data_8QG7
# 
_entry.id   8QG7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8QG7         pdb_00008qg7 10.2210/pdb8qg7/pdb 
WWPDB D_1292133109 ?            ?                   
# 
_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       2025-03-19 
_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                        8QG7 
_pdbx_database_status.recvd_initial_deposition_date   2023-09-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        . 
_pdbx_database_related.db_id          8A9V 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              gilles.labesse@cbs.cnrs.fr 
_pdbx_contact_author.name_first         Gilles 
_pdbx_contact_author.name_last          Labesse 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6861-3300 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gelin, M.'   1 ? 
'Labesse, G.' 2 ? 
'Lionne, C.'  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 NAD kinase 1 from Listeria monocytogenes in complex with a di-adenosine derivative' 
_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 'Gelin, M.'      1 ? 
primary 'Labesse, G.'    2 ? 
primary 'Clement, D.'    3 ? 
primary 'Pochet, S.'     4 ? 
primary 'Lionne, C.'     5 ? 
primary 'Leseigneur, C.' 6 ? 
primary 'Huteau, V.'     7 ? 
# 
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 'NAD kinase 1' 31045.279 1  2.7.1.23 ? ? ? 
2 non-polymer syn 'CITRIC ACID' 192.124   1  ?        ? ? ? 
3 non-polymer syn 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-pent-4-ynyl-amino]methyl]oxolane-3,4-diol
;
635.631   1  ?        ? ? ? 
4 water       nat water 18.015    46 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ATP-dependent NAD kinase' 
# 
_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       
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIEDLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CITRIC ACID' CIT 
3 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-pent-4-ynyl-amino]methyl]oxolane-3,4-diol
;
UXO 
4 water 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   TYR n 
1 4   MET n 
1 5   ILE n 
1 6   THR n 
1 7   SER n 
1 8   LYS n 
1 9   GLY n 
1 10  ASP n 
1 11  GLU n 
1 12  LYS n 
1 13  SER n 
1 14  ASP n 
1 15  LEU n 
1 16  LEU n 
1 17  ARG n 
1 18  LEU n 
1 19  ASN n 
1 20  MET n 
1 21  ILE n 
1 22  ALA n 
1 23  GLY n 
1 24  PHE n 
1 25  GLY n 
1 26  GLU n 
1 27  TYR n 
1 28  ASP n 
1 29  MET n 
1 30  GLU n 
1 31  TYR n 
1 32  ASP n 
1 33  ASP n 
1 34  VAL n 
1 35  GLU n 
1 36  PRO n 
1 37  GLU n 
1 38  ILE n 
1 39  VAL n 
1 40  ILE n 
1 41  SER n 
1 42  ILE n 
1 43  GLY n 
1 44  GLY n 
1 45  ASP n 
1 46  GLY n 
1 47  THR n 
1 48  PHE n 
1 49  LEU n 
1 50  SER n 
1 51  ALA n 
1 52  PHE n 
1 53  HIS n 
1 54  GLN n 
1 55  TYR n 
1 56  GLU n 
1 57  GLU n 
1 58  ARG n 
1 59  LEU n 
1 60  ASP n 
1 61  GLU n 
1 62  ILE n 
1 63  ALA n 
1 64  PHE n 
1 65  ILE n 
1 66  GLY n 
1 67  ILE n 
1 68  HIS n 
1 69  THR n 
1 70  GLY n 
1 71  HIS n 
1 72  LEU n 
1 73  GLY n 
1 74  PHE n 
1 75  TYR n 
1 76  ALA n 
1 77  ASP n 
1 78  TRP n 
1 79  ARG n 
1 80  PRO n 
1 81  ALA n 
1 82  GLU n 
1 83  ALA n 
1 84  ASP n 
1 85  LYS n 
1 86  LEU n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  LEU n 
1 91  ALA n 
1 92  LYS n 
1 93  GLY n 
1 94  GLU n 
1 95  TYR n 
1 96  GLN n 
1 97  LYS n 
1 98  VAL n 
1 99  SER n 
1 100 TYR n 
1 101 PRO n 
1 102 LEU n 
1 103 LEU n 
1 104 LYS n 
1 105 THR n 
1 106 THR n 
1 107 VAL n 
1 108 LYS n 
1 109 TYR n 
1 110 GLY n 
1 111 ILE n 
1 112 GLY n 
1 113 LYS n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 THR n 
1 118 TYR n 
1 119 LEU n 
1 120 ALA n 
1 121 LEU n 
1 122 ASN n 
1 123 GLU n 
1 124 SER n 
1 125 THR n 
1 126 VAL n 
1 127 LYS n 
1 128 SER n 
1 129 SER n 
1 130 GLY n 
1 131 GLY n 
1 132 PRO n 
1 133 PHE n 
1 134 VAL n 
1 135 VAL n 
1 136 ASP n 
1 137 VAL n 
1 138 VAL n 
1 139 ILE n 
1 140 ASN n 
1 141 ASP n 
1 142 ILE n 
1 143 HIS n 
1 144 PHE n 
1 145 GLU n 
1 146 ARG n 
1 147 PHE n 
1 148 ARG n 
1 149 GLY n 
1 150 ASP n 
1 151 GLY n 
1 152 LEU n 
1 153 CYS n 
1 154 MET n 
1 155 SER n 
1 156 THR n 
1 157 PRO n 
1 158 SER n 
1 159 GLY n 
1 160 THR n 
1 161 THR n 
1 162 ALA n 
1 163 TYR n 
1 164 ASN n 
1 165 LYS n 
1 166 SER n 
1 167 LEU n 
1 168 GLY n 
1 169 GLY n 
1 170 ALA n 
1 171 LEU n 
1 172 MET n 
1 173 HIS n 
1 174 PRO n 
1 175 SER n 
1 176 ILE n 
1 177 GLU n 
1 178 ALA n 
1 179 MET n 
1 180 GLN n 
1 181 LEU n 
1 182 THR n 
1 183 GLU n 
1 184 MET n 
1 185 ALA n 
1 186 SER n 
1 187 ILE n 
1 188 ASN n 
1 189 ASN n 
1 190 ARG n 
1 191 VAL n 
1 192 TYR n 
1 193 ARG n 
1 194 THR n 
1 195 ILE n 
1 196 GLY n 
1 197 SER n 
1 198 PRO n 
1 199 LEU n 
1 200 VAL n 
1 201 PHE n 
1 202 PRO n 
1 203 LYS n 
1 204 HIS n 
1 205 HIS n 
1 206 VAL n 
1 207 VAL n 
1 208 SER n 
1 209 LEU n 
1 210 GLN n 
1 211 PRO n 
1 212 VAL n 
1 213 ASN n 
1 214 ASP n 
1 215 LYS n 
1 216 ASP n 
1 217 PHE n 
1 218 GLN n 
1 219 ILE n 
1 220 SER n 
1 221 VAL n 
1 222 ASP n 
1 223 HIS n 
1 224 LEU n 
1 225 SER n 
1 226 ILE n 
1 227 LEU n 
1 228 HIS n 
1 229 ARG n 
1 230 ASP n 
1 231 VAL n 
1 232 GLN n 
1 233 GLU n 
1 234 ILE n 
1 235 ARG n 
1 236 TYR n 
1 237 GLU n 
1 238 VAL n 
1 239 SER n 
1 240 ALA n 
1 241 LYS n 
1 242 LYS n 
1 243 ILE n 
1 244 HIS n 
1 245 PHE n 
1 246 ALA n 
1 247 ARG n 
1 248 PHE n 
1 249 ARG n 
1 250 SER n 
1 251 PHE n 
1 252 PRO n 
1 253 PHE n 
1 254 TRP n 
1 255 ARG n 
1 256 ARG n 
1 257 VAL n 
1 258 HIS n 
1 259 ASP n 
1 260 SER n 
1 261 PHE n 
1 262 ILE n 
1 263 GLU n 
1 264 ASP n 
1 265 LEU n 
1 266 GLU n 
1 267 HIS n 
1 268 HIS n 
1 269 HIS n 
1 270 HIS n 
1 271 HIS n 
1 272 HIS 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                   272 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'nadK1, lmo0968' 
_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      'Listeria monocytogenes EGD-e' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     169963 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_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 
CIT non-polymer         . 'CITRIC ACID' ? 'C6 H8 O7'       192.124 
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 
UXO non-polymer         . 
;(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[[3-[6-azanyl-9-[(2~{R},3~{R},4~{S},5~{R})-5-(hydroxymethyl)-3,4-bis(oxidanyl)oxolan-2-yl]purin-8-yl]prop-2-ynyl-pent-4-ynyl-amino]methyl]oxolane-3,4-diol
;
? 'C28 H33 N11 O7' 635.631 
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   1   MET MET A . n 
A 1 2   LYS 2   2   2   LYS LYS A . n 
A 1 3   TYR 3   3   3   TYR TYR A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   LYS 8   8   8   LYS LYS A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLU 11  11  11  GLU GLU A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ARG 17  17  17  ARG ARG A . n 
A 1 18  LEU 18  18  18  LEU LEU A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  MET 20  20  20  MET MET A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  ALA 22  22  22  ALA ALA A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  TYR 27  27  27  TYR TYR A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  MET 29  29  29  MET MET A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  TYR 31  31  31  TYR TYR A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  PRO 36  36  36  PRO PRO A . n 
A 1 37  GLU 37  37  37  GLU GLU A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  SER 41  41  41  SER SER 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  GLY 44  44  44  GLY GLY A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  THR 47  47  47  THR THR A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  HIS 53  53  53  HIS HIS A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  GLU 61  61  61  GLU GLU A . n 
A 1 62  ILE 62  62  62  ILE ILE A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  THR 69  69  69  THR THR A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PHE 74  74  74  PHE PHE A . n 
A 1 75  TYR 75  75  75  TYR TYR A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  TRP 78  78  78  TRP TRP A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  PRO 80  80  80  PRO PRO A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  GLU 82  82  82  GLU GLU A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ASP 84  84  84  ASP ASP A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  TYR 95  95  95  TYR TYR A . n 
A 1 96  GLN 96  96  96  GLN GLN A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 THR 106 106 106 THR THR 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 TYR 109 109 109 TYR TYR A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 ILE 111 111 ?   ?   ?   A . n 
A 1 112 GLY 112 112 ?   ?   ?   A . n 
A 1 113 LYS 113 113 ?   ?   ?   A . n 
A 1 114 LYS 114 114 114 LYS LYS A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 THR 117 117 117 THR THR A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 HIS 143 143 143 HIS HIS A . n 
A 1 144 PHE 144 144 144 PHE PHE A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 ARG 146 146 146 ARG ARG A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 ASP 150 150 150 ASP ASP A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 MET 154 154 154 MET MET A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PRO 157 157 157 PRO PRO A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 THR 160 160 160 THR THR A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 TYR 163 163 163 TYR TYR A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 LYS 165 165 165 LYS LYS A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 GLY 168 168 168 GLY GLY A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 MET 172 172 172 MET MET A . n 
A 1 173 HIS 173 173 173 HIS HIS A . n 
A 1 174 PRO 174 174 174 PRO PRO A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ILE 176 176 176 ILE ILE A . n 
A 1 177 GLU 177 177 177 GLU GLU A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLN 180 180 180 GLN GLN A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 THR 182 182 182 THR THR A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 MET 184 184 184 MET MET A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 SER 186 186 186 SER SER A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ASN 188 188 188 ASN ASN A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 TYR 192 192 192 TYR TYR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 PRO 198 198 198 PRO PRO A . n 
A 1 199 LEU 199 199 199 LEU LEU A . n 
A 1 200 VAL 200 200 200 VAL VAL A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 PRO 202 202 202 PRO PRO A . n 
A 1 203 LYS 203 203 203 LYS LYS A . n 
A 1 204 HIS 204 204 204 HIS HIS A . n 
A 1 205 HIS 205 205 205 HIS HIS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 VAL 207 207 207 VAL VAL A . n 
A 1 208 SER 208 208 208 SER SER A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 GLN 210 210 210 GLN GLN A . n 
A 1 211 PRO 211 211 211 PRO PRO 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 ASP 214 214 214 ASP ASP A . n 
A 1 215 LYS 215 215 215 LYS LYS A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 PHE 217 217 217 PHE PHE A . n 
A 1 218 GLN 218 218 218 GLN GLN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 SER 220 220 220 SER SER A . n 
A 1 221 VAL 221 221 221 VAL VAL A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 HIS 223 223 223 HIS HIS A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 ILE 226 226 226 ILE ILE A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 HIS 228 228 228 HIS HIS A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 VAL 231 231 231 VAL VAL A . n 
A 1 232 GLN 232 232 232 GLN GLN A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 TYR 236 236 236 TYR TYR A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 VAL 238 238 238 VAL VAL A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 ALA 240 240 240 ALA ALA A . n 
A 1 241 LYS 241 241 241 LYS LYS A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 HIS 244 244 244 HIS HIS A . n 
A 1 245 PHE 245 245 245 PHE PHE A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 PHE 248 248 248 PHE PHE A . n 
A 1 249 ARG 249 249 249 ARG ARG A . n 
A 1 250 SER 250 250 250 SER SER A . n 
A 1 251 PHE 251 251 251 PHE PHE A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 TRP 254 254 254 TRP TRP A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ARG 256 256 256 ARG ARG A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 HIS 258 258 258 HIS HIS A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 ILE 262 262 262 ILE ILE A . n 
A 1 263 GLU 263 263 263 GLU GLU A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 LEU 265 265 ?   ?   ?   A . n 
A 1 266 GLU 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
A 1 268 HIS 268 268 ?   ?   ?   A . n 
A 1 269 HIS 269 269 ?   ?   ?   A . n 
A 1 270 HIS 270 270 ?   ?   ?   A . n 
A 1 271 HIS 271 271 ?   ?   ?   A . n 
A 1 272 HIS 272 272 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        UXO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UXO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 CIT 1  301 1  CIT CIT A . 
C 3 UXO 1  302 1  UXO XXX A . 
D 4 HOH 1  401 4  HOH HOH A . 
D 4 HOH 2  402 49 HOH HOH A . 
D 4 HOH 3  403 3  HOH HOH A . 
D 4 HOH 4  404 25 HOH HOH A . 
D 4 HOH 5  405 54 HOH HOH A . 
D 4 HOH 6  406 5  HOH HOH A . 
D 4 HOH 7  407 2  HOH HOH A . 
D 4 HOH 8  408 1  HOH HOH A . 
D 4 HOH 9  409 38 HOH HOH A . 
D 4 HOH 10 410 43 HOH HOH A . 
D 4 HOH 11 411 45 HOH HOH A . 
D 4 HOH 12 412 6  HOH HOH A . 
D 4 HOH 13 413 26 HOH HOH A . 
D 4 HOH 14 414 9  HOH HOH A . 
D 4 HOH 15 415 31 HOH HOH A . 
D 4 HOH 16 416 37 HOH HOH A . 
D 4 HOH 17 417 7  HOH HOH A . 
D 4 HOH 18 418 8  HOH HOH A . 
D 4 HOH 19 419 44 HOH HOH A . 
D 4 HOH 20 420 47 HOH HOH A . 
D 4 HOH 21 421 16 HOH HOH A . 
D 4 HOH 22 422 29 HOH HOH A . 
D 4 HOH 23 423 46 HOH HOH A . 
D 4 HOH 24 424 39 HOH HOH A . 
D 4 HOH 25 425 40 HOH HOH A . 
D 4 HOH 26 426 13 HOH HOH A . 
D 4 HOH 27 427 32 HOH HOH A . 
D 4 HOH 28 428 21 HOH HOH A . 
D 4 HOH 29 429 41 HOH HOH A . 
D 4 HOH 30 430 30 HOH HOH A . 
D 4 HOH 31 431 12 HOH HOH A . 
D 4 HOH 32 432 17 HOH HOH A . 
D 4 HOH 33 433 11 HOH HOH A . 
D 4 HOH 34 434 33 HOH HOH A . 
D 4 HOH 35 435 20 HOH HOH A . 
D 4 HOH 36 436 48 HOH HOH A . 
D 4 HOH 37 437 27 HOH HOH A . 
D 4 HOH 38 438 18 HOH HOH A . 
D 4 HOH 39 439 34 HOH HOH A . 
D 4 HOH 40 440 51 HOH HOH A . 
D 4 HOH 41 441 35 HOH HOH A . 
D 4 HOH 42 442 14 HOH HOH A . 
D 4 HOH 43 443 53 HOH HOH A . 
D 4 HOH 44 444 50 HOH HOH A . 
D 4 HOH 45 445 55 HOH HOH A . 
D 4 HOH 46 446 42 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 LYS 85  ? CG  ? A LYS 85  CG  
2  1 Y 1 A LYS 85  ? CD  ? A LYS 85  CD  
3  1 Y 1 A LYS 85  ? CE  ? A LYS 85  CE  
4  1 Y 1 A LYS 85  ? NZ  ? A LYS 85  NZ  
5  1 Y 1 A LYS 88  ? CG  ? A LYS 88  CG  
6  1 Y 1 A LYS 88  ? CD  ? A LYS 88  CD  
7  1 Y 1 A LYS 88  ? CE  ? A LYS 88  CE  
8  1 Y 1 A LYS 88  ? NZ  ? A LYS 88  NZ  
9  1 Y 1 A LEU 89  ? CG  ? A LEU 89  CG  
10 1 Y 1 A LEU 89  ? CD1 ? A LEU 89  CD1 
11 1 Y 1 A LEU 89  ? CD2 ? A LEU 89  CD2 
12 1 Y 1 A GLU 94  ? CG  ? A GLU 94  CG  
13 1 Y 1 A GLU 94  ? CD  ? A GLU 94  CD  
14 1 Y 1 A GLU 94  ? OE1 ? A GLU 94  OE1 
15 1 Y 1 A GLU 94  ? OE2 ? A GLU 94  OE2 
16 1 Y 1 A LYS 108 ? CG  ? A LYS 108 CG  
17 1 Y 1 A LYS 108 ? CD  ? A LYS 108 CD  
18 1 Y 1 A LYS 108 ? CE  ? A LYS 108 CE  
19 1 Y 1 A LYS 108 ? NZ  ? A LYS 108 NZ  
20 1 Y 1 A ARG 190 ? CG  ? A ARG 190 CG  
21 1 Y 1 A ARG 190 ? CD  ? A ARG 190 CD  
22 1 Y 1 A ARG 190 ? NE  ? A ARG 190 NE  
23 1 Y 1 A ARG 190 ? CZ  ? A ARG 190 CZ  
24 1 Y 1 A ARG 190 ? NH1 ? A ARG 190 NH1 
25 1 Y 1 A ARG 190 ? NH2 ? A ARG 190 NH2 
26 1 Y 1 A HIS 228 ? CG  ? A HIS 228 CG  
27 1 Y 1 A HIS 228 ? ND1 ? A HIS 228 ND1 
28 1 Y 1 A HIS 228 ? CD2 ? A HIS 228 CD2 
29 1 Y 1 A HIS 228 ? CE1 ? A HIS 228 CE1 
30 1 Y 1 A HIS 228 ? NE2 ? A HIS 228 NE2 
31 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
32 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
33 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
34 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
# 
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 ? ? ? 1.19.1_4122 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QG7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.376 
_cell.length_a_esd                 ? 
