.05566  -25.54663 -17.05267 1.000 20.33860 ? 168 PRO   A CB  1 
ATOM   1303 C CG  . PRO   A 1 168 ? -7.84727  -24.68246 -16.98562 1.000 23.52511 ? 168 PRO   A CG  1 
ATOM   1304 C CD  . PRO   A 1 168 ? -7.98582  -23.89266 -15.72853 1.000 20.59889 ? 168 PRO   A CD  1 
ATOM   1305 N N   . THR   A 1 169 ? -11.05857 -25.75456 -14.38205 1.000 15.90446 ? 169 THR   A N   1 
ATOM   1306 C CA  . THR   A 1 169 ? -12.09034 -26.49695 -13.66588 1.000 19.04780 ? 169 THR   A CA  1 
ATOM   1307 C C   . THR   A 1 169 ? -13.29661 -25.63239 -13.32505 1.000 19.02235 ? 169 THR   A C   1 
ATOM   1308 O O   . THR   A 1 169 ? -14.21024 -26.11057 -12.64701 1.000 21.72163 ? 169 THR   A O   1 
ATOM   1309 C CB  . THR   A 1 169 ? -11.53776 -27.11573 -12.37428 1.000 17.51642 ? 169 THR   A CB  1 
ATOM   1310 O OG1 . THR   A 1 169 ? -10.77076 -26.13660 -11.66502 1.000 18.85839 ? 169 THR   A OG1 1 
ATOM   1311 C CG2 . THR   A 1 169 ? -10.64938 -28.30262 -12.69267 1.000 18.40627 ? 169 THR   A CG2 1 
ATOM   1312 N N   . GLY   A 1 170 ? -13.32300 -24.38132 -13.76563 1.000 17.90866 ? 170 GLY   A N   1 
ATOM   1313 C CA  . GLY   A 1 170 ? -14.43099 -23.51560 -13.43826 1.000 16.77821 ? 170 GLY   A CA  1 
ATOM   1314 C C   . GLY   A 1 170 ? -14.31072 -22.78669 -12.12192 1.000 20.02249 ? 170 GLY   A C   1 
ATOM   1315 O O   . GLY   A 1 170 ? -15.26768 -22.11224 -11.72647 1.000 18.89756 ? 170 GLY   A O   1 
ATOM   1316 N N   . VAL   A 1 171 ? -13.16923 -22.89087 -11.43072 1.000 15.56375 ? 171 VAL   A N   1 
ATOM   1317 C CA  . VAL   A 1 171 ? -12.92928 -22.12441 -10.21442 1.000 12.16299 ? 171 VAL   A CA  1 
ATOM   1318 C C   . VAL   A 1 171 ? -12.15706 -20.86353 -10.56775 1.000 12.46927 ? 171 VAL   A C   1 
ATOM   1319 O O   . VAL   A 1 171 ? -11.73182 -20.67777 -11.71304 1.000 14.50714 ? 171 VAL   A O   1 
ATOM   1320 C CB  . VAL   A 1 171 ? -12.18066 -22.94428 -9.14640  1.000 14.51758 ? 171 VAL   A CB  1 
ATOM   1321 C CG1 . VAL   A 1 171 ? -12.98407 -24.19561 -8.77721  1.000 14.56126 ? 171 VAL   A CG1 1 
ATOM   1322 C CG2 . VAL   A 1 171 ? -10.79519 -23.31569 -9.61495  1.000 14.19170 ? 171 VAL   A CG2 1 
ATOM   1323 N N   . HIS   A 1 172 ? -11.95879 -19.99325 -9.59034  1.000 10.44608 ? 172 HIS   A N   1 
ATOM   1324 C CA  . HIS   A 1 172 ? -11.59761 -18.62118 -9.89398  1.000 10.29310 ? 172 HIS   A CA  1 
ATOM   1325 C C   . HIS   A 1 172 ? -10.33660 -18.23342 -9.14662  1.000 10.18114 ? 172 HIS   A C   1 
ATOM   1326 O O   . HIS   A 1 172 ? -10.06609 -18.71761 -8.04128  1.000 8.88377  ? 172 HIS   A O   1 
ATOM   1327 C CB  . HIS   A 1 172 ? -12.78300 -17.72226 -9.56135  1.000 13.07443 ? 172 HIS   A CB  1 
ATOM   1328 C CG  . HIS   A 1 172 ? -13.99463 -18.06790 -10.37281 1.000 12.67546 ? 172 HIS   A CG  1 
ATOM   1329 N ND1 . HIS   A 1 172 ? -15.08690 -18.71827 -9.83742  1.000 11.75711 ? 172 HIS   A ND1 1 
ATOM   1330 C CD2 . HIS   A 1 172 ? -14.25847 -17.91576 -11.69220 1.000 13.40159 ? 172 HIS   A CD2 1 
ATOM   1331 C CE1 . HIS   A 1 172 ? -15.98619 -18.92254 -10.78363 1.000 14.93730 ? 172 HIS   A CE1 1 
ATOM   1332 N NE2 . HIS   A 1 172 ? -15.51003 -18.44418 -11.92149 1.000 11.77887 ? 172 HIS   A NE2 1 
ATOM   1333 N N   . ALA   A 1 173 ? -9.56723  -17.36034 -9.76881  1.000 10.85676 ? 173 ALA   A N   1 
ATOM   1334 C CA  . ALA   A 1 173 ? -8.29306  -16.93811 -9.22092  1.000 8.24069  ? 173 ALA   A CA  1 
ATOM   1335 C C   . ALA   A 1 173 ? -8.19651  -15.42702 -9.30438  1.000 9.99686  ? 173 ALA   A C   1 
ATOM   1336 O O   . ALA   A 1 173 ? -8.71335  -14.81307 -10.24797 1.000 9.14741  ? 173 ALA   A O   1 
ATOM   1337 C CB  . ALA   A 1 173 ? -7.13386  -17.60666 -9.96954  1.000 11.34487 ? 173 ALA   A CB  1 
ATOM   1338 N N   . GLY   A 1 174 ? -7.56170  -14.83027 -8.30579  1.000 8.65430  ? 174 GLY   A N   1 
ATOM   1339 C CA  . GLY   A 1 174 ? -7.38469  -13.39617 -8.30504  1.000 8.48203  ? 174 GLY   A CA  1 
ATOM   1340 C C   . GLY   A 1 174 ? -6.32965  -12.97540 -7.32421  1.000 8.55587  ? 174 GLY   A C   1 
ATOM   1341 O O   . GLY   A 1 174 ? -5.54324  -13.79038 -6.83578  1.000 8.31174  ? 174 GLY   A O   1 
ATOM   1342 N N   . THR   A 1 175 ? -6.34110  -11.68972 -6.99161  1.000 8.54855  ? 175 THR   A N   1 
ATOM   1343 C CA  . THR   A 1 175 ? -5.29212  -11.10390 -6.18065  1.000 7.79378  ? 175 THR   A CA  1 
ATOM   1344 C C   . THR   A 1 175 ? -5.87086  -10.50458 -4.91039  1.000 8.27837  ? 175 THR   A C   1 
ATOM   1345 O O   . THR   A 1 175 ? -7.08653  -10.31304 -4.77622  1.000 8.21126  ? 175 THR   A O   1 
ATOM   1346 C CB  . THR   A 1 175 ? -4.55810  -9.99483  -6.95006  1.000 10.07584 ? 175 THR   A CB  1 
ATOM   1347 O OG1 . THR   A 1 175 ? -5.47499  -8.90399  -7.16676  1.000 9.34387  ? 175 THR   A OG1 1 
ATOM   1348 C CG2 . THR   A 1 175 ? -4.09654  -10.51060 -8.27832  1.000 9.10505  ? 175 THR   A CG2 1 
ATOM   1349 N N   . ASP   A 1 176 ? -4.97208  -10.14428 -4.00405  1.000 10.35254 ? 176 ASP   A N   1 
ATOM   1350 C CA  . ASP   A 1 176 ? -5.36345  -9.21711  -2.95789  1.000 8.26064  ? 176 ASP   A CA  1 
ATOM   1351 C C   . ASP   A 1 176 ? -5.36433  -7.81477  -3.57212  1.000 8.54141  ? 176 ASP   A C   1 
ATOM   1352 O O   . ASP   A 1 176 ? -5.08056  -7.63736  -4.75606  1.000 9.30179  ? 176 ASP   A O   1 
ATOM   1353 C CB  . ASP   A 1 176 ? -4.47352  -9.39165  -1.72239  1.000 10.08335 ? 176 ASP   A CB  1 
ATOM   1354 C CG  . ASP   A 1 176 ? -3.01408  -9.04205  -1.96096  1.000 11.89400 ? 176 ASP   A CG  1 
ATOM   1355 O OD1 . ASP   A 1 176 ? -2.70296  -8.21569  -2.83198  1.000 10.31733 ? 176 ASP   A OD1 1 
ATOM   1356 O OD2 . ASP   A 1 176 ? -2.16319  -9.59549  -1.22476  1.000 13.31489 ? 176 ASP   A OD2 1 
ATOM   1357 N N   . LEU   A 1 177 ? -5.72588  -6.81401  -2.78754  1.000 9.68107  ? 177 LEU   A N   1 
ATOM   1358 C CA  . LEU   A 1 177 ? -5.85042  -5.46809  -3.33466  1.000 8.65045  ? 177 LEU   A CA  1 
ATOM   1359 C C   . LEU   A 1 177 ? -4.50503  -4.77154  -3.47013  1.000 12.05505 ? 177 LEU   A C   1 
ATOM   1360 O O   . LEU   A 1 177 ? -4.45385  -3.63292  -3.95261  1.000 12.96521 ? 177 LEU   A O   1 
ATOM   1361 C CB  . LEU   A 1 177 ? -6.83082  -4.63081  -2.49585  1.000 8.82011  ? 177 LEU   A CB  1 
ATOM   1362 C CG  . LEU   A 1 177 ? -8.31085  -4.71258  -2.92091  1.000 9.95454  ? 177 LEU   A CG  1 
ATOM   1363 C CD1 . LEU   A 1 177 ? -8.44318  -4.10070  -4.30539  1.000 9.93708  ? 177 LEU   A CD1 1 
ATOM   1364 C CD2 . LEU   A 1 177 ? -8.77955  -6.16044  -2.97619  1.000 10.90142 ? 177 LEU   A CD2 1 
ATOM   1365 N N   . GLU   A 1 178 ? -3.42826  -5.41723  -3.04615  1.000 10.48484 ? 178 GLU   A N   1 
ATOM   1366 C CA  . GLU   A 1 178 ? -2.09753  -4.97801  -3.44128  1.000 12.47582 ? 178 GLU   A CA  1 
ATOM   1367 C C   . GLU   A 1 178 ? -1.66658  -5.56489  -4.78074  1.000 12.85636 ? 178 GLU   A C   1 
ATOM   1368 O O   . GLU   A 1 178 ? -0.55765  -5.27376  -5.22470  1.000 13.45894 ? 178 GLU   A O   1 
ATOM   1369 C CB  . GLU   A 1 178 ? -1.07282  -5.35133  -2.36276  1.000 10.94737 ? 178 GLU   A CB  1 
ATOM   1370 N N   . GLY   A 1 179 ? -2.50301  -6.37528  -5.42933  1.000 10.48895 ? 179 GLY   A N   1 
ATOM   1371 C CA  . GLY   A 1 179 ? -2.18999  -6.95322  -6.72194  1.000 10.10349 ? 179 GLY   A CA  1 
ATOM   1372 C C   . GLY   A 1 179 ? -1.35606  -8.21444  -6.68555  1.000 11.76306 ? 179 GLY   A C   1 
ATOM   1373 O O   . GLY   A 1 179 ? -0.80073  -8.61041  -7.72957  1.000 10.83887 ? 179 GLY   A O   1 
ATOM   1374 N N   . ASN   A 1 180 ? -1.24245  -8.85521  -5.52372  1.000 10.37082 ? 180 ASN   A N   1 
ATOM   1375 C CA  . ASN   A 1 180 ? -0.45389  -10.07302 -5.38223  1.000 9.54063  ? 180 ASN   A CA  1 
ATOM   1376 C C   . ASN   A 1 180 ? -1.40233  -11.24833 -5.47832  1.000 9.80246  ? 180 ASN   A C   1 
ATOM   1377 O O   . ASN   A 1 180 ? -2.38480  -11.29601 -4.74156  1.000 8.22561  ? 180 ASN   A O   1 
ATOM   1378 C CB  . ASN   A 1 180 ? 0.29175   -10.06919 -4.04368  1.000 9.85004  ? 180 ASN   A CB  1 
ATOM   1379 C CG  . ASN   A 1 180 ? 1.17047   -8.86240  -3.90068  1.000 13.41943 ? 180 ASN   A CG  1 
ATOM   1380 O OD1 . ASN   A 1 180 ? 0.94971   -7.99096  -3.03170  1.000 16.47103 ? 180 ASN   A OD1 1 
ATOM   1381 N ND2 . ASN   A 1 180 ? 2.16570   -8.78101  -4.75324  1.000 11.25555 ? 180 ASN   A ND2 1 
ATOM   1382 N N   . PHE   A 1 181 ? -1.14384  -12.16554 -6.41008  1.000 8.99621  ? 181 PHE   A N   1 
ATOM   1383 C CA  . PHE   A 1 181 ? -2.07916  -13.25734 -6.61232  1.000 10.26973 ? 181 PHE   A CA  1 
ATOM   1384 C C   . PHE   A 1 181 ? -2.18656  -14.13364 -5.38198  1.000 9.11580  ? 181 PHE   A C   1 
ATOM   1385 O O   . PHE   A 1 181 ? -1.20928  -14.37195 -4.66836  1.000 8.62183  ? 181 PHE   A O   1 
ATOM   1386 C CB  . PHE   A 1 181 ? -1.69089  -14.12594 -7.81426  1.000 9.15535  ? 181 PHE   A CB  1 
ATOM   1387 C CG  . PHE   A 1 181 ? -2.41678  -13.76790 -9.05630  1.000 9.69609  ? 181 PHE   A CG  1 
ATOM   1388 C CD1 . PHE   A 1 181 ? -3.66782  -14.33463 -9.30420  1.000 12.34291 ? 181 PHE   A CD1 1 
ATOM   1389 C CD2 . PHE   A 1 181 ? -1.90050  -12.85448 -9.95734  1.000 9.82669  ? 181 PHE   A CD2 1 
ATOM   1390 C CE1 . PHE   A 1 181 ? -4.36910  -14.02064 -10.44299 1.000 10.78948 ? 181 PHE   A CE1 1 
ATOM   1391 C CE2 . PHE   A 1 181 ? -2.59940  -12.54119 -11.11646 1.000 12.22424 ? 181 PHE   A CE2 1 
ATOM   1392 C CZ  . PHE   A 1 181 ? -3.84419  -13.12179 -11.34741 1.000 13.23207 ? 181 PHE   A CZ  1 
ATOM   1393 N N   . TYR   A 1 182 ? -3.39644  -14.62358 -5.15292  1.000 8.17742  ? 182 TYR   A N   1 
ATOM   1394 C CA  . TYR   A 1 182 ? -3.56339  -15.75979 -4.27466  1.000 7.59876  ? 182 TYR   A CA  1 
ATOM   1395 C C   . TYR   A 1 182 ? -3.16500  -17.00747 -5.03983  1.000 8.67847  ? 182 TYR   A C   1 
ATOM   1396 O O   . TYR   A 1 182 ? -3.74681  -17.30888 -6.08917  1.000 10.20076 ? 182 TYR   A O   1 
ATOM   1397 C CB  . TYR   A 1 182 ? -5.00133  -15.84883 -3.78229  1.000 6.99501  ? 182 TYR   A CB  1 
ATOM   1398 C CG  . TYR   A 1 182 ? -5.36214  -14.78595 -2.77886  1.000 6.68015  ? 182 TYR   A CG  1 
ATOM   1399 C CD1 . TYR   A 1 182 ? -4.99579  -14.93816 -1.44255  1.000 9.18862  ? 182 TYR   A CD1 1 
ATOM   1400 C CD2 . TYR   A 1 182 ? -6.11918  -13.68071 -3.13664  1.000 8.96106  ? 182 TYR   A CD2 1 
ATOM   1401 C CE1 . TYR   A 1 182 ? -5.34840  -14.00510 -0.50253  1.000 7.81859  ? 182 TYR   A CE1 1 
ATOM   1402 C CE2 . TYR   A 1 182 ? -6.49934  -12.73000 -2.18960  1.000 7.97631  ? 182 TYR   A CE2 1 
ATOM   1403 C CZ  . TYR   A 1 182 ? -6.10224  -12.90172 -0.87905  1.000 8.03459  ? 182 TYR   A CZ  1 
ATOM   1404 O OH  . TYR   A 1 182 ? -6.44121  -11.98596 0.09137   1.000 8.65746  ? 182 TYR   A OH  1 
ATOM   1405 N N   . GLY   A 1 183 ? -2.13772  -17.68985 -4.55129  1.000 9.81736  ? 183 GLY   A N   1 
ATOM   1406 C CA  . GLY   A 1 183 ? -1.72323  -18.95021 -5.11726  1.000 9.70759  ? 183 GLY   A CA  1 
ATOM   1407 C C   . GLY   A 1 183 ? -0.82063  -18.79914 -6.31750  1.000 10.49399 ? 183 GLY   A C   1 
ATOM   1408 O O   . GLY   A 1 183 ? -0.44610  -17.69329 -6.71189  1.000 10.00354 ? 183 GLY   A O   1 
ATOM   1409 N N   . PRO   A 1 184 ? -0.47349  -19.91555 -6.92355  1.000 10.74687 ? 184 PRO   A N   1 
ATOM   1410 C CA  . PRO   A 1 184 ? 0.56449   -19.94382 -7.97100  1.000 11.90286 ? 184 PRO   A CA  1 
ATOM   1411 C C   . PRO   A 1 184 ? -0.03123  -19.69403 -9.35306  1.000 15.76137 ? 184 PRO   A C   1 
ATOM   1412 O O   . PRO   A 1 184 ? 0.03944   -20.53581 -10.25250 1.000 16.94892 ? 184 PRO   A O   1 
ATOM   1413 C CB  . PRO   A 1 184 ? 1.10857   -21.36905 -7.85123  1.000 16.44503 ? 184 PRO   A CB  1 
ATOM   1414 C CG  . PRO   A 1 184 ? -0.10148  -22.15791 -7.41212  1.000 13.98776 ? 184 PRO   A CG  1 
ATOM   1415 C CD  . PRO   A 1 184 ? -0.94573  -21.26127 -6.56230  1.000 11.77788 ? 184 PRO   A CD  1 
ATOM   1416 N N   . PHE   A 1 185 ? -0.64804  -18.54414 -9.51272  1.000 12.02100 ? 185 PHE   A N   1 
ATOM   1417 C CA  . PHE   A 1 185 ? -1.33192  -18.18700 -10.74821 1.000 12.53641 ? 185 PHE   A CA  1 
ATOM   1418 C C   . PHE   A 1 185 ? -0.79493  -16.85968 -11.24375 1.000 15.74231 ? 185 PHE   A C   1 
ATOM   1419 O O   . PHE   A 1 185 ? -0.30131  -16.04345 -10.45939 1.000 13.63198 ? 185 PHE   A O   1 
ATOM   1420 C CB  . PHE   A 1 185 ? -2.84624  -18.12438 -10.53510 1.000 13.03538 ? 185 PHE   A CB  1 
ATOM   1421 C CG  . PHE   A 1 185 ? -3.38518  -19.35590 -9.91691  1.000 12.47139 ? 185 PHE   A CG  1 
ATOM   1422 C CD1 . PHE   A 1 185 ? -3.29285  -20.55665 -10.58591 1.000 11.69272 ? 185 PHE   A CD1 1 
ATOM   1423 C CD2 . PHE   A 1 185 ? -3.96454  -19.33157 -8.66463  1.000 13.80805 ? 185 PHE   A CD2 1 
ATOM   1424 C CE1 . PHE   A 1 185 ? -3.76395  -21.71535 -10.01300 1.000 14.61787 ? 185 PHE   A CE1 1 
ATOM   1425 C CE2 . PHE   A 1 185 ? -4.43288  -20.48343 -8.10003  1.000 12.93547 ? 185 PHE   A CE2 1 
ATOM   1426 C CZ  . PHE   A 1 185 ? -4.32432  -21.68712 -8.78553  1.000 11.93103 ? 185 PHE   A CZ  1 
ATOM   1427 N N   . VAL   A 1 186 ? -0.87134  -16.66476 -12.55724 1.000 15.70147 ? 186 VAL   A N   1 
ATOM   1428 C CA  . VAL   A 1 186 ? -0.28638  -15.50267 -13.21009 1.000 15.90714 ? 186 VAL   A CA  1 
ATOM   1429 C C   . VAL   A 1 186 ? -1.29635  -14.93436 -14.19325 1.000 16.73136 ? 186 VAL   A C   1 
ATOM   1430 O O   . VAL   A 1 186 ? -2.17257  -15.64504 -14.69625 1.000 17.42289 ? 186 VAL   A O   1 
ATOM   1431 C CB  . VAL   A 1 186 ? 1.03696   -15.85304 -13.92314 1.000 19.52093 ? 186 VAL   A CB  1 
ATOM   1432 C CG1 . VAL   A 1 186 ? 2.11854   -16.19575 -12.88805 1.000 21.75236 ? 186 VAL   A CG1 1 
ATOM   1433 C CG2 . VAL   A 1 186 ? 0.82907   -17.01884 -14.86149 1.000 16.73031 ? 186 VAL   A CG2 1 
ATOM   1434 N N   . ASP   A 1 187 ? -1.18155  -13.63977 -14.46113 1.000 16.87699 ? 187 ASP   A N   1 
ATOM   1435 C CA  . ASP   A 1 187 ? -2.08901  -12.99728 -15.41015 1.000 20.84277 ? 187 ASP   A CA  1 
ATOM   1436 C C   . ASP   A 1 187 ? -1.45045  -12.96160 -16.79833 1.000 20.52595 ? 187 ASP   A C   1 
ATOM   1437 O O   . ASP   A 1 187 ? -1.26577  -11.92710 -17.43982 1.000 18.32438 ? 187 ASP   A O   1 
ATOM   1438 C CB  . ASP   A 1 187 ? -2.51817  -11.61949 -14.89413 1.000 16.74706 ? 187 ASP   A CB  1 
ATOM   1439 C CG  . ASP   A 1 187 ? -1.35631  -10.70335 -14.55830 1.000 19.04471 ? 187 ASP   A CG  1 
ATOM   1440 O OD1 . ASP   A 1 187 ? -0.17916  -11.12667 -14.61494 1.000 16.18777 ? 187 ASP   A OD1 1 
ATOM   1441 O OD2 . ASP   A 1 187 ? -1.65385  -9.55176  -14.15781 1.000 16.83114 ? 187 ASP   A OD2 1 
ATOM   1442 N N   . ARG   A 1 188 ? -1.08031  -14.16108 -17.24477 1.000 22.26583 ? 188 ARG   A N   1 
ATOM   1443 C CA  . ARG   A 1 188 ? -0.67737  -14.40728 -18.61698 1.000 22.73106 ? 188 ARG   A CA  1 
ATOM   1444 C C   . ARG   A 1 188 ? -1.19720  -15.78353 -19.00463 1.000 24.99954 ? 188 ARG   A C   1 
ATOM   1445 O O   . ARG   A 1 188 ? -1.50805  -16.61088 -18.13762 1.000 24.49008 ? 188 ARG   A O   1 
ATOM   1446 C CB  . ARG   A 1 188 ? 0.84597   -14.32905 -18.80557 1.000 24.57578 ? 188 ARG   A CB  1 
ATOM   1447 C CG  . ARG   A 1 188 ? 1.62508   -15.27886 -17.92042 1.000 25.17537 ? 188 ARG   A CG  1 
ATOM   1448 C CD  . ARG   A 1 188 ? 3.12805   -15.14747 -18.11756 1.000 26.97874 ? 188 ARG   A CD  1 
ATOM   1449 N NE  . ARG   A 1 188 ? 3.81004   -15.85588 -17.04379 1.000 26.20145 ? 188 ARG   A NE  1 
ATOM   1450 C CZ  . ARG   A 1 188 ? 4.13694   -17.14180 -17.10638 1.000 28.96238 ? 188 ARG   A CZ  1 
ATOM   1451 N NH1 . ARG   A 1 188 ? 3.85752   -17.83953 -18.20567 1.000 30.22277 ? 188 ARG   A NH1 1 
ATOM   1452 N NH2 . ARG   A 1 188 ? 4.73675   -17.73225 -16.07386 1.000 28.30605 ? 188 ARG   A NH2 1 
ATOM   1453 N N   . GLN   A 1 189 ? -1.30334  -16.02049 -20.31505 1.000 28.17982 ? 189 GLN   A N   1 
ATOM   1454 C CA  . GLN   A 1 189 ? -1.97717  -17.21349 -20.82414 1.000 30.44532 ? 189 GLN   A CA  1 
ATOM   1455 C C   . GLN   A 1 189 ? -1.06458  -18.42527 -20.69187 1.000 26.72475 ? 189 GLN   A C   1 
ATOM   1456 O O   . GLN   A 1 189 ? -0.01163  -18.50408 -21.33867 1.000 26.52002 ? 189 GLN   A O   1 
ATOM   1457 C CB  . GLN   A 1 189 ? -2.40962  -17.03149 -22.27383 1.000 34.21184 ? 189 GLN   A CB  1 
ATOM   1458 C CG  . GLN   A 1 189 ? -3.01553  -18.28123 -22.87605 1.000 33.12380 ? 189 GLN   A CG  1 
ATOM   1459 C CD  . GLN   A 1 189 ? -4.29341  -18.67208 -22.16014 1.000 33.14280 ? 189 GLN   A CD  1 
ATOM   1460 O OE1 . GLN   A 1 189 ? -5.21934  -17.86685 -22.02063 1.000 37.62530 ? 189 GLN   A OE1 1 
ATOM   1461 N NE2 . GLN   A 1 189 ? -4.35006  -19.91400 -21.69240 1.000 34.53228 ? 189 GLN   A NE2 1 
ATOM   1462 N N   . THR   A 1 190 ? -1.47764  -19.36909 -19.85029 1.000 25.40073 ? 190 THR   A N   1 
ATOM   1463 C CA  . THR   A 1 190 ? -0.79543  -20.63590 -19.64332 1.000 24.79213 ? 190 THR   A CA  1 
ATOM   1464 C C   . THR   A 1 190 ? -1.85054  -21.69660 -19.39381 1.000 27.08287 ? 190 THR   A C   1 
ATOM   1465 O O   . THR   A 1 190 ? -3.03821  -21.39905 -19.24899 1.000 24.46502 ? 190 THR   A O   1 
ATOM   1466 C CB  . THR   A 1 190 ? 0.15430   -20.60160 -18.44160 1.000 25.73038 ? 190 THR   A CB  1 
ATOM   1467 O OG1 . THR   A 1 190 ? -0.62408  -20.55512 -17.24356 1.000 21.68235 ? 190 THR   A OG1 1 
ATOM   1468 C CG2 . THR   A 1 190 ? 1.06548   -19.38396 -18.48844 1.000 26.92296 ? 190 THR   A CG2 1 
ATOM   1469 N N   . ALA   A 1 191 ? -1.40012  -22.94408 -19.30533 1.000 28.03949 ? 191 ALA   A N   1 
ATOM   1470 C CA  . ALA   A 1 191 ? -2.29941  -24.03440 -18.95550 1.000 25.41979 ? 191 ALA   A CA  1 
ATOM   1471 C C   . ALA   A 1 191 ? -2.43858  -24.17798 -17.44207 1.000 26.00515 ? 191 ALA   A C   1 
ATOM   1472 O O   . ALA   A 1 191 ? -2.70004  -25.28075 -16.95191 1.000 27.68825 ? 191 ALA   A O   1 
ATOM   1473 C CB  . ALA   A 1 191 ? -1.79890  -25.34322 -19.58070 1.000 28.35498 ? 191 ALA   A CB  1 
ATOM   1474 N N   . GLN   A 1 192 ? -2.28245  -23.08128 -16.69466 1.000 23.30810 ? 192 GLN   A N   1 
ATOM   1475 C CA  . GLN   A 1 192 ? -2.33172  -23.16231 -15.23804 1.000 21.29857 ? 192 GLN   A CA  1 
ATOM   1476 C C   . GLN   A 1 192 ? -3.65451  -23.75986 -14.77857 1.000 27.31557 ? 192 GLN   A C   1 
ATOM   1477 O O   . GLN   A 1 192 ? -4.71427  -23.49744 -15.36072 1.000 26.31077 ? 192 GLN   A O   1 
ATOM   1478 C CB  . GLN   A 1 192 ? -2.14624  -21.78303 -14.58679 1.000 18.78228 ? 192 GLN   A CB  1 
ATOM   1479 C CG  . GLN   A 1 192 ? -3.05972  -20.68810 -15.09992 1.000 22.45719 ? 192 GLN   A CG  1 
ATOM   1480 C CD  . GLN   A 1 192 ? -2.57533  -19.28883 -14.73278 1.000 19.11811 ? 192 GLN   A CD  1 
ATOM   1481 O OE1 . GLN   A 1 192 ? -1.86006  -19.09723 -13.74045 1.000 19.01198 ? 192 GLN   A OE1 1 
ATOM   1482 N NE2 . GLN   A 1 192 ? -2.96886  -18.30396 -15.53038 1.000 20.08343 ? 192 GLN   A NE2 1 
ATOM   1483 N N   . ALA   A 1 193 ? -3.58452  -24.55873 -13.71569 1.000 23.43647 ? 193 ALA   A N   1 
ATOM   1484 C CA  . ALA   A 1 193 ? -4.74556  -25.24367 -13.17884 1.000 21.92812 ? 193 ALA   A CA  1 
ATOM   1485 C C   . ALA   A 1 193 ? -4.68197  -25.20654 -11.65888 1.000 20.35083 ? 193 ALA   A C   1 
ATOM   1486 O O   . ALA   A 1 193 ? -3.61894  -25.02598 -11.06501 1.000 21.03427 ? 193 ALA   A O   1 
ATOM   1487 C CB  . ALA   A 1 193 ? -4.83574  -26.69552 -13.66954 1.000 22.38131 ? 193 ALA   A CB  1 
ATOM   1488 N N   . ALA   A 1 194 ? -5.84399  -25.40950 -11.04042 1.000 19.49792 ? 194 ALA   A N   1 
ATOM   1489 C CA  . ALA   A 1 194 ? -5.96937  -25.27446 -9.59231  1.000 20.87483 ? 194 ALA   A CA  1 
ATOM   1490 C C   . ALA   A 1 194 ? -4.93985  -26.10766 -8.83150  1.000 24.38590 ? 194 ALA   A C   1 
ATOM   1491 O O   . ALA   A 1 194 ? -4.24847  -25.60165 -7.94124  1.000 30.14415 ? 194 ALA   A O   1 
ATOM   1492 C CB  . ALA   A 1 194 ? -7.38250  -25.66447 -9.16962  1.000 19.14368 ? 194 ALA   A CB  1 
ATOM   1493 N N   . GLY   A 1 195 ? -4.83263  -27.38583 -9.14063  1.000 25.62470 ? 195 GLY   A N   1 
ATOM   1494 C CA  . GLY   A 1 195 ? -4.04196  -28.23723 -8.27657  1.000 29.35721 ? 195 GLY   A CA  1 
ATOM   1495 C C   . GLY   A 1 195 ? -4.82874  -28.71612 -7.06644  1.000 28.55282 ? 195 GLY   A C   1 
ATOM   1496 O O   . GLY   A 1 195 ? -5.91092  -28.22347 -6.75018  1.000 24.43413 ? 195 GLY   A O   1 
ATOM   1497 N N   . THR   A 1 196 ? -4.26832  -29.71319 -6.38206  1.000 24.48160 ? 196 THR   A N   1 
ATOM   1498 C CA  . THR   A 1 196 ? -5.06759  -30.50334 -5.45532  1.000 25.91356 ? 196 THR   A CA  1 
ATOM   1499 C C   . THR   A 1 196 ? -5.53428  -29.67244 -4.26084  1.000 21.73774 ? 196 THR   A C   1 
ATOM   1500 O O   . THR   A 1 196 ? -4.80509  -28.82096 -3.73996  1.000 22.68724 ? 196 THR   A O   1 
ATOM   1501 C CB  . THR   A 1 196 ? -4.27220  -31.71591 -4.98655  1.000 27.60860 ? 196 THR   A CB  1 
ATOM   1502 O OG1 . THR   A 1 196 ? -3.09252  -31.26503 -4.31570  1.000 33.46285 ? 196 THR   A OG1 1 
ATOM   1503 C CG2 . THR   A 1 196 ? -3.86094  -32.57174 -6.19691  1.000 26.27918 ? 196 THR   A CG2 1 
ATOM   1504 N N   . ASP   A 1 197 ? -6.77681  -29.90424 -3.85204  1.000 19.02955 ? 197 ASP   A N   1 
ATOM   1505 C CA  . ASP   A 1 197 ? -7.39572  -29.22430 -2.72481  1.000 18.94986 ? 197 ASP   A CA  1 
ATOM   1506 C C   . ASP   A 1 197 ? -7.51474  -30.18835 -1.54193  1.000 19.51063 ? 197 ASP   A C   1 
ATOM   1507 O O   . ASP   A 1 197 ? -7.27888  -31.38938 -1.66957  1.000 19.97837 ? 197 ASP   A O   1 
ATOM   1508 C CB  . ASP   A 1 197 ? -8.78170  -28.69721 -3.10689  1.000 14.49124 ? 197 ASP   A CB  1 
ATOM   1509 C CG  . ASP   A 1 197 ? -9.17655  -27.45967 -2.31614  1.000 16.58037 ? 197 ASP   A CG  1 
ATOM   1510 O OD1 . ASP   A 1 197 ? -10.37996 -27.09723 -2.33460  1.000 16.80268 ? 197 ASP   A OD1 1 
ATOM   1511 O OD2 . ASP   A 1 197 ? -8.27525  -26.81104 -1.72567  1.000 17.42655 ? 197 ASP   A OD2 1 
ATOM   1512 N N   . THR   A 1 198 ? -7.89140  -29.64490 -0.38168  1.000 17.12491 ? 198 THR   A N   1 
ATOM   1513 C CA  . THR   A 1 198 ? -8.18923  -30.43516 0.80567   1.000 15.18872 ? 198 THR   A CA  1 
ATOM   1514 C C   . THR   A 1 198 ? -9.41731  -29.83180 1.46531   1.000 15.32271 ? 198 THR   A C   1 
ATOM   1515 O O   . THR   A 1 198 ? -9.85227  -28.73524 1.11079   1.000 15.89054 ? 198 THR   A O   1 
ATOM   1516 C CB  . THR   A 1 198 ? -7.02336  -30.46829 1.81548   1.000 19.55076 ? 198 THR   A CB  1 
ATOM   1517 O OG1 . THR   A 1 198 ? -6.59794  -29.13084 2.11979   1.000 19.88939 ? 198 THR   A OG1 1 
ATOM   1518 C CG2 . THR   A 1 198 ? -5.84664  -31.17896 1.21987   1.000 23.95021 ? 198 THR   A CG2 1 
ATOM   1519 N N   . THR   A 1 199 ? -9.99235  -30.55969 2.41982   1.000 15.84811 ? 199 THR   A N   1 
ATOM   1520 C CA  . THR   A 1 199 ? -11.15704 -30.05132 3.13004   1.000 16.98056 ? 199 THR   A CA  1 
ATOM   1521 C C   . THR   A 1 199 ? -10.70436 -29.31469 4.38202   1.000 14.60551 ? 199 THR   A C   1 
ATOM   1522 O O   . THR   A 1 199 ? -9.77016  -29.74132 5.07005   1.000 14.78558 ? 199 THR   A O   1 
ATOM   1523 C CB  . THR   A 1 199 ? -12.11130 -31.19602 3.47820   1.000 16.81845 ? 199 THR   A CB  1 
ATOM   1524 O OG1 . THR   A 1 199 ? -12.59262 -31.76093 2.25702   1.000 17.84755 ? 199 THR   A OG1 1 
ATOM   1525 C CG2 . THR   A 1 199 ? -13.30457 -30.68435 4.27316   1.000 16.28639 ? 199 THR   A CG2 1 
ATOM   1526 N N   . ILE   A 1 200 ? -11.36039 -28.19450 4.66392   1.000 14.40207 ? 200 ILE   A N   1 
ATOM   1527 C CA  . ILE   A 1 200 ? -10.97140 -27.33671 5.77325   1.000 12.65359 ? 200 ILE   A CA  1 
ATOM   1528 C C   . ILE   A 1 200 ? -11.56784 -27.88668 7.06704   1.000 14.61556 ? 200 ILE   A C   1 
ATOM   1529 O O   . ILE   A 1 200 ? -12.70993 -27.58468 7.42623   1.000 13.08194 ? 200 ILE   A O   1 
ATOM   1530 C CB  . ILE   A 1 200 ? -11.38886 -25.88184 5.50797   1.000 13.65802 ? 200 ILE   A CB  1 
ATOM   1531 C CG1 . ILE   A 1 200 ? -10.99944 -25.47916 4.07963   1.000 13.89457 ? 200 ILE   A CG1 1 
ATOM   1532 C CG2 . ILE   A 1 200 ? -10.71609 -24.96032 6.53678   1.000 11.98804 ? 200 ILE   A CG2 1 
ATOM   1533 C CD1 . ILE   A 1 200 ? -11.73103 -24.23967 3.57656   1.000 11.26844 ? 200 ILE   A CD1 1 
ATOM   1534 N N   . THR   A 1 201 ? -10.77258 -28.68414 7.77674   1.000 14.15635 ? 201 THR   A N   1 
ATOM   1535 C CA  . THR   A 1 201 ? -11.26193 -29.47819 8.91235   1.000 13.77247 ? 201 THR   A CA  1 
ATOM   1536 C C   . THR   A 1 201 ? -11.87395 -28.60719 9.99940   1.000 12.86182 ? 201 THR   A C   1 
ATOM   1537 O O   . THR   A 1 201 ? -12.95561 -28.92065 10.52696  1.000 14.86848 ? 201 THR   A O   1 
ATOM   1538 C CB  . THR   A 1 201 ? -10.09968 -30.29473 9.45480   1.000 16.08730 ? 201 THR   A CB  1 
ATOM   1539 O OG1 . THR   A 1 201 ? -9.57795  -31.08239 8.38120   1.000 16.30722 ? 201 THR   A OG1 1 
ATOM   1540 C CG2 . THR   A 1 201 ? -10.53279 -31.19875 10.61126  1.000 16.00514 ? 201 THR   A CG2 1 
ATOM   1541 N N   . VAL   A 1 202 ? -11.20098 -27.50988 10.36092  1.000 11.46673 ? 202 VAL   A N   1 
ATOM   1542 C CA  . VAL   A 1 202 ? -11.70175 -26.72009 11.48497  1.000 12.10030 ? 202 VAL   A CA  1 
ATOM   1543 C C   . VAL   A 1 202 ? -13.05377 -26.12096 11.13058  1.000 10.91232 ? 202 VAL   A C   1 
ATOM   1544 O O   . VAL   A 1 202 ? -13.91226 -25.95127 12.00242  1.000 11.24808 ? 202 VAL   A O   1 
ATOM   1545 C CB  . VAL   A 1 202 ? -10.69660 -25.62979 11.90423  1.000 12.70992 ? 202 VAL   A CB  1 
ATOM   1546 C CG1 . VAL   A 1 202 ? -10.44220 -24.63515 10.75261  1.000 15.97142 ? 202 VAL   A CG1 1 
ATOM   1547 C CG2 . VAL   A 1 202 ? -11.16957 -24.91012 13.17299  1.000 13.79285 ? 202 VAL   A CG2 1 
ATOM   1548 N N   . ASN   A 1 203 ? -13.27678 -25.82168 9.84658   1.000 14.32168 ? 203 ASN   A N   1 
ATOM   1549 C CA  . ASN   A 1 203 ? -14.55702 -25.24960 9.43658   1.000 12.32988 ? 203 ASN   A CA  1 
ATOM   1550 C C   . ASN   A 1 203 ? -15.67495 -26.27946 9.51749   1.000 10.33682 ? 203 ASN   A C   1 
ATOM   1551 O O   . ASN   A 1 203 ? -16.79199 -25.95684 9.94707   1.000 11.07029 ? 203 ASN   A O   1 
ATOM   1552 C CB  . ASN   A 1 203 ? -14.46975 -24.68738 8.01829   1.000 13.45825 ? 203 ASN   A CB  1 
ATOM   1553 C CG  . ASN   A 1 203 ? -13.68840 -23.38444 7.94250   1.000 11.22393 ? 203 ASN   A CG  1 
ATOM   1554 O OD1 . ASN   A 1 203 ? -13.17493 -22.87465 8.95084   1.000 10.81014 ? 203 ASN   A OD1 1 
ATOM   1555 N ND2 . ASN   A 1 203 ? -13.62912 -22.82154 6.73995   1.000 10.10465 ? 203 ASN   A ND2 1 
ATOM   1556 N N   . VAL   A 1 204 ? -15.40658 -27.51352 9.08145   1.000 11.78988 ? 204 VAL   A N   1 
ATOM   1557 C CA  . VAL   A 1 204 ? -16.38960 -28.58175 9.23370   1.000 14.01559 ? 204 VAL   A CA  1 
ATOM   1558 C C   . VAL   A 1 204 ? -16.78363 -28.73550 10.69576  1.000 14.72033 ? 204 VAL   A C   1 
ATOM   1559 O O   . VAL   A 1 204 ? -17.96624 -28.90503 11.01325  1.000 13.21396 ? 204 VAL   A O   1 
ATOM   1560 C CB  . VAL   A 1 204 ? -15.85964 -29.91038 8.65772   1.000 13.58499 ? 204 VAL   A CB  1 
ATOM   1561 C CG1 . VAL   A 1 204 ? -16.89948 -31.00292 8.82188   1.000 14.32998 ? 204 VAL   A CG1 1 
ATOM   1562 C CG2 . VAL   A 1 204 ? -15.54144 -29.76787 7.17877   1.000 13.51897 ? 204 VAL   A CG2 1 
ATOM   1563 N N   . LEU   A 1 205 ? -15.80018 -28.72640 11.60606  1.000 12.45692 ? 205 LEU   A N   1 
ATOM   1564 C CA  . LEU   A 1 205 ? -16.13621 -28.83002 13.02298  1.000 14.16628 ? 205 LEU   A CA  1 
ATOM   1565 C C   . LEU   A 1 205 ? -17.00236 -27.65922 13.45769  1.000 13.42736 ? 205 LEU   A C   1 
ATOM   1566 O O   . LEU   A 1 205 ? -17.99122 -27.85099 14.16508  1.000 15.21209 ? 205 LEU   A O   1 
ATOM   1567 C CB  . LEU   A 1 205 ? -14.86975 -28.92059 13.88711  1.000 13.83371 ? 205 LEU   A CB  1 
ATOM   1568 C CG  . LEU   A 1 205 ? -13.97503 -30.12779 13.65276  1.000 14.46188 ? 205 LEU   A CG  1 
ATOM   1569 C CD1 . LEU   A 1 205 ? -12.63277 -29.99658 14.38146  1.000 14.96060 ? 205 LEU   A CD1 1 
ATOM   1570 C CD2 . LEU   A 1 205 ? -14.69297 -31.36921 14.11424  1.000 15.53997 ? 205 LEU   A CD2 1 
ATOM   1571 N N   . ALA   A 1 206 ? -16.67309 -26.44133 13.00036  1.000 12.99198 ? 206 ALA   A N   1 
ATOM   1572 C CA  . ALA   A 1 206 ? -17.49525 -25.28408 13.34395  1.000 12.03110 ? 206 ALA   A CA  1 
ATOM   1573 C C   . ALA   A 1 206 ? -18.93566 -25.47864 12.88914  1.000 12.89660 ? 206 ALA   A C   1 
ATOM   1574 O O   . ALA   A 1 206 ? -19.87914 -25.14289 13.61413  1.000 13.82685 ? 206 ALA   A O   1 
ATOM   1575 C CB  . ALA   A 1 206 ? -16.91256 -24.01735 12.71754  1.000 14.14770 ? 206 ALA   A CB  1 
ATOM   1576 N N   . TRP   A 1 207 ? -19.10859 -26.02838 11.69252  1.000 12.61222 ? 207 TRP   A N   1 
ATOM   1577 C CA  . TRP   A 1 207 ? -20.42291 -26.23193 11.10109  1.000 13.73715 ? 207 TRP   A CA  1 
ATOM   1578 C C   . TRP   A 1 207 ? -21.17465 -27.33853 11.83021  1.000 14.81978 ? 207 TRP   A C   1 
ATOM   1579 O O   . TRP   A 1 207 ? -22.39667 -27.25812 12.02793  1.000 16.27560 ? 207 TRP   A O   1 
ATOM   1580 C CB  . TRP   A 1 207 ? -20.22116 -26.55636 9.62777   1.000 12.68792 ? 207 TRP   A CB  1 
ATOM   1581 C CG  . TRP   A 1 207 ? -21.41573 -26.98811 8.86259   1.000 13.69969 ? 207 TRP   A CG  1 
ATOM   1582 C CD1 . TRP   A 1 207 ? -22.39860 -26.19372 8.31399   1.000 14.31025 ? 207 TRP   A CD1 1 
ATOM   1583 C CD2 . TRP   A 1 207 ? -21.71371 -28.32037 8.47558   1.000 13.81051 ? 207 TRP   A CD2 1 
ATOM   1584 N NE1 . TRP   A 1 207 ? -23.30776 -26.97562 7.63891   1.000 15.76751 ? 207 TRP   A NE1 1 
ATOM   1585 C CE2 . TRP   A 1 207 ? -22.91055 -28.28429 7.72371   1.000 14.20518 ? 207 TRP   A CE2 1 
ATOM   1586 C CE3 . TRP   A 1 207 ? -21.09357 -29.55143 8.70527   1.000 14.03977 ? 207 TRP   A CE3 1 
ATOM   1587 C CZ2 . TRP   A 1 207 ? -23.48717 -29.42901 7.19669   1.000 18.25288 ? 207 TRP   A CZ2 1 
ATOM   1588 C CZ3 . TRP   A 1 207 ? -21.68191 -30.69111 8.18898   1.000 17.50459 ? 207 TRP   A CZ3 1 
ATOM   1589 C CH2 . TRP   A 1 207 ? -22.85760 -30.61934 7.43507   1.000 15.57403 ? 207 TRP   A CH2 1 
ATOM   1590 N N   . LEU   A 1 208 ? -20.44916 -28.35617 12.28883  1.000 14.69125 ? 208 LEU   A N   1 
ATOM   1591 C CA  . LEU   A 1 208 ? -21.08593 -29.36454 13.13283  1.000 14.43702 ? 208 LEU   A CA  1 
ATOM   1592 C C   . LEU   A 1 208 ? -21.59867 -28.74521 14.43088  1.000 15.42459 ? 208 LEU   A C   1 
ATOM   1593 O O   . LEU   A 1 208 ? -22.67706 -29.10662 14.91747  1.000 17.84695 ? 208 LEU   A O   1 
ATOM   1594 C CB  . LEU   A 1 208 ? -20.10991 -30.50298 13.41775  1.000 15.93374 ? 208 LEU   A CB  1 
ATOM   1595 C CG  . LEU   A 1 208 ? -19.85480 -31.42744 12.22496  1.000 17.52676 ? 208 LEU   A CG  1 
ATOM   1596 C CD1 . LEU   A 1 208 ? -18.87668 -32.52422 12.60502  1.000 16.56006 ? 208 LEU   A CD1 1 
ATOM   1597 C CD2 . LEU   A 1 208 ? -21.14428 -32.03841 11.70785  1.000 18.15387 ? 208 LEU   A CD2 1 
ATOM   1598 N N   . TYR   A 1 209 ? -20.84567 -27.79674 14.99942  1.000 15.75095 ? 209 TYR   A N   1 
ATOM   1599 C CA  . TYR   A 1 209 ? -21.34487 -27.06200 16.15629  1.000 17.35642 ? 209 TYR   A CA  1 
ATOM   1600 C C   . TYR   A 1 209 ? -22.55465 -26.20577 15.79908  1.000 16.76942 ? 209 TYR   A C   1 
ATOM   1601 O O   . TYR   A 1 209 ? -23.51242 -26.13900 16.57559  1.000 15.92979 ? 209 TYR   A O   1 
ATOM   1602 C CB  . TYR   A 1 209 ? -20.24407 -26.19226 16.75175  1.000 16.91520 ? 209 TYR   A CB  1 
ATOM   1603 C CG  . TYR   A 1 209 ? -19.29956 -26.97204 17.62670  1.000 17.10118 ? 209 TYR   A CG  1 
ATOM   1604 C CD1 . TYR   A 1 209 ? -19.70670 -27.47308 18.85950  1.000 17.25144 ? 209 TYR   A CD1 1 
ATOM   1605 C CD2 . TYR   A 1 209 ? -17.98962 -27.19197 17.22799  1.000 15.82022 ? 209 TYR   A CD2 1 
ATOM   1606 C CE1 . TYR   A 1 209 ? -18.83240 -28.18657 19.65892  1.000 20.81923 ? 209 TYR   A CE1 1 
ATOM   1607 C CE2 . TYR   A 1 209 ? -17.10977 -27.89989 18.01935  1.000 19.32916 ? 209 TYR   A CE2 1 
ATOM   1608 C CZ  . TYR   A 1 209 ? -17.53549 -28.39579 19.23260  1.000 18.57951 ? 209 TYR   A CZ  1 
ATOM   1609 O OH  . TYR   A 1 209 ? -16.66005 -29.10585 20.01999  1.000 21.17935 ? 209 TYR   A OH  1 
ATOM   1610 N N   . ALA   A 1 210 ? -22.50860 -25.50412 14.65789  1.000 16.70885 ? 210 ALA   A N   1 
ATOM   1611 C CA  . ALA   A 1 210 ? -23.69176 -24.79470 14.18010  1.000 16.54228 ? 210 ALA   A CA  1 
ATOM   1612 C C   . ALA   A 1 210 ? -24.89930 -25.72592 14.12923  1.000 16.53186 ? 210 ALA   A C   1 
ATOM   1613 O O   . ALA   A 1 210 ? -26.00269 -25.36890 14.56713  1.000 16.02726 ? 210 ALA   A O   1 
ATOM   1614 C CB  . ALA   A 1 210 ? -23.42105 -24.19072 12.79910  1.000 17.33477 ? 210 ALA   A CB  1 
ATOM   1615 N N   . ALA   A 1 211 ? -24.69771 -26.94040 13.61663  1.000 14.76775 ? 211 ALA   A N   1 
ATOM   1616 C CA  . ALA   A 1 211 ? -25.78195 -27.90710 13.53983  1.000 16.64960 ? 211 ALA   A CA  1 
ATOM   1617 C C   . ALA   A 1 211 ? -26.33285 -28.21743 14.92317  1.000 17.40456 ? 211 ALA   A C   1 
ATOM   1618 O O   . ALA   A 1 211 ? -27.54981 -28.16074 15.15186  1.000 17.69529 ? 211 ALA   A O   1 
ATOM   1619 C CB  . ALA   A 1 211 ? -25.28703 -29.17963 12.86413  1.000 15.74084 ? 211 ALA   A CB  1 
ATOM   1620 N N   . VAL   A 1 212 ? -25.44575 -28.53713 15.86632  1.000 17.26696 ? 212 VAL   A N   1 
ATOM   1621 C CA  . VAL   A 1 212 ? -25.89986 -28.84632 17.22206  1.000 18.60164 ? 212 VAL   A CA  1 
ATOM   1622 C C   . VAL   A 1 212 ? -26.65705 -27.66617 17.81063  1.000 18.88680 ? 212 VAL   A C   1 
ATOM   1623 O O   . VAL   A 1 212 ? -27.71337 -27.83777 18.43138  1.000 21.20277 ? 212 VAL   A O   1 
ATOM   1624 C CB  . VAL   A 1 212 ? -24.71172 -29.24861 18.11599  1.000 20.54054 ? 212 VAL   A CB  1 
ATOM   1625 C CG1 . VAL   A 1 212 ? -25.18318 -29.39496 19.55273  1.000 20.43930 ? 212 VAL   A CG1 1 
ATOM   1626 C CG2 . VAL   A 1 212 ? -24.08064 -30.56144 17.63482  1.000 19.05942 ? 212 VAL   A CG2 1 
ATOM   1627 N N   . ILE   A 1 213 ? -26.13339 -26.44786 17.62596  1.000 18.66192 ? 213 ILE   A N   1 
ATOM   1628 C CA  . ILE   A 1 213 ? -26.82119 -25.26662 18.14808  1.000 18.93842 ? 213 ILE   A CA  1 
ATOM   1629 C C   . ILE   A 1 213 ? -28.22489 -25.18132 17.57541  1.000 20.96626 ? 213 ILE   A C   1 
ATOM   1630 O O   . ILE   A 1 213 ? -29.17700 -24.80295 18.27661  1.000 23.36296 ? 213 ILE   A O   1 
ATOM   1631 C CB  . ILE   A 1 213 ? -25.99031 -24.00169 17.84725  1.000 22.67994 ? 213 ILE   A CB  1 
ATOM   1632 C CG1 . ILE   A 1 213 ? -24.68745 -24.04123 18.65949  1.000 22.27991 ? 213 ILE   A CG1 1 
ATOM   1633 C CG2 . ILE   A 1 213 ? -26.78944 -22.73670 18.15660  1.000 23.38410 ? 213 ILE   A CG2 1 
ATOM   1634 C CD1 . ILE   A 1 213 ? -23.73977 -22.90084 18.38847  1.000 22.77339 ? 213 ILE   A CD1 1 
ATOM   1635 N N   . ASN   A 1 214 ? -28.39349 -25.60637 16.32718  1.000 20.27026 ? 214 ASN   A N   1 
ATOM   1636 C CA  . ASN   A 1 214 ? -29.66004 -25.53247 15.62080  1.000 20.55305 ? 214 ASN   A CA  1 
ATOM   1637 C C   . ASN   A 1 214 ? -30.50793 -26.79618 15.74369  1.000 21.53517 ? 214 ASN   A C   1 
ATOM   1638 O O   . ASN   A 1 214 ? -31.55980 -26.88804 15.09524  1.000 23.61047 ? 214 ASN   A O   1 
ATOM   1639 C CB  . ASN   A 1 214 ? -29.39537 -25.20102 14.16333  1.000 24.46440 ? 214 ASN   A CB  1 
ATOM   1640 C CG  . ASN   A 1 214 ? -29.39504 -23.70727 13.91866  1.000 25.81816 ? 214 ASN   A CG  1 
ATOM   1641 O OD1 . ASN   A 1 214 ? -30.46445 -23.09397 13.84759  1.000 26.05589 ? 214 ASN   A OD1 1 
ATOM   1642 N ND2 . ASN   A 1 214 ? -28.21156 -23.10568 13.85078  1.000 23.81185 ? 214 ASN   A ND2 1 
ATOM   1643 N N   . GLY   A 1 215 ? -30.08954 -27.76461 16.55584  1.000 21.36201 ? 215 GLY   A N   1 
ATOM   1644 C CA  . GLY   A 1 215 ? -30.93957 -28.88413 16.91120  1.000 21.38251 ? 215 GLY   A CA  1 
ATOM   1645 C C   . GLY   A 1 215 ? -30.64636 -30.18447 16.19563  1.000 24.06152 ? 215 GLY   A C   1 
ATOM   1646 O O   . GLY   A 1 215 ? -31.35458 -31.16905 16.43108  1.000 25.01588 ? 215 GLY   A O   1 
ATOM   1647 N N   . ASP   A 1 216 ? -29.64190 -30.21980 15.32722  1.000 20.15608 ? 216 ASP   A N   1 
ATOM   1648 C CA  . ASP   A 1 216 ? -29.21924 -31.44320 14.64990  1.000 21.55647 ? 216 ASP   A CA  1 
ATOM   1649 C C   . ASP   A 1 216 ? -28.21827 -32.15159 15.55531  1.000 22.92590 ? 216 ASP   A C   1 
ATOM   1650 O O   . ASP   A 1 216 ? -27.08979 -31.67914 15.72575  1.000 24.03498 ? 216 ASP   A O   1 
ATOM   1651 C CB  . ASP   A 1 216 ? -28.58618 -31.12625 13.29469  1.000 22.50946 ? 216 ASP   A CB  1 
ATOM   1652 C CG  . ASP   A 1 216 ? -29.61284 -30.94686 12.19965  1.000 26.33998 ? 216 ASP   A CG  1 
ATOM   1653 O OD1 . ASP   A 1 216 ? -30.77285 -31.32530 12.43104  1.000 29.11334 ? 216 ASP   A OD1 1 
ATOM   1654 O OD2 . ASP   A 1 216 ? -29.27174 -30.38397 11.13170  1.000 23.48232 ? 216 ASP   A OD2 1 
ATOM   1655 N N   . ARG   A 1 217 ? -28.62055 -33.29606 16.12605  1.000 22.02237 ? 217 ARG   A N   1 
ATOM   1656 C CA  . ARG   A 1 217 ? -27.79415 -33.99323 17.10556  1.000 22.71380 ? 217 ARG   A CA  1 
ATOM   1657 C C   . ARG   A 1 217 ? -27.51850 -35.45207 16.76605  1.000 23.90510 ? 217 ARG   A C   1 
ATOM   1658 O O   . ARG   A 1 217 ? -26.84337 -36.12718 17.54557  1.000 24.26263 ? 217 ARG   A O   1 
ATOM   1659 C CB  . ARG   A 1 217 ? -28.45492 -33.93935 18.49688  1.000 24.03683 ? 217 ARG   A CB  1 
ATOM   1660 C CG  . ARG   A 1 217 ? -28.80039 -32.53799 18.97079  1.000 25.55367 ? 217 ARG   A CG  1 
ATOM   1661 C CD  . ARG   A 1 217 ? -29.32521 -32.54665 20.40480  1.000 26.07842 ? 217 ARG   A CD  1 
ATOM   1662 N NE  . ARG   A 1 217 ? -28.38699 -33.17737 21.33218  1.000 25.82172 ? 217 ARG   A NE  1 
ATOM   1663 C CZ  . ARG   A 1 217 ? -27.47470 -32.51854 22.03745  1.000 25.56776 ? 217 ARG   A CZ  1 
ATOM   1664 N NH1 . ARG   A 1 217 ? -27.34279 -31.20389 21.90609  1.000 24.58696 ? 217 ARG   A NH1 1 
ATOM   1665 N NH2 . ARG   A 1 217 ? -26.67231 -33.17781 22.85446  1.000 26.40435 ? 217 ARG   A NH2 1 
ATOM   1666 N N   . TRP   A 1 218 ? -28.02154 -35.96076 15.64102  1.000 23.53002 ? 218 TRP   A N   1 
ATOM   1667 C CA  . TRP   A 1 218 ? -28.00197 -37.39869 15.40437  1.000 24.70511 ? 218 TRP   A CA  1 
ATOM   1668 C C   . TRP   A 1 218 ? -26.59608 -37.95695 15.23419  1.000 24.42954 ? 218 TRP   A C   1 
ATOM   1669 O O   . TRP   A 1 218 ? -26.38830 -39.15699 15.44808  1.000 25.67562 ? 218 TRP   A O   1 
ATOM   1670 C CB  . TRP   A 1 218 ? -28.84088 -37.73785 14.17535  1.000 25.24661 ? 218 TRP   A CB  1 
ATOM   1671 C CG  . TRP   A 1 218 ? -28.36293 -37.10475 12.87970  1.000 23.40713 ? 218 TRP   A CG  1 
ATOM   1672 C CD1 . TRP   A 1 218 ? -28.85428 -35.97910 12.28763  1.000 25.18741 ? 218 TRP   A CD1 1 
ATOM   1673 C CD2 . TRP   A 1 218 ? -27.32714 -37.58962 12.02049  1.000 22.97074 ? 218 TRP   A CD2 1 
ATOM   1674 N NE1 . TRP   A 1 218 ? -28.18206 -35.72759 11.11238  1.000 22.83866 ? 218 TRP   A NE1 1 
ATOM   1675 C CE2 . TRP   A 1 218 ? -27.24446 -36.70790 10.92482  1.000 23.36420 ? 218 TRP   A CE2 1 
ATOM   1676 C CE3 . TRP   A 1 218 ? -26.46126 -38.68667 12.06930  1.000 24.56586 ? 218 TRP   A CE3 1 
ATOM   1677 C CZ2 . TRP   A 1 218 ? -26.32518 -36.88470 9.89647   1.000 23.01382 ? 218 TRP   A CZ2 1 
ATOM   1678 C CZ3 . TRP   A 1 218 ? -25.55376 -38.86185 11.04220  1.000 24.88744 ? 218 TRP   A CZ3 1 
ATOM   1679 C CH2 . TRP   A 1 218 ? -25.49468 -37.96372 9.97064   1.000 24.23539 ? 218 TRP   A CH2 1 
ATOM   1680 N N   . PHE   A 1 219 ? -25.64607 -37.12536 14.82751  1.000 22.95851 ? 219 PHE   A N   1 
ATOM   1681 C CA  . PHE   A 1 219 ? -24.25871 -37.51732 14.62930  1.000 25.00485 ? 219 PHE   A CA  1 
ATOM   1682 C C   . PHE   A 1 219 ? -23.42504 -37.44652 15.90391  1.000 23.01056 ? 219 PHE   A C   1 
ATOM   1683 O O   . PHE   A 1 219 ? -22.23228 -37.76943 15.86522  1.000 24.63993 ? 219 PHE   A O   1 
ATOM   1684 C CB  . PHE   A 1 219 ? -23.63281 -36.62765 13.55267  1.000 23.38172 ? 219 PHE   A CB  1 
ATOM   1685 C CG  . PHE   A 1 219 ? -23.80514 -35.15890 13.81817  1.000 19.88301 ? 219 PHE   A CG  1 
ATOM   1686 C CD1 . PHE   A 1 219 ? -22.94751 -34.48432 14.67452  1.000 19.46826 ? 219 PHE   A CD1 1 
ATOM   1687 C CD2 . PHE   A 1 219 ? -24.84576 -34.45461 13.22336  1.000 20.71459 ? 219 PHE   A CD2 1 
ATOM   1688 C CE1 . PHE   A 1 219 ? -23.11535 -33.12665 14.92279  1.000 19.94249 ? 219 PHE   A CE1 1 
ATOM   1689 C CE2 . PHE   A 1 219 ? -25.02079 -33.10085 13.46598  1.000 19.45901 ? 219 PHE   A CE2 1 
ATOM   1690 C CZ  . PHE   A 1 219 ? -24.15377 -32.43325 14.31813  1.000 18.11596 ? 219 PHE   A CZ  1 
ATOM   1691 N N   . LEU   A 1 220 ? -24.00408 -36.99898 17.01319  1.000 23.48459 ? 220 LEU   A N   1 
ATOM   1692 C CA  . LEU   A 1 220 ? -23.27780 -36.95140 18.27148  1.000 24.07132 ? 220 LEU   A CA  1 
ATOM   1693 C C   . LEU   A 1 220 ? -23.09687 -38.35399 18.83484  1.000 25.77236 ? 220 LEU   A C   1 
ATOM   1694 O O   . LEU   A 1 220 ? -23.81291 -39.29596 18.48669  1.000 28.73402 ? 220 LEU   A O   1 
ATOM   1695 C CB  . LEU   A 1 220 ? -24.01117 -36.08387 19.29494  1.000 24.32586 ? 220 LEU   A CB  1 
ATOM   1696 C CG  . LEU   A 1 220 ? -24.07975 -34.60348 18.93024  1.000 22.84134 ? 220 LEU   A CG  1 
ATOM   1697 C CD1 . LEU   A 1 220 ? -24.73980 -33.83772 20.03188  1.000 23.41292 ? 220 LEU   A CD1 1 
ATOM   1698 C CD2 . LEU   A 1 220 ? -22.66328 -34.07720 18.68304  1.000 21.76864 ? 220 LEU   A CD2 1 
ATOM   1699 N N   . ASN   A 1 221 ? -22.13024 -38.47573 19.73370  1.000 26.32108 ? 221 ASN   A N   1 
ATOM   1700 C CA  . ASN   A 1 221 ? -21.84356 -39.74444 20.37532  1.000 28.12477 ? 221 ASN   A CA  1 
ATOM   1701 C C   . ASN   A 1 221 ? -21.11699 -39.47634 21.68023  1.000 30.86654 ? 221 ASN   A C   1 
ATOM   1702 O O   . ASN   A 1 221 ? -20.66429 -38.35891 21.94150  1.000 27.80345 ? 221 ASN   A O   1 
ATOM   1703 C CB  . ASN   A 1 221 ? -21.05314 -40.65479 19.43104  1.000 34.46939 ? 221 ASN   A CB  1 
ATOM   1704 C CG  . ASN   A 1 221 ? -19.85505 -39.94930 18.78129  1.000 38.13825 ? 221 ASN   A CG  1 
ATOM   1705 O OD1 . ASN   A 1 221 ? -19.02896 -39.29806 19.44583  1.000 38.75984 ? 221 ASN   A OD1 1 
ATOM   1706 N ND2 . ASN   A 1 221 ? -19.79315 -40.03341 17.45376  1.000 35.38536 ? 221 ASN   A ND2 1 
ATOM   1707 N N   . ARG   A 1 222 ? -21.05911 -40.50637 22.52001  1.000 30.60262 ? 222 ARG   A N   1 
ATOM   1708 C CA  . ARG   A 1 222 ? -20.27773 -40.43956 23.74518  1.000 32.94884 ? 222 ARG   A CA  1 
ATOM   1709 C C   . ARG   A 1 222 ? -18.82524 -40.83369 23.53260  1.000 34.96845 ? 222 ARG   A C   1 
ATOM   1710 O O   . ARG   A 1 222 ? -18.00249 -40.58791 24.41827  1.000 41.55744 ? 222 ARG   A O   1 
ATOM   1711 C CB  . ARG   A 1 222 ? -20.91545 -41.32274 24.82435  1.000 35.71989 ? 222 ARG   A CB  1 
ATOM   1712 C CG  . ARG   A 1 222 ? -22.05049 -40.62573 25.52377  1.000 36.29001 ? 222 ARG   A CG  1 
ATOM   1713 C CD  . ARG   A 1 222 ? -21.55325 -39.82278 26.71111  1.000 39.74528 ? 222 ARG   A CD  1 
ATOM   1714 N NE  . ARG   A 1 222 ? -21.53903 -40.62895 27.93044  1.000 43.70574 ? 222 ARG   A NE  1 
ATOM   1715 C CZ  . ARG   A 1 222 ? -22.38584 -40.46240 28.94115  1.000 42.39885 ? 222 ARG   A CZ  1 
ATOM   1716 N NH1 . ARG   A 1 222 ? -23.32077 -39.51881 28.87419  1.000 44.80865 ? 222 ARG   A NH1 1 
ATOM   1717 N NH2 . ARG   A 1 222 ? -22.30456 -41.24014 30.01314  1.000 45.95707 ? 222 ARG   A NH2 1 
ATOM   1718 N N   . PHE   A 1 223 ? -18.49993 -41.41673 22.37769  1.000 39.16697 ? 223 PHE   A N   1 
ATOM   1719 C CA  . PHE   A 1 223 ? -17.11844 -41.68752 22.00455  1.000 39.24504 ? 223 PHE   A CA  1 
ATOM   1720 C C   . PHE   A 1 223 ? -16.29069 -40.41325 22.10187  1.000 36.33021 ? 223 PHE   A C   1 
ATOM   1721 O O   . PHE   A 1 223 ? -16.79858 -39.29742 21.94115  1.000 33.24384 ? 223 PHE   A O   1 
ATOM   1722 C CB  . PHE   A 1 223 ? -17.02642 -42.19132 20.55775  1.000 38.80948 ? 223 PHE   A CB  1 
ATOM   1723 C CG  . PHE   A 1 223 ? -17.87390 -43.39719 20.26284  1.000 42.20845 ? 223 PHE   A CG  1 
ATOM   1724 C CD1 . PHE   A 1 223 ? -17.49586 -44.66381 20.67169  1.000 46.60510 ? 223 PHE   A CD1 1 
ATOM   1725 C CD2 . PHE   A 1 223 ? -19.03643 -43.25734 19.51995  1.000 43.44297 ? 223 PHE   A CD2 1 
ATOM   1726 C CE1 . PHE   A 1 223 ? -18.28951 -45.76858 20.37402  1.000 48.38626 ? 223 PHE   A CE1 1 
ATOM   1727 C CE2 . PHE   A 1 223 ? -19.83569 -44.34234 19.21901  1.000 44.02684 ? 223 PHE   A CE2 1 
ATOM   1728 C CZ  . PHE   A 1 223 ? -19.46365 -45.60474 19.64535  1.000 51.25445 ? 223 PHE   A CZ  1 
ATOM   1729 N N   . THR   A 1 224 ? -14.99407 -40.58471 22.33149  1.000 32.97391 ? 224 THR   A N   1 
ATOM   1730 C CA  . THR   A 1 224 ? -14.05051 -39.50368 22.10618  1.000 34.12322 ? 224 THR   A CA  1 
ATOM   1731 C C   . THR   A 1 224 ? -12.86797 -40.07327 21.33577  1.000 33.43455 ? 224 THR   A C   1 
ATOM   1732 O O   . THR   A 1 224 ? -12.78870 -41.27719 21.08072  1.000 34.21773 ? 224 THR   A O   1 
ATOM   1733 C CB  . THR   A 1 224 ? -13.59660 -38.85379 23.42166  1.000 36.88523 ? 224 THR   A CB  1 
ATOM   1734 O OG1 . THR   A 1 224 ? -12.89662 -37.63248 23.13647  1.000 34.21458 ? 224 THR   A OG1 1 
ATOM   1735 C CG2 . THR   A 1 224 ? -12.68066 -39.79941 24.20183  1.000 33.94611 ? 224 THR   A CG2 1 
ATOM   1736 N N   . THR   A 1 225 ? -11.94688 -39.19752 20.95453  1.000 29.00273 ? 225 THR   A N   1 
ATOM   1737 C CA  . THR   A 1 225 ? -10.73397 -39.61953 20.26958  1.000 33.20971 ? 225 THR   A CA  1 
ATOM   1738 C C   . THR   A 1 225 ? -9.60686  -38.68870 20.69087  1.000 32.71223 ? 225 THR   A C   1 
ATOM   1739 O O   . THR   A 1 225 ? -9.83804  -37.64068 21.29770  1.000 34.05802 ? 225 THR   A O   1 
ATOM   1740 C CB  . THR   A 1 225 ? -10.91143 -39.59882 18.74439  1.000 33.70825 ? 225 THR   A CB  1 
ATOM   1741 O OG1 . THR   A 1 225 ? -9.73998  -40.13200 18.11256  1.000 34.70573 ? 225 THR   A OG1 1 
ATOM   1742 C CG2 . THR   A 1 225 ? -11.11036 -38.17952 18.26143  1.000 31.19122 ? 225 THR   A CG2 1 
ATOM   1743 N N   . THR   A 1 226 ? -8.37661  -39.08202 20.37598  1.000 33.27349 ? 226 THR   A N   1 
ATOM   1744 C CA  . THR   A 1 226 ? -7.24221  -38.20540 20.61144  1.000 31.98080 ? 226 THR   A CA  1 
ATOM   1745 C C   . THR   A 1 226 ? -7.01599  -37.34396 19.38009  1.000 30.86306 ? 226 THR   A C   1 
ATOM   1746 O O   . THR   A 1 226 ? -7.47837  -37.66132 18.28026  1.000 27.33865 ? 226 THR   A O   1 
ATOM   1747 C CB  . THR   A 1 226 ? -5.96332  -38.98816 20.92935  1.000 35.53870 ? 226 THR   A CB  1 
ATOM   1748 O OG1 . THR   A 1 226 ? -5.53369  -39.69167 19.76134  1.000 35.33241 ? 226 THR   A OG1 1 
ATOM   1749 C CG2 . THR   A 1 226 ? -6.21319  -39.99531 22.03881  1.000 31.92766 ? 226 THR   A CG2 1 
ATOM   1750 N N   . LEU   A 1 227 ? -6.30573  -36.23650 19.57812  1.000 29.65314 ? 227 LEU   A N   1 
ATOM   1751 C CA  . LEU   A 1 227 ? -5.96541  -35.36975 18.45780  1.000 28.20411 ? 227 LEU   A CA  1 
ATOM   1752 C C   . LEU   A 1 227 ? -5.16065  -36.11726 17.40388  1.000 30.57451 ? 227 LEU   A C   1 
ATOM   1753 O O   . LEU   A 1 227 ? -5.43258  -36.01559 16.20506  1.000 29.03466 ? 227 LEU   A O   1 
ATOM   1754 C CB  . LEU   A 1 227 ? -5.21464  -34.13202 18.95981  1.000 30.70880 ? 227 LEU   A CB  1 
ATOM   1755 C CG  . LEU   A 1 227 ? -5.09564  -32.97793 17.96362  1.000 26.37458 ? 227 LEU   A CG  1 
ATOM   1756 C CD1 . LEU   A 1 227 ? -6.43994  -32.62984 17.30686  1.000 26.81234 ? 227 LEU   A CD1 1 
ATOM   1757 C CD2 . LEU   A 1 227 ? -4.51912  -31.74382 18.64953  1.000 27.37884 ? 227 LEU   A CD2 1 
ATOM   1758 N N   . ASN   A 1 228 ? -4.16351  -36.88430 17.83463  1.000 30.48066 ? 228 ASN   A N   1 
