data_8Z3I
# 
_entry.id   8Z3I 
# 
_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   8Z3I         pdb_00008z3i 10.2210/pdb8z3i/pdb 
WWPDB D_1300046956 ?            ?                   
# 
_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       2025-04-23 
_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                        8Z3I 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              yonghw@scut.edu.cn 
_pdbx_contact_author.name_first         YongHua 
_pdbx_contact_author.name_last          Wang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-8790-4357 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Long, Y.T.' 1 ? 
'Lan, D.M.'  2 ? 
'Wang, Y.H.' 3 ? 
# 
_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                     'Crystal Structure of Protein Glutaminase FBPG(Flavobacterium sp.316)' 
_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 'Long, Y.T.' 1 ? 
primary 'Lan, D.M.'  2 ? 
primary 'Wang, Y.H.' 3 ? 
# 
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 'Protein glutaminase domain-containing protein' 35610.859 1   ? ? ? ? 
2 water   nat water                                           18.015    272 ? ? ? ? 
# 
_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       
;MKKNLLKLTLLLGLAIVLGSCNNEQEKNPQEVNPQTSNDYIIGLIKKCDDCEVSTSKTFFYCGIKAGASYVENDSPYLND
IKESISNGTPIKIYFDENEPERIISVVKISNSEEKNWNLNVKYDETPFKTIEDLNRKVSTQKASSFDFTTTEAVNFFNAM
KNKSCAINNQNLCIPFQYANDGCYARAHMMRQHMNYASKDCYKIFAYGNLKVNTSSTGVCGIAWRYHVAPLISVNGVWNV
IDPSLFNQPVTITTWLNKMKYNGGTVATTSYQNSSVYYYDYVSNYTQYDNNYTDTYSTLANYRYRQTSCSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKKNLLKLTLLLGLAIVLGSCNNEQEKNPQEVNPQTSNDYIIGLIKKCDDCEVSTSKTFFYCGIKAGASYVENDSPYLND
IKESISNGTPIKIYFDENEPERIISVVKISNSEEKNWNLNVKYDETPFKTIEDLNRKVSTQKASSFDFTTTEAVNFFNAM
KNKSCAINNQNLCIPFQYANDGCYARAHMMRQHMNYASKDCYKIFAYGNLKVNTSSTGVCGIAWRYHVAPLISVNGVWNV
IDPSLFNQPVTITTWLNKMKYNGGTVATTSYQNSSVYYYDYVSNYTQYDNNYTDTYSTLANYRYRQTSCSFL
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   LYS n 
1 3   LYS n 
1 4   ASN n 
1 5   LEU n 
1 6   LEU n 
1 7   LYS n 
1 8   LEU n 
1 9   THR n 
1 10  LEU n 
1 11  LEU n 
1 12  LEU n 
1 13  GLY n 
1 14  LEU n 
1 15  ALA n 
1 16  ILE n 
1 17  VAL n 
1 18  LEU n 
1 19  GLY n 
1 20  SER n 
1 21  CYS n 
1 22  ASN n 
1 23  ASN n 
1 24  GLU n 
1 25  GLN n 
1 26  GLU n 
1 27  LYS n 
1 28  ASN n 
1 29  PRO n 
1 30  GLN n 
1 31  GLU n 
1 32  VAL n 
1 33  ASN n 
1 34  PRO n 
1 35  GLN n 
1 36  THR n 
1 37  SER n 
1 38  ASN n 
1 39  ASP n 
1 40  TYR n 
1 41  ILE n 
1 42  ILE n 
1 43  GLY n 
1 44  LEU n 
1 45  ILE n 
1 46  LYS n 
1 47  LYS n 
1 48  CYS n 
1 49  ASP n 
1 50  ASP n 
1 51  CYS n 
1 52  GLU n 
1 53  VAL n 
1 54  SER n 
1 55  THR n 
1 56  SER n 
1 57  LYS n 
1 58  THR n 
1 59  PHE n 
1 60  PHE n 
1 61  TYR n 
1 62  CYS n 
1 63  GLY n 
1 64  ILE n 
1 65  LYS n 
1 66  ALA n 
1 67  GLY n 
1 68  ALA n 
1 69  SER n 
1 70  TYR n 
1 71  VAL n 
1 72  GLU n 
1 73  ASN n 
1 74  ASP n 
1 75  SER n 
1 76  PRO n 
1 77  TYR n 
1 78  LEU n 
1 79  ASN n 
1 80  ASP n 
1 81  ILE n 
1 82  LYS n 
1 83  GLU n 
1 84  SER n 
1 85  ILE n 
1 86  SER n 
1 87  ASN n 
1 88  GLY n 
1 89  THR n 
1 90  PRO n 
1 91  ILE n 
1 92  LYS n 
1 93  ILE n 
1 94  TYR n 
1 95  PHE n 
1 96  ASP n 
1 97  GLU n 
1 98  ASN n 
1 99  GLU n 
1 100 PRO n 
1 101 GLU n 
1 102 ARG n 
1 103 ILE n 
1 104 ILE n 
1 105 SER n 
1 106 VAL n 
1 107 VAL n 
1 108 LYS n 
1 109 ILE n 
1 110 SER n 
1 111 ASN n 
1 112 SER n 
1 113 GLU n 
1 114 GLU n 
1 115 LYS n 
1 116 ASN n 
1 117 TRP n 
1 118 ASN n 
1 119 LEU n 
1 120 ASN n 
1 121 VAL n 
1 122 LYS n 
1 123 TYR n 
1 124 ASP n 
1 125 GLU n 
1 126 THR n 
1 127 PRO n 
1 128 PHE n 
1 129 LYS n 
1 130 THR n 
1 131 ILE n 
1 132 GLU n 
1 133 ASP n 
1 134 LEU n 
1 135 ASN n 
1 136 ARG n 
1 137 LYS n 
1 138 VAL n 
1 139 SER n 
1 140 THR n 
1 141 GLN n 
1 142 LYS n 
1 143 ALA n 
1 144 SER n 
1 145 SER n 
1 146 PHE n 
1 147 ASP n 
1 148 PHE n 
1 149 THR n 
1 150 THR n 
1 151 THR n 
1 152 GLU n 
1 153 ALA n 
1 154 VAL n 
1 155 ASN n 
1 156 PHE n 
1 157 PHE n 
1 158 ASN n 
1 159 ALA n 
1 160 MET n 
1 161 LYS n 
1 162 ASN n 
1 163 LYS n 
1 164 SER n 
1 165 CYS n 
1 166 ALA n 
1 167 ILE n 
1 168 ASN n 
1 169 ASN n 
1 170 GLN n 
1 171 ASN n 
1 172 LEU n 
1 173 CYS n 
1 174 ILE n 
1 175 PRO n 
1 176 PHE n 
1 177 GLN n 
1 178 TYR n 
1 179 ALA n 
1 180 ASN n 
1 181 ASP n 
1 182 GLY n 
1 183 CYS n 
1 184 TYR n 
1 185 ALA n 
1 186 ARG n 
1 187 ALA n 
1 188 HIS n 
1 189 MET n 
1 190 MET n 
1 191 ARG n 
1 192 GLN n 
1 193 HIS n 
1 194 MET n 
1 195 ASN n 
1 196 TYR n 
1 197 ALA n 
1 198 SER n 
1 199 LYS n 
1 200 ASP n 
1 201 CYS n 
1 202 TYR n 
1 203 LYS n 
1 204 ILE n 
1 205 PHE n 
1 206 ALA n 
1 207 TYR n 
1 208 GLY n 
1 209 ASN n 
1 210 LEU n 
1 211 LYS n 
1 212 VAL n 
1 213 ASN n 
1 214 THR n 
1 215 SER n 
1 216 SER n 
1 217 THR n 
1 218 GLY n 
1 219 VAL n 
1 220 CYS n 
1 221 GLY n 
1 222 ILE n 
1 223 ALA n 
1 224 TRP n 
1 225 ARG n 
1 226 TYR n 
1 227 HIS n 
1 228 VAL n 
1 229 ALA n 
1 230 PRO n 
1 231 LEU n 
1 232 ILE n 
1 233 SER n 
1 234 VAL n 
1 235 ASN n 
1 236 GLY n 
1 237 VAL n 
1 238 TRP n 
1 239 ASN n 
1 240 VAL n 
1 241 ILE n 
1 242 ASP n 
1 243 PRO n 
1 244 SER n 
1 245 LEU n 
1 246 PHE n 
1 247 ASN n 
1 248 GLN n 
1 249 PRO n 
1 250 VAL n 
1 251 THR n 
1 252 ILE n 
1 253 THR n 
1 254 THR n 
1 255 TRP n 
1 256 LEU n 
1 257 ASN n 
1 258 LYS n 
1 259 MET n 
1 260 LYS n 
1 261 TYR n 
1 262 ASN n 
1 263 GLY n 
1 264 GLY n 
1 265 THR n 
1 266 VAL n 
1 267 ALA n 
1 268 THR n 
1 269 THR n 
1 270 SER n 
1 271 TYR n 
1 272 GLN n 
1 273 ASN n 
1 274 SER n 
1 275 SER n 
1 276 VAL n 
1 277 TYR n 
1 278 TYR n 
1 279 TYR n 
1 280 ASP n 
1 281 TYR n 
1 282 VAL n 
1 283 SER n 
1 284 ASN n 
1 285 TYR n 
1 286 THR n 
1 287 GLN n 
1 288 TYR n 
1 289 ASP n 
1 290 ASN n 
1 291 ASN n 
1 292 TYR n 
1 293 THR n 
1 294 ASP n 
1 295 THR n 
1 296 TYR n 
1 297 SER n 
1 298 THR n 
1 299 LEU n 
1 300 ALA n 
1 301 ASN n 
1 302 TYR n 
1 303 ARG n 
1 304 TYR n 
1 305 ARG n 
1 306 GLN n 
1 307 THR n 
1 308 SER n 
1 309 CYS n 
1 310 SER n 
1 311 PHE n 
1 312 LEU 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                   312 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SY27_02215 
_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      'Flavobacterium sp. 316' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1603293 
_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 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   LYS 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   LEU 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   ?   ?   ?   A . n 
A 1 7   LYS 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   THR 9   9   ?   ?   ?   A . n 
A 1 10  LEU 10  10  ?   ?   ?   A . n 
A 1 11  LEU 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  GLY 13  13  ?   ?   ?   A . n 
A 1 14  LEU 14  14  ?   ?   ?   A . n 
A 1 15  ALA 15  15  ?   ?   ?   A . n 
A 1 16  ILE 16  16  ?   ?   ?   A . n 
A 1 17  VAL 17  17  ?   ?   ?   A . n 
A 1 18  LEU 18  18  ?   ?   ?   A . n 
A 1 19  GLY 19  19  ?   ?   ?   A . n 
A 1 20  SER 20  20  ?   ?   ?   A . n 
A 1 21  CYS 21  21  ?   ?   ?   A . n 
A 1 22  ASN 22  22  ?   ?   ?   A . n 
A 1 23  ASN 23  23  ?   ?   ?   A . n 
A 1 24  GLU 24  24  ?   ?   ?   A . n 
A 1 25  GLN 25  25  ?   ?   ?   A . n 
A 1 26  GLU 26  26  ?   ?   ?   A . n 
A 1 27  LYS 27  27  ?   ?   ?   A . n 
A 1 28  ASN 28  28  ?   ?   ?   A . n 
A 1 29  PRO 29  29  ?   ?   ?   A . n 
A 1 30  GLN 30  30  ?   ?   ?   A . n 
A 1 31  GLU 31  31  ?   ?   ?   A . n 
A 1 32  VAL 32  32  ?   ?   ?   A . n 
A 1 33  ASN 33  33  ?   ?   ?   A . n 
A 1 34  PRO 34  34  ?   ?   ?   A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  SER 37  37  37  SER SER A . n 
A 1 38  ASN 38  38  38  ASN ASN A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ILE 41  41  41  ILE ILE A . n 
A 1 42  ILE 42  42  42  ILE ILE A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  ILE 45  45  45  ILE ILE A . n 
A 1 46  LYS 46  46  46  LYS LYS A . n 
A 1 47  LYS 47  47  47  LYS LYS A . n 
A 1 48  CYS 48  48  48  CYS CYS A . n 
A 1 49  ASP 49  49  49  ASP ASP A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  CYS 51  51  51  CYS CYS A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  PHE 60  60  60  PHE PHE A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  CYS 62  62  62  CYS CYS A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  LYS 65  65  65  LYS LYS A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  ALA 68  68  68  ALA ALA A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  TYR 70  70  70  TYR TYR A . n 
A 1 71  VAL 71  71  71  VAL VAL A . n 
A 1 72  GLU 72  72  72  GLU GLU A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  PRO 76  76  76  PRO PRO A . n 
A 1 77  TYR 77  77  77  TYR TYR A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ASN 79  79  79  ASN ASN A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  ILE 81  81  81  ILE ILE A . n 
A 1 82  LYS 82  82  82  LYS LYS A . n 
A 1 83  GLU 83  83  83  GLU GLU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  GLU 97  97  97  GLU GLU A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 GLU 101 101 101 GLU GLU A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 ILE 103 103 103 ILE ILE A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 LYS 108 108 108 LYS LYS A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 SER 110 110 110 SER SER A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 LYS 115 115 115 LYS LYS A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 TRP 117 117 117 TRP TRP A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ASN 120 120 120 ASN ASN A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LYS 129 129 129 LYS LYS A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ASN 135 135 135 ASN ASN A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 LYS 137 137 ?   ?   ?   A . n 
A 1 138 VAL 138 138 ?   ?   ?   A . n 
A 1 139 SER 139 139 ?   ?   ?   A . n 
A 1 140 THR 140 140 ?   ?   ?   A . n 
A 1 141 GLN 141 141 ?   ?   ?   A . n 
A 1 142 LYS 142 142 ?   ?   ?   A . n 
A 1 143 ALA 143 143 ?   ?   ?   A . n 
A 1 144 SER 144 144 ?   ?   ?   A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 THR 150 150 150 THR THR A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ALA 159 159 159 ALA ALA A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 LYS 161 161 161 LYS LYS A . n 
A 1 162 ASN 162 162 162 ASN ASN A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 SER 164 164 164 SER SER A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 ASN 168 168 168 ASN ASN A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 CYS 173 173 173 CYS CYS A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 PHE 176 176 176 PHE PHE A . n 
A 1 177 GLN 177 177 177 GLN GLN A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 ASP 181 181 181 ASP ASP A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 CYS 183 183 183 CYS CYS A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 HIS 188 188 188 HIS HIS A . n 
A 1 189 MET 189 189 189 MET MET A . n 
A 1 190 MET 190 190 190 MET MET A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 MET 194 194 194 MET MET A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 TYR 196 196 196 TYR TYR A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 LYS 199 199 199 LYS LYS A . n 
A 1 200 ASP 200 200 200 ASP ASP A . n 
A 1 201 CYS 201 201 201 CYS CYS A . n 
A 1 202 TYR 202 202 202 TYR TYR A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 PHE 205 205 205 PHE PHE A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TYR 207 207 207 TYR TYR A . n 
A 1 208 GLY 208 208 208 GLY GLY A . n 
A 1 209 ASN 209 209 209 ASN ASN A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 THR 214 214 214 THR THR A . n 
A 1 215 SER 215 215 215 SER SER A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 GLY 218 218 218 GLY GLY A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 CYS 220 220 220 CYS CYS A . n 
A 1 221 GLY 221 221 221 GLY GLY A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 TRP 224 224 224 TRP TRP A . n 
A 1 225 ARG 225 225 225 ARG ARG A . n 
A 1 226 TYR 226 226 226 TYR TYR A . n 
A 1 227 HIS 227 227 227 HIS HIS A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 ALA 229 229 229 ALA ALA A . n 
A 1 230 PRO 230 230 230 PRO PRO A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 ILE 232 232 232 ILE ILE A . n 
A 1 233 SER 233 233 233 SER SER A . n 
A 1 234 VAL 234 234 234 VAL VAL A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 TRP 238 238 238 TRP TRP A . n 
A 1 239 ASN 239 239 239 ASN ASN A . n 
A 1 240 VAL 240 240 240 VAL VAL A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 PRO 243 243 243 PRO PRO A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ASN 247 247 247 ASN ASN A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 VAL 250 250 250 VAL VAL A . n 
A 1 251 THR 251 251 251 THR THR A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 THR 254 254 254 THR THR A . n 
A 1 255 TRP 255 255 255 TRP TRP A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 ASN 257 257 257 ASN ASN A . n 
A 1 258 LYS 258 258 258 LYS LYS A . n 
A 1 259 MET 259 259 259 MET MET A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
A 1 261 TYR 261 261 261 TYR TYR A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 THR 265 265 265 THR THR A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 ALA 267 267 267 ALA ALA A . n 
A 1 268 THR 268 268 268 THR THR A . n 
A 1 269 THR 269 269 269 THR THR A . n 
A 1 270 SER 270 270 270 SER SER A . n 
A 1 271 TYR 271 271 271 TYR TYR A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 SER 274 274 274 SER SER A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 TYR 277 277 277 TYR TYR A . n 
A 1 278 TYR 278 278 278 TYR TYR A . n 
A 1 279 TYR 279 279 279 TYR TYR A . n 
A 1 280 ASP 280 280 280 ASP ASP A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 VAL 282 282 282 VAL VAL A . n 
A 1 283 SER 283 283 283 SER SER A . n 
A 1 284 ASN 284 284 284 ASN ASN A . n 
A 1 285 TYR 285 285 285 TYR TYR A . n 
A 1 286 THR 286 286 286 THR THR A . n 
A 1 287 GLN 287 287 287 GLN GLN A . n 
A 1 288 TYR 288 288 288 TYR TYR A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 ASN 290 290 290 ASN ASN A . n 
A 1 291 ASN 291 291 291 ASN ASN A . n 
A 1 292 TYR 292 292 292 TYR TYR A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 ASP 294 294 294 ASP ASP A . n 
A 1 295 THR 295 295 295 THR THR A . n 
A 1 296 TYR 296 296 296 TYR TYR A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 THR 298 298 298 THR THR A . n 
A 1 299 LEU 299 299 299 LEU LEU A . n 
A 1 300 ALA 300 300 300 ALA ALA A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 TYR 302 302 302 TYR TYR A . n 
A 1 303 ARG 303 303 303 ARG ARG A . n 
A 1 304 TYR 304 304 304 TYR TYR A . n 
A 1 305 ARG 305 305 305 ARG ARG A . n 
A 1 306 GLN 306 306 306 GLN GLN A . n 
A 1 307 THR 307 307 307 THR THR A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 CYS 309 309 309 CYS CYS A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 PHE 311 311 311 PHE PHE A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
# 
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 HOH 1   401 148 HOH HOH A . 
B 2 HOH 2   402 102 HOH HOH A . 
B 2 HOH 3   403 75  HOH HOH A . 
B 2 HOH 4   404 250 HOH HOH A . 
B 2 HOH 5   405 261 HOH HOH A . 
B 2 HOH 6   406 141 HOH HOH A . 
B 2 HOH 7   407 245 HOH HOH A . 
B 2 HOH 8   408 35  HOH HOH A . 
B 2 HOH 9   409 134 HOH HOH A . 
B 2 HOH 10  410 259 HOH HOH A . 
B 2 HOH 11  411 163 HOH HOH A . 
B 2 HOH 12  412 129 HOH HOH A . 
B 2 HOH 13  413 54  HOH HOH A . 
B 2 HOH 14  414 206 HOH HOH A . 
B 2 HOH 15  415 12  HOH HOH A . 
B 2 HOH 16  416 171 HOH HOH A . 
B 2 HOH 17  417 59  HOH HOH A . 
B 2 HOH 18  418 86  HOH HOH A . 
B 2 HOH 19  419 7   HOH HOH A . 
B 2 HOH 20  420 135 HOH HOH A . 
B 2 HOH 21  421 161 HOH HOH A . 
B 2 HOH 22  422 38  HOH HOH A . 
B 2 HOH 23  423 180 HOH HOH A . 
B 2 HOH 24  424 1   HOH HOH A . 
B 2 HOH 25  425 124 HOH HOH A . 
B 2 HOH 26  426 29  HOH HOH A . 
B 2 HOH 27  427 265 HOH HOH A . 
B 2 HOH 28  428 4   HOH HOH A . 
B 2 HOH 29  429 151 HOH HOH A . 
B 2 HOH 30  430 76  HOH HOH A . 
B 2 HOH 31  431 2   HOH HOH A . 
B 2 HOH 32  432 56  HOH HOH A . 
B 2 HOH 33  433 98  HOH HOH A . 
B 2 HOH 34  434 23  HOH HOH A . 
B 2 HOH 35  435 53  HOH HOH A . 
B 2 HOH 36  436 174 HOH HOH A . 
B 2 HOH 37  437 69  HOH HOH A . 
B 2 HOH 38  438 36  HOH HOH A . 
B 2 HOH 39  439 51  HOH HOH A . 
B 2 HOH 40  440 212 HOH HOH A . 
B 2 HOH 41  441 41  HOH HOH A . 
B 2 HOH 42  442 52  HOH HOH A . 
B 2 HOH 43  443 162 HOH HOH A . 
B 2 HOH 44  444 221 HOH HOH A . 
B 2 HOH 45  445 34  HOH HOH A . 
B 2 HOH 46  446 24  HOH HOH A . 
B 2 HOH 47  447 71  HOH HOH A . 
B 2 HOH 48  448 205 HOH HOH A . 
B 2 HOH 49  449 14  HOH HOH A . 
B 2 HOH 50  450 172 HOH HOH A . 
B 2 HOH 51  451 8   HOH HOH A . 
B 2 HOH 52  452 175 HOH HOH A . 
B 2 HOH 53  453 130 HOH HOH A . 
B 2 HOH 54  454 37  HOH HOH A . 
B 2 HOH 55  455 85  HOH HOH A . 
B 2 HOH 56  456 100 HOH HOH A . 
B 2 HOH 57  457 236 HOH HOH A . 
B 2 HOH 58  458 21  HOH HOH A . 
B 2 HOH 59  459 43  HOH HOH A . 
B 2 HOH 60  460 110 HOH HOH A . 
B 2 HOH 61  461 122 HOH HOH A . 
B 2 HOH 62  462 10  HOH HOH A . 
B 2 HOH 63  463 266 HOH HOH A . 
B 2 HOH 64  464 80  HOH HOH A . 
B 2 HOH 65  465 156 HOH HOH A . 
B 2 HOH 66  466 3   HOH HOH A . 
B 2 HOH 67  467 149 HOH HOH A . 
B 2 HOH 68  468 178 HOH HOH A . 
B 2 HOH 69  469 139 HOH HOH A . 
B 2 HOH 70  470 64  HOH HOH A . 
B 2 HOH 71  471 68  HOH HOH A . 
B 2 HOH 72  472 9   HOH HOH A . 
B 2 HOH 73  473 67  HOH HOH A . 
B 2 HOH 74  474 146 HOH HOH A . 
B 2 HOH 75  475 13  HOH HOH A . 
B 2 HOH 76  476 160 HOH HOH A . 
B 2 HOH 77  477 246 HOH HOH A . 
B 2 HOH 78  478 30  HOH HOH A . 
B 2 HOH 79  479 182 HOH HOH A . 
B 2 HOH 80  480 40  HOH HOH A . 
B 2 HOH 81  481 57  HOH HOH A . 
B 2 HOH 82  482 116 HOH HOH A . 
B 2 HOH 83  483 49  HOH HOH A . 
B 2 HOH 84  484 113 HOH HOH A . 
B 2 HOH 85  485 45  HOH HOH A . 
B 2 HOH 86  486 88  HOH HOH A . 
B 2 HOH 87  487 83  HOH HOH A . 
B 2 HOH 88  488 81  HOH HOH A . 
B 2 HOH 89  489 211 HOH HOH A . 
B 2 HOH 90  490 11  HOH HOH A . 
B 2 HOH 91  491 6   HOH HOH A . 
B 2 HOH 92  492 133 HOH HOH A . 
B 2 HOH 93  493 147 HOH HOH A . 
B 2 HOH 94  494 121 HOH HOH A . 
B 2 HOH 95  495 128 HOH HOH A . 
B 2 HOH 96  496 20  HOH HOH A . 
B 2 HOH 97  497 74  HOH HOH A . 
B 2 HOH 98  498 39  HOH HOH A . 
B 2 HOH 99  499 87  HOH HOH A . 
B 2 HOH 100 500 117 HOH HOH A . 
B 2 HOH 101 501 109 HOH HOH A . 
B 2 HOH 102 502 96  HOH HOH A . 
B 2 HOH 103 503 269 HOH HOH A . 
B 2 HOH 104 504 105 HOH HOH A . 
B 2 HOH 105 505 195 HOH HOH A . 
B 2 HOH 106 506 58  HOH HOH A . 
B 2 HOH 107 507 262 HOH HOH A . 
B 2 HOH 108 508 216 HOH HOH A . 
B 2 HOH 109 509 22  HOH HOH A . 
B 2 HOH 110 510 17  HOH HOH A . 
B 2 HOH 111 511 44  HOH HOH A . 
B 2 HOH 112 512 257 HOH HOH A . 
B 2 HOH 113 513 111 HOH HOH A . 
B 2 HOH 114 514 19  HOH HOH A . 
B 2 HOH 115 515 26  HOH HOH A . 
B 2 HOH 116 516 179 HOH HOH A . 
B 2 HOH 117 517 127 HOH HOH A . 
B 2 HOH 118 518 63  HOH HOH A . 
B 2 HOH 119 519 185 HOH HOH A . 
B 2 HOH 120 520 138 HOH HOH A . 
B 2 HOH 121 521 92  HOH HOH A . 
B 2 HOH 122 522 50  HOH HOH A . 
B 2 HOH 123 523 224 HOH HOH A . 
B 2 HOH 124 524 115 HOH HOH A . 
B 2 HOH 125 525 42  HOH HOH A . 
B 2 HOH 126 526 194 HOH HOH A . 
B 2 HOH 127 527 189 HOH HOH A . 
B 2 HOH 128 528 241 HOH HOH A . 
B 2 HOH 129 529 78  HOH HOH A . 
B 2 HOH 130 530 203 HOH HOH A . 
B 2 HOH 131 531 72  HOH HOH A . 
B 2 HOH 132 532 107 HOH HOH A . 
B 2 HOH 133 533 60  HOH HOH A . 
B 2 HOH 134 534 70  HOH HOH A . 
B 2 HOH 135 535 15  HOH HOH A . 
B 2 HOH 136 536 235 HOH HOH A . 
B 2 HOH 137 537 164 HOH HOH A . 
B 2 HOH 138 538 254 HOH HOH A . 
B 2 HOH 139 539 132 HOH HOH A . 
B 2 HOH 140 540 48  HOH HOH A . 
B 2 HOH 141 541 197 HOH HOH A . 
B 2 HOH 142 542 181 HOH HOH A . 
B 2 HOH 143 543 234 HOH HOH A . 
B 2 HOH 144 544 176 HOH HOH A . 
B 2 HOH 145 545 55  HOH HOH A . 
B 2 HOH 146 546 153 HOH HOH A . 
B 2 HOH 147 547 131 HOH HOH A . 
B 2 HOH 148 548 119 HOH HOH A . 
B 2 HOH 149 549 120 HOH HOH A . 
B 2 HOH 150 550 33  HOH HOH A . 
B 2 HOH 151 551 143 HOH HOH A . 
B 2 HOH 152 552 16  HOH HOH A . 
B 2 HOH 153 553 106 HOH HOH A . 
B 2 HOH 154 554 65  HOH HOH A . 
B 2 HOH 155 555 183 HOH HOH A . 
B 2 HOH 156 556 28  HOH HOH A . 
B 2 HOH 157 557 177 HOH HOH A . 
B 2 HOH 158 558 225 HOH HOH A . 
B 2 HOH 159 559 144 HOH HOH A . 
B 2 HOH 160 560 237 HOH HOH A . 
B 2 HOH 161 561 118 HOH HOH A . 
B 2 HOH 162 562 47  HOH HOH A . 
B 2 HOH 163 563 77  HOH HOH A . 
B 2 HOH 164 564 158 HOH HOH A . 
B 2 HOH 165 565 165 HOH HOH A . 
B 2 HOH 166 566 215 HOH HOH A . 
B 2 HOH 167 567 198 HOH HOH A . 
B 2 HOH 168 568 214 HOH HOH A . 
B 2 HOH 169 569 32  HOH HOH A . 
B 2 HOH 170 570 101 HOH HOH A . 
B 2 HOH 171 571 5   HOH HOH A . 
B 2 HOH 172 572 18  HOH HOH A . 
B 2 HOH 173 573 209 HOH HOH A . 
B 2 HOH 174 574 207 HOH HOH A . 
B 2 HOH 175 575 142 HOH HOH A . 
B 2 HOH 176 576 79  HOH HOH A . 
B 2 HOH 177 577 268 HOH HOH A . 
B 2 HOH 178 578 201 HOH HOH A . 
B 2 HOH 179 579 94  HOH HOH A . 
B 2 HOH 180 580 46  HOH HOH A . 
B 2 HOH 181 581 97  HOH HOH A . 
B 2 HOH 182 582 104 HOH HOH A . 
B 2 HOH 183 583 66  HOH HOH A . 
B 2 HOH 184 584 244 HOH HOH A . 
B 2 HOH 185 585 186 HOH HOH A . 
B 2 HOH 186 586 270 HOH HOH A . 
B 2 HOH 187 587 193 HOH HOH A . 
B 2 HOH 188 588 136 HOH HOH A . 
B 2 HOH 189 589 166 HOH HOH A . 
B 2 HOH 190 590 25  HOH HOH A . 
B 2 HOH 191 591 263 HOH HOH A . 
B 2 HOH 192 592 159 HOH HOH A . 
B 2 HOH 193 593 27  HOH HOH A . 
B 2 HOH 194 594 258 HOH HOH A . 
B 2 HOH 195 595 62  HOH HOH A . 
B 2 HOH 196 596 125 HOH HOH A . 
B 2 HOH 197 597 248 HOH HOH A . 
B 2 HOH 198 598 31  HOH HOH A . 
B 2 HOH 199 599 260 HOH HOH A . 
B 2 HOH 200 600 247 HOH HOH A . 
B 2 HOH 201 601 126 HOH HOH A . 
B 2 HOH 202 602 271 HOH HOH A . 
B 2 HOH 203 603 238 HOH HOH A . 
B 2 HOH 204 604 219 HOH HOH A . 
B 2 HOH 205 605 123 HOH HOH A . 
B 2 HOH 206 606 264 HOH HOH A . 
B 2 HOH 207 607 173 HOH HOH A . 
B 2 HOH 208 608 239 HOH HOH A . 
B 2 HOH 209 609 95  HOH HOH A . 
B 2 HOH 210 610 137 HOH HOH A . 
B 2 HOH 211 611 140 HOH HOH A . 
B 2 HOH 212 612 61  HOH HOH A . 
B 2 HOH 213 613 114 HOH HOH A . 
B 2 HOH 214 614 191 HOH HOH A . 
B 2 HOH 215 615 89  HOH HOH A . 
B 2 HOH 216 616 112 HOH HOH A . 
B 2 HOH 217 617 252 HOH HOH A . 
B 2 HOH 218 618 230 HOH HOH A . 
B 2 HOH 219 619 108 HOH HOH A . 
B 2 HOH 220 620 167 HOH HOH A . 
B 2 HOH 221 621 93  HOH HOH A . 
B 2 HOH 222 622 202 HOH HOH A . 
B 2 HOH 223 623 199 HOH HOH A . 
B 2 HOH 224 624 150 HOH HOH A . 
B 2 HOH 225 625 152 HOH HOH A . 
B 2 HOH 226 626 217 HOH HOH A . 
B 2 HOH 227 627 154 HOH HOH A . 
B 2 HOH 228 628 155 HOH HOH A . 
B 2 HOH 229 629 267 HOH HOH A . 
B 2 HOH 230 630 168 HOH HOH A . 
B 2 HOH 231 631 200 HOH HOH A . 
B 2 HOH 232 632 170 HOH HOH A . 
B 2 HOH 233 633 190 HOH HOH A . 
B 2 HOH 234 634 192 HOH HOH A . 
B 2 HOH 235 635 184 HOH HOH A . 
B 2 HOH 236 636 208 HOH HOH A . 
B 2 HOH 237 637 227 HOH HOH A . 
B 2 HOH 238 638 73  HOH HOH A . 
B 2 HOH 239 639 210 HOH HOH A . 
B 2 HOH 240 640 145 HOH HOH A . 
B 2 HOH 241 641 251 HOH HOH A . 
B 2 HOH 242 642 90  HOH HOH A . 
B 2 HOH 243 643 249 HOH HOH A . 
B 2 HOH 244 644 220 HOH HOH A . 
B 2 HOH 245 645 233 HOH HOH A . 
B 2 HOH 246 646 240 HOH HOH A . 
B 2 HOH 247 647 99  HOH HOH A . 
B 2 HOH 248 648 157 HOH HOH A . 
B 2 HOH 249 649 169 HOH HOH A . 
B 2 HOH 250 650 223 HOH HOH A . 
B 2 HOH 251 651 255 HOH HOH A . 
B 2 HOH 252 652 187 HOH HOH A . 
B 2 HOH 253 653 229 HOH HOH A . 
B 2 HOH 254 654 204 HOH HOH A . 
B 2 HOH 255 655 231 HOH HOH A . 
B 2 HOH 256 656 196 HOH HOH A . 
B 2 HOH 257 657 272 HOH HOH A . 
B 2 HOH 258 658 226 HOH HOH A . 
B 2 HOH 259 659 91  HOH HOH A . 
B 2 HOH 260 660 103 HOH HOH A . 
B 2 HOH 261 661 82  HOH HOH A . 
B 2 HOH 262 662 243 HOH HOH A . 
B 2 HOH 263 663 242 HOH HOH A . 
B 2 HOH 264 664 188 HOH HOH A . 
B 2 HOH 265 665 232 HOH HOH A . 
B 2 HOH 266 666 256 HOH HOH A . 
B 2 HOH 267 667 84  HOH HOH A . 
B 2 HOH 268 668 222 HOH HOH A . 
B 2 HOH 269 669 218 HOH HOH A . 
B 2 HOH 270 670 253 HOH HOH A . 
B 2 HOH 271 671 213 HOH HOH A . 
B 2 HOH 272 672 228 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 52 ? CG  ? A GLU 52 CG  
2 1 Y 1 A GLU 52 ? CD  ? A GLU 52 CD  
3 1 Y 1 A GLU 52 ? OE1 ? A GLU 52 OE1 
4 1 Y 1 A GLU 52 ? OE2 ? A GLU 52 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   ? ? ? 1.9_1692+SVN 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .            2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .            4 
# 
_cell.angle_alpha                  90.0 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.0 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.0 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8Z3I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.338 
_cell.length_a_esd                 ? 
_cell.length_b                     52.455 
_cell.length_b_esd                 ? 
_cell.length_c                     109.467 
_cell.length_c_esd                 ? 
_cell.volume                       294787.492657 
_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                         8Z3I 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8Z3I 
_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             2.07 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.57 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              8.0 
_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    '0.1 M HEPES pH 7.4, 25% (w/v)polyethylene glycol 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.17 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_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                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-04 
_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   0.987 
_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                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8Z3I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.88 
_reflns.d_resolution_low                               50.00 
_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                                     24837 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          1.67 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.88 
_reflns_shell.d_res_low                                     1.91 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             24837 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.844 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               25.5241516965 
_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                                 8Z3I 
_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                            1.88000083544 
_refine.ls_d_res_low                             24.2631499632 
_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                     23357 
_refine.ls_number_reflns_R_free                  3193 
_refine.ls_number_reflns_R_work                  33844 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    79.7970439953 
_refine.ls_percent_reflns_R_free                 8.62110862111 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.165299339158 
_refine.ls_R_factor_R_free                       0.207612183786 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.161278379226 
_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                          1.36394567655 
_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       ? 
_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             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9 
_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                 20.9363112294 
_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                            0.170167632604 
_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                       1.88000083544 
_refine_hist.d_res_low                        24.2631499632 
_refine_hist.number_atoms_solvent             272 
_refine_hist.number_atoms_total               2449 
_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        2177 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.00689828774662 ? 2233 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.895306684911   ? 3031 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.036493412971   ? 327  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.00443518100834 ? 389  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.1140185449    ? 795  ? 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' 1.88000083544 1.9081        . . 47  519  28.2717282717 . . . . 0.260397115202 . . . . . . . . . . . 
0.297111815284 
'X-RAY DIFFRACTION' 1.9081        1.9379        . . 62  650  35.2126607319 . . . . 0.232552389559 . . . . . . . . . . . 
0.300131185257 
'X-RAY DIFFRACTION' 1.9379        1.9696        . . 76  764  41.958041958  . . . . 0.220113983743 . . . . . . . . . . . 
0.256690165444 
'X-RAY DIFFRACTION' 1.9696        2.0036        . . 77  893  48.3549351944 . . . . 0.207492359946 . . . . . . . . . . . 
0.249129192234 
'X-RAY DIFFRACTION' 2.0036        2.04          . . 94  994  53.4906588004 . . . . 0.19524594043  . . . . . . . . . . . 
0.263224607581 
'X-RAY DIFFRACTION' 2.04          2.0792        . . 98  1064 57.4110671937 . . . . 0.202225004091 . . . . . . . . . . . 
0.234352705995 
'X-RAY DIFFRACTION' 2.0792        2.1216        . . 112 1160 63.1578947368 . . . . 0.185082973929 . . . . . . . . . . . 
0.198718980721 
'X-RAY DIFFRACTION' 2.1216        2.1677        . . 106 1274 68.4523809524 . . . . 0.173245489161 . . . . . . . . . . . 
0.247959802345 
'X-RAY DIFFRACTION' 2.1677        2.2181        . . 144 1329 73.0292513634 . . . . 0.175216424977 . . . . . . . . . . . 
0.219928589425 
'X-RAY DIFFRACTION' 2.2181        2.2735        . . 142 1553 83.1697742885 . . . . 0.17186172979  . . . . . . . . . . . 
0.22173007722  
'X-RAY DIFFRACTION' 2.2735        2.335         . . 165 1644 90.45         . . . . 0.170418967478 . . . . . . . . . . . 
0.241731751892 
'X-RAY DIFFRACTION' 2.335         2.4036        . . 157 1770 95.2545724172 . . . . 0.175592257248 . . . . . . . . . . . 
0.219656738263 
'X-RAY DIFFRACTION' 2.4036        2.4811        . . 172 1840 99.4071146245 . . . . 0.176516720916 . . . . . . . . . . . 
0.255272238944 
'X-RAY DIFFRACTION' 2.4811        2.5697        . . 167 1836 99.850448654  . . . . 0.173762342418 . . . . . . . . . . . 
0.242686348195 
'X-RAY DIFFRACTION' 2.5697        2.6725        . . 179 1828 100.0         . . . . 0.176204219349 . . . . . . . . . . . 
0.210246850902 
'X-RAY DIFFRACTION' 2.6725        2.7939        . . 170 1839 99.9502487562 . . . . 0.170162969558 . . . . . . . . . . . 
0.241687893371 
'X-RAY DIFFRACTION' 2.7939        2.941         . . 178 1865 99.902200489  . . . . 0.166971065334 . . . . . . . . . . . 
0.243401947552 
'X-RAY DIFFRACTION' 2.941         3.1249        . . 177 1825 99.9001996008 . . . . 0.158091330468 . . . . . . . . . . . 
0.194423469842 
'X-RAY DIFFRACTION' 3.1249        3.3656        . . 177 1858 99.8527968597 . . . . 0.147075311617 . . . . . . . . . . . 
0.205287380696 
'X-RAY DIFFRACTION' 3.3656        3.7032        . . 183 1829 99.7026759167 . . . . 0.141855451251 . . . . . . . . . . . 
0.186046610607 
'X-RAY DIFFRACTION' 3.7032        4.2366        . . 170 1842 99.554675903  . . . . 0.131568670552 . . . . . . . . . . . 
0.182288576707 
'X-RAY DIFFRACTION' 4.2366        5.3284        . . 169 1835 99.6023856859 . . . . 0.127786004626 . . . . . . . . . . . 
0.149055134299 
'X-RAY DIFFRACTION' 5.3284        24.2631499632 . . 171 1833 99.0118577075 . . . . 0.174753345236 . . . . . . . . . . . 
0.194165668166 
# 
_struct.entry_id                     8Z3I 
_struct.title                        'Crystal Structure of Protein Glutaminase FBPG(Flavobacterium sp.316)' 
_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        8Z3I 
_struct_keywords.text            'Protein Glutaminase, HYDROLASE' 
_struct_keywords.pdbx_keywords   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 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A0D6TQX4_9FLAO 
_struct_ref.pdbx_db_accession          A0A0D6TQX4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKKNLLKLTLLLGLAIVLGSCNNEQEKNPQEVNPQTSNDYIIGLIKKCDDCEVSTSKTFFYCGIKAGASYVENDSPYLND
IKESISNGTPIKIYFDENEPERIISVVKISNSEEKNWNLNVKYDETPFKTIEDLNRKVSTQKASSFDFTTTEAVNFFNAM
KNKSCAINNQNLCIPFQYANDGCYARAHMMRQHMNYASKDCYKIFAYGNLKVNTSSTGVCGIAWRYHVAPLISVNGVWNV
IDPSLFNQPVTITTWLNKMKYNGGTVATTSYQNSSVYYYDYVSNYTQYDNNYTDTYSTLANYRYRQTSCSF
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8Z3I 
_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                 311 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             A0A0D6TQX4 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  311 
_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       311 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             8Z3I 
_struct_ref_seq_dif.mon_id                       LEU 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      312 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   A0A0D6TQX4 
_struct_ref_seq_dif.db_mon_id                    ? 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          ? 
_struct_ref_seq_dif.details                      'expression tag' 
_struct_ref_seq_dif.pdbx_auth_seq_num            312 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            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 TYR A 77  ? GLY A 88  ? TYR A 77  GLY A 88  1 ? 12 
HELX_P HELX_P2 AA2 SER A 110 ? LEU A 119 ? SER A 110 LEU A 119 1 ? 10 
HELX_P HELX_P3 AA3 THR A 130 ? ASN A 135 ? THR A 130 ASN A 135 1 ? 6  
HELX_P HELX_P4 AA4 THR A 149 ? ASN A 162 ? THR A 149 ASN A 162 1 ? 14 
HELX_P HELX_P5 AA5 GLY A 182 ? ALA A 197 ? GLY A 182 ALA A 197 1 ? 16 
HELX_P HELX_P6 AA6 ILE A 252 ? MET A 259 ? ILE A 252 MET A 259 1 ? 8  
HELX_P HELX_P7 AA7 LYS A 260 ? GLY A 264 ? LYS A 260 GLY A 264 5 ? 5  
HELX_P HELX_P8 AA8 TYR A 292 ? ARG A 303 ? TYR A 292 ARG A 303 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_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 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_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 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 48  SG ? ? ? 1_555 A CYS 51  SG ? ? A CYS 48  A CYS 51  1_555 ? ? ? ? ? ? ? 2.035 ? ? 
disulf2 disulf ? ? A CYS 165 SG ? ? ? 1_555 A CYS 173 SG ? ? A CYS 165 A CYS 173 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
disulf3 disulf ? ? A CYS 220 SG ? ? ? 1_555 A CYS 309 SG ? ? A CYS 220 A CYS 309 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 48  ? CYS A 51  ? CYS A 48  ? 1_555 CYS A 51  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 165 ? CYS A 173 ? CYS A 165 ? 1_555 CYS A 173 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 220 ? CYS A 309 ? CYS A 220 ? 1_555 CYS A 309 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? 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 TYR A 40  ? GLY A 43  ? TYR A 40  GLY A 43  
AA1 2 ILE A 91  ? ASP A 96  ? ILE A 91  ASP A 96  
AA1 3 GLU A 99  ? VAL A 107 ? GLU A 99  VAL A 107 
AA2 1 ILE A 45  ? LYS A 47  ? ILE A 45  LYS A 47  
AA2 2 LYS A 57  ? CYS A 62  ? LYS A 57  CYS A 62  
AA2 3 SER A 69  ? GLU A 72  ? SER A 69  GLU A 72  
AA3 1 VAL A 121 ? TYR A 123 ? VAL A 121 TYR A 123 
AA3 2 TYR A 285 ? TYR A 288 ? TYR A 285 TYR A 288 
AA3 3 VAL A 276 ? TYR A 279 ? VAL A 276 TYR A 279 
AA4 1 ASP A 147 ? PHE A 148 ? ASP A 147 PHE A 148 
AA4 2 GLY A 221 ? VAL A 234 ? GLY A 221 VAL A 234 
AA4 3 VAL A 237 ? VAL A 240 ? VAL A 237 VAL A 240 
AA4 4 VAL A 250 ? THR A 251 ? VAL A 250 THR A 251 
AA5 1 ASP A 147 ? PHE A 148 ? ASP A 147 PHE A 148 
AA5 2 GLY A 221 ? VAL A 234 ? GLY A 221 VAL A 234 
AA5 3 TYR A 202 ? ASN A 213 ? TYR A 202 ASN A 213 
AA5 4 THR A 265 ? ASN A 273 ? THR A 265 ASN A 273 
# 
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 N ILE A 41  ? N ILE A 41  O ILE A 93  ? O ILE A 93  
AA1 2 3 N TYR A 94  ? N TYR A 94  O SER A 105 ? O SER A 105 
AA2 1 2 N LYS A 46  ? N LYS A 46  O TYR A 61  ? O TYR A 61  
AA2 2 3 N PHE A 60  ? N PHE A 60  O SER A 69  ? O SER A 69  
AA3 1 2 N LYS A 122 ? N LYS A 122 O THR A 286 ? O THR A 286 
AA3 2 3 O GLN A 287 ? O GLN A 287 N TYR A 278 ? N TYR A 278 
AA4 1 2 N PHE A 148 ? N PHE A 148 O SER A 233 ? O SER A 233 
AA4 2 3 N ILE A 232 ? N ILE A 232 O ASN A 239 ? O ASN A 239 
AA4 3 4 N VAL A 240 ? N VAL A 240 O VAL A 250 ? O VAL A 250 
AA5 1 2 N PHE A 148 ? N PHE A 148 O SER A 233 ? O SER A 233 
AA5 2 3 O LEU A 231 ? O LEU A 231 N TYR A 202 ? N TYR A 202 
AA5 3 4 N PHE A 205 ? N PHE A 205 O SER A 270 ? O SER A 270 
# 
_pdbx_entry_details.entry_id                   8Z3I 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_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 403 ? ? O A HOH 610 ? ? 1.87 
2 1 O   A HOH 461 ? ? O A HOH 488 ? ? 1.89 
3 1 O   A HOH 671 ? ? O A HOH 672 ? ? 1.91 
4 1 O   A HOH 541 ? ? O A HOH 607 ? ? 2.00 
5 1 ND2 A ASN 116 ? ? O A HOH 401 ? ? 2.02 
6 1 OD2 A ASP 74  ? ? O A HOH 402 ? ? 2.08 
7 1 OE2 A GLU 114 ? ? O A HOH 403 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     562 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     644 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_555 
_pdbx_validate_symm_contact.dist              2.06 
# 
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 GLU A 99  ? ? -150.81 87.99 
2 1 ASN A 135 ? ? -66.02  6.71  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -15.8152513496 -10.0452902415 34.84483675   0.0869179951602 ? -0.0129063618291  ? 0.0518699218827  
? 0.18676015677   ? 0.0161614840456   ? 0.186710241708  ? 1.37549202184   ? 0.544559647444  ? -0.554837308567 ? 0.835523320264 ? 
-0.0434284319247 ? 1.12366525009  ? 0.0478310278701   ? -0.212397874265 ? -0.141203647863  ? 0.035220856961  ? 0.0308213682017  ? 
0.509502820103  ? -0.025579735824  ? -0.113934302196 ? -0.00504404280215 ? 
2 'X-RAY DIFFRACTION' ? refined -7.97101682238 -9.97481675002 38.2059778932 0.129929625334  ? -0.00177755257339 ? 0.0275659106528  
? 0.12422935676   ? -0.0137192945512  ? 0.0955316491574 ? 1.07502436446   ? 0.257249750477  ? 0.205526472227  ? 1.06551578653  ? 
-0.343180426853  ? 0.776182158759 ? 0.0412873474927   ? -0.131852968242 ? -0.0829488396444 ? 0.277879195103  ? 0.00341861637796 ? 
0.0406474702754 ? -0.0228248977051 ? -0.100029986232 ? -0.0194874110797  ? 
3 'X-RAY DIFFRACTION' ? refined -8.032085796   9.44766195433  9.99306795855 0.414913718316  ? 0.00699917878339  ? -0.0275252884577 
? 0.239670656347  ? 0.0406373553549   ? 0.257431524077  ? 0.0553984839094 ? 0.0496127589288 ? 0.0792869213435 ? 1.82128351343  ? 
1.94082598098    ? 2.92640853859  ? -0.094647616406   ? 0.127897248831  ? 0.144538118881   ? -0.241155361271 ? -0.0384932350253 ? 
0.148664152652  ? -0.20132126782   ? -0.142288200945 ? -0.0342194123681  ? 
4 'X-RAY DIFFRACTION' ? refined -12.7854484004 -6.97420176014 14.7367932327 0.118500245685  ? 0.00201624072026  ? -0.0700269545341 
? 0.0936013666051 ? -0.00367078392163 ? 0.114904134948  ? 0.817397228097  ? -0.441895166186 ? 0.0934840240657 ? 1.39877787994  ? 
-0.132387383065  ? 0.911231711047 ? 0.000454840660123 ? 0.0645188557247 ? 0.00119674808129 ? -0.339721693379 ? -0.030001786149  ? 
0.315163768228  ? 0.0465645119311  ? -0.047189394322 ? 0.0176864381059   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   35  through   68 )
;
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid   69  through  123 )
;
3 'X-RAY DIFFRACTION' 3 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  124  through  149 )
;
4 'X-RAY DIFFRACTION' 4 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid  150  through  312 )
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       672 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.15 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A LYS 2   ? A LYS 2   
3  1 Y 1 A LYS 3   ? A LYS 3   
4  1 Y 1 A ASN 4   ? A ASN 4   
5  1 Y 1 A LEU 5   ? A LEU 5   
6  1 Y 1 A LEU 6   ? A LEU 6   
7  1 Y 1 A LYS 7   ? A LYS 7   
8  1 Y 1 A LEU 8   ? A LEU 8   
9  1 Y 1 A THR 9   ? A THR 9   
10 1 Y 1 A LEU 10  ? A LEU 10  
11 1 Y 1 A LEU 11  ? A LEU 11  
12 1 Y 1 A LEU 12  ? A LEU 12  
13 1 Y 1 A GLY 13  ? A GLY 13  
14 1 Y 1 A LEU 14  ? A LEU 14  
15 1 Y 1 A ALA 15  ? A ALA 15  
16 1 Y 1 A ILE 16  ? A ILE 16  
17 1 Y 1 A VAL 17  ? A VAL 17  
18 1 Y 1 A LEU 18  ? A LEU 18  
19 1 Y 1 A GLY 19  ? A GLY 19  
20 1 Y 1 A SER 20  ? A SER 20  
21 1 Y 1 A CYS 21  ? A CYS 21  
22 1 Y 1 A ASN 22  ? A ASN 22  
23 1 Y 1 A ASN 23  ? A ASN 23  
24 1 Y 1 A GLU 24  ? A GLU 24  
25 1 Y 1 A GLN 25  ? A GLN 25  
26 1 Y 1 A GLU 26  ? A GLU 26  
27 1 Y 1 A LYS 27  ? A LYS 27  
28 1 Y 1 A ASN 28  ? A ASN 28  
29 1 Y 1 A PRO 29  ? A PRO 29  
30 1 Y 1 A GLN 30  ? A GLN 30  
31 1 Y 1 A GLU 31  ? A GLU 31  
32 1 Y 1 A VAL 32  ? A VAL 32  
33 1 Y 1 A ASN 33  ? A ASN 33  
34 1 Y 1 A PRO 34  ? A PRO 34  
35 1 Y 1 A LYS 137 ? A LYS 137 
36 1 Y 1 A VAL 138 ? A VAL 138 
37 1 Y 1 A SER 139 ? A SER 139 
38 1 Y 1 A THR 140 ? A THR 140 
39 1 Y 1 A GLN 141 ? A GLN 141 
40 1 Y 1 A LYS 142 ? A LYS 142 
41 1 Y 1 A ALA 143 ? A ALA 143 
42 1 Y 1 A SER 144 ? A SER 144 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8Z3I 
_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]   0.019479 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019064 
_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]   0.009135 
_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_b1 
_atom_type.scat_Cromer_Mann_b2 
_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   . GLN A 1 35  ? -10.75234 -26.33049 41.50844 1.000 45.33136 ? 35  GLN A N   1 
ATOM   2    C CA  . GLN A 1 35  ? -10.88763 -25.89884 40.12071 1.000 41.64931 ? 35  GLN A CA  1 
ATOM   3    C C   . GLN A 1 35  ? -9.59414  -25.31313 39.57948 1.000 41.02775 ? 35  GLN A C   1 
ATOM   4    O O   . GLN A 1 35  ? -8.95949  -24.47414 40.22413 1.000 41.71227 ? 35  GLN A O   1 
ATOM   5    C CB  . GLN A 1 35  ? -12.00427 -24.86993 39.97198 1.000 44.36389 ? 35  GLN A CB  1 
ATOM   6    C CG  . GLN A 1 35  ? -13.29857 -25.45824 39.45950 1.000 56.18282 ? 35  GLN A CG  1 
ATOM   7    C CD  . GLN A 1 35  ? -14.16954 -24.43133 38.77479 1.000 62.49036 ? 35  GLN A CD  1 
ATOM   8    O OE1 . GLN A 1 35  ? -14.95468 -23.73563 39.42180 1.000 60.07691 ? 35  GLN A OE1 1 
ATOM   9    N NE2 . GLN A 1 35  ? -14.03501 -24.32764 37.45353 1.000 64.86869 ? 35  GLN A NE2 1 
ATOM   10   N N   . THR A 1 36  ? -9.21645  -25.76219 38.38648 1.000 34.15113 ? 36  THR A N   1 
ATOM   11   C CA  . THR A 1 36  ? -8.01010  -25.28531 37.72323 1.000 29.93280 ? 36  THR A CA  1 
ATOM   12   C C   . THR A 1 36  ? -8.36031  -24.75598 36.35434 1.000 22.08055 ? 36  THR A C   1 
ATOM   13   O O   . THR A 1 36  ? -9.39838  -25.10874 35.79689 1.000 26.78601 ? 36  THR A O   1 
ATOM   14   C CB  . THR A 1 36  ? -6.95368  -26.39974 37.57375 1.000 32.06794 ? 36  THR A CB  1 
ATOM   15   O OG1 . THR A 1 36  ? -7.46463  -27.43252 36.71052 1.000 26.88109 ? 36  THR A OG1 1 
ATOM   16   C CG2 . THR A 1 36  ? -6.61116  -26.99011 38.93830 1.000 35.87665 ? 36  THR A CG2 1 
ATOM   17   N N   . SER A 1 37  ? -7.48160  -23.92465 35.80855 1.000 21.85083 ? 37  SER A N   1 
ATOM   18   C CA  . SER A 1 37  ? -7.68577  -23.34536 34.48947 1.000 23.89773 ? 37  SER A CA  1 
ATOM   19   C C   . SER A 1 37  ? -6.39489  -22.77387 33.91701 1.000 25.03158 ? 37  SER A C   1 
ATOM   20   O O   . SER A 1 37  ? -5.57960  -22.22074 34.65044 1.000 20.89348 ? 37  SER A O   1 
ATOM   21   C CB  . SER A 1 37  ? -8.74779  -22.24346 34.55489 1.000 19.55767 ? 37  SER A CB  1 
ATOM   22   O OG  . SER A 1 37  ? -8.79754  -21.52347 33.34286 1.000 24.35978 ? 37  SER A OG  1 
ATOM   23   N N   . ASN A 1 38  ? -6.22103  -22.89428 32.60172 1.000 18.73053 ? 38  ASN A N   1 
ATOM   24   C CA  . ASN A 1 38  ? -5.15057  -22.19216 31.91211 1.000 12.93289 ? 38  ASN A CA  1 
ATOM   25   C C   . ASN A 1 38  ? -5.65003  -20.91239 31.24074 1.000 18.63718 ? 38  ASN A C   1 
ATOM   26   O O   . ASN A 1 38  ? -4.92555  -20.28800 30.48247 1.000 19.09185 ? 38  ASN A O   1 
ATOM   27   C CB  . ASN A 1 38  ? -4.49318  -23.11273 30.88120 1.000 15.26493 ? 38  ASN A CB  1 
ATOM   28   C CG  . ASN A 1 38  ? -3.86603  -24.33228 31.52614 1.000 21.57329 ? 38  ASN A CG  1 
ATOM   29   O OD1 . ASN A 1 38  ? -3.32660  -24.24797 32.62935 1.000 21.21903 ? 38  ASN A OD1 1 
ATOM   30   N ND2 . ASN A 1 38  ? -3.97798  -25.47662 30.87168 1.000 20.84876 ? 38  ASN A ND2 1 
ATOM   31   N N   . ASP A 1 39  ? -6.88309  -20.52062 31.53620 1.000 12.93088 ? 39  ASP A N   1 
ATOM   32   C CA  . ASP A 1 39  ? -7.48003  -19.33262 30.93316 1.000 13.30330 ? 39  ASP A CA  1 
ATOM   33   C C   . ASP A 1 39  ? -7.36510  -18.15526 31.88433 1.000 15.74832 ? 39  ASP A C   1 
ATOM   34   O O   . ASP A 1 39  ? -8.16846  -18.01206 32.80479 1.000 12.30402 ? 39  ASP A O   1 
ATOM   35   C CB  . ASP A 1 39  ? -8.95574  -19.57817 30.57192 1.000 11.89403 ? 39  ASP A CB  1 
ATOM   36   C CG  . ASP A 1 39  ? -9.61444  -18.36810 29.90607 1.000 14.17660 ? 39  ASP A CG  1 
ATOM   37   O OD1 . ASP A 1 39  ? -8.89370  -17.44110 29.45468 1.000 16.39999 ? 39  ASP A OD1 1 
ATOM   38   O OD2 . ASP A 1 39  ? -10.86502 -18.35331 29.82243 1.000 17.20072 ? 39  ASP A OD2 1 
ATOM   39   N N   . TYR A 1 40  ? -6.35293  -17.32014 31.67080 1.000 17.42672 ? 40  TYR A N   1 
ATOM   40   C CA  . TYR A 1 40  ? -6.18774  -16.12803 32.49622 1.000 13.50782 ? 40  TYR A CA  1 
ATOM   41   C C   . TYR A 1 40  ? -5.89524  -14.89726 31.66574 1.000 14.59319 ? 40  TYR A C   1 
ATOM   42   O O   . TYR A 1 40  ? -5.40963  -14.98570 30.52996 1.000 13.55169 ? 40  TYR A O   1 
ATOM   43   C CB  . TYR A 1 40  ? -5.07522  -16.33105 33.53847 1.000 14.53102 ? 40  TYR A CB  1 
ATOM   44   C CG  . TYR A 1 40  ? -3.69348  -16.57751 32.97466 1.000 19.51739 ? 40  TYR A CG  1 
ATOM   45   C CD1 . TYR A 1 40  ? -2.82931  -15.51870 32.69016 1.000 19.21905 ? 40  TYR A CD1 1 
ATOM   46   C CD2 . TYR A 1 40  ? -3.23926  -17.87353 32.74652 1.000 24.89740 ? 40  TYR A CD2 1 
ATOM   47   C CE1 . TYR A 1 40  ? -1.54745  -15.75074 32.17767 1.000 25.97760 ? 40  TYR A CE1 1 
ATOM   48   C CE2 . TYR A 1 40  ? -1.96730  -18.11682 32.23441 1.000 22.74138 ? 40  TYR A CE2 1 
ATOM   49   C CZ  . TYR A 1 40  ? -1.12540  -17.05060 31.95770 1.000 33.73746 ? 40  TYR A CZ  1 
ATOM   50   O OH  . TYR A 1 40  ? 0.13160   -17.28800 31.45159 1.000 37.58884 ? 40  TYR A OH  1 
ATOM   51   N N   . ILE A 1 41  ? -6.19336  -13.73963 32.23783 1.000 14.52720 ? 41  ILE A N   1 
ATOM   52   C CA  . ILE A 1 41  ? -5.66527  -12.48677 31.70852 1.000 15.23511 ? 41  ILE A CA  1 
ATOM   53   C C   . ILE A 1 41  ? -5.12118  -11.61971 32.84202 1.000 18.86660 ? 41  ILE A C   1 
ATOM   54   O O   . ILE A 1 41  ? -5.42168  -11.85542 34.01384 1.000 18.17830 ? 41  ILE A O   1 
ATOM   55   C CB  . ILE A 1 41  ? -6.73018  -11.65771 30.93404 1.000 12.78087 ? 41  ILE A CB  1 
ATOM   56   C CG1 . ILE A 1 41  ? -7.87714  -11.25649 31.85788 1.000 12.47496 ? 41  ILE A CG1 1 
ATOM   57   C CG2 . ILE A 1 41  ? -7.22733  -12.40474 29.70788 1.000 24.34853 ? 41  ILE A CG2 1 
ATOM   58   C CD1 . ILE A 1 41  ? -8.78650  -10.22285 31.28711 1.000 24.98957 ? 41  ILE A CD1 1 
ATOM   59   N N   . ILE A 1 42  ? -4.32601  -10.61820 32.47108 1.000 14.24949 ? 42  ILE A N   1 
ATOM   60   C CA  . ILE A 1 42  ? -3.84800  -9.59961  33.39808 1.000 16.66144 ? 42  ILE A CA  1 
ATOM   61   C C   . ILE A 1 42  ? -4.42366  -8.24224  32.99206 1.000 17.08285 ? 42  ILE A C   1 
ATOM   62   O O   . ILE A 1 42  ? -4.28870  -7.81916  31.84227 1.000 11.38949 ? 42  ILE A O   1 
ATOM   63   C CB  . ILE A 1 42  ? -2.31150  -9.52371  33.41428 1.000 16.84365 ? 42  ILE A CB  1 
ATOM   64   C CG1 . ILE A 1 42  ? -1.71654  -10.79897 34.00526 1.000 12.92781 ? 42  ILE A CG1 1 
ATOM   65   C CG2 . ILE A 1 42  ? -1.83127  -8.32791  34.23426 1.000 15.14877 ? 42  ILE A CG2 1 
ATOM   66   C CD1 . ILE A 1 42  ? -0.18941  -10.81747 33.95006 1.000 17.76781 ? 42  ILE A CD1 1 
ATOM   67   N N   . GLY A 1 43  ? -5.07982  -7.56143  33.92112 1.000 11.83482 ? 43  GLY A N   1 
ATOM   68   C CA  . GLY A 1 43  ? -5.60162  -6.24938  33.61137 1.000 18.46758 ? 43  GLY A CA  1 
ATOM   69   C C   . GLY A 1 43  ? -6.39727  -5.66110  34.74641 1.000 16.27581 ? 43  GLY A C   1 
ATOM   70   O O   . GLY A 1 43  ? -6.45571  -6.23364  35.83808 1.000 14.87983 ? 43  GLY A O   1 
ATOM   71   N N   . LEU A 1 44  ? -6.99320  -4.50321  34.48140 1.000 15.22342 ? 44  LEU A N   1 
ATOM   72   C CA  . LEU A 1 44  ? -7.89417  -3.84905  35.42805 1.000 13.09920 ? 44  LEU A CA  1 
ATOM   73   C C   . LEU A 1 44  ? -9.24907  -4.52546  35.43077 1.000 15.66585 ? 44  LEU A C   1 
ATOM   74   O O   . LEU A 1 44  ? -9.67144  -5.09227  34.42145 1.000 22.52618 ? 44  LEU A O   1 
ATOM   75   C CB  . LEU A 1 44  ? -8.08770  -2.37836  35.07237 1.000 16.74224 ? 44  LEU A CB  1 
ATOM   76   C CG  . LEU A 1 44  ? -6.83243  -1.53046  34.95519 1.000 18.07321 ? 44  LEU A CG  1 
ATOM   77   C CD1 . LEU A 1 44  ? -7.19597  -0.17390  34.35181 1.000 22.80438 ? 44  LEU A CD1 1 
ATOM   78   C CD2 . LEU A 1 44  ? -6.19869  -1.37956  36.32336 1.000 14.42014 ? 44  LEU A CD2 1 
ATOM   79   N N   . ILE A 1 45  ? -9.93102  -4.44909  36.56343 1.000 13.78165 ? 45  ILE A N   1 
ATOM   80   C CA  . ILE A 1 45  ? -11.30750 -4.88758  36.65524 1.000 14.60286 ? 45  ILE A CA  1 
ATOM   81   C C   . ILE A 1 45  ? -12.17371 -3.65618  36.87189 1.000 20.72955 ? 45  ILE A C   1 
ATOM   82   O O   . ILE A 1 45  ? -11.78348 -2.74940  37.60272 1.000 18.10260 ? 45  ILE A O   1 
ATOM   83   C CB  . ILE A 1 45  ? -11.53885 -5.90612  37.81559 1.000 23.26918 ? 45  ILE A CB  1 
ATOM   84   C CG1 . ILE A 1 45  ? -10.69873 -7.15796  37.62539 1.000 33.42039 ? 45  ILE A CG1 1 
ATOM   85   C CG2 . ILE A 1 45  ? -12.99696 -6.33109  37.88108 1.000 18.55209 ? 45  ILE A CG2 1 
ATOM   86   C CD1 . ILE A 1 45  ? -10.96987 -8.23410  38.67639 1.000 37.11710 ? 45  ILE A CD1 1 
ATOM   87   N N   . LYS A 1 46  ? -13.33118 -3.62046  36.21276 1.000 19.27044 ? 46  LYS A N   1 
ATOM   88   C CA  . LYS A 1 46  ? -14.32085 -2.56311  36.42026 1.000 25.32884 ? 46  LYS A CA  1 
ATOM   89   C C   . LYS A 1 46  ? -15.65771 -3.21295  36.72941 1.000 20.69108 ? 46  LYS A C   1 
ATOM   90   O O   . LYS A 1 46  ? -15.98501 -4.25237  36.16537 1.000 19.44355 ? 46  LYS A O   1 
ATOM   91   C CB  . LYS A 1 46  ? -14.46083 -1.65442  35.18776 1.000 25.48811 ? 46  LYS A CB  1 
ATOM   92   C CG  . LYS A 1 46  ? -13.17492 -0.97470  34.73177 1.000 39.01772 ? 46  LYS A CG  1 
ATOM   93   C CD  . LYS A 1 46  ? -12.56944 -0.08138  35.81712 1.000 43.24573 ? 46  LYS A CD  1 
ATOM   94   C CE  . LYS A 1 46  ? -11.27129 0.56319   35.33338 1.000 42.79098 ? 46  LYS A CE  1 
ATOM   95   N NZ  . LYS A 1 46  ? -10.44230 1.11938   36.44948 1.000 46.82242 ? 46  LYS A NZ  1 
ATOM   96   N N   . LYS A 1 47  ? -16.42079 -2.61379  37.63543 1.000 24.08766 ? 47  LYS A N   1 
ATOM   97   C CA  . LYS A 1 47  ? -17.78140 -3.06914  37.88436 1.000 26.88546 ? 47  LYS A CA  1 
ATOM   98   C C   . LYS A 1 47  ? -18.59148 -2.88807  36.60512 1.000 23.47670 ? 47  LYS A C   1 
ATOM   99   O O   . LYS A 1 47  ? -18.35659 -1.94456  35.86457 1.000 23.36458 ? 47  LYS A O   1 
ATOM   100  C CB  . LYS A 1 47  ? -18.40945 -2.29177  39.05041 1.000 30.49258 ? 47  LYS A CB  1 
ATOM   101  C CG  . LYS A 1 47  ? -19.78357 -2.77880  39.44542 1.000 41.28811 ? 47  LYS A CG  1 
ATOM   102  C CD  . LYS A 1 47  ? -19.78090 -4.27879  39.70840 1.000 46.59004 ? 47  LYS A CD  1 
ATOM   103  C CE  . LYS A 1 47  ? -21.19970 -4.83377  39.76865 1.000 52.95519 ? 47  LYS A CE  1 
ATOM   104  N NZ  . LYS A 1 47  ? -21.87337 -4.48930  41.05587 1.000 61.46034 ? 47  LYS A NZ  1 
ATOM   105  N N   . CYS A 1 48  ? -19.51444 -3.80280  36.31773 1.000 22.50759 ? 48  CYS A N   1 
ATOM   106  C CA  . CYS A 1 48  ? -20.38700 -3.62113  35.16629 1.000 24.09867 ? 48  CYS A CA  1 
ATOM   107  C C   . CYS A 1 48  ? -21.68986 -3.01691  35.64623 1.000 35.48081 ? 48  CYS A C   1 
ATOM   108  O O   . CYS A 1 48  ? -22.40904 -3.64845  36.40956 1.000 34.74931 ? 48  CYS A O   1 
ATOM   109  C CB  . CYS A 1 48  ? -20.65393 -4.94100  34.44250 1.000 28.35418 ? 48  CYS A CB  1 
ATOM   110  S SG  . CYS A 1 48  ? -21.95504 -4.80793  33.16568 1.000 33.17037 ? 48  CYS A SG  1 
ATOM   111  N N   . ASP A 1 49  ? -21.99311 -1.80116  35.20119 1.000 44.87324 ? 49  ASP A N   1 
ATOM   112  C CA  . ASP A 1 49  ? -23.14639 -1.06777  35.72127 1.000 54.60861 ? 49  ASP A CA  1 
ATOM   113  C C   . ASP A 1 49  ? -24.46808 -1.46901  35.06627 1.000 53.73830 ? 49  ASP A C   1 
ATOM   114  O O   . ASP A 1 49  ? -25.50487 -1.52625  35.72888 1.000 57.96034 ? 49  ASP A O   1 
ATOM   115  C CB  . ASP A 1 49  ? -22.92707 0.43815   35.55530 1.000 58.96480 ? 49  ASP A CB  1 
ATOM   116  C CG  . ASP A 1 49  ? -21.81198 0.96228   36.43572 1.000 62.12639 ? 49  ASP A CG  1 
ATOM   117  O OD1 . ASP A 1 49  ? -21.66172 0.45489   37.56980 1.000 63.17207 ? 49  ASP A OD1 1 
ATOM   118  O OD2 . ASP A 1 49  ? -21.08387 1.87633   35.99262 1.000 60.37693 ? 49  ASP A OD2 1 
ATOM   119  N N   . ASP A 1 50  ? -24.42781 -1.74786  33.76826 1.000 52.80693 ? 50  ASP A N   1 
ATOM   120  C CA  . ASP A 1 50  ? -25.64587 -2.03553  33.02063 1.000 57.39815 ? 50  ASP A CA  1 
ATOM   121  C C   . ASP A 1 50  ? -25.84311 -3.52835  32.78125 1.000 50.54311 ? 50  ASP A C   1 
ATOM   122  O O   . ASP A 1 50  ? -26.40048 -3.92394  31.76009 1.000 52.97706 ? 50  ASP A O   1 
ATOM   123  C CB  . ASP A 1 50  ? -25.63252 -1.29592  31.67788 1.000 65.23038 ? 50  ASP A CB  1 
ATOM   124  C CG  . ASP A 1 50  ? -25.52699 0.21438   31.84030 1.000 69.63875 ? 50  ASP A CG  1 
ATOM   125  O OD1 . ASP A 1 50  ? -26.55934 0.85811   32.12898 1.000 72.77251 ? 50  ASP A OD1 1 
ATOM   126  O OD2 . ASP A 1 50  ? -24.41277 0.75850   31.67424 1.000 65.87753 ? 50  ASP A OD2 1 
ATOM   127  N N   . CYS A 1 51  ? -25.39144 -4.35869  33.71679 1.000 42.32158 ? 51  CYS A N   1 
ATOM   128  C CA  . CYS A 1 51  ? -25.53473 -5.80186  33.55432 1.000 37.02614 ? 51  CYS A CA  1 
ATOM   129  C C   . CYS A 1 51  ? -26.76499 -6.33149  34.29292 1.000 47.16630 ? 51  CYS A C   1 
ATOM   130  O O   . CYS A 1 51  ? -27.41541 -5.60397  35.04349 1.000 43.86132 ? 51  CYS A O   1 
ATOM   131  C CB  . CYS A 1 51  ? -24.27436 -6.53306  34.03045 1.000 30.22618 ? 51  CYS A CB  1 
ATOM   132  S SG  . CYS A 1 51  ? -22.92276 -6.56263  32.80960 1.000 33.11194 ? 51  CYS A SG  1 
ATOM   133  N N   . GLU A 1 52  ? -27.06764 -7.60644  34.06473 1.000 54.07020 ? 52  GLU A N   1 
ATOM   134  C CA  . GLU A 1 52  ? -28.23104 -8.25752  34.65324 1.000 57.85345 ? 52  GLU A CA  1 
ATOM   135  C C   . GLU A 1 52  ? -28.21532 -8.21108  36.17636 1.000 56.28034 ? 52  GLU A C   1 
ATOM   136  O O   . GLU A 1 52  ? -27.21449 -8.55839  36.80234 1.000 51.71371 ? 52  GLU A O   1 
ATOM   137  C CB  . GLU A 1 52  ? -28.30854 -9.71440  34.18392 1.000 56.22724 ? 52  GLU A CB  1 
ATOM   138  N N   . VAL A 1 53  ? -29.32891 -7.78429  36.76707 1.000 59.73780 ? 53  VAL A N   1 
ATOM   139  C CA  . VAL A 1 53  ? -29.48828 -7.81734  38.21938 1.000 56.40613 ? 53  VAL A CA  1 
ATOM   140  C C   . VAL A 1 53  ? -29.43396 -9.25693  38.73091 1.000 53.42706 ? 53  VAL A C   1 
ATOM   141  O O   . VAL A 1 53  ? -29.99719 -10.17257 38.11997 1.000 54.74700 ? 53  VAL A O   1 
ATOM   142  C CB  . VAL A 1 53  ? -30.81960 -7.15894  38.67443 1.000 57.25462 ? 53  VAL A CB  1 
ATOM   143  C CG1 . VAL A 1 53  ? -30.78547 -5.65034  38.44165 1.000 58.58446 ? 53  VAL A CG1 1 
ATOM   144  C CG2 . VAL A 1 53  ? -32.00745 -7.78670  37.95976 1.000 55.02045 ? 53  VAL A CG2 1 
ATOM   145  N N   . SER A 1 54  ? -28.74725 -9.45335  39.85167 1.000 49.87111 ? 54  SER A N   1 
ATOM   146  C CA  . SER A 1 54  ? -28.59436 -10.78359 40.42685 1.000 48.94017 ? 54  SER A CA  1 
ATOM   147  C C   . SER A 1 54  ? -28.19783 -10.70233 41.89544 1.000 50.47683 ? 54  SER A C   1 
ATOM   148  O O   . SER A 1 54  ? -27.36419 -9.88019  42.27501 1.000 50.36494 ? 54  SER A O   1 
ATOM   149  C CB  . SER A 1 54  ? -27.55558 -11.58840 39.64160 1.000 44.52984 ? 54  SER A CB  1 
ATOM   150  O OG  . SER A 1 54  ? -27.29915 -12.83541 40.26239 1.000 39.59549 ? 54  SER A OG  1 
ATOM   151  N N   . THR A 1 55  ? -28.80026 -11.55672 42.71872 1.000 42.57770 ? 55  THR A N   1 
ATOM   152  C CA  . THR A 1 55  ? -28.47865 -11.59925 44.14054 1.000 46.23162 ? 55  THR A CA  1 
ATOM   153  C C   . THR A 1 55  ? -27.37833 -12.61309 44.43011 1.000 51.31085 ? 55  THR A C   1 
ATOM   154  O O   . THR A 1 55  ? -26.89255 -12.70691 45.55958 1.000 55.98920 ? 55  THR A O   1 
ATOM   155  C CB  . THR A 1 55  ? -29.70876 -11.95466 44.98638 1.000 52.25603 ? 55  THR A CB  1 
ATOM   156  O OG1 . THR A 1 55  ? -30.22259 -13.22604 44.56623 1.000 55.57527 ? 55  THR A OG1 1 
ATOM   157  C CG2 . THR A 1 55  ? -30.78597 -10.89330 44.82707 1.000 51.89573 ? 55  THR A CG2 1 
ATOM   158  N N   . SER A 1 56  ? -26.98997 -13.36858 43.40525 1.000 46.37039 ? 56  SER A N   1 
ATOM   159  C CA  . SER A 1 56  ? -25.98952 -14.41928 43.56111 1.000 41.65641 ? 56  SER A CA  1 
ATOM   160  C C   . SER A 1 56  ? -24.69648 -14.15491 42.77757 1.000 34.58511 ? 56  SER A C   1 
ATOM   161  O O   . SER A 1 56  ? -23.65103 -14.70753 43.11034 1.000 33.94757 ? 56  SER A O   1 
ATOM   162  C CB  . SER A 1 56  ? -26.57251 -15.76291 43.13129 1.000 34.30792 ? 56  SER A CB  1 
ATOM   163  O OG  . SER A 1 56  ? -26.99087 -15.70977 41.78022 1.000 38.02174 ? 56  SER A OG  1 
ATOM   164  N N   . LYS A 1 57  ? -24.77691 -13.33595 41.73106 1.000 30.92006 ? 57  LYS A N   1 
ATOM   165  C CA  . LYS A 1 57  ? -23.59931 -13.00162 40.92386 1.000 28.28330 ? 57  LYS A CA  1 
ATOM   166  C C   . LYS A 1 57  ? -23.34199 -11.50292 40.89405 1.000 25.81104 ? 57  LYS A C   1 
ATOM   167  O O   . LYS A 1 57  ? -24.27193 -10.70206 40.93433 1.000 29.99620 ? 57  LYS A O   1 
ATOM   168  C CB  . LYS A 1 57  ? -23.74854 -13.49251 39.48035 1.000 30.10263 ? 57  LYS A CB  1 
ATOM   169  C CG  . LYS A 1 57  ? -24.21113 -14.92885 39.30081 1.000 36.11898 ? 57  LYS A CG  1 
ATOM   170  C CD  . LYS A 1 57  ? -24.41486 -15.21281 37.81725 1.000 35.06989 ? 57  LYS A CD  1 
ATOM   171  C CE  . LYS A 1 57  ? -24.89329 -16.63473 37.56246 1.000 39.67294 ? 57  LYS A CE  1 
ATOM   172  N NZ  . LYS A 1 57  ? -25.12582 -16.89390 36.10458 1.000 47.54801 ? 57  LYS A NZ  1 
ATOM   173  N N   . THR A 1 58  ? -22.06941 -11.13993 40.79878 1.000 24.20692 ? 58  THR A N   1 
ATOM   174  C CA  . THR A 1 58  ? -21.66533 -9.75834  40.60095 1.000 24.90847 ? 58  THR A CA  1 
ATOM   175  C C   . THR A 1 58  ? -20.87095 -9.67949  39.29631 1.000 21.95108 ? 58  THR A C   1 
ATOM   176  O O   . THR A 1 58  ? -19.93833 -10.46398 39.08036 1.000 21.99451 ? 58  THR A O   1 
ATOM   177  C CB  . THR A 1 58  ? -20.82408 -9.23411  41.78571 1.000 23.26448 ? 58  THR A CB  1 
ATOM   178  O OG1 . THR A 1 58  ? -21.59857 -9.30143  42.99373 1.000 27.59837 ? 58  THR A OG1 1 
ATOM   179  C CG2 . THR A 1 58  ? -20.40322 -7.79498  41.55209 1.000 20.54934 ? 58  THR A CG2 1 
ATOM   180  N N   . PHE A 1 59  ? -21.24940 -8.75449  38.41810 1.000 20.41237 ? 59  PHE A N   1 
ATOM   181  C CA  . PHE A 1 59  ? -20.66006 -8.70928  37.08104 1.000 23.92076 ? 59  PHE A CA  1 
ATOM   182  C C   . PHE A 1 59  ? -19.55222 -7.67836  36.96212 1.000 20.93522 ? 59  PHE A C   1 
ATOM   183  O O   . PHE A 1 59  ? -19.63731 -6.59314  37.52662 1.000 17.67504 ? 59  PHE A O   1 
ATOM   184  C CB  . PHE A 1 59  ? -21.74508 -8.43807  36.03510 1.000 22.57834 ? 59  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 59  ? -22.69322 -9.59027  35.84203 1.000 25.36464 ? 59  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 59  ? -23.82913 -9.71258  36.63361 1.000 35.17677 ? 59  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 59  ? -22.44551 -10.55352 34.87282 1.000 23.19304 ? 59  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 59  ? -24.70088 -10.77511 36.46282 1.000 33.95776 ? 59  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 59  ? -23.31530 -11.62648 34.69272 1.000 30.19728 ? 59  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 59  ? -24.44494 -11.73358 35.48830 1.000 32.39958 ? 59  PHE A CZ  1 