_cell.length_b                     75.308 
_cell.length_b_esd                 ? 
_cell.length_c                     118.605 
_cell.length_c_esd                 ? 
_cell.volume                       566068.434 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         8QG7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_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                   8QG7 
_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             2.28 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.03 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '30 mM NaBr, 220 mM Kcitrate, glycerol 6%, 15-16% w/v PEG400' 
_exptl_crystal_grow.pdbx_pH_range   4.8-5.1 
_exptl_crystal_grow.temp            291.15 
# 
_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 PILATUS 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         2019-09-27 
_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   0.979257 
_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                        'ALBA BEAMLINE XALOC' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979257 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   XALOC 
_diffrn_source.pdbx_synchrotron_site       ALBA 
# 
_reflns.B_iso_Wilson_estimate                          47.24 
_reflns.entry_id                                       8QG7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.3 
_reflns.d_resolution_low                               48.49 
_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                                     12912 
_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                           99.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          23.48 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.039 
_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                                   1.0 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.034 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_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 
_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 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
2.30 2.44  ? ? ? ? ? ? 2063 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.326 ? ? 1 1 0.961              ? ? ? ? 0.285                ? ? ? ? ? 
? ? ? ? 
2.44 2.6   ? ? ? ? ? ? 1921 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.193 ? ? 2 1 0.987              ? ? ? ? 0.17                 ? ? ? ? ? 
? ? ? ? 
2.60 2.81  ? ? ? ? ? ? 1813 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.128 ? ? 3 1 0.9940000000000001 ? ? ? ? 0.113                ? ? ? ? ? 
? ? ? ? 
2.81 3.08  ? ? ? ? ? ? 1674 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.087 ? ? 4 1 0.997              ? ? ? ? 0.076                ? ? ? ? ? 
? ? ? ? 
3.08 3.44  ? ? ? ? ? ? 1502 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.049 ? ? 5 1 0.9990000000000001 ? ? ? ? 0.044000000000000004 ? ? ? ? ? 
? ? ? ? 
3.44 3.97  ? ? ? ? ? ? 1323 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.034 ? ? 6 1 0.9990000000000001 ? ? ? ? 0.03                 ? ? ? ? ? 
? ? ? ? 
3.97 4.85  ? ? ? ? ? ? 1167 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.023 ? ? 7 1 1.0                ? ? ? ? 0.02                 ? ? ? ? ? 
? ? ? ? 
4.85 6.83  ? ? ? ? ? ? 905  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.021 ? ? 8 1 1.0                ? ? ? ? 0.018000000000000002 ? ? ? ? ? 
? ? ? ? 
6.83 48.49 ? ? ? ? ? ? 544  ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 0.015 ? ? 9 1 1.0                ? ? ? ? 0.013000000000000001 ? ? ? ? ? 
? ? ? ? 
# 
_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                               62.85 
_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                                 8QG7 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.30 
_refine.ls_d_res_low                             48.49 
_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                     12873 
_refine.ls_number_reflns_R_free                  645 
_refine.ls_number_reflns_R_work                  12228 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.75 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2102 
_refine.ls_R_factor_R_free                       0.2483 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2083 
_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                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.8971 
_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                            0.2839 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.30 
_refine_hist.d_res_low                        48.49 
_refine_hist.number_atoms_solvent             46 
_refine_hist.number_atoms_total               2161 
_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        2056 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         59 
_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' ? 0.0022  ? 2206 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.5201  ? 2994 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0446  ? 323  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0048  ? 412  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.0616 ? 821  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.30 2.47  . . 127 2401 98.67 . . . . 0.2486 . . . . . . . . . . . 0.2896 
'X-RAY DIFFRACTION' 2.47 2.72  . . 126 2402 98.71 . . . . 0.2247 . . . . . . . . . . . 0.3192 
'X-RAY DIFFRACTION' 2.72 3.12  . . 129 2433 99.11 . . . . 0.2430 . . . . . . . . . . . 0.3772 
'X-RAY DIFFRACTION' 3.12 3.93  . . 128 2429 98.23 . . . . 0.2038 . . . . . . . . . . . 0.2282 
'X-RAY DIFFRACTION' 3.93 48.49 . . 135 2563 99.01 . . . . 0.1930 . . . . . . . . . . . 0.2134 
# 
_struct.entry_id                     8QG7 
_struct.title                        
'Crystal structure of NAD kinase 1 from Listeria monocytogenes in complex with a di-adenosine derivative' 
_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        8QG7 
_struct_keywords.text            'tetrameric NAD-kinase, Transferase' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NADK1_LISMO 
_struct_ref.pdbx_db_accession          Q8Y8D7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MKYMITSKGDEKSDLLRLNMIAGFGEYDMEYDDVEPEIVISIGGDGTFLSAFHQYEERLDEIAFIGIHTGHLGFYADWRP
AEADKLVKLLAKGEYQKVSYPLLKTTVKYGIGKKEATYLALNESTVKSSGGPFVVDVVINDIHFERFRGDGLCMSTPSGT
TAYNKSLGGALMHPSIEAMQLTEMASINNRVYRTIGSPLVFPKHHVVSLQPVNDKDFQISVDHLSILHRDVQEIRYEVSA
KKIHFARFRSFPFWRRVHDSFIED
;
_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              8QG7 
_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                 264 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8Y8D7 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  264 
_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       264 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8QG7 LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QG7 GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QG7 HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QG7 HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QG7 HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QG7 HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QG7 HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QG7 HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D 
1 2 A,B,C,D 
1 3 A,B,C,D 
1 4 A,B,C,D 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   SAXS 
_pdbx_struct_assembly_auth_evidence.details                Tetramer 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 2_655 -x+1,-y,z -1.0000000000 0.0000000000 0.0000000000 63.3760000000 0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 3_655 -x+1,y,-z -1.0000000000 0.0000000000 0.0000000000 63.3760000000 0.0000000000 1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_555 x,-y,-z   1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 -1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
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 ASP A 10  ? GLY A 25  ? ASP A 10  GLY A 25  1 ? 16 
HELX_P HELX_P2 AA2 GLY A 44  ? TYR A 55  ? GLY A 44  TYR A 55  1 ? 12 
HELX_P HELX_P3 AA3 ARG A 58  ? ILE A 62  ? ARG A 58  ILE A 62  5 ? 5  
HELX_P HELX_P4 AA4 ARG A 79  ? ALA A 81  ? ARG A 79  ALA A 81  5 ? 3  
HELX_P HELX_P5 AA5 GLU A 82  ? GLY A 93  ? GLU A 82  GLY A 93  1 ? 12 
HELX_P HELX_P6 AA6 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P7 AA7 PRO A 252 ? ILE A 262 ? PRO A 252 ILE A 262 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? 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 GLU A 30  ? TYR A 31  ? GLU A 30  TYR A 31  
AA1 2 LYS A 2   ? SER A 7   ? LYS A 2   SER A 7   
AA1 3 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 4 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 GLU A 115 ? ALA A 120 ? GLU A 115 ALA A 120 
AA2 2 GLN A 96  ? LYS A 108 ? GLN A 96  LYS A 108 
AA2 3 GLU A 233 ? ARG A 247 ? GLU A 233 ARG A 247 
AA2 4 VAL A 207 ? PRO A 211 ? VAL A 207 PRO A 211 
AA2 5 PHE A 133 ? ILE A 139 ? PHE A 133 ILE A 139 
AA2 6 ILE A 142 ? GLY A 149 ? ILE A 142 GLY A 149 
AA3 1 LEU A 199 ? PHE A 201 ? LEU A 199 PHE A 201 
AA3 2 MET A 179 ? MET A 184 ? MET A 179 MET A 184 
AA3 3 GLY A 151 ? SER A 155 ? GLY A 151 SER A 155 
AA3 4 GLU A 123 ? SER A 128 ? GLU A 123 SER A 128 
AA3 5 PHE A 217 ? VAL A 221 ? PHE A 217 VAL A 221 
AA3 6 LEU A 224 ? HIS A 228 ? LEU A 224 HIS A 228 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O GLU A 30  ? O GLU A 30  N TYR A 3   ? N TYR A 3   
AA1 2 3 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 3 4 N SER A 41  ? N SER A 41  O ILE A 67  ? O ILE A 67  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N GLN A 96  ? N GLN A 96  O ARG A 247 ? O ARG A 247 
AA2 3 4 O TYR A 236 ? O TYR A 236 N VAL A 207 ? N VAL A 207 
AA2 4 5 O SER A 208 ? O SER A 208 N VAL A 138 ? N VAL A 138 
AA2 5 6 N VAL A 137 ? N VAL A 137 O GLU A 145 ? O GLU A 145 
AA3 1 2 O PHE A 201 ? O PHE A 201 N MET A 179 ? N MET A 179 
AA3 2 3 O GLN A 180 ? O GLN A 180 N SER A 155 ? N SER A 155 
AA3 3 4 O MET A 154 ? O MET A 154 N SER A 124 ? N SER A 124 
AA3 4 5 N LYS A 127 ? N LYS A 127 O GLN A 218 ? O GLN A 218 
AA3 5 6 N ILE A 219 ? N ILE A 219 O ILE A 226 ? O ILE A 226 
# 
_pdbx_entry_details.entry_id                   8QG7 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 GLU A 94  ? ? 56.84   9.92    
2  1 ASN A 122 ? ? -96.65  -70.55  
3  1 SER A 129 ? ? -49.84  -73.63  
4  1 ALA A 162 ? ? -102.62 -120.57 
5  1 ALA A 185 ? ? 49.95   74.09   
6  1 ASN A 189 ? ? -145.11 -150.93 
7  1 HIS A 204 ? ? 68.83   -7.72   
8  1 ASN A 213 ? ? -124.92 -73.64  
9  1 ASP A 222 ? ? 57.94   -117.78 
10 1 ILE A 262 ? ? -79.67  -72.19  
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,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 13.8202033758 24.5445651662 22.3038991471  0.645775860836 ? 0.129927777689  ? 0.0432400211785  ? 
0.575998262266 ? -0.130690532372   ? 0.522067253969 ? 2.92734260856 ? -1.47409012001  ? -2.12761025706  ? 2.02364258898 ? 
1.90676711622    ? 6.49187052627 ? -0.101443272344 ? -0.508482661963  ? 0.382307575946  ? 0.317735931246   ? 0.099203588103  ? 
0.0109137098587 ? -0.471812643143  ? -0.286303045961 ? -0.0469678037746 ? 
2 'X-RAY DIFFRACTION' ? refined 16.1423900433 11.8024134049 -5.43592297755 0.270644294518 ? 0.0332325919803 ? -0.0185671720536 ? 
0.387027650089 ? -0.00109464239181 ? 0.364657212582 ? 1.59096802086 ? -0.84458661452  ? -0.396464302274 ? 1.98414820441 ? 
1.67351768656    ? 5.30539839914 ? 0.132836919171  ? 0.214497421094   ? -0.016118581764 ? -0.104354376851  ? -0.172627998202 ? 
0.29203911601   ? -0.0516341872704 ? -0.679049526246 ? 0.175276502544   ? 
3 'X-RAY DIFFRACTION' ? refined 21.0458937243 14.426852219  0.621523946732 0.265639048014 ? 0.0275301248462 ? 0.0610087630307  ? 
0.315004925612 ? 0.00810749503031  ? 0.403519624266 ? 2.31429197839 ? -0.608610197863 ? 0.811924965261  ? 3.03411366348 ? 
-0.0403691460299 ? 4.93990242678 ? 0.0206382936216 ? -0.0277486827942 ? 0.0975387747257 ? 0.00948240665724 ? -0.106511861943 ? 
0.36525665892   ? -0.106452859465  ? -0.319401448948 ? 0.151027858889   ? 
# 
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 A 1   A 1   ? A 102 A 102 ? ? 
;chain 'A' and (resid    1  through  102 )
;
2 'X-RAY DIFFRACTION' 2 A 103 A 103 ? A 163 A 166 ? ? 
;chain 'A' and (resid  103  through  166 )
;
3 'X-RAY DIFFRACTION' 3 A 164 A 167 ? A 261 A 264 ? ? 
;chain 'A' and (resid  167  through  264 )
;
# 
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 ILE 111 ? A ILE 111 
2  1 Y 1 A GLY 112 ? A GLY 112 
3  1 Y 1 A LYS 113 ? A LYS 113 
4  1 Y 1 A LEU 265 ? A LEU 265 
5  1 Y 1 A GLU 266 ? A GLU 266 
6  1 Y 1 A HIS 267 ? A HIS 267 
7  1 Y 1 A HIS 268 ? A HIS 268 
8  1 Y 1 A HIS 269 ? A HIS 269 
9  1 Y 1 A HIS 270 ? A HIS 270 
10 1 Y 1 A HIS 271 ? A HIS 271 
11 1 Y 1 A HIS 272 ? A HIS 272 
# 
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  
CIT C1   C N N 74  
CIT O1   O N N 75  
CIT O2   O N N 76  
CIT C2   C N N 77  
CIT C3   C N N 78  
CIT O7   O N N 79  
CIT C4   C N N 80  
CIT C5   C N N 81  
CIT O3   O N N 82  
CIT O4   O N N 83  
CIT C6   C N N 84  
CIT O5   O N N 85  
CIT O6   O N N 86  
CIT HO2  H N N 87  
CIT H21  H N N 88  
CIT H22  H N N 89  
CIT HO7  H N N 90  
CIT H41  H N N 91  
CIT H42  H N N 92  
CIT HO4  H N N 93  
CIT HO6  H N N 94  
CYS N    N N N 95  
CYS CA   C N R 96  
CYS C    C N N 97  
CYS O    O N N 98  
CYS CB   C N N 99  
CYS SG   S N N 100 
CYS OXT  O N N 101 
CYS H    H N N 102 
CYS H2   H N N 103 
CYS HA   H N N 104 
CYS HB2  H N N 105 
CYS HB3  H N N 106 
CYS HG   H N N 107 
CYS HXT  H N N 108 
GLN N    N N N 109 
GLN CA   C N S 110 
GLN C    C N N 111 
GLN O    O N N 112 
GLN CB   C N N 113 
GLN CG   C N N 114 
GLN CD   C N N 115 
GLN OE1  O N N 116 
GLN NE2  N N N 117 
GLN OXT  O N N 118 
GLN H    H N N 119 
GLN H2   H N N 120 
GLN HA   H N N 121 
GLN HB2  H N N 122 
GLN HB3  H N N 123 
GLN HG2  H N N 124 
GLN HG3  H N N 125 
GLN HE21 H N N 126 
GLN HE22 H N N 127 
GLN HXT  H N N 128 
GLU N    N N N 129 
GLU CA   C N S 130 
GLU C    C N N 131 
GLU O    O N N 132 
GLU CB   C N N 133 
GLU CG   C N N 134 
GLU CD   C N N 135 
GLU OE1  O N N 136 
GLU OE2  O N N 137 
GLU OXT  O N N 138 
GLU H    H N N 139 
GLU H2   H N N 140 
GLU HA   H N N 141 
GLU HB2  H N N 142 
GLU HB3  H N N 143 
GLU HG2  H N N 144 
GLU HG3  H N N 145 
GLU HE2  H N N 146 
GLU HXT  H N N 147 
GLY N    N N N 148 
GLY CA   C N N 149 
GLY C    C N N 150 
GLY O    O N N 151 
GLY OXT  O N N 152 
GLY H    H N N 153 
GLY H2   H N N 154 
GLY HA2  H N N 155 
GLY HA3  H N N 156 
GLY HXT  H N N 157 
HIS N    N N N 158 
HIS CA   C N S 159 
HIS C    C N N 160 
HIS O    O N N 161 
HIS CB   C N N 162 
HIS CG   C Y N 163 
HIS ND1  N Y N 164 
HIS CD2  C Y N 165 
HIS CE1  C Y N 166 
HIS NE2  N Y N 167 
HIS OXT  O N N 168 
HIS H    H N N 169 
HIS H2   H N N 170 
HIS HA   H N N 171 
HIS HB2  H N N 172 
HIS HB3  H N N 173 
HIS HD1  H N N 174 
HIS HD2  H N N 175 
HIS HE1  H N N 176 
HIS HE2  H N N 177 
HIS HXT  H N N 178 
HOH O    O N N 179 
HOH H1   H N N 180 
HOH H2   H N N 181 
ILE N    N N N 182 
ILE CA   C N S 183 
ILE C    C N N 184 
ILE O    O N N 185 
ILE CB   C N S 186 
ILE CG1  C N N 187 
ILE CG2  C N N 188 
ILE CD1  C N N 189 
ILE OXT  O N N 190 
ILE H    H N N 191 
ILE H2   H N N 192 
ILE HA   H N N 193 
ILE HB   H N N 194 
ILE HG12 H N N 195 
ILE HG13 H N N 196 
ILE HG21 H N N 197 
ILE HG22 H N N 198 
ILE HG23 H N N 199 
ILE HD11 H N N 200 
ILE HD12 H N N 201 
ILE HD13 H N N 202 
ILE HXT  H N N 203 
LEU N    N N N 204 
LEU CA   C N S 205 
LEU C    C N N 206 
LEU O    O N N 207 
LEU CB   C N N 208 
LEU CG   C N N 209 
LEU CD1  C N N 210 
LEU CD2  C N N 211 
LEU OXT  O N N 212 
LEU H    H N N 213 
LEU H2   H N N 214 
LEU HA   H N N 215 
LEU HB2  H N N 216 
LEU HB3  H N N 217 
LEU HG   H N N 218 
LEU HD11 H N N 219 
LEU HD12 H N N 220 
LEU HD13 H N N 221 
LEU HD21 H N N 222 
LEU HD22 H N N 223 
LEU HD23 H N N 224 
LEU HXT  H N N 225 
LYS N    N N N 226 
LYS CA   C N S 227 
LYS C    C N N 228 
LYS O    O N N 229 
LYS CB   C N N 230 
LYS CG   C N N 231 
LYS CD   C N N 232 
LYS CE   C N N 233 
LYS NZ   N N N 234 
LYS OXT  O N N 235 
LYS H    H N N 236 
LYS H2   H N N 237 
LYS HA   H N N 238 
LYS HB2  H N N 239 
LYS HB3  H N N 240 
LYS HG2  H N N 241 
LYS HG3  H N N 242 
LYS HD2  H N N 243 
LYS HD3  H N N 244 
LYS HE2  H N N 245 
LYS HE3  H N N 246 
LYS HZ1  H N N 247 
LYS HZ2  H N N 248 
LYS HZ3  H N N 249 
LYS HXT  H N N 250 
MET N    N N N 251 
MET CA   C N S 252 
MET C    C N N 253 
MET O    O N N 254 
MET CB   C N N 255 
MET CG   C N N 256 
MET SD   S N N 257 
MET CE   C N N 258 
MET OXT  O N N 259 
MET H    H N N 260 
MET H2   H N N 261 
MET HA   H N N 262 
MET HB2  H N N 263 
MET HB3  H N N 264 
MET HG2  H N N 265 
MET HG3  H N N 266 
MET HE1  H N N 267 
MET HE2  H N N 268 
MET HE3  H N N 269 
MET HXT  H N N 270 
PHE N    N N N 271 
PHE CA   C N S 272 
PHE C    C N N 273 
PHE O    O N N 274 
PHE CB   C N N 275 
PHE CG   C Y N 276 
PHE CD1  C Y N 277 
PHE CD2  C Y N 278 
PHE CE1  C Y N 279 
PHE CE2  C Y N 280 
PHE CZ   C Y N 281 
PHE OXT  O N N 282 
PHE H    H N N 283 
PHE H2   H N N 284 
PHE HA   H N N 285 
PHE HB2  H N N 286 
PHE HB3  H N N 287 
PHE HD1  H N N 288 
PHE HD2  H N N 289 
PHE HE1  H N N 290 
PHE HE2  H N N 291 
PHE HZ   H N N 292 
PHE HXT  H N N 293 
PRO N    N N N 294 
PRO CA   C N S 295 
PRO C    C N N 296 
PRO O    O N N 297 
PRO CB   C N N 298 
PRO CG   C N N 299 
PRO CD   C N N 300 
PRO OXT  O N N 301 
PRO H    H N N 302 
PRO HA   H N N 303 
PRO HB2  H N N 304 
PRO HB3  H N N 305 
PRO HG2  H N N 306 
PRO HG3  H N N 307 
PRO HD2  H N N 308 
PRO HD3  H N N 309 
PRO HXT  H N N 310 
SER N    N N N 311 
SER CA   C N S 312 
SER C    C N N 313 
SER O    O N N 314 
SER CB   C N N 315 
SER OG   O N N 316 
SER OXT  O N N 317 
SER H    H N N 318 
SER H2   H N N 319 
SER HA   H N N 320 
SER HB2  H N N 321 
SER HB3  H N N 322 
SER HG   H N N 323 
SER HXT  H N N 324 
THR N    N N N 325 
THR CA   C N S 326 
THR C    C N N 327 
THR O    O N N 328 
THR CB   C N R 329 
THR OG1  O N N 330 
THR CG2  C N N 331 
THR OXT  O N N 332 
THR H    H N N 333 
THR H2   H N N 334 
THR HA   H N N 335 
THR HB   H N N 336 
THR HG1  H N N 337 
THR HG21 H N N 338 