ATOM   1759 C CA  . ASN   A 1 228 ? -3.34666  -37.63174 16.87029  1.000 32.67399 ? 228 ASN   A CA  1 
ATOM   1760 C C   . ASN   A 1 228 ? -4.17874  -38.66716 16.11326  1.000 33.22609 ? 228 ASN   A C   1 
ATOM   1761 O O   . ASN   A 1 228 ? -4.09485  -38.76858 14.87934  1.000 33.75157 ? 228 ASN   A O   1 
ATOM   1762 C CB  . ASN   A 1 228 ? -2.18372  -38.33252 17.57642  1.000 34.78089 ? 228 ASN   A CB  1 
ATOM   1763 C CG  . ASN   A 1 228 ? -1.23344  -37.36286 18.19452  1.000 40.27600 ? 228 ASN   A CG  1 
ATOM   1764 O OD1 . ASN   A 1 228 ? -1.08688  -37.31683 19.42368  1.000 45.41053 ? 228 ASN   A OD1 1 
ATOM   1765 N ND2 . ASN   A 1 228 ? -0.62334  -36.52788 17.35944  1.000 40.28250 ? 228 ASN   A ND2 1 
ATOM   1766 N N   . ASP   A 1 229 ? -5.00636  -39.42283 16.83095  1.000 33.78802 ? 229 ASP   A N   1 
ATOM   1767 C CA  . ASP   A 1 229 ? -5.81247  -40.43415 16.16754  1.000 32.32158 ? 229 ASP   A CA  1 
ATOM   1768 C C   . ASP   A 1 229 ? -6.79915  -39.78652 15.20724  1.000 30.48693 ? 229 ASP   A C   1 
ATOM   1769 O O   . ASP   A 1 229 ? -7.03435  -40.31344 14.11533  1.000 29.54207 ? 229 ASP   A O   1 
ATOM   1770 C CB  . ASP   A 1 229 ? -6.52409  -41.30403 17.20363  1.000 33.84441 ? 229 ASP   A CB  1 
ATOM   1771 C CG  . ASP   A 1 229 ? -5.54667  -42.11996 18.05437  1.000 38.74287 ? 229 ASP   A CG  1 
ATOM   1772 O OD1 . ASP   A 1 229 ? -4.32735  -42.02997 17.81112  1.000 42.99789 ? 229 ASP   A OD1 1 
ATOM   1773 O OD2 . ASP   A 1 229 ? -5.99608  -42.87544 18.94082  1.000 43.06671 ? 229 ASP   A OD2 1 
ATOM   1774 N N   . PHE   A 1 230 ? -7.35612  -38.62262 15.56343  1.000 28.75700 ? 230 PHE   A N   1 
ATOM   1775 C CA  . PHE   A 1 230 ? -8.22421  -37.94833 14.60687  1.000 29.93369 ? 230 PHE   A CA  1 
ATOM   1776 C C   . PHE   A 1 230 ? -7.43724  -37.52104 13.37671  1.000 27.64230 ? 230 PHE   A C   1 
ATOM   1777 O O   . PHE   A 1 230 ? -7.90276  -37.68721 12.24538  1.000 24.44012 ? 230 PHE   A O   1 
ATOM   1778 C CB  . PHE   A 1 230 ? -8.91096  -36.73047 15.22278  1.000 27.21380 ? 230 PHE   A CB  1 
ATOM   1779 C CG  . PHE   A 1 230 ? -9.66982  -35.91619 14.21051  1.000 26.40918 ? 230 PHE   A CG  1 
ATOM   1780 C CD1 . PHE   A 1 230 ? -10.92710 -36.32551 13.77215  1.000 24.08271 ? 230 PHE   A CD1 1 
ATOM   1781 C CD2 . PHE   A 1 230 ? -9.09730  -34.78564 13.63367  1.000 23.56016 ? 230 PHE   A CD2 1 
ATOM   1782 C CE1 . PHE   A 1 230 ? -11.60995 -35.60002 12.81047  1.000 24.01534 ? 230 PHE   A CE1 1 
ATOM   1783 C CE2 . PHE   A 1 230 ? -9.77914  -34.05896 12.67562  1.000 25.93512 ? 230 PHE   A CE2 1 
ATOM   1784 C CZ  . PHE   A 1 230 ? -11.03815 -34.46320 12.26370  1.000 20.53878 ? 230 PHE   A CZ  1 
ATOM   1785 N N   . ASN   A 1 231 ? -6.23323  -36.98485 13.57944  1.000 27.28106 ? 231 ASN   A N   1 
ATOM   1786 C CA  . ASN   A 1 231 ? -5.45857  -36.46565 12.45997  1.000 27.35804 ? 231 ASN   A CA  1 
ATOM   1787 C C   . ASN   A 1 231 ? -5.00561  -37.56449 11.50906  1.000 27.31064 ? 231 ASN   A C   1 
ATOM   1788 O O   . ASN   A 1 231 ? -4.76033  -37.28083 10.33160  1.000 26.95436 ? 231 ASN   A O   1 
ATOM   1789 C CB  . ASN   A 1 231 ? -4.27193  -35.65425 12.98056  1.000 26.61741 ? 231 ASN   A CB  1 
ATOM   1790 C CG  . ASN   A 1 231 ? -4.64528  -34.20761 13.22748  1.000 24.84834 ? 231 ASN   A CG  1 
ATOM   1791 O OD1 . ASN   A 1 231 ? -5.39719  -33.64220 12.46022  1.000 29.04205 ? 231 ASN   A OD1 1 
ATOM   1792 N ND2 . ASN   A 1 231 ? -4.14175  -33.61424 14.30172  1.000 25.91258 ? 231 ASN   A ND2 1 
ATOM   1793 N N   . LEU   A 1 232 ? -4.92450  -38.81013 11.98162  1.000 29.60048 ? 232 LEU   A N   1 
ATOM   1794 C CA  . LEU   A 1 232 ? -4.66625  -39.92406 11.07620  1.000 28.81716 ? 232 LEU   A CA  1 
ATOM   1795 C C   . LEU   A 1 232 ? -5.86175  -40.16941 10.16645  1.000 30.96070 ? 232 LEU   A C   1 
ATOM   1796 O O   . LEU   A 1 232 ? -5.69266  -40.50206 8.98767   1.000 29.60196 ? 232 LEU   A O   1 
ATOM   1797 C CB  . LEU   A 1 232 ? -4.33129  -41.18490 11.86952  1.000 30.77162 ? 232 LEU   A CB  1 
ATOM   1798 C CG  . LEU   A 1 232 ? -2.94143  -41.25597 12.51465  1.000 36.70590 ? 232 LEU   A CG  1 
ATOM   1799 C CD1 . LEU   A 1 232 ? -2.81667  -42.49951 13.38046  1.000 36.11181 ? 232 LEU   A CD1 1 
ATOM   1800 C CD2 . LEU   A 1 232 ? -1.83054  -41.20044 11.47768  1.000 33.95839 ? 232 LEU   A CD2 1 
ATOM   1801 N N   . VAL   A 1 233 ? -7.08200  -40.00938 10.69445  1.000 27.82945 ? 233 VAL   A N   1 
ATOM   1802 C CA  . VAL   A 1 233 ? -8.26852  -40.14599 9.85521   1.000 27.87446 ? 233 VAL   A CA  1 
ATOM   1803 C C   . VAL   A 1 233 ? -8.37167  -38.97484 8.88924   1.000 29.22783 ? 233 VAL   A C   1 
ATOM   1804 O O   . VAL   A 1 233 ? -8.68430  -39.15137 7.70261   1.000 28.55107 ? 233 VAL   A O   1 
ATOM   1805 C CB  . VAL   A 1 233 ? -9.52716  -40.27463 10.73249  1.000 30.19894 ? 233 VAL   A CB  1 
ATOM   1806 C CG1 . VAL   A 1 233 ? -10.79749 -40.23906 9.87647   1.000 29.65013 ? 233 VAL   A CG1 1 
ATOM   1807 C CG2 . VAL   A 1 233 ? -9.46277  -41.54219 11.55761  1.000 30.42632 ? 233 VAL   A CG2 1 
ATOM   1808 N N   . ALA   A 1 234 ? -8.11793  -37.75991 9.38495   1.000 27.59886 ? 234 ALA   A N   1 
ATOM   1809 C CA  . ALA   A 1 234 ? -8.13327  -36.57549 8.53976   1.000 25.10798 ? 234 ALA   A CA  1 
ATOM   1810 C C   . ALA   A 1 234 ? -7.25823  -36.77094 7.30718   1.000 27.08653 ? 234 ALA   A C   1 
ATOM   1811 O O   . ALA   A 1 234 ? -7.70196  -36.55750 6.17239   1.000 25.75453 ? 234 ALA   A O   1 
ATOM   1812 C CB  . ALA   A 1 234 ? -7.67030  -35.36251 9.35026   1.000 24.88090 ? 234 ALA   A CB  1 
ATOM   1813 N N   . MET   A 1 235 ? -6.00633  -37.18396 7.52029   1.000 27.99147 ? 235 MET   A N   1 
ATOM   1814 C CA  . MET   A 1 235 ? -5.10419  -37.46773 6.41059   1.000 28.76944 ? 235 MET   A CA  1 
ATOM   1815 C C   . MET   A 1 235 ? -5.72584  -38.43992 5.41605   1.000 28.45096 ? 235 MET   A C   1 
ATOM   1816 O O   . MET   A 1 235 ? -5.65812  -38.22890 4.19859   1.000 27.96016 ? 235 MET   A O   1 
ATOM   1817 C CB  . MET   A 1 235 ? -3.80088  -38.04648 6.95210   1.000 28.46571 ? 235 MET   A CB  1 
ATOM   1818 C CG  . MET   A 1 235 ? -2.67090  -38.14636 5.95277   1.000 36.39513 ? 235 MET   A CG  1 
ATOM   1819 S SD  . MET   A 1 235 ? -1.12453  -37.65504 6.73305   1.000 50.22258 ? 235 MET   A SD  1 
ATOM   1820 C CE  . MET   A 1 235 ? -1.04690  -38.86405 8.05876   1.000 37.65096 ? 235 MET   A CE  1 
ATOM   1821 N N   . LYS   A 1 236 ? -6.34535  -39.50959 5.92078   1.000 28.25839 ? 236 LYS   A N   1 
ATOM   1822 C CA  . LYS   A 1 236 ? -6.85036  -40.55653 5.04251   1.000 27.76834 ? 236 LYS   A CA  1 
ATOM   1823 C C   . LYS   A 1 236 ? -7.97646  -40.05538 4.14601   1.000 27.86040 ? 236 LYS   A C   1 
ATOM   1824 O O   . LYS   A 1 236 ? -8.11573  -40.52635 3.01139   1.000 30.61844 ? 236 LYS   A O   1 
ATOM   1825 C CB  . LYS   A 1 236 ? -7.30535  -41.75511 5.87711   1.000 28.61159 ? 236 LYS   A CB  1 
ATOM   1826 C CG  . LYS   A 1 236 ? -7.99032  -42.83183 5.06803   1.000 32.50034 ? 236 LYS   A CG  1 
ATOM   1827 C CD  . LYS   A 1 236 ? -8.49207  -43.96874 5.93310   1.000 34.80883 ? 236 LYS   A CD  1 
ATOM   1828 C CE  . LYS   A 1 236 ? -9.45305  -44.84980 5.14947   1.000 32.28278 ? 236 LYS   A CE  1 
ATOM   1829 N NZ  . LYS   A 1 236 ? -9.36191  -46.27509 5.56500   1.000 36.09482 ? 236 LYS   A NZ  1 
ATOM   1830 N N   . TYR   A 1 237 ? -8.77383  -39.09679 4.61968   1.000 25.94894 ? 237 TYR   A N   1 
ATOM   1831 C CA  . TYR   A 1 237 ? -9.89591  -38.55397 3.86115   1.000 23.34398 ? 237 TYR   A CA  1 
ATOM   1832 C C   . TYR   A 1 237 ? -9.58867  -37.19089 3.27148   1.000 23.15885 ? 237 TYR   A C   1 
ATOM   1833 O O   . TYR   A 1 237 ? -10.51402 -36.43929 2.94697   1.000 21.67588 ? 237 TYR   A O   1 
ATOM   1834 C CB  . TYR   A 1 237 ? -11.13958 -38.47853 4.74144   1.000 23.92362 ? 237 TYR   A CB  1 
ATOM   1835 C CG  . TYR   A 1 237 ? -11.68304 -39.84520 5.05624   1.000 26.64372 ? 237 TYR   A CG  1 
ATOM   1836 C CD1 . TYR   A 1 237 ? -12.60847 -40.45825 4.21637   1.000 27.22462 ? 237 TYR   A CD1 1 
ATOM   1837 C CD2 . TYR   A 1 237 ? -11.23645 -40.54423 6.16619   1.000 28.10067 ? 237 TYR   A CD2 1 
ATOM   1838 C CE1 . TYR   A 1 237 ? -13.08891 -41.71894 4.49392   1.000 26.08722 ? 237 TYR   A CE1 1 
ATOM   1839 C CE2 . TYR   A 1 237 ? -11.71106 -41.80535 6.45010   1.000 28.73830 ? 237 TYR   A CE2 1 
ATOM   1840 C CZ  . TYR   A 1 237 ? -12.63631 -42.38415 5.61148   1.000 28.28166 ? 237 TYR   A CZ  1 
ATOM   1841 O OH  . TYR   A 1 237 ? -13.10265 -43.63842 5.90463   1.000 31.16411 ? 237 TYR   A OH  1 
ATOM   1842 N N   . ASN   A 1 238 ? -8.30799  -36.85476 3.14321   1.000 22.28204 ? 238 ASN   A N   1 
ATOM   1843 C CA  . ASN   A 1 238 ? -7.89200  -35.62345 2.47981   1.000 23.00737 ? 238 ASN   A CA  1 
ATOM   1844 C C   . ASN   A 1 238 ? -8.43775  -34.40090 3.22604   1.000 20.27938 ? 238 ASN   A C   1 
ATOM   1845 O O   . ASN   A 1 238 ? -8.88340  -33.41935 2.63145   1.000 19.42740 ? 238 ASN   A O   1 
ATOM   1846 C CB  . ASN   A 1 238 ? -8.33017  -35.63527 1.01537   1.000 20.56592 ? 238 ASN   A CB  1 
ATOM   1847 C CG  . ASN   A 1 238 ? -7.72576  -34.51584 0.22953   1.000 24.97598 ? 238 ASN   A CG  1 
ATOM   1848 O OD1 . ASN   A 1 238 ? -8.25242  -34.08882 -0.79733  1.000 29.60111 ? 238 ASN   A OD1 1 
ATOM   1849 N ND2 . ASN   A 1 238 ? -6.59104  -34.03752 0.70137   1.000 25.52476 ? 238 ASN   A ND2 1 
ATOM   1850 N N   . TYR   A 1 239 ? -8.42324  -34.47150 4.54726   1.000 20.74812 ? 239 TYR   A N   1 
ATOM   1851 C CA  . TYR   A 1 239 ? -8.78122  -33.34754 5.39312   1.000 19.98086 ? 239 TYR   A CA  1 
ATOM   1852 C C   . TYR   A 1 239 ? -7.51240  -32.71259 5.93390   1.000 21.09605 ? 239 TYR   A C   1 
ATOM   1853 O O   . TYR   A 1 239 ? -6.50093  -33.38306 6.13543   1.000 20.70080 ? 239 TYR   A O   1 
ATOM   1854 C CB  . TYR   A 1 239 ? -9.66453  -33.77717 6.56707   1.000 18.31503 ? 239 TYR   A CB  1 
ATOM   1855 C CG  . TYR   A 1 239 ? -11.15560 -33.74217 6.31224   1.000 16.97432 ? 239 TYR   A CG  1 
ATOM   1856 C CD1 . TYR   A 1 239 ? -11.71511 -34.36956 5.20314   1.000 18.90429 ? 239 TYR   A CD1 1 
ATOM   1857 C CD2 . TYR   A 1 239 ? -12.00228 -33.09423 7.19809   1.000 16.78510 ? 239 TYR   A CD2 1 
ATOM   1858 C CE1 . TYR   A 1 239 ? -13.08908 -34.34213 4.98412   1.000 18.33880 ? 239 TYR   A CE1 1 
ATOM   1859 C CE2 . TYR   A 1 239 ? -13.37078 -33.06358 6.99973   1.000 15.38937 ? 239 TYR   A CE2 1 
ATOM   1860 C CZ  . TYR   A 1 239 ? -13.90860 -33.68651 5.89158   1.000 17.56506 ? 239 TYR   A CZ  1 
ATOM   1861 O OH  . TYR   A 1 239 ? -15.25949 -33.65051 5.68868   1.000 16.62652 ? 239 TYR   A OH  1 
ATOM   1862 N N   . GLU   A 1 240 ? -7.58967  -31.41634 6.18784   1.000 20.52907 ? 240 GLU   A N   1 
ATOM   1863 C CA  . GLU   A 1 240 ? -6.44898  -30.68926 6.70132   1.000 20.71399 ? 240 GLU   A CA  1 
ATOM   1864 C C   . GLU   A 1 240 ? -6.16379  -31.14470 8.13006   1.000 21.04602 ? 240 GLU   A C   1 
ATOM   1865 O O   . GLU   A 1 240 ? -7.08456  -31.51865 8.85977   1.000 21.96204 ? 240 GLU   A O   1 
ATOM   1866 C CB  . GLU   A 1 240 ? -6.75284  -29.20097 6.66896   1.000 19.85371 ? 240 GLU   A CB  1 
ATOM   1867 C CG  . GLU   A 1 240 ? -6.45472  -28.60259 5.33540   1.000 22.90852 ? 240 GLU   A CG  1 
ATOM   1868 C CD  . GLU   A 1 240 ? -6.50657  -27.10366 5.35836   1.000 29.09888 ? 240 GLU   A CD  1 
ATOM   1869 O OE1 . GLU   A 1 240 ? -5.60640  -26.48372 4.75365   1.000 34.29875 ? 240 GLU   A OE1 1 
ATOM   1870 O OE2 . GLU   A 1 240 ? -7.43322  -26.54686 6.00010   1.000 26.39158 ? 240 GLU   A OE2 1 
ATOM   1871 N N   . PRO   A 1 241 ? -4.89733  -31.17118 8.54320   1.000 23.10415 ? 241 PRO   A N   1 
ATOM   1872 C CA  . PRO   A 1 241 ? -4.60085  -31.50239 9.94070   1.000 23.06603 ? 241 PRO   A CA  1 
ATOM   1873 C C   . PRO   A 1 241 ? -5.27033  -30.51379 10.88262  1.000 23.42208 ? 241 PRO   A C   1 
ATOM   1874 O O   . PRO   A 1 241 ? -5.42052  -29.33034 10.57400  1.000 25.75615 ? 241 PRO   A O   1 
ATOM   1875 C CB  . PRO   A 1 241 ? -3.07109  -31.41342 10.01508  1.000 24.69473 ? 241 PRO   A CB  1 
ATOM   1876 C CG  . PRO   A 1 241 ? -2.61532  -31.54298 8.59582   1.000 25.38172 ? 241 PRO   A CG  1 
ATOM   1877 C CD  . PRO   A 1 241 ? -3.67175  -30.90240 7.76822   1.000 22.36828 ? 241 PRO   A CD  1 
ATOM   1878 N N   . LEU   A 1 242 ? -5.71373  -31.01802 12.02807  1.000 25.37300 ? 242 LEU   A N   1 
ATOM   1879 C CA  . LEU   A 1 242 ? -6.28562  -30.16689 13.06200  1.000 25.07086 ? 242 LEU   A CA  1 
ATOM   1880 C C   . LEU   A 1 242 ? -5.19221  -29.82836 14.06330  1.000 22.62259 ? 242 LEU   A C   1 
ATOM   1881 O O   . LEU   A 1 242 ? -4.51483  -30.72065 14.56469  1.000 21.35682 ? 242 LEU   A O   1 
ATOM   1882 C CB  . LEU   A 1 242 ? -7.45439  -30.85721 13.76465  1.000 23.32458 ? 242 LEU   A CB  1 
ATOM   1883 C CG  . LEU   A 1 242 ? -8.38570  -29.91408 14.52208  1.000 20.83678 ? 242 LEU   A CG  1 
ATOM   1884 C CD1 . LEU   A 1 242 ? -9.20971  -29.10492 13.52704  1.000 21.93292 ? 242 LEU   A CD1 1 
ATOM   1885 C CD2 . LEU   A 1 242 ? -9.27556  -30.69892 15.49983  1.000 22.44526 ? 242 LEU   A CD2 1 
ATOM   1886 N N   . THR   A 1 243 ? -4.99811  -28.54359 14.32063  1.000 23.82771 ? 243 THR   A N   1 
ATOM   1887 C CA  . THR   A 1 243 ? -3.97406  -28.10429 15.25178  1.000 24.75933 ? 243 THR   A CA  1 
ATOM   1888 C C   . THR   A 1 243 ? -4.59101  -27.77942 16.60241  1.000 23.27236 ? 243 THR   A C   1 
ATOM   1889 O O   . THR   A 1 243 ? -5.80847  -27.61960 16.74155  1.000 22.99336 ? 243 THR   A O   1 
ATOM   1890 C CB  . THR   A 1 243 ? -3.24913  -26.87000 14.72056  1.000 22.57414 ? 243 THR   A CB  1 
ATOM   1891 O OG1 . THR   A 1 243 ? -4.17545  -25.78148 14.69544  1.000 22.28152 ? 243 THR   A OG1 1 
ATOM   1892 C CG2 . THR   A 1 243 ? -2.71645  -27.12924 13.31931  1.000 23.64923 ? 243 THR   A CG2 1 
ATOM   1893 N N   . GLN   A 1 244 ? -3.72197  -27.65118 17.60505  1.000 22.09590 ? 244 GLN   A N   1 
ATOM   1894 C CA  . GLN   A 1 244 ? -4.19847  -27.22444 18.91433  1.000 22.61476 ? 244 GLN   A CA  1 
ATOM   1895 C C   . GLN   A 1 244 ? -4.77090  -25.81959 18.86152  1.000 21.87045 ? 244 GLN   A C   1 
ATOM   1896 O O   . GLN   A 1 244 ? -5.69085  -25.49949 19.62511  1.000 23.11640 ? 244 GLN   A O   1 
ATOM   1897 C CB  . GLN   A 1 244 ? -3.08739  -27.30265 19.95858  1.000 25.73665 ? 244 GLN   A CB  1 
ATOM   1898 C CG  . GLN   A 1 244 ? -3.58423  -26.94458 21.35491  1.000 25.53207 ? 244 GLN   A CG  1 
ATOM   1899 C CD  . GLN   A 1 244 ? -4.70105  -27.85926 21.82283  1.000 26.94223 ? 244 GLN   A CD  1 
ATOM   1900 O OE1 . GLN   A 1 244 ? -4.64803  -29.07161 21.62385  1.000 28.52357 ? 244 GLN   A OE1 1 
ATOM   1901 N NE2 . GLN   A 1 244 ? -5.72677  -27.27862 22.43510  1.000 30.14521 ? 244 GLN   A NE2 1 
ATOM   1902 N N   . ASP   A 1 245 ? -4.26442  -24.97123 17.95847  1.000 22.70883 ? 245 ASP   A N   1 
ATOM   1903 C CA  . ASP   A 1 245 ? -4.86082  -23.64658 17.82925  1.000 23.56335 ? 245 ASP   A CA  1 
ATOM   1904 C C   . ASP   A 1 245 ? -6.28561  -23.72872 17.29500  1.000 22.41857 ? 245 ASP   A C   1 
ATOM   1905 O O   . ASP   A 1 245 ? -7.15898  -22.98112 17.75064  1.000 22.43789 ? 245 ASP   A O   1 
ATOM   1906 C CB  . ASP   A 1 245 ? -4.02113  -22.73403 16.94092  1.000 22.52149 ? 245 ASP   A CB  1 
ATOM   1907 C CG  . ASP   A 1 245 ? -4.40818  -21.28364 17.10969  1.000 23.27585 ? 245 ASP   A CG  1 
ATOM   1908 O OD1 . ASP   A 1 245 ? -4.38321  -20.81430 18.26863  1.000 26.72616 ? 245 ASP   A OD1 1 
ATOM   1909 O OD2 . ASP   A 1 245 ? -4.77011  -20.62009 16.11611  1.000 27.24968 ? 245 ASP   A OD2 1 
ATOM   1910 N N   . HIS   A 1 246 ? -6.53745  -24.62283 16.32795  1.000 22.80853 ? 246 HIS   A N   1 
ATOM   1911 C CA  . HIS   A 1 246 ? -7.90862  -24.89301 15.89519  1.000 21.53863 ? 246 HIS   A CA  1 
ATOM   1912 C C   . HIS   A 1 246 ? -8.77772  -25.33900 17.06139  1.000 21.01701 ? 246 HIS   A C   1 
ATOM   1913 O O   . HIS   A 1 246 ? -9.93017  -24.91041 17.19191  1.000 22.38467 ? 246 HIS   A O   1 
ATOM   1914 C CB  . HIS   A 1 246 ? -7.93475  -25.96884 14.80760  1.000 22.10336 ? 246 HIS   A CB  1 
ATOM   1915 C CG  . HIS   A 1 246 ? -7.29270  -25.55742 13.52113  1.000 19.67243 ? 246 HIS   A CG  1 
ATOM   1916 N ND1 . HIS   A 1 246 ? -6.59135  -26.44106 12.72755  1.000 23.34474 ? 246 HIS   A ND1 1 
ATOM   1917 C CD2 . HIS   A 1 246 ? -7.23012  -24.35830 12.89700  1.000 23.90480 ? 246 HIS   A CD2 1 
ATOM   1918 C CE1 . HIS   A 1 246 ? -6.13811  -25.80641 11.65994  1.000 24.61665 ? 246 HIS   A CE1 1 
ATOM   1919 N NE2 . HIS   A 1 246 ? -6.51456  -24.54126 11.73629  1.000 23.26763 ? 246 HIS   A NE2 1 
ATOM   1920 N N   . VAL   A 1 247 ? -8.26515  -26.25166 17.88431  1.000 24.67141 ? 247 VAL   A N   1 
ATOM   1921 C CA  . VAL   A 1 247 ? -9.02119  -26.69776 19.05365  1.000 22.17168 ? 247 VAL   A CA  1 
ATOM   1922 C C   . VAL   A 1 247 ? -9.34533  -25.51202 19.95097  1.000 25.18552 ? 247 VAL   A C   1 
ATOM   1923 O O   . VAL   A 1 247 ? -10.48075 -25.36204 20.42972  1.000 23.26409 ? 247 VAL   A O   1 
ATOM   1924 C CB  . VAL   A 1 247 ? -8.24564  -27.79408 19.80808  1.000 25.69535 ? 247 VAL   A CB  1 
ATOM   1925 C CG1 . VAL   A 1 247 ? -8.95552  -28.15942 21.09810  1.000 26.77825 ? 247 VAL   A CG1 1 
ATOM   1926 C CG2 . VAL   A 1 247 ? -8.08853  -29.01811 18.92387  1.000 26.15827 ? 247 VAL   A CG2 1 
ATOM   1927 N N   . ASP   A 1 248 ? -8.35946  -24.64083 20.17698  1.000 22.16670 ? 248 ASP   A N   1 
ATOM   1928 C CA  . ASP   A 1 248 ? -8.58750  -23.47532 21.02204  1.000 27.30645 ? 248 ASP   A CA  1 
ATOM   1929 C C   . ASP   A 1 248 ? -9.62708  -22.54786 20.40500  1.000 23.64267 ? 248 ASP   A C   1 
ATOM   1930 O O   . ASP   A 1 248 ? -10.52392 -22.06131 21.10309  1.000 25.16751 ? 248 ASP   A O   1 
ATOM   1931 C CB  . ASP   A 1 248 ? -7.26828  -22.73269 21.26040  1.000 26.16414 ? 248 ASP   A CB  1 
ATOM   1932 C CG  . ASP   A 1 248 ? -6.26984  -23.55339 22.06081  1.000 26.07845 ? 248 ASP   A CG  1 
ATOM   1933 O OD1 . ASP   A 1 248 ? -6.69391  -24.48625 22.77751  1.000 26.56573 ? 248 ASP   A OD1 1 
ATOM   1934 O OD2 . ASP   A 1 248 ? -5.05114  -23.26549 21.97824  1.000 27.00871 ? 248 ASP   A OD2 1 
ATOM   1935 N N   . ILE   A 1 249 ? -9.53417  -22.30761 19.09145  1.000 19.81321 ? 249 ILE   A N   1 
ATOM   1936 C CA  . ILE   A 1 249 ? -10.49015 -21.43858 18.40916  1.000 21.94309 ? 249 ILE   A CA  1 
ATOM   1937 C C   . ILE   A 1 249 ? -11.90557 -21.99018 18.54474  1.000 21.87431 ? 249 ILE   A C   1 
ATOM   1938 O O   . ILE   A 1 249 ? -12.87636 -21.22852 18.64604  1.000 22.36963 ? 249 ILE   A O   1 
ATOM   1939 C CB  . ILE   A 1 249 ? -10.06796 -21.25885 16.93268  1.000 20.43764 ? 249 ILE   A CB  1 
ATOM   1940 C CG1 . ILE   A 1 249 ? -8.84983  -20.33555 16.84363  1.000 24.08440 ? 249 ILE   A CG1 1 
ATOM   1941 C CG2 . ILE   A 1 249 ? -11.20647 -20.73428 16.07770  1.000 22.46750 ? 249 ILE   A CG2 1 
ATOM   1942 C CD1 . ILE   A 1 249 ? -7.97471  -20.57950 15.59550  1.000 21.80520 ? 249 ILE   A CD1 1 
ATOM   1943 N N   . LEU   A 1 250 ? -12.04331 -23.31024 18.59959  1.000 20.95461 ? 250 LEU   A N   1 
ATOM   1944 C CA  . LEU   A 1 250 ? -13.34800 -23.94330 18.73589  1.000 23.78925 ? 250 LEU   A CA  1 
ATOM   1945 C C   . LEU   A 1 250 ? -13.85249 -23.98234 20.17740  1.000 21.25607 ? 250 LEU   A C   1 
ATOM   1946 O O   . LEU   A 1 250 ? -14.95526 -24.48880 20.41415  1.000 24.07482 ? 250 LEU   A O   1 
ATOM   1947 C CB  . LEU   A 1 250 ? -13.29338 -25.36033 18.16098  1.000 20.76944 ? 250 LEU   A CB  1 
ATOM   1948 C CG  . LEU   A 1 250 ? -13.08249 -25.49477 16.65317  1.000 18.23119 ? 250 LEU   A CG  1 
ATOM   1949 C CD1 . LEU   A 1 250 ? -12.84672 -26.96042 16.34034  1.000 17.42049 ? 250 LEU   A CD1 1 
ATOM   1950 C CD2 . LEU   A 1 250 ? -14.28882 -24.97361 15.89444  1.000 15.89312 ? 250 LEU   A CD2 1 
ATOM   1951 N N   . GLY   A 1 251 ? -13.08342 -23.46488 21.13804  1.000 22.65217 ? 251 GLY   A N   1 
ATOM   1952 C CA  . GLY   A 1 251 ? -13.46025 -23.45002 22.53724  1.000 22.60449 ? 251 GLY   A CA  1 
ATOM   1953 C C   . GLY   A 1 251 ? -14.83588 -22.87801 22.83987  1.000 24.84283 ? 251 GLY   A C   1 
ATOM   1954 O O   . GLY   A 1 251 ? -15.66861 -23.53467 23.47617  1.000 26.11060 ? 251 GLY   A O   1 
ATOM   1955 N N   . PRO   A 1 252 ? -15.09101 -21.62987 22.41941  1.000 26.42549 ? 252 PRO   A N   1 
ATOM   1956 C CA  . PRO   A 1 252 ? -16.40159 -21.01873 22.70618  1.000 27.14064 ? 252 PRO   A CA  1 
ATOM   1957 C C   . PRO   A 1 252 ? -17.57234 -21.84044 22.20665  1.000 24.48003 ? 252 PRO   A C   1 
ATOM   1958 O O   . PRO   A 1 252 ? -18.58629 -21.97228 22.90672  1.000 26.22444 ? 252 PRO   A O   1 
ATOM   1959 C CB  . PRO   A 1 252 ? -16.31656 -19.66633 21.98186  1.000 27.72084 ? 252 PRO   A CB  1 
ATOM   1960 C CG  . PRO   A 1 252 ? -14.86382 -19.34653 21.96910  1.000 27.18108 ? 252 PRO   A CG  1 
ATOM   1961 C CD  . PRO   A 1 252 ? -14.17595 -20.67245 21.76721  1.000 26.27626 ? 252 PRO   A CD  1 
ATOM   1962 N N   . LEU   A 1 253 ? -17.45660 -22.40121 21.00570  1.000 23.77034 ? 253 LEU   A N   1 
ATOM   1963 C CA  . LEU   A 1 253 ? -18.53028 -23.23159 20.47647  1.000 22.15344 ? 253 LEU   A CA  1 
ATOM   1964 C C   . LEU   A 1 253 ? -18.65496 -24.52508 21.26678  1.000 21.84028 ? 253 LEU   A C   1 
ATOM   1965 O O   . LEU   A 1 253 ? -19.76475 -24.95641 21.59782  1.000 23.42027 ? 253 LEU   A O   1 
ATOM   1966 C CB  . LEU   A 1 253 ? -18.26362 -23.52051 19.00971  1.000 18.71221 ? 253 LEU   A CB  1 
ATOM   1967 C CG  . LEU   A 1 253 ? -18.58903 -22.35457 18.08058  1.000 18.84493 ? 253 LEU   A CG  1 
ATOM   1968 C CD1 . LEU   A 1 253 ? -18.19895 -22.71258 16.66524  1.000 19.45222 ? 253 LEU   A CD1 1 
ATOM   1969 C CD2 . LEU   A 1 253 ? -20.07155 -22.01911 18.18082  1.000 21.27424 ? 253 LEU   A CD2 1 
ATOM   1970 N N   . SER   A 1 254 ? -17.52105 -25.15212 21.58226  1.000 20.63170 ? 254 SER   A N   1 
ATOM   1971 C CA  . SER   A 1 254 ? -17.52460 -26.30447 22.47161  1.000 23.30887 ? 254 SER   A CA  1 
ATOM   1972 C C   . SER   A 1 254 ? -18.20997 -25.97920 23.79341  1.000 25.20012 ? 254 SER   A C   1 
ATOM   1973 O O   . SER   A 1 254 ? -19.00674 -26.77559 24.30902  1.000 27.79017 ? 254 SER   A O   1 
ATOM   1974 C CB  . SER   A 1 254 ? -16.08400 -26.76117 22.70327  1.000 23.67640 ? 254 SER   A CB  1 
ATOM   1975 O OG  . SER   A 1 254 ? -16.00811 -27.76610 23.67855  1.000 26.84164 ? 254 SER   A OG  1 
ATOM   1976 N N   . ALA   A 1 255 ? -17.91483 -24.80737 24.35817  1.000 25.13191 ? 255 ALA   A N   1 
ATOM   1977 C CA  . ALA   A 1 255 ? -18.48220 -24.43947 25.65060  1.000 28.34591 ? 255 ALA   A CA  1 
ATOM   1978 C C   . ALA   A 1 255 ? -19.98336 -24.20442 25.55212  1.000 28.96027 ? 255 ALA   A C   1 
ATOM   1979 O O   . ALA   A 1 255 ? -20.74558 -24.62845 26.43175  1.000 28.46980 ? 255 ALA   A O   1 
ATOM   1980 C CB  . ALA   A 1 255 ? -17.78145 -23.19344 26.18796  1.000 30.06748 ? 255 ALA   A CB  1 
ATOM   1981 N N   . GLN   A 1 256 ? -20.42052 -23.52421 24.49058  1.000 26.10237 ? 256 GLN   A N   1 
ATOM   1982 C CA  . GLN   A 1 256 ? -21.83969 -23.23748 24.31680  1.000 27.99911 ? 256 GLN   A CA  1 
ATOM   1983 C C   . GLN   A 1 256 ? -22.65227 -24.51857 24.18282  1.000 28.58589 ? 256 GLN   A C   1 
ATOM   1984 O O   . GLN   A 1 256 ? -23.75155 -24.62918 24.74017  1.000 30.76459 ? 256 GLN   A O   1 
ATOM   1985 C CB  . GLN   A 1 256 ? -22.03599 -22.34233 23.09453  1.000 25.82090 ? 256 GLN   A CB  1 
ATOM   1986 C CG  . GLN   A 1 256 ? -23.48841 -22.13755 22.70118  1.000 26.74848 ? 256 GLN   A CG  1 
ATOM   1987 C CD  . GLN   A 1 256 ? -23.63977 -21.22785 21.50806  1.000 26.84676 ? 256 GLN   A CD  1 
ATOM   1988 O OE1 . GLN   A 1 256 ? -22.65596 -20.86618 20.86202  1.000 31.53253 ? 256 GLN   A OE1 1 
ATOM   1989 N NE2 . GLN   A 1 256 ? -24.87573 -20.86167 21.19420  1.000 30.49073 ? 256 GLN   A NE2 1 
ATOM   1990 N N   . THR   A 1 257 ? -22.12919 -25.49819 23.44813  1.000 26.93969 ? 257 THR   A N   1 
ATOM   1991 C CA  . THR   A 1 257 ? -22.83216 -26.75314 23.23228  1.000 24.84490 ? 257 THR   A CA  1 
ATOM   1992 C C   . THR   A 1 257 ? -22.53593 -27.79200 24.30032  1.000 26.11512 ? 257 THR   A C   1 
ATOM   1993 O O   . THR   A 1 257 ? -23.29382 -28.75688 24.43142  1.000 30.39123 ? 257 THR   A O   1 
ATOM   1994 C CB  . THR   A 1 257 ? -22.47117 -27.32320 21.86125  1.000 25.36963 ? 257 THR   A CB  1 
ATOM   1995 O OG1 . THR   A 1 257 ? -21.04994 -27.50922 21.77741  1.000 22.28703 ? 257 THR   A OG1 1 
ATOM   1996 C CG2 . THR   A 1 257 ? -22.88621 -26.34604 20.77322  1.000 21.60944 ? 257 THR   A CG2 1 
ATOM   1997 N N   . GLY   A 1 258 ? -21.46273 -27.62224 25.06449  1.000 26.88629 ? 258 GLY   A N   1 
ATOM   1998 C CA  . GLY   A 1 258 ? -21.07268 -28.64420 26.01154  1.000 27.25208 ? 258 GLY   A CA  1 
ATOM   1999 C C   . GLY   A 1 258 ? -20.51684 -29.90229 25.38862  1.000 27.44717 ? 258 GLY   A C   1 
ATOM   2000 O O   . GLY   A 1 258 ? -20.43551 -30.93385 26.06073  1.000 28.94156 ? 258 GLY   A O   1 
ATOM   2001 N N   . ILE   A 1 259 ? -20.13003 -29.85458 24.12289  1.000 23.94576 ? 259 ILE   A N   1 
ATOM   2002 C CA  . ILE   A 1 259 ? -19.54346 -30.99743 23.43603  1.000 25.07753 ? 259 ILE   A CA  1 
ATOM   2003 C C   . ILE   A 1 259 ? -18.05504 -30.71292 23.27250  1.000 24.49771 ? 259 ILE   A C   1 
ATOM   2004 O O   . ILE   A 1 259 ? -17.66843 -29.78718 22.54998  1.000 23.91567 ? 259 ILE   A O   1 
ATOM   2005 C CB  . ILE   A 1 259 ? -20.22524 -31.25626 22.08825  1.000 24.34565 ? 259 ILE   A CB  1 
ATOM   2006 C CG1 . ILE   A 1 259 ? -21.68987 -31.63016 22.31498  1.000 27.23765 ? 259 ILE   A CG1 1 
ATOM   2007 C CG2 . ILE   A 1 259 ? -19.50043 -32.35664 21.31753  1.000 25.86907 ? 259 ILE   A CG2 1 
ATOM   2008 C CD1 . ILE   A 1 259 ? -22.53429 -31.35772 21.12858  1.000 27.26441 ? 259 ILE   A CD1 1 
ATOM   2009 N N   . ALA   A 1 260 ? -17.22047 -31.48735 23.96673  1.000 24.16373 ? 260 ALA   A N   1 
ATOM   2010 C CA  . ALA   A 1 260 ? -15.77968 -31.28069 23.89646  1.000 25.17139 ? 260 ALA   A CA  1 
ATOM   2011 C C   . ALA   A 1 260 ? -15.31979 -31.31034 22.44620  1.000 24.21091 ? 260 ALA   A C   1 
ATOM   2012 O O   . ALA   A 1 260 ? -15.86819 -32.04642 21.62320  1.000 24.62174 ? 260 ALA   A O   1 
ATOM   2013 C CB  . ALA   A 1 260 ? -15.04604 -32.35025 24.71190  1.000 25.60006 ? 260 ALA   A CB  1 
ATOM   2014 N N   . VAL   A 1 261 ? -14.32338 -30.48352 22.12097  1.000 23.76993 ? 261 VAL   A N   1 
ATOM   2015 C CA  . VAL   A 1 261 ? -13.85187 -30.44578 20.74070  1.000 20.29361 ? 261 VAL   A CA  1 
ATOM   2016 C C   . VAL   A 1 261 ? -13.48062 -31.84801 20.28033  1.000 21.53177 ? 261 VAL   A C   1 
ATOM   2017 O O   . VAL   A 1 261 ? -13.93469 -32.31792 19.23041  1.000 22.31255 ? 261 VAL   A O   1 
ATOM   2018 C CB  . VAL   A 1 261 ? -12.67497 -29.46403 20.59101  1.000 23.78716 ? 261 VAL   A CB  1 
ATOM   2019 C CG1 . VAL   A 1 261 ? -12.03166 -29.62271 19.21072  1.000 20.03092 ? 261 VAL   A CG1 1 
ATOM   2020 C CG2 . VAL   A 1 261 ? -13.13844 -28.03227 20.80752  1.000 22.30397 ? 261 VAL   A CG2 1 
ATOM   2021 N N   . LEU   A 1 262 ? -12.71557 -32.56648 21.09633  1.000 22.51173 ? 262 LEU   A N   1 
ATOM   2022 C CA  . LEU   A 1 262 ? -12.28772 -33.89935 20.70401  1.000 25.05027 ? 262 LEU   A CA  1 
ATOM   2023 C C   . LEU   A 1 262 ? -13.45725 -34.87637 20.59782  1.000 24.79906 ? 262 LEU   A C   1 
ATOM   2024 O O   . LEU   A 1 262 ? -13.35701 -35.86309 19.85871  1.000 25.58453 ? 262 LEU   A O   1 
ATOM   2025 C CB  . LEU   A 1 262 ? -11.24700 -34.41697 21.69236  1.000 28.38120 ? 262 LEU   A CB  1 
ATOM   2026 C CG  . LEU   A 1 262 ? -9.83223  -33.86663 21.44464  1.000 25.02144 ? 262 LEU   A CG  1 
ATOM   2027 C CD1 . LEU   A 1 262 ? -8.86351  -34.52856 22.40937  1.000 32.24161 ? 262 LEU   A CD1 1 
ATOM   2028 C CD2 . LEU   A 1 262 ? -9.37653  -34.00406 19.99871  1.000 27.81566 ? 262 LEU   A CD2 1 
ATOM   2029 N N   . ASP   A 1 263 ? -14.56216 -34.63652 21.31110  1.000 24.37064 ? 263 ASP   A N   1 
ATOM   2030 C CA  . ASP   A 1 263 ? -15.74606 -35.46290 21.08456  1.000 24.44756 ? 263 ASP   A CA  1 
ATOM   2031 C C   . ASP   A 1 263 ? -16.32837 -35.19135 19.70504  1.000 22.56455 ? 263 ASP   A C   1 
ATOM   2032 O O   . ASP   A 1 263 ? -16.72327 -36.11880 18.98663  1.000 22.76884 ? 263 ASP   A O   1 
ATOM   2033 C CB  . ASP   A 1 263 ? -16.81692 -35.21054 22.15357  1.000 24.85354 ? 263 ASP   A CB  1 
ATOM   2034 C CG  . ASP   A 1 263 ? -16.43382 -35.75043 23.52805  1.000 30.89163 ? 263 ASP   A CG  1 
ATOM   2035 O OD1 . ASP   A 1 263 ? -15.30298 -36.24784 23.69752  1.000 29.21139 ? 263 ASP   A OD1 1 
ATOM   2036 O OD2 . ASP   A 1 263 ? -17.29247 -35.70230 24.43763  1.000 28.60232 ? 263 ASP   A OD2 1 
ATOM   2037 N N   . MET   A 1 264 ? -16.38294 -33.92102 19.31650  1.000 22.06807 ? 264 MET   A N   1 
ATOM   2038 C CA  . MET   A 1 264 ? -16.89547 -33.59174 17.99669  1.000 19.88109 ? 264 MET   A CA  1 
ATOM   2039 C C   . MET   A 1 264 ? -15.98012 -34.15512 16.91338  1.000 20.67143 ? 264 MET   A C   1 
ATOM   2040 O O   . MET   A 1 264 ? -16.45357 -34.53493 15.83686  1.000 21.57967 ? 264 MET   A O   1 
ATOM   2041 C CB  . MET   A 1 264 ? -17.04884 -32.07329 17.86430  1.000 18.67456 ? 264 MET   A CB  1 
ATOM   2042 C CG  . MET   A 1 264 ? -17.81363 -31.64231 16.63303  1.000 17.50026 ? 264 MET   A CG  1 
ATOM   2043 S SD  . MET   A 1 264 ? -19.53732 -32.21951 16.74285  1.000 19.52007 ? 264 MET   A SD  1 
ATOM   2044 C CE  . MET   A 1 264 ? -20.31284 -30.81102 17.54588  1.000 18.02584 ? 264 MET   A CE  1 
ATOM   2045 N N   . CYS   A 1 265 ? -14.67398 -34.23181 17.18716  1.000 21.44795 ? 265 CYS   A N   1 
ATOM   2046 C CA  . CYS   A 1 265 ? -13.75388 -34.90174 16.26962  1.000 23.46237 ? 265 CYS   A CA  1 
ATOM   2047 C C   . CYS   A 1 265 ? -14.11414 -36.37156 16.10065  1.000 24.87311 ? 265 CYS   A C   1 
ATOM   2048 O O   . CYS   A 1 265 ? -14.13965 -36.88695 14.97714  1.000 22.19266 ? 265 CYS   A O   1 
ATOM   2049 C CB  . CYS   A 1 265 ? -12.31538 -34.76618 16.76810  1.000 22.69172 ? 265 CYS   A CB  1 
ATOM   2050 S SG  . CYS   A 1 265 ? -11.61979 -33.11764 16.58358  1.000 21.77167 ? 265 CYS   A SG  1 
ATOM   2051 N N   . ALA   A 1 266 ? -14.38576 -37.06664 17.21380  1.000 23.49492 ? 266 ALA   A N   1 
ATOM   2052 C CA  . ALA   A 1 266 ? -14.85802 -38.44422 17.13211  1.000 23.67073 ? 266 ALA   A CA  1 
ATOM   2053 C C   . ALA   A 1 266 ? -16.09135 -38.55058 16.24252  1.000 25.70709 ? 266 ALA   A C   1 
ATOM   2054 O O   . ALA   A 1 266 ? -16.18393 -39.45649 15.40585  1.000 26.17233 ? 266 ALA   A O   1 
ATOM   2055 C CB  . ALA   A 1 266 ? -15.15376 -38.98953 18.53180  1.000 27.58398 ? 266 ALA   A CB  1 
ATOM   2056 N N   . SER   A 1 267 ? -17.04057 -37.61607 16.39383  1.000 25.03852 ? 267 SER   A N   1 
ATOM   2057 C CA  . SER   A 1 267 ? -18.24248 -37.62043 15.56243  1.000 23.19864 ? 267 SER   A CA  1 
ATOM   2058 C C   . SER   A 1 267 ? -17.89429 -37.42999 14.09434  1.000 24.07431 ? 267 SER   A C   1 
ATOM   2059 O O   . SER   A 1 267 ? -18.42682 -38.12293 13.21783  1.000 23.91239 ? 267 SER   A O   1 
ATOM   2060 C CB  . SER   A 1 267 ? -19.19966 -36.52448 16.02928  1.000 24.09331 ? 267 SER   A CB  1 
ATOM   2061 O OG  . SER   A 1 267 ? -19.70969 -36.84231 17.30546  1.000 26.99441 ? 267 SER   A OG  1 
ATOM   2062 N N   . LEU   A 1 268 ? -17.01288 -36.47282 13.80643  1.000 21.82245 ? 268 LEU   A N   1 
ATOM   2063 C CA  . LEU   A 1 268 ? -16.55630 -36.28233 12.43542  1.000 20.72868 ? 268 LEU   A CA  1 
ATOM   2064 C C   . LEU   A 1 268 ? -15.87105 -37.53395 11.90132  1.000 21.63967 ? 268 LEU   A C   1 
ATOM   2065 O O   . LEU   A 1 268 ? -16.07444 -37.90609 10.74128  1.000 22.65391 ? 268 LEU   A O   1 
ATOM   2066 C CB  . LEU   A 1 268 ? -15.63899 -35.06094 12.35419  1.000 21.40661 ? 268 LEU   A CB  1 
ATOM   2067 C CG  . LEU   A 1 268 ? -15.07592 -34.70139 10.97776  1.000 16.62796 ? 268 LEU   A CG  1 
ATOM   2068 C CD1 . LEU   A 1 268 ? -16.17205 -34.53237 9.93220   1.000 17.49208 ? 268 LEU   A CD1 1 
ATOM   2069 C CD2 . LEU   A 1 268 ? -14.26344 -33.40717 11.07058  1.000 17.78821 ? 268 LEU   A CD2 1 
ATOM   2070 N N   . LYS   A 1 269 ? -15.08354 -38.21567 12.74043  1.000 22.20568 ? 269 LYS   A N   1 
ATOM   2071 C CA  . LYS   A 1 269 ? -14.45425 -39.46522 12.32123  1.000 23.27546 ? 269 LYS   A CA  1 
ATOM   2072 C C   . LYS   A 1 269 ? -15.49499 -40.47311 11.85569  1.000 25.07066 ? 269 LYS   A C   1 
ATOM   2073 O O   . LYS   A 1 269 ? -15.35723 -41.08046 10.78761  1.000 24.21847 ? 269 LYS   A O   1 
ATOM   2074 C CB  . LYS   A 1 269 ? -13.63279 -40.04084 13.47199  1.000 26.08548 ? 269 LYS   A CB  1 
ATOM   2075 C CG  . LYS   A 1 269 ? -13.02283 -41.39742 13.20232  1.000 29.32739 ? 269 LYS   A CG  1 
ATOM   2076 C CD  . LYS   A 1 269 ? -11.98854 -41.73774 14.26931  1.000 29.68912 ? 269 LYS   A CD  1 
ATOM   2077 C CE  . LYS   A 1 269 ? -11.69485 -43.23130 14.26992  1.000 36.09030 ? 269 LYS   A CE  1 
ATOM   2078 N NZ  . LYS   A 1 269 ? -10.95100 -43.65105 15.48609  1.000 36.52685 ? 269 LYS   A NZ  1 
ATOM   2079 N N   . GLU   A 1 270 ? -16.55421 -40.66047 12.65106  1.000 27.52831 ? 270 GLU   A N   1 
ATOM   2080 C CA  . GLU   A 1 270 ? -17.60953 -41.59611 12.27199  1.000 26.63745 ? 270 GLU   A CA  1 
ATOM   2081 C C   . GLU   A 1 270 ? -18.32619 -41.15313 11.00687  1.000 25.74140 ? 270 GLU   A C   1 
ATOM   2082 O O   . GLU   A 1 270 ? -18.66099 -41.98689 10.15862  1.000 30.30301 ? 270 GLU   A O   1 
ATOM   2083 C CB  . GLU   A 1 270 ? -18.59919 -41.77445 13.42389  1.000 27.11272 ? 270 GLU   A CB  1 
ATOM   2084 C CG  . GLU   A 1 270 ? -17.90303 -42.22097 14.68135  1.000 29.03888 ? 270 GLU   A CG  1 
ATOM   2085 C CD  . GLU   A 1 270 ? -17.35678 -43.62425 14.53803  1.000 31.82685 ? 270 GLU   A CD  1 
ATOM   2086 O OE1 . GLU   A 1 270 ? -18.08934 -44.48496 14.00459  1.000 37.43584 ? 270 GLU   A OE1 1 
ATOM   2087 O OE2 . GLU   A 1 270 ? -16.18049 -43.85431 14.90588  1.000 37.71306 ? 270 GLU   A OE2 1 
ATOM   2088 N N   . LEU   A 1 271 ? -18.56571 -39.84736 10.85319  1.000 23.90736 ? 271 LEU   A N   1 
ATOM   2089 C CA  . LEU   A 1 271 ? -19.21639 -39.36891 9.63589   1.000 24.96287 ? 271 LEU   A CA  1 
ATOM   2090 C C   . LEU   A 1 271 ? -18.34415 -39.61776 8.41441   1.000 25.87627 ? 271 LEU   A C   1 
ATOM   2091 O O   . LEU   A 1 271 ? -18.85080 -39.94119 7.33337   1.000 26.90053 ? 271 LEU   A O   1 
ATOM   2092 C CB  . LEU   A 1 271 ? -19.54956 -37.88455 9.76016   1.000 24.27099 ? 271 LEU   A CB  1 
ATOM   2093 C CG  . LEU   A 1 271 ? -20.67193 -37.53998 10.73470  1.000 23.80251 ? 271 LEU   A CG  1 
ATOM   2094 C CD1 . LEU   A 1 271 ? -20.65127 -36.04488 11.01911  1.000 18.51326 ? 271 LEU   A CD1 1 
ATOM   2095 C CD2 . LEU   A 1 271 ? -22.00169 -37.97102 10.14813  1.000 24.32360 ? 271 LEU   A CD2 1 
ATOM   2096 N N   . LEU   A 1 272 ? -17.02584 -39.48511 8.57466   1.000 24.51945 ? 272 LEU   A N   1 
ATOM   2097 C CA  . LEU   A 1 272 ? -16.10937 -39.73904 7.47029   1.000 25.85837 ? 272 LEU   A CA  1 
ATOM   2098 C C   . LEU   A 1 272 ? -16.07646 -41.21972 7.11101   1.000 26.97877 ? 272 LEU   A C   1 
ATOM   2099 O O   . LEU   A 1 272 ? -16.08026 -41.57641 5.92726   1.000 28.77975 ? 272 LEU   A O   1 
ATOM   2100 C CB  . LEU   A 1 272 ? -14.71635 -39.23861 7.84141   1.000 23.83341 ? 272 LEU   A CB  1 
ATOM   2101 C CG  . LEU   A 1 272 ? -14.56276 -37.72167 7.82765   1.000 22.99212 ? 272 LEU   A CG  1 
ATOM   2102 C CD1 . LEU   A 1 272 ? -13.20015 -37.33045 8.37050   1.000 25.02642 ? 272 LEU   A CD1 1 
ATOM   2103 C CD2 . LEU   A 1 272 ? -14.75753 -37.17627 6.41707   1.000 21.77472 ? 272 LEU   A CD2 1 
ATOM   2104 N N   . GLN   A 1 273 ? -16.06713 -42.09748 8.11659   1.000 28.18772 ? 273 GLN   A N   1 
ATOM   2105 C CA  . GLN   A 1 273 ? -15.93833 -43.52720 7.86001   1.000 30.24627 ? 273 GLN   A CA  1 
ATOM   2106 C C   . GLN   A 1 273 ? -17.25960 -44.17063 7.47551   1.000 30.27828 ? 273 GLN   A C   1 
ATOM   2107 O O   . GLN   A 1 273 ? -17.25716 -45.19477 6.78878   1.000 30.91797 ? 273 GLN   A O   1 
ATOM   2108 C CB  . GLN   A 1 273 ? -15.37770 -44.24395 9.09017   1.000 29.41350 ? 273 GLN   A CB  1 
ATOM   2109 C CG  . GLN   A 1 273 ? -13.92464 -43.93684 9.37491   1.000 31.77356 ? 273 GLN   A CG  1 
ATOM   2110 C CD  . GLN   A 1 273 ? -13.47438 -44.45933 10.72032  1.000 32.24629 ? 273 GLN   A CD  1 
ATOM   2111 O OE1 . GLN   A 1 273 ? -14.28956 -44.87312 11.54994  1.000 38.00150 ? 273 GLN   A OE1 1 
ATOM   2112 N NE2 . GLN   A 1 273 ? -12.16994 -44.41908 10.95872  1.000 35.07721 ? 273 GLN   A NE2 1 
ATOM   2113 N N   . ASN   A 1 274 ? -18.38288 -43.58734 7.88852   1.000 29.64238 ? 274 ASN   A N   1 
ATOM   2114 C CA  . ASN   A 1 274 ? -19.68402 -44.21017 7.71452   1.000 32.01851 ? 274 ASN   A CA  1 
ATOM   2115 C C   . ASN   A 1 274 ? -20.56848 -43.49477 6.70716   1.000 29.79664 ? 274 ASN   A C   1 
ATOM   2116 O O   . ASN   A 1 274 ? -21.52576 -44.09713 6.21356   1.000 32.33931 ? 274 ASN   A O   1 
ATOM   2117 C CB  . ASN   A 1 274 ? -20.42503 -44.24848 9.05793   1.000 33.67376 ? 274 ASN   A CB  1 
ATOM   2118 C CG  . ASN   A 1 274 ? -19.70338 -45.08284 10.09245  1.000 38.53257 ? 274 ASN   A CG  1 
ATOM   2119 O OD1 . ASN   A 1 274 ? -18.91013 -45.96660 9.75681   1.000 39.23228 ? 274 ASN   A OD1 1 
ATOM   2120 N ND2 . ASN   A 1 274 ? -19.95408 -44.78756 11.36694  1.000 38.42575 ? 274 ASN   A ND2 1 
ATOM   2121 N N   . GLY   A 1 275 ? -20.27931 -42.24057 6.39411   1.000 31.09434 ? 275 GLY   A N   1 
ATOM   2122 C CA  . GLY   A 1 275 ? -21.23920 -41.43111 5.68621   1.000 30.04550 ? 275 GLY   A CA  1 
ATOM   2123 C C   . GLY   A 1 275 ? -22.36172 -41.00452 6.62458   1.000 33.06805 ? 275 GLY   A C   1 
ATOM   2124 O O   . GLY   A 1 275 ? -22.27036 -41.09324 7.84662   1.000 34.43695 ? 275 GLY   A O   1 
ATOM   2125 N N   . MET   A 1 276 ? -23.44508 -40.53212 6.01883   1.000 34.73487 ? 276 MET   A N   1 
ATOM   2126 C CA  . MET   A 1 276 ? -24.57620 -40.02848 6.78392   1.000 34.05316 ? 276 MET   A CA  1 
ATOM   2127 C C   . MET   A 1 276 ? -25.75365 -40.99102 6.83965   1.000 37.75861 ? 276 MET   A C   1 
ATOM   2128 O O   . MET   A 1 276 ? -26.65807 -40.78609 7.65802   1.000 37.62869 ? 276 MET   A O   1 
ATOM   2129 C CB  . MET   A 1 276 ? -25.03827 -38.68101 6.22098   1.000 35.04363 ? 276 MET   A CB  1 
ATOM   2130 C CG  . MET   A 1 276 ? -23.96439 -37.61190 6.25924   1.000 33.67538 ? 276 MET   A CG  1 
ATOM   2131 S SD  . MET   A 1 276 ? -24.71302 -35.98206 6.13197   1.000 33.39685 ? 276 MET   A SD  1 
ATOM   2132 C CE  . MET   A 1 276 ? -23.27815 -34.97931 5.79557   1.000 24.05090 ? 276 MET   A CE  1 
ATOM   2133 N N   . ASN   A 1 277 ? -25.75384 -42.03877 6.01565   1.000 37.53352 ? 277 ASN   A N   1 
ATOM   2134 C CA  . ASN   A 1 277 ? -26.82309 -43.03038 6.00637   1.000 39.23257 ? 277 ASN   A CA  1 
ATOM   2135 C C   . ASN   A 1 277 ? -28.17622 -42.37937 5.72701   1.000 38.87124 ? 277 ASN   A C   1 
ATOM   2136 O O   . ASN   A 1 277 ? -29.17308 -42.63756 6.40941   1.000 39.73677 ? 277 ASN   A O   1 
ATOM   2137 C CB  . ASN   A 1 277 ? -26.85754 -43.81890 7.31562   1.000 40.43044 ? 277 ASN   A CB  1 
ATOM   2138 C CG  . ASN   A 1 277 ? -27.71873 -45.05237 7.21942   1.000 45.38467 ? 277 ASN   A CG  1 
ATOM   2139 O OD1 . ASN   A 1 277 ? -27.86852 -45.63515 6.14154   1.000 48.47052 ? 277 ASN   A OD1 1 
ATOM   2140 N ND2 . ASN   A 1 277 ? -28.32539 -45.44188 8.33920   1.000 48.56590 ? 277 ASN   A ND2 1 
ATOM   2141 N N   . GLY   A 1 278 ? -28.20650 -41.52747 4.70661   1.000 37.64715 ? 278 GLY   A N   1 
ATOM   2142 C CA  . GLY   A 1 278 ? -29.45529 -40.95428 4.25226   1.000 34.02131 ? 278 GLY   A CA  1 
ATOM   2143 C C   . GLY   A 1 278 ? -29.94807 -39.76923 5.04737   1.000 37.44836 ? 278 GLY   A C   1 
ATOM   2144 O O   . GLY   A 1 278 ? -31.06569 -39.30122 4.80477   1.000 36.65021 ? 278 GLY   A O   1 
ATOM   2145 N N   . ARG   A 1 279 ? -29.15562 -39.25995 5.97958   1.000 36.32217 ? 279 ARG   A N   1 
ATOM   2146 C CA  . ARG   A 1 279 ? -29.56774 -38.13725 6.80206   1.000 30.55743 ? 279 ARG   A CA  1 
ATOM   2147 C C   . ARG   A 1 279 ? -28.86809 -36.87274 6.32958   1.000 29.60918 ? 279 ARG   A C   1 
ATOM   2148 O O   . ARG   A 1 279 ? -27.93695 -36.90779 5.52129   1.000 28.87695 ? 279 ARG   A O   1 
ATOM   2149 C CB  . ARG   A 1 279 ? -29.25619 -38.42244 8.27143   1.000 30.30528 ? 279 ARG   A CB  1 
ATOM   2150 C CG  . ARG   A 1 279 ? -30.18332 -39.46519 8.85576   1.000 32.49250 ? 279 ARG   A CG  1 
ATOM   2151 C CD  . ARG   A 1 279 ? -29.71452 -39.87523 10.22281  1.000 33.27335 ? 279 ARG   A CD  1 
ATOM   2152 N NE  . ARG   A 1 279 ? -28.45835 -40.61773 10.14490  1.000 35.48259 ? 279 ARG   A NE  1 
ATOM   2153 C CZ  . ARG   A 1 279 ? -27.97654 -41.37551 11.12354  1.000 34.29164 ? 279 ARG   A CZ  1 
ATOM   2154 N NH1 . ARG   A 1 279 ? -28.66231 -41.51280 12.25821  1.000 32.41459 ? 279 ARG   A NH1 1 
ATOM   2155 N NH2 . ARG   A 1 279 ? -26.80945 -41.99255 10.96668  1.000 33.36251 ? 279 ARG   A NH2 1 
ATOM   2156 N N   . THR   A 1 280 ? -29.33254 -35.73827 6.83713   1.000 27.68074 ? 280 THR   A N   1 
ATOM   2157 C CA  . THR   A 1 280 ? -28.74250 -34.46306 6.47828   1.000 24.70983 ? 280 THR   A CA  1 
ATOM   2158 C C   . THR   A 1 280 ? -28.34761 -33.71727 7.74201   1.000 22.14100 ? 280 THR   A C   1 
ATOM   2159 O O   . THR   A 1 280 ? -28.81595 -34.01155 8.84475   1.000 21.57579 ? 280 THR   A O   1 
ATOM   2160 C CB  . THR   A 1 280 ? -29.69295 -33.59638 5.63654   1.000 24.43880 ? 280 THR   A CB  1 
ATOM   2161 O OG1 . THR   A 1 280 ? -30.92950 -33.41493 6.33240   1.000 23.50960 ? 280 THR   A OG1 1 
ATOM   2162 C CG2 . THR   A 1 280 ? -29.98007 -34.27889 4.30561   1.000 25.94089 ? 280 THR   A CG2 1 
ATOM   2163 N N   . ILE   A 1 281 ? -27.45243 -32.75908 7.55768   1.000 18.55764 ? 281 ILE   A N   1 
ATOM   2164 C CA  . ILE   A 1 281 ? -27.00960 -31.84948 8.60182   1.000 18.95491 ? 281 ILE   A CA  1 
ATOM   2165 C C   . ILE   A 1 281 ? -27.17924 -30.43438 8.08155   1.000 19.20832 ? 281 ILE   A C   1 
ATOM   2166 O O   . ILE   A 1 281 ? -26.56877 -30.06656 7.07195   1.000 17.79722 ? 281 ILE   A O   1 
ATOM   2167 C CB  . ILE   A 1 281 ? -25.54776 -32.10028 9.00187   1.000 18.96886 ? 281 ILE   A CB  1 
ATOM   2168 C CG1 . ILE   A 1 281 ? -25.32783 -33.56776 9.39367   1.000 17.43147 ? 281 ILE   A CG1 1 
ATOM   2169 C CG2 . ILE   A 1 281 ? -25.12482 -31.10992 10.06307  1.000 16.86196 ? 281 ILE   A CG2 1 
ATOM   2170 C CD1 . ILE   A 1 281 ? -23.88744 -33.88402 9.86610   1.000 19.63222 ? 281 ILE   A CD1 1 
ATOM   2171 N N   . LEU   A 1 282 ? -27.98693 -29.63522 8.77737   1.000 19.63647 ? 282 LEU   A N   1 
ATOM   2172 C CA  . LEU   A 1 282 ? -28.27262 -28.26296 8.36518   1.000 20.09640 ? 282 LEU   A CA  1 
ATOM   2173 C C   . LEU   A 1 282 ? -28.65452 -28.21642 6.88559   1.000 20.75262 ? 282 LEU   A C   1 
ATOM   2174 O O   . LEU   A 1 282 ? -28.17038 -27.37976 6.11353   1.000 22.72362 ? 282 LEU   A O   1 
ATOM   2175 C CB  . LEU   A 1 282 ? -27.09243 -27.33107 8.66830   1.000 17.14760 ? 282 LEU   A CB  1 
ATOM   2176 C CG  . LEU   A 1 282 ? -26.93252 -26.99752 10.15545  1.000 17.47523 ? 282 LEU   A CG  1 
ATOM   2177 C CD1 . LEU   A 1 282 ? -25.66521 -26.16668 10.41018  1.000 18.19942 ? 282 LEU   A CD1 1 
ATOM   2178 C CD2 . LEU   A 1 282 ? -28.18238 -26.33949 10.75240  1.000 19.41602 ? 282 LEU   A CD2 1 
ATOM   2179 N N   . GLY   A 1 283 ? -29.51851 -29.15583 6.49044   1.000 21.30821 ? 283 GLY   A N   1 
ATOM   2180 C CA  . GLY   A 1 283 ? -30.01274 -29.21139 5.12824   1.000 24.91435 ? 283 GLY   A CA  1 
ATOM   2181 C C   . GLY   A 1 283 ? -28.99973 -29.63999 4.08948   1.000 25.34980 ? 283 GLY   A C   1 
ATOM   2182 O O   . GLY   A 1 283 ? -29.23638 -29.45401 2.89281   1.000 24.68237 ? 283 GLY   A O   1 
ATOM   2183 N N   . SER   A 1 284 ? -27.87893 -30.22515 4.50259   1.000 22.17293 ? 284 SER   A N   1 
ATOM   2184 C CA  . SER   A 1 284 ? -26.85837 -30.66912 3.56532   1.000 19.85585 ? 284 SER   A CA  1 
ATOM   2185 C C   . SER   A 1 284 ? -26.59999 -32.15642 3.74521   1.000 21.22673 ? 284 SER   A C   1 
ATOM   2186 O O   . SER   A 1 284 ? -26.59331 -32.66539 4.87093   1.000 18.58382 ? 284 SER   A O   1 
ATOM   2187 C CB  . SER   A 1 284 ? -25.55537 -29.88212 3.74873   1.000 20.48055 ? 284 SER   A CB  1 
ATOM   2188 O OG  . SER   A 1 284 ? -24.55442 -30.36818 2.86601   1.000 19.94235 ? 284 SER   A OG  1 
ATOM   2189 N N   . ALA   A 1 285 ? -26.40995 -32.85276 2.62789   1.000 21.42566 ? 285 ALA   A N   1 
ATOM   2190 C CA  . ALA   A 1 285 ? -26.00155 -34.24504 2.63385   1.000 20.52613 ? 285 ALA   A CA  1 
ATOM   2191 C C   . ALA   A 1 285 ? -24.48862 -34.39795 2.52663   1.000 22.70625 ? 285 ALA   A C   1 
ATOM   2192 O O   . ALA   A 1 285 ? -24.00131 -35.52017 2.36504   1.000 23.30889 ? 285 ALA   A O   1 
ATOM   2193 C CB  . ALA   A 1 285 ? -26.68264 -35.00161 1.49734   1.000 24.38689 ? 285 ALA   A CB  1 
ATOM   2194 N N   . LEU   A 1 286 ? -23.75124 -33.29528 2.60822   1.000 18.37430 ? 286 LEU   A N   1 
ATOM   2195 C CA  . LEU   A 1 286 ? -22.29615 -33.28210 2.55812   1.000 22.98913 ? 286 LEU   A CA  1 
ATOM   2196 C C   . LEU   A 1 286 ? -21.76198 -32.55901 3.78631   1.000 21.25797 ? 286 LEU   A C   1 
ATOM   2197 O O   . LEU   A 1 286 ? -22.44512 -31.70948 4.36202   1.000 18.84107 ? 286 LEU   A O   1 
ATOM   2198 C CB  . LEU   A 1 286 ? -21.78772 -32.56199 1.30435   1.000 22.57562 ? 286 LEU   A CB  1 
ATOM   2199 C CG  . LEU   A 1 286 ? -21.97382 -33.20185 -0.06169  1.000 24.17693 ? 286 LEU   A CG  1 
ATOM   2200 C CD1 . LEU   A 1 286 ? -21.23665 -32.37932 -1.09880  1.000 24.92075 ? 286 LEU   A CD1 1 
ATOM   2201 C CD2 . LEU   A 1 286 ? -21.47057 -34.65049 -0.04419  1.000 28.44623 ? 286 LEU   A CD2 1 
ATOM   2202 N N   . LEU   A 1 287 ? -20.53303 -32.88925 4.18460   1.000 19.95998 ? 287 LEU   A N   1 
ATOM   2203 C CA  . LEU   A 1 287 ? -19.86750 -32.13609 5.24502   1.000 18.23168 ? 287 LEU   A CA  1 
ATOM   2204 C C   . LEU   A 1 287 ? -19.38943 -30.79825 4.68184   1.000 18.51677 ? 287 LEU   A C   1 
ATOM   2205 O O   . LEU   A 1 287 ? -18.54231 -30.76508 3.78641   1.000 20.59014 ? 287 LEU   A O   1 
ATOM   2206 C CB  . LEU   A 1 287 ? -18.71189 -32.95253 5.83110   1.000 17.41350 ? 287 LEU   A CB  1 
ATOM   2207 C CG  . LEU   A 1 287 ? -19.18567 -34.31087 6.36480   1.000 19.87605 ? 287 LEU   A CG  1 
ATOM   2208 C CD1 . LEU   A 1 287 ? -18.04540 -35.21981 6.82613   1.000 22.18693 ? 287 LEU   A CD1 1 
ATOM   2209 C CD2 . LEU   A 1 287 ? -20.18307 -34.10391 7.47941   1.000 19.80832 ? 287 LEU   A CD2 1 
ATOM   2210 N N   . GLU   A 1 288 ? -19.93842 -29.69844 5.19983   1.000 15.04628 ? 288 GLU   A N   1 
ATOM   2211 C CA  . GLU   A 1 288 ? -19.68532 -28.34743 4.70303   1.000 15.76239 ? 288 GLU   A CA  1 
ATOM   2212 C C   . GLU   A 1 288 ? -18.45613 -27.73681 5.34914   1.000 13.01183 ? 288 GLU   A C   1 
ATOM   2213 O O   . GLU   A 1 288 ? -18.34247 -27.70956 6.57764   1.000 14.08279 ? 288 GLU   A O   1 
ATOM   2214 C CB  . GLU   A 1 288 ? -20.88299 -27.44244 4.98912   1.000 17.71150 ? 288 GLU   A CB  1 