ATOM   191  N N   . PHE A 1 60  ? -18.51424 -8.03069  36.21325 1.000 19.69175 ? 60  PHE A N   1 
ATOM   192  C CA  . PHE A 1 60  ? -17.35803 -7.17123  36.01726 1.000 18.04496 ? 60  PHE A CA  1 
ATOM   193  C C   . PHE A 1 60  ? -16.92948 -7.17801  34.55451 1.000 22.44513 ? 60  PHE A C   1 
ATOM   194  O O   . PHE A 1 60  ? -17.27708 -8.09868  33.81236 1.000 21.96234 ? 60  PHE A O   1 
ATOM   195  C CB  . PHE A 1 60  ? -16.18183 -7.63240  36.88366 1.000 13.56353 ? 60  PHE A CB  1 
ATOM   196  C CG  . PHE A 1 60  ? -16.46315 -7.62500  38.35926 1.000 18.44249 ? 60  PHE A CG  1 
ATOM   197  C CD1 . PHE A 1 60  ? -16.38496 -6.44450  39.08903 1.000 19.37170 ? 60  PHE A CD1 1 
ATOM   198  C CD2 . PHE A 1 60  ? -16.78887 -8.79963  39.02409 1.000 20.22599 ? 60  PHE A CD2 1 
ATOM   199  C CE1 . PHE A 1 60  ? -16.63784 -6.43166  40.45766 1.000 26.50400 ? 60  PHE A CE1 1 
ATOM   200  C CE2 . PHE A 1 60  ? -17.04383 -8.79037  40.39819 1.000 28.39375 ? 60  PHE A CE2 1 
ATOM   201  C CZ  . PHE A 1 60  ? -16.96777 -7.60681  41.11142 1.000 22.70207 ? 60  PHE A CZ  1 
ATOM   202  N N   . TYR A 1 61  ? -16.18855 -6.14644  34.14853 1.000 12.08676 ? 61  TYR A N   1 
ATOM   203  C CA  . TYR A 1 61  ? -15.41042 -6.20355  32.92086 1.000 16.81896 ? 61  TYR A CA  1 
ATOM   204  C C   . TYR A 1 61  ? -13.94072 -6.39783  33.26737 1.000 14.09159 ? 61  TYR A C   1 
ATOM   205  O O   . TYR A 1 61  ? -13.35647 -5.61402  34.01413 1.000 15.02639 ? 61  TYR A O   1 
ATOM   206  C CB  . TYR A 1 61  ? -15.59357 -4.94410  32.07749 1.000 18.97536 ? 61  TYR A CB  1 
ATOM   207  C CG  . TYR A 1 61  ? -16.96884 -4.84101  31.46112 1.000 21.83946 ? 61  TYR A CG  1 
ATOM   208  C CD1 . TYR A 1 61  ? -17.35815 -5.69097  30.43120 1.000 13.82054 ? 61  TYR A CD1 1 
ATOM   209  C CD2 . TYR A 1 61  ? -17.88420 -3.90547  31.92066 1.000 22.24556 ? 61  TYR A CD2 1 
ATOM   210  C CE1 . TYR A 1 61  ? -18.61947 -5.59833  29.87275 1.000 19.68012 ? 61  TYR A CE1 1 
ATOM   211  C CE2 . TYR A 1 61  ? -19.14692 -3.80286  31.36479 1.000 25.79070 ? 61  TYR A CE2 1 
ATOM   212  C CZ  . TYR A 1 61  ? -19.50656 -4.65232  30.34275 1.000 27.44693 ? 61  TYR A CZ  1 
ATOM   213  O OH  . TYR A 1 61  ? -20.76233 -4.55647  29.79186 1.000 29.67408 ? 61  TYR A OH  1 
ATOM   214  N N   . CYS A 1 62  ? -13.34830 -7.44768  32.71184 1.000 13.01361 ? 62  CYS A N   1 
ATOM   215  C CA  . CYS A 1 62  ? -11.95776 -7.79170  32.99159 1.000 14.43100 ? 62  CYS A CA  1 
ATOM   216  C C   . CYS A 1 62  ? -11.03184 -7.37697  31.85281 1.000 11.63290 ? 62  CYS A C   1 
ATOM   217  O O   . CYS A 1 62  ? -11.29099 -7.69289  30.68831 1.000 12.94804 ? 62  CYS A O   1 
ATOM   218  C CB  . CYS A 1 62  ? -11.84470 -9.29228  33.25201 1.000 11.06267 ? 62  CYS A CB  1 
ATOM   219  S SG  . CYS A 1 62  ? -12.85840 -9.78871  34.66880 1.000 17.73860 ? 62  CYS A SG  1 
ATOM   220  N N   . GLY A 1 63  ? -9.94725  -6.68472  32.20346 1.000 10.69221 ? 63  GLY A N   1 
ATOM   221  C CA  . GLY A 1 63  ? -8.98504  -6.20075  31.23938 1.000 16.12431 ? 63  GLY A CA  1 
ATOM   222  C C   . GLY A 1 63  ? -9.69097  -5.46303  30.11925 1.000 13.92193 ? 63  GLY A C   1 
ATOM   223  O O   . GLY A 1 63  ? -10.53229 -4.59037  30.36273 1.000 12.11456 ? 63  GLY A O   1 
ATOM   224  N N   . ILE A 1 64  ? -9.37143  -5.84640  28.89011 1.000 8.56880  ? 64  ILE A N   1 
ATOM   225  C CA  . ILE A 1 64  ? -9.96764  -5.21686  27.71906 1.000 8.20557  ? 64  ILE A CA  1 
ATOM   226  C C   . ILE A 1 64  ? -11.01301 -6.10135  27.04498 1.000 8.40547  ? 64  ILE A C   1 
ATOM   227  O O   . ILE A 1 64  ? -11.30273 -5.92893  25.85723 1.000 11.33131 ? 64  ILE A O   1 
ATOM   228  C CB  . ILE A 1 64  ? -8.86992  -4.83339  26.68966 1.000 9.78335  ? 64  ILE A CB  1 
ATOM   229  C CG1 . ILE A 1 64  ? -8.09952  -6.07452  26.22509 1.000 14.85449 ? 64  ILE A CG1 1 
ATOM   230  C CG2 . ILE A 1 64  ? -7.91943  -3.78376  27.29385 1.000 6.99223  ? 64  ILE A CG2 1 
ATOM   231  C CD1 . ILE A 1 64  ? -7.02655  -5.76450  25.16405 1.000 15.09890 ? 64  ILE A CD1 1 
ATOM   232  N N   . LYS A 1 65  ? -11.58799 -7.04604  27.79216 1.000 8.72479  ? 65  LYS A N   1 
ATOM   233  C CA  . LYS A 1 65  ? -12.58998 -7.93437  27.21769 1.000 9.53103  ? 65  LYS A CA  1 
ATOM   234  C C   . LYS A 1 65  ? -13.80371 -7.11557  26.82419 1.000 15.24985 ? 65  LYS A C   1 
ATOM   235  O O   . LYS A 1 65  ? -14.17345 -6.18557  27.53115 1.000 15.69541 ? 65  LYS A O   1 
ATOM   236  C CB  . LYS A 1 65  ? -13.00196 -9.03362  28.19453 1.000 15.81058 ? 65  LYS A CB  1 
ATOM   237  C CG  . LYS A 1 65  ? -11.92921 -10.08992 28.42513 1.000 18.95818 ? 65  LYS A CG  1 
ATOM   238  C CD  . LYS A 1 65  ? -12.49435 -11.23323 29.25645 1.000 19.34471 ? 65  LYS A CD  1 
ATOM   239  C CE  . LYS A 1 65  ? -11.68494 -12.47865 29.02721 1.000 17.73684 ? 65  LYS A CE  1 
ATOM   240  N NZ  . LYS A 1 65  ? -12.33352 -13.70347 29.58159 1.000 22.08815 ? 65  LYS A NZ  1 
ATOM   241  N N   . ALA A 1 66  ? -14.40348 -7.45994  25.69073 1.000 10.92432 ? 66  ALA A N   1 
ATOM   242  C CA  . ALA A 1 66  ? -15.56537 -6.74569  25.18867 1.000 11.60276 ? 66  ALA A CA  1 
ATOM   243  C C   . ALA A 1 66  ? -16.84463 -7.26561  25.84210 1.000 16.39471 ? 66  ALA A C   1 
ATOM   244  O O   . ALA A 1 66  ? -17.86834 -6.58080  25.84501 1.000 18.39516 ? 66  ALA A O   1 
ATOM   245  C CB  . ALA A 1 66  ? -15.64673 -6.86970  23.66625 1.000 13.36882 ? 66  ALA A CB  1 
ATOM   246  N N   . GLY A 1 67  ? -16.77531 -8.47214  26.40523 1.000 16.31907 ? 67  GLY A N   1 
ATOM   247  C CA  . GLY A 1 67  ? -17.91811 -9.07600  27.06859 1.000 20.31410 ? 67  GLY A CA  1 
ATOM   248  C C   . GLY A 1 67  ? -17.73788 -9.13363  28.57618 1.000 18.79076 ? 67  GLY A C   1 
ATOM   249  O O   . GLY A 1 67  ? -16.61402 -9.20502  29.06850 1.000 14.84588 ? 67  GLY A O   1 
ATOM   250  N N   . ALA A 1 68  ? -18.84753 -9.10228  29.31102 1.000 15.36603 ? 68  ALA A N   1 
ATOM   251  C CA  . ALA A 1 68  ? -18.79688 -9.12344  30.77360 1.000 19.90581 ? 68  ALA A CA  1 
ATOM   252  C C   . ALA A 1 68  ? -18.45671 -10.50292 31.35823 1.000 17.20106 ? 68  ALA A C   1 
ATOM   253  O O   . ALA A 1 68  ? -18.74147 -11.55232 30.76483 1.000 15.76089 ? 68  ALA A O   1 
ATOM   254  C CB  . ALA A 1 68  ? -20.12510 -8.63731  31.34983 1.000 18.68717 ? 68  ALA A CB  1 
ATOM   255  N N   . SER A 1 69  ? -17.85538 -10.47598 32.53954 1.000 13.20559 ? 69  SER A N   1 
ATOM   256  C CA  . SER A 1 69  ? -17.59918 -11.67367 33.33129 1.000 13.81592 ? 69  SER A CA  1 
ATOM   257  C C   . SER A 1 69  ? -18.42674 -11.56528 34.59319 1.000 16.58872 ? 69  SER A C   1 
ATOM   258  O O   . SER A 1 69  ? -19.05850 -10.53768 34.83614 1.000 16.96824 ? 69  SER A O   1 
ATOM   259  C CB  . SER A 1 69  ? -16.11946 -11.81121 33.70088 1.000 16.28617 ? 69  SER A CB  1 
ATOM   260  O OG  . SER A 1 69  ? -15.27428 -11.51989 32.61266 1.000 13.74844 ? 69  SER A OG  1 
ATOM   261  N N   . TYR A 1 70  ? -18.40400 -12.60458 35.41705 1.000 14.48560 ? 70  TYR A N   1 
ATOM   262  C CA  . TYR A 1 70  ? -19.05396 -12.50317 36.71170 1.000 16.06121 ? 70  TYR A CA  1 
ATOM   263  C C   . TYR A 1 70  ? -18.30962 -13.34988 37.70551 1.000 18.41585 ? 70  TYR A C   1 
ATOM   264  O O   . TYR A 1 70  ? -17.58864 -14.27141 37.32900 1.000 15.85550 ? 70  TYR A O   1 
ATOM   265  C CB  . TYR A 1 70  ? -20.53128 -12.93046 36.64334 1.000 13.27973 ? 70  TYR A CB  1 
ATOM   266  C CG  . TYR A 1 70  ? -20.76484 -14.42655 36.54713 1.000 16.80538 ? 70  TYR A CG  1 
ATOM   267  C CD1 . TYR A 1 70  ? -20.87562 -15.21285 37.69729 1.000 17.86680 ? 70  TYR A CD1 1 
ATOM   268  C CD2 . TYR A 1 70  ? -20.90113 -15.04797 35.31500 1.000 15.60768 ? 70  TYR A CD2 1 
ATOM   269  C CE1 . TYR A 1 70  ? -21.09186 -16.57119 37.62041 1.000 20.88522 ? 70  TYR A CE1 1 
ATOM   270  C CE2 . TYR A 1 70  ? -21.11518 -16.40885 35.22929 1.000 21.65367 ? 70  TYR A CE2 1 
ATOM   271  C CZ  . TYR A 1 70  ? -21.21403 -17.16561 36.38739 1.000 23.55359 ? 70  TYR A CZ  1 
ATOM   272  O OH  . TYR A 1 70  ? -21.43424 -18.52145 36.31586 1.000 21.11509 ? 70  TYR A OH  1 
ATOM   273  N N   . VAL A 1 71  ? -18.47286 -13.01703 38.97675 1.000 15.67463 ? 71  VAL A N   1 
ATOM   274  C CA  . VAL A 1 71  ? -18.03012 -13.89185 40.04187 1.000 18.09738 ? 71  VAL A CA  1 
ATOM   275  C C   . VAL A 1 71  ? -19.22338 -14.18347 40.94749 1.000 23.45344 ? 71  VAL A C   1 
ATOM   276  O O   . VAL A 1 71  ? -20.15136 -13.36678 41.05861 1.000 22.94823 ? 71  VAL A O   1 
ATOM   277  C CB  . VAL A 1 71  ? -16.87404 -13.27282 40.85707 1.000 23.16902 ? 71  VAL A CB  1 
ATOM   278  C CG1 . VAL A 1 71  ? -17.40872 -12.24578 41.86503 1.000 24.92399 ? 71  VAL A CG1 1 
ATOM   279  C CG2 . VAL A 1 71  ? -16.07772 -14.36583 41.56008 1.000 24.71968 ? 71  VAL A CG2 1 
ATOM   280  N N   . GLU A 1 72  ? -19.21352 -15.36090 41.56578 1.000 23.05744 ? 72  GLU A N   1 
ATOM   281  C CA  . GLU A 1 72  ? -20.23343 -15.71974 42.53836 1.000 28.48987 ? 72  GLU A CA  1 
ATOM   282  C C   . GLU A 1 72  ? -20.10688 -14.81528 43.75399 1.000 33.11082 ? 72  GLU A C   1 
ATOM   283  O O   . GLU A 1 72  ? -18.99848 -14.48708 44.17716 1.000 32.99603 ? 72  GLU A O   1 
ATOM   284  C CB  . GLU A 1 72  ? -20.09550 -17.18117 42.94811 1.000 27.42896 ? 72  GLU A CB  1 
ATOM   285  C CG  . GLU A 1 72  ? -19.94817 -18.14026 41.78346 1.000 41.41016 ? 72  GLU A CG  1 
ATOM   286  C CD  . GLU A 1 72  ? -21.27649 -18.54599 41.18774 1.000 55.67571 ? 72  GLU A CD  1 
ATOM   287  O OE1 . GLU A 1 72  ? -22.30100 -17.90815 41.51506 1.000 56.94777 ? 72  GLU A OE1 1 
ATOM   288  O OE2 . GLU A 1 72  ? -21.29519 -19.51297 40.39547 1.000 64.89840 ? 72  GLU A OE2 1 
ATOM   289  N N   . ASN A 1 73  ? -21.23901 -14.41501 44.31945 1.000 34.47300 ? 73  ASN A N   1 
ATOM   290  C CA  . ASN A 1 73  ? -21.23504 -13.49277 45.45355 1.000 34.41164 ? 73  ASN A CA  1 
ATOM   291  C C   . ASN A 1 73  ? -20.59422 -14.05227 46.72846 1.000 33.86997 ? 73  ASN A C   1 
ATOM   292  O O   . ASN A 1 73  ? -20.13451 -13.28944 47.57732 1.000 33.00194 ? 73  ASN A O   1 
ATOM   293  C CB  . ASN A 1 73  ? -22.66240 -13.03823 45.76057 1.000 39.72593 ? 73  ASN A CB  1 
ATOM   294  C CG  . ASN A 1 73  ? -23.11453 -11.89537 44.86739 1.000 41.41847 ? 73  ASN A CG  1 
ATOM   295  O OD1 . ASN A 1 73  ? -22.42579 -11.52178 43.91511 1.000 34.69015 ? 73  ASN A OD1 1 
ATOM   296  N ND2 . ASN A 1 73  ? -24.27612 -11.33365 45.17284 1.000 38.60158 ? 73  ASN A ND2 1 
ATOM   297  N N   . ASP A 1 74  ? -20.55761 -15.37036 46.88056 1.000 31.76548 ? 74  ASP A N   1 
ATOM   298  C CA  . ASP A 1 74  ? -19.94926 -15.92205 48.08866 1.000 36.91610 ? 74  ASP A CA  1 
ATOM   299  C C   . ASP A 1 74  ? -18.50139 -16.30599 47.84072 1.000 37.44777 ? 74  ASP A C   1 
ATOM   300  O O   . ASP A 1 74  ? -17.86677 -16.92694 48.68941 1.000 33.00095 ? 74  ASP A O   1 
ATOM   301  C CB  . ASP A 1 74  ? -20.73549 -17.12990 48.62154 1.000 35.04109 ? 74  ASP A CB  1 
ATOM   302  C CG  . ASP A 1 74  ? -20.78714 -18.29412 47.64148 1.000 40.82931 ? 74  ASP A CG  1 
ATOM   303  O OD1 . ASP A 1 74  ? -20.10921 -18.25835 46.59180 1.000 42.71613 ? 74  ASP A OD1 1 
ATOM   304  O OD2 . ASP A 1 74  ? -21.51701 -19.26487 47.93460 1.000 43.84883 ? 74  ASP A OD2 1 
ATOM   305  N N   . SER A 1 75  ? -17.99017 -15.94131 46.66774 1.000 38.57895 ? 75  SER A N   1 
ATOM   306  C CA  . SER A 1 75  ? -16.61460 -16.26167 46.30675 1.000 28.80448 ? 75  SER A CA  1 
ATOM   307  C C   . SER A 1 75  ? -15.63493 -15.63843 47.27634 1.000 27.39379 ? 75  SER A C   1 
ATOM   308  O O   . SER A 1 75  ? -15.74083 -14.45684 47.60134 1.000 25.87147 ? 75  SER A O   1 
ATOM   309  C CB  . SER A 1 75  ? -16.28848 -15.79023 44.88994 1.000 25.70018 ? 75  SER A CB  1 
ATOM   310  O OG  . SER A 1 75  ? -14.89135 -15.88582 44.65175 1.000 28.61816 ? 75  SER A OG  1 
ATOM   311  N N   . PRO A 1 76  ? -14.65612 -16.43410 47.72354 1.000 28.42642 ? 76  PRO A N   1 
ATOM   312  C CA  . PRO A 1 76  ? -13.60002 -15.95485 48.61635 1.000 31.87149 ? 76  PRO A CA  1 
ATOM   313  C C   . PRO A 1 76  ? -12.65030 -14.97393 47.94023 1.000 31.46106 ? 76  PRO A C   1 
ATOM   314  O O   . PRO A 1 76  ? -11.73514 -14.51271 48.61127 1.000 30.87294 ? 76  PRO A O   1 
ATOM   315  C CB  . PRO A 1 76  ? -12.86002 -17.23681 49.00106 1.000 33.75245 ? 76  PRO A CB  1 
ATOM   316  C CG  . PRO A 1 76  ? -13.11758 -18.16880 47.87863 1.000 32.88143 ? 76  PRO A CG  1 
ATOM   317  C CD  . PRO A 1 76  ? -14.49132 -17.85846 47.38108 1.000 29.02188 ? 76  PRO A CD  1 
ATOM   318  N N   . TYR A 1 77  ? -12.86128 -14.67160 46.65555 1.000 26.43307 ? 77  TYR A N   1 
ATOM   319  C CA  . TYR A 1 77  ? -11.99600 -13.74393 45.92494 1.000 27.35641 ? 77  TYR A CA  1 
ATOM   320  C C   . TYR A 1 77  ? -12.66776 -12.39803 45.67542 1.000 23.85393 ? 77  TYR A C   1 
ATOM   321  O O   . TYR A 1 77  ? -12.04889 -11.47894 45.13480 1.000 21.67632 ? 77  TYR A O   1 
ATOM   322  C CB  . TYR A 1 77  ? -11.55358 -14.34687 44.58459 1.000 17.01878 ? 77  TYR A CB  1 
ATOM   323  C CG  . TYR A 1 77  ? -10.66863 -15.56648 44.73442 1.000 20.28514 ? 77  TYR A CG  1 
ATOM   324  C CD1 . TYR A 1 77  ? -9.30764  -15.44023 44.99731 1.000 23.60345 ? 77  TYR A CD1 1 
ATOM   325  C CD2 . TYR A 1 77  ? -11.20108 -16.84682 44.62292 1.000 23.38914 ? 77  TYR A CD2 1 
ATOM   326  C CE1 . TYR A 1 77  ? -8.50329  -16.55886 45.14819 1.000 19.83980 ? 77  TYR A CE1 1 
ATOM   327  C CE2 . TYR A 1 77  ? -10.41043 -17.96074 44.76663 1.000 29.63618 ? 77  TYR A CE2 1 
ATOM   328  C CZ  . TYR A 1 77  ? -9.06474  -17.81213 45.02926 1.000 28.51792 ? 77  TYR A CZ  1 
ATOM   329  O OH  . TYR A 1 77  ? -8.28698  -18.93072 45.17042 1.000 38.67225 ? 77  TYR A OH  1 
ATOM   330  N N   . LEU A 1 78  ? -13.93147 -12.27871 46.06744 1.000 27.58009 ? 78  LEU A N   1 
ATOM   331  C CA  . LEU A 1 78  ? -14.68114 -11.05411 45.78938 1.000 25.40220 ? 78  LEU A CA  1 
ATOM   332  C C   . LEU A 1 78  ? -14.00427 -9.83131  46.42569 1.000 24.70361 ? 78  LEU A C   1 
ATOM   333  O O   . LEU A 1 78  ? -13.94295 -8.75724  45.82089 1.000 25.14179 ? 78  LEU A O   1 
ATOM   334  C CB  . LEU A 1 78  ? -16.12939 -11.19292 46.27444 1.000 23.32000 ? 78  LEU A CB  1 
ATOM   335  C CG  . LEU A 1 78  ? -17.07366 -10.01269 46.02827 1.000 24.05682 ? 78  LEU A CG  1 
ATOM   336  C CD1 . LEU A 1 78  ? -17.00018 -9.56286  44.56870 1.000 26.77529 ? 78  LEU A CD1 1 
ATOM   337  C CD2 . LEU A 1 78  ? -18.49758 -10.37357 46.41837 1.000 32.41998 ? 78  LEU A CD2 1 
ATOM   338  N N   . ASN A 1 79  ? -13.48435 -9.99192  47.63753 1.000 22.86443 ? 79  ASN A N   1 
ATOM   339  C CA  . ASN A 1 79  ? -12.82259 -8.87497  48.29660 1.000 20.14089 ? 79  ASN A CA  1 
ATOM   340  C C   . ASN A 1 79  ? -11.51719 -8.51852  47.59892 1.000 25.38979 ? 79  ASN A C   1 
ATOM   341  O O   . ASN A 1 79  ? -11.15585 -7.34547  47.52965 1.000 24.81079 ? 79  ASN A O   1 
ATOM   342  C CB  . ASN A 1 79  ? -12.57928 -9.17893  49.77305 1.000 21.52927 ? 79  ASN A CB  1 
ATOM   343  C CG  . ASN A 1 79  ? -13.81286 -8.92512  50.62623 1.000 26.44897 ? 79  ASN A CG  1 
ATOM   344  O OD1 . ASN A 1 79  ? -14.57501 -7.99227  50.37047 1.000 28.98617 ? 79  ASN A OD1 1 
ATOM   345  N ND2 . ASN A 1 79  ? -14.01902 -9.75812  51.63350 1.000 30.56220 ? 79  ASN A ND2 1 
ATOM   346  N N   . ASP A 1 80  ? -10.81014 -9.51957  47.07827 1.000 20.32877 ? 80  ASP A N   1 
ATOM   347  C CA  . ASP A 1 80  ? -9.61154  -9.24270  46.29264 1.000 21.80956 ? 80  ASP A CA  1 
ATOM   348  C C   . ASP A 1 80  ? -9.94968  -8.42828  45.05064 1.000 20.16745 ? 80  ASP A C   1 
ATOM   349  O O   . ASP A 1 80  ? -9.17533  -7.55687  44.63981 1.000 18.67079 ? 80  ASP A O   1 
ATOM   350  C CB  . ASP A 1 80  ? -8.90799  -10.53793 45.89021 1.000 26.80384 ? 80  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 80  ? -8.24273  -11.22683 47.06591 1.000 34.00275 ? 80  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 80  ? -7.81907  -10.52143 48.00594 1.000 37.43864 ? 80  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 80  ? -8.13964  -12.46996 47.04775 1.000 37.03434 ? 80  ASP A OD2 1 
ATOM   354  N N   . ILE A 1 81  ? -11.10576 -8.70518  44.45365 1.000 20.86566 ? 81  ILE A N   1 
ATOM   355  C CA  . ILE A 1 81  ? -11.52633 -7.95382  43.27201 1.000 16.01062 ? 81  ILE A CA  1 
ATOM   356  C C   . ILE A 1 81  ? -11.81530 -6.50569  43.64406 1.000 22.52865 ? 81  ILE A C   1 
ATOM   357  O O   . ILE A 1 81  ? -11.35613 -5.57677  42.96707 1.000 20.79028 ? 81  ILE A O   1 
ATOM   358  C CB  . ILE A 1 81  ? -12.76330 -8.59097  42.61131 1.000 15.60568 ? 81  ILE A CB  1 
ATOM   359  C CG1 . ILE A 1 81  ? -12.38597 -9.96044  42.02858 1.000 22.78906 ? 81  ILE A CG1 1 
ATOM   360  C CG2 . ILE A 1 81  ? -13.34192 -7.67249  41.54484 1.000 16.71568 ? 81  ILE A CG2 1 
ATOM   361  C CD1 . ILE A 1 81  ? -13.56412 -10.75872 41.49819 1.000 23.70690 ? 81  ILE A CD1 1 
ATOM   362  N N   . LYS A 1 82  ? -12.55656 -6.31461  44.73352 1.000 22.05118 ? 82  LYS A N   1 
ATOM   363  C CA  . LYS A 1 82  ? -12.91027 -4.96947  45.18586 1.000 22.28234 ? 82  LYS A CA  1 
ATOM   364  C C   . LYS A 1 82  ? -11.66370 -4.16535  45.53268 1.000 23.56633 ? 82  LYS A C   1 
ATOM   365  O O   . LYS A 1 82  ? -11.55297 -2.99797  45.17058 1.000 26.61551 ? 82  LYS A O   1 
ATOM   366  C CB  . LYS A 1 82  ? -13.85448 -5.03066  46.39090 1.000 28.95917 ? 82  LYS A CB  1 
ATOM   367  C CG  . LYS A 1 82  ? -15.12503 -5.80374  46.12159 1.000 33.88194 ? 82  LYS A CG  1 
ATOM   368  C CD  . LYS A 1 82  ? -16.36227 -5.01135  46.47926 1.000 50.89859 ? 82  LYS A CD  1 
ATOM   369  C CE  . LYS A 1 82  ? -17.29619 -5.82361  47.36311 1.000 56.36049 ? 82  LYS A CE  1 
ATOM   370  N NZ  . LYS A 1 82  ? -16.64437 -6.14854  48.65915 1.000 64.13646 ? 82  LYS A NZ  1 
ATOM   371  N N   . GLU A 1 83  ? -10.71531 -4.80003  46.21237 1.000 19.53406 ? 83  GLU A N   1 
ATOM   372  C CA  . GLU A 1 83  ? -9.48247  -4.11769  46.57520 1.000 22.73190 ? 83  GLU A CA  1 
ATOM   373  C C   . GLU A 1 83  ? -8.72977  -3.68375  45.32435 1.000 26.12904 ? 83  GLU A C   1 
ATOM   374  O O   . GLU A 1 83  ? -8.17740  -2.59184  45.27537 1.000 26.16181 ? 83  GLU A O   1 
ATOM   375  C CB  . GLU A 1 83  ? -8.58954  -5.00254  47.44422 1.000 22.35407 ? 83  GLU A CB  1 
ATOM   376  C CG  . GLU A 1 83  ? -7.46765  -4.22499  48.12788 1.000 39.80716 ? 83  GLU A CG  1 
ATOM   377  C CD  . GLU A 1 83  ? -7.98801  -3.19946  49.14046 1.000 63.61504 ? 83  GLU A CD  1 
ATOM   378  O OE1 . GLU A 1 83  ? -7.37121  -2.11912  49.27730 1.000 74.74290 ? 83  GLU A OE1 1 
ATOM   379  O OE2 . GLU A 1 83  ? -9.00959  -3.47294  49.80946 1.000 67.92493 ? 83  GLU A OE2 1 
ATOM   380  N N   . SER A 1 84  ? -8.72896  -4.53728  44.30648 1.000 24.82199 ? 84  SER A N   1 
ATOM   381  C CA  . SER A 1 84  ? -8.03525  -4.22249  43.07083 1.000 21.57638 ? 84  SER A CA  1 
ATOM   382  C C   . SER A 1 84  ? -8.68357  -3.00582  42.39266 1.000 27.59576 ? 84  SER A C   1 
ATOM   383  O O   . SER A 1 84  ? -7.98582  -2.10571  41.91369 1.000 29.51562 ? 84  SER A O   1 
ATOM   384  C CB  . SER A 1 84  ? -8.02439  -5.43965  42.15408 1.000 20.60352 ? 84  SER A CB  1 
ATOM   385  O OG  . SER A 1 84  ? -8.42834  -5.09947  40.85206 1.000 33.31621 ? 84  SER A OG  1 
ATOM   386  N N   . ILE A 1 85  ? -10.01365 -2.96917  42.37758 1.000 28.41019 ? 85  ILE A N   1 
ATOM   387  C CA  . ILE A 1 85  ? -10.74998 -1.81526  41.86014 1.000 29.54373 ? 85  ILE A CA  1 
ATOM   388  C C   . ILE A 1 85  ? -10.42686 -0.52811  42.62824 1.000 35.86839 ? 85  ILE A C   1 
ATOM   389  O O   . ILE A 1 85  ? -10.16709 0.51399   42.02109 1.000 35.12912 ? 85  ILE A O   1 
ATOM   390  C CB  . ILE A 1 85  ? -12.26467 -2.06948  41.89989 1.000 32.93034 ? 85  ILE A CB  1 
ATOM   391  C CG1 . ILE A 1 85  ? -12.61717 -3.22064  40.95870 1.000 30.73384 ? 85  ILE A CG1 1 
ATOM   392  C CG2 . ILE A 1 85  ? -13.03779 -0.80904  41.52657 1.000 37.36311 ? 85  ILE A CG2 1 
ATOM   393  C CD1 . ILE A 1 85  ? -14.08590 -3.54443  40.89983 1.000 25.67322 ? 85  ILE A CD1 1 
ATOM   394  N N   . SER A 1 86  ? -10.42937 -0.59995  43.95728 1.000 27.83241 ? 86  SER A N   1 
ATOM   395  C CA  . SER A 1 86  ? -10.11088 0.56840   44.77490 1.000 27.87701 ? 86  SER A CA  1 
ATOM   396  C C   . SER A 1 86  ? -8.70321  1.09733   44.50697 1.000 31.52051 ? 86  SER A C   1 
ATOM   397  O O   . SER A 1 86  ? -8.48571  2.30540   44.49267 1.000 36.21904 ? 86  SER A O   1 
ATOM   398  C CB  . SER A 1 86  ? -10.25573 0.24007   46.26607 1.000 35.13177 ? 86  SER A CB  1 
ATOM   399  O OG  . SER A 1 86  ? -11.57120 -0.18546  46.56941 1.000 41.64591 ? 86  SER A OG  1 
ATOM   400  N N   . ASN A 1 87  ? -7.74570  0.19693   44.30145 1.000 25.35604 ? 87  ASN A N   1 
ATOM   401  C CA  . ASN A 1 87  ? -6.36646  0.62325   44.10126 1.000 28.35358 ? 87  ASN A CA  1 
ATOM   402  C C   . ASN A 1 87  ? -6.03807  0.96443   42.65309 1.000 27.70039 ? 87  ASN A C   1 
ATOM   403  O O   . ASN A 1 87  ? -4.96347  1.48509   42.37714 1.000 32.31606 ? 87  ASN A O   1 
ATOM   404  C CB  . ASN A 1 87  ? -5.39973  -0.44600  44.60254 1.000 28.19177 ? 87  ASN A CB  1 
ATOM   405  C CG  . ASN A 1 87  ? -5.39834  -0.56250  46.11312 1.000 50.58268 ? 87  ASN A CG  1 
ATOM   406  O OD1 . ASN A 1 87  ? -5.68004  0.40351   46.82520 1.000 57.74057 ? 87  ASN A OD1 1 
ATOM   407  N ND2 . ASN A 1 87  ? -5.08100  -1.74996  46.61128 1.000 58.19508 ? 87  ASN A ND2 1 
ATOM   408  N N   . GLY A 1 88  ? -6.96552  0.66544   41.74596 1.000 23.41819 ? 88  GLY A N   1 
ATOM   409  C CA  . GLY A 1 88  ? -6.79499  0.92866   40.32857 1.000 26.74127 ? 88  GLY A CA  1 
ATOM   410  C C   . GLY A 1 88  ? -5.59621  0.21861   39.73127 1.000 22.55293 ? 88  GLY A C   1 
ATOM   411  O O   . GLY A 1 88  ? -4.91524  0.75246   38.85635 1.000 29.38031 ? 88  GLY A O   1 
ATOM   412  N N   . THR A 1 89  ? -5.32373  -0.98640  40.20746 1.000 18.73948 ? 89  THR A N   1 
ATOM   413  C CA  . THR A 1 89  ? -4.14568  -1.71348  39.75606 1.000 19.52328 ? 89  THR A CA  1 
ATOM   414  C C   . THR A 1 89  ? -4.54275  -2.97580  39.01155 1.000 18.25266 ? 89  THR A C   1 
ATOM   415  O O   . THR A 1 89  ? -5.60547  -3.53756  39.26792 1.000 16.14865 ? 89  THR A O   1 
ATOM   416  C CB  . THR A 1 89  ? -3.23885  -2.07316  40.93633 1.000 27.51275 ? 89  THR A CB  1 
ATOM   417  O OG1 . THR A 1 89  ? -4.02154  -2.71966  41.94384 1.000 25.86506 ? 89  THR A OG1 1 
ATOM   418  C CG2 . THR A 1 89  ? -2.59942  -0.81147  41.51600 1.000 30.01239 ? 89  THR A CG2 1 
ATOM   419  N N   . PRO A 1 90  ? -3.68842  -3.42525  38.07867 1.000 20.11706 ? 90  PRO A N   1 
ATOM   420  C CA  . PRO A 1 90  ? -3.97649  -4.65268  37.33553 1.000 19.93111 ? 90  PRO A CA  1 
ATOM   421  C C   . PRO A 1 90  ? -3.78572  -5.88708  38.21464 1.000 18.12803 ? 90  PRO A C   1 
ATOM   422  O O   . PRO A 1 90  ? -2.96985  -5.85327  39.14229 1.000 13.05957 ? 90  PRO A O   1 
ATOM   423  C CB  . PRO A 1 90  ? -2.95605  -4.61011  36.20252 1.000 16.97256 ? 90  PRO A CB  1 
ATOM   424  C CG  . PRO A 1 90  ? -1.77122  -3.89768  36.82023 1.000 15.73418 ? 90  PRO A CG  1 
ATOM   425  C CD  . PRO A 1 90  ? -2.40266  -2.82358  37.66967 1.000 16.60876 ? 90  PRO A CD  1 
ATOM   426  N N   . ILE A 1 91  ? -4.55051  -6.94200  37.93714 1.000 13.38685 ? 91  ILE A N   1 
ATOM   427  C CA  . ILE A 1 91  ? -4.42114  -8.23565  38.61605 1.000 10.79424 ? 91  ILE A CA  1 
ATOM   428  C C   . ILE A 1 91  ? -4.59420  -9.34335  37.59433 1.000 10.31037 ? 91  ILE A C   1 
ATOM   429  O O   . ILE A 1 91  ? -5.04010  -9.09967  36.47164 1.000 15.90619 ? 91  ILE A O   1 
ATOM   430  C CB  . ILE A 1 91  ? -5.46568  -8.46642  39.74416 1.000 24.31317 ? 91  ILE A CB  1 
ATOM   431  C CG1 . ILE A 1 91  ? -6.69294  -7.60638  39.52441 1.000 32.16718 ? 91  ILE A CG1 1 
ATOM   432  C CG2 . ILE A 1 91  ? -4.89646  -8.19066  41.11106 1.000 41.55782 ? 91  ILE A CG2 1 
ATOM   433  C CD1 . ILE A 1 91  ? -7.49918  -8.06402  38.41505 1.000 30.41463 ? 91  ILE A CD1 1 
ATOM   434  N N   . LYS A 1 92  ? -4.25837  -10.55895 37.99953 1.000 11.70326 ? 92  LYS A N   1 
ATOM   435  C CA  . LYS A 1 92  ? -4.40448  -11.72134 37.14800 1.000 13.46671 ? 92  LYS A CA  1 
ATOM   436  C C   . LYS A 1 92  ? -5.74951  -12.36822 37.45984 1.000 14.70540 ? 92  LYS A C   1 
ATOM   437  O O   . LYS A 1 92  ? -6.07377  -12.61015 38.62170 1.000 14.63146 ? 92  LYS A O   1 
ATOM   438  C CB  . LYS A 1 92  ? -3.24500  -12.69841 37.37042 1.000 11.15033 ? 92  LYS A CB  1 
ATOM   439  C CG  . LYS A 1 92  ? -3.23281  -13.89715 36.42645 1.000 12.58253 ? 92  LYS A CG  1 
ATOM   440  C CD  . LYS A 1 92  ? -1.96795  -14.73088 36.60974 1.000 15.21781 ? 92  LYS A CD  1 
ATOM   441  C CE  . LYS A 1 92  ? -0.70941  -13.97458 36.17574 1.000 20.81343 ? 92  LYS A CE  1 
ATOM   442  N NZ  . LYS A 1 92  ? 0.52697   -14.77383 36.43750 1.000 17.68262 ? 92  LYS A NZ  1 
ATOM   443  N N   . ILE A 1 93  ? -6.53976  -12.62136 36.42489 1.000 13.90250 ? 93  ILE A N   1 
ATOM   444  C CA  . ILE A 1 93  ? -7.88856  -13.16201 36.60998 1.000 14.25176 ? 93  ILE A CA  1 
ATOM   445  C C   . ILE A 1 93  ? -7.98716  -14.50387 35.90947 1.000 18.14920 ? 93  ILE A C   1 
ATOM   446  O O   . ILE A 1 93  ? -7.67681  -14.59272 34.73104 1.000 15.13603 ? 93  ILE A O   1 
ATOM   447  C CB  . ILE A 1 93  ? -8.95533  -12.21259 36.04000 1.000 11.64211 ? 93  ILE A CB  1 
ATOM   448  C CG1 . ILE A 1 93  ? -8.79166  -10.81950 36.63822 1.000 15.50266 ? 93  ILE A CG1 1 
ATOM   449  C CG2 . ILE A 1 93  ? -10.36813 -12.73866 36.28169 1.000 11.73247 ? 93  ILE A CG2 1 
ATOM   450  C CD1 . ILE A 1 93  ? -8.86947  -9.72880  35.60551 1.000 24.88316 ? 93  ILE A CD1 1 
ATOM   451  N N   . TYR A 1 94  ? -8.40854  -15.54333 36.62640 1.000 11.18271 ? 94  TYR A N   1 
ATOM   452  C CA  . TYR A 1 94  ? -8.58969  -16.85539 36.01504 1.000 12.94726 ? 94  TYR A CA  1 
ATOM   453  C C   . TYR A 1 94  ? -10.05923 -17.12628 35.74248 1.000 16.71801 ? 94  TYR A C   1 
ATOM   454  O O   . TYR A 1 94  ? -10.91457 -16.82151 36.57992 1.000 15.48410 ? 94  TYR A O   1 
ATOM   455  C CB  . TYR A 1 94  ? -8.03538  -17.95843 36.91308 1.000 14.16047 ? 94  TYR A CB  1 
ATOM   456  C CG  . TYR A 1 94  ? -6.52506  -18.05840 36.91903 1.000 13.79260 ? 94  TYR A CG  1 
ATOM   457  C CD1 . TYR A 1 94  ? -5.76333  -17.26248 37.76244 1.000 14.52309 ? 94  TYR A CD1 1 
ATOM   458  C CD2 . TYR A 1 94  ? -5.86789  -18.96948 36.09818 1.000 11.80870 ? 94  TYR A CD2 1 
ATOM   459  C CE1 . TYR A 1 94  ? -4.37773  -17.34396 37.77341 1.000 17.70314 ? 94  TYR A CE1 1 
ATOM   460  C CE2 . TYR A 1 94  ? -4.47787  -19.06473 36.10429 1.000 18.69773 ? 94  TYR A CE2 1 
ATOM   461  C CZ  . TYR A 1 94  ? -3.74284  -18.24820 36.94552 1.000 18.12701 ? 94  TYR A CZ  1 
ATOM   462  O OH  . TYR A 1 94  ? -2.37034  -18.33880 36.96739 1.000 21.31620 ? 94  TYR A OH  1 
ATOM   463  N N   . PHE A 1 95  ? -10.34304 -17.73935 34.59511 1.000 12.42180 ? 95  PHE A N   1 
ATOM   464  C CA  . PHE A 1 95  ? -11.72098 -18.05134 34.21483 1.000 11.63433 ? 95  PHE A CA  1 
ATOM   465  C C   . PHE A 1 95  ? -11.98211 -19.55287 34.15394 1.000 17.42852 ? 95  PHE A C   1 
ATOM   466  O O   . PHE A 1 95  ? -11.09153 -20.33418 33.83848 1.000 12.82846 ? 95  PHE A O   1 
ATOM   467  C CB  . PHE A 1 95  ? -12.05157 -17.39204 32.86868 1.000 14.63912 ? 95  PHE A CB  1 
ATOM   468  C CG  . PHE A 1 95  ? -11.80354 -15.91385 32.86382 1.000 13.58625 ? 95  PHE A CG  1 
ATOM   469  C CD1 . PHE A 1 95  ? -12.71492 -15.05279 33.44180 1.000 9.36759  ? 95  PHE A CD1 1 
ATOM   470  C CD2 . PHE A 1 95  ? -10.64010 -15.38956 32.32484 1.000 19.21882 ? 95  PHE A CD2 1 
ATOM   471  C CE1 . PHE A 1 95  ? -12.48982 -13.70299 33.46634 1.000 12.25097 ? 95  PHE A CE1 1 
ATOM   472  C CE2 . PHE A 1 95  ? -10.40052 -14.01286 32.35318 1.000 11.52999 ? 95  PHE A CE2 1 
ATOM   473  C CZ  . PHE A 1 95  ? -11.32698 -13.17802 32.91919 1.000 14.37813 ? 95  PHE A CZ  1 
ATOM   474  N N   . ASP A 1 96  ? -13.21411 -19.93349 34.47954 1.000 14.86887 ? 96  ASP A N   1 
ATOM   475  C CA  . ASP A 1 96  ? -13.69301 -21.31419 34.41037 1.000 15.80590 ? 96  ASP A CA  1 
ATOM   476  C C   . ASP A 1 96  ? -13.51576 -21.86985 33.01202 1.000 17.63278 ? 96  ASP A C   1 
ATOM   477  O O   . ASP A 1 96  ? -14.07229 -21.34071 32.04809 1.000 17.29339 ? 96  ASP A O   1 
ATOM   478  C CB  . ASP A 1 96  ? -15.16875 -21.36322 34.81674 1.000 14.83891 ? 96  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 96  ? -15.66632 -22.76545 35.09516 1.000 23.35843 ? 96  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 96  ? -15.25395 -23.72234 34.39938 1.000 19.43456 ? 96  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 96  ? -16.49825 -22.89837 36.01947 1.000 22.15121 ? 96  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 97  ? -12.75047 -22.94949 32.89269 1.000 18.22483 ? 97  GLU A N   1 
ATOM   483  C CA  . GLU A 1 97  ? -12.51367 -23.52874 31.57755 1.000 18.19755 ? 97  GLU A CA  1 
ATOM   484  C C   . GLU A 1 97  ? -13.79318 -24.06265 30.93838 1.000 19.97090 ? 97  GLU A C   1 
ATOM   485  O O   . GLU A 1 97  ? -13.86579 -24.19695 29.72665 1.000 18.44650 ? 97  GLU A O   1 
ATOM   486  C CB  . GLU A 1 97  ? -11.45215 -24.62250 31.66722 1.000 28.15749 ? 97  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 97  ? -10.07156 -24.01256 31.71117 1.000 38.10978 ? 97  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 97  ? -8.96905  -25.03036 31.73740 1.000 47.20985 ? 97  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 97  ? -9.23725  -26.19193 32.13094 1.000 50.25194 ? 97  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 97  ? -7.83560  -24.65325 31.36234 1.000 35.86051 ? 97  GLU A OE2 1 
ATOM   491  N N   . ASN A 1 98  ? -14.81158 -24.32945 31.74633 1.000 22.63705 ? 98  ASN A N   1 
ATOM   492  C CA  . ASN A 1 98  ? -16.08893 -24.80766 31.21481 1.000 28.45098 ? 98  ASN A CA  1 
ATOM   493  C C   . ASN A 1 98  ? -17.10763 -23.69249 31.05673 1.000 26.65588 ? 98  ASN A C   1 
ATOM   494  O O   . ASN A 1 98  ? -18.17612 -23.88282 30.47030 1.000 21.67070 ? 98  ASN A O   1 
ATOM   495  C CB  . ASN A 1 98  ? -16.65738 -25.89813 32.11783 1.000 26.82335 ? 98  ASN A CB  1 
ATOM   496  C CG  . ASN A 1 98  ? -15.82240 -27.15146 32.09483 1.000 29.64859 ? 98  ASN A CG  1 
ATOM   497  O OD1 . ASN A 1 98  ? -15.55857 -27.70056 31.02731 1.000 33.41563 ? 98  ASN A OD1 1 
ATOM   498  N ND2 . ASN A 1 98  ? -15.37906 -27.60191 33.26613 1.000 22.36956 ? 98  ASN A ND2 1 
ATOM   499  N N   . GLU A 1 99  ? -16.77785 -22.52671 31.59689 1.000 23.84507 ? 99  GLU A N   1 
ATOM   500  C CA  . GLU A 1 99  ? -17.67513 -21.38323 31.53008 1.000 23.69591 ? 99  GLU A CA  1 
ATOM   501  C C   . GLU A 1 99  ? -16.84328 -20.11207 31.53593 1.000 17.99401 ? 99  GLU A C   1 
ATOM   502  O O   . GLU A 1 99  ? -16.55663 -19.54945 32.59969 1.000 19.63211 ? 99  GLU A O   1 
ATOM   503  C CB  . GLU A 1 99  ? -18.66370 -21.40433 32.69363 1.000 20.71503 ? 99  GLU A CB  1 
ATOM   504  C CG  . GLU A 1 99  ? -19.68473 -20.30520 32.63164 1.000 25.06490 ? 99  GLU A CG  1 
ATOM   505  C CD  . GLU A 1 99  ? -20.72529 -20.42930 33.71808 1.000 33.68519 ? 99  GLU A CD  1 
ATOM   506  O OE1 . GLU A 1 99  ? -20.61744 -21.37818 34.52174 1.000 26.36141 ? 99  GLU A OE1 1 
ATOM   507  O OE2 . GLU A 1 99  ? -21.64321 -19.57430 33.76432 1.000 32.39748 ? 99  GLU A OE2 1 
ATOM   508  N N   . PRO A 1 100 ? -16.42990 -19.66650 30.33943 1.000 18.05882 ? 100 PRO A N   1 
ATOM   509  C CA  . PRO A 1 100 ? -15.41893 -18.61361 30.20020 1.000 18.30159 ? 100 PRO A CA  1 
ATOM   510  C C   . PRO A 1 100 ? -15.83828 -17.28420 30.84825 1.000 16.87565 ? 100 PRO A C   1 
ATOM   511  O O   . PRO A 1 100 ? -14.97997 -16.45849 31.18935 1.000 16.77097 ? 100 PRO A O   1 
ATOM   512  C CB  . PRO A 1 100 ? -15.27382 -18.47044 28.68064 1.000 23.58262 ? 100 PRO A CB  1 
ATOM   513  C CG  . PRO A 1 100 ? -15.72850 -19.78608 28.12550 1.000 24.70016 ? 100 PRO A CG  1 
ATOM   514  C CD  . PRO A 1 100 ? -16.81760 -20.24769 29.04077 1.000 21.79889 ? 100 PRO A CD  1 
ATOM   515  N N   . GLU A 1 101 ? -17.14279 -17.09629 31.03360 1.000 14.79129 ? 101 GLU A N   1 
ATOM   516  C CA  . GLU A 1 101 ? -17.65842 -15.86963 31.61849 1.000 13.70967 ? 101 GLU A CA  1 
ATOM   517  C C   . GLU A 1 101 ? -17.43217 -15.83801 33.12221 1.000 18.07169 ? 101 GLU A C   1 
ATOM   518  O O   . GLU A 1 101 ? -17.51486 -14.78381 33.74308 1.000 19.25462 ? 101 GLU A O   1 
ATOM   519  C CB  . GLU A 1 101 ? -19.16059 -15.71157 31.31786 1.000 14.74427 ? 101 GLU A CB  1 
ATOM   520  C CG  . GLU A 1 101 ? -19.48529 -15.56780 29.83074 1.000 25.88885 ? 101 GLU A CG  1 
ATOM   521  C CD  . GLU A 1 101 ? -19.36905 -16.88307 29.03964 1.000 33.02792 ? 101 GLU A CD  1 
ATOM   522  O OE1 . GLU A 1 101 ? -19.19449 -16.79922 27.80161 1.000 23.78224 ? 101 GLU A OE1 1 
ATOM   523  O OE2 . GLU A 1 101 ? -19.47142 -17.99056 29.64322 1.000 27.63956 ? 101 GLU A OE2 1 
ATOM   524  N N   . ARG A 1 102 ? -17.16142 -16.99849 33.71165 1.000 17.41805 ? 102 ARG A N   1 
ATOM   525  C CA  . ARG A 1 102 ? -17.11160 -17.09891 35.17074 1.000 18.28417 ? 102 ARG A CA  1 
ATOM   526  C C   . ARG A 1 102 ? -15.68580 -16.98028 35.71151 1.000 14.01363 ? 102 ARG A C   1 
ATOM   527  O O   . ARG A 1 102 ? -14.80135 -17.74255 35.33424 1.000 13.68145 ? 102 ARG A O   1 
ATOM   528  C CB  . ARG A 1 102 ? -17.73772 -18.41612 35.63698 1.000 20.78894 ? 102 ARG A CB  1 
ATOM   529  C CG  . ARG A 1 102 ? -17.65544 -18.62506 37.15270 1.000 20.81170 ? 102 ARG A CG  1 
ATOM   530  C CD  . ARG A 1 102 ? -18.32411 -19.92597 37.60048 1.000 23.02546 ? 102 ARG A CD  1 
ATOM   531  N NE  . ARG A 1 102 ? -18.09431 -20.17493 39.02311 1.000 30.65887 ? 102 ARG A NE  1 
ATOM   532  C CZ  . ARG A 1 102 ? -17.36659 -21.17815 39.50538 1.000 35.34356 ? 102 ARG A CZ  1 
ATOM   533  N NH1 . ARG A 1 102 ? -16.80354 -22.05807 38.68464 1.000 30.16661 ? 102 ARG A NH1 1 
ATOM   534  N NH2 . ARG A 1 102 ? -17.21446 -21.31116 40.81344 1.000 33.51269 ? 102 ARG A NH2 1 
ATOM   535  N N   . ILE A 1 103 ? -15.47601 -16.00874 36.59077 1.000 17.44462 ? 103 ILE A N   1 
ATOM   536  C CA  . ILE A 1 103 ? -14.20532 -15.85846 37.30360 1.000 14.28327 ? 103 ILE A CA  1 
ATOM   537  C C   . ILE A 1 103 ? -14.09023 -16.91972 38.39490 1.000 18.72161 ? 103 ILE A C   1 
ATOM   538  O O   . ILE A 1 103 ? -14.98004 -17.04477 39.22582 1.000 15.42704 ? 103 ILE A O   1 
ATOM   539  C CB  . ILE A 1 103 ? -14.08579 -14.45390 37.94024 1.000 14.73685 ? 103 ILE A CB  1 
ATOM   540  C CG1 . ILE A 1 103 ? -14.10449 -13.37223 36.85274 1.000 10.34472 ? 103 ILE A CG1 1 
ATOM   541  C CG2 . ILE A 1 103 ? -12.82046 -14.34143 38.79403 1.000 14.48710 ? 103 ILE A CG2 1 
ATOM   542  C CD1 . ILE A 1 103 ? -14.43296 -11.99745 37.37437 1.000 12.84628 ? 103 ILE A CD1 1 
ATOM   543  N N   . ILE A 1 104 ? -13.01006 -17.69417 38.40132 1.000 17.83133 ? 104 ILE A N   1 
ATOM   544  C CA  . ILE A 1 104 ? -12.84397 -18.68240 39.46638 1.000 13.89554 ? 104 ILE A CA  1 
ATOM   545  C C   . ILE A 1 104 ? -11.82449 -18.23199 40.50388 1.000 18.41124 ? 104 ILE A C   1 
ATOM   546  O O   . ILE A 1 104 ? -11.87165 -18.67477 41.64623 1.000 17.13572 ? 104 ILE A O   1 
ATOM   547  C CB  . ILE A 1 104 ? -12.44889 -20.07866 38.91212 1.000 16.17261 ? 104 ILE A CB  1 
ATOM   548  C CG1 . ILE A 1 104 ? -11.09163 -20.05760 38.19738 1.000 15.50836 ? 104 ILE A CG1 1 
ATOM   549  C CG2 . ILE A 1 104 ? -13.53362 -20.60312 37.98530 1.000 19.35645 ? 104 ILE A CG2 1 
ATOM   550  C CD1 . ILE A 1 104 ? -10.64071 -21.44901 37.79631 1.000 17.35730 ? 104 ILE A CD1 1 
ATOM   551  N N   . SER A 1 105 ? -10.91844 -17.33430 40.12225 1.000 17.15458 ? 105 SER A N   1 
ATOM   552  C CA  . SER A 1 105 ? -9.99146  -16.74903 41.09372 1.000 18.98339 ? 105 SER A CA  1 
ATOM   553  C C   . SER A 1 105 ? -9.30298  -15.50506 40.54206 1.000 17.36565 ? 105 SER A C   1 
ATOM   554  O O   . SER A 1 105 ? -9.33527  -15.24118 39.33336 1.000 12.17767 ? 105 SER A O   1 
ATOM   555  C CB  . SER A 1 105 ? -8.93210  -17.76985 41.51993 1.000 22.46554 ? 105 SER A CB  1 
ATOM   556  O OG  . SER A 1 105 ? -8.06219  -18.07379 40.44217 1.000 21.73990 ? 105 SER A OG  1 
ATOM   557  N N   . VAL A 1 106 ? -8.69632  -14.73171 41.44083 1.000 14.46101 ? 106 VAL A N   1 
ATOM   558  C CA  . VAL A 1 106 ? -7.78861  -13.67614 41.03033 1.000 13.23553 ? 106 VAL A CA  1 
ATOM   559  C C   . VAL A 1 106 ? -6.54563  -13.73698 41.91141 1.000 20.45041 ? 106 VAL A C   1 
ATOM   560  O O   . VAL A 1 106 ? -6.56821  -14.29222 43.00829 1.000 20.16484 ? 106 VAL A O   1 
ATOM   561  C CB  . VAL A 1 106 ? -8.41747  -12.26149 41.12070 1.000 11.14573 ? 106 VAL A CB  1 
ATOM   562  C CG1 . VAL A 1 106 ? -9.70828  -12.17149 40.29214 1.000 10.49656 ? 106 VAL A CG1 1 
ATOM   563  C CG2 . VAL A 1 106 ? -8.66420  -11.88796 42.55171 1.000 17.11088 ? 106 VAL A CG2 1 
ATOM   564  N N   . VAL A 1 107 ? -5.45176  -13.17404 41.42993 1.000 16.10510 ? 107 VAL A N   1 
ATOM   565  C CA  . VAL A 1 107 ? -4.24163  -13.15852 42.22538 1.000 17.98022 ? 107 VAL A CA  1 
ATOM   566  C C   . VAL A 1 107 ? -3.44070  -11.90360 41.88602 1.000 16.76028 ? 107 VAL A C   1 
ATOM   567  O O   . VAL A 1 107 ? -3.41532  -11.46115 40.73015 1.000 15.81214 ? 107 VAL A O   1 
ATOM   568  C CB  . VAL A 1 107 ? -3.41758  -14.46039 41.98333 1.000 28.80515 ? 107 VAL A CB  1 
ATOM   569  C CG1 . VAL A 1 107 ? -3.06198  -14.60373 40.51951 1.000 27.81661 ? 107 VAL A CG1 1 
ATOM   570  C CG2 . VAL A 1 107 ? -2.17416  -14.51279 42.86334 1.000 30.78685 ? 107 VAL A CG2 1 
ATOM   571  N N   . LYS A 1 108 ? -2.81592  -11.31271 42.89338 1.000 14.79189 ? 108 LYS A N   1 
ATOM   572  C CA  . LYS A 1 108 ? -1.95067  -10.15005 42.67554 1.000 18.56868 ? 108 LYS A CA  1 
ATOM   573  C C   . LYS A 1 108 ? -0.77088  -10.48626 41.75455 1.000 18.04786 ? 108 LYS A C   1 
ATOM   574  O O   . LYS A 1 108 ? -0.22376  -11.59098 41.79948 1.000 17.73493 ? 108 LYS A O   1 
ATOM   575  C CB  . LYS A 1 108 ? -1.43259  -9.61484  44.00971 1.000 18.99496 ? 108 LYS A CB  1 
ATOM   576  C CG  . LYS A 1 108 ? -2.46995  -8.85939  44.82755 1.000 30.73911 ? 108 LYS A CG  1 
ATOM   577  C CD  . LYS A 1 108 ? -1.82335  -8.21473  46.04985 1.000 38.06448 ? 108 LYS A CD  1 
ATOM   578  C CE  . LYS A 1 108 ? -2.83159  -7.42157  46.85967 1.000 48.77103 ? 108 LYS A CE  1 
ATOM   579  N NZ  . LYS A 1 108 ? -3.93259  -8.28678  47.38339 1.000 56.45448 ? 108 LYS A NZ  1 
ATOM   580  N N   . ILE A 1 109 ? -0.36844  -9.54210  40.91474 1.000 16.35277 ? 109 ILE A N   1 
ATOM   581  C CA  . ILE A 1 109 ? 0.70763   -9.84066  39.97362 1.000 18.32606 ? 109 ILE A CA  1 
ATOM   582  C C   . ILE A 1 109 ? 2.06514   -9.38357  40.52577 1.000 19.60845 ? 109 ILE A C   1 
ATOM   583  O O   . ILE A 1 109 ? 2.12593   -8.61012  41.47534 1.000 15.14115 ? 109 ILE A O   1 
ATOM   584  C CB  . ILE A 1 109 ? 0.43611   -9.19536  38.61603 1.000 19.91775 ? 109 ILE A CB  1 
ATOM   585  C CG1 . ILE A 1 109 ? 0.44986   -7.67793  38.73329 1.000 20.22828 ? 109 ILE A CG1 1 
ATOM   586  C CG2 . ILE A 1 109 ? -0.91623  -9.67543  38.05313 1.000 16.02410 ? 109 ILE A CG2 1 
ATOM   587  C CD1 . ILE A 1 109 ? 0.10954   -6.99703  37.42890 1.000 17.15407 ? 109 ILE A CD1 1 
ATOM   588  N N   . SER A 1 110 ? 3.15217   -9.88405  39.94772 1.000 11.76247 ? 110 SER A N   1 
ATOM   589  C CA  . SER A 1 110 ? 4.48867   -9.51944  40.40920 1.000 14.48965 ? 110 SER A CA  1 
ATOM   590  C C   . SER A 1 110 ? 4.88007   -8.12820  39.92568 1.000 11.58488 ? 110 SER A C   1 
ATOM   591  O O   . SER A 1 110 ? 4.18939   -7.53576  39.08551 1.000 12.36739 ? 110 SER A O   1 
ATOM   592  C CB  . SER A 1 110 ? 5.50958   -10.53244 39.90224 1.000 20.24326 ? 110 SER A CB  1 
ATOM   593  O OG  . SER A 1 110 ? 5.63993   -10.42132 38.49380 1.000 15.14496 ? 110 SER A OG  1 
ATOM   594  N N   . ASN A 1 111 ? 6.00907   -7.62352  40.41484 1.000 20.03164 ? 111 ASN A N   1 
ATOM   595  C CA  . ASN A 1 111 ? 6.49899   -6.31700  39.98568 1.000 16.19244 ? 111 ASN A CA  1 
ATOM   596  C C   . ASN A 1 111 ? 6.83732   -6.29374  38.50301 1.000 15.79420 ? 111 ASN A C   1 
ATOM   597  O O   . ASN A 1 111 ? 6.56594   -5.30792  37.82954 1.000 12.58962 ? 111 ASN A O   1 
ATOM   598  C CB  . ASN A 1 111 ? 7.73655   -5.89284  40.78801 1.000 22.61030 ? 111 ASN A CB  1 
ATOM   599  C CG  . ASN A 1 111 ? 7.45275   -5.72441  42.26557 1.000 28.75114 ? 111 ASN A CG  1 
ATOM   600  O OD1 . ASN A 1 111 ? 6.36428   -5.30584  42.66735 1.000 25.81871 ? 111 ASN A OD1 1 
ATOM   601  N ND2 . ASN A 1 111 ? 8.43887   -6.06045  43.08863 1.000 34.30577 ? 111 ASN A ND2 1 
ATOM   602  N N   . SER A 1 112 ? 7.44721   -7.36561  37.99342 1.000 14.44539 ? 112 SER A N   1 
ATOM   603  C CA  . SER A 1 112 ? 7.77874   -7.42535  36.56927 1.000 12.36727 ? 112 SER A CA  1 
ATOM   604  C C   . SER A 1 112 ? 6.52254   -7.55861  35.68871 1.000 16.09702 ? 112 SER A C   1 
ATOM   605  O O   . SER A 1 112 ? 6.45686   -6.97195  34.60558 1.000 11.80811 ? 112 SER A O   1 
ATOM   606  C CB  . SER A 1 112 ? 8.76210   -8.57607  36.27828 1.000 18.07826 ? 112 SER A CB  1 
ATOM   607  O OG  . SER A 1 112 ? 8.28892   -9.83040  36.74514 1.000 19.46096 ? 112 SER A OG  1 
ATOM   608  N N   . GLU A 1 113 ? 5.52802   -8.32820  36.13706 1.000 14.43343 ? 113 GLU A N   1 
ATOM   609  C CA  . GLU A 1 113 ? 4.25055   -8.37716  35.42107 1.000 14.59066 ? 113 GLU A CA  1 
ATOM   610  C C   . GLU A 1 113 ? 3.59662   -6.99490  35.40256 1.000 12.72180 ? 113 GLU A C   1 
ATOM   611  O O   . GLU A 1 113 ? 3.02821   -6.56849  34.38478 1.000 11.95672 ? 113 GLU A O   1 
ATOM   612  C CB  . GLU A 1 113 ? 3.29100   -9.40819  36.05241 1.000 14.30977 ? 113 GLU A CB  1 
ATOM   613  C CG  . GLU A 1 113 ? 3.67030   -10.86614 35.74105 1.000 14.77299 ? 113 GLU A CG  1 
ATOM   614  C CD  . GLU A 1 113 ? 2.81397   -11.87739 36.48835 1.000 18.85970 ? 113 GLU A CD  1 
ATOM   615  O OE1 . GLU A 1 113 ? 2.50016   -11.64276 37.67362 1.000 15.78135 ? 113 GLU A OE1 1 
ATOM   616  O OE2 . GLU A 1 113 ? 2.45192   -12.91529 35.89058 1.000 18.12346 ? 113 GLU A OE2 1 
ATOM   617  N N   . GLU A 1 114 ? 3.65880   -6.29603  36.52964 1.000 8.96627  ? 114 GLU A N   1 
ATOM   618  C CA  . GLU A 1 114 ? 3.03350   -4.98780  36.60297 1.000 8.89151  ? 114 GLU A CA  1 
ATOM   619  C C   . GLU A 1 114 ? 3.75644   -3.98607  35.68729 1.000 14.21366 ? 114 GLU A C   1 
ATOM   620  O O   . GLU A 1 114 ? 3.11454   -3.20373  34.96818 1.000 14.22546 ? 114 GLU A O   1 
ATOM   621  C CB  . GLU A 1 114 ? 3.01127   -4.48026  38.04845 1.000 11.99031 ? 114 GLU A CB  1 
ATOM   622  C CG  . GLU A 1 114 ? 2.39252   -3.09660  38.15783 1.000 15.94507 ? 114 GLU A CG  1 
ATOM   623  C CD  . GLU A 1 114 ? 2.18235   -2.67948  39.60136 1.000 37.24098 ? 114 GLU A CD  1 
ATOM   624  O OE1 . GLU A 1 114 ? 2.57326   -3.44713  40.50228 1.000 44.58405 ? 114 GLU A OE1 1 
ATOM   625  O OE2 . GLU A 1 114 ? 1.62563   -1.58860  39.83423 1.000 50.04799 ? 114 GLU A OE2 1 
ATOM   626  N N   . LYS A 1 115 ? 5.08886   -4.00832  35.71585 1.000 13.50935 ? 115 LYS A N   1 
ATOM   627  C CA  . LYS A 1 115 ? 5.88249   -3.18794  34.79759 1.000 9.11247  ? 115 LYS A CA  1 
ATOM   628  C C   . LYS A 1 115 ? 5.55395   -3.47199  33.33280 1.000 10.45736 ? 115 LYS A C   1 
ATOM   629  O O   . LYS A 1 115 ? 5.34720   -2.54063  32.56383 1.000 13.32612 ? 115 LYS A O   1 
ATOM   630  C CB  . LYS A 1 115 ? 7.37169   -3.40758  35.03379 1.000 13.82620 ? 115 LYS A CB  1 
ATOM   631  C CG  . LYS A 1 115 ? 8.27045   -2.77209  33.96919 1.000 13.43155 ? 115 LYS A CG  1 
ATOM   632  C CD  . LYS A 1 115 ? 9.74968   -2.98481  34.30350 1.000 12.22543 ? 115 LYS A CD  1 
ATOM   633  C CE  . LYS A 1 115 ? 10.64473  -2.24193  33.32684 1.000 20.83505 ? 115 LYS A CE  1 
ATOM   634  N NZ  . LYS A 1 115 ? 12.08868  -2.45211  33.63243 1.000 28.35985 ? 115 LYS A NZ  1 
ATOM   635  N N   . ASN A 1 116 ? 5.52267   -4.74959  32.94280 1.000 10.50429 ? 116 ASN A N   1 
ATOM   636  C CA  . ASN A 1 116 ? 5.24701   -5.10537  31.55057 1.000 9.13432  ? 116 ASN A CA  1 
ATOM   637  C C   . ASN A 1 116 ? 3.85473   -4.65388  31.13612 1.000 12.35531 ? 116 ASN A C   1 
ATOM   638  O O   . ASN A 1 116 ? 3.64791   -4.17495  30.01674 1.000 16.00897 ? 116 ASN A O   1 
ATOM   639  C CB  . ASN A 1 116 ? 5.39309   -6.60861  31.32472 1.000 17.50506 ? 116 ASN A CB  1 
ATOM   640  C CG  . ASN A 1 116 ? 6.83509   -7.06524  31.42446 1.000 41.79617 ? 116 ASN A CG  1 
ATOM   641  O OD1 . ASN A 1 116 ? 7.76092   -6.29022  31.16651 1.000 45.53261 ? 116 ASN A OD1 1 
ATOM   642  N ND2 . ASN A 1 116 ? 7.03632   -8.32513  31.80287 1.000 51.38828 ? 116 ASN A ND2 1 
ATOM   643  N N   . TRP A 1 117 ? 2.90109   -4.79021  32.04327 1.000 12.78786 ? 117 TRP A N   1 
ATOM   644  C CA  . TRP A 1 117 ? 1.55907   -4.31413  31.76252 1.000 14.77993 ? 117 TRP A CA  1 
ATOM   645  C C   . TRP A 1 117 ? 1.56679   -2.79969  31.57695 1.000 14.86244 ? 117 TRP A C   1 
ATOM   646  O O   . TRP A 1 117 ? 1.04179   -2.29256  30.59354 1.000 15.24428 ? 117 TRP A O   1 
ATOM   647  C CB  . TRP A 1 117 ? 0.59279   -4.69590  32.87096 1.000 17.34527 ? 117 TRP A CB  1 
ATOM   648  C CG  . TRP A 1 117 ? -0.82239  -4.27157  32.58770 1.000 14.50199 ? 117 TRP A CG  1 
ATOM   649  C CD1 . TRP A 1 117 ? -1.76479  -4.97300  31.87191 1.000 13.07902 ? 117 TRP A CD1 1 
ATOM   650  C CD2 . TRP A 1 117 ? -1.47467  -3.07012  33.04220 1.000 14.88337 ? 117 TRP A CD2 1 
ATOM   651  N NE1 . TRP A 1 117 ? -2.94989  -4.27159  31.84361 1.000 10.92128 ? 117 TRP A NE1 1 
ATOM   652  C CE2 . TRP A 1 117 ? -2.79663  -3.10255  32.55041 1.000 18.44155 ? 117 TRP A CE2 1 
ATOM   653  C CE3 . TRP A 1 117 ? -1.06282  -1.96983  33.80516 1.000 14.72951 ? 117 TRP A CE3 1 
ATOM   654  C CZ2 . TRP A 1 117 ? -3.70592  -2.08432  32.80144 1.000 11.94380 ? 117 TRP A CZ2 1 
ATOM   655  C CZ3 . TRP A 1 117 ? -1.96659  -0.95235  34.05600 1.000 17.53302 ? 117 TRP A CZ3 1 
ATOM   656  C CH2 . TRP A 1 117 ? -3.27728  -1.01821  33.55953 1.000 14.71333 ? 117 TRP A CH2 1 
ATOM   657  N N   . ASN A 1 118 ? 2.18097   -2.07903  32.51005 1.000 11.00183 ? 118 ASN A N   1 
ATOM   658  C CA  . ASN A 1 118 ? 2.23758   -0.61626  32.41696 1.000 11.23616 ? 118 ASN A CA  1 
ATOM   659  C C   . ASN A 1 118 ? 2.93728   -0.09413  31.16481 1.000 15.41760 ? 118 ASN A C   1 
ATOM   660  O O   . ASN A 1 118 ? 2.56178   0.95563   30.64111 1.000 12.90814 ? 118 ASN A O   1 
ATOM   661  C CB  . ASN A 1 118 ? 2.92510   -0.03540  33.64789 1.000 10.61602 ? 118 ASN A CB  1 
ATOM   662  C CG  . ASN A 1 118 ? 1.98255   0.11915   34.81769 1.000 16.57862 ? 118 ASN A CG  1 
ATOM   663  O OD1 . ASN A 1 118 ? 0.87833   0.60598   34.66581 1.000 23.00080 ? 118 ASN A OD1 1 
ATOM   664  N ND2 . ASN A 1 118 ? 2.42760   -0.28283  35.99448 1.000 21.54939 ? 118 ASN A ND2 1 
ATOM   665  N N   . LEU A 1 119 ? 3.95035   -0.81218  30.68420 1.000 12.24720 ? 119 LEU A N   1 
ATOM   666  C CA  . LEU A 1 119 ? 4.69828   -0.36364  29.50114 1.000 19.65831 ? 119 LEU A CA  1 
ATOM   667  C C   . LEU A 1 119 ? 3.84176   -0.30441  28.22983 1.000 19.98453 ? 119 LEU A C   1 
ATOM   668  O O   . LEU A 1 119 ? 4.22866   0.34173   27.24943 1.000 14.80633 ? 119 LEU A O   1 
ATOM   669  C CB  . LEU A 1 119 ? 5.91775   -1.26757  29.24695 1.000 17.82426 ? 119 LEU A CB  1 
ATOM   670  C CG  . LEU A 1 119 ? 7.02809   -1.15664  30.30443 1.000 28.52175 ? 119 LEU A CG  1 
ATOM   671  C CD1 . LEU A 1 119 ? 8.29392   -1.91255  29.89761 1.000 25.26206 ? 119 LEU A CD1 1 
ATOM   672  C CD2 . LEU A 1 119 ? 7.34752   0.28280   30.63058 1.000 24.99226 ? 119 LEU A CD2 1 
ATOM   673  N N   . ASN A 1 120 ? 2.68785   -0.97154  28.23130 1.000 12.60757 ? 120 ASN A N   1 
ATOM   674  C CA  . ASN A 1 120 ? 1.79261   -0.90589  27.07254 1.000 10.90452 ? 120 ASN A CA  1 
ATOM   675  C C   . ASN A 1 120 ? 0.61913   0.06347   27.21737 1.000 17.28459 ? 120 ASN A C   1 
ATOM   676  O O   . ASN A 1 120 ? -0.24179  0.13627   26.33409 1.000 16.14969 ? 120 ASN A O   1 
ATOM   677  C CB  . ASN A 1 120 ? 1.25391   -2.28838  26.74877 1.000 10.00154 ? 120 ASN A CB  1 
ATOM   678  C CG  . ASN A 1 120 ? 2.31615   -3.20238  26.15668 1.000 18.25780 ? 120 ASN A CG  1 
ATOM   679  O OD1 . ASN A 1 120 ? 3.16213   -2.77332  25.38303 1.000 20.81407 ? 120 ASN A OD1 1 
ATOM   680  N ND2 . ASN A 1 120 ? 2.26974   -4.46454  26.52420 1.000 24.07075 ? 120 ASN A ND2 1 
ATOM   681  N N   . VAL A 1 121 ? 0.59856   0.81457   28.31474 1.000 14.67578 ? 121 VAL A N   1 
ATOM   682  C CA  . VAL A 1 121 ? -0.52373  1.68840   28.63484 1.000 15.46043 ? 121 VAL A CA  1 
ATOM   683  C C   . VAL A 1 121 ? -0.17872  3.17638   28.50742 1.000 19.90054 ? 121 VAL A C   1 
ATOM   684  O O   . VAL A 1 121 ? 0.86880   3.63495   28.97073 1.000 16.92123 ? 121 VAL A O   1 
ATOM   685  C CB  . VAL A 1 121 ? -1.04764  1.40990   30.07344 1.000 16.20657 ? 121 VAL A CB  1 
ATOM   686  C CG1 . VAL A 1 121 ? -2.05445  2.46865   30.51316 1.000 18.13785 ? 121 VAL A CG1 1 
ATOM   687  C CG2 . VAL A 1 121 ? -1.67770  0.03689   30.13623 1.000 13.85042 ? 121 VAL A CG2 1 
ATOM   688  N N   . LYS A 1 122 ? -1.06828  3.91784   27.85652 1.000 16.07840 ? 122 LYS A N   1 
ATOM   689  C CA  . LYS A 1 122 ? -0.98437  5.36875   27.80896 1.000 12.73087 ? 122 LYS A CA  1 
ATOM   690  C C   . LYS A 1 122 ? -2.34416  5.97120   28.09672 1.000 15.04383 ? 122 LYS A C   1 
ATOM   691  O O   . LYS A 1 122 ? -3.37143  5.37966   27.78360 1.000 17.05793 ? 122 LYS A O   1 
ATOM   692  C CB  . LYS A 1 122 ? -0.49434  5.83412   26.44471 1.000 10.62202 ? 122 LYS A CB  1 
ATOM   693  C CG  . LYS A 1 122 ? 0.93033   5.41319   26.14252 1.000 21.97425 ? 122 LYS A CG  1 
ATOM   694  C CD  . LYS A 1 122 ? 1.89280   6.45194   26.68636 1.000 31.48872 ? 122 LYS A CD  1 
ATOM   695  C CE  . LYS A 1 122 ? 3.31346   5.94740   26.74545 1.000 40.48185 ? 122 LYS A CE  1 
ATOM   696  N NZ  . LYS A 1 122 ? 4.29155   7.05099   27.01610 1.000 49.22899 ? 122 LYS A NZ  1 
ATOM   697  N N   . TYR A 1 123 ? -2.35328  7.14815   28.70839 1.000 14.82544 ? 123 TYR A N   1 
ATOM   698  C CA  . TYR A 1 123 ? -3.58033  7.91018   28.78971 1.000 17.91286 ? 123 TYR A CA  1 
ATOM   699  C C   . TYR A 1 123 ? -3.40251  9.14500   27.91049 1.000 19.69158 ? 123 TYR A C   1 
ATOM   700  O O   . TYR A 1 123 ? -2.56141  9.99611   28.17786 1.000 34.76622 ? 123 TYR A O   1 
ATOM   701  C CB  . TYR A 1 123 ? -3.90756  8.27256   30.23787 1.000 11.15606 ? 123 TYR A CB  1 
ATOM   702  C CG  . TYR A 1 123 ? -4.30664  7.07878   31.07954 1.000 14.23186 ? 123 TYR A CG  1 
ATOM   703  C CD1 . TYR A 1 123 ? -3.34464  6.27100   31.68402 1.000 14.19937 ? 123 TYR A CD1 1 
ATOM   704  C CD2 . TYR A 1 123 ? -5.64580  6.74146   31.24787 1.000 16.05086 ? 123 TYR A CD2 1 
ATOM   705  C CE1 . TYR A 1 123 ? -3.70619  5.17428   32.45426 1.000 14.12247 ? 123 TYR A CE1 1 
ATOM   706  C CE2 . TYR A 1 123 ? -6.01951  5.64451   32.01086 1.000 18.03499 ? 123 TYR A CE2 1 
ATOM   707  C CZ  . TYR A 1 123 ? -5.04670  4.86623   32.60881 1.000 19.00914 ? 123 TYR A CZ  1 
ATOM   708  O OH  . TYR A 1 123 ? -5.42010  3.78487   33.36603 1.000 24.50284 ? 123 TYR A OH  1 
ATOM   709  N N   . ASP A 1 124 ? -4.17893  9.21270   26.83961 1.000 29.39806 ? 124 ASP A N   1 
ATOM   710  C CA  . ASP A 1 124 ? -4.08699  10.29650  25.87929 1.000 27.40624 ? 124 ASP A CA  1 
ATOM   711  C C   . ASP A 1 124 ? -5.37204  10.35600  25.09342 1.000 32.85782 ? 124 ASP A C   1 
ATOM   712  O O   . ASP A 1 124 ? -5.95924  9.31670   24.78144 1.000 27.82641 ? 124 ASP A O   1 
ATOM   713  C CB  . ASP A 1 124 ? -2.90404  10.10070  24.92857 1.000 39.25755 ? 124 ASP A CB  1 
ATOM   714  C CG  . ASP A 1 124 ? -1.76642  11.05487  25.21034 1.000 53.75409 ? 124 ASP A CG  1 
ATOM   715  O OD1 . ASP A 1 124 ? -0.94854  10.77560  26.11840 1.000 64.00165 ? 124 ASP A OD1 1 
ATOM   716  O OD2 . ASP A 1 124 ? -1.68905  12.08554  24.51394 1.000 56.70582 ? 124 ASP A OD2 1 
ATOM   717  N N   . GLU A 1 125 ? -5.82000  11.57124  24.79382 1.000 24.59349 ? 125 GLU A N   1 
ATOM   718  C CA  . GLU A 1 125 ? -6.95782  11.76981  23.90131 1.000 39.99096 ? 125 GLU A CA  1 
ATOM   719  C C   . GLU A 1 125 ? -6.69492  11.10760  22.55291 1.000 35.42152 ? 125 GLU A C   1 
ATOM   720  O O   . GLU A 1 125 ? -5.55856  11.09630  22.08794 1.000 32.78889 ? 125 GLU A O   1 
ATOM   721  C CB  . GLU A 1 125 ? -7.22101  13.26617  23.70133 1.000 45.64625 ? 125 GLU A CB  1 
ATOM   722  C CG  . GLU A 1 125 ? -7.91459  13.94153  24.86382 1.000 54.25532 ? 125 GLU A CG  1 
ATOM   723  C CD  . GLU A 1 125 ? -9.41017  13.98744  24.67118 1.000 65.62900 ? 125 GLU A CD  1 
ATOM   724  O OE1 . GLU A 1 125 ? -10.14351 13.62601  25.61765 1.000 70.43742 ? 125 GLU A OE1 1 
ATOM   725  O OE2 . GLU A 1 125 ? -9.84721  14.38536  23.56794 1.000 64.96008 ? 125 GLU A OE2 1 
ATOM   726  N N   . THR A 1 126 ? -7.72823  10.54962  21.92599 1.000 29.96486 ? 126 THR A N   1 
ATOM   727  C CA  . THR A 1 126 ? -7.57469  10.13606  20.53968 1.000 31.74388 ? 126 THR A CA  1 
ATOM   728  C C   . THR A 1 126 ? -7.26575  11.37712  19.69483 1.000 22.05657 ? 126 THR A C   1 
ATOM   729  O O   . THR A 1 126 ? -7.80216  12.45889  19.94595 1.000 22.29725 ? 126 THR A O   1 
ATOM   730  C CB  . THR A 1 126 ? -8.82587  9.41577   19.97803 1.000 32.33635 ? 126 THR A CB  1 
ATOM   731  O OG1 . THR A 1 126 ? -8.58890  9.05380   18.61088 1.000 22.34966 ? 126 THR A OG1 1 
ATOM   732  C CG2 . THR A 1 126 ? -10.05821 10.30536  20.04901 1.000 30.19496 ? 126 THR A CG2 1 
ATOM   733  N N   . PRO A 1 127 ? -6.37231  11.23593  18.70622 1.000 21.99165 ? 127 PRO A N   1 
ATOM   734  C CA  . PRO A 1 127 ? -6.11199  12.37806  17.82301 1.000 22.29691 ? 127 PRO A CA  1 
ATOM   735  C C   . PRO A 1 127 ? -7.31249  12.70264  16.95073 1.000 22.77461 ? 127 PRO A C   1 
ATOM   736  O O   . PRO A 1 127 ? -7.48933  13.84467  16.54846 1.000 23.24934 ? 127 PRO A O   1 
ATOM   737  C CB  . PRO A 1 127 ? -4.94348  11.90464  16.95122 1.000 22.26980 ? 127 PRO A CB  1 
ATOM   738  C CG  . PRO A 1 127 ? -4.40561  10.66377  17.61246 1.000 21.91950 ? 127 PRO A CG  1 
ATOM   739  C CD  . PRO A 1 127 ? -5.52843  10.07079  18.38655 1.000 24.75145 ? 127 PRO A CD  1 
ATOM   740  N N   . PHE A 1 128 ? -8.12915  11.69833  16.66066 1.000 22.80814 ? 128 PHE A N   1 
ATOM   741  C CA  . PHE A 1 128 ? -9.13961  11.84235  15.62412 1.000 25.85889 ? 128 PHE A CA  1 
ATOM   742  C C   . PHE A 1 128 ? -10.53416 12.03373  16.19048 1.000 27.92675 ? 128 PHE A C   1 
ATOM   743  O O   . PHE A 1 128 ? -11.01231 11.23486  16.98631 1.000 32.77395 ? 128 PHE A O   1 
ATOM   744  C CB  . PHE A 1 128 ? -9.11493  10.63027  14.69977 1.000 23.31843 ? 128 PHE A CB  1 
ATOM   745  C CG  . PHE A 1 128 ? -7.75391  10.31375  14.16566 1.000 22.95819 ? 128 PHE A CG  1 
ATOM   746  C CD1 . PHE A 1 128 ? -7.10273  11.20780  13.32073 1.000 23.27202 ? 128 PHE A CD1 1 
ATOM   747  C CD2 . PHE A 1 128 ? -7.12355  9.11869   14.49487 1.000 27.90054 ? 128 PHE A CD2 1 
ATOM   748  C CE1 . PHE A 1 128 ? -5.84123  10.92403  12.82401 1.000 25.76046 ? 128 PHE A CE1 1 
ATOM   749  C CE2 . PHE A 1 128 ? -5.85924  8.82131   13.99549 1.000 27.78596 ? 128 PHE A CE2 1 
ATOM   750  C CZ  . PHE A 1 128 ? -5.21767  9.72719   13.16026 1.000 26.68355 ? 128 PHE A CZ  1 
ATOM   751  N N   . LYS A 1 129 ? -11.18726 13.10151  15.76018 1.000 29.14652 ? 129 LYS A N   1 
ATOM   752  C CA  . LYS A 1 129 ? -12.50891 13.40516  16.26287 1.000 37.32351 ? 129 LYS A CA  1 
ATOM   753  C C   . LYS A 1 129 ? -13.54426 13.23900  15.16901 1.000 35.74584 ? 129 LYS A C   1 
ATOM   754  O O   . LYS A 1 129 ? -14.69389 12.93229  15.46123 1.000 34.87085 ? 129 LYS A O   1 
ATOM   755  C CB  . LYS A 1 129 ? -12.55289 14.82188  16.84782 1.000 36.81992 ? 129 LYS A CB  1 
ATOM   756  C CG  . LYS A 1 129 ? -11.58879 15.01851  18.02923 1.000 43.19207 ? 129 LYS A CG  1 
ATOM   757  C CD  . LYS A 1 129 ? -12.12713 16.01538  19.05492 1.000 60.90247 ? 129 LYS A CD  1 
ATOM   758  C CE  . LYS A 1 129 ? -13.10738 15.36019  20.03231 1.000 69.07773 ? 129 LYS A CE  1 
ATOM   759  N NZ  . LYS A 1 129 ? -13.77881 16.35723  20.92445 1.000 69.53520 ? 129 LYS A NZ  1 
ATOM   760  N N   . THR A 1 130 ? -13.13769 13.43689  13.91482 1.000 31.13071 ? 130 THR A N   1 
ATOM   761  C CA  . THR A 1 130 ? -14.06336 13.32603  12.78807 1.000 37.85994 ? 130 THR A CA  1 
ATOM   762  C C   . THR A 1 130 ? -13.49369 12.46774  11.66759 1.000 37.07798 ? 130 THR A C   1 
ATOM   763  O O   . THR A 1 130 ? -12.32134 12.08990  11.68523 1.000 34.72368 ? 130 THR A O   1 
ATOM   764  C CB  . THR A 1 130 ? -14.43962 14.71563  12.17591 1.000 34.80313 ? 130 THR A CB  1 
ATOM   765  O OG1 . THR A 1 130 ? -13.31754 15.25189  11.46362 1.000 35.35450 ? 130 THR A OG1 1 
ATOM   766  C CG2 . THR A 1 130 ? -14.88457 15.70242  13.24357 1.000 38.47809 ? 130 THR A CG2 1 
ATOM   767  N N   . ILE A 1 131 ? -14.34703 12.17983  10.69123 1.000 33.86961 ? 131 ILE A N   1 
ATOM   768  C CA  . ILE A 1 131 ? -13.96905 11.46873  9.47777  1.000 32.03904 ? 131 ILE A CA  1 
ATOM   769  C C   . ILE A 1 131 ? -12.96887 12.28204  8.66102  1.000 35.26120 ? 131 ILE A C   1 
ATOM   770  O O   . ILE A 1 131 ? -12.01857 11.73688  8.08797  1.000 37.34866 ? 131 ILE A O   1 
ATOM   771  C CB  . ILE A 1 131 ? -15.22401 11.15813  8.61060  1.000 50.36207 ? 131 ILE A CB  1 
ATOM   772  C CG1 . ILE A 1 131 ? -15.95852 9.92478   9.14448  1.000 43.54163 ? 131 ILE A CG1 1 
ATOM   773  C CG2 . ILE A 1 131 ? -14.85518 10.96947  7.13805  1.000 49.04672 ? 131 ILE A CG2 1 
ATOM   774  C CD1 . ILE A 1 131 ? -15.28306 8.60647   8.80072  1.000 34.71715 ? 131 ILE A CD1 1 
ATOM   775  N N   . GLU A 1 132 ? -13.18831 13.59218  8.60807  1.000 30.84227 ? 132 GLU A N   1 
ATOM   776  C CA  . GLU A 1 132 ? -12.29592 14.46966  7.87053  1.000 34.10983 ? 132 GLU A CA  1 
ATOM   777  C C   . GLU A 1 132 ? -10.89027 14.40476  8.45410  1.000 31.89542 ? 132 GLU A C   1 
ATOM   778  O O   . GLU A 1 132 ? -9.91093  14.56680  7.72489  1.000 30.20484 ? 132 GLU A O   1 
ATOM   779  C CB  . GLU A 1 132 ? -12.81185 15.91151  7.87837  1.000 37.63528 ? 132 GLU A CB  1 
ATOM   780  C CG  . GLU A 1 132 ? -11.95380 16.88349  7.07505  1.000 58.42127 ? 132 GLU A CG  1 
ATOM   781  C CD  . GLU A 1 132 ? -11.98931 16.60733  5.57771  1.000 72.36805 ? 132 GLU A CD  1 
ATOM   782  O OE1 . GLU A 1 132 ? -12.95700 15.96162  5.11731  1.000 78.08811 ? 132 GLU A OE1 1 
ATOM   783  O OE2 . GLU A 1 132 ? -11.05046 17.03353  4.86595  1.000 72.71120 ? 132 GLU A OE2 1 
ATOM   784  N N   . ASP A 1 133 ? -10.79179 14.17405  9.76296  1.000 28.29746 ? 133 ASP A N   1 
ATOM   785  C CA  . ASP A 1 133 ? -9.48865  14.01837  10.40243 1.000 26.23676 ? 133 ASP A CA  1 
ATOM   786  C C   . ASP A 1 133 ? -8.74073  12.83762  9.80712  1.000 25.64869 ? 133 ASP A C   1 
ATOM   787  O O   . ASP A 1 133 ? -7.52705  12.90048  9.64156  1.000 31.74633 ? 133 ASP A O   1 
ATOM   788  C CB  . ASP A 1 133 ? -9.62409  13.83716  11.91297 1.000 25.53243 ? 133 ASP A CB  1 
ATOM   789  C CG  . ASP A 1 133 ? -10.01625 15.12051  12.62463 1.000 28.26312 ? 133 ASP A CG  1 
ATOM   790  O OD1 . ASP A 1 133 ? -9.86674  16.21756  12.03239 1.000 26.82475 ? 133 ASP A OD1 1 
ATOM   791  O OD2 . ASP A 1 133 ? -10.47136 15.02958  13.78287 1.000 28.55702 ? 133 ASP A OD2 1 
ATOM   792  N N   . LEU A 1 134 ? -9.46690  11.76820  9.48284  1.000 25.54680 ? 134 LEU A N   1 
ATOM   793  C CA  . LEU A 1 134 ? -8.85027  10.56803  8.90768  1.000 25.05672 ? 134 LEU A CA  1 
ATOM   794  C C   . LEU A 1 134 ? -8.33887  10.84430  7.50363  1.000 29.66264 ? 134 LEU A C   1 
ATOM   795  O O   . LEU A 1 134 ? -7.27683  10.35638  7.11041  1.000 28.34755 ? 134 LEU A O   1 
ATOM   796  C CB  . LEU A 1 134 ? -9.83898  9.39790   8.86877  1.000 24.99069 ? 134 LEU A CB  1 
ATOM   797  C CG  . LEU A 1 134 ? -10.45998 8.99359   10.19989 1.000 30.46770 ? 134 LEU A CG  1 
ATOM   798  C CD1 . LEU A 1 134 ? -11.32211 7.75393   10.00422 1.000 33.59972 ? 134 LEU A CD1 1 
ATOM   799  C CD2 . LEU A 1 134 ? -9.37423  8.76429   11.24989 1.000 23.85051 ? 134 LEU A CD2 1 
ATOM   800  N N   . ASN A 1 135 ? -9.08942  11.64948  6.75595  1.000 31.63683 ? 135 ASN A N   1 