THR HG22 H N N 339 
THR HG23 H N N 340 
THR HXT  H N N 341 
TRP N    N N N 342 
TRP CA   C N S 343 
TRP C    C N N 344 
TRP O    O N N 345 
TRP CB   C N N 346 
TRP CG   C Y N 347 
TRP CD1  C Y N 348 
TRP CD2  C Y N 349 
TRP NE1  N Y N 350 
TRP CE2  C Y N 351 
TRP CE3  C Y N 352 
TRP CZ2  C Y N 353 
TRP CZ3  C Y N 354 
TRP CH2  C Y N 355 
TRP OXT  O N N 356 
TRP H    H N N 357 
TRP H2   H N N 358 
TRP HA   H N N 359 
TRP HB2  H N N 360 
TRP HB3  H N N 361 
TRP HD1  H N N 362 
TRP HE1  H N N 363 
TRP HE3  H N N 364 
TRP HZ2  H N N 365 
TRP HZ3  H N N 366 
TRP HH2  H N N 367 
TRP HXT  H N N 368 
TYR N    N N N 369 
TYR CA   C N S 370 
TYR C    C N N 371 
TYR O    O N N 372 
TYR CB   C N N 373 
TYR CG   C Y N 374 
TYR CD1  C Y N 375 
TYR CD2  C Y N 376 
TYR CE1  C Y N 377 
TYR CE2  C Y N 378 
TYR CZ   C Y N 379 
TYR OH   O N N 380 
TYR OXT  O N N 381 
TYR H    H N N 382 
TYR H2   H N N 383 
TYR HA   H N N 384 
TYR HB2  H N N 385 
TYR HB3  H N N 386 
TYR HD1  H N N 387 
TYR HD2  H N N 388 
TYR HE1  H N N 389 
TYR HE2  H N N 390 
TYR HH   H N N 391 
TYR HXT  H N N 392 
UXO N1   N Y N 393 
UXO C7   C N N 394 
UXO C8   C N N 395 
UXO N2   N Y N 396 
UXO C9   C N N 397 
UXO O1   O N N 398 
UXO C1   C Y N 399 
UXO O5   O N N 400 
UXO C5   C N R 401 
UXO C6   C N R 402 
UXO N3   N Y N 403 
UXO C4   C Y N 404 
UXO O4   O N N 405 
UXO C3   C Y N 406 
UXO O3   O N N 407 
UXO C2   C Y N 408 
UXO N4   N Y N 409 
UXO N    N N N 410 
UXO C    C Y N 411 
UXO O    O N N 412 
UXO C10  C N N 413 
UXO C11  C N N 414 
UXO C12  C N N 415 
UXO C13  C N N 416 
UXO C14  C N N 417 
UXO C15  C N N 418 
UXO C16  C Y N 419 
UXO C17  C Y N 420 
UXO C18  C Y N 421 
UXO C19  C Y N 422 
UXO C20  C Y N 423 
UXO C21  C N R 424 
UXO C22  C N R 425 
UXO C23  C N N 426 
UXO C24  C N S 427 
UXO C25  C N R 428 
UXO C26  C N S 429 
UXO C27  C N R 430 
UXO N10  N Y N 431 
UXO N5   N N N 432 
UXO N6   N Y N 433 
UXO N7   N Y N 434 
UXO N8   N Y N 435 
UXO N9   N N N 436 
UXO O2   O N N 437 
UXO O6   O N N 438 
UXO H8   H N N 439 
UXO H9   H N N 440 
UXO H10  H N N 441 
UXO H11  H N N 442 
UXO H12  H N N 443 
UXO H13  H N N 444 
UXO H6   H N N 445 
UXO H30  H N N 446 
UXO H    H N N 447 
UXO H1   H N N 448 
UXO H7   H N N 449 
UXO H28  H N N 450 
UXO H26  H N N 451 
UXO H5   H N N 452 
UXO H4   H N N 453 
UXO H15  H N N 454 
UXO H14  H N N 455 
UXO H16  H N N 456 
UXO H18  H N N 457 
UXO H17  H N N 458 
UXO H19  H N N 459 
UXO H2   H N N 460 
UXO H3   H N N 461 
UXO H23  H N N 462 
UXO H22  H N N 463 
UXO H25  H N N 464 
UXO H27  H N N 465 
UXO H29  H N N 466 
UXO H31  H N N 467 
UXO H21  H N N 468 
UXO H20  H N N 469 
UXO H24  H N N 470 
UXO H32  H N N 471 
VAL N    N N N 472 
VAL CA   C N S 473 
VAL C    C N N 474 
VAL O    O N N 475 
VAL CB   C N N 476 
VAL CG1  C N N 477 
VAL CG2  C N N 478 
VAL OXT  O N N 479 
VAL H    H N N 480 
VAL H2   H N N 481 
VAL HA   H N N 482 
VAL HB   H N N 483 
VAL HG11 H N N 484 
VAL HG12 H N N 485 
VAL HG13 H N N 486 
VAL HG21 H N N 487 
VAL HG22 H N N 488 
VAL HG23 H N N 489 
VAL HXT  H N N 490 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
GLN N   CA   sing N N 103 
GLN N   H    sing N N 104 
GLN N   H2   sing N N 105 
GLN CA  C    sing N N 106 
GLN CA  CB   sing N N 107 
GLN CA  HA   sing N N 108 
GLN C   O    doub N N 109 
GLN C   OXT  sing N N 110 
GLN CB  CG   sing N N 111 
GLN CB  HB2  sing N N 112 
GLN CB  HB3  sing N N 113 
GLN CG  CD   sing N N 114 
GLN CG  HG2  sing N N 115 
GLN CG  HG3  sing N N 116 
GLN CD  OE1  doub N N 117 
GLN CD  NE2  sing N N 118 
GLN NE2 HE21 sing N N 119 
GLN NE2 HE22 sing N N 120 
GLN OXT HXT  sing N N 121 
GLU N   CA   sing N N 122 
GLU N   H    sing N N 123 
GLU N   H2   sing N N 124 
GLU CA  C    sing N N 125 
GLU CA  CB   sing N N 126 
GLU CA  HA   sing N N 127 
GLU C   O    doub N N 128 
GLU C   OXT  sing N N 129 
GLU CB  CG   sing N N 130 
GLU CB  HB2  sing N N 131 
GLU CB  HB3  sing N N 132 
GLU CG  CD   sing N N 133 
GLU CG  HG2  sing N N 134 
GLU CG  HG3  sing N N 135 
GLU CD  OE1  doub N N 136 
GLU CD  OE2  sing N N 137 
GLU OE2 HE2  sing N N 138 
GLU OXT HXT  sing N N 139 
GLY N   CA   sing N N 140 
GLY N   H    sing N N 141 
GLY N   H2   sing N N 142 
GLY CA  C    sing N N 143 
GLY CA  HA2  sing N N 144 
GLY CA  HA3  sing N N 145 
GLY C   O    doub N N 146 
GLY C   OXT  sing N N 147 
GLY OXT HXT  sing N N 148 
HIS N   CA   sing N N 149 
HIS N   H    sing N N 150 
HIS N   H2   sing N N 151 
HIS CA  C    sing N N 152 
HIS CA  CB   sing N N 153 
HIS CA  HA   sing N N 154 
HIS C   O    doub N N 155 
HIS C   OXT  sing N N 156 
HIS CB  CG   sing N N 157 
HIS CB  HB2  sing N N 158 
HIS CB  HB3  sing N N 159 
HIS CG  ND1  sing Y N 160 
HIS CG  CD2  doub Y N 161 
HIS ND1 CE1  doub Y N 162 
HIS ND1 HD1  sing N N 163 
HIS CD2 NE2  sing Y N 164 
HIS CD2 HD2  sing N N 165 
HIS CE1 NE2  sing Y N 166 
HIS CE1 HE1  sing N N 167 
HIS NE2 HE2  sing N N 168 
HIS OXT HXT  sing N N 169 
HOH O   H1   sing N N 170 
HOH O   H2   sing N N 171 
ILE N   CA   sing N N 172 
ILE N   H    sing N N 173 
ILE N   H2   sing N N 174 
ILE CA  C    sing N N 175 
ILE CA  CB   sing N N 176 
ILE CA  HA   sing N N 177 
ILE C   O    doub N N 178 
ILE C   OXT  sing N N 179 
ILE CB  CG1  sing N N 180 
ILE CB  CG2  sing N N 181 
ILE CB  HB   sing N N 182 
ILE CG1 CD1  sing N N 183 
ILE CG1 HG12 sing N N 184 
ILE CG1 HG13 sing N N 185 
ILE CG2 HG21 sing N N 186 
ILE CG2 HG22 sing N N 187 
ILE CG2 HG23 sing N N 188 
ILE CD1 HD11 sing N N 189 
ILE CD1 HD12 sing N N 190 
ILE CD1 HD13 sing N N 191 
ILE OXT HXT  sing N N 192 
LEU N   CA   sing N N 193 
LEU N   H    sing N N 194 
LEU N   H2   sing N N 195 
LEU CA  C    sing N N 196 
LEU CA  CB   sing N N 197 
LEU CA  HA   sing N N 198 
LEU C   O    doub N N 199 
LEU C   OXT  sing N N 200 
LEU CB  CG   sing N N 201 
LEU CB  HB2  sing N N 202 
LEU CB  HB3  sing N N 203 
LEU CG  CD1  sing N N 204 
LEU CG  CD2  sing N N 205 
LEU CG  HG   sing N N 206 
LEU CD1 HD11 sing N N 207 
LEU CD1 HD12 sing N N 208 
LEU CD1 HD13 sing N N 209 
LEU CD2 HD21 sing N N 210 
LEU CD2 HD22 sing N N 211 
LEU CD2 HD23 sing N N 212 
LEU OXT HXT  sing N N 213 
LYS N   CA   sing N N 214 
LYS N   H    sing N N 215 
LYS N   H2   sing N N 216 
LYS CA  C    sing N N 217 
LYS CA  CB   sing N N 218 
LYS CA  HA   sing N N 219 
LYS C   O    doub N N 220 
LYS C   OXT  sing N N 221 
LYS CB  CG   sing N N 222 
LYS CB  HB2  sing N N 223 
LYS CB  HB3  sing N N 224 
LYS CG  CD   sing N N 225 
LYS CG  HG2  sing N N 226 
LYS CG  HG3  sing N N 227 
LYS CD  CE   sing N N 228 
LYS CD  HD2  sing N N 229 
LYS CD  HD3  sing N N 230 
LYS CE  NZ   sing N N 231 
LYS CE  HE2  sing N N 232 
LYS CE  HE3  sing N N 233 
LYS NZ  HZ1  sing N N 234 
LYS NZ  HZ2  sing N N 235 
LYS NZ  HZ3  sing N N 236 
LYS OXT HXT  sing N N 237 
MET N   CA   sing N N 238 
MET N   H    sing N N 239 
MET N   H2   sing N N 240 
MET CA  C    sing N N 241 
MET CA  CB   sing N N 242 
MET CA  HA   sing N N 243 
MET C   O    doub N N 244 
MET C   OXT  sing N N 245 
MET CB  CG   sing N N 246 
MET CB  HB2  sing N N 247 
MET CB  HB3  sing N N 248 
MET CG  SD   sing N N 249 
MET CG  HG2  sing N N 250 
MET CG  HG3  sing N N 251 
MET SD  CE   sing N N 252 
MET CE  HE1  sing N N 253 
MET CE  HE2  sing N N 254 
MET CE  HE3  sing N N 255 
MET OXT HXT  sing N N 256 
PHE N   CA   sing N N 257 
PHE N   H    sing N N 258 
PHE N   H2   sing N N 259 
PHE CA  C    sing N N 260 
PHE CA  CB   sing N N 261 
PHE CA  HA   sing N N 262 
PHE C   O    doub N N 263 
PHE C   OXT  sing N N 264 
PHE CB  CG   sing N N 265 
PHE CB  HB2  sing N N 266 
PHE CB  HB3  sing N N 267 
PHE CG  CD1  doub Y N 268 
PHE CG  CD2  sing Y N 269 
PHE CD1 CE1  sing Y N 270 
PHE CD1 HD1  sing N N 271 
PHE CD2 CE2  doub Y N 272 
PHE CD2 HD2  sing N N 273 
PHE CE1 CZ   doub Y N 274 
PHE CE1 HE1  sing N N 275 
PHE CE2 CZ   sing Y N 276 
PHE CE2 HE2  sing N N 277 
PHE CZ  HZ   sing N N 278 
PHE OXT HXT  sing N N 279 
PRO N   CA   sing N N 280 
PRO N   CD   sing N N 281 
PRO N   H    sing N N 282 
PRO CA  C    sing N N 283 
PRO CA  CB   sing N N 284 
PRO CA  HA   sing N N 285 
PRO C   O    doub N N 286 
PRO C   OXT  sing N N 287 
PRO CB  CG   sing N N 288 
PRO CB  HB2  sing N N 289 
PRO CB  HB3  sing N N 290 
PRO CG  CD   sing N N 291 
PRO CG  HG2  sing N N 292 
PRO CG  HG3  sing N N 293 
PRO CD  HD2  sing N N 294 
PRO CD  HD3  sing N N 295 
PRO OXT HXT  sing N N 296 
SER N   CA   sing N N 297 
SER N   H    sing N N 298 
SER N   H2   sing N N 299 
SER CA  C    sing N N 300 
SER CA  CB   sing N N 301 
SER CA  HA   sing N N 302 
SER C   O    doub N N 303 
SER C   OXT  sing N N 304 
SER CB  OG   sing N N 305 
SER CB  HB2  sing N N 306 
SER CB  HB3  sing N N 307 
SER OG  HG   sing N N 308 
SER OXT HXT  sing N N 309 
THR N   CA   sing N N 310 
THR N   H    sing N N 311 
THR N   H2   sing N N 312 
THR CA  C    sing N N 313 
THR CA  CB   sing N N 314 
THR CA  HA   sing N N 315 
THR C   O    doub N N 316 
THR C   OXT  sing N N 317 
THR CB  OG1  sing N N 318 
THR CB  CG2  sing N N 319 
THR CB  HB   sing N N 320 
THR OG1 HG1  sing N N 321 
THR CG2 HG21 sing N N 322 
THR CG2 HG22 sing N N 323 
THR CG2 HG23 sing N N 324 
THR OXT HXT  sing N N 325 
TRP N   CA   sing N N 326 
TRP N   H    sing N N 327 
TRP N   H2   sing N N 328 
TRP CA  C    sing N N 329 
TRP CA  CB   sing N N 330 
TRP CA  HA   sing N N 331 
TRP C   O    doub N N 332 
TRP C   OXT  sing N N 333 
TRP CB  CG   sing N N 334 
TRP CB  HB2  sing N N 335 
TRP CB  HB3  sing N N 336 
TRP CG  CD1  doub Y N 337 
TRP CG  CD2  sing Y N 338 
TRP CD1 NE1  sing Y N 339 
TRP CD1 HD1  sing N N 340 
TRP CD2 CE2  doub Y N 341 
TRP CD2 CE3  sing Y N 342 
TRP NE1 CE2  sing Y N 343 
TRP NE1 HE1  sing N N 344 
TRP CE2 CZ2  sing Y N 345 
TRP CE3 CZ3  doub Y N 346 
TRP CE3 HE3  sing N N 347 
TRP CZ2 CH2  doub Y N 348 
TRP CZ2 HZ2  sing N N 349 
TRP CZ3 CH2  sing Y N 350 
TRP CZ3 HZ3  sing N N 351 
TRP CH2 HH2  sing N N 352 
TRP OXT HXT  sing N N 353 
TYR N   CA   sing N N 354 
TYR N   H    sing N N 355 
TYR N   H2   sing N N 356 
TYR CA  C    sing N N 357 
TYR CA  CB   sing N N 358 
TYR CA  HA   sing N N 359 
TYR C   O    doub N N 360 
TYR C   OXT  sing N N 361 
TYR CB  CG   sing N N 362 
TYR CB  HB2  sing N N 363 
TYR CB  HB3  sing N N 364 
TYR CG  CD1  doub Y N 365 
TYR CG  CD2  sing Y N 366 
TYR CD1 CE1  sing Y N 367 
TYR CD1 HD1  sing N N 368 
TYR CD2 CE2  doub Y N 369 
TYR CD2 HD2  sing N N 370 
TYR CE1 CZ   doub Y N 371 
TYR CE1 HE1  sing N N 372 
TYR CE2 CZ   sing Y N 373 
TYR CE2 HE2  sing N N 374 
TYR CZ  OH   sing N N 375 
TYR OH  HH   sing N N 376 
TYR OXT HXT  sing N N 377 
UXO N   C    sing N N 378 
UXO C   N1   doub Y N 379 
UXO N1  C1   sing Y N 380 
UXO C1  N2   doub Y N 381 
UXO N2  C2   sing Y N 382 
UXO C2  C3   doub Y N 383 
UXO C   C3   sing Y N 384 
UXO C3  N3   sing Y N 385 
UXO N3  C4   doub Y N 386 
UXO C4  N4   sing Y N 387 
UXO C2  N4   sing Y N 388 
UXO N4  C5   sing N N 389 
UXO C5  O    sing N N 390 
UXO O   C6   sing N N 391 
UXO C7  C6   sing N N 392 
UXO N5  C7   sing N N 393 
UXO C8  N5   sing N N 394 
UXO C9  C8   sing N N 395 
UXO C10 C9   sing N N 396 
UXO C11 C10  sing N N 397 
UXO C12 C11  trip N N 398 
UXO C13 N5   sing N N 399 
UXO C14 C13  sing N N 400 
UXO C15 C14  trip N N 401 
UXO C16 C15  sing N N 402 
UXO C16 N6   doub Y N 403 
UXO N6  C17  sing Y N 404 
UXO C17 C18  doub Y N 405 
UXO N7  C18  sing Y N 406 
UXO C19 N7   doub Y N 407 
UXO N8  C19  sing Y N 408 
UXO C20 N8   doub Y N 409 
UXO C17 C20  sing Y N 410 
UXO N9  C20  sing N N 411 
UXO C18 N10  sing Y N 412 
UXO N10 C16  sing Y N 413 
UXO C21 N10  sing N N 414 
UXO C21 O1   sing N N 415 
UXO O1  C22  sing N N 416 
UXO C23 C22  sing N N 417 
UXO O2  C23  sing N N 418 
UXO C22 C24  sing N N 419 
UXO O3  C24  sing N N 420 
UXO C24 C25  sing N N 421 
UXO C25 C21  sing N N 422 
UXO O4  C25  sing N N 423 
UXO C6  C26  sing N N 424 
UXO O5  C26  sing N N 425 
UXO C26 C27  sing N N 426 
UXO C5  C27  sing N N 427 
UXO C27 O6   sing N N 428 
UXO C7  H8   sing N N 429 
UXO C7  H9   sing N N 430 
UXO C8  H10  sing N N 431 
UXO C8  H11  sing N N 432 
UXO C9  H12  sing N N 433 
UXO C9  H13  sing N N 434 
UXO C1  H6   sing N N 435 
UXO O5  H30  sing N N 436 
UXO C5  H    sing N N 437 
UXO C6  H1   sing N N 438 
UXO C4  H7   sing N N 439 
UXO O4  H28  sing N N 440 
UXO O3  H26  sing N N 441 
UXO N   H5   sing N N 442 
UXO N   H4   sing N N 443 
UXO C10 H15  sing N N 444 
UXO C10 H14  sing N N 445 
UXO C12 H16  sing N N 446 
UXO C13 H18  sing N N 447 
UXO C13 H17  sing N N 448 
UXO C19 H19  sing N N 449 
UXO C21 H2   sing N N 450 
UXO C22 H3   sing N N 451 
UXO C23 H23  sing N N 452 
UXO C23 H22  sing N N 453 
UXO C24 H25  sing N N 454 
UXO C25 H27  sing N N 455 
UXO C26 H29  sing N N 456 
UXO C27 H31  sing N N 457 
UXO N9  H21  sing N N 458 
UXO N9  H20  sing N N 459 
UXO O2  H24  sing N N 460 
UXO O6  H32  sing N N 461 
VAL N   CA   sing N N 462 
VAL N   H    sing N N 463 
VAL N   H2   sing N N 464 
VAL CA  C    sing N N 465 
VAL CA  CB   sing N N 466 
VAL CA  HA   sing N N 467 
VAL C   O    doub N N 468 
VAL C   OXT  sing N N 469 
VAL CB  CG1  sing N N 470 
VAL CB  CG2  sing N N 471 
VAL CB  HB   sing N N 472 
VAL CG1 HG11 sing N N 473 
VAL CG1 HG12 sing N N 474 
VAL CG1 HG13 sing N N 475 
VAL CG2 HG21 sing N N 476 
VAL CG2 HG22 sing N N 477 
VAL CG2 HG23 sing N N 478 
VAL OXT HXT  sing N N 479 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ANR-17-CE18-0011-02 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.accession_code   8A9V 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8QG7 
_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]   0.015779 
_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]   0.013279 
_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]   0.008431 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . MET A 1 1   ? 11.18146 36.95594 25.29945  1.000 109.29680 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.35637 36.92592 24.10112  1.000 96.65069  ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.46944  35.68808 24.06809  1.000 83.19196  ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.30961  34.99622 25.07442  1.000 79.92975  ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.23155 36.98420 22.84696  1.000 102.43074 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.62935 36.41168 23.02377  1.000 102.75389 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 13.64714 36.65009 21.55355  1.000 109.83519 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.27868 36.29476 22.20039  1.000 103.88915 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 8.89026  35.41989 22.90249  1.000 88.51738  ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 7.99472  34.28588 22.74471  1.000 79.43462  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.79389  33.00246 22.57001  1.000 68.47601  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.83953  32.98732 21.91392  1.000 69.17426  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.06836  34.50515 21.54908  1.000 80.49595  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.38401  35.86416 21.55511  1.000 81.67124  ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 4.89934  35.74198 21.26387  1.000 93.41623  ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.16612  37.05139 21.51239  1.000 97.18977  ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 4.54122  38.10273 20.52801  1.000 99.42526  ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.29747  31.92291 23.16942  1.000 68.64702  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 8.98812  30.64442 23.12045  1.000 65.43583  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.97017  29.52079 23.23232  1.000 65.62286  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.85457  29.71092 23.72354  1.000 69.31935  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 10.03215 30.52122 24.23846  1.000 63.64350  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.44568  30.11905 25.57422  1.000 72.20639  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.89469  31.06669 26.42857  1.000 77.34207  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.44128  28.78920 25.98109  1.000 65.25742  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.35551  30.70122 27.64644  1.000 78.07929  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.89983  28.41601 27.19478  1.000 72.48362  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.36188  29.37594 28.02536  1.000 74.50358  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.82511  29.01025 29.23800  1.000 65.19907  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.37715  28.33941 22.77507  1.000 63.77103  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.59163  27.12812 22.95308  1.000 60.26807  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.55203  25.96090 23.12056  1.000 52.84803  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.74900  26.07013 22.84460  1.000 55.61025  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.62871  26.89634 21.78135  1.000 59.62458  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.28264  26.41295 20.49110  1.000 56.39569  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.46323  24.61745 20.39330  1.000 66.77731  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.83717  24.08678 20.92484  1.000 65.33516  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 8.01358  24.83392 23.58022  1.000 53.91685  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.80328  23.63382 23.83478  1.000 60.71886  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 8.01286  22.41760 23.37303  1.000 59.73749  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.86380  22.22561 23.78439  1.000 61.09484  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 9.17467  23.49089 25.32432  1.000 58.34778  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.95152  24.71504 25.81367  1.000 54.20003  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.99751  22.23351 25.54460  1.000 51.27179  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 10.13551 24.76367 27.31004  1.000 55.65821  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.62572  21.59693 22.52363  1.000 52.98761  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 8.05613  20.31954 