ATOM   2215 C CG  . GLU   A 1 288 ? -22.18196 -27.93315 4.35515   1.000 18.98802 ? 288 GLU   A CG  1 
ATOM   2216 C CD  . GLU   A 1 288 ? -22.15833 -27.84662 2.83652   1.000 27.07436 ? 288 GLU   A CD  1 
ATOM   2217 O OE1 . GLU   A 1 288 ? -23.07644 -28.40550 2.19269   1.000 29.37255 ? 288 GLU   A OE1 1 
ATOM   2218 O OE2 . GLU   A 1 288 ? -21.26811 -27.15378 2.28752   1.000 26.24016 ? 288 GLU   A OE2 1 
ATOM   2219 N N   . ASP   A 1 289 ? -17.55981 -27.18523 4.52805   1.000 14.66985 ? 289 ASP   A N   1 
ATOM   2220 C CA  . ASP   A 1 289 ? -16.32465 -26.65731 5.08793   1.000 13.24563 ? 289 ASP   A CA  1 
ATOM   2221 C C   . ASP   A 1 289 ? -16.10035 -25.17770 4.76777   1.000 15.09204 ? 289 ASP   A C   1 
ATOM   2222 O O   . ASP   A 1 289 ? -14.97186 -24.70069 4.90680   1.000 13.35608 ? 289 ASP   A O   1 
ATOM   2223 C CB  . ASP   A 1 289 ? -15.13067 -27.50723 4.63166   1.000 12.32233 ? 289 ASP   A CB  1 
ATOM   2224 C CG  . ASP   A 1 289 ? -14.63912 -27.17651 3.20467   1.000 15.77270 ? 289 ASP   A CG  1 
ATOM   2225 O OD1 . ASP   A 1 289 ? -15.39487 -26.60431 2.39199   1.000 13.91343 ? 289 ASP   A OD1 1 
ATOM   2226 O OD2 . ASP   A 1 289 ? -13.46955 -27.54297 2.90732   1.000 13.36656 ? 289 ASP   A OD2 1 
ATOM   2227 N N   . GLU   A 1 290 ? -17.14012 -24.42645 4.36547   1.000 12.39907 ? 290 GLU   A N   1 
ATOM   2228 C CA  . GLU   A 1 290 ? -16.94812 -23.01738 4.04533   1.000 14.79452 ? 290 GLU   A CA  1 
ATOM   2229 C C   . GLU   A 1 290 ? -17.61401 -22.07686 5.04184   1.000 13.88765 ? 290 GLU   A C   1 
ATOM   2230 O O   . GLU   A 1 290 ? -17.93625 -20.94150 4.69513   1.000 13.68378 ? 290 GLU   A O   1 
ATOM   2231 C CB  . GLU   A 1 290 ? -17.38177 -22.69144 2.61160   1.000 16.38681 ? 290 GLU   A CB  1 
ATOM   2232 C CG  . GLU   A 1 290 ? -16.52443 -23.45438 1.57826   1.000 14.80596 ? 290 GLU   A CG  1 
ATOM   2233 C CD  . GLU   A 1 290 ? -16.39897 -22.77081 0.20957   1.000 20.66228 ? 290 GLU   A CD  1 
ATOM   2234 O OE1 . GLU   A 1 290 ? -17.15779 -21.80973 -0.08056  1.000 16.06992 ? 290 GLU   A OE1 1 
ATOM   2235 O OE2 . GLU   A 1 290 ? -15.54524 -23.24029 -0.59737  1.000 17.83646 ? 290 GLU   A OE2 1 
ATOM   2236 N N   . PHE   A 1 291 ? -17.74355 -22.50403 6.29873   1.000 14.28415 ? 291 PHE   A N   1 
ATOM   2237 C CA  . PHE   A 1 291 ? -18.11029 -21.62625 7.40856   1.000 13.37613 ? 291 PHE   A CA  1 
ATOM   2238 C C   . PHE   A 1 291 ? -16.99250 -21.65448 8.44534   1.000 12.99719 ? 291 PHE   A C   1 
ATOM   2239 O O   . PHE   A 1 291 ? -16.66374 -22.72235 8.97705   1.000 11.76513 ? 291 PHE   A O   1 
ATOM   2240 C CB  . PHE   A 1 291 ? -19.42053 -22.06814 8.07559   1.000 14.78201 ? 291 PHE   A CB  1 
ATOM   2241 C CG  . PHE   A 1 291 ? -20.59224 -22.09368 7.16164   1.000 15.14267 ? 291 PHE   A CG  1 
ATOM   2242 C CD1 . PHE   A 1 291 ? -21.25166 -20.92019 6.83330   1.000 19.41485 ? 291 PHE   A CD1 1 
ATOM   2243 C CD2 . PHE   A 1 291 ? -21.01767 -23.27986 6.59808   1.000 14.78257 ? 291 PHE   A CD2 1 
ATOM   2244 C CE1 . PHE   A 1 291 ? -22.35217 -20.93417 5.98834   1.000 17.84803 ? 291 PHE   A CE1 1 
ATOM   2245 C CE2 . PHE   A 1 291 ? -22.09668 -23.30031 5.73747   1.000 17.87815 ? 291 PHE   A CE2 1 
ATOM   2246 C CZ  . PHE   A 1 291 ? -22.76962 -22.12319 5.43569   1.000 19.24561 ? 291 PHE   A CZ  1 
ATOM   2247 N N   . THR   A 1 292 ? -16.43011 -20.48902 8.75852   1.000 11.36767 ? 292 THR   A N   1 
ATOM   2248 C CA  . THR   A 1 292 ? -15.41347 -20.44058 9.79471   1.000 15.69731 ? 292 THR   A CA  1 
ATOM   2249 C C   . THR   A 1 292 ? -16.04413 -20.46012 11.18430  1.000 12.96859 ? 292 THR   A C   1 
ATOM   2250 O O   . THR   A 1 292 ? -17.24300 -20.18338 11.33819  1.000 13.60057 ? 292 THR   A O   1 
ATOM   2251 C CB  . THR   A 1 292 ? -14.58189 -19.17546 9.67093   1.000 15.10166 ? 292 THR   A CB  1 
ATOM   2252 O OG1 . THR   A 1 292 ? -15.42097 -18.05956 9.99256   1.000 16.37511 ? 292 THR   A OG1 1 
ATOM   2253 C CG2 . THR   A 1 292 ? -13.99521 -19.02751 8.30389   1.000 12.82369 ? 292 THR   A CG2 1 
ATOM   2254 N N   . PRO   A 1 293 ? -15.25602 -20.75933 12.22069  1.000 16.48383 ? 293 PRO   A N   1 
ATOM   2255 C CA  . PRO   A 1 293 ? -15.77048 -20.58525 13.58692  1.000 14.74815 ? 293 PRO   A CA  1 
ATOM   2256 C C   . PRO   A 1 293 ? -16.36168 -19.20181 13.79916  1.000 17.60665 ? 293 PRO   A C   1 
ATOM   2257 O O   . PRO   A 1 293 ? -17.41521 -19.07231 14.43087  1.000 16.42610 ? 293 PRO   A O   1 
ATOM   2258 C CB  . PRO   A 1 293 ? -14.52717 -20.82940 14.45198  1.000 15.85594 ? 293 PRO   A CB  1 
ATOM   2259 C CG  . PRO   A 1 293 ? -13.78076 -21.87861 13.69938  1.000 16.95934 ? 293 PRO   A CG  1 
ATOM   2260 C CD  . PRO   A 1 293 ? -13.94886 -21.45480 12.22419  1.000 15.42999 ? 293 PRO   A CD  1 
ATOM   2261 N N   . PHE   A 1 294 ? -15.72885 -18.16816 13.22776  1.000 17.40423 ? 294 PHE   A N   1 
ATOM   2262 C CA  . PHE   A 1 294 ? -16.26940 -16.81466 13.32395  1.000 19.11762 ? 294 PHE   A CA  1 
ATOM   2263 C C   . PHE   A 1 294 ? -17.65001 -16.73376 12.70166  1.000 18.77857 ? 294 PHE   A C   1 
ATOM   2264 O O   . PHE   A 1 294 ? -18.57812 -16.17091 13.29987  1.000 19.53272 ? 294 PHE   A O   1 
ATOM   2265 C CB  . PHE   A 1 294 ? -15.33864 -15.80567 12.63917  1.000 20.30296 ? 294 PHE   A CB  1 
ATOM   2266 C CG  . PHE   A 1 294 ? -15.92827 -14.41515 12.55149  1.000 25.02443 ? 294 PHE   A CG  1 
ATOM   2267 C CD1 . PHE   A 1 294 ? -15.64631 -13.47165 13.52263  1.000 27.22860 ? 294 PHE   A CD1 1 
ATOM   2268 C CD2 . PHE   A 1 294 ? -16.75926 -14.05272 11.49075  1.000 26.65257 ? 294 PHE   A CD2 1 
ATOM   2269 C CE1 . PHE   A 1 294 ? -16.19945 -12.20173 13.45898  1.000 30.28335 ? 294 PHE   A CE1 1 
ATOM   2270 C CE2 . PHE   A 1 294 ? -17.31767 -12.78563 11.42687  1.000 30.05842 ? 294 PHE   A CE2 1 
ATOM   2271 C CZ  . PHE   A 1 294 ? -17.02660 -11.85814 12.41176  1.000 30.32453 ? 294 PHE   A CZ  1 
ATOM   2272 N N   . ASP   A 1 295 ? -17.78339 -17.25034 11.47296  1.000 14.94601 ? 295 ASP   A N   1 
ATOM   2273 C CA  . ASP   A 1 295 ? -19.06089 -17.22633 10.76930  1.000 16.83612 ? 295 ASP   A CA  1 
ATOM   2274 C C   . ASP   A 1 295 ? -20.15462 -17.88183 11.59739  1.000 17.60841 ? 295 ASP   A C   1 
ATOM   2275 O O   . ASP   A 1 295 ? -21.28633 -17.39098 11.64853  1.000 19.55458 ? 295 ASP   A O   1 
ATOM   2276 C CB  . ASP   A 1 295 ? -18.93811 -17.94092 9.42677   1.000 15.63621 ? 295 ASP   A CB  1 
ATOM   2277 C CG  . ASP   A 1 295 ? -17.93450 -17.28278 8.50927   1.000 17.43623 ? 295 ASP   A CG  1 
ATOM   2278 O OD1 . ASP   A 1 295 ? -17.60059 -16.11344 8.76831   1.000 17.81183 ? 295 ASP   A OD1 1 
ATOM   2279 O OD2 . ASP   A 1 295 ? -17.46903 -17.93942 7.55013   1.000 18.59286 ? 295 ASP   A OD2 1 
ATOM   2280 N N   . VAL   A 1 296 ? -19.83281 -19.00065 12.25496  1.000 14.70250 ? 296 VAL   A N   1 
ATOM   2281 C CA  . VAL   A 1 296 ? -20.84654 -19.70165 13.03825  1.000 17.48593 ? 296 VAL   A CA  1 
ATOM   2282 C C   . VAL   A 1 296 ? -21.23339 -18.87700 14.25275  1.000 19.22902 ? 296 VAL   A C   1 
ATOM   2283 O O   . VAL   A 1 296 ? -22.41575 -18.72437 14.56863  1.000 21.12357 ? 296 VAL   A O   1 
ATOM   2284 C CB  . VAL   A 1 296 ? -20.34163 -21.10013 13.43515  1.000 15.64185 ? 296 VAL   A CB  1 
ATOM   2285 C CG1 . VAL   A 1 296 ? -21.28326 -21.74571 14.42732  1.000 16.07802 ? 296 VAL   A CG1 1 
ATOM   2286 C CG2 . VAL   A 1 296 ? -20.14935 -21.97746 12.18937  1.000 14.84052 ? 296 VAL   A CG2 1 
ATOM   2287 N N   . VAL   A 1 297 ? -20.24844 -18.31220 14.94094  1.000 19.65531 ? 297 VAL   A N   1 
ATOM   2288 C CA  . VAL   A 1 297 ? -20.55998 -17.47005 16.08688  1.000 23.72827 ? 297 VAL   A CA  1 
ATOM   2289 C C   . VAL   A 1 297 ? -21.31214 -16.21391 15.64168  1.000 25.89127 ? 297 VAL   A C   1 
ATOM   2290 O O   . VAL   A 1 297 ? -22.22898 -15.75906 16.33310  1.000 27.09157 ? 297 VAL   A O   1 
ATOM   2291 C CB  . VAL   A 1 297 ? -19.27134 -17.13333 16.85779  1.000 22.27514 ? 297 VAL   A CB  1 
ATOM   2292 C CG1 . VAL   A 1 297 ? -19.54116 -16.09433 17.93126  1.000 22.45497 ? 297 VAL   A CG1 1 
ATOM   2293 C CG2 . VAL   A 1 297 ? -18.64476 -18.40163 17.45247  1.000 23.44801 ? 297 VAL   A CG2 1 
ATOM   2294 N N   . ARG   A 1 298 ? -20.95682 -15.64867 14.47426  1.000 24.30853 ? 298 ARG   A N   1 
ATOM   2295 C CA  . ARG   A 1 298 ? -21.66328 -14.46940 13.95856  1.000 28.63179 ? 298 ARG   A CA  1 
ATOM   2296 C C   . ARG   A 1 298 ? -23.14045 -14.75087 13.77360  1.000 30.36876 ? 298 ARG   A C   1 
ATOM   2297 O O   . ARG   A 1 298 ? -23.98803 -13.92800 14.13751  1.000 34.95310 ? 298 ARG   A O   1 
ATOM   2298 C CB  . ARG   A 1 298 ? -21.04517 -13.96532 12.63129  1.000 27.66548 ? 298 ARG   A CB  1 
ATOM   2299 C CG  . ARG   A 1 298 ? -22.01169 -13.10086 11.69500  1.000 32.32342 ? 298 ARG   A CG  1 
ATOM   2300 C CD  . ARG   A 1 298 ? -21.30968 -12.29172 10.50632  1.000 30.29482 ? 298 ARG   A CD  1 
ATOM   2301 N NE  . ARG   A 1 298 ? -20.96758 -12.88646 9.19869   1.000 32.14826 ? 298 ARG   A NE  1 
ATOM   2302 C CZ  . ARG   A 1 298 ? -21.54018 -12.58898 8.01909   1.000 25.53579 ? 298 ARG   A CZ  1 
ATOM   2303 N NH1 . ARG   A 1 298 ? -22.54127 -11.69062 7.91451   1.000 20.46510 ? 298 ARG   A NH1 1 
ATOM   2304 N NH2 . ARG   A 1 298 ? -21.08166 -13.17203 6.90990   1.000 23.66168 ? 298 ARG   A NH2 1 
ATOM   2305 N N   . GLN   A 1 299 ? -23.46773 -15.91872 13.23613  1.000 28.73716 ? 299 GLN   A N   1 
ATOM   2306 C CA  . GLN   A 1 299 ? -24.83477 -16.21075 12.84536  1.000 29.72552 ? 299 GLN   A CA  1 
ATOM   2307 C C   . GLN   A 1 299 ? -25.61540 -16.86313 13.96802  1.000 28.50702 ? 299 GLN   A C   1 
ATOM   2308 O O   . GLN   A 1 299 ? -26.79800 -16.56387 14.15298  1.000 34.34787 ? 299 GLN   A O   1 
ATOM   2309 C CB  . GLN   A 1 299 ? -24.84091 -17.11029 11.61132  1.000 28.38770 ? 299 GLN   A CB  1 
ATOM   2310 C CG  . GLN   A 1 299 ? -26.08103 -16.97903 10.81190  1.000 22.85833 ? 299 GLN   A CG  1 
ATOM   2311 C CD  . GLN   A 1 299 ? -26.04301 -17.80576 9.57124   1.000 20.95416 ? 299 GLN   A CD  1 
ATOM   2312 O OE1 . GLN   A 1 299 ? -27.05223 -18.39171 9.19282   1.000 20.23766 ? 299 GLN   A OE1 1 
ATOM   2313 N NE2 . GLN   A 1 299 ? -24.86601 -17.89015 8.92829   1.000 17.39906 ? 299 GLN   A NE2 1 
ATOM   2314 N N   . CYS   A 1 300 ? -24.98162 -17.74495 14.73398  1.000 29.46577 ? 300 CYS   A N   1 
ATOM   2315 C CA  . CYS   A 1 300 ? -25.60942 -18.32901 15.90642  1.000 29.71319 ? 300 CYS   A CA  1 
ATOM   2316 C C   . CYS   A 1 300 ? -25.44868 -17.44296 17.15268  1.000 36.64587 ? 300 CYS   A C   1 
ATOM   2317 O O   . CYS   A 1 300 ? -25.48710 -17.96175 18.27825  1.000 43.02417 ? 300 CYS   A O   1 
ATOM   2318 C CB  . CYS   A 1 300 ? -25.05634 -19.74250 16.14977  1.000 27.22453 ? 300 CYS   A CB  1 
ATOM   2319 S SG  . CYS   A 1 300 ? -25.09900 -20.88947 14.68916  1.000 27.99536 ? 300 CYS   A SG  1 
ATOM   2320 N N   . SER   A 1 301 ? -25.26481 -16.11992 16.96487  1.000 38.14908 ? 301 SER   A N   1 
ATOM   2321 C CA  . SER   A 1 301 ? -25.26400 -15.13280 18.05030  1.000 41.42723 ? 301 SER   A CA  1 
ATOM   2322 C C   . SER   A 1 301 ? -25.82261 -13.77017 17.62038  1.000 43.16391 ? 301 SER   A C   1 
ATOM   2323 O O   . SER   A 1 301 ? -26.61622 -13.17056 18.35474  1.000 41.48157 ? 301 SER   A O   1 
ATOM   2324 C CB  . SER   A 1 301 ? -23.85670 -14.95398 18.63139  1.000 43.99171 ? 301 SER   A CB  1 
ATOM   2325 O OG  . SER   A 1 301 ? -23.84368 -13.94314 19.62717  1.000 49.27154 ? 301 SER   A OG  1 
ATOM   2326 N N   . GLY   A 1 302 ? -25.40254 -13.24572 16.46402  1.000 44.39844 ? 302 GLY   A N   1 
ATOM   2327 C CA  . GLY   A 1 302 ? -26.13243 -12.14303 15.84849  1.000 45.87497 ? 302 GLY   A CA  1 
ATOM   2328 C C   . GLY   A 1 302 ? -25.50532 -10.75886 15.77512  1.000 51.62273 ? 302 GLY   A C   1 
ATOM   2329 O O   . GLY   A 1 302 ? -26.18146 -9.76168  16.05630  1.000 50.28909 ? 302 GLY   A O   1 
ATOM   2330 N N   . VAL   A 1 303 ? -24.24046 -10.66459 15.35692  1.000 51.90138 ? 303 VAL   A N   1 
ATOM   2331 C CA  . VAL   A 1 303 ? -23.54440 -9.37964  15.33662  1.000 54.32271 ? 303 VAL   A CA  1 
ATOM   2332 C C   . VAL   A 1 303 ? -23.92018 -8.60611  14.07419  1.000 52.20168 ? 303 VAL   A C   1 
ATOM   2333 O O   . VAL   A 1 303 ? -24.26472 -9.19203  13.04020  1.000 47.83278 ? 303 VAL   A O   1 
ATOM   2334 C CB  . VAL   A 1 303 ? -22.02024 -9.59281  15.44449  1.000 53.42200 ? 303 VAL   A CB  1 
ATOM   2335 C CG1 . VAL   A 1 303 ? -21.29792 -8.26297  15.65195  1.000 56.75298 ? 303 VAL   A CG1 1 
ATOM   2336 C CG2 . VAL   A 1 303 ? -21.69730 -10.57833 16.56603  1.000 51.38073 ? 303 VAL   A CG2 1 
ATOM   2337 N N   . THR   A 1 304 ? -23.86040 -7.27162  14.16242  1.000 49.88995 ? 304 THR   A N   1 
ATOM   2338 C CA  . THR   A 1 304 ? -24.23988 -6.35617  13.08930  1.000 45.84078 ? 304 THR   A CA  1 
ATOM   2339 C C   . THR   A 1 304 ? -23.08244 -5.40680  12.79852  1.000 53.57065 ? 304 THR   A C   1 
ATOM   2340 O O   . THR   A 1 304 ? -22.01047 -5.48844  13.41160  1.000 55.82996 ? 304 THR   A O   1 
ATOM   2341 C CB  . THR   A 1 304 ? -25.49486 -5.54698  13.44818  1.000 42.28702 ? 304 THR   A CB  1 
ATOM   2342 O OG1 . THR   A 1 304 ? -25.31304 -4.92192  14.72485  1.000 50.12074 ? 304 THR   A OG1 1 
ATOM   2343 C CG2 . THR   A 1 304 ? -26.70426 -6.44614  13.52109  1.000 33.43676 ? 304 THR   A CG2 1 
ATOM   2344 N N   . PHE   A 1 305 ? -23.31177 -4.48516  11.85778  1.000 51.50465 ? 305 PHE   A N   1 
ATOM   2345 C CA  . PHE   A 1 305 ? -22.24521 -3.64381  11.32558  1.000 56.40387 ? 305 PHE   A CA  1 
ATOM   2346 C C   . PHE   A 1 305 ? -22.79280 -2.26951  10.97033  1.000 55.77587 ? 305 PHE   A C   1 
ATOM   2347 O O   . PHE   A 1 305 ? -23.88046 -2.15151  10.39740  1.000 52.25772 ? 305 PHE   A O   1 
ATOM   2348 C CB  . PHE   A 1 305 ? -21.59022 -4.30912  10.10353  1.000 51.35684 ? 305 PHE   A CB  1 
ATOM   2349 C CG  . PHE   A 1 305 ? -21.36757 -5.77324  10.29755  1.000 49.54355 ? 305 PHE   A CG  1 
ATOM   2350 C CD1 . PHE   A 1 305 ? -20.20895 -6.22824  10.90506  1.000 46.16581 ? 305 PHE   A CD1 1 
ATOM   2351 C CD2 . PHE   A 1 305 ? -22.34149 -6.69514  9.92577   1.000 45.04390 ? 305 PHE   A CD2 1 
ATOM   2352 C CE1 . PHE   A 1 305 ? -20.01888 -7.57247  11.12890  1.000 47.61694 ? 305 PHE   A CE1 1 
ATOM   2353 C CE2 . PHE   A 1 305 ? -22.15378 -8.04232  10.14528  1.000 44.10123 ? 305 PHE   A CE2 1 
ATOM   2354 C CZ  . PHE   A 1 305 ? -20.99786 -8.48343  10.75500  1.000 46.64244 ? 305 PHE   A CZ  1 
ATOM   2355 N N   . GLN   A 1 306 ? -22.02902 -1.23775  11.31803  1.000 57.47759 ? 306 GLN   A N   1 
ATOM   2356 C CA  . GLN   A 1 306 ? -22.44204 0.14382   11.09582  1.000 60.15721 ? 306 GLN   A CA  1 
ATOM   2357 C C   . GLN   A 1 306 ? -21.31330 0.96747   10.48707  1.000 54.69031 ? 306 GLN   A C   1 
ATOM   2358 O O   . GLN   A 1 306 ? -21.25225 1.15086   9.27378   1.000 51.64315 ? 306 GLN   A O   1 
ATOM   2359 C CB  . GLN   A 1 306 ? -22.90076 0.78298   12.40707  1.000 62.10168 ? 306 GLN   A CB  1 
ATOM   2360 C CG  . GLN   A 1 306 ? -24.17046 0.19125   12.97977  1.000 58.79561 ? 306 GLN   A CG  1 
ATOM   2361 C CD  . GLN   A 1 306 ? -25.02507 1.22846   13.68011  1.000 62.86392 ? 306 GLN   A CD  1 
ATOM   2362 O OE1 . GLN   A 1 306 ? -25.24715 1.14592   14.88969  1.000 66.95107 ? 306 GLN   A OE1 1 
ATOM   2363 N NE2 . GLN   A 1 306 ? -25.51157 2.21186   12.92541  1.000 62.09685 ? 306 GLN   A NE2 1 
HETATM 2364 C C1  . A1AQ3 B 2 .   ? -10.48600 -18.50474 -18.86213 1.000 24.24917 ? 401 A1AQ3 A C1  1 
HETATM 2365 C C10 . A1AQ3 B 2 .   ? -5.10159  -13.93895 -18.63838 1.000 27.91399 ? 401 A1AQ3 A C10 1 
HETATM 2366 C C11 . A1AQ3 B 2 .   ? -4.33961  -14.53798 -17.46806 1.000 25.67646 ? 401 A1AQ3 A C11 1 
HETATM 2367 C C12 . A1AQ3 B 2 .   ? -9.92003  -16.13743 -18.29477 1.000 23.36315 ? 401 A1AQ3 A C12 1 
HETATM 2368 C C13 . A1AQ3 B 2 .   ? -8.27644  -14.96674 -19.76437 1.000 24.76921 ? 401 A1AQ3 A C13 1 
HETATM 2369 C C14 . A1AQ3 B 2 .   ? -9.40335  -13.80396 -17.94641 1.000 21.61476 ? 401 A1AQ3 A C14 1 
HETATM 2370 C C15 . A1AQ3 B 2 .   ? -10.81050 -13.30565 -18.07512 1.000 21.16715 ? 401 A1AQ3 A C15 1 
HETATM 2371 C C16 . A1AQ3 B 2 .   ? -7.42175  -13.78389 -19.35871 1.000 27.74344 ? 401 A1AQ3 A C16 1 
HETATM 2372 C C17 . A1AQ3 B 2 .   ? -12.67976 -12.28709 -16.99287 1.000 20.22289 ? 401 A1AQ3 A C17 1 
HETATM 2373 C C18 . A1AQ3 B 2 .   ? -4.91417  -12.42534 -18.69842 1.000 28.21491 ? 401 A1AQ3 A C18 1 
HETATM 2374 C C19 . A1AQ3 B 2 .   ? -13.56698 -13.05628 -16.00248 1.000 16.82178 ? 401 A1AQ3 A C19 1 
HETATM 2375 C C20 . A1AQ3 B 2 .   ? -13.56855 -14.52794 -16.39581 1.000 17.21805 ? 401 A1AQ3 A C20 1 
HETATM 2376 C C21 . A1AQ3 B 2 .   ? -14.34129 -14.78107 -17.68648 1.000 22.16441 ? 401 A1AQ3 A C21 1 
HETATM 2377 C C22 . A1AQ3 B 2 .   ? -15.16345 -16.04667 -17.41836 1.000 21.81618 ? 401 A1AQ3 A C22 1 
HETATM 2378 C C23 . A1AQ3 B 2 .   ? -4.59155  -14.58200 -19.92079 1.000 30.22977 ? 401 A1AQ3 A C23 1 
HETATM 2379 C C24 . A1AQ3 B 2 .   ? -14.29233 -15.37722 -15.38604 1.000 18.27526 ? 401 A1AQ3 A C24 1 
HETATM 2380 C C3  . A1AQ3 B 2 .   ? -11.92653 -18.37760 -19.29562 1.000 25.05803 ? 401 A1AQ3 A C3  1 
HETATM 2381 C C34 . A1AQ3 B 2 .   ? -8.42246  -12.88259 -18.65797 1.000 26.03284 ? 401 A1AQ3 A C34 1 
HETATM 2382 C C4  . A1AQ3 B 2 .   ? -12.84969 -19.32533 -18.87327 1.000 25.16854 ? 401 A1AQ3 A C4  1 
HETATM 2383 C C5  . A1AQ3 B 2 .   ? -14.17629 -19.20894 -19.27846 1.000 25.65612 ? 401 A1AQ3 A C5  1 
HETATM 2384 C C6  . A1AQ3 B 2 .   ? -14.57682 -18.15529 -20.09419 1.000 25.54102 ? 401 A1AQ3 A C6  1 
HETATM 2385 C C7  . A1AQ3 B 2 .   ? -13.64995 -17.20818 -20.52021 1.000 26.60165 ? 401 A1AQ3 A C7  1 
HETATM 2386 C C8  . A1AQ3 B 2 .   ? -12.54788 -10.80245 -16.67986 1.000 18.82637 ? 401 A1AQ3 A C8  1 
HETATM 2387 C C9  . A1AQ3 B 2 .   ? -12.32639 -17.32209 -20.11483 1.000 26.83922 ? 401 A1AQ3 A C9  1 
HETATM 2388 N N13 . A1AQ3 B 2 .   ? -9.23600  -15.05793 -18.66347 1.000 24.43212 ? 401 A1AQ3 A N13 1 
HETATM 2389 N N16 . A1AQ3 B 2 .   ? -11.34674 -12.84250 -16.96552 1.000 20.48236 ? 401 A1AQ3 A N16 1 
HETATM 2390 N N23 . A1AQ3 B 2 .   ? -15.15475 -16.20676 -15.97943 1.000 20.60067 ? 401 A1AQ3 A N23 1 
HETATM 2391 O O11 . A1AQ3 B 2 .   ? -9.81205  -17.28609 -19.16001 1.000 23.62715 ? 401 A1AQ3 A O11 1 
HETATM 2392 O O26 . A1AQ3 B 2 .   ? -14.08852 -15.31142 -14.19022 1.000 15.57269 ? 401 A1AQ3 A O26 1 
HETATM 2393 O O3  . A1AQ3 B 2 .   ? -6.47309  -14.26118 -18.41987 1.000 26.89160 ? 401 A1AQ3 A O3  1 
HETATM 2394 O O33 . A1AQ3 B 2 .   ? -10.60809 -16.19906 -17.28300 1.000 20.56778 ? 401 A1AQ3 A O33 1 
HETATM 2395 O O38 . A1AQ3 B 2 .   ? -11.41154 -13.35595 -19.14433 1.000 25.36363 ? 401 A1AQ3 A O38 1 
HETATM 2396 O O9  . A1AQ3 B 2 .   ? -13.82162 -10.16791 -16.61258 1.000 17.94984 ? 401 A1AQ3 A O9  1 
HETATM 2397 O O   . HOH   C 3 .   ? -7.65595  5.89246   -0.05957  1.000 25.44086 ? 501 HOH   A O   1 
HETATM 2398 O O   . HOH   C 3 .   ? -18.92598 -13.37569 -8.38100  1.000 34.10321 ? 502 HOH   A O   1 
HETATM 2399 O O   . HOH   C 3 .   ? -3.49736  -24.28235 -6.47773  1.000 19.16777 ? 503 HOH   A O   1 
HETATM 2400 O O   . HOH   C 3 .   ? -13.66290 -22.27200 -16.97685 1.000 24.30328 ? 504 HOH   A O   1 
HETATM 2401 O O   . HOH   C 3 .   ? -7.33475  -6.53251  9.98819   1.000 28.35708 ? 505 HOH   A O   1 
HETATM 2402 O O   . HOH   C 3 .   ? -16.55023 -7.86241  13.69179  1.000 38.73130 ? 506 HOH   A O   1 
HETATM 2403 O O   . HOH   C 3 .   ? -1.98201  -3.27679  -24.58299 1.000 36.88395 ? 507 HOH   A O   1 
HETATM 2404 O O   . HOH   C 3 .   ? -26.85298 -4.55894  16.29419  1.000 36.17718 ? 508 HOH   A O   1 
HETATM 2405 O O   . HOH   C 3 .   ? -24.71289 -2.38355  8.29831   1.000 35.31148 ? 509 HOH   A O   1 
HETATM 2406 O O   . HOH   C 3 .   ? 3.07963   -10.27258 -6.20002  1.000 17.21645 ? 510 HOH   A O   1 
HETATM 2407 O O   . HOH   C 3 .   ? -4.34925  -36.68462 3.11364   1.000 32.85712 ? 511 HOH   A O   1 
HETATM 2408 O O   . HOH   C 3 .   ? -5.11718  -24.29466 4.16688   1.000 23.92128 ? 512 HOH   A O   1 
HETATM 2409 O O   . HOH   C 3 .   ? 0.33401   1.09295   -2.85402  1.000 31.41946 ? 513 HOH   A O   1 
HETATM 2410 O O   . HOH   C 3 .   ? -19.50765 -24.18603 0.13802   1.000 27.87599 ? 514 HOH   A O   1 
HETATM 2411 O O   . HOH   C 3 .   ? -2.37741  8.21631   -5.86587  1.000 34.45492 ? 515 HOH   A O   1 
HETATM 2412 O O   . HOH   C 3 .   ? -0.34174  -14.24335 -21.67229 1.000 41.12113 ? 516 HOH   A O   1 
HETATM 2413 O O   . HOH   C 3 .   ? -29.75902 -19.41427 1.28947   1.000 39.24908 ? 517 HOH   A O   1 
HETATM 2414 O O   . HOH   C 3 .   ? -4.28657  -26.94304 -17.77845 1.000 33.68465 ? 518 HOH   A O   1 
HETATM 2415 O O   . HOH   C 3 .   ? -12.90052 -4.84727  8.52408   1.000 23.52507 ? 519 HOH   A O   1 
HETATM 2416 O O   . HOH   C 3 .   ? -16.08632 -34.69474 3.61604   1.000 23.61487 ? 520 HOH   A O   1 
HETATM 2417 O O   . HOH   C 3 .   ? -29.54754 -19.39218 13.99770  1.000 29.64113 ? 521 HOH   A O   1 
HETATM 2418 O O   . HOH   C 3 .   ? -19.13946 -20.50902 0.63843   1.000 22.36989 ? 522 HOH   A O   1 
HETATM 2419 O O   . HOH   C 3 .   ? -3.35102  -21.69603 20.34851  1.000 26.49487 ? 523 HOH   A O   1 
HETATM 2420 O O   . HOH   C 3 .   ? -8.51504  -25.61609 24.03304  1.000 32.13305 ? 524 HOH   A O   1 
HETATM 2421 O O   . HOH   C 3 .   ? 2.29758   -17.45652 -25.68067 1.000 44.51084 ? 525 HOH   A O   1 
HETATM 2422 O O   . HOH   C 3 .   ? -17.78877 -37.50580 26.08455  1.000 36.97450 ? 526 HOH   A O   1 
HETATM 2423 O O   . HOH   C 3 .   ? -7.20141  13.61070  -7.08814  1.000 29.03140 ? 527 HOH   A O   1 
HETATM 2424 O O   . HOH   C 3 .   ? -4.24882  -34.07196 7.00488   1.000 27.38761 ? 528 HOH   A O   1 
HETATM 2425 O O   . HOH   C 3 .   ? -1.76868  -34.61207 16.20481  1.000 34.89119 ? 529 HOH   A O   1 
HETATM 2426 O O   . HOH   C 3 .   ? -12.63990 8.61412   -17.91590 1.000 30.09351 ? 530 HOH   A O   1 
HETATM 2427 O O   . HOH   C 3 .   ? -11.56464 -45.40927 6.82170   1.000 38.82860 ? 531 HOH   A O   1 
HETATM 2428 O O   . HOH   C 3 .   ? -10.13057 9.19252   -18.68614 1.000 28.78494 ? 532 HOH   A O   1 
HETATM 2429 O O   . HOH   C 3 .   ? -18.31549 -33.64557 25.54298  1.000 27.89060 ? 533 HOH   A O   1 
HETATM 2430 O O   . HOH   C 3 .   ? -11.14017 -33.32270 0.85131   1.000 24.32923 ? 534 HOH   A O   1 
HETATM 2431 O O   . HOH   C 3 .   ? -7.45184  -24.05023 5.43313   1.000 24.15628 ? 535 HOH   A O   1 
HETATM 2432 O O   . HOH   C 3 .   ? -17.34901 -5.87962  -6.40621  1.000 13.28200 ? 536 HOH   A O   1 
HETATM 2433 O O   . HOH   C 3 .   ? -3.26772  -36.85811 20.69078  1.000 33.68016 ? 537 HOH   A O   1 
HETATM 2434 O O   . HOH   C 3 .   ? -1.40567  6.02255   -25.67642 1.000 42.83621 ? 538 HOH   A O   1 
HETATM 2435 O O   . HOH   C 3 .   ? -19.85237 -25.05368 2.73073   1.000 20.83571 ? 539 HOH   A O   1 
HETATM 2436 O O   . HOH   C 3 .   ? -16.84702 -13.78488 6.03762   1.000 18.65139 ? 540 HOH   A O   1 
HETATM 2437 O O   . HOH   C 3 .   ? -2.44169  -27.92499 -4.22931  1.000 29.26639 ? 541 HOH   A O   1 
HETATM 2438 O O   . HOH   C 3 .   ? -3.83029  -22.41985 -22.00138 1.000 35.71772 ? 542 HOH   A O   1 
HETATM 2439 O O   . HOH   C 3 .   ? -18.70236 -13.72157 8.29191   1.000 36.73577 ? 543 HOH   A O   1 
HETATM 2440 O O   . HOH   C 3 .   ? -15.59298 14.09993  -3.84452  1.000 34.29778 ? 544 HOH   A O   1 
HETATM 2441 O O   . HOH   C 3 .   ? -3.75070  -41.83630 7.93060   1.000 32.26410 ? 545 HOH   A O   1 
HETATM 2442 O O   . HOH   C 3 .   ? 1.31319   7.79163   -20.30995 1.000 29.91886 ? 546 HOH   A O   1 
HETATM 2443 O O   . HOH   C 3 .   ? -1.74104  5.77238   -10.02858 1.000 22.52881 ? 547 HOH   A O   1 
HETATM 2444 O O   . HOH   C 3 .   ? -10.99706 -21.48475 9.07435   1.000 17.91329 ? 548 HOH   A O   1 
HETATM 2445 O O   . HOH   C 3 .   ? -25.37797 -22.90966 25.80603  1.000 34.93965 ? 549 HOH   A O   1 
HETATM 2446 O O   . HOH   C 3 .   ? -29.53608 -24.54321 6.88324   1.000 29.94839 ? 550 HOH   A O   1 
HETATM 2447 O O   . HOH   C 3 .   ? -17.99999 -25.26010 7.37245   1.000 9.36669  ? 551 HOH   A O   1 
HETATM 2448 O O   . HOH   C 3 .   ? -5.52070  -1.05369  -25.06246 1.000 27.54852 ? 552 HOH   A O   1 
HETATM 2449 O O   . HOH   C 3 .   ? -20.01989 -36.34717 19.84679  1.000 27.20832 ? 553 HOH   A O   1 
HETATM 2450 O O   . HOH   C 3 .   ? -21.87160 -13.30820 -11.34856 1.000 20.56667 ? 554 HOH   A O   1 
HETATM 2451 O O   . HOH   C 3 .   ? -19.85325 3.31805   -0.00121  1.000 22.04378 ? 555 HOH   A O   1 
HETATM 2452 O O   . HOH   C 3 .   ? -10.44155 -44.26897 8.99912   1.000 31.94513 ? 556 HOH   A O   1 
HETATM 2453 O O   . HOH   C 3 .   ? -3.55279  -23.75735 13.15124  1.000 21.79777 ? 557 HOH   A O   1 
HETATM 2454 O O   . HOH   C 3 .   ? 3.46689   -11.57509 -18.35269 1.000 32.89267 ? 558 HOH   A O   1 
HETATM 2455 O O   . HOH   C 3 .   ? -28.83251 -29.28126 20.31854  1.000 23.88383 ? 559 HOH   A O   1 
HETATM 2456 O O   . HOH   C 3 .   ? -32.33669 -29.11050 13.92670  1.000 30.09897 ? 560 HOH   A O   1 
HETATM 2457 O O   . HOH   C 3 .   ? -3.31891  -24.41782 23.58469  1.000 30.82535 ? 561 HOH   A O   1 
HETATM 2458 O O   . HOH   C 3 .   ? -11.24936 -13.96051 -21.70122 1.000 29.85703 ? 562 HOH   A O   1 
HETATM 2459 O O   . HOH   C 3 .   ? -9.06073  1.74098   8.09347   1.000 28.04081 ? 563 HOH   A O   1 
HETATM 2460 O O   . HOH   C 3 .   ? 4.68276   -14.59479 -14.90164 1.000 30.31066 ? 564 HOH   A O   1 
HETATM 2461 O O   . HOH   C 3 .   ? 2.14420   5.37024   -19.57913 1.000 27.07708 ? 565 HOH   A O   1 
HETATM 2462 O O   . HOH   C 3 .   ? -30.85811 -40.39628 13.23396  1.000 46.39144 ? 566 HOH   A O   1 
HETATM 2463 O O   . HOH   C 3 .   ? -17.44375 -8.53077  11.48811  1.000 35.92940 ? 567 HOH   A O   1 
HETATM 2464 O O   . HOH   C 3 .   ? -29.15087 -16.41867 12.93507  1.000 24.53186 ? 568 HOH   A O   1 
HETATM 2465 O O   . HOH   C 3 .   ? -0.26220  -1.17108  -24.42249 1.000 29.40105 ? 569 HOH   A O   1 
HETATM 2466 O O   . HOH   C 3 .   ? -23.38054 -0.20517  -15.80850 1.000 35.43681 ? 570 HOH   A O   1 
HETATM 2467 O O   . HOH   C 3 .   ? -1.93259  -24.80995 -8.98607  1.000 23.85089 ? 571 HOH   A O   1 
HETATM 2468 O O   . HOH   C 3 .   ? -9.52095  -6.80838  8.84712   1.000 27.61229 ? 572 HOH   A O   1 
HETATM 2469 O O   . HOH   C 3 .   ? -15.83634 2.55039   -18.82047 1.000 24.30029 ? 573 HOH   A O   1 
HETATM 2470 O O   . HOH   C 3 .   ? 3.55527   -4.83840  -11.83088 1.000 24.60389 ? 574 HOH   A O   1 
HETATM 2471 O O   . HOH   C 3 .   ? -21.21061 -11.59768 -18.87872 1.000 27.02193 ? 575 HOH   A O   1 
HETATM 2472 O O   . HOH   C 3 .   ? -12.54932 -18.60122 18.98990  1.000 33.45477 ? 576 HOH   A O   1 
HETATM 2473 O O   . HOH   C 3 .   ? -6.47632  -17.07544 -6.65826  1.000 10.55631 ? 577 HOH   A O   1 
HETATM 2474 O O   . HOH   C 3 .   ? -29.00900 -24.36102 20.91200  1.000 34.64794 ? 578 HOH   A O   1 
HETATM 2475 O O   . HOH   C 3 .   ? -20.87801 -39.23828 14.08027  1.000 25.76914 ? 579 HOH   A O   1 
HETATM 2476 O O   . HOH   C 3 .   ? -13.48224 1.10854   12.55500  1.000 38.15649 ? 580 HOH   A O   1 
HETATM 2477 O O   . HOH   C 3 .   ? -11.40231 -27.09444 -4.81447  1.000 21.71511 ? 581 HOH   A O   1 
HETATM 2478 O O   . HOH   C 3 .   ? -8.76169  2.95841   -24.80159 1.000 33.01680 ? 582 HOH   A O   1 
HETATM 2479 O O   . HOH   C 3 .   ? -24.62950 -26.50191 3.27639   1.000 30.41694 ? 583 HOH   A O   1 
HETATM 2480 O O   . HOH   C 3 .   ? -10.76711 -26.89095 -9.08780  1.000 17.47103 ? 584 HOH   A O   1 
HETATM 2481 O O   . HOH   C 3 .   ? -1.93824  -24.54672 -1.35939  1.000 21.93278 ? 585 HOH   A O   1 
HETATM 2482 O O   . HOH   C 3 .   ? -15.56618 -21.28826 18.80197  1.000 23.91519 ? 586 HOH   A O   1 
HETATM 2483 O O   . HOH   C 3 .   ? -14.82061 -21.08961 -2.45046  1.000 12.92477 ? 587 HOH   A O   1 
HETATM 2484 O O   . HOH   C 3 .   ? -19.85133 7.69423   -5.24490  1.000 25.70533 ? 588 HOH   A O   1 
HETATM 2485 O O   . HOH   C 3 .   ? -8.65834  -8.48432  -20.24364 1.000 32.25028 ? 589 HOH   A O   1 
HETATM 2486 O O   . HOH   C 3 .   ? -17.31991 3.24623   6.88486   1.000 28.80629 ? 590 HOH   A O   1 
HETATM 2487 O O   . HOH   C 3 .   ? -6.76257  2.16008   5.62235   1.000 31.68050 ? 591 HOH   A O   1 
HETATM 2488 O O   . HOH   C 3 .   ? -4.85120  -21.44953 13.52997  1.000 27.70430 ? 592 HOH   A O   1 
HETATM 2489 O O   . HOH   C 3 .   ? -23.966   -29.120   -0.275    1.000 29.43455 ? 593 HOH   A O   1 
HETATM 2490 O O   . HOH   C 3 .   ? -12.91209 -14.56805 7.17964   1.000 18.64019 ? 594 HOH   A O   1 
HETATM 2491 O O   . HOH   C 3 .   ? -0.00000  -8.49191  0.00000   0.50  16.20559 ? 595 HOH   A O   1 
HETATM 2492 O O   . HOH   C 3 .   ? -6.33819  -19.85752 19.90443  1.000 31.41688 ? 596 HOH   A O   1 
HETATM 2493 O O   . HOH   C 3 .   ? -23.73760 -43.65809 4.68071   1.000 34.17133 ? 597 HOH   A O   1 
HETATM 2494 O O   . HOH   C 3 .   ? -5.36330  -22.15212 -17.64888 1.000 25.81605 ? 598 HOH   A O   1 
HETATM 2495 O O   . HOH   C 3 .   ? -7.08163  -15.97141 9.22608   1.000 32.85975 ? 599 HOH   A O   1 
HETATM 2496 O O   . HOH   C 3 .   ? 0.57712   -20.20002 -12.91325 1.000 21.47890 ? 600 HOH   A O   1 
HETATM 2497 O O   . HOH   C 3 .   ? -3.81587  -34.78473 9.71690   1.000 27.32418 ? 601 HOH   A O   1 
HETATM 2498 O O   . HOH   C 3 .   ? -19.90295 -25.90825 28.70618  1.000 35.65119 ? 602 HOH   A O   1 
HETATM 2499 O O   . HOH   C 3 .   ? -2.23375  14.36753  -15.39134 1.000 38.84901 ? 603 HOH   A O   1 
HETATM 2500 O O   . HOH   C 3 .   ? -13.12384 -29.63027 24.43644  1.000 33.86296 ? 604 HOH   A O   1 
HETATM 2501 O O   . HOH   C 3 .   ? -6.21064  -6.83827  0.06283   1.000 15.06187 ? 605 HOH   A O   1 
HETATM 2502 O O   . HOH   C 3 .   ? 4.08301   -9.95392  -12.74883 1.000 49.16641 ? 606 HOH   A O   1 
HETATM 2503 O O   . HOH   C 3 .   ? -7.04022  -25.54332 8.53539   1.000 31.89950 ? 607 HOH   A O   1 
HETATM 2504 O O   . HOH   C 3 .   ? -7.39945  -3.64869  -23.67556 1.000 35.44269 ? 608 HOH   A O   1 
HETATM 2505 O O   . HOH   C 3 .   ? -24.90996 -37.93857 1.40288   1.000 34.92675 ? 609 HOH   A O   1 
HETATM 2506 O O   . HOH   C 3 .   ? -15.30169 -46.73672 5.60603   1.000 34.93884 ? 610 HOH   A O   1 
HETATM 2507 O O   . HOH   C 3 .   ? 1.29212   -21.16050 -15.35019 1.000 24.07408 ? 611 HOH   A O   1 
HETATM 2508 O O   . HOH   C 3 .   ? -32.86961 -18.40222 17.96070  1.000 23.65266 ? 612 HOH   A O   1 
HETATM 2509 O O   . HOH   C 3 .   ? -16.40910 -22.11856 -9.20496  1.000 17.00195 ? 613 HOH   A O   1 
HETATM 2510 O O   . HOH   C 3 .   ? -10.08305 -25.61125 -6.75462  1.000 16.24023 ? 614 HOH   A O   1 
HETATM 2511 O O   . HOH   C 3 .   ? -17.52805 -31.82643 1.43607   1.000 33.35634 ? 615 HOH   A O   1 
HETATM 2512 O O   . HOH   C 3 .   ? 5.28312   1.28330   -17.62806 1.000 28.52628 ? 616 HOH   A O   1 
HETATM 2513 O O   . HOH   C 3 .   ? -28.64127 -2.35584  -3.41209  1.000 18.78825 ? 617 HOH   A O   1 
HETATM 2514 O O   . HOH   C 3 .   ? -31.01249 -31.06499 7.83624   1.000 24.97257 ? 618 HOH   A O   1 
HETATM 2515 O O   . HOH   C 3 .   ? -8.26601  -25.80988 -12.82314 1.000 21.89772 ? 619 HOH   A O   1 
HETATM 2516 O O   . HOH   C 3 .   ? -15.02775 -32.97808 1.68409   1.000 26.88506 ? 620 HOH   A O   1 
HETATM 2517 O O   . HOH   C 3 .   ? -1.64970  -38.03451 13.76367  1.000 33.09371 ? 621 HOH   A O   1 
HETATM 2518 O O   . HOH   C 3 .   ? -11.08732 -25.49555 23.14590  1.000 26.75698 ? 622 HOH   A O   1 
HETATM 2519 O O   . HOH   C 3 .   ? -19.36488 -18.12451 5.51444   1.000 18.76895 ? 623 HOH   A O   1 
HETATM 2520 O O   . HOH   C 3 .   ? -12.86418 -37.26508 1.69277   1.000 25.94090 ? 624 HOH   A O   1 
HETATM 2521 O O   . HOH   C 3 .   ? -2.43917  -30.76381 21.43129  1.000 37.13355 ? 625 HOH   A O   1 
HETATM 2522 O O   . HOH   C 3 .   ? -15.04437 -41.75830 16.50420  1.000 30.54268 ? 626 HOH   A O   1 
HETATM 2523 O O   . HOH   C 3 .   ? -9.56750  -21.72446 -17.53785 1.000 25.13716 ? 627 HOH   A O   1 
HETATM 2524 O O   . HOH   C 3 .   ? -7.15855  -18.74253 -16.45024 1.000 32.96946 ? 628 HOH   A O   1 
HETATM 2525 O O   . HOH   C 3 .   ? -7.78351  -20.06355 7.90216   1.000 23.71198 ? 629 HOH   A O   1 
HETATM 2526 O O   . HOH   C 3 .   ? -28.85459 -25.71772 3.97013   1.000 34.03809 ? 630 HOH   A O   1 
HETATM 2527 O O   . HOH   C 3 .   ? -15.98892 -28.41828 0.34554   1.000 28.61308 ? 631 HOH   A O   1 
HETATM 2528 O O   . HOH   C 3 .   ? 1.11229   -12.65630 -12.65950 1.000 17.09440 ? 632 HOH   A O   1 
HETATM 2529 O O   . HOH   C 3 .   ? -17.77798 -5.35396  -17.04044 1.000 21.40517 ? 633 HOH   A O   1 
HETATM 2530 O O   . HOH   C 3 .   ? -14.77942 -15.48920 9.08154   1.000 21.53108 ? 634 HOH   A O   1 
HETATM 2531 O O   . HOH   C 3 .   ? -10.09707 -21.55593 23.83845  1.000 36.92473 ? 635 HOH   A O   1 
HETATM 2532 O O   . HOH   C 3 .   ? -13.63263 -8.26400  -18.68058 1.000 21.74799 ? 636 HOH   A O   1 
HETATM 2533 O O   . HOH   C 3 .   ? -14.73884 7.49318   5.03334   1.000 34.14600 ? 637 HOH   A O   1 
HETATM 2534 O O   . HOH   C 3 .   ? -2.36947  -15.33217 2.44043   1.000 11.28587 ? 638 HOH   A O   1 
HETATM 2535 O O   . HOH   C 3 .   ? -1.16480  -19.63528 3.97000   1.000 12.26535 ? 639 HOH   A O   1 
HETATM 2536 O O   . HOH   C 3 .   ? -12.03781 -29.34485 -1.95646  1.000 23.74130 ? 640 HOH   A O   1 
HETATM 2537 O O   . HOH   C 3 .   ? -25.85712 -17.10250 20.93688  1.000 38.34404 ? 641 HOH   A O   1 
HETATM 2538 O O   . HOH   C 3 .   ? 1.10829   -11.90642 -8.08586  1.000 13.72565 ? 642 HOH   A O   1 
HETATM 2539 O O   . HOH   C 3 .   ? -17.20753 -6.46168  -20.20042 1.000 29.57308 ? 643 HOH   A O   1 
HETATM 2540 O O   . HOH   C 3 .   ? -31.05464 -23.90857 9.34205   1.000 26.35187 ? 644 HOH   A O   1 
HETATM 2541 O O   . HOH   C 3 .   ? -23.71576 -16.88883 -0.24781  1.000 19.61010 ? 645 HOH   A O   1 
HETATM 2542 O O   . HOH   C 3 .   ? 2.45672   -17.19705 -20.93140 1.000 33.39695 ? 646 HOH   A O   1 
HETATM 2543 O O   . HOH   C 3 .   ? -7.36138  4.66073   -2.39953  1.000 22.34811 ? 647 HOH   A O   1 
HETATM 2544 O O   . HOH   C 3 .   ? -16.13542 -39.91308 3.64266   1.000 29.49774 ? 648 HOH   A O   1 
HETATM 2545 O O   . HOH   C 3 .   ? -19.20517 -6.38489  -19.12858 1.000 31.91187 ? 649 HOH   A O   1 
HETATM 2546 O O   . HOH   C 3 .   ? -23.76083 -39.85305 3.29035   1.000 39.08916 ? 650 HOH   A O   1 
HETATM 2547 O O   . HOH   C 3 .   ? -18.13445 -14.24828 15.33106  1.000 31.34507 ? 651 HOH   A O   1 
HETATM 2548 O O   . HOH   C 3 .   ? -26.07203 -29.14046 23.37605  1.000 32.36015 ? 652 HOH   A O   1 
HETATM 2549 O O   . HOH   C 3 .   ? -22.11154 0.79065   -8.21063  1.000 34.49180 ? 653 HOH   A O   1 
HETATM 2550 O O   . HOH   C 3 .   ? -18.75740 -39.17936 4.60285   1.000 32.00887 ? 654 HOH   A O   1 
HETATM 2551 O O   . HOH   C 3 .   ? -3.00042  -23.93324 1.95617   1.000 21.05507 ? 655 HOH   A O   1 
HETATM 2552 O O   . HOH   C 3 .   ? -2.44843  -5.34111  2.24929   1.000 15.89043 ? 656 HOH   A O   1 
HETATM 2553 O O   . HOH   C 3 .   ? -20.72002 2.49355   -11.71609 1.000 25.55913 ? 657 HOH   A O   1 
HETATM 2554 O O   . HOH   C 3 .   ? 1.69205   -20.63886 -22.14370 1.000 30.39255 ? 658 HOH   A O   1 
HETATM 2555 O O   . HOH   C 3 .   ? -5.82968  9.14897   -1.94633  1.000 42.09075 ? 659 HOH   A O   1 
HETATM 2556 O O   . HOH   C 3 .   ? -25.07802 -31.67111 24.67633  1.000 33.08017 ? 660 HOH   A O   1 
HETATM 2557 O O   . HOH   C 3 .   ? 4.49462   -7.37588  -24.32088 1.000 38.47346 ? 661 HOH   A O   1 
HETATM 2558 O O   . HOH   C 3 .   ? -25.57136 -26.19605 5.86181   1.000 21.14894 ? 662 HOH   A O   1 
HETATM 2559 O O   . HOH   C 3 .   ? -0.05535  -23.37845 -10.62108 1.000 22.82686 ? 663 HOH   A O   1 
HETATM 2560 O O   . HOH   C 3 .   ? 5.64758   -16.82393 -13.50905 1.000 28.81687 ? 664 HOH   A O   1 
HETATM 2561 O O   . HOH   C 3 .   ? -19.07752 -19.86623 24.79330  1.000 32.39154 ? 665 HOH   A O   1 
HETATM 2562 O O   . HOH   C 3 .   ? -34.02065 -25.47285 14.64855  1.000 31.34296 ? 666 HOH   A O   1 
HETATM 2563 O O   . HOH   C 3 .   ? -11.30965 -9.55859  4.37191   1.000 16.20893 ? 667 HOH   A O   1 
HETATM 2564 O O   . HOH   C 3 .   ? -2.12706  -9.45466  -22.14361 1.000 45.88274 ? 668 HOH   A O   1 
HETATM 2565 O O   . HOH   C 3 .   ? -11.05883 -7.57664  -24.90133 1.000 38.00843 ? 669 HOH   A O   1 
HETATM 2566 O O   . HOH   C 3 .   ? -2.91250  -1.19837  -4.05081  1.000 23.49002 ? 670 HOH   A O   1 
HETATM 2567 O O   . HOH   C 3 .   ? -5.52795  -35.81912 22.32311  1.000 33.51109 ? 671 HOH   A O   1 
HETATM 2568 O O   . HOH   C 3 .   ? 1.35272   -23.75782 -19.62161 1.000 27.53424 ? 672 HOH   A O   1 
HETATM 2569 O O   . HOH   C 3 .   ? 1.47066   -13.36714 -4.25097  1.000 9.17277  ? 673 HOH   A O   1 
HETATM 2570 O O   . HOH   C 3 .   ? -4.38360  -8.59053  -14.24841 1.000 15.23268 ? 674 HOH   A O   1 
HETATM 2571 O O   . HOH   C 3 .   ? 2.03623   -12.22173 -16.13325 1.000 23.65119 ? 675 HOH   A O   1 
HETATM 2572 O O   . HOH   C 3 .   ? 4.57124   -3.00587  -9.15989  1.000 23.12256 ? 676 HOH   A O   1 
HETATM 2573 O O   . HOH   C 3 .   ? -22.18909 -2.15826  6.19100   1.000 29.99162 ? 677 HOH   A O   1 
HETATM 2574 O O   . HOH   C 3 .   ? -25.73637 -1.15009  -6.56903  1.000 26.65610 ? 678 HOH   A O   1 
HETATM 2575 O O   . HOH   C 3 .   ? -22.19118 -16.41758 9.05172   1.000 15.35091 ? 679 HOH   A O   1 
HETATM 2576 O O   . HOH   C 3 .   ? -9.42130  -37.38079 24.17878  1.000 34.83644 ? 680 HOH   A O   1 
HETATM 2577 O O   . HOH   C 3 .   ? -20.06516 -35.71351 23.49452  1.000 31.84609 ? 681 HOH   A O   1 
HETATM 2578 O O   . HOH   C 3 .   ? -25.099   -1.386    -16.118   1.000 37.73844 ? 682 HOH   A O   1 
HETATM 2579 O O   . HOH   C 3 .   ? 1.39054   -13.65113 -10.18246 1.000 13.85879 ? 683 HOH   A O   1 
HETATM 2580 O O   . HOH   C 3 .   ? -4.96348  -0.93532  4.41599   1.000 21.45673 ? 684 HOH   A O   1 
HETATM 2581 O O   . HOH   C 3 .   ? -27.65498 -14.25382 12.49483  1.000 36.36635 ? 685 HOH   A O   1 
HETATM 2582 O O   . HOH   C 3 .   ? -3.57476  6.41635   -27.50955 1.000 35.74967 ? 686 HOH   A O   1 
HETATM 2583 O O   . HOH   C 3 .   ? 3.89413   2.01407   -12.56032 1.000 25.69976 ? 687 HOH   A O   1 
HETATM 2584 O O   . HOH   C 3 .   ? -10.14619 4.19960   5.91384   1.000 21.92742 ? 688 HOH   A O   1 
HETATM 2585 O O   . HOH   C 3 .   ? 0.59014   8.77184   -14.76168 1.000 26.45187 ? 689 HOH   A O   1 
HETATM 2586 O O   . HOH   C 3 .   ? -14.99869 -11.85024 8.94894   1.000 25.44326 ? 690 HOH   A O   1 
HETATM 2587 O O   . HOH   C 3 .   ? -18.72071 6.71276   3.39488   1.000 34.70279 ? 691 HOH   A O   1 
HETATM 2588 O O   . HOH   C 3 .   ? -24.407   -12.597   -11.518   1.000 35.04278 ? 692 HOH   A O   1 
HETATM 2589 O O   . HOH   C 3 .   ? -12.83220 -18.17257 12.47550  1.000 21.23944 ? 693 HOH   A O   1 
HETATM 2590 O O   . HOH   C 3 .   ? -18.79524 -34.82891 2.70828   1.000 24.23978 ? 694 HOH   A O   1 
HETATM 2591 O O   . HOH   C 3 .   ? -31.50868 -28.49068 10.50747  1.000 33.60530 ? 695 HOH   A O   1 
HETATM 2592 O O   . HOH   C 3 .   ? -31.44708 -34.01534 10.28345  1.000 35.20539 ? 696 HOH   A O   1 
HETATM 2593 O O   . HOH   C 3 .   ? -0.69762  -24.90074 -12.95244 1.000 23.54444 ? 697 HOH   A O   1 
HETATM 2594 O O   . HOH   C 3 .   ? -26.23462 -12.12703 13.26634  1.000 50.68150 ? 698 HOH   A O   1 
HETATM 2595 O O   . HOH   C 3 .   ? -8.26630  -27.41800 9.68608   1.000 19.04400 ? 699 HOH   A O   1 
HETATM 2596 O O   . HOH   C 3 .   ? 1.36227   -2.34293  -26.89729 1.000 30.06753 ? 700 HOH   A O   1 
HETATM 2597 O O   . HOH   C 3 .   ? -14.29383 -24.89020 25.80160  1.000 29.86321 ? 701 HOH   A O   1 
HETATM 2598 O O   . HOH   C 3 .   ? -0.00000  -16.62511 0.00000   0.50  10.63757 ? 702 HOH   A O   1 
HETATM 2599 O O   . HOH   C 3 .   ? -25.86009 1.18821   -2.87861  1.000 35.38078 ? 703 HOH   A O   1 
HETATM 2600 O O   . HOH   C 3 .   ? -4.04196  8.71150   -3.45902  1.000 35.24986 ? 704 HOH   A O   1 
HETATM 2601 O O   . HOH   C 3 .   ? -4.08035  11.57885  -21.55522 1.000 29.28469 ? 705 HOH   A O   1 
HETATM 2602 O O   . HOH   C 3 .   ? -6.69729  -31.31193 21.63647  1.000 28.44260 ? 706 HOH   A O   1 
HETATM 2603 O O   . HOH   C 3 .   ? -1.30741  -24.94509 17.24795  1.000 22.37069 ? 707 HOH   A O   1 
HETATM 2604 O O   . HOH   C 3 .   ? -19.61794 -22.09844 -7.50256  1.000 27.36198 ? 708 HOH   A O   1 
HETATM 2605 O O   . HOH   C 3 .   ? -18.70894 -16.03217 -19.39187 1.000 26.21863 ? 709 HOH   A O   1 
HETATM 2606 O O   . HOH   C 3 .   ? -21.89185 -17.19211 6.30395   1.000 12.98061 ? 710 HOH   A O   1 
HETATM 2607 O O   . HOH   C 3 .   ? -13.53686 -29.98471 -0.03276  1.000 32.74202 ? 711 HOH   A O   1 
HETATM 2608 O O   . HOH   C 3 .   ? -4.33210  -21.07368 6.52487   1.000 19.89718 ? 712 HOH   A O   1 
HETATM 2609 O O   . HOH   C 3 .   ? -11.40255 -36.02243 25.25143  1.000 33.95090 ? 713 HOH   A O   1 
HETATM 2610 O O   . HOH   C 3 .   ? -25.22619 -26.59833 0.99106   1.000 34.42049 ? 714 HOH   A O   1 
HETATM 2611 O O   . HOH   C 3 .   ? -2.92891  -13.47400 6.53584   1.000 17.25161 ? 715 HOH   A O   1 
HETATM 2612 O O   . HOH   C 3 .   ? 0.32678   -17.28238 -2.75690  1.000 12.19301 ? 716 HOH   A O   1 
HETATM 2613 O O   . HOH   C 3 .   ? -31.07059 -34.78678 15.01188  1.000 24.67292 ? 717 HOH   A O   1 
HETATM 2614 O O   . HOH   C 3 .   ? -25.70760 -31.41359 0.00000   0.50  20.15754 ? 718 HOH   A O   1 
HETATM 2615 O O   . HOH   C 3 .   ? -11.86922 6.20500   4.34867   1.000 26.11753 ? 719 HOH   A O   1 
HETATM 2616 O O   . HOH   C 3 .   ? -14.87099 -6.61999  -22.66934 1.000 34.12352 ? 720 HOH   A O   1 
HETATM 2617 O O   . HOH   C 3 .   ? -4.46624  -28.28037 -0.69730  1.000 22.06834 ? 721 HOH   A O   1 
HETATM 2618 O O   . HOH   C 3 .   ? 4.74880   -3.30125  -6.73552  1.000 21.11166 ? 722 HOH   A O   1 
HETATM 2619 O O   . HOH   C 3 .   ? -0.63706  -27.86884 17.11123  1.000 23.90148 ? 723 HOH   A O   1 
HETATM 2620 O O   . HOH   C 3 .   ? -31.69867 -36.31129 8.81488   1.000 31.91350 ? 724 HOH   A O   1 
HETATM 2621 O O   . HOH   C 3 .   ? -1.31616  -30.02307 -7.40677  1.000 28.87360 ? 725 HOH   A O   1 
HETATM 2622 O O   . HOH   C 3 .   ? -4.50181  -18.77752 -18.32739 1.000 28.59293 ? 726 HOH   A O   1 
HETATM 2623 O O   . HOH   C 3 .   ? -5.24589  -13.46276 8.11903   1.000 24.39394 ? 727 HOH   A O   1 
HETATM 2624 O O   . HOH   C 3 .   ? 2.41476   -17.12996 -9.29162  1.000 19.53235 ? 728 HOH   A O   1 
HETATM 2625 O O   . HOH   C 3 .   ? -7.85351  -28.49613 24.42152  1.000 29.35208 ? 729 HOH   A O   1 
HETATM 2626 O O   . HOH   C 3 .   ? -8.23156  -3.92880  -25.77232 1.000 38.10690 ? 730 HOH   A O   1 
HETATM 2627 O O   . HOH   C 3 .   ? -32.32065 -25.19896 18.37169  1.000 33.55368 ? 731 HOH   A O   1 
HETATM 2628 O O   . HOH   C 3 .   ? -22.68566 -43.16994 11.09476  1.000 37.44088 ? 732 HOH   A O   1 
HETATM 2629 O O   . HOH   C 3 .   ? -27.82805 -20.77461 2.21065   1.000 23.92754 ? 733 HOH   A O   1 
HETATM 2630 O O   . HOH   C 3 .   ? -17.54362 -8.50444  -21.47302 1.000 38.44839 ? 734 HOH   A O   1 
HETATM 2631 O O   . HOH   C 3 .   ? -15.224   -25.253   -16.321   1.000 29.28210 ? 735 HOH   A O   1 
HETATM 2632 O O   . HOH   C 3 .   ? 0.13866   10.89692  -15.87816 1.000 31.93100 ? 736 HOH   A O   1 
HETATM 2633 O O   . HOH   C 3 .   ? -21.52325 -26.19951 -0.81554  1.000 44.22697 ? 737 HOH   A O   1 
HETATM 2634 O O   . HOH   C 3 .   ? -22.21207 -37.70547 0.73611   1.000 48.70492 ? 738 HOH   A O   1 
HETATM 2635 O O   . HOH   C 3 .   ? -24.25438 2.81025   -1.83330  1.000 36.76903 ? 739 HOH   A O   1 
HETATM 2636 O O   . HOH   C 3 .   ? -20.98277 -34.08947 25.36077  1.000 32.06657 ? 740 HOH   A O   1 
HETATM 2637 O O   . HOH   C 3 .   ? -19.70915 4.50032   3.06684   1.000 31.21505 ? 741 HOH   A O   1 
HETATM 2638 O O   . HOH   C 3 .   ? -13.10584 -42.21560 17.87347  1.000 35.75417 ? 742 HOH   A O   1 
HETATM 2639 O O   . HOH   C 3 .   ? -23.99399 2.74206   -4.44005  1.000 33.93321 ? 743 HOH   A O   1 
HETATM 2640 O O   . HOH   C 3 .   ? 5.64223   -5.65997  -25.77179 1.000 35.97229 ? 744 HOH   A O   1 
HETATM 2641 O O   . HOH   C 3 .   ? -5.33469  -20.30232 23.58762  1.000 37.25907 ? 745 HOH   A O   1 
HETATM 2642 O O   . HOH   C 3 .   ? -23.98213 2.44459   1.67688   1.000 32.19056 ? 746 HOH   A O   1 
HETATM 2643 O O   . HOH   C 3 .   ? -3.56008  -7.33730  0.89508   1.000 17.25222 ? 747 HOH   A O   1 
HETATM 2644 O O   . HOH   C 3 .   ? -22.43464 3.74188   0.03768   1.000 26.22414 ? 748 HOH   A O   1 
HETATM 2645 O O   . HOH   C 3 .   ? 4.700     -19.097   -21.839   1.000 36.18486 ? 749 HOH   A O   1 
HETATM 2646 O O   . HOH   C 3 .   ? -20.41268 -7.76506  -18.82840 1.000 31.37843 ? 750 HOH   A O   1 
HETATM 2647 O O   . HOH   C 3 .   ? 4.10398   3.69275   -17.59168 1.000 26.64644 ? 751 HOH   A O   1 
HETATM 2648 O O   . HOH   C 3 .   ? -6.01114  7.31913   -29.10635 1.000 38.68700 ? 752 HOH   A O   1 
HETATM 2649 O O   . HOH   C 3 .   ? -15.09843 -9.84402  9.86168   1.000 38.73999 ? 753 HOH   A O   1 
HETATM 2650 O O   . HOH   C 3 .   ? -7.46875  -21.10480 12.16689  1.000 26.22875 ? 754 HOH   A O   1 
HETATM 2651 O O   . HOH   C 3 .   ? -24.30651 1.00395   -7.20725  1.000 29.58457 ? 755 HOH   A O   1 
HETATM 2652 O O   . HOH   C 3 .   ? -3.75693  -19.36113 12.89296  1.000 33.64243 ? 756 HOH   A O   1 
HETATM 2653 O O   . HOH   C 3 .   ? -1.040    -24.000   14.592    1.000 22.11161 ? 757 HOH   A O   1 
HETATM 2654 O O   . HOH   C 3 .   ? -15.23343 -16.61170 16.44537  1.000 28.42277 ? 758 HOH   A O   1 
HETATM 2655 O O   . HOH   C 3 .   ? -12.74653 -26.75086 24.87114  1.000 35.52431 ? 759 HOH   A O   1 
HETATM 2656 O O   . HOH   C 3 .   ? -23.28919 -33.25507 26.21787  1.000 40.13294 ? 760 HOH   A O   1 
HETATM 2657 O O   . HOH   C 3 .   ? -13.79766 -29.77484 -3.74874  1.000 36.17755 ? 761 HOH   A O   1 
HETATM 2658 O O   . HOH   C 3 .   ? -5.43600  -37.72458 0.48585   1.000 36.19393 ? 762 HOH   A O   1 
HETATM 2659 O O   . HOH   C 3 .   ? -2.98413  -24.09680 10.48345  1.000 25.05760 ? 763 HOH   A O   1 
HETATM 2660 O O   . HOH   C 3 .   ? 7.07206   -14.23831 -16.02451 1.000 38.49939 ? 764 HOH   A O   1 
HETATM 2661 O O   . HOH   C 3 .   ? -10.76234 -9.71230  7.16851   1.000 20.57918 ? 765 HOH   A O   1 
HETATM 2662 O O   . HOH   C 3 .   ? -29.14678 -27.05891 21.86285  1.000 36.22666 ? 766 HOH   A O   1 
HETATM 2663 O O   . HOH   C 3 .   ? 3.38412   -12.64791 -14.29817 1.000 28.38268 ? 767 HOH   A O   1 
HETATM 2664 O O   . HOH   C 3 .   ? -0.961    -27.353   -12.600   1.000 26.48228 ? 768 HOH   A O   1 
HETATM 2665 O O   . HOH   C 3 .   ? 2.77478   -9.96867  -8.37457  1.000 27.13434 ? 769 HOH   A O   1 
HETATM 2666 O O   . HOH   C 3 .   ? -15.46454 13.52434  -1.08101  1.000 35.89192 ? 770 HOH   A O   1 
HETATM 2667 O O   . HOH   C 3 .   ? -11.31394 -9.44210  -19.51465 1.000 29.95096 ? 771 HOH   A O   1 
HETATM 2668 O O   . HOH   C 3 .   ? -4.08636  -24.46241 -21.75554 1.000 36.64903 ? 772 HOH   A O   1 
HETATM 2669 O O   . HOH   C 3 .   ? -33.50670 -28.79186 11.15117  1.000 43.03119 ? 773 HOH   A O   1 
HETATM 2670 O O   . HOH   C 3 .   ? -7.90820  -28.15177 -14.54818 1.000 29.22142 ? 774 HOH   A O   1 
HETATM 2671 O O   . HOH   C 3 .   ? -34.45661 -29.19776 13.65768  1.000 35.05572 ? 775 HOH   A O   1 