ATOM   801  C CA  . ASN A 1 135 ? -8.69386  12.05574  5.40661  1.000 47.15283 ? 135 ASN A CA  1 
ATOM   802  C C   . ASN A 1 135 ? -7.44583  12.92819  5.42638  1.000 56.27280 ? 135 ASN A C   1 
ATOM   803  O O   . ASN A 1 135 ? -7.04792  13.48333  4.40202  1.000 67.49742 ? 135 ASN A O   1 
ATOM   804  C CB  . ASN A 1 135 ? -9.83958  12.79460  4.71199  1.000 51.46622 ? 135 ASN A CB  1 
ATOM   805  C CG  . ASN A 1 135 ? -11.06796 11.92449  4.53559  1.000 62.35576 ? 135 ASN A CG  1 
ATOM   806  O OD1 . ASN A 1 135 ? -10.95971 10.72731  4.27490  1.000 63.53279 ? 135 ASN A OD1 1 
ATOM   807  N ND2 . ASN A 1 135 ? -12.24459 12.52138  4.68392  1.000 66.01319 ? 135 ASN A ND2 1 
ATOM   808  N N   . ARG A 1 136 ? -6.86222  13.05055  6.61668  1.000 55.12194 ? 136 ARG A N   1 
ATOM   809  C CA  . ARG A 1 136 ? -5.56839  13.67050  6.84487  1.000 56.29234 ? 136 ARG A CA  1 
ATOM   810  C C   . ARG A 1 136 ? -5.67181  15.17919  6.71463  1.000 61.90211 ? 136 ARG A C   1 
ATOM   811  O O   . ARG A 1 136 ? -6.20345  15.83973  7.60958  1.000 62.56751 ? 136 ARG A O   1 
ATOM   812  C CB  . ARG A 1 136 ? -4.52172  13.08859  5.88611  1.000 55.67131 ? 136 ARG A CB  1 
ATOM   813  C CG  . ARG A 1 136 ? -4.43661  11.56923  5.94987  1.000 57.35098 ? 136 ARG A CG  1 
ATOM   814  C CD  . ARG A 1 136 ? -3.32809  11.04437  5.07239  1.000 71.88932 ? 136 ARG A CD  1 
ATOM   815  N NE  . ARG A 1 136 ? -2.38288  10.22014  5.82342  1.000 78.95271 ? 136 ARG A NE  1 
ATOM   816  C CZ  . ARG A 1 136 ? -1.19853  9.83396   5.35554  1.000 84.11445 ? 136 ARG A CZ  1 
ATOM   817  N NH1 . ARG A 1 136 ? -0.81207  10.20240  4.13765  1.000 89.93145 ? 136 ARG A NH1 1 
ATOM   818  N NH2 . ARG A 1 136 ? -0.39759  9.08490   6.10344  1.000 78.84630 ? 136 ARG A NH2 1 
ATOM   819  N N   . SER A 1 145 ? -1.91474  3.86882   0.32008  1.000 28.21995 ? 145 SER A N   1 
ATOM   820  C CA  . SER A 1 145 ? -1.37325  3.17745   1.48853  1.000 38.01339 ? 145 SER A CA  1 
ATOM   821  C C   . SER A 1 145 ? -2.48266  2.88197   2.47711  1.000 30.28194 ? 145 SER A C   1 
ATOM   822  O O   . SER A 1 145 ? -2.60753  1.75814   2.95009  1.000 24.83297 ? 145 SER A O   1 
ATOM   823  C CB  . SER A 1 145 ? -0.28076  3.99283   2.16373  1.000 46.02359 ? 145 SER A CB  1 
ATOM   824  O OG  . SER A 1 145 ? 0.09439   3.37869   3.38083  1.000 48.19611 ? 145 SER A OG  1 
ATOM   825  N N   . PHE A 1 146 ? -3.27911  3.90186   2.79309  1.000 31.95235 ? 146 PHE A N   1 
ATOM   826  C CA  . PHE A 1 146 ? -4.59454  3.68779   3.39905  1.000 31.70804 ? 146 PHE A CA  1 
ATOM   827  C C   . PHE A 1 146 ? -5.60752  3.39078   2.29376  1.000 31.25197 ? 146 PHE A C   1 
ATOM   828  O O   . PHE A 1 146 ? -6.74119  2.99845   2.56326  1.000 35.16994 ? 146 PHE A O   1 
ATOM   829  C CB  . PHE A 1 146 ? -5.06087  4.90966   4.19436  1.000 33.80144 ? 146 PHE A CB  1 
ATOM   830  C CG  . PHE A 1 146 ? -4.35152  5.10231   5.49785  1.000 32.39704 ? 146 PHE A CG  1 
ATOM   831  C CD1 . PHE A 1 146 ? -4.75778  4.41661   6.62690  1.000 34.77260 ? 146 PHE A CD1 1 
ATOM   832  C CD2 . PHE A 1 146 ? -3.29748  5.99038   5.60162  1.000 34.71892 ? 146 PHE A CD2 1 
ATOM   833  C CE1 . PHE A 1 146 ? -4.11352  4.59818   7.83085  1.000 41.79351 ? 146 PHE A CE1 1 
ATOM   834  C CE2 . PHE A 1 146 ? -2.65116  6.17850   6.80602  1.000 36.67664 ? 146 PHE A CE2 1 
ATOM   835  C CZ  . PHE A 1 146 ? -3.05606  5.48056   7.92104  1.000 37.29885 ? 146 PHE A CZ  1 
ATOM   836  N N   . ASP A 1 147 ? -5.19374  3.59831   1.04716  1.000 27.14785 ? 147 ASP A N   1 
ATOM   837  C CA  . ASP A 1 147 ? -6.10253  3.47575   -0.08837 1.000 25.69196 ? 147 ASP A CA  1 
ATOM   838  C C   . ASP A 1 147 ? -6.11409  2.06767   -0.68439 1.000 30.06002 ? 147 ASP A C   1 
ATOM   839  O O   . ASP A 1 147 ? -5.08125  1.56190   -1.11608 1.000 34.89083 ? 147 ASP A O   1 
ATOM   840  C CB  . ASP A 1 147 ? -5.73134  4.48983   -1.17288 1.000 26.58282 ? 147 ASP A CB  1 
ATOM   841  C CG  . ASP A 1 147 ? -6.05930  5.92411   -0.77915 1.000 44.05223 ? 147 ASP A CG  1 
ATOM   842  O OD1 . ASP A 1 147 ? -6.68122  6.13637   0.28365  1.000 38.02640 ? 147 ASP A OD1 1 
ATOM   843  O OD2 . ASP A 1 147 ? -5.70603  6.84494   -1.54547 1.000 51.24712 ? 147 ASP A OD2 1 
ATOM   844  N N   . PHE A 1 148 ? -7.29066  1.44686   -0.70227 1.000 25.51336 ? 148 PHE A N   1 
ATOM   845  C CA  . PHE A 1 148 ? -7.48700  0.13724   -1.32705 1.000 25.48103 ? 148 PHE A CA  1 
ATOM   846  C C   . PHE A 1 148 ? -8.35918  0.32793   -2.55978 1.000 29.10549 ? 148 PHE A C   1 
ATOM   847  O O   . PHE A 1 148 ? -9.32570  1.08467   -2.51197 1.000 26.73648 ? 148 PHE A O   1 
ATOM   848  C CB  . PHE A 1 148 ? -8.18385  -0.84924  -0.37711 1.000 25.11547 ? 148 PHE A CB  1 
ATOM   849  C CG  . PHE A 1 148 ? -7.32010  -1.37795  0.74127  1.000 24.51653 ? 148 PHE A CG  1 
ATOM   850  C CD1 . PHE A 1 148 ? -6.87158  -0.54316  1.75958  1.000 27.49522 ? 148 PHE A CD1 1 
ATOM   851  C CD2 . PHE A 1 148 ? -7.01532  -2.73039  0.80854  1.000 24.37097 ? 148 PHE A CD2 1 
ATOM   852  C CE1 . PHE A 1 148 ? -6.10283  -1.04403  2.80663  1.000 28.10881 ? 148 PHE A CE1 1 
ATOM   853  C CE2 . PHE A 1 148 ? -6.25084  -3.23704  1.85251  1.000 36.02408 ? 148 PHE A CE2 1 
ATOM   854  C CZ  . PHE A 1 148 ? -5.79419  -2.39080  2.85479  1.000 30.65076 ? 148 PHE A CZ  1 
ATOM   855  N N   . THR A 1 149 ? -8.06122  -0.35646  -3.65760 1.000 26.46014 ? 149 THR A N   1 
ATOM   856  C CA  . THR A 1 149 ? -9.05745  -0.41451  -4.73032 1.000 30.97615 ? 149 THR A CA  1 
ATOM   857  C C   . THR A 1 149 ? -10.22342 -1.26790  -4.24728 1.000 31.51893 ? 149 THR A C   1 
ATOM   858  O O   . THR A 1 149 ? -10.13111 -1.92886  -3.21014 1.000 28.73960 ? 149 THR A O   1 
ATOM   859  C CB  . THR A 1 149 ? -8.50910  -1.00590  -6.03760 1.000 34.44052 ? 149 THR A CB  1 
ATOM   860  O OG1 . THR A 1 149 ? -8.12249  -2.37131  -5.81846 1.000 29.06117 ? 149 THR A OG1 1 
ATOM   861  C CG2 . THR A 1 149 ? -7.31588  -0.17625  -6.55826 1.000 27.78463 ? 149 THR A CG2 1 
ATOM   862  N N   . THR A 1 150 ? -11.32090 -1.25570  -4.98817 1.000 25.79442 ? 150 THR A N   1 
ATOM   863  C CA  . THR A 1 150 ? -12.46386 -2.08649  -4.63738 1.000 28.30672 ? 150 THR A CA  1 
ATOM   864  C C   . THR A 1 150 ? -12.07230 -3.55710  -4.57420 1.000 36.92697 ? 150 THR A C   1 
ATOM   865  O O   . THR A 1 150 ? -12.45792 -4.27666  -3.65097 1.000 32.91432 ? 150 THR A O   1 
ATOM   866  C CB  . THR A 1 150 ? -13.61577 -1.88900  -5.63460 1.000 38.12223 ? 150 THR A CB  1 
ATOM   867  O OG1 . THR A 1 150 ? -14.20920 -0.60324  -5.40881 1.000 38.45832 ? 150 THR A OG1 1 
ATOM   868  C CG2 . THR A 1 150 ? -14.68002 -2.96949  -5.45999 1.000 41.58005 ? 150 THR A CG2 1 
ATOM   869  N N   . THR A 1 151 ? -11.26752 -4.00188  -5.52894 1.000 38.32077 ? 151 THR A N   1 
ATOM   870  C CA  . THR A 1 151 ? -10.90161 -5.40863  -5.55071 1.000 37.52138 ? 151 THR A CA  1 
ATOM   871  C C   . THR A 1 151 ? -9.77550  -5.69377  -4.55446 1.000 35.41660 ? 151 THR A C   1 
ATOM   872  O O   . THR A 1 151 ? -9.68885  -6.80165  -4.02208 1.000 32.88623 ? 151 THR A O   1 
ATOM   873  C CB  . THR A 1 151 ? -10.51476 -5.88148  -6.97961 1.000 44.15322 ? 151 THR A CB  1 
ATOM   874  O OG1 . THR A 1 151 ? -9.40808  -5.12146  -7.47353 1.000 44.84853 ? 151 THR A OG1 1 
ATOM   875  C CG2 . THR A 1 151 ? -11.70240 -5.70530  -7.92222 1.000 39.92866 ? 151 THR A CG2 1 
ATOM   876  N N   . GLU A 1 152 ? -8.92835  -4.70421  -4.27597 1.000 38.96515 ? 152 GLU A N   1 
ATOM   877  C CA  . GLU A 1 152 ? -7.93320  -4.86533  -3.21744 1.000 39.28906 ? 152 GLU A CA  1 
ATOM   878  C C   . GLU A 1 152 ? -8.62287  -5.12716  -1.87538 1.000 29.69642 ? 152 GLU A C   1 
ATOM   879  O O   . GLU A 1 152 ? -8.20937  -5.99525  -1.10274 1.000 29.40058 ? 152 GLU A O   1 
ATOM   880  C CB  . GLU A 1 152 ? -7.03455  -3.63114  -3.11206 1.000 45.91834 ? 152 GLU A CB  1 
ATOM   881  C CG  . GLU A 1 152 ? -5.80967  -3.66887  -4.00891 1.000 47.59842 ? 152 GLU A CG  1 
ATOM   882  C CD  . GLU A 1 152 ? -4.91317  -2.45623  -3.81788 1.000 47.82754 ? 152 GLU A CD  1 
ATOM   883  O OE1 . GLU A 1 152 ? -3.69938  -2.57310  -4.08647 1.000 47.51536 ? 152 GLU A OE1 1 
ATOM   884  O OE2 . GLU A 1 152 ? -5.42109  -1.38879  -3.40084 1.000 38.00453 ? 152 GLU A OE2 1 
ATOM   885  N N   . ALA A 1 153 ? -9.68225  -4.36879  -1.61817 1.000 26.60985 ? 153 ALA A N   1 
ATOM   886  C CA  . ALA A 1 153 ? -10.45797 -4.49834  -0.39283 1.000 21.69554 ? 153 ALA A CA  1 
ATOM   887  C C   . ALA A 1 153 ? -11.10368 -5.86803  -0.29434 1.000 26.33668 ? 153 ALA A C   1 
ATOM   888  O O   . ALA A 1 153 ? -11.02674 -6.52833  0.73745  1.000 25.57449 ? 153 ALA A O   1 
ATOM   889  C CB  . ALA A 1 153 ? -11.51246 -3.42494  -0.33114 1.000 18.40180 ? 153 ALA A CB  1 
ATOM   890  N N   . VAL A 1 154 ? -11.75341 -6.28168  -1.37633 1.000 27.87849 ? 154 VAL A N   1 
ATOM   891  C CA  . VAL A 1 154 ? -12.44324 -7.56072  -1.40989 1.000 28.11217 ? 154 VAL A CA  1 
ATOM   892  C C   . VAL A 1 154 ? -11.46576 -8.72531  -1.28998 1.000 27.72634 ? 154 VAL A C   1 
ATOM   893  O O   . VAL A 1 154 ? -11.72679 -9.66614  -0.55348 1.000 23.51235 ? 154 VAL A O   1 
ATOM   894  C CB  . VAL A 1 154 ? -13.28733 -7.69772  -2.69702 1.000 32.21315 ? 154 VAL A CB  1 
ATOM   895  C CG1 . VAL A 1 154 ? -13.86553 -9.10065  -2.82287 1.000 32.18534 ? 154 VAL A CG1 1 
ATOM   896  C CG2 . VAL A 1 154 ? -14.40488 -6.65648  -2.69262 1.000 31.73678 ? 154 VAL A CG2 1 
ATOM   897  N N   . ASN A 1 155 ? -10.33360 -8.65799  -1.98846 1.000 25.61757 ? 155 ASN A N   1 
ATOM   898  C CA  . ASN A 1 155 ? -9.33409  -9.72490  -1.89191 1.000 28.11890 ? 155 ASN A CA  1 
ATOM   899  C C   . ASN A 1 155 ? -8.80114  -9.82060  -0.46834 1.000 24.04420 ? 155 ASN A C   1 
ATOM   900  O O   . ASN A 1 155 ? -8.56092  -10.90945 0.05295  1.000 19.60354 ? 155 ASN A O   1 
ATOM   901  C CB  . ASN A 1 155 ? -8.15469  -9.49290  -2.85412 1.000 29.62372 ? 155 ASN A CB  1 
ATOM   902  C CG  . ASN A 1 155 ? -8.48715  -9.80997  -4.32039 1.000 37.84734 ? 155 ASN A CG  1 
ATOM   903  O OD1 . ASN A 1 155 ? -9.59312  -10.23969 -4.66053 1.000 31.12300 ? 155 ASN A OD1 1 
ATOM   904  N ND2 . ASN A 1 155 ? -7.51067  -9.58173  -5.19612 1.000 35.59772 ? 155 ASN A ND2 1 
ATOM   905  N N   . PHE A 1 156 ? -8.59828  -8.66790  0.15912  1.000 23.36684 ? 156 PHE A N   1 
ATOM   906  C CA  . PHE A 1 156 ? -8.04435  -8.67367  1.50960  1.000 25.09689 ? 156 PHE A CA  1 
ATOM   907  C C   . PHE A 1 156 ? -9.05677  -9.26919  2.47100  1.000 21.63381 ? 156 PHE A C   1 
ATOM   908  O O   . PHE A 1 156 ? -8.70342  -10.09786 3.30925  1.000 22.86240 ? 156 PHE A O   1 
ATOM   909  C CB  . PHE A 1 156 ? -7.64376  -7.27713  1.98388  1.000 25.46318 ? 156 PHE A CB  1 
ATOM   910  C CG  . PHE A 1 156 ? -7.09486  -7.27196  3.38918  1.000 23.93484 ? 156 PHE A CG  1 
ATOM   911  C CD1 . PHE A 1 156 ? -5.80064  -7.71071  3.64101  1.000 20.43564 ? 156 PHE A CD1 1 
ATOM   912  C CD2 . PHE A 1 156 ? -7.88380  -6.86692  4.45661  1.000 24.25574 ? 156 PHE A CD2 1 
ATOM   913  C CE1 . PHE A 1 156 ? -5.29340  -7.73132  4.93016  1.000 20.39674 ? 156 PHE A CE1 1 
ATOM   914  C CE2 . PHE A 1 156 ? -7.38858  -6.88193  5.74143  1.000 19.23592 ? 156 PHE A CE2 1 
ATOM   915  C CZ  . PHE A 1 156 ? -6.08355  -7.32287  5.98208  1.000 19.92365 ? 156 PHE A CZ  1 
ATOM   916  N N   . PHE A 1 157 ? -10.31308 -8.84519  2.33898  1.000 25.86633 ? 157 PHE A N   1 
ATOM   917  C CA  . PHE A 1 157 ? -11.37197 -9.40891  3.15389  1.000 24.97710 ? 157 PHE A CA  1 
ATOM   918  C C   . PHE A 1 157 ? -11.37854 -10.91836 3.02714  1.000 29.80469 ? 157 PHE A C   1 
ATOM   919  O O   . PHE A 1 157 ? -11.37846 -11.62982 4.03813  1.000 24.17245 ? 157 PHE A O   1 
ATOM   920  C CB  . PHE A 1 157 ? -12.74530 -8.86380  2.76497  1.000 22.19055 ? 157 PHE A CB  1 
ATOM   921  C CG  . PHE A 1 157 ? -13.81789 -9.19312  3.77049  1.000 26.23391 ? 157 PHE A CG  1 
ATOM   922  C CD1 . PHE A 1 157 ? -14.39445 -10.45995 3.80976  1.000 22.86092 ? 157 PHE A CD1 1 
ATOM   923  C CD2 . PHE A 1 157 ? -14.22687 -8.24747  4.69416  1.000 26.02685 ? 157 PHE A CD2 1 
ATOM   924  C CE1 . PHE A 1 157 ? -15.35765 -10.77260 4.74863  1.000 22.74437 ? 157 PHE A CE1 1 
ATOM   925  C CE2 . PHE A 1 157 ? -15.20184 -8.55268  5.62936  1.000 28.45813 ? 157 PHE A CE2 1 
ATOM   926  C CZ  . PHE A 1 157 ? -15.76683 -9.81564  5.65598  1.000 26.84577 ? 157 PHE A CZ  1 
ATOM   927  N N   . ASN A 1 158 ? -11.38548 -11.40250 1.78507  1.000 24.10427 ? 158 ASN A N   1 
ATOM   928  C CA  . ASN A 1 158 ? -11.42241 -12.84089 1.52907  1.000 22.31847 ? 158 ASN A CA  1 
ATOM   929  C C   . ASN A 1 158 ? -10.21820 -13.56757 2.10908  1.000 23.59462 ? 158 ASN A C   1 
ATOM   930  O O   . ASN A 1 158 ? -10.35209 -14.65471 2.68063  1.000 24.32039 ? 158 ASN A O   1 
ATOM   931  C CB  . ASN A 1 158 ? -11.51912 -13.11911 0.02403  1.000 26.36568 ? 158 ASN A CB  1 
ATOM   932  C CG  . ASN A 1 158 ? -12.88452 -12.77655 -0.54379 1.000 32.08101 ? 158 ASN A CG  1 
ATOM   933  O OD1 . ASN A 1 158 ? -13.83332 -12.52403 0.20103  1.000 31.94645 ? 158 ASN A OD1 1 
ATOM   934  N ND2 . ASN A 1 158 ? -12.99276 -12.77203 -1.87050 1.000 32.88935 ? 158 ASN A ND2 1 
ATOM   935  N N   . ALA A 1 159 ? -9.04273  -12.96346 1.96236  1.000 24.22926 ? 159 ALA A N   1 
ATOM   936  C CA  . ALA A 1 159 ? -7.82123  -13.54474 2.49884  1.000 29.15005 ? 159 ALA A CA  1 
ATOM   937  C C   . ALA A 1 159 ? -7.89693  -13.63729 4.02428  1.000 29.12749 ? 159 ALA A C   1 
ATOM   938  O O   . ALA A 1 159 ? -7.41623  -14.60835 4.61003  1.000 22.70717 ? 159 ALA A O   1 
ATOM   939  C CB  . ALA A 1 159 ? -6.60523  -12.73861 2.06862  1.000 25.80065 ? 159 ALA A CB  1 
ATOM   940  N N   . MET A 1 160 ? -8.51873  -12.64820 4.66715  1.000 16.55458 ? 160 MET A N   1 
ATOM   941  C CA  . MET A 1 160 ? -8.65130  -12.69387 6.12754  1.000 21.74659 ? 160 MET A CA  1 
ATOM   942  C C   . MET A 1 160 ? -9.69917  -13.71500 6.54555  1.000 24.06419 ? 160 MET A C   1 
ATOM   943  O O   . MET A 1 160 ? -9.51438  -14.43595 7.53221  1.000 24.92414 ? 160 MET A O   1 
ATOM   944  C CB  . MET A 1 160 ? -8.99641  -11.31285 6.69702  1.000 21.55340 ? 160 MET A CB  1 
ATOM   945  C CG  . MET A 1 160 ? -7.88640  -10.28677 6.55044  1.000 20.30320 ? 160 MET A CG  1 
ATOM   946  S SD  . MET A 1 160 ? -6.33602  -10.80509 7.31589  1.000 18.95866 ? 160 MET A SD  1 
ATOM   947  C CE  . MET A 1 160 ? -5.43064  -11.46206 5.90116  1.000 16.88442 ? 160 MET A CE  1 
ATOM   948  N N   . LYS A 1 161 ? -10.78836 -13.78789 5.78388  1.000 24.47837 ? 161 LYS A N   1 
ATOM   949  C CA  . LYS A 1 161 ? -11.84168 -14.76695 6.04488  1.000 28.47865 ? 161 LYS A CA  1 
ATOM   950  C C   . LYS A 1 161 ? -11.29815 -16.19748 5.96822  1.000 28.25834 ? 161 LYS A C   1 
ATOM   951  O O   . LYS A 1 161 ? -11.71499 -17.06511 6.73092  1.000 25.99407 ? 161 LYS A O   1 
ATOM   952  C CB  . LYS A 1 161 ? -12.99837 -14.58434 5.06048  1.000 34.99987 ? 161 LYS A CB  1 
ATOM   953  C CG  . LYS A 1 161 ? -14.20853 -15.46295 5.33323  1.000 42.09884 ? 161 LYS A CG  1 
ATOM   954  C CD  . LYS A 1 161 ? -15.41909 -14.95727 4.55337  1.000 56.48323 ? 161 LYS A CD  1 
ATOM   955  C CE  . LYS A 1 161 ? -16.67308 -15.77146 4.85575  1.000 64.30524 ? 161 LYS A CE  1 
ATOM   956  N NZ  . LYS A 1 161 ? -17.88681 -15.18046 4.21773  1.000 66.86954 ? 161 LYS A NZ  1 
ATOM   957  N N   . ASN A 1 162 ? -10.35537 -16.42829 5.05734  1.000 27.40640 ? 162 ASN A N   1 
ATOM   958  C CA  . ASN A 1 162 ? -9.74670  -17.74426 4.88811  1.000 33.72989 ? 162 ASN A CA  1 
ATOM   959  C C   . ASN A 1 162 ? -8.73004  -18.08458 5.96524  1.000 27.52264 ? 162 ASN A C   1 
ATOM   960  O O   . ASN A 1 162 ? -8.22826  -19.20623 6.01598  1.000 22.92365 ? 162 ASN A O   1 
ATOM   961  C CB  . ASN A 1 162 ? -9.06744  -17.85186 3.52508  1.000 40.80746 ? 162 ASN A CB  1 
ATOM   962  C CG  . ASN A 1 162 ? -10.05728 -17.92674 2.39007  1.000 54.40517 ? 162 ASN A CG  1 
ATOM   963  O OD1 . ASN A 1 162 ? -11.21038 -18.31267 2.58298  1.000 55.68099 ? 162 ASN A OD1 1 
ATOM   964  N ND2 . ASN A 1 162 ? -9.61234  -17.56106 1.19198  1.000 60.92244 ? 162 ASN A ND2 1 
ATOM   965  N N   . LYS A 1 163 ? -8.40789  -17.11787 6.81661  1.000 24.67189 ? 163 LYS A N   1 
ATOM   966  C CA  . LYS A 1 163 ? -7.50424  -17.38966 7.92320  1.000 28.13905 ? 163 LYS A CA  1 
ATOM   967  C C   . LYS A 1 163 ? -8.29341  -17.71751 9.17986  1.000 21.66701 ? 163 LYS A C   1 
ATOM   968  O O   . LYS A 1 163 ? -7.70734  -17.94658 10.23466 1.000 25.79492 ? 163 LYS A O   1 
ATOM   969  C CB  . LYS A 1 163 ? -6.56359  -16.20313 8.16815  1.000 28.98442 ? 163 LYS A CB  1 
ATOM   970  C CG  . LYS A 1 163 ? -5.43033  -16.12830 7.15268  1.000 30.74830 ? 163 LYS A CG  1 
ATOM   971  C CD  . LYS A 1 163 ? -4.57407  -14.89425 7.32711  1.000 30.67232 ? 163 LYS A CD  1 
ATOM   972  C CE  . LYS A 1 163 ? -3.51828  -14.82311 6.23221  1.000 33.87068 ? 163 LYS A CE  1 
ATOM   973  N NZ  . LYS A 1 163 ? -2.64501  -16.03159 6.25819  1.000 33.17612 ? 163 LYS A NZ  1 
ATOM   974  N N   . SER A 1 164 ? -9.62049  -17.72829 9.06961  1.000 18.49298 ? 164 SER A N   1 
ATOM   975  C CA  . SER A 1 164 ? -10.46074 -18.11486 10.20046 1.000 21.64589 ? 164 SER A CA  1 
ATOM   976  C C   . SER A 1 164 ? -10.09685 -19.51225 10.67915 1.000 22.06234 ? 164 SER A C   1 
ATOM   977  O O   . SER A 1 164 ? -9.86426  -20.40693 9.86767  1.000 17.35535 ? 164 SER A O   1 
ATOM   978  C CB  . SER A 1 164 ? -11.94026 -18.06802 9.83429  1.000 23.87845 ? 164 SER A CB  1 
ATOM   979  O OG  . SER A 1 164 ? -12.73554 -18.55548 10.90780 1.000 22.00599 ? 164 SER A OG  1 
ATOM   980  N N   . CYS A 1 165 ? -10.04838 -19.69598 11.99725 1.000 17.48366 ? 165 CYS A N   1 
ATOM   981  C CA  . CYS A 1 165 ? -9.76647  -21.00488 12.57430 1.000 18.46298 ? 165 CYS A CA  1 
ATOM   982  C C   . CYS A 1 165 ? -10.82239 -22.02679 12.16706 1.000 21.95857 ? 165 CYS A C   1 
ATOM   983  O O   . CYS A 1 165 ? -10.55535 -23.22155 12.15045 1.000 18.57959 ? 165 CYS A O   1 
ATOM   984  C CB  . CYS A 1 165 ? -9.68952  -20.91201 14.10119 1.000 19.61238 ? 165 CYS A CB  1 
ATOM   985  S SG  . CYS A 1 165 ? -8.45644  -19.73237 14.69941 1.000 16.82406 ? 165 CYS A SG  1 
ATOM   986  N N   . ALA A 1 166 ? -12.01915 -21.55414 11.83100 1.000 24.97468 ? 166 ALA A N   1 
ATOM   987  C CA  . ALA A 1 166 ? -13.09592 -22.45582 11.43670 1.000 26.58053 ? 166 ALA A CA  1 
ATOM   988  C C   . ALA A 1 166 ? -12.85474 -23.02060 10.03840 1.000 30.18894 ? 166 ALA A C   1 
ATOM   989  O O   . ALA A 1 166 ? -13.36087 -24.08660 9.69506  1.000 29.34851 ? 166 ALA A O   1 
ATOM   990  C CB  . ALA A 1 166 ? -14.43386 -21.74489 11.49185 1.000 25.18659 ? 166 ALA A CB  1 
ATOM   991  N N   . ILE A 1 167 ? -12.07596 -22.30126 9.23951  1.000 24.43394 ? 167 ILE A N   1 
ATOM   992  C CA  . ILE A 1 167 ? -11.82527 -22.68499 7.85108  1.000 28.38849 ? 167 ILE A CA  1 
ATOM   993  C C   . ILE A 1 167 ? -10.44333 -23.30689 7.70211  1.000 26.94400 ? 167 ILE A C   1 
ATOM   994  O O   . ILE A 1 167 ? -10.27031 -24.33917 7.06037  1.000 27.53592 ? 167 ILE A O   1 
ATOM   995  C CB  . ILE A 1 167 ? -11.95873 -21.46516 6.91535  1.000 30.85513 ? 167 ILE A CB  1 
ATOM   996  C CG1 . ILE A 1 167 ? -13.39440 -20.93622 6.94864  1.000 31.50603 ? 167 ILE A CG1 1 
ATOM   997  C CG2 . ILE A 1 167 ? -11.55312 -21.80407 5.48155  1.000 34.01711 ? 167 ILE A CG2 1 
ATOM   998  C CD1 . ILE A 1 167 ? -13.66615 -19.90623 5.89828  1.000 36.19951 ? 167 ILE A CD1 1 
ATOM   999  N N   . ASN A 1 168 ? -9.45903  -22.67977 8.32670  1.000 22.79315 ? 168 ASN A N   1 
ATOM   1000 C CA  . ASN A 1 168 ? -8.10157  -23.19142 8.30605  1.000 24.50716 ? 168 ASN A CA  1 
ATOM   1001 C C   . ASN A 1 168 ? -7.50540  -23.19700 9.70704  1.000 25.31057 ? 168 ASN A C   1 
ATOM   1002 O O   . ASN A 1 168 ? -6.86260  -22.23926 10.12614 1.000 20.29698 ? 168 ASN A O   1 
ATOM   1003 C CB  . ASN A 1 168 ? -7.24226  -22.35491 7.35280  1.000 29.47822 ? 168 ASN A CB  1 
ATOM   1004 C CG  . ASN A 1 168 ? -6.49698  -23.19648 6.35857  1.000 46.53977 ? 168 ASN A CG  1 
ATOM   1005 O OD1 . ASN A 1 168 ? -7.08992  -23.71838 5.42579  1.000 40.66765 ? 168 ASN A OD1 1 
ATOM   1006 N ND2 . ASN A 1 168 ? -5.18785  -23.34833 6.55749  1.000 57.92437 ? 168 ASN A ND2 1 
ATOM   1007 N N   . ASN A 1 169 ? -7.74044  -24.27691 10.43770 1.000 27.33222 ? 169 ASN A N   1 
ATOM   1008 C CA  . ASN A 1 169 ? -7.24935  -24.36055 11.80858 1.000 29.23946 ? 169 ASN A CA  1 
ATOM   1009 C C   . ASN A 1 169 ? -5.75546  -24.64271 11.86239 1.000 27.78285 ? 169 ASN A C   1 
ATOM   1010 O O   . ASN A 1 169 ? -5.32224  -25.75607 11.59064 1.000 23.07104 ? 169 ASN A O   1 
ATOM   1011 C CB  . ASN A 1 169 ? -8.00667  -25.43447 12.59504 1.000 30.50607 ? 169 ASN A CB  1 
ATOM   1012 C CG  . ASN A 1 169 ? -7.92676  -25.21086 14.08853 1.000 32.12947 ? 169 ASN A CG  1 
ATOM   1013 O OD1 . ASN A 1 169 ? -6.83665  -25.10383 14.65157 1.000 27.52836 ? 169 ASN A OD1 1 
ATOM   1014 N ND2 . ASN A 1 169 ? -9.08520  -25.09446 14.73477 1.000 35.39745 ? 169 ASN A ND2 1 
ATOM   1015 N N   . GLN A 1 170 ? -4.98111  -23.61848 12.21409 1.000 25.98788 ? 170 GLN A N   1 
ATOM   1016 C CA  . GLN A 1 170 ? -3.52986  -23.72055 12.30309 1.000 22.64504 ? 170 GLN A CA  1 
ATOM   1017 C C   . GLN A 1 170 ? -3.00285  -22.56609 13.13938 1.000 25.49919 ? 170 GLN A C   1 
ATOM   1018 O O   . GLN A 1 170 ? -3.75188  -21.64438 13.44806 1.000 21.39286 ? 170 GLN A O   1 
ATOM   1019 C CB  . GLN A 1 170 ? -2.89908  -23.69933 10.92077 1.000 28.39507 ? 170 GLN A CB  1 
ATOM   1020 C CG  . GLN A 1 170 ? -3.09040  -22.38362 10.19185 1.000 43.45425 ? 170 GLN A CG  1 
ATOM   1021 C CD  . GLN A 1 170 ? -2.68881  -22.46757 8.73264  1.000 53.25209 ? 170 GLN A CD  1 
ATOM   1022 O OE1 . GLN A 1 170 ? -3.53498  -22.40414 7.84631  1.000 61.27102 ? 170 GLN A OE1 1 
ATOM   1023 N NE2 . GLN A 1 170 ? -1.39443  -22.61314 8.47743  1.000 54.12892 ? 170 GLN A NE2 1 
ATOM   1024 N N   . ASN A 1 171 ? -1.72333  -22.61703 13.50377 1.000 21.33829 ? 171 ASN A N   1 
ATOM   1025 C CA  . ASN A 1 171 ? -1.10998  -21.54560 14.28146 1.000 19.32833 ? 171 ASN A CA  1 
ATOM   1026 C C   . ASN A 1 171 ? -1.40950  -20.17083 13.69528 1.000 23.79328 ? 171 ASN A C   1 
ATOM   1027 O O   . ASN A 1 171 ? -1.29488  -19.96906 12.48295 1.000 20.10543 ? 171 ASN A O   1 
ATOM   1028 C CB  . ASN A 1 171 ? 0.40272   -21.75333 14.37868 1.000 27.14620 ? 171 ASN A CB  1 
ATOM   1029 C CG  . ASN A 1 171 ? 0.78329   -22.82060 15.39572 1.000 40.20369 ? 171 ASN A CG  1 
ATOM   1030 O OD1 . ASN A 1 171 ? 0.13964   -22.95666 16.43870 1.000 49.06993 ? 171 ASN A OD1 1 
ATOM   1031 N ND2 . ASN A 1 171 ? 1.84016   -23.57771 15.10112 1.000 34.66766 ? 171 ASN A ND2 1 
ATOM   1032 N N   . LEU A 1 172 ? -1.82862  -19.25432 14.56836 1.000 18.54395 ? 172 LEU A N   1 
ATOM   1033 C CA  . LEU A 1 172 ? -2.10476  -17.85137 14.23036 1.000 20.47204 ? 172 LEU A CA  1 
ATOM   1034 C C   . LEU A 1 172 ? -3.40677  -17.67054 13.45467 1.000 17.47004 ? 172 LEU A C   1 
ATOM   1035 O O   . LEU A 1 172 ? -3.68969  -16.57445 12.96714 1.000 19.49554 ? 172 LEU A O   1 
ATOM   1036 C CB  . LEU A 1 172 ? -0.94417  -17.22962 13.42499 1.000 16.12661 ? 172 LEU A CB  1 
ATOM   1037 C CG  . LEU A 1 172 ? 0.44729   -17.26596 14.06381 1.000 23.21050 ? 172 LEU A CG  1 
ATOM   1038 C CD1 . LEU A 1 172 ? 1.49152   -16.81257 13.04999 1.000 28.83286 ? 172 LEU A CD1 1 
ATOM   1039 C CD2 . LEU A 1 172 ? 0.48547   -16.38577 15.29661 1.000 23.80880 ? 172 LEU A CD2 1 
ATOM   1040 N N   . CYS A 1 173 ? -4.20847  -18.72239 13.33491 1.000 14.98654 ? 173 CYS A N   1 
ATOM   1041 C CA  . CYS A 1 173 ? -5.49230  -18.55428 12.66943 1.000 14.97222 ? 173 CYS A CA  1 
ATOM   1042 C C   . CYS A 1 173 ? -6.31553  -17.56268 13.47841 1.000 13.73701 ? 173 CYS A C   1 
ATOM   1043 O O   . CYS A 1 173 ? -6.12985  -17.42459 14.68970 1.000 11.13432 ? 173 CYS A O   1 
ATOM   1044 C CB  . CYS A 1 173 ? -6.23361  -19.88344 12.50266 1.000 17.46006 ? 173 CYS A CB  1 
ATOM   1045 S SG  . CYS A 1 173 ? -6.75270  -20.68798 14.03617 1.000 18.86472 ? 173 CYS A SG  1 
ATOM   1046 N N   . ILE A 1 174 ? -7.19797  -16.83967 12.80252 1.000 14.93213 ? 174 ILE A N   1 
ATOM   1047 C CA  . ILE A 1 174 ? -7.96376  -15.79082 13.46874 1.000 15.19648 ? 174 ILE A CA  1 
ATOM   1048 C C   . ILE A 1 174 ? -9.32101  -16.34455 13.89444 1.000 14.49648 ? 174 ILE A C   1 
ATOM   1049 O O   . ILE A 1 174 ? -10.08524 -16.82960 13.05852 1.000 14.61943 ? 174 ILE A O   1 
ATOM   1050 C CB  . ILE A 1 174 ? -8.13213  -14.56085 12.55508 1.000 12.55661 ? 174 ILE A CB  1 
ATOM   1051 C CG1 . ILE A 1 174 ? -6.74915  -14.00229 12.17735 1.000 16.08178 ? 174 ILE A CG1 1 
ATOM   1052 C CG2 . ILE A 1 174 ? -8.95903  -13.47950 13.26423 1.000 15.61465 ? 174 ILE A CG2 1 
ATOM   1053 C CD1 . ILE A 1 174 ? -6.76121  -13.00620 11.01650 1.000 15.88091 ? 174 ILE A CD1 1 
ATOM   1054 N N   . PRO A 1 175 ? -9.62288  -16.29506 15.20357 1.000 16.79126 ? 175 PRO A N   1 
ATOM   1055 C CA  . PRO A 1 175 ? -10.84653 -16.97754 15.65311 1.000 18.44525 ? 175 PRO A CA  1 
ATOM   1056 C C   . PRO A 1 175 ? -12.12795 -16.18496 15.38429 1.000 19.27478 ? 175 PRO A C   1 
ATOM   1057 O O   . PRO A 1 175 ? -12.81951 -15.77739 16.32320 1.000 14.86888 ? 175 PRO A O   1 
ATOM   1058 C CB  . PRO A 1 175 ? -10.60684 -17.16123 17.15933 1.000 16.98124 ? 175 PRO A CB  1 
ATOM   1059 C CG  . PRO A 1 175 ? -9.68770  -16.04435 17.53342 1.000 15.99905 ? 175 PRO A CG  1 
ATOM   1060 C CD  . PRO A 1 175 ? -8.78870  -15.84332 16.33347 1.000 19.92360 ? 175 PRO A CD  1 
ATOM   1061 N N   . PHE A 1 176 ? -12.44973 -15.99766 14.10460 1.000 18.81341 ? 176 PHE A N   1 
ATOM   1062 C CA  . PHE A 1 176 ? -13.65522 -15.28535 13.72459 1.000 20.94424 ? 176 PHE A CA  1 
ATOM   1063 C C   . PHE A 1 176 ? -14.88525 -16.04334 14.21322 1.000 17.96953 ? 176 PHE A C   1 
ATOM   1064 O O   . PHE A 1 176 ? -15.93015 -15.44063 14.45455 1.000 20.31674 ? 176 PHE A O   1 
ATOM   1065 C CB  . PHE A 1 176 ? -13.70694 -15.06563 12.19838 1.000 11.32373 ? 176 PHE A CB  1 
ATOM   1066 C CG  . PHE A 1 176 ? -12.72063 -14.03291 11.70011 1.000 16.61869 ? 176 PHE A CG  1 
ATOM   1067 C CD1 . PHE A 1 176 ? -12.78620 -12.72327 12.14186 1.000 18.42662 ? 176 PHE A CD1 1 
ATOM   1068 C CD2 . PHE A 1 176 ? -11.74017 -14.37091 10.78398 1.000 13.77768 ? 176 PHE A CD2 1 
ATOM   1069 C CE1 . PHE A 1 176 ? -11.88298 -11.76399 11.68287 1.000 19.12729 ? 176 PHE A CE1 1 
ATOM   1070 C CE2 . PHE A 1 176 ? -10.83816 -13.42506 10.31457 1.000 13.77260 ? 176 PHE A CE2 1 
ATOM   1071 C CZ  . PHE A 1 176 ? -10.90032 -12.12072 10.77007 1.000 15.17359 ? 176 PHE A CZ  1 
ATOM   1072 N N   . GLN A 1 177 ? -14.75294 -17.35675 14.39243 1.000 15.57231 ? 177 GLN A N   1 
ATOM   1073 C CA  . GLN A 1 177 ? -15.90037 -18.17741 14.78353 1.000 17.70797 ? 177 GLN A CA  1 
ATOM   1074 C C   . GLN A 1 177 ? -16.31908 -17.94117 16.23635 1.000 20.95645 ? 177 GLN A C   1 
ATOM   1075 O O   . GLN A 1 177 ? -17.39644 -18.36958 16.65693 1.000 24.86015 ? 177 GLN A O   1 
ATOM   1076 C CB  . GLN A 1 177 ? -15.60246 -19.66790 14.55704 1.000 19.97272 ? 177 GLN A CB  1 
ATOM   1077 C CG  . GLN A 1 177 ? -14.83649 -20.34772 15.68819 1.000 25.06674 ? 177 GLN A CG  1 
ATOM   1078 C CD  . GLN A 1 177 ? -13.39247 -19.89248 15.78596 1.000 23.30289 ? 177 GLN A CD  1 
ATOM   1079 O OE1 . GLN A 1 177 ? -12.83241 -19.35558 14.82860 1.000 20.56206 ? 177 GLN A OE1 1 
ATOM   1080 N NE2 . GLN A 1 177 ? -12.77886 -20.11532 16.94324 1.000 18.86533 ? 177 GLN A NE2 1 
ATOM   1081 N N   . TYR A 1 178 ? -15.48353 -17.24032 16.99822 1.000 15.93120 ? 178 TYR A N   1 
ATOM   1082 C CA  . TYR A 1 178 ? -15.77646 -16.99762 18.40536 1.000 15.64778 ? 178 TYR A CA  1 
ATOM   1083 C C   . TYR A 1 178 ? -16.17750 -15.54470 18.64494 1.000 15.03250 ? 178 TYR A C   1 
ATOM   1084 O O   . TYR A 1 178 ? -15.32472 -14.66419 18.77989 1.000 16.74999 ? 178 TYR A O   1 
ATOM   1085 C CB  . TYR A 1 178 ? -14.58066 -17.35074 19.26877 1.000 17.60795 ? 178 TYR A CB  1 
ATOM   1086 C CG  . TYR A 1 178 ? -14.85040 -17.18045 20.74819 1.000 17.81997 ? 178 TYR A CG  1 
ATOM   1087 C CD1 . TYR A 1 178 ? -15.84929 -17.92007 21.37931 1.000 18.32562 ? 178 TYR A CD1 1 
ATOM   1088 C CD2 . TYR A 1 178 ? -14.09785 -16.29805 21.51262 1.000 18.04692 ? 178 TYR A CD2 1 
ATOM   1089 C CE1 . TYR A 1 178 ? -16.09755 -17.77585 22.74124 1.000 20.00386 ? 178 TYR A CE1 1 
ATOM   1090 C CE2 . TYR A 1 178 ? -14.33694 -16.14069 22.87878 1.000 21.26594 ? 178 TYR A CE2 1 
ATOM   1091 C CZ  . TYR A 1 178 ? -15.33671 -16.88497 23.48593 1.000 21.38231 ? 178 TYR A CZ  1 
ATOM   1092 O OH  . TYR A 1 178 ? -15.57907 -16.73616 24.83361 1.000 23.60245 ? 178 TYR A OH  1 
ATOM   1093 N N   . ALA A 1 179 ? -17.48043 -15.29864 18.70274 1.000 15.30761 ? 179 ALA A N   1 
ATOM   1094 C CA  . ALA A 1 179 ? -17.98307 -13.92736 18.70536 1.000 17.05275 ? 179 ALA A CA  1 
ATOM   1095 C C   . ALA A 1 179 ? -17.96369 -13.26067 20.06955 1.000 14.86514 ? 179 ALA A C   1 
ATOM   1096 O O   . ALA A 1 179 ? -17.95159 -12.03865 20.13988 1.000 18.25584 ? 179 ALA A O   1 
ATOM   1097 C CB  . ALA A 1 179 ? -19.39854 -13.88750 18.14057 1.000 16.38019 ? 179 ALA A CB  1 
ATOM   1098 N N   . ASN A 1 180 ? -17.97212 -14.04256 21.14732 1.000 14.15127 ? 180 ASN A N   1 
ATOM   1099 C CA  . ASN A 1 180 ? -18.10743 -13.46150 22.48681 1.000 18.77287 ? 180 ASN A CA  1 
ATOM   1100 C C   . ASN A 1 180 ? -17.03213 -12.42363 22.83901 1.000 21.09406 ? 180 ASN A C   1 
ATOM   1101 O O   . ASN A 1 180 ? -17.32128 -11.44086 23.52919 1.000 16.44020 ? 180 ASN A O   1 
ATOM   1102 C CB  . ASN A 1 180 ? -18.10178 -14.56530 23.54227 1.000 16.62273 ? 180 ASN A CB  1 
ATOM   1103 C CG  . ASN A 1 180 ? -19.24720 -15.53657 23.36839 1.000 19.24039 ? 180 ASN A CG  1 
ATOM   1104 O OD1 . ASN A 1 180 ? -19.21822 -16.38291 22.48244 1.000 21.57974 ? 180 ASN A OD1 1 
ATOM   1105 N ND2 . ASN A 1 180 ? -20.27162 -15.41881 24.21944 1.000 24.44898 ? 180 ASN A ND2 1 
ATOM   1106 N N   . ASP A 1 181 ? -15.79891 -12.64543 22.37705 1.000 14.76159 ? 181 ASP A N   1 
ATOM   1107 C CA  . ASP A 1 181 ? -14.68419 -11.75305 22.70655 1.000 14.97813 ? 181 ASP A CA  1 
ATOM   1108 C C   . ASP A 1 181 ? -13.52052 -11.89140 21.71882 1.000 14.06523 ? 181 ASP A C   1 
ATOM   1109 O O   . ASP A 1 181 ? -13.51218 -12.78979 20.88852 1.000 13.75595 ? 181 ASP A O   1 
ATOM   1110 C CB  . ASP A 1 181 ? -14.17483 -12.02051 24.12849 1.000 14.09357 ? 181 ASP A CB  1 
ATOM   1111 C CG  . ASP A 1 181 ? -13.22937 -10.92088 24.61809 1.000 31.11830 ? 181 ASP A CG  1 
ATOM   1112 O OD1 . ASP A 1 181 ? -13.58170 -9.73249  24.43805 1.000 18.70243 ? 181 ASP A OD1 1 
ATOM   1113 O OD2 . ASP A 1 181 ? -12.11839 -11.23667 25.12416 1.000 35.54353 ? 181 ASP A OD2 1 
ATOM   1114 N N   . GLY A 1 182 ? -12.53516 -11.00143 21.81056 1.000 12.21468 ? 182 GLY A N   1 
ATOM   1115 C CA  . GLY A 1 182 ? -11.31459 -11.16042 21.03889 1.000 14.41349 ? 182 GLY A CA  1 
ATOM   1116 C C   . GLY A 1 182 ? -11.21991 -10.22852 19.85226 1.000 15.86864 ? 182 GLY A C   1 
ATOM   1117 O O   . GLY A 1 182 ? -10.26873 -10.32022 19.07991 1.000 16.86808 ? 182 GLY A O   1 
ATOM   1118 N N   . CYS A 1 183 ? -12.18325 -9.31468  19.71304 1.000 12.99307 ? 183 CYS A N   1 
ATOM   1119 C CA  . CYS A 1 183 ? -12.21079 -8.40909  18.55745 1.000 14.65579 ? 183 CYS A CA  1 
ATOM   1120 C C   . CYS A 1 183 ? -10.91433 -7.60212  18.45013 1.000 13.33978 ? 183 CYS A C   1 
ATOM   1121 O O   . CYS A 1 183 ? -10.38975 -7.40550  17.35635 1.000 11.10856 ? 183 CYS A O   1 
ATOM   1122 C CB  . CYS A 1 183 ? -13.41704 -7.45969  18.63870 1.000 14.28220 ? 183 CYS A CB  1 
ATOM   1123 S SG  . CYS A 1 183 ? -13.44899 -6.50541  20.17058 1.000 22.39026 ? 183 CYS A SG  1 
ATOM   1124 N N   . TYR A 1 184 ? -10.38434 -7.16409  19.59211 1.000 9.37057  ? 184 TYR A N   1 
ATOM   1125 C CA  . TYR A 1 184 ? -9.13074  -6.40490  19.61781 1.000 9.71267  ? 184 TYR A CA  1 
ATOM   1126 C C   . TYR A 1 184 ? -7.97469  -7.15716  18.94639 1.000 11.33551 ? 184 TYR A C   1 
ATOM   1127 O O   . TYR A 1 184 ? -7.23350  -6.57312  18.14844 1.000 10.83537 ? 184 TYR A O   1 
ATOM   1128 C CB  . TYR A 1 184 ? -8.76563  -6.03487  21.06682 1.000 12.91546 ? 184 TYR A CB  1 
ATOM   1129 C CG  . TYR A 1 184 ? -8.95490  -7.16626  22.05541 1.000 9.75898  ? 184 TYR A CG  1 
ATOM   1130 C CD1 . TYR A 1 184 ? -10.20160 -7.41022  22.64456 1.000 10.19602 ? 184 TYR A CD1 1 
ATOM   1131 C CD2 . TYR A 1 184 ? -7.88531  -7.99763  22.39829 1.000 12.37838 ? 184 TYR A CD2 1 
ATOM   1132 C CE1 . TYR A 1 184 ? -10.37585 -8.46397  23.54481 1.000 12.27480 ? 184 TYR A CE1 1 
ATOM   1133 C CE2 . TYR A 1 184 ? -8.04726  -9.05153  23.30535 1.000 12.64157 ? 184 TYR A CE2 1 
ATOM   1134 C CZ  . TYR A 1 184 ? -9.29387  -9.27368  23.86634 1.000 14.58364 ? 184 TYR A CZ  1 
ATOM   1135 O OH  . TYR A 1 184 ? -9.44762  -10.31574 24.74190 1.000 16.75006 ? 184 TYR A OH  1 
ATOM   1136 N N   . ALA A 1 185 ? -7.83156  -8.45200  19.24191 1.000 11.49770 ? 185 ALA A N   1 
ATOM   1137 C CA  . ALA A 1 185 ? -6.75790  -9.26124  18.65028 1.000 9.47368  ? 185 ALA A CA  1 
ATOM   1138 C C   . ALA A 1 185 ? -7.02646  -9.58661  17.17549 1.000 11.02839 ? 185 ALA A C   1 
ATOM   1139 O O   . ALA A 1 185 ? -6.10446  -9.60547  16.35985 1.000 14.02181 ? 185 ALA A O   1 
ATOM   1140 C CB  . ALA A 1 185 ? -6.57077  -10.54101 19.43194 1.000 8.60657  ? 185 ALA A CB  1 
ATOM   1141 N N   . ARG A 1 186 ? -8.28154  -9.84492  16.83916 1.000 10.40145 ? 186 ARG A N   1 
ATOM   1142 C CA  . ARG A 1 186 ? -8.63877  -10.11124 15.45496 1.000 13.30466 ? 186 ARG A CA  1 
ATOM   1143 C C   . ARG A 1 186 ? -8.31324  -8.87626  14.60326 1.000 14.02053 ? 186 ARG A C   1 
ATOM   1144 O O   . ARG A 1 186 ? -7.71401  -9.00657  13.54738 1.000 14.88904 ? 186 ARG A O   1 
ATOM   1145 C CB  . ARG A 1 186 ? -10.11587 -10.50201 15.33276 1.000 11.85846 ? 186 ARG A CB  1 
ATOM   1146 C CG  . ARG A 1 186 ? -10.51325 -11.73535 16.16057 1.000 12.47793 ? 186 ARG A CG  1 
ATOM   1147 C CD  . ARG A 1 186 ? -11.85414 -12.32524 15.69977 1.000 18.49695 ? 186 ARG A CD  1 
ATOM   1148 N NE  . ARG A 1 186 ? -12.95748 -11.36407 15.74345 1.000 19.08672 ? 186 ARG A NE  1 
ATOM   1149 C CZ  . ARG A 1 186 ? -13.74608 -11.15821 16.79928 1.000 18.52806 ? 186 ARG A CZ  1 
ATOM   1150 N NH1 . ARG A 1 186 ? -13.55462 -11.83010 17.92883 1.000 12.28436 ? 186 ARG A NH1 1 
ATOM   1151 N NH2 . ARG A 1 186 ? -14.71834 -10.25943 16.73481 1.000 20.21549 ? 186 ARG A NH2 1 
ATOM   1152 N N   . ALA A 1 187 ? -8.65915  -7.68107  15.07982 1.000 13.96055 ? 187 ALA A N   1 
ATOM   1153 C CA  . ALA A 1 187 ? -8.34742  -6.45770  14.33484 1.000 10.88054 ? 187 ALA A CA  1 
ATOM   1154 C C   . ALA A 1 187 ? -6.84571  -6.20427  14.22677 1.000 11.80632 ? 187 ALA A C   1 
ATOM   1155 O O   . ALA A 1 187 ? -6.35778  -5.71906  13.20591 1.000 11.06833 ? 187 ALA A O   1 
ATOM   1156 C CB  . ALA A 1 187 ? -9.03586  -5.24664  14.97004 1.000 7.54782  ? 187 ALA A CB  1 
ATOM   1157 N N   . HIS A 1 188 ? -6.10924  -6.50811  15.28593 1.000 11.53588 ? 188 HIS A N   1 
ATOM   1158 C CA  . HIS A 1 188 ? -4.68774  -6.21730  15.26685 1.000 13.09447 ? 188 HIS A CA  1 
ATOM   1159 C C   . HIS A 1 188 ? -3.95671  -7.21388  14.35125 1.000 17.84976 ? 188 HIS A C   1 
ATOM   1160 O O   . HIS A 1 188 ? -2.97420  -6.86222  13.70512 1.000 11.30236 ? 188 HIS A O   1 
ATOM   1161 C CB  . HIS A 1 188 ? -4.11478  -6.25586  16.68363 1.000 10.90234 ? 188 HIS A CB  1 
ATOM   1162 C CG  . HIS A 1 188 ? -3.06754  -5.21912  16.93832 1.000 14.01143 ? 188 HIS A CG  1 
ATOM   1163 N ND1 . HIS A 1 188 ? -3.24887  -3.88927  16.62731 1.000 16.62575 ? 188 HIS A ND1 1 
ATOM   1164 C CD2 . HIS A 1 188 ? -1.82976  -5.31249  17.48317 1.000 10.61689 ? 188 HIS A CD2 1 
ATOM   1165 C CE1 . HIS A 1 188 ? -2.16969  -3.20737  16.96703 1.000 16.70392 ? 188 HIS A CE1 1 
ATOM   1166 N NE2 . HIS A 1 188 ? -1.29344  -4.04885  17.49026 1.000 12.60416 ? 188 HIS A NE2 1 
ATOM   1167 N N   . MET A 1 189 ? -4.42806  -8.46044  14.30579 1.000 13.59907 ? 189 MET A N   1 
ATOM   1168 C CA  . MET A 1 189 ? -3.82452  -9.44055  13.40712 1.000 10.47493 ? 189 MET A CA  1 
ATOM   1169 C C   . MET A 1 189 ? -4.09597  -9.06951  11.94507 1.000 12.93540 ? 189 MET A C   1 
ATOM   1170 O O   . MET A 1 189 ? -3.21070  -9.18441  11.09571 1.000 16.26319 ? 189 MET A O   1 
ATOM   1171 C CB  . MET A 1 189 ? -4.34223  -10.85193 13.70306 1.000 15.82426 ? 189 MET A CB  1 
ATOM   1172 C CG  . MET A 1 189 ? -3.52667  -11.95491 13.02877 1.000 17.53439 ? 189 MET A CG  1 
ATOM   1173 S SD  . MET A 1 189 ? -1.79788  -11.93262 13.57399 1.000 17.26706 ? 189 MET A SD  1 
ATOM   1174 C CE  . MET A 1 189 ? -1.04605  -13.18737 12.55210 1.000 25.35046 ? 189 MET A CE  1 
ATOM   1175 N N   . MET A 1 190 ? -5.32195  -8.63578  11.64566 1.000 15.21540 ? 190 MET A N   1 
ATOM   1176 C CA  . MET A 1 190 ? -5.63300  -8.14898  10.29955 1.000 14.40409 ? 190 MET A CA  1 
ATOM   1177 C C   . MET A 1 190 ? -4.71706  -6.98181  9.92241  1.000 15.69647 ? 190 MET A C   1 
ATOM   1178 O O   . MET A 1 190 ? -4.22696  -6.90045  8.78894  1.000 14.85006 ? 190 MET A O   1 
ATOM   1179 C CB  . MET A 1 190 ? -7.10455  -7.73647  10.19825 1.000 10.54889 ? 190 MET A CB  1 
ATOM   1180 C CG  . MET A 1 190 ? -8.04899  -8.94070  10.17448 1.000 12.87954 ? 190 MET A CG  1 
ATOM   1181 S SD  . MET A 1 190 ? -9.74008  -8.55645  9.69529  1.000 15.91700 ? 190 MET A SD  1 
ATOM   1182 C CE  . MET A 1 190 ? -10.45088 -8.08564  11.27102 1.000 11.59258 ? 190 MET A CE  1 
ATOM   1183 N N   . ARG A 1 191 ? -4.48092  -6.09032  10.88326 1.000 10.92983 ? 191 ARG A N   1 
ATOM   1184 C CA  . ARG A 1 191 ? -3.54401  -4.98905  10.69208 1.000 10.94281 ? 191 ARG A CA  1 
ATOM   1185 C C   . ARG A 1 191 ? -2.14117  -5.48630  10.32149 1.000 15.12604 ? 191 ARG A C   1 
ATOM   1186 O O   . ARG A 1 191 ? -1.50967  -4.94440  9.42595  1.000 13.33061 ? 191 ARG A O   1 
ATOM   1187 C CB  . ARG A 1 191 ? -3.46050  -4.12379  11.95284 1.000 10.46944 ? 191 ARG A CB  1 
ATOM   1188 C CG  . ARG A 1 191 ? -2.44336  -2.95844  11.85410 1.000 12.11388 ? 191 ARG A CG  1 
ATOM   1189 C CD  . ARG A 1 191 ? -1.76694  -2.71752  13.20472 1.000 15.79169 ? 191 ARG A CD  1 
ATOM   1190 N NE  . ARG A 1 191 ? -0.94336  -1.50622  13.21779 1.000 14.09610 ? 191 ARG A NE  1 
ATOM   1191 C CZ  . ARG A 1 191 ? 0.20525   -1.38672  13.87365 1.000 16.89173 ? 191 ARG A CZ  1 
ATOM   1192 N NH1 . ARG A 1 191 ? 0.69596   -2.40698  14.57063 1.000 18.15387 ? 191 ARG A NH1 1 
ATOM   1193 N NH2 . ARG A 1 191 ? 0.87253   -0.24412  13.81961 1.000 18.21734 ? 191 ARG A NH2 1 
ATOM   1194 N N   . GLN A 1 192 ? -1.64384  -6.49904  11.01917 1.000 13.92809 ? 192 GLN A N   1 
ATOM   1195 C CA  . GLN A 1 192 ? -0.31457  -7.01957  10.70463 1.000 17.71243 ? 192 GLN A CA  1 
ATOM   1196 C C   . GLN A 1 192 ? -0.21769  -7.51717  9.26565  1.000 16.40831 ? 192 GLN A C   1 
ATOM   1197 O O   . GLN A 1 192 ? 0.75697   -7.22003  8.57179  1.000 19.79226 ? 192 GLN A O   1 
ATOM   1198 C CB  . GLN A 1 192 ? 0.07338   -8.14911  11.65336 1.000 12.20662 ? 192 GLN A CB  1 
ATOM   1199 C CG  . GLN A 1 192 ? 1.51026   -8.62152  11.44579 1.000 18.13503 ? 192 GLN A CG  1 
ATOM   1200 C CD  . GLN A 1 192 ? 1.80897   -9.90147  12.16583 1.000 28.01192 ? 192 GLN A CD  1 
ATOM   1201 O OE1 . GLN A 1 192 ? 2.01141   -10.94195 11.54394 1.000 42.68862 ? 192 GLN A OE1 1 
ATOM   1202 N NE2 . GLN A 1 192 ? 1.83281   -9.84302  13.48295 1.000 22.17963 ? 192 GLN A NE2 1 
ATOM   1203 N N   . HIS A 1 193 ? -1.23305  -8.26252  8.82787  1.000 15.39964 ? 193 HIS A N   1 
ATOM   1204 C CA  . HIS A 1 193 ? -1.30431  -8.77567  7.45480  1.000 23.30383 ? 193 HIS A CA  1 
ATOM   1205 C C   . HIS A 1 193 ? -1.37283  -7.64999  6.42345  1.000 25.50224 ? 193 HIS A C   1 
ATOM   1206 O O   . HIS A 1 193 ? -0.74207  -7.72900  5.37241  1.000 21.74425 ? 193 HIS A O   1 
ATOM   1207 C CB  . HIS A 1 193 ? -2.51821  -9.70394  7.28507  1.000 19.60223 ? 193 HIS A CB  1 
ATOM   1208 C CG  . HIS A 1 193 ? -2.41107  -10.98829 8.05076  1.000 23.16779 ? 193 HIS A CG  1 
ATOM   1209 N ND1 . HIS A 1 193 ? -1.34326  -11.84340 7.91811  1.000 19.84269 ? 193 HIS A ND1 1 
ATOM   1210 C CD2 . HIS A 1 193 ? -3.24193  -11.55625 8.95923  1.000 21.10606 ? 193 HIS A CD2 1 
ATOM   1211 C CE1 . HIS A 1 193 ? -1.51380  -12.88536 8.71693  1.000 24.90994 ? 193 HIS A CE1 1 
ATOM   1212 N NE2 . HIS A 1 193 ? -2.65556  -12.73462 9.35743  1.000 19.48598 ? 193 HIS A NE2 1 
ATOM   1213 N N   . MET A 1 194 ? -2.15825  -6.61337  6.70916  1.000 20.16032 ? 194 MET A N   1 
ATOM   1214 C CA  . MET A 1 194 ? -2.16918  -5.41466  5.86431  1.000 19.66643 ? 194 MET A CA  1 
ATOM   1215 C C   . MET A 1 194 ? -0.79578  -4.81250  5.70278  1.000 22.33252 ? 194 MET A C   1 
ATOM   1216 O O   . MET A 1 194 ? -0.35361  -4.53506  4.58533  1.000 17.60301 ? 194 MET A O   1 
ATOM   1217 C CB  . MET A 1 194 ? -3.05199  -4.33459  6.45301  1.000 22.75056 ? 194 MET A CB  1 
ATOM   1218 C CG  . MET A 1 194 ? -4.44603  -4.34443  6.00999  1.000 28.60688 ? 194 MET A CG  1 
ATOM   1219 S SD  . MET A 1 194 ? -5.18150  -2.91223  6.80085  1.000 26.88502 ? 194 MET A SD  1 
ATOM   1220 C CE  . MET A 1 194 ? -6.82079  -3.58082  7.06320  1.000 20.66838 ? 194 MET A CE  1 
ATOM   1221 N N   . ASN A 1 195 ? -0.15309  -4.56198  6.84523  1.000 19.06739 ? 195 ASN A N   1 
ATOM   1222 C CA  . ASN A 1 195 ? 1.14358   -3.89510  6.88113  1.000 19.73253 ? 195 ASN A CA  1 
ATOM   1223 C C   . ASN A 1 195 ? 2.17540   -4.67162  6.05584  1.000 29.55573 ? 195 ASN A C   1 
ATOM   1224 O O   . ASN A 1 195 ? 3.01294   -4.07193  5.37360  1.000 24.26296 ? 195 ASN A O   1 
ATOM   1225 C CB  . ASN A 1 195 ? 1.62182   -3.72536  8.32910  1.000 20.80290 ? 195 ASN A CB  1 
ATOM   1226 C CG  . ASN A 1 195 ? 0.77481   -2.73047  9.12145  1.000 20.17668 ? 195 ASN A CG  1 
ATOM   1227 O OD1 . ASN A 1 195 ? -0.05326  -2.00462  8.56043  1.000 22.41263 ? 195 ASN A OD1 1 
ATOM   1228 N ND2 . ASN A 1 195 ? 0.99917   -2.67642  10.42986 1.000 18.49975 ? 195 ASN A ND2 1 
ATOM   1229 N N   . TYR A 1 196 ? 2.09003   -6.00257  6.09343  1.000 26.57190 ? 196 TYR A N   1 
ATOM   1230 C CA  . TYR A 1 196 ? 2.97409   -6.84246  5.28871  1.000 32.67994 ? 196 TYR A CA  1 
ATOM   1231 C C   . TYR A 1 196 ? 2.81803   -6.55345  3.79450  1.000 31.86168 ? 196 TYR A C   1 
ATOM   1232 O O   . TYR A 1 196 ? 3.77973   -6.66478  3.04012  1.000 30.43662 ? 196 TYR A O   1 
ATOM   1233 C CB  . TYR A 1 196 ? 2.72438   -8.32888  5.56592  1.000 36.67835 ? 196 TYR A CB  1 
ATOM   1234 C CG  . TYR A 1 196 ? 3.51890   -8.85175  6.73810  1.000 52.07724 ? 196 TYR A CG  1 
ATOM   1235 C CD1 . TYR A 1 196 ? 4.79446   -8.36932  7.00200  1.000 56.09540 ? 196 TYR A CD1 1 
ATOM   1236 C CD2 . TYR A 1 196 ? 2.99111   -9.81720  7.59354  1.000 62.87107 ? 196 TYR A CD2 1 
ATOM   1237 C CE1 . TYR A 1 196 ? 5.53101   -8.83821  8.08085  1.000 65.14443 ? 196 TYR A CE1 1 
ATOM   1238 C CE2 . TYR A 1 196 ? 3.72082   -10.29402 8.67849  1.000 65.40457 ? 196 TYR A CE2 1 
ATOM   1239 C CZ  . TYR A 1 196 ? 4.99090   -9.79902  8.91550  1.000 70.38395 ? 196 TYR A CZ  1 
ATOM   1240 O OH  . TYR A 1 196 ? 5.72566   -10.26201 9.98500  1.000 77.05833 ? 196 TYR A OH  1 
ATOM   1241 N N   . ALA A 1 197 ? 1.61332   -6.17590  3.37658  1.000 23.08937 ? 197 ALA A N   1 
ATOM   1242 C CA  . ALA A 1 197 ? 1.36891   -5.79077  1.98658  1.000 27.53564 ? 197 ALA A CA  1 
ATOM   1243 C C   . ALA A 1 197 ? 1.50624   -4.27344  1.77818  1.000 30.93223 ? 197 ALA A C   1 
ATOM   1244 O O   . ALA A 1 197 ? 0.98089   -3.72442  0.80994  1.000 34.22569 ? 197 ALA A O   1 
ATOM   1245 C CB  . ALA A 1 197 ? -0.00797  -6.26077  1.54920  1.000 27.89301 ? 197 ALA A CB  1 
ATOM   1246 N N   . SER A 1 198 ? 2.21287   -3.60952  2.69507  1.000 32.52434 ? 198 SER A N   1 
ATOM   1247 C CA  . SER A 1 198 ? 2.42322   -2.16101  2.65432  1.000 30.60797 ? 198 SER A CA  1 
ATOM   1248 C C   . SER A 1 198 ? 1.11003   -1.38024  2.62613  1.000 29.66581 ? 198 SER A C   1 
ATOM   1249 O O   . SER A 1 198 ? 1.01032   -0.31845  2.01275  1.000 29.17319 ? 198 SER A O   1 
ATOM   1250 C CB  . SER A 1 198 ? 3.29686   -1.77728  1.45324  1.000 37.86221 ? 198 SER A CB  1 
ATOM   1251 O OG  . SER A 1 198 ? 4.64123   -2.17729  1.66292  1.000 42.40130 ? 198 SER A OG  1 
ATOM   1252 N N   . LYS A 1 199 ? 0.09938   -1.91117  3.29918  1.000 20.24453 ? 199 LYS A N   1 
ATOM   1253 C CA  . LYS A 1 199 ? -1.14484  -1.18660  3.47209  1.000 23.14691 ? 199 LYS A CA  1 
ATOM   1254 C C   . LYS A 1 199 ? -1.34854  -0.92446  4.94646  1.000 27.47231 ? 199 LYS A C   1 
ATOM   1255 O O   . LYS A 1 199 ? -0.77752  -1.60889  5.78693  1.000 23.34629 ? 199 LYS A O   1 
ATOM   1256 C CB  . LYS A 1 199 ? -2.31876  -1.98003  2.90594  1.000 24.34145 ? 199 LYS A CB  1 
ATOM   1257 C CG  . LYS A 1 199 ? -2.22526  -2.23360  1.42767  1.000 24.91093 ? 199 LYS A CG  1 
ATOM   1258 C CD  . LYS A 1 199 ? -2.55758  -0.98036  0.66038  1.000 27.96683 ? 199 LYS A CD  1 
ATOM   1259 C CE  . LYS A 1 199 ? -2.88532  -1.30178  -0.78030 1.000 36.11377 ? 199 LYS A CE  1 
ATOM   1260 N NZ  . LYS A 1 199 ? -3.17172  -0.08323  -1.57942 1.000 36.90866 ? 199 LYS A NZ  1 
ATOM   1261 N N   . ASP A 1 200 ? -2.16964  0.06297   5.26687  1.000 27.36392 ? 200 ASP A N   1 
ATOM   1262 C CA  . ASP A 1 200 ? -2.47715  0.32167   6.65615  1.000 21.50595 ? 200 ASP A CA  1 
ATOM   1263 C C   . ASP A 1 200 ? -3.95443  0.67927   6.79159  1.000 28.71890 ? 200 ASP A C   1 
ATOM   1264 O O   . ASP A 1 200 ? -4.66450  0.84742   5.78946  1.000 23.20523 ? 200 ASP A O   1 
ATOM   1265 C CB  . ASP A 1 200 ? -1.58730  1.43449   7.20688  1.000 22.79124 ? 200 ASP A CB  1 
ATOM   1266 C CG  . ASP A 1 200 ? -1.43996  1.37518   8.72584  1.000 24.72765 ? 200 ASP A CG  1 
ATOM   1267 O OD1 . ASP A 1 200 ? -1.88241  0.37863   9.34081  1.000 25.34201 ? 200 ASP A OD1 1 
ATOM   1268 O OD2 . ASP A 1 200 ? -0.87923  2.32393   9.30865  1.000 25.71841 ? 200 ASP A OD2 1 
ATOM   1269 N N   . CYS A 1 201 ? -4.41168  0.77707   8.03509  1.000 18.36870 ? 201 CYS A N   1 
ATOM   1270 C CA  . CYS A 1 201 ? -5.80480  1.06067   8.31806  1.000 17.88965 ? 201 CYS A CA  1 
ATOM   1271 C C   . CYS A 1 201 ? -5.92333  1.99689   9.52096  1.000 18.63628 ? 201 CYS A C   1 
ATOM   1272 O O   . CYS A 1 201 ? -4.92402  2.35447   10.14408 1.000 19.12967 ? 201 CYS A O   1 
ATOM   1273 C CB  . CYS A 1 201 ? -6.55953  -0.25079  8.58477  1.000 16.99782 ? 201 CYS A CB  1 
ATOM   1274 S SG  . CYS A 1 201 ? -5.91622  -1.19681  10.02562 1.000 22.03518 ? 201 CYS A SG  1 
ATOM   1275 N N   . TYR A 1 202 ? -7.14424  2.41632   9.82234  1.000 16.58770 ? 202 TYR A N   1 
ATOM   1276 C CA  . TYR A 1 202 ? -7.45871  2.91081   11.15849 1.000 14.76802 ? 202 TYR A CA  1 
ATOM   1277 C C   . TYR A 1 202 ? -8.24739  1.82951   11.89819 1.000 17.49034 ? 202 TYR A C   1 
ATOM   1278 O O   . TYR A 1 202 ? -8.63555  0.82000   11.29787 1.000 17.13652 ? 202 TYR A O   1 
ATOM   1279 C CB  . TYR A 1 202 ? -8.24759  4.21165   11.09388 1.000 15.47745 ? 202 TYR A CB  1 
ATOM   1280 C CG  . TYR A 1 202 ? -7.43942  5.36297   10.53786 1.000 18.42952 ? 202 TYR A CG  1 
ATOM   1281 C CD1 . TYR A 1 202 ? -6.47582  5.99590   11.31462 1.000 18.22923 ? 202 TYR A CD1 1 
ATOM   1282 C CD2 . TYR A 1 202 ? -7.62571  5.80629   9.23502  1.000 21.95992 ? 202 TYR A CD2 1 
ATOM   1283 C CE1 . TYR A 1 202 ? -5.72939  7.04778   10.81295 1.000 24.49833 ? 202 TYR A CE1 1 
ATOM   1284 C CE2 . TYR A 1 202 ? -6.88385  6.86581   8.72657  1.000 28.21096 ? 202 TYR A CE2 1 
ATOM   1285 C CZ  . TYR A 1 202 ? -5.93927  7.47535   9.51910  1.000 27.72529 ? 202 TYR A CZ  1 
ATOM   1286 O OH  . TYR A 1 202 ? -5.20235  8.52096   9.01495  1.000 39.19689 ? 202 TYR A OH  1 
ATOM   1287 N N   . LYS A 1 203 ? -8.43924  2.02435   13.20105 1.000 12.83420 ? 203 LYS A N   1 
ATOM   1288 C CA  . LYS A 1 203 ? -9.33495  1.19827   13.99728 1.000 13.62954 ? 203 LYS A CA  1 
ATOM   1289 C C   . LYS A 1 203 ? -10.59426 2.01861   14.25479 1.000 14.97141 ? 203 LYS A C   1 
ATOM   1290 O O   . LYS A 1 203 ? -10.50570 3.19569   14.60528 1.000 18.69582 ? 203 LYS A O   1 
ATOM   1291 C CB  . LYS A 1 203 ? -8.68596  0.78268   15.33016 1.000 14.74791 ? 203 LYS A CB  1 
ATOM   1292 C CG  . LYS A 1 203 ? -7.35323  0.01297   15.23094 1.000 14.00907 ? 203 LYS A CG  1 
ATOM   1293 C CD  . LYS A 1 203 ? -7.57621  -1.45052  14.91765 1.000 14.35110 ? 203 LYS A CD  1 
ATOM   1294 C CE  . LYS A 1 203 ? -6.27235  -2.25911  14.92654 1.000 11.16911 ? 203 LYS A CE  1 
ATOM   1295 N NZ  . LYS A 1 203 ? -5.61953  -2.34909  16.26936 1.000 7.49102  ? 203 LYS A NZ  1 
ATOM   1296 N N   . ILE A 1 204 ? -11.76097 1.42415   14.03873 1.000 16.12949 ? 204 ILE A N   1 
ATOM   1297 C CA  . ILE A 1 204 ? -12.98922 2.03687   14.50446 1.000 13.36630 ? 204 ILE A CA  1 
ATOM   1298 C C   . ILE A 1 204 ? -13.50724 1.24385   15.70586 1.000 10.79378 ? 204 ILE A C   1 
ATOM   1299 O O   . ILE A 1 204 ? -13.65278 0.01283   15.65623 1.000 15.87038 ? 204 ILE A O   1 
ATOM   1300 C CB  . ILE A 1 204 ? -14.07462 2.14011   13.38126 1.000 13.85423 ? 204 ILE A CB  1 
ATOM   1301 C CG1 . ILE A 1 204 ? -15.36058 2.76016   13.93915 1.000 17.09150 ? 204 ILE A CG1 1 
ATOM   1302 C CG2 . ILE A 1 204 ? -14.35235 0.77829   12.71342 1.000 10.38347 ? 204 ILE A CG2 1 
ATOM   1303 C CD1 . ILE A 1 204 ? -16.42548 3.07549   12.86081 1.000 17.02301 ? 204 ILE A CD1 1 
ATOM   1304 N N   . PHE A 1 205 ? -13.73393 1.96145   16.80002 1.000 13.80620 ? 205 PHE A N   1 
ATOM   1305 C CA  . PHE A 1 205 ? -14.30699 1.40151   18.02314 1.000 13.03300 ? 205 PHE A CA  1 
ATOM   1306 C C   . PHE A 1 205 ? -15.75934 1.85529   18.12842 1.000 11.15278 ? 205 PHE A C   1 
ATOM   1307 O O   . PHE A 1 205 ? -16.03895 3.03717   17.98704 1.000 13.35618 ? 205 PHE A O   1 
ATOM   1308 C CB  . PHE A 1 205 ? -13.54810 1.87626   19.28245 1.000 11.32156 ? 205 PHE A CB  1 
ATOM   1309 C CG  . PHE A 1 205 ? -12.16226 1.31346   19.42422 1.000 12.69730 ? 205 PHE A CG  1 
ATOM   1310 C CD1 . PHE A 1 205 ? -11.08863 1.89181   18.75689 1.000 9.88905  ? 205 PHE A CD1 1 
ATOM   1311 C CD2 . PHE A 1 205 ? -11.93273 0.22240   20.24399 1.000 12.98656 ? 205 PHE A CD2 1 
ATOM   1312 C CE1 . PHE A 1 205 ? -9.80524  1.37417   18.89268 1.000 12.46834 ? 205 PHE A CE1 1 
ATOM   1313 C CE2 . PHE A 1 205 ? -10.66456 -0.30446  20.39264 1.000 10.63017 ? 205 PHE A CE2 1 
ATOM   1314 C CZ  . PHE A 1 205 ? -9.59114  0.27003   19.71417 1.000 15.52345 ? 205 PHE A CZ  1 
ATOM   1315 N N   . ALA A 1 206 ? -16.67844 0.93229   18.37486 1.000 13.43347 ? 206 ALA A N   1 
ATOM   1316 C CA  . ALA A 1 206 ? -18.03426 1.31351   18.74930 1.000 13.42160 ? 206 ALA A CA  1 
ATOM   1317 C C   . ALA A 1 206 ? -18.22231 0.96434   20.21162 1.000 14.92372 ? 206 ALA A C   1 
ATOM   1318 O O   . ALA A 1 206 ? -17.68294 -0.02918  20.68154 1.000 16.16226 ? 206 ALA A O   1 
ATOM   1319 C CB  . ALA A 1 206 ? -19.06558 0.60663   17.89324 1.000 12.46457 ? 206 ALA A CB  1 
ATOM   1320 N N   . TYR A 1 207 ? -18.97676 1.78571   20.92661 1.000 14.96371 ? 207 TYR A N   1 
ATOM   1321 C CA  . TYR A 1 207 ? -19.25561 1.55386   22.34067 1.000 14.04228 ? 207 TYR A CA  1 
ATOM   1322 C C   . TYR A 1 207 ? -20.74002 1.73188   22.61124 1.000 17.02293 ? 207 TYR A C   1 
ATOM   1323 O O   . TYR A 1 207 ? -21.39466 2.57958   21.99310 1.000 20.17186 ? 207 TYR A O   1 
ATOM   1324 C CB  . TYR A 1 207 ? -18.49601 2.53501   23.23282 1.000 16.88760 ? 207 TYR A CB  1 
ATOM   1325 C CG  . TYR A 1 207 ? -17.03987 2.74449   22.90649 1.000 13.42920 ? 207 TYR A CG  1 
ATOM   1326 C CD1 . TYR A 1 207 ? -16.65024 3.66159   21.93746 1.000 13.29514 ? 207 TYR A CD1 1 
ATOM   1327 C CD2 . TYR A 1 207 ? -16.05419 2.05983   23.60337 1.000 13.41231 ? 207 TYR A CD2 1 
ATOM   1328 C CE1 . TYR A 1 207 ? -15.30937 3.87035   21.65068 1.000 15.10351 ? 207 TYR A CE1 1 
ATOM   1329 C CE2 . TYR A 1 207 ? -14.71241 2.25576   23.31989 1.000 10.03331 ? 207 TYR A CE2 1 
ATOM   1330 C CZ  . TYR A 1 207 ? -14.34616 3.16215   22.34335 1.000 12.41466 ? 207 TYR A CZ  1 
ATOM   1331 O OH  . TYR A 1 207 ? -13.00205 3.37422   22.06565 1.000 14.72034 ? 207 TYR A OH  1 
ATOM   1332 N N   . GLY A 1 208 ? -21.25101 0.97893   23.57713 1.000 12.69908 ? 208 GLY A N   1 
ATOM   1333 C CA  . GLY A 1 208 ? -22.62896 1.13458   24.01444 1.000 13.28148 ? 208 GLY A CA  1 
ATOM   1334 C C   . GLY A 1 208 ? -23.19425 -0.15949  24.56153 1.000 18.27138 ? 208 GLY A C   1 
ATOM   1335 O O   . GLY A 1 208 ? -22.46793 -1.02681  25.06622 1.000 16.90382 ? 208 GLY A O   1 
ATOM   1336 N N   . ASN A 1 209 ? -24.50948 -0.29307  24.47086 1.000 17.74175 ? 209 ASN A N   1 
ATOM   1337 C CA  . ASN A 1 209 ? -25.14827 -1.55710  24.78638 1.000 18.44485 ? 209 ASN A CA  1 
ATOM   1338 C C   . ASN A 1 209 ? -25.25893 -2.39627  23.51060 1.000 20.47201 ? 209 ASN A C   1 
ATOM   1339 O O   . ASN A 1 209 ? -26.34811 -2.57040  22.95266 1.000 19.98730 ? 209 ASN A O   1 
ATOM   1340 C CB  . ASN A 1 209 ? -26.51868 -1.31803  25.40931 1.000 15.92121 ? 209 ASN A CB  1 
ATOM   1341 C CG  . ASN A 1 209 ? -27.21003 -2.60608  25.77845 1.000 28.66783 ? 209 ASN A CG  1 
ATOM   1342 O OD1 . ASN A 1 209 ? -26.55560 -3.62242  26.02360 1.000 32.35416 ? 209 ASN A OD1 1 
ATOM   1343 N ND2 . ASN A 1 209 ? -28.53868 -2.58199  25.80147 1.000 35.18475 ? 209 ASN A ND2 1 
ATOM   1344 N N   . LEU A 1 210 ? -24.12065 -2.90213  23.03814 1.000 18.25755 ? 210 LEU A N   1 
ATOM   1345 C CA  . LEU A 1 210 ? -24.07487 -3.53032  21.72658 1.000 16.49218 ? 210 LEU A CA  1 
ATOM   1346 C C   . LEU A 1 210 ? -24.64082 -4.94310  21.81215 1.000 20.86682 ? 210 LEU A C   1 
ATOM   1347 O O   . LEU A 1 210 ? -24.36327 -5.67779  22.75804 1.000 18.94771 ? 210 LEU A O   1 
ATOM   1348 C CB  . LEU A 1 210 ? -22.64539 -3.55358  21.17557 1.000 12.40972 ? 210 LEU A CB  1 
ATOM   1349 C CG  . LEU A 1 210 ? -21.88751 -2.21249  21.17703 1.000 15.49210 ? 210 LEU A CG  1 
ATOM   1350 C CD1 . LEU A 1 210 ? -20.48782 -2.38424  20.58035 1.000 15.94226 ? 210 LEU A CD1 1 
ATOM   1351 C CD2 . LEU A 1 210 ? -22.66931 -1.11091  20.44983 1.000 19.94511 ? 210 LEU A CD2 1 
ATOM   1352 N N   . LYS A 1 211 ? -25.45885 -5.29966  20.82985 1.000 20.32601 ? 211 LYS A N   1 
ATOM   1353 C CA  . LYS A 1 211 ? -26.04853 -6.62909  20.75944 1.000 22.64269 ? 211 LYS A CA  1 
ATOM   1354 C C   . LYS A 1 211 ? -26.06882 -7.08505  19.31588 1.000 15.38739 ? 211 LYS A C   1 
ATOM   1355 O O   . LYS A 1 211 ? -26.42694 -6.31205  18.42138 1.000 22.67562 ? 211 LYS A O   1 
ATOM   1356 C CB  . LYS A 1 211 ? -27.47110 -6.63828  21.32424 1.000 20.66584 ? 211 LYS A CB  1 
ATOM   1357 C CG  . LYS A 1 211 ? -27.60369 -6.28648  22.79561 1.000 28.81336 ? 211 LYS A CG  1 
ATOM   1358 C CD  . LYS A 1 211 ? -29.06410 -6.44559  23.22382 1.000 35.37985 ? 211 LYS A CD  1 
ATOM   1359 C CE  . LYS A 1 211 ? -29.43559 -5.54200  24.38571 1.000 38.23117 ? 211 LYS A CE  1 
ATOM   1360 N NZ  . LYS A 1 211 ? -28.77850 -5.92162  25.66832 1.000 47.87711 ? 211 LYS A NZ  1 
ATOM   1361 N N   . VAL A 1 212 ? -25.69304 -8.33515  19.07908 1.000 14.98964 ? 212 VAL A N   1 
ATOM   1362 C CA  . VAL A 1 212 ? -25.76785 -8.87639  17.73487 1.000 16.61018 ? 212 VAL A CA  1 
ATOM   1363 C C   . VAL A 1 212 ? -26.42372 -10.24789 17.75818 1.000 22.38088 ? 212 VAL A C   1 
ATOM   1364 O O   . VAL A 1 212 ? -26.37269 -10.96612 18.75982 1.000 26.70121 ? 212 VAL A O   1 
ATOM   1365 C CB  . VAL A 1 212 ? -24.36662 -8.97735  17.05677 1.000 25.38052 ? 212 VAL A CB  1 
ATOM   1366 C CG1 . VAL A 1 212 ? -23.67213 -7.61229  17.02416 1.000 25.93650 ? 212 VAL A CG1 1 
ATOM   1367 C CG2 . VAL A 1 212 ? -23.48654 -10.01484 17.75274 1.000 23.35545 ? 212 VAL A CG2 1 
ATOM   1368 N N   . ASN A 1 213 ? -27.05839 -10.60298 16.64838 1.000 17.71219 ? 213 ASN A N   1 
ATOM   1369 C CA  . ASN A 1 213 ? -27.52975 -11.96548 16.45569 1.000 22.57262 ? 213 ASN A CA  1 
ATOM   1370 C C   . ASN A 1 213 ? -26.55988 -12.66947 15.51975 1.000 25.27312 ? 213 ASN A C   1 
ATOM   1371 O O   . ASN A 1 213 ? -26.40964 -12.27329 14.36221 1.000 20.69749 ? 213 ASN A O   1 
ATOM   1372 C CB  . ASN A 1 213 ? -28.95740 -11.98179 15.89805 1.000 26.62758 ? 213 ASN A CB  1 
ATOM   1373 C CG  . ASN A 1 213 ? -29.54662 -13.38816 15.81682 1.000 27.71973 ? 213 ASN A CG  1 
ATOM   1374 O OD1 . ASN A 1 213 ? -28.92553 -14.36893 16.22889 1.000 29.29985 ? 213 ASN A OD1 1 
ATOM   1375 N ND2 . ASN A 1 213 ? -30.76036 -13.48429 15.28964 1.000 33.74516 ? 213 ASN A ND2 1 
ATOM   1376 N N   . THR A 1 214 ? -25.88764 -13.69387 16.03796 1.000 21.72551 ? 214 THR A N   1 
ATOM   1377 C CA  . THR A 1 214 ? -24.86199 -14.40519 15.28608 1.000 26.74954 ? 214 THR A CA  1 
ATOM   1378 C C   . THR A 1 214 ? -25.44409 -15.61009 14.56000 1.000 36.43978 ? 214 THR A C   1 
ATOM   1379 O O   . THR A 1 214 ? -24.76884 -16.23563 13.74605 1.000 40.64842 ? 214 THR A O   1 
ATOM   1380 C CB  . THR A 1 214 ? -23.71073 -14.87178 16.20680 1.000 27.74567 ? 214 THR A CB  1 
ATOM   1381 O OG1 . THR A 1 214 ? -24.16409 -15.92774 17.06608 1.000 27.82790 ? 214 THR A OG1 1 
ATOM   1382 C CG2 . THR A 1 214 ? -23.20009 -13.69951 17.05431 1.000 22.48780 ? 214 THR A CG2 1 
ATOM   1383 N N   . SER A 1 215 ? -26.70369 -15.92299 14.85061 1.000 37.77259 ? 215 SER A N   1 
ATOM   1384 C CA  . SER A 1 215 ? -27.37157 -17.06039 14.22725 1.000 45.69344 ? 215 SER A CA  1 
ATOM   1385 C C   . SER A 1 215 ? -28.06313 -16.66211 12.92900 1.000 52.50854 ? 215 SER A C   1 
ATOM   1386 O O   . SER A 1 215 ? -28.80068 -15.67522 12.87558 1.000 42.55215 ? 215 SER A O   1 
ATOM   1387 C CB  . SER A 1 215 ? -28.39318 -17.68809 15.18226 1.000 45.16157 ? 215 SER A CB  1 
ATOM   1388 O OG  . SER A 1 215 ? -29.09781 -18.74460 14.54644 1.000 46.49885 ? 215 SER A OG  1 
ATOM   1389 N N   . SER A 1 216 ? -27.82316 -17.44925 11.88632 1.000 65.40992 ? 216 SER A N   1 
ATOM   1390 C CA  . SER A 1 216 ? -28.44119 -17.21909 10.58819 1.000 69.20330 ? 216 SER A CA  1 
ATOM   1391 C C   . SER A 1 216 ? -29.85153 -17.80200 10.55245 1.000 66.42022 ? 216 SER A C   1 
ATOM   1392 O O   . SER A 1 216 ? -30.73305 -17.27568 9.87334  1.000 63.09125 ? 216 SER A O   1 
ATOM   1393 C CB  . SER A 1 216 ? -27.58163 -17.82344 9.47715  1.000 69.35494 ? 216 SER A CB  1 
ATOM   1394 O OG  . SER A 1 216 ? -27.21098 -19.15401 9.79807  1.000 70.99465 ? 216 SER A OG  1 
ATOM   1395 N N   . THR A 1 217 ? -30.06103 -18.88100 11.30099 1.000 66.42181 ? 217 THR A N   1 
ATOM   1396 C CA  . THR A 1 217 ? -31.35359 -19.56268 11.31715 1.000 64.75130 ? 217 THR A CA  1 
ATOM   1397 C C   . THR A 1 217 ? -32.26896 -19.06523 12.43258 1.000 62.23189 ? 217 THR A C   1 
ATOM   1398 O O   . THR A 1 217 ? -33.45783 -18.83313 12.20857 1.000 69.00106 ? 217 THR A O   1 
ATOM   1399 C CB  . THR A 1 217 ? -31.18930 -21.08970 11.47317 1.000 59.99568 ? 217 THR A CB  1 
ATOM   1400 O OG1 . THR A 1 217 ? -30.68735 -21.39342 12.78197 1.000 56.90593 ? 217 THR A OG1 1 
ATOM   1401 C CG2 . THR A 1 217 ? -30.23685 -21.63802 10.41687 1.000 60.56779 ? 217 THR A CG2 1 
ATOM   1402 N N   . GLY A 1 218 ? -31.71625 -18.91035 13.63238 1.000 48.92456 ? 218 GLY A N   1 
ATOM   1403 C CA  . GLY A 1 218 ? -32.50871 -18.53168 14.78890 1.000 42.64967 ? 218 GLY A CA  1 
ATOM   1404 C C   . GLY A 1 218 ? -31.92482 -17.37731 15.58175 1.000 40.99436 ? 218 GLY A C   1 
ATOM   1405 O O   . GLY A 1 218 ? -31.50930 -16.36743 15.01338 1.000 43.87660 ? 218 GLY A O   1 
ATOM   1406 N N   . VAL A 1 219 ? -31.90326 -17.52570 16.90294 1.000 38.29190 ? 219 VAL A N   1 
ATOM   1407 C CA  . VAL A 1 219 ? -31.38575 -16.48014 17.78102 1.000 41.19617 ? 219 VAL A CA  1 
ATOM   1408 C C   . VAL A 1 219 ? -30.23355 -16.95800 18.66471 1.000 38.04260 ? 219 VAL A C   1 
ATOM   1409 O O   . VAL A 1 219 ? -30.39562 -17.80869 19.54303 1.000 34.15935 ? 219 VAL A O   1 
ATOM   1410 C CB  . VAL A 1 219 ? -32.48980 -15.91065 18.68442 1.000 34.72317 ? 219 VAL A CB  1 
ATOM   1411 C CG1 . VAL A 1 219 ? -31.90677 -14.90660 19.66339 1.000 27.34864 ? 219 VAL A CG1 1 
ATOM   1412 C CG2 . VAL A 1 219 ? -33.58770 -15.27905 17.83837 1.000 37.55256 ? 219 VAL A CG2 1 
ATOM   1413 N N   . CYS A 1 220 ? -29.06208 -16.39759 18.40766 1.000 35.27999 ? 220 CYS A N   1 
ATOM   1414 C CA  . CYS A 1 220 ? -27.90710 -16.59029 19.26477 1.000 30.92131 ? 220 CYS A CA  1 
ATOM   1415 C C   . CYS A 1 220 ? -27.32089 -15.21252 19.54589 1.000 23.86880 ? 220 CYS A C   1 
ATOM   1416 O O   . CYS A 1 220 ? -26.46334 -14.72298 18.80374 1.000 23.24747 ? 220 CYS A O   1 