22.12160  1.000 58.71059  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.68929  19.19268 22.92817  1.000 56.44167  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.85422  19.26926 23.32769  1.000 59.28182  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 8.26066  20.05916 20.62681  1.000 59.16442  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 9.63118  20.29666 20.27664  1.000 54.28840  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.35910  20.95781 19.79348  1.000 60.38502  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.90856  18.13945 23.16149  1.000 58.75271  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 8.34415  17.01390 23.97130  1.000 53.85240  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 8.14342  15.71531 23.20507  1.000 62.59228  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 7.21974  15.58504 22.39803  1.000 63.05639  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.58327  16.95490 25.30322  1.000 63.29930  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.97420  15.82594 26.06318  1.000 58.92397  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 9.02848  14.75036 23.46812  1.000 67.12577  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.90394  13.44289 22.83168  1.000 69.69350  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.64161  12.72844 23.29040  1.000 69.54745  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 7.10424  11.88156 22.56763  1.000 74.17191  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 10.14007 12.59175 23.12260  1.000 68.04092  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 10.20683 11.29779 22.32747  1.000 78.40224  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 11.05768 10.25772 23.04244  1.000 80.06163  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 11.25684 9.02386  22.17448  1.000 93.11368  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 9.96747  8.49453  21.64570  1.000 102.67174 ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 7.15729  13.05402 24.48416  1.000 66.66527  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.93110  12.50492 25.01550  1.000 75.40250  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 6.11786  11.58675 26.20368  1.000 65.55126  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 5.15253  11.34949 26.94488  1.000 87.67558  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 7.32162  11.06064 26.40829  1.000 68.39454  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 7.55752  10.19718 27.55321  1.000 75.33280  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.64881  11.02630 28.83353  1.000 76.49311  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.69816  12.25870 28.80694  1.000 75.12711  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.82547  9.36292  27.35692  1.000 72.76289  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 10.04791 10.21155 27.07382  1.000 70.47192  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.89397  11.43730 26.90224  1.000 72.15705  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 11.16404 9.65424  27.02109  1.000 75.69642  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.67349  10.32660 29.97236  1.000 75.74093  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.65259  11.01091 31.26303  1.000 77.09651  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.87433  11.90241 31.44747  1.000 75.39905  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.76959  12.99957 32.00679  1.000 73.92339  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.56391  9.99512  32.40084  0.700 83.67402  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 6.21850  9.30033  32.52527  0.600 77.44087  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 6.13932  8.41558  33.75237  0.600 94.79655  ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.96852  8.59555  34.66943  0.600 95.73648  ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 5.25239  7.53723  33.80116  0.600 98.22026  ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 10.04236 11.45352 30.98426  1.000 70.74007  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 11.25833 12.23377 31.19365  1.000 64.61207  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 11.19183 13.56741 30.45907  1.000 70.67368  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 11.47150 14.62335 31.03852  1.000 62.33163  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 12.48800 11.44021 30.75273  1.000 80.58445  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.77208 12.24001 30.88027  1.000 85.62237  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 15.01266 11.37154 30.83137  1.000 85.07128  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 16.21765 12.16011 31.32204  1.000 90.01635  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 17.50628 11.45694 31.08136  1.000 83.78986  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.81665 13.54117 29.17892  1.000 69.83885  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.78909 14.77648 28.40276  1.000 61.59243  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.61030  15.65608 28.79930  1.000 64.66276  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.73610  16.88542 28.84465  1.000 63.77247  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.74497 14.45754 26.91130  1.000 67.29112  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.77607 13.55216 26.55962  1.000 61.06909  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 8.45809  15.04592 29.09004  1.000 69.02396  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 7.28214  15.82394 29.46737  1.000 70.66581  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.53127  16.62803 30.73667  1.000 62.05795  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 7.11972  17.79007 30.83351  1.000 59.17966  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 6.07467  14.90379 29.65003  1.000 70.34719  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 5.23271  14.78274 28.39408  1.000 79.80657  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.68955  15.22405 27.31929  1.000 65.86937  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 4.10516  14.25402 28.48834  1.000 86.70533  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 8.20919  16.03125 31.71897  1.000 67.61398  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 8.41563  16.71575 32.98889  1.000 70.31835  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.61530  17.65486 32.95329  1.000 62.05978  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.65233  18.62682 33.71605  1.000 61.07814  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.56266  15.69729 34.12054  1.000 64.87573  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 7.23274  15.25064 34.74101  1.000 86.29609  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 6.51838  14.21836 33.87741  1.000 76.44016  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 7.43612  14.72640 36.15270  1.000 70.74423  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.59982 17.39197 32.08976  1.000 58.57277  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.65357 18.37860 31.87429  1.000 58.01230  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 11.08900 19.63266 31.22064  1.000 62.88057  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 11.53774 20.74890 31.50805  1.000 64.81556  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.77359 17.78623 31.01956  1.000 58.23909  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.99154 18.68890 30.80313  1.000 62.69574  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.65495 19.01827 32.13106  1.000 56.80944  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.98727 18.04362 29.85358  1.000 54.06915  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 10.09810 19.46329 30.34223  1.000 60.96792  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 9.44892  20.60663 29.71065  1.000 62.77325  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.68475  21.44443 30.72770  1.000 60.70848  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.74784  22.67825 30.69302  1.000 63.73076  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.51793  20.11971 28.60165  1.000 53.89172  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.59423  21.17805 28.02296  1.000 53.96540  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.75476  20.59140 26.89892  1.000 63.12197  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.79384  21.54689 26.36116  1.000 61.27204  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.58532  21.75628 26.86569  1.000 62.11482  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 4.16211  21.10843 27.93880  1.000 58.15414  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.78089  22.63801 26.27943  1.000 57.26427  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.96170  20.79514 31.64419  1.000 61.27786  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 7.20636  21.54094 32.64567  1.000 68.98241  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 8.12159  22.28566 33.60610  1.000 60.81893  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.74228  23.33901 34.12711  1.000 61.92202  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 6.27921  20.60465 33.41982  1.000 71.58241  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 5.02201  20.13903 32.68318  1.000 73.21317  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 4.09821  19.36644 33.61525  1.000 78.19276  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 4.29809  21.32558 32.06475  1.000 74.85953  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 9.32064  21.75921 33.85594  1.000 60.90827  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 10.25080 22.44600 34.74594  1.000 63.10965  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.87975 23.65183 34.05938  1.000 65.61985  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 11.11575 24.68489 34.69836  1.000 69.57275  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 11.32764 21.47659 35.24149  1.000 62.06263  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.94348 20.79560 36.54269  1.000 64.71126  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 10.07435 21.27268 37.27532  1.000 66.25308  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 11.60418 19.68447 36.84458  1.000 65.55199  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 11.16546 23.53845 32.76040  1.000 58.73895  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.73072 24.67308 32.03725  1.000 62.58824  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.70796 25.79262 31.87574  1.000 65.43324  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 11.05555 26.97693 31.96337  1.000 72.57854  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 12.26526 24.22171 30.67889  1.000 55.03173  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 13.51851 23.36178 30.77002  1.000 59.58707  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 14.22372 22.98284 29.15776  1.000 60.35872  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.70900 24.61514 28.59902  1.000 62.23912  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.43876  25.43947 31.65446  1.000 63.68413  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 8.38187  26.44770 31.60161  1.000 61.97857  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 8.29025  27.19129 32.92794  1.000 64.66071  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 8.17424  28.42239 32.95837  1.000 66.69159  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 7.03633  25.79927 31.22647  1.000 62.11162  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 7.07359  25.26058 29.79391  1.000 59.68698  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.89225  26.79064 31.39591  1.000 62.08991  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.80229  24.55410 29.37612  1.000 57.89700  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 8.35340  26.45762 34.04215  1.000 62.62613  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 8.30355  27.09073 35.35651  1.000 66.42136  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.47540  28.04415 35.54761  1.000 66.95409  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 9.29852  29.17863 36.00739  1.000 67.08937  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 8.29005  26.02424 36.45155  1.000 66.00153  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.68598 27.59929 35.19765  1.000 64.10103  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.83626 28.48306 35.26821  1.000 64.85713  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.72369 29.67114 34.33417  1.000 77.90304  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 12.19394 30.76581 34.65580  1.000 78.79346  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 11.10013 29.47728 33.16842  1.000 65.80249  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.85996 30.59664 32.26446  1.000 70.91534  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.84896  31.57706 32.84418  1.000 74.29183  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.88741  32.77068 32.52005  1.000 78.63277  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 10.37901 30.08305 30.91053  1.000 72.15935  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.49306 29.67660 29.98343  1.000 73.43232  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.58721 30.50350 29.78865  1.000 75.63426  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.44856 28.46751 29.30954  1.000 68.67331  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.61165 30.13361 28.93639  1.000 80.62437  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.46875 28.09067 28.45650  1.000 70.10404  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.55225 28.92555 28.26914  1.000 70.23690  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.94193  31.09943 33.70207  1.000 75.23119  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.96930  31.98720 34.31405  1.000 68.53638  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.58685  32.99763 35.25732  1.000 81.17749  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.92568  33.96906 35.64303  1.000 79.08327  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.84012  32.78891 35.64469  1.000 82.51516  ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.56173 33.72139 36.49874  1.000 83.81955  ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 11.27007 34.81097 35.70486  1.000 87.57650  ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 12.02206 35.59879 36.28662  1.000 93.67732  ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.56835 32.96736 37.36961  1.000 75.79089  ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.94059 31.87296 38.22288  1.000 75.17870  ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.87398  32.39910 39.16680  1.000 77.50491  ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 9.98460  33.56048 39.61642  1.000 81.41129  ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.91955  31.64791 39.45828  1.000 78.89660  ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 11.05004 34.86848 34.39408  1.000 82.46540  ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.58666 35.91753 33.54145  1.000 90.66786  ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 10.46116 36.46400 32.67485  1.000 90.34961  ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 9.33675  35.95642 32.68792  1.000 89.62473  ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.73103 35.40091 32.65764  1.000 90.76379  ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.89668 34.81075 33.41909  1.000 91.42959  ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.90910 33.46919 33.77998  1.000 76.39367  ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 14.99131 35.59195 33.76379  1.000 95.97541  ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.97523 32.92542 34.46966  1.000 78.58534  ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 16.06172 35.05724 34.45162  1.000 92.00378  ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 16.04855 33.72453 34.80228  1.000 90.56169  ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 17.11400 33.19056 35.48885  1.000 85.58939  ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 10.76698 37.51158 31.90841  1.000 99.81532  ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 9.81844  38.02812 30.92167  1.000 100.39744 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 9.92694  37.18298 29.65193  1.000 102.87880 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 10.45076 37.59971 28.61646  1.000 107.39538 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 10.06381 39.50258 30.63639  1.000 113.12455 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 9.01778  40.09520 29.70530  1.000 120.96077 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 7.92498  39.50101 29.58048  1.000 115.80246 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 9.28920  41.14787 29.08927  1.000 130.69831 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 9.42279  35.95681 29.75928  1.000 96.94133  ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 9.37180  35.01241 28.64865  1.000 99.23286  ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.96904  34.42583 28.60420  1.000 103.14768 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.57106  33.69613 29.51729  1.000 108.11229 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 10.42259 33.91093 28.80596  1.000 96.21046  ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 11.85735 34.40785 28.72585  1.000 101.29784 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.39391 34.67468 27.02691  1.000 115.88440 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 13.51091 36.05864 27.23234  1.000 115.35122 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 7.21857  34.75088 27.55644  1.000 91.12850  ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.84774  34.28676 27.40780  1.000 87.31277  ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.80342  33.05879 26.51089  1.000 79.85157  ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.48050  33.00113 