HETATM 2672 O O   . HOH   C 3 .   ? -1.25113  -25.20497 -5.35185  1.000 30.77287 ? 776 HOH   A O   1 
HETATM 2673 O O   . HOH   C 3 .   ? -28.62156 -18.24950 20.73540  1.000 45.83259 ? 777 HOH   A O   1 
HETATM 2674 O O   . HOH   C 3 .   ? -8.53817  -21.87906 8.81017   1.000 32.57295 ? 778 HOH   A O   1 
HETATM 2675 O O   . HOH   C 3 .   ? -2.518    -24.603   6.460     1.000 28.61007 ? 779 HOH   A O   1 
HETATM 2676 O O   . HOH   C 3 .   ? 4.01758   -9.62428  -10.84054 1.000 34.78964 ? 780 HOH   A O   1 
HETATM 2677 O O   . HOH   C 3 .   ? 0.901     -24.943   -21.916   1.000 29.70968 ? 781 HOH   A O   1 
HETATM 2678 O O   . HOH   C 3 .   ? -12.48129 -16.76086 15.13118  1.000 29.38426 ? 782 HOH   A O   1 
HETATM 2679 O O   . HOH   C 3 .   ? -26.35238 -26.40112 21.93114  1.000 35.48317 ? 783 HOH   A O   1 
HETATM 2680 O O   . HOH   C 3 .   ? -2.40877  -26.14589 2.31031   1.000 24.18505 ? 784 HOH   A O   1 
HETATM 2681 O O   . HOH   C 3 .   ? -17.50595 -33.04160 27.87733  1.000 36.37949 ? 785 HOH   A O   1 
HETATM 2682 O O   . HOH   C 3 .   ? -0.34793  -26.72210 -7.85121  1.000 31.40067 ? 786 HOH   A O   1 
HETATM 2683 O O   . HOH   C 3 .   ? -29.356   -38.072   1.322     1.000 37.80465 ? 787 HOH   A O   1 
HETATM 2684 O O   . HOH   C 3 .   ? -3.482    -23.059   5.446     1.000 22.26277 ? 788 HOH   A O   1 
HETATM 2685 O O   . HOH   C 3 .   ? -15.14057 -17.77023 18.74030  1.000 32.70778 ? 789 HOH   A O   1 
HETATM 2686 O O   . HOH   C 3 .   ? -18.78514 -25.22364 -2.29190  1.000 35.53258 ? 790 HOH   A O   1 
HETATM 2687 O O   . HOH   C 3 .   ? -29.09531 -20.00573 18.62498  1.000 37.60167 ? 791 HOH   A O   1 
HETATM 2688 O O   . HOH   C 3 .   ? -1.84721  6.50624   -7.50821  1.000 32.75989 ? 792 HOH   A O   1 
HETATM 2689 O O   . HOH   C 3 .   ? -1.33016  -34.87977 10.54934  1.000 31.70219 ? 793 HOH   A O   1 
HETATM 2690 O O   . HOH   C 3 .   ? 4.820     0.609     -6.483    1.000 28.20391 ? 794 HOH   A O   1 
HETATM 2691 O O   . HOH   C 3 .   ? -9.03598  -40.16650 24.63335  1.000 36.78352 ? 795 HOH   A O   1 
HETATM 2692 O O   . HOH   C 3 .   ? -32.01565 -25.40138 10.59461  1.000 34.32399 ? 796 HOH   A O   1 
HETATM 2693 O O   . HOH   C 3 .   ? -11.20191 -17.83861 21.30803  1.000 35.30229 ? 797 HOH   A O   1 
HETATM 2694 O O   . HOH   C 3 .   ? -6.72138  -37.01519 24.22866  1.000 39.85523 ? 798 HOH   A O   1 
HETATM 2695 O O   . HOH   C 3 .   ? -22.52610 -41.07945 13.06905  1.000 36.11823 ? 799 HOH   A O   1 
HETATM 2696 O O   . HOH   C 3 .   ? -0.80222  -23.67407 -3.69082  1.000 23.73384 ? 800 HOH   A O   1 
HETATM 2697 O O   . HOH   C 3 .   ? -18.09217 14.37188  -5.37249  1.000 32.88504 ? 801 HOH   A O   1 
HETATM 2698 O O   . HOH   C 3 .   ? -19.94920 -37.15050 3.00955   1.000 34.01531 ? 802 HOH   A O   1 
HETATM 2699 O O   . HOH   C 3 .   ? -19.35918 4.07771   4.82854   1.000 30.29982 ? 803 HOH   A O   1 
HETATM 2700 O O   . HOH   C 3 .   ? -23.62226 -25.34192 -1.01973  1.000 39.56861 ? 804 HOH   A O   1 
HETATM 2701 O O   . HOH   C 3 .   ? -0.00000  -23.78630 0.00000   0.50  25.23280 ? 805 HOH   A O   1 
HETATM 2702 O O   . HOH   C 3 .   ? -4.45144  -21.09862 9.21808   1.000 23.85224 ? 806 HOH   A O   1 
HETATM 2703 O O   . HOH   C 3 .   ? -6.65407  -18.20648 9.71399   1.000 28.23714 ? 807 HOH   A O   1 
HETATM 2704 O O   . HOH   C 3 .   ? -2.90094  -29.13828 -19.35824 1.000 36.97989 ? 808 HOH   A O   1 
HETATM 2705 O O   . HOH   C 3 .   ? 1.515     -22.181   -3.498    1.000 18.37155 ? 809 HOH   A O   1 
HETATM 2706 O O   . HOH   C 3 .   ? -18.54488 12.26217  -6.87807  1.000 34.09718 ? 810 HOH   A O   1 
HETATM 2707 O O   . HOH   C 3 .   ? 5.11724   -15.33199 -12.20480 1.000 32.22440 ? 811 HOH   A O   1 
HETATM 2708 O O   . HOH   C 3 .   ? 4.02028   -14.65639 -9.81674  1.000 20.41302 ? 812 HOH   A O   1 
HETATM 2709 O O   . HOH   C 3 .   ? -13.75551 -13.31576 10.03252  1.000 33.32365 ? 813 HOH   A O   1 
HETATM 2710 O O   . HOH   C 3 .   ? -11.21034 -33.32173 25.49562  1.000 33.71721 ? 814 HOH   A O   1 
HETATM 2711 O O   . HOH   C 3 .   ? -11.08718 -16.90858 17.86101  1.000 31.51068 ? 815 HOH   A O   1 
HETATM 2712 O O   . HOH   C 3 .   ? 0.48396   -28.58084 19.68623  1.000 31.25299 ? 816 HOH   A O   1 
HETATM 2713 O O   . HOH   C 3 .   ? -10.29370 -20.52720 11.97468  1.000 27.07975 ? 817 HOH   A O   1 
HETATM 2714 O O   . HOH   C 3 .   ? -1.177    -25.925   6.496     1.000 32.95482 ? 818 HOH   A O   1 
HETATM 2715 O O   . HOH   C 3 .   ? -15.22472 -37.49818 2.82036   1.000 28.45430 ? 819 HOH   A O   1 
HETATM 2716 O O   . HOH   C 3 .   ? 0.01736   -27.82780 21.73310  1.000 34.31107 ? 820 HOH   A O   1 
HETATM 2717 O O   . HOH   C 3 .   ? -25.70760 -21.65132 0.00000   0.50  28.04871 ? 821 HOH   A O   1 
HETATM 2718 O O   . HOH   C 3 .   ? -15.27885 7.90095   7.84745   1.000 41.36451 ? 822 HOH   A O   1 
HETATM 2719 O O   . HOH   C 3 .   ? -16.15208 -31.20070 -4.01047  1.000 37.18455 ? 823 HOH   A O   1 
HETATM 2720 O O   . HOH   C 3 .   ? -0.20899  -29.46511 10.99287  1.000 35.54551 ? 824 HOH   A O   1 
HETATM 2721 O O   . HOH   C 3 .   ? -16.87315 -16.46658 20.39738  1.000 30.69294 ? 825 HOH   A O   1 
HETATM 2722 O O   . HOH   C 3 .   ? -16.47933 -14.34181 19.49122  1.000 31.87227 ? 826 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   ? 0.19493 0.37202 0.27833 0.01956  0.09280  0.07599  1   SER   A N   
2    C CA  . SER   A 1   ? 0.17692 0.34817 0.25880 0.01139  0.08309  0.08008  1   SER   A CA  
3    C C   . SER   A 1   ? 0.16466 0.33445 0.26159 0.00712  0.07273  0.08017  1   SER   A C   
4    O O   . SER   A 1   ? 0.15968 0.33323 0.26762 0.01087  0.07219  0.07756  1   SER   A O   
5    C CB  . SER   A 1   ? 0.23631 0.41296 0.32308 0.00523  0.08427  0.09054  1   SER   A CB  
6    O OG  . SER   A 1   ? 0.23593 0.42247 0.34561 0.00134  0.08235  0.09725  1   SER   A OG  
7    N N   . GLY   A 2   ? 0.17025 0.33363 0.26679 -0.00076 0.06444  0.08307  2   GLY   A N   
8    C CA  . GLY   A 2   ? 0.16443 0.32376 0.26969 -0.00564 0.05421  0.08122  2   GLY   A CA  
9    C C   . GLY   A 2   ? 0.15740 0.30568 0.24810 -0.00429 0.05051  0.07438  2   GLY   A C   
10   O O   . GLY   A 2   ? 0.17853 0.32357 0.25357 0.00217  0.05570  0.06922  2   GLY   A O   
11   N N   . PHE   A 3   ? 0.15350 0.29565 0.24861 -0.01103 0.04116  0.07383  3   PHE   A N   
12   C CA  . PHE   A 3   ? 0.18466 0.31323 0.26564 -0.01000 0.03581  0.06627  3   PHE   A CA  
13   C C   . PHE   A 3   ? 0.19371 0.31747 0.28163 -0.01428 0.02597  0.06232  3   PHE   A C   
14   O O   . PHE   A 3   ? 0.22734 0.35025 0.32404 -0.02300 0.02036  0.06580  3   PHE   A O   
15   C CB  . PHE   A 3   ? 0.20504 0.32216 0.27396 -0.01335 0.03422  0.06821  3   PHE   A CB  
16   C CG  . PHE   A 3   ? 0.15869 0.26279 0.20966 -0.00902 0.03077  0.05994  3   PHE   A CG  
17   C CD1 . PHE   A 3   ? 0.20478 0.31046 0.24164 -0.00223 0.03590  0.05631  3   PHE   A CD1 
18   C CD2 . PHE   A 3   ? 0.20743 0.29840 0.25577 -0.01210 0.02259  0.05545  3   PHE   A CD2 
19   C CE1 . PHE   A 3   ? 0.22941 0.32500 0.25157 0.00052  0.03175  0.04913  3   PHE   A CE1 
20   C CE2 . PHE   A 3   ? 0.21439 0.29595 0.24903 -0.00817 0.01973  0.04899  3   PHE   A CE2 
21   C CZ  . PHE   A 3   ? 0.21272 0.29721 0.23513 -0.00231 0.02370  0.04622  3   PHE   A CZ  
22   N N   . ARG   A 4   ? 0.16892 0.28875 0.25172 -0.00872 0.02389  0.05493  4   ARG   A N   
23   C CA  . ARG   A 4   ? 0.15167 0.26903 0.23966 -0.01170 0.01534  0.05193  4   ARG   A CA  
24   C C   . ARG   A 4   ? 0.12592 0.22843 0.19826 -0.00865 0.01160  0.04320  4   ARG   A C   
25   O O   . ARG   A 4   ? 0.15753 0.25542 0.21880 -0.00255 0.01591  0.03902  4   ARG   A O   
26   C CB  . ARG   A 4   ? 0.16965 0.30106 0.27276 -0.00757 0.01692  0.05472  4   ARG   A CB  
27   C CG  . ARG   A 4   ? 0.13018 0.27538 0.25027 -0.01212 0.01724  0.06312  4   ARG   A CG  
28   C CD  . ARG   A 4   ? 0.20940 0.35262 0.33370 -0.02146 0.00584  0.06342  4   ARG   A CD  
29   N NE  . ARG   A 4   ? 0.22704 0.38078 0.36477 -0.02440 0.00391  0.06937  4   ARG   A NE  
30   C CZ  . ARG   A 4   ? 0.22077 0.37454 0.36183 -0.03363 -0.00530 0.07028  4   ARG   A CZ  
31   N NH1 . ARG   A 4   ? 0.17579 0.34106 0.32975 -0.03628 -0.00694 0.07638  4   ARG   A NH1 
32   N NH2 . ARG   A 4   ? 0.27558 0.41782 0.40626 -0.04014 -0.01270 0.06460  4   ARG   A NH2 
33   N N   . LYS   A 5   ? 0.16063 0.25643 0.23188 -0.01351 0.00358  0.04042  5   LYS   A N   
34   C CA  . LYS   A 5   ? 0.15413 0.23916 0.21411 -0.01038 0.00044  0.03329  5   LYS   A CA  
35   C C   . LYS   A 5   ? 0.15364 0.24450 0.21863 -0.00401 0.00222  0.03240  5   LYS   A C   
36   O O   . LYS   A 5   ? 0.18136 0.28151 0.25838 -0.00503 -0.00046 0.03629  5   LYS   A O   
37   C CB  . LYS   A 5   ? 0.21784 0.29501 0.27457 -0.01687 -0.00712 0.03069  5   LYS   A CB  
38   C CG  . LYS   A 5   ? 0.23828 0.30231 0.28161 -0.01455 -0.00832 0.02441  5   LYS   A CG  
39   C CD  . LYS   A 5   ? 0.25726 0.31099 0.29538 -0.02060 -0.01259 0.02168  5   LYS   A CD  
40   C CE  . LYS   A 5   ? 0.26881 0.31448 0.30400 -0.02187 -0.00984 0.02301  5   LYS   A CE  
41   N NZ  . LYS   A 5   ? 0.36045 0.39219 0.38888 -0.02490 -0.01195 0.01863  5   LYS   A NZ  
42   N N   . MET   A 6   ? 0.09811 0.18394 0.15474 0.00240  0.00688  0.02788  6   MET   A N   
43   C CA  . MET   A 6   ? 0.13165 0.22073 0.19314 0.00943  0.01147  0.02666  6   MET   A CA  
44   C C   . MET   A 6   ? 0.12805 0.20584 0.18090 0.01183  0.00891  0.02021  6   MET   A C   
45   O O   . MET   A 6   ? 0.16352 0.23263 0.20350 0.01148  0.00858  0.01514  6   MET   A O   
46   C CB  . MET   A 6   ? 0.13827 0.23009 0.19609 0.01450  0.02080  0.02563  6   MET   A CB  
47   C CG  . MET   A 6   ? 0.19562 0.29130 0.26171 0.02203  0.02733  0.02499  6   MET   A CG  
48   S SD  . MET   A 6   ? 0.25767 0.35965 0.32022 0.02726  0.03991  0.02477  6   MET   A SD  
49   C CE  . MET   A 6   ? 0.20929 0.32849 0.28740 0.02202  0.04037  0.03655  6   MET   A CE  
50   N N   . ALA   A 7   ? 0.12000 0.19902 0.18108 0.01411  0.00704  0.02153  7   ALA   A N   
51   C CA  . ALA   A 7   ? 0.09365 0.16210 0.14858 0.01619  0.00537  0.01657  7   ALA   A CA  
52   C C   . ALA   A 7   ? 0.12720 0.19158 0.18332 0.02336  0.01268  0.01281  7   ALA   A C   
53   O O   . ALA   A 7   ? 0.11328 0.18445 0.17685 0.02780  0.01939  0.01484  7   ALA   A O   
54   C CB  . ALA   A 7   ? 0.12156 0.19189 0.18308 0.01431  -0.00088 0.02074  7   ALA   A CB  
55   N N   . PHE   A 8   ? 0.09337 0.14605 0.14215 0.02424  0.01197  0.00690  8   PHE   A N   
56   C CA  . PHE   A 8   ? 0.10124 0.14652 0.15107 0.03036  0.01865  0.00208  8   PHE   A CA  
57   C C   . PHE   A 8   ? 0.09515 0.14337 0.16191 0.03533  0.01989  0.00838  8   PHE   A C   
58   O O   . PHE   A 8   ? 0.09083 0.14367 0.16422 0.03266  0.01334  0.01499  8   PHE   A O   
59   C CB  . PHE   A 8   ? 0.10257 0.13411 0.14106 0.02830  0.01660  -0.00581 8   PHE   A CB  
60   C CG  . PHE   A 8   ? 0.14379 0.17334 0.16635 0.02494  0.01641  -0.01202 8   PHE   A CG  
61   C CD1 . PHE   A 8   ? 0.21520 0.24274 0.22940 0.02777  0.02324  -0.01799 8   PHE   A CD1 
62   C CD2 . PHE   A 8   ? 0.18069 0.21170 0.19688 0.01938  0.00978  -0.01093 8   PHE   A CD2 
63   C CE1 . PHE   A 8   ? 0.28821 0.31604 0.28683 0.02428  0.02207  -0.02217 8   PHE   A CE1 
64   C CE2 . PHE   A 8   ? 0.21678 0.24795 0.22015 0.01677  0.00896  -0.01447 8   PHE   A CE2 
65   C CZ  . PHE   A 8   ? 0.23124 0.26147 0.22548 0.01886  0.01445  -0.01962 8   PHE   A CZ  
66   N N   . PRO   A 9   ? 0.10005 0.14601 0.17381 0.04291  0.02859  0.00684  9   PRO   A N   
67   C CA  . PRO   A 9   ? 0.10377 0.15040 0.19509 0.04904  0.03028  0.01340  9   PRO   A CA  
68   C C   . PRO   A 9   ? 0.13727 0.17297 0.22667 0.04633  0.02418  0.01342  9   PRO   A C   
69   O O   . PRO   A 9   ? 0.12373 0.14587 0.20016 0.04323  0.02356  0.00480  9   PRO   A O   
70   C CB  . PRO   A 9   ? 0.14615 0.18492 0.23984 0.05783  0.04241  0.00735  9   PRO   A CB  
71   C CG  . PRO   A 9   ? 0.12711 0.16849 0.20647 0.05606  0.04701  0.00059  9   PRO   A CG  
72   C CD  . PRO   A 9   ? 0.12218 0.16196 0.18582 0.04642  0.03758  -0.00209 9   PRO   A CD  
73   N N   . SER   A 10  ? 0.09645 0.13972 0.19884 0.04675  0.01912  0.02405  10  SER   A N   
74   C CA  . SER   A 10  ? 0.09928 0.13606 0.19844 0.04254  0.01231  0.02633  10  SER   A CA  
75   C C   . SER   A 10  ? 0.11111 0.13626 0.22052 0.04844  0.01592  0.02881  10  SER   A C   
76   O O   . SER   A 10  ? 0.10662 0.12543 0.21410 0.04512  0.01137  0.03138  10  SER   A O   
77   C CB  . SER   A 10  ? 0.08414 0.13579 0.18683 0.03765  0.00344  0.03638  10  SER   A CB  
78   O OG  . SER   A 10  ? 0.10189 0.16760 0.22218 0.04224  0.00363  0.04682  10  SER   A OG  
79   N N   . GLY   A 11  ? 0.11992 0.14157 0.24061 0.05732  0.02481  0.02838  11  GLY   A N   
80   C CA  . GLY   A 11  ? 0.13033 0.14074 0.26390 0.06386  0.02873  0.03264  11  GLY   A CA  
81   C C   . GLY   A 11  ? 0.14808 0.13800 0.27331 0.06025  0.02811  0.02592  11  GLY   A C   
82   O O   . GLY   A 11  ? 0.17958 0.16390 0.31361 0.06103  0.02591  0.03383  11  GLY   A O   
83   N N   . LYS   A 12  ? 0.14273 0.12200 0.25073 0.05547  0.02970  0.01189  12  LYS   A N   
84   C CA  . LYS   A 12  ? 0.15713 0.11746 0.25776 0.05069  0.02886  0.00462  12  LYS   A CA  
85   C C   . LYS   A 12  ? 0.17536 0.14063 0.27400 0.04317  0.01960  0.01186  12  LYS   A C   
86   O O   . LYS   A 12  ? 0.21451 0.16716 0.31583 0.04067  0.01874  0.01276  12  LYS   A O   
87   C CB  . LYS   A 12  ? 0.21544 0.16753 0.29745 0.04588  0.03061  -0.01093 12  LYS   A CB  
88   C CG  . LYS   A 12  ? 0.26176 0.20629 0.34119 0.05266  0.04107  -0.02044 12  LYS   A CG  
89   C CD  . LYS   A 12  ? 0.32302 0.25776 0.38143 0.04624  0.04128  -0.03584 12  LYS   A CD  
90   C CE  . LYS   A 12  ? 0.37568 0.29339 0.42959 0.05191  0.05244  -0.04804 12  LYS   A CE  
91   N NZ  . LYS   A 12  ? 0.47516 0.40421 0.53383 0.06116  0.06125  -0.04564 12  LYS   A NZ  
92   N N   . VAL   A 13  ? 0.15077 0.13342 0.24448 0.03925  0.01332  0.01674  13  VAL   A N   
93   C CA  . VAL   A 13  ? 0.14031 0.12802 0.23057 0.03273  0.00590  0.02305  13  VAL   A CA  
94   C C   . VAL   A 13  ? 0.12272 0.11812 0.22599 0.03591  0.00338  0.03778  13  VAL   A C   
95   O O   . VAL   A 13  ? 0.12382 0.11714 0.22768 0.03263  0.00006  0.04414  13  VAL   A O   
96   C CB  . VAL   A 13  ? 0.10210 0.10231 0.17992 0.02712  0.00105  0.02047  13  VAL   A CB  
97   C CG1 . VAL   A 13  ? 0.13915 0.14417 0.21204 0.02104  -0.00502 0.02584  13  VAL   A CG1 
98   C CG2 . VAL   A 13  ? 0.11230 0.10648 0.17830 0.02459  0.00312  0.00804  13  VAL   A CG2 
99   N N   . GLU   A 14  ? 0.11504 0.12112 0.22946 0.04215  0.00478  0.04450  14  GLU   A N   
100  C CA  . GLU   A 14  ? 0.11629 0.13222 0.24412 0.04526  0.00133  0.06002  14  GLU   A CA  
101  C C   . GLU   A 14  ? 0.13095 0.13214 0.26597 0.04738  0.00423  0.06423  14  GLU   A C   
102  O O   . GLU   A 14  ? 0.14644 0.15268 0.28208 0.04434  -0.00023 0.07438  14  GLU   A O   
103  C CB  . GLU   A 14  ? 0.11814 0.14588 0.25511 0.05007  0.00384  0.06376  14  GLU   A CB  
104  C CG  . GLU   A 14  ? 0.10515 0.14919 0.23698 0.04668  0.00031  0.06200  14  GLU   A CG  
105  C CD  . GLU   A 14  ? 0.11320 0.16674 0.25511 0.05116  0.00434  0.06470  14  GLU   A CD  
106  O OE1 . GLU   A 14  ? 0.13971 0.19764 0.29203 0.05389  0.00453  0.07367  14  GLU   A OE1 
107  O OE2 . GLU   A 14  ? 0.11146 0.16800 0.25167 0.05231  0.00811  0.05816  14  GLU   A OE2 
108  N N   . GLY   A 15  ? 0.14363 0.12609 0.28208 0.05155  0.01206  0.05549  15  GLY   A N   
109  C CA  . GLY   A 15  ? 0.16082 0.12789 0.30576 0.05259  0.01521  0.05837  15  GLY   A CA  
110  C C   . GLY   A 15  ? 0.16816 0.12587 0.30810 0.04550  0.01161  0.05909  15  GLY   A C   
111  O O   . GLY   A 15  ? 0.17554 0.12173 0.32103 0.04489  0.01349  0.06282  15  GLY   A O   
112  N N   . CYS   A 16  ? 0.14745 0.11166 0.27450 0.03856  0.00666  0.05442  16  CYS   A N   
113  C CA  . CYS   A 16  ? 0.14739 0.10709 0.26724 0.03018  0.00336  0.05439  16  CYS   A CA  
114  C C   . CYS   A 16  ? 0.13863 0.11482 0.25488 0.02658  -0.00290 0.06679  16  CYS   A C   
115  O O   . CYS   A 16  ? 0.13938 0.11392 0.25082 0.02026  -0.00467 0.06886  16  CYS   A O   
116  C CB  . CYS   A 16  ? 0.14119 0.09860 0.24606 0.02340  0.00253  0.03946  16  CYS   A CB  
117  S SG  . CYS   A 16  ? 0.18848 0.12652 0.29177 0.02540  0.00910  0.02299  16  CYS   A SG  
118  N N   . MET   A 17  ? 0.13175 0.12445 0.24931 0.02968  -0.00625 0.07459  17  MET   A N   
119  C CA  . MET   A 17  ? 0.12585 0.13402 0.23353 0.02439  -0.01249 0.08185  17  MET   A CA  
120  C C   . MET   A 17  ? 0.14389 0.15534 0.25739 0.02451  -0.01350 0.09550  17  MET   A C   
121  O O   . MET   A 17  ? 0.16302 0.17466 0.28763 0.02945  -0.01133 0.10030  17  MET   A O   
122  C CB  . MET   A 17  ? 0.14403 0.16930 0.24641 0.02443  -0.01676 0.08174  17  MET   A CB  
123  C CG  . MET   A 17  ? 0.11421 0.13783 0.20760 0.02268  -0.01501 0.06674  17  MET   A CG  
124  S SD  . MET   A 17  ? 0.10796 0.12557 0.18568 0.01508  -0.01492 0.05641  17  MET   A SD  
125  C CE  . MET   A 17  ? 0.21266 0.24479 0.27801 0.00955  -0.02054 0.06311  17  MET   A CE  
126  N N   . VAL   A 18  ? 0.15999 0.17470 0.26498 0.01866  -0.01577 0.10053  18  VAL   A N   
127  C CA  . VAL   A 18  ? 0.18361 0.20320 0.29089 0.01739  -0.01633 0.11210  18  VAL   A CA  
128  C C   . VAL   A 18  ? 0.15557 0.19068 0.24653 0.01146  -0.02090 0.11584  18  VAL   A C   
129  O O   . VAL   A 18  ? 0.15158 0.19071 0.22982 0.00804  -0.02273 0.10911  18  VAL   A O   
130  C CB  . VAL   A 18  ? 0.15954 0.16357 0.27454 0.01614  -0.01193 0.11429  18  VAL   A CB  
131  C CG1 . VAL   A 18  ? 0.17942 0.16462 0.30720 0.02084  -0.00677 0.10702  18  VAL   A CG1 
132  C CG2 . VAL   A 18  ? 0.17076 0.17255 0.27587 0.00932  -0.01189 0.11085  18  VAL   A CG2 
133  N N   . GLN   A 19  ? 0.23358 0.27668 0.32457 0.01037  -0.02224 0.12633  19  GLN   A N   
134  C CA  . GLN   A 19  ? 0.21212 0.26904 0.28658 0.00493  -0.02576 0.12960  19  GLN   A CA  
135  C C   . GLN   A 19  ? 0.19105 0.24379 0.26239 0.00159  -0.02240 0.13406  19  GLN   A C   
136  O O   . GLN   A 19  ? 0.20582 0.25103 0.28990 0.00341  -0.01953 0.14108  19  GLN   A O   
137  C CB  . GLN   A 19  ? 0.21265 0.28318 0.28854 0.00556  -0.03003 0.13844  19  GLN   A CB  
138  C CG  . GLN   A 19  ? 0.25403 0.33811 0.31193 -0.00021 -0.03387 0.14147  19  GLN   A CG  
139  C CD  . GLN   A 19  ? 0.30876 0.40674 0.36876 -0.00023 -0.03932 0.14905  19  GLN   A CD  
140  O OE1 . GLN   A 19  ? 0.37524 0.48434 0.41978 -0.00524 -0.04398 0.14740  19  GLN   A OE1 
141  N NE2 . GLN   A 19  ? 0.30773 0.40465 0.38714 0.00525  -0.03854 0.15709  19  GLN   A NE2 
142  N N   . VAL   A 20  ? 0.18280 0.23972 0.23809 -0.00323 -0.02193 0.12958  20  VAL   A N   
143  C CA  . VAL   A 20  ? 0.20759 0.26315 0.25941 -0.00674 -0.01786 0.13372  20  VAL   A CA  
144  C C   . VAL   A 20  ? 0.18300 0.25257 0.21636 -0.01022 -0.01941 0.13671  20  VAL   A C   
145  O O   . VAL   A 20  ? 0.23855 0.31421 0.25613 -0.01235 -0.02123 0.12894  20  VAL   A O   
146  C CB  . VAL   A 20  ? 0.18846 0.23598 0.23920 -0.00930 -0.01382 0.12570  20  VAL   A CB  
147  C CG1 . VAL   A 20  ? 0.17742 0.22642 0.22604 -0.01329 -0.00902 0.13058  20  VAL   A CG1 
148  C CG2 . VAL   A 20  ? 0.19250 0.22449 0.26007 -0.00679 -0.01257 0.12158  20  VAL   A CG2 
149  N N   . THR   A 21  ? 0.25650 0.33016 0.29123 -0.01089 -0.01851 0.14745  21  THR   A N   
150  C CA  . THR   A 21  ? 0.25046 0.33640 0.26679 -0.01425 -0.01941 0.15078  21  THR   A CA  
151  C C   . THR   A 21  ? 0.28104 0.36600 0.29560 -0.01657 -0.01323 0.15600  21  THR   A C   
152  O O   . THR   A 21  ? 0.28414 0.36236 0.31498 -0.01547 -0.01075 0.16366  21  THR   A O   
153  C CB  . THR   A 21  ? 0.26987 0.36533 0.28773 -0.01322 -0.02489 0.16062  21  THR   A CB  
154  O OG1 . THR   A 21  ? 0.26633 0.36378 0.28874 -0.01121 -0.03013 0.15625  21  THR   A OG1 
155  C CG2 . THR   A 21  ? 0.26190 0.36931 0.25772 -0.01745 -0.02622 0.16263  21  THR   A CG2 
156  N N   . CYS   A 22  ? 0.26843 0.35942 0.26370 -0.01977 -0.01016 0.15134  22  CYS   A N   
157  C CA  . CYS   A 22  ? 0.29829 0.39092 0.29050 -0.02196 -0.00348 0.15654  22  CYS   A CA  
158  C C   . CYS   A 22  ? 0.34567 0.44832 0.31260 -0.02443 -0.00240 0.15464  22  CYS   A C   
159  O O   . CYS   A 22  ? 0.30655 0.41000 0.25807 -0.02533 -0.00218 0.14309  22  CYS   A O   
160  C CB  . CYS   A 22  ? 0.29830 0.38403 0.29773 -0.02289 0.00276  0.14999  22  CYS   A CB  
161  S SG  . CYS   A 22  ? 0.41782 0.50768 0.41612 -0.02577 0.01152  0.15671  22  CYS   A SG  
162  N N   . GLY   A 23  ? 0.33137 0.44048 0.29357 -0.02556 -0.00150 0.16561  23  GLY   A N   
163  C CA  . GLY   A 23  ? 0.33456 0.45253 0.27111 -0.02802 -0.00146 0.16428  23  GLY   A CA  
164  C C   . GLY   A 23  ? 0.37969 0.50163 0.30798 -0.02840 -0.01052 0.16000  23  GLY   A C   
165  O O   . GLY   A 23  ? 0.42013 0.54442 0.36198 -0.02683 -0.01720 0.16769  23  GLY   A O   
166  N N   . THR   A 24  ? 0.38591 0.50828 0.29315 -0.03050 -0.01049 0.14740  24  THR   A N   
167  C CA  . THR   A 24  ? 0.40509 0.53108 0.30400 -0.03214 -0.01919 0.14192  24  THR   A CA  
168  C C   . THR   A 24  ? 0.40290 0.52177 0.30776 -0.03111 -0.02084 0.12950  24  THR   A C   
169  O O   . THR   A 24  ? 0.45158 0.57240 0.34875 -0.03318 -0.02712 0.12264  24  THR   A O   
170  C CB  . THR   A 24  ? 0.43718 0.56759 0.30644 -0.03617 -0.01909 0.13609  24  THR   A CB  
171  O OG1 . THR   A 24  ? 0.46062 0.58392 0.31613 -0.03612 -0.00976 0.12465  24  THR   A OG1 
172  C CG2 . THR   A 24  ? 0.43349 0.57279 0.29531 -0.03753 -0.01907 0.14954  24  THR   A CG2 
173  N N   . THR   A 25  ? 0.34639 0.45746 0.26459 -0.02851 -0.01549 0.12664  25  THR   A N   
174  C CA  . THR   A 25  ? 0.36175 0.46627 0.28559 -0.02737 -0.01659 0.11577  25  THR   A CA  
175  C C   . THR   A 25  ? 0.33104 0.43316 0.27894 -0.02422 -0.02137 0.12169  25  THR   A C   
176  O O   . THR   A 25  ? 0.30506 0.40404 0.26951 -0.02194 -0.01892 0.13055  25  THR   A O   
177  C CB  . THR   A 25  ? 0.38208 0.48033 0.30584 -0.02645 -0.00782 0.10895  25  THR   A CB  
178  O OG1 . THR   A 25  ? 0.43627 0.53565 0.33739 -0.02836 -0.00211 0.10178  25  THR   A OG1 
179  C CG2 . THR   A 25  ? 0.33536 0.42743 0.26641 -0.02509 -0.00951 0.09944  25  THR   A CG2 
180  N N   . THR   A 26  ? 0.27422 0.37705 0.22440 -0.02412 -0.02762 0.11661  26  THR   A N   
181  C CA  . THR   A 26  ? 0.26924 0.36847 0.24136 -0.02029 -0.03055 0.11978  26  THR   A CA  
182  C C   . THR   A 26  ? 0.24333 0.33611 0.21625 -0.01963 -0.03033 0.10789  26  THR   A C   
183  O O   . THR   A 26  ? 0.24023 0.33457 0.19865 -0.02260 -0.03213 0.09825  26  THR   A O   
184  C CB  . THR   A 26  ? 0.27271 0.38040 0.25128 -0.01995 -0.03761 0.12689  26  THR   A CB  
185  O OG1 . THR   A 26  ? 0.31528 0.42813 0.29730 -0.01953 -0.03740 0.13996  26  THR   A OG1 
186  C CG2 . THR   A 26  ? 0.29614 0.39966 0.29597 -0.01533 -0.03924 0.12774  26  THR   A CG2 
187  N N   . LEU   A 27  ? 0.22520 0.30970 0.21450 -0.01605 -0.02784 0.10840  27  LEU   A N   
188  C CA  . LEU   A 27  ? 0.23004 0.30843 0.22259 -0.01474 -0.02784 0.09893  27  LEU   A CA  
189  C C   . LEU   A 27  ? 0.21465 0.28504 0.22885 -0.00989 -0.02752 0.10261  27  LEU   A C   
190  O O   . LEU   A 27  ? 0.19684 0.26593 0.22355 -0.00752 -0.02724 0.11178  27  LEU   A O   
191  C CB  . LEU   A 27  ? 0.23266 0.30791 0.21351 -0.01685 -0.02247 0.09137  27  LEU   A CB  
192  C CG  . LEU   A 27  ? 0.21097 0.28254 0.19787 -0.01690 -0.01583 0.09687  27  LEU   A CG  
193  C CD1 . LEU   A 27  ? 0.22891 0.29005 0.23480 -0.01458 -0.01385 0.09518  27  LEU   A CD1 
194  C CD2 . LEU   A 27  ? 0.24290 0.31660 0.21405 -0.01923 -0.01015 0.08887  27  LEU   A CD2 
195  N N   . ASN   A 28  ? 0.20153 0.26592 0.21978 -0.00817 -0.02739 0.09491  28  ASN   A N   
196  C CA  . ASN   A 28  ? 0.18390 0.23886 0.22069 -0.00330 -0.02634 0.09440  28  ASN   A CA  
197  C C   . ASN   A 28  ? 0.12908 0.17194 0.17258 -0.00377 -0.02060 0.08989  28  ASN   A C   
198  O O   . ASN   A 28  ? 0.15163 0.19456 0.18672 -0.00718 -0.01768 0.08371  28  ASN   A O   
199  C CB  . ASN   A 28  ? 0.16950 0.22429 0.20732 -0.00160 -0.02793 0.08374  28  ASN   A CB  
200  C CG  . ASN   A 28  ? 0.16763 0.23469 0.20002 -0.00292 -0.03365 0.08642  28  ASN   A CG  
201  O OD1 . ASN   A 28  ? 0.14193 0.21272 0.18455 -0.00045 -0.03500 0.09273  28  ASN   A OD1 
202  N ND2 . ASN   A 28  ? 0.16368 0.23542 0.18027 -0.00756 -0.03560 0.07895  28  ASN   A ND2 
203  N N   . GLY   A 29  ? 0.13703 0.16940 0.19666 -0.00041 -0.01889 0.09298  29  GLY   A N   
204  C CA  . GLY   A 29  ? 0.12979 0.14944 0.19658 -0.00195 -0.01466 0.08667  29  GLY   A CA  
205  C C   . GLY   A 29  ? 0.13602 0.14463 0.21205 0.00194  -0.01356 0.07769  29  GLY   A C   
206  O O   . GLY   A 29  ? 0.12185 0.13142 0.20367 0.00714  -0.01466 0.08010  29  GLY   A O   
207  N N   . LEU   A 30  ? 0.15301 0.15235 0.23025 -0.00080 -0.01124 0.06764  30  LEU   A N   
208  C CA  . LEU   A 30  ? 0.15550 0.14304 0.23833 0.00183  -0.00951 0.05759  30  LEU   A CA  
209  C C   . LEU   A 30  ? 0.13726 0.10842 0.23175 0.00034  -0.00669 0.05886  30  LEU   A C   
210  O O   . LEU   A 30  ? 0.15398 0.12237 0.24908 -0.00596 -0.00645 0.05822  30  LEU   A O   
211  C CB  . LEU   A 30  ? 0.13604 0.12587 0.20938 -0.00092 -0.01010 0.04450  30  LEU   A CB  
212  C CG  . LEU   A 30  ? 0.11478 0.09406 0.18967 0.00102  -0.00836 0.03332  30  LEU   A CG  
213  C CD1 . LEU   A 30  ? 0.14698 0.13146 0.22108 0.00731  -0.00798 0.03290  30  LEU   A CD1 
214  C CD2 . LEU   A 30  ? 0.10930 0.09030 0.17599 -0.00349 -0.00963 0.02278  30  LEU   A CD2 
215  N N   . TRP   A 31  ? 0.14506 0.10519 0.25012 0.00611  -0.00416 0.06098  31  TRP   A N   
216  C CA  . TRP   A 31  ? 0.16237 0.10398 0.28009 0.00549  -0.00084 0.06370  31  TRP   A CA  
217  C C   . TRP   A 31  ? 0.19302 0.11814 0.31065 0.00558  0.00219  0.04790  31  TRP   A C   
218  O O   . TRP   A 31  ? 0.17266 0.09429 0.29157 0.01265  0.00504  0.04315  31  TRP   A O   
219  C CB  . TRP   A 31  ? 0.17179 0.11183 0.30184 0.01271  0.00072  0.07787  31  TRP   A CB  
220  C CG  . TRP   A 31  ? 0.19248 0.11675 0.33255 0.01272  0.00481  0.07916  31  TRP   A CG  
221  C CD1 . TRP   A 31  ? 0.20317 0.11469 0.34522 0.00538  0.00589  0.07556  31  TRP   A CD1 
222  C CD2 . TRP   A 31  ? 0.23797 0.15850 0.38793 0.02006  0.00808  0.08508  31  TRP   A CD2 
223  N NE1 . TRP   A 31  ? 0.22387 0.12226 0.37544 0.00781  0.00962  0.07860  31  TRP   A NE1 
224  C CE2 . TRP   A 31  ? 0.24378 0.14706 0.40069 0.01719  0.01131  0.08467  31  TRP   A CE2 
225  C CE3 . TRP   A 31  ? 0.23000 0.16090 0.38448 0.02828  0.00847  0.09094  31  TRP   A CE3 
226  C CZ2 . TRP   A 31  ? 0.26097 0.15547 0.42901 0.02314  0.01534  0.09007  31  TRP   A CZ2 
227  C CZ3 . TRP   A 31  ? 0.25688 0.18089 0.42328 0.03398  0.01242  0.09659  31  TRP   A CZ3 
228  C CH2 . TRP   A 31  ? 0.26153 0.16668 0.43459 0.03187  0.01606  0.09616  31  TRP   A CH2 
229  N N   . LEU   A 32  ? 0.17623 0.09259 0.29189 -0.00267 0.00156  0.03985  32  LEU   A N   
230  C CA  . LEU   A 32  ? 0.18761 0.08826 0.30009 -0.00481 0.00337  0.02392  32  LEU   A CA  
231  C C   . LEU   A 32  ? 0.24572 0.12737 0.36769 -0.01169 0.00450  0.02355  32  LEU   A C   
232  O O   . LEU   A 32  ? 0.22000 0.10734 0.34465 -0.01960 0.00150  0.02938  32  LEU   A O   
233  C CB  . LEU   A 32  ? 0.18735 0.09910 0.28574 -0.01011 -0.00061 0.01276  32  LEU   A CB  
234  C CG  . LEU   A 32  ? 0.15809 0.08799 0.24674 -0.00518 -0.00207 0.01266  32  LEU   A CG  
235  C CD1 . LEU   A 32  ? 0.15365 0.09506 0.23168 -0.01119 -0.00632 0.00605  32  LEU   A CD1 
236  C CD2 . LEU   A 32  ? 0.18738 0.11118 0.27399 0.00240  0.00205  0.00567  32  LEU   A CD2 
237  N N   . ASP   A 33  ? 0.23619 0.09813 0.36083 -0.00851 0.00924  0.01651  33  ASP   A N   
238  C CA  . ASP   A 33  ? 0.28099 0.12730 0.41007 -0.01372 0.01064  0.01628  33  ASP   A CA  
239  C C   . ASP   A 33  ? 0.29955 0.15511 0.43880 -0.01333 0.01004  0.03489  33  ASP   A C   
240  O O   . ASP   A 33  ? 0.26556 0.13121 0.40898 -0.00484 0.01123  0.04625  33  ASP   A O   
241  C CB  . ASP   A 33  ? 0.31662 0.15774 0.43819 -0.02592 0.00660  0.00366  33  ASP   A CB  
242  C CG  . ASP   A 33  ? 0.34690 0.18023 0.45523 -0.02558 0.00720  -0.01451 33  ASP   A CG  
243  O OD1 . ASP   A 33  ? 0.38667 0.20614 0.49252 -0.01807 0.01298  -0.02025 33  ASP   A OD1 
244  O OD2 . ASP   A 33  ? 0.34632 0.18923 0.44632 -0.03222 0.00210  -0.02238 33  ASP   A OD2 
245  N N   . ASP   A 34  ? 0.26243 0.11739 0.40508 -0.02251 0.00797  0.03896  34  ASP   A N   
246  C CA  . ASP   A 34  ? 0.25882 0.12301 0.40952 -0.02173 0.00827  0.05650  34  ASP   A CA  
247  C C   . ASP   A 34  ? 0.24639 0.13288 0.39396 -0.02613 0.00461  0.06464  34  ASP   A C   
248  O O   . ASP   A 34  ? 0.26422 0.15770 0.41608 -0.02982 0.00468  0.07574  34  ASP   A O   
249  C CB  . ASP   A 34  ? 0.27887 0.12756 0.43691 -0.02758 0.01000  0.05831  34  ASP   A CB  
250  C CG  . ASP   A 34  ? 0.36299 0.20953 0.51844 -0.04037 0.00674  0.05004  34  ASP   A CG  
251  O OD1 . ASP   A 34  ? 0.32388 0.17692 0.47133 -0.04421 0.00338  0.03951  34  ASP   A OD1 
252  O OD2 . ASP   A 34  ? 0.35444 0.19352 0.51654 -0.04684 0.00731  0.05448  34  ASP   A OD2 
253  N N   . VAL   A 35  ? 0.21344 0.11136 0.35327 -0.02539 0.00206  0.05968  35  VAL   A N   
254  C CA  . VAL   A 35  ? 0.19489 0.11341 0.33042 -0.02886 -0.00049 0.06668  35  VAL   A CA  
255  C C   . VAL   A 35  ? 0.19700 0.12838 0.32529 -0.02099 -0.00126 0.07132  35  VAL   A C   
256  O O   . VAL   A 35  ? 0.19673 0.12543 0.32004 -0.01518 -0.00134 0.06226  35  VAL   A O   
257  C CB  . VAL   A 35  ? 0.18730 0.11004 0.31974 -0.03762 -0.00368 0.05598  35  VAL   A CB  
258  C CG1 . VAL   A 35  ? 0.19304 0.13952 0.31810 -0.03839 -0.00489 0.06123  35  VAL   A CG1 
259  C CG2 . VAL   A 35  ? 0.23938 0.15321 0.37782 -0.04641 -0.00398 0.05247  35  VAL   A CG2 
260  N N   . VAL   A 36  ? 0.17239 0.12026 0.29673 -0.02065 -0.00169 0.08363  36  VAL   A N   
261  C CA  . VAL   A 36  ? 0.15916 0.12345 0.27137 -0.01500 -0.00352 0.08537  36  VAL   A CA  
262  C C   . VAL   A 36  ? 0.17206 0.15186 0.27302 -0.01932 -0.00443 0.08115  36  VAL   A C   
263  O O   . VAL   A 36  ? 0.16134 0.14721 0.26397 -0.02447 -0.00278 0.08799  36  VAL   A O   
264  C CB  . VAL   A 36  ? 0.16488 0.13644 0.27818 -0.01073 -0.00357 0.10138  36  VAL   A CB  
265  C CG1 . VAL   A 36  ? 0.19051 0.17935 0.29001 -0.00764 -0.00657 0.10282  36  VAL   A CG1 
266  C CG2 . VAL   A 36  ? 0.18994 0.14978 0.31384 -0.00431 -0.00220 0.10256  36  VAL   A CG2 
267  N N   . TYR   A 37  ? 0.13457 0.12049 0.22536 -0.01690 -0.00626 0.07042  37  TYR   A N   
268  C CA  . TYR   A 37  ? 0.16789 0.16652 0.24913 -0.01953 -0.00654 0.06527  37  TYR   A CA  
269  C C   . TYR   A 37  ? 0.11809 0.12924 0.18683 -0.01590 -0.00712 0.06913  37  TYR   A C   
270  O O   . TYR   A 37  ? 0.13541 0.14635 0.20127 -0.01133 -0.00920 0.06877  37  TYR   A O   
271  C CB  . TYR   A 37  ? 0.12249 0.11855 0.20066 -0.01968 -0.00834 0.05103  37  TYR   A CB  
272  C CG  . TYR   A 37  ? 0.14193 0.12590 0.22892 -0.02441 -0.00897 0.04460  37  TYR   A CG  
273  C CD1 . TYR   A 37  ? 0.13908 0.10690 0.23160 -0.02254 -0.00848 0.04135  37  TYR   A CD1 
274  C CD2 . TYR   A 37  ? 0.16136 0.15007 0.25172 -0.03111 -0.00994 0.04172  37  TYR   A CD2 
275  C CE1 . TYR   A 37  ? 0.17270 0.12728 0.27093 -0.02798 -0.00911 0.03352  37  TYR   A CE1 
276  C CE2 . TYR   A 37  ? 0.13274 0.11087 0.23022 -0.03718 -0.01187 0.03522  37  TYR   A CE2 
277  C CZ  . TYR   A 37  ? 0.19608 0.15611 0.29610 -0.03602 -0.01152 0.03029  37  TYR   A CZ  
278  O OH  . TYR   A 37  ? 0.22588 0.17314 0.33080 -0.04306 -0.01342 0.02209  37  TYR   A OH  
279  N N   . CYS   A 38  ? 0.11670 0.13893 0.17803 -0.01818 -0.00506 0.07232  38  CYS   A N   
280  C CA  . CYS   A 38  ? 0.12069 0.15304 0.16751 -0.01590 -0.00562 0.07411  38  CYS   A CA  
281  C C   . CYS   A 38  ? 0.14872 0.19024 0.18702 -0.01788 -0.00174 0.07144  38  CYS   A C   
282  O O   . CYS   A 38  ? 0.14452 0.18714 0.19068 -0.02088 0.00144  0.07225  38  CYS   A O   
283  C CB  . CYS   A 38  ? 0.12587 0.16152 0.17108 -0.01520 -0.00648 0.08773  38  CYS   A CB  
284  S SG  . CYS   A 38  ? 0.20184 0.24290 0.24841 -0.01946 -0.00159 0.10125  38  CYS   A SG  
285  N N   . PRO   A 39  ? 0.11643 0.16443 0.13962 -0.01634 -0.00163 0.06802  39  PRO   A N   
286  C CA  . PRO   A 39  ? 0.15068 0.20575 0.16538 -0.01692 0.00370  0.06477  39  PRO   A CA  
287  C C   . PRO   A 39  ? 0.16203 0.22371 0.17639 -0.01937 0.00898  0.07527  39  PRO   A C   
288  O O   . PRO   A 39  ? 0.16142 0.22491 0.17200 -0.02033 0.00790  0.08520  39  PRO   A O   
289  C CB  . PRO   A 39  ? 0.14897 0.20629 0.14620 -0.01544 0.00221  0.05948  39  PRO   A CB  
290  C CG  . PRO   A 39  ? 0.13004 0.18206 0.13118 -0.01399 -0.00438 0.05679  39  PRO   A CG  
291  C CD  . PRO   A 39  ? 0.13364 0.18187 0.14825 -0.01411 -0.00625 0.06538  39  PRO   A CD  
292  N N   . ARG   A 40  ? 0.14662 0.21337 0.16617 -0.02029 0.01490  0.07442  40  ARG   A N   
293  C CA  . ARG   A 40  ? 0.14969 0.22397 0.17061 -0.02284 0.02096  0.08545  40  ARG   A CA  
294  C C   . ARG   A 40  ? 0.17404 0.25554 0.17362 -0.02184 0.02539  0.08796  40  ARG   A C   
295  O O   . ARG   A 40  ? 0.19132 0.27811 0.18844 -0.02354 0.02919  0.09757  40  ARG   A O   
296  C CB  . ARG   A 40  ? 0.13766 0.21814 0.17233 -0.02425 0.02655  0.08519  40  ARG   A CB  
297  C CG  . ARG   A 40  ? 0.16114 0.24751 0.18842 -0.02032 0.03201  0.07673  40  ARG   A CG  
298  C CD  . ARG   A 40  ? 0.14149 0.23732 0.18587 -0.02128 0.03757  0.07908  40  ARG   A CD  
299  N NE  . ARG   A 40  ? 0.15982 0.26092 0.19899 -0.01594 0.04381  0.07192  40  ARG   A NE  
300  C CZ  . ARG   A 40  ? 0.20806 0.32038 0.26079 -0.01469 0.05046  0.07418  40  ARG   A CZ  
301  N NH1 . ARG   A 40  ? 0.16686 0.28505 0.23793 -0.01933 0.04972  0.08160  40  ARG   A NH1 
302  N NH2 . ARG   A 40  ? 0.15529 0.27077 0.20350 -0.00846 0.05695  0.06799  40  ARG   A NH2 
303  N N   . HIS   A 41  ? 0.20157 0.28172 0.18502 -0.01931 0.02449  0.07790  41  HIS   A N   
304  C CA  . HIS   A 41  ? 0.24614 0.33195 0.20668 -0.01959 0.02845  0.07888  41  HIS   A CA  
305  C C   . HIS   A 41  ? 0.24759 0.33350 0.20061 -0.02157 0.02186  0.08678  41  HIS   A C   
306  O O   . HIS   A 41  ? 0.26118 0.34954 0.19584 -0.02216 0.02304  0.08553  41  HIS   A O   
307  C CB  . HIS   A 41  ? 0.21734 0.29922 0.16234 -0.01731 0.02932  0.06471  41  HIS   A CB  
308  C CG  . HIS   A 41  ? 0.20224 0.27720 0.14408 -0.01764 0.01962  0.05855  41  HIS   A CG  
309  N ND1 . HIS   A 41  ? 0.26142 0.33821 0.19330 -0.02033 0.01233  0.06350  41  HIS   A ND1 
310  C CD2 . HIS   A 41  ? 0.24482 0.31268 0.19199 -0.01568 0.01650  0.04849  41  HIS   A CD2 
311  C CE1 . HIS   A 41  ? 0.26209 0.33364 0.19523 -0.02011 0.00532  0.05669  41  HIS   A CE1 
312  N NE2 . HIS   A 41  ? 0.21729 0.28280 0.15896 -0.01738 0.00800  0.04748  41  HIS   A NE2 
313  N N   . VAL   A 42  ? 0.22432 0.30654 0.19246 -0.02214 0.01528  0.09410  42  VAL   A N   
314  C CA  . VAL   A 42  ? 0.23627 0.31932 0.20326 -0.02269 0.00998  0.10292  42  VAL   A CA  
315  C C   . VAL   A 42  ? 0.29361 0.38158 0.25876 -0.02393 0.01535  0.11126  42  VAL   A C   
316  O O   . VAL   A 42  ? 0.33775 0.42923 0.29509 -0.02453 0.01239  0.11769  42  VAL   A O   
317  C CB  . VAL   A 42  ? 0.23869 0.31495 0.22564 -0.02171 0.00406  0.10880  42  VAL   A CB  
318  C CG1 . VAL   A 42  ? 0.19830 0.26998 0.20455 -0.02292 0.00816  0.11414  42  VAL   A CG1 
319  C CG2 . VAL   A 42  ? 0.25917 0.33765 0.24529 -0.02091 -0.00202 0.11664  42  VAL   A CG2 
320  N N   . ILE   A 43  ? 0.26783 0.35735 0.24102 -0.02450 0.02310  0.11197  43  ILE   A N   
321  C CA  . ILE   A 43  ? 0.32996 0.42449 0.30276 -0.02585 0.02831  0.12081  43  ILE   A CA  
322  C C   . ILE   A 43  ? 0.33922 0.43969 0.28892 -0.02553 0.03477  0.11641  43  ILE   A C   
323  O O   . ILE   A 43  ? 0.41240 0.51782 0.35797 -0.02658 0.03999  0.12336  43  ILE   A O   
324  C CB  . ILE   A 43  ? 0.36761 0.46171 0.36189 -0.02734 0.03308  0.12472  43  ILE   A CB  
325  C CG1 . ILE   A 43  ? 0.35698 0.45395 0.35375 -0.02637 0.03912  0.11546  43  ILE   A CG1 
326  C CG2 . ILE   A 43  ? 0.34782 0.43274 0.36262 -0.02836 0.02658  0.12828  43  ILE   A CG2 
327  C CD1 . ILE   A 43  ? 0.32102 0.41941 0.34067 -0.02871 0.04232  0.11898  43  ILE   A CD1 
328  N N   . CYS   A 44  ? 0.42044 0.51930 0.35398 -0.02431 0.03446  0.10498  44  CYS   A N   
329  C CA  . CYS   A 44  ? 0.50153 0.60200 0.41247 -0.02368 0.04171  0.09722  44  CYS   A CA  
330  C C   . CYS   A 44  ? 0.58694 0.68755 0.47529 -0.02553 0.03644  0.09696  44  CYS   A C   
331  O O   . CYS   A 44  ? 0.59689 0.69579 0.48482 -0.02649 0.02639  0.09651  44  CYS   A O   
332  C CB  . CYS   A 44  ? 0.51872 0.61498 0.42615 -0.02130 0.04461  0.08364  44  CYS   A CB  
333  S SG  . CYS   A 44  ? 0.55036 0.64946 0.48291 -0.01881 0.05206  0.08339  44  CYS   A SG  
334  N N   . THR   A 45  ? 0.67837 0.78150 0.54837 -0.02615 0.04339  0.09712  45  THR   A N   
335  C CA  . THR   A 45  ? 0.74360 0.84604 0.58751 -0.02813 0.03983  0.09351  45  THR   A CA  
336  C C   . THR   A 45  ? 0.81274 0.90734 0.63760 -0.02693 0.04464  0.07697  45  THR   A C   
337  O O   . THR   A 45  ? 0.80360 0.89460 0.63560 -0.02396 0.05233  0.06974  45  THR   A O   
338  C CB  . THR   A 45  ? 0.76987 0.87820 0.60200 -0.02958 0.04489  0.10279  45  THR   A CB  
339  O OG1 . THR   A 45  ? 0.79996 0.90734 0.62437 -0.02781 0.05890  0.09791  45  THR   A OG1 
340  C CG2 . THR   A 45  ? 0.67290 0.78740 0.52749 -0.03022 0.04178  0.11918  45  THR   A CG2 
341  N N   . SER   A 46  ? 0.86255 0.95444 0.66401 -0.02922 0.03981  0.07105  46  SER   A N   
342  C CA  . SER   A 46  ? 0.89757 0.97954 0.68065 -0.02823 0.04326  0.05465  46  SER   A CA  
343  C C   . SER   A 46  ? 0.91897 0.99606 0.68988 -0.02455 0.05934  0.04837  46  SER   A C   
344  O O   . SER   A 46  ? 0.91228 0.97967 0.67545 -0.02148 0.06516  0.03499  46  SER   A O   
345  C CB  . SER   A 46  ? 0.89437 0.97533 0.65579 -0.03228 0.03393  0.05019  46  SER   A CB  
346  O OG  . SER   A 46  ? 0.91594 0.99929 0.69041 -0.03504 0.02045  0.05164  46  SER   A OG  
347  N N   . GLU   A 47  ? 0.89216 0.97556 0.66255 -0.02446 0.06721  0.05793  47  GLU   A N   
348  C CA  . GLU   A 47  ? 0.87558 0.95618 0.64089 -0.02096 0.08383  0.05362  47  GLU   A CA  
349  C C   . GLU   A 47  ? 0.86376 0.95124 0.65971 -0.01898 0.08984  0.05946  47  GLU   A C   
350  O O   . GLU   A 47  ? 0.85252 0.93863 0.65123 -0.01584 0.10284  0.05356  47  GLU   A O   
351  C CB  . GLU   A 47  ? 0.91058 0.99481 0.65570 -0.02252 0.09046  0.05973  47  GLU   A CB  
352  C CG  . GLU   A 47  ? 0.91070 1.00790 0.67270 -0.02529 0.08733  0.07755  47  GLU   A CG  
353  C CD  . GLU   A 47  ? 0.92784 1.02958 0.68272 -0.02919 0.07309  0.08584  47  GLU   A CD  
354  O OE1 . GLU   A 47  ? 0.93195 1.02853 0.66638 -0.03052 0.06626  0.07741  47  GLU   A OE1 
355  O OE2 . GLU   A 47  ? 0.89676 1.00757 0.66776 -0.03092 0.06864  0.10084  47  GLU   A OE2 
356  N N   . ASP   A 48  ? 0.84724 0.94241 0.66735 -0.02062 0.08064  0.07074  48  ASP   A N   
357  C CA  . ASP   A 48  ? 0.80544 0.90568 0.65562 -0.01848 0.08333  0.07419  48  ASP   A CA  
358  C C   . ASP   A 48  ? 0.81372 0.90746 0.66871 -0.01513 0.08416  0.06165  48  ASP   A C   
359  O O   . ASP   A 48  ? 0.75781 0.85525 0.63193 -0.01191 0.09065  0.06048  48  ASP   A O   
360  C CB  . ASP   A 48  ? 0.73039 0.83539 0.60241 -0.02076 0.07217  0.08633  48  ASP   A CB  
361  C CG  . ASP   A 48  ? 0.69155 0.80380 0.56848 -0.02315 0.07331  0.10047  48  ASP   A CG  
362  O OD1 . ASP   A 48  ? 0.70279 0.82001 0.57933 -0.02252 0.08446  0.10273  48  ASP   A OD1 
363  O OD2 . ASP   A 48  ? 0.65166 0.76483 0.53428 -0.02544 0.06343  0.10960  48  ASP   A OD2 
364  N N   . MET   A 49  ? 0.85156 0.93668 0.69163 -0.01588 0.07656  0.05299  49  MET   A N   
365  C CA  . MET   A 49  ? 0.81680 0.89600 0.66426 -0.01338 0.07436  0.04307  49  MET   A CA  
366  C C   . MET   A 49  ? 0.80961 0.88016 0.64573 -0.00915 0.08638  0.02964  49  MET   A C   
367  O O   . MET   A 49  ? 0.81813 0.87895 0.64801 -0.00747 0.08426  0.01866  49  MET   A O   
368  C CB  . MET   A 49  ? 0.82426 0.89963 0.66539 -0.01686 0.05992  0.04145  49  MET   A CB  
369  C CG  . MET   A 49  ? 0.90150 0.97082 0.71504 -0.01956 0.05592  0.03545  49  MET   A CG  
370  S SD  . MET   A 49  ? 1.04170 1.11073 0.85803 -0.02420 0.03805  0.03542  49  MET   A SD  
371  C CE  . MET   A 49  ? 0.75138 0.81039 0.57263 -0.02136 0.04062  0.02087  49  MET   A CE  
372  N N   . LEU   A 50  ? 0.74766 0.82271 0.58650 -0.00715 0.09942  0.03102  50  LEU   A N   
373  C CA  . LEU   A 50  ? 0.75686 0.82450 0.58386 -0.00422 0.11295  0.01847  50  LEU   A CA  
374  C C   . LEU   A 50  ? 0.69657 0.77720 0.55145 0.00042  0.12239  0.01985  50  LEU   A C   
375  O O   . LEU   A 50  ? 0.68098 0.76094 0.53834 0.00479  0.12996  0.00893  50  LEU   A O   
376  C CB  . LEU   A 50  ? 0.84594 0.90815 0.64344 -0.00632 0.11973  0.01769  50  LEU   A CB  
377  C CG  . LEU   A 50  ? 0.83499 0.88745 0.60579 -0.00692 0.10818  0.01595  50  LEU   A CG  
378  C CD1 . LEU   A 50  ? 0.86184 0.91275 0.60486 -0.00758 0.11376  0.01742  50  LEU   A CD1 
379  C CD2 . LEU   A 50  ? 0.77759 0.81892 0.54060 -0.00201 0.10306  0.00299  50  LEU   A CD2 
380  N N   . ASN   A 51  ? 0.67553 0.76925 0.55367 0.00067  0.12084  0.03380  51  ASN   A N   
381  C CA  . ASN   A 51  ? 0.57113 0.67522 0.48041 0.00598  0.12480  0.03758  51  ASN   A CA  
382  C C   . ASN   A 51  ? 0.52072 0.63608 0.45136 0.00290  0.11953  0.05308  51  ASN   A C   
383  O O   . ASN   A 51  ? 0.54528 0.67093 0.48620 0.00310  0.12661  0.06014  51  ASN   A O   
384  C CB  . ASN   A 51  ? 0.62152 0.73065 0.53168 0.01086  0.13919  0.03241  51  ASN   A CB  
385  C CG  . ASN   A 51  ? 0.61882 0.73255 0.55654 0.01880  0.14189  0.03103  51  ASN   A CG  
386  O OD1 . ASN   A 51  ? 0.55700 0.67559 0.51826 0.01908  0.13427  0.03848  51  ASN   A OD1 
387  N ND2 . ASN   A 51  ? 0.58659 0.69838 0.52117 0.02527  0.15215  0.02151  51  ASN   A ND2 
388  N N   . PRO   A 52  ? 0.52353 0.63728 0.46239 -0.00024 0.10727  0.05828  52  PRO   A N   
389  C CA  . PRO   A 52  ? 0.45455 0.57512 0.40652 -0.00517 0.10130  0.07195  52  PRO   A CA  
390  C C   . PRO   A 52  ? 0.42816 0.55902 0.41101 -0.00449 0.10258  0.07885  52  PRO   A C   
391  O O   . PRO   A 52  ? 0.39694 0.52888 0.39562 -0.00121 0.10133  0.07484  52  PRO   A O   
392  C CB  . PRO   A 52  ? 0.45982 0.57392 0.41171 -0.00804 0.08815  0.07265  52  PRO   A CB  
393  C CG  . PRO   A 52  ? 0.51642 0.62077 0.44542 -0.00626 0.08751  0.06076  52  PRO   A CG  
394  C CD  . PRO   A 52  ? 0.49354 0.59686 0.42140 -0.00067 0.09852  0.05101  52  PRO   A CD  
395  N N   . ASN   A 53  ? 0.37936 0.51765 0.37095 -0.00813 0.10399  0.08979  53  ASN   A N   
396  C CA  . ASN   A 53  ? 0.36508 0.51114 0.38615 -0.01055 0.10052  0.09791  53  ASN   A CA  
397  C C   . ASN   A 53  ? 0.32997 0.47009 0.35577 -0.01642 0.08885  0.10437  53  ASN   A C   
398  O O   . ASN   A 53  ? 0.28933 0.42958 0.31166 -0.02025 0.08797  0.11314  53  ASN   A O   
399  C CB  . ASN   A 53  ? 0.34398 0.50139 0.37406 -0.01125 0.10932  0.10584  53  ASN   A CB  
400  C CG  . ASN   A 53  ? 0.34550 0.51119 0.40630 -0.01406 0.10550  0.11266  53  ASN   A CG  
401  O OD1 . ASN   A 53  ? 0.32728 0.48883 0.39984 -0.01928 0.09528  0.11660  53  ASN   A OD1 
402  N ND2 . ASN   A 53  ? 0.37259 0.54961 0.44648 -0.01090 0.11348  0.11368  53  ASN   A ND2 
403  N N   . TYR   A 54  ? 0.30207 0.43644 0.33570 -0.01678 0.08023  0.10003  54  TYR   A N   
404  C CA  . TYR   A 54  ? 0.26653 0.39303 0.30293 -0.02151 0.06974  0.10438  54  TYR   A CA  
405  C C   . TYR   A 54  ? 0.25749 0.38584 0.31370 -0.02712 0.06681  0.11440  54  TYR   A C   
406  O O   . TYR   A 54  ? 0.24369 0.36553 0.29896 -0.03056 0.06152  0.12073  54  TYR   A O   
407  C CB  . TYR   A 54  ? 0.23068 0.35116 0.27258 -0.02096 0.06221  0.09729  54  TYR   A CB  
408  C CG  . TYR   A 54  ? 0.26409 0.37894 0.28417 -0.01733 0.06178  0.08927  54  TYR   A CG  
409  C CD1 . TYR   A 54  ? 0.25109 0.35890 0.25749 -0.01926 0.05541  0.09121  54  TYR   A CD1 
410  C CD2 . TYR   A 54  ? 0.25789 0.37387 0.27201 -0.01194 0.06708  0.07973  54  TYR   A CD2 
411  C CE1 . TYR   A 54  ? 0.26270 0.36580 0.24925 -0.01705 0.05353  0.08369  54  TYR   A CE1 
412  C CE2 . TYR   A 54  ? 0.23247 0.34165 0.22594 -0.00944 0.06617  0.07151  54  TYR   A CE2 
413  C CZ  . TYR   A 54  ? 0.27971 0.38296 0.25904 -0.01265 0.05884  0.07343  54  TYR   A CZ  
414  O OH  . TYR   A 54  ? 0.26674 0.36378 0.22575 -0.01143 0.05630  0.06509  54  TYR   A OH  
415  N N   . GLU   A 55  ? 0.28514 0.42183 0.36008 -0.02812 0.06976  0.11602  55  GLU   A N   
416  C CA  . GLU   A 55  ? 0.26498 0.40289 0.35817 -0.03438 0.06701  0.12498  55  GLU   A CA  
417  C C   . GLU   A 55  ? 0.26842 0.40900 0.35322 -0.03554 0.07258  0.13457  55  GLU   A C   
418  O O   . GLU   A 55  ? 0.24435 0.37908 0.33467 -0.04017 0.06819  0.14231  55  GLU   A O   
419  C CB  . GLU   A 55  ? 0.27904 0.42726 0.39307 -0.03543 0.06850  0.12461  55  GLU   A CB  
420  C CG  . GLU   A 55  ? 0.34046 0.48490 0.46430 -0.03615 0.06018  0.11669  55  GLU   A CG  
421  C CD  . GLU   A 55  ? 0.41981 0.56884 0.53679 -0.02862 0.06412  0.10830  55  GLU   A CD  
422  O OE1 . GLU   A 55  ? 0.43381 0.58436 0.56165 -0.02844 0.05887  0.10320  55  GLU   A OE1 
423  O OE2 . GLU   A 55  ? 0.39232 0.54246 0.49199 -0.02300 0.07234  0.10639  55  GLU   A OE2 
424  N N   . ASP   A 56  ? 0.30031 0.44871 0.37088 -0.03125 0.08251  0.13392  56  ASP   A N   
425  C CA  . ASP   A 56  ? 0.30664 0.45767 0.36529 -0.03237 0.08785  0.14257  56  ASP   A CA  
426  C C   . ASP   A 56  ? 0.29615 0.43720 0.33731 -0.03291 0.08161  0.14420  56  ASP   A C   
427  O O   . ASP   A 56  ? 0.25643 0.39594 0.29817 -0.03612 0.07982  0.15444  56  ASP   A O   
428  C CB  . ASP   A 56  ? 0.35818 0.51796 0.40185 -0.02771 0.10024  0.13945  56  ASP   A CB  
429  C CG  . ASP   A 56  ? 0.36824 0.54046 0.43120 -0.02692 0.10758  0.14131  56  ASP   A CG  
430  O OD1 . ASP   A 56  ? 0.35369 0.52975 0.43938 -0.03181 0.10402  0.14898  56  ASP   A OD1 
431  O OD2 . ASP   A 56  ? 0.46266 0.64060 0.51819 -0.02150 0.11704  0.13507  56  ASP   A OD2 
432  N N   . LEU   A 57  ? 0.27339 0.40809 0.29983 -0.02971 0.07797  0.13480  57  LEU   A N   
433  C CA  . LEU   A 57  ? 0.27931 0.40622 0.29033 -0.03011 0.07110  0.13656  57  LEU   A CA  
434  C C   . LEU   A 57  ? 0.27530 0.39462 0.30366 -0.03378 0.06197  0.14369  57  LEU   A C   
435  O O   . LEU   A 57  ? 0.25079 0.36693 0.27412 -0.03492 0.05837  0.15175  57  LEU   A O   