ATOM   1417 C CB  . CYS A 1 220 ? -26.87667 -17.50922 18.61233 1.000 31.81575 ? 220 CYS A CB  1 
ATOM   1418 S SG  . CYS A 1 220 ? -25.44676 -17.82763 19.66057 1.000 33.02396 ? 220 CYS A SG  1 
ATOM   1419 N N   . GLY A 1 221 ? -27.82389 -14.58094 20.59999 1.000 18.20141 ? 221 GLY A N   1 
ATOM   1420 C CA  . GLY A 1 221 ? -27.53307 -13.18753 20.86741 1.000 18.78407 ? 221 GLY A CA  1 
ATOM   1421 C C   . GLY A 1 221 ? -26.27337 -13.06227 21.68482 1.000 23.75148 ? 221 GLY A C   1 
ATOM   1422 O O   . GLY A 1 221 ? -26.02765 -13.88260 22.57274 1.000 23.77634 ? 221 GLY A O   1 
ATOM   1423 N N   . ILE A 1 222 ? -25.47408 -12.04585 21.37416 1.000 20.18247 ? 222 ILE A N   1 
ATOM   1424 C CA  . ILE A 1 222 ? -24.22334 -11.78428 22.08155 1.000 23.09923 ? 222 ILE A CA  1 
ATOM   1425 C C   . ILE A 1 222 ? -24.19402 -10.31000 22.44874 1.000 19.15874 ? 222 ILE A C   1 
ATOM   1426 O O   . ILE A 1 222 ? -24.57948 -9.46970  21.63873 1.000 19.20638 ? 222 ILE A O   1 
ATOM   1427 C CB  . ILE A 1 222 ? -22.98730 -12.17095 21.21854 1.000 30.74964 ? 222 ILE A CB  1 
ATOM   1428 C CG1 . ILE A 1 222 ? -22.50539 -13.58273 21.57138 1.000 27.73052 ? 222 ILE A CG1 1 
ATOM   1429 C CG2 . ILE A 1 222 ? -21.83992 -11.19033 21.39401 1.000 27.98973 ? 222 ILE A CG2 1 
ATOM   1430 C CD1 . ILE A 1 222 ? -23.38677 -14.66094 21.05064 1.000 34.96645 ? 222 ILE A CD1 1 
ATOM   1431 N N   . ALA A 1 223 ? -23.76754 -9.99828  23.67205 1.000 18.08353 ? 223 ALA A N   1 
ATOM   1432 C CA  . ALA A 1 223 ? -23.73141 -8.61278  24.13522 1.000 20.58433 ? 223 ALA A CA  1 
ATOM   1433 C C   . ALA A 1 223 ? -22.29500 -8.13807  24.39716 1.000 24.53574 ? 223 ALA A C   1 
ATOM   1434 O O   . ALA A 1 223 ? -21.49690 -8.87049  24.99833 1.000 17.53790 ? 223 ALA A O   1 
ATOM   1435 C CB  . ALA A 1 223 ? -24.58331 -8.45738  25.39216 1.000 21.41519 ? 223 ALA A CB  1 
ATOM   1436 N N   . TRP A 1 224 ? -21.97313 -6.92132  23.93626 1.000 19.55676 ? 224 TRP A N   1 
ATOM   1437 C CA  . TRP A 1 224 ? -20.64861 -6.31700  24.13315 1.000 16.01998 ? 224 TRP A CA  1 
ATOM   1438 C C   . TRP A 1 224 ? -20.75328 -4.90852  24.72553 1.000 17.50854 ? 224 TRP A C   1 
ATOM   1439 O O   . TRP A 1 224 ? -21.72693 -4.20389  24.47538 1.000 16.49982 ? 224 TRP A O   1 
ATOM   1440 C CB  . TRP A 1 224 ? -19.86989 -6.19496  22.81371 1.000 16.21268 ? 224 TRP A CB  1 
ATOM   1441 C CG  . TRP A 1 224 ? -19.56192 -7.44177  22.02419 1.000 16.80733 ? 224 TRP A CG  1 
ATOM   1442 C CD1 . TRP A 1 224 ? -19.01961 -8.61140  22.48604 1.000 16.25592 ? 224 TRP A CD1 1 
ATOM   1443 C CD2 . TRP A 1 224 ? -19.70934 -7.59817  20.60664 1.000 17.57484 ? 224 TRP A CD2 1 
ATOM   1444 N NE1 . TRP A 1 224 ? -18.85063 -9.49744  21.44179 1.000 17.51897 ? 224 TRP A NE1 1 
ATOM   1445 C CE2 . TRP A 1 224 ? -19.25656 -8.89403  20.27788 1.000 16.09661 ? 224 TRP A CE2 1 
ATOM   1446 C CE3 . TRP A 1 224 ? -20.17411 -6.75814  19.58043 1.000 19.73178 ? 224 TRP A CE3 1 
ATOM   1447 C CZ2 . TRP A 1 224 ? -19.26591 -9.37887  18.96429 1.000 18.54892 ? 224 TRP A CZ2 1 
ATOM   1448 C CZ3 . TRP A 1 224 ? -20.18104 -7.23624  18.28043 1.000 20.65752 ? 224 TRP A CZ3 1 
ATOM   1449 C CH2 . TRP A 1 224 ? -19.73564 -8.54140  17.98328 1.000 16.45784 ? 224 TRP A CH2 1 
ATOM   1450 N N   . ARG A 1 225 ? -19.73738 -4.48161  25.47655 1.000 14.02162 ? 225 ARG A N   1 
ATOM   1451 C CA  . ARG A 1 225 ? -19.63257 -3.06898  25.84751 1.000 17.20651 ? 225 ARG A CA  1 
ATOM   1452 C C   . ARG A 1 225 ? -18.94031 -2.28117  24.73101 1.000 16.62586 ? 225 ARG A C   1 
ATOM   1453 O O   . ARG A 1 225 ? -19.09844 -1.06537  24.62498 1.000 10.63725 ? 225 ARG A O   1 
ATOM   1454 C CB  . ARG A 1 225 ? -18.88574 -2.88972  27.17821 1.000 17.50148 ? 225 ARG A CB  1 
ATOM   1455 C CG  . ARG A 1 225 ? -17.49025 -3.51078  27.20655 1.000 16.38937 ? 225 ARG A CG  1 
ATOM   1456 C CD  . ARG A 1 225 ? -16.61246 -2.92469  28.32355 1.000 15.34929 ? 225 ARG A CD  1 
ATOM   1457 N NE  . ARG A 1 225 ? -15.34146 -3.65315  28.43974 1.000 15.57368 ? 225 ARG A NE  1 
ATOM   1458 C CZ  . ARG A 1 225 ? -14.28647 -3.25081  29.15286 1.000 17.45116 ? 225 ARG A CZ  1 
ATOM   1459 N NH1 . ARG A 1 225 ? -14.32483 -2.10956  29.82907 1.000 15.82097 ? 225 ARG A NH1 1 
ATOM   1460 N NH2 . ARG A 1 225 ? -13.18597 -4.00008  29.19056 1.000 14.75901 ? 225 ARG A NH2 1 
ATOM   1461 N N   . TYR A 1 226 ? -18.18199 -2.97116  23.88664 1.000 11.80972 ? 226 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 226 ? -17.54707 -2.30305  22.75446 1.000 11.20602 ? 226 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 226 ? -17.17965 -3.31952  21.67568 1.000 13.87683 ? 226 TYR A C   1 
ATOM   1464 O O   . TYR A 1 226 ? -17.17876 -4.53190  21.91577 1.000 15.19358 ? 226 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 226 ? -16.28850 -1.52911  23.19458 1.000 8.77530  ? 226 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 226 ? -15.03698 -2.38399  23.26288 1.000 13.19113 ? 226 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 226 ? -14.72514 -3.10288  24.41262 1.000 8.62959  ? 226 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 226 ? -14.15975 -2.46226  22.18446 1.000 13.45017 ? 226 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 226 ? -13.57946 -3.88513  24.48212 1.000 14.44105 ? 226 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 226 ? -13.01484 -3.25517  22.23901 1.000 13.71964 ? 226 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 226 ? -12.73256 -3.96258  23.39253 1.000 14.70487 ? 226 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 226 ? -11.58908 -4.72747  23.46924 1.000 13.35819 ? 226 TYR A OH  1 
ATOM   1473 N N   . HIS A 1 227 ? -16.88034 -2.82464  20.48110 1.000 11.57009 ? 227 HIS A N   1 
ATOM   1474 C CA  . HIS A 1 227 ? -16.41815 -3.69142  19.40115 1.000 12.96182 ? 227 HIS A CA  1 
ATOM   1475 C C   . HIS A 1 227 ? -15.42657 -2.90038  18.55361 1.000 15.14004 ? 227 HIS A C   1 
ATOM   1476 O O   . HIS A 1 227 ? -15.53822 -1.68558  18.45037 1.000 18.91191 ? 227 HIS A O   1 
ATOM   1477 C CB  . HIS A 1 227 ? -17.59981 -4.19419  18.56857 1.000 10.52518 ? 227 HIS A CB  1 
ATOM   1478 C CG  . HIS A 1 227 ? -17.23434 -5.24628  17.56599 1.000 14.46688 ? 227 HIS A CG  1 
ATOM   1479 N ND1 . HIS A 1 227 ? -16.47576 -6.35099  17.88903 1.000 18.15483 ? 227 HIS A ND1 1 
ATOM   1480 C CD2 . HIS A 1 227 ? -17.53827 -5.37124  16.25119 1.000 15.42886 ? 227 HIS A CD2 1 
ATOM   1481 C CE1 . HIS A 1 227 ? -16.31984 -7.10485  16.81472 1.000 18.43214 ? 227 HIS A CE1 1 
ATOM   1482 N NE2 . HIS A 1 227 ? -16.95920 -6.53584  15.80897 1.000 17.25637 ? 227 HIS A NE2 1 
ATOM   1483 N N   . VAL A 1 228 ? -14.43032 -3.56966  17.98615 1.000 10.36364 ? 228 VAL A N   1 
ATOM   1484 C CA  . VAL A 1 228 ? -13.45159 -2.86354  17.17350 1.000 12.64365 ? 228 VAL A CA  1 
ATOM   1485 C C   . VAL A 1 228 ? -13.17275 -3.64377  15.88655 1.000 14.07370 ? 228 VAL A C   1 
ATOM   1486 O O   . VAL A 1 228 ? -13.23979 -4.86458  15.88538 1.000 11.93267 ? 228 VAL A O   1 
ATOM   1487 C CB  . VAL A 1 228 ? -12.13502 -2.62566  17.95975 1.000 10.31328 ? 228 VAL A CB  1 
ATOM   1488 C CG1 . VAL A 1 228 ? -11.47991 -3.95390  18.35295 1.000 9.90402  ? 228 VAL A CG1 1 
ATOM   1489 C CG2 . VAL A 1 228 ? -11.17324 -1.77525  17.15292 1.000 10.59168 ? 228 VAL A CG2 1 
ATOM   1490 N N   . ALA A 1 229 ? -12.89657 -2.93829  14.79270 1.000 10.75717 ? 229 ALA A N   1 
ATOM   1491 C CA  . ALA A 1 229 ? -12.52631 -3.58138  13.53288 1.000 14.61473 ? 229 ALA A CA  1 
ATOM   1492 C C   . ALA A 1 229 ? -11.65742 -2.62171  12.71130 1.000 16.74958 ? 229 ALA A C   1 
ATOM   1493 O O   . ALA A 1 229 ? -11.67060 -1.41918  12.96227 1.000 14.92573 ? 229 ALA A O   1 
ATOM   1494 C CB  . ALA A 1 229 ? -13.77872 -4.00490  12.74356 1.000 10.08137 ? 229 ALA A CB  1 
ATOM   1495 N N   . PRO A 1 230 ? -10.87190 -3.15074  11.75151 1.000 15.02063 ? 230 PRO A N   1 
ATOM   1496 C CA  . PRO A 1 230 ? -10.09292 -2.24679  10.90159 1.000 14.46073 ? 230 PRO A CA  1 
ATOM   1497 C C   . PRO A 1 230 ? -10.98388 -1.40506  9.99790  1.000 16.12291 ? 230 PRO A C   1 
ATOM   1498 O O   . PRO A 1 230 ? -12.07258 -1.82375  9.60727  1.000 16.47521 ? 230 PRO A O   1 
ATOM   1499 C CB  . PRO A 1 230 ? -9.21631  -3.19167  10.06200 1.000 15.24076 ? 230 PRO A CB  1 
ATOM   1500 C CG  . PRO A 1 230 ? -9.20933  -4.47406  10.78396 1.000 12.36109 ? 230 PRO A CG  1 
ATOM   1501 C CD  . PRO A 1 230 ? -10.54520 -4.56239  11.49007 1.000 12.33907 ? 230 PRO A CD  1 
ATOM   1502 N N   . LEU A 1 231 ? -10.48440 -0.22665  9.65899  1.000 13.70882 ? 231 LEU A N   1 
ATOM   1503 C CA  . LEU A 1 231 ? -11.17504 0.71211   8.79819  1.000 15.65690 ? 231 LEU A CA  1 
ATOM   1504 C C   . LEU A 1 231 ? -10.25946 1.13310   7.64914  1.000 17.53695 ? 231 LEU A C   1 
ATOM   1505 O O   . LEU A 1 231 ? -9.16496  1.66224   7.87495  1.000 15.94347 ? 231 LEU A O   1 
ATOM   1506 C CB  . LEU A 1 231 ? -11.61307 1.92824   9.61005  1.000 11.32604 ? 231 LEU A CB  1 
ATOM   1507 C CG  . LEU A 1 231 ? -12.60711 2.86869   8.96226  1.000 21.16251 ? 231 LEU A CG  1 
ATOM   1508 C CD1 . LEU A 1 231 ? -14.01351 2.27333   9.02660  1.000 18.76829 ? 231 LEU A CD1 1 
ATOM   1509 C CD2 . LEU A 1 231 ? -12.51472 4.24213   9.63473  1.000 20.42892 ? 231 LEU A CD2 1 
ATOM   1510 N N   . ILE A 1 232 ? -10.69708 0.89314   6.41871  1.000 13.06500 ? 232 ILE A N   1 
ATOM   1511 C CA  . ILE A 1 232 ? -9.86715  1.20239   5.25755  1.000 17.90723 ? 232 ILE A CA  1 
ATOM   1512 C C   . ILE A 1 232 ? -10.59704 2.11346   4.27201  1.000 18.21967 ? 232 ILE A C   1 
ATOM   1513 O O   . ILE A 1 232 ? -11.82860 2.18315   4.26802  1.000 18.76650 ? 232 ILE A O   1 
ATOM   1514 C CB  . ILE A 1 232 ? -9.41618  -0.07578  4.51610  1.000 20.30849 ? 232 ILE A CB  1 
ATOM   1515 C CG1 . ILE A 1 232 ? -10.62950 -0.90518  4.08759  1.000 19.70617 ? 232 ILE A CG1 1 
ATOM   1516 C CG2 . ILE A 1 232 ? -8.46942  -0.89258  5.39047  1.000 21.11565 ? 232 ILE A CG2 1 
ATOM   1517 C CD1 . ILE A 1 232 ? -10.28124 -2.07883  3.16332  1.000 21.13697 ? 232 ILE A CD1 1 
ATOM   1518 N N   . SER A 1 233 ? -9.82424  2.81564   3.44608  1.000 18.52099 ? 233 SER A N   1 
ATOM   1519 C CA  . SER A 1 233 ? -10.38222 3.75800   2.47547  1.000 25.93418 ? 233 SER A CA  1 
ATOM   1520 C C   . SER A 1 233 ? -10.48683 3.11626   1.09959  1.000 25.08954 ? 233 SER A C   1 
ATOM   1521 O O   . SER A 1 233 ? -9.47721  2.74982   0.49295  1.000 25.71578 ? 233 SER A O   1 
ATOM   1522 C CB  . SER A 1 233 ? -9.53080  5.03271   2.40067  1.000 25.11402 ? 233 SER A CB  1 
ATOM   1523 O OG  . SER A 1 233 ? -10.13189 6.00562   1.55250  1.000 21.65869 ? 233 SER A OG  1 
ATOM   1524 N N   . VAL A 1 234 ? -11.71881 2.97581   0.62130  1.000 19.69900 ? 234 VAL A N   1 
ATOM   1525 C CA  . VAL A 1 234 ? -11.98739 2.39388   -0.68517 1.000 23.08208 ? 234 VAL A CA  1 
ATOM   1526 C C   . VAL A 1 234 ? -12.73682 3.40568   -1.54287 1.000 27.26645 ? 234 VAL A C   1 
ATOM   1527 O O   . VAL A 1 234 ? -13.89136 3.72874   -1.26169 1.000 27.06199 ? 234 VAL A O   1 
ATOM   1528 C CB  . VAL A 1 234 ? -12.81298 1.10258   -0.56545 1.000 27.82607 ? 234 VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 234 ? -13.02613 0.47207   -1.93347 1.000 23.68930 ? 234 VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 234 ? -12.12530 0.13456   0.37907  1.000 33.01866 ? 234 VAL A CG2 1 
ATOM   1531 N N   . ASN A 1 235 ? -12.07494 3.90701   -2.58132 1.000 26.15645 ? 235 ASN A N   1 
ATOM   1532 C CA  . ASN A 1 235 ? -12.64216 4.95504   -3.42174 1.000 27.32882 ? 235 ASN A CA  1 
ATOM   1533 C C   . ASN A 1 235 ? -13.21419 6.11075   -2.59048 1.000 30.13825 ? 235 ASN A C   1 
ATOM   1534 O O   . ASN A 1 235 ? -14.32614 6.58030   -2.84149 1.000 31.79708 ? 235 ASN A O   1 
ATOM   1535 C CB  . ASN A 1 235 ? -13.72843 4.38400   -4.34092 1.000 23.24026 ? 235 ASN A CB  1 
ATOM   1536 C CG  . ASN A 1 235 ? -13.21524 3.25597   -5.23991 1.000 32.80254 ? 235 ASN A CG  1 
ATOM   1537 O OD1 . ASN A 1 235 ? -12.02391 3.17252   -5.55034 1.000 27.80453 ? 235 ASN A OD1 1 
ATOM   1538 N ND2 . ASN A 1 235 ? -14.12491 2.38838   -5.66787 1.000 31.50628 ? 235 ASN A ND2 1 
ATOM   1539 N N   . GLY A 1 236 ? -12.45267 6.55225   -1.59395 1.000 24.83294 ? 236 GLY A N   1 
ATOM   1540 C CA  . GLY A 1 236 ? -12.84724 7.68021   -0.76693 1.000 29.50373 ? 236 GLY A CA  1 
ATOM   1541 C C   . GLY A 1 236 ? -13.93746 7.41020   0.25709  1.000 28.84826 ? 236 GLY A C   1 
ATOM   1542 O O   . GLY A 1 236 ? -14.39249 8.32961   0.93712  1.000 32.91563 ? 236 GLY A O   1 
ATOM   1543 N N   . VAL A 1 237 ? -14.36799 6.15759   0.36534  1.000 25.04559 ? 237 VAL A N   1 
ATOM   1544 C CA  . VAL A 1 237 ? -15.36463 5.77756   1.36648  1.000 25.43800 ? 237 VAL A CA  1 
ATOM   1545 C C   . VAL A 1 237 ? -14.72764 4.85482   2.39931  1.000 25.33782 ? 237 VAL A C   1 
ATOM   1546 O O   . VAL A 1 237 ? -14.16602 3.80972   2.03652  1.000 23.23852 ? 237 VAL A O   1 
ATOM   1547 C CB  . VAL A 1 237 ? -16.58787 5.06798   0.72662  1.000 37.72860 ? 237 VAL A CB  1 
ATOM   1548 C CG1 . VAL A 1 237 ? -17.65269 4.76816   1.77878  1.000 32.39363 ? 237 VAL A CG1 1 
ATOM   1549 C CG2 . VAL A 1 237 ? -17.17345 5.91002   -0.39672 1.000 40.34932 ? 237 VAL A CG2 1 
ATOM   1550 N N   . TRP A 1 238 ? -14.80356 5.22646   3.67955  1.000 23.43364 ? 238 TRP A N   1 
ATOM   1551 C CA  . TRP A 1 238 ? -14.25038 4.36409   4.72315  1.000 18.64618 ? 238 TRP A CA  1 
ATOM   1552 C C   . TRP A 1 238 ? -15.11713 3.12147   4.89943  1.000 25.81730 ? 238 TRP A C   1 
ATOM   1553 O O   . TRP A 1 238 ? -16.32911 3.21120   5.09964  1.000 29.20503 ? 238 TRP A O   1 
ATOM   1554 C CB  . TRP A 1 238 ? -14.09983 5.11560   6.04796  1.000 21.62988 ? 238 TRP A CB  1 
ATOM   1555 C CG  . TRP A 1 238 ? -13.05090 6.17594   5.95519  1.000 21.26510 ? 238 TRP A CG  1 
ATOM   1556 C CD1 . TRP A 1 238 ? -13.25373 7.51778   5.78519  1.000 24.69351 ? 238 TRP A CD1 1 
ATOM   1557 C CD2 . TRP A 1 238 ? -11.63246 5.98151   5.96347  1.000 16.45858 ? 238 TRP A CD2 1 
ATOM   1558 N NE1 . TRP A 1 238 ? -12.04408 8.17147   5.70902  1.000 22.85468 ? 238 TRP A NE1 1 
ATOM   1559 C CE2 . TRP A 1 238 ? -11.03479 7.25140   5.81298  1.000 22.23259 ? 238 TRP A CE2 1 
ATOM   1560 C CE3 . TRP A 1 238 ? -10.80679 4.85945   6.09987  1.000 22.79193 ? 238 TRP A CE3 1 
ATOM   1561 C CZ2 . TRP A 1 238 ? -9.65047  7.42934   5.79513  1.000 24.15777 ? 238 TRP A CZ2 1 
ATOM   1562 C CZ3 . TRP A 1 238 ? -9.42994  5.03577   6.07744  1.000 23.79695 ? 238 TRP A CZ3 1 
ATOM   1563 C CH2 . TRP A 1 238 ? -8.86721  6.31246   5.92947  1.000 24.48392 ? 238 TRP A CH2 1 
ATOM   1564 N N   . ASN A 1 239 ? -14.46716 1.96381   4.81401  1.000 21.26990 ? 239 ASN A N   1 
ATOM   1565 C CA  . ASN A 1 239 ? -15.11740 0.66983   4.90895  1.000 20.31727 ? 239 ASN A CA  1 
ATOM   1566 C C   . ASN A 1 239 ? -14.61365 -0.11026  6.11013  1.000 21.10452 ? 239 ASN A C   1 
ATOM   1567 O O   . ASN A 1 239 ? -13.41631 -0.15520  6.35942  1.000 20.65590 ? 239 ASN A O   1 
ATOM   1568 C CB  . ASN A 1 239 ? -14.86003 -0.14762  3.65077  1.000 20.33056 ? 239 ASN A CB  1 
ATOM   1569 C CG  . ASN A 1 239 ? -15.85309 0.14219   2.54674  1.000 27.62266 ? 239 ASN A CG  1 
ATOM   1570 O OD1 . ASN A 1 239 ? -16.49838 -0.76779  2.03706  1.000 30.31241 ? 239 ASN A OD1 1 
ATOM   1571 N ND2 . ASN A 1 239 ? -15.98139 1.40701   2.17497  1.000 32.69425 ? 239 ASN A ND2 1 
ATOM   1572 N N   . VAL A 1 240 ? -15.52341 -0.73919  6.83698  1.000 13.72040 ? 240 VAL A N   1 
ATOM   1573 C CA  . VAL A 1 240 ? -15.13666 -1.62843  7.91762  1.000 15.16653 ? 240 VAL A CA  1 
ATOM   1574 C C   . VAL A 1 240 ? -14.85600 -3.03825  7.39029  1.000 20.62628 ? 240 VAL A C   1 
ATOM   1575 O O   . VAL A 1 240 ? -15.61074 -3.57785  6.57696  1.000 21.00551 ? 240 VAL A O   1 
ATOM   1576 C CB  . VAL A 1 240 ? -16.22831 -1.69639  9.00049  1.000 23.58726 ? 240 VAL A CB  1 
ATOM   1577 C CG1 . VAL A 1 240 ? -15.72985 -2.49501  10.20367 1.000 27.58134 ? 240 VAL A CG1 1 
ATOM   1578 C CG2 . VAL A 1 240 ? -16.65140 -0.29079  9.41289  1.000 17.06494 ? 240 VAL A CG2 1 
ATOM   1579 N N   . ILE A 1 241 ? -13.75904 -3.62427  7.85506  1.000 19.22250 ? 241 ILE A N   1 
ATOM   1580 C CA  . ILE A 1 241 ? -13.40264 -4.99701  7.52170  1.000 16.36790 ? 241 ILE A CA  1 
ATOM   1581 C C   . ILE A 1 241 ? -13.65030 -5.89278  8.73594  1.000 17.85191 ? 241 ILE A C   1 
ATOM   1582 O O   . ILE A 1 241 ? -12.81534 -5.97359  9.63561  1.000 15.11572 ? 241 ILE A O   1 
ATOM   1583 C CB  . ILE A 1 241 ? -11.92076 -5.10445  7.09098  1.000 17.71062 ? 241 ILE A CB  1 
ATOM   1584 C CG1 . ILE A 1 241 ? -11.62210 -4.11301  5.95472  1.000 16.83519 ? 241 ILE A CG1 1 
ATOM   1585 C CG2 . ILE A 1 241 ? -11.56849 -6.56407  6.69888  1.000 18.26206 ? 241 ILE A CG2 1 
ATOM   1586 C CD1 . ILE A 1 241 ? -12.56347 -4.29592  4.76120  1.000 19.69443 ? 241 ILE A CD1 1 
ATOM   1587 N N   . ASP A 1 242 ? -14.79451 -6.56387  8.77731  1.000 17.47236 ? 242 ASP A N   1 
ATOM   1588 C CA  . ASP A 1 242 ? -15.11926 -7.37099  9.95275  1.000 17.06095 ? 242 ASP A CA  1 
ATOM   1589 C C   . ASP A 1 242 ? -15.70041 -8.74119  9.59225  1.000 17.80508 ? 242 ASP A C   1 
ATOM   1590 O O   . ASP A 1 242 ? -16.92702 -8.90900  9.55321  1.000 15.24598 ? 242 ASP A O   1 
ATOM   1591 C CB  . ASP A 1 242 ? -16.09679 -6.60493  10.85125 1.000 14.30234 ? 242 ASP A CB  1 
ATOM   1592 C CG  . ASP A 1 242 ? -16.25767 -7.24947  12.22379 1.000 15.07388 ? 242 ASP A CG  1 
ATOM   1593 O OD1 . ASP A 1 242 ? -15.76608 -8.38402  12.42177 1.000 16.54982 ? 242 ASP A OD1 1 
ATOM   1594 O OD2 . ASP A 1 242 ? -16.88831 -6.62328  13.10029 1.000 15.31699 ? 242 ASP A OD2 1 
ATOM   1595 N N   . PRO A 1 243 ? -14.82051 -9.73445  9.34821  1.000 14.38724 ? 243 PRO A N   1 
ATOM   1596 C CA  . PRO A 1 243 ? -15.30107 -11.07278 8.99588  1.000 19.27795 ? 243 PRO A CA  1 
ATOM   1597 C C   . PRO A 1 243 ? -16.03736 -11.77200 10.13277 1.000 20.49400 ? 243 PRO A C   1 
ATOM   1598 O O   . PRO A 1 243 ? -16.65186 -12.79718 9.88641  1.000 24.49153 ? 243 PRO A O   1 
ATOM   1599 C CB  . PRO A 1 243 ? -14.01301 -11.82905 8.63812  1.000 18.82653 ? 243 PRO A CB  1 
ATOM   1600 C CG  . PRO A 1 243 ? -13.06320 -10.75523 8.22145  1.000 16.93934 ? 243 PRO A CG  1 
ATOM   1601 C CD  . PRO A 1 243 ? -13.36633 -9.60936  9.14885  1.000 13.89055 ? 243 PRO A CD  1 
ATOM   1602 N N   . SER A 1 244 ? -15.99048 -11.24104 11.35004 1.000 15.45242 ? 244 SER A N   1 
ATOM   1603 C CA  . SER A 1 244 ? -16.75972 -11.86966 12.41534 1.000 14.53139 ? 244 SER A CA  1 
ATOM   1604 C C   . SER A 1 244 ? -18.24504 -11.48959 12.30306 1.000 22.35199 ? 244 SER A C   1 
ATOM   1605 O O   . SER A 1 244 ? -19.10041 -12.13998 12.90101 1.000 18.98833 ? 244 SER A O   1 
ATOM   1606 C CB  . SER A 1 244 ? -16.19392 -11.50023 13.79950 1.000 20.69776 ? 244 SER A CB  1 
ATOM   1607 O OG  . SER A 1 244 ? -16.43860 -10.14507 14.14105 1.000 21.38759 ? 244 SER A OG  1 
ATOM   1608 N N   . LEU A 1 245 ? -18.56344 -10.45461 11.52985 1.000 22.83798 ? 245 LEU A N   1 
ATOM   1609 C CA  . LEU A 1 245 ? -19.95788 -10.01558 11.43861 1.000 23.04200 ? 245 LEU A CA  1 
ATOM   1610 C C   . LEU A 1 245 ? -20.49967 -10.00514 10.01145 1.000 21.89788 ? 245 LEU A C   1 
ATOM   1611 O O   . LEU A 1 245 ? -21.70899 -10.08240 9.81054  1.000 22.39633 ? 245 LEU A O   1 
ATOM   1612 C CB  . LEU A 1 245 ? -20.13082 -8.61624  12.05639 1.000 20.03441 ? 245 LEU A CB  1 
ATOM   1613 C CG  . LEU A 1 245 ? -20.03483 -8.52370  13.58259 1.000 22.16918 ? 245 LEU A CG  1 
ATOM   1614 C CD1 . LEU A 1 245 ? -20.24269 -7.09465  14.06255 1.000 16.72980 ? 245 LEU A CD1 1 
ATOM   1615 C CD2 . LEU A 1 245 ? -21.03602 -9.45883  14.24273 1.000 22.52336 ? 245 LEU A CD2 1 
ATOM   1616 N N   . PHE A 1 246 ? -19.61426 -9.89847  9.02575  1.000 22.55607 ? 246 PHE A N   1 
ATOM   1617 C CA  . PHE A 1 246 ? -20.03770 -9.75645  7.62714  1.000 20.46762 ? 246 PHE A CA  1 
ATOM   1618 C C   . PHE A 1 246 ? -19.24100 -10.65494 6.68040  1.000 29.38245 ? 246 PHE A C   1 
ATOM   1619 O O   . PHE A 1 246 ? -18.21340 -11.22261 7.06624  1.000 23.54721 ? 246 PHE A O   1 
ATOM   1620 C CB  . PHE A 1 246 ? -19.90510 -8.29850  7.17549  1.000 21.06879 ? 246 PHE A CB  1 
ATOM   1621 C CG  . PHE A 1 246 ? -20.80870 -7.34686  7.92069  1.000 25.62918 ? 246 PHE A CG  1 
ATOM   1622 C CD1 . PHE A 1 246 ? -22.11512 -7.13260  7.49961  1.000 33.26149 ? 246 PHE A CD1 1 
ATOM   1623 C CD2 . PHE A 1 246 ? -20.35673 -6.68162  9.04932  1.000 17.72549 ? 246 PHE A CD2 1 
ATOM   1624 C CE1 . PHE A 1 246 ? -22.94889 -6.26496  8.18878  1.000 30.89422 ? 246 PHE A CE1 1 
ATOM   1625 C CE2 . PHE A 1 246 ? -21.18641 -5.81083  9.74245  1.000 22.57112 ? 246 PHE A CE2 1 
ATOM   1626 C CZ  . PHE A 1 246 ? -22.47996 -5.60503  9.31342  1.000 23.41684 ? 246 PHE A CZ  1 
ATOM   1627 N N   . ASN A 1 247 ? -19.71046 -10.76408 5.43468  1.000 28.16015 ? 247 ASN A N   1 
ATOM   1628 C CA  . ASN A 1 247 ? -19.03655 -11.58185 4.42772  1.000 28.05783 ? 247 ASN A CA  1 
ATOM   1629 C C   . ASN A 1 247 ? -18.35002 -10.73568 3.37035  1.000 29.59485 ? 247 ASN A C   1 
ATOM   1630 O O   . ASN A 1 247 ? -17.84537 -11.26702 2.38261  1.000 26.62353 ? 247 ASN A O   1 
ATOM   1631 C CB  . ASN A 1 247 ? -20.02680 -12.53227 3.76465  1.000 31.78386 ? 247 ASN A CB  1 
ATOM   1632 C CG  . ASN A 1 247 ? -20.75602 -13.39350 4.77155  1.000 43.58346 ? 247 ASN A CG  1 
ATOM   1633 O OD1 . ASN A 1 247 ? -20.13754 -14.01277 5.63567  1.000 43.71992 ? 247 ASN A OD1 1 
ATOM   1634 N ND2 . ASN A 1 247 ? -22.08204 -13.41453 4.68447  1.000 56.89677 ? 247 ASN A ND2 1 
ATOM   1635 N N   . GLN A 1 248 ? -18.31500 -9.42356  3.60299  1.000 22.63028 ? 248 GLN A N   1 
ATOM   1636 C CA  . GLN A 1 248 ? -17.69944 -8.47080  2.68021  1.000 26.53785 ? 248 GLN A CA  1 
ATOM   1637 C C   . GLN A 1 248 ? -17.42556 -7.14464  3.39008  1.000 28.98107 ? 248 GLN A C   1 
ATOM   1638 O O   . GLN A 1 248 ? -17.96106 -6.91239  4.47178  1.000 25.51521 ? 248 GLN A O   1 
ATOM   1639 C CB  . GLN A 1 248 ? -18.61049 -8.23548  1.48052  1.000 31.32502 ? 248 GLN A CB  1 
ATOM   1640 C CG  . GLN A 1 248 ? -19.96025 -7.64997  1.86198  1.000 36.74943 ? 248 GLN A CG  1 
ATOM   1641 C CD  . GLN A 1 248 ? -20.80982 -7.34093  0.65045  1.000 57.85800 ? 248 GLN A CD  1 
ATOM   1642 O OE1 . GLN A 1 248 ? -21.77587 -8.04741  0.35944  1.000 68.37786 ? 248 GLN A OE1 1 
ATOM   1643 N NE2 . GLN A 1 248 ? -20.45051 -6.28305  -0.07025 1.000 62.23045 ? 248 GLN A NE2 1 
ATOM   1644 N N   . PRO A 1 249 ? -16.58935 -6.26794  2.79099  1.000 26.60593 ? 249 PRO A N   1 
ATOM   1645 C CA  . PRO A 1 249 ? -16.44596 -4.91995  3.35890  1.000 27.11549 ? 249 PRO A CA  1 
ATOM   1646 C C   . PRO A 1 249 ? -17.78645 -4.19634  3.38809  1.000 24.42600 ? 249 PRO A C   1 
ATOM   1647 O O   . PRO A 1 249 ? -18.59731 -4.39677  2.48145  1.000 23.88237 ? 249 PRO A O   1 
ATOM   1648 C CB  . PRO A 1 249 ? -15.46918 -4.22931  2.39940  1.000 24.38459 ? 249 PRO A CB  1 
ATOM   1649 C CG  . PRO A 1 249 ? -14.69395 -5.35623  1.78219  1.000 20.70783 ? 249 PRO A CG  1 
ATOM   1650 C CD  . PRO A 1 249 ? -15.66905 -6.48996  1.65943  1.000 25.91438 ? 249 PRO A CD  1 
ATOM   1651 N N   . VAL A 1 250 ? -18.02701 -3.39570  4.42361  1.000 18.19229 ? 250 VAL A N   1 
ATOM   1652 C CA  . VAL A 1 250 ? -19.27387 -2.63748  4.53470  1.000 16.87166 ? 250 VAL A CA  1 
ATOM   1653 C C   . VAL A 1 250 ? -19.01450 -1.20933  5.01916  1.000 24.80491 ? 250 VAL A C   1 
ATOM   1654 O O   . VAL A 1 250 ? -17.91767 -0.88506  5.49529  1.000 22.19821 ? 250 VAL A O   1 
ATOM   1655 C CB  . VAL A 1 250 ? -20.29116 -3.31985  5.50129  1.000 29.34207 ? 250 VAL A CB  1 
ATOM   1656 C CG1 . VAL A 1 250 ? -20.69610 -4.69628  4.98397  1.000 30.82241 ? 250 VAL A CG1 1 
ATOM   1657 C CG2 . VAL A 1 250 ? -19.71940 -3.43430  6.90510  1.000 15.51548 ? 250 VAL A CG2 1 
ATOM   1658 N N   . THR A 1 251 ? -20.02218 -0.35356  4.88674  1.000 20.73906 ? 251 THR A N   1 
ATOM   1659 C CA  . THR A 1 251 ? -19.92890 1.00378   5.41452  1.000 21.18825 ? 251 THR A CA  1 
ATOM   1660 C C   . THR A 1 251 ? -19.98026 0.99289   6.94006  1.000 22.96902 ? 251 THR A C   1 
ATOM   1661 O O   . THR A 1 251 ? -20.38121 -0.00305  7.56076  1.000 18.86859 ? 251 THR A O   1 
ATOM   1662 C CB  . THR A 1 251 ? -21.06550 1.89945   4.90807  1.000 24.76662 ? 251 THR A CB  1 
ATOM   1663 O OG1 . THR A 1 251 ? -22.30709 1.39873   5.41036  1.000 22.47749 ? 251 THR A OG1 1 
ATOM   1664 C CG2 . THR A 1 251 ? -21.10180 1.91586   3.37824  1.000 28.26544 ? 251 THR A CG2 1 
ATOM   1665 N N   . ILE A 1 252 ? -19.59788 2.11756   7.53306  1.000 20.24819 ? 252 ILE A N   1 
ATOM   1666 C CA  . ILE A 1 252 ? -19.66400 2.28198   8.97768  1.000 19.00037 ? 252 ILE A CA  1 
ATOM   1667 C C   . ILE A 1 252 ? -21.11205 2.15960   9.46166  1.000 22.57448 ? 252 ILE A C   1 
ATOM   1668 O O   . ILE A 1 252 ? -21.39796 1.47938   10.45512 1.000 22.75621 ? 252 ILE A O   1 
ATOM   1669 C CB  . ILE A 1 252 ? -19.06343 3.63182   9.39035  1.000 24.68430 ? 252 ILE A CB  1 
ATOM   1670 C CG1 . ILE A 1 252 ? -17.56725 3.64607   9.04908  1.000 25.21255 ? 252 ILE A CG1 1 
ATOM   1671 C CG2 . ILE A 1 252 ? -19.31343 3.91211   10.87332 1.000 15.75375 ? 252 ILE A CG2 1 
ATOM   1672 C CD1 . ILE A 1 252 ? -16.87519 4.99967   9.25933  1.000 22.60894 ? 252 ILE A CD1 1 
ATOM   1673 N N   . THR A 1 253 ? -22.03184 2.79429   8.73870  1.000 20.23977 ? 253 THR A N   1 
ATOM   1674 C CA  . THR A 1 253 ? -23.44557 2.73100   9.10069  1.000 22.65977 ? 253 THR A CA  1 
ATOM   1675 C C   . THR A 1 253 ? -23.95909 1.28238   9.14409  1.000 19.85196 ? 253 THR A C   1 
ATOM   1676 O O   . THR A 1 253 ? -24.60081 0.86638   10.12587 1.000 23.21219 ? 253 THR A O   1 
ATOM   1677 C CB  . THR A 1 253 ? -24.28348 3.58388   8.13075  1.000 27.47697 ? 253 THR A CB  1 
ATOM   1678 O OG1 . THR A 1 253 ? -23.97467 4.96431   8.35597  1.000 31.17443 ? 253 THR A OG1 1 
ATOM   1679 C CG2 . THR A 1 253 ? -25.76161 3.37248   8.36414  1.000 26.70821 ? 253 THR A CG2 1 
ATOM   1680 N N   . THR A 1 254 ? -23.64198 0.50568   8.10786  1.000 19.01000 ? 254 THR A N   1 
ATOM   1681 C CA  . THR A 1 254 ? -24.04514 -0.89816  8.05442  1.000 19.28056 ? 254 THR A CA  1 
ATOM   1682 C C   . THR A 1 254 ? -23.45413 -1.69133  9.22872  1.000 23.78581 ? 254 THR A C   1 
ATOM   1683 O O   . THR A 1 254 ? -24.13469 -2.52094  9.84137  1.000 22.45822 ? 254 THR A O   1 
ATOM   1684 C CB  . THR A 1 254 ? -23.61392 -1.57427  6.71696  1.000 23.20170 ? 254 THR A CB  1 
ATOM   1685 O OG1 . THR A 1 254 ? -24.26826 -0.93815  5.61122  1.000 26.61181 ? 254 THR A OG1 1 
ATOM   1686 C CG2 . THR A 1 254 ? -23.95644 -3.06823  6.71927  1.000 26.83339 ? 254 THR A CG2 1 
ATOM   1687 N N   . TRP A 1 255 ? -22.18169 -1.44056  9.52682  1.000 25.18186 ? 255 TRP A N   1 
ATOM   1688 C CA  . TRP A 1 255 ? -21.50557 -2.08656  10.64727 1.000 24.24964 ? 255 TRP A CA  1 
ATOM   1689 C C   . TRP A 1 255 ? -22.16863 -1.73079  11.98258 1.000 20.65702 ? 255 TRP A C   1 
ATOM   1690 O O   . TRP A 1 255 ? -22.46181 -2.61418  12.79092 1.000 22.05564 ? 255 TRP A O   1 
ATOM   1691 C CB  . TRP A 1 255 ? -20.03006 -1.68433  10.65289 1.000 18.16168 ? 255 TRP A CB  1 
ATOM   1692 C CG  . TRP A 1 255 ? -19.13065 -2.37688  11.66478 1.000 17.44007 ? 255 TRP A CG  1 
ATOM   1693 C CD1 . TRP A 1 255 ? -18.74929 -3.69872  11.67758 1.000 13.80009 ? 255 TRP A CD1 1 
ATOM   1694 C CD2 . TRP A 1 255 ? -18.45266 -1.75418  12.77001 1.000 15.94803 ? 255 TRP A CD2 1 
ATOM   1695 N NE1 . TRP A 1 255 ? -17.89695 -3.93287  12.73365 1.000 15.46022 ? 255 TRP A NE1 1 
ATOM   1696 C CE2 . TRP A 1 255 ? -17.69079 -2.75507  13.41085 1.000 12.96389 ? 255 TRP A CE2 1 
ATOM   1697 C CE3 . TRP A 1 255 ? -18.42015 -0.45173  13.27562 1.000 17.64039 ? 255 TRP A CE3 1 
ATOM   1698 C CZ2 . TRP A 1 255 ? -16.91631 -2.49462  14.53788 1.000 15.84422 ? 255 TRP A CZ2 1 
ATOM   1699 C CZ3 . TRP A 1 255 ? -17.63970 -0.19256  14.40428 1.000 16.13833 ? 255 TRP A CZ3 1 
ATOM   1700 C CH2 . TRP A 1 255 ? -16.90342 -1.21155  15.02126 1.000 16.76687 ? 255 TRP A CH2 1 
ATOM   1701 N N   . LEU A 1 256 ? -22.40023 -0.44050  12.21292 1.000 16.80413 ? 256 LEU A N   1 
ATOM   1702 C CA  . LEU A 1 256 ? -23.04274 0.00673   13.44952 1.000 21.29441 ? 256 LEU A CA  1 
ATOM   1703 C C   . LEU A 1 256 ? -24.46220 -0.54583  13.59635 1.000 20.99410 ? 256 LEU A C   1 
ATOM   1704 O O   . LEU A 1 256 ? -24.85430 -0.96559  14.68973 1.000 22.61593 ? 256 LEU A O   1 
ATOM   1705 C CB  . LEU A 1 256 ? -23.07657 1.53755   13.52221 1.000 17.47757 ? 256 LEU A CB  1 
ATOM   1706 C CG  . LEU A 1 256 ? -21.73413 2.24747   13.67984 1.000 19.36286 ? 256 LEU A CG  1 
ATOM   1707 C CD1 . LEU A 1 256 ? -21.96064 3.75028   13.81675 1.000 21.44425 ? 256 LEU A CD1 1 
ATOM   1708 C CD2 . LEU A 1 256 ? -20.95928 1.68812   14.87590 1.000 17.74958 ? 256 LEU A CD2 1 
ATOM   1709 N N   . ASN A 1 257 ? -25.22820 -0.54582  12.50438 1.000 23.14582 ? 257 ASN A N   1 
ATOM   1710 C CA  . ASN A 1 257 ? -26.60980 -1.03306  12.53626 1.000 25.19172 ? 257 ASN A CA  1 
ATOM   1711 C C   . ASN A 1 257 ? -26.69086 -2.50309  12.92596 1.000 24.08297 ? 257 ASN A C   1 
ATOM   1712 O O   . ASN A 1 257 ? -27.68430 -2.93950  13.48771 1.000 23.49344 ? 257 ASN A O   1 
ATOM   1713 C CB  . ASN A 1 257 ? -27.30512 -0.83421  11.17691 1.000 27.92720 ? 257 ASN A CB  1 
ATOM   1714 C CG  . ASN A 1 257 ? -27.70511 0.60709   10.92510 1.000 36.60887 ? 257 ASN A CG  1 
ATOM   1715 O OD1 . ASN A 1 257 ? -27.83187 1.40984   11.85600 1.000 32.96172 ? 257 ASN A OD1 1 
ATOM   1716 N ND2 . ASN A 1 257 ? -27.92042 0.94020   9.65691  1.000 38.31351 ? 257 ASN A ND2 1 
ATOM   1717 N N   . LYS A 1 258 ? -25.64293 -3.26375  12.62962 1.000 17.97427 ? 258 LYS A N   1 
ATOM   1718 C CA  . LYS A 1 258 ? -25.62762 -4.68525  12.96463 1.000 22.47672 ? 258 LYS A CA  1 
ATOM   1719 C C   . LYS A 1 258 ? -25.62321 -4.89515  14.48054 1.000 24.30342 ? 258 LYS A C   1 
ATOM   1720 O O   . LYS A 1 258 ? -26.04389 -5.94422  14.98889 1.000 22.86767 ? 258 LYS A O   1 
ATOM   1721 C CB  . LYS A 1 258 ? -24.40592 -5.36794  12.34023 1.000 20.82422 ? 258 LYS A CB  1 
ATOM   1722 C CG  . LYS A 1 258 ? -24.41739 -6.89474  12.41097 1.000 25.28740 ? 258 LYS A CG  1 
ATOM   1723 C CD  . LYS A 1 258 ? -25.34531 -7.49127  11.35706 1.000 27.36152 ? 258 LYS A CD  1 
ATOM   1724 C CE  . LYS A 1 258 ? -25.05000 -8.96295  11.10129 1.000 40.22240 ? 258 LYS A CE  1 
ATOM   1725 N NZ  . LYS A 1 258 ? -25.41001 -9.82481  12.25622 1.000 47.26746 ? 258 LYS A NZ  1 
ATOM   1726 N N   . MET A 1 259 ? -25.14832 -3.88673  15.20085 1.000 18.86006 ? 259 MET A N   1 
ATOM   1727 C CA  . MET A 1 259 ? -24.91720 -4.02270  16.63299 1.000 21.27673 ? 259 MET A CA  1 
ATOM   1728 C C   . MET A 1 259 ? -26.05467 -3.44121  17.45636 1.000 20.96739 ? 259 MET A C   1 
ATOM   1729 O O   . MET A 1 259 ? -25.89923 -3.17827  18.65410 1.000 21.64280 ? 259 MET A O   1 
ATOM   1730 C CB  . MET A 1 259 ? -23.58372 -3.37656  17.00342 1.000 13.41836 ? 259 MET A CB  1 
ATOM   1731 C CG  . MET A 1 259 ? -22.41684 -4.18097  16.46035 1.000 15.83421 ? 259 MET A CG  1 
ATOM   1732 S SD  . MET A 1 259 ? -20.77766 -3.55767  16.88233 1.000 22.89541 ? 259 MET A SD  1 
ATOM   1733 C CE  . MET A 1 259 ? -20.76127 -1.99640  16.00686 1.000 25.43512 ? 259 MET A CE  1 
ATOM   1734 N N   . LYS A 1 260 ? -27.20752 -3.27882  16.80969 1.000 20.55546 ? 260 LYS A N   1 
ATOM   1735 C CA  . LYS A 1 260 ? -28.40802 -2.79727  17.47750 1.000 18.08873 ? 260 LYS A CA  1 
ATOM   1736 C C   . LYS A 1 260 ? -29.49281 -3.85106  17.51165 1.000 26.02210 ? 260 LYS A C   1 
ATOM   1737 O O   . LYS A 1 260 ? -30.67781 -3.53492  17.46762 1.000 29.69378 ? 260 LYS A O   1 
ATOM   1738 C CB  . LYS A 1 260 ? -28.92506 -1.54610  16.78332 1.000 22.09748 ? 260 LYS A CB  1 
ATOM   1739 C CG  . LYS A 1 260 ? -27.87047 -0.46559  16.65438 1.000 24.79699 ? 260 LYS A CG  1 
ATOM   1740 C CD  . LYS A 1 260 ? -28.33365 0.66372   15.75521 1.000 30.03533 ? 260 LYS A CD  1 
ATOM   1741 C CE  . LYS A 1 260 ? -27.23635 1.71029   15.60827 1.000 42.27879 ? 260 LYS A CE  1 
ATOM   1742 N NZ  . LYS A 1 260 ? -27.71691 2.91621   14.87175 1.000 46.03657 ? 260 LYS A NZ  1 
ATOM   1743 N N   . TYR A 1 261 ? -29.09064 -5.10928  17.59771 1.000 22.26909 ? 261 TYR A N   1 
ATOM   1744 C CA  . TYR A 1 261 ? -30.05308 -6.20036  17.61183 1.000 23.65008 ? 261 TYR A CA  1 
ATOM   1745 C C   . TYR A 1 261 ? -30.82879 -6.20446  18.93254 1.000 28.31023 ? 261 TYR A C   1 
ATOM   1746 O O   . TYR A 1 261 ? -30.26061 -5.91685  19.98775 1.000 25.88196 ? 261 TYR A O   1 
ATOM   1747 C CB  . TYR A 1 261 ? -29.34572 -7.54446  17.38812 1.000 22.56653 ? 261 TYR A CB  1 
ATOM   1748 C CG  . TYR A 1 261 ? -30.27827 -8.73734  17.48982 1.000 24.79006 ? 261 TYR A CG  1 
ATOM   1749 C CD1 . TYR A 1 261 ? -31.20737 -9.00239  16.49179 1.000 29.05278 ? 261 TYR A CD1 1 
ATOM   1750 C CD2 . TYR A 1 261 ? -30.23257 -9.59082  18.58923 1.000 31.68643 ? 261 TYR A CD2 1 
ATOM   1751 C CE1 . TYR A 1 261 ? -32.06901 -10.09025 16.58302 1.000 36.92382 ? 261 TYR A CE1 1 
ATOM   1752 C CE2 . TYR A 1 261 ? -31.08932 -10.67747 18.69006 1.000 39.54961 ? 261 TYR A CE2 1 
ATOM   1753 C CZ  . TYR A 1 261 ? -32.00438 -10.92105 17.68534 1.000 41.53469 ? 261 TYR A CZ  1 
ATOM   1754 O OH  . TYR A 1 261 ? -32.85956 -11.99876 17.78276 1.000 45.49391 ? 261 TYR A OH  1 
ATOM   1755 N N   . ASN A 1 262 ? -32.12775 -6.49606  18.86985 1.000 27.28843 ? 262 ASN A N   1 
ATOM   1756 C CA  . ASN A 1 262 ? -32.91444 -6.68107  20.08897 1.000 26.45231 ? 262 ASN A CA  1 
ATOM   1757 C C   . ASN A 1 262 ? -32.79610 -5.48337  21.03708 1.000 26.04015 ? 262 ASN A C   1 
ATOM   1758 O O   . ASN A 1 262 ? -32.54157 -5.64178  22.23325 1.000 31.53232 ? 262 ASN A O   1 
ATOM   1759 C CB  . ASN A 1 262 ? -32.46671 -7.96626  20.80368 1.000 32.87251 ? 262 ASN A CB  1 
ATOM   1760 C CG  . ASN A 1 262 ? -33.43411 -8.40869  21.88306 1.000 48.04783 ? 262 ASN A CG  1 
ATOM   1761 O OD1 . ASN A 1 262 ? -34.64733 -8.29732  21.72247 1.000 55.36285 ? 262 ASN A OD1 1 
ATOM   1762 N ND2 . ASN A 1 262 ? -32.90027 -8.90559  22.99452 1.000 49.39717 ? 262 ASN A ND2 1 
ATOM   1763 N N   . GLY A 1 263 ? -32.91861 -4.28220  20.48887 1.000 25.51762 ? 263 GLY A N   1 
ATOM   1764 C CA  . GLY A 1 263 ? -32.86722 -3.08135  21.30061 1.000 29.51160 ? 263 GLY A CA  1 
ATOM   1765 C C   . GLY A 1 263 ? -31.47066 -2.64675  21.69914 1.000 28.88125 ? 263 GLY A C   1 
ATOM   1766 O O   . GLY A 1 263 ? -31.30307 -1.83954  22.61768 1.000 26.01804 ? 263 GLY A O   1 
ATOM   1767 N N   . GLY A 1 264 ? -30.45982 -3.18040  21.01925 1.000 24.79032 ? 264 GLY A N   1 
ATOM   1768 C CA  . GLY A 1 264 ? -29.09142 -2.75954  21.27380 1.000 24.95826 ? 264 GLY A CA  1 
ATOM   1769 C C   . GLY A 1 264 ? -28.89372 -1.31830  20.84085 1.000 24.71226 ? 264 GLY A C   1 
ATOM   1770 O O   . GLY A 1 264 ? -29.58376 -0.84493  19.93861 1.000 21.72259 ? 264 GLY A O   1 
ATOM   1771 N N   . THR A 1 265 ? -27.97140 -0.60732  21.48216 1.000 21.82344 ? 265 THR A N   1 
ATOM   1772 C CA  . THR A 1 265 ? -27.70730 0.78083   21.10536 1.000 26.55622 ? 265 THR A CA  1 
ATOM   1773 C C   . THR A 1 265 ? -26.21224 1.11370   21.06634 1.000 24.13883 ? 265 THR A C   1 
ATOM   1774 O O   . THR A 1 265 ? -25.41415 0.56094   21.83572 1.000 19.36823 ? 265 THR A O   1 
ATOM   1775 C CB  . THR A 1 265 ? -28.40565 1.77090   22.07356 1.000 26.54931 ? 265 THR A CB  1 
ATOM   1776 O OG1 . THR A 1 265 ? -28.04498 1.44829   23.42337 1.000 30.77791 ? 265 THR A OG1 1 
ATOM   1777 C CG2 . THR A 1 265 ? -29.92264 1.70091   21.92423 1.000 25.23824 ? 265 THR A CG2 1 
ATOM   1778 N N   . VAL A 1 266 ? -25.84655 2.01037   20.15296 1.000 19.31844 ? 266 VAL A N   1 
ATOM   1779 C CA  . VAL A 1 266 ? -24.49211 2.56366   20.08476 1.000 16.70820 ? 266 VAL A CA  1 
ATOM   1780 C C   . VAL A 1 266 ? -24.44037 3.93445   20.76175 1.000 21.15035 ? 266 VAL A C   1 
ATOM   1781 O O   . VAL A 1 266 ? -25.11467 4.86882   20.33181 1.000 22.02259 ? 266 VAL A O   1 
ATOM   1782 C CB  . VAL A 1 266 ? -24.01602 2.70621   18.62913 1.000 15.98978 ? 266 VAL A CB  1 
ATOM   1783 C CG1 . VAL A 1 266 ? -22.57740 3.24652   18.58065 1.000 13.29591 ? 266 VAL A CG1 1 
ATOM   1784 C CG2 . VAL A 1 266 ? -24.11874 1.37558   17.92303 1.000 16.62327 ? 266 VAL A CG2 1 
ATOM   1785 N N   . ALA A 1 267 ? -23.65281 4.07087   21.82157 1.000 21.67508 ? 267 ALA A N   1 
ATOM   1786 C CA  . ALA A 1 267 ? -23.57570 5.36078   22.49570 1.000 22.79150 ? 267 ALA A CA  1 
ATOM   1787 C C   . ALA A 1 267 ? -22.65890 6.32496   21.72919 1.000 23.22194 ? 267 ALA A C   1 
ATOM   1788 O O   . ALA A 1 267 ? -22.95848 7.52409   21.59863 1.000 22.23678 ? 267 ALA A O   1 
ATOM   1789 C CB  . ALA A 1 267 ? -23.09966 5.18455   23.92927 1.000 17.89781 ? 267 ALA A CB  1 
ATOM   1790 N N   . THR A 1 268 ? -21.55399 5.79522   21.21258 1.000 20.81665 ? 268 THR A N   1 
ATOM   1791 C CA  . THR A 1 268 ? -20.56674 6.60050   20.48822 1.000 18.33270 ? 268 THR A CA  1 
ATOM   1792 C C   . THR A 1 268 ? -19.57254 5.71873   19.73169 1.000 21.22763 ? 268 THR A C   1 
ATOM   1793 O O   . THR A 1 268 ? -19.56978 4.48534   19.86185 1.000 18.58156 ? 268 THR A O   1 
ATOM   1794 C CB  . THR A 1 268 ? -19.77944 7.54937   21.43959 1.000 22.91246 ? 268 THR A CB  1 
ATOM   1795 O OG1 . THR A 1 268 ? -19.19176 8.62224   20.68314 1.000 18.85082 ? 268 THR A OG1 1 
ATOM   1796 C CG2 . THR A 1 268 ? -18.68736 6.78926   22.19302 1.000 21.15998 ? 268 THR A CG2 1 
ATOM   1797 N N   . THR A 1 269 ? -18.75098 6.35473   18.90625 1.000 16.48458 ? 269 THR A N   1 
ATOM   1798 C CA  . THR A 1 269 ? -17.65518 5.65077   18.25763 1.000 15.59579 ? 269 THR A CA  1 
ATOM   1799 C C   . THR A 1 269 ? -16.39366 6.46497   18.40840 1.000 14.68921 ? 269 THR A C   1 
ATOM   1800 O O   . THR A 1 269 ? -16.45025 7.66571   18.68727 1.000 14.06180 ? 269 THR A O   1 
ATOM   1801 C CB  . THR A 1 269 ? -17.90549 5.39549   16.76541 1.000 19.68427 ? 269 THR A CB  1 
ATOM   1802 O OG1 . THR A 1 269 ? -18.03745 6.64658   16.07860 1.000 21.06938 ? 269 THR A OG1 1 
ATOM   1803 C CG2 . THR A 1 269 ? -19.15628 4.53456   16.56554 1.000 16.76911 ? 269 THR A CG2 1 
ATOM   1804 N N   . SER A 1 270 ? -15.25746 5.80560   18.22821 1.000 14.27459 ? 270 SER A N   1 
ATOM   1805 C CA  . SER A 1 270 ? -13.97456 6.48013   18.24790 1.000 18.20686 ? 270 SER A CA  1 
ATOM   1806 C C   . SER A 1 270 ? -13.09091 5.93665   17.11550 1.000 15.98305 ? 270 SER A C   1 
ATOM   1807 O O   . SER A 1 270 ? -13.10910 4.73462   16.82393 1.000 15.73246 ? 270 SER A O   1 
ATOM   1808 C CB  . SER A 1 270 ? -13.31578 6.30199   19.62395 1.000 14.63333 ? 270 SER A CB  1 
ATOM   1809 O OG  . SER A 1 270 ? -11.99125 6.79638   19.61916 1.000 33.37406 ? 270 SER A OG  1 
ATOM   1810 N N   . TYR A 1 271 ? -12.35948 6.83288   16.45415 1.000 14.31065 ? 271 TYR A N   1 
ATOM   1811 C CA  . TYR A 1 271 ? -11.36179 6.44075   15.44347 1.000 14.49859 ? 271 TYR A CA  1 
ATOM   1812 C C   . TYR A 1 271 ? -9.95391  6.54379   16.01224 1.000 14.36613 ? 271 TYR A C   1 
ATOM   1813 O O   . TYR A 1 271 ? -9.63615  7.51987   16.68925 1.000 19.39494 ? 271 TYR A O   1 
ATOM   1814 C CB  . TYR A 1 271 ? -11.45426 7.31837   14.20033 1.000 12.55199 ? 271 TYR A CB  1 
ATOM   1815 C CG  . TYR A 1 271 ? -12.84959 7.48006   13.64570 1.000 16.92562 ? 271 TYR A CG  1 
ATOM   1816 C CD1 . TYR A 1 271 ? -13.50729 6.41420   13.04685 1.000 17.82585 ? 271 TYR A CD1 1 
ATOM   1817 C CD2 . TYR A 1 271 ? -13.49413 8.71199   13.69105 1.000 25.02457 ? 271 TYR A CD2 1 
ATOM   1818 C CE1 . TYR A 1 271 ? -14.78693 6.56428   12.52645 1.000 24.41085 ? 271 TYR A CE1 1 
ATOM   1819 C CE2 . TYR A 1 271 ? -14.76452 8.87662   13.17401 1.000 31.02749 ? 271 TYR A CE2 1 
ATOM   1820 C CZ  . TYR A 1 271 ? -15.40911 7.80240   12.59338 1.000 37.18468 ? 271 TYR A CZ  1 
ATOM   1821 O OH  . TYR A 1 271 ? -16.67842 7.97295   12.07875 1.000 40.85983 ? 271 TYR A OH  1 
ATOM   1822 N N   . GLN A 1 272 ? -9.11142  5.55978   15.71301 1.000 13.33726 ? 272 GLN A N   1 
ATOM   1823 C CA  . GLN A 1 272 ? -7.75755  5.50037   16.27919 1.000 11.07790 ? 272 GLN A CA  1 
ATOM   1824 C C   . GLN A 1 272 ? -6.72556  5.03621   15.26451 1.000 11.29113 ? 272 GLN A C   1 
ATOM   1825 O O   . GLN A 1 272 ? -7.07211  4.37854   14.27602 1.000 11.02438 ? 272 GLN A O   1 
ATOM   1826 C CB  . GLN A 1 272 ? -7.72935  4.55546   17.49573 1.000 17.39752 ? 272 GLN A CB  1 
ATOM   1827 C CG  . GLN A 1 272 ? -8.04979  5.24059   18.83074 1.000 22.41334 ? 272 GLN A CG  1 
ATOM   1828 C CD  . GLN A 1 272 ? -6.89016  6.08625   19.34503 1.000 19.99659 ? 272 GLN A CD  1 
ATOM   1829 O OE1 . GLN A 1 272 ? -5.95430  6.42258   18.60279 1.000 27.67273 ? 272 GLN A OE1 1 
ATOM   1830 N NE2 . GLN A 1 272 ? -6.93655  6.42128   20.62569 1.000 26.89259 ? 272 GLN A NE2 1 
ATOM   1831 N N   . ASN A 1 273 ? -5.46251  5.39003   15.50262 1.000 10.87272 ? 273 ASN A N   1 
ATOM   1832 C CA  . ASN A 1 273 ? -4.34311  4.82609   14.76035 1.000 14.83005 ? 273 ASN A CA  1 
ATOM   1833 C C   . ASN A 1 273 ? -4.41657  3.30211   14.85137 1.000 15.64560 ? 273 ASN A C   1 
ATOM   1834 O O   . ASN A 1 273 ? -4.89955  2.77399   15.86001 1.000 14.46631 ? 273 ASN A O   1 
ATOM   1835 C CB  . ASN A 1 273 ? -3.00589  5.33607   15.32573 1.000 16.63457 ? 273 ASN A CB  1 
ATOM   1836 C CG  . ASN A 1 273 ? -2.78098  6.81924   15.06723 1.000 22.60373 ? 273 ASN A CG  1 
ATOM   1837 O OD1 . ASN A 1 273 ? -2.80224  7.26636   13.92286 1.000 21.43019 ? 273 ASN A OD1 1 
ATOM   1838 N ND2 . ASN A 1 273 ? -2.57276  7.59469   16.14219 1.000 22.45622 ? 273 ASN A ND2 1 
ATOM   1839 N N   . SER A 1 274 ? -3.93684  2.59248   13.82758 1.000 14.37731 ? 274 SER A N   1 
ATOM   1840 C CA  . SER A 1 274 ? -4.01700  1.12739   13.83270 1.000 15.41183 ? 274 SER A CA  1 
ATOM   1841 C C   . SER A 1 274 ? -3.14606  0.52638   14.93821 1.000 15.25355 ? 274 SER A C   1 
ATOM   1842 O O   . SER A 1 274 ? -3.41552  -0.58697  15.40133 1.000 13.59542 ? 274 SER A O   1 
ATOM   1843 C CB  . SER A 1 274 ? -3.62479  0.54304   12.46649 1.000 16.09657 ? 274 SER A CB  1 
ATOM   1844 O OG  . SER A 1 274 ? -2.24293  0.72853   12.21159 1.000 17.65474 ? 274 SER A OG  1 
ATOM   1845 N N   . SER A 1 275 ? -2.13068  1.27200   15.38013 1.000 8.15271  ? 275 SER A N   1 
ATOM   1846 C CA  . SER A 1 275 ? -1.24349  0.80573   16.44792 1.000 10.48519 ? 275 SER A CA  1 
ATOM   1847 C C   . SER A 1 275 ? -1.99420  0.64678   17.77273 1.000 13.65192 ? 275 SER A C   1 
ATOM   1848 O O   . SER A 1 275 ? -1.56641  -0.10322  18.66331 1.000 15.11919 ? 275 SER A O   1 
ATOM   1849 C CB  . SER A 1 275 ? -0.07639  1.77505   16.64344 1.000 15.18865 ? 275 SER A CB  1 
ATOM   1850 O OG  . SER A 1 275 ? -0.57920  3.06430   16.98484 1.000 21.05744 ? 275 SER A OG  1 
ATOM   1851 N N   . VAL A 1 276 ? -3.10182  1.36806   17.91051 1.000 14.41364 ? 276 VAL A N   1 
ATOM   1852 C CA  . VAL A 1 276 ? -3.90057  1.26826   19.12569 1.000 14.42863 ? 276 VAL A CA  1 
ATOM   1853 C C   . VAL A 1 276 ? -4.63496  -0.07493  19.18594 1.000 14.61252 ? 276 VAL A C   1 
ATOM   1854 O O   . VAL A 1 276 ? -5.42241  -0.42100  18.30311 1.000 15.46196 ? 276 VAL A O   1 
ATOM   1855 C CB  . VAL A 1 276 ? -4.91411  2.42014   19.23179 1.000 13.32507 ? 276 VAL A CB  1 
ATOM   1856 C CG1 . VAL A 1 276 ? -5.89261  2.15052   20.36935 1.000 9.17960  ? 276 VAL A CG1 1 
ATOM   1857 C CG2 . VAL A 1 276 ? -4.17967  3.76232   19.39752 1.000 12.67653 ? 276 VAL A CG2 1 
ATOM   1858 N N   . TYR A 1 277 ? -4.36057  -0.81942  20.24916 1.000 9.53882  ? 277 TYR A N   1 
ATOM   1859 C CA  . TYR A 1 277 ? -4.91625  -2.15337  20.45809 1.000 8.97913  ? 277 TYR A CA  1 
ATOM   1860 C C   . TYR A 1 277 ? -6.28385  -2.05214  21.10530 1.000 12.00830 ? 277 TYR A C   1 
ATOM   1861 O O   . TYR A 1 277 ? -7.24197  -2.70282  20.66758 1.000 9.95345  ? 277 TYR A O   1 
ATOM   1862 C CB  . TYR A 1 277 ? -3.95119  -2.94975  21.32139 1.000 8.08507  ? 277 TYR A CB  1 
ATOM   1863 C CG  . TYR A 1 277 ? -4.18264  -4.42865  21.46587 1.000 8.25545  ? 277 TYR A CG  1 
ATOM   1864 C CD1 . TYR A 1 277 ? -4.27190  -5.27233  20.35427 1.000 11.30976 ? 277 TYR A CD1 1 
ATOM   1865 C CD2 . TYR A 1 277 ? -4.22696  -4.99698  22.73303 1.000 6.01618  ? 277 TYR A CD2 1 
ATOM   1866 C CE1 . TYR A 1 277 ? -4.43356  -6.63834  20.51912 1.000 10.13127 ? 277 TYR A CE1 1 
ATOM   1867 C CE2 . TYR A 1 277 ? -4.38680  -6.33022  22.90249 1.000 8.58660  ? 277 TYR A CE2 1 
ATOM   1868 C CZ  . TYR A 1 277 ? -4.48815  -7.14521  21.80254 1.000 14.37981 ? 277 TYR A CZ  1 
ATOM   1869 O OH  . TYR A 1 277 ? -4.64790  -8.47465  22.01945 1.000 13.92520 ? 277 TYR A OH  1 
ATOM   1870 N N   . TYR A 1 278 ? -6.37568  -1.22624  22.14555 1.000 10.69818 ? 278 TYR A N   1 
ATOM   1871 C CA  . TYR A 1 278 ? -7.65931  -0.94721  22.77497 1.000 9.86149  ? 278 TYR A CA  1 
ATOM   1872 C C   . TYR A 1 278 ? -7.72147  0.49602   23.24772 1.000 9.97988  ? 278 TYR A C   1 
ATOM   1873 O O   . TYR A 1 278 ? -6.72978  1.05930   23.69778 1.000 12.41653 ? 278 TYR A O   1 
ATOM   1874 C CB  . TYR A 1 278 ? -7.92896  -1.92655  23.94380 1.000 9.65253  ? 278 TYR A CB  1 
ATOM   1875 C CG  . TYR A 1 278 ? -9.09579  -1.48004  24.80116 1.000 12.61265 ? 278 TYR A CG  1 
ATOM   1876 C CD1 . TYR A 1 278 ? -10.41585 -1.72138  24.40562 1.000 14.48907 ? 278 TYR A CD1 1 
ATOM   1877 C CD2 . TYR A 1 278 ? -8.88202  -0.77738  25.97598 1.000 11.31976 ? 278 TYR A CD2 1 
ATOM   1878 C CE1 . TYR A 1 278 ? -11.49953 -1.28538  25.17695 1.000 16.87058 ? 278 TYR A CE1 1 
ATOM   1879 C CE2 . TYR A 1 278 ? -9.95234  -0.33268  26.75618 1.000 11.90788 ? 278 TYR A CE2 1 
ATOM   1880 C CZ  . TYR A 1 278 ? -11.25150 -0.59866  26.36048 1.000 17.69157 ? 278 TYR A CZ  1 
ATOM   1881 O OH  . TYR A 1 278 ? -12.28570 -0.14717  27.13987 1.000 19.78852 ? 278 TYR A OH  1 
ATOM   1882 N N   . TYR A 1 279 ? -8.89344  1.10449   23.13754 1.000 11.99865 ? 279 TYR A N   1 
ATOM   1883 C CA  . TYR A 1 279 ? -9.07336  2.47221   23.60078 1.000 14.30181 ? 279 TYR A CA  1 
ATOM   1884 C C   . TYR A 1 279 ? -10.41145 2.62906   24.31380 1.000 14.53992 ? 279 TYR A C   1 
ATOM   1885 O O   . TYR A 1 279 ? -11.45311 2.18349   23.82505 1.000 11.60008 ? 279 TYR A O   1 
ATOM   1886 C CB  . TYR A 1 279 ? -8.97124  3.46379   22.42840 1.000 10.03964 ? 279 TYR A CB  1 
ATOM   1887 C CG  . TYR A 1 279 ? -9.26537  4.91122   22.79308 1.000 11.95696 ? 279 TYR A CG  1 
ATOM   1888 C CD1 . TYR A 1 279 ? -8.36151  5.66040   23.53946 1.000 16.90019 ? 279 TYR A CD1 1 
ATOM   1889 C CD2 . TYR A 1 279 ? -10.44256 5.53633   22.37385 1.000 13.93710 ? 279 TYR A CD2 1 
ATOM   1890 C CE1 . TYR A 1 279 ? -8.61990  6.98570   23.86104 1.000 15.88761 ? 279 TYR A CE1 1 
ATOM   1891 C CE2 . TYR A 1 279 ? -10.70722 6.86873   22.69351 1.000 17.15144 ? 279 TYR A CE2 1 
ATOM   1892 C CZ  . TYR A 1 279 ? -9.79332  7.58122   23.44207 1.000 21.48456 ? 279 TYR A CZ  1 
ATOM   1893 O OH  . TYR A 1 279 ? -10.04008 8.90031   23.77046 1.000 24.17611 ? 279 TYR A OH  1 
ATOM   1894 N N   . ASP A 1 280 ? -10.35909 3.24913   25.48469 1.000 13.95747 ? 280 ASP A N   1 
ATOM   1895 C CA  . ASP A 1 280 ? -11.53335 3.53043   26.29061 1.000 13.52437 ? 280 ASP A CA  1 
ATOM   1896 C C   . ASP A 1 280 ? -11.81473 5.02327   26.17518 1.000 14.76281 ? 280 ASP A C   1 
ATOM   1897 O O   . ASP A 1 280 ? -11.03547 5.84160   26.66081 1.000 15.75512 ? 280 ASP A O   1 
ATOM   1898 C CB  . ASP A 1 280 ? -11.28847 3.09111   27.74841 1.000 13.89130 ? 280 ASP A CB  1 
ATOM   1899 C CG  . ASP A 1 280 ? -12.49283 3.33330   28.66954 1.000 26.39641 ? 280 ASP A CG  1 
ATOM   1900 O OD1 . ASP A 1 280 ? -13.36666 4.15833   28.35387 1.000 27.75801 ? 280 ASP A OD1 1 
ATOM   1901 O OD2 . ASP A 1 280 ? -12.55423 2.68908   29.73200 1.000 31.66202 ? 280 ASP A OD2 1 
ATOM   1902 N N   . TYR A 1 281 ? -12.91772 5.39208   25.52161 1.000 17.00595 ? 281 TYR A N   1 
ATOM   1903 C CA  . TYR A 1 281 ? -13.19060 6.81398   25.27791 1.000 17.40816 ? 281 TYR A CA  1 
ATOM   1904 C C   . TYR A 1 281 ? -13.52536 7.59257   26.54601 1.000 19.17043 ? 281 TYR A C   1 
ATOM   1905 O O   . TYR A 1 281 ? -13.44483 8.82126   26.56778 1.000 28.58449 ? 281 TYR A O   1 
ATOM   1906 C CB  . TYR A 1 281 ? -14.33221 6.98433   24.27862 1.000 21.92879 ? 281 TYR A CB  1 
ATOM   1907 C CG  . TYR A 1 281 ? -15.71697 6.73421   24.84859 1.000 20.14216 ? 281 TYR A CG  1 
ATOM   1908 C CD1 . TYR A 1 281 ? -16.23312 5.44000   24.93610 1.000 23.63250 ? 281 TYR A CD1 1 
ATOM   1909 C CD2 . TYR A 1 281 ? -16.52551 7.79713   25.26785 1.000 19.18750 ? 281 TYR A CD2 1 
ATOM   1910 C CE1 . TYR A 1 281 ? -17.51066 5.20622   25.44345 1.000 24.06720 ? 281 TYR A CE1 1 
ATOM   1911 C CE2 . TYR A 1 281 ? -17.80845 7.57360   25.77169 1.000 21.27665 ? 281 TYR A CE2 1 
ATOM   1912 C CZ  . TYR A 1 281 ? -18.29331 6.27976   25.85963 1.000 29.77741 ? 281 TYR A CZ  1 
ATOM   1913 O OH  . TYR A 1 281 ? -19.55378 6.05364   26.36941 1.000 33.19195 ? 281 TYR A OH  1 
ATOM   1914 N N   . VAL A 1 282 ? -13.92141 6.88716   27.59150 1.000 20.31283 ? 282 VAL A N   1 
ATOM   1915 C CA  . VAL A 1 282 ? -14.31740 7.55314   28.82660 1.000 28.09485 ? 282 VAL A CA  1 
ATOM   1916 C C   . VAL A 1 282 ? -13.08963 7.95101   29.64985 1.000 33.67537 ? 282 VAL A C   1 
ATOM   1917 O O   . VAL A 1 282 ? -12.96754 9.10179   30.07391 1.000 25.49963 ? 282 VAL A O   1 
ATOM   1918 C CB  . VAL A 1 282 ? -15.24172 6.66009   29.67650 1.000 27.70889 ? 282 VAL A CB  1 
ATOM   1919 C CG1 . VAL A 1 282 ? -15.47615 7.27932   31.05773 1.000 26.08142 ? 282 VAL A CG1 1 
ATOM   1920 C CG2 . VAL A 1 282 ? -16.56609 6.43281   28.95239 1.000 27.80444 ? 282 VAL A CG2 1 
ATOM   1921 N N   . SER A 1 283 ? -12.17871 7.00154   29.85683 1.000 24.35430 ? 283 SER A N   1 
ATOM   1922 C CA  . SER A 1 283 ? -11.01093 7.22641   30.71147 1.000 19.94474 ? 283 SER A CA  1 
ATOM   1923 C C   . SER A 1 283 ? -9.75846  7.64114   29.95513 1.000 23.59243 ? 283 SER A C   1 
ATOM   1924 O O   . SER A 1 283 ? -8.77070  8.05261   30.57684 1.000 21.95288 ? 283 SER A O   1 
ATOM   1925 C CB  . SER A 1 283 ? -10.69770 5.96832   31.51025 1.000 21.04241 ? 283 SER A CB  1 
ATOM   1926 O OG  . SER A 1 283 ? -10.24058 4.93150   30.66053 1.000 21.30931 ? 283 SER A OG  1 
ATOM   1927 N N   . ASN A 1 284 ? -9.80905  7.53148   28.62751 1.000 15.88292 ? 284 ASN A N   1 
ATOM   1928 C CA  . ASN A 1 284 ? -8.63465  7.70178   27.74872 1.000 13.81316 ? 284 ASN A CA  1 
ATOM   1929 C C   . ASN A 1 284 ? -7.56798  6.60790   27.91097 1.000 8.33431  ? 284 ASN A C   1 
ATOM   1930 O O   . ASN A 1 284 ? -6.45996  6.75800   27.38943 1.000 16.00941 ? 284 ASN A O   1 
ATOM   1931 C CB  . ASN A 1 284 ? -7.96991  9.07655   27.95247 1.000 19.16579 ? 284 ASN A CB  1 
ATOM   1932 C CG  . ASN A 1 284 ? -8.76359  10.21380  27.32953 1.000 27.78202 ? 284 ASN A CG  1 
ATOM   1933 O OD1 . ASN A 1 284 ? -9.45346  10.04094  26.31991 1.000 25.76515 ? 284 ASN A OD1 1 
ATOM   1934 N ND2 . ASN A 1 284 ? -8.66585  11.38810  27.93246 1.000 27.23984 ? 284 ASN A ND2 1 
ATOM   1935 N N   . TYR A 1 285 ? -7.89521  5.53434   28.63818 1.000 14.19453 ? 285 TYR A N   1 
ATOM   1936 C CA  . TYR A 1 285 ? -7.03640  4.35420   28.71503 1.000 13.47313 ? 285 TYR A CA  1 
ATOM   1937 C C   . TYR A 1 285 ? -6.73413  3.85599   27.31326 1.000 11.72675 ? 285 TYR A C   1 
ATOM   1938 O O   . TYR A 1 285 ? -7.64612  3.60602   26.52703 1.000 11.67647 ? 285 TYR A O   1 
ATOM   1939 C CB  . TYR A 1 285 ? -7.68904  3.22416   29.52951 1.000 11.14785 ? 285 TYR A CB  1 
ATOM   1940 C CG  . TYR A 1 285 ? -6.87127  1.93909   29.56157 1.000 18.65199 ? 285 TYR A CG  1 
ATOM   1941 C CD1 . TYR A 1 285 ? -6.99621  0.97368   28.55502 1.000 12.93921 ? 285 TYR A CD1 1 
ATOM   1942 C CD2 . TYR A 1 285 ? -5.96543  1.69550   30.58967 1.000 17.94637 ? 285 TYR A CD2 1 
ATOM   1943 C CE1 . TYR A 1 285 ? -6.25654  -0.21266  28.58560 1.000 13.26895 ? 285 TYR A CE1 1 
ATOM   1944 C CE2 . TYR A 1 285 ? -5.21350  0.51855   30.62278 1.000 19.22678 ? 285 TYR A CE2 1 
ATOM   1945 C CZ  . TYR A 1 285 ? -5.36120  -0.42800  29.61841 1.000 18.94432 ? 285 TYR A CZ  1 
ATOM   1946 O OH  . TYR A 1 285 ? -4.61497  -1.58739  29.64520 1.000 16.43510 ? 285 TYR A OH  1 
ATOM   1947 N N   . THR A 1 286 ? -5.45535  3.70384   27.00862 1.000 11.09570 ? 286 THR A N   1 
ATOM   1948 C CA  . THR A 1 286 ? -5.04521  3.25572   25.68634 1.000 17.46597 ? 286 THR A CA  1 
ATOM   1949 C C   . THR A 1 286 ? -4.00630  2.16147   25.82110 1.000 16.51732 ? 286 THR A C   1 
ATOM   1950 O O   . THR A 1 286 ? -2.99419  2.32965   26.50209 1.000 16.19510 ? 286 THR A O   1 
ATOM   1951 C CB  . THR A 1 286 ? -4.45778  4.39603   24.84142 1.000 15.51805 ? 286 THR A CB  1 
ATOM   1952 O OG1 . THR A 1 286 ? -5.33267  5.52837   24.89061 1.000 13.04984 ? 286 THR A OG1 1 
ATOM   1953 C CG2 . THR A 1 286 ? -4.29479  3.95564   23.38938 1.000 15.19977 ? 286 THR A CG2 1 
ATOM   1954 N N   . GLN A 1 287 ? -4.25286  1.03284   25.17561 1.000 11.20369 ? 287 GLN A N   1 
ATOM   1955 C CA  . GLN A 1 287 ? -3.29371  -0.05819  25.23612 1.000 8.73725  ? 287 GLN A CA  1 
ATOM   1956 C C   . GLN A 1 287 ? -2.69492  -0.27123  23.86213 1.000 10.85776 ? 287 GLN A C   1 
ATOM   1957 O O   . GLN A 1 287 ? -3.40761  -0.23800  22.84485 1.000 12.97258 ? 287 GLN A O   1 
ATOM   1958 C CB  . GLN A 1 287 ? -3.95100  -1.34549  25.75613 1.000 8.75197  ? 287 GLN A CB  1 
ATOM   1959 C CG  . GLN A 1 287 ? -2.96158  -2.48787  26.04759 1.000 8.43732  ? 287 GLN A CG  1 
ATOM   1960 C CD  . GLN A 1 287 ? -3.61694  -3.64008  26.78957 1.000 9.56437  ? 287 GLN A CD  1 
ATOM   1961 O OE1 . GLN A 1 287 ? -4.53421  -3.43740  27.58712 1.000 10.00899 ? 287 GLN A OE1 1 
ATOM   1962 N NE2 . GLN A 1 287 ? -3.17974  -4.85247  26.49965 1.000 9.19034  ? 287 GLN A NE2 1 
ATOM   1963 N N   . TYR A 1 288 ? -1.37754  -0.45372  23.84667 1.000 9.54191  ? 288 TYR A N   1 
ATOM   1964 C CA  . TYR A 1 288 ? -0.63348  -0.80550  22.64117 1.000 11.38543 ? 288 TYR A CA  1 
ATOM   1965 C C   . TYR A 1 288 ? -0.16610  -2.26366  22.69809 1.000 17.25085 ? 288 TYR A C   1 
ATOM   1966 O O   . TYR A 1 288 ? -0.02325  -2.84268  23.77730 1.000 11.09140 ? 288 TYR A O   1 
ATOM   1967 C CB  . TYR A 1 288 ? 0.55874   0.14588   22.46474 1.000 11.56583 ? 288 TYR A CB  1 
ATOM   1968 C CG  . TYR A 1 288 ? 0.09650   1.55130   22.13588 1.000 13.03435 ? 288 TYR A CG  1 
ATOM   1969 C CD1 . TYR A 1 288 ? -0.17235  1.92159   20.81651 1.000 14.80291 ? 288 TYR A CD1 1 
ATOM   1970 C CD2 . TYR A 1 288 ? -0.10725  2.49202   23.13859 1.000 16.09217 ? 288 TYR A CD2 1 
ATOM   1971 C CE1 . TYR A 1 288 ? -0.62331  3.19490   20.50325 1.000 15.25231 ? 288 TYR A CE1 1 
ATOM   1972 C CE2 . TYR A 1 288 ? -0.54997  3.77815   22.83819 1.000 13.58465 ? 288 TYR A CE2 1 
ATOM   1973 C CZ  . TYR A 1 288 ? -0.80445  4.11676   21.51547 1.000 16.96710 ? 288 TYR A CZ  1 
ATOM   1974 O OH  . TYR A 1 288 ? -1.24464  5.36998   21.20070 1.000 18.98721 ? 288 TYR A OH  1 
ATOM   1975 N N   . ASP A 1 289 ? 0.05330   -2.85601  21.52810 1.000 11.62889 ? 289 ASP A N   1 
ATOM   1976 C CA  . ASP A 1 289 ? 0.53583   -4.23605  21.42299 1.000 11.69792 ? 289 ASP A CA  1 
ATOM   1977 C C   . ASP A 1 289 ? 1.50425   -4.31787  20.24527 1.000 11.20387 ? 289 ASP A C   1 
ATOM   1978 O O   . ASP A 1 289 ? 1.26367   -5.04956  19.26150 1.000 8.34703  ? 289 ASP A O   1 
ATOM   1979 C CB  . ASP A 1 289 ? -0.64194  -5.21606  21.24559 1.000 9.91315  ? 289 ASP A CB  1 
ATOM   1980 C CG  . ASP A 1 289 ? -0.22927  -6.66549  21.44840 1.000 12.90684 ? 289 ASP A CG  1 
ATOM   1981 O OD1 . ASP A 1 289 ? 0.58215   -6.94620  22.35377 1.000 12.31397 ? 289 ASP A OD1 1 
ATOM   1982 O OD2 . ASP A 1 289 ? -0.71555  -7.52835  20.69965 1.000 13.47970 ? 289 ASP A OD2 1 
ATOM   1983 N N   . ASN A 1 290 ? 2.59181   -3.55379  20.34331 1.000 9.27308  ? 290 ASN A N   1 
ATOM   1984 C CA  . ASN A 1 290 ? 3.44998   -3.27404  19.19932 1.000 11.79447 ? 290 ASN A CA  1 
ATOM   1985 C C   . ASN A 1 290 ? 4.16075   -4.50498  18.67737 1.000 16.52480 ? 290 ASN A C   1 
ATOM   1986 O O   . ASN A 1 290 ? 4.52356   -4.56647  17.49990 1.000 13.57945 ? 290 ASN A O   1 
ATOM   1987 C CB  . ASN A 1 290 ? 4.49641   -2.20735  19.55481 1.000 15.79636 ? 290 ASN A CB  1 
ATOM   1988 C CG  . ASN A 1 290 ? 3.88250   -0.83537  19.77818 1.000 17.74656 ? 290 ASN A CG  1 
ATOM   1989 O OD1 . ASN A 1 290 ? 2.79746   -0.54594  19.27680 1.000 16.02050 ? 290 ASN A OD1 1 
ATOM   1990 N ND2 . ASN A 1 290 ? 4.58528   0.02274   20.53330 1.000 14.37402 ? 290 ASN A ND2 1 
ATOM   1991 N N   . ASN A 1 291 ? 4.36992   -5.48200  19.55217 1.000 17.74120 ? 291 ASN A N   1 
ATOM   1992 C CA  . ASN A 1 291 ? 5.05279   -6.71510  19.16182 1.000 14.69841 ? 291 ASN A CA  1 
ATOM   1993 C C   . ASN A 1 291 ? 4.09256   -7.87136  18.96744 1.000 16.76098 ? 291 ASN A C   1 
ATOM   1994 O O   . ASN A 1 291 ? 4.52730   -8.99861  18.75587 1.000 14.09657 ? 291 ASN A O   1 
ATOM   1995 C CB  . ASN A 1 291 ? 6.10690   -7.09188  20.21036 1.000 20.48965 ? 291 ASN A CB  1 
ATOM   1996 C CG  . ASN A 1 291 ? 7.14291   -6.00003  20.41017 1.000 32.40278 ? 291 ASN A CG  1 
ATOM   1997 O OD1 . ASN A 1 291 ? 7.71786   -5.48638  19.44702 1.000 26.12161 ? 291 ASN A OD1 1 
ATOM   1998 N ND2 . ASN A 1 291 ? 7.37343   -5.62827  21.66620 1.000 38.87261 ? 291 ASN A ND2 1 
ATOM   1999 N N   . TYR A 1 292 ? 2.79135   -7.57534  19.05173 1.000 9.92405  ? 292 TYR A N   1 
ATOM   2000 C CA  . TYR A 1 292 ? 1.70820   -8.54728  18.83314 1.000 11.06140 ? 292 TYR A CA  1 
ATOM   2001 C C   . TYR A 1 292 ? 1.72844   -9.66910  19.86582 1.000 15.87230 ? 292 TYR A C   1 
ATOM   2002 O O   . TYR A 1 292 ? 1.17582   -10.73969 19.63576 1.000 14.80485 ? 292 TYR A O   1 
ATOM   2003 C CB  . TYR A 1 292 ? 1.77469   -9.12034  17.40760 1.000 15.64740 ? 292 TYR A CB  1 
ATOM   2004 C CG  . TYR A 1 292 ? 1.51706   -8.06050  16.34780 1.000 19.54191 ? 292 TYR A CG  1 
ATOM   2005 C CD1 . TYR A 1 292 ? 0.21632   -7.67624  16.03201 1.000 14.13022 ? 292 TYR A CD1 1 
ATOM   2006 C CD2 . TYR A 1 292 ? 2.56375   -7.42643  15.68652 1.000 19.63146 ? 292 TYR A CD2 1 
ATOM   2007 C CE1 . TYR A 1 292 ? -0.03303  -6.70067  15.09708 1.000 10.97544 ? 292 TYR A CE1 1 
ATOM   2008 C CE2 . TYR A 1 292 ? 2.31290   -6.43826  14.72937 1.000 20.39129 ? 292 TYR A CE2 1 
ATOM   2009 C CZ  . TYR A 1 292 ? 1.00314   -6.08981  14.44490 1.000 17.91186 ? 292 TYR A CZ  1 
ATOM   2010 O OH  . TYR A 1 292 ? 0.69592   -5.12804  13.50413 1.000 15.00726 ? 292 TYR A OH  1 
ATOM   2011 N N   . THR A 1 293 ? 2.35061   -9.40803  21.01161 1.000 11.79010 ? 293 THR A N   1 
ATOM   2012 C CA  . THR A 1 293 ? 2.39764   -10.37676 22.10556 1.000 15.49689 ? 293 THR A CA  1 
ATOM   2013 C C   . THR A 1 293 ? 1.01331   -10.77262 22.60373 1.000 15.14985 ? 293 THR A C   1 
ATOM   2014 O O   . THR A 1 293 ? 0.67985   -11.96366 22.67831 1.000 15.15752 ? 293 THR A O   1 
ATOM   2015 C CB  . THR A 1 293 ? 3.20585   -9.82891  23.29112 1.000 17.52036 ? 293 THR A CB  1 
ATOM   2016 O OG1 . THR A 1 293 ? 4.54950   -9.59933  22.86339 1.000 19.35666 ? 293 THR A OG1 1 
ATOM   2017 C CG2 . THR A 1 293 ? 3.21445   -10.82559 24.44817 1.000 17.87897 ? 293 THR A CG2 1 
ATOM   2018 N N   . ASP A 1 294 ? 0.20593   -9.77840  22.95423 1.000 12.54201 ? 294 ASP A N   1 
ATOM   2019 C CA  . ASP A 1 294 ? -1.14544  -10.06800 23.42144 1.000 12.65573 ? 294 ASP A CA  1 
ATOM   2020 C C   . ASP A 1 294 ? -2.03859  -10.57368 22.29737 1.000 11.87494 ? 294 ASP A C   1 
ATOM   2021 O O   . ASP A 1 294 ? -2.92871  -11.36939 22.53922 1.000 9.42253  ? 294 ASP A O   1 
ATOM   2022 C CB  . ASP A 1 294 ? -1.79447  -8.83695  24.05887 1.000 14.62133 ? 294 ASP A CB  1 
ATOM   2023 C CG  . ASP A 1 294 ? -2.98139  -9.20883  24.93164 1.000 25.20111 ? 294 ASP A CG  1 
ATOM   2024 O OD1 . ASP A 1 294 ? -2.74583  -9.62416  26.09244 1.000 22.73135 ? 294 ASP A OD1 1 
ATOM   2025 O OD2 . ASP A 1 294 ? -4.13568  -9.13364  24.44290 1.000 17.85655 ? 294 ASP A OD2 1 
ATOM   2026 N N   . THR A 1 295 ? -1.82431  -10.07849 21.08092 1.000 9.40330  ? 295 THR A N   1 
ATOM   2027 C CA  . THR A 1 295 ? -2.60239  -10.55243 19.93848 1.000 9.40552  ? 295 THR A CA  1 
ATOM   2028 C C   . THR A 1 295 ? -2.45468  -12.06424 19.79432 1.000 13.24699 ? 295 THR A C   1 
ATOM   2029 O O   . THR A 1 295 ? -3.45180  -12.79669 19.80314 1.000 12.91589 ? 295 THR A O   1 
ATOM   2030 C CB  . THR A 1 295 ? -2.16925  -9.86112  18.63655 1.000 10.32024 ? 295 THR A CB  1 