25.47962  1.000 80.02215  ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 4.95246  35.39022 26.83657  1.000 85.04707  ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 5.42121  35.96138 25.50979  1.000 90.91696  ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 4.59144  37.14786 25.06148  1.000 97.29779  ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 3.34945  37.09032 25.18327  1.000 101.27115 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 5.18463  38.14281 24.59509  1.000 96.68680  ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 5.01058  32.07252 26.91842  1.000 75.10584  ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.84182  30.85805 26.13199  1.000 76.68235  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.88335  31.13734 24.97993  1.000 74.67444  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.73876  31.55722 25.20207  1.000 70.85481  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 4.32016  29.71916 27.00900  1.000 61.75304  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.39617  28.35387 26.35752  1.000 71.57271  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 3.45786  27.95803 25.41248  1.000 76.66671  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.40370  27.45775 26.69388  1.000 75.93808  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.52395  26.71277 24.81514  1.000 64.72896  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.47641  26.20917 26.10244  1.000 71.47433  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.53305  25.84254 25.16403  1.000 64.78356  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.60108  24.60137 24.57325  1.000 62.57780  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.35537  30.90988 23.75547  1.000 65.60413  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.53738  31.08937 22.56260  1.000 70.11188  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 4.00276  30.08900 21.51974  1.000 72.89055  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 5.13700  30.18015 21.04098  1.000 67.83898  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.64600  32.51958 22.02344  1.000 82.29471  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.66100  32.80387 20.89675  1.000 88.16470  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 2.24236  31.86490 20.20206  1.000 81.17441  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.30655  33.98925 20.71263  1.000 97.75399  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 3.13358  29.14195 21.16923  1.000 73.62995  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.43510  28.15560 20.14007  1.000 75.40593  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.91582  28.56234 18.76698  1.000 72.86909  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.94416  27.74863 17.83971  1.000 73.12007  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.88197  26.78246 20.53756  1.000 67.99285  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.37018  26.77954 20.71798  1.000 74.69061  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.72214  27.82800 20.51657  1.000 78.09643  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.82657  25.70906 21.06911  1.000 71.07683  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.43815  29.79295 18.62009  1.000 75.46638  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.99617  30.31605 17.33144  1.000 81.76772  ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 3.08389  31.15027 16.67059  1.000 81.43746  ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.42910  30.92757 15.51031  1.000 75.51329  ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.69178  31.12728 17.49789  1.000 81.54532  ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.26399  31.72040 16.16564  1.000 79.24859  ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.40577 30.25089 18.07778  1.000 75.47986  ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.64235  32.11435 17.40016  1.000 80.31408  ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.72928  32.95774 16.89945  1.000 80.02161  ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.90185  32.95728 17.87469  1.000 78.55122  ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.25330  33.99535 18.44257  1.000 82.94169  ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.23555  34.38226 16.65375  1.000 89.19677  ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.29056  34.52959 15.47817  1.000 94.02980  ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 3.03529  35.98117 15.12360  1.000 99.73649  ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 2.79343  36.78901 16.04519  1.000 92.49892  ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 3.09044  36.31614 13.92159  1.000 110.45097 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.54470  31.81083 18.08368  1.000 68.37825  ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.71360  31.78490 18.96303  1.000 73.09773  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.95908  32.27993 18.24856  1.000 69.73990  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 9.10577  32.14873 17.03149  1.000 77.07404  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.84193  30.30193 19.32647  1.000 68.30455  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.35355  29.60365 18.10906  1.000 68.79309  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 6.26432  30.47609 17.52078  1.000 74.18913  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.85821  32.87430 19.02960  1.000 67.73838  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 11.18478 33.22756 18.54648  1.000 69.97135  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 12.24199 32.22101 18.97311  1.000 69.36888  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.34997 32.23447 18.42500  1.000 65.07049  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.57789 34.62686 19.03718  1.000 68.24854  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.50694 35.67986 18.80422  0.700 73.69506  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 11.02171 37.09409 18.98794  0.600 82.94374  ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 12.00606 37.46302 18.31240  0.600 74.29203  ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.44325 37.83546 19.80978  0.600 70.63611  ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.91940 31.35224 19.92804  1.000 68.06129  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.81240 30.30747 20.40864  1.000 65.44733  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 12.01581 29.01472 20.49832  1.000 57.85333  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.96636 28.97195 21.14940  1.000 58.90465  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.42321 30.66545 21.77664  1.000 64.04708  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 14.48712 31.75359 21.61605  1.000 70.76978  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 13.98605 29.42625 22.45455  1.000 58.55320  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 14.91415 32.38669 22.91965  1.000 82.03108  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.50443 27.96964 19.83727  1.000 58.03090  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.86231 26.66026 19.83914  1.000 62.88594  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.82552 25.66499 20.46554  1.000 55.01761  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.92205 25.43502 19.93936  1.000 47.41640  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.45369 26.21648 18.42645  1.000 51.44102  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 11.06783 24.74470 18.42537  1.000 56.68984  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.30013 27.06970 17.92273  1.000 52.82761  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.41566 25.07679 21.58500  1.000 51.05103  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 13.22209 24.11349 22.32435  1.000 51.15209  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.62909 22.72916 22.10809  1.000 50.21679  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.43775 22.50986 22.36150  1.000 57.24425  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 13.27847 24.46282 23.82239  1.000 59.77404  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.92062 25.83569 24.02709  1.000 57.78316  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 14.03127 23.39061 24.59030  1.000 47.07099  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.76571 26.38445 25.43158  1.000 60.40104  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.45532 21.80139 21.63613  1.000 50.71469  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 13.04478 20.42485 21.39759  1.000 50.65786  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.67576 19.51676 22.44277  1.000 44.93376  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.90033 19.51003 22.60952  1.000 49.64387  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.44638 19.96849 19.99442  1.000 44.34043  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 13.18793 18.58609 19.81282  1.000 46.37203  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.83878 18.76572 23.15148  1.000 46.13538  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 13.27808 17.86363 24.21203  1.000 54.05939  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.95561 16.44165 23.77464  1.000 51.06444  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.78011 16.07239 23.65227  1.000 58.54446  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.61644 18.19182 25.55590  1.000 53.10855  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.87278 19.65356 25.91931  1.000 48.31291  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 13.14273 17.27910 26.64812  1.000 53.83356  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 12.40330 20.02569 27.30340  1.000 49.80367  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.99501 15.64499 23.53866  1.000 50.30822  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.82640 14.27491 23.09744  1.000 60.44974  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 15.00941 13.77348 22.29630  1.000 57.50888  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 16.13412 13.73349 22.80113  1.000 66.32081  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.77163 13.38807 21.04579  1.000 63.94346  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.84859 12.94326 20.18367  1.000 51.48537  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.96374 13.76116 18.91461  1.000 53.98913  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 15.36599 14.83575 18.80542  1.000 48.55724  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.73822 13.26795 17.94544  1.000 51.98399  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.81284 13.94952 16.65857  1.000 52.50286  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 15.48900 13.87363 15.91105  1.000 50.24454  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 15.15577 14.79031 15.15089  1.000 45.29277  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.94117 13.36208 15.81144  1.000 49.00238  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 19.31384 13.75516 16.31901  1.000 49.43183  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 19.44092 14.85455 16.90016  1.000 48.81467  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 20.26504 12.96634 16.13878  1.000 50.53170  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.72378 12.79942 16.11390  1.000 50.96979  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 13.40548 12.72269 15.50764  1.000 43.61775  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 12.44639 13.74574 16.08317  1.000 52.74657  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.64413 14.33762 15.35530  1.000 45.60847  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 12.51527 13.96870 17.39751  1.000 47.14862  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.70711 15.01649 18.01039  1.000 45.66177  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 12.12664 16.39324 17.50938  1.000 43.05920  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 11.28308 17.27631 17.31264  1.000 45.62228  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.81772 14.94298 19.53192  1.000 53.74867  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.38971 13.65344 19.98521  1.000 57.12534  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.95064 16.01153 20.18528  1.000 44.84809  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.42765 16.59112 17.28349  1.000 41.14623  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.89333 17.85669 16.72689  1.000 43.77550  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.43825 18.01967 15.28335  1.000 49.17579  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 13.06258 19.12198 14.86789  1.000 41.12381  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.41674 17.95038 16.81954  1.000 42.22101  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.96737 19.29296 16.42208  1.000 50.36716  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 16.21823 19.59371 15.08975  1.000 44.43273  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 16.23662 20.25452 17.38117  1.000 49.81214  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.72501 20.82755 14.72528  1.000 47.41141  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.74369 21.48931 17.02101  1.000 56.06000  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.98753 21.77657 15.69376  1.000 50.23484  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.48627 16.93940 14.49801  1.000 48.05721  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 13.01745 17.01101 13.11788  1.000 48.20824  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.54313 17.38503 13.05917  1.000 44.78130  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 11.12088 18.13842 12.17553  1.000 44.68681  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 13.26356 15.68068 12.40756  1.000 45.74767  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.70383 15.38701 11.98095  1.000 50.49824  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.81029 13.99416 11.38180  1.000 52.03177  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 15.19150 16.43740 10.99511  1.000 55.86468  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.74515 16.87110 13.99707  1.000 50.28659  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 9.33850  17.25229 14.06200  1.000 59.54564  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 9.18826  18.73760 14.36198  1.000 56.47183  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.33632  19.41472 13.77481  1.000 54.18909  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.61493  16.41708 15.12101  1.000 57.02413  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.73879  15.02979 14.85906  1.000 68.24062  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 10.01654 19.26305 15.26875  1.000 49.29804  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.92564  20.67300 15.63406  1.000 54.70165  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 10.32185 21.57701 14.47289  1.000 48.27205  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.73134  22.64716 14.28540  1.000 49.39493  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.79694 20.95309 16.85742  1.000 47.90729  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 11.31619 21.16439 13.68280  1.000 49.27760  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.71860 21.95048 12.52006  1.000 54.76534  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.57101 22.08674 11.52782  1.000 50.41205  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 10.26463 23.18958 11.06004  1.000 49.99526  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.93669 21.30995 11.85070  1.000 48.32443  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 13.22337 21.84205 10.47358  1.000 55.10340  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.87571 23.05156 10.30669  1.000 53.12085  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.84514 21.12909 9.34601   1.000 50.15995  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 14.14296 23.54285 9.04169   1.000 53.18957  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 13.10842 21.61581 8.07844   1.000 53.38962  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.75866 22.82453 7.92799   1.000 51.69294  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.92505  20.96846 11.19091  1.000 50.16234  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.83088  21.00170 10.22850  1.000 49.56120  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.57243  21.64002 10.79990  1.000 60.40929  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.71961  22.09353 10.02962  1.000 62.98429  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.52963  19.58840 9.73158   1.000 50.32055  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.59596  19.02601 8.84586   1.000 53.48462  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.72771  19.38744 7.52272   1.000 55.29461  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.58575 18.13615 9.09365   1.000 52.79903  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.74974 18.74087 6.99172   1.000 55.16815  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.28802 17.97559 7.92391   1.000 60.21117  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.43542  21.68345 12.12679  1.000 59.87124  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 6.31555  22.39899 12.72820  1.000 58.79911  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.37863  23.88515 12.40179  1.000 56.90632  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.34370  24.52998 12.19577  1.000 62.20404  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 6.31172  22.18704 14.24166  1.000 66.80366  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 5.11547  21.41881 14.77367  1.000 63.59373  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 5.25505  21.08799 16.24796  1.000 78.05197  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.98997  20.17365 16.62312  1.000 79.33611  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 4.55463  