436  C CB  . LEU   A 57  ? 0.30133 0.42308 0.29628 -0.02666 0.06813  0.12478  57  LEU   A CB  
437  C CG  . LEU   A 57  ? 0.36501 0.49035 0.33887 -0.02305 0.07738  0.11637  57  LEU   A CG  
438  C CD1 . LEU   A 57  ? 0.35503 0.47318 0.31153 -0.02074 0.07317  0.10528  57  LEU   A CD1 
439  C CD2 . LEU   A 57  ? 0.34981 0.47907 0.30613 -0.02424 0.08291  0.12270  57  LEU   A CD2 
440  N N   . LEU   A 58  ? 0.25425 0.37016 0.30330 -0.03569 0.05834  0.14071  58  LEU   A N   
441  C CA  . LEU   A 58  ? 0.23641 0.34139 0.29988 -0.03899 0.04993  0.14440  58  LEU   A CA  
442  C C   . LEU   A 58  ? 0.22537 0.33021 0.30303 -0.04347 0.05117  0.15575  58  LEU   A C   
443  O O   . LEU   A 58  ? 0.23136 0.32696 0.31382 -0.04498 0.04627  0.16202  58  LEU   A O   
444  C CB  . LEU   A 58  ? 0.24391 0.34374 0.32174 -0.04030 0.04521  0.13573  58  LEU   A CB  
445  C CG  . LEU   A 58  ? 0.28216 0.36745 0.37195 -0.04332 0.03697  0.13665  58  LEU   A CG  
446  C CD1 . LEU   A 58  ? 0.24292 0.32154 0.31945 -0.03986 0.03290  0.13851  58  LEU   A CD1 
447  C CD2 . LEU   A 58  ? 0.26521 0.34514 0.36642 -0.04527 0.03222  0.12693  58  LEU   A CD2 
448  N N   . ILE   A 59  ? 0.23177 0.34675 0.31734 -0.04539 0.05799  0.15886  59  ILE   A N   
449  C CA  . ILE   A 59  ? 0.24673 0.36234 0.34571 -0.05018 0.05961  0.17030  59  ILE   A CA  
450  C C   . ILE   A 59  ? 0.26543 0.38189 0.35077 -0.04899 0.06163  0.18068  59  ILE   A C   
451  O O   . ILE   A 59  ? 0.27812 0.39050 0.37387 -0.05250 0.06052  0.19109  59  ILE   A O   
452  C CB  . ILE   A 59  ? 0.25580 0.38442 0.36656 -0.05239 0.06683  0.17207  59  ILE   A CB  
453  C CG1 . ILE   A 59  ? 0.26468 0.39227 0.39334 -0.05887 0.06693  0.18316  59  ILE   A CG1 
454  C CG2 . ILE   A 59  ? 0.26111 0.40250 0.35491 -0.04797 0.07685  0.17301  59  ILE   A CG2 
455  C CD1 . ILE   A 59  ? 0.29192 0.40519 0.43766 -0.06421 0.05816  0.18093  59  ILE   A CD1 
456  N N   . ARG   A 60  ? 0.26950 0.39076 0.33137 -0.04448 0.06422  0.17802  60  ARG   A N   
457  C CA  . ARG   A 60  ? 0.28861 0.41149 0.33527 -0.04365 0.06474  0.18732  60  ARG   A CA  
458  C C   . ARG   A 60  ? 0.28600 0.39851 0.33078 -0.04242 0.05532  0.18932  60  ARG   A C   
459  O O   . ARG   A 60  ? 0.30218 0.41650 0.33674 -0.04177 0.05421  0.19822  60  ARG   A O   
460  C CB  . ARG   A 60  ? 0.29867 0.43057 0.31915 -0.04033 0.07145  0.18272  60  ARG   A CB  
461  C CG  . ARG   A 60  ? 0.30167 0.44367 0.32488 -0.04017 0.08198  0.17969  60  ARG   A CG  
462  C CD  . ARG   A 60  ? 0.31193 0.45914 0.30887 -0.03639 0.08931  0.17170  60  ARG   A CD  
463  N NE  . ARG   A 60  ? 0.31438 0.47085 0.31733 -0.03523 0.10001  0.16847  60  ARG   A NE  
464  C CZ  . ARG   A 60  ? 0.40184 0.56149 0.38786 -0.03129 0.10819  0.15855  60  ARG   A CZ  
465  N NH1 . ARG   A 60  ? 0.38610 0.53914 0.34718 -0.02899 0.10605  0.14977  60  ARG   A NH1 
466  N NH2 . ARG   A 60  ? 0.39404 0.56294 0.38952 -0.02965 0.11824  0.15686  60  ARG   A NH2 
467  N N   . LYS   A 61  ? 0.27250 0.37494 0.32759 -0.04202 0.04876  0.18188  61  LYS   A N   
468  C CA  . LYS   A 61  ? 0.28642 0.37908 0.34191 -0.04008 0.04054  0.18309  61  LYS   A CA  
469  C C   . LYS   A 61  ? 0.30557 0.38751 0.38260 -0.04285 0.03781  0.19136  61  LYS   A C   
470  O O   . LYS   A 61  ? 0.28897 0.36888 0.38184 -0.04720 0.04060  0.19278  61  LYS   A O   
471  C CB  . LYS   A 61  ? 0.26419 0.35084 0.31845 -0.03787 0.03574  0.17031  61  LYS   A CB  
472  C CG  . LYS   A 61  ? 0.27064 0.36578 0.30571 -0.03552 0.03904  0.16085  61  LYS   A CG  
473  C CD  . LYS   A 61  ? 0.31895 0.41942 0.33116 -0.03322 0.03799  0.16280  61  LYS   A CD  
474  C CE  . LYS   A 61  ? 0.37484 0.46892 0.38721 -0.03128 0.02899  0.16367  61  LYS   A CE  
475  N NZ  . LYS   A 61  ? 0.40191 0.50210 0.39039 -0.02964 0.02649  0.16104  61  LYS   A NZ  
476  N N   . SER   A 62  ? 0.36716 0.44220 0.44504 -0.04034 0.03235  0.19666  62  SER   A N   
477  C CA  . SER   A 62  ? 0.34179 0.40352 0.43909 -0.04158 0.02968  0.20330  62  SER   A CA  
478  C C   . SER   A 62  ? 0.30040 0.34993 0.40225 -0.03804 0.02338  0.19598  62  SER   A C   
479  O O   . SER   A 62  ? 0.33603 0.39031 0.42455 -0.03425 0.02033  0.19044  62  SER   A O   
480  C CB  . SER   A 62  ? 0.34822 0.41359 0.44438 -0.04070 0.03017  0.21897  62  SER   A CB  
481  O OG  . SER   A 62  ? 0.44285 0.52197 0.52896 -0.04295 0.03627  0.22590  62  SER   A OG  
482  N N   . ASN   A 63  ? 0.30396 0.33718 0.42426 -0.03945 0.02181  0.19551  63  ASN   A N   
483  C CA  . ASN   A 63  ? 0.30212 0.32258 0.42741 -0.03530 0.01705  0.18933  63  ASN   A CA  
484  C C   . ASN   A 63  ? 0.30947 0.33661 0.42607 -0.02915 0.01373  0.19611  63  ASN   A C   
485  O O   . ASN   A 63  ? 0.28026 0.30787 0.39081 -0.02516 0.01002  0.18920  63  ASN   A O   
486  C CB  . ASN   A 63  ? 0.30503 0.30571 0.44989 -0.03734 0.01713  0.18984  63  ASN   A CB  
487  C CG  . ASN   A 63  ? 0.29953 0.29170 0.45275 -0.04402 0.01816  0.17926  63  ASN   A CG  
488  O OD1 . ASN   A 63  ? 0.30484 0.30366 0.45118 -0.04534 0.01767  0.16957  63  ASN   A OD1 
489  N ND2 . ASN   A 63  ? 0.29225 0.27010 0.46043 -0.04877 0.01937  0.18131  63  ASN   A ND2 
490  N N   . HIS   A 64  ? 0.31944 0.35294 0.43574 -0.02874 0.01474  0.21014  64  HIS   A N   
491  C CA  . HIS   A 64  ? 0.33283 0.37407 0.44283 -0.02370 0.01085  0.21804  64  HIS   A CA  
492  C C   . HIS   A 64  ? 0.30307 0.36081 0.39035 -0.02291 0.00871  0.21400  64  HIS   A C   
493  O O   . HIS   A 64  ? 0.31329 0.37776 0.39467 -0.01934 0.00396  0.21729  64  HIS   A O   
494  C CB  . HIS   A 64  ? 0.34525 0.38925 0.46133 -0.02405 0.01242  0.23497  64  HIS   A CB  
495  C CG  . HIS   A 64  ? 0.37862 0.43881 0.47906 -0.02728 0.01544  0.24210  64  HIS   A CG  
496  N ND1 . HIS   A 64  ? 0.40675 0.46733 0.50990 -0.03246 0.02137  0.24424  64  HIS   A ND1 
497  C CD2 . HIS   A 64  ? 0.37617 0.45249 0.45798 -0.02627 0.01369  0.24767  64  HIS   A CD2 
498  C CE1 . HIS   A 64  ? 0.37866 0.45473 0.46516 -0.03379 0.02403  0.25062  64  HIS   A CE1 
499  N NE2 . HIS   A 64  ? 0.42495 0.51004 0.49721 -0.03031 0.01932  0.25240  64  HIS   A NE2 
500  N N   . ASN   A 65  ? 0.29951 0.36359 0.37445 -0.02623 0.01212  0.20643  65  ASN   A N   
501  C CA  . ASN   A 65  ? 0.28250 0.35860 0.33526 -0.02547 0.01044  0.19979  65  ASN   A CA  
502  C C   . ASN   A 65  ? 0.31457 0.38619 0.36674 -0.02254 0.00550  0.18864  65  ASN   A C   
503  O O   . ASN   A 65  ? 0.33508 0.41540 0.37021 -0.02178 0.00258  0.18370  65  ASN   A O   
504  C CB  . ASN   A 65  ? 0.32099 0.40361 0.36182 -0.02885 0.01668  0.19366  65  ASN   A CB  
505  C CG  . ASN   A 65  ? 0.36896 0.45846 0.40761 -0.03163 0.02239  0.20438  65  ASN   A CG  
506  O OD1 . ASN   A 65  ? 0.34600 0.43708 0.38713 -0.03457 0.02871  0.20235  65  ASN   A OD1 
507  N ND2 . ASN   A 65  ? 0.35507 0.45007 0.38944 -0.03075 0.02029  0.21649  65  ASN   A ND2 
508  N N   . PHE   A 66  ? 0.29966 0.35736 0.36918 -0.02130 0.00470  0.18406  66  PHE   A N   
509  C CA  . PHE   A 66  ? 0.28675 0.33941 0.35669 -0.01855 0.00097  0.17339  66  PHE   A CA  
510  C C   . PHE   A 66  ? 0.30260 0.35029 0.38408 -0.01365 -0.00314 0.17842  66  PHE   A C   
511  O O   . PHE   A 66  ? 0.28727 0.32188 0.38637 -0.01231 -0.00168 0.18151  66  PHE   A O   
512  C CB  . PHE   A 66  ? 0.24148 0.28209 0.32130 -0.02063 0.00342  0.16343  66  PHE   A CB  
513  C CG  . PHE   A 66  ? 0.23570 0.28288 0.30693 -0.02488 0.00771  0.15824  66  PHE   A CG  
514  C CD1 . PHE   A 66  ? 0.26836 0.32260 0.32493 -0.02455 0.00739  0.14915  66  PHE   A CD1 
515  C CD2 . PHE   A 66  ? 0.27732 0.32413 0.35610 -0.02903 0.01247  0.16275  66  PHE   A CD2 
516  C CE1 . PHE   A 66  ? 0.27608 0.33673 0.32627 -0.02741 0.01242  0.14448  66  PHE   A CE1 
517  C CE2 . PHE   A 66  ? 0.29861 0.35328 0.37171 -0.03220 0.01711  0.15835  66  PHE   A CE2 
518  C CZ  . PHE   A 66  ? 0.26949 0.33104 0.32858 -0.03094 0.01741  0.14916  66  PHE   A CZ  
519  N N   . LEU   A 67  ? 0.27812 0.33610 0.35006 -0.01118 -0.00797 0.17874  67  LEU   A N   
520  C CA  . LEU   A 67  ? 0.31072 0.36697 0.39425 -0.00607 -0.01172 0.18290  67  LEU   A CA  
521  C C   . LEU   A 67  ? 0.25044 0.29907 0.33781 -0.00346 -0.01295 0.17079  67  LEU   A C   
522  O O   . LEU   A 67  ? 0.26855 0.32439 0.34234 -0.00465 -0.01547 0.16274  67  LEU   A O   
523  C CB  . LEU   A 67  ? 0.31771 0.39095 0.39028 -0.00573 -0.01686 0.19008  67  LEU   A CB  
524  C CG  . LEU   A 67  ? 0.37978 0.46099 0.45362 -0.00611 -0.01723 0.20568  67  LEU   A CG  
525  C CD1 . LEU   A 67  ? 0.38129 0.45391 0.47855 -0.00115 -0.01652 0.21546  67  LEU   A CD1 
526  C CD2 . LEU   A 67  ? 0.36649 0.44829 0.43194 -0.01061 -0.01230 0.20861  67  LEU   A CD2 
527  N N   . VAL   A 68  ? 0.27667 0.30985 0.38160 -0.00004 -0.01075 0.16894  68  VAL   A N   
528  C CA  . VAL   A 68  ? 0.24459 0.26916 0.35395 0.00306  -0.01108 0.15772  68  VAL   A CA  
529  C C   . VAL   A 68  ? 0.26403 0.28760 0.38638 0.00971  -0.01216 0.16216  68  VAL   A C   
530  O O   . VAL   A 68  ? 0.24479 0.25939 0.38159 0.01258  -0.00941 0.16911  68  VAL   A O   
531  C CB  . VAL   A 68  ? 0.27411 0.28015 0.39133 0.00118  -0.00683 0.14900  68  VAL   A CB  
532  C CG1 . VAL   A 68  ? 0.27361 0.27097 0.39385 0.00464  -0.00701 0.13730  68  VAL   A CG1 
533  C CG2 . VAL   A 68  ? 0.24312 0.25290 0.34964 -0.00556 -0.00547 0.14568  68  VAL   A CG2 
534  N N   . GLN   A 69  ? 0.23648 0.26933 0.35437 0.01205  -0.01574 0.15819  69  GLN   A N   
535  C CA  . GLN   A 69  ? 0.29167 0.32815 0.42130 0.01810  -0.01689 0.16253  69  GLN   A CA  
536  C C   . GLN   A 69  ? 0.26143 0.28835 0.39614 0.02206  -0.01478 0.15066  69  GLN   A C   
537  O O   . GLN   A 69  ? 0.23271 0.26451 0.35629 0.01987  -0.01711 0.14188  69  GLN   A O   
538  C CB  . GLN   A 69  ? 0.29958 0.35746 0.41952 0.01632  -0.02324 0.16816  69  GLN   A CB  
539  C CG  . GLN   A 69  ? 0.34797 0.41823 0.46116 0.01282  -0.02605 0.18038  69  GLN   A CG  
540  C CD  . GLN   A 69  ? 0.41450 0.48981 0.54341 0.01736  -0.02681 0.19429  69  GLN   A CD  
541  O OE1 . GLN   A 69  ? 0.45513 0.51808 0.59992 0.02145  -0.02218 0.19951  69  GLN   A OE1 
542  N NE2 . GLN   A 69  ? 0.48664 0.57990 0.61173 0.01645  -0.03274 0.20019  69  GLN   A NE2 
543  N N   . ALA   A 70  ? 0.27684 0.28986 0.42756 0.02798  -0.00996 0.15005  70  ALA   A N   
544  C CA  . ALA   A 70  ? 0.29551 0.30018 0.45119 0.03281  -0.00699 0.13919  70  ALA   A CA  
545  C C   . ALA   A 70  ? 0.34811 0.36237 0.51533 0.03918  -0.00709 0.14622  70  ALA   A C   
546  O O   . ALA   A 70  ? 0.31872 0.32504 0.50071 0.04447  -0.00290 0.15214  70  ALA   A O   
547  C CB  . ALA   A 70  ? 0.28275 0.26297 0.44566 0.03441  -0.00047 0.13046  70  ALA   A CB  
548  N N   . GLY   A 71  ? 0.34808 0.37929 0.50921 0.03832  -0.01174 0.14569  71  GLY   A N   
549  C CA  . GLY   A 71  ? 0.38288 0.42766 0.55475 0.04243  -0.01326 0.15502  71  GLY   A CA  
550  C C   . GLY   A 71  ? 0.41782 0.47203 0.59244 0.04065  -0.01652 0.17001  71  GLY   A C   
551  O O   . GLY   A 71  ? 0.43591 0.49740 0.59688 0.03404  -0.02099 0.17270  71  GLY   A O   
552  N N   . ASN   A 72  ? 0.43910 0.49304 0.63150 0.04691  -0.01372 0.18014  72  ASN   A N   
553  C CA  . ASN   A 72  ? 0.47008 0.53207 0.66786 0.04631  -0.01617 0.19585  72  ASN   A CA  
554  C C   . ASN   A 72  ? 0.46979 0.51242 0.67587 0.04846  -0.01030 0.19852  72  ASN   A C   
555  O O   . ASN   A 72  ? 0.45811 0.50166 0.67758 0.05198  -0.00911 0.21177  72  ASN   A O   
556  C CB  . ASN   A 72  ? 0.46222 0.53881 0.67546 0.05138  -0.01765 0.20789  72  ASN   A CB  
557  C CG  . ASN   A 72  ? 0.54840 0.61290 0.77993 0.06077  -0.00975 0.20460  72  ASN   A CG  
558  O OD1 . ASN   A 72  ? 0.60833 0.65082 0.84252 0.06393  -0.00268 0.19523  72  ASN   A OD1 
559  N ND2 . ASN   A 72  ? 0.49494 0.57382 0.73885 0.06502  -0.01073 0.21216  72  ASN   A ND2 
560  N N   . VAL   A 73  ? 0.41707 0.44214 0.61597 0.04595  -0.00680 0.18649  73  VAL   A N   
561  C CA  . VAL   A 73  ? 0.42814 0.43294 0.63370 0.04620  -0.00147 0.18692  73  VAL   A CA  
562  C C   . VAL   A 73  ? 0.37499 0.37878 0.56487 0.03769  -0.00375 0.18335  73  VAL   A C   
563  O O   . VAL   A 73  ? 0.35662 0.36016 0.53381 0.03397  -0.00503 0.17163  73  VAL   A O   
564  C CB  . VAL   A 73  ? 0.43556 0.41694 0.64964 0.05130  0.00609  0.17445  73  VAL   A CB  
565  C CG1 . VAL   A 73  ? 0.41804 0.37693 0.63505 0.04874  0.01057  0.17170  73  VAL   A CG1 
566  C CG2 . VAL   A 73  ? 0.46732 0.44877 0.69854 0.06060  0.01002  0.17947  73  VAL   A CG2 
567  N N   . GLN   A 74  ? 0.40223 0.40619 0.59356 0.03480  -0.00390 0.19407  74  GLN   A N   
568  C CA  . GLN   A 74  ? 0.39416 0.39788 0.57211 0.02696  -0.00491 0.19190  74  GLN   A CA  
569  C C   . GLN   A 74  ? 0.37968 0.35970 0.56188 0.02491  0.00048  0.18205  74  GLN   A C   
570  O O   . GLN   A 74  ? 0.40267 0.36570 0.59917 0.02827  0.00511  0.18345  74  GLN   A O   
571  C CB  . GLN   A 74  ? 0.43510 0.44947 0.61197 0.02417  -0.00678 0.20752  74  GLN   A CB  
572  C CG  . GLN   A 74  ? 0.43826 0.45413 0.60068 0.01630  -0.00686 0.20499  74  GLN   A CG  
573  C CD  . GLN   A 74  ? 0.49849 0.52545 0.65747 0.01326  -0.00797 0.21980  74  GLN   A CD  
574  O OE1 . GLN   A 74  ? 0.54336 0.57687 0.71121 0.01678  -0.00926 0.23315  74  GLN   A OE1 
575  N NE2 . GLN   A 74  ? 0.46595 0.49505 0.61281 0.00684  -0.00691 0.21805  74  GLN   A NE2 
576  N N   . LEU   A 75  ? 0.30944 0.28838 0.47901 0.01882  -0.00024 0.17224  75  LEU   A N   
577  C CA  . LEU   A 75  ? 0.30752 0.26665 0.47935 0.01467  0.00361  0.16239  75  LEU   A CA  
578  C C   . LEU   A 75  ? 0.35286 0.31496 0.52091 0.00743  0.00380  0.16916  75  LEU   A C   
579  O O   . LEU   A 75  ? 0.37594 0.35381 0.53056 0.00334  0.00116  0.17077  75  LEU   A O   
580  C CB  . LEU   A 75  ? 0.31503 0.27165 0.47731 0.01268  0.00284  0.14701  75  LEU   A CB  
581  C CG  . LEU   A 75  ? 0.31596 0.26441 0.48256 0.01913  0.00446  0.13712  75  LEU   A CG  
582  C CD1 . LEU   A 75  ? 0.31358 0.25818 0.47053 0.01570  0.00384  0.12254  75  LEU   A CD1 
583  C CD2 . LEU   A 75  ? 0.38158 0.30865 0.56233 0.02324  0.00997  0.13494  75  LEU   A CD2 
584  N N   . ARG   A 76  ? 0.31440 0.26100 0.49393 0.00577  0.00742  0.17263  76  ARG   A N   
585  C CA  . ARG   A 76  ? 0.35371 0.30232 0.53172 -0.00144 0.00835  0.17908  76  ARG   A CA  
586  C C   . ARG   A 76  ? 0.32591 0.27120 0.49658 -0.00887 0.00864  0.16690  76  ARG   A C   
587  O O   . ARG   A 76  ? 0.30070 0.22834 0.47606 -0.01081 0.01019  0.15479  76  ARG   A O   
588  C CB  . ARG   A 76  ? 0.37421 0.30574 0.56769 -0.00174 0.01208  0.18587  76  ARG   A CB  
589  C CG  . ARG   A 76  ? 0.38431 0.32138 0.57792 -0.00825 0.01311  0.19676  76  ARG   A CG  
590  C CD  . ARG   A 76  ? 0.46700 0.38868 0.67662 -0.00754 0.01641  0.20626  76  ARG   A CD  
591  N NE  . ARG   A 76  ? 0.50329 0.39871 0.72135 -0.01014 0.01935  0.19380  76  ARG   A NE  
592  C CZ  . ARG   A 76  ? 0.55467 0.43730 0.77784 -0.01845 0.02145  0.19220  76  ARG   A CZ  
593  N NH1 . ARG   A 76  ? 0.56414 0.45863 0.78639 -0.02416 0.02167  0.20324  76  ARG   A NH1 
594  N NH2 . ARG   A 76  ? 0.58783 0.44598 0.81639 -0.02149 0.02341  0.17932  76  ARG   A NH2 
595  N N   . VAL   A 77  ? 0.32715 0.28957 0.48610 -0.01319 0.00739  0.16996  77  VAL   A N   
596  C CA  . VAL   A 77  ? 0.28638 0.24907 0.44018 -0.02039 0.00810  0.16088  77  VAL   A CA  
597  C C   . VAL   A 77  ? 0.30058 0.25475 0.46421 -0.02707 0.01111  0.16500  77  VAL   A C   
598  O O   . VAL   A 77  ? 0.28802 0.24838 0.45407 -0.02759 0.01259  0.17829  77  VAL   A O   
599  C CB  . VAL   A 77  ? 0.26930 0.25353 0.40683 -0.02161 0.00685  0.16248  77  VAL   A CB  
600  C CG1 . VAL   A 77  ? 0.26767 0.25378 0.40220 -0.02840 0.00833  0.15409  77  VAL   A CG1 
601  C CG2 . VAL   A 77  ? 0.27542 0.26736 0.40309 -0.01600 0.00332  0.15806  77  VAL   A CG2 
602  N N   . ILE   A 78  ? 0.29797 0.23837 0.46707 -0.03280 0.01171  0.15369  78  ILE   A N   
603  C CA  . ILE   A 78  ? 0.29257 0.22347 0.47187 -0.04050 0.01391  0.15586  78  ILE   A CA  
604  C C   . ILE   A 78  ? 0.30261 0.24218 0.47930 -0.04889 0.01376  0.14982  78  ILE   A C   
605  O O   . ILE   A 78  ? 0.34470 0.27982 0.52996 -0.05644 0.01521  0.15178  78  ILE   A O   
606  C CB  . ILE   A 78  ? 0.31080 0.21527 0.50072 -0.04127 0.01468  0.14825  78  ILE   A CB  
607  C CG1 . ILE   A 78  ? 0.31397 0.20911 0.49918 -0.04240 0.01266  0.13006  78  ILE   A CG1 
608  C CG2 . ILE   A 78  ? 0.34436 0.24138 0.54005 -0.03239 0.01601  0.15661  78  ILE   A CG2 
609  C CD1 . ILE   A 78  ? 0.38918 0.25819 0.58142 -0.04705 0.01360  0.11945  78  ILE   A CD1 
610  N N   . GLY   A 79  ? 0.28496 0.23752 0.45104 -0.04780 0.01212  0.14312  79  GLY   A N   
611  C CA  . GLY   A 79  ? 0.25117 0.21545 0.41546 -0.05437 0.01236  0.13868  79  GLY   A CA  
612  C C   . GLY   A 79  ? 0.24530 0.22490 0.39625 -0.05029 0.01140  0.13459  79  GLY   A C   
613  O O   . GLY   A 79  ? 0.26084 0.23835 0.40501 -0.04393 0.00949  0.13196  79  GLY   A O   
614  N N   . HIS   A 80  ? 0.23046 0.22580 0.37823 -0.05378 0.01317  0.13447  80  HIS   A N   
615  C CA  . HIS   A 80  ? 0.21555 0.22471 0.35068 -0.05039 0.01313  0.12987  80  HIS   A CA  
616  C C   . HIS   A 80  ? 0.21763 0.23760 0.35637 -0.05564 0.01440  0.12475  80  HIS   A C   
617  O O   . HIS   A 80  ? 0.20885 0.23361 0.35593 -0.06048 0.01700  0.13001  80  HIS   A O   
618  C CB  . HIS   A 80  ? 0.22731 0.25000 0.34900 -0.04528 0.01589  0.13950  80  HIS   A CB  
619  C CG  . HIS   A 80  ? 0.23890 0.27130 0.36229 -0.04801 0.02066  0.14986  80  HIS   A CG  
620  N ND1 . HIS   A 80  ? 0.27827 0.30563 0.40763 -0.04843 0.02154  0.16090  80  HIS   A ND1 
621  C CD2 . HIS   A 80  ? 0.24857 0.29572 0.36897 -0.05006 0.02541  0.15116  80  HIS   A CD2 
622  C CE1 . HIS   A 80  ? 0.31786 0.35650 0.44730 -0.05122 0.02637  0.16873  80  HIS   A CE1 
623  N NE2 . HIS   A 80  ? 0.28599 0.33673 0.41009 -0.05204 0.02906  0.16276  80  HIS   A NE2 
624  N N   . SER   A 81  ? 0.18716 0.21179 0.32086 -0.05452 0.01253  0.11513  81  SER   A N   
625  C CA  . SER   A 81  ? 0.18395 0.22177 0.32109 -0.05776 0.01361  0.11063  81  SER   A CA  
626  C C   . SER   A 81  ? 0.18534 0.23172 0.31118 -0.05283 0.01368  0.10441  81  SER   A C   
627  O O   . SER   A 81  ? 0.22316 0.26261 0.34087 -0.04892 0.01136  0.10161  81  SER   A O   
628  C CB  . SER   A 81  ? 0.17391 0.20422 0.32376 -0.06503 0.00886  0.10235  81  SER   A CB  
629  O OG  . SER   A 81  ? 0.23516 0.24929 0.38325 -0.06461 0.00391  0.09330  81  SER   A OG  
630  N N   . MET   A 82  ? 0.14780 0.20931 0.27409 -0.05268 0.01664  0.10250  82  MET   A N   
631  C CA  . MET   A 82  ? 0.16732 0.23590 0.28554 -0.04848 0.01660  0.09524  82  MET   A CA  
632  C C   . MET   A 82  ? 0.14993 0.21886 0.27783 -0.05191 0.01115  0.08596  82  MET   A C   
633  O O   . MET   A 82  ? 0.14449 0.21754 0.28419 -0.05684 0.00988  0.08605  82  MET   A O   
634  C CB  . MET   A 82  ? 0.23822 0.32287 0.34880 -0.04392 0.02418  0.09768  82  MET   A CB  
635  C CG  . MET   A 82  ? 0.30471 0.39053 0.39670 -0.03873 0.02834  0.10089  82  MET   A CG  
636  S SD  . MET   A 82  ? 0.24412 0.34592 0.32795 -0.03399 0.03833  0.10081  82  MET   A SD  
637  C CE  . MET   A 82  ? 0.26712 0.37655 0.36987 -0.03859 0.04120  0.10760  82  MET   A CE  
638  N N   . GLN   A 83  ? 0.14535 0.21150 0.26686 -0.04908 0.00770  0.07797  83  GLN   A N   
639  C CA  . GLN   A 83  ? 0.20469 0.27553 0.33012 -0.04980 0.00300  0.06882  83  GLN   A CA  
640  C C   . GLN   A 83  ? 0.12196 0.20077 0.23464 -0.04114 0.00632  0.06484  83  GLN   A C   
641  O O   . GLN   A 83  ? 0.11902 0.18934 0.21722 -0.03586 0.00495  0.05915  83  GLN   A O   
642  C CB  . GLN   A 83  ? 0.21262 0.26808 0.33614 -0.05211 -0.00477 0.05897  83  GLN   A CB  
643  C CG  . GLN   A 83  ? 0.24493 0.30669 0.36871 -0.05234 -0.00994 0.05024  83  GLN   A CG  
644  C CD  . GLN   A 83  ? 0.37608 0.42568 0.50174 -0.05866 -0.01757 0.04154  83  GLN   A CD  
645  O OE1 . GLN   A 83  ? 0.41826 0.45149 0.54427 -0.06157 -0.01825 0.04040  83  GLN   A OE1 
646  N NE2 . GLN   A 83  ? 0.35962 0.41683 0.48590 -0.06059 -0.02309 0.03537  83  GLN   A NE2 
647  N N   . ASN   A 84  ? 0.10898 0.20386 0.22841 -0.03973 0.01123  0.06830  84  ASN   A N   
648  C CA  . ASN   A 84  ? 0.13536 0.23616 0.24414 -0.03131 0.01595  0.06467  84  ASN   A CA  
649  C C   . ASN   A 84  ? 0.10714 0.20097 0.19683 -0.02654 0.02034  0.06471  84  ASN   A C   
650  O O   . ASN   A 84  ? 0.12065 0.21741 0.20851 -0.02785 0.02573  0.07273  84  ASN   A O   
651  C CB  . ASN   A 84  ? 0.09957 0.19754 0.20636 -0.02902 0.00947  0.05549  84  ASN   A CB  
652  C CG  . ASN   A 84  ? 0.11201 0.21893 0.23647 -0.03495 0.00382  0.05621  84  ASN   A CG  
653  O OD1 . ASN   A 84  ? 0.08889 0.20893 0.22505 -0.03524 0.00726  0.06164  84  ASN   A OD1 
654  N ND2 . ASN   A 84  ? 0.10551 0.20314 0.22904 -0.03950 -0.00493 0.04984  84  ASN   A ND2 
655  N N   . CYS   A 85  ? 0.11065 0.19601 0.18598 -0.02189 0.01761  0.05667  85  CYS   A N   
656  C CA  . CYS   A 85  ? 0.10719 0.18801 0.16460 -0.01862 0.02065  0.05667  85  CYS   A CA  
657  C C   . CYS   A 85  ? 0.14817 0.21807 0.20051 -0.02061 0.01486  0.05777  85  CYS   A C   
658  O O   . CYS   A 85  ? 0.12132 0.18846 0.15917 -0.01847 0.01517  0.05796  85  CYS   A O   
659  C CB  . CYS   A 85  ? 0.11346 0.19246 0.15864 -0.01279 0.02209  0.04822  85  CYS   A CB  
660  S SG  . CYS   A 85  ? 0.12728 0.21828 0.17754 -0.00827 0.03195  0.04874  85  CYS   A SG  
661  N N   . VAL   A 86  ? 0.09734 0.16118 0.16163 -0.02475 0.00982  0.05879  86  VAL   A N   
662  C CA  . VAL   A 86  ? 0.12848 0.18188 0.19102 -0.02558 0.00618  0.06160  86  VAL   A CA  
663  C C   . VAL   A 86  ? 0.12128 0.17404 0.19488 -0.03054 0.00800  0.07220  86  VAL   A C   
664  O O   . VAL   A 86  ? 0.12229 0.18104 0.20817 -0.03503 0.01023  0.07567  86  VAL   A O   
665  C CB  . VAL   A 86  ? 0.16578 0.20826 0.23073 -0.02515 -0.00004 0.05337  86  VAL   A CB  
666  C CG1 . VAL   A 86  ? 0.15141 0.19520 0.20577 -0.02053 -0.00139 0.04457  86  VAL   A CG1 
667  C CG2 . VAL   A 86  ? 0.16427 0.20439 0.24256 -0.03031 -0.00257 0.05060  86  VAL   A CG2 
668  N N   . LEU   A 87  ? 0.11805 0.16470 0.18806 -0.02972 0.00710  0.07871  87  LEU   A N   
669  C CA  . LEU   A 87  ? 0.12898 0.17138 0.20945 -0.03370 0.00826  0.09012  87  LEU   A CA  
670  C C   . LEU   A 87  ? 0.13166 0.15782 0.22209 -0.03470 0.00355  0.08675  87  LEU   A C   
671  O O   . LEU   A 87  ? 0.16161 0.18128 0.24639 -0.03026 0.00015  0.07979  87  LEU   A O   
672  C CB  . LEU   A 87  ? 0.14249 0.18922 0.21222 -0.03137 0.01034  0.10109  87  LEU   A CB  
673  C CG  . LEU   A 87  ? 0.22502 0.27348 0.29979 -0.03376 0.01345  0.11348  87  LEU   A CG  
674  C CD1 . LEU   A 87  ? 0.23443 0.29309 0.31321 -0.03680 0.01903  0.11430  87  LEU   A CD1 
675  C CD2 . LEU   A 87  ? 0.23026 0.28419 0.28922 -0.02990 0.01316  0.11992  87  LEU   A CD2 
676  N N   . LYS   A 88  ? 0.15870 0.17788 0.26429 -0.04076 0.00394  0.09124  88  LYS   A N   
677  C CA  . LYS   A 88  ? 0.22041 0.22095 0.33564 -0.04221 0.00092  0.08804  88  LYS   A CA  
678  C C   . LYS   A 88  ? 0.18774 0.18190 0.30850 -0.04178 0.00296  0.09920  88  LYS   A C   
679  O O   . LYS   A 88  ? 0.21650 0.21319 0.34387 -0.04626 0.00503  0.10398  88  LYS   A O   
680  C CB  . LYS   A 88  ? 0.14957 0.14465 0.27450 -0.04929 -0.00179 0.07834  88  LYS   A CB  
681  C CG  . LYS   A 88  ? 0.16677 0.17036 0.28328 -0.04760 -0.00461 0.06593  88  LYS   A CG  
682  C CD  . LYS   A 88  ? 0.17628 0.17809 0.30149 -0.05547 -0.00856 0.05775  88  LYS   A CD  
683  C CE  . LYS   A 88  ? 0.25627 0.23719 0.38960 -0.06077 -0.01080 0.05374  88  LYS   A CE  
684  N NZ  . LYS   A 88  ? 0.36373 0.34333 0.49856 -0.06787 -0.01615 0.04189  88  LYS   A NZ  
685  N N   . LEU   A 89  ? 0.16817 0.15578 0.28618 -0.03566 0.00221  0.10316  89  LEU   A N   
686  C CA  . LEU   A 89  ? 0.18395 0.16662 0.30704 -0.03360 0.00361  0.11338  89  LEU   A CA  
687  C C   . LEU   A 89  ? 0.20325 0.16482 0.33786 -0.03382 0.00307  0.10788  89  LEU   A C   
688  O O   . LEU   A 89  ? 0.21626 0.16847 0.35060 -0.02899 0.00181  0.10160  89  LEU   A O   
689  C CB  . LEU   A 89  ? 0.18745 0.17797 0.30163 -0.02649 0.00265  0.12118  89  LEU   A CB  
690  C CG  . LEU   A 89  ? 0.19702 0.20642 0.29541 -0.02612 0.00305  0.12383  89  LEU   A CG  
691  C CD1 . LEU   A 89  ? 0.22603 0.24330 0.31446 -0.02044 0.00044  0.12965  89  LEU   A CD1 
692  C CD2 . LEU   A 89  ? 0.20679 0.22542 0.30453 -0.03048 0.00704  0.13024  89  LEU   A CD2 
693  N N   . LYS   A 90  ? 0.21067 0.16418 0.35480 -0.03938 0.00450  0.10938  90  LYS   A N   
694  C CA  . LYS   A 90  ? 0.23121 0.16277 0.38418 -0.03941 0.00482  0.10393  90  LYS   A CA  
695  C C   . LYS   A 90  ? 0.26466 0.19117 0.42204 -0.03245 0.00669  0.11459  90  LYS   A C   
696  O O   . LYS   A 90  ? 0.31243 0.24809 0.47120 -0.03240 0.00798  0.12764  90  LYS   A O   
697  C CB  . LYS   A 90  ? 0.29103 0.21340 0.45219 -0.04901 0.00509  0.10008  90  LYS   A CB  
698  C CG  . LYS   A 90  ? 0.34329 0.24067 0.50993 -0.04893 0.00573  0.09194  90  LYS   A CG  
699  C CD  . LYS   A 90  ? 0.39698 0.28248 0.56994 -0.05919 0.00535  0.08664  90  LYS   A CD  
700  C CE  . LYS   A 90  ? 0.47730 0.36857 0.64503 -0.06624 0.00141  0.07361  90  LYS   A CE  
701  N NZ  . LYS   A 90  ? 0.50480 0.38479 0.66462 -0.06264 -0.00010 0.05893  90  LYS   A NZ  
702  N N   . VAL   A 91  ? 0.24521 0.15868 0.40471 -0.02617 0.00705  0.10911  91  VAL   A N   
703  C CA  . VAL   A 91  ? 0.28581 0.19546 0.45148 -0.01853 0.00881  0.11872  91  VAL   A CA  
704  C C   . VAL   A 91  ? 0.30801 0.19300 0.48387 -0.01910 0.01184  0.11355  91  VAL   A C   
705  O O   . VAL   A 91  ? 0.32924 0.19968 0.50439 -0.02463 0.01198  0.10004  91  VAL   A O   
706  C CB  . VAL   A 91  ? 0.27341 0.19114 0.43420 -0.00952 0.00750  0.11838  91  VAL   A CB  
707  C CG1 . VAL   A 91  ? 0.27671 0.21713 0.42545 -0.01042 0.00435  0.12283  91  VAL   A CG1 
708  C CG2 . VAL   A 91  ? 0.26086 0.16548 0.42016 -0.00757 0.00809  0.10248  91  VAL   A CG2 
709  N N   . ASP   A 92  ? 0.32677 0.20731 0.51149 -0.01388 0.01413  0.12452  92  ASP   A N   
710  C CA  . ASP   A 92  ? 0.37145 0.22747 0.56614 -0.01425 0.01772  0.12125  92  ASP   A CA  
711  C C   . ASP   A 92  ? 0.38429 0.22498 0.57934 -0.00710 0.02024  0.10950  92  ASP   A C   
712  O O   . ASP   A 92  ? 0.41391 0.23243 0.61579 -0.00624 0.02398  0.10540  92  ASP   A O   
713  C CB  . ASP   A 92  ? 0.39964 0.25631 0.60518 -0.01124 0.01968  0.13855  92  ASP   A CB  
714  C CG  . ASP   A 92  ? 0.42123 0.29094 0.62922 -0.00042 0.01946  0.14904  92  ASP   A CG  
715  O OD1 . ASP   A 92  ? 0.40164 0.27713 0.60441 0.00526  0.01847  0.14235  92  ASP   A OD1 
716  O OD2 . ASP   A 92  ? 0.48048 0.35527 0.69634 0.00206  0.02012  0.16457  92  ASP   A OD2 
717  N N   . THR   A 93  ? 0.35219 0.20382 0.53985 -0.00184 0.01879  0.10411  93  THR   A N   
718  C CA  . THR   A 93  ? 0.37038 0.21109 0.55833 0.00616  0.02199  0.09419  93  THR   A CA  
719  C C   . THR   A 93  ? 0.31943 0.16250 0.49540 0.00409  0.02015  0.07897  93  THR   A C   
720  O O   . THR   A 93  ? 0.28649 0.14891 0.45583 0.00336  0.01629  0.08172  93  THR   A O   
721  C CB  . THR   A 93  ? 0.34880 0.20335 0.54292 0.01704  0.02271  0.10611  93  THR   A CB  
722  O OG1 . THR   A 93  ? 0.40999 0.26722 0.61450 0.01807  0.02319  0.12250  93  THR   A OG1 
723  C CG2 . THR   A 93  ? 0.36488 0.20688 0.56271 0.02592  0.02776  0.09735  93  THR   A CG2 
724  N N   . ALA   A 94  ? 0.33099 0.15412 0.50317 0.00300  0.02291  0.06282  94  ALA   A N   
725  C CA  . ALA   A 94  ? 0.29895 0.12413 0.45968 0.00255  0.02181  0.04825  94  ALA   A CA  
726  C C   . ALA   A 94  ? 0.32076 0.15471 0.48232 0.01436  0.02444  0.04959  94  ALA   A C   
727  O O   . ALA   A 94  ? 0.32350 0.15098 0.49348 0.02268  0.02913  0.05371  94  ALA   A O   
728  C CB  . ALA   A 94  ? 0.32056 0.12272 0.47418 -0.00299 0.02362  0.03012  94  ALA   A CB  
729  N N   . ASN   A 95  ? 0.29566 0.14519 0.44961 0.01492  0.02143  0.04684  95  ASN   A N   
730  C CA  . ASN   A 95  ? 0.27707 0.13788 0.43163 0.02496  0.02323  0.04838  95  ASN   A CA  
731  C C   . ASN   A 95  ? 0.29259 0.13715 0.44490 0.03044  0.02977  0.03442  95  ASN   A C   
732  O O   . ASN   A 95  ? 0.31233 0.14869 0.45325 0.02620  0.03007  0.01888  95  ASN   A O   
733  C CB  . ASN   A 95  ? 0.22892 0.10744 0.37479 0.02304  0.01845  0.04699  95  ASN   A CB  
734  C CG  . ASN   A 95  ? 0.21735 0.11070 0.36445 0.03231  0.01933  0.05038  95  ASN   A CG  
735  O OD1 . ASN   A 95  ? 0.22869 0.11977 0.38342 0.04028  0.02398  0.05271  95  ASN   A OD1 
736  N ND2 . ASN   A 95  ? 0.20096 0.11011 0.34110 0.03091  0.01481  0.05072  95  ASN   A ND2 
737  N N   . PRO   A 96  ? 0.32852 0.16917 0.49048 0.03969  0.03516  0.03922  96  PRO   A N   
738  C CA  . PRO   A 96  ? 0.32340 0.14857 0.48211 0.04535  0.04244  0.02558  96  PRO   A CA  
739  C C   . PRO   A 96  ? 0.29115 0.12762 0.44112 0.04916  0.04358  0.01730  96  PRO   A C   
740  O O   . PRO   A 96  ? 0.34482 0.16950 0.48710 0.05193  0.04926  0.00331  96  PRO   A O   
741  C CB  . PRO   A 96  ? 0.32295 0.14610 0.49735 0.05494  0.04757  0.03656  96  PRO   A CB  
742  C CG  . PRO   A 96  ? 0.32123 0.16839 0.50454 0.05615  0.04206  0.05552  96  PRO   A CG  
743  C CD  . PRO   A 96  ? 0.28808 0.13997 0.46398 0.04541  0.03487  0.05746  96  PRO   A CD  
744  N N   . LYS   A 97  ? 0.26378 0.12258 0.41341 0.04889  0.03834  0.02517  97  LYS   A N   
745  C CA  . LYS   A 97  ? 0.28764 0.15821 0.42963 0.05183  0.03902  0.01838  97  LYS   A CA  
746  C C   . LYS   A 97  ? 0.25371 0.12426 0.38191 0.04310  0.03458  0.00786  97  LYS   A C   
747  O O   . LYS   A 97  ? 0.24118 0.12462 0.36372 0.04454  0.03367  0.00478  97  LYS   A O   
748  C CB  . LYS   A 97  ? 0.23289 0.12857 0.38316 0.05693  0.03580  0.03310  97  LYS   A CB  
749  C CG  . LYS   A 97  ? 0.26318 0.16260 0.42736 0.06599  0.04045  0.04228  97  LYS   A CG  
750  C CD  . LYS   A 97  ? 0.30996 0.23617 0.48081 0.06815  0.03517  0.05675  97  LYS   A CD  
751  C CE  . LYS   A 97  ? 0.32480 0.25670 0.51043 0.07186  0.03474  0.07233  97  LYS   A CE  
752  N NZ  . LYS   A 97  ? 0.38131 0.33969 0.56914 0.07026  0.02709  0.08561  97  LYS   A NZ  
753  N N   . THR   A 98  ? 0.25553 0.11289 0.37910 0.03371  0.03167  0.00256  98  THR   A N   
754  C CA  . THR   A 98  ? 0.23395 0.09359 0.34610 0.02449  0.02658  -0.00669 98  THR   A CA  
755  C C   . THR   A 98  ? 0.28017 0.13592 0.37831 0.02557  0.03028  -0.02352 98  THR   A C   
756  O O   . THR   A 98  ? 0.28129 0.12057 0.37255 0.02589  0.03505  -0.03450 98  THR   A O   
757  C CB  . THR   A 98  ? 0.24607 0.09381 0.35661 0.01324  0.02271  -0.00960 98  THR   A CB  
758  O OG1 . THR   A 98  ? 0.23985 0.09265 0.36233 0.01260  0.02034  0.00688  98  THR   A OG1 
759  C CG2 . THR   A 98  ? 0.22989 0.08696 0.32920 0.00304  0.01584  -0.01682 98  THR   A CG2 
760  N N   . PRO   A 99  ? 0.26695 0.14177 0.35550 0.02554  0.02727  -0.02479 99  PRO   A N   
761  C CA  . PRO   A 99  ? 0.26399 0.13770 0.33667 0.02555  0.03031  -0.03952 99  PRO   A CA  
762  C C   . PRO   A 99  ? 0.27993 0.14738 0.33834 0.01354  0.02465  -0.05111 99  PRO   A C   
763  O O   . PRO   A 99  ? 0.25023 0.11966 0.31195 0.00540  0.01787  -0.04633 99  PRO   A O   
764  C CB  . PRO   A 99  ? 0.22732 0.12634 0.29584 0.02804  0.02721  -0.03312 99  PRO   A CB  
765  C CG  . PRO   A 99  ? 0.22995 0.14108 0.30222 0.02219  0.01875  -0.02214 99  PRO   A CG  
766  C CD  . PRO   A 99  ? 0.24375 0.14248 0.33152 0.02333  0.01997  -0.01357 99  PRO   A CD  
767  N N   . LYS   A 100 ? 0.25861 0.12064 0.30097 0.01221  0.02733  -0.06573 100 LYS   A N   
768  C CA  . LYS   A 100 ? 0.27420 0.13836 0.30161 0.00045  0.01967  -0.07470 100 LYS   A CA  
769  C C   . LYS   A 100 ? 0.28163 0.17129 0.30746 -0.00208 0.01186  -0.06497 100 LYS   A C   
770  O O   . LYS   A 100 ? 0.22771 0.13182 0.25303 0.00456  0.01369  -0.05932 100 LYS   A O   
771  C CB  . LYS   A 100 ? 0.36784 0.22452 0.37557 -0.00027 0.02357  -0.09114 100 LYS   A CB  
772  C CG  . LYS   A 100 ? 0.41415 0.27403 0.40643 -0.01319 0.01419  -0.09947 100 LYS   A CG  
773  C CD  . LYS   A 100 ? 0.52137 0.37763 0.48989 -0.01413 0.01544  -0.11164 100 LYS   A CD  
774  C CE  . LYS   A 100 ? 0.45699 0.31843 0.41273 -0.02729 0.00375  -0.11631 100 LYS   A CE  
775  N NZ  . LYS   A 100 ? 0.48699 0.37247 0.44337 -0.03106 -0.00340 -0.10968 100 LYS   A NZ  
776  N N   . TYR   A 101 ? 0.21306 0.10821 0.24011 -0.01147 0.00369  -0.06218 101 TYR   A N   
777  C CA  . TYR   A 101 ? 0.20099 0.11844 0.22861 -0.01217 -0.00191 -0.05235 101 TYR   A CA  
778  C C   . TYR   A 101 ? 0.21697 0.14207 0.23889 -0.02254 -0.01013 -0.05515 101 TYR   A C   
779  O O   . TYR   A 101 ? 0.20685 0.12111 0.22745 -0.03076 -0.01292 -0.06252 101 TYR   A O   
780  C CB  . TYR   A 101 ? 0.18181 0.10496 0.22445 -0.00911 -0.00205 -0.03796 101 TYR   A CB  
781  C CG  . TYR   A 101 ? 0.21272 0.12882 0.26508 -0.01620 -0.00494 -0.03409 101 TYR   A CG  
782  C CD1 . TYR   A 101 ? 0.22046 0.11725 0.28244 -0.01561 -0.00087 -0.03417 101 TYR   A CD1 
783  C CD2 . TYR   A 101 ? 0.22634 0.15561 0.28003 -0.02301 -0.01097 -0.02903 101 TYR   A CD2 
784  C CE1 . TYR   A 101 ? 0.24637 0.13680 0.31837 -0.02284 -0.00330 -0.02934 101 TYR   A CE1 
785  C CE2 . TYR   A 101 ? 0.20012 0.12489 0.26413 -0.02978 -0.01293 -0.02425 101 TYR   A CE2 
786  C CZ  . TYR   A 101 ? 0.22533 0.13072 0.29820 -0.03018 -0.00936 -0.02428 101 TYR   A CZ  
787  O OH  . TYR   A 101 ? 0.27360 0.17423 0.35780 -0.03771 -0.01109 -0.01849 101 TYR   A OH  
788  N N   . LYS   A 102 ? 0.21683 0.16113 0.23692 -0.02212 -0.01401 -0.04848 102 LYS   A N   
789  C CA  . LYS   A 102 ? 0.17971 0.13630 0.19900 -0.02982 -0.02147 -0.04688 102 LYS   A CA  
790  C C   . LYS   A 102 ? 0.16496 0.13690 0.19166 -0.02663 -0.02225 -0.03489 102 LYS   A C   
791  O O   . LYS   A 102 ? 0.15005 0.12623 0.17616 -0.01944 -0.01877 -0.03043 102 LYS   A O   
792  C CB  . LYS   A 102 ? 0.20914 0.17353 0.21369 -0.03209 -0.02503 -0.05373 102 LYS   A CB  
793  C CG  . LYS   A 102 ? 0.30140 0.25187 0.29334 -0.03583 -0.02431 -0.06739 102 LYS   A CG  
794  C CD  . LYS   A 102 ? 0.33589 0.29826 0.31273 -0.03941 -0.02959 -0.07158 102 LYS   A CD  
795  C CE  . LYS   A 102 ? 0.33139 0.30279 0.30171 -0.03056 -0.02512 -0.06773 102 LYS   A CE  
796  N NZ  . LYS   A 102 ? 0.44159 0.42972 0.40269 -0.03322 -0.03127 -0.06528 102 LYS   A NZ  
797  N N   . PHE   A 103 ? 0.15769 0.13833 0.19119 -0.03240 -0.02667 -0.03014 103 PHE   A N   
798  C CA  . PHE   A 103 ? 0.11446 0.11016 0.15250 -0.02980 -0.02700 -0.02072 103 PHE   A CA  
799  C C   . PHE   A 103 ? 0.13281 0.14173 0.16504 -0.03103 -0.03128 -0.02188 103 PHE   A C   
800  O O   . PHE   A 103 ? 0.13542 0.14963 0.16979 -0.03789 -0.03661 -0.02355 103 PHE   A O   
801  C CB  . PHE   A 103 ? 0.11449 0.11330 0.16502 -0.03430 -0.02760 -0.01347 103 PHE   A CB  
802  C CG  . PHE   A 103 ? 0.12161 0.11008 0.17878 -0.03251 -0.02345 -0.00876 103 PHE   A CG  
803  C CD1 . PHE   A 103 ? 0.11697 0.09778 0.17064 -0.02561 -0.01954 -0.00897 103 PHE   A CD1 
804  C CD2 . PHE   A 103 ? 0.12367 0.11206 0.19204 -0.03754 -0.02337 -0.00224 103 PHE   A CD2 
805  C CE1 . PHE   A 103 ? 0.13677 0.10989 0.19787 -0.02343 -0.01632 -0.00257 103 PHE   A CE1 
806  C CE2 . PHE   A 103 ? 0.13467 0.11426 0.20930 -0.03563 -0.01962 0.00420  103 PHE   A CE2 
807  C CZ  . PHE   A 103 ? 0.12530 0.09725 0.19628 -0.02841 -0.01644 0.00422  103 PHE   A CZ  
808  N N   . VAL   A 104 ? 0.10014 0.11497 0.12636 -0.02483 -0.02939 -0.02000 104 VAL   A N   
809  C CA  . VAL   A 104 ? 0.12494 0.15125 0.14610 -0.02473 -0.03277 -0.01953 104 VAL   A CA  
810  C C   . VAL   A 104 ? 0.13486 0.16989 0.16080 -0.01992 -0.03042 -0.01165 104 VAL   A C   
811  O O   . VAL   A 104 ? 0.21889 0.25002 0.24571 -0.01593 -0.02614 -0.00907 104 VAL   A O   
812  C CB  . VAL   A 104 ? 0.11313 0.13668 0.12121 -0.02204 -0.03196 -0.02508 104 VAL   A CB  
813  C CG1 . VAL   A 104 ? 0.16857 0.18051 0.16944 -0.02626 -0.03253 -0.03498 104 VAL   A CG1 
814  C CG2 . VAL   A 104 ? 0.18943 0.21020 0.19612 -0.01509 -0.02638 -0.02265 104 VAL   A CG2 
815  N N   . ARG   A 105 ? 0.09945 0.14626 0.12855 -0.02033 -0.03323 -0.00778 105 ARG   A N   
816  C CA  . ARG   A 105 ? 0.06967 0.12254 0.10197 -0.01497 -0.02994 -0.00171 105 ARG   A CA  
817  C C   . ARG   A 105 ? 0.08670 0.14190 0.11137 -0.01145 -0.03048 -0.00171 105 ARG   A C   
818  O O   . ARG   A 105 ? 0.11292 0.17359 0.13426 -0.01381 -0.03511 -0.00262 105 ARG   A O   
819  C CB  . ARG   A 105 ? 0.07093 0.13550 0.11499 -0.01626 -0.03104 0.00415  105 ARG   A CB  
820  C CG  . ARG   A 105 ? 0.06044 0.12841 0.10772 -0.01005 -0.02559 0.00925  105 ARG   A CG  
821  C CD  . ARG   A 105 ? 0.05927 0.13977 0.12040 -0.01062 -0.02515 0.01537  105 ARG   A CD  
822  N NE  . ARG   A 105 ? 0.06895 0.15198 0.13283 -0.00376 -0.01891 0.01932  105 ARG   A NE  
823  C CZ  . ARG   A 105 ? 0.05606 0.13600 0.12000 -0.00144 -0.01219 0.02020  105 ARG   A CZ  
824  N NH1 . ARG   A 105 ? 0.05704 0.13286 0.11964 -0.00538 -0.01151 0.01922  105 ARG   A NH1 
825  N NH2 . ARG   A 105 ? 0.05706 0.13729 0.12171 0.00479  -0.00582 0.02208  105 ARG   A NH2 
826  N N   . ILE   A 106 ? 0.10577 0.15704 0.12727 -0.00662 -0.02615 -0.00037 106 ILE   A N   
827  C CA  . ILE   A 106 ? 0.12243 0.17530 0.13815 -0.00369 -0.02610 0.00090  106 ILE   A CA  
828  C C   . ILE   A 106 ? 0.09716 0.15625 0.11897 -0.00019 -0.02515 0.00712  106 ILE   A C   
829  O O   . ILE   A 106 ? 0.12757 0.18900 0.15726 0.00089  -0.02299 0.00965  106 ILE   A O   
830  C CB  . ILE   A 106 ? 0.12053 0.16567 0.13042 -0.00137 -0.02235 -0.00100 106 ILE   A CB  
831  C CG1 . ILE   A 106 ? 0.09466 0.13618 0.10802 0.00032  -0.01880 0.00066  106 ILE   A CG1 
832  C CG2 . ILE   A 106 ? 0.17957 0.21940 0.18447 -0.00312 -0.02235 -0.00647 106 ILE   A CG2 
833  C CD1 . ILE   A 106 ? 0.16584 0.20234 0.17513 0.00166  -0.01636 0.00008  106 ILE   A CD1 
834  N N   . GLN   A 107 ? 0.08803 0.14970 0.10660 0.00201  -0.02597 0.01013  107 GLN   A N   
835  C CA  . GLN   A 107 ? 0.11442 0.17970 0.13807 0.00648  -0.02460 0.01682  107 GLN   A CA  
836  C C   . GLN   A 107 ? 0.10708 0.16209 0.12820 0.00950  -0.01911 0.01641  107 GLN   A C   
837  O O   . GLN   A 107 ? 0.12973 0.17904 0.14367 0.00800  -0.01832 0.01310  107 GLN   A O   
838  C CB  . GLN   A 107 ? 0.13132 0.20425 0.15127 0.00634  -0.02907 0.02111  107 GLN   A CB  
839  C CG  . GLN   A 107 ? 0.12474 0.20998 0.14783 0.00267  -0.03588 0.02262  107 GLN   A CG  
840  C CD  . GLN   A 107 ? 0.15461 0.24864 0.19294 0.00549  -0.03574 0.02929  107 GLN   A CD  
841  O OE1 . GLN   A 107 ? 0.12370 0.21691 0.16854 0.01162  -0.03165 0.03528  107 GLN   A OE1 
842  N NE2 . GLN   A 107 ? 0.11900 0.22037 0.16428 0.00122  -0.03916 0.02825  107 GLN   A NE2 
843  N N   . PRO   A 108 ? 0.11556 0.16807 0.14298 0.01356  -0.01505 0.01957  108 PRO   A N   
844  C CA  . PRO   A 108 ? 0.13197 0.17387 0.15651 0.01550  -0.01072 0.01935  108 PRO   A CA  
845  C C   . PRO   A 108 ? 0.13055 0.17289 0.15065 0.01501  -0.01268 0.02260  108 PRO   A C   
846  O O   . PRO   A 108 ? 0.17164 0.22288 0.19243 0.01557  -0.01636 0.02749  108 PRO   A O   
847  C CB  . PRO   A 108 ? 0.12227 0.16240 0.15542 0.02092  -0.00620 0.02327  108 PRO   A CB  
848  C CG  . PRO   A 108 ? 0.15755 0.21084 0.19982 0.02229  -0.00871 0.02745  108 PRO   A CG  
849  C CD  . PRO   A 108 ? 0.10193 0.16165 0.14036 0.01660  -0.01397 0.02380  108 PRO   A CD  
850  N N   . GLY   A 109 ? 0.10514 0.13933 0.12043 0.01332  -0.01053 0.02032  109 GLY   A N   
851  C CA  . GLY   A 109 ? 0.16213 0.19732 0.17314 0.01223  -0.01125 0.02343  109 GLY   A CA  
852  C C   . GLY   A 109 ? 0.19431 0.23324 0.19856 0.00902  -0.01289 0.01922  109 GLY   A C   
853  O O   . GLY   A 109 ? 0.20463 0.24319 0.20555 0.00791  -0.01150 0.02066  109 GLY   A O   
854  N N   . GLN   A 110 ? 0.14887 0.19097 0.15201 0.00772  -0.01505 0.01445  110 GLN   A N   
855  C CA  . GLN   A 110 ? 0.14880 0.19193 0.14655 0.00561  -0.01542 0.00974  110 GLN   A CA  
856  C C   . GLN   A 110 ? 0.12680 0.16461 0.12643 0.00460  -0.01317 0.00655  110 GLN   A C   
857  O O   . GLN   A 110 ? 0.10940 0.14310 0.11241 0.00437  -0.01247 0.00621  110 GLN   A O   
858  C CB  . GLN   A 110 ? 0.14159 0.18832 0.13780 0.00398  -0.01872 0.00584  110 GLN   A CB  
859  C CG  . GLN   A 110 ? 0.19507 0.24974 0.18865 0.00336  -0.02287 0.00847  110 GLN   A CG  
860  C CD  . GLN   A 110 ? 0.28296 0.33952 0.27376 -0.00034 -0.02652 0.00270  110 GLN   A CD  
861  O OE1 . GLN   A 110 ? 0.14753 0.20657 0.14511 -0.00191 -0.02911 0.00276  110 GLN   A OE1 
862  N NE2 . GLN   A 110 ? 0.32349 0.37806 0.30451 -0.00194 -0.02597 -0.00265 110 GLN   A NE2 
863  N N   . THR   A 111 ? 0.10368 0.14243 0.10080 0.00415  -0.01184 0.00452  111 THR   A N   
864  C CA  . THR   A 111 ? 0.10045 0.13712 0.10125 0.00343  -0.01039 0.00341  111 THR   A CA  
865  C C   . THR   A 111 ? 0.13286 0.16878 0.13449 0.00381  -0.01067 -0.00051 111 THR   A C   
866  O O   . THR   A 111 ? 0.11939 0.15530 0.11745 0.00402  -0.01128 -0.00362 111 THR   A O   
867  C CB  . THR   A 111 ? 0.11870 0.15822 0.12017 0.00337  -0.00759 0.00591  111 THR   A CB  
868  O OG1 . THR   A 111 ? 0.13742 0.18037 0.13342 0.00499  -0.00566 0.00451  111 THR   A OG1 
869  C CG2 . THR   A 111 ? 0.13876 0.17693 0.14100 0.00219  -0.00714 0.01054  111 THR   A CG2 
870  N N   . PHE   A 112 ? 0.10809 0.14314 0.11452 0.00345  -0.01050 0.00000  112 PHE   A N   
871  C CA  . PHE   A 112 ? 0.11623 0.14983 0.12580 0.00455  -0.01010 -0.00183 112 PHE   A CA  
872  C C   . PHE   A 112 ? 0.11777 0.15407 0.13370 0.00463  -0.00998 0.00152  112 PHE   A C   
873  O O   . PHE   A 112 ? 0.13134 0.16977 0.14789 0.00228  -0.01144 0.00407  112 PHE   A O   
874  C CB  . PHE   A 112 ? 0.11267 0.14305 0.12262 0.00338  -0.01224 -0.00303 112 PHE   A CB  
875  C CG  . PHE   A 112 ? 0.14106 0.17170 0.15120 0.00174  -0.01366 -0.00066 112 PHE   A CG  
876  C CD1 . PHE   A 112 ? 0.14129 0.17217 0.14880 0.00140  -0.01375 -0.00029 112 PHE   A CD1 
877  C CD2 . PHE   A 112 ? 0.07859 0.10900 0.09107 0.00092  -0.01441 0.00141  112 PHE   A CD2 
878  C CE1 . PHE   A 112 ? 0.16041 0.18978 0.16711 0.00056  -0.01345 0.00056  112 PHE   A CE1 
879  C CE2 . PHE   A 112 ? 0.10691 0.13716 0.11656 -0.00078 -0.01490 0.00249  112 PHE   A CE2 
880  C CZ  . PHE   A 112 ? 0.11571 0.14470 0.12223 -0.00078 -0.01385 0.00126  112 PHE   A CZ  
881  N N   . SER   A 113 ? 0.10615 0.14209 0.12726 0.00711  -0.00847 0.00160  113 SER   A N   
882  C CA  . SER   A 113 ? 0.10389 0.14457 0.13327 0.00774  -0.00914 0.00645  113 SER   A CA  
883  C C   . SER   A 113 ? 0.09384 0.13270 0.12404 0.00623  -0.01244 0.00874  113 SER   A C   
884  O O   . SER   A 113 ? 0.13551 0.16851 0.16418 0.00658  -0.01218 0.00668  113 SER   A O   
885  C CB  . SER   A 113 ? 0.10578 0.14739 0.14254 0.01271  -0.00469 0.00679  113 SER   A CB  
886  O OG  . SER   A 113 ? 0.11585 0.15938 0.14982 0.01439  -0.00030 0.00432  113 SER   A OG  
887  N N   . VAL   A 114 ? 0.08100 0.12555 0.11339 0.00387  -0.01570 0.01337  114 VAL   A N   
888  C CA  . VAL   A 114 ? 0.11833 0.16312 0.14986 0.00222  -0.01878 0.01684  114 VAL   A CA  
889  C C   . VAL   A 114 ? 0.11918 0.17089 0.16102 0.00429  -0.02026 0.02400  114 VAL   A C   
890  O O   . VAL   A 114 ? 0.09721 0.15731 0.14460 0.00366  -0.02164 0.02710  114 VAL   A O   
891  C CB  . VAL   A 114 ? 0.10446 0.15021 0.12696 -0.00288 -0.02180 0.01599  114 VAL   A CB  
892  C CG1 . VAL   A 114 ? 0.13507 0.18342 0.15494 -0.00483 -0.02485 0.02056  114 VAL   A CG1 
893  C CG2 . VAL   A 114 ? 0.15404 0.19318 0.16909 -0.00341 -0.01954 0.01035  114 VAL   A CG2 
894  N N   . LEU   A 115 ? 0.09414 0.14304 0.14030 0.00671  -0.01999 0.02773  115 LEU   A N   
895  C CA  . LEU   A 115 ? 0.10439 0.16043 0.16143 0.00921  -0.02195 0.03690  115 LEU   A CA  
896  C C   . LEU   A 115 ? 0.10867 0.16942 0.15918 0.00468  -0.02734 0.04233  115 LEU   A C   
897  O O   . LEU   A 115 ? 0.11667 0.17232 0.16439 0.00460  -0.02684 0.04427  115 LEU   A O   
898  C CB  . LEU   A 115 ? 0.07310 0.12158 0.14016 0.01540  -0.01743 0.03852  115 LEU   A CB  
899  C CG  . LEU   A 115 ? 0.08406 0.13922 0.16485 0.01940  -0.01892 0.04990  115 LEU   A CG  
900  C CD1 . LEU   A 115 ? 0.13015 0.19835 0.22198 0.02194  -0.01928 0.05425  115 LEU   A CD1 
901  C CD2 . LEU   A 115 ? 0.09653 0.13922 0.18627 0.02535  -0.01342 0.05031  115 LEU   A CD2 
902  N N   . ALA   A 116 ? 0.10055 0.17089 0.14724 0.00001  -0.03237 0.04426  116 ALA   A N   
903  C CA  . ALA   A 116 ? 0.09834 0.17377 0.13540 -0.00511 -0.03769 0.04838  116 ALA   A CA  
904  C C   . ALA   A 116 ? 0.14418 0.22434 0.18953 -0.00238 -0.03902 0.05884  116 ALA   A C   
905  O O   . ALA   A 116 ? 0.14713 0.23224 0.20523 0.00092  -0.03852 0.06359  116 ALA   A O   
906  C CB  . ALA   A 116 ? 0.13498 0.21596 0.16453 -0.01175 -0.04181 0.04554  116 ALA   A CB  
907  N N   . CYS   A 117 ? 0.09093 0.16921 0.12898 -0.00375 -0.03964 0.06255  117 CYS   A N   
908  C CA  . CYS   A 117 ? 0.10862 0.18915 0.15422 -0.00117 -0.03973 0.07275  117 CYS   A CA  
909  C C   . CYS   A 117 ? 0.14907 0.23485 0.18089 -0.00685 -0.04302 0.07620  117 CYS   A C   
910  O O   . CYS   A 117 ? 0.15060 0.23419 0.16671 -0.01120 -0.04307 0.07061  117 CYS   A O   
911  C CB  . CYS   A 117 ? 0.15645 0.22728 0.21044 0.00406  -0.03546 0.07568  117 CYS   A CB  
912  S SG  . CYS   A 117 ? 0.21413 0.27665 0.28492 0.01176  -0.03013 0.07168  117 CYS   A SG  
913  N N   . TYR   A 118 ? 0.17768 0.27060 0.21568 -0.00635 -0.04516 0.08561  118 TYR   A N   
914  C CA  . TYR   A 118 ? 0.17714 0.27625 0.20365 -0.01097 -0.04816 0.09065  118 TYR   A CA  
915  C C   . TYR   A 118 ? 0.21484 0.31595 0.25416 -0.00674 -0.04718 0.10301  118 TYR   A C   
916  O O   . TYR   A 118 ? 0.18744 0.29088 0.24348 -0.00210 -0.04681 0.10838  118 TYR   A O   
917  C CB  . TYR   A 118 ? 0.18402 0.29300 0.20242 -0.01714 -0.05399 0.08897  118 TYR   A CB  
918  C CG  . TYR   A 118 ? 0.20241 0.30678 0.20911 -0.02138 -0.05422 0.07644  118 TYR   A CG  
919  C CD1 . TYR   A 118 ? 0.19340 0.29685 0.20936 -0.02009 -0.05390 0.07185  118 TYR   A CD1 
920  C CD2 . TYR   A 118 ? 0.20544 0.30548 0.19227 -0.02610 -0.05363 0.06924  118 TYR   A CD2 
921  C CE1 . TYR   A 118 ? 0.17625 0.27444 0.18277 -0.02386 -0.05366 0.06106  118 TYR   A CE1 
922  C CE2 . TYR   A 118 ? 0.20677 0.30068 0.18396 -0.02939 -0.05294 0.05781  118 TYR   A CE2 
923  C CZ  . TYR   A 118 ? 0.23335 0.32624 0.22074 -0.02851 -0.05330 0.05403  118 TYR   A CZ  
924  O OH  . TYR   A 118 ? 0.19147 0.27757 0.17029 -0.03188 -0.05241 0.04344  118 TYR   A OH  
925  N N   . ASN   A 119 ? 0.24913 0.34872 0.28124 -0.00798 -0.04586 0.10755  119 ASN   A N   