ATOM   2031 O OG1 . THR A 1 295 ? -2.51569  -8.47571  18.70737 1.000 10.78681 ? 295 THR A OG1 1 
ATOM   2032 C CG2 . THR A 1 295 ? -2.86167  -10.48982 17.42506 1.000 12.82898 ? 295 THR A CG2 1 
ATOM   2033 N N   . TYR A 1 296 ? -1.20757  -12.52295 19.68018 1.000 10.60773 ? 296 TYR A N   1 
ATOM   2034 C CA  . TYR A 1 296 ? -0.91263  -13.94425 19.52200 1.000 8.36446  ? 296 TYR A CA  1 
ATOM   2035 C C   . TYR A 1 296 ? -1.48225  -14.77156 20.65741 1.000 12.02454 ? 296 TYR A C   1 
ATOM   2036 O O   . TYR A 1 296 ? -2.06878  -15.83581 20.43067 1.000 15.34739 ? 296 TYR A O   1 
ATOM   2037 C CB  . TYR A 1 296 ? 0.59429   -14.18043 19.43461 1.000 10.69262 ? 296 TYR A CB  1 
ATOM   2038 C CG  . TYR A 1 296 ? 1.24057   -13.61218 18.19306 1.000 17.88302 ? 296 TYR A CG  1 
ATOM   2039 C CD1 . TYR A 1 296 ? 0.47358   -13.23881 17.09147 1.000 20.19660 ? 296 TYR A CD1 1 
ATOM   2040 C CD2 . TYR A 1 296 ? 2.61553   -13.45505 18.11899 1.000 26.35593 ? 296 TYR A CD2 1 
ATOM   2041 C CE1 . TYR A 1 296 ? 1.06159   -12.72620 15.94878 1.000 22.42270 ? 296 TYR A CE1 1 
ATOM   2042 C CE2 . TYR A 1 296 ? 3.21524   -12.94104 16.97938 1.000 33.38021 ? 296 TYR A CE2 1 
ATOM   2043 C CZ  . TYR A 1 296 ? 2.43179   -12.58348 15.89754 1.000 29.59969 ? 296 TYR A CZ  1 
ATOM   2044 O OH  . TYR A 1 296 ? 3.02605   -12.07365 14.76722 1.000 31.33294 ? 296 TYR A OH  1 
ATOM   2045 N N   . SER A 1 297 ? -1.29899  -14.28849 21.88384 1.000 7.70642  ? 297 SER A N   1 
ATOM   2046 C CA  . SER A 1 297 ? -1.82263  -14.96985 23.05830 1.000 13.52081 ? 297 SER A CA  1 
ATOM   2047 C C   . SER A 1 297 ? -3.35686  -15.11854 22.97344 1.000 17.34030 ? 297 SER A C   1 
ATOM   2048 O O   . SER A 1 297 ? -3.91787  -16.18183 23.27684 1.000 10.48292 ? 297 SER A O   1 
ATOM   2049 C CB  . SER A 1 297 ? -1.40934  -14.19812 24.31927 1.000 13.74252 ? 297 SER A CB  1 
ATOM   2050 O OG  . SER A 1 297 ? -1.95290  -14.79142 25.48354 1.000 22.27143 ? 297 SER A OG  1 
ATOM   2051 N N   . THR A 1 298 ? -4.03811  -14.05830 22.53810 1.000 13.96008 ? 298 THR A N   1 
ATOM   2052 C CA  . THR A 1 298 ? -5.50514  -14.09065 22.47009 1.000 10.20028 ? 298 THR A CA  1 
ATOM   2053 C C   . THR A 1 298 ? -5.99555  -15.00074 21.34293 1.000 12.97164 ? 298 THR A C   1 
ATOM   2054 O O   . THR A 1 298 ? -6.95020  -15.77221 21.53098 1.000 12.48799 ? 298 THR A O   1 
ATOM   2055 C CB  . THR A 1 298 ? -6.08684  -12.67478 22.29812 1.000 14.88569 ? 298 THR A CB  1 
ATOM   2056 O OG1 . THR A 1 298 ? -5.71812  -11.86934 23.42741 1.000 11.10987 ? 298 THR A OG1 1 
ATOM   2057 C CG2 . THR A 1 298 ? -7.59385  -12.72082 22.21585 1.000 14.44284 ? 298 THR A CG2 1 
ATOM   2058 N N   . LEU A 1 299 ? -5.33317  -14.94172 20.18704 1.000 11.46329 ? 299 LEU A N   1 
ATOM   2059 C CA  . LEU A 1 299 ? -5.67945  -15.82335 19.07642 1.000 12.66139 ? 299 LEU A CA  1 
ATOM   2060 C C   . LEU A 1 299 ? -5.56876  -17.26878 19.52511 1.000 15.76160 ? 299 LEU A C   1 
ATOM   2061 O O   . LEU A 1 299 ? -6.42642  -18.08327 19.21175 1.000 15.60884 ? 299 LEU A O   1 
ATOM   2062 C CB  . LEU A 1 299 ? -4.77028  -15.60802 17.85500 1.000 12.03950 ? 299 LEU A CB  1 
ATOM   2063 C CG  . LEU A 1 299 ? -4.68792  -14.23428 17.17075 1.000 17.01184 ? 299 LEU A CG  1 
ATOM   2064 C CD1 . LEU A 1 299 ? -3.95773  -14.33489 15.84296 1.000 20.28145 ? 299 LEU A CD1 1 
ATOM   2065 C CD2 . LEU A 1 299 ? -6.05158  -13.58791 16.98138 1.000 13.77667 ? 299 LEU A CD2 1 
ATOM   2066 N N   . ALA A 1 300 ? -4.49788  -17.58348 20.25002 1.000 9.45725  ? 300 ALA A N   1 
ATOM   2067 C CA  . ALA A 1 300 ? -4.27083  -18.95030 20.68470 1.000 13.42607 ? 300 ALA A CA  1 
ATOM   2068 C C   . ALA A 1 300 ? -5.34524  -19.35196 21.67494 1.000 15.14098 ? 300 ALA A C   1 
ATOM   2069 O O   . ALA A 1 300 ? -5.83873  -20.48041 21.64426 1.000 16.37238 ? 300 ALA A O   1 
ATOM   2070 C CB  . ALA A 1 300 ? -2.87984  -19.10679 21.31175 1.000 14.17782 ? 300 ALA A CB  1 
ATOM   2071 N N   . ASN A 1 301 ? -5.70819  -18.42914 22.55853 1.000 10.41287 ? 301 ASN A N   1 
ATOM   2072 C CA  . ASN A 1 301 ? -6.66360  -18.73792 23.61741 1.000 12.28485 ? 301 ASN A CA  1 
ATOM   2073 C C   . ASN A 1 301 ? -8.04631  -19.06471 23.06686 1.000 13.35870 ? 301 ASN A C   1 
ATOM   2074 O O   . ASN A 1 301 ? -8.77441  -19.88438 23.62985 1.000 16.19014 ? 301 ASN A O   1 
ATOM   2075 C CB  . ASN A 1 301 ? -6.78481  -17.56330 24.60303 1.000 19.77604 ? 301 ASN A CB  1 
ATOM   2076 C CG  . ASN A 1 301 ? -7.46249  -17.96469 25.91011 1.000 31.65091 ? 301 ASN A CG  1 
ATOM   2077 O OD1 . ASN A 1 301 ? -7.24527  -19.06667 26.42189 1.000 38.62990 ? 301 ASN A OD1 1 
ATOM   2078 N ND2 . ASN A 1 301 ? -8.27789  -17.06979 26.45956 1.000 30.75990 ? 301 ASN A ND2 1 
ATOM   2079 N N   . TYR A 1 302 ? -8.40523  -18.41729 21.96681 1.000 11.09401 ? 302 TYR A N   1 
ATOM   2080 C CA  . TYR A 1 302 ? -9.75786  -18.52324 21.44142 1.000 12.48680 ? 302 TYR A CA  1 
ATOM   2081 C C   . TYR A 1 302 ? -9.80655  -19.41993 20.21894 1.000 15.32540 ? 302 TYR A C   1 
ATOM   2082 O O   . TYR A 1 302 ? -10.86196 -19.57296 19.59640 1.000 16.38733 ? 302 TYR A O   1 
ATOM   2083 C CB  . TYR A 1 302 ? -10.29916 -17.13862 21.08363 1.000 12.95008 ? 302 TYR A CB  1 
ATOM   2084 C CG  . TYR A 1 302 ? -10.52225 -16.24357 22.28104 1.000 14.81801 ? 302 TYR A CG  1 
ATOM   2085 C CD1 . TYR A 1 302 ? -10.70173 -16.78222 23.54904 1.000 22.15379 ? 302 TYR A CD1 1 
ATOM   2086 C CD2 . TYR A 1 302 ? -10.56322 -14.86417 22.14242 1.000 8.56357  ? 302 TYR A CD2 1 
ATOM   2087 C CE1 . TYR A 1 302 ? -10.91479 -15.97019 24.64715 1.000 23.67436 ? 302 TYR A CE1 1 
ATOM   2088 C CE2 . TYR A 1 302 ? -10.77818 -14.03805 23.23258 1.000 12.61185 ? 302 TYR A CE2 1 
ATOM   2089 C CZ  . TYR A 1 302 ? -10.95055 -14.60560 24.48787 1.000 18.27583 ? 302 TYR A CZ  1 
ATOM   2090 O OH  . TYR A 1 302 ? -11.15719 -13.79989 25.57898 1.000 17.82683 ? 302 TYR A OH  1 
ATOM   2091 N N   . ARG A 1 303 ? -8.65871  -20.00119 19.88390 1.000 14.83258 ? 303 ARG A N   1 
ATOM   2092 C CA  . ARG A 1 303 ? -8.49920  -20.79603 18.66168 1.000 15.46273 ? 303 ARG A CA  1 
ATOM   2093 C C   . ARG A 1 303 ? -9.56966  -21.86865 18.50282 1.000 15.35200 ? 303 ARG A C   1 
ATOM   2094 O O   . ARG A 1 303 ? -10.13187 -22.04360 17.41248 1.000 18.06641 ? 303 ARG A O   1 
ATOM   2095 C CB  . ARG A 1 303 ? -7.11168  -21.44689 18.64104 1.000 12.40386 ? 303 ARG A CB  1 
ATOM   2096 C CG  . ARG A 1 303 ? -6.89118  -22.42596 17.49361 1.000 16.01825 ? 303 ARG A CG  1 
ATOM   2097 C CD  . ARG A 1 303 ? -5.41248  -22.69442 17.26534 1.000 10.95141 ? 303 ARG A CD  1 
ATOM   2098 N NE  . ARG A 1 303 ? -5.21445  -23.77681 16.29498 1.000 15.62049 ? 303 ARG A NE  1 
ATOM   2099 C CZ  . ARG A 1 303 ? -4.03769  -24.33109 16.01427 1.000 17.86076 ? 303 ARG A CZ  1 
ATOM   2100 N NH1 . ARG A 1 303 ? -2.94640  -23.92006 16.63193 1.000 19.24029 ? 303 ARG A NH1 1 
ATOM   2101 N NH2 . ARG A 1 303 ? -3.95114  -25.29643 15.11069 1.000 17.56631 ? 303 ARG A NH2 1 
ATOM   2102 N N   . TYR A 1 304 ? -9.86238  -22.57153 19.58997 1.000 12.41431 ? 304 TYR A N   1 
ATOM   2103 C CA  . TYR A 1 304 ? -10.77300 -23.70389 19.52010 1.000 14.01421 ? 304 TYR A CA  1 
ATOM   2104 C C   . TYR A 1 304 ? -12.16157 -23.40821 20.08040 1.000 21.80727 ? 304 TYR A C   1 
ATOM   2105 O O   . TYR A 1 304 ? -13.00055 -24.30671 20.16398 1.000 18.24943 ? 304 TYR A O   1 
ATOM   2106 C CB  . TYR A 1 304 ? -10.16032 -24.89360 20.25337 1.000 14.67686 ? 304 TYR A CB  1 
ATOM   2107 C CG  . TYR A 1 304 ? -8.87656  -25.38439 19.60812 1.000 16.14040 ? 304 TYR A CG  1 
ATOM   2108 C CD1 . TYR A 1 304 ? -8.91951  -26.17123 18.45456 1.000 11.66979 ? 304 TYR A CD1 1 
ATOM   2109 C CD2 . TYR A 1 304 ? -7.62667  -25.05089 20.13590 1.000 17.82013 ? 304 TYR A CD2 1 
ATOM   2110 C CE1 . TYR A 1 304 ? -7.76375  -26.62179 17.84819 1.000 15.22097 ? 304 TYR A CE1 1 
ATOM   2111 C CE2 . TYR A 1 304 ? -6.44272  -25.52157 19.53228 1.000 12.41534 ? 304 TYR A CE2 1 
ATOM   2112 C CZ  . TYR A 1 304 ? -6.52918  -26.29960 18.39299 1.000 15.71437 ? 304 TYR A CZ  1 
ATOM   2113 O OH  . TYR A 1 304 ? -5.38525  -26.76170 17.77275 1.000 18.82202 ? 304 TYR A OH  1 
ATOM   2114 N N   . ARG A 1 305 ? -12.40465 -22.15864 20.46732 1.000 18.48802 ? 305 ARG A N   1 
ATOM   2115 C CA  . ARG A 1 305 ? -13.68914 -21.78880 21.06616 1.000 21.06538 ? 305 ARG A CA  1 
ATOM   2116 C C   . ARG A 1 305 ? -14.79173 -21.54756 20.05051 1.000 19.01074 ? 305 ARG A C   1 
ATOM   2117 O O   . ARG A 1 305 ? -14.56055 -21.05334 18.95467 1.000 21.51080 ? 305 ARG A O   1 
ATOM   2118 C CB  . ARG A 1 305 ? -13.54204 -20.53779 21.93373 1.000 22.28191 ? 305 ARG A CB  1 
ATOM   2119 C CG  . ARG A 1 305 ? -12.75597 -20.76059 23.20943 1.000 21.52661 ? 305 ARG A CG  1 
ATOM   2120 C CD  . ARG A 1 305 ? -12.94461 -19.60236 24.18636 1.000 26.37741 ? 305 ARG A CD  1 
ATOM   2121 N NE  . ARG A 1 305 ? -11.99799 -19.67712 25.29127 1.000 27.25079 ? 305 ARG A NE  1 
ATOM   2122 C CZ  . ARG A 1 305 ? -11.98522 -18.85053 26.33287 1.000 26.68367 ? 305 ARG A CZ  1 
ATOM   2123 N NH1 . ARG A 1 305 ? -12.87664 -17.87454 26.42680 1.000 21.14014 ? 305 ARG A NH1 1 
ATOM   2124 N NH2 . ARG A 1 305 ? -11.07282 -19.00390 27.28631 1.000 26.14903 ? 305 ARG A NH2 1 
ATOM   2125 N N   . GLN A 1 306 ? -16.00535 -21.89072 20.45360 1.000 21.53676 ? 306 GLN A N   1 
ATOM   2126 C CA  . GLN A 1 306 ? -17.19721 -21.65712 19.65818 1.000 28.22850 ? 306 GLN A CA  1 
ATOM   2127 C C   . GLN A 1 306 ? -18.07627 -20.63567 20.38120 1.000 24.42290 ? 306 GLN A C   1 
ATOM   2128 O O   . GLN A 1 306 ? -18.15437 -20.63715 21.61080 1.000 26.38186 ? 306 GLN A O   1 
ATOM   2129 C CB  . GLN A 1 306 ? -17.94774 -22.97534 19.43349 1.000 41.86472 ? 306 GLN A CB  1 
ATOM   2130 C CG  . GLN A 1 306 ? -18.12686 -23.37623 17.97342 1.000 52.34188 ? 306 GLN A CG  1 
ATOM   2131 C CD  . GLN A 1 306 ? -16.82855 -23.40077 17.18211 1.000 54.64379 ? 306 GLN A CD  1 
ATOM   2132 O OE1 . GLN A 1 306 ? -16.79503 -22.97498 16.02469 1.000 59.40842 ? 306 GLN A OE1 1 
ATOM   2133 N NE2 . GLN A 1 306 ? -15.75913 -23.91112 17.79236 1.000 47.21953 ? 306 GLN A NE2 1 
ATOM   2134 N N   . THR A 1 307 ? -18.70752 -19.75356 19.61825 1.000 24.83527 ? 307 THR A N   1 
ATOM   2135 C CA  . THR A 1 307 ? -19.56434 -18.71265 20.17965 1.000 21.83534 ? 307 THR A CA  1 
ATOM   2136 C C   . THR A 1 307 ? -20.56995 -19.28115 21.19006 1.000 26.89791 ? 307 THR A C   1 
ATOM   2137 O O   . THR A 1 307 ? -21.22267 -20.28603 20.93099 1.000 28.32163 ? 307 THR A O   1 
ATOM   2138 C CB  . THR A 1 307 ? -20.30747 -17.97602 19.05014 1.000 24.65684 ? 307 THR A CB  1 
ATOM   2139 O OG1 . THR A 1 307 ? -19.35172 -17.33214 18.19981 1.000 25.33238 ? 307 THR A OG1 1 
ATOM   2140 C CG2 . THR A 1 307 ? -21.24759 -16.94033 19.60454 1.000 26.30126 ? 307 THR A CG2 1 
ATOM   2141 N N   . SER A 1 308 ? -20.65532 -18.66075 22.36105 1.000 27.08048 ? 308 SER A N   1 
ATOM   2142 C CA  . SER A 1 308 ? -21.61697 -19.07236 23.37743 1.000 31.57449 ? 308 SER A CA  1 
ATOM   2143 C C   . SER A 1 308 ? -22.75123 -18.04474 23.47214 1.000 32.81408 ? 308 SER A C   1 
ATOM   2144 O O   . SER A 1 308 ? -22.50511 -16.88327 23.80275 1.000 30.50727 ? 308 SER A O   1 
ATOM   2145 C CB  . SER A 1 308 ? -20.92190 -19.23231 24.73133 1.000 30.88511 ? 308 SER A CB  1 
ATOM   2146 O OG  . SER A 1 308 ? -21.86271 -19.33752 25.78507 1.000 37.26503 ? 308 SER A OG  1 
ATOM   2147 N N   . CYS A 1 309 ? -23.98345 -18.46522 23.19511 1.000 22.66585 ? 309 CYS A N   1 
ATOM   2148 C CA  . CYS A 1 309 ? -25.10528 -17.51712 23.14689 1.000 29.26122 ? 309 CYS A CA  1 
ATOM   2149 C C   . CYS A 1 309 ? -25.36112 -16.83475 24.49347 1.000 39.77346 ? 309 CYS A C   1 
ATOM   2150 O O   . CYS A 1 309 ? -25.67522 -17.49191 25.48561 1.000 48.93113 ? 309 CYS A O   1 
ATOM   2151 C CB  . CYS A 1 309 ? -26.37634 -18.21872 22.67547 1.000 31.25840 ? 309 CYS A CB  1 
ATOM   2152 S SG  . CYS A 1 309 ? -26.20619 -19.04896 21.09107 1.000 39.70941 ? 309 CYS A SG  1 
ATOM   2153 N N   . SER A 1 310 ? -25.21529 -15.51280 24.51524 1.000 44.50171 ? 310 SER A N   1 
ATOM   2154 C CA  . SER A 1 310 ? -25.49256 -14.72219 25.70737 1.000 46.55970 ? 310 SER A CA  1 
ATOM   2155 C C   . SER A 1 310 ? -26.98006 -14.78319 26.06274 1.000 40.72560 ? 310 SER A C   1 
ATOM   2156 O O   . SER A 1 310 ? -27.33693 -14.96860 27.22273 1.000 44.76531 ? 310 SER A O   1 
ATOM   2157 C CB  . SER A 1 310 ? -25.04687 -13.27456 25.50184 1.000 54.09654 ? 310 SER A CB  1 
ATOM   2158 O OG  . SER A 1 310 ? -25.42245 -12.45807 26.59432 1.000 62.26721 ? 310 SER A OG  1 
ATOM   2159 N N   . PHE A 1 311 ? -27.84386 -14.62798 25.06512 1.000 35.09148 ? 311 PHE A N   1 
ATOM   2160 C CA  . PHE A 1 311 ? -29.27542 -14.83541 25.27169 1.000 34.87778 ? 311 PHE A CA  1 
ATOM   2161 C C   . PHE A 1 311 ? -29.91126 -15.59416 24.10968 1.000 38.42247 ? 311 PHE A C   1 
ATOM   2162 O O   . PHE A 1 311 ? -29.45350 -15.51212 22.96086 1.000 30.38142 ? 311 PHE A O   1 
ATOM   2163 C CB  . PHE A 1 311 ? -30.00777 -13.49958 25.50063 1.000 39.60782 ? 311 PHE A CB  1 
ATOM   2164 C CG  . PHE A 1 311 ? -29.78442 -12.47265 24.41911 1.000 39.76971 ? 311 PHE A CG  1 
ATOM   2165 C CD1 . PHE A 1 311 ? -28.69640 -11.60816 24.47851 1.000 39.76940 ? 311 PHE A CD1 1 
ATOM   2166 C CD2 . PHE A 1 311 ? -30.67333 -12.35404 23.36056 1.000 33.16259 ? 311 PHE A CD2 1 
ATOM   2167 C CE1 . PHE A 1 311 ? -28.48842 -10.65466 23.49571 1.000 39.57773 ? 311 PHE A CE1 1 
ATOM   2168 C CE2 . PHE A 1 311 ? -30.47146 -11.40537 22.37479 1.000 40.75646 ? 311 PHE A CE2 1 
ATOM   2169 C CZ  . PHE A 1 311 ? -29.37954 -10.55343 22.44226 1.000 43.11024 ? 311 PHE A CZ  1 
ATOM   2170 N N   . LEU A 1 312 ? -30.96033 -16.34830 24.43301 1.000 39.93119 ? 312 LEU A N   1 
ATOM   2171 C CA  . LEU A 1 312 ? -31.68980 -17.14936 23.45526 1.000 41.37448 ? 312 LEU A CA  1 
ATOM   2172 C C   . LEU A 1 312 ? -33.10030 -16.60883 23.26075 1.000 44.28741 ? 312 LEU A C   1 
ATOM   2173 O O   . LEU A 1 312 ? -33.43644 -16.09497 22.19857 1.000 49.52255 ? 312 LEU A O   1 
ATOM   2174 C CB  . LEU A 1 312 ? -31.75104 -18.61471 23.89512 1.000 37.66937 ? 312 LEU A CB  1 
ATOM   2175 C CG  . LEU A 1 312 ? -30.43648 -19.34999 24.17343 1.000 36.65640 ? 312 LEU A CG  1 
ATOM   2176 C CD1 . LEU A 1 312 ? -30.71588 -20.66434 24.86573 1.000 39.52127 ? 312 LEU A CD1 1 
ATOM   2177 C CD2 . LEU A 1 312 ? -29.67208 -19.59110 22.88590 1.000 36.41467 ? 312 LEU A CD2 1 
HETATM 2178 O O   . HOH B 2 .   ? 5.96239   -9.75753  32.73050 1.000 55.69009 ? 401 HOH A O   1 
HETATM 2179 O O   . HOH B 2 .   ? -23.49041 -19.57069 47.34427 1.000 43.15620 ? 402 HOH A O   1 
HETATM 2180 O O   . HOH B 2 .   ? 0.89473   0.21323   38.81674 1.000 38.82959 ? 403 HOH A O   1 
HETATM 2181 O O   . HOH B 2 .   ? -15.72932 -0.07973  -3.76245 1.000 43.91517 ? 404 HOH A O   1 
HETATM 2182 O O   . HOH B 2 .   ? 0.09204   -22.54646 18.70488 1.000 50.42192 ? 405 HOH A O   1 
HETATM 2183 O O   . HOH B 2 .   ? 3.15341   9.07729   26.90989 1.000 38.66443 ? 406 HOH A O   1 
HETATM 2184 O O   . HOH B 2 .   ? -0.862    14.236    24.139   1.000 44.87293 ? 407 HOH A O   1 
HETATM 2185 O O   . HOH B 2 .   ? -8.19737  -3.60385  39.02890 1.000 23.68191 ? 408 HOH A O   1 
HETATM 2186 O O   . HOH B 2 .   ? -12.42521 9.65709   2.69824  1.000 44.34784 ? 409 HOH A O   1 
HETATM 2187 O O   . HOH B 2 .   ? -28.05690 -14.66807 38.88273 1.000 42.23111 ? 410 HOH A O   1 
HETATM 2188 O O   . HOH B 2 .   ? -10.21624 1.36824   39.74314 1.000 42.41782 ? 411 HOH A O   1 
HETATM 2189 O O   . HOH B 2 .   ? -22.51432 -15.46448 13.09499 1.000 41.26897 ? 412 HOH A O   1 
HETATM 2190 O O   . HOH B 2 .   ? -24.89969 -5.24093  25.13599 1.000 29.86201 ? 413 HOH A O   1 
HETATM 2191 O O   . HOH B 2 .   ? -3.53940  7.19510   25.35016 1.000 51.45804 ? 414 HOH A O   1 
HETATM 2192 O O   . HOH B 2 .   ? -12.88732 9.60146   17.27197 1.000 20.20872 ? 415 HOH A O   1 
HETATM 2193 O O   . HOH B 2 .   ? -2.34526  12.42721  28.78082 1.000 36.82626 ? 416 HOH A O   1 
HETATM 2194 O O   . HOH B 2 .   ? -7.343    14.937    20.128   1.000 30.26848 ? 417 HOH A O   1 
HETATM 2195 O O   . HOH B 2 .   ? -11.04048 -12.08407 48.70056 1.000 36.87857 ? 418 HOH A O   1 
HETATM 2196 O O   . HOH B 2 .   ? 1.80259   -19.19017 31.51862 1.000 16.69539 ? 419 HOH A O   1 
HETATM 2197 O O   . HOH B 2 .   ? -10.79924 18.45060  12.79736 1.000 31.80247 ? 420 HOH A O   1 
HETATM 2198 O O   . HOH B 2 .   ? -4.50445  -11.00388 27.30057 1.000 28.08909 ? 421 HOH A O   1 
HETATM 2199 O O   . HOH B 2 .   ? -12.60052 -16.55544 29.29360 1.000 20.30851 ? 422 HOH A O   1 
HETATM 2200 O O   . HOH B 2 .   ? -25.71773 -6.71167  37.77250 1.000 43.50121 ? 423 HOH A O   1 
HETATM 2201 O O   . HOH B 2 .   ? 0.28214   -1.87452  18.89732 1.000 9.98337  ? 424 HOH A O   1 
HETATM 2202 O O   . HOH B 2 .   ? -5.51253  -14.17748 45.35959 1.000 31.19364 ? 425 HOH A O   1 
HETATM 2203 O O   . HOH B 2 .   ? 3.08059   -6.37258  22.06098 1.000 14.07394 ? 426 HOH A O   1 
HETATM 2204 O O   . HOH B 2 .   ? -8.83509  -15.60307 -0.30643 1.000 48.31490 ? 427 HOH A O   1 
HETATM 2205 O O   . HOH B 2 .   ? -14.85490 -13.87439 30.84328 1.000 15.63404 ? 428 HOH A O   1 
HETATM 2206 O O   . HOH B 2 .   ? -1.16495  -18.04179 39.27085 1.000 25.68049 ? 429 HOH A O   1 
HETATM 2207 O O   . HOH B 2 .   ? -18.51112 6.59590   13.34079 1.000 23.52519 ? 430 HOH A O   1 
HETATM 2208 O O   . HOH B 2 .   ? 3.29438   -2.22565  22.82359 1.000 10.31164 ? 431 HOH A O   1 
HETATM 2209 O O   . HOH B 2 .   ? 2.55047   -4.32998  11.74613 1.000 22.68789 ? 432 HOH A O   1 
HETATM 2210 O O   . HOH B 2 .   ? -12.34527 10.00999  23.18902 1.000 36.67166 ? 433 HOH A O   1 
HETATM 2211 O O   . HOH B 2 .   ? -2.04781  -7.10353  41.26352 1.000 21.64087 ? 434 HOH A O   1 
HETATM 2212 O O   . HOH B 2 .   ? -17.02540 -12.79438 29.20455 1.000 26.19325 ? 435 HOH A O   1 
HETATM 2213 O O   . HOH B 2 .   ? -12.28565 6.98515   2.70898  1.000 44.36668 ? 436 HOH A O   1 
HETATM 2214 O O   . HOH B 2 .   ? -18.93248 -20.49657 16.96920 1.000 36.24280 ? 437 HOH A O   1 
HETATM 2215 O O   . HOH B 2 .   ? -14.87495 0.05195   26.61798 1.000 23.14405 ? 438 HOH A O   1 
HETATM 2216 O O   . HOH B 2 .   ? -11.85663 -24.18576 35.42802 1.000 18.69025 ? 439 HOH A O   1 
HETATM 2217 O O   . HOH B 2 .   ? -11.01820 -27.48978 33.60786 1.000 41.37771 ? 440 HOH A O   1 
HETATM 2218 O O   . HOH B 2 .   ? -17.83892 -17.82408 25.76037 1.000 30.48431 ? 441 HOH A O   1 
HETATM 2219 O O   . HOH B 2 .   ? -12.30653 -20.58555 29.83279 1.000 19.30255 ? 442 HOH A O   1 
HETATM 2220 O O   . HOH B 2 .   ? -4.17329  -13.48647 26.15053 1.000 36.73574 ? 443 HOH A O   1 
HETATM 2221 O O   . HOH B 2 .   ? -24.82755 -8.16042  41.50768 1.000 49.89640 ? 444 HOH A O   1 
HETATM 2222 O O   . HOH B 2 .   ? -1.27056  -17.32715 18.36945 1.000 19.45831 ? 445 HOH A O   1 
HETATM 2223 O O   . HOH B 2 .   ? 9.035     -9.572    39.295   1.000 22.23862 ? 446 HOH A O   1 
HETATM 2224 O O   . HOH B 2 .   ? -13.98890 -18.69710 43.27189 1.000 44.55417 ? 447 HOH A O   1 
HETATM 2225 O O   . HOH B 2 .   ? -17.69278 10.42279  12.42386 1.000 40.47219 ? 448 HOH A O   1 
HETATM 2226 O O   . HOH B 2 .   ? 2.18874   -14.15477 22.98528 1.000 14.01387 ? 449 HOH A O   1 
HETATM 2227 O O   . HOH B 2 .   ? -8.95051  3.71188   -2.87744 1.000 36.40573 ? 450 HOH A O   1 
HETATM 2228 O O   . HOH B 2 .   ? -19.69209 -11.28473 24.77665 1.000 20.30476 ? 451 HOH A O   1 
HETATM 2229 O O   . HOH B 2 .   ? -19.66472 0.80499   26.46942 1.000 26.35702 ? 452 HOH A O   1 
HETATM 2230 O O   . HOH B 2 .   ? -6.61603  -7.40473  45.44676 1.000 25.62906 ? 453 HOH A O   1 
HETATM 2231 O O   . HOH B 2 .   ? -18.63062 4.39517   5.82757  1.000 21.06901 ? 454 HOH A O   1 
HETATM 2232 O O   . HOH B 2 .   ? 7.12209   -0.77608  20.93143 1.000 27.32569 ? 455 HOH A O   1 
HETATM 2233 O O   . HOH B 2 .   ? -22.05430 -21.32060 46.27433 1.000 41.50052 ? 456 HOH A O   1 
HETATM 2234 O O   . HOH B 2 .   ? 0.33705   4.06301   7.63197  1.000 41.59306 ? 457 HOH A O   1 
HETATM 2235 O O   . HOH B 2 .   ? -12.04197 -7.07612  14.88834 1.000 13.81583 ? 458 HOH A O   1 
HETATM 2236 O O   . HOH B 2 .   ? -9.04188  -26.48232 9.55350  1.000 27.43111 ? 459 HOH A O   1 
HETATM 2237 O O   . HOH B 2 .   ? -25.25763 -9.01851  43.75387 1.000 36.58272 ? 460 HOH A O   1 
HETATM 2238 O O   . HOH B 2 .   ? -10.41832 -21.87534 25.53667 1.000 42.06831 ? 461 HOH A O   1 
HETATM 2239 O O   . HOH B 2 .   ? -5.39012  -19.10229 16.69639 1.000 13.48806 ? 462 HOH A O   1 
HETATM 2240 O O   . HOH B 2 .   ? 4.44410   -4.75375  0.81298  1.000 50.82444 ? 463 HOH A O   1 
HETATM 2241 O O   . HOH B 2 .   ? -11.82955 -3.64839  32.90198 1.000 19.62894 ? 464 HOH A O   1 
HETATM 2242 O O   . HOH B 2 .   ? -5.41473  -16.03684 3.43184  1.000 29.31342 ? 465 HOH A O   1 
HETATM 2243 O O   . HOH B 2 .   ? -14.82679 -9.26776  31.13867 1.000 16.18578 ? 466 HOH A O   1 
HETATM 2244 O O   . HOH B 2 .   ? -16.56083 -25.96604 35.24866 1.000 41.06639 ? 467 HOH A O   1 
HETATM 2245 O O   . HOH B 2 .   ? -7.97171  3.60730   34.33262 1.000 28.06886 ? 468 HOH A O   1 
HETATM 2246 O O   . HOH B 2 .   ? -21.31163 10.34642  20.57987 1.000 38.67881 ? 469 HOH A O   1 
HETATM 2247 O O   . HOH B 2 .   ? -9.79918  5.78068   -1.15281 1.000 30.43272 ? 470 HOH A O   1 
HETATM 2248 O O   . HOH B 2 .   ? -11.18194 0.84808   -6.73391 1.000 37.51163 ? 471 HOH A O   1 
HETATM 2249 O O   . HOH B 2 .   ? -5.18467  -4.77655  29.88866 1.000 13.00271 ? 472 HOH A O   1 
HETATM 2250 O O   . HOH B 2 .   ? -21.37494 -8.72836  27.73396 1.000 23.78591 ? 473 HOH A O   1 
HETATM 2251 O O   . HOH B 2 .   ? -2.82914  1.10857   37.11077 1.000 36.12736 ? 474 HOH A O   1 
HETATM 2252 O O   . HOH B 2 .   ? -7.22440  -3.76133  18.13550 1.000 15.00629 ? 475 HOH A O   1 
HETATM 2253 O O   . HOH B 2 .   ? -9.60636  -1.33337  38.49235 1.000 35.79751 ? 476 HOH A O   1 
HETATM 2254 O O   . HOH B 2 .   ? 5.93208   -7.70722  24.29812 1.000 39.84653 ? 477 HOH A O   1 
HETATM 2255 O O   . HOH B 2 .   ? -16.85146 -6.08761  6.85074  1.000 17.03838 ? 478 HOH A O   1 
HETATM 2256 O O   . HOH B 2 .   ? -2.27212  -8.15007  29.99810 1.000 27.10245 ? 479 HOH A O   1 
HETATM 2257 O O   . HOH B 2 .   ? -16.54762 -7.31942  20.46520 1.000 20.89052 ? 480 HOH A O   1 
HETATM 2258 O O   . HOH B 2 .   ? -21.13262 8.28109   26.74905 1.000 29.85198 ? 481 HOH A O   1 
HETATM 2259 O O   . HOH B 2 .   ? -15.37996 -17.94939 10.39331 1.000 27.84621 ? 482 HOH A O   1 
HETATM 2260 O O   . HOH B 2 .   ? -3.44137  -15.11220 10.63667 1.000 21.12283 ? 483 HOH A O   1 
HETATM 2261 O O   . HOH B 2 .   ? -1.43729  6.48060   -0.44470 1.000 44.59523 ? 484 HOH A O   1 
HETATM 2262 O O   . HOH B 2 .   ? -0.72598  -5.33935  24.73294 1.000 16.33423 ? 485 HOH A O   1 
HETATM 2263 O O   . HOH B 2 .   ? -6.37086  -22.82398 23.01198 1.000 36.78380 ? 486 HOH A O   1 
HETATM 2264 O O   . HOH B 2 .   ? -5.62101  -19.95079 9.18532  1.000 27.41575 ? 487 HOH A O   1 
HETATM 2265 O O   . HOH B 2 .   ? -9.25254  -21.02697 26.76108 1.000 34.02067 ? 488 HOH A O   1 
HETATM 2266 O O   . HOH B 2 .   ? 2.84527   3.05779   3.21616  1.000 42.35761 ? 489 HOH A O   1 
HETATM 2267 O O   . HOH B 2 .   ? -2.63033  -19.46273 17.21657 1.000 15.90580 ? 490 HOH A O   1 
HETATM 2268 O O   . HOH B 2 .   ? -12.36392 -14.19021 18.77240 1.000 14.16397 ? 491 HOH A O   1 
HETATM 2269 O O   . HOH B 2 .   ? -22.16071 -2.21988  30.33526 1.000 35.53894 ? 492 HOH A O   1 
HETATM 2270 O O   . HOH B 2 .   ? -1.19617  -20.19136 35.24994 1.000 30.20277 ? 493 HOH A O   1 
HETATM 2271 O O   . HOH B 2 .   ? 2.79329   3.64244   31.34823 1.000 36.76636 ? 494 HOH A O   1 
HETATM 2272 O O   . HOH B 2 .   ? -20.55555 3.46197   26.13923 1.000 28.72155 ? 495 HOH A O   1 
HETATM 2273 O O   . HOH B 2 .   ? -9.85728  -14.89095 28.85964 1.000 17.16479 ? 496 HOH A O   1 
HETATM 2274 O O   . HOH B 2 .   ? -26.58654 -3.68680  9.17855  1.000 29.46497 ? 497 HOH A O   1 
HETATM 2275 O O   . HOH B 2 .   ? -21.69811 -17.92212 31.50438 1.000 23.85379 ? 498 HOH A O   1 
HETATM 2276 O O   . HOH B 2 .   ? -2.79299  -22.42785 34.83828 1.000 27.07346 ? 499 HOH A O   1 
HETATM 2277 O O   . HOH B 2 .   ? -13.83686 -1.26997  45.32812 1.000 30.39318 ? 500 HOH A O   1 
HETATM 2278 O O   . HOH B 2 .   ? 0.90806   -17.18780 35.06660 1.000 36.22071 ? 501 HOH A O   1 
HETATM 2279 O O   . HOH B 2 .   ? -13.45011 -14.57943 26.99192 1.000 31.01454 ? 502 HOH A O   1 
HETATM 2280 O O   . HOH B 2 .   ? -3.82824  -18.17640 4.88585  1.000 49.48093 ? 503 HOH A O   1 
HETATM 2281 O O   . HOH B 2 .   ? -6.17250  14.48237  11.52739 1.000 22.21290 ? 504 HOH A O   1 
HETATM 2282 O O   . HOH B 2 .   ? -8.10878  2.62357   36.88383 1.000 33.84010 ? 505 HOH A O   1 
HETATM 2283 O O   . HOH B 2 .   ? -6.09439  -28.69833 15.86051 1.000 22.24887 ? 506 HOH A O   1 
HETATM 2284 O O   . HOH B 2 .   ? -10.41247 -2.72866  -8.56251 1.000 39.96354 ? 507 HOH A O   1 
HETATM 2285 O O   . HOH B 2 .   ? 8.53132   -3.76595  17.37349 1.000 40.13456 ? 508 HOH A O   1 
HETATM 2286 O O   . HOH B 2 .   ? -2.61575  -18.01914 24.96789 1.000 13.43500 ? 509 HOH A O   1 
HETATM 2287 O O   . HOH B 2 .   ? -22.51010 -1.43297  3.46744  1.000 27.09394 ? 510 HOH A O   1 
HETATM 2288 O O   . HOH B 2 .   ? -25.65934 2.70772   24.25066 1.000 25.84504 ? 511 HOH A O   1 
HETATM 2289 O O   . HOH B 2 .   ? 9.517     -6.917    33.285   1.000 35.12622 ? 512 HOH A O   1 
HETATM 2290 O O   . HOH B 2 .   ? -9.21511  -22.13559 41.78721 1.000 36.13685 ? 513 HOH A O   1 
HETATM 2291 O O   . HOH B 2 .   ? -6.91688  -3.65854  31.78716 1.000 14.21635 ? 514 HOH A O   1 
HETATM 2292 O O   . HOH B 2 .   ? -9.02701  -22.38382 22.32332 1.000 18.67973 ? 515 HOH A O   1 
HETATM 2293 O O   . HOH B 2 .   ? -1.63953  6.38189   11.49673 1.000 45.66526 ? 516 HOH A O   1 
HETATM 2294 O O   . HOH B 2 .   ? -16.81266 10.00605  21.36106 1.000 33.27066 ? 517 HOH A O   1 
HETATM 2295 O O   . HOH B 2 .   ? -15.65542 -0.12307  38.75586 1.000 18.70784 ? 518 HOH A O   1 
HETATM 2296 O O   . HOH B 2 .   ? 5.88526   -11.77930 21.62966 1.000 39.44854 ? 519 HOH A O   1 
HETATM 2297 O O   . HOH B 2 .   ? -25.38319 4.53311   14.88005 1.000 45.95933 ? 520 HOH A O   1 
HETATM 2298 O O   . HOH B 2 .   ? -17.13866 -14.23570 7.48753  1.000 37.53099 ? 521 HOH A O   1 
HETATM 2299 O O   . HOH B 2 .   ? -13.34361 -9.25060  13.62395 1.000 18.49805 ? 522 HOH A O   1 
HETATM 2300 O O   . HOH B 2 .   ? -2.74771  3.22827   42.72149 1.000 44.27701 ? 523 HOH A O   1 
HETATM 2301 O O   . HOH B 2 .   ? -3.25302  -14.97860 28.68142 1.000 32.80275 ? 524 HOH A O   1 
HETATM 2302 O O   . HOH B 2 .   ? -3.22919  4.18345   11.52935 1.000 22.96023 ? 525 HOH A O   1 
HETATM 2303 O O   . HOH B 2 .   ? -15.74169 -10.40755 0.34856  1.000 42.58835 ? 526 HOH A O   1 
HETATM 2304 O O   . HOH B 2 .   ? -33.82056 -6.45408  16.57211 1.000 39.69314 ? 527 HOH A O   1 
HETATM 2305 O O   . HOH B 2 .   ? -20.25989 -16.73370 15.56029 1.000 47.86242 ? 528 HOH A O   1 
HETATM 2306 O O   . HOH B 2 .   ? -3.45604  2.31533   34.82737 1.000 20.88980 ? 529 HOH A O   1 
HETATM 2307 O O   . HOH B 2 .   ? -21.78832 -19.70729 50.74237 1.000 46.62044 ? 530 HOH A O   1 
HETATM 2308 O O   . HOH B 2 .   ? -0.03810  -9.95816  26.93812 1.000 24.46114 ? 531 HOH A O   1 
HETATM 2309 O O   . HOH B 2 .   ? -8.50516  -13.81755 26.64259 1.000 31.60166 ? 532 HOH A O   1 
HETATM 2310 O O   . HOH B 2 .   ? -3.19548  -12.36812 45.52976 1.000 26.37431 ? 533 HOH A O   1 
HETATM 2311 O O   . HOH B 2 .   ? 3.60442   3.05512   27.93367 1.000 37.87021 ? 534 HOH A O   1 
HETATM 2312 O O   . HOH B 2 .   ? 3.50642   -2.67171  15.60111 1.000 23.05753 ? 535 HOH A O   1 
HETATM 2313 O O   . HOH B 2 .   ? -5.40831  2.84807   36.95312 1.000 41.63175 ? 536 HOH A O   1 
HETATM 2314 O O   . HOH B 2 .   ? -3.83395  -7.35839  27.75364 1.000 28.11423 ? 537 HOH A O   1 
HETATM 2315 O O   . HOH B 2 .   ? -12.17902 11.40183  26.39556 1.000 50.33062 ? 538 HOH A O   1 
HETATM 2316 O O   . HOH B 2 .   ? -24.42611 2.86043   4.11801  1.000 41.79799 ? 539 HOH A O   1 
HETATM 2317 O O   . HOH B 2 .   ? 1.11588   -13.59813 39.29292 1.000 27.49330 ? 540 HOH A O   1 
HETATM 2318 O O   . HOH B 2 .   ? -22.23384 -6.09882  27.83772 1.000 46.14593 ? 541 HOH A O   1 
HETATM 2319 O O   . HOH B 2 .   ? -18.72640 -14.79851 14.82939 1.000 33.41602 ? 542 HOH A O   1 
HETATM 2320 O O   . HOH B 2 .   ? -17.14477 12.50403  11.37106 1.000 50.42212 ? 543 HOH A O   1 
HETATM 2321 O O   . HOH B 2 .   ? 3.36684   -6.50729  9.61314  1.000 31.70705 ? 544 HOH A O   1 
HETATM 2322 O O   . HOH B 2 .   ? -23.46686 -7.02812  39.14433 1.000 26.57078 ? 545 HOH A O   1 
HETATM 2323 O O   . HOH B 2 .   ? -7.44369  -20.84856 39.84832 1.000 34.89391 ? 546 HOH A O   1 
HETATM 2324 O O   . HOH B 2 .   ? -22.31116 -9.54012  4.99527  1.000 41.81858 ? 547 HOH A O   1 
HETATM 2325 O O   . HOH B 2 .   ? 5.12893   -13.93646 14.01591 1.000 43.05106 ? 548 HOH A O   1 
HETATM 2326 O O   . HOH B 2 .   ? -6.052    -16.835   28.377   1.000 30.05402 ? 549 HOH A O   1 
HETATM 2327 O O   . HOH B 2 .   ? 0.03090   -24.72324 12.52778 1.000 23.46687 ? 550 HOH A O   1 
HETATM 2328 O O   . HOH B 2 .   ? -27.33864 -8.53781  14.61691 1.000 25.61345 ? 551 HOH A O   1 
HETATM 2329 O O   . HOH B 2 .   ? -7.10635  17.15417  12.02104 1.000 20.63921 ? 552 HOH A O   1 
HETATM 2330 O O   . HOH B 2 .   ? 3.18918   -12.88738 33.06773 1.000 39.36605 ? 553 HOH A O   1 
HETATM 2331 O O   . HOH B 2 .   ? -3.33924  -10.80931 29.72946 1.000 17.98403 ? 554 HOH A O   1 
HETATM 2332 O O   . HOH B 2 .   ? -5.37111  -7.87121  -4.17972 1.000 43.90094 ? 555 HOH A O   1 
HETATM 2333 O O   . HOH B 2 .   ? -15.67700 -10.29628 19.56161 1.000 21.12706 ? 556 HOH A O   1 
HETATM 2334 O O   . HOH B 2 .   ? -2.84207  -19.19650 10.12531 1.000 32.51315 ? 557 HOH A O   1 
HETATM 2335 O O   . HOH B 2 .   ? 0.77699   -6.11172  42.17782 1.000 45.09173 ? 558 HOH A O   1 
HETATM 2336 O O   . HOH B 2 .   ? 2.933     1.989     17.823   1.000 36.00601 ? 559 HOH A O   1 
HETATM 2337 O O   . HOH B 2 .   ? -15.75402 14.99283  8.43015  1.000 40.16199 ? 560 HOH A O   1 
HETATM 2338 O O   . HOH B 2 .   ? -9.92945  2.67465   32.50846 1.000 31.44998 ? 561 HOH A O   1 
HETATM 2339 O O   . HOH B 2 .   ? -9.77584  17.83369  9.58448  1.000 39.70348 ? 562 HOH A O   1 
HETATM 2340 O O   . HOH B 2 .   ? -8.05890  -14.86558 48.74577 1.000 42.20412 ? 563 HOH A O   1 
HETATM 2341 O O   . HOH B 2 .   ? -27.89484 3.65639   18.83887 1.000 26.69099 ? 564 HOH A O   1 
HETATM 2342 O O   . HOH B 2 .   ? -2.745    6.936     19.001   1.000 32.09168 ? 565 HOH A O   1 
HETATM 2343 O O   . HOH B 2 .   ? 0.75252   2.01317   11.94010 1.000 33.75417 ? 566 HOH A O   1 
HETATM 2344 O O   . HOH B 2 .   ? 6.39608   -5.67839  15.52307 1.000 35.43254 ? 567 HOH A O   1 
HETATM 2345 O O   . HOH B 2 .   ? -7.95847  -13.33407 -1.50187 1.000 43.31030 ? 568 HOH A O   1 
HETATM 2346 O O   . HOH B 2 .   ? -20.39407 -20.52552 28.46176 1.000 30.39098 ? 569 HOH A O   1 
HETATM 2347 O O   . HOH B 2 .   ? -17.77652 1.58170   -0.15786 1.000 32.86088 ? 570 HOH A O   1 
HETATM 2348 O O   . HOH B 2 .   ? -1.39495  -3.25699  29.23643 1.000 14.18519 ? 571 HOH A O   1 
HETATM 2349 O O   . HOH B 2 .   ? -4.03206  -22.67422 20.83788 1.000 15.96304 ? 572 HOH A O   1 
HETATM 2350 O O   . HOH B 2 .   ? -8.15532  8.46596   33.44066 1.000 36.17913 ? 573 HOH A O   1 
HETATM 2351 O O   . HOH B 2 .   ? -32.483   -0.284    19.690   1.000 38.06998 ? 574 HOH A O   1 
HETATM 2352 O O   . HOH B 2 .   ? -8.03631  -8.48906  28.76104 1.000 23.78336 ? 575 HOH A O   1 
HETATM 2353 O O   . HOH B 2 .   ? -6.01338  -7.50251  29.45183 1.000 21.73846 ? 576 HOH A O   1 
HETATM 2354 O O   . HOH B 2 .   ? -2.36161  -2.41143  44.38170 1.000 45.27151 ? 577 HOH A O   1 
HETATM 2355 O O   . HOH B 2 .   ? -17.06196 6.55911   -3.99260 1.000 47.10362 ? 578 HOH A O   1 
HETATM 2356 O O   . HOH B 2 .   ? -1.60465  -16.81048 8.92716  1.000 28.56307 ? 579 HOH A O   1 
HETATM 2357 O O   . HOH B 2 .   ? -14.29028 -12.27170 49.36008 1.000 33.19879 ? 580 HOH A O   1 
HETATM 2358 O O   . HOH B 2 .   ? -21.45959 5.02159   6.76619  1.000 32.92300 ? 581 HOH A O   1 
HETATM 2359 O O   . HOH B 2 .   ? 2.29195   -8.45316  32.20244 1.000 23.25832 ? 582 HOH A O   1 
HETATM 2360 O O   . HOH B 2 .   ? -16.52319 7.48590   4.59923  1.000 38.59426 ? 583 HOH A O   1 
HETATM 2361 O O   . HOH B 2 .   ? -16.01269 2.91414   28.97078 1.000 32.96454 ? 584 HOH A O   1 
HETATM 2362 O O   . HOH B 2 .   ? -16.30655 2.15034   -2.13238 1.000 40.07813 ? 585 HOH A O   1 
HETATM 2363 O O   . HOH B 2 .   ? 9.05234   -4.76211  45.73834 1.000 48.10423 ? 586 HOH A O   1 
HETATM 2364 O O   . HOH B 2 .   ? -23.13733 -18.74642 16.72142 1.000 46.15916 ? 587 HOH A O   1 
HETATM 2365 O O   . HOH B 2 .   ? 3.27375   0.01769   15.63966 1.000 27.25914 ? 588 HOH A O   1 
HETATM 2366 O O   . HOH B 2 .   ? -20.71381 -12.16193 28.55374 1.000 42.11250 ? 589 HOH A O   1 
HETATM 2367 O O   . HOH B 2 .   ? -2.50830  -21.84748 18.79356 1.000 18.30136 ? 590 HOH A O   1 
HETATM 2368 O O   . HOH B 2 .   ? 5.64844   -4.53023  27.73743 1.000 45.03375 ? 591 HOH A O   1 
HETATM 2369 O O   . HOH B 2 .   ? -12.08889 -23.63400 15.68414 1.000 37.50717 ? 592 HOH A O   1 
HETATM 2370 O O   . HOH B 2 .   ? -0.70486  3.38995   13.69349 1.000 23.56803 ? 593 HOH A O   1 
HETATM 2371 O O   . HOH B 2 .   ? -11.01738 -27.92285 37.17662 1.000 41.68555 ? 594 HOH A O   1 
HETATM 2372 O O   . HOH B 2 .   ? 0.16713   7.92099   30.29803 1.000 19.39044 ? 595 HOH A O   1 
HETATM 2373 O O   . HOH B 2 .   ? -19.12287 -0.89129  0.42879  1.000 47.46827 ? 596 HOH A O   1 
HETATM 2374 O O   . HOH B 2 .   ? -1.09770  9.70345   9.04937  1.000 45.85606 ? 597 HOH A O   1 
HETATM 2375 O O   . HOH B 2 .   ? -1.01044  10.16566  15.42921 1.000 21.04608 ? 598 HOH A O   1 
HETATM 2376 O O   . HOH B 2 .   ? -13.24986 9.51717   20.37648 1.000 42.79794 ? 599 HOH A O   1 
HETATM 2377 O O   . HOH B 2 .   ? -20.12283 -0.26798  33.22849 1.000 53.28280 ? 600 HOH A O   1 
HETATM 2378 O O   . HOH B 2 .   ? -16.52239 0.11243   29.83957 1.000 27.06747 ? 601 HOH A O   1 
HETATM 2379 O O   . HOH B 2 .   ? -5.01100  0.26245   49.87956 1.000 44.71911 ? 602 HOH A O   1 
HETATM 2380 O O   . HOH B 2 .   ? -15.14772 -25.22252 7.38748  1.000 45.75134 ? 603 HOH A O   1 
HETATM 2381 O O   . HOH B 2 .   ? 4.63762   -5.39415  24.49407 1.000 41.54385 ? 604 HOH A O   1 
HETATM 2382 O O   . HOH B 2 .   ? -15.56816 10.23322  16.80249 1.000 45.11197 ? 605 HOH A O   1 
HETATM 2383 O O   . HOH B 2 .   ? -36.33369 -5.65863  21.95251 1.000 44.66891 ? 606 HOH A O   1 
HETATM 2384 O O   . HOH B 2 .   ? -23.16769 -4.42440  27.26838 1.000 44.82167 ? 607 HOH A O   1 
HETATM 2385 O O   . HOH B 2 .   ? 4.01095   -13.37574 11.80357 1.000 49.46263 ? 608 HOH A O   1 
HETATM 2386 O O   . HOH B 2 .   ? -25.10795 -11.92760 48.20105 1.000 51.23333 ? 609 HOH A O   1 
HETATM 2387 O O   . HOH B 2 .   ? -0.42521  -0.06269  37.51397 1.000 29.61678 ? 610 HOH A O   1 
HETATM 2388 O O   . HOH B 2 .   ? 4.004     5.703     29.910   1.000 24.56495 ? 611 HOH A O   1 
HETATM 2389 O O   . HOH B 2 .   ? -9.30198  -1.65587  30.82848 1.000 33.73652 ? 612 HOH A O   1 
HETATM 2390 O O   . HOH B 2 .   ? -24.66019 -15.27073 33.35925 1.000 35.66818 ? 613 HOH A O   1 
HETATM 2391 O O   . HOH B 2 .   ? -16.697   -8.805    53.162   1.000 45.46227 ? 614 HOH A O   1 
HETATM 2392 O O   . HOH B 2 .   ? 0.13595   5.30476   31.66426 1.000 24.27709 ? 615 HOH A O   1 
HETATM 2393 O O   . HOH B 2 .   ? -5.31497  -19.00379 43.81779 1.000 35.25132 ? 616 HOH A O   1 
HETATM 2394 O O   . HOH B 2 .   ? -13.40224 11.46208  0.73392  1.000 43.05348 ? 617 HOH A O   1 
HETATM 2395 O O   . HOH B 2 .   ? -11.51616 -1.03805  31.17819 1.000 36.00225 ? 618 HOH A O   1 
HETATM 2396 O O   . HOH B 2 .   ? 0.93450   -16.63699 22.49213 1.000 16.71126 ? 619 HOH A O   1 
HETATM 2397 O O   . HOH B 2 .   ? -16.06668 -23.71846 23.20313 1.000 36.03087 ? 620 HOH A O   1 
HETATM 2398 O O   . HOH B 2 .   ? -19.84166 -13.39864 26.81508 1.000 34.28782 ? 621 HOH A O   1 
HETATM 2399 O O   . HOH B 2 .   ? 0.66163   -7.36525  26.26889 1.000 45.80423 ? 622 HOH A O   1 
HETATM 2400 O O   . HOH B 2 .   ? 1.279     13.554    24.978   1.000 47.75859 ? 623 HOH A O   1 
HETATM 2401 O O   . HOH B 2 .   ? -0.37478  -5.29080  28.39995 1.000 29.53838 ? 624 HOH A O   1 
HETATM 2402 O O   . HOH B 2 .   ? -2.55908  6.96927   1.54013  1.000 32.81567 ? 625 HOH A O   1 
HETATM 2403 O O   . HOH B 2 .   ? -27.081   4.203     32.364   1.000 57.97781 ? 626 HOH A O   1 
HETATM 2404 O O   . HOH B 2 .   ? 5.87708   -2.73988  22.82863 1.000 30.61819 ? 627 HOH A O   1 
HETATM 2405 O O   . HOH B 2 .   ? -17.60898 -20.62186 25.05269 1.000 31.84011 ? 628 HOH A O   1 
HETATM 2406 O O   . HOH B 2 .   ? -20.63555 -22.93927 23.13005 1.000 47.07798 ? 629 HOH A O   1 
HETATM 2407 O O   . HOH B 2 .   ? -0.526    13.647    28.071   1.000 32.34091 ? 630 HOH A O   1 
HETATM 2408 O O   . HOH B 2 .   ? -9.53848  -11.72745 50.80443 1.000 39.65390 ? 631 HOH A O   1 
HETATM 2409 O O   . HOH B 2 .   ? 8.408     -2.539    43.512   1.000 41.94412 ? 632 HOH A O   1 
HETATM 2410 O O   . HOH B 2 .   ? -11.81769 -26.63328 16.44331 1.000 41.85268 ? 633 HOH A O   1 
HETATM 2411 O O   . HOH B 2 .   ? -15.19233 1.40673   31.82421 1.000 38.59640 ? 634 HOH A O   1 
HETATM 2412 O O   . HOH B 2 .   ? -16.92655 -11.55795 50.35087 1.000 45.84160 ? 635 HOH A O   1 
HETATM 2413 O O   . HOH B 2 .   ? 10.362    -5.229    37.464   1.000 36.62617 ? 636 HOH A O   1 
HETATM 2414 O O   . HOH B 2 .   ? -28.165   3.551     30.254   1.000 48.16516 ? 637 HOH A O   1 
HETATM 2415 O O   . HOH B 2 .   ? -16.14391 -12.75134 52.07402 1.000 48.26500 ? 638 HOH A O   1 
HETATM 2416 O O   . HOH B 2 .   ? -23.55761 5.29494   4.67756  1.000 42.15850 ? 639 HOH A O   1 
HETATM 2417 O O   . HOH B 2 .   ? 10.991    -7.723    39.111   1.000 33.80711 ? 640 HOH A O   1 
HETATM 2418 O O   . HOH B 2 .   ? 7.34009   -2.75279  -0.96614 1.000 52.74734 ? 641 HOH A O   1 
HETATM 2419 O O   . HOH B 2 .   ? 3.87397   -10.44852 32.04961 1.000 31.12557 ? 642 HOH A O   1 
HETATM 2420 O O   . HOH B 2 .   ? 7.70673   -0.59586  -0.04236 1.000 51.33313 ? 643 HOH A O   1 
HETATM 2421 O O   . HOH B 2 .   ? 11.207    -6.982    45.617   1.000 51.59228 ? 644 HOH A O   1 
HETATM 2422 O O   . HOH B 2 .   ? 0.91752   -18.44024 20.37390 1.000 42.62150 ? 645 HOH A O   1 
HETATM 2423 O O   . HOH B 2 .   ? -36.94413 -16.73601 20.30517 1.000 46.93997 ? 646 HOH A O   1 
HETATM 2424 O O   . HOH B 2 .   ? -23.85417 -3.84623  2.76347  1.000 43.98223 ? 647 HOH A O   1 
HETATM 2425 O O   . HOH B 2 .   ? 4.57888   -3.25602  13.25732 1.000 31.91318 ? 648 HOH A O   1 
HETATM 2426 O O   . HOH B 2 .   ? -0.69778  -10.54246 29.62818 1.000 41.50559 ? 649 HOH A O   1 
HETATM 2427 O O   . HOH B 2 .   ? 3.530     -11.984   43.833   1.000 39.17107 ? 650 HOH A O   1 
HETATM 2428 O O   . HOH B 2 .   ? 7.63068   -5.11906  0.69899  1.000 47.31182 ? 651 HOH A O   1 
HETATM 2429 O O   . HOH B 2 .   ? 0.15295   -7.55177  30.20246 1.000 34.77477 ? 652 HOH A O   1 
HETATM 2430 O O   . HOH B 2 .   ? 11.297    -6.393    35.204   1.000 41.13379 ? 653 HOH A O   1 
HETATM 2431 O O   . HOH B 2 .   ? 10.102    -2.854    38.439   1.000 40.13729 ? 654 HOH A O   1 
HETATM 2432 O O   . HOH B 2 .   ? -11.02005 -24.11863 24.10194 1.000 40.65398 ? 655 HOH A O   1 
HETATM 2433 O O   . HOH B 2 .   ? -15.60462 -22.16211 25.65022 1.000 35.01152 ? 656 HOH A O   1 
HETATM 2434 O O   . HOH B 2 .   ? -23.59999 0.38517   1.33326  1.000 44.09313 ? 657 HOH A O   1 
HETATM 2435 O O   . HOH B 2 .   ? 1.54390   6.89641   1.16397  1.000 57.48823 ? 658 HOH A O   1 
HETATM 2436 O O   . HOH B 2 .   ? -30.165   -18.807   42.160   1.000 31.84247 ? 659 HOH A O   1 
HETATM 2437 O O   . HOH B 2 .   ? -8.10836  -17.08001 49.37968 1.000 44.02001 ? 660 HOH A O   1 
HETATM 2438 O O   . HOH B 2 .   ? -22.25167 -15.05712 31.65858 1.000 34.36681 ? 661 HOH A O   1 
HETATM 2439 O O   . HOH B 2 .   ? -23.29184 3.68299   27.52881 1.000 39.40830 ? 662 HOH A O   1 
HETATM 2440 O O   . HOH B 2 .   ? 1.04717   -16.28805 8.95495  1.000 45.71457 ? 663 HOH A O   1 
HETATM 2441 O O   . HOH B 2 .   ? -13.29843 -20.99310 45.38941 1.000 39.95722 ? 664 HOH A O   1 
HETATM 2442 O O   . HOH B 2 .   ? -36.64721 -17.53248 17.38039 1.000 43.83605 ? 665 HOH A O   1 
HETATM 2443 O O   . HOH B 2 .   ? 4.72732   -14.11496 21.30349 1.000 44.13626 ? 666 HOH A O   1 
HETATM 2444 O O   . HOH B 2 .   ? 3.053     8.856     9.456    1.000 36.30392 ? 667 HOH A O   1 
HETATM 2445 O O   . HOH B 2 .   ? -26.60375 -5.97223  7.48265  1.000 33.35168 ? 668 HOH A O   1 
HETATM 2446 O O   . HOH B 2 .   ? -16.38144 0.14526   41.63528 1.000 34.56784 ? 669 HOH A O   1 
HETATM 2447 O O   . HOH B 2 .   ? -19.00536 7.12950   6.78850  1.000 48.61136 ? 670 HOH A O   1 
HETATM 2448 O O   . HOH B 2 .   ? 0.82921   9.18967   -0.96408 1.000 50.87726 ? 671 HOH A O   1 
HETATM 2449 O O   . HOH B 2 .   ? 2.64102   8.62762   -0.70580 1.000 47.71671 ? 672 HOH A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLN A 35  ? 0.50929 0.57607 0.63703 -0.00613 0.07862  0.13070  35  GLN A N   
2    C CA  . GLN A 35  ? 0.46306 0.52265 0.59678 -0.00896 0.07548  0.12018  35  GLN A CA  
3    C C   . GLN A 35  ? 0.45823 0.52136 0.57927 -0.00481 0.07202  0.11673  35  GLN A C   
4    O O   . GLN A 35  ? 0.46867 0.54475 0.57145 -0.00223 0.07009  0.11530  35  GLN A O   
5    C CB  . GLN A 35  ? 0.49543 0.56080 0.62939 -0.01449 0.07399  0.11011  35  GLN A CB  
6    C CG  . GLN A 35  ? 0.64139 0.69782 0.79548 -0.02038 0.07491  0.10771  35  GLN A CG  
7    C CD  . GLN A 35  ? 0.71857 0.77939 0.87639 -0.02479 0.07129  0.09636  35  GLN A CD  
8    O OE1 . GLN A 35  ? 0.68581 0.75610 0.84074 -0.02622 0.07274  0.09421  35  GLN A OE1 
9    N NE2 . GLN A 35  ? 0.74874 0.80250 0.91347 -0.02704 0.06646  0.08875  35  GLN A NE2 
10   N N   . THR A 36  ? 0.37215 0.42274 0.50270 -0.00509 0.07118  0.11400  36  THR A N   
11   C CA  . THR A 36  ? 0.32254 0.37422 0.44054 -0.00109 0.06686  0.10785  36  THR A CA  
12   C C   . THR A 36  ? 0.22615 0.26853 0.34428 -0.00517 0.05971  0.09061  36  THR A C   
13   O O   . THR A 36  ? 0.28426 0.31694 0.41655 -0.01073 0.05883  0.08599  36  THR A O   
14   C CB  . THR A 36  ? 0.35151 0.39350 0.47343 0.00540  0.06815  0.11483  36  THR A CB  
15   O OG1 . THR A 36  ? 0.28710 0.30788 0.42639 0.00263  0.06861  0.11090  36  THR A OG1 
16   C CG2 . THR A 36  ? 0.39674 0.44810 0.51831 0.01029  0.07350  0.13242  36  THR A CG2 
17   N N   . SER A 37  ? 0.22733 0.27344 0.32947 -0.00292 0.05450  0.08147  37  SER A N   
18   C CA  . SER A 37  ? 0.25688 0.29506 0.35606 -0.00665 0.04720  0.06575  37  SER A CA  
19   C C   . SER A 37  ? 0.27651 0.31631 0.35827 -0.00313 0.04288  0.05810  37  SER A C   
20   O O   . SER A 37  ? 0.22416 0.27735 0.29234 0.00065  0.04457  0.06239  37  SER A O   
21   C CB  . SER A 37  ? 0.19960 0.24582 0.29768 -0.01131 0.04542  0.06057  37  SER A CB  
22   O OG  . SER A 37  ? 0.26419 0.30519 0.35618 -0.01400 0.03774  0.04690  37  SER A OG  
23   N N   . ASN A 38  ? 0.20098 0.22805 0.28265 -0.00530 0.03745  0.04634  38  ASN A N   
24   C CA  . ASN A 38  ? 0.13279 0.16125 0.19735 -0.00364 0.03294  0.03687  38  ASN A CA  
25   C C   . ASN A 38  ? 0.20776 0.23825 0.26212 -0.00846 0.02682  0.02569  38  ASN A C   
26   O O   . ASN A 38  ? 0.21860 0.24787 0.25893 -0.00874 0.02248  0.01639  38  ASN A O   
27   C CB  . ASN A 38  ? 0.16591 0.17935 0.23473 -0.00289 0.03165  0.03076  38  ASN A CB  
28   C CG  . ASN A 38  ? 0.24329 0.25400 0.32240 0.00345  0.03819  0.04241  38  ASN A CG  
29   O OD1 . ASN A 38  ? 0.23570 0.25981 0.31072 0.00888  0.04184  0.05376  38  ASN A OD1 
30   N ND2 . ASN A 38  ? 0.23526 0.22876 0.32814 0.00247  0.04000  0.04019  38  ASN A ND2 
31   N N   . ASP A 39  ? 0.13180 0.16566 0.19385 -0.01200 0.02689  0.02722  39  ASP A N   
32   C CA  . ASP A 39  ? 0.13811 0.17369 0.19366 -0.01568 0.02139  0.01840  39  ASP A CA  
33   C C   . ASP A 39  ? 0.16849 0.21794 0.21194 -0.01365 0.02482  0.02110  39  ASP A C   
34   O O   . ASP A 39  ? 0.11971 0.17691 0.17087 -0.01394 0.02964  0.02773  39  ASP A O   
35   C CB  . ASP A 39  ? 0.11560 0.14726 0.18906 -0.02080 0.01905  0.01761  39  ASP A CB  
36   C CG  . ASP A 39  ? 0.14520 0.17929 0.21416 -0.02368 0.01277  0.00992  39  ASP A CG  
37   O OD1 . ASP A 39  ? 0.17915 0.21352 0.23045 -0.02264 0.00939  0.00346  39  ASP A OD1 
38   O OD2 . ASP A 39  ? 0.17790 0.21381 0.26184 -0.02698 0.01128  0.01079  39  ASP A OD2 
39   N N   . TYR A 40  ? 0.19512 0.24762 0.21939 -0.01227 0.02310  0.01539  40  TYR A N   
40   C CA  . TYR A 40  ? 0.14596 0.21037 0.15690 -0.01159 0.02679  0.01591  40  TYR A CA  
41   C C   . TYR A 40  ? 0.16594 0.22722 0.16131 -0.01343 0.02199  0.00510  40  TYR A C   
42   O O   . TYR A 40  ? 0.15757 0.20978 0.14755 -0.01460 0.01597  -0.00230 40  TYR A O   
43   C CB  . TYR A 40  ? 0.15835 0.23429 0.15947 -0.00819 0.03228  0.02289  40  TYR A CB  
44   C CG  . TYR A 40  ? 0.22571 0.29989 0.21597 -0.00599 0.02942  0.01905  40  TYR A CG  
45   C CD1 . TYR A 40  ? 0.22712 0.30534 0.19778 -0.00701 0.02773  0.01099  40  TYR A CD1 
46   C CD2 . TYR A 40  ? 0.29243 0.36079 0.29277 -0.00292 0.02930  0.02345  40  TYR A CD2 
47   C CE1 . TYR A 40  ? 0.31615 0.39190 0.27898 -0.00505 0.02478  0.00702  40  TYR A CE1 
48   C CE2 . TYR A 40  ? 0.26808 0.33560 0.26039 -0.00032 0.02751  0.01979  40  TYR A CE2 
49   C CZ  . TYR A 40  ? 0.41182 0.48520 0.38485 -0.00155 0.02551  0.01169  40  TYR A CZ  
50   O OH  . TYR A 40  ? 0.46275 0.53670 0.42875 0.00077  0.02415  0.00779  40  TYR A OH  
51   N N   . ILE A 41  ? 0.16534 0.23349 0.15314 -0.01403 0.02538  0.00408  41  ILE A N   
52   C CA  . ILE A 41  ? 0.18106 0.24720 0.15060 -0.01538 0.02306  -0.00485 41  ILE A CA  
53   C C   . ILE A 41  ? 0.23020 0.29285 0.19379 -0.01234 0.02479  -0.00311 41  ILE A C   
54   O O   . ILE A 41  ? 0.21829 0.28567 0.18674 -0.01124 0.02972  0.00286  41  ILE A O   
55   C CB  . ILE A 41  ? 0.15084 0.20951 0.12526 -0.01713 0.01867  -0.00983 41  ILE A CB  
56   C CG1 . ILE A 41  ? 0.14079 0.20610 0.12710 -0.01646 0.02476  -0.00487 41  ILE A CG1 
57   C CG2 . ILE A 41  ? 0.29689 0.34536 0.28288 -0.01881 0.01015  -0.01216 41  ILE A CG2 
58   C CD1 . ILE A 41  ? 0.29966 0.36022 0.28961 -0.01679 0.02201  -0.00893 41  ILE A CD1 
59   N N   . ILE A 42  ? 0.17803 0.22882 0.13457 -0.01120 0.02019  -0.00780 42  ILE A N   
60   C CA  . ILE A 42  ? 0.20957 0.25938 0.16411 -0.01086 0.02106  -0.00780 42  ILE A CA  
61   C C   . ILE A 42  ? 0.21700 0.26195 0.17012 -0.01200 0.02065  -0.01177 42  ILE A C   
62   O O   . ILE A 42  ? 0.14733 0.18643 0.09899 -0.01276 0.01680  -0.01519 42  ILE A O   
63   C CB  . ILE A 42  ? 0.21056 0.26539 0.16404 -0.01225 0.01762  -0.00942 42  ILE A CB  
64   C CG1 . ILE A 42  ? 0.15864 0.21957 0.11299 -0.01023 0.01868  -0.00465 42  ILE A CG1 
65   C CG2 . ILE A 42  ? 0.18749 0.24797 0.14012 -0.01510 0.01827  -0.01138 42  ILE A CG2 
66   C CD1 . ILE A 42  ? 0.21762 0.28537 0.17211 -0.01087 0.01571  -0.00598 42  ILE A CD1 
67   N N   . GLY A 43  ? 0.14982 0.19656 0.10329 -0.01194 0.02525  -0.01092 43  GLY A N   
68   C CA  . GLY A 43  ? 0.23619 0.27777 0.18773 -0.01228 0.02612  -0.01426 43  GLY A CA  
69   C C   . GLY A 43  ? 0.20732 0.25110 0.15999 -0.01151 0.03288  -0.01294 43  GLY A C   
70   O O   . GLY A 43  ? 0.18697 0.23672 0.14167 -0.01151 0.03645  -0.00950 43  GLY A O   
71   N N   . LEU A 44  ? 0.19606 0.23490 0.14746 -0.01070 0.03504  -0.01551 44  LEU A N   
72   C CA  . LEU A 44  ? 0.16769 0.20831 0.12171 -0.00914 0.04262  -0.01455 44  LEU A CA  
73   C C   . LEU A 44  ? 0.19455 0.24056 0.16013 -0.00669 0.04812  -0.01055 44  LEU A C   
74   O O   . LEU A 44  ? 0.27784 0.32889 0.24917 -0.00899 0.04616  -0.01232 44  LEU A O   
75   C CB  . LEU A 44  ? 0.21697 0.25168 0.16747 -0.00885 0.04394  -0.01869 44  LEU A CB  
76   C CG  . LEU A 44  ? 0.23736 0.26872 0.18062 -0.01368 0.04022  -0.02307 44  LEU A CG  
77   C CD1 . LEU A 44  ? 0.30090 0.32424 0.24133 -0.01277 0.04208  -0.02626 44  LEU A CD1 
78   C CD2 . LEU A 44  ? 0.18966 0.22737 0.13088 -0.01780 0.04287  -0.02396 44  LEU A CD2 
79   N N   . ILE A 45  ? 0.16702 0.21790 0.13872 -0.00523 0.05526  -0.00713 45  ILE A N   
80   C CA  . ILE A 45  ? 0.16791 0.22989 0.15705 -0.00553 0.06159  -0.00450 45  ILE A CA  
81   C C   . ILE A 45  ? 0.24307 0.30732 0.23724 -0.00344 0.06696  -0.00681 45  ILE A C   
82   O O   . ILE A 45  ? 0.21460 0.27439 0.19883 -0.00191 0.06798  -0.00794 45  ILE A O   
83   C CB  . ILE A 45  ? 0.27378 0.34073 0.26962 -0.00562 0.06606  0.00218  45  ILE A CB  
84   C CG1 . ILE A 45  ? 0.40396 0.46974 0.39612 -0.00828 0.06124  0.00353  45  ILE A CG1 
85   C CG2 . ILE A 45  ? 0.20225 0.28197 0.22067 -0.00574 0.07109  0.00616  45  ILE A CG2 
86   C CD1 . ILE A 45  ? 0.44719 0.51669 0.44640 -0.01013 0.06606  0.00867  45  ILE A CD1 
87   N N   . LYS A 46  ? 0.21606 0.28754 0.22859 -0.00384 0.07025  -0.00847 46  LYS A N   
88   C CA  . LYS A 46  ? 0.28904 0.36141 0.31194 -0.00178 0.07670  -0.01139 46  LYS A CA  
89   C C   . LYS A 46  ? 0.21772 0.30168 0.26676 -0.00139 0.08080  -0.00749 46  LYS A C   
90   O O   . LYS A 46  ? 0.19480 0.28421 0.25976 -0.00240 0.07781  -0.00397 46  LYS A O   
91   C CB  . LYS A 46  ? 0.29330 0.35611 0.31903 -0.00012 0.07740  -0.01712 46  LYS A CB  
92   C CG  . LYS A 46  ? 0.47755 0.52770 0.47725 -0.00144 0.07167  -0.02133 46  LYS A CG  
93   C CD  . LYS A 46  ? 0.53731 0.58317 0.52266 -0.00105 0.07195  -0.02159 46  LYS A CD  
94   C CE  . LYS A 46  ? 0.54141 0.57601 0.50843 -0.00186 0.06460  -0.02399 46  LYS A CE  
95   N NZ  . LYS A 46  ? 0.59612 0.62893 0.55400 -0.00432 0.06485  -0.02489 46  LYS A NZ  
96   N N   . LYS A 47  ? 0.25796 0.34475 0.31250 -0.00008 0.08688  -0.00792 47  LYS A N   
97   C CA  . LYS A 47  ? 0.28198 0.37738 0.36217 0.00104  0.09033  -0.00448 47  LYS A CA  
98   C C   . LYS A 47  ? 0.23067 0.32446 0.33687 0.00585  0.08853  -0.00315 47  LYS A C   
99   O O   . LYS A 47  ? 0.23285 0.31798 0.33692 0.00920  0.08905  -0.00653 47  LYS A O   
100  C CB  . LYS A 47  ? 0.32714 0.42445 0.40699 0.00174  0.09799  -0.00642 47  LYS A CB  
101  C CG  . LYS A 47  ? 0.45281 0.55922 0.55672 0.00260  0.10159  -0.00290 47  LYS A CG  
102  C CD  . LYS A 47  ? 0.51589 0.63146 0.62286 -0.00169 0.09740  0.00249  47  LYS A CD  
103  C CE  . LYS A 47  ? 0.58502 0.70812 0.71891 -0.00070 0.09899  0.00646  47  LYS A CE  
104  N NZ  . LYS A 47  ? 0.69088 0.81977 0.82456 -0.00164 0.10719  0.00524  47  LYS A NZ  
105  N N   . CYS A 48  ? 0.20702 0.30991 0.33825 0.00631  0.08466  0.00264  48  CYS A N   
106  C CA  . CYS A 48  ? 0.21676 0.32256 0.37632 0.01139  0.07886  0.00590  48  CYS A CA  
107  C C   . CYS A 48  ? 0.35361 0.46331 0.53119 0.01568  0.08405  0.00700  48  CYS A C   
108  O O   . CYS A 48  ? 0.33937 0.45655 0.52439 0.01333  0.08628  0.00933  48  CYS A O   
109  C CB  . CYS A 48  ? 0.26422 0.37610 0.43701 0.00827  0.06643  0.01116  48  CYS A CB  
110  S SG  . CYS A 48  ? 0.31366 0.43056 0.51611 0.01264  0.05325  0.01567  48  CYS A SG  
111  N N   . ASP A 49  ? 0.47203 0.57620 0.65674 0.02214  0.08638  0.00546  49  ASP A N   
112  C CA  . ASP A 49  ? 0.58956 0.69569 0.78963 0.02677  0.09301  0.00586  49  ASP A CA  
113  C C   . ASP A 49  ? 0.56396 0.68158 0.79627 0.03040  0.08484  0.01270  49  ASP A C   
114  O O   . ASP A 49  ? 0.61073 0.73522 0.85628 0.03101  0.08948  0.01398  49  ASP A O   
115  C CB  . ASP A 49  ? 0.65105 0.74450 0.84484 0.03246  0.09942  0.00175  49  ASP A CB  
116  C CG  . ASP A 49  ? 0.70592 0.78834 0.86625 0.02739  0.10770  -0.00598 49  ASP A CG  
117  O OD1 . ASP A 49  ? 0.72184 0.80895 0.86946 0.02145  0.11111  -0.00762 49  ASP A OD1 
118  O OD2 . ASP A 49  ? 0.69277 0.76233 0.83895 0.02907  0.10936  -0.00998 49  ASP A OD2 
119  N N   . ASP A 50  ? 0.54748 0.66785 0.79109 0.03207  0.07165  0.01684  50  ASP A N   
120  C CA  . ASP A 50  ? 0.59297 0.72424 0.86365 0.03466  0.06096  0.02323  50  ASP A CA  
121  C C   . ASP A 50  ? 0.50134 0.64184 0.77723 0.02715  0.05151  0.02598  50  ASP A C   
122  O O   . ASP A 50  ? 0.52507 0.67238 0.81544 0.02670  0.03801  0.03016  50  ASP A O   
123  C CB  . ASP A 50  ? 0.69034 0.81884 0.96927 0.04099  0.04965  0.02675  50  ASP A CB  
124  C CG  . ASP A 50  ? 0.75130 0.86818 1.02647 0.04922  0.05928  0.02472  50  ASP A CG  
125  O OD1 . ASP A 50  ? 0.78505 0.90439 1.07558 0.05458  0.06411  0.02681  50  ASP A OD1 
126  O OD2 . ASP A 50  ? 0.71684 0.81874 0.96747 0.04891  0.06115  0.02028  50  ASP A OD2 
127  N N   . CYS A 51  ? 0.40198 0.54182 0.66423 0.02082  0.05824  0.02366  51  CYS A N   
128  C CA  . CYS A 51  ? 0.33172 0.47739 0.59771 0.01371  0.05094  0.02614  51  CYS A CA  
129  C C   . CYS A 51  ? 0.45212 0.60706 0.73293 0.01204  0.05541  0.02831  51  CYS A C   
130  O O   . CYS A 51  ? 0.40765 0.56480 0.69408 0.01598  0.06481  0.02745  51  CYS A O   
131  C CB  . CYS A 51  ? 0.25546 0.39460 0.49840 0.00798  0.05409  0.02382  51  CYS A CB  
132  S SG  . CYS A 51  ? 0.29908 0.43039 0.52864 0.00659  0.04335  0.02204  51  CYS A SG  
133  N N   . GLU A 52  ? 0.53590 0.69567 0.82286 0.00583  0.04898  0.03066  52  GLU A N   
134  C CA  . GLU A 52  ? 0.57572 0.74486 0.87759 0.00321  0.05232  0.03281  52  GLU A CA  
135  C C   . GLU A 52  ? 0.55933 0.72772 0.85135 0.00247  0.06663  0.03124  52  GLU A C   
136  O O   . GLU A 52  ? 0.51069 0.67223 0.78197 -0.00066 0.07115  0.02983  52  GLU A O   
137  C CB  . GLU A 52  ? 0.55330 0.72437 0.85871 -0.00449 0.04419  0.03469  52  GLU A CB  
138  N N   . VAL A 53  ? 0.59567 0.77195 0.90214 0.00510  0.07318  0.03154  53  VAL A N   
139  C CA  . VAL A 53  ? 0.55563 0.73329 0.85426 0.00323  0.08584  0.02994  53  VAL A CA  
140  C C   . VAL A 53  ? 0.51867 0.69832 0.81299 -0.00453 0.08598  0.03240  53  VAL A C   
141  O O   . VAL A 53  ? 0.52898 0.71355 0.83760 -0.00799 0.07881  0.03539  53  VAL A O   
142  C CB  . VAL A 53  ? 0.55661 0.74375 0.87505 0.00723  0.09240  0.02979  53  VAL A CB  
143  C CG1 . VAL A 53  ? 0.57449 0.75699 0.89446 0.01536  0.09552  0.02721  53  VAL A CG1 
144  C CG2 . VAL A 53  ? 0.51574 0.71471 0.86008 0.00617  0.08456  0.03371  53  VAL A CG2 
145  N N   . SER A 54  ? 0.48168 0.65749 0.75571 -0.00760 0.09391  0.03120  54  SER A N   
146  C CA  . SER A 54  ? 0.47162 0.64802 0.73986 -0.01445 0.09482  0.03438  54  SER A CA  
147  C C   . SER A 54  ? 0.49727 0.67403 0.74659 -0.01701 0.10500  0.03312  54  SER A C   
148  O O   . SER A 54  ? 0.50362 0.67579 0.73424 -0.01516 0.10824  0.02951  54  SER A O   
149  C CB  . SER A 54  ? 0.42183 0.58969 0.68040 -0.01701 0.08636  0.03616  54  SER A CB  
150  O OG  . SER A 54  ? 0.36209 0.52845 0.61391 -0.02288 0.08831  0.03973  54  SER A OG  
151  N N   . THR A 55  ? 0.39366 0.57666 0.64744 -0.02197 0.10962  0.03601  55  THR A N   
152  C CA  . THR A 55  ? 0.44495 0.63050 0.68114 -0.02568 0.11825  0.03550  55  THR A CA  
153  C C   . THR A 55  ? 0.51751 0.69685 0.73521 -0.03044 0.11598  0.03888  55  THR A C   
154  O O   . THR A 55  ? 0.58191 0.76338 0.78205 -0.03418 0.12134  0.03887  55  THR A O   
155  C CB  . THR A 55  ? 0.51299 0.70949 0.76301 -0.02895 0.12543  0.03708  55  THR A CB  
156  O OG1 . THR A 55  ? 0.54991 0.74742 0.81428 -0.03292 0.12135  0.04209  55  THR A OG1 
157  C CG2 . THR A 55  ? 0.50001 0.70331 0.76847 -0.02367 0.12892  0.03368  55  THR A CG2 
158  N N   . SER A 56  ? 0.45580 0.62803 0.67803 -0.03044 0.10784  0.04184  56  SER A N   
159  C CA  . SER A 56  ? 0.40314 0.56821 0.61140 -0.03396 0.10565  0.04596  56  SER A CA  
160  C C   . SER A 56  ? 0.32127 0.47713 0.51567 -0.03108 0.09927  0.04433  56  SER A C   
161  O O   . SER A 56  ? 0.32045 0.47095 0.49845 -0.03286 0.09886  0.04665  56  SER A O   
162  C CB  . SER A 56  ? 0.30498 0.46873 0.52983 -0.03753 0.10254  0.05154  56  SER A CB  
163  O OG  . SER A 56  ? 0.34672 0.50927 0.58867 -0.03550 0.09454  0.05027  56  SER A OG  
164  N N   . LYS A 57  ? 0.27289 0.42727 0.47466 -0.02665 0.09432  0.04072  57  LYS A N   
165  C CA  . LYS A 57  ? 0.24625 0.39271 0.43567 -0.02417 0.08851  0.03869  57  LYS A CA  
166  C C   . LYS A 57  ? 0.21776 0.36440 0.39855 -0.01989 0.09055  0.03267  57  LYS A C   
167  O O   . LYS A 57  ? 0.26510 0.41663 0.45799 -0.01711 0.09358  0.03045  57  LYS A O   
168  C CB  . LYS A 57  ? 0.26528 0.40810 0.47038 -0.02373 0.07902  0.04005  57  LYS A CB  
169  C CG  . LYS A 57  ? 0.33748 0.47949 0.55539 -0.02836 0.07638  0.04507  57  LYS A CG  
170  C CD  . LYS A 57  ? 0.32011 0.45971 0.55268 -0.02896 0.06600  0.04415  57  LYS A CD  
171  C CE  . LYS A 57  ? 0.37483 0.51257 0.61998 -0.03461 0.06327  0.04777  57  LYS A CE  
172  N NZ  . LYS A 57  ? 0.47093 0.60699 0.72869 -0.03672 0.05229  0.04526  57  LYS A NZ  
173  N N   . THR A 58  ? 0.20617 0.34703 0.36655 -0.01931 0.08902  0.03015  58  THR A N   
174  C CA  . THR A 58  ? 0.21898 0.35769 0.36974 -0.01560 0.09017  0.02439  58  THR A CA  
175  C C   . THR A 58  ? 0.18450 0.31602 0.33352 -0.01347 0.08260  0.02368  58  THR A C   
176  O O   . THR A 58  ? 0.18970 0.31722 0.32877 -0.01573 0.07884  0.02560  58  THR A O   
177  C CB  . THR A 58  ? 0.20616 0.34646 0.33132 -0.01812 0.09525  0.02070  58  THR A CB  
178  O OG1 . THR A 58  ? 0.25741 0.40615 0.38504 -0.02078 0.10204  0.02137  58  THR A OG1 
179  C CG2 . THR A 58  ? 0.17628 0.31326 0.29125 -0.01438 0.09622  0.01505  58  THR A CG2 
180  N N   . PHE A 59  ? 0.16189 0.29200 0.32169 -0.00906 0.08045  0.02122  59  PHE A N   
181  C CA  . PHE A 59  ? 0.20724 0.33234 0.36930 -0.00761 0.07241  0.02080  59  PHE A CA  
182  C C   . PHE A 59  ? 0.17872 0.29721 0.31951 -0.00572 0.07445  0.01562  59  PHE A C   
183  O O   . PHE A 59  ? 0.14059 0.25770 0.27328 -0.00353 0.08078  0.01164  59  PHE A O   
184  C CB  . PHE A 59  ? 0.18022 0.30888 0.36878 -0.00455 0.06614  0.02198  59  PHE A CB  
185  C CG  . PHE A 59  ? 0.20718 0.34150 0.41506 -0.00783 0.06112  0.02642  59  PHE A CG  
186  C CD1 . PHE A 59  ? 0.32530 0.46640 0.54486 -0.00803 0.06670  0.02807  59  PHE A CD1 
187  C CD2 . PHE A 59  ? 0.17841 0.31086 0.39195 -0.01145 0.05106  0.02818  59  PHE A CD2 
188  C CE1 . PHE A 59  ? 0.30260 0.44871 0.53894 -0.01170 0.06278  0.03166  59  PHE A CE1 
189  C CE2 . PHE A 59  ? 0.26056 0.39681 0.48999 -0.01547 0.04687  0.03124  59  PHE A CE2 
190  C CZ  . PHE A 59  ? 0.28229 0.42557 0.52318 -0.01554 0.05294  0.03314  59  PHE A CZ  
191  N N   . PHE A 60  ? 0.16756 0.28149 0.29915 -0.00699 0.06910  0.01538  60  PHE A N   
192  C CA  . PHE A 60  ? 0.15657 0.26350 0.26555 -0.00612 0.07057  0.01007  60  PHE A CA  
193  C C   . PHE A 60  ? 0.21662 0.31429 0.32190 -0.00541 0.05751  0.00790  60  PHE A C   
194  O O   . PHE A 60  ? 0.20649 0.30420 0.32378 -0.00696 0.04785  0.01080  60  PHE A O   
195  C CB  . PHE A 60  ? 0.10889 0.21522 0.19125 -0.00985 0.07166  0.00947  60  PHE A CB  
196  C CG  . PHE A 60  ? 0.17100 0.28365 0.24608 -0.01208 0.07666  0.00969  60  PHE A CG  
197  C CD1 . PHE A 60  ? 0.18652 0.30034 0.24918 -0.01012 0.08038  0.00692  60  PHE A CD1 
198  C CD2 . PHE A 60  ? 0.19013 0.30684 0.27153 -0.01558 0.07754  0.01387  60  PHE A CD2 
199  C CE1 . PHE A 60  ? 0.27631 0.39700 0.33372 -0.01166 0.08373  0.00849  60  PHE A CE1 
200  C CE2 . PHE A 60  ? 0.29363 0.41672 0.36848 -0.01887 0.08262  0.01323  60  PHE A CE2 
201  C CZ  . PHE A 60  ? 0.22466 0.35067 0.28724 -0.01709 0.08442  0.01044  60  PHE A CZ  
202  N N   . TYR A 61  ? 0.09480 0.18342 0.18102 -0.00391 0.05659  0.00213  61  TYR A N   
203  C CA  . TYR A 61  ? 0.16270 0.24115 0.23520 -0.00476 0.04444  -0.00089 61  TYR A CA  
204  C C   . TYR A 61  ? 0.13784 0.21342 0.18416 -0.00776 0.04670  -0.00402 61  TYR A C   
205  O O   . TYR A 61  ? 0.15482 0.23066 0.18546 -0.00814 0.05584  -0.00757 61  TYR A O   
206  C CB  . TYR A 61  ? 0.19385 0.26367 0.26346 -0.00130 0.04058  -0.00437 61  TYR A CB  
207  C CG  . TYR A 61  ? 0.21999 0.29370 0.31612 0.00204  0.03472  -0.00021 61  TYR A CG  
208  C CD1 . TYR A 61  ? 0.11428 0.18941 0.22143 -0.00002 0.02155  0.00244  61  TYR A CD1 
209  C CD2 . TYR A 61  ? 0.21910 0.29609 0.33003 0.00698  0.04271  0.00088  61  TYR A CD2 