21.83617 17.09256  1.000 67.09326  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.58501  24.44191 12.33802  1.000 62.37362  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.80011  25.87279 12.16951  1.000 62.52413  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.68603  26.15838 10.96326  1.000 62.61771  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.53540  27.05114 10.98874  1.000 59.18736  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.40408  26.47540 13.43463  1.000 59.94598  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.56122  26.27107 14.67147  1.000 63.53894  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.57620  27.18415 15.01865  1.000 61.45701  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.75148  25.16735 15.49405  1.000 62.17050  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.80170  27.00503 16.14860  1.000 63.91770  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.98156  24.97983 16.62626  1.000 70.85512  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 6.00875  25.90245 16.94808  1.000 72.08136  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 5.23655  25.72510 18.07343  1.000 66.49995  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.49153  25.39923 9.88433   1.000 54.46693  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.30816  25.55934 8.68732   1.000 65.02933  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.98211  26.82426 7.90527   1.000 61.11606  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.75915  27.19893 7.02082   1.000 69.77089  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.14864  24.33602 7.78263   1.000 53.53461  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.72771  24.10641 7.29925   1.000 60.23572  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.57240  22.79749 6.55334   0.700 65.41931  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.48306  21.94861 6.64969   0.700 54.83360  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 6.54236  22.61786 5.86957   0.700 63.98131  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.86617  27.48474 8.20133   1.000 63.43677  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.48005  28.71258 7.51822   1.000 69.27116  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.88910  29.96653 8.27714   1.000 72.66857  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.65649  31.07619 7.78742   1.000 71.83884  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.96814  28.71885 7.26918   1.000 73.41188  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.51362  27.67215 6.26573   0.800 71.19499  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 4.02234  27.41294 6.32337   0.700 78.08192  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 3.47505  27.32503 7.44287   0.700 89.79480  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 3.39584  27.29837 5.24886   0.700 99.58906  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.48543  29.81514 9.45612   1.000 66.53224  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 9.01135  30.92077 10.24778  1.000 74.70250  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.47017 30.67554 10.59356  1.000 67.35500  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.93676 31.02234 11.67916  1.000 77.39962  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.17993  31.13037 11.51217  1.000 71.32437  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.80302  31.71136 11.25992  1.000 82.16657  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.97362  31.75670 12.53535  1.000 87.40664  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.75299  32.20534 13.68356  1.000 85.34703  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.05226  33.47204 13.93917  1.000 91.62626  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 6.67362  34.44932 13.13244  1.000 84.03972  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.75159  33.76628 15.03076  1.000 74.02257  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.21089 30.06960 9.66173   1.000 66.86054  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.58566 29.66755 9.94622   1.000 66.81760  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.47965 30.86912 10.21634  1.000 66.85166  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.39666 30.79393 11.03996  1.000 73.01597  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.14050 28.84300 8.78302   1.000 64.40117  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.56112 27.44074 8.62271   1.000 70.67603  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.24074 26.71643 7.48125   1.000 50.84756  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.71702 26.66455 9.91522   1.000 54.14961  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.23101 31.98596 9.53471   1.000 70.77112  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 14.09284 33.15111 9.67761   1.000 79.66408  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.84242 33.92608 10.96447  1.000 77.01856  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.65657 34.78652 11.31559  1.000 80.24753  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.92009 34.08227 8.47545   1.000 74.60991  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 15.22927 34.69912 8.02576   1.000 87.34023  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 16.03422 33.98502 7.39006   1.000 87.56733  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.45601 35.89443 8.30983   1.000 93.70141  ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.75005 33.64394 11.67529  1.000 74.15199  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.41174 34.34983 12.90453  1.000 72.70324  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.52661 33.45872 14.13763  1.000 73.60797  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 12.00283 33.80832 15.20019  1.000 71.74130  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 11.00140 34.93525 12.80655  1.000 73.31414  ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.78353 35.84346 11.60433  1.000 91.20044  ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 9.91548  35.20509 10.53441  1.000 95.81775  ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 8.71668  34.97177 10.79877  1.000 100.68553 ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 10.43375 34.93171 9.43119   1.000 97.11306  ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.20826 32.32026 14.02383  1.000 79.97411  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.23491 31.31438 15.08061  1.000 68.12277  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.65795 30.80080 15.25969  1.000 64.89374  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.38083 30.58340 14.28143  1.000 57.81583  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.26807 30.15116 14.76772  1.000 65.01116  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.81707 30.62901 14.83666  1.000 59.95228  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.48601 28.98883 15.71908  1.000 58.18257  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.80491  29.56676 14.48804  1.000 64.71122  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 15.05830 30.61389 16.51601  1.000 62.89563  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.30379 29.94616 16.87030  1.000 60.45759  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.97738 28.64393 17.58923  1.000 60.70442  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.20208 28.64009 18.55131  1.000 60.87466  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.17872 30.83818 17.75294  1.000 55.21299  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.56571 27.54627 17.12414  1.000 53.73551  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 16.25311 26.21741 17.62849  1.000 53.07562  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.27171 25.76651 18.67018  1.000 56.02214  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.46087 26.08554 18.58708  1.000 52.73013  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 16.20774 25.20010 16.48531  1.000 50.77093  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 15.01073 25.34168 15.58410  1.000 52.75964  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 15.01693 26.24595 14.53498  1.000 51.12681  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 13.88380 24.55840 15.77917  1.000 51.56105  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 13.91793 26.37288 13.70257  1.000 54.76250  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 12.78314 24.68059 14.95085  1.000 51.79499  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.80032 25.58973 13.91100  1.000 47.88325  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.78490 25.01655 19.65821  1.000 52.03662  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.62078 24.37980 20.66902  1.000 50.44047  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 17.16513 22.93660 20.82322  1.000 50.47006  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.96154 22.65675 20.85562  1.000 48.73205  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.55607 25.10938 22.02873  1.000 52.35473  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 18.07441 26.53976 21.90534  1.000 54.72829  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.34615 24.35209 23.08847  1.000 55.22965  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 16.98207 27.57651 21.90934  1.000 63.71491  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 18.12574 22.02097 20.91650  1.000 46.91328  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.80774 20.62470 21.13266  1.000 54.81199  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 18.35493 20.07382 22.43319  1.000 58.20377  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.53884 20.24598 22.74009  1.000 59.05051  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.49878 19.40957 23.20565  1.000 58.04045  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.88373 18.76367 24.45575  1.000 53.95142  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.61056 17.27451 24.30856  1.000 51.82032  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.47113 16.87215 24.04190  1.000 55.40930  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 17.12440 19.34123 25.66072  1.000 57.28722  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 17.36187 20.84732 25.77629  1.000 62.27671  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 17.54324 18.63203 26.94361  1.000 52.71157  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.60541 21.49533 26.91629  1.000 48.98767  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.64712 16.45861 24.47977  1.000 53.59206  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.52603 15.01285 24.34508  1.000 57.38630  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 18.34536 14.39054 25.72577  1.000 60.85716  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 19.22279 14.50852 26.58644  1.000 65.24320  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.73962 14.41955 23.62195  1.000 61.35044  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 21.02849 14.54200 24.37513  1.000 55.06488  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.47967 13.56720 25.23897  1.000 59.30449  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.96633 15.51846 24.38780  1.000 54.87156  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.63713 13.94007 25.75485  1.000 62.99351  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.95476 15.12064 25.25495  1.000 66.70131  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 17.19535 13.75379 25.94163  1.000 64.42700  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.94583 13.02322 27.17541  1.000 77.10370  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 17.44908 11.59140 27.10954  1.000 78.61871  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 17.63814 10.96309 28.15644  1.000 77.72408  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 15.44987 13.02218 27.50545  1.000 70.49939  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.70823 12.54737 26.37352  1.000 69.86097  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.98809 14.42145 27.85969  1.000 66.20106  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 17.66404 11.06406 25.91064  1.000 81.12996  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 18.33519 9.79106  25.76412  1.000 80.04197  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 19.79165 9.95207  25.38856  1.000 73.25395  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 20.52623 10.66625 26.07438  1.000 73.56620  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 20.21552 9.30306  24.30990  1.000 80.50537  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 21.59154 9.43664  23.86653  1.000 79.71105  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.80471 10.78301 23.16526  1.000 74.30985  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.84918 11.49207 22.82615  1.000 75.46057  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.95956 8.28358  22.93556  1.000 76.88032  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 21.10206 8.20072  21.70782  1.000 82.47690  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 21.35001 8.95811  20.58468  1.000 80.30954  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 20.00855 7.45177  21.42097  1.000 80.42533  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 20.44533 8.68763  19.66095  1.000 76.26846  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 19.61827 7.77668  20.14262  1.000 86.42464  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 23.08305 11.11696 22.94662  1.000 62.37673  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 23.46398 12.36751 22.29653  1.000 67.47406  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.99053 12.38185 20.85346  1.000 65.45367  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 23.21655 11.43079 20.10141  1.000 66.80875  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.97515 12.53808 22.33541  1.000 62.16778  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 25.56163 13.72339 21.55597  1.000 67.91603  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 25.02304 15.06418 22.04746  1.000 63.41666  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 27.06912 13.71213 21.64645  1.000 66.79070  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 22.36066 13.47140 20.47063  1.000 57.66771  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.93439 13.68039 19.10887  1.000 56.43191  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.79055 14.72709 18.42085  1.000 57.06887  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 23.57012 15.43573 19.04216  1.000 61.24832  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.62546 14.81525 17.10545  1.000 40.29285  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 23.36488 15.81822 16.35563  1.000 53.97144  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.66649 17.16677 16.36448  1.000 51.16121  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.33465 18.19674 16.23785  1.000 51.79793  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.59075 15.34826 14.92387  1.000 44.54988  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.79906 14.47748 14.76138  1.000 39.65517  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.71700 13.11759 14.97929  1.000 40.26597  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 26.02091 15.02287 14.40471  1.000 43.62942  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.82179 12.30976 14.82939  1.000 45.77035  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 27.13324 14.22291 14.25811  1.000 41.32822  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 27.03661 12.86342 14.47076  1.000 49.17852  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 21.34385 17.18447 16.50592  1.000 45.87669  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.59405 18.41611 16.71212  1.000 47.56524  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 20.26800 18.65266 18.17913  1.000 54.77575  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 20.28472 19.79794 18.63829  1.000 57.64801  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.29945 18.39522 15.89328  1.000 48.74826  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.52272 18.11894 14.42555  1.000 53.39702  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.26903 18.98929 13.64460  1.000 49.93359  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.98798 16.98895 13.82155  1.000 49.49631  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.48221 18.74123 12.29945  1.000 44.64913  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 19.19172 16.73212 12.48026  1.000 47.07334  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.93920 17.60996 11.72376  1.000 51.55613  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.14392 17.35461 10.38718  1.000 44.35190  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.98381 17.58707 18.92736  1.000 51.73040  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.76397 17.66667 20.36903  1.000 61.29882  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 21.09286 17.37299 21.06333  1.000 59.11487  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 21.36583 16.25693 21.50471  1.000 59.23706  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.66506 16.69628 20.79856  1.000 57.13045  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.93259 18.40614 21.16341  1.000 55.88292  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 23.27778 18.27336 21.71102  1.000 63.37180  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 23.42811 18.94094 23.07370  1.000 57.38655  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 24.54586 19.27820 23.47229  1.000 67.22069  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 24.30579 18.83799 20.72924  1.000 58.81227  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.93342 20.21584 20.21986  1.000 63.49678  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.93243 20.78145 20.70599  1.000 61.51191  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.63896 20.72957 