926  C CA  . ASN   A 119 ? 0.23103 0.33205 0.27438 -0.00472 -0.04483 0.11997  119 ASN   A CA  
927  C C   . ASN   A 119 ? 0.22729 0.31803 0.29087 0.00267  -0.04004 0.12222  119 ASN   A C   
928  O O   . ASN   A 119 ? 0.20535 0.29780 0.28379 0.00685  -0.03943 0.13150  119 ASN   A O   
929  C CB  . ASN   A 119 ? 0.26410 0.37920 0.30960 -0.00653 -0.05035 0.12857  119 ASN   A CB  
930  C CG  . ASN   A 119 ? 0.27214 0.39568 0.29656 -0.01428 -0.05526 0.12483  119 ASN   A CG  
931  O OD1 . ASN   A 119 ? 0.29684 0.42716 0.31761 -0.01792 -0.05986 0.12089  119 ASN   A OD1 
932  N ND2 . ASN   A 119 ? 0.27603 0.39848 0.28621 -0.01702 -0.05382 0.12570  119 ASN   A ND2 
933  N N   . GLY   A 120 ? 0.17278 0.25232 0.23674 0.00435  -0.03643 0.11336  120 GLY   A N   
934  C CA  . GLY   A 120 ? 0.17893 0.24650 0.25962 0.01095  -0.03159 0.11245  120 GLY   A CA  
935  C C   . GLY   A 120 ? 0.24241 0.31292 0.33501 0.01558  -0.03128 0.11095  120 GLY   A C   
936  O O   . GLY   A 120 ? 0.22175 0.28184 0.32794 0.02182  -0.02620 0.10968  120 GLY   A O   
937  N N   . SER   A 121 ? 0.21709 0.30074 0.30491 0.01245  -0.03595 0.11047  121 SER   A N   
938  C CA  . SER   A 121 ? 0.15007 0.23862 0.25023 0.01636  -0.03527 0.11035  121 SER   A CA  
939  C C   . SER   A 121 ? 0.21892 0.30846 0.31225 0.01405  -0.03599 0.09953  121 SER   A C   
940  O O   . SER   A 121 ? 0.18142 0.27758 0.26072 0.00706  -0.04081 0.09592  121 SER   A O   
941  C CB  . SER   A 121 ? 0.27722 0.38112 0.38128 0.01434  -0.04013 0.12021  121 SER   A CB  
942  O OG  . SER   A 121 ? 0.31790 0.42138 0.43182 0.01779  -0.03880 0.13133  121 SER   A OG  
943  N N   . PRO   A 122 ? 0.20438 0.28704 0.30671 0.01956  -0.03091 0.09381  122 PRO   A N   
944  C CA  . PRO   A 122 ? 0.16240 0.24724 0.25948 0.01743  -0.03126 0.08453  122 PRO   A CA  
945  C C   . PRO   A 122 ? 0.17012 0.26893 0.26633 0.01272  -0.03601 0.08667  122 PRO   A C   
946  O O   . PRO   A 122 ? 0.20263 0.30965 0.31069 0.01506  -0.03629 0.09451  122 PRO   A O   
947  C CB  . PRO   A 122 ? 0.20183 0.27863 0.31171 0.02556  -0.02387 0.08065  122 PRO   A CB  
948  C CG  . PRO   A 122 ? 0.25223 0.31522 0.36632 0.02971  -0.02003 0.08255  122 PRO   A CG  
949  C CD  . PRO   A 122 ? 0.19917 0.26851 0.31401 0.02739  -0.02388 0.09370  122 PRO   A CD  
950  N N   . SER   A 123 ? 0.18941 0.29019 0.27225 0.00591  -0.03953 0.07962  123 SER   A N   
951  C CA  . SER   A 123 ? 0.16899 0.28032 0.24871 -0.00043 -0.04450 0.07973  123 SER   A CA  
952  C C   . SER   A 123 ? 0.16008 0.27236 0.24353 -0.00068 -0.04247 0.07354  123 SER   A C   
953  O O   . SER   A 123 ? 0.14038 0.26239 0.23191 -0.00222 -0.04409 0.07711  123 SER   A O   
954  C CB  . SER   A 123 ? 0.24484 0.35589 0.30526 -0.00888 -0.04968 0.07590  123 SER   A CB  
955  O OG  . SER   A 123 ? 0.35139 0.46977 0.40752 -0.01586 -0.05447 0.07405  123 SER   A OG  
956  N N   . GLY   A 124 ? 0.11447 0.21797 0.19276 0.00041  -0.03908 0.06519  124 GLY   A N   
957  C CA  . GLY   A 124 ? 0.09176 0.19663 0.17267 -0.00042 -0.03698 0.05992  124 GLY   A CA  
958  C C   . GLY   A 124 ? 0.13819 0.23376 0.21569 0.00277  -0.03246 0.05264  124 GLY   A C   
959  O O   . GLY   A 124 ? 0.11323 0.20114 0.18403 0.00375  -0.03229 0.05068  124 GLY   A O   
960  N N   . VAL   A 125 ? 0.09107 0.18851 0.17371 0.00412  -0.02875 0.04939  125 VAL   A N   
961  C CA  . VAL   A 125 ? 0.10554 0.19228 0.18176 0.00659  -0.02324 0.04119  125 VAL   A CA  
962  C C   . VAL   A 125 ? 0.11694 0.20443 0.18738 0.00129  -0.02337 0.03674  125 VAL   A C   
963  O O   . VAL   A 125 ? 0.11463 0.21341 0.19414 -0.00120 -0.02484 0.04103  125 VAL   A O   
964  C CB  . VAL   A 125 ? 0.10506 0.18782 0.19049 0.01544  -0.01510 0.04037  125 VAL   A CB  
965  C CG1 . VAL   A 125 ? 0.18052 0.27551 0.28007 0.01834  -0.01189 0.04495  125 VAL   A CG1 
966  C CG2 . VAL   A 125 ? 0.12435 0.19355 0.19792 0.01641  -0.01010 0.03044  125 VAL   A CG2 
967  N N   . TYR   A 126 ? 0.11579 0.19189 0.17262 -0.00076 -0.02212 0.02924  126 TYR   A N   
968  C CA  . TYR   A 126 ? 0.10802 0.18234 0.15964 -0.00506 -0.02159 0.02571  126 TYR   A CA  
969  C C   . TYR   A 126 ? 0.14420 0.20678 0.18510 -0.00331 -0.01787 0.01899  126 TYR   A C   
970  O O   . TYR   A 126 ? 0.10118 0.15717 0.13720 -0.00088 -0.01719 0.01631  126 TYR   A O   
971  C CB  . TYR   A 126 ? 0.08136 0.15723 0.12767 -0.01335 -0.02799 0.02584  126 TYR   A CB  
972  C CG  . TYR   A 126 ? 0.11356 0.18198 0.14761 -0.01524 -0.03063 0.02257  126 TYR   A CG  
973  C CD1 . TYR   A 126 ? 0.17811 0.23506 0.20085 -0.01593 -0.02831 0.01611  126 TYR   A CD1 
974  C CD2 . TYR   A 126 ? 0.14574 0.21993 0.18041 -0.01591 -0.03497 0.02715  126 TYR   A CD2 
975  C CE1 . TYR   A 126 ? 0.18074 0.23236 0.19338 -0.01701 -0.02928 0.01361  126 TYR   A CE1 
976  C CE2 . TYR   A 126 ? 0.19661 0.26519 0.21936 -0.01758 -0.03637 0.02494  126 TYR   A CE2 
977  C CZ  . TYR   A 126 ? 0.18318 0.24060 0.19506 -0.01809 -0.03307 0.01781  126 TYR   A CZ  
978  O OH  . TYR   A 126 ? 0.19852 0.25156 0.19925 -0.01929 -0.03309 0.01589  126 TYR   A OH  
979  N N   . GLN   A 127 ? 0.11580 0.17691 0.15423 -0.00514 -0.01593 0.01744  127 GLN   A N   
980  C CA  . GLN   A 127 ? 0.16341 0.21637 0.19340 -0.00343 -0.01295 0.01308  127 GLN   A CA  
981  C C   . GLN   A 127 ? 0.16117 0.20676 0.18324 -0.00736 -0.01542 0.01050  127 GLN   A C   
982  O O   . GLN   A 127 ? 0.19036 0.23594 0.21249 -0.01248 -0.01800 0.01121  127 GLN   A O   
983  C CB  . GLN   A 127 ? 0.17862 0.23505 0.21082 -0.00236 -0.00873 0.01467  127 GLN   A CB  
984  C CG  . GLN   A 127 ? 0.21695 0.26842 0.24116 0.00035  -0.00586 0.01170  127 GLN   A CG  
985  C CD  . GLN   A 127 ? 0.17979 0.23065 0.20250 0.00518  -0.00302 0.00848  127 GLN   A CD  
986  O OE1 . GLN   A 127 ? 0.18456 0.23607 0.21272 0.00714  -0.00321 0.00841  127 GLN   A OE1 
987  N NE2 . GLN   A 127 ? 0.19214 0.24116 0.20707 0.00685  -0.00056 0.00593  127 GLN   A NE2 
988  N N   . CYS   A 128 ? 0.12742 0.16679 0.14329 -0.00512 -0.01452 0.00729  128 CYS   A N   
989  C CA  . CYS   A 128 ? 0.15408 0.18631 0.16363 -0.00662 -0.01483 0.00484  128 CYS   A CA  
990  C C   . CYS   A 128 ? 0.15638 0.18592 0.16387 -0.00353 -0.01249 0.00430  128 CYS   A C   
991  O O   . CYS   A 128 ? 0.14196 0.17448 0.14987 -0.00085 -0.01162 0.00425  128 CYS   A O   
992  C CB  . CYS   A 128 ? 0.14948 0.17976 0.15532 -0.00668 -0.01606 0.00316  128 CYS   A CB  
993  S SG  . CYS   A 128 ? 0.29334 0.32624 0.29695 -0.01127 -0.01982 0.00408  128 CYS   A SG  
994  N N   . ALA   A 129 ? 0.17513 0.19875 0.18009 -0.00392 -0.01157 0.00384  129 ALA   A N   
995  C CA  . ALA   A 129 ? 0.15557 0.17822 0.15999 -0.00059 -0.01021 0.00484  129 ALA   A CA  
996  C C   . ALA   A 129 ? 0.14672 0.16590 0.15004 0.00073  -0.00941 0.00293  129 ALA   A C   
997  O O   . ALA   A 129 ? 0.15069 0.16441 0.15128 -0.00111 -0.00850 0.00055  129 ALA   A O   
998  C CB  . ALA   A 129 ? 0.15523 0.17461 0.16062 -0.00053 -0.00857 0.00822  129 ALA   A CB  
999  N N   . MET   A 130 ? 0.13668 0.15976 0.14182 0.00347  -0.00963 0.00389  130 MET   A N   
1000 C CA  . MET   A 130 ? 0.08879 0.11076 0.09583 0.00571  -0.00769 0.00388  130 MET   A CA  
1001 C C   . MET   A 130 ? 0.13145 0.14772 0.14027 0.00822  -0.00477 0.00599  130 MET   A C   
1002 O O   . MET   A 130 ? 0.13907 0.15809 0.15087 0.01023  -0.00551 0.01039  130 MET   A O   
1003 C CB  . MET   A 130 ? 0.12442 0.15428 0.13544 0.00694  -0.00963 0.00544  130 MET   A CB  
1004 C CG  . MET   A 130 ? 0.17251 0.20527 0.18859 0.00895  -0.00759 0.00653  130 MET   A CG  
1005 S SD  . MET   A 130 ? 0.19098 0.21977 0.20359 0.00786  -0.00399 0.00352  130 MET   A SD  
1006 C CE  . MET   A 130 ? 0.08733 0.11965 0.09931 0.00401  -0.00785 0.00288  130 MET   A CE  
1007 N N   . ARG   A 131 ? 0.11971 0.12722 0.12595 0.00799  -0.00130 0.00291  131 ARG   A N   
1008 C CA  . ARG   A 131 ? 0.14945 0.14807 0.15807 0.01086  0.00273  0.00412  131 ARG   A CA  
1009 C C   . ARG   A 131 ? 0.13827 0.14218 0.15520 0.01708  0.00483  0.00891  131 ARG   A C   
1010 O O   . ARG   A 131 ? 0.12777 0.14077 0.14750 0.01813  0.00399  0.00942  131 ARG   A O   
1011 C CB  . ARG   A 131 ? 0.14359 0.13027 0.14564 0.00900  0.00664  -0.00232 131 ARG   A CB  
1012 C CG  . ARG   A 131 ? 0.18451 0.16663 0.17912 0.00171  0.00357  -0.00652 131 ARG   A CG  
1013 C CD  . ARG   A 131 ? 0.15733 0.13971 0.15583 -0.00078 0.00090  -0.00258 131 ARG   A CD  
1014 N NE  . ARG   A 131 ? 0.16989 0.14309 0.17314 0.00215  0.00452  0.00049  131 ARG   A NE  
1015 C CZ  . ARG   A 131 ? 0.18758 0.16039 0.19507 0.00074  0.00351  0.00576  131 ARG   A CZ  
1016 N NH1 . ARG   A 131 ? 0.16192 0.14348 0.16923 -0.00334 -0.00034 0.00749  131 ARG   A NH1 
1017 N NH2 . ARG   A 131 ? 0.20204 0.16599 0.21475 0.00386  0.00702  0.01007  131 ARG   A NH2 
1018 N N   . PRO   A 132 ? 0.12135 0.12056 0.14402 0.02112  0.00734  0.01364  132 PRO   A N   
1019 C CA  . PRO   A 132 ? 0.13730 0.14223 0.17037 0.02795  0.00984  0.01938  132 PRO   A CA  
1020 C C   . PRO   A 132 ? 0.14215 0.14596 0.17694 0.03101  0.01555  0.01556  132 PRO   A C   
1021 O O   . PRO   A 132 ? 0.12562 0.14088 0.17021 0.03517  0.01607  0.02041  132 PRO   A O   
1022 C CB  . PRO   A 132 ? 0.16326 0.15829 0.20148 0.03179  0.01310  0.02451  132 PRO   A CB  
1023 C CG  . PRO   A 132 ? 0.16337 0.15658 0.19529 0.02604  0.00880  0.02515  132 PRO   A CG  
1024 C CD  . PRO   A 132 ? 0.15494 0.14534 0.17705 0.01965  0.00754  0.01598  132 PRO   A CD  
1025 N N   . ASN   A 133 ? 0.13121 0.12331 0.15647 0.02853  0.01966  0.00731  133 ASN   A N   
1026 C CA  . ASN   A 133 ? 0.12161 0.11359 0.14606 0.03134  0.02604  0.00360  133 ASN   A CA  
1027 C C   . ASN   A 133 ? 0.10868 0.11090 0.12817 0.02678  0.02264  0.00168  133 ASN   A C   
1028 O O   . ASN   A 133 ? 0.13452 0.13574 0.14937 0.02734  0.02790  -0.00203 133 ASN   A O   
1029 C CB  . ASN   A 133 ? 0.18385 0.15731 0.19854 0.03128  0.03320  -0.00475 133 ASN   A CB  
1030 C CG  . ASN   A 133 ? 0.15040 0.11648 0.15075 0.02240  0.02866  -0.01159 133 ASN   A CG  
1031 O OD1 . ASN   A 133 ? 0.16512 0.14029 0.16376 0.01734  0.02118  -0.00977 133 ASN   A OD1 
1032 N ND2 . ASN   A 133 ? 0.21182 0.16114 0.20232 0.02040  0.03328  -0.01959 133 ASN   A ND2 
1033 N N   . PHE   A 134 ? 0.12357 0.13462 0.14350 0.02249  0.01475  0.00421  134 PHE   A N   
1034 C CA  . PHE   A 134 ? 0.11249 0.13243 0.13056 0.01863  0.01140  0.00379  134 PHE   A CA  
1035 C C   . PHE   A 134 ? 0.14922 0.16305 0.15494 0.01412  0.01185  -0.00179 134 PHE   A C   
1036 O O   . PHE   A 134 ? 0.16355 0.18291 0.16751 0.01222  0.01178  -0.00152 134 PHE   A O   
1037 C CB  . PHE   A 134 ? 0.10532 0.13565 0.13286 0.02177  0.01454  0.00751  134 PHE   A CB  
1038 C CG  . PHE   A 134 ? 0.09010 0.13168 0.13038 0.02383  0.01081  0.01409  134 PHE   A CG  
1039 C CD1 . PHE   A 134 ? 0.09949 0.14872 0.14093 0.01924  0.00326  0.01550  134 PHE   A CD1 
1040 C CD2 . PHE   A 134 ? 0.13095 0.17559 0.18217 0.03043  0.01481  0.01904  134 PHE   A CD2 
1041 C CE1 . PHE   A 134 ? 0.11915 0.17989 0.17051 0.01985  -0.00141 0.02117  134 PHE   A CE1 
1042 C CE2 . PHE   A 134 ? 0.17142 0.22930 0.23482 0.03180  0.00989  0.02654  134 PHE   A CE2 
1043 C CZ  . PHE   A 134 ? 0.13673 0.20294 0.19899 0.02580  0.00125  0.02720  134 PHE   A CZ  
1044 N N   . THR   A 135 ? 0.16150 0.16464 0.15903 0.01182  0.01193  -0.00605 135 THR   A N   
1045 C CA  . THR   A 135 ? 0.12626 0.12631 0.11254 0.00608  0.00950  -0.01017 135 THR   A CA  
1046 C C   . THR   A 135 ? 0.15776 0.15957 0.14535 0.00233  0.00293  -0.00863 135 THR   A C   
1047 O O   . THR   A 135 ? 0.13532 0.13799 0.12950 0.00406  0.00161  -0.00569 135 THR   A O   
1048 C CB  . THR   A 135 ? 0.13133 0.11858 0.10663 0.00463  0.01398  -0.01699 135 THR   A CB  
1049 O OG1 . THR   A 135 ? 0.18546 0.16284 0.16308 0.00461  0.01413  -0.01810 135 THR   A OG1 
1050 C CG2 . THR   A 135 ? 0.14698 0.13168 0.12146 0.00997  0.02279  -0.01889 135 THR   A CG2 
1051 N N   . ILE   A 136 ? 0.12509 0.12871 0.10665 -0.00251 -0.00083 -0.00979 136 ILE   A N   
1052 C CA  . ILE   A 136 ? 0.15135 0.15730 0.13501 -0.00589 -0.00597 -0.00826 136 ILE   A CA  
1053 C C   . ILE   A 136 ? 0.15197 0.15354 0.12731 -0.01189 -0.00819 -0.01176 136 ILE   A C   
1054 O O   . ILE   A 136 ? 0.16636 0.16682 0.13235 -0.01426 -0.00780 -0.01456 136 ILE   A O   
1055 C CB  . ILE   A 136 ? 0.16255 0.17795 0.15135 -0.00560 -0.00948 -0.00437 136 ILE   A CB  
1056 C CG1 . ILE   A 136 ? 0.15487 0.17375 0.13879 -0.00807 -0.01113 -0.00368 136 ILE   A CG1 
1057 C CG2 . ILE   A 136 ? 0.13378 0.15296 0.12940 -0.00144 -0.00818 -0.00219 136 ILE   A CG2 
1058 C CD1 . ILE   A 136 ? 0.15215 0.17784 0.14241 -0.00778 -0.01440 0.00060  136 ILE   A CD1 
1059 N N   . LYS   A 137 ? 0.17586 0.17553 0.15414 -0.01502 -0.01061 -0.01137 137 LYS   A N   
1060 C CA  . LYS   A 137 ? 0.22634 0.22311 0.19853 -0.02240 -0.01413 -0.01436 137 LYS   A CA  
1061 C C   . LYS   A 137 ? 0.19345 0.20319 0.16988 -0.02483 -0.01996 -0.00953 137 LYS   A C   
1062 O O   . LYS   A 137 ? 0.22428 0.23995 0.20977 -0.02558 -0.02220 -0.00557 137 LYS   A O   
1063 C CB  . LYS   A 137 ? 0.21978 0.20824 0.19549 -0.02504 -0.01343 -0.01528 137 LYS   A CB  
1064 C CG  . LYS   A 137 ? 0.23166 0.20581 0.20481 -0.02149 -0.00696 -0.01913 137 LYS   A CG  
1065 C CD  . LYS   A 137 ? 0.27067 0.23538 0.24902 -0.02404 -0.00606 -0.01834 137 LYS   A CD  
1066 C CE  . LYS   A 137 ? 0.32064 0.26838 0.29680 -0.02048 0.00084  -0.02233 137 LYS   A CE  
1067 N NZ  . LYS   A 137 ? 0.39980 0.33430 0.36287 -0.02570 0.00236  -0.03230 137 LYS   A NZ  
1068 N N   . GLY   A 138 ? 0.19491 0.20975 0.16585 -0.02511 -0.02156 -0.00879 138 GLY   A N   
1069 C CA  . GLY   A 138 ? 0.17950 0.20634 0.15611 -0.02569 -0.02637 -0.00269 138 GLY   A CA  
1070 C C   . GLY   A 138 ? 0.21793 0.25004 0.18895 -0.03327 -0.03279 -0.00218 138 GLY   A C   
1071 O O   . GLY   A 138 ? 0.21997 0.24547 0.18207 -0.03946 -0.03409 -0.00779 138 GLY   A O   
1072 N N   . SER   A 139 ? 0.14866 0.19274 0.12533 -0.03298 -0.03717 0.00492  139 SER   A N   
1073 C CA  . SER   A 139 ? 0.17402 0.22722 0.14625 -0.03989 -0.04472 0.00791  139 SER   A CA  
1074 C C   . SER   A 139 ? 0.17278 0.23195 0.14366 -0.03630 -0.04498 0.01409  139 SER   A C   
1075 O O   . SER   A 139 ? 0.16291 0.22931 0.14713 -0.03138 -0.04527 0.02170  139 SER   A O   
1076 C CB  . SER   A 139 ? 0.19207 0.25413 0.17921 -0.04109 -0.04802 0.01316  139 SER   A CB  
1077 O OG  . SER   A 139 ? 0.19795 0.26664 0.18310 -0.04553 -0.05289 0.01621  139 SER   A OG  
1078 N N   . PHE   A 140 ? 0.19973 0.25508 0.15460 -0.03872 -0.04410 0.01087  140 PHE   A N   
1079 C CA  . PHE   A 140 ? 0.19399 0.25362 0.14558 -0.03576 -0.04307 0.01674  140 PHE   A CA  
1080 C C   . PHE   A 140 ? 0.22807 0.28893 0.16466 -0.04080 -0.04519 0.01568  140 PHE   A C   
1081 O O   . PHE   A 140 ? 0.23898 0.29172 0.16103 -0.04505 -0.04373 0.00655  140 PHE   A O   
1082 C CB  . PHE   A 140 ? 0.19510 0.24686 0.14360 -0.03091 -0.03551 0.01347  140 PHE   A CB  
1083 C CG  . PHE   A 140 ? 0.14464 0.19405 0.10994 -0.02421 -0.03193 0.01517  140 PHE   A CG  
1084 C CD1 . PHE   A 140 ? 0.17430 0.22963 0.15253 -0.02043 -0.03332 0.02336  140 PHE   A CD1 
1085 C CD2 . PHE   A 140 ? 0.18362 0.22428 0.15101 -0.02170 -0.02701 0.00856  140 PHE   A CD2 
1086 C CE1 . PHE   A 140 ? 0.16474 0.21621 0.15522 -0.01513 -0.02976 0.02297  140 PHE   A CE1 
1087 C CE2 . PHE   A 140 ? 0.17390 0.21326 0.15382 -0.01654 -0.02447 0.00969  140 PHE   A CE2 
1088 C CZ  . PHE   A 140 ? 0.12681 0.17109 0.11713 -0.01365 -0.02580 0.01600  140 PHE   A CZ  
1089 N N   . LEU   A 141 ? 0.19194 0.26228 0.13201 -0.04026 -0.04839 0.02482  141 LEU   A N   
1090 C CA  . LEU   A 141 ? 0.25223 0.32568 0.17763 -0.04465 -0.05062 0.02534  141 LEU   A CA  
1091 C C   . LEU   A 141 ? 0.22318 0.29899 0.14450 -0.04110 -0.04705 0.03169  141 LEU   A C   
1092 O O   . LEU   A 141 ? 0.20930 0.28434 0.14047 -0.03578 -0.04349 0.03595  141 LEU   A O   
1093 C CB  . LEU   A 141 ? 0.19861 0.28298 0.13125 -0.04814 -0.05808 0.03190  141 LEU   A CB  
1094 C CG  . LEU   A 141 ? 0.26740 0.35084 0.20777 -0.05147 -0.06107 0.02749  141 LEU   A CG  
1095 C CD1 . LEU   A 141 ? 0.31002 0.40678 0.26375 -0.05305 -0.06737 0.03668  141 LEU   A CD1 
1096 C CD2 . LEU   A 141 ? 0.27037 0.34428 0.19370 -0.05834 -0.06132 0.01555  141 LEU   A CD2 
1097 N N   . ASN   A 142 ? 0.27508 0.35400 0.18181 -0.04443 -0.04806 0.03274  142 ASN   A N   
1098 C CA  . ASN   A 142 ? 0.26808 0.35021 0.17170 -0.04143 -0.04444 0.04027  142 ASN   A CA  
1099 C C   . ASN   A 142 ? 0.25508 0.34478 0.17940 -0.03707 -0.04683 0.05319  142 ASN   A C   
1100 O O   . ASN   A 142 ? 0.23389 0.33034 0.16989 -0.03761 -0.05252 0.05818  142 ASN   A O   
1101 C CB  . ASN   A 142 ? 0.30772 0.39364 0.19280 -0.04572 -0.04586 0.04067  142 ASN   A CB  
1102 C CG  . ASN   A 142 ? 0.43874 0.52626 0.31801 -0.04277 -0.04002 0.04708  142 ASN   A CG  
1103 O OD1 . ASN   A 142 ? 0.43266 0.51610 0.31831 -0.03835 -0.03351 0.04806  142 ASN   A OD1 
1104 N ND2 . ASN   A 142 ? 0.45727 0.55148 0.32486 -0.04553 -0.04230 0.05213  142 ASN   A ND2 
1105 N N   . GLY   A 143 ? 0.23390 0.32185 0.16385 -0.03259 -0.04178 0.05858  143 GLY   A N   
1106 C CA  . GLY   A 143 ? 0.24958 0.34099 0.19944 -0.02789 -0.04265 0.06981  143 GLY   A CA  
1107 C C   . GLY   A 143 ? 0.19952 0.28529 0.16501 -0.02346 -0.04107 0.06779  143 GLY   A C   
1108 O O   . GLY   A 143 ? 0.20150 0.28682 0.18330 -0.01885 -0.04033 0.07570  143 GLY   A O   
1109 N N   . SER   A 144 ? 0.15990 0.24048 0.12077 -0.02463 -0.04027 0.05725  144 SER   A N   
1110 C CA  . SER   A 144 ? 0.17976 0.25593 0.15425 -0.02065 -0.03925 0.05490  144 SER   A CA  
1111 C C   . SER   A 144 ? 0.16039 0.22842 0.13823 -0.01724 -0.03245 0.05284  144 SER   A C   
1112 O O   . SER   A 144 ? 0.16567 0.22755 0.15615 -0.01350 -0.03010 0.04938  144 SER   A O   
1113 C CB  . SER   A 144 ? 0.16759 0.24091 0.13735 -0.02347 -0.04052 0.04438  144 SER   A CB  
1114 O OG  . SER   A 144 ? 0.18177 0.24934 0.13440 -0.02645 -0.03689 0.03580  144 SER   A OG  
1115 N N   . CYS   A 145 ? 0.14868 0.21614 0.11609 -0.01862 -0.02826 0.05371  145 CYS   A N   
1116 C CA  . CYS   A 145 ? 0.16710 0.22772 0.14098 -0.01596 -0.02136 0.05128  145 CYS   A CA  
1117 C C   . CYS   A 145 ? 0.12958 0.18700 0.12185 -0.01256 -0.02143 0.05787  145 CYS   A C   
1118 O O   . CYS   A 145 ? 0.16223 0.22336 0.16049 -0.01173 -0.02471 0.06810  145 CYS   A O   
1119 C CB  . CYS   A 145 ? 0.19791 0.26107 0.16009 -0.01781 -0.01625 0.05364  145 CYS   A CB  
1120 S SG  . CYS   A 145 ? 0.24676 0.30857 0.18731 -0.02057 -0.01316 0.04192  145 CYS   A SG  
1121 N N   . GLY   A 146 ? 0.15486 0.20494 0.15604 -0.01067 -0.01786 0.05194  146 GLY   A N   
1122 C CA  . GLY   A 146 ? 0.14014 0.18408 0.15695 -0.00818 -0.01755 0.05478  146 GLY   A CA  
1123 C C   . GLY   A 146 ? 0.13757 0.17834 0.16201 -0.00512 -0.01978 0.05071  146 GLY   A C   
1124 O O   . GLY   A 146 ? 0.13487 0.16811 0.17051 -0.00283 -0.01831 0.04993  146 GLY   A O   
1125 N N   . SER   A 147 ? 0.11550 0.16150 0.13410 -0.00542 -0.02286 0.04789  147 SER   A N   
1126 C CA  . SER   A 147 ? 0.11407 0.15833 0.13930 -0.00278 -0.02356 0.04304  147 SER   A CA  
1127 C C   . SER   A 147 ? 0.12153 0.15861 0.14674 -0.00234 -0.02013 0.03368  147 SER   A C   
1128 O O   . SER   A 147 ? 0.09440 0.13089 0.11249 -0.00449 -0.01839 0.02977  147 SER   A O   
1129 C CB  . SER   A 147 ? 0.09409 0.14578 0.11263 -0.00502 -0.02738 0.04152  147 SER   A CB  
1130 O OG  . SER   A 147 ? 0.13233 0.19315 0.14977 -0.00660 -0.03213 0.05059  147 SER   A OG  
1131 N N   . VAL   A 148 ? 0.09219 0.12443 0.12543 0.00071  -0.01885 0.03052  148 VAL   A N   
1132 C CA  . VAL   A 148 ? 0.08266 0.10901 0.11524 0.00058  -0.01656 0.02260  148 VAL   A CA  
1133 C C   . VAL   A 148 ? 0.11236 0.14011 0.14289 0.00198  -0.01641 0.01721  148 VAL   A C   
1134 O O   . VAL   A 148 ? 0.10789 0.13973 0.14157 0.00378  -0.01715 0.01945  148 VAL   A O   
1135 C CB  . VAL   A 148 ? 0.09545 0.11288 0.13604 0.00163  -0.01460 0.02167  148 VAL   A CB  
1136 C CG1 . VAL   A 148 ? 0.09566 0.11138 0.13905 -0.00098 -0.01436 0.02745  148 VAL   A CG1 
1137 C CG2 . VAL   A 148 ? 0.11002 0.12438 0.15889 0.00618  -0.01339 0.02386  148 VAL   A CG2 
1138 N N   . GLY   A 149 ? 0.11566 0.14140 0.14195 0.00096  -0.01549 0.01125  149 GLY   A N   
1139 C CA  . GLY   A 149 ? 0.08460 0.11086 0.10865 0.00217  -0.01476 0.00671  149 GLY   A CA  
1140 C C   . GLY   A 149 ? 0.09661 0.11724 0.12184 0.00303  -0.01322 0.00183  149 GLY   A C   
1141 O O   . GLY   A 149 ? 0.08781 0.10447 0.11444 0.00111  -0.01362 0.00073  149 GLY   A O   
1142 N N   . PHE   A 150 ? 0.09112 0.11166 0.11518 0.00526  -0.01135 -0.00131 150 PHE   A N   
1143 C CA  . PHE   A 150 ? 0.09112 0.10513 0.11404 0.00606  -0.00932 -0.00705 150 PHE   A CA  
1144 C C   . PHE   A 150 ? 0.13169 0.14822 0.14932 0.00799  -0.00684 -0.01043 150 PHE   A C   
1145 O O   . PHE   A 150 ? 0.11612 0.13894 0.13498 0.00944  -0.00597 -0.00703 150 PHE   A O   
1146 C CB  . PHE   A 150 ? 0.12730 0.13438 0.15811 0.00886  -0.00676 -0.00600 150 PHE   A CB  
1147 C CG  . PHE   A 150 ? 0.12003 0.13145 0.15726 0.01367  -0.00406 -0.00183 150 PHE   A CG  
1148 C CD1 . PHE   A 150 ? 0.09874 0.11744 0.14170 0.01378  -0.00661 0.00636  150 PHE   A CD1 
1149 C CD2 . PHE   A 150 ? 0.10532 0.11501 0.14284 0.01783  0.00106  -0.00576 150 PHE   A CD2 
1150 C CE1 . PHE   A 150 ? 0.11719 0.14296 0.16839 0.01750  -0.00530 0.01157  150 PHE   A CE1 
1151 C CE2 . PHE   A 150 ? 0.12348 0.13990 0.17006 0.02259  0.00397  -0.00052 150 PHE   A CE2 
1152 C CZ  . PHE   A 150 ? 0.14005 0.16520 0.19464 0.02220  0.00020  0.00860  150 PHE   A CZ  
1153 N N   . ASN   A 151 ? 0.13001 0.14157 0.14151 0.00739  -0.00566 -0.01708 151 ASN   A N   
1154 C CA  . ASN   A 151 ? 0.17071 0.18335 0.17539 0.00962  -0.00184 -0.02104 151 ASN   A CA  
1155 C C   . ASN   A 151 ? 0.16747 0.16962 0.17132 0.01171  0.00259  -0.02792 151 ASN   A C   
1156 O O   . ASN   A 151 ? 0.16726 0.16066 0.17433 0.00979  0.00125  -0.03026 151 ASN   A O   
1157 C CB  . ASN   A 151 ? 0.16025 0.17718 0.15431 0.00630  -0.00486 -0.02313 151 ASN   A CB  
1158 C CG  . ASN   A 151 ? 0.18051 0.20579 0.17577 0.00582  -0.00704 -0.01655 151 ASN   A CG  
1159 O OD1 . ASN   A 151 ? 0.17386 0.20100 0.17054 0.00342  -0.01101 -0.01414 151 ASN   A OD1 
1160 N ND2 . ASN   A 151 ? 0.18315 0.21316 0.17773 0.00800  -0.00383 -0.01384 151 ASN   A ND2 
1161 N N   . ILE   A 152 ? 0.15969 0.16186 0.15971 0.01574  0.00877  -0.03115 152 ILE   A N   
1162 C CA  . ILE   A 152 ? 0.21349 0.20372 0.21116 0.01859  0.01478  -0.03932 152 ILE   A CA  
1163 C C   . ILE   A 152 ? 0.31892 0.30889 0.29936 0.01720  0.01719  -0.04755 152 ILE   A C   
1164 O O   . ILE   A 152 ? 0.28000 0.28047 0.25562 0.01855  0.01904  -0.04433 152 ILE   A O   
1165 C CB  . ILE   A 152 ? 0.22434 0.21427 0.23482 0.02649  0.02222  -0.03554 152 ILE   A CB  
1166 C CG1 . ILE   A 152 ? 0.16950 0.16064 0.19570 0.02725  0.01863  -0.02643 152 ILE   A CG1 
1167 C CG2 . ILE   A 152 ? 0.26863 0.24381 0.27602 0.03044  0.03015  -0.04523 152 ILE   A CG2 
1168 C CD1 . ILE   A 152 ? 0.24616 0.23666 0.28776 0.03530  0.02504  -0.02151 152 ILE   A CD1 
1169 N N   . ASP   A 153 ? 0.35548 0.33356 0.32605 0.01366  0.01677  -0.05786 153 ASP   A N   
1170 C CA  . ASP   A 153 ? 0.43423 0.41144 0.38490 0.01072  0.01771  -0.06700 153 ASP   A CA  
1171 C C   . ASP   A 153 ? 0.48711 0.44719 0.43224 0.01331  0.02570  -0.07901 153 ASP   A C   
1172 O O   . ASP   A 153 ? 0.46303 0.40896 0.41045 0.00968  0.02353  -0.08500 153 ASP   A O   
1173 C CB  . ASP   A 153 ? 0.43737 0.41772 0.37947 0.00163  0.00731  -0.06865 153 ASP   A CB  
1174 C CG  . ASP   A 153 ? 0.59661 0.58314 0.51809 -0.00172 0.00598  -0.07354 153 ASP   A CG  
1175 O OD1 . ASP   A 153 ? 0.58839 0.57941 0.50250 0.00318  0.01317  -0.07331 153 ASP   A OD1 
1176 O OD2 . ASP   A 153 ? 0.64916 0.63764 0.56226 -0.00954 -0.00249 -0.07659 153 ASP   A OD2 
1177 N N   . TYR   A 154 ? 0.52121 0.48208 0.45951 0.01955  0.03564  -0.08240 154 TYR   A N   
1178 C CA  . TYR   A 154 ? 0.60108 0.54657 0.54009 0.02614  0.04703  -0.09123 154 TYR   A CA  
1179 C C   . TYR   A 154 ? 0.58676 0.52325 0.54860 0.03056  0.04832  -0.08598 154 TYR   A C   
1180 O O   . TYR   A 154 ? 0.59195 0.53863 0.57126 0.03690  0.05061  -0.07443 154 TYR   A O   
1181 C CB  . TYR   A 154 ? 0.61346 0.54285 0.53140 0.02089  0.04752  -0.10712 154 TYR   A CB  
1182 C CG  . TYR   A 154 ? 0.74088 0.65712 0.65959 0.02980  0.05823  -0.11229 154 TYR   A CG  
1183 C CD1 . TYR   A 154 ? 0.72867 0.65469 0.65302 0.03986  0.06878  -0.10756 154 TYR   A CD1 
1184 C CD2 . TYR   A 154 ? 0.72640 0.62212 0.64279 0.02820  0.05768  -0.12121 154 TYR   A CD2 
1185 C CE1 . TYR   A 154 ? 0.78864 0.70592 0.71649 0.04845  0.07836  -0.11189 154 TYR   A CE1 
1186 C CE2 . TYR   A 154 ? 0.75777 0.64229 0.67634 0.03692  0.06765  -0.12624 154 TYR   A CE2 
1187 C CZ  . TYR   A 154 ? 0.82333 0.71932 0.74787 0.04729  0.07802  -0.12160 154 TYR   A CZ  
1188 O OH  . TYR   A 154 ? 0.83182 0.71868 0.76021 0.05617  0.08812  -0.12636 154 TYR   A OH  
1189 N N   . ASP   A 155 ? 0.53598 0.45393 0.49817 0.02676  0.04651  -0.09361 155 ASP   A N   
1190 C CA  . ASP   A 155 ? 0.52293 0.43043 0.50616 0.03111  0.04845  -0.08816 155 ASP   A CA  
1191 C C   . ASP   A 155 ? 0.44716 0.35722 0.43935 0.02363  0.03704  -0.08045 155 ASP   A C   
1192 O O   . ASP   A 155 ? 0.37280 0.27473 0.38142 0.02590  0.03744  -0.07462 155 ASP   A O   
1193 C CB  . ASP   A 155 ? 0.58186 0.46585 0.56150 0.03295  0.05466  -0.09902 155 ASP   A CB  
1194 C CG  . ASP   A 155 ? 0.60294 0.47676 0.56237 0.02182  0.04740  -0.11080 155 ASP   A CG  
1195 O OD1 . ASP   A 155 ? 0.60288 0.48866 0.54954 0.01399  0.04001  -0.11233 155 ASP   A OD1 
1196 O OD2 . ASP   A 155 ? 0.65431 0.50933 0.61158 0.02076  0.04836  -0.11759 155 ASP   A OD2 
1197 N N   . CYS   A 156 ? 0.40627 0.32759 0.38850 0.01519  0.02754  -0.07968 156 CYS   A N   
1198 C CA  . CYS   A 156 ? 0.33749 0.25997 0.32582 0.00729  0.01783  -0.07495 156 CYS   A CA  
1199 C C   . CYS   A 156 ? 0.27099 0.21260 0.26822 0.00837  0.01286  -0.06112 156 CYS   A C   
1200 O O   . CYS   A 156 ? 0.25858 0.21419 0.24883 0.00905  0.01173  -0.05858 156 CYS   A O   
1201 C CB  . CYS   A 156 ? 0.34918 0.27058 0.32169 -0.00323 0.01063  -0.08411 156 CYS   A CB  
1202 S SG  . CYS   A 156 ? 0.31143 0.23994 0.29312 -0.01273 -0.00085 -0.07666 156 CYS   A SG  
1203 N N   . VAL   A 157 ? 0.22099 0.16228 0.23287 0.00836  0.01034  -0.05224 157 VAL   A N   
1204 C CA  . VAL   A 157 ? 0.14984 0.10704 0.16857 0.00883  0.00599  -0.04041 157 VAL   A CA  
1205 C C   . VAL   A 157 ? 0.18885 0.15211 0.20380 0.00072  -0.00188 -0.03956 157 VAL   A C   
1206 O O   . VAL   A 157 ? 0.15501 0.11104 0.17466 -0.00423 -0.00454 -0.03999 157 VAL   A O   
1207 C CB  . VAL   A 157 ? 0.16018 0.11591 0.19483 0.01302  0.00736  -0.03045 157 VAL   A CB  
1208 C CG1 . VAL   A 157 ? 0.12235 0.09377 0.16022 0.01218  0.00254  -0.02016 157 VAL   A CG1 
1209 C CG2 . VAL   A 157 ? 0.18011 0.13143 0.22221 0.02207  0.01538  -0.02975 157 VAL   A CG2 
1210 N N   . SER   A 158 ? 0.18525 0.16203 0.19366 -0.00040 -0.00515 -0.03731 158 SER   A N   
1211 C CA  . SER   A 158 ? 0.12942 0.11433 0.13713 -0.00636 -0.01177 -0.03457 158 SER   A CA  
1212 C C   . SER   A 158 ? 0.12348 0.11681 0.13941 -0.00434 -0.01259 -0.02455 158 SER   A C   
1213 O O   . SER   A 158 ? 0.13360 0.13512 0.14752 -0.00130 -0.01196 -0.02097 158 SER   A O   
1214 C CB  . SER   A 158 ? 0.14956 0.14328 0.14579 -0.00834 -0.01464 -0.03745 158 SER   A CB  
1215 O OG  . SER   A 158 ? 0.21001 0.19657 0.19550 -0.01168 -0.01481 -0.04749 158 SER   A OG  
1216 N N   . PHE   A 159 ? 0.11775 0.10845 0.14217 -0.00655 -0.01374 -0.02018 159 PHE   A N   
1217 C CA  . PHE   A 159 ? 0.10555 0.10390 0.13497 -0.00538 -0.01429 -0.01143 159 PHE   A CA  
1218 C C   . PHE   A 159 ? 0.10326 0.11139 0.13003 -0.00827 -0.01738 -0.01009 159 PHE   A C   
1219 O O   . PHE   A 159 ? 0.11068 0.11969 0.13858 -0.01290 -0.02013 -0.01216 159 PHE   A O   
1220 C CB  . PHE   A 159 ? 0.10764 0.10075 0.14607 -0.00680 -0.01381 -0.00613 159 PHE   A CB  
1221 C CG  . PHE   A 159 ? 0.10268 0.08620 0.14677 -0.00267 -0.01037 -0.00501 159 PHE   A CG  
1222 C CD1 . PHE   A 159 ? 0.10405 0.09253 0.15091 0.00254  -0.00892 0.00126  159 PHE   A CD1 
1223 C CD2 . PHE   A 159 ? 0.14520 0.11465 0.19274 -0.00411 -0.00865 -0.01009 159 PHE   A CD2 
1224 C CE1 . PHE   A 159 ? 0.10511 0.08678 0.16001 0.00737  -0.00565 0.00403  159 PHE   A CE1 
1225 C CE2 . PHE   A 159 ? 0.12700 0.08644 0.18159 0.00106  -0.00432 -0.00858 159 PHE   A CE2 
1226 C CZ  . PHE   A 159 ? 0.16720 0.13378 0.22647 0.00745  -0.00270 -0.00070 159 PHE   A CZ  
1227 N N   . CYS   A 160 ? 0.10000 0.11539 0.12428 -0.00569 -0.01692 -0.00654 160 CYS   A N   
1228 C CA  . CYS   A 160 ? 0.08860 0.11184 0.11181 -0.00693 -0.01849 -0.00492 160 CYS   A CA  
1229 C C   . CYS   A 160 ? 0.08455 0.11180 0.10935 -0.00599 -0.01690 0.00039  160 CYS   A C   
1230 O O   . CYS   A 160 ? 0.11862 0.15156 0.14449 -0.00632 -0.01681 0.00195  160 CYS   A O   
1231 C CB  . CYS   A 160 ? 0.06676 0.09375 0.08366 -0.00500 -0.01892 -0.00682 160 CYS   A CB  
1232 S SG  . CYS   A 160 ? 0.14555 0.17149 0.15922 -0.00108 -0.01615 -0.00570 160 CYS   A SG  
1233 N N   . TYR   A 161 ? 0.07482 0.09995 0.09968 -0.00476 -0.01553 0.00342  161 TYR   A N   
1234 C CA  . TYR   A 161 ? 0.06855 0.09745 0.09044 -0.00431 -0.01412 0.00700  161 TYR   A CA  
1235 C C   . TYR   A 161 ? 0.09638 0.12428 0.11989 -0.00489 -0.01377 0.01204  161 TYR   A C   
1236 O O   . TYR   A 161 ? 0.10657 0.13123 0.13298 -0.00375 -0.01458 0.01327  161 TYR   A O   
1237 C CB  . TYR   A 161 ? 0.08303 0.11275 0.09894 -0.00262 -0.01404 0.00554  161 TYR   A CB  
1238 C CG  . TYR   A 161 ? 0.06173 0.09301 0.07191 -0.00311 -0.01274 0.00717  161 TYR   A CG  
1239 C CD1 . TYR   A 161 ? 0.10354 0.13584 0.11132 -0.00258 -0.01007 0.00609  161 TYR   A CD1 
1240 C CD2 . TYR   A 161 ? 0.06419 0.09617 0.07101 -0.00407 -0.01416 0.00957  161 TYR   A CD2 
1241 C CE1 . TYR   A 161 ? 0.10078 0.13237 0.10100 -0.00303 -0.00783 0.00568  161 TYR   A CE1 
1242 C CE2 . TYR   A 161 ? 0.08176 0.11468 0.08014 -0.00575 -0.01353 0.00964  161 TYR   A CE2 
1243 C CZ  . TYR   A 161 ? 0.07252 0.10404 0.06672 -0.00519 -0.00979 0.00684  161 TYR   A CZ  
1244 O OH  . TYR   A 161 ? 0.11421 0.14449 0.09808 -0.00673 -0.00803 0.00509  161 TYR   A OH  
1245 N N   . MET   A 162 ? 0.08132 0.11266 0.10336 -0.00616 -0.01202 0.01572  162 MET   A N   
1246 C CA  . MET   A 162 ? 0.07197 0.10448 0.09234 -0.00682 -0.01181 0.02189  162 MET   A CA  
1247 C C   . MET   A 162 ? 0.09950 0.13610 0.10921 -0.00711 -0.01025 0.02176  162 MET   A C   
1248 O O   . MET   A 162 ? 0.07522 0.11366 0.08260 -0.00692 -0.00691 0.01962  162 MET   A O   
1249 C CB  . MET   A 162 ? 0.10252 0.13477 0.12983 -0.00898 -0.01033 0.02739  162 MET   A CB  
1250 C CG  . MET   A 162 ? 0.11198 0.14551 0.13790 -0.00929 -0.01057 0.03568  162 MET   A CG  
1251 S SD  . MET   A 162 ? 0.16773 0.19814 0.20467 -0.01177 -0.00911 0.04446  162 MET   A SD  
1252 C CE  . MET   A 162 ? 0.20329 0.22263 0.25031 -0.00954 -0.01144 0.04291  162 MET   A CE  
1253 N N   . HIS   A 163 ? 0.11673 0.15490 0.12040 -0.00764 -0.01256 0.02410  163 HIS   A N   
1254 C CA  . HIS   A 163 ? 0.14467 0.18507 0.13547 -0.00920 -0.01183 0.02227  163 HIS   A CA  
1255 C C   . HIS   A 163 ? 0.11068 0.15478 0.09456 -0.01069 -0.00858 0.02672  163 HIS   A C   
1256 O O   . HIS   A 163 ? 0.11670 0.16376 0.10323 -0.01156 -0.00975 0.03462  163 HIS   A O   
1257 C CB  . HIS   A 163 ? 0.15588 0.19859 0.14239 -0.01082 -0.01682 0.02346  163 HIS   A CB  
1258 C CG  . HIS   A 163 ? 0.11332 0.15604 0.08543 -0.01383 -0.01681 0.01895  163 HIS   A CG  
1259 N ND1 . HIS   A 163 ? 0.13449 0.17150 0.10230 -0.01321 -0.01315 0.01124  163 HIS   A ND1 
1260 C CD2 . HIS   A 163 ? 0.17072 0.21753 0.13081 -0.01772 -0.01963 0.02077  163 HIS   A CD2 
1261 C CE1 . HIS   A 163 ? 0.14541 0.18080 0.09920 -0.01660 -0.01319 0.00725  163 HIS   A CE1 
1262 N NE2 . HIS   A 163 ? 0.14986 0.19163 0.09762 -0.01995 -0.01751 0.01245  163 HIS   A NE2 
1263 N N   . HIS   A 164 ? 0.16353 0.20719 0.13782 -0.01068 -0.00388 0.02198  164 HIS   A N   
1264 C CA  . HIS   A 164 ? 0.11869 0.16623 0.08383 -0.01165 0.00115  0.02494  164 HIS   A CA  
1265 C C   . HIS   A 164 ? 0.16873 0.21516 0.11451 -0.01375 0.00246  0.01992  164 HIS   A C   
1266 O O   . HIS   A 164 ? 0.16053 0.21161 0.09489 -0.01603 0.00368  0.02411  164 HIS   A O   
1267 C CB  . HIS   A 164 ? 0.10949 0.15835 0.08203 -0.00904 0.00829  0.02421  164 HIS   A CB  
1268 C CG  . HIS   A 164 ? 0.11385 0.16527 0.10299 -0.00924 0.00728  0.03024  164 HIS   A CG  
1269 N ND1 . HIS   A 164 ? 0.12253 0.17961 0.11659 -0.01038 0.01157  0.03732  164 HIS   A ND1 
1270 C CD2 . HIS   A 164 ? 0.12516 0.17351 0.12657 -0.00910 0.00278  0.02952  164 HIS   A CD2 
1271 C CE1 . HIS   A 164 ? 0.11941 0.17590 0.12891 -0.01165 0.00898  0.04053  164 HIS   A CE1 
1272 N NE2 . HIS   A 164 ? 0.12313 0.17392 0.13619 -0.01078 0.00375  0.03518  164 HIS   A NE2 
1273 N N   . MET   A 165 ? 0.16077 0.20054 0.10151 -0.01357 0.00245  0.01104  165 MET   A N   
1274 C CA  . MET   A 165 ? 0.17676 0.21308 0.09777 -0.01600 0.00557  0.00464  165 MET   A CA  
1275 C C   . MET   A 165 ? 0.17291 0.19991 0.09013 -0.01727 0.00361  -0.00455 165 MET   A C   
1276 O O   . MET   A 165 ? 0.16894 0.19278 0.09929 -0.01490 0.00201  -0.00555 165 MET   A O   
1277 C CB  . MET   A 165 ? 0.18575 0.22193 0.10293 -0.01244 0.01634  0.00297  165 MET   A CB  
1278 C CG  . MET   A 165 ? 0.19895 0.23057 0.12959 -0.00694 0.02138  -0.00085 165 MET   A CG  
1279 S SD  . MET   A 165 ? 0.33013 0.36515 0.26010 -0.00193 0.03470  -0.00064 165 MET   A SD  
1280 C CE  . MET   A 165 ? 0.27475 0.30682 0.22398 0.00451  0.03778  -0.00278 165 MET   A CE  
1281 N N   . GLU   A 166 ? 0.21555 0.23776 0.11367 -0.02168 0.00383  -0.01130 166 GLU   A N   
1282 C CA  . GLU   A 166 ? 0.21111 0.22233 0.10425 -0.02425 0.00257  -0.02063 166 GLU   A CA  
1283 C C   . GLU   A 166 ? 0.24660 0.24634 0.12813 -0.02165 0.01305  -0.03018 166 GLU   A C   
1284 O O   . GLU   A 166 ? 0.26964 0.27096 0.13710 -0.02151 0.01898  -0.03151 166 GLU   A O   
1285 C CB  . GLU   A 166 ? 0.20389 0.21769 0.08556 -0.03296 -0.00700 -0.02159 166 GLU   A CB  
1286 C CG  . GLU   A 166 ? 0.29549 0.29624 0.16821 -0.03781 -0.00765 -0.03259 166 GLU   A CG  
1287 C CD  . GLU   A 166 ? 0.28927 0.29521 0.16030 -0.04570 -0.01856 -0.03107 166 GLU   A CD  
1288 O OE1 . GLU   A 166 ? 0.27291 0.29070 0.15753 -0.04602 -0.02569 -0.02180 166 GLU   A OE1 
1289 O OE2 . GLU   A 166 ? 0.33553 0.33384 0.19530 -0.05024 -0.01933 -0.03847 166 GLU   A OE2 
1290 N N   . LEU   A 167 ? 0.26009 0.24867 0.14890 -0.01859 0.01637  -0.03574 167 LEU   A N   
1291 C CA  . LEU   A 167 ? 0.27201 0.24758 0.15370 -0.01444 0.02732  -0.04451 167 LEU   A CA  
1292 C C   . LEU   A 167 ? 0.29788 0.25927 0.16015 -0.02162 0.02612  -0.05600 167 LEU   A C   
1293 O O   . LEU   A 167 ? 0.34834 0.31120 0.20757 -0.02966 0.01585  -0.05603 167 LEU   A O   
1294 C CB  . LEU   A 167 ? 0.27143 0.24269 0.17308 -0.00697 0.03117  -0.04262 167 LEU   A CB  
1295 C CG  . LEU   A 167 ? 0.20929 0.19409 0.12967 -0.00068 0.03238  -0.03255 167 LEU   A CG  
1296 C CD1 . LEU   A 167 ? 0.24881 0.23066 0.18687 0.00473  0.03307  -0.03026 167 LEU   A CD1 
1297 C CD2 . LEU   A 167 ? 0.25299 0.24211 0.17024 0.00419  0.04276  -0.03198 167 LEU   A CD2 
1298 N N   . PRO   A 168 ? 0.32426 0.27147 0.17384 -0.01913 0.03667  -0.06617 168 PRO   A N   
1299 C CA  . PRO   A 168 ? 0.34114 0.27765 0.17730 -0.02516 0.03314  -0.07503 168 PRO   A CA  
1300 C C   . PRO   A 168 ? 0.36776 0.29342 0.20994 -0.03082 0.02645  -0.07856 168 PRO   A C   
1301 O O   . PRO   A 168 ? 0.39732 0.31920 0.23014 -0.03866 0.01981  -0.08341 168 PRO   A O   
1302 C CB  . PRO   A 168 ? 0.33901 0.26423 0.16953 -0.01778 0.04623  -0.08258 168 PRO   A CB  
1303 C CG  . PRO   A 168 ? 0.37299 0.31013 0.21072 -0.00942 0.05473  -0.07538 168 PRO   A CG  
1304 C CD  . PRO   A 168 ? 0.32782 0.27329 0.18156 -0.00895 0.05049  -0.06659 168 PRO   A CD  
1305 N N   . THR   A 169 ? 0.27527 0.19617 0.13286 -0.02739 0.02807  -0.07591 169 THR   A N   
1306 C CA  . THR   A 169 ? 0.31576 0.22812 0.17985 -0.03356 0.02130  -0.07748 169 THR   A CA  
1307 C C   . THR   A 169 ? 0.30806 0.23676 0.17794 -0.04087 0.00817  -0.06952 169 THR   A C   
1308 O O   . THR   A 169 ? 0.34035 0.26616 0.21882 -0.04592 0.00221  -0.06846 169 THR   A O   
1309 C CB  . THR   A 169 ? 0.29256 0.19678 0.17621 -0.02538 0.02687  -0.07394 169 THR   A CB  
1310 O OG1 . THR   A 169 ? 0.29877 0.21940 0.19837 -0.01668 0.02793  -0.06287 169 THR   A OG1 
1311 C CG2 . THR   A 169 ? 0.31236 0.19572 0.19127 -0.01960 0.03933  -0.08300 169 THR   A CG2 
1312 N N   . GLY   A 170 ? 0.28876 0.23512 0.15657 -0.04084 0.00407  -0.06262 170 GLY   A N   
1313 C CA  . GLY   A 170 ? 0.26613 0.22859 0.14278 -0.04564 -0.00730 -0.05370 170 GLY   A CA  
1314 C C   . GLY   A 170 ? 0.29639 0.26866 0.19572 -0.03856 -0.00812 -0.04330 170 GLY   A C   
1315 O O   . GLY   A 170 ? 0.27507 0.25936 0.18359 -0.04139 -0.01613 -0.03622 170 GLY   A O   
1316 N N   . VAL   A 171 ? 0.23818 0.20637 0.14680 -0.02947 -0.00005 -0.04213 171 VAL   A N   
1317 C CA  . VAL   A 171 ? 0.18571 0.16356 0.11287 -0.02339 -0.00102 -0.03317 171 VAL   A CA  
1318 C C   . VAL   A 171 ? 0.18539 0.17450 0.11388 -0.01928 0.00059  -0.02770 171 VAL   A C   
1319 O O   . VAL   A 171 ? 0.21528 0.20488 0.13104 -0.02023 0.00360  -0.03005 171 VAL   A O   
1320 C CB  . VAL   A 171 ? 0.21475 0.18410 0.15275 -0.01690 0.00494  -0.03332 171 VAL   A CB  
1321 C CG1 . VAL   A 171 ? 0.21943 0.17643 0.15739 -0.02146 0.00360  -0.03743 171 VAL   A CG1 
1322 C CG2 . VAL   A 171 ? 0.21382 0.17696 0.14845 -0.01045 0.01468  -0.03671 171 VAL   A CG2 
1323 N N   . HIS   A 172 ? 0.15201 0.14972 0.09517 -0.01518 -0.00107 -0.02054 172 HIS   A N   
1324 C CA  . HIS   A 172 ? 0.14553 0.15398 0.09157 -0.01372 -0.00203 -0.01435 172 HIS   A CA  
1325 C C   . HIS   A 172 ? 0.13933 0.15050 0.09701 -0.00739 0.00262  -0.01119 172 HIS   A C   
1326 O O   . HIS   A 172 ? 0.12069 0.12937 0.08748 -0.00422 0.00346  -0.01122 172 HIS   A O   
1327 C CB  . HIS   A 172 ? 0.17597 0.19255 0.12825 -0.01658 -0.00990 -0.00879 172 HIS   A CB  
1328 C CG  . HIS   A 172 ? 0.17384 0.19131 0.11647 -0.02347 -0.01555 -0.01036 172 HIS   A CG  
1329 N ND1 . HIS   A 172 ? 0.16143 0.17749 0.10779 -0.02715 -0.01995 -0.01167 172 HIS   A ND1 
1330 C CD2 . HIS   A 172 ? 0.18657 0.20713 0.11551 -0.02815 -0.01783 -0.01063 172 HIS   A CD2 
1331 C CE1 . HIS   A 172 ? 0.20392 0.22279 0.14084 -0.03425 -0.02548 -0.01268 172 HIS   A CE1 
1332 N NE2 . HIS   A 172 ? 0.16693 0.18856 0.09205 -0.03502 -0.02465 -0.01223 172 HIS   A NE2 
1333 N N   . ALA   A 173 ? 0.14588 0.16326 0.10337 -0.00621 0.00521  -0.00762 173 ALA   A N   
1334 C CA  . ALA   A 173 ? 0.10733 0.12929 0.07650 -0.00161 0.00919  -0.00414 173 ALA   A CA  
1335 C C   . ALA   A 173 ? 0.12476 0.15500 0.10007 -0.00303 0.00626  0.00259  173 ALA   A C   
1336 O O   . ALA   A 173 ? 0.11564 0.14837 0.08355 -0.00611 0.00447  0.00521  173 ALA   A O   
1337 C CB  . ALA   A 173 ? 0.14865 0.16883 0.11357 0.00185  0.01833  -0.00665 173 ALA   A CB  
1338 N N   . GLY   A 174 ? 0.10200 0.13612 0.09070 -0.00126 0.00530  0.00566  174 GLY   A N   
1339 C CA  . GLY   A 174 ? 0.09573 0.13496 0.09159 -0.00305 0.00300  0.01131  174 GLY   A CA  
1340 C C   . GLY   A 174 ? 0.09085 0.13415 0.10009 -0.00200 0.00305  0.01309  174 GLY   A C   
1341 O O   . GLY   A 174 ? 0.08577 0.13078 0.09926 0.00081  0.00561  0.01162  174 GLY   A O   
1342 N N   . THR   A 175 ? 0.08788 0.13250 0.10443 -0.00451 -0.00027 0.01646  175 THR   A N   
1343 C CA  . THR   A 175 ? 0.07282 0.12176 0.10155 -0.00568 -0.00124 0.01809  175 THR   A CA  
1344 C C   . THR   A 175 ? 0.07928 0.12396 0.11130 -0.00718 -0.00690 0.01527  175 THR   A C   
1345 O O   . THR   A 175 ? 0.08198 0.12096 0.10905 -0.00681 -0.00903 0.01350  175 THR   A O   
1346 C CB  . THR   A 175 ? 0.09821 0.15127 0.13336 -0.00874 0.00079  0.02427  175 THR   A CB  
1347 O OG1 . THR   A 175 ? 0.09127 0.13849 0.12527 -0.01096 -0.00219 0.02644  175 THR   A OG1 
1348 C CG2 . THR   A 175 ? 0.08641 0.14393 0.11561 -0.00712 0.00751  0.02708  175 THR   A CG2 
1349 N N   . ASP   A 176 ? 0.10144 0.14981 0.14209 -0.00920 -0.00914 0.01506  176 ASP   A N   
1350 C CA  . ASP   A 176 ? 0.07603 0.11922 0.11862 -0.01204 -0.01377 0.01190  176 ASP   A CA  
1351 C C   . ASP   A 176 ? 0.07935 0.11816 0.12702 -0.01554 -0.01352 0.01515  176 ASP   A C   
1352 O O   . ASP   A 176 ? 0.08762 0.12915 0.13665 -0.01575 -0.01017 0.02074  176 ASP   A O   
1353 C CB  . ASP   A 176 ? 0.09565 0.14440 0.14307 -0.01405 -0.01747 0.00983  176 ASP   A CB  
1354 C CG  . ASP   A 176 ? 0.11153 0.16968 0.17071 -0.01762 -0.01756 0.01432  176 ASP   A CG  
1355 O OD1 . ASP   A 176 ? 0.08992 0.14766 0.15443 -0.02032 -0.01540 0.01818  176 ASP   A OD1 
1356 O OD2 . ASP   A 176 ? 0.12475 0.19209 0.18906 -0.01790 -0.02006 0.01502  176 ASP   A OD2 
1357 N N   . LEU   A 177 ? 0.09571 0.12671 0.14542 -0.01809 -0.01641 0.01179  177 LEU   A N   
1358 C CA  . LEU   A 177 ? 0.08313 0.10691 0.13864 -0.02081 -0.01572 0.01523  177 LEU   A CA  
1359 C C   . LEU   A 177 ? 0.12146 0.14885 0.18773 -0.02699 -0.01628 0.01863  177 LEU   A C   
1360 O O   . LEU   A 177 ? 0.13293 0.15389 0.20579 -0.03016 -0.01543 0.02266  177 LEU   A O   
1361 C CB  . LEU   A 177 ? 0.08987 0.10121 0.14404 -0.02034 -0.01709 0.00981  177 LEU   A CB  
1362 C CG  . LEU   A 177 ? 0.10702 0.11445 0.15676 -0.01464 -0.01519 0.01141  177 LEU   A CG  
1363 C CD1 . LEU   A 177 ? 0.10535 0.11272 0.15949 -0.01445 -0.01329 0.02077  177 LEU   A CD1 
1364 C CD2 . LEU   A 177 ? 0.11915 0.13450 0.16055 -0.01098 -0.01507 0.01041  177 LEU   A CD2 
1365 N N   . GLU   A 178 ? 0.09682 0.13485 0.16671 -0.02885 -0.01772 0.01812  178 GLU   A N   
1366 C CA  . GLU   A 178 ? 0.11510 0.16149 0.19743 -0.03422 -0.01729 0.02383  178 GLU   A CA  
1367 C C   . GLU   A 178 ? 0.11631 0.17240 0.19977 -0.03089 -0.01097 0.03164  178 GLU   A C   
1368 O O   . GLU   A 178 ? 0.11716 0.18240 0.21182 -0.03453 -0.00898 0.03775  178 GLU   A O   
1369 C CB  . GLU   A 178 ? 0.09046 0.14674 0.17875 -0.03792 -0.02219 0.02112  178 GLU   A CB  
1370 N N   . GLY   A 179 ? 0.09066 0.14528 0.16259 -0.02463 -0.00757 0.03135  179 GLY   A N   
1371 C CA  . GLY   A 179 ? 0.08443 0.14626 0.15320 -0.02161 -0.00105 0.03685  179 GLY   A CA  
1372 C C   . GLY   A 179 ? 0.10154 0.17381 0.17159 -0.01782 0.00243  0.03617  179 GLY   A C   
1373 O O   . GLY   A 179 ? 0.08774 0.16692 0.15716 -0.01562 0.00938  0.04052  179 GLY   A O   
1374 N N   . ASN   A 180 ? 0.08287 0.15654 0.15464 -0.01654 -0.00152 0.03135  180 ASN   A N   
1375 C CA  . ASN   A 180 ? 0.06799 0.15107 0.14344 -0.01193 0.00165  0.03186  180 ASN   A CA  
1376 C C   . ASN   A 180 ? 0.07841 0.15397 0.14006 -0.00611 0.00357  0.02682  180 ASN   A C   
1377 O O   . ASN   A 180 ? 0.06339 0.13104 0.11811 -0.00634 -0.00126 0.02213  180 ASN   A O   
1378 C CB  . ASN   A 180 ? 0.06568 0.15637 0.15220 -0.01450 -0.00467 0.03158  180 ASN   A CB  
1379 C CG  . ASN   A 180 ? 0.10417 0.20131 0.20440 -0.02229 -0.00791 0.03561  180 ASN   A CG  
1380 O OD1 . ASN   A 180 ? 0.14448 0.23612 0.24523 -0.02845 -0.01502 0.03200  180 ASN   A OD1 
1381 N ND2 . ASN   A 180 ? 0.06939 0.17757 0.18070 -0.02253 -0.00223 0.04277  180 ASN   A ND2 
1382 N N   . PHE   A 181 ? 0.06905 0.14634 0.12642 -0.00131 0.01114  0.02746  181 PHE   A N   
1383 C CA  . PHE   A 181 ? 0.09282 0.16088 0.13650 0.00270  0.01288  0.02200  181 PHE   A CA  
1384 C C   . PHE   A 181 ? 0.07783 0.14451 0.12402 0.00542  0.00936  0.01932  181 PHE   A C   
1385 O O   . PHE   A 181 ? 0.06459 0.14010 0.12290 0.00692  0.00864  0.02250  181 PHE   A O   
1386 C CB  . PHE   A 181 ? 0.08078 0.14898 0.11810 0.00706  0.02242  0.02155  181 PHE   A CB  
1387 C CG  . PHE   A 181 ? 0.09409 0.15740 0.11692 0.00479  0.02458  0.02079  181 PHE   A CG  
1388 C CD1 . PHE   A 181 ? 0.13603 0.18917 0.14378 0.00441  0.02238  0.01512  181 PHE   A CD1 
1389 C CD2 . PHE   A 181 ? 0.09300 0.16286 0.11751 0.00232  0.02804  0.02666  181 PHE   A CD2 
1390 C CE1 . PHE   A 181 ? 0.12177 0.17244 0.11574 0.00167  0.02288  0.01518  181 PHE   A CE1 
1391 C CE2 . PHE   A 181 ? 0.12938 0.19598 0.13910 0.00016  0.02939  0.02728  181 PHE   A CE2 
1392 C CZ  . PHE   A 181 ? 0.15038 0.20783 0.14455 -0.00023 0.02623  0.02145  181 PHE   A CZ  
1393 N N   . TYR   A 182 ? 0.07285 0.12972 0.10813 0.00580  0.00699  0.01459  182 TYR   A N   
1394 C CA  . TYR   A 182 ? 0.06645 0.12051 0.10175 0.00928  0.00612  0.01279  182 TYR   A CA  
1395 C C   . TYR   A 182 ? 0.08204 0.13269 0.11501 0.01459  0.01415  0.01167  182 TYR   A C   
1396 O O   . TYR   A 182 ? 0.10781 0.15077 0.12900 0.01424  0.01795  0.00775  182 TYR   A O   
1397 C CB  . TYR   A 182 ? 0.06477 0.11027 0.09075 0.00736  0.00161  0.00888  182 TYR   A CB  
1398 C CG  . TYR   A 182 ? 0.05929 0.10678 0.08774 0.00374  -0.00490 0.00896  182 TYR   A CG  
1399 C CD1 . TYR   A 182 ? 0.08801 0.13991 0.12121 0.00399  -0.00876 0.00988  182 TYR   A CD1 
1400 C CD2 . TYR   A 182 ? 0.09035 0.13465 0.11549 0.00040  -0.00694 0.00806  182 TYR   A CD2 
1401 C CE1 . TYR   A 182 ? 0.07084 0.12293 0.10330 0.00047  -0.01396 0.00815  182 TYR   A CE1 
1402 C CE2 . TYR   A 182 ? 0.07763 0.12100 0.10444 -0.00217 -0.01151 0.00676  182 TYR   A CE2 
1403 C CZ  . TYR   A 182 ? 0.07640 0.12314 0.10574 -0.00237 -0.01473 0.00591  182 TYR   A CZ  
1404 O OH  . TYR   A 182 ? 0.08531 0.13001 0.11362 -0.00518 -0.01857 0.00300  182 TYR   A OH  
1405 N N   . GLY   A 183 ? 0.09069 0.14735 0.13497 0.01943  0.01684  0.01523  183 GLY   A N   
1406 C CA  . GLY   A 183 ? 0.09110 0.14261 0.13513 0.02593  0.02554  0.01400  183 GLY   A CA  
1407 C C   . GLY   A 183 ? 0.09879 0.15518 0.14475 0.02839  0.03450  0.01499  183 GLY   A C   
1408 O O   . GLY   A 183 ? 0.08858 0.15388 0.13764 0.02463  0.03362  0.01810  183 GLY   A O   
1409 N N   . PRO   A 184 ? 0.10491 0.15460 0.14883 0.03477  0.04407  0.01232  184 PRO   A N   
1410 C CA  . PRO   A 184 ? 0.11637 0.17205 0.16384 0.03915  0.05511  0.01372  184 PRO   A CA  
1411 C C   . PRO   A 184 ? 0.17469 0.22243 0.20174 0.03559  0.05961  0.00728  184 PRO   A C   
1412 O O   . PRO   A 184 ? 0.19649 0.23470 0.21279 0.03953  0.06948  0.00122  184 PRO   A O   
1413 C CB  . PRO   A 184 ? 0.17383 0.22312 0.22789 0.04864  0.06383  0.01292  184 PRO   A CB  
1414 C CG  . PRO   A 184 ? 0.15253 0.18433 0.19461 0.04676  0.05914  0.00661  184 PRO   A CG  
1415 C CD  . PRO   A 184 ? 0.12380 0.15971 0.16400 0.03886  0.04602  0.00842  184 PRO   A CD  
1416 N N   . PHE   A 185 ? 0.12827 0.17930 0.14917 0.02808  0.05228  0.00851  185 PHE   A N   