210  C CE1 . TYR A 61  ? 0.17812 0.25968 0.30996 0.00238  0.01549  0.00657  61  TYR A CE1 
211  C CE2 . TYR A 61  ? 0.25327 0.33621 0.39045 0.01066  0.03706  0.00550  61  TYR A CE2 
212  C CZ  . TYR A 61  ? 0.26977 0.35594 0.41714 0.00814  0.02293  0.00860  61  TYR A CZ  
213  O OH  . TYR A 61  ? 0.28628 0.38110 0.46010 0.01113  0.01658  0.01349  61  TYR A OH  
214  N N   . CYS A 62  ? 0.12623 0.19964 0.16858 -0.01015 0.03860  -0.00299 62  CYS A N   
215  C CA  . CYS A 62  ? 0.15160 0.22424 0.17247 -0.01234 0.03986  -0.00484 62  CYS A CA  
216  C C   . CYS A 62  ? 0.12563 0.18780 0.12856 -0.01316 0.03157  -0.01113 62  CYS A C   
217  O O   . CYS A 62  ? 0.14245 0.19835 0.15116 -0.01362 0.02128  -0.01200 62  CYS A O   
218  C CB  . CYS A 62  ? 0.10470 0.18174 0.13390 -0.01387 0.03839  0.00101  62  CYS A CB  
219  S SG  . CYS A 62  ? 0.17884 0.26841 0.22674 -0.01391 0.04918  0.00905  62  CYS A SG  
220  N N   . GLY A 63  ? 0.12145 0.18269 0.10211 -0.01426 0.03631  -0.01575 63  GLY A N   
221  C CA  . GLY A 63  ? 0.19977 0.25028 0.16260 -0.01526 0.02934  -0.02148 63  GLY A CA  
222  C C   . GLY A 63  ? 0.17332 0.21560 0.14006 -0.01439 0.02315  -0.02415 63  GLY A C   
223  O O   . GLY A 63  ? 0.14793 0.18949 0.12288 -0.01184 0.02743  -0.02339 63  GLY A O   
224  N N   . ILE A 64  ? 0.10920 0.14454 0.07184 -0.01608 0.01247  -0.02630 64  ILE A N   
225  C CA  . ILE A 64  ? 0.10637 0.13348 0.07193 -0.01552 0.00403  -0.02729 64  ILE A CA  
226  C C   . ILE A 64  ? 0.10085 0.13056 0.08797 -0.01577 -0.00493 -0.02308 64  ILE A C   
227  O O   . ILE A 64  ? 0.13961 0.16397 0.12697 -0.01704 -0.01494 -0.02397 64  ILE A O   
228  C CB  . ILE A 64  ? 0.13721 0.15416 0.08035 -0.01843 -0.00194 -0.03317 64  ILE A CB  
229  C CG1 . ILE A 64  ? 0.20150 0.21550 0.14741 -0.01825 -0.00676 -0.03065 64  ILE A CG1 
230  C CG2 . ILE A 64  ? 0.10649 0.11531 0.04387 -0.01323 0.00479  -0.02942 64  ILE A CG2 
231  C CD1 . ILE A 64  ? 0.21064 0.21080 0.15225 -0.01274 -0.01110 -0.02810 64  ILE A CD1 
232  N N   . LYS A 65  ? 0.09611 0.13454 0.10086 -0.01536 -0.00139 -0.01840 65  LYS A N   
233  C CA  . LYS A 65  ? 0.09820 0.13987 0.12407 -0.01682 -0.00902 -0.01497 65  LYS A CA  
234  C C   . LYS A 65  ? 0.16493 0.20875 0.20574 -0.01410 -0.01264 -0.01208 65  LYS A C   
235  O O   . LYS A 65  ? 0.16881 0.21476 0.21279 -0.00991 -0.00485 -0.01051 65  LYS A O   
236  C CB  . LYS A 65  ? 0.16950 0.21961 0.21162 -0.01710 -0.00298 -0.01001 65  LYS A CB  
237  C CG  . LYS A 65  ? 0.21329 0.26152 0.24552 -0.01932 -0.00131 -0.01095 65  LYS A CG  
238  C CD  . LYS A 65  ? 0.20976 0.26487 0.26038 -0.01980 0.00363  -0.00460 65  LYS A CD  
239  C CE  . LYS A 65  ? 0.19221 0.24270 0.23901 -0.02211 0.00182  -0.00504 65  LYS A CE  
240  N NZ  . LYS A 65  ? 0.23957 0.29370 0.30598 -0.02342 0.00514  0.00130  65  LYS A NZ  
241  N N   . ALA A 66  ? 0.10711 0.15085 0.15711 -0.01666 -0.02425 -0.01150 66  ALA A N   
242  C CA  . ALA A 66  ? 0.10910 0.15694 0.17480 -0.01392 -0.02971 -0.00753 66  ALA A CA  
243  C C   . ALA A 66  ? 0.15582 0.21644 0.25066 -0.01260 -0.02658 -0.00184 66  ALA A C   
244  O O   . ALA A 66  ? 0.17340 0.24038 0.28516 -0.00840 -0.02700 0.00245  66  ALA A O   
245  C CB  . ALA A 66  ? 0.13385 0.17847 0.19564 -0.01824 -0.04434 -0.00901 66  ALA A CB  
246  N N   . GLY A 67  ? 0.15149 0.21583 0.25273 -0.01601 -0.02294 -0.00146 67  GLY A N   
247  C CA  . GLY A 67  ? 0.18931 0.26543 0.31710 -0.01601 -0.01907 0.00370  67  GLY A CA  
248  C C   . GLY A 67  ? 0.16876 0.24833 0.29688 -0.01349 -0.00453 0.00575  67  GLY A C   
249  O O   . GLY A 67  ? 0.12737 0.20106 0.23565 -0.01371 0.00100  0.00326  67  GLY A O   
250  N N   . ALA A 68  ? 0.11419 0.20472 0.26493 -0.01148 0.00166  0.01040  68  ALA A N   
251  C CA  . ALA A 68  ? 0.16979 0.26517 0.32137 -0.00987 0.01600  0.01258  68  ALA A CA  
252  C C   . ALA A 68  ? 0.13500 0.23158 0.28698 -0.01442 0.01942  0.01506  68  ALA A C   
253  O O   . ALA A 68  ? 0.11346 0.20981 0.27557 -0.01885 0.01237  0.01606  68  ALA A O   
254  C CB  . ALA A 68  ? 0.14218 0.24920 0.31864 -0.00646 0.02231  0.01640  68  ALA A CB  
255  N N   . SER A 69  ? 0.12392 0.19754 0.18030 -0.00433 0.05224  0.00152  69  SER A N   
256  C CA  . SER A 69  ? 0.13532 0.20314 0.18648 -0.00780 0.05178  0.00290  69  SER A CA  
257  C C   . SER A 69  ? 0.17048 0.24032 0.21950 -0.00654 0.05962  0.00704  69  SER A C   
258  O O   . SER A 69  ? 0.17305 0.24764 0.22402 -0.00227 0.06545  0.00756  69  SER A O   
259  C CB  . SER A 69  ? 0.17472 0.23053 0.21355 -0.00721 0.04809  -0.00113 69  SER A CB  
260  O OG  . SER A 69  ? 0.14263 0.19739 0.18236 -0.00672 0.04279  -0.00547 69  SER A OG  
261  N N   . TYR A 70  ? 0.14654 0.21253 0.19131 -0.01005 0.06007  0.01003  70  TYR A N   
262  C CA  . TYR A 70  ? 0.16775 0.23505 0.20745 -0.00908 0.06805  0.01390  70  TYR A CA  
263  C C   . TYR A 70  ? 0.20503 0.26225 0.23244 -0.01193 0.06638  0.01522  70  TYR A C   
264  O O   . TYR A 70  ? 0.17440 0.22584 0.20220 -0.01534 0.05922  0.01466  70  TYR A O   
265  C CB  . TYR A 70  ? 0.12345 0.20375 0.17737 -0.01163 0.07250  0.02021  70  TYR A CB  
266  C CG  . TYR A 70  ? 0.16596 0.24676 0.22581 -0.01879 0.06825  0.02479  70  TYR A CG  
267  C CD1 . TYR A 70  ? 0.18257 0.26021 0.23607 -0.02197 0.07122  0.02972  70  TYR A CD1 
268  C CD2 . TYR A 70  ? 0.14593 0.22988 0.21720 -0.02273 0.06116  0.02434  70  TYR A CD2 
269  C CE1 . TYR A 70  ? 0.21898 0.29598 0.27859 -0.02873 0.06692  0.03439  70  TYR A CE1 
270  C CE2 . TYR A 70  ? 0.22116 0.30384 0.29775 -0.02939 0.05691  0.02797  70  TYR A CE2 
271  C CZ  . TYR A 70  ? 0.24814 0.32718 0.31962 -0.03233 0.05973  0.03322  70  TYR A CZ  
272  O OH  . TYR A 70  ? 0.21600 0.29278 0.29350 -0.03922 0.05510  0.03738  70  TYR A OH  
273  N N   . VAL A 71  ? 0.17484 0.22970 0.19103 -0.01032 0.07300  0.01688  71  VAL A N   
274  C CA  . VAL A 71  ? 0.21177 0.25908 0.21677 -0.01392 0.07213  0.02035  71  VAL A CA  
275  C C   . VAL A 71  ? 0.27678 0.33179 0.28255 -0.01574 0.08082  0.02695  71  VAL A C   
276  O O   . VAL A 71  ? 0.26611 0.32986 0.27596 -0.01211 0.08905  0.02699  71  VAL A O   
277  C CB  . VAL A 71  ? 0.28616 0.32164 0.27252 -0.01131 0.07090  0.01632  71  VAL A CB  
278  C CG1 . VAL A 71  ? 0.31178 0.34813 0.28708 -0.00743 0.08052  0.01540  71  VAL A CG1 
279  C CG2 . VAL A 71  ? 0.31167 0.33818 0.28939 -0.01581 0.06541  0.01984  71  VAL A CG2 
280  N N   . GLU A 72  ? 0.27355 0.32584 0.27669 -0.02131 0.07909  0.03295  72  GLU A N   
281  C CA  . GLU A 72  ? 0.34038 0.39965 0.34245 -0.02392 0.08735  0.04019  72  GLU A CA  
282  C C   . GLU A 72  ? 0.40639 0.46206 0.38962 -0.02000 0.09524  0.03824  72  GLU A C   
283  O O   . GLU A 72  ? 0.41408 0.45796 0.38166 -0.01857 0.09130  0.03406  72  GLU A O   
284  C CB  . GLU A 72  ? 0.32836 0.38345 0.33037 -0.03121 0.08252  0.04744  72  GLU A CB  
285  C CG  . GLU A 72  ? 0.50068 0.55473 0.51798 -0.03510 0.07316  0.04764  72  GLU A CG  
286  C CD  . GLU A 72  ? 0.67076 0.73797 0.70670 -0.03853 0.07570  0.05241  72  GLU A CD  
287  O OE1 . GLU A 72  ? 0.68174 0.76066 0.72136 -0.03653 0.08501  0.05483  72  GLU A OE1 
288  O OE2 . GLU A 72  ? 0.78427 0.85003 0.83155 -0.04325 0.06828  0.05366  72  GLU A OE2 
289  N N   . ASN A 73  ? 0.41984 0.48535 0.40463 -0.01860 0.10446  0.04015  73  ASN A N   
290  C CA  . ASN A 73  ? 0.42592 0.48823 0.39334 -0.01490 0.10962  0.03579  73  ASN A CA  
291  C C   . ASN A 73  ? 0.42908 0.48234 0.37548 -0.01879 0.11013  0.03969  73  ASN A C   
292  O O   . ASN A 73  ? 0.42633 0.47286 0.35473 -0.01590 0.11172  0.03497  73  ASN A O   
293  C CB  . ASN A 73  ? 0.48615 0.56118 0.46208 -0.01328 0.11632  0.03557  73  ASN A CB  
294  C CG  . ASN A 73  ? 0.50169 0.58184 0.49017 -0.00689 0.11639  0.02927  73  ASN A CG  
295  O OD1 . ASN A 73  ? 0.41671 0.49225 0.40911 -0.00442 0.11103  0.02559  73  ASN A OD1 
296  N ND2 . ASN A 73  ? 0.46070 0.55033 0.45565 -0.00431 0.12254  0.02842  73  ASN A ND2 
297  N N   . ASP A 74  ? 0.40194 0.45454 0.35046 -0.02558 0.10788  0.04859  74  ASP A N   
298  C CA  . ASP A 74  ? 0.47695 0.52052 0.40518 -0.02978 0.10725  0.05345  74  ASP A CA  
299  C C   . ASP A 74  ? 0.49037 0.51983 0.41264 -0.03125 0.09464  0.05143  74  ASP A C   
300  O O   . ASP A 74  ? 0.44136 0.46258 0.34995 -0.03550 0.09031  0.05605  74  ASP A O   
301  C CB  . ASP A 74  ? 0.44939 0.49936 0.38264 -0.03727 0.10861  0.06375  74  ASP A CB  
302  C CG  . ASP A 74  ? 0.51535 0.56722 0.46875 -0.04189 0.10155  0.06993  74  ASP A CG  
303  O OD1 . ASP A 74  ? 0.53811 0.58473 0.50018 -0.03994 0.09274  0.06415  74  ASP A OD1 
304  O OD2 . ASP A 74  ? 0.54967 0.60629 0.51010 -0.04800 0.10227  0.07800  74  ASP A OD2 
305  N N   . SER A 75  ? 0.50156 0.52916 0.43510 -0.02784 0.08829  0.04480  75  SER A N   
306  C CA  . SER A 75  ? 0.38238 0.39850 0.31356 -0.02852 0.07638  0.04214  75  SER A CA  
307  C C   . SER A 75  ? 0.37563 0.38095 0.28426 -0.02727 0.07466  0.03912  75  SER A C   
308  O O   . SER A 75  ? 0.36000 0.36484 0.25816 -0.02287 0.08068  0.03328  75  SER A O   
309  C CB  . SER A 75  ? 0.33780 0.35528 0.28342 -0.02459 0.07174  0.03496  75  SER A CB  
310  O OG  . SER A 75  ? 0.37960 0.38665 0.32111 -0.02425 0.06186  0.03158  75  SER A OG  
311  N N   . PRO A 76  ? 0.39414 0.39020 0.29574 -0.03119 0.06575  0.04306  76  PRO A N   
312  C CA  . PRO A 76  ? 0.44827 0.43363 0.32907 -0.03108 0.06166  0.04106  76  PRO A CA  
313  C C   . PRO A 76  ? 0.44451 0.42494 0.32593 -0.02632 0.05662  0.03193  76  PRO A C   
314  O O   . PRO A 76  ? 0.44538 0.41697 0.31068 -0.02646 0.05233  0.02989  76  PRO A O   
315  C CB  . PRO A 76  ? 0.47453 0.45318 0.35473 -0.03656 0.05201  0.04898  76  PRO A CB  
316  C CG  . PRO A 76  ? 0.45425 0.43721 0.35789 -0.03749 0.04843  0.05093  76  PRO A CG  
317  C CD  . PRO A 76  ? 0.39791 0.39271 0.31208 -0.03603 0.05835  0.04984  76  PRO A CD  
318  N N   . TYR A 77  ? 0.37298 0.35915 0.27220 -0.02280 0.05675  0.02713  77  TYR A N   
319  C CA  . TYR A 77  ? 0.38517 0.36780 0.28645 -0.01869 0.05223  0.01925  77  TYR A CA  
320  C C   . TYR A 77  ? 0.33976 0.32648 0.24010 -0.01360 0.06042  0.01281  77  TYR A C   
321  O O   . TYR A 77  ? 0.31299 0.29666 0.21396 -0.01027 0.05757  0.00652  77  TYR A O   
322  C CB  . TYR A 77  ? 0.24683 0.23194 0.16787 -0.01845 0.04530  0.01825  77  TYR A CB  
323  C CG  . TYR A 77  ? 0.28939 0.26857 0.21278 -0.02213 0.03621  0.02315  77  TYR A CG  
324  C CD1 . TYR A 77  ? 0.33633 0.30742 0.25307 -0.02199 0.02807  0.02190  77  TYR A CD1 
325  C CD2 . TYR A 77  ? 0.32458 0.30615 0.25795 -0.02580 0.03546  0.02939  77  TYR A CD2 
326  C CE1 . TYR A 77  ? 0.28903 0.25503 0.20976 -0.02473 0.01973  0.02686  77  TYR A CE1 
327  C CE2 . TYR A 77  ? 0.40477 0.37992 0.34135 -0.02867 0.02713  0.03395  77  TYR A CE2 
328  C CZ  . TYR A 77  ? 0.39512 0.36271 0.32573 -0.02778 0.01944  0.03270  77  TYR A CZ  
329  O OH  . TYR A 77  ? 0.52402 0.48558 0.45977 -0.03004 0.01111  0.03768  77  TYR A OH  
330  N N   . LEU A 78  ? 0.38472 0.37857 0.28462 -0.01295 0.07061  0.01480  78  LEU A N   
331  C CA  . LEU A 78  ? 0.35481 0.35337 0.25699 -0.00741 0.07891  0.00923  78  LEU A CA  
332  C C   . LEU A 78  ? 0.35561 0.34372 0.23929 -0.00439 0.07915  0.00240  78  LEU A C   
333  O O   . LEU A 78  ? 0.36003 0.34740 0.24784 0.00020  0.07991  -0.00381 78  LEU A O   
334  C CB  . LEU A 78  ? 0.32434 0.33285 0.22886 -0.00717 0.09049  0.01326  78  LEU A CB  
335  C CG  . LEU A 78  ? 0.32895 0.34472 0.24038 -0.00092 0.09846  0.00838  78  LEU A CG  
336  C CD1 . LEU A 78  ? 0.35647 0.37564 0.28523 0.00219  0.09542  0.00503  78  LEU A CD1 
337  C CD2 . LEU A 78  ? 0.42719 0.45660 0.34802 -0.00164 0.10530  0.01323  78  LEU A CD2 
338  N N   . ASN A 79  ? 0.34208 0.32156 0.20510 -0.00741 0.07783  0.00377  79  ASN A N   
339  C CA  . ASN A 79  ? 0.31773 0.28604 0.16149 -0.00550 0.07715  -0.00291 79  ASN A CA  
340  C C   . ASN A 79  ? 0.38509 0.34677 0.23283 -0.00538 0.06590  -0.00659 79  ASN A C   
341  O O   . ASN A 79  ? 0.38181 0.33722 0.22367 -0.00227 0.06557  -0.01342 79  ASN A O   
342  C CB  . ASN A 79  ? 0.34543 0.30680 0.16578 -0.00957 0.07718  -0.00011 79  ASN A CB  
343  C CG  . ASN A 79  ? 0.40516 0.37539 0.22440 -0.00734 0.08648  0.00015  79  ASN A CG  
344  O OD1 . ASN A 79  ? 0.43231 0.40843 0.26060 -0.00182 0.09215  -0.00511 79  ASN A OD1 
345  N ND2 . ASN A 79  ? 0.46036 0.43193 0.26893 -0.01179 0.08779  0.00671  79  ASN A ND2 
346  N N   . ASP A 80  ? 0.31702 0.28004 0.17535 -0.00869 0.05693  -0.00207 80  ASP A N   
347  C CA  . ASP A 80  ? 0.33463 0.29397 0.20006 -0.00827 0.04722  -0.00509 80  ASP A CA  
348  C C   . ASP A 80  ? 0.30678 0.27185 0.18764 -0.00368 0.04973  -0.01002 80  ASP A C   
349  O O   . ASP A 80  ? 0.28936 0.24994 0.17011 -0.00210 0.04527  -0.01469 80  ASP A O   
350  C CB  . ASP A 80  ? 0.39367 0.35463 0.27012 -0.01174 0.03864  0.00047  80  ASP A CB  
351  C CG  . ASP A 80  ? 0.49225 0.44583 0.35387 -0.01639 0.03307  0.00569  80  ASP A CG  
352  O OD1 . ASP A 80  ? 0.54492 0.49032 0.38726 -0.01727 0.03205  0.00347  80  ASP A OD1 
353  O OD2 . ASP A 80  ? 0.52758 0.48294 0.39662 -0.01936 0.02923  0.01210  80  ASP A OD2 
354  N N   . ILE A 81  ? 0.30772 0.28296 0.20212 -0.00202 0.05640  -0.00832 81  ILE A N   
355  C CA  . ILE A 81  ? 0.23922 0.22071 0.14840 0.00203  0.05858  -0.01194 81  ILE A CA  
356  C C   . ILE A 81  ? 0.32647 0.30311 0.22641 0.00642  0.06418  -0.01771 81  ILE A C   
357  O O   . ILE A 81  ? 0.30389 0.27808 0.20796 0.00884  0.06118  -0.02196 81  ILE A O   
358  C CB  . ILE A 81  ? 0.22447 0.21835 0.15013 0.00227  0.06391  -0.00817 81  ILE A CB  
359  C CG1 . ILE A 81  ? 0.31086 0.30784 0.24718 -0.00188 0.05720  -0.00382 81  ILE A CG1 
360  C CG2 . ILE A 81  ? 0.23193 0.23237 0.17082 0.00658  0.06682  -0.01135 81  ILE A CG2 
361  C CD1 . ILE A 81  ? 0.31397 0.32177 0.26501 -0.00322 0.06113  0.00050  81  ILE A CD1 
362  N N   . LYS A 82  ? 0.32530 0.30011 0.21243 0.00738  0.07243  -0.01786 82  LYS A N   
363  C CA  . LYS A 82  ? 0.33179 0.30250 0.21234 0.01190  0.07689  -0.02368 82  LYS A CA  
364  C C   . LYS A 82  ? 0.35746 0.31439 0.22357 0.01117  0.06993  -0.02883 82  LYS A C   
365  O O   . LYS A 82  ? 0.39591 0.34970 0.26566 0.01451  0.06877  -0.03368 82  LYS A O   
366  C CB  . LYS A 82  ? 0.41774 0.39185 0.29072 0.01232  0.08381  -0.02246 82  LYS A CB  
367  C CG  . LYS A 82  ? 0.47037 0.45883 0.35816 0.01241  0.09027  -0.01684 82  LYS A CG  
368  C CD  . LYS A 82  ? 0.68149 0.67735 0.57507 0.01695  0.09763  -0.01899 82  LYS A CD  
369  C CE  . LYS A 82  ? 0.74864 0.75298 0.63983 0.01470  0.10423  -0.01389 82  LYS A CE  
370  N NZ  . LYS A 82  ? 0.85774 0.85315 0.72600 0.01112  0.10329  -0.01356 82  LYS A NZ  
371  N N   . GLU A 83  ? 0.31439 0.26306 0.16476 0.00628  0.06451  -0.02712 83  GLU A N   
372  C CA  . GLU A 83  ? 0.36342 0.29964 0.20064 0.00451  0.05635  -0.03117 83  GLU A CA  
373  C C   . GLU A 83  ? 0.40059 0.33848 0.25372 0.00533  0.04902  -0.03258 83  GLU A C   
374  O O   . GLU A 83  ? 0.40541 0.33506 0.25356 0.00639  0.04597  -0.03760 83  GLU A O   
375  C CB  . GLU A 83  ? 0.36476 0.29577 0.18882 -0.00144 0.04881  -0.02691 83  GLU A CB  
376  C CG  . GLU A 83  ? 0.59632 0.51368 0.40249 -0.00385 0.04127  -0.03109 83  GLU A CG  
377  C CD  . GLU A 83  ? 0.90246 0.81606 0.69857 -0.00154 0.04591  -0.03603 83  GLU A CD  
378  O OE1 . GLU A 83  ? 1.04771 0.95308 0.83910 -0.00121 0.04137  -0.04127 83  GLU A OE1 
379  O OE2 . GLU A 83  ? 0.95626 0.87524 0.74934 -0.00026 0.05403  -0.03467 83  GLU A OE2 
380  N N   . SER A 84  ? 0.37426 0.32267 0.24619 0.00460  0.04641  -0.02819 84  SER A N   
381  C CA  . SER A 84  ? 0.32714 0.27872 0.21395 0.00509  0.04022  -0.02907 84  SER A CA  
382  C C   . SER A 84  ? 0.40060 0.35346 0.29445 0.00985  0.04518  -0.03314 84  SER A C   
383  O O   . SER A 84  ? 0.42576 0.37425 0.32146 0.01030  0.04052  -0.03601 84  SER A O   
384  C CB  . SER A 84  ? 0.30563 0.26784 0.20937 0.00353  0.03764  -0.02429 84  SER A CB  
385  O OG  . SER A 84  ? 0.45841 0.42884 0.37861 0.00608  0.03913  -0.02516 84  SER A OG  
386  N N   . ILE A 85  ? 0.40734 0.36631 0.30581 0.01325  0.05443  -0.03278 85  ILE A N   
387  C CA  . ILE A 85  ? 0.41899 0.37902 0.32451 0.01840  0.05972  -0.03604 85  ILE A CA  
388  C C   . ILE A 85  ? 0.50772 0.45515 0.39996 0.02015  0.05918  -0.04173 85  ILE A C   
389  O O   . ILE A 85  ? 0.49797 0.44160 0.39518 0.02223  0.05688  -0.04456 85  ILE A O   
390  C CB  . ILE A 85  ? 0.45515 0.42601 0.37005 0.02139  0.06855  -0.03350 85  ILE A CB  
391  C CG1 . ILE A 85  ? 0.41810 0.40126 0.34838 0.01937  0.06822  -0.02817 85  ILE A CG1 
392  C CG2 . ILE A 85  ? 0.50732 0.48039 0.43192 0.02657  0.07152  -0.03592 85  ILE A CG2 
393  C CD1 . ILE A 85  ? 0.34620 0.34133 0.28794 0.02127  0.07545  -0.02469 85  ILE A CD1 
394  N N   . SER A 86  ? 0.41323 0.35469 0.28959 0.01877  0.06039  -0.04296 86  SER A N   
395  C CA  . SER A 86  ? 0.42172 0.35171 0.28576 0.01964  0.05891  -0.04849 86  SER A CA  
396  C C   . SER A 86  ? 0.47334 0.39262 0.33168 0.01658  0.04936  -0.05087 86  SER A C   
397  O O   . SER A 86  ? 0.53588 0.44735 0.39293 0.01819  0.04757  -0.05523 86  SER A O   
398  C CB  . SER A 86  ? 0.52076 0.44683 0.36725 0.01768  0.06126  -0.04900 86  SER A CB  
399  O OG  . SER A 86  ? 0.59812 0.53442 0.44982 0.02028  0.07028  -0.04675 86  SER A OG  
400  N N   . ASN A 87  ? 0.39646 0.31517 0.25179 0.01199  0.04296  -0.04787 87  ASN A N   
401  C CA  . ASN A 87  ? 0.43871 0.34882 0.28978 0.00837  0.03289  -0.04931 87  ASN A CA  
402  C C   . ASN A 87  ? 0.42113 0.33869 0.29266 0.00921  0.02908  -0.04762 87  ASN A C   
403  O O   . ASN A 87  ? 0.48082 0.39380 0.35324 0.00644  0.02099  -0.04815 87  ASN A O   
404  C CB  . ASN A 87  ? 0.43845 0.34899 0.28372 0.00270  0.02513  -0.04499 87  ASN A CB  
405  C CG  . ASN A 87  ? 0.73266 0.63390 0.55535 0.00033  0.02574  -0.04631 87  ASN A CG  
406  O OD1 . ASN A 87  ? 0.82775 0.72310 0.64302 0.00186  0.02799  -0.05054 87  ASN A OD1 
407  N ND2 . ASN A 87  ? 0.83009 0.73360 0.64746 -0.00349 0.02267  -0.04128 87  ASN A ND2 
408  N N   . GLY A 88  ? 0.35759 0.28704 0.24516 0.01253  0.03476  -0.04521 88  GLY A N   
409  C CA  . GLY A 88  ? 0.39074 0.32851 0.29679 0.01319  0.03195  -0.04316 88  GLY A CA  
410  C C   . GLY A 88  ? 0.33348 0.27666 0.24677 0.00875  0.02344  -0.03967 88  GLY A C   
411  O O   . GLY A 88  ? 0.41638 0.36144 0.33850 0.00775  0.01858  -0.03913 88  GLY A O   
412  N N   . THR A 89  ? 0.28537 0.23120 0.19545 0.00617  0.02178  -0.03698 89  THR A N   
413  C CA  . THR A 89  ? 0.29141 0.24178 0.20860 0.00262  0.01401  -0.03392 89  THR A CA  
414  C C   . THR A 89  ? 0.26700 0.22932 0.19720 0.00288  0.01599  -0.03044 89  THR A C   
415  O O   . THR A 89  ? 0.23957 0.20485 0.16915 0.00429  0.02204  -0.02949 89  THR A O   
416  C CB  . THR A 89  ? 0.39999 0.34198 0.30338 -0.00110 0.00809  -0.03330 89  THR A CB  
417  O OG1 . THR A 89  ? 0.38373 0.32317 0.27585 -0.00087 0.01299  -0.03262 89  THR A OG1 
418  C CG2 . THR A 89  ? 0.43970 0.36950 0.33114 -0.00256 0.00382  -0.03697 89  THR A CG2 
419  N N   . PRO A 90  ? 0.28431 0.25352 0.22652 0.00141  0.01103  -0.02867 90  PRO A N   
420  C CA  . PRO A 90  ? 0.27480 0.25383 0.22867 0.00149  0.01233  -0.02634 90  PRO A CA  
421  C C   . PRO A 90  ? 0.25440 0.23097 0.20341 -0.00036 0.01057  -0.02374 90  PRO A C   
422  O O   . PRO A 90  ? 0.19579 0.16508 0.13534 -0.00238 0.00573  -0.02304 90  PRO A O   
423  C CB  . PRO A 90  ? 0.23129 0.21668 0.19691 0.00062  0.00768  -0.02613 90  PRO A CB  
424  C CG  . PRO A 90  ? 0.22029 0.19836 0.17917 -0.00141 0.00151  -0.02646 90  PRO A CG  
425  C CD  . PRO A 90  ? 0.23902 0.20733 0.18471 -0.00052 0.00422  -0.02887 90  PRO A CD  
426  N N   . ILE A 91  ? 0.19038 0.17257 0.14569 -0.00008 0.01391  -0.02189 91  ILE A N   
427  C CA  . ILE A 91  ? 0.15880 0.13917 0.11216 -0.00201 0.01200  -0.01853 91  ILE A CA  
428  C C   . ILE A 91  ? 0.14530 0.13337 0.11308 -0.00196 0.01209  -0.01760 91  ILE A C   
429  O O   . ILE A 91  ? 0.21084 0.20586 0.18767 -0.00068 0.01465  -0.01955 91  ILE A O   
430  C CB  . ILE A 91  ? 0.33511 0.31161 0.27707 -0.00250 0.01716  -0.01663 91  ILE A CB  
431  C CG1 . ILE A 91  ? 0.43372 0.41315 0.37533 0.00014  0.02489  -0.01886 91  ILE A CG1 
432  C CG2 . ILE A 91  ? 0.56241 0.52905 0.48756 -0.00438 0.01413  -0.01587 91  ILE A CG2 
433  C CD1 . ILE A 91  ? 0.40348 0.39264 0.35950 0.00103  0.02797  -0.01825 91  ILE A CD1 
434  N N   . LYS A 92  ? 0.16309 0.14919 0.13239 -0.00354 0.00900  -0.01459 92  LYS A N   
435  C CA  . LYS A 92  ? 0.17959 0.17060 0.16148 -0.00365 0.00873  -0.01419 92  LYS A CA  
436  C C   . LYS A 92  ? 0.19530 0.18720 0.17623 -0.00485 0.01355  -0.01169 92  LYS A C   
437  O O   . LYS A 92  ? 0.19919 0.18618 0.17055 -0.00639 0.01445  -0.00816 92  LYS A O   
438  C CB  . LYS A 92  ? 0.14986 0.13764 0.13616 -0.00432 0.00231  -0.01216 92  LYS A CB  
439  C CG  . LYS A 92  ? 0.16237 0.15360 0.16211 -0.00387 0.00170  -0.01301 92  LYS A CG  
440  C CD  . LYS A 92  ? 0.19474 0.18279 0.20068 -0.00339 -0.00455 -0.01138 92  LYS A CD  
441  C CE  . LYS A 92  ? 0.26321 0.25454 0.27306 -0.00172 -0.00764 -0.01367 92  LYS A CE  
442  N NZ  . LYS A 92  ? 0.22170 0.21091 0.23925 -0.00087 -0.01374 -0.01133 92  LYS A NZ  
443  N N   . ILE A 93  ? 0.17969 0.17835 0.17019 -0.00458 0.01654  -0.01318 93  ILE A N   
444  C CA  . ILE A 93  ? 0.18281 0.18406 0.17463 -0.00613 0.02108  -0.01046 93  ILE A CA  
445  C C   . ILE A 93  ? 0.22811 0.23077 0.23070 -0.00794 0.01873  -0.01001 93  ILE A C   
446  O O   . ILE A 93  ? 0.18593 0.19238 0.19678 -0.00717 0.01714  -0.01378 93  ILE A O   
447  C CB  . ILE A 93  ? 0.14662 0.15495 0.14078 -0.00467 0.02659  -0.01206 93  ILE A CB  
448  C CG1 . ILE A 93  ? 0.19982 0.20521 0.18401 -0.00230 0.02874  -0.01357 93  ILE A CG1 
449  C CG2 . ILE A 93  ? 0.14538 0.15794 0.14246 -0.00638 0.03143  -0.00850 93  ILE A CG2 
450  C CD1 . ILE A 93  ? 0.31516 0.32569 0.30459 -0.00003 0.02966  -0.01683 93  ILE A CD1 
451  N N   . TYR A 94  ? 0.14127 0.14039 0.14323 -0.01057 0.01848  -0.00548 94  TYR A N   
452  C CA  . TYR A 94  ? 0.16035 0.15905 0.17254 -0.01268 0.01602  -0.00506 94  TYR A CA  
453  C C   . TYR A 94  ? 0.20460 0.20907 0.22154 -0.01524 0.02016  -0.00305 94  TYR A C   
454  O O   . TYR A 94  ? 0.19013 0.19650 0.20170 -0.01626 0.02469  0.00105  94  TYR A O   
455  C CB  . TYR A 94  ? 0.17902 0.16926 0.18975 -0.01445 0.01172  -0.00051 94  TYR A CB  
456  C CG  . TYR A 94  ? 0.17569 0.16105 0.18732 -0.01214 0.00606  -0.00226 94  TYR A CG  
457  C CD1 . TYR A 94  ? 0.18908 0.17178 0.19096 -0.01099 0.00453  -0.00108 94  TYR A CD1 
458  C CD2 . TYR A 94  ? 0.14755 0.13094 0.17018 -0.01115 0.00221  -0.00512 94  TYR A CD2 
459  C CE1 . TYR A 94  ? 0.22953 0.20911 0.23400 -0.00918 -0.00111 -0.00188 94  TYR A CE1 
460  C CE2 . TYR A 94  ? 0.23482 0.21516 0.26044 -0.00852 -0.00248 -0.00632 94  TYR A CE2 
461  C CZ  . TYR A 94  ? 0.23082 0.20991 0.24802 -0.00772 -0.00433 -0.00421 94  TYR A CZ  
462  O OH  . TYR A 94  ? 0.27028 0.24758 0.29206 -0.00546 -0.00945 -0.00456 94  TYR A OH  
463  N N   . PHE A 95  ? 0.14587 0.15323 0.17287 -0.01652 0.01857  -0.00586 95  PHE A N   
464  C CA  . PHE A 95  ? 0.13175 0.14525 0.16505 -0.01970 0.02122  -0.00378 95  PHE A CA  
465  C C   . PHE A 95  ? 0.20451 0.21311 0.24458 -0.02386 0.01778  -0.00152 95  PHE A C   
466  O O   . PHE A 95  ? 0.14768 0.14921 0.19053 -0.02346 0.01308  -0.00429 95  PHE A O   
467  C CB  . PHE A 95  ? 0.16528 0.18696 0.20398 -0.01876 0.02186  -0.00857 95  PHE A CB  
468  C CG  . PHE A 95  ? 0.15242 0.17808 0.18572 -0.01486 0.02470  -0.01039 95  PHE A CG  
469  C CD1 . PHE A 95  ? 0.09820 0.12879 0.12894 -0.01393 0.03000  -0.00724 95  PHE A CD1 
470  C CD2 . PHE A 95  ? 0.22494 0.24908 0.25620 -0.01206 0.02227  -0.01508 95  PHE A CD2 
471  C CE1 . PHE A 95  ? 0.13567 0.16811 0.16169 -0.01023 0.03233  -0.00912 95  PHE A CE1 
472  C CE2 . PHE A 95  ? 0.12827 0.15502 0.15480 -0.00900 0.02433  -0.01625 95  PHE A CE2 
473  C CZ  . PHE A 95  ? 0.16416 0.19423 0.18792 -0.00807 0.02909  -0.01349 95  PHE A CZ  
474  N N   . ASP A 96  ? 0.16969 0.18211 0.21315 -0.02777 0.02030  0.00373  96  ASP A N   
475  C CA  . ASP A 96  ? 0.18044 0.18877 0.23134 -0.03283 0.01710  0.00678  96  ASP A CA  
476  C C   . ASP A 96  ? 0.20146 0.20844 0.26007 -0.03375 0.01266  0.00016  96  ASP A C   
477  O O   . ASP A 96  ? 0.19334 0.20841 0.25532 -0.03403 0.01368  -0.00310 96  ASP A O   
478  C CB  . ASP A 96  ? 0.16427 0.18055 0.21899 -0.03697 0.02140  0.01345  96  ASP A CB  
479  C CG  . ASP A 96  ? 0.27171 0.28295 0.33285 -0.04303 0.01830  0.01887  96  ASP A CG  
480  O OD1 . ASP A 96  ? 0.22272 0.22629 0.28942 -0.04479 0.01236  0.01537  96  ASP A OD1 
481  O OD2 . ASP A 96  ? 0.25532 0.27031 0.31602 -0.04611 0.02216  0.02673  96  ASP A OD2 
482  N N   . GLU A 97  ? 0.21156 0.20806 0.27283 -0.03423 0.00764  -0.00185 97  GLU A N   
483  C CA  . GLU A 97  ? 0.21018 0.20395 0.27730 -0.03477 0.00388  -0.00936 97  GLU A CA  
484  C C   . GLU A 97  ? 0.22911 0.22655 0.30315 -0.04080 0.00279  -0.00846 97  GLU A C   
485  O O   . GLU A 97  ? 0.20853 0.20709 0.28526 -0.04179 0.00059  -0.01501 97  GLU A O   
486  C CB  . GLU A 97  ? 0.33980 0.32064 0.40942 -0.03343 -0.00082 -0.01167 97  GLU A CB  
487  C CG  . GLU A 97  ? 0.46762 0.44735 0.53303 -0.02715 -0.00063 -0.01553 97  GLU A CG  
488  C CD  . GLU A 97  ? 0.58513 0.55348 0.65514 -0.02480 -0.00500 -0.01794 97  GLU A CD  
489  O OE1 . GLU A 97  ? 0.62504 0.58439 0.69991 -0.02795 -0.00833 -0.01434 97  GLU A OE1 
490  O OE2 . GLU A 97  ? 0.44137 0.41009 0.51108 -0.01975 -0.00508 -0.02305 97  GLU A OE2 
491  N N   . ASN A 98  ? 0.26114 0.26123 0.33773 -0.04514 0.00437  -0.00015 98  ASN A N   
492  C CA  . ASN A 98  ? 0.33043 0.33545 0.41513 -0.05156 0.00306  0.00203  98  ASN A CA  
493  C C   . ASN A 98  ? 0.30216 0.32244 0.38821 -0.05169 0.00782  0.00475  98  ASN A C   
494  O O   . ASN A 98  ? 0.23418 0.26131 0.32790 -0.05665 0.00656  0.00639  98  ASN A O   
495  C CB  . ASN A 98  ? 0.31011 0.30957 0.39948 -0.05716 0.00157  0.01035  98  ASN A CB  
496  C CG  . ASN A 98  ? 0.35063 0.33415 0.44173 -0.05786 -0.00439 0.00783  98  ASN A CG  
497  O OD1 . ASN A 98  ? 0.39925 0.37681 0.49358 -0.05852 -0.00877 0.00009  98  ASN A OD1 
498  N ND2 . ASN A 98  ? 0.26171 0.23790 0.35033 -0.05750 -0.00462 0.01418  98  ASN A ND2 
499  N N   . GLU A 99  ? 0.26715 0.29248 0.34637 -0.04627 0.01294  0.00542  99  GLU A N   
500  C CA  . GLU A 99  ? 0.26018 0.29906 0.34110 -0.04509 0.01799  0.00793  99  GLU A CA  
501  C C   . GLU A 99  ? 0.19030 0.23055 0.26285 -0.03824 0.02090  0.00376  99  GLU A C   
502  O O   . GLU A 99  ? 0.21379 0.25287 0.27927 -0.03494 0.02511  0.00646  99  GLU A O   
503  C CB  . GLU A 99  ? 0.21977 0.26429 0.30302 -0.04732 0.02321  0.01717  99  GLU A CB  
504  C CG  . GLU A 99  ? 0.26861 0.32754 0.35620 -0.04573 0.02891  0.02000  99  GLU A CG  
505  C CD  . GLU A 99  ? 0.37427 0.44001 0.46560 -0.04813 0.03486  0.02903  99  GLU A CD  
506  O OE1 . GLU A 99  ? 0.28449 0.34330 0.37383 -0.05161 0.03412  0.03345  99  GLU A OE1 
507  O OE2 . GLU A 99  ? 0.35199 0.43027 0.44869 -0.04641 0.04046  0.03198  99  GLU A OE2 
508  N N   . PRO A 100 ? 0.19043 0.23270 0.26302 -0.03654 0.01839  -0.00284 100 PRO A N   
509  C CA  . PRO A 100 ? 0.19616 0.23789 0.26133 -0.03074 0.01971  -0.00732 100 PRO A CA  
510  C C   . PRO A 100 ? 0.17673 0.22549 0.23897 -0.02706 0.02560  -0.00395 100 PRO A C   
511  O O   . PRO A 100 ? 0.17889 0.22474 0.23359 -0.02256 0.02707  -0.00613 100 PRO A O   
512  C CB  . PRO A 100 ? 0.26107 0.30637 0.32859 -0.03139 0.01623  -0.01341 100 PRO A CB  
513  C CG  . PRO A 100 ? 0.27443 0.31631 0.34775 -0.03709 0.01170  -0.01442 100 PRO A CG  
514  C CD  . PRO A 100 ? 0.23514 0.27919 0.31394 -0.04078 0.01350  -0.00652 100 PRO A CD  
515  N N   . GLU A 101 ? 0.14517 0.20286 0.21396 -0.02897 0.02892  0.00130  101 GLU A N   
516  C CA  . GLU A 101 ? 0.12968 0.19407 0.19716 -0.02500 0.03521  0.00412  101 GLU A CA  
517  C C   . GLU A 101 ? 0.18967 0.24845 0.24852 -0.02319 0.03982  0.00720  101 GLU A C   
518  O O   . GLU A 101 ? 0.20579 0.26630 0.25950 -0.01894 0.04508  0.00761  101 GLU A O   
519  C CB  . GLU A 101 ? 0.13458 0.21168 0.21396 -0.02726 0.03765  0.00912  101 GLU A CB  
520  C CG  . GLU A 101 ? 0.27089 0.35483 0.35794 -0.02929 0.03275  0.00681  101 GLU A CG  
521  C CD  . GLU A 101 ? 0.36179 0.44147 0.45165 -0.03540 0.02581  0.00444  101 GLU A CD  
522  O OE1 . GLU A 101 ? 0.24375 0.32533 0.33454 -0.03670 0.02111  0.00021  101 GLU A OE1 
523  O OE2 . GLU A 101 ? 0.29511 0.36921 0.38586 -0.03907 0.02499  0.00683  101 GLU A OE2 
524  N N   . ARG A 102 ? 0.18451 0.23599 0.24131 -0.02659 0.03764  0.00943  102 ARG A N   
525  C CA  . ARG A 102 ? 0.19974 0.24689 0.24808 -0.02623 0.04176  0.01386  102 ARG A CA  
526  C C   . ARG A 102 ? 0.15341 0.18937 0.18967 -0.02347 0.03910  0.01066  102 ARG A C   
527  O O   . ARG A 102 ? 0.15146 0.18010 0.18827 -0.02456 0.03305  0.00817  102 ARG A O   
528  C CB  . ARG A 102 ? 0.23007 0.27634 0.28347 -0.03220 0.04092  0.02019  102 ARG A CB  
529  C CG  . ARG A 102 ? 0.23524 0.27692 0.27859 -0.03272 0.04477  0.02566  102 ARG A CG  
530  C CD  . ARG A 102 ? 0.26144 0.30279 0.31063 -0.03929 0.04388  0.03317  102 ARG A CD  
531  N NE  . ARG A 102 ? 0.36370 0.39972 0.40148 -0.04022 0.04666  0.03870  102 ARG A NE  
532  C CZ  . ARG A 102 ? 0.42798 0.45316 0.46175 -0.04311 0.04120  0.04146  102 ARG A CZ  
533  N NH1 . ARG A 102 ? 0.36236 0.38035 0.40348 -0.04484 0.03323  0.03860  102 ARG A NH1 
534  N NH2 . ARG A 102 ? 0.40991 0.43126 0.43217 -0.04425 0.04374  0.04719  102 ARG A NH2 
535  N N   . ILE A 103 ? 0.20077 0.23547 0.22658 -0.01982 0.04358  0.01061  103 ILE A N   
536  C CA  . ILE A 103 ? 0.16819 0.19274 0.18176 -0.01796 0.04092  0.00881  103 ILE A CA  
537  C C   . ILE A 103 ? 0.22833 0.24644 0.23657 -0.02160 0.03976  0.01459  103 ILE A C   
538  O O   . ILE A 103 ? 0.18636 0.20777 0.19202 -0.02350 0.04512  0.01995  103 ILE A O   
539  C CB  . ILE A 103 ? 0.17764 0.20186 0.18043 -0.01356 0.04576  0.00670  103 ILE A CB  
540  C CG1 . ILE A 103 ? 0.11838 0.14787 0.12680 -0.01002 0.04602  0.00167  103 ILE A CG1 
541  C CG2 . ILE A 103 ? 0.18247 0.19613 0.17184 -0.01275 0.04227  0.00566  103 ILE A CG2 
542  C CD1 . ILE A 103 ? 0.15197 0.18256 0.15357 -0.00579 0.05205  0.00021  103 ILE A CD1 
543  N N   . ILE A 104 ? 0.22029 0.22969 0.22752 -0.02257 0.03296  0.01407  104 ILE A N   
544  C CA  . ILE A 104 ? 0.17440 0.17698 0.17658 -0.02607 0.03098  0.02049  104 ILE A CA  
545  C C   . ILE A 104 ? 0.23896 0.23406 0.22652 -0.02438 0.02928  0.02091  104 ILE A C   
546  O O   . ILE A 104 ? 0.22709 0.21808 0.20591 -0.02711 0.02959  0.02702  104 ILE A O   
547  C CB  . ILE A 104 ? 0.20172 0.19860 0.21417 -0.02895 0.02397  0.02133  104 ILE A CB  
548  C CG1 . ILE A 104 ? 0.19431 0.18582 0.20911 -0.02557 0.01791  0.01505  104 ILE A CG1 
549  C CG2 . ILE A 104 ? 0.23558 0.23886 0.26101 -0.03193 0.02497  0.02136  104 ILE A CG2 
550  C CD1 . ILE A 104 ? 0.21701 0.20130 0.24120 -0.02755 0.01157  0.01554  104 ILE A CD1 
551  N N   . SER A 105 ? 0.22457 0.21817 0.20905 -0.02043 0.02724  0.01491  105 SER A N   
552  C CA  . SER A 105 ? 0.25469 0.24169 0.22490 -0.01921 0.02530  0.01498  105 SER A CA  
553  C C   . SER A 105 ? 0.23456 0.22231 0.20295 -0.01510 0.02470  0.00814  105 SER A C   
554  O O   . SER A 105 ? 0.16366 0.15649 0.14254 -0.01318 0.02462  0.00365  105 SER A O   
555  C CB  . SER A 105 ? 0.30161 0.28027 0.27171 -0.02111 0.01730  0.01860  105 SER A CB  
556  O OG  . SER A 105 ? 0.28869 0.26668 0.27065 -0.01904 0.01190  0.01419  105 SER A OG  
557  N N   . VAL A 106 ? 0.20423 0.18667 0.15855 -0.01429 0.02402  0.00765  106 VAL A N   
558  C CA  . VAL A 106 ? 0.18973 0.17086 0.14230 -0.01135 0.02136  0.00216  106 VAL A CA  
559  C C   . VAL A 106 ? 0.28713 0.25999 0.22990 -0.01260 0.01450  0.00396  106 VAL A C   
560  O O   . VAL A 106 ? 0.28836 0.25634 0.22147 -0.01543 0.01334  0.00913  106 VAL A O   
561  C CB  . VAL A 106 ? 0.16495 0.14816 0.11037 -0.00871 0.02783  -0.00170 106 VAL A CB  
562  C CG1 . VAL A 106 ? 0.15001 0.14249 0.10632 -0.00745 0.03429  -0.00241 106 VAL A CG1 
563  C CG2 . VAL A 106 ? 0.24841 0.22592 0.17580 -0.00971 0.03110  0.00018  106 VAL A CG2 
564  N N   . VAL A 107 ? 0.23148 0.20335 0.17709 -0.01090 0.00959  0.00037  107 VAL A N   
565  C CA  . VAL A 107 ? 0.26010 0.22516 0.19791 -0.01230 0.00229  0.00237  107 VAL A CA  
566  C C   . VAL A 107 ? 0.24536 0.21003 0.18142 -0.01056 0.00002  -0.00253 107 VAL A C   
567  O O   . VAL A 107 ? 0.22782 0.19828 0.17468 -0.00819 0.00157  -0.00660 107 VAL A O   
568  C CB  . VAL A 107 ? 0.39348 0.35777 0.34321 -0.01307 -0.00461 0.00603  107 VAL A CB  
569  C CG1 . VAL A 107 ? 0.37309 0.34361 0.34021 -0.01025 -0.00504 0.00165  107 VAL A CG1 
570  C CG2 . VAL A 107 ? 0.42280 0.38091 0.36604 -0.01471 -0.01301 0.00950  107 VAL A CG2 
571  N N   . LYS A 108 ? 0.22751 0.18519 0.14932 -0.01227 -0.00384 -0.00189 108 LYS A N   
572  C CA  . LYS A 108 ? 0.27650 0.23255 0.19647 -0.01161 -0.00741 -0.00581 108 LYS A CA  
573  C C   . LYS A 108 ? 0.26276 0.22365 0.19933 -0.01078 -0.01367 -0.00567 108 LYS A C   
574  O O   . LYS A 108 ? 0.25595 0.21751 0.20038 -0.01139 -0.01823 -0.00173 108 LYS A O   
575  C CB  . LYS A 108 ? 0.29143 0.23801 0.19228 -0.01462 -0.01189 -0.00473 108 LYS A CB  
576  C CG  . LYS A 108 ? 0.44799 0.38932 0.33064 -0.01463 -0.00471 -0.00734 108 LYS A CG  
577  C CD  . LYS A 108 ? 0.55103 0.48193 0.41332 -0.01789 -0.00994 -0.00769 108 LYS A CD  
578  C CE  . LYS A 108 ? 0.69500 0.61994 0.53813 -0.01732 -0.00187 -0.01155 108 LYS A CE  
579  N NZ  . LYS A 108 ? 0.79295 0.72058 0.63148 -0.01762 0.00532  -0.00775 108 LYS A NZ  
580  N N   . ILE A 109 ? 0.23811 0.20253 0.18069 -0.00927 -0.01368 -0.00970 109 ILE A N   
581  C CA  . ILE A 109 ? 0.25558 0.22630 0.21443 -0.00828 -0.01815 -0.00969 109 ILE A CA  
582  C C   . ILE A 109 ? 0.27370 0.24120 0.23013 -0.01045 -0.02667 -0.00787 109 ILE A C   
583  O O   . ILE A 109 ? 0.22472 0.18464 0.16594 -0.01285 -0.02896 -0.00796 109 ILE A O   
584  C CB  . ILE A 109 ? 0.26994 0.24824 0.23860 -0.00594 -0.01356 -0.01402 109 ILE A CB  
585  C CG1 . ILE A 109 ? 0.27777 0.25286 0.23795 -0.00645 -0.01315 -0.01674 109 ILE A CG1 
586  C CG2 . ILE A 109 ? 0.21831 0.20041 0.19012 -0.00436 -0.00619 -0.01529 109 ILE A CG2 
587  C CD1 . ILE A 109 ? 0.23343 0.21572 0.20263 -0.00451 -0.00892 -0.01989 109 ILE A CD1 
588  N N   . SER A 110 ? 0.16735 0.14066 0.13892 -0.00969 -0.03139 -0.00629 110 SER A N   
589  C CA  . SER A 110 ? 0.20190 0.17413 0.17451 -0.01193 -0.04005 -0.00364 110 SER A CA  
590  C C   . SER A 110 ? 0.16457 0.13858 0.13701 -0.01276 -0.04039 -0.00683 110 SER A C   
591  O O   . SER A 110 ? 0.17291 0.15009 0.14691 -0.01100 -0.03390 -0.01082 110 SER A O   
592  C CB  . SER A 110 ? 0.26612 0.24538 0.25765 -0.01014 -0.04418 -0.00067 110 SER A CB  
593  O OG  . SER A 110 ? 0.19341 0.18237 0.19966 -0.00716 -0.03957 -0.00437 110 SER A OG  
594  N N   . ASN A 111 ? 0.27234 0.24466 0.24412 -0.01576 -0.04854 -0.00447 111 ASN A N   
595  C CA  . ASN A 111 ? 0.22296 0.19652 0.19576 -0.01738 -0.05008 -0.00663 111 ASN A CA  
596  C C   . ASN A 111 ? 0.20746 0.19347 0.19918 -0.01473 -0.04641 -0.00788 111 ASN A C   
597  O O   . ASN A 111 ? 0.16636 0.15397 0.15802 -0.01476 -0.04302 -0.01073 111 ASN A O   
598  C CB  . ASN A 111 ? 0.30618 0.27635 0.27656 -0.02188 -0.06074 -0.00303 111 ASN A CB  
599  C CG  . ASN A 111 ? 0.39573 0.35267 0.34401 -0.02544 -0.06493 -0.00235 111 ASN A CG  
600  O OD1 . ASN A 111 ? 0.36665 0.31556 0.29878 -0.02505 -0.05927 -0.00618 111 ASN A OD1 
601  N ND2 . ASN A 111 ? 0.46696 0.42204 0.41446 -0.02894 -0.07486 0.00275  111 ASN A ND2 
602  N N   . SER A 112 ? 0.18218 0.17677 0.18991 -0.01243 -0.04706 -0.00569 112 SER A N   
603  C CA  . SER A 112 ? 0.14618 0.15302 0.17071 -0.00979 -0.04272 -0.00739 112 SER A CA  
604  C C   . SER A 112 ? 0.19330 0.20204 0.21627 -0.00701 -0.03355 -0.01181 112 SER A C   
605  O O   . SER A 112 ? 0.13476 0.15053 0.16337 -0.00641 -0.02954 -0.01402 112 SER A O   
606  C CB  . SER A 112 ? 0.20994 0.22487 0.25208 -0.00735 -0.04517 -0.00469 112 SER A CB  
607  O OG  . SER A 112 ? 0.22936 0.23974 0.27032 -0.00529 -0.04467 -0.00383 112 SER A OG  
608  N N   . GLU A 113 ? 0.17656 0.17962 0.19223 -0.00580 -0.03060 -0.01247 113 GLU A N   
609  C CA  . GLU A 113 ? 0.17882 0.18330 0.19226 -0.00396 -0.02279 -0.01607 113 GLU A CA  
610  C C   . GLU A 113 ? 0.15959 0.16078 0.16300 -0.00523 -0.02034 -0.01801 113 GLU A C   
611  O O   . GLU A 113 ? 0.14695 0.15349 0.15386 -0.00411 -0.01540 -0.02037 113 GLU A O   
612  C CB  . GLU A 113 ? 0.17921 0.17793 0.18657 -0.00326 -0.02064 -0.01544 113 GLU A CB  
613  C CG  . GLU A 113 ? 0.17995 0.18188 0.19948 -0.00123 -0.02146 -0.01447 113 GLU A CG  
614  C CD  . GLU A 113 ? 0.23591 0.23112 0.24955 -0.00150 -0.02063 -0.01253 113 GLU A CD  
615  O OE1 . GLU A 113 ? 0.20390 0.19146 0.20427 -0.00376 -0.02257 -0.00981 113 GLU A OE1 
616  O OE2 . GLU A 113 ? 0.22316 0.22047 0.24498 0.00024  -0.01801 -0.01374 113 GLU A OE2 
617  N N   . GLU A 114 ? 0.11942 0.11125 0.11001 -0.00756 -0.02398 -0.01707 114 GLU A N   
618  C CA  . GLU A 114 ? 0.12340 0.11011 0.10433 -0.00823 -0.02165 -0.01943 114 GLU A CA  
619  C C   . GLU A 114 ? 0.18615 0.17848 0.17542 -0.00929 -0.02329 -0.01960 114 GLU A C   
620  O O   . GLU A 114 ? 0.18557 0.17960 0.17533 -0.00842 -0.01912 -0.02139 114 GLU A O   
621  C CB  . GLU A 114 ? 0.17252 0.14667 0.13639 -0.01060 -0.02527 -0.01928 114 GLU A CB  
622  C CG  . GLU A 114 ? 0.22820 0.19541 0.18223 -0.01069 -0.02268 -0.02256 114 GLU A CG  
623  C CD  . GLU A 114 ? 0.50884 0.46265 0.44350 -0.01252 -0.02461 -0.02382 114 GLU A CD  
624  O OE1 . GLU A 114 ? 0.60492 0.55556 0.53352 -0.01438 -0.02869 -0.02135 114 GLU A OE1 
625  O OE2 . GLU A 114 ? 0.67675 0.62290 0.60194 -0.01205 -0.02205 -0.02730 114 GLU A OE2 
626  N N   . LYS A 115 ? 0.17362 0.16937 0.17030 -0.01136 -0.02957 -0.01700 115 LYS A N   
627  C CA  . LYS A 115 ? 0.11210 0.11526 0.11887 -0.01285 -0.03105 -0.01608 115 LYS A CA  
628  C C   . LYS A 115 ? 0.12146 0.13639 0.13948 -0.01034 -0.02466 -0.01726 115 LYS A C   
629  O O   . LYS A 115 ? 0.15635 0.17412 0.17586 -0.01105 -0.02258 -0.01759 115 LYS A O   
630  C CB  . LYS A 115 ? 0.16725 0.17485 0.18323 -0.01516 -0.03831 -0.01239 115 LYS A CB  
631  C CG  . LYS A 115 ? 0.15404 0.17264 0.18366 -0.01666 -0.03893 -0.01057 115 LYS A CG  
632  C CD  . LYS A 115 ? 0.13348 0.15733 0.17370 -0.01901 -0.04636 -0.00624 115 LYS A CD  
633  C CE  . LYS A 115 ? 0.23434 0.26947 0.28783 -0.02124 -0.04684 -0.00374 115 LYS A CE  
634  N NZ  . LYS A 115 ? 0.32308 0.36515 0.38931 -0.02349 -0.05391 0.00109  115 LYS A NZ  
635  N N   . ASN A 116 ? 0.11748 0.13865 0.14299 -0.00769 -0.02195 -0.01781 116 ASN A N   
636  C CA  . ASN A 116 ? 0.09355 0.12536 0.12815 -0.00566 -0.01615 -0.01965 116 ASN A CA  
637  C C   . ASN A 116 ? 0.13743 0.16708 0.16493 -0.00494 -0.01098 -0.02181 116 ASN A C   
638  O O   . ASN A 116 ? 0.17993 0.21679 0.21155 -0.00508 -0.00788 -0.02225 116 ASN A O   
639  C CB  . ASN A 116 ? 0.19555 0.23163 0.23793 -0.00286 -0.01446 -0.02079 116 ASN A CB  
640  C CG  . ASN A 116 ? 0.49752 0.53903 0.55152 -0.00264 -0.01868 -0.01846 116 ASN A CG  
641  O OD1 . ASN A 116 ? 0.54107 0.58812 0.60084 -0.00459 -0.02119 -0.01629 116 ASN A OD1 
642  N ND2 . ASN A 116 ? 0.61788 0.65807 0.67657 -0.00033 -0.01968 -0.01837 116 ASN A ND2 
643  N N   . TRP A 117 ? 0.14945 0.16984 0.16659 -0.00428 -0.01009 -0.02261 117 TRP A N   
644  C CA  . TRP A 117 ? 0.17704 0.19573 0.18881 -0.00331 -0.00530 -0.02407 117 TRP A CA  
645  C C   . TRP A 117 ? 0.17975 0.19615 0.18880 -0.00466 -0.00621 -0.02342 117 TRP A C   
646  O O   . TRP A 117 ? 0.18162 0.20337 0.19422 -0.00433 -0.00326 -0.02339 117 TRP A O   
647  C CB  . TRP A 117 ? 0.21587 0.22569 0.21748 -0.00235 -0.00368 -0.02464 117 TRP A CB  
648  C CG  . TRP A 117 ? 0.18095 0.19060 0.17946 -0.00088 0.00170  -0.02574 117 TRP A CG  
649  C CD1 . TRP A 117 ? 0.15929 0.17508 0.16258 0.00031  0.00594  -0.02635 117 TRP A CD1 
650  C CD2 . TRP A 117 ? 0.19061 0.19349 0.18140 -0.00032 0.00318  -0.02627 117 TRP A CD2 
651  N NE1 . TRP A 117 ? 0.13336 0.14799 0.13360 0.00151  0.00976  -0.02646 117 TRP A NE1 
652  C CE2 . TRP A 117 ? 0.23372 0.24035 0.22662 0.00161  0.00855  -0.02661 117 TRP A CE2 
653  C CE3 . TRP A 117 ? 0.19446 0.18806 0.17713 -0.00127 0.00027  -0.02671 117 TRP A CE3 
654  C CZ2 . TRP A 117 ? 0.15437 0.15650 0.14294 0.00336  0.01161  -0.02712 117 TRP A CZ2 
655  C CZ3 . TRP A 117 ? 0.23391 0.22148 0.21079 0.00043  0.00344  -0.02806 117 TRP A CZ3 
656  C CH2 . TRP A 117 ? 0.19545 0.18764 0.17595 0.00310  0.00935  -0.02815 117 TRP A CH2 
657  N N   . ASN A 118 ? 0.13578 0.14374 0.13851 -0.00654 -0.01090 -0.02267 118 ASN A N   
658  C CA  . ASN A 118 ? 0.14116 0.14462 0.14115 -0.00811 -0.01254 -0.02223 118 ASN A CA  
659  C C   . ASN A 118 ? 0.18707 0.20065 0.19808 -0.00991 -0.01341 -0.01986 118 ASN A C   
660  O O   . ASN A 118 ? 0.15548 0.16826 0.16671 -0.01044 -0.01261 -0.01903 118 ASN A O   
661  C CB  . ASN A 118 ? 0.14013 0.13216 0.13107 -0.01063 -0.01853 -0.02221 118 ASN A CB  
662  C CG  . ASN A 118 ? 0.22474 0.20425 0.20092 -0.00915 -0.01658 -0.02501 118 ASN A CG  
663  O OD1 . ASN A 118 ? 0.30802 0.28487 0.28104 -0.00668 -0.01155 -0.02677 118 ASN A OD1 
664  N ND2 . ASN A 118 ? 0.29308 0.26535 0.26034 -0.01069 -0.02052 -0.02513 118 ASN A ND2 
665  N N   . LEU A 119 ? 0.14052 0.16379 0.16103 -0.01076 -0.01481 -0.01847 119 LEU A N   
666  C CA  . LEU A 119 ? 0.22721 0.26161 0.25810 -0.01273 -0.01490 -0.01592 119 LEU A CA  
667  C C   . LEU A 119 ? 0.22778 0.27008 0.26146 -0.01154 -0.00940 -0.01624 119 LEU A C   
668  O O   . LEU A 119 ? 0.15769 0.20777 0.19711 -0.01365 -0.00918 -0.01359 119 LEU A O   
669  C CB  . LEU A 119 ? 0.19715 0.24148 0.23861 -0.01295 -0.01620 -0.01486 119 LEU A CB  
670  C CG  . LEU A 119 ? 0.33401 0.37359 0.37609 -0.01527 -0.02324 -0.01272 119 LEU A CG  
671  C CD1 . LEU A 119 ? 0.28398 0.33572 0.34015 -0.01517 -0.02428 -0.01075 119 LEU A CD1 
672  C CD2 . LEU A 119 ? 0.29286 0.32566 0.33107 -0.01935 -0.02814 -0.01044 119 LEU A CD2 
673  N N   . ASN A 120 ? 0.13617 0.17700 0.16586 -0.00871 -0.00533 -0.01887 120 ASN A N   
674  C CA  . ASN A 120 ? 0.11158 0.15948 0.14326 -0.00808 -0.00111 -0.01885 120 ASN A CA  
675  C C   . ASN A 120 ? 0.19638 0.23755 0.22280 -0.00730 -0.00015 -0.01811 120 ASN A C   
676  O O   . ASN A 120 ? 0.17955 0.22626 0.20780 -0.00680 0.00264  -0.01741 120 ASN A O   
677  C CB  . ASN A 120 ? 0.09817 0.15071 0.13113 -0.00598 0.00253  -0.02185 120 ASN A CB  
678  C CG  . ASN A 120 ? 0.19724 0.25882 0.23766 -0.00609 0.00297  -0.02296 120 ASN A CG  
679  O OD1 . ASN A 120 ? 0.22506 0.29481 0.27098 -0.00786 0.00275  -0.02118 120 ASN A OD1 
680  N ND2 . ASN A 120 ? 0.27109 0.33124 0.31225 -0.00408 0.00387  -0.02571 120 ASN A ND2 
681  N N   . VAL A 121 ? 0.16944 0.19869 0.18949 -0.00717 -0.00262 -0.01830 121 VAL A N   
682  C CA  . VAL A 121 ? 0.18366 0.20493 0.19884 -0.00531 -0.00105 -0.01847 121 VAL A CA  
683  C C   . VAL A 121 ? 0.24154 0.25746 0.25713 -0.00720 -0.00437 -0.01596 121 VAL A C   
684  O O   . VAL A 121 ? 0.20583 0.21692 0.22018 -0.00990 -0.00896 -0.01537 121 VAL A O   
685  C CB  . VAL A 121 ? 0.20015 0.20995 0.20568 -0.00301 -0.00003 -0.02165 121 VAL A CB  
686  C CG1 . VAL A 121 ? 0.22935 0.22984 0.22996 -0.00061 0.00197  -0.02241 121 VAL A CG1 
687  C CG2 . VAL A 121 ? 0.16861 0.18319 0.17445 -0.00122 0.00364  -0.02317 121 VAL A CG2 
688  N N   . LYS A 122 ? 0.19196 0.20879 0.21016 -0.00603 -0.00259 -0.01400 122 LYS A N   
689  C CA  . LYS A 122 ? 0.15192 0.16124 0.17055 -0.00711 -0.00554 -0.01159 122 LYS A CA  
690  C C   . LYS A 122 ? 0.18431 0.18628 0.20101 -0.00287 -0.00243 -0.01252 122 LYS A C   
691  O O   . LYS A 122 ? 0.20701 0.21517 0.22595 -0.00013 0.00179  -0.01272 122 LYS A O   
692  C CB  . LYS A 122 ? 0.11886 0.13882 0.14591 -0.01062 -0.00734 -0.00617 122 LYS A CB  
693  C CG  . LYS A 122 ? 0.25883 0.28671 0.28938 -0.01467 -0.00990 -0.00484 122 LYS A CG  
694  C CD  . LYS A 122 ? 0.38254 0.40141 0.41248 -0.01809 -0.01557 -0.00311 122 LYS A CD  
695  C CE  . LYS A 122 ? 0.49296 0.51848 0.52669 -0.02158 -0.01837 -0.00225 122 LYS A CE  
696  N NZ  . LYS A 122 ? 0.60519 0.62454 0.64074 -0.02630 -0.02466 0.00103  122 LYS A NZ  
697  N N   . TYR A 123 ? 0.18722 0.17575 0.20033 -0.00226 -0.00456 -0.01320 123 TYR A N   
698  C CA  . TYR A 123 ? 0.22805 0.21034 0.24222 0.00218  -0.00158 -0.01336 123 TYR A CA  
699  C C   . TYR A 123 ? 0.24841 0.22986 0.26992 0.00022  -0.00538 -0.00803 123 TYR A C   
700  O O   . TYR A 123 ? 0.44307 0.41526 0.46263 -0.00273 -0.01016 -0.00758 123 TYR A O   
701  C CB  . TYR A 123 ? 0.15143 0.11743 0.15502 0.00550  0.00011  -0.01922 123 TYR A CB  
702  C CG  . TYR A 123 ? 0.19225 0.15973 0.18877 0.00761  0.00455  -0.02329 123 TYR A CG  
703  C CD1 . TYR A 123 ? 0.19417 0.16132 0.18402 0.00447  0.00199  -0.02516 123 TYR A CD1 
704  C CD2 . TYR A 123 ? 0.21402 0.18404 0.21180 0.01250  0.01102  -0.02439 123 TYR A CD2 
705  C CE1 . TYR A 123 ? 0.19498 0.16306 0.17854 0.00601  0.00555  -0.02793 123 TYR A CE1 
706  C CE2 . TYR A 123 ? 0.24062 0.21231 0.23232 0.01380  0.01503  -0.02723 123 TYR A CE2 
707  C CZ  . TYR A 123 ? 0.25595 0.22619 0.24012 0.01046  0.01216  -0.02890 123 TYR A CZ  
708  O OH  . TYR A 123 ? 0.32710 0.29851 0.30539 0.01141  0.01568  -0.03081 123 TYR A OH  
709  N N   . ASP A 124 ? 0.52651 0.25309 0.33739 0.04419  -0.00327 0.00141  124 ASP A N   
710  C CA  . ASP A 124 ? 0.48366 0.23606 0.32159 0.04139  -0.00568 0.00587  124 ASP A CA  
711  C C   . ASP A 124 ? 0.54651 0.30856 0.39338 0.03319  -0.00143 0.00879  124 ASP A C   
712  O O   . ASP A 124 ? 0.48859 0.24484 0.32385 0.02890  0.00289  0.00720  124 ASP A O   
713  C CB  . ASP A 124 ? 0.62824 0.39289 0.47047 0.04440  -0.01016 0.00531  124 ASP A CB  
714  C CG  . ASP A 124 ? 0.80429 0.57924 0.65887 0.04837  -0.01470 0.00267  124 ASP A CG  
715  O OD1 . ASP A 124 ? 0.93958 0.70666 0.78552 0.05694  -0.01868 -0.00393 124 ASP A OD1 
716  O OD2 . ASP A 124 ? 0.83157 0.62077 0.70222 0.04277  -0.01444 0.00626  124 ASP A OD2 
717  N N   . GLU A 125 ? 0.43110 0.20655 0.29678 0.03162  -0.00328 0.01185  125 GLU A N   
718  C CA  . GLU A 125 ? 0.61854 0.40626 0.49468 0.02709  -0.00260 0.01301  125 GLU A CA  
719  C C   . GLU A 125 ? 0.55932 0.35355 0.43299 0.02480  -0.00366 0.01556  125 GLU A C   
720  O O   . GLU A 125 ? 0.52637 0.32155 0.39791 0.02658  -0.00624 0.01781  125 GLU A O   
721  C CB  . GLU A 125 ? 0.68237 0.47832 0.57366 0.02930  -0.00762 0.01598  125 GLU A CB  
722  C CG  . GLU A 125 ? 0.79041 0.58379 0.68726 0.03116  -0.00645 0.01241  125 GLU A CG  
723  C CD  . GLU A 125 ? 0.92732 0.73225 0.83403 0.02947  -0.00526 0.00691  125 GLU A CD  
724  O OE1 . GLU A 125 ? 0.98894 0.79247 0.89489 0.02636  0.00117  -0.00023 125 GLU A OE1 
725  O OE2 . GLU A 125 ? 0.91290 0.72817 0.82712 0.03120  -0.01078 0.00831  125 GLU A OE2 
726  N N   . THR A 126 ? 0.48778 0.28824 0.36251 0.02037  -0.00131 0.01369  126 THR A N   
727  C CA  . THR A 126 ? 0.50812 0.31575 0.38225 0.01850  -0.00336 0.01677  126 THR A CA  
728  C C   . THR A 126 ? 0.38021 0.19431 0.26353 0.02071  -0.00986 0.02225  126 THR A C   
729  O O   . THR A 126 ? 0.37990 0.19570 0.27159 0.02339  -0.01333 0.02245  126 THR A O   
730  C CB  . THR A 126 ? 0.51263 0.32796 0.38804 0.01327  -0.00042 0.01251  126 THR A CB  
731  O OG1 . THR A 126 ? 0.38496 0.20572 0.25850 0.01219  -0.00321 0.01616  126 THR A OG1 
732  C CG2 . THR A 126 ? 0.47572 0.30406 0.36749 0.01429  -0.00298 0.00819  126 THR A CG2 
733  N N   . PRO A 127 ? 0.38068 0.19557 0.25933 0.01928  -0.01115 0.02602  127 PRO A N   
734  C CA  . PRO A 127 ? 0.38413 0.19877 0.26427 0.01870  -0.01565 0.03097  127 PRO A CA  
735  C C   . PRO A 127 ? 0.38874 0.20607 0.27052 0.02006  -0.02069 0.03195  127 PRO A C   
736  O O   . PRO A 127 ? 0.39763 0.20853 0.27722 0.02246  -0.02631 0.03499  127 PRO A O   
737  C CB  . PRO A 127 ? 0.38564 0.20155 0.25897 0.01469  -0.01356 0.03240  127 PRO A CB  
738  C CG  . PRO A 127 ? 0.38189 0.19901 0.25194 0.01650  -0.00994 0.02759  127 PRO A CG  
739  C CD  . PRO A 127 ? 0.41922 0.23286 0.28836 0.01807  -0.00835 0.02492  127 PRO A CD  
740  N N   . PHE A 128 ? 0.38604 0.21118 0.26939 0.01897  -0.01925 0.02828  128 PHE A N   
741  C CA  . PHE A 128 ? 0.42221 0.25308 0.30723 0.02088  -0.02514 0.02735  128 PHE A CA  
742  C C   . PHE A 128 ? 0.44030 0.28247 0.33831 0.02469  -0.02740 0.01892  128 PHE A C   
743  O O   . PHE A 128 ? 0.49761 0.34680 0.40086 0.02075  -0.02050 0.01215  128 PHE A O   
744  C CB  . PHE A 128 ? 0.39056 0.22570 0.26973 0.01628  -0.02245 0.02726  128 PHE A CB  
745  C CG  . PHE A 128 ? 0.39193 0.21997 0.26041 0.01256  -0.01944 0.03279  128 PHE A CG  
746  C CD1 . PHE A 128 ? 0.40125 0.22101 0.26197 0.01171  -0.02271 0.03843  128 PHE A CD1 
747  C CD2 . PHE A 128 ? 0.45607 0.28422 0.31980 0.00974  -0.01318 0.03086  128 PHE A CD2 
748  C CE1 . PHE A 128 ? 0.43607 0.25343 0.28928 0.00651  -0.01835 0.04062  128 PHE A CE1 
749  C CE2 . PHE A 128 ? 0.45768 0.28373 0.31432 0.00778  -0.01118 0.03300  128 PHE A CE2 
750  C CZ  . PHE A 128 ? 0.44550 0.26905 0.29930 0.00535  -0.01304 0.03716  128 PHE A CZ  
751  N N   . LYS A 129 ? 0.45472 0.29715 0.35557 0.03234  -0.03709 0.01800  129 LYS A N   
752  C CA  . LYS A 129 ? 0.54818 0.40560 0.46435 0.03791  -0.04074 0.00712  129 LYS A CA  
753  C C   . LYS A 129 ? 0.52245 0.39285 0.44288 0.04269  -0.04895 0.00030  129 LYS A C   
754  O O   . LYS A 129 ? 0.49872 0.39064 0.43558 0.04359  -0.04875 -0.01300 129 LYS A O   
755  C CB  . LYS A 129 ? 0.54429 0.39308 0.46162 0.04647  -0.04745 0.00804  129 LYS A CB  
756  C CG  . LYS A 129 ? 0.62924 0.46747 0.54440 0.04208  -0.03972 0.01300  129 LYS A CG  
757  C CD  . LYS A 129 ? 0.85017 0.68943 0.77441 0.04881  -0.04281 0.00804  129 LYS A CD  
758  C CE  . LYS A 129 ? 0.94192 0.80026 0.88246 0.04589  -0.03576 -0.00442 129 LYS A CE  
759  N NZ  . LYS A 129 ? 0.94256 0.80546 0.89400 0.05334  -0.03945 -0.01144 129 LYS A NZ  
760  N N   . THR A 130 ? 0.47325 0.33108 0.37849 0.04515  -0.05578 0.00788  130 THR A N   
761  C CA  . THR A 130 ? 0.55523 0.42218 0.46110 0.05159  -0.06575 0.00167  130 THR A CA  
762  C C   . THR A 130 ? 0.55189 0.41255 0.44436 0.04471  -0.06300 0.00854  130 THR A C   
763  O O   . THR A 130 ? 0.52965 0.37811 0.41158 0.03617  -0.05447 0.01808  130 THR A O   
764  C CB  . THR A 130 ? 0.52547 0.37723 0.41966 0.06676  -0.08247 0.00220  130 THR A CB  
765  O OG1 . THR A 130 ? 0.55214 0.37235 0.41882 0.06435  -0.08354 0.01653  130 THR A OG1 
766  C CG2 . THR A 130 ? 0.56785 0.42195 0.47220 0.07517  -0.08642 -0.00360 130 THR A CG2 
767  N N   . ILE A 131 ? 0.50742 0.37820 0.40127 0.04947  -0.07106 0.00197  131 ILE A N   
768  C CA  . ILE A 131 ? 0.49104 0.35530 0.37099 0.04485  -0.07079 0.00760  131 ILE A CA  
769  C C   . ILE A 131 ? 0.55136 0.38428 0.40413 0.04632  -0.07520 0.02095  131 ILE A C   
770  O O   . ILE A 131 ? 0.58538 0.40834 0.42535 0.03729  -0.06815 0.02918  131 ILE A O   
771  C CB  . ILE A 131 ? 0.71463 0.59681 0.60209 0.05192  -0.08108 -0.00429 131 ILE A CB  
772  C CG1 . ILE A 131 ? 0.61097 0.52300 0.52042 0.04253  -0.07097 -0.01703 131 ILE A CG1 
773  C CG2 . ILE A 131 ? 0.71086 0.57650 0.57619 0.05250  -0.08677 0.00339  131 ILE A CG2 
774  C CD1 . ILE A 131 ? 0.50345 0.41166 0.40399 0.02890  -0.05899 -0.01078 131 ILE A CD1 
775  N N   . GLU A 132 ? 0.50465 0.32064 0.34657 0.05716  -0.08640 0.02191  132 GLU A N   
776  C CA  . GLU A 132 ? 0.56837 0.34888 0.37877 0.05649  -0.08940 0.03348  132 GLU A CA  
777  C C   . GLU A 132 ? 0.54376 0.31666 0.35146 0.04285  -0.07478 0.04205  132 GLU A C   
778  O O   . GLU A 132 ? 0.53655 0.28878 0.32232 0.03483  -0.07053 0.05010  132 GLU A O   
779  C CB  . GLU A 132 ? 0.62535 0.38413 0.42049 0.07089  -0.10392 0.03221  132 GLU A CB  
780  C CG  . GLU A 132 ? 0.91714 0.63122 0.67139 0.06849  -0.10642 0.04359  132 GLU A CG  
781  C CD  . GLU A 132 ? 1.10842 0.80461 0.83663 0.06888  -0.11226 0.04676  132 GLU A CD  
782  O OE1 . GLU A 132 ? 1.16995 0.88641 0.91064 0.07737  -0.12060 0.03851  132 GLU A OE1 
783  O OE2 . GLU A 132 ? 1.13525 0.79736 0.83008 0.05964  -0.10779 0.05641  132 GLU A OE2 
784  N N   . ASP A 133 ? 0.48533 0.27520 0.31464 0.04018  -0.06715 0.03871  133 ASP A N   
785  C CA  . ASP A 133 ? 0.46009 0.24700 0.28978 0.02949  -0.05485 0.04399  133 ASP A CA  
786  C C   . ASP A 133 ? 0.45131 0.24446 0.27876 0.01993  -0.04625 0.04621  133 ASP A C   
787  O O   . ASP A 133 ? 0.53442 0.31912 0.35267 0.01176  -0.03922 0.05065  133 ASP A O   
788  C CB  . ASP A 133 ? 0.43886 0.24148 0.28978 0.02995  -0.04947 0.03897  133 ASP A CB  
789  C CG  . ASP A 133 ? 0.47594 0.27009 0.32785 0.03784  -0.05591 0.03779  133 ASP A CG  
790  O OD1 . ASP A 133 ? 0.47216 0.24293 0.30413 0.04139  -0.06304 0.04253  133 ASP A OD1 
791  O OD2 . ASP A 133 ? 0.46921 0.27710 0.33873 0.04011  -0.05350 0.03189  133 ASP A OD2 
792  N N   . LEU A 134 ? 0.44186 0.25088 0.27792 0.02067  -0.04664 0.04154  134 LEU A N   
793  C CA  . LEU A 134 ? 0.43514 0.24915 0.26775 0.01289  -0.03932 0.04304  134 LEU A CA  
794  C C   . LEU A 134 ? 0.50612 0.30361 0.31732 0.00976  -0.04161 0.04912  134 LEU A C   
795  O O   . LEU A 134 ? 0.49238 0.28792 0.29678 0.00169  -0.03388 0.05189  134 LEU A O   
796  C CB  . LEU A 134 ? 0.42467 0.25650 0.26837 0.01323  -0.03892 0.03605  134 LEU A CB  
797  C CG  . LEU A 134 ? 0.48372 0.32951 0.34440 0.01332  -0.03448 0.02836  134 LEU A CG  
798  C CD1 . LEU A 134 ? 0.51672 0.37684 0.38307 0.00937  -0.03136 0.02071  134 LEU A CD1 
799  C CD2 . LEU A 134 ? 0.40184 0.24244 0.26193 0.00939  -0.02574 0.03087  134 LEU A CD2 
800  N N   . ASN A 135 ? 0.53976 0.32394 0.33836 0.01678  -0.05263 0.05001  135 ASN A N   
801  C CA  . ASN A 135 ? 0.75353 0.51383 0.52423 0.01403  -0.05563 0.05599  135 ASN A CA  
802  C C   . ASN A 135 ? 0.88195 0.62091 0.63525 0.00501  -0.04859 0.06176  135 ASN A C   
803  O O   . ASN A 135 ? 1.04253 0.75505 0.76702 0.00027  -0.04927 0.06652  135 ASN A O   
804  C CB  . ASN A 135 ? 0.81765 0.56355 0.57428 0.02667  -0.07155 0.05438  135 ASN A CB  
805  C CG  . ASN A 135 ? 0.94118 0.71198 0.71607 0.03419  -0.07830 0.04569  135 ASN A CG  
806  O OD1 . ASN A 135 ? 0.94781 0.73464 0.73150 0.02743  -0.07142 0.04437  135 ASN A OD1 
807  N ND2 . ASN A 135 ? 0.98421 0.75915 0.76484 0.04818  -0.09179 0.03808  135 ASN A ND2 
808  N N   . ARG A 136 ? 0.85844 0.60804 0.62790 0.00197  -0.04150 0.06014  136 ARG A N   
809  C CA  . ARG A 136 ? 0.87951 0.61874 0.64061 -0.00859 -0.03229 0.06216  136 ARG A CA  
810  C C   . ARG A 136 ? 0.96902 0.67687 0.70610 -0.00752 -0.03767 0.06601  136 ARG A C   
811  O O   . ARG A 136 ? 0.97512 0.68215 0.72001 0.00066  -0.04331 0.06489  136 ARG A O   
812  C CB  . ARG A 136 ? 0.87544 0.61405 0.62577 -0.02085 -0.02287 0.06270  136 ARG A CB  
813  C CG  . ARG A 136 ? 0.88146 0.64674 0.65087 -0.02018 -0.01898 0.05881  136 ARG A CG  
814  C CD  . ARG A 136 ? 1.06796 0.83493 0.82858 -0.03132 -0.00974 0.05759  136 ARG A CD  
815  N NE  . ARG A 136 ? 1.14300 0.93368 0.92317 -0.03318 -0.00205 0.05074  136 ARG A NE  
816  C CZ  . ARG A 136 ? 1.20599 1.00509 0.98489 -0.04206 0.00678  0.04568  136 ARG A CZ  
817  N NH1 . ARG A 136 ? 1.29131 1.07609 1.04959 -0.05271 0.01127  0.04747  136 ARG A NH1 
818  N NH2 . ARG A 136 ? 1.12618 0.94699 0.92263 -0.03982 0.01081  0.03751  136 ARG A NH2 
819  N N   . SER A 145 ? 0.50269 0.31998 0.24956 -0.04250 0.00802  0.04616  145 SER A N   
820  C CA  . SER A 145 ? 0.61588 0.44937 0.37909 -0.03637 0.00995  0.03906  145 SER A CA  
821  C C   . SER A 145 ? 0.51566 0.34829 0.28662 -0.02801 0.00374  0.04102  145 SER A C   
822  O O   . SER A 145 ? 0.44470 0.28143 0.21741 -0.02291 0.00353  0.03759  145 SER A O   
823  C CB  . SER A 145 ? 0.71176 0.55289 0.48404 -0.03954 0.01507  0.03325  145 SER A CB  
824  O OG  . SER A 145 ? 0.73065 0.58411 0.51647 -0.03060 0.01402  0.02639  145 SER A OG  
825  N N   . PHE A 146 ? 0.53852 0.36388 0.31164 -0.02708 -0.00089 0.04548  146 PHE A N   
826  C CA  . PHE A 146 ? 0.53319 0.35886 0.31271 -0.02134 -0.00662 0.04626  146 PHE A CA  
827  C C   . PHE A 146 ? 0.53163 0.35316 0.30264 -0.02182 -0.01172 0.04890  146 PHE A C   
828  O O   . PHE A 146 ? 0.57776 0.40389 0.35465 -0.01876 -0.01561 0.04671  146 PHE A O   
829  C CB  . PHE A 146 ? 0.55831 0.38065 0.34535 -0.01843 -0.01054 0.04779  146 PHE A CB  
830  C CG  . PHE A 146 ? 0.53529 0.36280 0.33285 -0.01649 -0.00686 0.04433  146 PHE A CG  
831  C CD1 . PHE A 146 ? 0.56133 0.39333 0.36654 -0.01189 -0.00646 0.04052  146 PHE A CD1 
832  C CD2 . PHE A 146 ? 0.56517 0.39126 0.36273 -0.02015 -0.00345 0.04396  146 PHE A CD2 
833  C CE1 . PHE A 146 ? 0.64740 0.48124 0.45932 -0.00882 -0.00431 0.03716  146 PHE A CE1 
834  C CE2 . PHE A 146 ? 0.58433 0.41670 0.39251 -0.01751 -0.00114 0.03952  146 PHE A CE2 
835  C CZ  . PHE A 146 ? 0.58883 0.42451 0.40385 -0.01073 -0.00239 0.03650  146 PHE A CZ  
836  N N   . ASP A 147 ? 0.48726 0.30039 0.24385 -0.02643 -0.01130 0.05222  147 ASP A N   
837  C CA  . ASP A 147 ? 0.47480 0.28107 0.22030 -0.02580 -0.01779 0.05473  147 ASP A CA  
838  C C   . ASP A 147 ? 0.52921 0.34165 0.27128 -0.02784 -0.01495 0.05269  147 ASP A C   
839  O O   . ASP A 147 ? 0.59247 0.40517 0.32805 -0.03223 -0.00833 0.05221  147 ASP A O   
840  C CB  . ASP A 147 ? 0.49969 0.28616 0.22418 -0.02991 -0.01935 0.05990  147 ASP A CB  
841  C CG  . ASP A 147 ? 0.72672 0.49974 0.44732 -0.02645 -0.02521 0.06243  147 ASP A CG  
842  O OD1 . ASP A 147 ? 0.64150 0.42422 0.37911 -0.01990 -0.02901 0.05986  147 ASP A OD1 
843  O OD2 . ASP A 147 ? 0.83331 0.58316 0.53069 -0.03070 -0.02572 0.06665  147 ASP A OD2 
844  N N   . PHE A 148 ? 0.46807 0.28654 0.21478 -0.02502 -0.01971 0.04995  148 PHE A N   
845  C CA  . PHE A 148 ? 0.46852 0.29023 0.20941 -0.02765 -0.01767 0.04787  148 PHE A CA  
846  C C   . PHE A 148 ? 0.51896 0.33616 0.25076 -0.02665 -0.02601 0.04911  148 PHE A C   
847  O O   . PHE A 148 ? 0.48686 0.30527 0.22373 -0.02140 -0.03486 0.04739  148 PHE A O   
848  C CB  . PHE A 148 ? 0.45777 0.28848 0.20802 -0.02771 -0.01503 0.04160  148 PHE A CB  
849  C CG  . PHE A 148 ? 0.45025 0.27965 0.20161 -0.02735 -0.00771 0.03967  148 PHE A CG  
850  C CD1 . PHE A 148 ? 0.48470 0.31484 0.24515 -0.02431 -0.00701 0.03997  148 PHE A CD1 
851  C CD2 . PHE A 148 ? 0.45340 0.27842 0.19416 -0.02887 -0.00269 0.03673  148 PHE A CD2 
852  C CE1 . PHE A 148 ? 0.49352 0.32125 0.25324 -0.02199 -0.00213 0.03695  148 PHE A CE1 
853  C CE2 . PHE A 148 ? 0.60413 0.42354 0.34108 -0.02568 0.00164  0.03381  148 PHE A CE2 
854  C CZ  . PHE A 148 ? 0.53207 0.35350 0.27902 -0.02182 0.00153  0.03365  148 PHE A CZ  
855  N N   . THR A 149 ? 0.49175 0.30389 0.20973 -0.03023 -0.02444 0.05086  149 THR A N   
856  C CA  . THR A 149 ? 0.55244 0.36198 0.26253 -0.02818 -0.03339 0.05009  149 THR A CA  
857  C C   . THR A 149 ? 0.54882 0.37523 0.27353 -0.02773 -0.03499 0.04170  149 THR A C   
858  O O   . THR A 149 ? 0.50792 0.34190 0.24216 -0.03073 -0.02750 0.03812  149 THR A O   
859  C CB  . THR A 149 ? 0.60610 0.40564 0.29685 -0.03276 -0.03097 0.05359  149 THR A CB  
860  O OG1 . THR A 149 ? 0.53439 0.34204 0.22777 -0.03690 -0.02265 0.05076  149 THR A OG1 
861  C CG2 . THR A 149 ? 0.53281 0.31566 0.20722 -0.03680 -0.02652 0.05972  149 THR A CG2 
862  N N   . THR A 150 ? 0.49071 0.28134 0.20802 0.04777  -0.10291 0.02048  150 THR A N   
863  C CA  . THR A 150 ? 0.51812 0.30972 0.24768 0.04633  -0.11422 0.01321  150 THR A CA  
864  C C   . THR A 150 ? 0.62900 0.41929 0.35477 0.04654  -0.11176 0.00833  150 THR A C   
865  O O   . THR A 150 ? 0.56969 0.36799 0.31292 0.04293  -0.11414 0.00433  150 THR A O   