19.32504  1.000 64.03955  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 22.32983 19.13581 23.79537  1.000 55.07704  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 22.35811 19.68824 25.14095  1.000 64.43230  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.89078 18.63540 26.13474  1.000 61.40543  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.89292 17.94791 25.89930  1.000 63.54955  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 21.47479 20.93209 25.24422  1.000 69.28911  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 22.05158 22.12478 24.56276  0.700 70.41222  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.90491 22.47279 23.25434  0.700 68.45262  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.87132 23.13355 25.15865  0.700 73.87911  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.58379 23.64045 22.99582  0.700 66.58829  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 23.18587 24.06626 24.15063  0.700 80.79951  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 23.36993 23.33848 26.44807  0.700 76.87920  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.97575 25.18683 24.39302  0.700 79.47365  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 24.15229 24.44763 26.68657  0.700 76.39328  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 24.44836 25.35804 25.66554  0.700 84.66225  ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 22.61876 18.51007 27.24709  1.000 64.11402  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 22.21000 17.50451 28.21242  1.000 66.33289  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 21.12740 18.05567 29.13553  1.000 72.65731  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 21.04806 19.26945 29.35700  1.000 70.36299  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 23.40700 17.04247 29.03744  1.000 67.20053  ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 24.52997 16.45424 28.20315  1.000 73.28138  ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 25.61940 15.85508 29.07312  0.700 72.85488  ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 26.01767 16.75680 30.14753  0.600 75.89436  ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 26.81928 17.80175 29.99253  0.600 80.33926  ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 27.31440 18.12417 28.80884  0.600 83.17101  ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 27.12901 18.54444 31.05135  0.600 77.40573  ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 20.27350 17.17953 29.67213  1.000 66.12709  ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 19.19520 17.65758 30.55333  1.000 72.84793  ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 19.69355 18.39493 31.78341  1.000 81.40742  ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.96308 19.23182 32.32910  1.000 75.05015  ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 18.45786 16.36581 30.93296  1.000 63.37610  ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 18.75934 15.41975 29.82082  1.000 66.02052  ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 20.15690 15.74029 29.38517  1.000 64.70524  ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.91720 18.11295 32.23841  1.000 76.58231  ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 21.43892 18.78956 33.42085  1.000 82.59146  ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 21.67113 20.27344 33.16752  1.000 80.43169  ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.65893 21.07098 34.11202  1.000 88.56630  ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 22.73353 18.12067 33.87994  1.000 85.63891  ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.87744 20.66205 31.91175  1.000 82.24178  ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 22.13060 22.04900 31.54837  1.000 80.96146  ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.85094 22.83525 31.28426  1.000 77.59968  ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.92227 23.95191 30.76107  1.000 72.43996  ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 23.03671 22.10874 30.31561  1.000 85.77083  ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 24.22886 23.03775 30.45762  0.700 88.94894  ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 25.54830 22.31658 30.26930  0.600 89.99516  ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 25.53146 21.07757 30.11123  0.600 87.18117  ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 26.60167 22.98752 30.27865  0.600 93.38901  ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.68855 22.28425 31.64349  1.000 76.30351  ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 18.42301 22.93579 31.31486  1.000 80.56683  ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 18.24611 24.23796 32.08844  1.000 77.51576  ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.75678 25.23259 31.53714  1.000 78.78837  ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 17.25752 21.98526 31.58946  1.000 79.95538  ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.62803 24.25274 33.36770  1.000 75.11078  ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.48167 25.47234 34.15869  1.000 78.75282  ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.48382 26.53762 33.73042  1.000 77.73758  ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 19.15771 27.73109 33.71228  1.000 76.96143  ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.62887 25.16526 35.64589  1.000 78.93986  ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.47851 24.34577 36.18514  1.000 77.71483  ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 16.40680 24.32309 35.54138  1.000 84.65444  ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.64337 23.73014 37.25700  1.000 83.41926  ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.70887 26.13277 33.38685  1.000 70.44066  ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.63514 27.07242 32.77027  1.000 69.90846  ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 21.14183 27.52787 31.40348  1.000 86.82875  ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.53460 28.60460 30.94166  1.000 88.47109  ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 23.02378 26.44442 32.64423  1.000 68.76570  ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.27934 26.73841 30.75760  1.000 82.68261  ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.77429 27.09885 29.43910  1.000 76.60628  ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.74714 28.22046 29.53479  1.000 75.57994  ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.80437 29.18687 28.76660  1.000 74.69343  ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.17785 25.86495 28.75998  1.000 78.02246  ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 19.36939 25.71187 27.25353  1.000 70.79200  ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.75810 26.16733 26.85026  1.000 71.96060  ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 19.16015 24.25795 26.86364  1.000 72.37054  ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.79325 28.10603 30.46899  1.000 78.79671  ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.70706 29.08372 30.55291  1.000 76.26549  ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.24972 30.46939 30.90353  1.000 76.60133  ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.77621 31.48622 30.37998  1.000 79.54795  ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.63025 28.61745 31.55746  1.000 82.43352  ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.90336 27.36995 31.04886  1.000 79.68710  ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 16.23337 28.34525 32.91669  1.000 85.79000  ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.25132 30.53450 31.78832  1.000 83.05719  ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.82830 31.82256 32.17176  1.000 93.31353  ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.44234 32.52601 30.96998  1.000 81.33775  ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 19.14933 33.69688 30.69665  1.000 82.66742  ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.88636 31.62255 33.25954  1.000 82.17896  ? 88  LYS A CB  1 
ATOM   698  N N   . LEU A 1 89  ? 20.30442 31.81756 30.23802  1.000 88.60611  ? 89  LEU A N   1 
ATOM   699  C CA  . LEU A 1 89  ? 20.95073 32.40992 29.07430  1.000 77.63777  ? 89  LEU A CA  1 
ATOM   700  C C   . LEU A 1 89  ? 19.95979 32.63349 27.93608  1.000 89.36587  ? 89  LEU A C   1 
ATOM   701  O O   . LEU A 1 89  ? 20.11995 33.58220 27.15890  1.000 92.04989  ? 89  LEU A O   1 
ATOM   702  C CB  . LEU A 1 89  ? 22.11785 31.53089 28.62540  1.000 82.04200  ? 89  LEU A CB  1 
ATOM   703  N N   . LEU A 1 90  ? 18.92320 31.79311 27.83118  1.000 87.27092  ? 90  LEU A N   1 
ATOM   704  C CA  . LEU A 1 90  ? 17.83849 32.07225 26.88889  1.000 87.55431  ? 90  LEU A CA  1 
ATOM   705  C C   . LEU A 1 90  ? 17.10080 33.35604 27.25637  1.000 95.79766  ? 90  LEU A C   1 
ATOM   706  O O   . LEU A 1 90  ? 16.63190 34.08824 26.37300  1.000 95.89043  ? 90  LEU A O   1 
ATOM   707  C CB  . LEU A 1 90  ? 16.84430 30.90636 26.84992  1.000 83.20855  ? 90  LEU A CB  1 
ATOM   708  C CG  . LEU A 1 90  ? 16.71364 30.01036 25.61000  1.000 82.13751  ? 90  LEU A CG  1 
ATOM   709  C CD1 . LEU A 1 90  ? 17.50622 30.55764 24.43465  1.000 84.06255  ? 90  LEU A CD1 1 
ATOM   710  C CD2 . LEU A 1 90  ? 17.12851 28.57573 25.91919  1.000 78.13842  ? 90  LEU A CD2 1 
ATOM   711  N N   . ALA A 1 91  ? 16.98714 33.64303 28.55440  1.000 93.94806  ? 91  ALA A N   1 
ATOM   712  C CA  . ALA A 1 91  ? 16.23499 34.81519 28.99377  1.000 102.52220 ? 91  ALA A CA  1 
ATOM   713  C C   . ALA A 1 91  ? 17.01563 36.10074 28.74292  1.000 105.87425 ? 91  ALA A C   1 
ATOM   714  O O   . ALA A 1 91  ? 16.49557 37.05089 28.14312  1.000 107.56910 ? 91  ALA A O   1 
ATOM   715  C CB  . ALA A 1 91  ? 15.87219 34.68623 30.47280  1.000 105.98200 ? 91  ALA A CB  1 
ATOM   716  N N   . LYS A 1 92  ? 18.27124 36.14495 29.19667  1.000 108.78968 ? 92  LYS A N   1 
ATOM   717  C CA  . LYS A 1 92  ? 19.10991 37.31952 28.97194  1.000 109.86501 ? 92  LYS A CA  1 
ATOM   718  C C   . LYS A 1 92  ? 19.23820 37.63197 27.48654  1.000 112.48459 ? 92  LYS A C   1 
ATOM   719  O O   . LYS A 1 92  ? 19.26929 38.80298 27.08783  1.000 121.49183 ? 92  LYS A O   1 
ATOM   720  C CB  . LYS A 1 92  ? 20.49374 37.10320 29.58762  1.000 105.53057 ? 92  LYS A CB  1 
ATOM   721  C CG  . LYS A 1 92  ? 21.54884 38.08003 29.09278  1.000 111.37764 ? 92  LYS A CG  1 
ATOM   722  C CD  . LYS A 1 92  ? 22.95730 37.59525 29.38537  1.000 117.14696 ? 92  LYS A CD  1 
ATOM   723  C CE  . LYS A 1 92  ? 23.98663 38.43379 28.64347  1.000 119.41524 ? 92  LYS A CE  1 
ATOM   724  N NZ  . LYS A 1 92  ? 25.37780 37.99190 28.93578  1.000 117.16039 ? 92  LYS A NZ  1 
ATOM   725  N N   . GLY A 1 93  ? 19.29563 36.60038 26.65277  1.000 106.50735 ? 93  GLY A N   1 
ATOM   726  C CA  . GLY A 1 93  ? 19.54402 36.80061 25.24306  1.000 109.77441 ? 93  GLY A CA  1 
ATOM   727  C C   . GLY A 1 93  ? 21.02404 36.97213 24.98767  1.000 107.96741 ? 93  GLY A C   1 
ATOM   728  O O   . GLY A 1 93  ? 21.84297 36.27426 25.59374  1.000 98.14562  ? 93  GLY A O   1 
ATOM   729  N N   . GLU A 1 94  ? 21.38039 37.89570 24.09706  1.000 114.68541 ? 94  GLU A N   1 
ATOM   730  C CA  . GLU A 1 94  ? 22.76090 38.19394 23.72482  1.000 119.35723 ? 94  GLU A CA  1 
ATOM   731  C C   . GLU A 1 94  ? 23.51153 36.97321 23.20622  1.000 117.92155 ? 94  GLU A C   1 
ATOM   732  O O   . GLU A 1 94  ? 24.73466 37.03149 23.03114  1.000 122.73732 ? 94  GLU A O   1 
ATOM   733  C CB  . GLU A 1 94  ? 23.53354 38.82214 24.89297  1.000 115.10416 ? 94  GLU A CB  1 
ATOM   734  N N   . TYR A 1 95  ? 22.81418 35.86913 22.95916  1.000 107.30702 ? 95  TYR A N   1 
ATOM   735  C CA  . TYR A 1 95  ? 23.43840 34.67432 22.42283  1.000 101.88937 ? 95  TYR A CA  1 
ATOM   736  C C   . TYR A 1 95  ? 23.70348 34.84093 20.93059  1.000 102.04400 ? 95  TYR A C   1 
ATOM   737  O O   . TYR A 1 95  ? 23.15547 35.72623 20.26807  1.000 103.63736 ? 95  TYR A O   1 
ATOM   738  C CB  . TYR A 1 95  ? 22.55511 33.44888 22.66757  1.000 95.42445  ? 95  TYR A CB  1 
ATOM   739  C CG  . TYR A 1 95  ? 21.12857 33.60311 22.18034  1.000 92.34755  ? 95  TYR A CG  1 
ATOM   740  C CD1 . TYR A 1 95  ? 20.78385 33.30209 20.86842  1.000 85.85282  ? 95  TYR A CD1 1 
ATOM   741  C CD2 . TYR A 1 95  ? 20.12562 34.04408 23.03505  1.000 97.85048  ? 95  TYR A CD2 1 
ATOM   742  C CE1 . TYR A 1 95  ? 19.48278 33.44139 20.42031  1.000 82.11519  ? 95  TYR A CE1 1 
ATOM   743  C CE2 . TYR A 1 95  ? 18.82166 34.18586 22.59562  1.000 97.16785  ? 95  TYR A CE2 1 
ATOM   744  C CZ  . TYR A 1 95  ? 18.50670 33.88295 21.28780  1.000 87.16671  ? 95  TYR A CZ  1 
ATOM   745  O OH  . TYR A 1 95  ? 17.21075 34.02185 20.84632  1.000 92.91105  ? 95  TYR A OH  1 
ATOM   746  N N   . GLN A 1 96  ? 24.56072 33.97607 20.40464  1.000 95.10610  ? 96  GLN A N   1 
ATOM   747  C CA  . GLN A 1 96  ? 24.84904 33.94589 18.98041  1.000 88.72976  ? 96  GLN A CA  1 
ATOM   748  C C   . GLN A 1 96  ? 24.01326 32.87523 18.29126  1.000 83.45226  ? 96  GLN A C   1 
ATOM   749  O O   . GLN A 1 96  ? 23.54704 31.91711 18.91252  1.000 78.21641  ? 96  GLN A O   1 
ATOM   750  C CB  . GLN A 1 96  ? 26.33656 33.69225 18.72496  1.000 89.85930  ? 96  GLN A CB  1 
ATOM   751  C CG  . GLN A 1 96  ? 27.15198 34.95672 18.53309  0.800 95.86880  ? 96  GLN A CG  1 
ATOM   752  C CD  . GLN A 1 96  ? 28.50617 34.68514 17.91103  0.700 104.48174 ? 96  GLN A CD  1 
ATOM   753  O OE1 . GLN A 1 96  ? 29.00998 33.56303 17.95724  0.700 98.85392  ? 96  GLN A OE1 1 
ATOM   754  N NE2 . GLN A 1 96  ? 29.09995 35.71282 17.31562  0.700 110.02645 ? 96  GLN A NE2 1 
ATOM   755  N N   . LYS A 1 97  ? 23.82525 33.05603 16.98839  1.000 73.58631  ? 97  LYS A N   1 
ATOM   756  C CA  . LYS A 1 97  ? 23.09359 32.11190 16.15952  1.000 69.51581  ? 97  LYS A CA  1 
ATOM   757  C C   . LYS A 1 97  ? 24.03372 31.49283 15.13486  1.000 70.40763  ? 97  LYS A C   1 
ATOM   758  O O   . LYS A 1 97  ? 24.86619 32.18806 14.54423  1.000 72.05633  ? 97  LYS A O   1 
ATOM   759  C CB  . LYS A 1 97  ? 21.92507 32.79305 15.43931  1.000 69.97679  ? 97  LYS A CB  1 
ATOM   760  C CG  . LYS A 1 97  ? 21.04316 33.66019 16.32476  1.000 70.46228  ? 97  LYS A CG  1 
ATOM   761  C CD  . LYS A 1 97  ? 19.80014 34.11471 15.57120  1.000 69.69977  ? 97  LYS A CD  1 
ATOM   762  C CE  . LYS A 1 97  ? 19.01024 35.15159 16.35408  1.000 72.31037  ? 97  LYS A CE  1 
ATOM   763  N NZ  . LYS A 1 97  ? 19.69622 36.47319 16.37932  1.000 73.02863  ? 97  LYS A NZ  1 
ATOM   764  N N   . VAL A 1 98  ? 23.90405 30.18419 14.93102  1.000 62.54088  ? 98  VAL A N   1 
ATOM   765  C CA  . VAL A 1 98  ? 24.59581 29.49885 13.84785  1.000 61.23507  ? 98  VAL A CA  1 
ATOM   766  C C   . VAL A 1 98  ? 23.54821 28.96736 12.88256  1.000 60.47949  ? 98  VAL A C   1 
ATOM   767  O O   . VAL A 1 98  ? 22.42272 28.63877 13.27308  1.000 60.90140  ? 98  VAL A O   1 
ATOM   768  C CB  . VAL A 1 98  ? 25.51581 28.36098 14.34507  1.000 66.36115  ? 98  VAL A CB  1 
ATOM   769  C CG1 . VAL A 1 98  ? 26.38170 28.85030 15.48106  1.000 72.66651  ? 98  VAL A CG1 1 
ATOM   770  C CG2 . VAL A 1 98  ? 24.70880 27.14246 14.76485  1.000 63.51679  ? 98  VAL A CG2 1 
ATOM   771  N N   . SER A 1 99  ? 23.92133 28.89635 11.60880  1.000 60.69801  ? 99  SER A N   1 
ATOM   772  C CA  . SER A 1 99  ? 22.99043 28.52969 10.55435  1.000 57.89638  ? 99  SER A CA  1 
ATOM   773  C C   . SER A 1 99  ? 23.53445 27.35586 9.75666   1.000 48.51585  ? 99  SER A C   1 
ATOM   774  O O   . SER A 1 99  ? 24.72375 27.31298 9.42780   1.000 50.80971  ? 99  SER A O   1 
ATOM   775  C CB  . SER A 1 99  ? 22.71609 29.71755 9.62365   1.000 59.76682  ? 99  SER A CB  1 
ATOM   776  O OG  . SER A 1 99  ? 22.15501 30.80521 10.33982  1.000 60.37681  ? 99  SER A OG  1 
ATOM   777  N N   . TYR A 1 100 ? 22.65205 26.40268 9.45427   1.000 49.43774  ? 100 TYR A N   1 
ATOM   778  C CA  . TYR A 1 100 ? 22.96928 25.24522 8.63941   1.000 50.50045  ? 100 TYR A CA  1 
ATOM   779  C C   . TYR A 1 100 ? 22.16712 25.27940 7.34387   1.000 56.14223  ? 100 TYR A C   1 
ATOM   780  O O   . TYR A 1 100 ? 21.01474 25.72544 7.34331   1.000 54.73326  ? 100 TYR A O   1 
ATOM   781  C CB  . TYR A 1 100 ? 22.67067 23.93456 9.38411   1.000 45.02591  ? 100 TYR A CB  1 
ATOM   782  C CG  . TYR A 1 100 ? 23.68258 23.56113 10.44517  1.000 51.21783  ? 100 TYR A CG  1 
ATOM   783  C CD1 . TYR A 1 100 ? 24.74941 24.39823 10.75103  1.000 52.87614  ? 100 TYR A CD1 1 
ATOM   784  C CD2 . TYR A 1 100 ? 23.57619 22.35884 11.13141  1.000 42.98954  ? 100 TYR A CD2 1 
ATOM   785  C CE1 . TYR A 1 100 ? 25.67361 24.05222 11.72056  1.000 47.05619  ? 100 TYR A CE1 1 
ATOM   786  C CE2 . TYR A 1 100 ? 24.49549 22.00255 12.09709  1.000 47.72071  ? 100 TYR A CE2 1 
ATOM   787  C CZ  . TYR A 1 100 ? 25.54191 22.85123 12.38759  1.000 56.39689  ? 100 TYR A CZ  1 
ATOM   788  O OH  . TYR A 1 100 ? 26.45553 22.49309 13.35153  1.000 56.60654  ? 100 TYR A OH  1 
ATOM   789  N N   . PRO A 1 101 ? 22.74008 24.82298 6.23316   1.000 46.69210  ? 101 PRO A N   1 
ATOM   790  C CA  . PRO A 1 101 ? 22.00298 24.83012 4.96632   1.000 53.00984  ? 101 PRO A CA  1 
ATOM   791  C C   . PRO A 1 101 ? 20.87378 23.81173 4.96939   1.000 51.16970  ? 101 PRO A C   1 
ATOM   792  O O   . PRO A 1 101 ? 20.87614 22.83207 5.71791   1.000 46.82257  ? 101 PRO A O   1 
ATOM   793  C CB  . PRO A 1 101 ? 23.06910 24.46483 3.92535   1.000 47.66128  ? 101 PRO A CB  1 
ATOM   794  C CG  . PRO A 1 101 ? 24.38560 24.68157 4.60885   1.000 45.71824  ? 101 PRO A CG  1 
ATOM   795  C CD  . PRO A 1 101 ? 24.13362 24.39139 6.05507   1.000 49.46611  ? 101 PRO A CD  1 
ATOM   796  N N   . LEU A 1 102 ? 19.89525 24.06227 4.10732   1.000 51.68867  ? 102 LEU A N   1 
ATOM   797  C CA  . LEU A 1 102 ? 18.74884 23.18712 3.93225   1.000 51.40626  ? 102 LEU A CA  1 
ATOM   798  C C   . LEU A 1 102 ? 18.63912 22.78135 2.46853   1.000 46.11091  ? 102 LEU A C   1 
ATOM   799  O O   . LEU A 1 102 ? 19.27276 23.36615 1.58621   1.000 46.61674  ? 102 LEU A O   1 
ATOM   800  C CB  . LEU A 1 102 ? 17.45648 23.87090 4.39718   1.000 46.72092  ? 102 LEU A CB  1 
ATOM   801  C CG  . LEU A 1 102 ? 17.46168 24.45870 5.80958   1.000 54.66687  ? 102 LEU A CG  1 