1417 C CA  . PHE   A 185 ? 0.14305 0.18879 0.14448 0.02372  0.05402  0.00447  185 PHE   A CA  
1418 C C   . PHE   A 185 ? 0.17758 0.23638 0.18417 0.02026  0.05416  0.01193  185 PHE   A C   
1419 O O   . PHE   A 185 ? 0.14192 0.21079 0.16524 0.01848  0.04904  0.01861  185 PHE   A O   
1420 C CB  . PHE   A 185 ? 0.15689 0.19275 0.14565 0.01787  0.04446  -0.00007 185 PHE   A CB  
1421 C CG  . PHE   A 185 ? 0.15452 0.17831 0.14102 0.02005  0.04353  -0.00585 185 PHE   A CG  
1422 C CD1 . PHE   A 185 ? 0.15191 0.16406 0.12830 0.02350  0.05202  -0.01305 185 PHE   A CD1 
1423 C CD2 . PHE   A 185 ? 0.16911 0.19226 0.16327 0.01861  0.03501  -0.00418 185 PHE   A CD2 
1424 C CE1 . PHE   A 185 ? 0.19343 0.19270 0.16928 0.02517  0.05156  -0.01774 185 PHE   A CE1 
1425 C CE2 . PHE   A 185 ? 0.16201 0.17446 0.15502 0.02042  0.03476  -0.00798 185 PHE   A CE2 
1426 C CZ  . PHE   A 185 ? 0.15622 0.15622 0.14089 0.02358  0.04293  -0.01446 185 PHE   A CZ  
1427 N N   . VAL   A 186 ? 0.18225 0.24056 0.17377 0.01878  0.06013  0.01084  186 VAL   A N   
1428 C CA  . VAL   A 186 ? 0.17946 0.24990 0.17503 0.01589  0.06252  0.01910  186 VAL   A CA  
1429 C C   . VAL   A 186 ? 0.19795 0.26440 0.17336 0.01012  0.05929  0.01864  186 VAL   A C   
1430 O O   . VAL   A 186 ? 0.21662 0.27273 0.17264 0.00920  0.05875  0.01085  186 VAL   A O   
1431 C CB  . VAL   A 186 ? 0.22057 0.29988 0.22126 0.02163  0.07656  0.02169  186 VAL   A CB  
1432 C CG1 . VAL   A 186 ? 0.23738 0.32554 0.26357 0.02700  0.07813  0.02576  186 VAL   A CG1 
1433 C CG2 . VAL   A 186 ? 0.19601 0.26410 0.17557 0.02576  0.08635  0.01195  186 VAL   A CG2 
1434 N N   . ASP   A 187 ? 0.19518 0.27008 0.17599 0.00570  0.05655  0.02769  187 ASP   A N   
1435 C CA  . ASP   A 187 ? 0.25152 0.32496 0.21545 0.00064  0.05310  0.03020  187 ASP   A CA  
1436 C C   . ASP   A 187 ? 0.24951 0.32965 0.20074 0.00117  0.06403  0.03342  187 ASP   A C   
1437 O O   . ASP   A 187 ? 0.21881 0.30701 0.17042 -0.00220 0.06484  0.04326  187 ASP   A O   
1438 C CB  . ASP   A 187 ? 0.19476 0.27066 0.17090 -0.00411 0.04363  0.03846  187 ASP   A CB  
1439 C CG  . ASP   A 187 ? 0.21358 0.29920 0.21083 -0.00503 0.04613  0.04725  187 ASP   A CG  
1440 O OD1 . ASP   A 187 ? 0.17204 0.26529 0.17773 -0.00171 0.05459  0.04809  187 ASP   A OD1 
1441 O OD2 . ASP   A 187 ? 0.18241 0.26756 0.18953 -0.00924 0.03924  0.05321  187 ASP   A OD2 
1442 N N   . ARG   A 188 ? 0.27678 0.35267 0.21655 0.00588  0.07358  0.02484  188 ARG   A N   
1443 C CA  . ARG   A 188 ? 0.28827 0.36620 0.20921 0.00653  0.08443  0.02362  188 ARG   A CA  
1444 C C   . ARG   A 188 ? 0.32906 0.39279 0.22802 0.00824  0.08781  0.00917  188 ARG   A C   
1445 O O   . ARG   A 188 ? 0.32400 0.37849 0.22803 0.01106  0.08497  0.00189  188 ARG   A O   
1446 C CB  . ARG   A 188 ? 0.30329 0.38978 0.24070 0.01040  0.09491  0.02780  188 ARG   A CB  
1447 C CG  . ARG   A 188 ? 0.30536 0.39108 0.26011 0.01782  0.09987  0.02310  188 ARG   A CG  
1448 C CD  . ARG   A 188 ? 0.31826 0.41540 0.29141 0.02120  0.10834  0.02852  188 ARG   A CD  
1449 N NE  . ARG   A 188 ? 0.30074 0.39943 0.29537 0.02771  0.10915  0.02739  188 ARG   A NE  
1450 C CZ  . ARG   A 188 ? 0.33902 0.43026 0.33115 0.03466  0.11635  0.01885  188 ARG   A CZ  
1451 N NH1 . ARG   A 188 ? 0.36595 0.44787 0.33451 0.03529  0.12354  0.00930  188 ARG   A NH1 
1452 N NH2 . ARG   A 188 ? 0.32315 0.41615 0.33620 0.04054  0.11560  0.02001  188 ARG   A NH2 
1453 N N   . GLN   A 189 ? 0.37884 0.43751 0.25435 0.00497  0.09249  0.00453  189 GLN   A N   
1454 C CA  . GLN   A 189 ? 0.42064 0.46383 0.27231 0.00356  0.09339  -0.00970 189 GLN   A CA  
1455 C C   . GLN   A 189 ? 0.36979 0.41495 0.23068 0.01225  0.10269  -0.01901 189 GLN   A C   
1456 O O   . GLN   A 189 ? 0.36400 0.41593 0.22772 0.01513  0.11315  -0.01863 189 GLN   A O   
1457 C CB  . GLN   A 189 ? 0.47911 0.51761 0.30317 0.00402  0.09304  -0.00787 189 GLN   A CB  
1458 C CG  . GLN   A 189 ? 0.47365 0.50648 0.27841 0.00586  0.09054  -0.02190 189 GLN   A CG  
1459 C CD  . GLN   A 189 ? 0.47759 0.49993 0.28175 -0.00061 0.07755  -0.02801 189 GLN   A CD  
1460 O OE1 . GLN   A 189 ? 0.53329 0.55874 0.33757 -0.00750 0.06603  -0.02121 189 GLN   A OE1 
1461 N NE2 . GLN   A 189 ? 0.49842 0.50910 0.30455 0.00137  0.07929  -0.04026 189 GLN   A NE2 
1462 N N   . THR   A 190 ? 0.35649 0.38748 0.22114 0.01566  0.09993  -0.02668 190 THR   A N   
1463 C CA  . THR   A 190 ? 0.34968 0.37086 0.22145 0.02330  0.10832  -0.03527 190 THR   A CA  
1464 C C   . THR   A 190 ? 0.38929 0.39070 0.24904 0.02132  0.10227  -0.04662 190 THR   A C   
1465 O O   . THR   A 190 ? 0.36085 0.35824 0.21047 0.01399  0.09123  -0.04698 190 THR   A O   
1466 C CB  . THR   A 190 ? 0.34977 0.37593 0.25193 0.03025  0.11180  -0.02809 190 THR   A CB  
1467 O OG1 . THR   A 190 ? 0.29811 0.31798 0.20774 0.02883  0.10287  -0.02664 190 THR   A OG1 
1468 C CG2 . THR   A 190 ? 0.35309 0.39868 0.27118 0.03002  0.11421  -0.01494 190 THR   A CG2 
1469 N N   . ALA   A 191 ? 0.40440 0.39330 0.26767 0.02742  0.10928  -0.05507 191 ALA   A N   
1470 C CA  . ALA   A 191 ? 0.38033 0.34902 0.23649 0.02514  0.10428  -0.06510 191 ALA   A CA  
1471 C C   . ALA   A 191 ? 0.38219 0.34674 0.25915 0.02741  0.10034  -0.06074 191 ALA   A C   
1472 O O   . ALA   A 191 ? 0.40789 0.35628 0.28786 0.02912  0.10040  -0.06704 191 ALA   A O   
1473 C CB  . ALA   A 191 ? 0.42425 0.37912 0.27399 0.03040  0.11385  -0.07595 191 ALA   A CB  
1474 N N   . GLN   A 192 ? 0.33857 0.31727 0.22976 0.02735  0.09690  -0.04964 192 GLN   A N   
1475 C CA  . GLN   A 192 ? 0.30698 0.28416 0.21811 0.03051  0.09354  -0.04472 192 GLN   A CA  
1476 C C   . GLN   A 192 ? 0.39094 0.35318 0.29374 0.02401  0.08387  -0.05131 192 GLN   A C   
1477 O O   . GLN   A 192 ? 0.38513 0.34501 0.26955 0.01478  0.07614  -0.05536 192 GLN   A O   
1478 C CB  . GLN   A 192 ? 0.26273 0.25985 0.19106 0.02868  0.08537  -0.03150 192 GLN   A CB  
1479 C CG  . GLN   A 192 ? 0.31123 0.31517 0.22687 0.01927  0.07544  -0.02866 192 GLN   A CG  
1480 C CD  . GLN   A 192 ? 0.25722 0.27948 0.18970 0.01848  0.07109  -0.01600 192 GLN   A CD  
1481 O OE1 . GLN   A 192 ? 0.24590 0.27561 0.20086 0.02257  0.07044  -0.00970 192 GLN   A OE1 
1482 N NE2 . GLN   A 192 ? 0.27071 0.30004 0.19233 0.01265  0.06764  -0.01191 192 GLN   A NE2 
1483 N N   . ALA   A 193 ? 0.33926 0.29353 0.25769 0.02856  0.08346  -0.05078 193 ALA   A N   
1484 C CA  . ALA   A 193 ? 0.32602 0.26655 0.24060 0.02286  0.07513  -0.05565 193 ALA   A CA  
1485 C C   . ALA   A 193 ? 0.29606 0.24267 0.23451 0.02622  0.06885  -0.04614 193 ALA   A C   
1486 O O   . ALA   A 193 ? 0.29512 0.25196 0.25213 0.03410  0.07283  -0.03819 193 ALA   A O   
1487 C CB  . ALA   A 193 ? 0.34277 0.26090 0.24672 0.02391  0.08221  -0.06737 193 ALA   A CB  
1488 N N   . ALA   A 194 ? 0.28743 0.22855 0.22485 0.01973  0.05895  -0.04681 194 ALA   A N   
1489 C CA  . ALA   A 194 ? 0.29634 0.24433 0.25248 0.02139  0.05198  -0.03785 194 ALA   A CA  
1490 C C   . ALA   A 194 ? 0.33626 0.28090 0.30939 0.03146  0.05926  -0.03355 194 ALA   A C   
1491 O O   . ALA   A 194 ? 0.39865 0.35791 0.38878 0.03597  0.05700  -0.02376 194 ALA   A O   
1492 C CB  . ALA   A 194 ? 0.27884 0.21853 0.23001 0.01346  0.04329  -0.04043 194 ALA   A CB  
1493 N N   . GLY   A 195 ? 0.35959 0.28504 0.32900 0.03490  0.06760  -0.04036 195 GLY   A N   
1494 C CA  . GLY   A 195 ? 0.40198 0.32360 0.38986 0.04456  0.07314  -0.03426 195 GLY   A CA  
1495 C C   . GLY   A 195 ? 0.39069 0.30786 0.38633 0.04178  0.06515  -0.02915 195 GLY   A C   
1496 O O   . GLY   A 195 ? 0.33920 0.26025 0.32893 0.03301  0.05506  -0.02898 195 GLY   A O   
1497 N N   . THR   A 196 ? 0.33692 0.24630 0.34697 0.04998  0.07051  -0.02396 196 THR   A N   
1498 C CA  . THR   A 196 ? 0.35716 0.25589 0.37155 0.04727  0.06587  -0.02063 196 THR   A CA  
1499 C C   . THR   A 196 ? 0.29577 0.21339 0.31678 0.04317  0.05388  -0.01058 196 THR   A C   
1500 O O   . THR   A 196 ? 0.29795 0.23564 0.32842 0.04666  0.05071  -0.00259 196 THR   A O   
1501 C CB  . THR   A 196 ? 0.37736 0.26433 0.40731 0.05807  0.07475  -0.01517 196 THR   A CB  
1502 O OG1 . THR   A 196 ? 0.43825 0.34720 0.48598 0.06635  0.07414  -0.00272 196 THR   A OG1 
1503 C CG2 . THR   A 196 ? 0.36863 0.24041 0.38945 0.05935  0.08383  -0.02578 196 THR   A CG2 
1504 N N   . ASP   A 197 ? 0.26550 0.17659 0.28095 0.03509  0.04744  -0.01161 197 ASP   A N   
1505 C CA  . ASP   A 197 ? 0.25813 0.18434 0.27753 0.03097  0.03757  -0.00354 197 ASP   A CA  
1506 C C   . ASP   A 197 ? 0.26338 0.18418 0.29376 0.03383  0.03740  0.00577  197 ASP   A C   
1507 O O   . ASP   A 197 ? 0.27371 0.17675 0.30863 0.03790  0.04436  0.00545  197 ASP   A O   
1508 C CB  . ASP   A 197 ? 0.20590 0.13213 0.21257 0.01994  0.03082  -0.00981 197 ASP   A CB  
1509 C CG  . ASP   A 197 ? 0.22514 0.17121 0.23363 0.01711  0.02239  -0.00400 197 ASP   A CG  
1510 O OD1 . ASP   A 197 ? 0.22934 0.17722 0.23186 0.00945  0.01692  -0.00615 197 ASP   A OD1 
1511 O OD2 . ASP   A 197 ? 0.22870 0.18870 0.24474 0.02233  0.02138  0.00226  197 ASP   A OD2 
1512 N N   . THR   A 198 ? 0.22701 0.16260 0.26106 0.03173  0.02989  0.01425  198 THR   A N   
1513 C CA  . THR   A 198 ? 0.20068 0.13385 0.24258 0.03284  0.02864  0.02431  198 THR   A CA  
1514 C C   . THR   A 198 ? 0.20141 0.14349 0.23729 0.02460  0.02125  0.02565  198 THR   A C   
1515 O O   . THR   A 198 ? 0.20795 0.15964 0.23617 0.01988  0.01702  0.02013  198 THR   A O   
1516 C CB  . THR   A 198 ? 0.24711 0.19365 0.30208 0.04179  0.02824  0.03705  198 THR   A CB  
1517 O OG1 . THR   A 198 ? 0.24472 0.21283 0.29816 0.04110  0.02218  0.03824  198 THR   A OG1 
1518 C CG2 . THR   A 198 ? 0.30239 0.24061 0.36700 0.05124  0.03679  0.03747  198 THR   A CG2 
1519 N N   . THR   A 199 ? 0.20773 0.14650 0.24792 0.02329  0.02049  0.03373  199 THR   A N   
1520 C CA  . THR   A 199 ? 0.22038 0.16869 0.25612 0.01639  0.01511  0.03607  199 THR   A CA  
1521 C C   . THR   A 199 ? 0.18326 0.15130 0.22039 0.01991  0.01087  0.04507  199 THR   A C   
1522 O O   . THR   A 199 ? 0.18190 0.15370 0.22619 0.02648  0.01156  0.05431  199 THR   A O   
1523 C CB  . THR   A 199 ? 0.22159 0.15683 0.26061 0.01176  0.01696  0.04019  199 THR   A CB  
1524 O OG1 . THR   A 199 ? 0.24188 0.15890 0.27734 0.00639  0.01959  0.02961  199 THR   A OG1 
1525 C CG2 . THR   A 199 ? 0.21169 0.15923 0.24788 0.00542  0.01271  0.04398  199 THR   A CG2 
1526 N N   . ILE   A 200 ? 0.17879 0.15947 0.20895 0.01551  0.00642  0.04226  200 ILE   A N   
1527 C CA  . ILE   A 200 ? 0.15156 0.14973 0.17950 0.01750  0.00226  0.04763  200 ILE   A CA  
1528 C C   . ILE   A 200 ? 0.17515 0.17722 0.20295 0.01659  0.00200  0.05779  200 ILE   A C   
1529 O O   . ILE   A 200 ? 0.15616 0.16166 0.17923 0.01171  0.00167  0.05699  200 ILE   A O   
1530 C CB  . ILE   A 200 ? 0.16368 0.17107 0.18419 0.01387  -0.00107 0.03955  200 ILE   A CB  
1531 C CG1 . ILE   A 200 ? 0.16863 0.17043 0.18888 0.01372  -0.00004 0.03054  200 ILE   A CG1 
1532 C CG2 . ILE   A 200 ? 0.13845 0.16124 0.15580 0.01580  -0.00525 0.04275  200 ILE   A CG2 
1533 C CD1 . ILE   A 200 ? 0.13569 0.14245 0.15001 0.00935  -0.00253 0.02333  200 ILE   A CD1 
1534 N N   . THR   A 201 ? 0.16705 0.16997 0.20086 0.02177  0.00252  0.06854  201 THR   A N   
1535 C CA  . THR   A 201 ? 0.16142 0.16566 0.19620 0.02138  0.00333  0.08057  201 THR   A CA  
1536 C C   . THR   A 201 ? 0.14813 0.16839 0.17217 0.01815  0.00021  0.08237  201 THR   A C   
1537 O O   . THR   A 201 ? 0.17434 0.19451 0.19608 0.01431  0.00246  0.08636  201 THR   A O   
1538 C CB  . THR   A 201 ? 0.18740 0.19284 0.23101 0.02870  0.00340  0.09288  201 THR   A CB  
1539 O OG1 . THR   A 201 ? 0.19248 0.18104 0.24608 0.03252  0.00820  0.08964  201 THR   A OG1 
1540 C CG2 . THR   A 201 ? 0.18554 0.19213 0.23045 0.02841  0.00443  0.10645  201 THR   A CG2 
1541 N N   . VAL   A 202 ? 0.12812 0.16204 0.14552 0.01935  -0.00441 0.07927  202 VAL   A N   
1542 C CA  . VAL   A 202 ? 0.13571 0.18320 0.14084 0.01670  -0.00656 0.08019  202 VAL   A CA  
1543 C C   . VAL   A 202 ? 0.12299 0.16789 0.12374 0.01191  -0.00356 0.07150  202 VAL   A C   
1544 O O   . VAL   A 202 ? 0.12734 0.17901 0.12102 0.00979  -0.00161 0.07432  202 VAL   A O   
1545 C CB  . VAL   A 202 ? 0.14134 0.20191 0.13966 0.01760  -0.01256 0.07688  202 VAL   A CB  
1546 C CG1 . VAL   A 202 ? 0.18329 0.24015 0.18341 0.01654  -0.01348 0.06393  202 VAL   A CG1 
1547 C CG2 . VAL   A 202 ? 0.15614 0.22892 0.13900 0.01480  -0.01418 0.07722  202 VAL   A CG2 
1548 N N   . ASN   A 203 ? 0.16754 0.20375 0.17287 0.01041  -0.00279 0.06180  203 ASN   A N   
1549 C CA  . ASN   A 203 ? 0.14306 0.17867 0.14675 0.00618  -0.00073 0.05500  203 ASN   A CA  
1550 C C   . ASN   A 203 ? 0.11772 0.14804 0.12699 0.00269  0.00315  0.06088  203 ASN   A C   
1551 O O   . ASN   A 203 ? 0.12541 0.16224 0.13297 -0.00009 0.00554  0.06143  203 ASN   A O   
1552 C CB  . ASN   A 203 ? 0.15851 0.18769 0.16515 0.00513  -0.00187 0.04473  203 ASN   A CB  
1553 C CG  . ASN   A 203 ? 0.12972 0.16540 0.13134 0.00693  -0.00513 0.03836  203 ASN   A CG  
1554 O OD1 . ASN   A 203 ? 0.12361 0.16816 0.11897 0.00836  -0.00719 0.04026  203 ASN   A OD1 
1555 N ND2 . ASN   A 203 ? 0.11632 0.14760 0.12002 0.00600  -0.00582 0.03081  203 ASN   A ND2 
1556 N N   . VAL   A 204 ? 0.13759 0.15566 0.15471 0.00266  0.00439  0.06518  204 VAL   A N   
1557 C CA  . VAL   A 204 ? 0.16579 0.17740 0.18934 -0.00171 0.00781  0.07177  204 VAL   A CA  
1558 C C   . VAL   A 204 ? 0.17219 0.19507 0.19204 -0.00129 0.00991  0.08304  204 VAL   A C   
1559 O O   . VAL   A 204 ? 0.15111 0.17764 0.17332 -0.00578 0.01306  0.08650  204 VAL   A O   
1560 C CB  . VAL   A 204 ? 0.16344 0.15730 0.19542 -0.00104 0.00938  0.07470  204 VAL   A CB  
1561 C CG1 . VAL   A 204 ? 0.17317 0.15873 0.21257 -0.00699 0.01266  0.08140  204 VAL   A CG1 
1562 C CG2 . VAL   A 204 ? 0.16605 0.14871 0.19890 -0.00187 0.00843  0.06253  204 VAL   A CG2 
1563 N N   . LEU   A 205 ? 0.14309 0.17281 0.15741 0.00378  0.00822  0.08986  205 LEU   A N   
1564 C CA  . LEU   A 205 ? 0.16303 0.20481 0.17041 0.00397  0.01004  0.10069  205 LEU   A CA  
1565 C C   . LEU   A 205 ? 0.15279 0.20702 0.15037 0.00202  0.01174  0.09430  205 LEU   A C   
1566 O O   . LEU   A 205 ? 0.17369 0.23442 0.16988 -0.00038 0.01649  0.10050  205 LEU   A O   
1567 C CB  . LEU   A 205 ? 0.15824 0.20724 0.16015 0.00910  0.00618  0.10748  205 LEU   A CB  
1568 C CG  . LEU   A 205 ? 0.16581 0.20415 0.17953 0.01265  0.00556  0.11403  205 LEU   A CG  
1569 C CD1 . LEU   A 205 ? 0.16971 0.21831 0.18042 0.01726  0.00060  0.11681  205 LEU   A CD1 
1570 C CD2 . LEU   A 205 ? 0.17930 0.21112 0.20003 0.01043  0.00991  0.12294  205 LEU   A CD2 
1571 N N   . ALA   A 206 ? 0.14820 0.20519 0.14025 0.00322  0.00882  0.08209  206 ALA   A N   
1572 C CA  . ALA   A 206 ? 0.13559 0.20178 0.11976 0.00237  0.01144  0.07517  206 ALA   A CA  
1573 C C   . ALA   A 206 ? 0.14359 0.20894 0.13748 -0.00145 0.01630  0.07516  206 ALA   A C   
1574 O O   . ALA   A 206 ? 0.15324 0.22830 0.14381 -0.00194 0.02160  0.07726  206 ALA   A O   
1575 C CB  . ALA   A 206 ? 0.16395 0.22946 0.14413 0.00387  0.00759  0.06242  206 ALA   A CB  
1576 N N   . TRP   A 207 ? 0.13958 0.19418 0.14545 -0.00439 0.01463  0.07284  207 TRP   A N   
1577 C CA  . TRP   A 207 ? 0.15022 0.20478 0.16695 -0.00949 0.01715  0.07258  207 TRP   A CA  
1578 C C   . TRP   A 207 ? 0.16128 0.21778 0.18403 -0.01306 0.02171  0.08501  207 TRP   A C   
1579 O O   . TRP   A 207 ? 0.17470 0.23996 0.20374 -0.01633 0.02593  0.08800  207 TRP   A O   
1580 C CB  . TRP   A 207 ? 0.13867 0.18040 0.16302 -0.01251 0.01292  0.06595  207 TRP   A CB  
1581 C CG  . TRP   A 207 ? 0.14822 0.18823 0.18407 -0.01957 0.01316  0.06586  207 TRP   A CG  
1582 C CD1 . TRP   A 207 ? 0.15140 0.19996 0.19237 -0.02197 0.01265  0.06138  207 TRP   A CD1 
1583 C CD2 . TRP   A 207 ? 0.15050 0.17910 0.19513 -0.02575 0.01310  0.07029  207 TRP   A CD2 
1584 N NE1 . TRP   A 207 ? 0.16706 0.21258 0.21945 -0.03006 0.01140  0.06336  207 TRP   A NE1 
1585 C CE2 . TRP   A 207 ? 0.15118 0.18325 0.20531 -0.03304 0.01174  0.06799  207 TRP   A CE2 
1586 C CE3 . TRP   A 207 ? 0.15727 0.17259 0.20359 -0.02592 0.01409  0.07645  207 TRP   A CE3 
1587 C CZ2 . TRP   A 207 ? 0.20254 0.22472 0.26627 -0.04182 0.01071  0.07032  207 TRP   A CZ2 
1588 C CZ3 . TRP   A 207 ? 0.20184 0.20513 0.25812 -0.03372 0.01429  0.07873  207 TRP   A CZ3 
1589 C CH2 . TRP   A 207 ? 0.17373 0.18017 0.23784 -0.04224 0.01229  0.07496  207 TRP   A CH2 
1590 N N   . LEU   A 208 ? 0.16216 0.21177 0.18427 -0.01209 0.02138  0.09367  208 LEU   A N   
1591 C CA  . LEU   A 208 ? 0.15655 0.20847 0.18352 -0.01511 0.02617  0.10750  208 LEU   A CA  
1592 C C   . LEU   A 208 ? 0.16691 0.23535 0.18381 -0.01241 0.03040  0.10962  208 LEU   A C   
1593 O O   . LEU   A 208 ? 0.19387 0.26789 0.21634 -0.01527 0.03483  0.11416  208 LEU   A O   
1594 C CB  . LEU   A 208 ? 0.17889 0.21943 0.20709 -0.01269 0.02430  0.11469  208 LEU   A CB  
1595 C CG  . LEU   A 208 ? 0.20179 0.22228 0.24187 -0.01594 0.02261  0.11318  208 LEU   A CG  
1596 C CD1 . LEU   A 208 ? 0.19237 0.20224 0.23460 -0.01159 0.02201  0.11985  208 LEU   A CD1 
1597 C CD2 . LEU   A 208 ? 0.20748 0.22275 0.25954 -0.02470 0.02455  0.11283  208 LEU   A CD2 
1598 N N   . TYR   A 209 ? 0.17372 0.24937 0.17538 -0.00718 0.02897  0.10517  209 TYR   A N   
1599 C CA  . TYR   A 209 ? 0.19360 0.28240 0.18347 -0.00489 0.03333  0.10366  209 TYR   A CA  
1600 C C   . TYR   A 209 ? 0.18206 0.27819 0.17691 -0.00595 0.03853  0.09779  209 TYR   A C   
1601 O O   . TYR   A 209 ? 0.16873 0.27329 0.16324 -0.00587 0.04457  0.10013  209 TYR   A O   
1602 C CB  . TYR   A 209 ? 0.19265 0.28524 0.16481 -0.00051 0.02961  0.09776  209 TYR   A CB  
1603 C CG  . TYR   A 209 ? 0.19707 0.28908 0.16362 0.00093  0.02580  0.10534  209 TYR   A CG  
1604 C CD1 . TYR   A 209 ? 0.19864 0.29702 0.15981 0.00066  0.02927  0.11282  209 TYR   A CD1 
1605 C CD2 . TYR   A 209 ? 0.18243 0.26869 0.14997 0.00285  0.01889  0.10554  209 TYR   A CD2 
1606 C CE1 . TYR   A 209 ? 0.24494 0.34419 0.20190 0.00199  0.02548  0.12077  209 TYR   A CE1 
1607 C CE2 . TYR   A 209 ? 0.22723 0.31481 0.19238 0.00460  0.01535  0.11321  209 TYR   A CE2 
1608 C CZ  . TYR   A 209 ? 0.21734 0.31154 0.17706 0.00403  0.01842  0.12101  209 TYR   A CZ  
1609 O OH  . TYR   A 209 ? 0.24999 0.34674 0.20798 0.00573  0.01467  0.12970  209 TYR   A OH  
1610 N N   . ALA   A 210 ? 0.18052 0.27383 0.18051 -0.00626 0.03616  0.08969  210 ALA   A N   
1611 C CA  . ALA   A 210 ? 0.17295 0.27299 0.18259 -0.00705 0.04002  0.08482  210 ALA   A CA  
1612 C C   . ALA   A 210 ? 0.16630 0.26971 0.19212 -0.01250 0.04336  0.09359  210 ALA   A C   
1613 O O   . ALA   A 210 ? 0.15500 0.26858 0.18538 -0.01165 0.04903  0.09409  210 ALA   A O   
1614 C CB  . ALA   A 210 ? 0.18365 0.27545 0.19954 -0.00729 0.03351  0.07383  210 ALA   A CB  
1615 N N   . ALA   A 211 ? 0.14455 0.23730 0.17927 -0.01785 0.03937  0.09915  211 ALA   A N   
1616 C CA  . ALA   A 211 ? 0.16340 0.25614 0.21306 -0.02403 0.04075  0.10551  211 ALA   A CA  
1617 C C   . ALA   A 211 ? 0.17155 0.27284 0.21690 -0.02207 0.04691  0.11282  211 ALA   A C   
1618 O O   . ALA   A 211 ? 0.16895 0.28009 0.22330 -0.02379 0.05135  0.11525  211 ALA   A O   
1619 C CB  . ALA   A 211 ? 0.15519 0.23106 0.21183 -0.02956 0.03585  0.10868  211 ALA   A CB  
1620 N N   . VAL   A 212 ? 0.17520 0.27384 0.20703 -0.01844 0.04702  0.11677  212 VAL   A N   
1621 C CA  . VAL   A 212 ? 0.19131 0.29829 0.21718 -0.01696 0.05263  0.12405  212 VAL   A CA  
1622 C C   . VAL   A 212 ? 0.19256 0.31321 0.21184 -0.01304 0.05925  0.11890  212 VAL   A C   
1623 O O   . VAL   A 212 ? 0.21733 0.34682 0.24146 -0.01394 0.06554  0.12386  212 VAL   A O   
1624 C CB  . VAL   A 212 ? 0.22196 0.32533 0.23316 -0.01352 0.05023  0.12842  212 VAL   A CB  
1625 C CG1 . VAL   A 212 ? 0.22024 0.33387 0.22249 -0.01208 0.05615  0.13510  212 VAL   A CG1 
1626 C CG2 . VAL   A 212 ? 0.20485 0.29391 0.22541 -0.01642 0.04542  0.13507  212 VAL   A CG2 
1627 N N   . ILE   A 213 ? 0.19291 0.31473 0.20143 -0.00846 0.05848  0.10868  213 ILE   A N   
1628 C CA  . ILE   A 213 ? 0.19522 0.32694 0.19742 -0.00401 0.06558  0.10217  213 ILE   A CA  
1629 C C   . ILE   A 213 ? 0.21185 0.35077 0.23401 -0.00604 0.06952  0.10350  213 ILE   A C   
1630 O O   . ILE   A 213 ? 0.23877 0.38737 0.26155 -0.00366 0.07750  0.10429  213 ILE   A O   
1631 C CB  . ILE   A 213 ? 0.24778 0.37652 0.23744 0.00054  0.06330  0.09011  213 ILE   A CB  
1632 C CG1 . ILE   A 213 ? 0.25110 0.37554 0.21990 0.00216  0.05922  0.08909  213 ILE   A CG1 
1633 C CG2 . ILE   A 213 ? 0.25531 0.39101 0.24217 0.00534  0.07120  0.08200  213 ILE   A CG2 
1634 C CD1 . ILE   A 213 ? 0.26291 0.38338 0.21900 0.00532  0.05542  0.07738  213 ILE   A CD1 
1635 N N   . ASN   A 214 ? 0.19889 0.33343 0.23786 -0.01098 0.06377  0.10431  214 ASN   A N   
1636 C CA  . ASN   A 214 ? 0.19336 0.33512 0.25244 -0.01399 0.06473  0.10534  214 ASN   A CA  
1637 C C   . ASN   A 214 ? 0.20057 0.34409 0.27358 -0.02091 0.06504  0.11559  214 ASN   A C   
1638 O O   . ASN   A 214 ? 0.21889 0.36850 0.30970 -0.02499 0.06410  0.11719  214 ASN   A O   
1639 C CB  . ASN   A 214 ? 0.24161 0.37824 0.30969 -0.01645 0.05730  0.09936  214 ASN   A CB  
1640 C CG  . ASN   A 214 ? 0.25822 0.39978 0.32297 -0.00959 0.05951  0.09029  214 ASN   A CG  
1641 O OD1 . ASN   A 214 ? 0.25439 0.40571 0.32991 -0.00728 0.06344  0.08980  214 ASN   A OD1 
1642 N ND2 . ASN   A 214 ? 0.23995 0.37469 0.29011 -0.00588 0.05739  0.08345  214 ASN   A ND2 
1643 N N   . GLY   A 215 ? 0.20238 0.34106 0.26822 -0.02246 0.06590  0.12284  215 GLY   A N   
1644 C CA  . GLY   A 215 ? 0.19785 0.33911 0.27548 -0.02818 0.06807  0.13307  215 GLY   A CA  
1645 C C   . GLY   A 215 ? 0.23325 0.36057 0.32041 -0.03617 0.06131  0.13718  215 GLY   A C   
1646 O O   . GLY   A 215 ? 0.24160 0.36943 0.33947 -0.04184 0.06278  0.14545  215 GLY   A O   
1647 N N   . ASP   A 216 ? 0.18933 0.30346 0.27306 -0.03692 0.05451  0.13138  216 ASP   A N   
1648 C CA  . ASP   A 216 ? 0.21049 0.30767 0.30089 -0.04369 0.04892  0.13358  216 ASP   A CA  
1649 C C   . ASP   A 216 ? 0.23439 0.32325 0.31344 -0.04020 0.04995  0.14006  216 ASP   A C   
1650 O O   . ASP   A 216 ? 0.25401 0.33967 0.31954 -0.03419 0.04823  0.13671  216 ASP   A O   
1651 C CB  . ASP   A 216 ? 0.22578 0.31236 0.31712 -0.04559 0.04190  0.12405  216 ASP   A CB  
1652 C CG  . ASP   A 216 ? 0.26798 0.35883 0.37399 -0.05241 0.03826  0.11952  216 ASP   A CG  
1653 O OD1 . ASP   A 216 ? 0.29644 0.39582 0.41392 -0.05681 0.04049  0.12472  216 ASP   A OD1 
1654 O OD2 . ASP   A 216 ? 0.23304 0.32024 0.33894 -0.05326 0.03296  0.11115  216 ASP   A OD2 
1655 N N   . ARG   A 217 ? 0.22185 0.30774 0.30715 -0.04407 0.05229  0.14985  217 ARG   A N   
1656 C CA  . ARG   A 217 ? 0.23543 0.31613 0.31146 -0.04038 0.05352  0.15803  217 ARG   A CA  
1657 C C   . ARG   A 217 ? 0.25354 0.31580 0.33894 -0.04559 0.05103  0.16367  217 ARG   A C   
1658 O O   . ARG   A 217 ? 0.26136 0.31901 0.34150 -0.04233 0.05183  0.17174  217 ARG   A O   
1659 C CB  . ARG   A 217 ? 0.24861 0.34498 0.31970 -0.03807 0.06062  0.16662  217 ARG   A CB  
1660 C CG  . ARG   A 217 ? 0.26577 0.37873 0.32642 -0.03252 0.06491  0.16062  217 ARG   A CG  
1661 C CD  . ARG   A 217 ? 0.27063 0.39686 0.32337 -0.03002 0.07259  0.16861  217 ARG   A CD  
1662 N NE  . ARG   A 217 ? 0.27282 0.39502 0.31327 -0.02738 0.07166  0.17618  217 ARG   A NE  
1663 C CZ  . ARG   A 217 ? 0.27512 0.40072 0.29562 -0.02131 0.07089  0.17299  217 ARG   A CZ  
1664 N NH1 . ARG   A 217 ? 0.26446 0.39541 0.27432 -0.01729 0.07140  0.16151  217 ARG   A NH1 
1665 N NH2 . ARG   A 217 ? 0.28944 0.41277 0.30103 -0.01957 0.06911  0.18120  217 ARG   A NH2 
1666 N N   . TRP   A 218 ? 0.24803 0.29931 0.34669 -0.05368 0.04801  0.15939  218 TRP   A N   
1667 C CA  . TRP   A 218 ? 0.26591 0.29893 0.37384 -0.05981 0.04715  0.16439  218 TRP   A CA  
1668 C C   . TRP   A 218 ? 0.27063 0.28501 0.37257 -0.05512 0.04452  0.16404  218 TRP   A C   
1669 O O   . TRP   A 218 ? 0.28939 0.28978 0.39639 -0.05697 0.04549  0.17100  218 TRP   A O   
1670 C CB  . TRP   A 218 ? 0.27115 0.29599 0.39212 -0.07046 0.04383  0.15746  218 TRP   A CB  
1671 C CG  . TRP   A 218 ? 0.25132 0.26849 0.36955 -0.07111 0.03819  0.14412  218 TRP   A CG  
1672 C CD1 . TRP   A 218 ? 0.26916 0.29971 0.38813 -0.07160 0.03591  0.13646  218 TRP   A CD1 
1673 C CD2 . TRP   A 218 ? 0.25456 0.24890 0.36932 -0.07116 0.03455  0.13739  218 TRP   A CD2 
1674 N NE1 . TRP   A 218 ? 0.24468 0.26278 0.36031 -0.07262 0.03057  0.12569  218 TRP   A NE1 
1675 C CE2 . TRP   A 218 ? 0.25987 0.25532 0.37254 -0.07239 0.02999  0.12566  218 TRP   A CE2 
1676 C CE3 . TRP   A 218 ? 0.28227 0.25522 0.39590 -0.06971 0.03512  0.14030  218 TRP   A CE3 
1677 C CZ2 . TRP   A 218 ? 0.26338 0.23930 0.37174 -0.07252 0.02634  0.11643  218 TRP   A CZ2 
1678 C CZ3 . TRP   A 218 ? 0.29415 0.24724 0.40422 -0.06906 0.03196  0.13079  218 TRP   A CZ3 
1679 C CH2 . TRP   A 218 ? 0.28642 0.24105 0.39336 -0.07065 0.02777  0.11876  218 TRP   A CH2 
1680 N N   . PHE   A 219 ? 0.25531 0.26913 0.34787 -0.04901 0.04145  0.15634  219 PHE   A N   
1681 C CA  . PHE   A 219 ? 0.28789 0.28653 0.37565 -0.04326 0.03902  0.15563  219 PHE   A CA  
1682 C C   . PHE   A 219 ? 0.26275 0.27098 0.34056 -0.03441 0.04024  0.16466  219 PHE   A C   
1683 O O   . PHE   A 219 ? 0.28738 0.28628 0.36254 -0.02865 0.03808  0.16565  219 PHE   A O   
1684 C CB  . PHE   A 219 ? 0.27017 0.26489 0.35333 -0.04130 0.03499  0.14335  219 PHE   A CB  
1685 C CG  . PHE   A 219 ? 0.22196 0.23716 0.29634 -0.03772 0.03493  0.13933  219 PHE   A CG  
1686 C CD1 . PHE   A 219 ? 0.21748 0.24328 0.27895 -0.02920 0.03494  0.14156  219 PHE   A CD1 
1687 C CD2 . PHE   A 219 ? 0.22791 0.25206 0.30709 -0.04306 0.03469  0.13305  219 PHE   A CD2 
1688 C CE1 . PHE   A 219 ? 0.22111 0.26348 0.27313 -0.02619 0.03543  0.13644  219 PHE   A CE1 
1689 C CE2 . PHE   A 219 ? 0.20861 0.25035 0.28039 -0.03899 0.03555  0.12910  219 PHE   A CE2 
1690 C CZ  . PHE   A 219 ? 0.19374 0.24340 0.25118 -0.03060 0.03635  0.13027  219 PHE   A CZ  
1691 N N   . LEU   A 220 ? 0.26434 0.29167 0.33630 -0.03312 0.04353  0.17068  220 LEU   A N   
1692 C CA  . LEU   A 220 ? 0.27217 0.30946 0.33297 -0.02613 0.04412  0.17890  220 LEU   A CA  
1693 C C   . LEU   A 220 ? 0.29437 0.32246 0.36240 -0.02657 0.04557  0.19155  220 LEU   A C   
1694 O O   . LEU   A 220 ? 0.33137 0.34831 0.41208 -0.03307 0.04761  0.19484  220 LEU   A O   
1695 C CB  . LEU   A 220 ? 0.27162 0.33040 0.32225 -0.02514 0.04808  0.18054  220 LEU   A CB  
1696 C CG  . LEU   A 220 ? 0.25252 0.32123 0.29411 -0.02302 0.04731  0.16851  220 LEU   A CG  
1697 C CD1 . LEU   A 220 ? 0.25727 0.34455 0.28777 -0.02116 0.05245  0.16984  220 LEU   A CD1 
1698 C CD2 . LEU   A 220 ? 0.24344 0.30851 0.27516 -0.01711 0.04179  0.16279  220 LEU   A CD2 
1699 N N   . ASN   A 221 ? 0.30225 0.33566 0.36217 -0.01994 0.04422  0.19884  221 ASN   A N   
1700 C CA  . ASN   A 221 ? 0.32514 0.35191 0.39156 -0.01901 0.04547  0.21233  221 ASN   A CA  
1701 C C   . ASN   A 221 ? 0.35880 0.40182 0.41217 -0.01272 0.04424  0.22064  221 ASN   A C   
1702 O O   . ASN   A 221 ? 0.32044 0.37619 0.35977 -0.00916 0.04162  0.21415  221 ASN   A O   
1703 C CB  . ASN   A 221 ? 0.40937 0.41311 0.48721 -0.01784 0.04331  0.21073  221 ASN   A CB  
1704 C CG  . ASN   A 221 ? 0.45833 0.45995 0.53079 -0.01164 0.03860  0.20121  221 ASN   A CG  
1705 O OD1 . ASN   A 221 ? 0.46503 0.48081 0.52685 -0.00558 0.03566  0.20270  221 ASN   A OD1 
1706 N ND2 . ASN   A 221 ? 0.42699 0.41129 0.50620 -0.01395 0.03774  0.19068  221 ASN   A ND2 
1707 N N   . ARG   A 222 ? 0.35417 0.39677 0.41182 -0.01215 0.04610  0.23511  222 ARG   A N   
1708 C CA  . ARG   A 222 ? 0.38287 0.43981 0.42923 -0.00668 0.04409  0.24463  222 ARG   A CA  
1709 C C   . ARG   A 222 ? 0.40933 0.45943 0.45989 -0.00024 0.03891  0.24699  222 ARG   A C   
1710 O O   . ARG   A 222 ? 0.49155 0.55521 0.53224 0.00430  0.03542  0.25271  222 ARG   A O   
1711 C CB  . ARG   A 222 ? 0.41545 0.47766 0.46409 -0.00895 0.04868  0.26063  222 ARG   A CB  
1712 C CG  . ARG   A 222 ? 0.42094 0.49932 0.45859 -0.01263 0.05353  0.25986  222 ARG   A CG  
1713 C CD  . ARG   A 222 ? 0.46536 0.56330 0.48149 -0.00853 0.05191  0.26166  222 ARG   A CD  
1714 N NE  . ARG   A 222 ? 0.51386 0.61943 0.52733 -0.00795 0.05392  0.27886  222 ARG   A NE  
1715 C CZ  . ARG   A 222 ? 0.49625 0.61554 0.49917 -0.01024 0.05956  0.28482  222 ARG   A CZ  
1716 N NH1 . ARG   A 222 ? 0.52692 0.65356 0.52204 -0.01281 0.06417  0.27458  222 ARG   A NH1 
1717 N NH2 . ARG   A 222 ? 0.53992 0.66574 0.54049 -0.00968 0.06109  0.30137  222 ARG   A NH2 
1718 N N   . PHE   A 223 ? 0.46456 0.49438 0.52923 0.00005  0.03848  0.24228  223 PHE   A N   
1719 C CA  . PHE   A 223 ? 0.46602 0.48906 0.53605 0.00687  0.03450  0.24240  223 PHE   A CA  
1720 C C   . PHE   A 223 ? 0.42855 0.46686 0.48496 0.01079  0.02907  0.23419  223 PHE   A C   
1721 O O   . PHE   A 223 ? 0.39053 0.43682 0.43577 0.00796  0.02867  0.22360  223 PHE   A O   
1722 C CB  . PHE   A 223 ? 0.46425 0.46270 0.54764 0.00600  0.03571  0.23337  223 PHE   A CB  
1723 C CG  . PHE   A 223 ? 0.50924 0.48886 0.60563 0.00047  0.04062  0.23809  223 PHE   A CG  
1724 C CD1 . PHE   A 223 ? 0.56449 0.53434 0.67195 0.00320  0.04261  0.25116  223 PHE   A CD1 
1725 C CD2 . PHE   A 223 ? 0.52703 0.49825 0.62535 -0.00794 0.04296  0.22909  223 PHE   A CD2 
1726 C CE1 . PHE   A 223 ? 0.58955 0.54022 0.70869 -0.00278 0.04706  0.25474  223 PHE   A CE1 
1727 C CE2 . PHE   A 223 ? 0.53638 0.49011 0.64634 -0.01458 0.04677  0.23241  223 PHE   A CE2 
1728 C CZ  . PHE   A 223 ? 0.62834 0.57080 0.74830 -0.01217 0.04892  0.24494  223 PHE   A CZ  
1729 N N   . THR   A 224 ? 0.38407 0.42617 0.44261 0.01721  0.02491  0.23906  224 THR   A N   
1730 C CA  . THR   A 224 ? 0.39819 0.45005 0.44829 0.02053  0.01931  0.22984  224 THR   A CA  
1731 C C   . THR   A 224 ? 0.38842 0.42894 0.45300 0.02658  0.01781  0.23010  224 THR   A C   
1732 O O   . THR   A 224 ? 0.39841 0.42384 0.47787 0.02853  0.02131  0.23738  224 THR   A O   
1733 C CB  . THR   A 224 ? 0.43074 0.50583 0.46490 0.02155  0.01472  0.23515  224 THR   A CB  
1734 O OG1 . THR   A 224 ? 0.39736 0.48096 0.42168 0.02263  0.00939  0.22343  224 THR   A OG1 
1735 C CG2 . THR   A 224 ? 0.38926 0.46954 0.43100 0.02628  0.01249  0.25122  224 THR   A CG2 
1736 N N   . THR   A 225 ? 0.33135 0.37874 0.39188 0.02959  0.01311  0.22182  225 THR   A N   
1737 C CA  . THR   A 225 ? 0.38262 0.42257 0.45663 0.03599  0.01206  0.22195  225 THR   A CA  
1738 C C   . THR   A 225 ? 0.37223 0.43184 0.43884 0.03874  0.00505  0.22057  225 THR   A C   
1739 O O   . THR   A 225 ? 0.38979 0.46455 0.43971 0.03505  0.00120  0.21613  225 THR   A O   
1740 C CB  . THR   A 225 ? 0.39340 0.41284 0.47452 0.03568  0.01544  0.20884  225 THR   A CB  
1741 O OG1 . THR   A 225 ? 0.40418 0.41550 0.49898 0.04266  0.01605  0.20957  225 THR   A OG1 
1742 C CG2 . THR   A 225 ? 0.36339 0.38988 0.43186 0.03260  0.01245  0.19485  225 THR   A CG2 
1743 N N   . THR   A 226 ? 0.37525 0.43434 0.45465 0.04500  0.00366  0.22419  226 THR   A N   
1744 C CA  . THR   A 226 ? 0.35440 0.43127 0.42946 0.04688  -0.00319 0.22211  226 THR   A CA  
1745 C C   . THR   A 226 ? 0.34255 0.41286 0.41724 0.04683  -0.00334 0.20651  226 THR   A C   
1746 O O   . THR   A 226 ? 0.30215 0.35312 0.38347 0.04721  0.00208  0.19930  226 THR   A O   
1747 C CB  . THR   A 226 ? 0.39225 0.47545 0.48261 0.05361  -0.00477 0.23494  226 THR   A CB  
1748 O OG1 . THR   A 226 ? 0.38985 0.45472 0.49790 0.05919  0.00084  0.23227  226 THR   A OG1 
1749 C CG2 . THR   A 226 ? 0.34422 0.43144 0.43745 0.05429  -0.00380 0.25186  226 THR   A CG2 
1750 N N   . LEU   A 227 ? 0.32470 0.41101 0.39097 0.04577  -0.00982 0.20121  227 LEU   A N   
1751 C CA  . LEU   A 227 ? 0.30765 0.38982 0.37416 0.04590  -0.01046 0.18761  227 LEU   A CA  
1752 C C   . LEU   A 227 ? 0.33546 0.40510 0.42113 0.05262  -0.00609 0.18810  227 LEU   A C   
1753 O O   . LEU   A 227 ? 0.32005 0.37434 0.40879 0.05316  -0.00189 0.17788  227 LEU   A O   
1754 C CB  . LEU   A 227 ? 0.33640 0.43823 0.39216 0.04327  -0.01856 0.18329  227 LEU   A CB  
1755 C CG  . LEU   A 227 ? 0.28366 0.38314 0.33532 0.04146  -0.01989 0.16835  227 LEU   A CG  
1756 C CD1 . LEU   A 227 ? 0.29642 0.38238 0.33995 0.03795  -0.01545 0.15835  227 LEU   A CD1 
1757 C CD2 . LEU   A 227 ? 0.29458 0.41229 0.33340 0.03714  -0.02811 0.16389  227 LEU   A CD2 
1758 N N   . ASN   A 228 ? 0.32785 0.40383 0.42644 0.05800  -0.00661 0.20006  228 ASN   A N   
1759 C CA  . ASN   A 228 ? 0.35333 0.41749 0.47064 0.06530  -0.00118 0.20071  228 ASN   A CA  
1760 C C   . ASN   A 228 ? 0.36692 0.40465 0.49087 0.06672  0.00753  0.19844  228 ASN   A C   
1761 O O   . ASN   A 228 ? 0.37713 0.39854 0.50674 0.06916  0.01275  0.18868  228 ASN   A O   
1762 C CB  . ASN   A 228 ? 0.37117 0.44797 0.50237 0.07105  -0.00286 0.21591  228 ASN   A CB  
1763 C CG  . ASN   A 228 ? 0.43401 0.53570 0.56060 0.06917  -0.01167 0.21762  228 ASN   A CG  
1764 O OD1 . ASN   A 228 ? 0.49533 0.61402 0.61604 0.06679  -0.01773 0.22756  228 ASN   A OD1 
1765 N ND2 . ASN   A 228 ? 0.43291 0.53693 0.56071 0.06933  -0.01277 0.20738  228 ASN   A ND2 
1766 N N   . ASP   A 229 ? 0.37617 0.40901 0.49860 0.06453  0.00918  0.20679  229 ASP   A N   
1767 C CA  . ASP   A 229 ? 0.36409 0.37110 0.49288 0.06447  0.01687  0.20468  229 ASP   A CA  
1768 C C   . ASP   A 229 ? 0.34852 0.34266 0.46719 0.05866  0.01850  0.18912  229 ASP   A C   
1769 O O   . ASP   A 229 ? 0.34210 0.31382 0.46654 0.05941  0.02442  0.18121  229 ASP   A O   
1770 C CB  . ASP   A 229 ? 0.38348 0.38980 0.51265 0.06228  0.01781  0.21762  229 ASP   A CB  
1771 C CG  . ASP   A 229 ? 0.43796 0.45438 0.57971 0.06874  0.01701  0.23442  229 ASP   A CG  
1772 O OD1 . ASP   A 229 ? 0.48625 0.51011 0.63736 0.07483  0.01596  0.23583  229 ASP   A OD1 
1773 O OD2 . ASP   A 229 ? 0.49196 0.50906 0.63532 0.06778  0.01775  0.24687  229 ASP   A OD2 
1774 N N   . PHE   A 230 ? 0.32720 0.33496 0.43047 0.05280  0.01343  0.18399  230 PHE   A N   
1775 C CA  . PHE   A 230 ? 0.34832 0.34548 0.44354 0.04778  0.01481  0.17008  230 PHE   A CA  
1776 C C   . PHE   A 230 ? 0.31990 0.31085 0.41953 0.05164  0.01597  0.15944  230 PHE   A C   
1777 O O   . PHE   A 230 ? 0.28538 0.25706 0.38617 0.05029  0.02047  0.14956  230 PHE   A O   
1778 C CB  . PHE   A 230 ? 0.31397 0.32753 0.39250 0.04165  0.00978  0.16666  230 PHE   A CB  
1779 C CG  . PHE   A 230 ? 0.30878 0.31418 0.38047 0.03724  0.01070  0.15320  230 PHE   A CG  
1780 C CD1 . PHE   A 230 ? 0.28449 0.27461 0.35594 0.03177  0.01493  0.15007  230 PHE   A CD1 
1781 C CD2 . PHE   A 230 ? 0.27185 0.28442 0.33891 0.03824  0.00733  0.14406  230 PHE   A CD2 
1782 C CE1 . PHE   A 230 ? 0.28758 0.27091 0.35398 0.02737  0.01550  0.13858  230 PHE   A CE1 
1783 C CE2 . PHE   A 230 ? 0.30621 0.31133 0.36788 0.03457  0.00821  0.13284  230 PHE   A CE2 
1784 C CZ  . PHE   A 230 ? 0.24276 0.23353 0.30409 0.02916  0.01223  0.13032  230 PHE   A CZ  
1785 N N   . ASN   A 231 ? 0.30905 0.31637 0.41113 0.05595  0.01204  0.16132  231 ASN   A N   
1786 C CA  . ASN   A 231 ? 0.30965 0.31419 0.41564 0.05938  0.01322  0.15167  231 ASN   A CA  
1787 C C   . ASN   A 231 ? 0.31125 0.29543 0.43100 0.06546  0.02134  0.15006  231 ASN   A C   
1788 O O   . ASN   A 231 ? 0.30963 0.28420 0.43031 0.06715  0.02482  0.13916  231 ASN   A O   
1789 C CB  . ASN   A 231 ? 0.29225 0.32041 0.39868 0.06138  0.00683  0.15496  231 ASN   A CB  
1790 C CG  . ASN   A 231 ? 0.27050 0.31232 0.36131 0.05511  0.00016  0.14772  231 ASN   A CG  
1791 O OD1 . ASN   A 231 ? 0.32892 0.36185 0.41270 0.05192  0.00150  0.13743  231 ASN   A OD1 
1792 N ND2 . ASN   A 231 ? 0.27897 0.34162 0.36397 0.05304  -0.00696 0.15284  231 ASN   A ND2 
1793 N N   . LEU   A 232 ? 0.33949 0.31609 0.46910 0.06867  0.02492  0.16016  232 LEU   A N   
1794 C CA  . LEU   A 232 ? 0.33353 0.28689 0.47450 0.07376  0.03357  0.15716  232 LEU   A CA  
1795 C C   . LEU   A 232 ? 0.37129 0.29989 0.50519 0.06789  0.03779  0.14517  232 LEU   A C   
1796 O O   . LEU   A 232 ? 0.35956 0.26938 0.49580 0.07000  0.04394  0.13454  232 LEU   A O   
1797 C CB  . LEU   A 232 ? 0.35485 0.30592 0.50842 0.07839  0.03614  0.17172  232 LEU   A CB  
1798 C CG  . LEU   A 232 ? 0.41935 0.39051 0.58479 0.08576  0.03398  0.18386  232 LEU   A CG  
1799 C CD1 . LEU   A 232 ? 0.40873 0.37747 0.58588 0.08953  0.03613  0.19958  232 LEU   A CD1 
1800 C CD2 . LEU   A 232 ? 0.38243 0.35045 0.55739 0.09278  0.03894  0.17749  232 LEU   A CD2 
1801 N N   . VAL   A 233 ? 0.33462 0.26340 0.45938 0.05993  0.03469  0.14645  233 VAL   A N   
1802 C CA  . VAL   A 233 ? 0.34435 0.25218 0.46256 0.05256  0.03750  0.13535  233 VAL   A CA  
1803 C C   . VAL   A 233 ? 0.36403 0.27339 0.47310 0.05008  0.03596  0.12173  233 VAL   A C   
1804 O O   . VAL   A 233 ? 0.36281 0.25239 0.46960 0.04773  0.04011  0.10924  233 VAL   A O   
1805 C CB  . VAL   A 233 ? 0.37467 0.28532 0.48743 0.04454  0.03494  0.14189  233 VAL   A CB  
1806 C CG1 . VAL   A 233 ? 0.37573 0.26887 0.48197 0.03514  0.03651  0.13047  233 VAL   A CG1 
1807 C CG2 . VAL   A 233 ? 0.37592 0.28172 0.49843 0.04689  0.03745  0.15509  233 VAL   A CG2 
1808 N N   . ALA   A 234 ? 0.33775 0.27030 0.44058 0.05005  0.02980  0.12357  234 ALA   A N   
1809 C CA  . ALA   A 234 ? 0.30764 0.24355 0.40281 0.04838  0.02800  0.11224  234 ALA   A CA  
1810 C C   . ALA   A 234 ? 0.33493 0.25881 0.43543 0.05407  0.03353  0.10303  234 ALA   A C   
1811 O O   . ALA   A 234 ? 0.32475 0.23400 0.41980 0.05094  0.03647  0.09045  234 ALA   A O   
1812 C CB  . ALA   A 234 ? 0.29754 0.26066 0.38716 0.04895  0.02062  0.11662  234 ALA   A CB  
1813 N N   . MET   A 235 ? 0.34063 0.27135 0.45157 0.06216  0.03533  0.10924  235 MET   A N   
1814 C CA  . MET   A 235 ? 0.35187 0.27249 0.46875 0.06837  0.04205  0.10156  235 MET   A CA  
1815 C C   . MET   A 235 ? 0.35844 0.24916 0.47341 0.06625  0.04955  0.09129  235 MET   A C   
1816 O O   . MET   A 235 ? 0.35783 0.23703 0.46750 0.06608  0.05390  0.07796  235 MET   A O   
1817 C CB  . MET   A 235 ? 0.33979 0.27095 0.47083 0.07690  0.04367  0.11264  235 MET   A CB  
1818 C CG  . MET   A 235 ? 0.43887 0.36674 0.57724 0.08416  0.05039  0.10687  235 MET   A CG  
1819 S SD  . MET   A 235 ? 0.59969 0.55813 0.75041 0.09036  0.04597  0.11960  235 MET   A SD  
1820 C CE  . MET   A 235 ? 0.43622 0.39656 0.59778 0.09314  0.04508  0.13682  235 MET   A CE  
1821 N N   . LYS   A 236 ? 0.35918 0.23717 0.47734 0.06381  0.05092  0.09690  236 LYS   A N   
1822 C CA  . LYS   A 236 ? 0.36317 0.21191 0.47999 0.06117  0.05752  0.08729  236 LYS   A CA  
1823 C C   . LYS   A 236 ? 0.37297 0.20965 0.47595 0.05111  0.05623  0.07286  236 LYS   A C   
1824 O O   . LYS   A 236 ? 0.41669 0.23221 0.51446 0.04900  0.06128  0.05946  236 LYS   A O   
1825 C CB  . LYS   A 236 ? 0.37464 0.21386 0.49861 0.05984  0.05836  0.09780  236 LYS   A CB  
1826 C CG  . LYS   A 236 ? 0.43502 0.24331 0.55653 0.05481  0.06367  0.08786  236 LYS   A CG  
1827 C CD  . LYS   A 236 ? 0.46475 0.26398 0.59385 0.05277  0.06415  0.09917  236 LYS   A CD  
1828 C CE  . LYS   A 236 ? 0.44447 0.21382 0.56831 0.04396  0.06704  0.08805  236 LYS   A CE  
1829 N NZ  . LYS   A 236 ? 0.49480 0.24709 0.62955 0.04664  0.07164  0.09618  236 LYS   A NZ  
1830 N N   . TYR   A 237 ? 0.34637 0.19682 0.44274 0.04454  0.04949  0.07508  237 TYR   A N   
1831 C CA  . TYR   A 237 ? 0.31997 0.16208 0.40491 0.03424  0.04751  0.06322  237 TYR   A CA  
1832 C C   . TYR   A 237 ? 0.31584 0.17015 0.39394 0.03530  0.04551  0.05604  237 TYR   A C   
1833 O O   . TYR   A 237 ? 0.29948 0.15471 0.36939 0.02705  0.04212  0.05002  237 TYR   A O   
1834 C CB  . TYR   A 237 ? 0.32581 0.17384 0.40934 0.02533  0.04241  0.07081  237 TYR   A CB  
1835 C CG  . TYR   A 237 ? 0.36404 0.19562 0.45267 0.02160  0.04478  0.07498  237 TYR   A CG  
1836 C CD1 . TYR   A 237 ? 0.38021 0.19008 0.46412 0.01174  0.04594  0.06410  237 TYR   A CD1 
1837 C CD2 . TYR   A 237 ? 0.37731 0.21507 0.47532 0.02747  0.04550  0.08964  237 TYR   A CD2 
1838 C CE1 . TYR   A 237 ? 0.36946 0.16337 0.45836 0.00788  0.04784  0.06802  237 TYR   A CE1 
1839 C CE2 . TYR   A 237 ? 0.38889 0.21068 0.49235 0.02433  0.04808  0.09414  237 TYR   A CE2 
1840 C CZ  . TYR   A 237 ? 0.39206 0.19139 0.49112 0.01458  0.04935  0.08330  237 TYR   A CZ  
1841 O OH  . TYR   A 237 ? 0.43219 0.21499 0.53691 0.01093  0.05161  0.08803  237 TYR   A OH  
1842 N N   . ASN   A 238 ? 0.29976 0.16457 0.38229 0.04495  0.04753  0.05734  238 ASN   A N   
1843 C CA  . ASN   A 238 ? 0.30728 0.18266 0.38423 0.04659  0.04655  0.05023  238 ASN   A CA  
1844 C C   . ASN   A 238 ? 0.26727 0.16340 0.33986 0.04229  0.03817  0.05560  238 ASN   A C   
1845 O O   . ASN   A 238 ? 0.25773 0.16150 0.31893 0.03604  0.03438  0.04526  238 ASN   A O   
1846 C CB  . ASN   A 238 ? 0.28652 0.14274 0.35215 0.04133  0.05090  0.03271  238 ASN   A CB  
1847 C CG  . ASN   A 238 ? 0.34070 0.20792 0.40035 0.04395  0.05131  0.02514  238 ASN   A CG  
1848 O OD1 . ASN   A 238 ? 0.40537 0.26815 0.45118 0.03678  0.05063  0.01177  238 ASN   A OD1 
1849 N ND2 . ASN   A 238 ? 0.33833 0.22388 0.40761 0.05302  0.05103  0.03391  238 ASN   A ND2 
1850 N N   . TYR   A 239 ? 0.26682 0.17662 0.34489 0.04382  0.03390  0.06982  239 TYR   A N   
1851 C CA  . TYR   A 239 ? 0.25157 0.18447 0.32314 0.04002  0.02583  0.07406  239 TYR   A CA  
1852 C C   . TYR   A 239 ? 0.25705 0.21056 0.33394 0.04766  0.02253  0.08150  239 TYR   A C   
1853 O O   . TYR   A 239 ? 0.24832 0.20378 0.33444 0.05386  0.02492  0.08659  239 TYR   A O   
1854 C CB  . TYR   A 239 ? 0.22952 0.16512 0.30125 0.03587  0.02341  0.08532  239 TYR   A CB  
1855 C CG  . TYR   A 239 ? 0.21738 0.14616 0.28140 0.02499  0.02265  0.07829  239 TYR   A CG  
1856 C CD1 . TYR   A 239 ? 0.24929 0.15635 0.31264 0.01983  0.02658  0.06767  239 TYR   A CD1 
1857 C CD2 . TYR   A 239 ? 0.21175 0.15660 0.26941 0.01972  0.01811  0.08245  239 TYR   A CD2 
1858 C CE1 . TYR   A 239 ? 0.24491 0.14860 0.30328 0.00900  0.02468  0.06251  239 TYR   A CE1 
1859 C CE2 . TYR   A 239 ? 0.19647 0.13799 0.25026 0.01032  0.01773  0.07775  239 TYR   A CE2 
1860 C CZ  . TYR   A 239 ? 0.23009 0.15206 0.28524 0.00469  0.02037  0.06838  239 TYR   A CZ  
1861 O OH  . TYR   A 239 ? 0.21907 0.14039 0.27228 -0.00539 0.01887  0.06470  239 TYR   A OH  
1862 N N   . GLU   A 240 ? 0.24655 0.21883 0.31463 0.04376  0.01598  0.07789  240 GLU   A N   
1863 C CA  . GLU   A 240 ? 0.24071 0.23357 0.31275 0.04846  0.01133  0.08363  240 GLU   A CA  
1864 C C   . GLU   A 240 ? 0.24011 0.24515 0.31440 0.04916  0.00759  0.09610  240 GLU   A C   
1865 O O   . GLU   A 240 ? 0.25416 0.25688 0.32342 0.04531  0.00688  0.10077  240 GLU   A O   
1866 C CB  . GLU   A 240 ? 0.22917 0.23578 0.28940 0.04205  0.00539  0.07483  240 GLU   A CB  
1867 C CG  . GLU   A 240 ? 0.26974 0.27210 0.32858 0.04157  0.00804  0.06265  240 GLU   A CG  
1868 C CD  . GLU   A 240 ? 0.34619 0.36266 0.39678 0.03663  0.00223  0.05641  240 GLU   A CD  
1869 O OE1 . GLU   A 240 ? 0.40865 0.43149 0.46306 0.03857  0.00230  0.05323  240 GLU   A OE1 
1870 O OE2 . GLU   A 240 ? 0.31354 0.33450 0.35472 0.03106  -0.00172 0.05511  240 GLU   A OE2 
1871 N N   . PRO   A 241 ? 0.25925 0.27762 0.34099 0.05318  0.00564  0.10129  241 PRO   A N   
1872 C CA  . PRO   A 241 ? 0.25422 0.28594 0.33625 0.05268  0.00131  0.11227  241 PRO   A CA  
1873 C C   . PRO   A 241 ? 0.25920 0.30434 0.32639 0.04595  -0.00567 0.11160  241 PRO   A C   
1874 O O   . PRO   A 241 ? 0.28943 0.34049 0.34869 0.04255  -0.00911 0.10346  241 PRO   A O   
1875 C CB  . PRO   A 241 ? 0.26687 0.31203 0.35939 0.05707  -0.00032 0.11620  241 PRO   A CB  
1876 C CG  . PRO   A 241 ? 0.27674 0.31023 0.37742 0.06173  0.00649  0.10885  241 PRO   A CG  
1877 C CD  . PRO   A 241 ? 0.24551 0.26830 0.33608 0.05789  0.00756  0.09799  241 PRO   A CD  
1878 N N   . LEU   A 242 ? 0.28394 0.33312 0.34699 0.04406  -0.00701 0.11980  242 LEU   A N   
1879 C CA  . LEU   A 242 ? 0.28090 0.34304 0.32865 0.03816  -0.01239 0.11912  242 LEU   A CA  
1880 C C   . LEU   A 242 ? 0.24405 0.32469 0.29081 0.03797  -0.01878 0.12413  242 LEU   A C   
1881 O O   . LEU   A 242 ? 0.22376 0.30786 0.27984 0.04160  -0.01854 0.13440  242 LEU   A O   
1882 C CB  . LEU   A 242 ? 0.26227 0.31918 0.30479 0.03563  -0.00953 0.12490  242 LEU   A CB  
1883 C CG  . LEU   A 242 ? 0.23348 0.29942 0.25880 0.02962  -0.01211 0.12094  242 LEU   A CG  
1884 C CD1 . LEU   A 242 ? 0.25141 0.31003 0.27191 0.02692  -0.01042 0.11020  242 LEU   A CD1 
1885 C CD2 . LEU   A 242 ? 0.25516 0.32080 0.27686 0.02773  -0.00928 0.12960  242 LEU   A CD2 
1886 N N   . THR   A 243 ? 0.25915 0.35091 0.29528 0.03351  -0.02449 0.11681  243 THR   A N   
1887 C CA  . THR   A 243 ? 0.26613 0.37461 0.30000 0.03170  -0.03139 0.12012  243 THR   A CA  
1888 C C   . THR   A 243 ? 0.25027 0.36691 0.26706 0.02673  -0.03481 0.12143  243 THR   A C   
1889 O O   . THR   A 243 ? 0.25236 0.36306 0.25823 0.02427  -0.03176 0.11765  243 THR   A O   
1890 C CB  . THR   A 243 ? 0.23667 0.35117 0.26987 0.02904  -0.03572 0.11064  243 THR   A CB  
1891 O OG1 . THR   A 243 ? 0.23895 0.35086 0.25679 0.02375  -0.03672 0.09966  243 THR   A OG1 
1892 C CG2 . THR   A 243 ? 0.24777 0.35428 0.29651 0.03404  -0.03118 0.10858  243 THR   A CG2 
1893 N N   . GLN   A 244 ? 0.23138 0.36245 0.24571 0.02513  -0.04103 0.12680  244 GLN   A N   
1894 C CA  . GLN   A 244 ? 0.24140 0.38071 0.23715 0.02012  -0.04460 0.12671  244 GLN   A CA  
1895 C C   . GLN   A 244 ? 0.23802 0.37563 0.21733 0.01452  -0.04613 0.11210  244 GLN   A C   
1896 O O   . GLN   A 244 ? 0.25931 0.39693 0.22208 0.01137  -0.04492 0.10908  244 GLN   A O   
1897 C CB  . GLN   A 244 ? 0.27558 0.43108 0.27121 0.01893  -0.05193 0.13493  244 GLN   A CB  
1898 C CG  . GLN   A 244 ? 0.27738 0.44078 0.25195 0.01393  -0.05529 0.13511  244 GLN   A CG  
1899 C CD  . GLN   A 244 ? 0.29837 0.45641 0.26890 0.01584  -0.04902 0.14245  244 GLN   A CD  
1900 O OE1 . GLN   A 244 ? 0.31463 0.46913 0.30000 0.02087  -0.04526 0.15375  244 GLN   A OE1 
1901 N NE2 . GLN   A 244 ? 0.34590 0.50258 0.29689 0.01187  -0.04722 0.13594  244 GLN   A NE2 
1902 N N   . ASP   A 245 ? 0.24774 0.38339 0.23170 0.01348  -0.04800 0.10300  245 ASP   A N   
1903 C CA  . ASP   A 245 ? 0.26448 0.39646 0.23436 0.00857  -0.04865 0.08908  245 ASP   A CA  
1904 C C   . ASP   A 245 ? 0.25518 0.37568 0.22095 0.00968  -0.04131 0.08497  245 ASP   A C   
1905 O O   . ASP   A 245 ? 0.26112 0.38012 0.21130 0.00630  -0.03991 0.07742  245 ASP   A O   
1906 C CB  . ASP   A 245 ? 0.24880 0.38089 0.22603 0.00699  -0.05198 0.08111  245 ASP   A CB  