866  C CB  . THR A 150 ? 0.64934 0.42913 0.37000 0.04987  -0.12763 0.01090  150 THR A CB  
867  O OG1 . THR A 150 ? 0.64900 0.43247 0.37978 0.04900  -0.13156 0.01445  150 THR A OG1 
868  C CG2 . THR A 150 ? 0.68984 0.46908 0.42094 0.04866  -0.13889 0.00344  150 THR A CG2 
869  N N   . THR A 151 ? 0.65757 0.43777 0.36068 0.05099  -0.10629 0.00903  151 THR A N   
870  C CA  . THR A 151 ? 0.65023 0.42726 0.34814 0.05208  -0.10434 0.00430  151 THR A CA  
871  C C   . THR A 151 ? 0.61589 0.40580 0.32397 0.04916  -0.09134 0.00636  151 THR A C   
872  O O   . THR A 151 ? 0.58090 0.37344 0.29518 0.04797  -0.09076 0.00224  151 THR A O   
873  C CB  . THR A 151 ? 0.74947 0.50963 0.41852 0.05890  -0.10401 0.00349  151 THR A CB  
874  O OG1 . THR A 151 ? 0.76282 0.52265 0.41857 0.06145  -0.09221 0.01027  151 THR A OG1 
875  C CG2 . THR A 151 ? 0.70360 0.45066 0.36285 0.06192  -0.11846 0.00065  151 THR A CG2 
876  N N   . GLU A 152 ? 0.65738 0.45523 0.36789 0.04792  -0.08135 0.01291  152 GLU A N   
877  C CA  . GLU A 152 ? 0.65262 0.46430 0.37589 0.04465  -0.07017 0.01499  152 GLU A CA  
878  C C   . GLU A 152 ? 0.51948 0.34223 0.26661 0.03953  -0.07505 0.01153  152 GLU A C   
879  O O   . GLU A 152 ? 0.51070 0.34040 0.26599 0.03789  -0.07071 0.00925  152 GLU A O   
880  C CB  . GLU A 152 ? 0.73404 0.55230 0.45834 0.04346  -0.06032 0.02299  152 GLU A CB  
881  C CG  . GLU A 152 ? 0.76276 0.57663 0.46914 0.04734  -0.04928 0.02735  152 GLU A CG  
882  C CD  . GLU A 152 ? 0.76178 0.58312 0.47233 0.04508  -0.03943 0.03593  152 GLU A CD  
883  O OE1 . GLU A 152 ? 0.75882 0.58305 0.46350 0.04632  -0.02783 0.03984  152 GLU A OE1 
884  O OE2 . GLU A 152 ? 0.63318 0.45723 0.35358 0.04207  -0.04338 0.03888  152 GLU A OE2 
885  N N   . ALA A 153 ? 0.47623 0.30045 0.23437 0.03741  -0.08397 0.01136  153 ALA A N   
886  C CA  . ALA A 153 ? 0.40269 0.23743 0.18421 0.03292  -0.08900 0.00847  153 ALA A CA  
887  C C   . ALA A 153 ? 0.46131 0.29311 0.24626 0.03262  -0.09560 0.00207  153 ALA A C   
888  O O   . ALA A 153 ? 0.44407 0.28481 0.24284 0.02964  -0.09325 0.00014  153 ALA A O   
889  C CB  . ALA A 153 ? 0.35743 0.19294 0.14881 0.03184  -0.09755 0.00947  153 ALA A CB  
890  N N   . VAL A 154 ? 0.48955 0.30813 0.26158 0.03579  -0.10425 -0.00099 154 VAL A N   
891  C CA  . VAL A 154 ? 0.49332 0.30693 0.26788 0.03553  -0.11202 -0.00683 154 VAL A CA  
892  C C   . VAL A 154 ? 0.49174 0.30362 0.25812 0.03674  -0.10409 -0.00838 154 VAL A C   
893  O O   . VAL A 154 ? 0.43321 0.24903 0.21113 0.03418  -0.10580 -0.01154 154 VAL A O   
894  C CB  . VAL A 154 ? 0.55509 0.35343 0.31543 0.03922  -0.12355 -0.00964 154 VAL A CB  
895  C CG1 . VAL A 154 ? 0.55683 0.34833 0.31773 0.03914  -0.13136 -0.01545 154 VAL A CG1 
896  C CG2 . VAL A 154 ? 0.54412 0.34547 0.31627 0.03791  -0.13259 -0.00868 154 VAL A CG2 
897  N N   . ASN A 155 ? 0.47315 0.27968 0.22052 0.04077  -0.09501 -0.00579 155 ASN A N   
898  C CA  . ASN A 155 ? 0.50760 0.31312 0.24767 0.04268  -0.08656 -0.00697 155 ASN A CA  
899  C C   . ASN A 155 ? 0.44442 0.26600 0.20315 0.03846  -0.07872 -0.00557 155 ASN A C   
900  O O   . ASN A 155 ? 0.38662 0.20944 0.14878 0.03809  -0.07669 -0.00831 155 ASN A O   
901  C CB  . ASN A 155 ? 0.53566 0.33519 0.25472 0.04787  -0.07671 -0.00348 155 ASN A CB  
902  C CG  . ASN A 155 ? 0.65385 0.43472 0.34946 0.05363  -0.08328 -0.00589 155 ASN A CG  
903  O OD1 . ASN A 155 ? 0.57202 0.34384 0.26667 0.05375  -0.09591 -0.01046 155 ASN A OD1 
904  N ND2 . ASN A 155 ? 0.63342 0.40879 0.31034 0.05855  -0.07462 -0.00257 155 ASN A ND2 
905  N N   . PHE A 156 ? 0.42825 0.26137 0.19822 0.03558  -0.07448 -0.00116 156 PHE A N   
906  C CA  . PHE A 156 ? 0.43963 0.28778 0.22615 0.03200  -0.06714 0.00034  156 PHE A CA  
907  C C   . PHE A 156 ? 0.38834 0.24121 0.19244 0.02824  -0.07481 -0.00363 156 PHE A C   
908  O O   . PHE A 156 ? 0.39966 0.25829 0.21072 0.02699  -0.07084 -0.00508 156 PHE A O   
909  C CB  . PHE A 156 ? 0.43821 0.29647 0.23280 0.02977  -0.06194 0.00589  156 PHE A CB  
910  C CG  . PHE A 156 ? 0.40847 0.28153 0.21942 0.02639  -0.05530 0.00715  156 PHE A CG  
911  C CD1 . PHE A 156 ? 0.36319 0.24188 0.17138 0.02750  -0.04416 0.00893  156 PHE A CD1 
912  C CD2 . PHE A 156 ? 0.40353 0.28504 0.23304 0.02252  -0.06037 0.00638  156 PHE A CD2 
913  C CE1 . PHE A 156 ? 0.35347 0.24548 0.17603 0.02478  -0.03858 0.00991  156 PHE A CE1 
914  C CE2 . PHE A 156 ? 0.33132 0.22543 0.17413 0.01999  -0.05471 0.00731  156 PHE A CE2 
915  C CZ  . PHE A 156 ? 0.33974 0.23883 0.17843 0.02112  -0.04395 0.00904  156 PHE A CZ  
916  N N   . PHE A 157 ? 0.44007 0.29084 0.25189 0.02661  -0.08557 -0.00507 157 PHE A N   
917  C CA  . PHE A 157 ? 0.42099 0.27672 0.25131 0.02299  -0.09313 -0.00844 157 PHE A CA  
918  C C   . PHE A 157 ? 0.48640 0.33475 0.31129 0.02380  -0.09506 -0.01255 157 PHE A C   
919  O O   . PHE A 157 ? 0.40870 0.26409 0.24565 0.02114  -0.09331 -0.01382 157 PHE A O   
920  C CB  . PHE A 157 ? 0.38389 0.23705 0.22219 0.02209  -0.10483 -0.00958 157 PHE A CB  
921  C CG  . PHE A 157 ? 0.42372 0.28651 0.28653 0.01786  -0.11066 -0.01165 157 PHE A CG  
922  C CD1 . PHE A 157 ? 0.38078 0.23988 0.24795 0.01663  -0.11636 -0.01548 157 PHE A CD1 
923  C CD2 . PHE A 157 ? 0.41041 0.28609 0.29240 0.01524  -0.10990 -0.00951 157 PHE A CD2 
924  C CE1 . PHE A 157 ? 0.36790 0.23714 0.25913 0.01252  -0.12052 -0.01666 157 PHE A CE1 
925  C CE2 . PHE A 157 ? 0.43001 0.31574 0.33552 0.01178  -0.11381 -0.01104 157 PHE A CE2 
926  C CZ  . PHE A 157 ? 0.40878 0.29183 0.31941 0.01025  -0.11879 -0.01436 157 PHE A CZ  
927  N N   . ASN A 158 ? 0.42549 0.25887 0.23149 0.02773  -0.09889 -0.01458 158 ASN A N   
928  C CA  . ASN A 158 ? 0.40856 0.23217 0.20726 0.02909  -0.10187 -0.01870 158 ASN A CA  
929  C C   . ASN A 158 ? 0.42491 0.25188 0.21970 0.03022  -0.09066 -0.01817 158 ASN A C   
930  O O   . ASN A 158 ? 0.43245 0.25884 0.23277 0.02877  -0.09200 -0.02083 158 ASN A O   
931  C CB  . ASN A 158 ? 0.47315 0.27914 0.24949 0.03412  -0.10733 -0.02079 158 ASN A CB  
932  C CG  . ASN A 158 ? 0.54573 0.34659 0.32661 0.03316  -0.12100 -0.02268 158 ASN A CG  
933  O OD1 . ASN A 158 ? 0.53353 0.34409 0.33619 0.02859  -0.12671 -0.02285 158 ASN A OD1 
934  N ND2 . ASN A 158 ? 0.56768 0.35361 0.32835 0.03786  -0.12618 -0.02407 158 ASN A ND2 
935  N N   . ALA A 159 ? 0.43452 0.26538 0.22070 0.03279  -0.07959 -0.01445 159 ALA A N   
936  C CA  . ALA A 159 ? 0.49576 0.33185 0.27996 0.03433  -0.06810 -0.01335 159 ALA A CA  
937  C C   . ALA A 159 ? 0.48407 0.33430 0.28834 0.02976  -0.06579 -0.01293 159 ALA A C   
938  O O   . ALA A 159 ? 0.40205 0.25341 0.20731 0.03032  -0.06145 -0.01422 159 ALA A O   
939  C CB  . ALA A 159 ? 0.45484 0.29517 0.23029 0.03724  -0.05697 -0.00869 159 ALA A CB  
940  N N   . MET A 160 ? 0.31636 0.17662 0.13601 0.02571  -0.06890 -0.01118 160 MET A N   
941  C CA  . MET A 160 ? 0.37151 0.24495 0.20980 0.02174  -0.06716 -0.01085 160 MET A CA  
942  C C   . MET A 160 ? 0.39878 0.26896 0.24659 0.01899  -0.07597 -0.01490 160 MET A C   
943  O O   . MET A 160 ? 0.40555 0.28073 0.26073 0.01747  -0.07308 -0.01578 160 MET A O   
944  C CB  . MET A 160 ? 0.36065 0.24548 0.21280 0.01877  -0.06780 -0.00778 160 MET A CB  
945  C CG  . MET A 160 ? 0.34506 0.23508 0.19129 0.02032  -0.05848 -0.00312 160 MET A CG  
946  S SD  . MET A 160 ? 0.32531 0.22440 0.17064 0.02177  -0.04491 -0.00118 160 MET A SD  
947  C CE  . MET A 160 ? 0.31013 0.19739 0.13401 0.02721  -0.03970 -0.00130 160 MET A CE  
948  N N   . LYS A 161 ? 0.40676 0.26857 0.25473 0.01834  -0.08670 -0.01716 161 LYS A N   
949  C CA  . LYS A 161 ? 0.45476 0.31363 0.31367 0.01524  -0.09571 -0.02067 161 LYS A CA  
950  C C   . LYS A 161 ? 0.45908 0.30807 0.30654 0.01712  -0.09361 -0.02340 161 LYS A C   
951  O O   . LYS A 161 ? 0.42601 0.27678 0.28487 0.01381  -0.09604 -0.02530 161 LYS A O   
952  C CB  . LYS A 161 ? 0.53981 0.39091 0.39912 0.01511  -0.10736 -0.02238 161 LYS A CB  
953  C CG  . LYS A 161 ? 0.62442 0.47531 0.49984 0.01112  -0.11701 -0.02534 161 LYS A CG  
954  C CD  . LYS A 161 ? 0.80562 0.65376 0.68672 0.01072  -0.12799 -0.02612 161 LYS A CD  
955  C CE  . LYS A 161 ? 0.89726 0.74785 0.79820 0.00629  -0.13709 -0.02853 161 LYS A CE  
956  N NZ  . LYS A 161 ? 0.92687 0.77741 0.83646 0.00597  -0.14738 -0.02899 161 LYS A NZ  
957  N N   . ASN A 162 ? 0.45897 0.29773 0.28462 0.02254  -0.08853 -0.02339 162 ASN A N   
958  C CA  . ASN A 162 ? 0.54673 0.37512 0.35973 0.02561  -0.08568 -0.02581 162 ASN A CA  
959  C C   . ASN A 162 ? 0.46428 0.30120 0.28026 0.02615  -0.07452 -0.02423 162 ASN A C   
960  O O   . ASN A 162 ? 0.41125 0.24070 0.21904 0.02869  -0.07152 -0.02603 162 ASN A O   
961  C CB  . ASN A 162 ? 0.64856 0.46388 0.43806 0.03203  -0.08329 -0.02612 162 ASN A CB  
962  C CG  . ASN A 162 ? 0.82751 0.62990 0.60973 0.03264  -0.09553 -0.02894 162 ASN A CG  
963  O OD1 . ASN A 162 ? 0.84002 0.64126 0.63434 0.02849  -0.10617 -0.03144 162 ASN A OD1 
964  N ND2 . ASN A 162 ? 0.91950 0.71264 0.68264 0.03788  -0.09401 -0.02841 162 ASN A ND2 
965  N N   . LYS A 163 ? 0.41931 0.27152 0.24659 0.02421  -0.06842 -0.02082 163 LYS A N   
966  C CA  . LYS A 163 ? 0.45865 0.32030 0.29021 0.02478  -0.05842 -0.01919 163 LYS A CA  
967  C C   . LYS A 163 ? 0.36891 0.23672 0.21761 0.01956  -0.06284 -0.02066 163 LYS A C   
968  O O   . LYS A 163 ? 0.41729 0.29265 0.27015 0.01981  -0.05574 -0.01959 163 LYS A O   
969  C CB  . LYS A 163 ? 0.46394 0.33925 0.29809 0.02590  -0.04859 -0.01447 163 LYS A CB  
970  C CG  . LYS A 163 ? 0.49247 0.36398 0.31184 0.03117  -0.04072 -0.01264 163 LYS A CG  
971  C CD  . LYS A 163 ? 0.48522 0.37041 0.30978 0.03098  -0.03226 -0.00782 163 LYS A CD  
972  C CE  . LYS A 163 ? 0.53144 0.41281 0.34268 0.03567  -0.02524 -0.00590 163 LYS A CE  
973  N NZ  . LYS A 163 ? 0.52536 0.40404 0.33114 0.04002  -0.01892 -0.00696 163 LYS A NZ  
974  N N   . SER A 164 ? 0.32562 0.19120 0.18583 0.01494  -0.07415 -0.02282 164 SER A N   
975  C CA  . SER A 164 ? 0.35664 0.22852 0.23728 0.00913  -0.07834 -0.02422 164 SER A CA  
976  C C   . SER A 164 ? 0.36626 0.22955 0.24246 0.00949  -0.07536 -0.02678 164 SER A C   
977  O O   . SER A 164 ? 0.31623 0.16556 0.17764 0.01261  -0.07656 -0.02889 164 SER A O   
978  C CB  . SER A 164 ? 0.37975 0.25136 0.27616 0.00452  -0.08988 -0.02554 164 SER A CB  
979  O OG  . SER A 164 ? 0.34588 0.22464 0.26560 -0.00144 -0.09202 -0.02613 164 SER A OG  
980  N N   . CYS A 165 ? 0.29716 0.17420 0.19294 0.00719  -0.06711 -0.02345 165 CYS A N   
981  C CA  . CYS A 165 ? 0.31114 0.18267 0.20771 0.00758  -0.06210 -0.02380 165 CYS A CA  
982  C C   . CYS A 165 ? 0.35897 0.21586 0.25949 0.00298  -0.07320 -0.02817 165 CYS A C   
983  O O   . CYS A 165 ? 0.32307 0.16711 0.21576 0.00421  -0.07204 -0.03011 165 CYS A O   
984  C CB  . CYS A 165 ? 0.31276 0.20206 0.23036 0.00575  -0.05224 -0.01892 165 CYS A CB  
985  S SG  . CYS A 165 ? 0.27229 0.17916 0.18778 0.01040  -0.04049 -0.01445 165 CYS A SG  
986  N N   . ALA A 166 ? 0.39232 0.25092 0.30568 -0.00229 -0.08442 -0.02978 166 ALA A N   
987  C CA  . ALA A 166 ? 0.41209 0.26286 0.33499 -0.00687 -0.09387 -0.03222 166 ALA A CA  
988  C C   . ALA A 166 ? 0.47084 0.30572 0.37048 -0.00216 -0.09894 -0.03531 166 ALA A C   
989  O O   . ALA A 166 ? 0.46305 0.28812 0.36394 -0.00416 -0.10441 -0.03775 166 ALA A O   
990  C CB  . ALA A 166 ? 0.38184 0.24592 0.32922 -0.01212 -0.10101 -0.03067 166 ALA A CB  
991  N N   . ILE A 167 ? 0.40559 0.23805 0.28473 0.00408  -0.09656 -0.03482 167 ILE A N   
992  C CA  . ILE A 167 ? 0.46804 0.28566 0.32493 0.00929  -0.10048 -0.03698 167 ILE A CA  
993  C C   . ILE A 167 ? 0.46027 0.26866 0.29482 0.01619  -0.09088 -0.03724 167 ILE A C   
994  O O   . ILE A 167 ? 0.47700 0.27102 0.29822 0.01907  -0.09296 -0.03995 167 ILE A O   
995  C CB  . ILE A 167 ? 0.50066 0.32075 0.35094 0.01192  -0.10354 -0.03540 167 ILE A CB  
996  C CG1 . ILE A 167 ? 0.49890 0.32712 0.37106 0.00623  -0.11353 -0.03524 167 ILE A CG1 
997  C CG2 . ILE A 167 ? 0.55447 0.35824 0.37979 0.01818  -0.10583 -0.03728 167 ILE A CG2 
998  C CD1 . ILE A 167 ? 0.56143 0.38810 0.42588 0.00911  -0.11809 -0.03433 167 ILE A CD1 
999  N N   . ASN A 168 ? 0.40549 0.22327 0.23728 0.01908  -0.08005 -0.03422 168 ASN A N   
1000 C CA  . ASN A 168 ? 0.43427 0.24766 0.24922 0.02607  -0.06913 -0.03334 168 ASN A CA  
1001 C C   . ASN A 168 ? 0.43820 0.26181 0.26168 0.02580  -0.05955 -0.03142 168 ASN A C   
1002 O O   . ASN A 168 ? 0.36947 0.20670 0.19502 0.02744  -0.05200 -0.02793 168 ASN A O   
1003 C CB  . ASN A 168 ? 0.50129 0.31668 0.30206 0.03200  -0.06343 -0.03061 168 ASN A CB  
1004 C CG  . ASN A 168 ? 0.72865 0.53021 0.50943 0.03889  -0.06062 -0.03182 168 ASN A CG  
1005 O OD1 . ASN A 168 ? 0.66190 0.44953 0.43376 0.03930  -0.06953 -0.03505 168 ASN A OD1 
1006 N ND2 . ASN A 168 ? 0.87326 0.67942 0.64818 0.04452  -0.04837 -0.02915 168 ASN A ND2 
1007 N N   . ASN A 169 ? 0.46397 0.28098 0.29355 0.02368  -0.05967 -0.03335 169 ASN A N   
1008 C CA  . ASN A 169 ? 0.47965 0.30914 0.32218 0.02373  -0.04915 -0.02943 169 ASN A CA  
1009 C C   . ASN A 169 ? 0.46639 0.29624 0.29299 0.03256  -0.03729 -0.02767 169 ASN A C   
1010 O O   . ASN A 169 ? 0.41597 0.23121 0.22942 0.03704  -0.03577 -0.02997 169 ASN A O   
1011 C CB  . ASN A 169 ? 0.49179 0.31676 0.35054 0.01848  -0.05121 -0.02950 169 ASN A CB  
1012 C CG  . ASN A 169 ? 0.49858 0.34319 0.37900 0.01640  -0.04167 -0.02323 169 ASN A CG  
1013 O OD1 . ASN A 169 ? 0.43873 0.29224 0.31498 0.02197  -0.03102 -0.01986 169 ASN A OD1 
1014 N ND2 . ASN A 169 ? 0.52963 0.38182 0.43349 0.00871  -0.04555 -0.02159 169 ASN A ND2 
1015 N N   . GLN A 170 ? 0.43667 0.28424 0.26651 0.03489  -0.02909 -0.02330 170 GLN A N   
1016 C CA  . GLN A 170 ? 0.39560 0.24877 0.21604 0.04267  -0.01756 -0.02050 170 GLN A CA  
1017 C C   . GLN A 170 ? 0.41971 0.29566 0.25349 0.04195  -0.01035 -0.01556 170 GLN A C   
1018 O O   . GLN A 170 ? 0.35970 0.24545 0.20769 0.03598  -0.01447 -0.01440 170 GLN A O   
1019 C CB  . GLN A 170 ? 0.47392 0.32222 0.28275 0.04690  -0.01691 -0.01998 170 GLN A CB  
1020 C CG  . GLN A 170 ? 0.66170 0.51699 0.47238 0.04447  -0.01951 -0.01866 170 GLN A CG  
1021 C CD  . GLN A 170 ? 0.79378 0.63937 0.59019 0.04866  -0.02003 -0.01921 170 GLN A CD  
1022 O OE1 . GLN A 170 ? 0.90184 0.73567 0.69051 0.04699  -0.02922 -0.02203 170 GLN A OE1 
1023 N NE2 . GLN A 170 ? 0.80404 0.65492 0.59769 0.05424  -0.01049 -0.01648 170 GLN A NE2 
1024 N N   . ASN A 171 ? 0.36096 0.24966 0.20014 0.04643  -0.00030 -0.01139 171 ASN A N   
1025 C CA  . ASN A 171 ? 0.32263 0.23377 0.17799 0.04500  0.00559  -0.00704 171 ASN A CA  
1026 C C   . ASN A 171 ? 0.37621 0.29334 0.23449 0.04103  0.00229  -0.00651 171 ASN A C   
1027 O O   . ASN A 171 ? 0.33489 0.24484 0.18419 0.04190  0.00029  -0.00734 171 ASN A O   
1028 C CB  . ASN A 171 ? 0.41596 0.33814 0.27733 0.04941  0.01370  -0.00379 171 ASN A CB  
1029 C CG  . ASN A 171 ? 0.57996 0.50292 0.44467 0.05288  0.01761  -0.00259 171 ASN A CG  
1030 O OD1 . ASN A 171 ? 0.69002 0.61472 0.55970 0.05116  0.01731  -0.00235 171 ASN A OD1 
1031 N ND2 . ASN A 171 ? 0.51146 0.43288 0.37288 0.05824  0.02155  -0.00147 171 ASN A ND2 
1032 N N   . LEU A 172 ? 0.30187 0.23103 0.17168 0.03718  0.00175  -0.00500 172 LEU A N   
1033 C CA  . LEU A 172 ? 0.32256 0.25847 0.19682 0.03346  -0.00106 -0.00391 172 LEU A CA  
1034 C C   . LEU A 172 ? 0.29190 0.21397 0.15791 0.03038  -0.01194 -0.00702 172 LEU A C   
1035 O O   . LEU A 172 ? 0.31601 0.24081 0.18392 0.02790  -0.01525 -0.00610 172 LEU A O   
1036 C CB  . LEU A 172 ? 0.26540 0.20754 0.13980 0.03486  0.00420  -0.00156 172 LEU A CB  
1037 C CG  . LEU A 172 ? 0.34676 0.30331 0.23182 0.03675  0.01248  0.00121  172 LEU A CG  
1038 C CD1 . LEU A 172 ? 0.41853 0.37684 0.30014 0.03819  0.01637  0.00299  172 LEU A CD1 
1039 C CD2 . LEU A 172 ? 0.34407 0.31616 0.24440 0.03349  0.01380  0.00297  172 LEU A CD2 
1040 N N   . CYS A 173 ? 0.26532 0.17484 0.12926 0.02924  -0.01788 -0.01034 173 CYS A N   
1041 C CA  . CYS A 173 ? 0.26802 0.16814 0.13271 0.02481  -0.02949 -0.01328 173 CYS A CA  
1042 C C   . CYS A 173 ? 0.24003 0.15479 0.12712 0.01916  -0.03197 -0.01133 173 CYS A C   
1043 O O   . CYS A 173 ? 0.19740 0.12606 0.09959 0.01818  -0.02575 -0.00879 173 CYS A O   
1044 C CB  . CYS A 173 ? 0.30521 0.19036 0.16783 0.02346  -0.03589 -0.01724 173 CYS A CB  
1045 S SG  . CYS A 173 ? 0.31254 0.20596 0.19828 0.01947  -0.03266 -0.01554 173 CYS A SG  
1046 N N   . ILE A 174 ? 0.25597 0.16732 0.14407 0.01624  -0.04104 -0.01254 174 ILE A N   
1047 C CA  . ILE A 174 ? 0.24815 0.17283 0.15642 0.01193  -0.04334 -0.01079 174 ILE A CA  
1048 C C   . ILE A 174 ? 0.23359 0.15802 0.15919 0.00701  -0.05037 -0.01262 174 ILE A C   
1049 O O   . ILE A 174 ? 0.24082 0.15282 0.16182 0.00541  -0.06023 -0.01590 174 ILE A O   
1050 C CB  . ILE A 174 ? 0.21770 0.14028 0.11911 0.01203  -0.04870 -0.01022 174 ILE A CB  
1051 C CG1 . ILE A 174 ? 0.26695 0.19077 0.15332 0.01629  -0.04028 -0.00740 174 ILE A CG1 
1052 C CG2 . ILE A 174 ? 0.24503 0.18059 0.16766 0.00825  -0.05123 -0.00873 174 ILE A CG2 
1053 C CD1 . ILE A 174 ? 0.26940 0.18784 0.14616 0.01702  -0.04339 -0.00611 174 ILE A CD1 
1054 N N   . PRO A 175 ? 0.25139 0.18950 0.19710 0.00469  -0.04530 -0.01044 175 PRO A N   
1055 C CA  . PRO A 175 ? 0.26649 0.20470 0.22965 0.00003  -0.05000 -0.01130 175 PRO A CA  
1056 C C   . PRO A 175 ? 0.27074 0.21296 0.24866 -0.00383 -0.05944 -0.01210 175 PRO A C   
1057 O O   . PRO A 175 ? 0.20362 0.15888 0.20245 -0.00625 -0.05735 -0.01016 175 PRO A O   
1058 C CB  . PRO A 175 ? 0.23902 0.19041 0.21577 0.00014  -0.03960 -0.00793 175 PRO A CB  
1059 C CG  . PRO A 175 ? 0.22417 0.18629 0.19743 0.00336  -0.03316 -0.00599 175 PRO A CG  
1060 C CD  . PRO A 175 ? 0.28433 0.23670 0.23598 0.00663  -0.03467 -0.00724 175 PRO A CD  
1061 N N   . PHE A 176 ? 0.27255 0.20327 0.23900 -0.00374 -0.06981 -0.01494 176 PHE A N   
1062 C CA  . PHE A 176 ? 0.29436 0.22778 0.27365 -0.00666 -0.08030 -0.01589 176 PHE A CA  
1063 C C   . PHE A 176 ? 0.24791 0.18460 0.25024 -0.01204 -0.08497 -0.01666 176 PHE A C   
1064 O O   . PHE A 176 ? 0.26763 0.21406 0.29025 -0.01467 -0.08964 -0.01599 176 PHE A O   
1065 C CB  . PHE A 176 ? 0.18386 0.10281 0.14359 -0.00446 -0.08983 -0.01834 176 PHE A CB  
1066 C CG  . PHE A 176 ? 0.25711 0.17521 0.19912 0.00009  -0.08512 -0.01624 176 PHE A CG  
1067 C CD1 . PHE A 176 ? 0.27276 0.20263 0.22474 0.00014  -0.08275 -0.01342 176 PHE A CD1 
1068 C CD2 . PHE A 176 ? 0.23366 0.13933 0.15050 0.00435  -0.08205 -0.01671 176 PHE A CD2 
1069 C CE1 . PHE A 176 ? 0.28685 0.21553 0.22437 0.00348  -0.07802 -0.01099 176 PHE A CE1 
1070 C CE2 . PHE A 176 ? 0.23784 0.14393 0.14153 0.00791  -0.07612 -0.01389 176 PHE A CE2 
1071 C CZ  . PHE A 176 ? 0.24837 0.16570 0.16245 0.00704  -0.07436 -0.01097 176 PHE A CZ  
1072 N N   . GLN A 177 ? 0.22078 0.14974 0.22116 -0.01353 -0.08298 -0.01764 177 GLN A N   
1073 C CA  . GLN A 177 ? 0.23997 0.17035 0.26250 -0.01946 -0.08740 -0.01799 177 GLN A CA  
1074 C C   . GLN A 177 ? 0.26666 0.21547 0.31412 -0.02139 -0.07768 -0.01331 177 GLN A C   
1075 O O   . GLN A 177 ? 0.30663 0.26072 0.37722 -0.02649 -0.08012 -0.01234 177 GLN A O   
1076 C CB  . GLN A 177 ? 0.27731 0.19195 0.28961 -0.02051 -0.08783 -0.02019 177 GLN A CB  
1077 C CG  . GLN A 177 ? 0.34046 0.25884 0.35312 -0.01895 -0.07382 -0.01650 177 GLN A CG  
1078 C CD  . GLN A 177 ? 0.32447 0.24436 0.31657 -0.01206 -0.06427 -0.01517 177 GLN A CD  
1079 O OE1 . GLN A 177 ? 0.29819 0.21166 0.27142 -0.00846 -0.06775 -0.01736 177 GLN A OE1 
1080 N NE2 . GLN A 177 ? 0.26415 0.19261 0.26004 -0.01012 -0.05220 -0.01129 177 GLN A NE2 
1081 N N   . TYR A 178 ? 0.20121 0.15987 0.24424 -0.01725 -0.06677 -0.01040 178 TYR A N   
1082 C CA  . TYR A 178 ? 0.18581 0.16059 0.24815 -0.01773 -0.05694 -0.00630 178 TYR A CA  
1083 C C   . TYR A 178 ? 0.17024 0.15809 0.24284 -0.01631 -0.05740 -0.00551 178 TYR A C   
1084 O O   . TYR A 178 ? 0.19464 0.18583 0.25596 -0.01222 -0.05285 -0.00511 178 TYR A O   
1085 C CB  . TYR A 178 ? 0.21391 0.19026 0.26485 -0.01382 -0.04449 -0.00385 178 TYR A CB  
1086 C CG  . TYR A 178 ? 0.20615 0.19733 0.27360 -0.01350 -0.03429 0.00028  178 TYR A CG  
1087 C CD1 . TYR A 178 ? 0.20476 0.19948 0.29205 -0.01764 -0.03240 0.00286  178 TYR A CD1 
1088 C CD2 . TYR A 178 ? 0.20732 0.20834 0.27004 -0.00899 -0.02648 0.00167  178 TYR A CD2 
1089 C CE1 . TYR A 178 ? 0.21732 0.22501 0.31772 -0.01653 -0.02198 0.00711  178 TYR A CE1 
1090 C CE2 . TYR A 178 ? 0.23991 0.25322 0.31488 -0.00776 -0.01732 0.00501  178 TYR A CE2 
1091 C CZ  . TYR A 178 ? 0.23436 0.25086 0.32721 -0.01115 -0.01463 0.00791  178 TYR A CZ  
1092 O OH  . TYR A 178 ? 0.25523 0.28328 0.35828 -0.00918 -0.00462 0.01165  178 TYR A OH  
1093 N N   . ALA A 179 ? 0.16376 0.15899 0.25887 -0.01968 -0.06299 -0.00528 179 ALA A N   
1094 C CA  . ALA A 179 ? 0.17944 0.18462 0.28387 -0.01791 -0.06582 -0.00522 179 ALA A CA  
1095 C C   . ALA A 179 ? 0.14289 0.16325 0.25867 -0.01525 -0.05436 -0.00217 179 ALA A C   
1096 O O   . ALA A 179 ? 0.18371 0.20991 0.30003 -0.01221 -0.05457 -0.00246 179 ALA A O   
1097 C CB  . ALA A 179 ? 0.16656 0.17181 0.28400 -0.01974 -0.07307 -0.00566 179 ALA A CB  
1098 N N   . ASN A 180 ? 0.12944 0.15505 0.25319 -0.01602 -0.04456 0.00073  180 ASN A N   
1099 C CA  . ASN A 180 ? 0.17963 0.21935 0.31430 -0.01304 -0.03391 0.00353  180 ASN A CA  
1100 C C   . ASN A 180 ? 0.21366 0.25539 0.33243 -0.00769 -0.02905 0.00262  180 ASN A C   
1101 O O   . ASN A 180 ? 0.14865 0.20035 0.27565 -0.00475 -0.02540 0.00296  180 ASN A O   
1102 C CB  . ASN A 180 ? 0.14968 0.19196 0.28995 -0.01402 -0.02358 0.00731  180 ASN A CB  
1103 C CG  . ASN A 180 ? 0.17625 0.21817 0.33663 -0.02006 -0.02712 0.00896  180 ASN A CG  
1104 O OD1 . ASN A 180 ? 0.21169 0.24151 0.36674 -0.02387 -0.03471 0.00713  180 ASN A OD1 
1105 N ND2 . ASN A 180 ? 0.23130 0.28515 0.41250 -0.02046 -0.02119 0.01226  180 ASN A ND2 
1106 N N   . ASP A 181 ? 0.14390 0.17620 0.24077 -0.00636 -0.02895 0.00139  181 ASP A N   
1107 C CA  . ASP A 181 ? 0.15052 0.18489 0.23369 -0.00214 -0.02446 0.00073  181 ASP A CA  
1108 C C   . ASP A 181 ? 0.14985 0.17311 0.21145 -0.00155 -0.02751 -0.00075 181 ASP A C   
1109 O O   . ASP A 181 ? 0.15157 0.16471 0.20638 -0.00355 -0.03196 -0.00145 181 ASP A O   
1110 C CB  . ASP A 181 ? 0.13693 0.17875 0.21980 0.00084  -0.01311 0.00284  181 ASP A CB  
1111 C CG  . ASP A 181 ? 0.35421 0.40039 0.42775 0.00488  -0.00970 0.00158  181 ASP A CG  
1112 O OD1 . ASP A 181 ? 0.19439 0.24351 0.27270 0.00555  -0.01340 -0.00002 181 ASP A OD1 
1113 O OD2 . ASP A 181 ? 0.41428 0.46029 0.47592 0.00730  -0.00417 0.00203  181 ASP A OD2 
1114 N N   . GLY A 182 ? 0.12936 0.15430 0.18044 0.00128  -0.02493 -0.00126 182 GLY A N   
1115 C CA  . GLY A 182 ? 0.16633 0.18305 0.19827 0.00234  -0.02516 -0.00175 182 GLY A CA  
1116 C C   . GLY A 182 ? 0.18953 0.19990 0.21351 0.00203  -0.03222 -0.00279 182 GLY A C   
1117 O O   . GLY A 182 ? 0.20997 0.21307 0.21786 0.00302  -0.03220 -0.00275 182 GLY A O   
1118 N N   . CYS A 183 ? 0.14857 0.16164 0.18346 0.00120  -0.03770 -0.00331 183 CYS A N   
1119 C CA  . CYS A 183 ? 0.17467 0.18044 0.20174 0.00122  -0.04510 -0.00371 183 CYS A CA  
1120 C C   . CYS A 183 ? 0.16256 0.16744 0.17685 0.00288  -0.04080 -0.00276 183 CYS A C   
1121 O O   . CYS A 183 ? 0.14222 0.13790 0.14195 0.00314  -0.04368 -0.00208 183 CYS A O   
1122 C CB  . CYS A 183 ? 0.16315 0.17363 0.20588 0.00104  -0.05078 -0.00413 183 CYS A CB  
1123 S SG  . CYS A 183 ? 0.25684 0.28082 0.31307 0.00325  -0.04311 -0.00409 183 CYS A SG  
1124 N N   . TYR A 184 ? 0.10737 0.12168 0.12699 0.00403  -0.03381 -0.00261 184 TYR A N   
1125 C CA  . TYR A 184 ? 0.11436 0.12942 0.12526 0.00485  -0.02987 -0.00183 184 TYR A CA  
1126 C C   . TYR A 184 ? 0.14199 0.15149 0.13722 0.00533  -0.02675 -0.00059 184 TYR A C   
1127 O O   . TYR A 184 ? 0.14065 0.14529 0.12576 0.00527  -0.02689 0.00090  184 TYR A O   
1128 C CB  . TYR A 184 ? 0.14852 0.17455 0.16766 0.00618  -0.02367 -0.00271 184 TYR A CB  
1129 C CG  . TYR A 184 ? 0.10495 0.13683 0.12902 0.00732  -0.01869 -0.00291 184 TYR A CG  
1130 C CD1 . TYR A 184 ? 0.10476 0.14070 0.14195 0.00736  -0.01919 -0.00330 184 TYR A CD1 
1131 C CD2 . TYR A 184 ? 0.14026 0.17369 0.15637 0.00864  -0.01308 -0.00217 184 TYR A CD2 
1132 C CE1 . TYR A 184 ? 0.12822 0.16865 0.16952 0.00828  -0.01373 -0.00249 184 TYR A CE1 
1133 C CE2 . TYR A 184 ? 0.14119 0.17858 0.16056 0.01007  -0.00837 -0.00167 184 TYR A CE2 
1134 C CZ  . TYR A 184 ? 0.16076 0.20111 0.19224 0.00967  -0.00852 -0.00162 184 TYR A CZ  
1135 O OH  . TYR A 184 ? 0.18628 0.22963 0.22051 0.01093  -0.00310 -0.00021 184 TYR A OH  
1136 N N   . ALA A 185 ? 0.14466 0.15436 0.13784 0.00610  -0.02350 -0.00085 185 ALA A N   
1137 C CA  . ALA A 185 ? 0.12570 0.13005 0.10421 0.00763  -0.02004 0.00006  185 ALA A CA  
1138 C C   . ALA A 185 ? 0.15426 0.14503 0.11974 0.00748  -0.02585 -0.00007 185 ALA A C   
1139 O O   . ALA A 185 ? 0.19885 0.18399 0.14993 0.00909  -0.02368 0.00118  185 ALA A O   
1140 C CB  . ALA A 185 ? 0.11334 0.12048 0.09319 0.00910  -0.01519 -0.00016 185 ALA A CB  
1141 N N   . ARG A 186 ? 0.14632 0.13204 0.11685 0.00582  -0.03324 -0.00159 186 ARG A N   
1142 C CA  . ARG A 186 ? 0.19197 0.16400 0.14955 0.00592  -0.04062 -0.00243 186 ARG A CA  
1143 C C   . ARG A 186 ? 0.20542 0.17333 0.15397 0.00655  -0.04282 -0.00058 186 ARG A C   
1144 O O   . ARG A 186 ? 0.22581 0.18372 0.15619 0.00846  -0.04292 0.00029  186 ARG A O   
1145 C CB  . ARG A 186 ? 0.17098 0.14022 0.13937 0.00350  -0.04950 -0.00455 186 ARG A CB  
1146 C CG  . ARG A 186 ? 0.17433 0.14677 0.15300 0.00214  -0.04698 -0.00555 186 ARG A CG  
1147 C CD  . ARG A 186 ? 0.24977 0.21638 0.23665 -0.00082 -0.05679 -0.00769 186 ARG A CD  
1148 N NE  . ARG A 186 ? 0.24998 0.22274 0.25248 -0.00247 -0.06319 -0.00767 186 ARG A NE  
1149 C CZ  . ARG A 186 ? 0.23151 0.21666 0.25582 -0.00402 -0.06091 -0.00686 186 ARG A CZ  
1150 N NH1 . ARG A 186 ? 0.14743 0.13977 0.17955 -0.00431 -0.05225 -0.00568 186 ARG A NH1 
1151 N NH2 . ARG A 186 ? 0.24672 0.23695 0.28443 -0.00458 -0.06686 -0.00694 186 ARG A NH2 
1152 N N   . ALA A 187 ? 0.19839 0.17334 0.15871 0.00537  -0.04378 0.00029  187 ALA A N   
1153 C CA  . ALA A 187 ? 0.16351 0.13376 0.11614 0.00571  -0.04550 0.00268  187 ALA A CA  
1154 C C   . ALA A 187 ? 0.17822 0.14968 0.12069 0.00663  -0.03686 0.00544  187 ALA A C   
1155 O O   . ALA A 187 ? 0.17628 0.13946 0.10480 0.00751  -0.03689 0.00815  187 ALA A O   
1156 C CB  . ALA A 187 ? 0.11381 0.09077 0.08220 0.00455  -0.04816 0.00270  187 ALA A CB  
1157 N N   . HIS A 188 ? 0.16874 0.15091 0.11866 0.00657  -0.02939 0.00511  188 HIS A N   
1158 C CA  . HIS A 188 ? 0.18915 0.17495 0.13344 0.00711  -0.02163 0.00773  188 HIS A CA  
1159 C C   . HIS A 188 ? 0.25770 0.23594 0.18457 0.00995  -0.01816 0.00876  188 HIS A C   
1160 O O   . HIS A 188 ? 0.17861 0.15493 0.09590 0.01087  -0.01330 0.01198  188 HIS A O   
1161 C CB  . HIS A 188 ? 0.15243 0.15210 0.10970 0.00676  -0.01592 0.00670  188 HIS A CB  
1162 C CG  . HIS A 188 ? 0.18847 0.19454 0.14936 0.00535  -0.01160 0.00881  188 HIS A CG  
1163 N ND1 . HIS A 188 ? 0.22173 0.22478 0.18519 0.00306  -0.01457 0.01030  188 HIS A ND1 
1164 C CD2 . HIS A 188 ? 0.14151 0.15678 0.10511 0.00571  -0.00505 0.00970  188 HIS A CD2 
1165 C CE1 . HIS A 188 ? 0.21905 0.22865 0.18698 0.00141  -0.00996 0.01196  188 HIS A CE1 
1166 N NE2 . HIS A 188 ? 0.16411 0.18198 0.13281 0.00294  -0.00439 0.01153  188 HIS A NE2 
1167 N N   . MET A 189 ? 0.20664 0.18032 0.12974 0.01145  -0.02020 0.00614  189 MET A N   
1168 C CA  . MET A 189 ? 0.17624 0.14050 0.08126 0.01492  -0.01760 0.00629  189 MET A CA  
1169 C C   . MET A 189 ? 0.21775 0.16785 0.10589 0.01600  -0.02252 0.00736  189 MET A C   
1170 O O   . MET A 189 ? 0.26382 0.21128 0.14283 0.01798  -0.01661 0.00910  189 MET A O   
1171 C CB  . MET A 189 ? 0.24518 0.20574 0.15033 0.01593  -0.01961 0.00288  189 MET A CB  
1172 C CG  . MET A 189 ? 0.27526 0.22752 0.16345 0.02029  -0.01515 0.00252  189 MET A CG  
1173 S SD  . MET A 189 ? 0.26522 0.23159 0.15927 0.02222  -0.00247 0.00552  189 MET A SD  
1174 C CE  . MET A 189 ? 0.37421 0.33188 0.25712 0.02623  0.00146  0.00447  189 MET A CE  
1175 N N   . MET A 190 ? 0.24767 0.19201 0.13844 0.01415  -0.03235 0.00600  190 MET A N   
1176 C CA  . MET A 190 ? 0.24413 0.17816 0.12500 0.01480  -0.03616 0.00685  190 MET A CA  
1177 C C   . MET A 190 ? 0.26140 0.19724 0.13775 0.01487  -0.03017 0.01188  190 MET A C   
1178 O O   . MET A 190 ? 0.25703 0.18617 0.12104 0.01687  -0.02715 0.01374  190 MET A O   
1179 C CB  . MET A 190 ? 0.19377 0.12436 0.08268 0.01282  -0.04742 0.00483  190 MET A CB  
1180 C CG  . MET A 190 ? 0.22394 0.14984 0.11558 0.01244  -0.05407 0.00025  190 MET A CG  
1181 S SD  . MET A 190 ? 0.26066 0.18215 0.16197 0.01059  -0.06671 -0.00195 190 MET A SD  
1182 C CE  . MET A 190 ? 0.19195 0.12906 0.11945 0.00731  -0.06830 -0.00214 190 MET A CE  
1183 N N   . ARG A 191 ? 0.19494 0.13922 0.08112 0.01269  -0.02864 0.01417  191 ARG A N   
1184 C CA  . ARG A 191 ? 0.19469 0.14143 0.07966 0.01170  -0.02233 0.01925  191 ARG A CA  
1185 C C   . ARG A 191 ? 0.24927 0.19901 0.12644 0.01376  -0.01149 0.02172  191 ARG A C   
1186 O O   . ARG A 191 ? 0.23010 0.17653 0.09987 0.01413  -0.00714 0.02575  191 ARG A O   
1187 C CB  . ARG A 191 ? 0.17689 0.13715 0.08376 0.00791  -0.02067 0.01902  191 ARG A CB  
1188 C CG  . ARG A 191 ? 0.19606 0.15933 0.10488 0.00572  -0.01447 0.02405  191 ARG A CG  
1189 C CD  . ARG A 191 ? 0.23121 0.21011 0.15869 0.00308  -0.00962 0.02273  191 ARG A CD  
1190 N NE  . ARG A 191 ? 0.20685 0.18865 0.14009 -0.00022 -0.00562 0.02681  191 ARG A NE  
1191 C CZ  . ARG A 191 ? 0.23502 0.22858 0.17821 -0.00210 0.00102  0.02772  191 ARG A CZ  
1192 N NH1 . ARG A 191 ? 0.24633 0.24990 0.19354 -0.00020 0.00465  0.02506  191 ARG A NH1 
1193 N NH2 . ARG A 191 ? 0.24920 0.24420 0.19877 -0.00593 0.00366  0.03149  191 ARG A NH2 
1194 N N   . GLN A 192 ? 0.22983 0.18749 0.11189 0.01496  -0.00685 0.01931  192 GLN A N   
1195 C CA  . GLN A 192 ? 0.27657 0.23958 0.15684 0.01668  0.00281  0.02088  192 GLN A CA  
1196 C C   . GLN A 192 ? 0.26818 0.22069 0.13457 0.01950  0.00314  0.02068  192 GLN A C   
1197 O O   . GLN A 192 ? 0.31219 0.26563 0.17420 0.02028  0.00976  0.02419  192 GLN A O   
1198 C CB  . GLN A 192 ? 0.20131 0.17292 0.08957 0.01802  0.00615  0.01772  192 GLN A CB  
1199 C CG  . GLN A 192 ? 0.27371 0.25184 0.16350 0.01968  0.01510  0.01912  192 GLN A CG  
1200 C CD  . GLN A 192 ? 0.39536 0.37819 0.29077 0.02190  0.01697  0.01583  192 GLN A CD  
1201 O OE1 . GLN A 192 ? 0.58577 0.56235 0.47385 0.02516  0.01799  0.01418  192 GLN A OE1 
1202 N NE2 . GLN A 192 ? 0.31389 0.30708 0.22176 0.02072  0.01732  0.01501  192 GLN A NE2 
1203 N N   . HIS A 193 ? 0.26109 0.20339 0.12064 0.02111  -0.00411 0.01656  193 HIS A N   
1204 C CA  . HIS A 193 ? 0.37034 0.30040 0.21469 0.02449  -0.00527 0.01549  193 HIS A CA  
1205 C C   . HIS A 193 ? 0.40330 0.32685 0.23882 0.02438  -0.00626 0.01933  193 HIS A C   
1206 O O   . HIS A 193 ? 0.36126 0.27966 0.18526 0.02725  -0.00179 0.02114  193 HIS A O   
1207 C CB  . HIS A 193 ? 0.32841 0.24799 0.16839 0.02546  -0.01449 0.01009  193 HIS A CB  
1208 C CG  . HIS A 193 ? 0.37114 0.29339 0.21574 0.02644  -0.01305 0.00671  193 HIS A CG  
1209 N ND1 . HIS A 193 ? 0.32958 0.25353 0.17082 0.02976  -0.00536 0.00674  193 HIS A ND1 
1210 C CD2 . HIS A 193 ? 0.34212 0.26524 0.19457 0.02471  -0.01837 0.00355  193 HIS A CD2 
1211 C CE1 . HIS A 193 ? 0.39176 0.31683 0.23787 0.03023  -0.00595 0.00383  193 HIS A CE1 
1212 N NE2 . HIS A 193 ? 0.32119 0.24563 0.17356 0.02708  -0.01351 0.00197  193 HIS A NE2 
1213 N N   . MET A 194 ? 0.33419 0.25716 0.17465 0.02149  -0.01224 0.02067  194 MET A N   
1214 C CA  . MET A 194 ? 0.33221 0.24940 0.16563 0.02119  -0.01272 0.02528  194 MET A CA  
1215 C C   . MET A 194 ? 0.36391 0.28743 0.19719 0.02060  -0.00194 0.03127  194 MET A C   
1216 O O   . MET A 194 ? 0.30989 0.22736 0.13158 0.02259  0.00160  0.03451  194 MET A O   
1217 C CB  . MET A 194 ? 0.36827 0.28568 0.21047 0.01802  -0.01982 0.02628  194 MET A CB  
1218 C CG  . MET A 194 ? 0.44628 0.35452 0.28613 0.01864  -0.03113 0.02274  194 MET A CG  
1219 S SD  . MET A 194 ? 0.41912 0.33008 0.27231 0.01516  -0.03734 0.02493  194 MET A SD  
1220 C CE  . MET A 194 ? 0.33798 0.24725 0.20007 0.01500  -0.04970 0.01808  194 MET A CE  
1221 N N   . ASN A 195 ? 0.31404 0.24970 0.16073 0.01769  0.00301  0.03288  195 ASN A N   
1222 C CA  . ASN A 195 ? 0.31849 0.26189 0.16936 0.01582  0.01287  0.03871  195 ASN A CA  
1223 C C   . ASN A 195 ? 0.44493 0.38928 0.28877 0.01907  0.02062  0.03904  195 ASN A C   
1224 O O   . ASN A 195 ? 0.37899 0.32355 0.21934 0.01873  0.02732  0.04431  195 ASN A O   
1225 C CB  . ASN A 195 ? 0.32228 0.27881 0.18932 0.01268  0.01617  0.03888  195 ASN A CB  
1226 C CG  . ASN A 195 ? 0.31315 0.26741 0.18606 0.00964  0.00978  0.03978  195 ASN A CG  
1227 O OD1 . ASN A 195 ? 0.34719 0.29057 0.21382 0.00918  0.00319  0.04107  195 ASN A OD1 
1228 N ND2 . ASN A 195 ? 0.28162 0.24884 0.17245 0.00697  0.01071  0.03754  195 ASN A ND2 
1229 N N   . TYR A 196 ? 0.40812 0.35186 0.24963 0.02241  0.01960  0.03364  196 TYR A N   
1230 C CA  . TYR A 196 ? 0.48865 0.43092 0.32211 0.02663  0.02598  0.03335  196 TYR A CA  
1231 C C   . TYR A 196 ? 0.48856 0.41791 0.30413 0.02969  0.02568  0.03553  196 TYR A C   
1232 O O   . TYR A 196 ? 0.47270 0.40193 0.28183 0.03238  0.03333  0.03828  196 TYR A O   
1233 C CB  . TYR A 196 ? 0.54022 0.48061 0.37278 0.02998  0.02352  0.02719  196 TYR A CB  
1234 C CG  . TYR A 196 ? 0.72569 0.67970 0.57331 0.02910  0.02828  0.02621  196 TYR A CG  
1235 C CD1 . TYR A 196 ? 0.76966 0.73524 0.62647 0.02776  0.03665  0.03020  196 TYR A CD1 
1236 C CD2 . TYR A 196 ? 0.86020 0.81531 0.71331 0.02961  0.02421  0.02145  196 TYR A CD2 
1237 C CE1 . TYR A 196 ? 0.87541 0.85337 0.74642 0.02738  0.04011  0.02899  196 TYR A CE1 
1238 C CE2 . TYR A 196 ? 0.88385 0.85095 0.75027 0.02931  0.02823  0.02071  196 TYR A CE2 
1239 C CZ  . TYR A 196 ? 0.94016 0.91865 0.81546 0.02837  0.03575  0.02425  196 TYR A CZ  
1240 O OH  . TYR A 196 ? 1.01634 1.00646 0.90506 0.02853  0.03874  0.02328  196 TYR A OH  
1241 N N   . ALA A 197 ? 0.38368 0.30221 0.19140 0.02961  0.01681  0.03430  197 ALA A N   
1242 C CA  . ALA A 197 ? 0.45017 0.35573 0.24033 0.03261  0.01548  0.03642  197 ALA A CA  
1243 C C   . ALA A 197 ? 0.49263 0.39869 0.28396 0.02933  0.01736  0.04351  197 ALA A C   
1244 O O   . ALA A 197 ? 0.54240 0.43717 0.32085 0.03102  0.01368  0.04541  197 ALA A O   
1245 C CB  . ALA A 197 ? 0.46228 0.35473 0.24280 0.03476  0.00407  0.03093  197 ALA A CB  
1246 N N   . SER A 198 ? 0.50361 0.42193 0.31024 0.02470  0.02288  0.04744  198 SER A N   
1247 C CA  . SER A 198 ? 0.47804 0.39675 0.28818 0.02073  0.02518  0.05467  198 SER A CA  
1248 C C   . SER A 198 ? 0.47008 0.37938 0.27770 0.01978  0.01475  0.05451  198 SER A C   
1249 O O   . SER A 198 ? 0.46791 0.37042 0.27012 0.01895  0.01458  0.06005  198 SER A O   
1250 C CB  . SER A 198 ? 0.57498 0.48970 0.37391 0.02250  0.03342  0.06063  198 SER A CB  
1251 O OG  . SER A 198 ? 0.62627 0.55215 0.43263 0.02216  0.04392  0.06215  198 SER A OG  
1252 N N   . LYS A 199 ? 0.34932 0.25819 0.16168 0.01999  0.00598  0.04821  199 LYS A N   
1253 C CA  . LYS A 199 ? 0.38778 0.28985 0.20185 0.01886  -0.00432 0.04733  199 LYS A CA  
1254 C C   . LYS A 199 ? 0.43401 0.34470 0.26511 0.01494  -0.00646 0.04605  199 LYS A C   
1255 O O   . LYS A 199 ? 0.37560 0.29643 0.21503 0.01404  -0.00195 0.04395  199 LYS A O   
1256 C CB  . LYS A 199 ? 0.40898 0.30173 0.21416 0.02239  -0.01418 0.04077  199 LYS A CB  
1257 C CG  . LYS A 199 ? 0.42630 0.30798 0.21222 0.02687  -0.01335 0.04144  199 LYS A CG  
1258 C CD  . LYS A 199 ? 0.47043 0.34343 0.24875 0.02707  -0.01589 0.04678  199 LYS A CD  
1259 C CE  . LYS A 199 ? 0.58501 0.44449 0.34267 0.03225  -0.01889 0.04569  199 LYS A CE  
1260 N NZ  . LYS A 199 ? 0.60097 0.45154 0.34985 0.03297  -0.02099 0.05140  199 LYS A NZ  
1261 N N   . ASP A 200 ? 0.43249 0.33866 0.26855 0.01298  -0.01361 0.04710  200 ASP A N   
1262 C CA  . ASP A 200 ? 0.35126 0.26361 0.20226 0.00961  -0.01700 0.04525  200 ASP A CA  
1263 C C   . ASP A 200 ? 0.44306 0.34972 0.29841 0.00995  -0.02957 0.04155  200 ASP A C   
1264 O O   . ASP A 200 ? 0.37910 0.27687 0.22573 0.01252  -0.03498 0.04114  200 ASP A O   
1265 C CB  . ASP A 200 ? 0.36431 0.27918 0.22248 0.00506  -0.01050 0.05181  200 ASP A CB  
1266 C CG  . ASP A 200 ? 0.37605 0.30620 0.25729 0.00120  -0.01005 0.04721  200 ASP A CG  
1267 O OD1 . ASP A 200 ? 0.38001 0.31665 0.26622 0.00271  -0.01316 0.04093  200 ASP A OD1 
1268 O OD2 . ASP A 200 ? 0.38168 0.31802 0.27748 -0.00336 -0.00661 0.04942  200 ASP A OD2 
1269 N N   . CYS A 201 ? 0.30517 0.21786 0.17490 0.00752  -0.03425 0.03872  201 CYS A N   
1270 C CA  . CYS A 201 ? 0.29650 0.20766 0.17556 0.00793  -0.04550 0.03475  201 CYS A CA  
1271 C C   . CYS A 201 ? 0.29585 0.21585 0.19639 0.00444  -0.04581 0.03379  201 CYS A C   
1272 O O   . CYS A 201 ? 0.29660 0.22457 0.20567 0.00125  -0.03770 0.03521  201 CYS A O   
1273 C CB  . CYS A 201 ? 0.28203 0.19824 0.16556 0.00940  -0.04989 0.02777  201 CYS A CB  
1274 S SG  . CYS A 201 ? 0.33607 0.26793 0.23324 0.00736  -0.04324 0.02424  201 CYS A SG  
1275 N N   . TYR A 202 ? 0.26685 0.18610 0.17731 0.00530  -0.05500 0.03088  202 TYR A N   
1276 C CA  . TYR A 202 ? 0.23265 0.16309 0.16537 0.00326  -0.05517 0.02709  202 TYR A CA  
1277 C C   . TYR A 202 ? 0.26032 0.20051 0.20372 0.00427  -0.05817 0.02094  202 TYR A C   
1278 O O   . TYR A 202 ? 0.26001 0.19670 0.19440 0.00606  -0.06164 0.01970  202 TYR A O   
1279 C CB  . TYR A 202 ? 0.24199 0.16567 0.18042 0.00406  -0.06192 0.02837  202 TYR A CB  
1280 C CG  . TYR A 202 ? 0.28520 0.19923 0.21581 0.00225  -0.05815 0.03482  202 TYR A CG  
1281 C CD1 . TYR A 202 ? 0.27727 0.19728 0.21808 -0.00189 -0.05094 0.03546  202 TYR A CD1 
1282 C CD2 . TYR A 202 ? 0.34099 0.23949 0.25390 0.00457  -0.06194 0.04048  202 TYR A CD2 
1283 C CE1 . TYR A 202 ? 0.36133 0.27244 0.29706 -0.00446 -0.04728 0.04179  202 TYR A CE1 
1284 C CE2 . TYR A 202 ? 0.42566 0.31463 0.33161 0.00266  -0.05756 0.04739  202 TYR A CE2 
1285 C CZ  . TYR A 202 ? 0.41316 0.30870 0.33158 -0.00225 -0.05004 0.04811  202 TYR A CZ  
1286 O OH  . TYR A 202 ? 0.56330 0.44927 0.47673 -0.00500 -0.04556 0.05536  202 TYR A OH  
1287 N N   . LYS A 203 ? 0.19141 0.14307 0.15316 0.00311  -0.05645 0.01723  203 LYS A N   
1288 C CA  . LYS A 203 ? 0.19422 0.15512 0.16853 0.00412  -0.05892 0.01227  203 LYS A CA  
1289 C C   . LYS A 203 ? 0.20708 0.16781 0.19395 0.00594  -0.06632 0.01072  203 LYS A C   
1290 O O   . LYS A 203 ? 0.25286 0.21232 0.24518 0.00586  -0.06597 0.01140  203 LYS A O   
1291 C CB  . LYS A 203 ? 0.20052 0.17457 0.18527 0.00267  -0.05105 0.00942  203 LYS A CB  
1292 C CG  . LYS A 203 ? 0.19356 0.16999 0.16873 0.00141  -0.04318 0.01088  203 LYS A CG  
1293 C CD  . LYS A 203 ? 0.20011 0.17627 0.16890 0.00271  -0.04352 0.00950  203 LYS A CD  
1294 C CE  . LYS A 203 ? 0.16153 0.14084 0.12201 0.00255  -0.03528 0.01060  203 LYS A CE  
1295 N NZ  . LYS A 203 ? 0.10677 0.09901 0.07884 0.00171  -0.02904 0.00872  203 LYS A NZ  
1296 N N   . ILE A 204 ? 0.21983 0.18133 0.21170 0.00768  -0.07332 0.00871  204 ILE A N   
1297 C CA  . ILE A 204 ? 0.17807 0.14364 0.18614 0.00949  -0.07729 0.00644  204 ILE A CA  
1298 C C   . ILE A 204 ? 0.13548 0.11480 0.15984 0.00927  -0.07314 0.00253  204 ILE A C   
1299 O O   . ILE A 204 ? 0.19897 0.18128 0.22275 0.00808  -0.07194 0.00140  204 ILE A O   
1300 C CB  . ILE A 204 ? 0.18804 0.14564 0.19272 0.01083  -0.08401 0.00667  204 ILE A CB  
1301 C CG1 . ILE A 204 ? 0.22117 0.18446 0.24377 0.01278  -0.08650 0.00435  204 ILE A CG1 
1302 C CG2 . ILE A 204 ? 0.14673 0.10278 0.14502 0.00984  -0.08546 0.00533  204 ILE A CG2 
1303 C CD1 . ILE A 204 ? 0.22346 0.17936 0.24397 0.01442  -0.09414 0.00474  204 ILE A CD1 
1304 N N   . PHE A 205 ? 0.16677 0.15334 0.20447 0.01065  -0.07055 0.00068  205 PHE A N   
1305 C CA  . PHE A 205 ? 0.14790 0.14695 0.20034 0.01129  -0.06538 -0.00242 205 PHE A CA  
1306 C C   . PHE A 205 ? 0.11927 0.12034 0.18414 0.01351  -0.06787 -0.00357 205 PHE A C   
1307 O O   . PHE A 205 ? 0.14815 0.14465 0.21468 0.01564  -0.07102 -0.00339 205 PHE A O   
1308 C CB  . PHE A 205 ? 0.12224 0.12828 0.17966 0.01217  -0.05975 -0.00431 205 PHE A CB  
1309 C CG  . PHE A 205 ? 0.14332 0.14975 0.18937 0.00937  -0.05339 -0.00369 205 PHE A CG  
1310 C CD1 . PHE A 205 ? 0.11470 0.11289 0.14816 0.00730  -0.05290 -0.00126 205 PHE A CD1 
1311 C CD2 . PHE A 205 ? 0.14315 0.15844 0.19184 0.00903  -0.04739 -0.00509 205 PHE A CD2 
1312 C CE1 . PHE A 205 ? 0.14945 0.14969 0.17460 0.00501  -0.04667 -0.00050 205 PHE A CE1 
1313 C CE2 . PHE A 205 ? 0.11619 0.13248 0.15523 0.00720  -0.04175 -0.00450 205 PHE A CE2 
1314 C CZ  . PHE A 205 ? 0.18412 0.19361 0.21209 0.00523  -0.04144 -0.00235 205 PHE A CZ  
1315 N N   . ALA A 206 ? 0.14288 0.15060 0.21693 0.01301  -0.06668 -0.00447 206 ALA A N   
1316 C CA  . ALA A 206 ? 0.13616 0.14909 0.22471 0.01517  -0.06739 -0.00547 206 ALA A CA  
1317 C C   . ALA A 206 ? 0.14747 0.17243 0.24713 0.01625  -0.05912 -0.00695 206 ALA A C   
1318 O O   . ALA A 206 ? 0.16225 0.19164 0.26020 0.01448  -0.05443 -0.00690 206 ALA A O   
1319 C CB  . ALA A 206 ? 0.12335 0.13476 0.21549 0.01379  -0.07295 -0.00490 206 ALA A CB  
1320 N N   . TYR A 207 ? 0.14296 0.17268 0.25291 0.01965  -0.05720 -0.00810 207 TYR A N   
1321 C CA  . TYR A 207 ? 0.12468 0.16523 0.24363 0.02169  -0.04881 -0.00922 207 TYR A CA  
1322 C C   . TYR A 207 ? 0.15538 0.20253 0.28888 0.02400  -0.04856 -0.00895 207 TYR A C   
1323 O O   . TYR A 207 ? 0.19547 0.23874 0.33223 0.02575  -0.05432 -0.00899 207 TYR A O   
1324 C CB  . TYR A 207 ? 0.16207 0.20225 0.27734 0.02493  -0.04496 -0.01153 207 TYR A CB  
1325 C CG  . TYR A 207 ? 0.12475 0.15803 0.22746 0.02314  -0.04659 -0.01196 207 TYR A CG  
1326 C CD1 . TYR A 207 ? 0.12881 0.15150 0.22485 0.02275  -0.05350 -0.01127 207 TYR A CD1 
1327 C CD2 . TYR A 207 ? 0.12473 0.16234 0.22254 0.02210  -0.04107 -0.01268 207 TYR A CD2 
1328 C CE1 . TYR A 207 ? 0.15709 0.17414 0.24264 0.02086  -0.05476 -0.01088 207 TYR A CE1 
1329 C CE2 . TYR A 207 ? 0.08684 0.11972 0.17466 0.02039  -0.04259 -0.01296 207 TYR A CE2 
1330 C CZ  . TYR A 207 ? 0.12220 0.14510 0.20440 0.01952  -0.04936 -0.01188 207 TYR A CZ  
1331 O OH  . TYR A 207 ? 0.15719 0.17462 0.22749 0.01654  -0.04874 -0.01113 207 TYR A OH  
1332 N N   . GLY A 208 ? 0.09432 0.15165 0.23653 0.02441  -0.04156 -0.00839 208 GLY A N   
1333 C CA  . GLY A 208 ? 0.09398 0.15960 0.25105 0.02702  -0.03969 -0.00775 208 GLY A CA  
1334 C C   . GLY A 208 ? 0.15110 0.22582 0.31731 0.02486  -0.03436 -0.00581 208 GLY A C   
1335 O O   . GLY A 208 ? 0.13518 0.21126 0.29582 0.02301  -0.02927 -0.00527 208 GLY A O   
1336 N N   . ASN A 209 ? 0.13729 0.21836 0.31845 0.02513  -0.03559 -0.00457 209 ASN A N   
1337 C CA  . ASN A 209 ? 0.14009 0.22858 0.33215 0.02203  -0.03208 -0.00240 209 ASN A CA  
1338 C C   . ASN A 209 ? 0.16764 0.24978 0.36042 0.01648  -0.04095 -0.00190 209 ASN A C   
1339 O O   . ASN A 209 ? 0.15646 0.24099 0.36198 0.01515  -0.04621 -0.00119 209 ASN A O   
1340 C CB  . ASN A 209 ? 0.09864 0.19825 0.30804 0.02511  -0.02834 -0.00118 209 ASN A CB  
1341 C CG  . ASN A 209 ? 0.25319 0.36048 0.47558 0.02153  -0.02426 0.00150  209 ASN A CG  
1342 O OD1 . ASN A 209 ? 0.30229 0.40782 0.51920 0.01819  -0.02083 0.00247  209 ASN A OD1 
1343 N ND2 . ASN A 209 ? 0.32684 0.44258 0.56745 0.02213  -0.02474 0.00290  209 ASN A ND2 
1344 N N   . LEU A 210 ? 0.14704 0.22092 0.32575 0.01365  -0.04295 -0.00246 210 LEU A N   
1345 C CA  . LEU A 210 ? 0.12887 0.19414 0.30362 0.00957  -0.05219 -0.00263 210 LEU A CA  
1346 C C   . LEU A 210 ? 0.17933 0.24843 0.36508 0.00539  -0.05141 -0.00106 210 LEU A C   
1347 O O   . LEU A 210 ? 0.15246 0.22688 0.34059 0.00457  -0.04323 0.00029  210 LEU A O   
1348 C CB  . LEU A 210 ? 0.08702 0.14218 0.24231 0.00860  -0.05428 -0.00363 210 LEU A CB  
1349 C CG  . LEU A 210 ? 0.13123 0.18195 0.27545 0.01207  -0.05426 -0.00485 210 LEU A CG  
1350 C CD1 . LEU A 210 ? 0.14592 0.18749 0.27232 0.01049  -0.05617 -0.00522 210 LEU A CD1 
1351 C CD2 . LEU A 210 ? 0.18773 0.23489 0.33521 0.01433  -0.06128 -0.00529 210 LEU A CD2 
1352 N N   . LYS A 211 ? 0.17123 0.23719 0.36387 0.00292  -0.06015 -0.00118 211 LYS A N   
1353 C CA  . LYS A 211 ? 0.19610 0.26406 0.40015 -0.00155 -0.06126 0.00007  211 LYS A CA  
1354 C C   . LYS A 211 ? 0.11027 0.16694 0.30745 -0.00428 -0.07309 -0.00149 211 LYS A C   
1355 O O   . LYS A 211 ? 0.20523 0.25710 0.39923 -0.00251 -0.08106 -0.00274 211 LYS A O   
1356 C CB  . LYS A 211 ? 0.15960 0.23929 0.38632 -0.00139 -0.05873 0.00185  211 LYS A CB  
1357 C CG  . LYS A 211 ? 0.25675 0.34780 0.49022 0.00185  -0.04640 0.00362  211 LYS A CG  
1358 C CD  . LYS A 211 ? 0.32835 0.43090 0.58503 0.00159  -0.04429 0.00579  211 LYS A CD  
1359 C CE  . LYS A 211 ? 0.35922 0.47228 0.62112 0.00717  -0.03486 0.00664  211 LYS A CE  
1360 N NZ  . LYS A 211 ? 0.48231 0.59892 0.73788 0.00851  -0.02270 0.00815  211 LYS A NZ  
1361 N N   . VAL A 212 ? 0.10793 0.15965 0.30196 -0.00819 -0.07442 -0.00144 212 VAL A N   
1362 C CA  . VAL A 212 ? 0.13473 0.17505 0.32133 -0.01043 -0.08574 -0.00325 212 VAL A CA  
1363 C C   . VAL A 212 ? 0.20291 0.24446 0.40300 -0.01521 -0.08761 -0.00257 212 VAL A C   
1364 O O   . VAL A 212 ? 0.25231 0.30054 0.46168 -0.01727 -0.07923 -0.00045 212 VAL A O   
1365 C CB  . VAL A 212 ? 0.25828 0.28609 0.41997 -0.00993 -0.08796 -0.00483 212 VAL A CB  
1366 C CG1 . VAL A 212 ? 0.27011 0.29630 0.41905 -0.00571 -0.08599 -0.00511 212 VAL A CG1 
1367 C CG2 . VAL A 212 ? 0.23360 0.26189 0.39191 -0.01227 -0.08112 -0.00408 212 VAL A CG2 
1368 N N   . ASN A 213 ? 0.14573 0.18037 0.34688 -0.01689 -0.09876 -0.00424 213 ASN A N   
1369 C CA  . ASN A 213 ? 0.20490 0.23736 0.41540 -0.02176 -0.10257 -0.00429 213 ASN A CA  
1370 C C   . ASN A 213 ? 0.25165 0.26860 0.44002 -0.02269 -0.10864 -0.00686 213 ASN A C   
1371 O O   . ASN A 213 ? 0.20221 0.20875 0.37545 -0.02058 -0.11753 -0.00924 213 ASN A O   
1372 C CB  . ASN A 213 ? 0.24928 0.28498 0.47747 -0.02317 -0.11137 -0.00472 213 ASN A CB  
1373 C CG  . ASN A 213 ? 0.25903 0.29382 0.50037 -0.02877 -0.11493 -0.00455 213 ASN A CG  
1374 O OD1 . ASN A 213 ? 0.28129 0.31294 0.51903 -0.03164 -0.11023 -0.00389 213 ASN A OD1 
1375 N ND2 . ASN A 213 ? 0.32909 0.36660 0.58647 -0.03045 -0.12350 -0.00514 213 ASN A ND2 
1376 N N   . THR A 214 ? 0.20824 0.22331 0.39393 -0.02546 -0.10335 -0.00623 214 THR A N   
1377 C CA  . THR A 214 ? 0.28404 0.28454 0.44778 -0.02599 -0.10757 -0.00870 214 THR A CA  
1378 C C   . THR A 214 ? 0.40844 0.40058 0.57552 -0.02993 -0.11648 -0.01061 214 THR A C   
1379 O O   . THR A 214 ? 0.47282 0.45091 0.62073 -0.02997 -0.12183 -0.01336 214 THR A O   
1380 C CB  . THR A 214 ? 0.29845 0.30001 0.45574 -0.02663 -0.09752 -0.00737 214 THR A CB  
1381 O OG1 . THR A 214 ? 0.29164 0.29890 0.46679 -0.03106 -0.09228 -0.00509 214 THR A OG1 
1382 C CG2 . THR A 214 ? 0.22891 0.24017 0.38536 -0.02287 -0.08851 -0.00554 214 THR A CG2 
1383 N N   . SER A 215 ? 0.41448 0.41504 0.60566 -0.03307 -0.11803 -0.00926 215 SER A N   
1384 C CA  . SER A 215 ? 0.51487 0.50869 0.71259 -0.03740 -0.12683 -0.01104 215 SER A CA  
1385 C C   . SER A 215 ? 0.60469 0.59188 0.79851 -0.03574 -0.14031 -0.01409 215 SER A C   
1386 O O   . SER A 215 ? 0.47262 0.46769 0.67648 -0.03352 -0.14212 -0.01329 215 SER A O   
1387 C CB  . SER A 215 ? 0.49427 0.50042 0.72125 -0.04223 -0.12178 -0.00771 215 SER A CB  
1388 O OG  . SER A 215 ? 0.51071 0.51048 0.74556 -0.04685 -0.13113 -0.00958 215 SER A OG  
1389 N N   . SER A 216 ? 0.77823 0.75023 0.95682 -0.03657 -0.14978 -0.01770 216 SER A N   
1390 C CA  . SER A 216 ? 0.83099 0.79460 1.00382 -0.03493 -0.16341 -0.02088 216 SER A CA  
1391 C C   . SER A 216 ? 0.78493 0.75465 0.98408 -0.03964 -0.17052 -0.02103 216 SER A C   
1392 O O   . SER A 216 ? 0.74018 0.71098 0.94603 -0.03841 -0.17984 -0.02224 216 SER A O   
1393 C CB  . SER A 216 ? 0.84914 0.79309 0.99295 -0.03319 -0.17035 -0.02485 216 SER A CB  
1394 O OG  . SER A 216 ? 0.87191 0.81046 1.01510 -0.03729 -0.16806 -0.02566 216 SER A OG  
1395 N N   . THR A 217 ? 0.77843 0.75223 0.99307 -0.04517 -0.16594 -0.01958 217 THR A N   
1396 C CA  . THR A 217 ? 0.74661 0.72613 0.98751 -0.05057 -0.17200 -0.01940 217 THR A CA  
1397 C C   . THR A 217 ? 0.69803 0.69766 0.96884 -0.05212 -0.16354 -0.01463 217 THR A C   
1398 O O   . THR A 217 ? 0.77450 0.78176 1.06547 -0.05343 -0.17007 -0.01450 217 THR A O   
1399 C CB  . THR A 217 ? 0.68824 0.66016 0.93117 -0.05643 -0.17204 -0.02024 217 THR A CB  
1400 O OG1 . THR A 217 ? 0.64424 0.62392 0.89401 -0.05840 -0.15726 -0.01600 217 THR A OG1 
1401 C CG2 . THR A 217 ? 0.71274 0.66399 0.92457 -0.05439 -0.17942 -0.02516 217 THR A CG2 
1402 N N   . GLY A 218 ? 0.52582 0.53388 0.79921 -0.05171 -0.14904 -0.01077 218 GLY A N   
1403 C CA  . GLY A 218 ? 0.43147 0.45781 0.73122 -0.05275 -0.13920 -0.00597 218 GLY A CA  
1404 C C   . GLY A 218 ? 0.41000 0.44439 0.70321 -0.04744 -0.12789 -0.00358 218 GLY A C   
1405 O O   . GLY A 218 ? 0.45330 0.48364 0.73017 -0.04237 -0.13138 -0.00566 218 GLY A O   
1406 N N   . VAL A 219 ? 0.36798 0.41328 0.67365 -0.04854 -0.11422 0.00090  219 VAL A N   
1407 C CA  . VAL A 219 ? 0.40380 0.45720 0.70427 -0.04356 -0.10290 0.00310  219 VAL A CA  
1408 C C   . VAL A 219 ? 0.36834 0.41957 0.65754 -0.04366 -0.09146 0.00510  219 VAL A C   
1409 O O   . VAL A 219 ? 0.31348 0.36930 0.61511 -0.04718 -0.08317 0.00872  219 VAL A O   
1410 C CB  . VAL A 219 ? 0.30776 0.37842 0.63314 -0.04284 -0.09563 0.00692  219 VAL A CB  
1411 C CG1 . VAL A 219 ? 0.21436 0.29222 0.53254 -0.03753 -0.08350 0.00884  219 VAL A CG1 
1412 C CG2 . VAL A 219 ? 0.33877 0.41264 0.67541 -0.04197 -0.10680 0.00496  219 VAL A CG2 
1413 N N   . CYS A 220 ? 0.34365 0.38763 0.60920 -0.03974 -0.09111 0.00292  220 CYS A N   
1414 C CA  . CYS A 220 ? 0.29235 0.33577 0.54675 -0.03874 -0.08032 0.00464  220 CYS A CA  
1415 C C   . CYS A 220 ? 0.20536 0.25304 0.44851 -0.03278 -0.07578 0.00425  220 CYS A C   
1416 O O   . CYS A 220 ? 0.20730 0.24603 0.42997 -0.03015 -0.08086 0.00121  220 CYS A O   
1417 C CB  . CYS A 220 ? 0.31517 0.34333 0.55036 -0.04073 -0.08509 0.00193  220 CYS A CB  
1418 S SG  . CYS A 220 ? 0.33470 0.36219 0.55788 -0.03983 -0.07234 0.00419  220 CYS A SG  
1419 N N   . GLY A 221 ? 0.12482 0.18571 0.38104 -0.03058 -0.06627 0.00733  221 GLY A N   
1420 C CA  . GLY A 221 ? 0.13320 0.19877 0.38173 -0.02496 -0.06285 0.00666  221 GLY A CA  
1421 C C   . GLY A 221 ? 0.20078 0.26636 0.43532 -0.02251 -0.05317 0.00748  221 GLY A C   
1422 O O   . GLY A 221 ? 0.19870 0.26716 0.43753 -0.02424 -0.04442 0.01043  221 GLY A O   
1423 N N   . ILE A 222 ? 0.16228 0.22436 0.38020 -0.01850 -0.05478 0.00509  222 ILE A N   
1424 C CA  . ILE A 222 ? 0.20367 0.26613 0.40787 -0.01575 -0.04671 0.00536  222 ILE A CA  
1425 C C   . ILE A 222 ? 0.15331 0.22110 0.35354 -0.01044 -0.04367 0.00454  222 ILE A C   
1426 O O   . ILE A 222 ? 0.15554 0.22039 0.35382 -0.00899 -0.05125 0.00260  222 ILE A O   
1427 C CB  . ILE A 222 ? 0.31111 0.36137 0.49587 -0.01678 -0.05261 0.00290  222 ILE A CB  
1428 C CG1 . ILE A 222 ? 0.27349 0.32081 0.45933 -0.02061 -0.04900 0.00449  222 ILE A CG1 
1429 C CG2 . ILE A 222 ? 0.28172 0.33149 0.45027 -0.01250 -0.04951 0.00167  222 ILE A CG2 
1430 C CD1 . ILE A 222 ? 0.36294 0.40584 0.55978 -0.02560 -0.05504 0.00471  222 ILE A CD1 
1431 N N   . ALA A 223 ? 0.13790 0.21277 0.33642 -0.00728 -0.03274 0.00601  223 ALA A N   
1432 C CA  . ALA A 223 ? 0.16950 0.24883 0.36379 -0.00203 -0.02958 0.00488  223 ALA A CA  
1433 C C   . ALA A 223 ? 0.22680 0.30266 0.40279 0.00082  -0.02646 0.00337  223 ALA A C   
1434 O O   . ALA A 223 ? 0.13982 0.21605 0.31048 0.00044  -0.02034 0.00453  223 ALA A O   
1435 C CB  . ALA A 223 ? 0.17202 0.26270 0.37897 0.00040  -0.01992 0.00727  223 ALA A CB  
1436 N N   . TRP A 224 ? 0.16789 0.24021 0.33497 0.00366  -0.03073 0.00104  224 TRP A N   
1437 C CA  . TRP A 224 ? 0.12948 0.19858 0.28062 0.00627  -0.02857 -0.00048 224 TRP A CA  
1438 C C   . TRP A 224 ? 0.14767 0.22008 0.29749 0.01115  -0.02577 -0.00177 224 TRP A C   
1439 O O   . TRP A 224 ? 0.13165 0.20553 0.28974 0.01243  -0.02904 -0.00204 224 TRP A O   
1440 C CB  . TRP A 224 ? 0.13985 0.19809 0.27807 0.00451  -0.03754 -0.00205 224 TRP A CB  
1441 C CG  . TRP A 224 ? 0.15064 0.20256 0.28540 0.00037  -0.04228 -0.00174 224 TRP A CG  
1442 C CD1 . TRP A 224 ? 0.14310 0.19651 0.27804 -0.00149 -0.03784 -0.00057 224 TRP A CD1 
1443 C CD2 . TRP A 224 ? 0.16591 0.20755 0.29430 -0.00182 -0.05266 -0.00283 224 TRP A CD2 
1444 N NE1 . TRP A 224 ? 0.16373 0.20822 0.29370 -0.00506 -0.04542 -0.00121 224 TRP A NE1 
1445 C CE2 . TRP A 224 ? 0.15011 0.18693 0.27456 -0.00508 -0.05448 -0.00275 224 TRP A CE2 
1446 C CE3 . TRP A 224 ? 0.19666 0.23190 0.32116 -0.00090 -0.06058 -0.00383 224 TRP A CE3 
1447 C CZ2 . TRP A 224 ? 0.18821 0.21334 0.30323 -0.00720 -0.06398 -0.00414 224 TRP A CZ2 
1448 C CZ3 . TRP A 224 ? 0.21504 0.23937 0.33049 -0.00283 -0.06951 -0.00472 224 TRP A CZ3 
1449 C CH2 . TRP A 224 ? 0.16538 0.18450 0.27545 -0.00581 -0.07112 -0.00508 224 TRP A CH2 
1450 N N   . ARG A 225 ? 0.10674 0.17977 0.24624 0.01407  -0.02040 -0.00277 225 ARG A N   
1451 C CA  . ARG A 225 ? 0.14825 0.22121 0.28431 0.01843  -0.01982 -0.00472 225 ARG A CA  
1452 C C   . ARG A 225 ? 0.14720 0.21053 0.27398 0.01749  -0.02795 -0.00633 225 ARG A C   
1453 O O   . ARG A 225 ? 0.07231 0.13303 0.19883 0.02011  -0.03054 -0.00774 225 ARG A O   
1454 C CB  . ARG A 225 ? 0.15305 0.23000 0.28193 0.02226  -0.01124 -0.00549 225 ARG A CB  
1455 C CG  . ARG A 225 ? 0.14382 0.21790 0.26100 0.02077  -0.00980 -0.00573 225 ARG A CG  
1456 C CD  . ARG A 225 ? 0.13329 0.20874 0.24117 0.02502  -0.00412 -0.00751 225 ARG A CD  
1457 N NE  . ARG A 225 ? 0.13982 0.21407 0.23784 0.02383  -0.00208 -0.00745 225 ARG A NE  
1458 C CZ  . ARG A 225 ? 0.16720 0.24051 0.25535 0.02618  0.00075  -0.00944 225 ARG A CZ  
1459 N NH1 . ARG A 225 ? 0.14736 0.21985 0.23392 0.02972  0.00157  -0.01219 225 ARG A NH1 
1460 N NH2 . ARG A 225 ? 0.13619 0.20880 0.21579 0.02498  0.00231  -0.00930 225 ARG A NH2 
1461 N N   . TYR A 226 ? 0.09082 0.14830 0.20960 0.01403  -0.03192 -0.00591 226 TYR A N   
1462 C CA  . TYR A 226 ? 0.08989 0.13763 0.19826 0.01314  -0.03928 -0.00662 226 TYR A CA  
1463 C C   . TYR A 226 ? 0.12819 0.16957 0.22949 0.00939  -0.04435 -0.00562 226 TYR A C   
1464 O O   . TYR A 226 ? 0.14287 0.18733 0.24709 0.00746  -0.04187 -0.00485 226 TYR A O   
1465 C CB  . TYR A 226 ? 0.06281 0.10901 0.16161 0.01495  -0.03677 -0.00810 226 TYR A CB  
1466 C CG  . TYR A 226 ? 0.12169 0.16804 0.21147 0.01327  -0.03425 -0.00785 226 TYR A CG  
1467 C CD1 . TYR A 226 ? 0.06072 0.11478 0.15238 0.01447  -0.02641 -0.00801 226 TYR A CD1 
1468 C CD2 . TYR A 226 ? 0.13137 0.16992 0.20975 0.01104  -0.03939 -0.00716 226 TYR A CD2 
1469 C CE1 . TYR A 226 ? 0.13754 0.19131 0.21984 0.01337  -0.02363 -0.00772 226 TYR A CE1 
1470 C CE2 . TYR A 226 ? 0.13879 0.17644 0.20605 0.00958  -0.03539 -0.00662 226 TYR A CE2 
1471 C CZ  . TYR A 226 ? 0.14811 0.19325 0.21735 0.01070  -0.02760 -0.00695 226 TYR A CZ  
1472 O OH  . TYR A 226 ? 0.13530 0.17929 0.19296 0.00985  -0.02338 -0.00624 226 TYR A OH  
1473 N N   . HIS A 227 ? 0.10560 0.13716 0.19686 0.00867  -0.05145 -0.00551 227 HIS A N   
1474 C CA  . HIS A 227 ? 0.12955 0.15307 0.20986 0.00599  -0.05633 -0.00486 227 HIS A CA  
1475 C C   . HIS A 227 ? 0.16559 0.17973 0.22994 0.00644  -0.05970 -0.00425 227 HIS A C   
1476 O O   . HIS A 227 ? 0.21410 0.22588 0.27860 0.00818  -0.06135 -0.00413 227 HIS A O   
1477 C CB  . HIS A 227 ? 0.09812 0.11797 0.18382 0.00444  -0.06287 -0.00478 227 HIS A CB  
1478 C CG  . HIS A 227 ? 0.15478 0.16578 0.22912 0.00204  -0.06776 -0.00483 227 HIS A CG  
1479 N ND1 . HIS A 227 ? 0.20257 0.21446 0.27277 0.00044  -0.06459 -0.00492 227 HIS A ND1 
1480 C CD2 . HIS A 227 ? 0.17353 0.17381 0.23888 0.00148  -0.07576 -0.00508 227 HIS A CD2 
1481 C CE1 . HIS A 227 ? 0.21349 0.21490 0.27194 -0.00104 -0.07043 -0.00547 227 HIS A CE1 
1482 N NE2 . HIS A 227 ? 0.20216 0.19640 0.25711 -0.00033 -0.07704 -0.00562 227 HIS A NE2 
1483 N N   . VAL A 228 ? 0.11158 0.12013 0.16206 0.00505  -0.06039 -0.00361 228 VAL A N   
1484 C CA  . VAL A 228 ? 0.14876 0.14840 0.18325 0.00537  -0.06256 -0.00211 228 VAL A CA  
1485 C C   . VAL A 228 ? 0.17610 0.16455 0.19409 0.00440  -0.06682 -0.00127 228 VAL A C   
1486 O O   . VAL A 228 ? 0.14918 0.13779 0.16642 0.00327  -0.06671 -0.00232 228 VAL A O   
1487 C CB  . VAL A 228 ? 0.11949 0.12332 0.14905 0.00534  -0.05408 -0.00184 228 VAL A CB  
1488 C CG1 . VAL A 228 ? 0.11473 0.12181 0.13977 0.00443  -0.04783 -0.00216 228 VAL A CG1 
1489 C CG2 . VAL A 228 ? 0.13077 0.12582 0.14585 0.00498  -0.05428 0.00050  228 VAL A CG2 
1490 N N   . ALA A 229 ? 0.14222 0.12001 0.14649 0.00514  -0.07047 0.00060  229 ALA A N   
1491 C CA  . ALA A 229 ? 0.20137 0.16729 0.18663 0.00521  -0.07308 0.00136  229 ALA A CA  
1492 C C   . ALA A 229 ? 0.23700 0.19375 0.20566 0.00631  -0.07260 0.00483  229 ALA A C   
1493 O O   . ALA A 229 ? 0.21183 0.16965 0.18563 0.00669  -0.07307 0.00646  229 ALA A O   
1494 C CB  . ALA A 229 ? 0.14481 0.10538 0.13285 0.00520  -0.08018 -0.00038 229 ALA A CB  
1495 N N   . PRO A 230 ? 0.22491 0.17223 0.17358 0.00701  -0.07086 0.00624  230 PRO A N   
1496 C CA  . PRO A 230 ? 0.22601 0.16443 0.15900 0.00804  -0.06904 0.01046  230 PRO A CA  
1497 C C   . PRO A 230 ? 0.25034 0.18064 0.18162 0.00929  -0.07586 0.01117  230 PRO A C   
1498 O O   . PRO A 230 ? 0.25397 0.18235 0.18966 0.00977  -0.08213 0.00823  230 PRO A O   
1499 C CB  . PRO A 230 ? 0.24468 0.17606 0.15834 0.00925  -0.06431 0.01105  230 PRO A CB  
1500 C CG  . PRO A 230 ? 0.20420 0.14191 0.12356 0.00861  -0.06254 0.00763  230 PRO A CG  
1501 C CD  . PRO A 230 ? 0.19489 0.13946 0.13448 0.00716  -0.06891 0.00437  230 PRO A CD  
1502 N N   . LEU A 231 ? 0.22376 0.14877 0.14834 0.00974  -0.07460 0.01548  231 LEU A N   
1503 C CA  . LEU A 231 ? 0.25252 0.16891 0.17346 0.01135  -0.08039 0.01701  231 LEU A CA  
1504 C C   . LEU A 231 ? 0.28724 0.19232 0.18676 0.01257  -0.07646 0.02202  231 LEU A C   
1505 O O   . LEU A 231 ? 0.26859 0.17349 0.16370 0.01135  -0.06960 0.02652  231 LEU A O   
1506 C CB  . LEU A 231 ? 0.19102 0.11171 0.12761 0.01101  -0.08271 0.01776  231 LEU A CB  
1507 C CG  . LEU A 231 ? 0.31738 0.23141 0.25529 0.01307  -0.08973 0.01829  231 LEU A CG  
1508 C CD1 . LEU A 231 ? 0.28111 0.20013 0.23187 0.01379  -0.09616 0.01336  231 LEU A CD1 
1509 C CD2 . LEU A 231 ? 0.30481 0.21933 0.25206 0.01306  -0.08945 0.02067  231 LEU A CD2 
1510 N N   . ILE A 232 ? 0.23799 0.13374 0.12468 0.01493  -0.08041 0.02149  232 ILE A N   
1511 C CA  . ILE A 232 ? 0.30962 0.19519 0.17559 0.01677  -0.07580 0.02617  232 ILE A CA  
1512 C C   . ILE A 232 ? 0.31925 0.19475 0.17827 0.01923  -0.08237 0.02809  232 ILE A C   
1513 O O   . ILE A 232 ? 0.32317 0.19874 0.19113 0.02002  -0.09144 0.02458  232 ILE A O   
1514 C CB  . ILE A 232 ? 0.34605 0.22807 0.19751 0.01845  -0.07262 0.02407  232 ILE A CB  
1515 C CG1 . ILE A 232 ? 0.33919 0.21763 0.19193 0.01974  -0.08223 0.01823  232 ILE A CG1 
1516 C CG2 . ILE A 232 ? 0.35182 0.24298 0.20749 0.01663  -0.06444 0.02334  232 ILE A CG2 
1517 C CD1 . ILE A 232 ? 0.36542 0.23634 0.20135 0.02213  -0.08079 0.01596  232 ILE A CD1 
1518 N N   . SER A 233 ? 0.33084 0.19822 0.17465 0.02051  -0.07729 0.03408  233 SER A N   
1519 C CA  . SER A 233 ? 0.43112 0.28807 0.26619 0.02323  -0.08255 0.03703  233 SER A CA  
1520 C C   . SER A 233 ? 0.43029 0.27753 0.24547 0.02691  -0.08459 0.03610  233 SER A C   
1521 O O   . SER A 233 ? 0.44424 0.28824 0.24460 0.02793  -0.07654 0.03891  233 SER A O   