1907 C CG  . ASP   A 245 ? 0.26421 0.39400 0.22617 0.00101  -0.05423 0.06748  245 ASP   A CG  
1908 O OD1 . ASP   A 245 ? 0.31110 0.44632 0.25805 -0.00328 -0.05819 0.06528  245 ASP   A OD1 
1909 O OD2 . ASP   A 245 ? 0.31640 0.43832 0.28064 0.00066  -0.05175 0.05892  245 ASP   A OD2 
1910 N N   . HIS   A 246 ? 0.25829 0.37033 0.23800 0.01437  -0.03625 0.08970  246 HIS   A N   
1911 C CA  . HIS   A 246 ? 0.24633 0.34845 0.22358 0.01499  -0.02962 0.08827  246 HIS   A CA  
1912 C C   . HIS   A 246 ? 0.24233 0.34727 0.20895 0.01364  -0.02696 0.09387  246 HIS   A C   
1913 O O   . HIS   A 246 ? 0.26383 0.36623 0.22046 0.01152  -0.02291 0.08892  246 HIS   A O   
1914 C CB  . HIS   A 246 ? 0.25153 0.34290 0.24539 0.01982  -0.02509 0.09381  246 HIS   A CB  
1915 C CG  . HIS   A 246 ? 0.21891 0.30606 0.22249 0.02167  -0.02575 0.08777  246 HIS   A CG  
1916 N ND1 . HIS   A 246 ? 0.26215 0.34315 0.28169 0.02688  -0.02331 0.09269  246 HIS   A ND1 
1917 C CD2 . HIS   A 246 ? 0.27347 0.36152 0.27328 0.01920  -0.02791 0.07718  246 HIS   A CD2 
1918 C CE1 . HIS   A 246 ? 0.27716 0.35632 0.30184 0.02762  -0.02369 0.08554  246 HIS   A CE1 
1919 N NE2 . HIS   A 246 ? 0.26234 0.34603 0.27569 0.02275  -0.02687 0.07650  246 HIS   A NE2 
1920 N N   . VAL   A 247 ? 0.28561 0.39621 0.25559 0.01524  -0.02845 0.10505  247 VAL   A N   
1921 C CA  . VAL   A 247 ? 0.25602 0.37057 0.21583 0.01391  -0.02602 0.11144  247 VAL   A CA  
1922 C C   . VAL   A 247 ? 0.29889 0.42023 0.23781 0.00932  -0.02797 0.10253  247 VAL   A C   
1923 O O   . VAL   A 247 ? 0.27856 0.39884 0.20653 0.00781  -0.02278 0.10070  247 VAL   A O   
1924 C CB  . VAL   A 247 ? 0.29605 0.41713 0.26312 0.01642  -0.02841 0.12541  247 VAL   A CB  
1925 C CG1 . VAL   A 247 ? 0.31190 0.43879 0.26675 0.01463  -0.02651 0.13222  247 VAL   A CG1 
1926 C CG2 . VAL   A 247 ? 0.29859 0.40936 0.28594 0.02142  -0.02446 0.13327  247 VAL   A CG2 
1927 N N   . ASP   A 248 ? 0.26037 0.38796 0.19390 0.00693  -0.03491 0.09647  248 ASP   A N   
1928 C CA  . ASP   A 248 ? 0.33118 0.46237 0.24397 0.00227  -0.03684 0.08653  248 ASP   A CA  
1929 C C   . ASP   A 248 ? 0.28977 0.41225 0.19629 0.00122  -0.03137 0.07413  248 ASP   A C   
1930 O O   . ASP   A 248 ? 0.31451 0.43648 0.20526 -0.00046 -0.02708 0.06908  248 ASP   A O   
1931 C CB  . ASP   A 248 ? 0.31517 0.45314 0.22581 -0.00088 -0.04588 0.08227  248 ASP   A CB  
1932 C CG  . ASP   A 248 ? 0.30876 0.45831 0.22379 -0.00023 -0.05159 0.09496  248 ASP   A CG  
1933 O OD1 . ASP   A 248 ? 0.31457 0.46736 0.22745 0.00158  -0.04890 0.10548  248 ASP   A OD1 
1934 O OD2 . ASP   A 248 ? 0.31613 0.47237 0.23771 -0.00164 -0.05873 0.09512  248 ASP   A OD2 
1935 N N   . ILE   A 249 ? 0.23932 0.35520 0.15829 0.00261  -0.03086 0.06950  249 ILE   A N   
1936 C CA  . ILE   A 249 ? 0.27000 0.37864 0.18510 0.00200  -0.02595 0.05871  249 ILE   A CA  
1937 C C   . ILE   A 249 ? 0.27050 0.37677 0.18386 0.00359  -0.01736 0.06271  249 ILE   A C   
1938 O O   . ILE   A 249 ? 0.28057 0.38476 0.18462 0.00280  -0.01199 0.05475  249 ILE   A O   
1939 C CB  . ILE   A 249 ? 0.24779 0.35092 0.17783 0.00346  -0.02742 0.05541  249 ILE   A CB  
1940 C CG1 . ILE   A 249 ? 0.29316 0.39881 0.22313 0.00061  -0.03473 0.04858  249 ILE   A CG1 
1941 C CG2 . ILE   A 249 ? 0.27578 0.37217 0.20572 0.00398  -0.02156 0.04828  249 ILE   A CG2 
1942 C CD1 . ILE   A 249 ? 0.25882 0.36269 0.20699 0.00282  -0.03714 0.05060  249 ILE   A CD1 
1943 N N   . LEU   A 250 ? 0.25551 0.36202 0.17865 0.00581  -0.01541 0.07527  250 LEU   A N   
1944 C CA  . LEU   A 250 ? 0.29169 0.39618 0.21602 0.00641  -0.00748 0.08064  250 LEU   A CA  
1945 C C   . LEU   A 250 ? 0.26228 0.37358 0.17178 0.00507  -0.00455 0.08354  250 LEU   A C   
1946 O O   . LEU   A 250 ? 0.29762 0.40875 0.20836 0.00524  0.00254  0.08852  250 LEU   A O   
1947 C CB  . LEU   A 250 ? 0.24940 0.34850 0.19124 0.00863  -0.00637 0.09245  250 LEU   A CB  
1948 C CG  . LEU   A 250 ? 0.21562 0.30531 0.17177 0.01014  -0.00690 0.09022  250 LEU   A CG  
1949 C CD1 . LEU   A 250 ? 0.20271 0.28513 0.17406 0.01242  -0.00577 0.10157  250 LEU   A CD1 
1950 C CD2 . LEU   A 250 ? 0.18740 0.27277 0.14370 0.00863  -0.00156 0.08397  250 LEU   A CD2 
1951 N N   . GLY   A 251 ? 0.28258 0.39989 0.17821 0.00334  -0.00977 0.08070  251 GLY   A N   
1952 C CA  . GLY   A 251 ? 0.28559 0.40907 0.16420 0.00188  -0.00748 0.08292  251 GLY   A CA  
1953 C C   . GLY   A 251 ? 0.31800 0.43972 0.18620 0.00166  0.00207  0.07654  251 GLY   A C   
1954 O O   . GLY   A 251 ? 0.33362 0.45849 0.19997 0.00210  0.00829  0.08436  251 GLY   A O   
1955 N N   . PRO   A 252 ? 0.34171 0.45858 0.20376 0.00117  0.00394  0.06248  252 PRO   A N   
1956 C CA  . PRO   A 252 ? 0.35407 0.46936 0.20779 0.00198  0.01432  0.05600  252 PRO   A CA  
1957 C C   . PRO   A 252 ? 0.31490 0.43103 0.18420 0.00390  0.02217  0.06438  252 PRO   A C   
1958 O O   . PRO   A 252 ? 0.33757 0.45707 0.20177 0.00435  0.03055  0.06696  252 PRO   A O   
1959 C CB  . PRO   A 252 ? 0.36444 0.47275 0.21608 0.00199  0.01407  0.04078  252 PRO   A CB  
1960 C CG  . PRO   A 252 ? 0.35893 0.46657 0.20726 -0.00065 0.00289  0.03757  252 PRO   A CG  
1961 C CD  . PRO   A 252 ? 0.34112 0.45386 0.20339 -0.00012 -0.00285 0.05190  252 PRO   A CD  
1962 N N   . LEU   A 253 ? 0.30065 0.41348 0.18904 0.00460  0.01973  0.06872  253 LEU   A N   
1963 C CA  . LEU   A 253 ? 0.27497 0.38743 0.17933 0.00505  0.02604  0.07680  253 LEU   A CA  
1964 C C   . LEU   A 253 ? 0.26898 0.38490 0.17596 0.00427  0.02698  0.09082  253 LEU   A C   
1965 O O   . LEU   A 253 ? 0.28670 0.40553 0.19764 0.00377  0.03445  0.09626  253 LEU   A O   
1966 C CB  . LEU   A 253 ? 0.22779 0.33381 0.14938 0.00516  0.02249  0.07738  253 LEU   A CB  
1967 C CG  . LEU   A 253 ? 0.22981 0.33337 0.15284 0.00601  0.02420  0.06563  253 LEU   A CG  
1968 C CD1 . LEU   A 253 ? 0.23472 0.33195 0.17242 0.00563  0.01996  0.06716  253 LEU   A CD1 
1969 C CD2 . LEU   A 253 ? 0.25821 0.36548 0.18463 0.00670  0.03415  0.06403  253 LEU   A CD2 
1970 N N   . SER   A 254 ? 0.25379 0.37006 0.16005 0.00426  0.01959  0.09727  254 SER   A N   
1971 C CA  . SER   A 254 ? 0.28614 0.40629 0.19320 0.00397  0.02016  0.11074  254 SER   A CA  
1972 C C   . SER   A 254 ? 0.31342 0.44118 0.20289 0.00317  0.02597  0.11071  254 SER   A C   
1973 O O   . SER   A 254 ? 0.34405 0.47482 0.23703 0.00262  0.03170  0.12044  254 SER   A O   
1974 C CB  . SER   A 254 ? 0.29028 0.41168 0.19764 0.00480  0.01107  0.11610  254 SER   A CB  
1975 O OG  . SER   A 254 ? 0.32902 0.45546 0.23538 0.00487  0.01126  0.12918  254 SER   A OG  
1976 N N   . ALA   A 255 ? 0.31832 0.44825 0.18833 0.00281  0.02495  0.09952  255 ALA   A N   
1977 C CA  . ALA   A 255 ? 0.36385 0.49926 0.21390 0.00209  0.03089  0.09816  255 ALA   A CA  
1978 C C   . ALA   A 255 ? 0.37031 0.50597 0.22408 0.00295  0.04274  0.09583  255 ALA   A C   
1979 O O   . ALA   A 255 ? 0.36406 0.50521 0.21245 0.00262  0.04974  0.10264  255 ALA   A O   
1980 C CB  . ALA   A 255 ? 0.39334 0.52770 0.22139 0.00096  0.02694  0.08495  255 ALA   A CB  
1981 N N   . GLN   A 256 ? 0.33234 0.46317 0.19626 0.00414  0.04520  0.08685  256 GLN   A N   
1982 C CA  . GLN   A 256 ? 0.35344 0.48603 0.22437 0.00536  0.05619  0.08472  256 GLN   A CA  
1983 C C   . GLN   A 256 ? 0.35355 0.48981 0.24277 0.00414  0.05980  0.09899  256 GLN   A C   
1984 O O   . GLN   A 256 ? 0.37904 0.52103 0.26884 0.00420  0.06900  0.10244  256 GLN   A O   
1985 C CB  . GLN   A 256 ? 0.32413 0.45159 0.20535 0.00701  0.05656  0.07400  256 GLN   A CB  
1986 C CG  . GLN   A 256 ? 0.33020 0.46089 0.22523 0.00857  0.06671  0.07354  256 GLN   A CG  
1987 C CD  . GLN   A 256 ? 0.32935 0.45588 0.23482 0.01061  0.06657  0.06378  256 GLN   A CD  
1988 O OE1 . GLN   A 256 ? 0.39126 0.51196 0.29487 0.01044  0.05873  0.05820  256 GLN   A OE1 
1989 N NE2 . GLN   A 256 ? 0.37005 0.50044 0.28802 0.01264  0.07509  0.06243  256 GLN   A NE2 
1990 N N   . THR   A 257 ? 0.32889 0.46108 0.23361 0.00279  0.05302  0.10716  257 THR   A N   
1991 C CA  . THR   A 257 ? 0.29619 0.42860 0.21920 0.00067  0.05561  0.11989  257 THR   A CA  
1992 C C   . THR   A 257 ? 0.31290 0.44874 0.23062 -0.00025 0.05477  0.13272  257 THR   A C   
1993 O O   . THR   A 257 ? 0.36261 0.49978 0.29234 -0.00226 0.05892  0.14340  257 THR   A O   
1994 C CB  . THR   A 257 ? 0.29947 0.42272 0.24175 -0.00065 0.04978  0.12149  257 THR   A CB  
1995 O OG1 . THR   A 257 ? 0.26360 0.38213 0.20107 0.00051  0.04097  0.12184  257 THR   A OG1 
1996 C CG2 . THR   A 257 ? 0.25037 0.37159 0.19910 -0.00011 0.05098  0.11038  257 THR   A CG2 
1997 N N   . GLY   A 258 ? 0.32765 0.46538 0.22852 0.00079  0.04919  0.13236  258 GLY   A N   
1998 C CA  . GLY   A 258 ? 0.33215 0.47377 0.22953 0.00022  0.04729  0.14576  258 GLY   A CA  
1999 C C   . GLY   A 258 ? 0.33047 0.46528 0.24713 -0.00002 0.04190  0.15655  258 GLY   A C   
2000 O O   . GLY   A 258 ? 0.34780 0.48484 0.26701 -0.00041 0.04199  0.16978  258 GLY   A O   
2001 N N   . ILE   A 259 ? 0.28468 0.41041 0.21473 0.00037  0.03777  0.15132  259 ILE   A N   
2002 C CA  . ILE   A 259 ? 0.29625 0.41255 0.24403 0.00059  0.03343  0.15956  259 ILE   A CA  
2003 C C   . ILE   A 259 ? 0.29068 0.40599 0.23413 0.00335  0.02470  0.15626  259 ILE   A C   
2004 O O   . ILE   A 259 ? 0.28489 0.39792 0.22588 0.00401  0.02167  0.14475  259 ILE   A O   
2005 C CB  . ILE   A 259 ? 0.28432 0.38995 0.25075 -0.00158 0.03570  0.15645  259 ILE   A CB  
2006 C CG1 . ILE   A 259 ? 0.31769 0.42621 0.29101 -0.00508 0.04370  0.16119  259 ILE   A CG1 
2007 C CG2 . ILE   A 259 ? 0.30264 0.39519 0.28507 -0.00111 0.03152  0.16239  259 ILE   A CG2 
2008 C CD1 . ILE   A 259 ? 0.31538 0.41864 0.30191 -0.00798 0.04595  0.15428  259 ILE   A CD1 
2009 N N   . ALA   A 260 ? 0.28555 0.40374 0.22881 0.00494  0.02069  0.16687  260 ALA   A N   
2010 C CA  . ALA   A 260 ? 0.29841 0.41815 0.23984 0.00748  0.01230  0.16533  260 ALA   A CA  
2011 C C   . ALA   A 260 ? 0.28503 0.39304 0.24184 0.00894  0.00994  0.15955  260 ALA   A C   
2012 O O   . ALA   A 260 ? 0.28893 0.38557 0.26102 0.00838  0.01367  0.16213  260 ALA   A O   
2013 C CB  . ALA   A 260 ? 0.30118 0.42528 0.24622 0.00937  0.00917  0.18026  260 ALA   A CB  
2014 N N   . VAL   A 261 ? 0.28022 0.39050 0.23244 0.01025  0.00379  0.15121  261 VAL   A N   
2015 C CA  . VAL   A 261 ? 0.23527 0.33504 0.20075 0.01187  0.00195  0.14554  261 VAL   A CA  
2016 C C   . VAL   A 261 ? 0.24812 0.33763 0.23236 0.01453  0.00274  0.15597  261 VAL   A C   
2017 O O   . VAL   A 261 ? 0.25847 0.33427 0.25503 0.01416  0.00621  0.15436  261 VAL   A O   
2018 C CB  . VAL   A 261 ? 0.27974 0.38505 0.23901 0.01290  -0.00522 0.13722  261 VAL   A CB  
2019 C CG1 . VAL   A 261 ? 0.23051 0.32551 0.20507 0.01546  -0.00682 0.13389  261 VAL   A CG1 
2020 C CG2 . VAL   A 261 ? 0.26495 0.37547 0.20703 0.01003  -0.00503 0.12440  261 VAL   A CG2 
2021 N N   . LEU   A 262 ? 0.25789 0.35319 0.24427 0.01695  -0.00001 0.16695  262 LEU   A N   
2022 C CA  . LEU   A 262 ? 0.28744 0.37222 0.29214 0.02034  0.00135  0.17680  262 LEU   A CA  
2023 C C   . LEU   A 262 ? 0.28531 0.35885 0.29810 0.01798  0.00820  0.18274  262 LEU   A C   
2024 O O   . LEU   A 262 ? 0.29512 0.35333 0.32365 0.01961  0.01070  0.18603  262 LEU   A O   
2025 C CB  . LEU   A 262 ? 0.32569 0.42139 0.33128 0.02352  -0.00301 0.18851  262 LEU   A CB  
2026 C CG  . LEU   A 262 ? 0.28023 0.38285 0.28762 0.02650  -0.00973 0.18478  262 LEU   A CG  
2027 C CD1 . LEU   A 262 ? 0.36660 0.48060 0.37784 0.02945  -0.01378 0.19851  262 LEU   A CD1 
2028 C CD2 . LEU   A 262 ? 0.31528 0.40400 0.33759 0.02970  -0.00833 0.17842  262 LEU   A CD2 
2029 N N   . ASP   A 263 ? 0.28103 0.36117 0.28377 0.01394  0.01167  0.18375  263 ASP   A N   
2030 C CA  . ASP   A 263 ? 0.28235 0.35222 0.29432 0.01048  0.01809  0.18810  263 ASP   A CA  
2031 C C   . ASP   A 263 ? 0.26045 0.31711 0.27979 0.00774  0.02023  0.17719  263 ASP   A C   
2032 O O   . ASP   A 263 ? 0.26371 0.30452 0.29689 0.00580  0.02323  0.17911  263 ASP   A O   
2033 C CB  . ASP   A 263 ? 0.28740 0.36915 0.28777 0.00694  0.02208  0.19165  263 ASP   A CB  
2034 C CG  . ASP   A 263 ? 0.36228 0.45505 0.35641 0.00864  0.02102  0.20491  263 ASP   A CG  
2035 O OD1 . ASP   A 263 ? 0.33927 0.43240 0.33823 0.01262  0.01650  0.21153  263 ASP   A OD1 
2036 O OD2 . ASP   A 263 ? 0.33338 0.43496 0.31842 0.00604  0.02513  0.20936  263 ASP   A OD2 
2037 N N   . MET   A 264 ? 0.25542 0.31782 0.26525 0.00710  0.01854  0.16545  264 MET   A N   
2038 C CA  . MET   A 264 ? 0.22919 0.28071 0.24549 0.00442  0.01998  0.15565  264 MET   A CA  
2039 C C   . MET   A 264 ? 0.24050 0.27637 0.26855 0.00731  0.01785  0.15375  264 MET   A C   
2040 O O   . MET   A 264 ? 0.25389 0.27462 0.29142 0.00426  0.02008  0.14939  264 MET   A O   
2041 C CB  . MET   A 264 ? 0.21474 0.27650 0.21831 0.00396  0.01860  0.14431  264 MET   A CB  
2042 C CG  . MET   A 264 ? 0.20043 0.25455 0.20995 0.00039  0.02059  0.13552  264 MET   A CG  
2043 S SD  . MET   A 264 ? 0.22347 0.27688 0.24132 -0.00623 0.02730  0.13975  264 MET   A SD  
2044 C CE  . MET   A 264 ? 0.20311 0.27565 0.20614 -0.00603 0.03047  0.13413  264 MET   A CE  
2045 N N   . CYS   A 265 ? 0.24922 0.28867 0.27703 0.01289  0.01378  0.15669  265 CYS   A N   
2046 C CA  . CYS   A 265 ? 0.27534 0.30039 0.31574 0.01696  0.01325  0.15614  265 CYS   A CA  
2047 C C   . CYS   A 265 ? 0.29436 0.30267 0.34803 0.01614  0.01779  0.16337  265 CYS   A C   
2048 O O   . CYS   A 265 ? 0.26365 0.25301 0.32656 0.01560  0.02019  0.15801  265 CYS   A O   
2049 C CB  . CYS   A 265 ? 0.26227 0.29791 0.30201 0.02300  0.00842  0.15994  265 CYS   A CB  
2050 S SG  . CYS   A 265 ? 0.25000 0.29955 0.27768 0.02361  0.00244  0.14877  265 CYS   A SG  
2051 N N   . ALA   A 266 ? 0.27483 0.28903 0.32885 0.01575  0.01910  0.17517  266 ALA   A N   
2052 C CA  . ALA   A 266 ? 0.27831 0.27652 0.34456 0.01397  0.02357  0.18242  266 ALA   A CA  
2053 C C   . ALA   A 266 ? 0.30755 0.29195 0.37725 0.00633  0.02703  0.17479  266 ALA   A C   
2054 O O   . ALA   A 266 ? 0.31698 0.28028 0.39717 0.00465  0.02963  0.17247  266 ALA   A O   
2055 C CB  . ALA   A 266 ? 0.32479 0.33431 0.38897 0.01363  0.02452  0.19652  266 ALA   A CB  
2056 N N   . SER   A 267 ? 0.29809 0.29422 0.35904 0.00137  0.02709  0.17013  267 SER   A N   
2057 C CA  . SER   A 267 ? 0.27641 0.26327 0.34177 -0.00663 0.02960  0.16319  267 SER   A CA  
2058 C C   . SER   A 267 ? 0.29152 0.26265 0.36055 -0.00723 0.02831  0.15108  267 SER   A C   
2059 O O   . SER   A 267 ? 0.29280 0.24587 0.36989 -0.01297 0.03008  0.14657  267 SER   A O   
2060 C CB  . SER   A 267 ? 0.28461 0.29013 0.34070 -0.01013 0.03019  0.16059  267 SER   A CB  
2061 O OG  . SER   A 267 ? 0.31838 0.33573 0.37156 -0.01067 0.03279  0.17121  267 SER   A OG  
2062 N N   . LEU   A 268 ? 0.26301 0.24081 0.32533 -0.00200 0.02507  0.14513  268 LEU   A N   
2063 C CA  . LEU   A 268 ? 0.25300 0.21636 0.31824 -0.00156 0.02424  0.13421  268 LEU   A CA  
2064 C C   . LEU   A 268 ? 0.26841 0.21030 0.34351 0.00148  0.02651  0.13479  268 LEU   A C   
2065 O O   . LEU   A 268 ? 0.28630 0.20897 0.36547 -0.00224 0.02808  0.12563  268 LEU   A O   
2066 C CB  . LEU   A 268 ? 0.26018 0.23613 0.31704 0.00418  0.02045  0.12950  268 LEU   A CB  
2067 C CG  . LEU   A 268 ? 0.20308 0.16683 0.26188 0.00564  0.01976  0.11862  268 LEU   A CG  
2068 C CD1 . LEU   A 268 ? 0.21688 0.17042 0.27733 -0.00313 0.02088  0.10971  268 LEU   A CD1 
2069 C CD2 . LEU   A 268 ? 0.21535 0.19491 0.26561 0.01061  0.01560  0.11541  268 LEU   A CD2 
2070 N N   . LYS   A 269 ? 0.27340 0.21818 0.35213 0.00790  0.02691  0.14511  269 LYS   A N   
2071 C CA  . LYS   A 269 ? 0.29012 0.21486 0.37938 0.01159  0.03011  0.14668  269 LYS   A CA  
2072 C C   . LYS   A 269 ? 0.31779 0.22200 0.41277 0.00336  0.03363  0.14465  269 LYS   A C   
2073 O O   . LYS   A 269 ? 0.31313 0.19487 0.41219 0.00221  0.03604  0.13586  269 LYS   A O   
2074 C CB  . LYS   A 269 ? 0.32101 0.25559 0.41453 0.01871  0.02980  0.16067  269 LYS   A CB  
2075 C CG  . LYS   A 269 ? 0.36436 0.27961 0.47034 0.02322  0.03388  0.16460  269 LYS   A CG  
2076 C CD  . LYS   A 269 ? 0.36259 0.29191 0.47355 0.03143  0.03257  0.17845  269 LYS   A CD  
2077 C CE  . LYS   A 269 ? 0.44529 0.35614 0.56984 0.03483  0.03745  0.18598  269 LYS   A CE  
2078 N NZ  . LYS   A 269 ? 0.44382 0.37007 0.57396 0.04112  0.03602  0.20246  269 LYS   A NZ  
2079 N N   . GLU   A 270 ? 0.34647 0.25835 0.44113 -0.00291 0.03405  0.15212  270 GLU   A N   
2080 C CA  . GLU   A 270 ? 0.33897 0.23346 0.43967 -0.01219 0.03673  0.15082  270 GLU   A CA  
2081 C C   . GLU   A 270 ? 0.33168 0.21656 0.42982 -0.02074 0.03559  0.13600  270 GLU   A C   
2082 O O   . GLU   A 270 ? 0.39569 0.25801 0.49769 -0.02686 0.03704  0.12910  270 GLU   A O   
2083 C CB  . GLU   A 270 ? 0.34010 0.24854 0.44152 -0.01693 0.03767  0.16245  270 GLU   A CB  
2084 C CG  . GLU   A 270 ? 0.36065 0.27919 0.46350 -0.00922 0.03831  0.17727  270 GLU   A CG  
2085 C CD  . GLU   A 270 ? 0.39955 0.29653 0.51320 -0.00631 0.04129  0.18241  270 GLU   A CD  
2086 O OE1 . GLU   A 270 ? 0.47515 0.35230 0.59495 -0.01383 0.04384  0.17966  270 GLU   A OE1 
2087 O OE2 . GLU   A 270 ? 0.47233 0.37190 0.58869 0.00323  0.04099  0.18856  270 GLU   A OE2 
2088 N N   . LEU   A 271 ? 0.30524 0.20680 0.39633 -0.02172 0.03272  0.13066  271 LEU   A N   
2089 C CA  . LEU   A 271 ? 0.32148 0.21619 0.41080 -0.02989 0.03095  0.11718  271 LEU   A CA  
2090 C C   . LEU   A 271 ? 0.34042 0.21409 0.42867 -0.02709 0.03132  0.10549  271 LEU   A C   
2091 O O   . LEU   A 271 ? 0.35901 0.21623 0.44686 -0.03534 0.03083  0.09428  271 LEU   A O   
2092 C CB  . LEU   A 271 ? 0.30720 0.22482 0.39017 -0.03010 0.02812  0.11497  271 LEU   A CB  
2093 C CG  . LEU   A 271 ? 0.29440 0.23237 0.37761 -0.03437 0.02867  0.12280  271 LEU   A CG  
2094 C CD1 . LEU   A 271 ? 0.22279 0.18290 0.29772 -0.03091 0.02685  0.12106  271 LEU   A CD1 
2095 C CD2 . LEU   A 271 ? 0.30058 0.23283 0.39078 -0.04648 0.02855  0.11870  271 LEU   A CD2 
2096 N N   . LEU   A 272 ? 0.32311 0.19811 0.41041 -0.01565 0.03217  0.10757  272 LEU   A N   
2097 C CA  . LEU   A 272 ? 0.34636 0.20301 0.43313 -0.01117 0.03400  0.09685  272 LEU   A CA  
2098 C C   . LEU   A 272 ? 0.36735 0.19828 0.45944 -0.01275 0.03785  0.09519  272 LEU   A C   
2099 O O   . LEU   A 272 ? 0.39795 0.20862 0.48693 -0.01640 0.03907  0.08183  272 LEU   A O   
2100 C CB  . LEU   A 272 ? 0.31679 0.18527 0.40350 0.00160  0.03405  0.10123  272 LEU   A CB  
2101 C CG  . LEU   A 272 ? 0.30187 0.19024 0.38149 0.00318  0.03020  0.09862  272 LEU   A CG  
2102 C CD1 . LEU   A 272 ? 0.32278 0.22506 0.40305 0.01459  0.02922  0.10463  272 LEU   A CD1 
2103 C CD2 . LEU   A 272 ? 0.29156 0.16916 0.36662 -0.00134 0.03008  0.08320  272 LEU   A CD2 
2104 N N   . GLN   A 273 ? 0.38025 0.21135 0.47940 -0.01044 0.03973  0.10832  273 GLN   A N   
2105 C CA  . GLN   A 273 ? 0.41262 0.21867 0.51794 -0.01077 0.04378  0.10822  273 GLN   A CA  
2106 C C   . GLN   A 273 ? 0.41817 0.20921 0.52306 -0.02487 0.04314  0.10362  273 GLN   A C   
2107 O O   . GLN   A 273 ? 0.43451 0.19968 0.54055 -0.02800 0.04556  0.09686  273 GLN   A O   
2108 C CB  . GLN   A 273 ? 0.39705 0.20919 0.51134 -0.00276 0.04599  0.12518  273 GLN   A CB  
2109 C CG  . GLN   A 273 ? 0.42227 0.24557 0.53940 0.01089  0.04670  0.12975  273 GLN   A CG  
2110 C CD  . GLN   A 273 ? 0.42150 0.25718 0.54653 0.01736  0.04711  0.14785  273 GLN   A CD  
2111 O OE1 . GLN   A 273 ? 0.49259 0.33191 0.61937 0.01203  0.04678  0.15765  273 GLN   A OE1 
2112 N NE2 . GLN   A 273 ? 0.45287 0.29695 0.58296 0.02860  0.04772  0.15284  273 GLN   A NE2 
2113 N N   . ASN   A 274 ? 0.40519 0.21251 0.50858 -0.03362 0.03996  0.10684  274 ASN   A N   
2114 C CA  . ASN   A 274 ? 0.43771 0.23577 0.54308 -0.04747 0.03916  0.10538  274 ASN   A CA  
2115 C C   . ASN   A 274 ? 0.41096 0.21121 0.50997 -0.05882 0.03486  0.09196  274 ASN   A C   
2116 O O   . ASN   A 274 ? 0.44701 0.23527 0.54646 -0.07148 0.03347  0.08687  274 ASN   A O   
2117 C CB  . ASN   A 274 ? 0.45026 0.26763 0.56156 -0.04939 0.03967  0.12131  274 ASN   A CB  
2118 C CG  . ASN   A 274 ? 0.51022 0.32572 0.62812 -0.04022 0.04326  0.13580  274 ASN   A CG  
2119 O OD1 . ASN   A 274 ? 0.52494 0.31957 0.64614 -0.03512 0.04599  0.13442  274 ASN   A OD1 
2120 N ND2 . ASN   A 274 ? 0.50066 0.33904 0.62030 -0.03763 0.04340  0.14983  274 ASN   A ND2 
2121 N N   . GLY   A 275 ? 0.42405 0.23985 0.51754 -0.05515 0.03236  0.08655  275 GLY   A N   
2122 C CA  . GLY   A 275 ? 0.40885 0.23405 0.49869 -0.06560 0.02783  0.07747  275 GLY   A CA  
2123 C C   . GLY   A 275 ? 0.43697 0.28655 0.53292 -0.07057 0.02687  0.08802  275 GLY   A C   
2124 O O   . GLY   A 275 ? 0.44893 0.31059 0.54893 -0.06456 0.02952  0.10163  275 GLY   A O   
2125 N N   . MET   A 276 ? 0.45504 0.31327 0.55146 -0.08152 0.02298  0.08127  276 MET   A N   
2126 C CA  . MET   A 276 ? 0.43561 0.31926 0.53900 -0.08555 0.02239  0.08987  276 MET   A CA  
2127 C C   . MET   A 276 ? 0.48145 0.36025 0.59296 -0.09764 0.02281  0.09251  276 MET   A C   
2128 O O   . MET   A 276 ? 0.47054 0.36952 0.58965 -0.09962 0.02390  0.10202  276 MET   A O   
2129 C CB  . MET   A 276 ? 0.44206 0.34573 0.54371 -0.08764 0.01773  0.08305  276 MET   A CB  
2130 C CG  . MET   A 276 ? 0.42467 0.33574 0.51910 -0.07646 0.01737  0.08166  276 MET   A CG  
2131 S SD  . MET   A 276 ? 0.41102 0.35197 0.50594 -0.07749 0.01320  0.07977  276 MET   A SD  
2132 C CE  . MET   A 276 ? 0.29630 0.23595 0.38157 -0.06704 0.01226  0.07480  276 MET   A CE  
2133 N N   . ASN   A 277 ? 0.48809 0.34040 0.59762 -0.10565 0.02242  0.08432  277 ASN   A N   
2134 C CA  . ASN   A 277 ? 0.50962 0.35449 0.62655 -0.11844 0.02281  0.08612  277 ASN   A CA  
2135 C C   . ASN   A 277 ? 0.49478 0.36307 0.61908 -0.12828 0.01884  0.08398  277 ASN   A C   
2136 O O   . ASN   A 277 ? 0.49763 0.37912 0.63306 -0.13333 0.02019  0.09350  277 ASN   A O   
2137 C CB  . ASN   A 277 ? 0.52211 0.36714 0.64693 -0.11458 0.02800  0.10239  277 ASN   A CB  
2138 C CG  . ASN   A 277 ? 0.58768 0.41730 0.71944 -0.12760 0.02900  0.10373  277 ASN   A CG  
2139 O OD1 . ASN   A 277 ? 0.63557 0.44347 0.76262 -0.13779 0.02674  0.09131  277 ASN   A OD1 
2140 N ND2 . ASN   A 277 ? 0.62073 0.46176 0.76280 -0.12815 0.03244  0.11851  277 ASN   A ND2 
2141 N N   . GLY   A 278 ? 0.47890 0.35356 0.59795 -0.13036 0.01379  0.07191  278 GLY   A N   
2142 C CA  . GLY   A 278 ? 0.42303 0.31946 0.55016 -0.13920 0.00873  0.06888  278 GLY   A CA  
2143 C C   . GLY   A 278 ? 0.45322 0.38260 0.58704 -0.13215 0.00831  0.07864  278 GLY   A C   
2144 O O   . GLY   A 278 ? 0.43342 0.38309 0.57603 -0.13801 0.00441  0.07871  278 GLY   A O   
2145 N N   . ARG   A 279 ? 0.43829 0.37383 0.56796 -0.11948 0.01235  0.08664  279 ARG   A N   
2146 C CA  . ARG   A 279 ? 0.35434 0.31896 0.48774 -0.11230 0.01351  0.09488  279 ARG   A CA  
2147 C C   . ARG   A 279 ? 0.34270 0.31497 0.46735 -0.10478 0.01051  0.08808  279 ARG   A C   
2148 O O   . ARG   A 279 ? 0.34209 0.29733 0.45778 -0.10372 0.00822  0.07879  279 ARG   A O   
2149 C CB  . ARG   A 279 ? 0.34973 0.31826 0.48347 -0.10409 0.02045  0.10865  279 ARG   A CB  
2150 C CG  . ARG   A 279 ? 0.37410 0.34187 0.51860 -0.11157 0.02350  0.11754  279 ARG   A CG  
2151 C CD  . ARG   A 279 ? 0.38438 0.35279 0.52707 -0.10345 0.02984  0.13067  279 ARG   A CD  
2152 N NE  . ARG   A 279 ? 0.42309 0.36674 0.55834 -0.09895 0.03076  0.12958  279 ARG   A NE  
2153 C CZ  . ARG   A 279 ? 0.41024 0.34745 0.54524 -0.09382 0.03517  0.14058  279 ARG   A CZ  
2154 N NH1 . ARG   A 279 ? 0.37936 0.33244 0.51981 -0.09348 0.03921  0.15317  279 ARG   A NH1 
2155 N NH2 . ARG   A 279 ? 0.40742 0.32313 0.53707 -0.08855 0.03565  0.13932  279 ARG   A NH2 
2156 N N   . THR   A 280 ? 0.30897 0.30660 0.43617 -0.09938 0.01110  0.09261  280 THR   A N   
2157 C CA  . THR   A 280 ? 0.27092 0.27730 0.39064 -0.09233 0.00875  0.08723  280 THR   A CA  
2158 C C   . THR   A 280 ? 0.23507 0.25558 0.35061 -0.08092 0.01471  0.09567  280 THR   A C   
2159 O O   . THR   A 280 ? 0.22387 0.25286 0.34305 -0.07897 0.02002  0.10536  280 THR   A O   
2160 C CB  . THR   A 280 ? 0.26002 0.28346 0.38508 -0.09660 0.00296  0.08181  280 THR   A CB  
2161 O OG1 . THR   A 280 ? 0.23758 0.28152 0.37416 -0.09726 0.00566  0.09020  280 THR   A OG1 
2162 C CG2 . THR   A 280 ? 0.28350 0.29326 0.40888 -0.10795 -0.00388 0.07179  280 THR   A CG2 
2163 N N   . ILE   A 281 ? 0.19203 0.21448 0.29860 -0.07379 0.01379  0.09136  281 ILE   A N   
2164 C CA  . ILE   A 281 ? 0.19485 0.23096 0.29439 -0.06331 0.01865  0.09639  281 ILE   A CA  
2165 C C   . ILE   A 281 ? 0.19357 0.24430 0.29196 -0.06053 0.01634  0.09026  281 ILE   A C   
2166 O O   . ILE   A 281 ? 0.17961 0.22282 0.27378 -0.06125 0.01126  0.08187  281 ILE   A O   
2167 C CB  . ILE   A 281 ? 0.20304 0.22594 0.29175 -0.05628 0.02024  0.09801  281 ILE   A CB  
2168 C CG1 . ILE   A 281 ? 0.18829 0.19454 0.27949 -0.05835 0.02220  0.10396  281 ILE   A CG1 
2169 C CG2 . ILE   A 281 ? 0.17457 0.21272 0.25339 -0.04652 0.02427  0.10176  281 ILE   A CG2 
2170 C CD1 . ILE   A 281 ? 0.22286 0.21779 0.30528 -0.04981 0.02363  0.10720  281 ILE   A CD1 
2171 N N   . LEU   A 282 ? 0.19143 0.26195 0.29271 -0.05637 0.02046  0.09379  282 LEU   A N   
2172 C CA  . LEU   A 282 ? 0.19230 0.27698 0.29428 -0.05245 0.01941  0.08863  282 LEU   A CA  
2173 C C   . LEU   A 282 ? 0.19925 0.28126 0.30799 -0.05984 0.01092  0.08160  282 LEU   A C   
2174 O O   . LEU   A 282 ? 0.22549 0.30788 0.33003 -0.05778 0.00696  0.07484  282 LEU   A O   
2175 C CB  . LEU   A 282 ? 0.16035 0.24359 0.24759 -0.04301 0.02103  0.08407  282 LEU   A CB  
2176 C CG  . LEU   A 282 ? 0.16433 0.25656 0.24308 -0.03547 0.02929  0.09009  282 LEU   A CG  
2177 C CD1 . LEU   A 282 ? 0.18136 0.26805 0.24208 -0.02652 0.02827  0.08221  282 LEU   A CD1 
2178 C CD2 . LEU   A 282 ? 0.18096 0.29062 0.26615 -0.03254 0.03494  0.09231  282 LEU   A CD2 
2179 N N   . GLY   A 283 ? 0.20424 0.28324 0.32214 -0.06879 0.00780  0.08293  283 GLY   A N   
2180 C CA  . GLY   A 283 ? 0.24903 0.32642 0.37118 -0.07670 -0.00076 0.07621  283 GLY   A CA  
2181 C C   . GLY   A 283 ? 0.26459 0.32180 0.37679 -0.08109 -0.00649 0.06712  283 GLY   A C   
2182 O O   . GLY   A 283 ? 0.25681 0.31334 0.36766 -0.08614 -0.01379 0.05984  283 GLY   A O   
2183 N N   . SER   A 284 ? 0.23255 0.27296 0.33696 -0.07876 -0.00318 0.06750  284 SER   A N   
2184 C CA  . SER   A 284 ? 0.21368 0.23255 0.30820 -0.08139 -0.00715 0.05847  284 SER   A CA  
2185 C C   . SER   A 284 ? 0.23808 0.23535 0.33308 -0.08601 -0.00471 0.05973  284 SER   A C   
2186 O O   . SER   A 284 ? 0.20342 0.20073 0.30195 -0.08261 0.00135  0.06907  284 SER   A O   
2187 C CB  . SER   A 284 ? 0.22762 0.24296 0.30758 -0.06832 -0.00478 0.05356  284 SER   A CB  
2188 O OG  . SER   A 284 ? 0.23125 0.22575 0.30072 -0.06836 -0.00692 0.04410  284 SER   A OG  
2189 N N   . ALA   A 285 ? 0.24850 0.22707 0.33850 -0.09318 -0.00897 0.04971  285 ALA   A N   
2190 C CA  . ALA   A 285 ? 0.24590 0.19938 0.33462 -0.09639 -0.00581 0.04827  285 ALA   A CA  
2191 C C   . ALA   A 285 ? 0.28322 0.21683 0.36268 -0.08873 -0.00312 0.04478  285 ALA   A C   
2192 O O   . ALA   A 285 ? 0.29946 0.20940 0.37677 -0.08963 0.00010  0.04182  285 ALA   A O   
2193 C CB  . ALA   A 285 ? 0.29857 0.24138 0.38664 -0.10832 -0.01036 0.03809  285 ALA   A CB  
2194 N N   . LEU   A 286 ? 0.22767 0.17230 0.29817 -0.07748 -0.00269 0.04244  286 LEU   A N   
2195 C CA  . LEU   A 286 ? 0.29359 0.22590 0.35399 -0.06655 0.00072  0.03829  286 LEU   A CA  
2196 C C   . LEU   A 286 ? 0.26669 0.21451 0.32650 -0.05513 0.00416  0.04740  286 LEU   A C   
2197 O O   . LEU   A 286 ? 0.22829 0.19678 0.29081 -0.05454 0.00349  0.05222  286 LEU   A O   
2198 C CB  . LEU   A 286 ? 0.29290 0.22363 0.34124 -0.06508 -0.00298 0.02510  286 LEU   A CB  
2199 C CG  . LEU   A 286 ? 0.32108 0.23426 0.36327 -0.07482 -0.00624 0.01298  286 LEU   A CG  
2200 C CD1 . LEU   A 286 ? 0.33477 0.24894 0.36317 -0.07022 -0.00806 0.00239  286 LEU   A CD1 
2201 C CD2 . LEU   A 286 ? 0.38408 0.26910 0.42765 -0.07611 -0.00098 0.01156  286 LEU   A CD2 
2202 N N   . LEU   A 287 ? 0.25468 0.19279 0.31092 -0.04604 0.00793  0.04959  287 LEU   A N   
2203 C CA  . LEU   A 287 ? 0.22895 0.18192 0.28185 -0.03588 0.00961  0.05646  287 LEU   A CA  
2204 C C   . LEU   A 287 ? 0.23203 0.19541 0.27611 -0.03119 0.00646  0.04746  287 LEU   A C   
2205 O O   . LEU   A 287 ? 0.26333 0.21681 0.30218 -0.02850 0.00590  0.03920  287 LEU   A O   
2206 C CB  . LEU   A 287 ? 0.22205 0.16347 0.27611 -0.02824 0.01350  0.06332  287 LEU   A CB  
2207 C CG  . LEU   A 287 ? 0.25410 0.18301 0.31809 -0.03289 0.01704  0.07352  287 LEU   A CG  
2208 C CD1 . LEU   A 287 ? 0.28674 0.20203 0.35423 -0.02480 0.02106  0.08138  287 LEU   A CD1 
2209 C CD2 . LEU   A 287 ? 0.24602 0.19269 0.31391 -0.03614 0.01788  0.08478  287 LEU   A CD2 
2210 N N   . GLU   A 288 ? 0.18206 0.16473 0.22490 -0.03009 0.00527  0.04926  288 GLU   A N   
2211 C CA  . GLU   A 288 ? 0.19001 0.18253 0.22636 -0.02666 0.00240  0.04171  288 GLU   A CA  
2212 C C   . GLU   A 288 ? 0.15584 0.15281 0.18574 -0.01757 0.00323  0.04272  288 GLU   A C   
2213 O O   . GLU   A 288 ? 0.16711 0.17186 0.19612 -0.01413 0.00523  0.05046  288 GLU   A O   
2214 C CB  . GLU   A 288 ? 0.20781 0.21756 0.24758 -0.02913 0.00166  0.04332  288 GLU   A CB  
2215 C CG  . GLU   A 288 ? 0.22087 0.23107 0.26952 -0.03902 -0.00042 0.04352  288 GLU   A CG  
2216 C CD  . GLU   A 288 ? 0.32679 0.32969 0.37222 -0.04378 -0.00558 0.03376  288 GLU   A CD  
2217 O OE1 . GLU   A 288 ? 0.35464 0.35562 0.40577 -0.05338 -0.00874 0.03282  288 GLU   A OE1 
2218 O OE2 . GLU   A 288 ? 0.31971 0.32059 0.35671 -0.03857 -0.00678 0.02737  288 GLU   A OE2 
2219 N N   . ASP   A 289 ? 0.17957 0.17332 0.20450 -0.01432 0.00139  0.03514  289 ASP   A N   
2220 C CA  . ASP   A 289 ? 0.16134 0.15982 0.18211 -0.00689 0.00139  0.03639  289 ASP   A CA  
2221 C C   . ASP   A 289 ? 0.18321 0.19119 0.19903 -0.00503 -0.00118 0.03008  289 ASP   A C   
2222 O O   . ASP   A 289 ? 0.16132 0.17176 0.17439 -0.00035 -0.00205 0.02917  289 ASP   A O   
2223 C CB  . ASP   A 289 ? 0.15334 0.13915 0.17570 -0.00309 0.00299  0.03606  289 ASP   A CB  
2224 C CG  . ASP   A 289 ? 0.20031 0.17949 0.21950 -0.00322 0.00246  0.02609  289 ASP   A CG  
2225 O OD1 . ASP   A 289 ? 0.17717 0.15816 0.19331 -0.00810 0.00025  0.01988  289 ASP   A OD1 
2226 O OD2 . ASP   A 289 ? 0.17156 0.14444 0.19187 0.00197  0.00467  0.02555  289 ASP   A OD2 
2227 N N   . GLU   A 290 ? 0.14701 0.16091 0.16319 -0.00859 -0.00246 0.02666  290 GLU   A N   
2228 C CA  . GLU   A 290 ? 0.17613 0.19701 0.18898 -0.00650 -0.00438 0.02158  290 GLU   A CA  
2229 C C   . GLU   A 290 ? 0.16113 0.19333 0.17321 -0.00499 -0.00318 0.02331  290 GLU   A C   
2230 O O   . GLU   A 290 ? 0.15700 0.19383 0.16909 -0.00433 -0.00402 0.01952  290 GLU   A O   
2231 C CB  . GLU   A 290 ? 0.19694 0.21527 0.21041 -0.01016 -0.00679 0.01603  290 GLU   A CB  
2232 C CG  . GLU   A 290 ? 0.18187 0.18820 0.19248 -0.01076 -0.00679 0.01209  290 GLU   A CG  
2233 C CD  . GLU   A 290 ? 0.25759 0.26333 0.26415 -0.01231 -0.00904 0.00612  290 GLU   A CD  
2234 O OE1 . GLU   A 290 ? 0.19627 0.21034 0.20398 -0.01391 -0.01157 0.00589  290 GLU   A OE1 
2235 O OE2 . GLU   A 290 ? 0.22612 0.22303 0.22855 -0.01159 -0.00767 0.00227  290 GLU   A OE2 
2236 N N   . PHE   A 291 ? 0.16531 0.20146 0.17596 -0.00381 -0.00064 0.02913  291 PHE   A N   
2237 C CA  . PHE   A 291 ? 0.15211 0.19796 0.15816 -0.00136 0.00173  0.02969  291 PHE   A CA  
2238 C C   . PHE   A 291 ? 0.14953 0.19716 0.14715 0.00175  0.00099  0.03180  291 PHE   A C   
2239 O O   . PHE   A 291 ? 0.13435 0.18058 0.13209 0.00185  0.00139  0.03887  291 PHE   A O   
2240 C CB  . PHE   A 291 ? 0.16635 0.21866 0.17664 -0.00336 0.00607  0.03566  291 PHE   A CB  
2241 C CG  . PHE   A 291 ? 0.16693 0.22086 0.18756 -0.00731 0.00589  0.03527  291 PHE   A CG  
2242 C CD1 . PHE   A 291 ? 0.21779 0.27829 0.24160 -0.00575 0.00646  0.03157  291 PHE   A CD1 
2243 C CD2 . PHE   A 291 ? 0.16176 0.21038 0.18953 -0.01288 0.00469  0.03874  291 PHE   A CD2 
2244 C CE1 . PHE   A 291 ? 0.19277 0.25775 0.22762 -0.00950 0.00522  0.03286  291 PHE   A CE1 
2245 C CE2 . PHE   A 291 ? 0.19676 0.24863 0.23390 -0.01796 0.00298  0.03844  291 PHE   A CE2 
2246 C CZ  . PHE   A 291 ? 0.20953 0.27112 0.25060 -0.01617 0.00287  0.03618  291 PHE   A CZ  
2247 N N   . THR   A 292 ? 0.13007 0.18098 0.12087 0.00384  -0.00044 0.02634  292 THR   A N   
2248 C CA  . THR   A 292 ? 0.18648 0.24143 0.16852 0.00542  -0.00250 0.02821  292 THR   A CA  
2249 C C   . THR   A 292 ? 0.15232 0.21491 0.12552 0.00573  0.00117  0.03190  292 THR   A C   
2250 O O   . THR   A 292 ? 0.15912 0.22429 0.13335 0.00556  0.00621  0.03110  292 THR   A O   
2251 C CB  . THR   A 292 ? 0.18034 0.23565 0.15780 0.00587  -0.00586 0.02044  292 THR   A CB  
2252 O OG1 . THR   A 292 ? 0.19751 0.25423 0.17044 0.00612  -0.00260 0.01441  292 THR   A OG1 
2253 C CG2 . THR   A 292 ? 0.15085 0.20016 0.13623 0.00562  -0.00840 0.01724  292 THR   A CG2 
2254 N N   . PRO   A 293 ? 0.19803 0.26587 0.16241 0.00632  -0.00109 0.03655  293 PRO   A N   
2255 C CA  . PRO   A 293 ? 0.17758 0.25362 0.12917 0.00640  0.00248  0.03876  293 PRO   A CA  
2256 C C   . PRO   A 293 ? 0.21609 0.29273 0.16015 0.00685  0.00601  0.02816  293 PRO   A C   
2257 O O   . PRO   A 293 ? 0.20114 0.28204 0.14094 0.00772  0.01293  0.02872  293 PRO   A O   
2258 C CB  . PRO   A 293 ? 0.19274 0.27481 0.13491 0.00634  -0.00334 0.04341  293 PRO   A CB  
2259 C CG  . PRO   A 293 ? 0.20380 0.28127 0.15931 0.00740  -0.00679 0.05051  293 PRO   A CG  
2260 C CD  . PRO   A 293 ? 0.18391 0.25185 0.15051 0.00719  -0.00639 0.04219  293 PRO   A CD  
2261 N N   . PHE   A 294 ? 0.21514 0.28694 0.15920 0.00658  0.00227  0.01891  294 PHE   A N   
2262 C CA  . PHE   A 294 ? 0.23942 0.30851 0.17846 0.00751  0.00611  0.00860  294 PHE   A CA  
2263 C C   . PHE   A 294 ? 0.23163 0.29965 0.18222 0.00961  0.01269  0.00906  294 PHE   A C   
2264 O O   . PHE   A 294 ? 0.24173 0.31228 0.18814 0.01190  0.01991  0.00612  294 PHE   A O   
2265 C CB  . PHE   A 294 ? 0.25605 0.31860 0.19677 0.00624  0.00071  0.00035  294 PHE   A CB  
2266 C CG  . PHE   A 294 ? 0.31844 0.37490 0.25748 0.00767  0.00514  -0.00967 294 PHE   A CG  
2267 C CD1 . PHE   A 294 ? 0.35216 0.40657 0.27584 0.00658  0.00592  -0.01840 294 PHE   A CD1 
2268 C CD2 . PHE   A 294 ? 0.33586 0.38816 0.28866 0.01000  0.00839  -0.01022 294 PHE   A CD2 
2269 C CE1 . PHE   A 294 ? 0.39389 0.43997 0.31677 0.00862  0.01121  -0.02794 294 PHE   A CE1 
2270 C CE2 . PHE   A 294 ? 0.38075 0.42716 0.33417 0.01250  0.01307  -0.01784 294 PHE   A CE2 
2271 C CZ  . PHE   A 294 ? 0.39042 0.43248 0.32930 0.01216  0.01503  -0.02700 294 PHE   A CZ  
2272 N N   . ASP   A 295 ? 0.17929 0.24410 0.14448 0.00881  0.01029  0.01243  295 ASP   A N   
2273 C CA  . ASP   A 295 ? 0.19868 0.26458 0.17644 0.00958  0.01446  0.01398  295 ASP   A CA  
2274 C C   . ASP   A 295 ? 0.20552 0.27961 0.18391 0.00993  0.02113  0.02073  295 ASP   A C   
2275 O O   . ASP   A 295 ? 0.22662 0.30540 0.21097 0.01212  0.02731  0.02031  295 ASP   A O   
2276 C CB  . ASP   A 295 ? 0.18091 0.24267 0.17053 0.00699  0.00975  0.01707  295 ASP   A CB  
2277 C CG  . ASP   A 295 ? 0.20580 0.26089 0.19580 0.00683  0.00447  0.01141  295 ASP   A CG  
2278 O OD1 . ASP   A 295 ? 0.21287 0.26624 0.19766 0.00844  0.00468  0.00509  295 ASP   A OD1 
2279 O OD2 . ASP   A 295 ? 0.22011 0.27110 0.21524 0.00491  0.00071  0.01313  295 ASP   A OD2 
2280 N N   . VAL   A 296 ? 0.16939 0.24607 0.14316 0.00811  0.02042  0.02822  296 VAL   A N   
2281 C CA  . VAL   A 296 ? 0.20146 0.28636 0.17657 0.00774  0.02708  0.03641  296 VAL   A CA  
2282 C C   . VAL   A 296 ? 0.22589 0.31720 0.18753 0.01107  0.03436  0.03275  296 VAL   A C   
2283 O O   . VAL   A 296 ? 0.24586 0.34438 0.21235 0.01286  0.04261  0.03488  296 VAL   A O   
2284 C CB  . VAL   A 296 ? 0.17860 0.26328 0.15244 0.00514  0.02457  0.04658  296 VAL   A CB  
2285 C CG1 . VAL   A 296 ? 0.18134 0.27523 0.15432 0.00454  0.03194  0.05605  296 VAL   A CG1 
2286 C CG2 . VAL   A 296 ? 0.16665 0.24283 0.15440 0.00201  0.01951  0.04908  296 VAL   A CG2 
2287 N N   . VAL   A 297 ? 0.23770 0.32685 0.18226 0.01174  0.03167  0.02677  297 VAL   A N   
2288 C CA  . VAL   A 297 ? 0.29346 0.38646 0.22165 0.01434  0.03869  0.02080  297 VAL   A CA  
2289 C C   . VAL   A 297 ? 0.32005 0.40919 0.25451 0.01827  0.04450  0.01136  297 VAL   A C   
2290 O O   . VAL   A 297 ? 0.33502 0.42892 0.26542 0.02194  0.05471  0.00940  297 VAL   A O   
2291 C CB  . VAL   A 297 ? 0.28242 0.37363 0.19031 0.01249  0.03261  0.01565  297 VAL   A CB  
2292 C CG1 . VAL   A 297 ? 0.29112 0.38141 0.18066 0.01409  0.03904  0.00569  297 VAL   A CG1 
2293 C CG2 . VAL   A 297 ? 0.29688 0.39412 0.19992 0.00981  0.02781  0.02754  297 VAL   A CG2 
2294 N N   . ARG   A 298 ? 0.29916 0.38001 0.24444 0.01814  0.03891  0.00634  298 ARG   A N   
2295 C CA  . ARG   A 298 ? 0.35235 0.42920 0.30633 0.02239  0.04394  -0.00053 298 ARG   A CA  
2296 C C   . ARG   A 298 ? 0.36583 0.45219 0.33585 0.02526  0.05181  0.00658  298 ARG   A C   
2297 O O   . ARG   A 298 ? 0.42260 0.51097 0.39448 0.03070  0.06127  0.00291  298 ARG   A O   
2298 C CB  . ARG   A 298 ? 0.33964 0.40759 0.30394 0.02116  0.03599  -0.00398 298 ARG   A CB  
2299 C CG  . ARG   A 298 ? 0.39325 0.45997 0.37492 0.02536  0.03975  -0.00499 298 ARG   A CG  
2300 C CD  . ARG   A 298 ? 0.36876 0.42548 0.35682 0.02460  0.03285  -0.00932 298 ARG   A CD  
2301 N NE  . ARG   A 298 ? 0.38873 0.44555 0.38721 0.02087  0.02464  -0.00400 298 ARG   A NE  
2302 C CZ  . ARG   A 298 ? 0.29966 0.35760 0.31299 0.02172  0.02303  -0.00071 298 ARG   A CZ  
2303 N NH1 . ARG   A 298 ? 0.23133 0.29135 0.25490 0.02699  0.02886  -0.00052 298 ARG   A NH1 
2304 N NH2 . ARG   A 298 ? 0.27471 0.33183 0.29249 0.01755  0.01562  0.00261  298 ARG   A NH2 
2305 N N   . GLN   A 299 ? 0.33905 0.43137 0.32146 0.02155  0.04841  0.01680  299 GLN   A N   
2306 C CA  . GLN   A 299 ? 0.34184 0.44432 0.34327 0.02239  0.05348  0.02430  299 GLN   A CA  
2307 C C   . GLN   A 299 ? 0.32343 0.43750 0.32221 0.02281  0.06251  0.03164  299 GLN   A C   
2308 O O   . GLN   A 299 ? 0.39035 0.51447 0.40025 0.02652  0.07155  0.03469  299 GLN   A O   
2309 C CB  . GLN   A 299 ? 0.32014 0.42215 0.33631 0.01664  0.04475  0.03054  299 GLN   A CB  
2310 C CG  . GLN   A 299 ? 0.24009 0.35102 0.27741 0.01688  0.04635  0.03535  299 GLN   A CG  
2311 C CD  . GLN   A 299 ? 0.21293 0.32212 0.26112 0.01005  0.03698  0.03945  299 GLN   A CD  
2312 O OE1 . GLN   A 299 ? 0.19543 0.31432 0.25919 0.00633  0.03703  0.04691  299 GLN   A OE1 
2313 N NE2 . GLN   A 299 ? 0.17472 0.27179 0.21458 0.00780  0.02898  0.03444  299 GLN   A NE2 
2314 N N   . CYS   A 300 ? 0.34010 0.45414 0.32533 0.01945  0.06071  0.03575  300 CYS   A N   
2315 C CA  . CYS   A 300 ? 0.34216 0.46489 0.32191 0.01937  0.06846  0.04264  300 CYS   A CA  
2316 C C   . CYS   A 300 ? 0.43812 0.55753 0.39672 0.02327  0.07456  0.03354  300 CYS   A C   
2317 O O   . CYS   A 300 ? 0.52213 0.64390 0.46870 0.02171  0.07728  0.03724  300 CYS   A O   
2318 C CB  . CYS   A 300 ? 0.31178 0.43410 0.28852 0.01366  0.06282  0.05257  300 CYS   A CB  
2319 S SG  . CYS   A 300 ? 0.31507 0.43458 0.31404 0.00712  0.05453  0.06076  300 CYS   A SG  
2320 N N   . SER   A 301 ? 0.46095 0.57378 0.41476 0.02779  0.07668  0.02156  301 SER   A N   
2321 C CA  . SER   A 301 ? 0.51058 0.61754 0.44593 0.03087  0.08364  0.01083  301 SER   A CA  
2322 C C   . SER   A 301 ? 0.53163 0.63304 0.47536 0.03710  0.09009  0.00120  301 SER   A C   
2323 O O   . SER   A 301 ? 0.51110 0.61249 0.45253 0.04062  0.10033  -0.00322 301 SER   A O   
2324 C CB  . SER   A 301 ? 0.55401 0.65254 0.46494 0.02754  0.07640  0.00372  301 SER   A CB  
2325 O OG  . SER   A 301 ? 0.62976 0.72035 0.52198 0.02903  0.08271  -0.00798 301 SER   A OG  
2326 N N   . GLY   A 302 ? 0.54571 0.64198 0.49925 0.03873  0.08461  -0.00212 302 GLY   A N   
2327 C CA  . GLY   A 302 ? 0.56035 0.65305 0.52964 0.04505  0.09009  -0.00665 302 GLY   A CA  
2328 C C   . GLY   A 302 ? 0.64152 0.71824 0.60166 0.04847  0.09070  -0.02067 302 GLY   A C   
2329 O O   . GLY   A 302 ? 0.62500 0.69653 0.58923 0.05362  0.09928  -0.02711 302 GLY   A O   
2330 N N   . VAL   A 303 ? 0.65121 0.71866 0.60215 0.04414  0.08011  -0.02541 303 VAL   A N   
2331 C CA  . VAL   A 303 ? 0.69062 0.74090 0.63249 0.04509  0.07917  -0.03885 303 VAL   A CA  
2332 C C   . VAL   A 303 ? 0.65796 0.70251 0.62296 0.04909  0.07820  -0.03749 303 VAL   A C   
2333 O O   . VAL   A 303 ? 0.59339 0.64643 0.57761 0.04800  0.07276  -0.02679 303 VAL   A O   
2334 C CB  . VAL   A 303 ? 0.68690 0.73059 0.61230 0.03675  0.06668  -0.04318 303 VAL   A CB  
2335 C CG1 . VAL   A 303 ? 0.73890 0.76505 0.65240 0.03606  0.06620  -0.05798 303 VAL   A CG1 
2336 C CG2 . VAL   A 303 ? 0.66426 0.71761 0.57036 0.03271  0.06583  -0.03990 303 VAL   A CG2 
2337 N N   . THR   A 304 ? 0.63455 0.66400 0.59704 0.05346  0.08347  -0.04836 304 THR   A N   
2338 C CA  . THR   A 304 ? 0.57852 0.60100 0.56223 0.05850  0.08410  -0.04689 304 THR   A CA  
2339 C C   . THR   A 304 ? 0.68546 0.68862 0.66136 0.05462  0.07759  -0.05688 304 THR   A C   
2340 O O   . THR   A 304 ? 0.72303 0.71993 0.67832 0.04762  0.07201  -0.06482 304 THR   A O   
2341 C CB  . THR   A 304 ? 0.52954 0.55257 0.52461 0.06747  0.09629  -0.04821 304 THR   A CB  
2342 O OG1 . THR   A 304 ? 0.63875 0.65244 0.61317 0.06749  0.10182  -0.06165 304 THR   A OG1 
2343 C CG2 . THR   A 304 ? 0.40574 0.44973 0.41497 0.06925  0.10010  -0.03607 304 THR   A CG2 
2344 N N   . PHE   A 305 ? 0.65620 0.65085 0.64989 0.05891  0.07810  -0.05538 305 PHE   A N   
2345 C CA  . PHE   A 305 ? 0.72456 0.70235 0.71619 0.05444  0.07095  -0.06143 305 PHE   A CA  
2346 C C   . PHE   A 305 ? 0.71689 0.67985 0.72249 0.06261  0.07915  -0.06435 305 PHE   A C   
2347 O O   . PHE   A 305 ? 0.66246 0.63427 0.68882 0.07000  0.08298  -0.05425 305 PHE   A O   
2348 C CB  . PHE   A 305 ? 0.65491 0.64043 0.65599 0.04801  0.05763  -0.05120 305 PHE   A CB  
2349 C CG  . PHE   A 305 ? 0.62908 0.63036 0.62299 0.04260  0.05163  -0.04526 305 PHE   A CG  
2350 C CD1 . PHE   A 305 ? 0.59296 0.59271 0.56842 0.03505  0.04505  -0.05052 305 PHE   A CD1 
2351 C CD2 . PHE   A 305 ? 0.56242 0.58013 0.56891 0.04496  0.05272  -0.03402 305 PHE   A CD2 
2352 C CE1 . PHE   A 305 ? 0.60869 0.62172 0.57882 0.03114  0.04043  -0.04411 305 PHE   A CE1 
2353 C CE2 . PHE   A 305 ? 0.54859 0.57809 0.54897 0.03991  0.04803  -0.02873 305 PHE   A CE2 
2354 C CZ  . PHE   A 305 ? 0.58776 0.61433 0.57011 0.03365  0.04236  -0.03351 305 PHE   A CZ  
2355 N N   . GLN   A 306 ? 0.74886 0.69160 0.74343 0.05957  0.07827  -0.07613 306 GLN   A N   
2356 C CA  . GLN   A 306 ? 0.78417 0.71206 0.78947 0.06534  0.08228  -0.07778 306 GLN   A CA  
2357 C C   . GLN   A 306 ? 0.72094 0.63050 0.72654 0.05901  0.07528  -0.08174 306 GLN   A C   
2358 O O   . GLN   A 306 ? 0.67611 0.58593 0.70016 0.05976  0.07152  -0.07197 306 GLN   A O   
2359 C CB  . GLN   A 306 ? 0.81611 0.73629 0.80718 0.06913  0.09047  -0.08897 306 GLN   A CB  
2360 C CG  . GLN   A 306 ? 0.76694 0.70506 0.76197 0.07634  0.09902  -0.08424 306 GLN   A CG  
2361 C CD  . GLN   A 306 ? 0.82095 0.75054 0.81706 0.08451  0.10932  -0.09059 306 GLN   A CD  
2362 O OE1 . GLN   A 306 ? 0.87782 0.80903 0.85699 0.08542  0.11519  -0.09936 306 GLN   A OE1 
2363 N NE2 . GLN   A 306 ? 0.80757 0.72841 0.82342 0.09065  0.11177  -0.08577 306 GLN   A NE2 
2364 C C1  . A1AQ3 B .   ? 0.35938 0.37347 0.18850 -0.03099 0.01373  -0.02739 401 A1AQ3 A C1  
2365 C C10 . A1AQ3 B .   ? 0.37162 0.43238 0.25661 -0.01063 0.04692  0.01847  401 A1AQ3 A C10 
2366 C C11 . A1AQ3 B .   ? 0.33826 0.39464 0.24269 -0.00482 0.05083  0.01378  401 A1AQ3 A C11 
2367 C C12 . A1AQ3 B .   ? 0.33313 0.36988 0.18468 -0.02756 0.01218  -0.00505 401 A1AQ3 A C12 
2368 C C13 . A1AQ3 B .   ? 0.34952 0.39719 0.19441 -0.02322 0.02510  0.00620  401 A1AQ3 A C13 
2369 C C14 . A1AQ3 B .   ? 0.29675 0.35104 0.17347 -0.02416 0.01032  0.01712  401 A1AQ3 A C14 
2370 C C15 . A1AQ3 B .   ? 0.28937 0.34815 0.16674 -0.02846 -0.00161 0.02271  401 A1AQ3 A C15 
2371 C C16 . A1AQ3 B .   ? 0.37779 0.43600 0.24034 -0.02032 0.02884  0.01831  401 A1AQ3 A C16 
2372 C C17 . A1AQ3 B .   ? 0.26729 0.33224 0.16884 -0.02948 -0.01736 0.03298  401 A1AQ3 A C17 
2373 C C18 . A1AQ3 B .   ? 0.36751 0.43892 0.26561 -0.01247 0.04395  0.03321  401 A1AQ3 A C18 
2374 C C19 . A1AQ3 B .   ? 0.22348 0.28413 0.13154 -0.03043 -0.02247 0.02620  401 A1AQ3 A C19 
2375 C C20 . A1AQ3 B .   ? 0.23680 0.28922 0.12819 -0.03397 -0.02044 0.01340  401 A1AQ3 A C20 
2376 C C21 . A1AQ3 B .   ? 0.30299 0.35741 0.18174 -0.03876 -0.02496 0.01262  401 A1AQ3 A C21 
2377 C C22 . A1AQ3 B .   ? 0.30200 0.34928 0.17764 -0.04305 -0.02872 0.00274  401 A1AQ3 A C22 
2378 C C23 . A1AQ3 B .   ? 0.40907 0.46758 0.27194 -0.00983 0.05727  0.01308  401 A1AQ3 A C23 
2379 C C24 . A1AQ3 B .   ? 0.24968 0.29663 0.14806 -0.03530 -0.02411 0.00693  401 A1AQ3 A C24 
2380 C C3  . A1AQ3 B .   ? 0.36924 0.38756 0.19530 -0.03799 0.00095  -0.02504 401 A1AQ3 A C3  
2381 C C34 . A1AQ3 B .   ? 0.34994 0.41256 0.22663 -0.02268 0.01710  0.02665  401 A1AQ3 A C34 
2382 C C4  . A1AQ3 B .   ? 0.37273 0.38326 0.20030 -0.04239 -0.00486 -0.03222 401 A1AQ3 A C4  
2383 C C5  . A1AQ3 B .   ? 0.37683 0.39372 0.20426 -0.04889 -0.01603 -0.02912 401 A1AQ3 A C5  
2384 C C6  . A1AQ3 B .   ? 0.37155 0.40174 0.19715 -0.05037 -0.02136 -0.01902 401 A1AQ3 A C6  
2385 C C7  . A1AQ3 B .   ? 0.38374 0.41996 0.20704 -0.04587 -0.01566 -0.01184 401 A1AQ3 A C7  
2386 C C8  . A1AQ3 B .   ? 0.24213 0.31253 0.16065 -0.02634 -0.01829 0.04599  401 A1AQ3 A C8  
2387 C C9  . A1AQ3 B .   ? 0.38851 0.41905 0.21221 -0.03998 -0.00451 -0.01482 401 A1AQ3 A C9  
2388 N N13 . A1AQ3 B .   ? 0.34197 0.38831 0.19803 -0.02539 0.01568  0.00524  401 A1AQ3 A N13 
2389 N N16 . A1AQ3 B .   ? 0.27427 0.33345 0.17052 -0.02689 -0.00717 0.02629  401 A1AQ3 A N16 
2390 N N23 . A1AQ3 B .   ? 0.28286 0.32700 0.17287 -0.04047 -0.02832 0.00150  401 A1AQ3 A N23 
2391 O O11 . A1AQ3 B .   ? 0.34615 0.37224 0.17933 -0.02824 0.01683  -0.01637 401 A1AQ3 A O11 
2392 O O26 . A1AQ3 B .   ? 0.21123 0.25446 0.12599 -0.03056 -0.02205 0.00664  401 A1AQ3 A O26 
2393 O O3  . A1AQ3 B .   ? 0.36326 0.41773 0.24077 -0.01478 0.03601  0.01381  401 A1AQ3 A O3  
2394 O O33 . A1AQ3 B .   ? 0.29387 0.32907 0.15854 -0.02808 0.00557  -0.00501 401 A1AQ3 A O33 
2395 O O38 . A1AQ3 B .   ? 0.34603 0.40605 0.21163 -0.03162 -0.00535 0.02302  401 A1AQ3 A O38 
2396 O O9  . A1AQ3 B .   ? 0.22596 0.30065 0.15540 -0.02653 -0.02635 0.05256  401 A1AQ3 A O9  
# 