1522 C CB  . SER A 233 ? 0.42342 0.27622 0.25458 0.02235  -0.07581 0.04505  233 SER A CB  
1523 O OG  . SER A 233 ? 0.38545 0.22813 0.20935 0.02514  -0.08117 0.04818  233 SER A OG  
1524 N N   . VAL A 234 ? 0.36336 0.20613 0.17899 0.02906  -0.09544 0.03202  234 VAL A N   
1525 C CA  . VAL A 234 ? 0.41610 0.24798 0.21293 0.03288  -0.09970 0.03033  234 VAL A CA  
1526 C C   . VAL A 234 ? 0.47473 0.29699 0.26427 0.03613  -0.10720 0.03294  234 VAL A C   
1527 O O   . VAL A 234 ? 0.46706 0.29143 0.26974 0.03618  -0.11661 0.03012  234 VAL A O   
1528 C CB  . VAL A 234 ? 0.47346 0.30733 0.27648 0.03260  -0.10706 0.02256  234 VAL A CB  
1529 C CG1 . VAL A 234 ? 0.43241 0.25315 0.21453 0.03678  -0.11186 0.02050  234 VAL A CG1 
1530 C CG2 . VAL A 234 ? 0.53318 0.37674 0.34463 0.02951  -0.09986 0.02026  234 VAL A CG2 
1531 N N   . ASN A 235 ? 0.47082 0.28301 0.23999 0.03906  -0.10261 0.03865  235 ASN A N   
1532 C CA  . ASN A 235 ? 0.49201 0.29420 0.25216 0.04251  -0.10850 0.04244  235 ASN A CA  
1533 C C   . ASN A 235 ? 0.51972 0.32689 0.29851 0.04077  -0.11190 0.04434  235 ASN A C   
1534 O O   . ASN A 235 ? 0.54051 0.34443 0.32320 0.04306  -0.12205 0.04280  235 ASN A O   
1535 C CB  . ASN A 235 ? 0.44602 0.23989 0.19712 0.04638  -0.12054 0.03715  235 ASN A CB  
1536 C CG  . ASN A 235 ? 0.57639 0.36273 0.30723 0.04894  -0.11811 0.03477  235 ASN A CG  
1537 O OD1 . ASN A 235 ? 0.51802 0.30245 0.23598 0.04940  -0.10703 0.03899  235 ASN A OD1 
1538 N ND2 . ASN A 235 ? 0.56221 0.34403 0.29085 0.05075  -0.12854 0.02804  235 ASN A ND2 
1539 N N   . GLY A 236 ? 0.44607 0.26089 0.23658 0.03698  -0.10359 0.04744  236 GLY A N   
1540 C CA  . GLY A 236 ? 0.49851 0.31674 0.30575 0.03552  -0.10567 0.04933  236 GLY A CA  
1541 C C   . GLY A 236 ? 0.47914 0.30770 0.30926 0.03412  -0.11344 0.04237  236 GLY A C   
1542 O O   . GLY A 236 ? 0.52488 0.35627 0.36950 0.03371  -0.11590 0.04305  236 GLY A O   
1543 N N   . VAL A 237 ? 0.42791 0.26186 0.26185 0.03351  -0.11695 0.03586  237 VAL A N   
1544 C CA  . VAL A 237 ? 0.42140 0.26657 0.27855 0.03176  -0.12280 0.02977  237 VAL A CA  
1545 C C   . VAL A 237 ? 0.41337 0.26922 0.28013 0.02786  -0.11597 0.02707  237 VAL A C   
1546 O O   . VAL A 237 ? 0.39086 0.24532 0.24677 0.02747  -0.11251 0.02567  237 VAL A O   
1547 C CB  . VAL A 237 ? 0.57752 0.42069 0.43530 0.03388  -0.13361 0.02452  237 VAL A CB  
1548 C CG1 . VAL A 237 ? 0.49690 0.35276 0.38115 0.03195  -0.13849 0.01938  237 VAL A CG1 
1549 C CG2 . VAL A 237 ? 0.61857 0.45034 0.46418 0.03836  -0.14089 0.02723  237 VAL A CG2 
1550 N N   . TRP A 238 ? 0.37929 0.24534 0.26574 0.02546  -0.11398 0.02625  238 TRP A N   
1551 C CA  . TRP A 238 ? 0.31193 0.18853 0.20801 0.02212  -0.10799 0.02373  238 TRP A CA  
1552 C C   . TRP A 238 ? 0.39752 0.28034 0.30308 0.02151  -0.11281 0.01759  238 TRP A C   
1553 O O   . TRP A 238 ? 0.43425 0.32113 0.35428 0.02216  -0.11983 0.01464  238 TRP A O   
1554 C CB  . TRP A 238 ? 0.34098 0.22608 0.25478 0.02021  -0.10483 0.02436  238 TRP A CB  
1555 C CG  . TRP A 238 ? 0.34163 0.21991 0.24643 0.01973  -0.09902 0.03069  238 TRP A CG  
1556 C CD1 . TRP A 238 ? 0.38714 0.25865 0.29245 0.02116  -0.10113 0.03434  238 TRP A CD1 
1557 C CD2 . TRP A 238 ? 0.28482 0.16163 0.17890 0.01755  -0.08976 0.03467  238 TRP A CD2 
1558 N NE1 . TRP A 238 ? 0.36890 0.23428 0.26519 0.01942  -0.09363 0.04053  238 TRP A NE1 
1559 C CE2 . TRP A 238 ? 0.36198 0.23105 0.25171 0.01709  -0.08643 0.04097  238 TRP A CE2 
1560 C CE3 . TRP A 238 ? 0.36533 0.24674 0.25392 0.01593  -0.08358 0.03369  238 TRP A CE3 
1561 C CZ2 . TRP A 238 ? 0.38999 0.25645 0.27145 0.01446  -0.07687 0.04657  238 TRP A CZ2 
1562 C CZ3 . TRP A 238 ? 0.38170 0.26117 0.26131 0.01404  -0.07414 0.03899  238 TRP A CZ3 
1563 C CH2 . TRP A 238 ? 0.39370 0.26608 0.27050 0.01300  -0.07074 0.04550  238 TRP A CH2 
1564 N N   . ASN A 239 ? 0.34241 0.22572 0.24003 0.02031  -0.10852 0.01610  239 ASN A N   
1565 C CA  . ASN A 239 ? 0.32692 0.21392 0.23112 0.01943  -0.11225 0.01093  239 ASN A CA  
1566 C C   . ASN A 239 ? 0.32937 0.22757 0.24494 0.01645  -0.10570 0.00925  239 ASN A C   
1567 O O   . ASN A 239 ? 0.32609 0.22503 0.23371 0.01568  -0.09771 0.01164  239 ASN A O   
1568 C CB  . ASN A 239 ? 0.33798 0.21348 0.22100 0.02140  -0.11388 0.01006  239 ASN A CB  
1569 C CG  . ASN A 239 ? 0.43568 0.30168 0.31217 0.02435  -0.12393 0.00918  239 ASN A CG  
1570 O OD1 . ASN A 239 ? 0.47165 0.33372 0.34636 0.02493  -0.13040 0.00532  239 ASN A OD1 
1571 N ND2 . ASN A 239 ? 0.50257 0.36428 0.37539 0.02633  -0.12572 0.01285  239 ASN A ND2 
1572 N N   . VAL A 240 ? 0.22670 0.13375 0.16086 0.01491  -0.10880 0.00552  240 VAL A N   
1573 C CA  . VAL A 240 ? 0.23837 0.15546 0.18244 0.01241  -0.10304 0.00382  240 VAL A CA  
1574 C C   . VAL A 240 ? 0.31304 0.22479 0.24587 0.01212  -0.10304 0.00155  240 VAL A C   
1575 O O   . VAL A 240 ? 0.32134 0.22617 0.25060 0.01295  -0.11018 -0.00072 240 VAL A O   
1576 C CB  . VAL A 240 ? 0.33232 0.26189 0.30200 0.01101  -0.10481 0.00147  240 VAL A CB  
1577 C CG1 . VAL A 240 ? 0.37621 0.31644 0.35531 0.00875  -0.09779 0.00039  240 VAL A CG1 
1578 C CG2 . VAL A 240 ? 0.24500 0.17821 0.22519 0.01225  -0.10566 0.00303  240 VAL A CG2 
1579 N N   . ILE A 241 ? 0.29628 0.21073 0.22336 0.01124  -0.09534 0.00207  241 ILE A N   
1580 C CA  . ILE A 241 ? 0.26500 0.17475 0.18216 0.01126  -0.09427 -0.00025 241 ILE A CA  
1581 C C   . ILE A 241 ? 0.27449 0.19508 0.20872 0.00861  -0.09246 -0.00253 241 ILE A C   
1582 O O   . ILE A 241 ? 0.23649 0.16458 0.17325 0.00776  -0.08523 -0.00150 241 ILE A O   
1583 C CB  . ILE A 241 ? 0.29050 0.19501 0.18742 0.01290  -0.08591 0.00219  241 ILE A CB  
1584 C CG1 . ILE A 241 ? 0.28794 0.18280 0.16892 0.01543  -0.08620 0.00552  241 ILE A CG1 
1585 C CG2 . ILE A 241 ? 0.30320 0.20160 0.18907 0.01380  -0.08469 -0.00066 241 ILE A CG2 
1586 C CD1 . ILE A 241 ? 0.33064 0.21417 0.20349 0.01751  -0.09550 0.00331  241 ILE A CD1 
1587 N N   . ASP A 242 ? 0.26531 0.18694 0.21162 0.00730  -0.09895 -0.00534 242 ASP A N   
1588 C CA  . ASP A 242 ? 0.25059 0.18293 0.21471 0.00458  -0.09688 -0.00686 242 ASP A CA  
1589 C C   . ASP A 242 ? 0.26172 0.18844 0.22635 0.00331  -0.10222 -0.00986 242 ASP A C   
1590 O O   . ASP A 242 ? 0.22370 0.15266 0.20292 0.00195  -0.10867 -0.01110 242 ASP A O   
1591 C CB  . ASP A 242 ? 0.20362 0.14837 0.19143 0.00346  -0.09748 -0.00633 242 ASP A CB  
1592 C CG  . ASP A 242 ? 0.20306 0.16060 0.20909 0.00106  -0.09260 -0.00697 242 ASP A CG  
1593 O OD1 . ASP A 242 ? 0.22376 0.17974 0.22531 -0.00022 -0.09063 -0.00808 242 ASP A OD1 
1594 O OD2 . ASP A 242 ? 0.19640 0.16495 0.22063 0.00080  -0.09052 -0.00637 242 ASP A OD2 
1595 N N   . PRO A 243 ? 0.22605 0.14539 0.17521 0.00386  -0.09942 -0.01098 243 PRO A N   
1596 C CA  . PRO A 243 ? 0.29069 0.20278 0.23900 0.00271  -0.10479 -0.01404 243 PRO A CA  
1597 C C   . PRO A 243 ? 0.29465 0.21751 0.26652 -0.00132 -0.10498 -0.01486 243 PRO A C   
1598 O O   . PRO A 243 ? 0.34566 0.26361 0.32129 -0.00309 -0.11040 -0.01708 243 PRO A O   
1599 C CB  . PRO A 243 ? 0.29565 0.19817 0.22150 0.00500  -0.09944 -0.01471 243 PRO A CB  
1600 C CG  . PRO A 243 ? 0.27690 0.17826 0.18846 0.00803  -0.09359 -0.01181 243 PRO A CG  
1601 C CD  . PRO A 243 ? 0.22771 0.14287 0.15720 0.00626  -0.09169 -0.00940 243 PRO A CD  
1602 N N   . SER A 244 ? 0.22074 0.15785 0.20853 -0.00271 -0.09900 -0.01300 244 SER A N   
1603 C CA  . SER A 244 ? 0.19772 0.14549 0.20892 -0.00636 -0.09815 -0.01324 244 SER A CA  
1604 C C   . SER A 244 ? 0.28864 0.24174 0.31889 -0.00748 -0.10387 -0.01304 244 SER A C   
1605 O O   . SER A 244 ? 0.23734 0.19726 0.28686 -0.01058 -0.10440 -0.01314 244 SER A O   
1606 C CB  . SER A 244 ? 0.26793 0.22916 0.28933 -0.00683 -0.08918 -0.01139 244 SER A CB  
1607 O OG  . SER A 244 ? 0.27100 0.24101 0.30062 -0.00520 -0.08683 -0.00951 244 SER A OG  
1608 N N   . LEU A 245 ? 0.29764 0.24738 0.32272 -0.00495 -0.10799 -0.01257 245 LEU A N   
1609 C CA  . LEU A 245 ? 0.29256 0.24754 0.33538 -0.00544 -0.11353 -0.01249 245 LEU A CA  
1610 C C   . LEU A 245 ? 0.28577 0.22827 0.31798 -0.00393 -0.12403 -0.01413 245 LEU A C   
1611 O O   . LEU A 245 ? 0.28644 0.23144 0.33308 -0.00496 -0.13065 -0.01486 245 LEU A O   
1612 C CB  . LEU A 245 ? 0.24799 0.21295 0.30028 -0.00364 -0.10920 -0.01043 245 LEU A CB  
1613 C CG  . LEU A 245 ? 0.26466 0.24431 0.33336 -0.00476 -0.09975 -0.00902 245 LEU A CG  
1614 C CD1 . LEU A 245 ? 0.19100 0.17805 0.26661 -0.00225 -0.09650 -0.00764 245 LEU A CD1 
1615 C CD2 . LEU A 245 ? 0.25936 0.24712 0.34931 -0.00798 -0.09954 -0.00913 245 LEU A CD2 
1616 N N   . PHE A 246 ? 0.30688 0.23617 0.31398 -0.00125 -0.12534 -0.01462 246 PHE A N   
1617 C CA  . PHE A 246 ? 0.28906 0.20549 0.28312 0.00107  -0.13486 -0.01606 246 PHE A CA  
1618 C C   . PHE A 246 ? 0.41539 0.31619 0.38482 0.00263  -0.13663 -0.01805 246 PHE A C   
1619 O O   . PHE A 246 ? 0.34491 0.24454 0.30523 0.00241  -0.12962 -0.01796 246 PHE A O   
1620 C CB  . PHE A 246 ? 0.29976 0.21454 0.28622 0.00423  -0.13489 -0.01406 246 PHE A CB  
1621 C CG  . PHE A 246 ? 0.34574 0.27348 0.35458 0.00371  -0.13460 -0.01262 246 PHE A CG  
1622 C CD1 . PHE A 246 ? 0.43806 0.36671 0.45902 0.00394  -0.14345 -0.01359 246 PHE A CD1 
1623 C CD2 . PHE A 246 ? 0.23899 0.17787 0.25663 0.00335  -0.12558 -0.01053 246 PHE A CD2 
1624 C CE1 . PHE A 246 ? 0.39735 0.33789 0.43860 0.00404  -0.14261 -0.01235 246 PHE A CE1 
1625 C CE2 . PHE A 246 ? 0.29019 0.24015 0.32727 0.00358  -0.12481 -0.00952 246 PHE A CE2 
1626 C CZ  . PHE A 246 ? 0.29670 0.24755 0.34549 0.00402  -0.13298 -0.01037 246 PHE A CZ  
1627 N N   . ASN A 247 ? 0.40784 0.29630 0.36582 0.00471  -0.14596 -0.01997 247 ASN A N   
1628 C CA  . ASN A 247 ? 0.42026 0.29242 0.35339 0.00715  -0.14803 -0.02219 247 ASN A CA  
1629 C C   . ASN A 247 ? 0.45150 0.31276 0.36021 0.01186  -0.14716 -0.02104 247 ASN A C   
1630 O O   . ASN A 247 ? 0.42615 0.27297 0.31246 0.01496  -0.14883 -0.02276 247 ASN A O   
1631 C CB  . ASN A 247 ? 0.46892 0.33347 0.40525 0.00623  -0.15953 -0.02575 247 ASN A CB  
1632 C CG  . ASN A 247 ? 0.60624 0.48172 0.56800 0.00108  -0.16019 -0.02648 247 ASN A CG  
1633 O OD1 . ASN A 247 ? 0.60533 0.48550 0.57033 -0.00103 -0.15262 -0.02599 247 ASN A OD1 
1634 N ND2 . ASN A 247 ? 0.76707 0.64710 0.74765 -0.00100 -0.16897 -0.02745 247 ASN A ND2 
1635 N N   . GLN A 248 ? 0.35956 0.22765 0.27263 0.01251  -0.14401 -0.01799 248 GLN A N   
1636 C CA  . GLN A 248 ? 0.41897 0.27818 0.31116 0.01651  -0.14252 -0.01600 248 GLN A CA  
1637 C C   . GLN A 248 ? 0.44346 0.31333 0.34435 0.01597  -0.13612 -0.01213 248 GLN A C   
1638 O O   . GLN A 248 ? 0.38752 0.27076 0.31118 0.01312  -0.13493 -0.01163 248 GLN A O   
1639 C CB  . GLN A 248 ? 0.48549 0.33413 0.37059 0.01910  -0.15417 -0.01766 248 GLN A CB  
1640 C CG  . GLN A 248 ? 0.54306 0.40125 0.45200 0.01728  -0.16148 -0.01769 248 GLN A CG  
1641 C CD  . GLN A 248 ? 0.81656 0.66428 0.71750 0.02031  -0.17336 -0.01923 248 GLN A CD  
1642 O OE1 . GLN A 248 ? 0.94769 0.79343 0.85692 0.01938  -0.18310 -0.02238 248 GLN A OE1 
1643 N NE2 . GLN A 248 ? 0.87963 0.72049 0.76435 0.02397  -0.17288 -0.01686 248 GLN A NE2 
1644 N N   . PRO A 249 ? 0.42137 0.28523 0.30430 0.01885  -0.13170 -0.00922 249 PRO A N   
1645 C CA  . PRO A 249 ? 0.42233 0.29447 0.31346 0.01844  -0.12752 -0.00550 249 PRO A CA  
1646 C C   . PRO A 249 ? 0.38158 0.25757 0.28893 0.01835  -0.13617 -0.00591 249 PRO A C   
1647 O O   . PRO A 249 ? 0.37883 0.24674 0.28186 0.02003  -0.14565 -0.00795 249 PRO A O   
1648 C CB  . PRO A 249 ? 0.39922 0.26114 0.26614 0.02182  -0.12330 -0.00222 249 PRO A CB  
1649 C CG  . PRO A 249 ? 0.36182 0.21477 0.21021 0.02345  -0.12008 -0.00393 249 PRO A CG  
1650 C CD  . PRO A 249 ? 0.42647 0.27647 0.28169 0.02257  -0.12906 -0.00881 249 PRO A CD  
1651 N N   . VAL A 250 ? 0.29239 0.18053 0.21830 0.01676  -0.13307 -0.00422 250 VAL A N   
1652 C CA  . VAL A 250 ? 0.26852 0.16149 0.21103 0.01722  -0.14002 -0.00442 250 VAL A CA  
1653 C C   . VAL A 250 ? 0.36610 0.26359 0.31278 0.01812  -0.13587 -0.00099 250 VAL A C   
1654 O O   . VAL A 250 ? 0.33436 0.23366 0.27540 0.01749  -0.12739 0.00142  250 VAL A O   
1655 C CB  . VAL A 250 ? 0.41347 0.31910 0.38230 0.01429  -0.14178 -0.00690 250 VAL A CB  
1656 C CG1 . VAL A 250 ? 0.43477 0.33503 0.40131 0.01319  -0.14760 -0.01016 250 VAL A CG1 
1657 C CG2 . VAL A 250 ? 0.23003 0.14818 0.21130 0.01178  -0.13173 -0.00601 250 VAL A CG2 
1658 N N   . THR A 251 ? 0.31082 0.20972 0.26745 0.01977  -0.14224 -0.00075 251 THR A N   
1659 C CA  . THR A 251 ? 0.31308 0.21600 0.27598 0.02089  -0.13923 0.00210  251 THR A CA  
1660 C C   . THR A 251 ? 0.32342 0.24129 0.30801 0.01857  -0.13255 0.00143  251 THR A C   
1661 O O   . THR A 251 ? 0.26431 0.19053 0.26208 0.01628  -0.13142 -0.00106 251 THR A O   
1662 C CB  . THR A 251 ? 0.35714 0.25795 0.32592 0.02385  -0.14801 0.00232  251 THR A CB  
1663 O OG1 . THR A 251 ? 0.31728 0.22827 0.30850 0.02283  -0.15241 -0.00073 251 THR A OG1 
1664 C CG2 . THR A 251 ? 0.41381 0.29954 0.36061 0.02674  -0.15538 0.00286  251 THR A CG2 
1665 N N   . ILE A 252 ? 0.28692 0.20752 0.27490 0.01941  -0.12826 0.00375  252 ILE A N   
1666 C CA  . ILE A 252 ? 0.26024 0.19411 0.26758 0.01818  -0.12207 0.00294  252 ILE A CA  
1667 C C   . ILE A 252 ? 0.29475 0.23858 0.32440 0.01865  -0.12578 0.00052  252 ILE A C   
1668 O O   . ILE A 252 ? 0.28811 0.24334 0.33318 0.01680  -0.12131 -0.00118 252 ILE A O   
1669 C CB  . ILE A 252 ? 0.33324 0.26563 0.33902 0.01962  -0.11854 0.00562  252 ILE A CB  
1670 C CG1 . ILE A 252 ? 0.34915 0.27363 0.33518 0.01847  -0.11353 0.00862  252 ILE A CG1 
1671 C CG2 . ILE A 252 ? 0.20895 0.15445 0.23518 0.01943  -0.11315 0.00403  252 ILE A CG2 
1672 C CD1 . ILE A 252 ? 0.31902 0.23893 0.30109 0.01947  -0.11090 0.01221  252 ILE A CD1 
1673 N N   . THR A 253 ? 0.26608 0.20575 0.29719 0.02130  -0.13379 0.00069  253 THR A N   
1674 C CA  . THR A 253 ? 0.28634 0.23571 0.33892 0.02205  -0.13779 -0.00119 253 THR A CA  
1675 C C   . THR A 253 ? 0.24635 0.20079 0.30714 0.01903  -0.13923 -0.00351 253 THR A C   
1676 O O   . THR A 253 ? 0.27793 0.24518 0.35885 0.01769  -0.13566 -0.00460 253 THR A O   
1677 C CB  . THR A 253 ? 0.35034 0.29305 0.40060 0.02568  -0.14743 -0.00049 253 THR A CB  
1678 O OG1 . THR A 253 ? 0.39883 0.33898 0.44668 0.02856  -0.14538 0.00174  253 THR A OG1 
1679 C CG2 . THR A 253 ? 0.32983 0.28276 0.40219 0.02634  -0.15247 -0.00236 253 THR A CG2 
1680 N N   . THR A 254 ? 0.24455 0.18852 0.28922 0.01809  -0.14394 -0.00411 254 THR A N   
1681 C CA  . THR A 254 ? 0.24530 0.19154 0.29574 0.01522  -0.14618 -0.00636 254 THR A CA  
1682 C C   . THR A 254 ? 0.29683 0.25221 0.35472 0.01209  -0.13633 -0.00657 254 THR A C   
1683 O O   . THR A 254 ? 0.27127 0.23582 0.34622 0.00977  -0.13551 -0.00775 254 THR A O   
1684 C CB  . THR A 254 ? 0.30753 0.23865 0.33538 0.01542  -0.15237 -0.00727 254 THR A CB  
1685 O OG1 . THR A 254 ? 0.35580 0.27847 0.37686 0.01856  -0.16230 -0.00729 254 THR A OG1 
1686 C CG2 . THR A 254 ? 0.35118 0.28358 0.38479 0.01236  -0.15471 -0.00980 254 THR A CG2 
1687 N N   . TRP A 255 ? 0.31962 0.27246 0.36472 0.01204  -0.12901 -0.00517 255 TRP A N   
1688 C CA  . TRP A 255 ? 0.30327 0.26445 0.35365 0.00965  -0.11973 -0.00523 255 TRP A CA  
1689 C C   . TRP A 255 ? 0.24519 0.22123 0.31846 0.00966  -0.11437 -0.00527 255 TRP A C   
1690 O O   . TRP A 255 ? 0.25559 0.24067 0.34175 0.00743  -0.11035 -0.00598 255 TRP A O   
1691 C CB  . TRP A 255 ? 0.23387 0.18966 0.26653 0.01009  -0.11385 -0.00352 255 TRP A CB  
1692 C CG  . TRP A 255 ? 0.22192 0.18466 0.25606 0.00801  -0.10500 -0.00360 255 TRP A CG  
1693 C CD1 . TRP A 255 ? 0.17747 0.13945 0.20742 0.00582  -0.10349 -0.00471 255 TRP A CD1 
1694 C CD2 . TRP A 255 ? 0.19885 0.16931 0.23779 0.00830  -0.09710 -0.00263 255 TRP A CD2 
1695 N NE1 . TRP A 255 ? 0.19522 0.16470 0.22749 0.00480  -0.09507 -0.00429 255 TRP A NE1 
1696 C CE2 . TRP A 255 ? 0.16003 0.13490 0.19763 0.00629  -0.09110 -0.00312 255 TRP A CE2 
1697 C CE3 . TRP A 255 ? 0.21763 0.19097 0.26165 0.01028  -0.09507 -0.00166 255 TRP A CE3 
1698 C CZ2 . TRP A 255 ? 0.19259 0.17544 0.23399 0.00627  -0.08329 -0.00270 255 TRP A CZ2 
1699 C CZ3 . TRP A 255 ? 0.19498 0.17552 0.24268 0.01016  -0.08735 -0.00151 255 TRP A CZ3 
1700 C CH2 . TRP A 255 ? 0.20169 0.18728 0.24809 0.00820  -0.08159 -0.00205 255 TRP A CH2 
1701 N N   . LEU A 256 ? 0.19432 0.17226 0.27190 0.01243  -0.11409 -0.00439 256 LEU A N   
1702 C CA  . LEU A 256 ? 0.24016 0.23127 0.33766 0.01345  -0.10876 -0.00463 256 LEU A CA  
1703 C C   . LEU A 256 ? 0.22699 0.22662 0.34407 0.01274  -0.11204 -0.00552 256 LEU A C   
1704 O O   . LEU A 256 ? 0.23838 0.24987 0.37105 0.01180  -0.10563 -0.00563 256 LEU A O   
1705 C CB  . LEU A 256 ? 0.19250 0.18187 0.28970 0.01716  -0.10928 -0.00382 256 LEU A CB  
1706 C CG  . LEU A 256 ? 0.22317 0.20652 0.30601 0.01775  -0.10489 -0.00265 256 LEU A CG  
1707 C CD1 . LEU A 256 ? 0.24921 0.23073 0.33485 0.02148  -0.10619 -0.00202 256 LEU A CD1 
1708 C CD2 . LEU A 256 ? 0.19898 0.19048 0.28494 0.01603  -0.09537 -0.00326 256 LEU A CD2 
1709 N N   . ASN A 257 ? 0.25647 0.25020 0.37277 0.01328  -0.12195 -0.00594 257 ASN A N   
1710 C CA  . ASN A 257 ? 0.27315 0.27490 0.40912 0.01247  -0.12643 -0.00667 257 ASN A CA  
1711 C C   . ASN A 257 ? 0.25509 0.26152 0.39844 0.00822  -0.12384 -0.00724 257 ASN A C   
1712 O O   . ASN A 257 ? 0.23722 0.25444 0.40099 0.00691  -0.12298 -0.00716 257 ASN A O   
1713 C CB  . ASN A 257 ? 0.31222 0.30524 0.44364 0.01383  -0.13886 -0.00733 257 ASN A CB  
1714 C CG  . ASN A 257 ? 0.42235 0.41421 0.55441 0.01833  -0.14233 -0.00650 257 ASN A CG  
1715 O OD1 . ASN A 257 ? 0.37000 0.37023 0.51217 0.02050  -0.13617 -0.00578 257 ASN A OD1 
1716 N ND2 . ASN A 257 ? 0.45140 0.43230 0.57204 0.02018  -0.15245 -0.00666 257 ASN A ND2 
1717 N N   . LYS A 258 ? 0.18589 0.18417 0.31288 0.00616  -0.12246 -0.00758 258 LYS A N   
1718 C CA  . LYS A 258 ? 0.24018 0.24124 0.37259 0.00225  -0.12035 -0.00809 258 LYS A CA  
1719 C C   . LYS A 258 ? 0.25374 0.26850 0.40118 0.00119  -0.10926 -0.00693 258 LYS A C   
1720 O O   . LYS A 258 ? 0.22929 0.25021 0.38937 -0.00194 -0.10701 -0.00668 258 LYS A O   
1721 C CB  . LYS A 258 ? 0.23077 0.21975 0.34070 0.00112  -0.12076 -0.00873 258 LYS A CB  
1722 C CG  . LYS A 258 ? 0.28649 0.27487 0.39944 -0.00270 -0.12116 -0.00967 258 LYS A CG  
1723 C CD  . LYS A 258 ? 0.31411 0.29598 0.42952 -0.00380 -0.13263 -0.01140 258 LYS A CD  
1724 C CE  . LYS A 258 ? 0.48086 0.45638 0.59103 -0.00706 -0.13466 -0.01284 258 LYS A CE  
1725 N NZ  . LYS A 258 ? 0.55958 0.54660 0.68977 -0.01079 -0.12834 -0.01187 258 LYS A NZ  
1726 N N   . MET A 259 ? 0.18401 0.20292 0.32967 0.00395  -0.10243 -0.00615 259 MET A N   
1727 C CA  . MET A 259 ? 0.20784 0.23789 0.36268 0.00379  -0.09136 -0.00525 259 MET A CA  
1728 C C   . MET A 259 ? 0.19303 0.23551 0.36812 0.00585  -0.08801 -0.00453 259 MET A C   
1729 O O   . MET A 259 ? 0.19686 0.24802 0.37745 0.00742  -0.07861 -0.00384 259 MET A O   
1730 C CB  . MET A 259 ? 0.11452 0.14131 0.25401 0.00564  -0.08557 -0.00520 259 MET A CB  
1731 C CG  . MET A 259 ? 0.15401 0.17165 0.27597 0.00341  -0.08636 -0.00549 259 MET A CG  
1732 S SD  . MET A 259 ? 0.24989 0.26478 0.35525 0.00497  -0.07978 -0.00517 259 MET A SD  
1733 C CE  . MET A 259 ? 0.28796 0.29427 0.38419 0.00816  -0.08565 -0.00488 259 MET A CE  
1734 N N   . LYS A 260 ? 0.18392 0.22732 0.36977 0.00615  -0.09580 -0.00472 260 LYS A N   
1735 C CA  . LYS A 260 ? 0.14158 0.19747 0.34824 0.00822  -0.09345 -0.00389 260 LYS A CA  
1736 C C   . LYS A 260 ? 0.23328 0.29643 0.45901 0.00472  -0.09556 -0.00312 260 LYS A C   
1737 O O   . LYS A 260 ? 0.27156 0.34232 0.51435 0.00591  -0.09879 -0.00267 260 LYS A O   
1738 C CB  . LYS A 260 ? 0.19351 0.24633 0.39976 0.01222  -0.10064 -0.00446 260 LYS A CB  
1739 C CG  . LYS A 260 ? 0.23669 0.28090 0.42459 0.01532  -0.09946 -0.00493 260 LYS A CG  
1740 C CD  . LYS A 260 ? 0.30587 0.34416 0.49117 0.01888  -0.10810 -0.00520 260 LYS A CD  
1741 C CE  . LYS A 260 ? 0.47019 0.49880 0.63740 0.02142  -0.10692 -0.00523 260 LYS A CE  
1742 N NZ  . LYS A 260 ? 0.52016 0.54327 0.68575 0.02545  -0.11441 -0.00501 260 LYS A NZ  
1743 N N   . TYR A 261 ? 0.18712 0.24812 0.41088 0.00041  -0.09383 -0.00285 261 TYR A N   
1744 C CA  . TYR A 261 ? 0.19668 0.26328 0.43863 -0.00364 -0.09608 -0.00199 261 TYR A CA  
1745 C C   . TYR A 261 ? 0.24337 0.32589 0.50640 -0.00310 -0.08597 0.00054  261 TYR A C   
1746 O O   . TYR A 261 ? 0.21234 0.29953 0.47153 -0.00097 -0.07531 0.00155  261 TYR A O   
1747 C CB  . TYR A 261 ? 0.18838 0.24731 0.42173 -0.00818 -0.09663 -0.00231 261 TYR A CB  
1748 C CG  . TYR A 261 ? 0.20835 0.27245 0.46110 -0.01291 -0.09838 -0.00121 261 TYR A CG  
1749 C CD1 . TYR A 261 ? 0.26046 0.32178 0.52163 -0.01468 -0.11011 -0.00250 261 TYR A CD1 
1750 C CD2 . TYR A 261 ? 0.28987 0.36138 0.55270 -0.01561 -0.08841 0.00129  261 TYR A CD2 
1751 C CE1 . TYR A 261 ? 0.35218 0.41829 0.63247 -0.01943 -0.11216 -0.00151 261 TYR A CE1 
1752 C CE2 . TYR A 261 ? 0.38178 0.45764 0.66328 -0.02033 -0.08971 0.00276  261 TYR A CE2 
1753 C CZ  . TYR A 261 ? 0.40470 0.47802 0.69541 -0.02243 -0.10172 0.00126  261 TYR A CZ  
1754 O OH  . TYR A 261 ? 0.44680 0.52451 0.75725 -0.02753 -0.10343 0.00267  261 TYR A OH  
1755 N N   . ASN A 262 ? 0.22035 0.31126 0.50523 -0.00467 -0.08932 0.00158  262 ASN A N   
1756 C CA  . ASN A 262 ? 0.19771 0.30387 0.50348 -0.00461 -0.07925 0.00454  262 ASN A CA  
1757 C C   . ASN A 262 ? 0.19067 0.30422 0.49452 0.00152  -0.07009 0.00506  262 ASN A C   
1758 O O   . ASN A 262 ? 0.25760 0.37782 0.56267 0.00258  -0.05821 0.00692  262 ASN A O   
1759 C CB  . ASN A 262 ? 0.27851 0.38519 0.58531 -0.00899 -0.07142 0.00657  262 ASN A CB  
1760 C CG  . ASN A 262 ? 0.45809 0.57933 0.78818 -0.01007 -0.06224 0.01028  262 ASN A CG  
1761 O OD1 . ASN A 262 ? 0.54110 0.67095 0.89149 -0.01043 -0.06577 0.01120  262 ASN A OD1 
1762 N ND2 . ASN A 262 ? 0.47515 0.59938 0.80234 -0.01034 -0.05020 0.01268  262 ASN A ND2 
1763 N N   . GLY A 263 ? 0.18653 0.29757 0.48545 0.00590  -0.07583 0.00331  263 GLY A N   
1764 C CA  . GLY A 263 ? 0.23568 0.35264 0.53298 0.01219  -0.06855 0.00337  263 GLY A CA  
1765 C C   . GLY A 263 ? 0.23775 0.34689 0.51271 0.01427  -0.06306 0.00215  263 GLY A C   
1766 O O   . GLY A 263 ? 0.20057 0.31463 0.47337 0.01924  -0.05514 0.00215  263 GLY A O   
1767 N N   . GLY A 264 ? 0.19553 0.29256 0.45383 0.01080  -0.06733 0.00098  264 GLY A N   
1768 C CA  . GLY A 264 ? 0.20702 0.29655 0.44473 0.01246  -0.06327 -0.00019 264 GLY A CA  
1769 C C   . GLY A 264 ? 0.20864 0.29275 0.43756 0.01714  -0.06749 -0.00177 264 GLY A C   
1770 O O   . GLY A 264 ? 0.17016 0.25174 0.40347 0.01802  -0.07640 -0.00223 264 GLY A O   
1771 N N   . THR A 265 ? 0.17676 0.25874 0.39369 0.02027  -0.06148 -0.00258 265 THR A N   
1772 C CA  . THR A 265 ? 0.24167 0.31714 0.45021 0.02451  -0.06533 -0.00394 265 THR A CA  
1773 C C   . THR A 265 ? 0.22109 0.28651 0.40956 0.02434  -0.06397 -0.00510 265 THR A C   
1774 O O   . THR A 265 ? 0.16192 0.22924 0.34475 0.02315  -0.05671 -0.00510 265 THR A O   
1775 C CB  . THR A 265 ? 0.23494 0.31973 0.45408 0.03065  -0.05954 -0.00399 265 THR A CB  
1776 O OG1 . THR A 265 ? 0.28615 0.37815 0.50512 0.03194  -0.04815 -0.00370 265 THR A OG1 
1777 C CG2 . THR A 265 ? 0.20824 0.30282 0.44788 0.03166  -0.06240 -0.00276 265 THR A CG2 
1778 N N   . VAL A 266 ? 0.16702 0.22184 0.34515 0.02557  -0.07114 -0.00584 266 VAL A N   
1779 C CA  . VAL A 266 ? 0.14284 0.18823 0.30377 0.02585  -0.07033 -0.00668 266 VAL A CA  
1780 C C   . VAL A 266 ? 0.19878 0.24437 0.36047 0.03116  -0.06744 -0.00788 266 VAL A C   
1781 O O   . VAL A 266 ? 0.20921 0.25243 0.37512 0.03439  -0.07251 -0.00791 266 VAL A O   
1782 C CB  . VAL A 266 ? 0.14279 0.17478 0.28996 0.02391  -0.07966 -0.00622 266 VAL A CB  
1783 C CG1 . VAL A 266 ? 0.11721 0.14022 0.24776 0.02385  -0.07825 -0.00645 266 VAL A CG1 
1784 C CG2 . VAL A 266 ? 0.15187 0.18232 0.29741 0.01944  -0.08320 -0.00561 266 VAL A CG2 
1785 N N   . ALA A 267 ? 0.20610 0.25394 0.36351 0.03248  -0.05970 -0.00907 267 ALA A N   
1786 C CA  . ALA A 267 ? 0.22066 0.26724 0.37807 0.03781  -0.05731 -0.01088 267 ALA A CA  
1787 C C   . ALA A 267 ? 0.23502 0.26773 0.37957 0.03773  -0.06347 -0.01150 267 ALA A C   
1788 O O   . ALA A 267 ? 0.22390 0.25148 0.36952 0.04169  -0.06674 -0.01223 267 ALA A O   
1789 C CB  . ALA A 267 ? 0.15671 0.20989 0.31343 0.03982  -0.04730 -0.01235 267 ALA A CB  
1790 N N   . THR A 268 ? 0.21066 0.23713 0.34314 0.03341  -0.06493 -0.01082 268 THR A N   
1791 C CA  . THR A 268 ? 0.18780 0.20129 0.30747 0.03278  -0.07003 -0.01046 268 THR A CA  
1792 C C   . THR A 268 ? 0.23019 0.23878 0.33759 0.02781  -0.07163 -0.00861 268 THR A C   
1793 O O   . THR A 268 ? 0.19421 0.20908 0.30272 0.02502  -0.06855 -0.00826 268 THR A O   
1794 C CB  . THR A 268 ? 0.24750 0.25843 0.36464 0.03564  -0.06627 -0.01312 268 THR A CB  
1795 O OG1 . THR A 268 ? 0.20348 0.20085 0.31191 0.03590  -0.07249 -0.01217 268 THR A OG1 
1796 C CG2 . THR A 268 ? 0.22551 0.24078 0.33769 0.03330  -0.06012 -0.01433 268 THR A CG2 
1797 N N   . THR A 269 ? 0.17810 0.17482 0.27341 0.02693  -0.07644 -0.00700 269 THR A N   
1798 C CA  . THR A 269 ? 0.17291 0.16468 0.25497 0.02295  -0.07699 -0.00495 269 THR A CA  
1799 C C   . THR A 269 ? 0.16651 0.15120 0.24041 0.02279  -0.07661 -0.00433 269 THR A C   
1800 O O   . THR A 269 ? 0.15928 0.13906 0.23595 0.02559  -0.07815 -0.00512 269 THR A O   
1801 C CB  . THR A 269 ? 0.23091 0.21375 0.30326 0.02139  -0.08402 -0.00213 269 THR A CB  
1802 O OG1 . THR A 269 ? 0.25361 0.22579 0.32114 0.02358  -0.08972 -0.00038 269 THR A OG1 
1803 C CG2 . THR A 269 ? 0.18871 0.17805 0.27039 0.02114  -0.08575 -0.00300 269 THR A CG2 
1804 N N   . SER A 270 ? 0.16473 0.14861 0.22903 0.01952  -0.07475 -0.00285 270 SER A N   
1805 C CA  . SER A 270 ? 0.21971 0.19675 0.27532 0.01788  -0.07369 -0.00143 270 SER A CA  
1806 C C   . SER A 270 ? 0.19957 0.16933 0.23839 0.01390  -0.07372 0.00284  270 SER A C   
1807 O O   . SER A 270 ? 0.19609 0.17007 0.23160 0.01265  -0.07316 0.00304  270 SER A O   
1808 C CB  . SER A 270 ? 0.16985 0.15619 0.22996 0.01704  -0.06539 -0.00537 270 SER A CB  
1809 O OG  . SER A 270 ? 0.41219 0.39294 0.46293 0.01334  -0.06200 -0.00437 270 SER A OG  
1810 N N   . TYR A 271 ? 0.18587 0.14386 0.21401 0.01223  -0.07423 0.00646  271 TYR A N   
1811 C CA  . TYR A 271 ? 0.19615 0.14720 0.20752 0.00884  -0.07211 0.01103  271 TYR A CA  
1812 C C   . TYR A 271 ? 0.19408 0.14836 0.20341 0.00471  -0.06369 0.01110  271 TYR A C   
1813 O O   . TYR A 271 ? 0.25596 0.20932 0.27164 0.00388  -0.06223 0.00971  271 TYR A O   
1814 C CB  . TYR A 271 ? 0.18059 0.11598 0.18035 0.00972  -0.07759 0.01644  271 TYR A CB  
1815 C CG  . TYR A 271 ? 0.23633 0.16762 0.23915 0.01441  -0.08757 0.01645  271 TYR A CG  
1816 C CD1 . TYR A 271 ? 0.24762 0.18233 0.24736 0.01470  -0.08963 0.01487  271 TYR A CD1 
1817 C CD2 . TYR A 271 ? 0.33885 0.26423 0.34774 0.01716  -0.09146 0.01649  271 TYR A CD2 
1818 C CE1 . TYR A 271 ? 0.32998 0.26364 0.33388 0.01705  -0.09505 0.01326  271 TYR A CE1 
1819 C CE2 . TYR A 271 ? 0.41383 0.33898 0.42610 0.01995  -0.09647 0.01497  271 TYR A CE2 
1820 C CZ  . TYR A 271 ? 0.49101 0.42056 0.50128 0.01975  -0.09848 0.01349  271 TYR A CZ  
1821 O OH  . TYR A 271 ? 0.53612 0.46533 0.55104 0.02233  -0.10420 0.01218  271 TYR A OH  
1822 N N   . GLN A 272 ? 0.18282 0.14040 0.18354 0.00236  -0.05874 0.01257  272 GLN A N   
1823 C CA  . GLN A 272 ? 0.15226 0.11558 0.15308 -0.00130 -0.05092 0.01254  272 GLN A CA  
1824 C C   . GLN A 272 ? 0.16113 0.12025 0.14763 -0.00356 -0.04655 0.01769  272 GLN A C   
1825 O O   . GLN A 272 ? 0.16344 0.11697 0.13847 -0.00176 -0.04891 0.01988  272 GLN A O   
1826 C CB  . GLN A 272 ? 0.22461 0.20211 0.23431 -0.00066 -0.04709 0.00740  272 GLN A CB  
1827 C CG  . GLN A 272 ? 0.28184 0.26502 0.30474 0.00059  -0.04720 0.00241  272 GLN A CG  
1828 C CD  . GLN A 272 ? 0.25068 0.23370 0.27540 -0.00278 -0.04400 0.00202  272 GLN A CD  
1829 O OE1 . GLN A 272 ? 0.35186 0.32943 0.37014 -0.00643 -0.04209 0.00647  272 GLN A OE1 
1830 N NE2 . GLN A 272 ? 0.33305 0.32208 0.36667 -0.00155 -0.04332 -0.00330 272 GLN A NE2 
1831 N N   . ASN A 273 ? 0.15466 0.11642 0.14204 -0.00727 -0.04034 0.01948  273 ASN A N   
1832 C CA  . ASN A 273 ? 0.20837 0.17007 0.18504 -0.00907 -0.03394 0.02401  273 ASN A CA  
1833 C C   . ASN A 273 ? 0.21755 0.18665 0.19026 -0.00665 -0.03204 0.02145  273 ASN A C   
1834 O O   . ASN A 273 ? 0.19645 0.17447 0.17873 -0.00536 -0.03309 0.01626  273 ASN A O   
1835 C CB  . ASN A 273 ? 0.22648 0.19465 0.21090 -0.01361 -0.02765 0.02505  273 ASN A CB  
1836 C CG  . ASN A 273 ? 0.30434 0.26295 0.29154 -0.01696 -0.02890 0.02864  273 ASN A CG  
1837 O OD1 . ASN A 273 ? 0.29712 0.24376 0.27338 -0.01708 -0.02903 0.03481  273 ASN A OD1 
1838 N ND2 . ASN A 273 ? 0.29654 0.25921 0.29748 -0.01946 -0.03006 0.02473  273 ASN A ND2 
1839 N N   . SER A 274 ? 0.20783 0.17251 0.16594 -0.00574 -0.02884 0.02513  274 SER A N   
1840 C CA  . SER A 274 ? 0.22115 0.19031 0.17412 -0.00320 -0.02749 0.02260  274 SER A CA  
1841 C C   . SER A 274 ? 0.21124 0.19453 0.17380 -0.00418 -0.02112 0.01996  274 SER A C   
1842 O O   . SER A 274 ? 0.18806 0.17676 0.15174 -0.00214 -0.02086 0.01660  274 SER A O   
1843 C CB  . SER A 274 ? 0.23961 0.19928 0.17270 -0.00121 -0.02524 0.02676  274 SER A CB  
1844 O OG  . SER A 274 ? 0.25959 0.22192 0.18929 -0.00289 -0.01632 0.03123  274 SER A OG  
1845 N N   . SER A 275 ? 0.11695 0.10583 0.08699 -0.00733 -0.01661 0.02151  275 SER A N   
1846 C CA  . SER A 275 ? 0.13873 0.14136 0.11830 -0.00805 -0.01168 0.01901  275 SER A CA  
1847 C C   . SER A 275 ? 0.17277 0.18248 0.16346 -0.00680 -0.01526 0.01293  275 SER A C   
1848 O O   . SER A 275 ? 0.18642 0.20634 0.18170 -0.00562 -0.01225 0.01027  275 SER A O   
1849 C CB  . SER A 275 ? 0.19424 0.20116 0.18170 -0.01234 -0.00786 0.02162  275 SER A CB  
1850 O OG  . SER A 275 ? 0.26765 0.26966 0.26278 -0.01479 -0.01293 0.02046  275 SER A OG  
1851 N N   . VAL A 276 ? 0.18290 0.18714 0.17761 -0.00648 -0.02129 0.01107  276 VAL A N   
1852 C CA  . VAL A 276 ? 0.17765 0.18818 0.18239 -0.00458 -0.02376 0.00577  276 VAL A CA  
1853 C C   . VAL A 276 ? 0.18007 0.19288 0.18225 -0.00158 -0.02394 0.00423  276 VAL A C   
1854 O O   . VAL A 276 ? 0.19531 0.20069 0.19149 -0.00057 -0.02758 0.00549  276 VAL A O   
1855 C CB  . VAL A 276 ? 0.16382 0.16811 0.17436 -0.00427 -0.02966 0.00432  276 VAL A CB  
1856 C CG1 . VAL A 276 ? 0.10609 0.11688 0.12581 -0.00115 -0.03118 -0.00067 276 VAL A CG1 
1857 C CG2 . VAL A 276 ? 0.15512 0.15666 0.16986 -0.00754 -0.02965 0.00503  276 VAL A CG2 
1858 N N   . TYR A 277 ? 0.11101 0.13362 0.11780 -0.00021 -0.02040 0.00154  277 TYR A N   
1859 C CA  . TYR A 277 ? 0.10353 0.12862 0.10901 0.00219  -0.01943 0.00047  277 TYR A CA  
1860 C C   . TYR A 277 ? 0.13834 0.16485 0.15307 0.00377  -0.02279 -0.00227 277 TYR A C   
1861 O O   . TYR A 277 ? 0.11340 0.13660 0.12818 0.00444  -0.02560 -0.00204 277 TYR A O   
1862 C CB  . TYR A 277 ? 0.08902 0.12340 0.09478 0.00339  -0.01372 -0.00036 277 TYR A CB  
1863 C CG  . TYR A 277 ? 0.09185 0.12760 0.09422 0.00570  -0.01134 -0.00045 277 TYR A CG  
1864 C CD1 . TYR A 277 ? 0.13633 0.16437 0.12901 0.00592  -0.01184 0.00149  277 TYR A CD1 
1865 C CD2 . TYR A 277 ? 0.05910 0.10288 0.06660 0.00795  -0.00838 -0.00243 277 TYR A CD2 
1866 C CE1 . TYR A 277 ? 0.12243 0.15037 0.11215 0.00784  -0.00983 0.00118  277 TYR A CE1 
1867 C CE2 . TYR A 277 ? 0.09253 0.13661 0.09711 0.00989  -0.00580 -0.00193 277 TYR A CE2 
1868 C CZ  . TYR A 277 ? 0.17130 0.20735 0.16771 0.00958  -0.00664 -0.00024 277 TYR A CZ  
1869 O OH  . TYR A 277 ? 0.16671 0.20179 0.16059 0.01135  -0.00431 0.00001  277 TYR A OH  
1870 N N   . TYR A 278 ? 0.11736 0.14879 0.14034 0.00448  -0.02258 -0.00498 278 TYR A N   
1871 C CA  . TYR A 278 ? 0.10303 0.13622 0.13545 0.00671  -0.02484 -0.00739 278 TYR A CA  
1872 C C   . TYR A 278 ? 0.10324 0.13512 0.14084 0.00708  -0.02702 -0.00969 278 TYR A C   
1873 O O   . TYR A 278 ? 0.13402 0.16743 0.17032 0.00596  -0.02552 -0.01088 278 TYR A O   
1874 C CB  . TYR A 278 ? 0.09607 0.13799 0.13270 0.00935  -0.02017 -0.00907 278 TYR A CB  
1875 C CG  . TYR A 278 ? 0.12887 0.17439 0.17596 0.01227  -0.02052 -0.01150 278 TYR A CG  
1876 C CD1 . TYR A 278 ? 0.15039 0.19495 0.20517 0.01278  -0.02335 -0.01064 278 TYR A CD1 
1877 C CD2 . TYR A 278 ? 0.11026 0.16005 0.15979 0.01482  -0.01834 -0.01481 278 TYR A CD2 
1878 C CE1 . TYR A 278 ? 0.17527 0.22441 0.24133 0.01599  -0.02280 -0.01247 278 TYR A CE1 
1879 C CE2 . TYR A 278 ? 0.11389 0.16660 0.17196 0.01852  -0.01776 -0.01710 278 TYR A CE2 
1880 C CZ  . TYR A 278 ? 0.18408 0.23712 0.25100 0.01920  -0.01936 -0.01562 278 TYR A CZ  
1881 O OH  . TYR A 278 ? 0.20599 0.26322 0.28267 0.02337  -0.01781 -0.01753 278 TYR A OH  
1882 N N   . TYR A 279 ? 0.12764 0.15642 0.17183 0.00875  -0.03104 -0.01050 279 TYR A N   
1883 C CA  . TYR A 279 ? 0.15615 0.18215 0.20511 0.01000  -0.03330 -0.01308 279 TYR A CA  
1884 C C   . TYR A 279 ? 0.15446 0.18427 0.21373 0.01448  -0.03376 -0.01567 279 TYR A C   
1885 O O   . TYR A 279 ? 0.11531 0.14560 0.17984 0.01542  -0.03603 -0.01410 279 TYR A O   
1886 C CB  . TYR A 279 ? 0.10715 0.12199 0.15232 0.00764  -0.03842 -0.01033 279 TYR A CB  
1887 C CG  . TYR A 279 ? 0.13158 0.14099 0.18174 0.00909  -0.04156 -0.01276 279 TYR A CG  
1888 C CD1 . TYR A 279 ? 0.19433 0.20345 0.24435 0.00785  -0.04016 -0.01558 279 TYR A CD1 
1889 C CD2 . TYR A 279 ? 0.15678 0.16074 0.21203 0.01188  -0.04660 -0.01245 279 TYR A CD2 
1890 C CE1 . TYR A 279 ? 0.18258 0.18471 0.23637 0.00921  -0.04346 -0.01829 279 TYR A CE1 
1891 C CE2 . TYR A 279 ? 0.19829 0.19587 0.25751 0.01388  -0.04946 -0.01475 279 TYR A CE2 
1892 C CZ  . TYR A 279 ? 0.25412 0.25013 0.31207 0.01248  -0.04774 -0.01781 279 TYR A CZ  
1893 O OH  . TYR A 279 ? 0.28984 0.27771 0.35103 0.01449  -0.05092 -0.02063 279 TYR A OH  
1894 N N   . ASP A 280 ? 0.14507 0.17786 0.20739 0.01744  -0.03159 -0.01979 280 ASP A N   
1895 C CA  . ASP A 280 ? 0.13522 0.17188 0.20676 0.02273  -0.03056 -0.02251 280 ASP A CA  
1896 C C   . ASP A 280 ? 0.15287 0.18119 0.22685 0.02445  -0.03522 -0.02469 280 ASP A C   
1897 O O   . ASP A 280 ? 0.16827 0.19243 0.23793 0.02408  -0.03561 -0.02777 280 ASP A O   
1898 C CB  . ASP A 280 ? 0.13751 0.18235 0.20794 0.02616  -0.02411 -0.02576 280 ASP A CB  
1899 C CG  . ASP A 280 ? 0.29143 0.34098 0.37053 0.03256  -0.02110 -0.02827 280 ASP A CG  
1900 O OD1 . ASP A 280 ? 0.30739 0.35343 0.39385 0.03487  -0.02452 -0.02887 280 ASP A OD1 
1901 O OD2 . ASP A 280 ? 0.35643 0.41271 0.43388 0.03546  -0.01467 -0.02906 280 ASP A OD2 
1902 N N   . TYR A 281 ? 0.17987 0.20517 0.26111 0.02633  -0.03940 -0.02317 281 TYR A N   
1903 C CA  . TYR A 281 ? 0.18765 0.20321 0.27057 0.02826  -0.04438 -0.02455 281 TYR A CA  
1904 C C   . TYR A 281 ? 0.20831 0.22493 0.29515 0.03415  -0.04189 -0.03022 281 TYR A C   
1905 O O   . TYR A 281 ? 0.33110 0.33806 0.41692 0.03557  -0.04539 -0.03258 281 TYR A O   
1906 C CB  . TYR A 281 ? 0.24356 0.25612 0.33351 0.02982  -0.05012 -0.02145 281 TYR A CB  
1907 C CG  . TYR A 281 ? 0.21461 0.23538 0.31532 0.03422  -0.04707 -0.02239 281 TYR A CG  
1908 C CD1 . TYR A 281 ? 0.25485 0.28480 0.35828 0.03238  -0.04266 -0.02012 281 TYR A CD1 
1909 C CD2 . TYR A 281 ? 0.20164 0.21970 0.30769 0.03914  -0.04753 -0.02476 281 TYR A CD2 
1910 C CE1 . TYR A 281 ? 0.25490 0.29212 0.36742 0.03505  -0.03881 -0.01968 281 TYR A CE1 
1911 C CE2 . TYR A 281 ? 0.22262 0.24872 0.33707 0.04226  -0.04327 -0.02444 281 TYR A CE2 
1912 C CZ  . TYR A 281 ? 0.32573 0.36173 0.44395 0.04005  -0.03893 -0.02164 281 TYR A CZ  
1913 O OH  . TYR A 281 ? 0.36293 0.40735 0.49086 0.04302  -0.03465 -0.02057 281 TYR A OH  
1914 N N   . VAL A 282 ? 0.21803 0.24524 0.30852 0.03795  -0.03569 -0.03231 282 VAL A N   
1915 C CA  . VAL A 282 ? 0.31560 0.34383 0.40804 0.04485  -0.03245 -0.03780 282 VAL A CA  
1916 C C   . VAL A 282 ? 0.39135 0.41559 0.47257 0.04385  -0.03157 -0.04243 282 VAL A C   
1917 O O   . VAL A 282 ? 0.29144 0.30719 0.37024 0.04657  -0.03415 -0.04718 282 VAL A O   
1918 C CB  . VAL A 282 ? 0.30636 0.34520 0.40125 0.04725  -0.02393 -0.03597 282 VAL A CB  
1919 C CG1 . VAL A 282 ? 0.28710 0.32578 0.37810 0.05358  -0.01898 -0.04065 282 VAL A CG1 
1920 C CG2 . VAL A 282 ? 0.30343 0.34495 0.40806 0.04667  -0.02463 -0.03108 282 VAL A CG2 
1921 N N   . SER A 283 ? 0.27357 0.30347 0.34831 0.04005  -0.02861 -0.04121 283 SER A N   
1922 C CA  . SER A 283 ? 0.22132 0.24984 0.28665 0.03934  -0.02822 -0.04562 283 SER A CA  
1923 C C   . SER A 283 ? 0.27121 0.29295 0.33224 0.03180  -0.03322 -0.04434 283 SER A C   
1924 O O   . SER A 283 ? 0.25294 0.27256 0.30861 0.03048  -0.03472 -0.04837 283 SER A O   
1925 C CB  . SER A 283 ? 0.23314 0.27236 0.29402 0.04060  -0.02196 -0.04510 283 SER A CB  
1926 O OG  . SER A 283 ? 0.23529 0.27846 0.29591 0.03491  -0.02144 -0.03949 283 SER A OG  
1927 N N   . ASN A 284 ? 0.17383 0.19233 0.23732 0.02706  -0.03581 -0.03868 284 ASN A N   
1928 C CA  . ASN A 284 ? 0.15055 0.16420 0.21010 0.01970  -0.03860 -0.03549 284 ASN A CA  
1929 C C   . ASN A 284 ? 0.07979 0.10219 0.13468 0.01646  -0.03501 -0.03392 284 ASN A C   
1930 O O   . ASN A 284 ? 0.17844 0.19883 0.23101 0.01090  -0.03626 -0.03185 284 ASN A O   
1931 C CB  . ASN A 284 ? 0.22201 0.22549 0.28071 0.01765  -0.04305 -0.03911 284 ASN A CB  
1932 C CG  . ASN A 284 ? 0.33399 0.32543 0.39617 0.01903  -0.04756 -0.03849 284 ASN A CG  
1933 O OD1 . ASN A 284 ? 0.30848 0.29788 0.37260 0.01896  -0.04870 -0.03350 284 ASN A OD1 
1934 N ND2 . ASN A 284 ? 0.33001 0.31257 0.39241 0.02062  -0.05077 -0.04380 284 ASN A ND2 
1935 N N   . TYR A 285 ? 0.15106 0.18307 0.20519 0.02015  -0.03021 -0.03453 285 TYR A N   
1936 C CA  . TYR A 285 ? 0.14076 0.18068 0.19048 0.01808  -0.02664 -0.03229 285 TYR A CA  
1937 C C   . TYR A 285 ? 0.11973 0.15756 0.16827 0.01308  -0.02721 -0.02626 285 TYR A C   
1938 O O   . TYR A 285 ? 0.11924 0.15446 0.16996 0.01337  -0.02806 -0.02326 285 TYR A O   
1939 C CB  . TYR A 285 ? 0.10854 0.15705 0.15798 0.02298  -0.02111 -0.03238 285 TYR A CB  
1940 C CG  . TYR A 285 ? 0.20294 0.25828 0.24746 0.02146  -0.01747 -0.02959 285 TYR A CG  
1941 C CD1 . TYR A 285 ? 0.13046 0.18623 0.17494 0.01875  -0.01625 -0.02444 285 TYR A CD1 
1942 C CD2 . TYR A 285 ? 0.19403 0.25458 0.23327 0.02324  -0.01588 -0.03237 285 TYR A CD2 
1943 C CE1 . TYR A 285 ? 0.13459 0.19544 0.17413 0.01811  -0.01278 -0.02207 285 TYR A CE1 
1944 C CE2 . TYR A 285 ? 0.20966 0.27626 0.24461 0.02266  -0.01272 -0.02960 285 TYR A CE2 
1945 C CZ  . TYR A 285 ? 0.20602 0.27252 0.24126 0.02017  -0.01084 -0.02442 285 TYR A CZ  
1946 O OH  . TYR A 285 ? 0.17419 0.24550 0.20476 0.02024  -0.00762 -0.02187 285 TYR A OH  
1947 N N   . THR A 286 ? 0.11245 0.15162 0.15751 0.00889  -0.02685 -0.02463 286 THR A N   
1948 C CA  . THR A 286 ? 0.19503 0.23168 0.23692 0.00484  -0.02646 -0.01896 286 THR A CA  
1949 C C   . THR A 286 ? 0.18161 0.22634 0.21964 0.00402  -0.02235 -0.01741 286 THR A C   
1950 O O   . THR A 286 ? 0.17558 0.22538 0.21439 0.00320  -0.02194 -0.01957 286 THR A O   
1951 C CB  . THR A 286 ? 0.17310 0.20126 0.21525 0.00012  -0.02966 -0.01686 286 THR A CB  
1952 O OG1 . THR A 286 ? 0.14338 0.16329 0.18916 0.00155  -0.03387 -0.01896 286 THR A OG1 
1953 C CG2 . THR A 286 ? 0.17239 0.19617 0.20897 -0.00263 -0.02882 -0.01061 286 THR A CG2 
1954 N N   . GLN A 287 ? 0.11532 0.16096 0.14940 0.00449  -0.01986 -0.01392 287 GLN A N   
1955 C CA  . GLN A 287 ? 0.08328 0.13553 0.11317 0.00451  -0.01575 -0.01223 287 GLN A CA  
1956 C C   . GLN A 287 ? 0.11332 0.16122 0.13800 0.00135  -0.01488 -0.00742 287 GLN A C   
1957 O O   . GLN A 287 ? 0.14386 0.18379 0.16524 0.00068  -0.01683 -0.00500 287 GLN A O   
1958 C CB  . GLN A 287 ? 0.08263 0.13900 0.11090 0.00836  -0.01263 -0.01237 287 GLN A CB  
1959 C CG  . GLN A 287 ? 0.07795 0.14094 0.10169 0.00963  -0.00837 -0.01109 287 GLN A CG  
1960 C CD  . GLN A 287 ? 0.09153 0.15772 0.11415 0.01356  -0.00510 -0.01126 287 GLN A CD  
1961 O OE1 . GLN A 287 ? 0.09557 0.16275 0.12197 0.01595  -0.00504 -0.01339 287 GLN A OE1 
1962 N NE2 . GLN A 287 ? 0.08820 0.15533 0.10566 0.01444  -0.00190 -0.00867 287 GLN A NE2 
1963 N N   . TYR A 288 ? 0.09510 0.14844 0.11901 -0.00016 -0.01207 -0.00608 288 TYR A N   
1964 C CA  . TYR A 288 ? 0.12113 0.17213 0.13933 -0.00211 -0.00923 -0.00124 288 TYR A CA  
1965 C C   . TYR A 288 ? 0.19530 0.25182 0.20833 0.00097  -0.00469 -0.00016 288 TYR A C   
1966 O O   . TYR A 288 ? 0.11400 0.17806 0.12937 0.00376  -0.00353 -0.00270 288 TYR A O   
1967 C CB  . TYR A 288 ? 0.12094 0.17434 0.14417 -0.00631 -0.00863 0.00036  288 TYR A CB  
1968 C CG  . TYR A 288 ? 0.14144 0.18594 0.16787 -0.00959 -0.01288 0.00045  288 TYR A CG  
1969 C CD1 . TYR A 288 ? 0.16938 0.20349 0.18957 -0.01136 -0.01305 0.00515  288 TYR A CD1 
1970 C CD2 . TYR A 288 ? 0.17742 0.22250 0.21151 -0.01019 -0.01693 -0.00425 288 TYR A CD2 
1971 C CE1 . TYR A 288 ? 0.17746 0.20219 0.19987 -0.01380 -0.01707 0.00575  288 TYR A CE1 
1972 C CE2 . TYR A 288 ? 0.14801 0.18343 0.18472 -0.01269 -0.02094 -0.00426 288 TYR A CE2 
1973 C CZ  . TYR A 288 ? 0.19601 0.22140 0.22726 -0.01455 -0.02092 0.00105  288 TYR A CZ  
1974 O OH  . TYR A 288 ? 0.22447 0.23931 0.25765 -0.01653 -0.02492 0.00161  288 TYR A OH  
1975 N N   . ASP A 289 ? 0.12855 0.18010 0.13319 0.00104  -0.00217 0.00362  289 ASP A N   
1976 C CA  . ASP A 289 ? 0.13051 0.18506 0.12891 0.00437  0.00225  0.00477  289 ASP A CA  
1977 C C   . ASP A 289 ? 0.12712 0.17960 0.11898 0.00368  0.00641  0.00913  289 ASP A C   
1978 O O   . ASP A 289 ? 0.09741 0.14177 0.07797 0.00555  0.00773  0.01101  289 ASP A O   
1979 C CB  . ASP A 289 ? 0.11219 0.15982 0.10464 0.00679  0.00072  0.00386  289 ASP A CB  
1980 C CG  . ASP A 289 ? 0.15099 0.20118 0.13823 0.01056  0.00484  0.00420  289 ASP A CG  
1981 O OD1 . ASP A 289 ? 0.13895 0.19876 0.13017 0.01246  0.00769  0.00355  289 ASP A OD1 
1982 O OD2 . ASP A 289 ? 0.16385 0.20568 0.14264 0.01185  0.00466  0.00494  289 ASP A OD2 
1983 N N   . ASN A 290 ? 0.09791 0.15746 0.09697 0.00105  0.00848  0.01070  290 ASN A N   
1984 C CA  . ASN A 290 ? 0.13179 0.18941 0.12694 -0.00056 0.01300  0.01575  290 ASN A CA  
1985 C C   . ASN A 290 ? 0.19375 0.25349 0.18062 0.00379  0.01925  0.01800  290 ASN A C   
1986 O O   . ASN A 290 ? 0.16143 0.21542 0.13911 0.00432  0.02346  0.02215  290 ASN A O   
1987 C CB  . ASN A 290 ? 0.17508 0.24163 0.18348 -0.00502 0.01398  0.01702  290 ASN A CB  
1988 C CG  . ASN A 290 ? 0.19960 0.26052 0.21417 -0.00955 0.00825  0.01556  290 ASN A CG  
1989 O OD1 . ASN A 290 ? 0.18389 0.23328 0.19153 -0.00949 0.00479  0.01552  290 ASN A OD1 
1990 N ND2 . ASN A 290 ? 0.14979 0.21855 0.17780 -0.01331 0.00664  0.01412  290 ASN A ND2 
1991 N N   . ASN A 291 ? 0.20595 0.27316 0.19498 0.00752  0.02016  0.01543  291 ASN A N   
1992 C CA  . ASN A 291 ? 0.16954 0.23768 0.15125 0.01245  0.02563  0.01693  291 ASN A CA  
1993 C C   . ASN A 291 ? 0.20335 0.25916 0.17433 0.01569  0.02318  0.01449  291 ASN A C   
1994 O O   . ASN A 291 ? 0.17250 0.22334 0.13977 0.01873  0.02469  0.01385  291 ASN A O   
1995 C CB  . ASN A 291 ? 0.23572 0.31432 0.22847 0.01395  0.02585  0.01528  291 ASN A CB  
1996 C CG  . ASN A 291 ? 0.37788 0.46939 0.38389 0.01015  0.02753  0.01726  291 ASN A CG  
1997 O OD1 . ASN A 291 ? 0.29839 0.38956 0.30455 0.00794  0.03178  0.02141  291 ASN A OD1 
1998 N ND2 . ASN A 291 ? 0.45261 0.55441 0.46997 0.00910  0.02380  0.01422  291 ASN A ND2 
1999 N N   . TYR A 292 ? 0.11949 0.16974 0.08783 0.01421  0.01845  0.01287  292 TYR A N   
2000 C CA  . TYR A 292 ? 0.14030 0.18011 0.09988 0.01633  0.01566  0.01097  292 TYR A CA  
2001 C C   . TYR A 292 ? 0.19873 0.24178 0.16257 0.01915  0.01630  0.00873  292 TYR A C   
2002 O O   . TYR A 292 ? 0.19018 0.22460 0.14773 0.02095  0.01552  0.00777  292 TYR A O   
2003 C CB  . TYR A 292 ? 0.20750 0.23458 0.15245 0.01805  0.01697  0.01250  292 TYR A CB  
2004 C CG  . TYR A 292 ? 0.26137 0.28144 0.19970 0.01557  0.01520  0.01508  292 TYR A CG  
2005 C CD1 . TYR A 292 ? 0.19661 0.20720 0.13308 0.01337  0.00785  0.01354  292 TYR A CD1 
2006 C CD2 . TYR A 292 ? 0.26236 0.28491 0.19864 0.01504  0.02053  0.01918  292 TYR A CD2 
2007 C CE1 . TYR A 292 ? 0.16106 0.16389 0.09207 0.01128  0.00531  0.01590  292 TYR A CE1 
2008 C CE2 . TYR A 292 ? 0.27671 0.29094 0.20712 0.01249  0.01890  0.02206  292 TYR A CE2 
2009 C CZ  . TYR A 292 ? 0.24992 0.25374 0.17691 0.01089  0.01091  0.02028  292 TYR A CZ  
2010 O OH  . TYR A 292 ? 0.21855 0.21297 0.13868 0.00905  0.00848  0.02329  292 TYR A OH  
2011 N N   . THR A 293 ? 0.13983 0.19367 0.11447 0.01912  0.01676  0.00796  293 THR A N   
2012 C CA  . THR A 293 ? 0.18519 0.24003 0.16359 0.02145  0.01616  0.00657  293 THR A CA  
2013 C C   . THR A 293 ? 0.18230 0.23355 0.15977 0.02176  0.01421  0.00502  293 THR A C   
2014 O O   . THR A 293 ? 0.18574 0.23068 0.15950 0.02366  0.01482  0.00510  293 THR A O   
2015 C CB  . THR A 293 ? 0.20414 0.26991 0.19164 0.02136  0.01527  0.00588  293 THR A CB  
2016 O OG1 . THR A 293 ? 0.22503 0.29578 0.21465 0.02134  0.01756  0.00764  293 THR A OG1 
2017 C CG2 . THR A 293 ? 0.20877 0.27369 0.19686 0.02404  0.01421  0.00527  293 THR A CG2 
2018 N N   . ASP A 294 ? 0.14629 0.20256 0.12769 0.02004  0.01235  0.00363  294 ASP A N   
2019 C CA  . ASP A 294 ? 0.14819 0.20052 0.13216 0.01962  0.01005  0.00228  294 ASP A CA  
2020 C C   . ASP A 294 ? 0.14434 0.18442 0.12243 0.01815  0.00734  0.00268  294 ASP A C   
2021 O O   . ASP A 294 ? 0.11432 0.15020 0.09349 0.01840  0.00661  0.00233  294 ASP A O   
2022 C CB  . ASP A 294 ? 0.16871 0.22497 0.16187 0.01721  0.00677  0.00028  294 ASP A CB  
2023 C CG  . ASP A 294 ? 0.30102 0.35731 0.29920 0.01812  0.00654  -0.00074 294 ASP A CG  
2024 O OD1 . ASP A 294 ? 0.26732 0.32979 0.26658 0.02124  0.00966  -0.00100 294 ASP A OD1 
2025 O OD2 . ASP A 294 ? 0.20906 0.25934 0.21007 0.01599  0.00342  -0.00091 294 ASP A OD2 
2026 N N   . THR A 295 ? 0.11703 0.15115 0.08910 0.01649  0.00556  0.00351  295 THR A N   
2027 C CA  . THR A 295 ? 0.12396 0.14537 0.08804 0.01567  0.00182  0.00342  295 THR A CA  
2028 C C   . THR A 295 ? 0.17731 0.19271 0.13331 0.01873  0.00422  0.00341  295 THR A C   
2029 O O   . THR A 295 ? 0.17495 0.18379 0.13200 0.01791  0.00119  0.00231  295 THR A O   
2030 C CB  . THR A 295 ? 0.14064 0.15585 0.09564 0.01476  0.00071  0.00493  295 THR A CB  
2031 O OG1 . THR A 295 ? 0.14315 0.16105 0.10564 0.01160  -0.00255 0.00504  295 THR A OG1 
2032 C CG2 . THR A 295 ? 0.18119 0.18192 0.12433 0.01507  -0.00365 0.00437  295 THR A CG2 
2033 N N   . TYR A 296 ? 0.14537 0.16316 0.09452 0.02226  0.00965  0.00471  296 TYR A N   
2034 C CA  . TYR A 296 ? 0.12197 0.13311 0.06273 0.02600  0.01236  0.00467  296 TYR A CA  
2035 C C   . TYR A 296 ? 0.16563 0.17860 0.11265 0.02680  0.01304  0.00430  296 TYR A C   
2036 O O   . TYR A 296 ? 0.21261 0.21528 0.15524 0.02723  0.01172  0.00365  296 TYR A O   
2037 C CB  . TYR A 296 ? 0.14913 0.16405 0.09308 0.02715  0.01637  0.00576  296 TYR A CB  
2038 C CG  . TYR A 296 ? 0.24328 0.25498 0.18121 0.02649  0.01722  0.00670  296 TYR A CG  
2039 C CD1 . TYR A 296 ? 0.27943 0.28124 0.20671 0.02539  0.01391  0.00641  296 TYR A CD1 
2040 C CD2 . TYR A 296 ? 0.34705 0.36506 0.28929 0.02726  0.02093  0.00816  296 TYR A CD2 
2041 C CE1 . TYR A 296 ? 0.31093 0.30921 0.23182 0.02504  0.01524  0.00785  296 TYR A CE1 
2042 C CE2 . TYR A 296 ? 0.43871 0.45427 0.37531 0.02691  0.02295  0.00965  296 TYR A CE2 
2043 C CZ  . TYR A 296 ? 0.39780 0.40338 0.32347 0.02580  0.02049  0.00963  296 TYR A CZ  
2044 O OH  . TYR A 296 ? 0.42290 0.42551 0.34209 0.02572  0.02288  0.01163  296 TYR A OH  
2045 N N   . SER A 297 ? 0.10344 0.12853 0.06084 0.02680  0.01493  0.00476  297 SER A N   
2046 C CA  . SER A 297 ? 0.17448 0.20198 0.13727 0.02800  0.01661  0.00518  297 SER A CA  
2047 C C   . SER A 297 ? 0.22319 0.24388 0.19178 0.02400  0.01247  0.00443  297 SER A C   
2048 O O   . SER A 297 ? 0.13806 0.15304 0.10720 0.02429  0.01340  0.00523  297 SER A O   
2049 C CB  . SER A 297 ? 0.17011 0.20820 0.14384 0.02704  0.01641  0.00515  297 SER A CB  
2050 O OG  . SER A 297 ? 0.27655 0.31559 0.25407 0.02808  0.01789  0.00598  297 SER A OG  
2051 N N   . THR A 298 ? 0.17844 0.19966 0.15232 0.02021  0.00778  0.00318  298 THR A N   
2052 C CA  . THR A 298 ? 0.12938 0.14651 0.11168 0.01655  0.00336  0.00251  298 THR A CA  
2053 C C   . THR A 298 ? 0.17138 0.17462 0.14686 0.01510  -0.00097 0.00168  298 THR A C   
2054 O O   . THR A 298 ? 0.16465 0.16346 0.14638 0.01306  -0.00257 0.00180  298 THR A O   
2055 C CB  . THR A 298 ? 0.18478 0.20612 0.17468 0.01377  -0.00099 0.00135  298 THR A CB  
2056 O OG1 . THR A 298 ? 0.13109 0.16385 0.12718 0.01519  0.00244  0.00133  298 THR A OG1 
2057 C CG2 . THR A 298 ? 0.17650 0.19522 0.17704 0.01055  -0.00568 0.00081  298 THR A CG2 
2058 N N   . LEU A 299 ? 0.15904 0.15500 0.12152 0.01622  -0.00269 0.00088  299 LEU A N   
2059 C CA  . LEU A 299 ? 0.18258 0.16356 0.13494 0.01585  -0.00719 -0.00068 299 LEU A CA  
2060 C C   . LEU A 299 ? 0.22447 0.19993 0.17447 0.01777  -0.00378 -0.00026 299 LEU A C   
2061 O O   . LEU A 299 ? 0.22551 0.19088 0.17667 0.01540  -0.00817 -0.00150 299 LEU A O   
2062 C CB  . LEU A 299 ? 0.18267 0.15666 0.11812 0.01850  -0.00732 -0.00117 299 LEU A CB  
2063 C CG  . LEU A 299 ? 0.24554 0.22171 0.17913 0.01714  -0.01009 -0.00076 299 LEU A CG  
2064 C CD1 . LEU A 299 ? 0.29682 0.26252 0.21126 0.02012  -0.00985 -0.00080 299 LEU A CD1 
2065 C CD2 . LEU A 299 ? 0.20190 0.17661 0.14494 0.01286  -0.01829 -0.00194 299 LEU A CD2 
2066 N N   . ALA A 300 ? 0.14352 0.12524 0.09058 0.02207  0.00357  0.00156  300 ALA A N   
2067 C CA  . ALA A 300 ? 0.19706 0.17271 0.14036 0.02491  0.00729  0.00251  300 ALA A CA  
2068 C C   . ALA A 300 ? 0.21353 0.19121 0.17055 0.02170  0.00745  0.00402  300 ALA A C   
2069 O O   . ALA A 300 ? 0.23275 0.19991 0.18941 0.02074  0.00672  0.00424  300 ALA A O   
2070 C CB  . ALA A 300 ? 0.20553 0.18920 0.14396 0.03086  0.01467  0.00446  300 ALA A CB  
2071 N N   . ASN A 301 ? 0.14528 0.13596 0.11440 0.02013  0.00878  0.00519  301 ASN A N   
2072 C CA  . ASN A 301 ? 0.16334 0.15790 0.14554 0.01802  0.01095  0.00741  301 ASN A CA  
2073 C C   . ASN A 301 ? 0.17642 0.16332 0.16783 0.01227  0.00492  0.00650  301 ASN A C   
2074 O O   . ASN A 301 ? 0.21029 0.19465 0.21021 0.01023  0.00683  0.00873  301 ASN A O   
2075 C CB  . ASN A 301 ? 0.25007 0.25954 0.24179 0.01831  0.01341  0.00812  301 ASN A CB  
2076 C CG  . ASN A 301 ? 0.39548 0.41003 0.39708 0.01850  0.01868  0.01130  301 ASN A CG  
2077 O OD1 . ASN A 301 ? 0.48660 0.49663 0.48454 0.02069  0.02321  0.01403  301 ASN A OD1 
2078 N ND2 . ASN A 301 ? 0.37728 0.40070 0.39076 0.01676  0.01866  0.01128  301 ASN A ND2 
2079 N N   . TYR A 302 ? 0.14933 0.13266 0.13954 0.00962  -0.00254 0.00353  302 TYR A N   
2080 C CA  . TYR A 302 ? 0.16497 0.14337 0.16609 0.00413  -0.00995 0.00225  302 TYR A CA  
2081 C C   . TYR A 302 ? 0.21033 0.17168 0.20029 0.00301  -0.01658 -0.00061 302 TYR A C   
2082 O O   . TYR A 302 ? 0.22335 0.17868 0.22061 -0.00160 -0.02478 -0.00251 302 TYR A O   
2083 C CB  . TYR A 302 ? 0.16603 0.15169 0.17432 0.00226  -0.01518 0.00080  302 TYR A CB  
2084 C CG  . TYR A 302 ? 0.18036 0.18130 0.20135 0.00302  -0.00987 0.00281  302 TYR A CG  
2085 C CD1 . TYR A 302 ? 0.26853 0.27558 0.29764 0.00387  -0.00232 0.00591  302 TYR A CD1 
2086 C CD2 . TYR A 302 ? 0.09796 0.10588 0.12154 0.00331  -0.01232 0.00163  302 TYR A CD2 
2087 C CE1 . TYR A 302 ? 0.28044 0.30029 0.31878 0.00546  0.00262  0.00730  302 TYR A CE1 
2088 C CE2 . TYR A 302 ? 0.14169 0.16197 0.17554 0.00457  -0.00784 0.00269  302 TYR A CE2 
2089 C CZ  . TYR A 302 ? 0.20917 0.23543 0.24979 0.00588  -0.00034 0.00530  302 TYR A CZ  
2090 O OH  . TYR A 302 ? 0.19718 0.23461 0.24555 0.00804  0.00429  0.00595  302 TYR A OH  
2091 N N   . ARG A 303 ? 0.21250 0.16620 0.18487 0.00763  -0.01332 -0.00117 303 ARG A N   
2092 C CA  . ARG A 303 ? 0.23150 0.16754 0.18848 0.00832  -0.01892 -0.00457 303 ARG A CA  
2093 C C   . ARG A 303 ? 0.23147 0.15586 0.19598 0.00348  -0.02468 -0.00579 303 ARG A C   
2094 O O   . ARG A 303 ? 0.27141 0.18385 0.23118 0.00097  -0.03438 -0.00971 303 ARG A O   
2095 C CB  . ARG A 303 ? 0.20011 0.13124 0.13995 0.01497  -0.01205 -0.00411 303 ARG A CB  
2096 C CG  . ARG A 303 ? 0.25839 0.16969 0.18054 0.01705  -0.01638 -0.00778 303 ARG A CG  
2097 C CD  . ARG A 303 ? 0.20082 0.11002 0.10526 0.02487  -0.00938 -0.00748 303 ARG A CD  
2098 N NE  . ARG A 303 ? 0.27264 0.16148 0.15940 0.02792  -0.01245 -0.01114 303 ARG A NE  
2099 C CZ  . ARG A 303 ? 0.30827 0.19150 0.17886 0.03543  -0.00655 -0.01137 303 ARG A CZ  
2100 N NH1 . ARG A 303 ? 0.32061 0.21822 0.19221 0.04015  0.00226  -0.00792 303 ARG A NH1 
2101 N NH2 . ARG A 303 ? 0.31686 0.18004 0.17054 0.03853  -0.00980 -0.01533 303 ARG A NH2 
2102 N N   . TYR A 304 ? 0.18930 0.11682 0.16557 0.00206  -0.01902 -0.00231 304 TYR A N   
2103 C CA  . TYR A 304 ? 0.21073 0.12656 0.19519 -0.00291 -0.02323 -0.00268 304 TYR A CA  
2104 C C   . TYR A 304 ? 0.29760 0.22327 0.30771 -0.00980 -0.02547 -0.00050 304 TYR A C   
2105 O O   . TYR A 304 ? 0.25107 0.16955 0.27278 -0.01502 -0.02819 0.00016  304 TYR A O   
2106 C CB  . TYR A 304 ? 0.22310 0.13229 0.20227 0.00021  -0.01513 0.00037  304 TYR A CB  
2107 C CG  . TYR A 304 ? 0.25353 0.15117 0.20857 0.00729  -0.01350 -0.00211 304 TYR A CG  
2108 C CD1 . TYR A 304 ? 0.20804 0.08563 0.14972 0.00722  -0.02093 -0.00702 304 TYR A CD1 
2109 C CD2 . TYR A 304 ? 0.27477 0.18166 0.22065 0.01436  -0.00484 0.00019  304 TYR A CD2 
2110 C CE1 . TYR A 304 ? 0.26404 0.13100 0.18329 0.01458  -0.01860 -0.00932 304 TYR A CE1 
2111 C CE2 . TYR A 304 ? 0.21617 0.11379 0.14176 0.02134  -0.00266 -0.00174 304 TYR A CE2 
2112 C CZ  . TYR A 304 ? 0.26906 0.14679 0.18123 0.02167  -0.00900 -0.00636 304 TYR A CZ  
2113 O OH  . TYR A 304 ? 0.31838 0.18675 0.21002 0.02939  -0.00613 -0.00835 304 TYR A OH  
2114 N N   . ARG A 305 ? 0.24690 0.18886 0.26670 -0.00977 -0.02409 0.00072  305 ARG A N   
2115 C CA  . ARG A 305 ? 0.26737 0.22078 0.31224 -0.01505 -0.02478 0.00311  305 ARG A CA  
2116 C C   . ARG A 305 ? 0.23921 0.18899 0.29413 -0.02053 -0.03755 -0.00057 305 ARG A C   
2117 O O   . ARG A 305 ? 0.27721 0.22079 0.31931 -0.01920 -0.04567 -0.00482 305 ARG A O   
2118 C CB  . ARG A 305 ? 0.27469 0.24623 0.32570 -0.01203 -0.01823 0.00547  305 ARG A CB  
2119 C CG  . ARG A 305 ? 0.26436 0.24233 0.31122 -0.00738 -0.00603 0.00970  305 ARG A CG  
2120 C CD  . ARG A 305 ? 0.31675 0.31200 0.37348 -0.00541 -0.00050 0.01172  305 ARG A CD  
2121 N NE  . ARG A 305 ? 0.32895 0.32949 0.37698 0.00020  0.00946  0.01463  305 ARG A NE  
2122 C CZ  . ARG A 305 ? 0.31579 0.32946 0.36860 0.00316  0.01548  0.01634  305 ARG A CZ  
2123 N NH1 . ARG A 305 ? 0.23782 0.26081 0.30460 0.00128  0.01345  0.01562  305 ARG A NH1 
2124 N NH2 . ARG A 305 ? 0.31120 0.32819 0.35416 0.00858  0.02314  0.01853  305 ARG A NH2 
2125 N N   . GLN A 306 ? 0.26176 0.21609 0.34045 -0.02654 -0.03905 0.00156  306 GLN A N   
2126 C CA  . GLN A 306 ? 0.34151 0.29563 0.43541 -0.03218 -0.05143 -0.00135 306 GLN A CA  
2127 C C   . GLN A 306 ? 0.27881 0.25288 0.39627 -0.03330 -0.04854 0.00174  306 GLN A C   
2128 O O   . GLN A 306 ? 0.29626 0.28153 0.42460 -0.03244 -0.03702 0.00682  306 GLN A O   
2129 C CB  . GLN A 306 ? 0.51431 0.45689 0.61946 -0.03898 -0.05685 -0.00175 306 GLN A CB  
2130 C CG  . GLN A 306 ? 0.65656 0.58155 0.75064 -0.04128 -0.07225 -0.00857 306 GLN A CG  
2131 C CD  . GLN A 306 ? 0.70165 0.61259 0.76197 -0.03447 -0.07295 -0.01254 306 GLN A CD  
2132 O OE1 . GLN A 306 ? 0.76908 0.67221 0.81595 -0.03307 -0.08350 -0.01758 306 GLN A OE1 
2133 N NE2 . GLN A 306 ? 0.61333 0.52102 0.65977 -0.02980 -0.06161 -0.01000 306 GLN A NE2 
2134 N N   . THR A 307 ? 0.28071 0.25855 0.40437 -0.03433 -0.05879 -0.00132 307 THR A N   
2135 C CA  . THR A 307 ? 0.22937 0.22536 0.37492 -0.03449 -0.05713 0.00095  307 THR A CA  
2136 C C   . THR A 307 ? 0.28142 0.28771 0.45287 -0.03821 -0.04982 0.00598  307 THR A C   
2137 O O   . THR A 307 ? 0.29937 0.29921 0.47751 -0.04232 -0.05312 0.00616  307 THR A O   
2138 C CB  . THR A 307 ? 0.26572 0.26071 0.41042 -0.03363 -0.06906 -0.00261 307 THR A CB  
2139 O OG1 . THR A 307 ? 0.28493 0.27143 0.40616 -0.02997 -0.07437 -0.00619 307 THR A OG1 
2140 C CG2 . THR A 307 ? 0.27541 0.28649 0.43743 -0.03154 -0.06548 -0.00016 307 THR A CG2 
2141 N N   . SER A 308 ? 0.27504 0.29664 0.45725 -0.03546 -0.03858 0.01018  308 SER A N   
2142 C CA  . SER A 308 ? 0.32228 0.35358 0.52382 -0.03675 -0.02945 0.01542  308 SER A CA  
2143 C C   . SER A 308 ? 0.32983 0.37313 0.54383 -0.03430 -0.03051 0.01537  308 SER A C   
2144 O O   . SER A 308 ? 0.29961 0.35051 0.50902 -0.02925 -0.02730 0.01476  308 SER A O   
2145 C CB  . SER A 308 ? 0.31182 0.34942 0.51225 -0.03402 -0.01414 0.02069  308 SER A CB  
2146 O OG  . SER A 308 ? 0.38437 0.43212 0.59941 -0.03322 -0.00447 0.02565  308 SER A OG  
2147 N N   . CYS A 309 ? 0.19579 0.24013 0.42528 -0.03778 -0.03492 0.01594  309 CYS A N   
2148 C CA  . CYS A 309 ? 0.27196 0.32612 0.51371 -0.03578 -0.03716 0.01566  309 CYS A CA  
2149 C C   . CYS A 309 ? 0.39832 0.46585 0.64705 -0.03153 -0.02398 0.01959  309 CYS A C   
2150 O O   . CYS A 309 ? 0.50958 0.58175 0.76783 -0.03258 -0.01391 0.02440  309 CYS A O   
2151 C CB  . CYS A 309 ? 0.29147 0.34526 0.55094 -0.04071 -0.04373 0.01606  309 CYS A CB  
2152 S SG  . CYS A 309 ? 0.40769 0.44443 0.65666 -0.04495 -0.05982 0.01077  309 CYS A SG  
2153 N N   . SER A 310 ? 0.45890 0.53120 0.70077 -0.02640 -0.02411 0.01744  310 SER A N   
2154 C CA  . SER A 310 ? 0.48014 0.56356 0.72535 -0.02157 -0.01311 0.01988  310 SER A CA  
2155 C C   . SER A 310 ? 0.39611 0.48838 0.66289 -0.02293 -0.01101 0.02266  310 SER A C   
2156 O O   . SER A 310 ? 0.44258 0.54217 0.71613 -0.02150 0.00035  0.02685  310 SER A O   
2157 C CB  . SER A 310 ? 0.57934 0.66395 0.81213 -0.01626 -0.01561 0.01621  310 SER A CB  
2158 O OG  . SER A 310 ? 0.67872 0.77304 0.91411 -0.01142 -0.00639 0.01767  310 SER A OG  
2159 N N   . PHE A 311 ? 0.32161 0.41315 0.59856 -0.02536 -0.02191 0.02046  311 PHE A N   
2160 C CA  . PHE A 311 ? 0.30829 0.40846 0.60845 -0.02757 -0.02120 0.02316  311 PHE A CA  
2161 C C   . PHE A 311 ? 0.35177 0.44604 0.66207 -0.03337 -0.03378 0.02150  311 PHE A C   
2162 O O   . PHE A 311 ? 0.25732 0.34153 0.55550 -0.03401 -0.04518 0.01714  311 PHE A O   
2163 C CB  . PHE A 311 ? 0.36287 0.47293 0.66912 -0.02267 -0.02014 0.02240  311 PHE A CB  
2164 C CG  . PHE A 311 ? 0.37014 0.47505 0.66588 -0.02026 -0.03124 0.01745  311 PHE A CG  
2165 C CD1 . PHE A 311 ? 0.37826 0.47917 0.65363 -0.01575 -0.02984 0.01496  311 PHE A CD1 
2166 C CD2 . PHE A 311 ? 0.28331 0.38727 0.58945 -0.02230 -0.04296 0.01554  311 PHE A CD2 
2167 C CE1 . PHE A 311 ? 0.38101 0.47640 0.64636 -0.01354 -0.03937 0.01109  311 PHE A CE1 
2168 C CE2 . PHE A 311 ? 0.38513 0.48331 0.68012 -0.01963 -0.05265 0.01158  311 PHE A CE2 
2169 C CZ  . PHE A 311 ? 0.42327 0.51692 0.69781 -0.01532 -0.05055 0.00957  311 PHE A CZ  
2170 N N   . LEU A 312 ? 0.36174 0.46194 0.69352 -0.03742 -0.03149 0.02506  312 LEU A N   
2171 C CA  . LEU A 312 ? 0.37742 0.47310 0.72152 -0.04330 -0.04303 0.02371  312 LEU A CA  
2172 C C   . LEU A 312 ? 0.40347 0.50991 0.76934 -0.04336 -0.04712 0.02412  312 LEU A C   
2173 O O   . LEU A 312 ? 0.47103 0.57456 0.83603 -0.04283 -0.05936 0.02014  312 LEU A O   
2174 C CB  . LEU A 312 ? 0.32854 0.42128 0.68145 -0.04912 -0.03827 0.02748  312 LEU A CB  
2175 C CG  . LEU A 312 ? 0.32541 0.40769 0.65968 -0.04966 -0.03337 0.02792  312 LEU A CG  
2176 C CD1 . LEU A 312 ? 0.35786 0.43961 0.70417 -0.05473 -0.02585 0.03311  312 LEU A CD1 
2177 C CD2 . LEU A 312 ? 0.33312 0.40074 0.64973 -0.05106 -0.04651 0.02210  312 LEU A CD2 
# 