ATOM   802  C CD1 . LEU A 1 102 ? 16.25396 25.35335 6.01813   1.000 49.48401  ? 102 LEU A CD1 1 
ATOM   803  C CD2 . LEU A 1 102 ? 17.49359 23.35182 6.84977   1.000 41.66914  ? 102 LEU A CD2 1 
ATOM   804  N N   . LEU A 1 103 ? 17.81942 21.76598 2.21614   1.000 46.69227  ? 103 LEU A N   1 
ATOM   805  C CA  . LEU A 1 103 ? 17.61174 21.23542 0.87624   1.000 48.73820  ? 103 LEU A CA  1 
ATOM   806  C C   . LEU A 1 103 ? 16.18972 21.53320 0.42564   1.000 54.42614  ? 103 LEU A C   1 
ATOM   807  O O   . LEU A 1 103 ? 15.23183 21.23152 1.14568   1.000 57.04908  ? 103 LEU A O   1 
ATOM   808  C CB  . LEU A 1 103 ? 17.87032 19.72805 0.84194   1.000 49.62189  ? 103 LEU A CB  1 
ATOM   809  C CG  . LEU A 1 103 ? 17.44426 18.99404 -0.43297  1.000 45.08923  ? 103 LEU A CG  1 
ATOM   810  C CD1 . LEU A 1 103 ? 18.38957 19.30049 -1.58599  1.000 39.39745  ? 103 LEU A CD1 1 
ATOM   811  C CD2 . LEU A 1 103 ? 17.34548 17.49542 -0.18657  1.000 42.70193  ? 103 LEU A CD2 1 
ATOM   812  N N   . LYS A 1 104 ? 16.05378 22.12528 -0.75734  1.000 54.97983  ? 104 LYS A N   1 
ATOM   813  C CA  . LYS A 1 104 ? 14.74804 22.36514 -1.35369  1.000 51.63554  ? 104 LYS A CA  1 
ATOM   814  C C   . LYS A 1 104 ? 14.43360 21.26110 -2.35241  1.000 50.54508  ? 104 LYS A C   1 
ATOM   815  O O   . LYS A 1 104 ? 15.25938 20.93724 -3.21289  1.000 45.21965  ? 104 LYS A O   1 
ATOM   816  C CB  . LYS A 1 104 ? 14.67749 23.72793 -2.04479  1.000 49.67732  ? 104 LYS A CB  1 
ATOM   817  C CG  . LYS A 1 104 ? 13.34638 23.95054 -2.75659  0.700 52.99671  ? 104 LYS A CG  1 
ATOM   818  C CD  . LYS A 1 104 ? 13.10095 25.40777 -3.11134  0.700 48.29086  ? 104 LYS A CD  1 
ATOM   819  C CE  . LYS A 1 104 ? 14.02409 25.88743 -4.21569  0.700 46.64571  ? 104 LYS A CE  1 
ATOM   820  N NZ  . LYS A 1 104 ? 13.66553 27.26187 -4.66939  0.600 72.08914  ? 104 LYS A NZ  1 
ATOM   821  N N   . THR A 1 105 ? 13.24057 20.68893 -2.23072  1.000 52.55187  ? 105 THR A N   1 
ATOM   822  C CA  . THR A 1 105 ? 12.74653 19.66767 -3.14105  1.000 56.53449  ? 105 THR A CA  1 
ATOM   823  C C   . THR A 1 105 ? 11.50616 20.19864 -3.84139  1.000 59.78425  ? 105 THR A C   1 
ATOM   824  O O   . THR A 1 105 ? 10.57899 20.67617 -3.18181  1.000 62.07066  ? 105 THR A O   1 
ATOM   825  C CB  . THR A 1 105 ? 12.41111 18.37639 -2.39126  1.000 53.79788  ? 105 THR A CB  1 
ATOM   826  O OG1 . THR A 1 105 ? 13.57387 17.90601 -1.69766  1.000 49.76032  ? 105 THR A OG1 1 
ATOM   827  C CG2 . THR A 1 105 ? 11.92829 17.30953 -3.36204  1.000 56.03727  ? 105 THR A CG2 1 
ATOM   828  N N   . THR A 1 106 ? 11.49132 20.12179 -5.16935  1.000 61.25298  ? 106 THR A N   1 
ATOM   829  C CA  . THR A 1 106 ? 10.33948 20.52151 -5.96662  1.000 63.64446  ? 106 THR A CA  1 
ATOM   830  C C   . THR A 1 106 ? 9.81575  19.30965 -6.72160  1.000 60.43806  ? 106 THR A C   1 
ATOM   831  O O   . THR A 1 106 ? 10.58656 18.60622 -7.38131  1.000 57.75121  ? 106 THR A O   1 
ATOM   832  C CB  . THR A 1 106 ? 10.69727 21.64313 -6.94676  1.000 63.62031  ? 106 THR A CB  1 
ATOM   833  O OG1 . THR A 1 106 ? 11.19105 22.77705 -6.22170  1.000 58.76690  ? 106 THR A OG1 1 
ATOM   834  C CG2 . THR A 1 106 ? 9.47106  22.06115 -7.74859  1.000 52.52316  ? 106 THR A CG2 1 
ATOM   835  N N   . VAL A 1 107 ? 8.51218  19.06522 -6.61731  1.000 62.24725  ? 107 VAL A N   1 
ATOM   836  C CA  . VAL A 1 107 ? 7.86214  17.92635 -7.25645  1.000 67.86973  ? 107 VAL A CA  1 
ATOM   837  C C   . VAL A 1 107 ? 6.81942  18.46374 -8.22623  1.000 73.42073  ? 107 VAL A C   1 
ATOM   838  O O   . VAL A 1 107 ? 5.91635  19.20759 -7.82327  1.000 68.32027  ? 107 VAL A O   1 
ATOM   839  C CB  . VAL A 1 107 ? 7.22072  16.98376 -6.22618  1.000 65.69572  ? 107 VAL A CB  1 
ATOM   840  C CG1 . VAL A 1 107 ? 6.55497  15.80927 -6.92416  1.000 72.64071  ? 107 VAL A CG1 1 
ATOM   841  C CG2 . VAL A 1 107 ? 8.26372  16.49833 -5.22924  1.000 63.28860  ? 107 VAL A CG2 1 
ATOM   842  N N   . LYS A 1 108 ? 6.93964  18.08647 -9.49643  1.000 77.74392  ? 108 LYS A N   1 
ATOM   843  C CA  . LYS A 1 108 ? 6.05427  18.57636 -10.54172 1.000 74.94204  ? 108 LYS A CA  1 
ATOM   844  C C   . LYS A 1 108 ? 5.02378  17.51997 -10.92228 1.000 88.43629  ? 108 LYS A C   1 
ATOM   845  O O   . LYS A 1 108 ? 5.27177  16.31609 -10.82132 1.000 93.53743  ? 108 LYS A O   1 
ATOM   846  C CB  . LYS A 1 108 ? 6.84995  18.99232 -11.78026 1.000 77.78213  ? 108 LYS A CB  1 
ATOM   847  N N   . TYR A 1 109 ? 3.85862  17.98802 -11.36422 1.000 107.90883 ? 109 TYR A N   1 
ATOM   848  C CA  . TYR A 1 109 ? 2.77790  17.12806 -11.82417 1.000 105.57421 ? 109 TYR A CA  1 
ATOM   849  C C   . TYR A 1 109 ? 2.31635  17.59672 -13.19898 1.000 111.90262 ? 109 TYR A C   1 
ATOM   850  O O   . TYR A 1 109 ? 2.85101  18.55196 -13.77062 1.000 116.90454 ? 109 TYR A O   1 
ATOM   851  C CB  . TYR A 1 109 ? 1.59801  17.12778 -10.84279 1.000 104.57901 ? 109 TYR A CB  1 
ATOM   852  C CG  . TYR A 1 109 ? 1.96146  16.80745 -9.41397  1.000 115.71514 ? 109 TYR A CG  1 
ATOM   853  C CD1 . TYR A 1 109 ? 2.19156  15.49946 -9.00945  1.000 115.60887 ? 109 TYR A CD1 1 
ATOM   854  C CD2 . TYR A 1 109 ? 2.05371  17.81361 -8.46255  1.000 119.22171 ? 109 TYR A CD2 1 
ATOM   855  C CE1 . TYR A 1 109 ? 2.51572  15.20520 -7.69869  1.000 121.97611 ? 109 TYR A CE1 1 
ATOM   856  C CE2 . TYR A 1 109 ? 2.37676  17.52998 -7.15206  1.000 108.61422 ? 109 TYR A CE2 1 
ATOM   857  C CZ  . TYR A 1 109 ? 2.60667  16.22525 -6.77524  1.000 113.93469 ? 109 TYR A CZ  1 
ATOM   858  O OH  . TYR A 1 109 ? 2.92780  15.94346 -5.46809  1.000 115.05428 ? 109 TYR A OH  1 
ATOM   859  N N   . GLY A 1 110 ? 1.30277  16.91755 -13.72491 1.000 108.11331 ? 110 GLY A N   1 
ATOM   860  C CA  . GLY A 1 110 ? 0.72084  17.27732 -15.00305 1.000 97.18099  ? 110 GLY A CA  1 
ATOM   861  C C   . GLY A 1 110 ? -0.79146 17.35426 -14.95065 1.000 91.27587  ? 110 GLY A C   1 
ATOM   862  O O   . GLY A 1 110 ? -1.41267 18.10119 -15.70498 1.000 78.02228  ? 110 GLY A O   1 
ATOM   863  N N   . LYS A 1 114 ? 1.57138  20.73410 -12.06801 1.000 96.43341  ? 114 LYS A N   1 
ATOM   864  C CA  . LYS A 1 114 ? 1.56854  21.52663 -10.84349 1.000 99.92772  ? 114 LYS A CA  1 
ATOM   865  C C   . LYS A 1 114 ? 2.79914  21.19638 -10.00212 1.000 98.31413  ? 114 LYS A C   1 
ATOM   866  O O   . LYS A 1 114 ? 3.36254  20.11189 -10.12791 1.000 104.40852 ? 114 LYS A O   1 
ATOM   867  C CB  . LYS A 1 114 ? 0.28561  21.27579 -10.04852 1.000 99.07369  ? 114 LYS A CB  1 
ATOM   868  C CG  . LYS A 1 114 ? -0.04868 22.36316 -9.04234  1.000 102.99652 ? 114 LYS A CG  1 
ATOM   869  C CD  . LYS A 1 114 ? -1.36585 22.07738 -8.34122  1.000 114.82269 ? 114 LYS A CD  1 
ATOM   870  C CE  . LYS A 1 114 ? -2.51488 21.99010 -9.33299  1.000 120.41684 ? 114 LYS A CE  1 
ATOM   871  N NZ  . LYS A 1 114 ? -3.82552 21.83008 -8.64392  1.000 105.17331 ? 114 LYS A NZ  1 
ATOM   872  N N   . GLU A 1 115 ? 3.21654  22.12729 -9.14462  1.000 78.85170  ? 115 GLU A N   1 
ATOM   873  C CA  . GLU A 1 115 ? 4.44483  21.97425 -8.37774  1.000 80.00108  ? 115 GLU A CA  1 
ATOM   874  C C   . GLU A 1 115 ? 4.17819  22.11564 -6.88645  1.000 77.06536  ? 115 GLU A C   1 
ATOM   875  O O   . GLU A 1 115 ? 3.41237  22.98428 -6.45732  1.000 80.39887  ? 115 GLU A O   1 
ATOM   876  C CB  . GLU A 1 115 ? 5.50228  22.99652 -8.80982  1.000 66.28477  ? 115 GLU A CB  1 
ATOM   877  C CG  . GLU A 1 115 ? 6.17028  22.67064 -10.13350 1.000 80.67442  ? 115 GLU A CG  1 
ATOM   878  C CD  . GLU A 1 115 ? 7.30858  23.61606 -10.46103 1.000 82.45761  ? 115 GLU A CD  1 
ATOM   879  O OE1 . GLU A 1 115 ? 7.60949  24.49624 -9.62790  1.000 88.53922  ? 115 GLU A OE1 1 
ATOM   880  O OE2 . GLU A 1 115 ? 7.90169  23.47874 -11.55144 1.000 85.26763  ? 115 GLU A OE2 1 
ATOM   881  N N   . ALA A 1 116 ? 4.82507  21.25360 -6.10419  1.000 78.35399  ? 116 ALA A N   1 
ATOM   882  C CA  . ALA A 1 116 ? 4.80691  21.31602 -4.64928  1.000 68.72140  ? 116 ALA A CA  1 
ATOM   883  C C   . ALA A 1 116 ? 6.24209  21.24643 -4.15238  1.000 68.38998  ? 116 ALA A C   1 
ATOM   884  O O   . ALA A 1 116 ? 7.00593  20.37468 -4.58005  1.000 65.16594  ? 116 ALA A O   1 
ATOM   885  C CB  . ALA A 1 116 ? 3.97525  20.17765 -4.04855  1.000 70.69508  ? 116 ALA A CB  1 
ATOM   886  N N   . THR A 1 117 ? 6.60923  22.16323 -3.26024  1.000 64.97481  ? 117 THR A N   1 
ATOM   887  C CA  . THR A 1 117 ? 7.97784  22.27512 -2.78056  1.000 71.38764  ? 117 THR A CA  1 
ATOM   888  C C   . THR A 1 117 ? 8.04972  21.96043 -1.29249  1.000 68.00699  ? 117 THR A C   1 
ATOM   889  O O   . THR A 1 117 ? 7.10069  22.20270 -0.54075  1.000 60.36602  ? 117 THR A O   1 
ATOM   890  C CB  . THR A 1 117 ? 8.55047  23.67447 -3.03930  1.000 70.47388  ? 117 THR A CB  1 
ATOM   891  O OG1 . THR A 1 117 ? 7.87122  24.63284 -2.21848  1.000 80.55356  ? 117 THR A OG1 1 
ATOM   892  C CG2 . THR A 1 117 ? 8.37942  24.05575 -4.50230  1.000 67.62630  ? 117 THR A CG2 1 
ATOM   893  N N   . TYR A 1 118 ? 9.19229  21.41867 -0.87463  1.000 69.05869  ? 118 TYR A N   1 
ATOM   894  C CA  . TYR A 1 118 ? 9.40403  21.02631 0.51019   1.000 61.19311  ? 118 TYR A CA  1 
ATOM   895  C C   . TYR A 1 118 ? 10.80630 21.42882 0.94239   1.000 59.37326  ? 118 TYR A C   1 
ATOM   896  O O   . TYR A 1 118 ? 11.69145 21.66749 0.11650   1.000 52.93461  ? 118 TYR A O   1 
ATOM   897  C CB  . TYR A 1 118 ? 9.21153  19.51600 0.71101   1.000 55.90776  ? 118 TYR A CB  1 
ATOM   898  C CG  . TYR A 1 118 ? 7.89974  18.98179 0.18379   1.000 63.73963  ? 118 TYR A CG  1 
ATOM   899  C CD1 . TYR A 1 118 ? 7.76427  18.61534 -1.14835  1.000 61.68799  ? 118 TYR A CD1 1 
ATOM   900  C CD2 . TYR A 1 118 ? 6.80005  18.83516 1.01887   1.000 64.05506  ? 118 TYR A CD2 1 
ATOM   901  C CE1 . TYR A 1 118 ? 6.57037  18.12555 -1.63707  1.000 68.48169  ? 118 TYR A CE1 1 
ATOM   902  C CE2 . TYR A 1 118 ? 5.60117  18.34471 0.54009   1.000 76.42466  ? 118 TYR A CE2 1 
ATOM   903  C CZ  . TYR A 1 118 ? 5.49253  17.99130 -0.78978  1.000 73.38783  ? 118 TYR A CZ  1 
ATOM   904  O OH  . TYR A 1 118 ? 4.30326  17.50168 -1.27599  1.000 83.05571  ? 118 TYR A OH  1 
ATOM   905  N N   . LEU A 1 119 ? 10.99721 21.49321 2.25780   1.000 54.31491  ? 119 LEU A N   1 
ATOM   906  C CA  . LEU A 1 119 ? 12.27756 21.82844 2.86463   1.000 49.09366  ? 119 LEU A CA  1 
ATOM   907  C C   . LEU A 1 119 ? 12.71232 20.67933 3.76083   1.000 46.95914  ? 119 LEU A C   1 
ATOM   908  O O   . LEU A 1 119 ? 11.91397 20.17444 4.55693   1.000 55.46737  ? 119 LEU A O   1 
ATOM   909  C CB  . LEU A 1 119 ? 12.17614 23.12563 3.66881   1.000 52.32250  ? 119 LEU A CB  1 
ATOM   910  C CG  . LEU A 1 119 ? 13.19608 24.22123 3.35885   1.000 55.16534  ? 119 LEU A CG  1 
ATOM   911  C CD1 . LEU A 1 119 ? 13.25107 24.50771 1.86725   1.000 60.26510  ? 119 LEU A CD1 1 
ATOM   912  C CD2 . LEU A 1 119 ? 12.84817 25.47933 4.13378   1.000 60.08173  ? 119 LEU A CD2 1 
ATOM   913  N N   . ALA A 1 120 ? 13.97165 20.26948 3.63275   1.000 41.91126  ? 120 ALA A N   1 
ATOM   914  C CA  . ALA A 1 120 ? 14.50695 19.14168 4.38170   1.000 47.03204  ? 120 ALA A CA  1 
ATOM   915  C C   . ALA A 1 120 ? 15.72663 19.56893 5.18601   1.000 44.92683  ? 120 ALA A C   1 
ATOM   916  O O   . ALA A 1 120 ? 16.58992 20.29949 4.68699   1.000 43.53679  ? 120 ALA A O   1 
ATOM   917  C CB  . ALA A 1 120 ? 14.88235 17.98379 3.45103   1.000 38.03457  ? 120 ALA A CB  1 
ATOM   918  N N   . LEU A 1 121 ? 15.78803 19.10623 6.43458   1.000 42.15525  ? 121 LEU A N   1 
ATOM   919  C CA  . LEU A 1 121 ? 16.94910 19.30418 7.29185   1.000 40.01812  ? 121 LEU A CA  1 
ATOM   920  C C   . LEU A 1 121 ? 17.92494 18.13789 7.24098   1.000 44.89205  ? 121 LEU A C   1 
ATOM   921  O O   . LEU A 1 121 ? 19.13618 18.35114 7.36339   1.000 43.46048  ? 121 LEU A O   1 
ATOM   922  C CB  . LEU A 1 121 ? 16.50123 19.52934 8.74078   1.000 49.04191  ? 121 LEU A CB  1 
ATOM   923  C CG  . LEU A 1 121 ? 17.56603 19.71833 9.82355   1.000 41.11853  ? 121 LEU A CG  1 
ATOM   924  C CD1 . LEU A 1 121 ? 18.39099 20.97151 9.57135   1.000 32.08505  ? 121 LEU A CD1 1 
ATOM   925  C CD2 . LEU A 1 121 ? 16.91593 19.76837 11.19779  1.000 49.25786  ? 121 LEU A CD2 1 
ATOM   926  N N   . ASN A 1 122 ? 17.42587 16.91434 7.05805   1.000 40.23608  ? 122 ASN A N   1 
ATOM   927  C CA  . ASN A 1 122 ? 18.28113 15.74337 6.91429   1.000 44.15335  ? 122 ASN A CA  1 
ATOM   928  C C   . ASN A 1 122 ? 18.49756 15.40976 5.44427   1.000 42.80164  ? 122 ASN A C   1 
ATOM   929  O O   . ASN A 1 122 ? 19.59915 15.59614 4.91778   1.000 46.03574  ? 122 ASN A O   1 
ATOM   930  C CB  . ASN A 1 122 ? 17.68140 14.54063 7.64728   1.000 40.60989  ? 122 ASN A CB  1 
ATOM   931  C CG  . ASN A 1 122 ? 18.28331 14.33625 9.02222   1.000 44.80081  ? 122 ASN A CG  1 
ATOM   932  O OD1 . ASN A 1 122 ? 19.02518 15.18280 9.51745   1.000 41.15014  ? 122 ASN A OD1 1 
ATOM   933  N ND2 . ASN A 1 122 ? 17.96678 13.20661 9.64661   1.000 42.87575  ? 122 ASN A ND2 1 
ATOM   934  N N   . GLU A 1 123 ? 17.45781 14.92319 4.77231   1.000 48.05186  ? 123 GLU A N   1 
ATOM   935  C CA  . GLU A 1 123 ? 17.59440 14.48178 3.39037   1.000 37.24444  ? 123 GLU A CA  1 
ATOM   936  C C   . GLU A 1 123 ? 16.21165 14.33615 2.77144   1.000 49.15916  ? 123 GLU A C   1 
ATOM   937  O O   . GLU A 1 123 ? 15.18723 14.39378 3.45798   1.000 41.13158  ? 123 GLU A O   1 
ATOM   938  C CB  . GLU A 1 123 ? 18.35597 13.15667 3.29437   1.000 36.11902  ? 123 GLU A CB  1 
ATOM   939  C CG  . GLU A 1 123 ? 17.53073 11.94321 3.69947   1.000 40.83660  ? 123 GLU A CG  1 
ATOM   940  C CD  . GLU A 1 123 ? 17.26144 11.89515 5.19401   1.000 46.91003  ? 123 GLU A CD  1 
ATOM   941  O OE1 . GLU A 1 123 ? 18.23832 11.82693 5.96715   1.000 35.67589  ? 123 GLU A OE1 1 
ATOM   942  O OE2 . GLU A 1 123 ? 16.07819 11.93569 5.58802   1.000 36.26740  ? 123 GLU A OE2 1 
ATOM   943  N N   . SER A 1 124 ? 16.20451 14.14927 1.45239   1.000 45.35876  ? 124 SER A N   1 
ATOM   944  C CA  . SER A 1 124 ? 15.02030 13.75419 0.70465   1.000 46.44011  ? 124 SER A CA  1 
ATOM   945  C C   . SER A 1 124 ? 15.39451 12.57183 -0.17326  1.000 46.05136  ? 124 SER A C   1 
ATOM   946  O O   . SER A 1 124 ? 16.42776 12.60242 -0.84919  1.000 47.09200  ? 124 SER A O   1 
ATOM   947  C CB  . SER A 1 124 ? 14.47520 14.90372 -0.14939  1.000 50.25527  ? 124 SER A CB  1 
ATOM   948  O OG  . SER A 1 124 ? 13.32642 14.49765 -0.87619  1.000 47.39844  ? 124 SER A OG  1 
ATOM   949  N N   . THR A 1 125 ? 14.56935 11.52864 -0.15244  1.000 45.20755  ? 125 THR A N   1 
ATOM   950  C CA  . THR A 1 125 ? 14.83814 10.31402 -0.90703  1.000 45.61110  ? 125 THR A CA  1 
ATOM   951  C C   . THR A 1 125 ? 13.67539 10.00534 -1.84006  1.000 51.17776  ? 125 THR A C   1 
ATOM   952  O O   . THR A 1 125 ? 12.51624 10.30477 -1.53671  1.000 51.60628  ? 125 THR A O   1 
ATOM   953  C CB  . THR A 1 125 ? 15.07824 9.10795  0.01577   1.000 36.93736  ? 125 THR A CB  1 
ATOM   954  O OG1 . THR A 1 125 ? 13.82569 8.62707  0.51727   1.000 48.29307  ? 125 THR A OG1 1 
ATOM   955  C CG2 . THR A 1 125 ? 15.97032 9.49472  1.18885   1.000 40.12837  ? 125 THR A CG2 1 
ATOM   956  N N   . VAL A 1 126 ? 14.00075 9.40159  -2.98049  1.000 53.50409  ? 126 VAL A N   1 
ATOM   957  C CA  . VAL A 1 126 ? 13.01692 8.91227  -3.93859  1.000 51.85222  ? 126 VAL A CA  1 
ATOM   958  C C   . VAL A 1 126 ? 13.20953 7.40790  -4.07258  1.000 48.51889  ? 126 VAL A C   1 
ATOM   959  O O   . VAL A 1 126 ? 14.32135 6.94785  -4.35258  1.000 51.19323  ? 126 VAL A O   1 
ATOM   960  C CB  . VAL A 1 126 ? 13.15593 9.60818  -5.30525  1.000 47.79035  ? 126 VAL A CB  1 
ATOM   961  C CG1 . VAL A 1 126 ? 12.03563 9.18317  -6.23199  1.000 55.91477  ? 126 VAL A CG1 1 
ATOM   962  C CG2 . VAL A 1 126 ? 13.17706 11.12292 -5.13890  1.000 47.62019  ? 126 VAL A CG2 1 
ATOM   963  N N   . LYS A 1 127 ? 12.13728 6.64292  -3.86140  1.000 50.48307  ? 127 LYS A N   1 
ATOM   964  C CA  . LYS A 1 127 ? 12.20425 5.18642  -3.92348  1.000 58.56414  ? 127 LYS A CA  1 
ATOM   965  C C   . LYS A 1 127 ? 11.01348 4.64824  -4.70232  1.000 72.93703  ? 127 LYS A C   1 
ATOM   966  O O   . LYS A 1 127 ? 9.97075  5.29436  -4.80724  1.000 71.23807  ? 127 LYS A O   1 
ATOM   967  C CB  . LYS A 1 127 ? 12.21244 4.54567  -2.53135  1.000 61.33032  ? 127 LYS A CB  1 
ATOM   968  C CG  . LYS A 1 127 ? 13.32350 4.99306  -1.61789  1.000 57.95517  ? 127 LYS A CG  1 
ATOM   969  C CD  . LYS A 1 127 ? 13.31868 4.14071  -0.36781  1.000 63.42610  ? 127 LYS A CD  1 
ATOM   970  C CE  . LYS A 1 127 ? 14.12374 4.77252  0.74375   1.000 64.37410  ? 127 LYS A CE  1 
ATOM   971  N NZ  . LYS A 1 127 ? 14.11202 3.90076  1.94529   1.000 56.99440  ? 127 LYS A NZ  1 
ATOM   972  N N   . SER A 1 128 ? 11.16932 3.43932  -5.22594  1.000 82.64357  ? 128 SER A N   1 
ATOM   973  C CA  . SER A 1 128 ? 10.10352 2.81507  -5.99467  1.000 94.16015  ? 128 SER A CA  1 
ATOM   974  C C   . SER A 1 128 ? 8.98004  2.32435  -5.09593  1.000 100.39177 ? 128 SER A C   1 
ATOM   975  O O   . SER A 1 128 ? 9.20646  1.94036  -3.94268  1.000 104.40794 ? 128 SER A O   1 
ATOM   976  C CB  . SER A 1 128 ? 10.65631 1.64740  -6.78935  1.000 90.98279  ? 128 SER A CB  1 
ATOM   977  O OG  . SER A 1 128 ? 11.80675 1.13330  -6.14489  1.000 93.50008  ? 128 SER A OG  1 
ATOM   978  N N   . SER A 1 129 ? 7.76393  2.34164  -5.64373  1.000 108.31932 ? 129 SER A N   1 
ATOM   979  C CA  . SER A 1 129 ? 6.61041  1.71452  -5.01512  1.000 120.50936 ? 129 SER A CA  1 
ATOM   980  C C   . SER A 1 129 ? 6.96728  0.28588  -4.61345  1.000 121.77820 ? 129 SER A C   1 
ATOM   981  O O   . SER A 1 129 ? 7.13616  -0.01460 -3.42663  1.000 118.64500 ? 129 SER A O   1 
ATOM   982  C CB  . SER A 1 129 ? 5.40277  1.72923  -5.96194  1.000 113.27022 ? 129 SER A CB  1 
ATOM   983  O OG  . SER A 1 129 ? 5.29031  2.95642  -6.66068  1.000 104.46792 ? 129 SER A OG  1 
ATOM   984  N N   A GLY A 1 130 ? 7.06335  -0.60195 -5.60069  0.500 125.98246 ? 130 GLY A N   1 
ATOM   985  N N   B GLY A 1 130 ? 7.16434  -0.57691 -5.60536  0.500 127.02194 ? 130 GLY A N   1 
ATOM   986  C CA  A GLY A 1 130 ? 7.51841  -1.95931 -5.38481  0.500 124.58869 ? 130 GLY A CA  1 
ATOM   987  C CA  B GLY A 1 130 ? 7.52357  -1.96469 -5.38900  0.500 124.70195 ? 130 GLY A CA  1 
ATOM   988  C C   A GLY A 1 130 ? 8.18881  -2.43116 -6.65301  0.500 118.77453 ? 130 GLY A C   1 
ATOM   989  C C   B GLY A 1 130 ? 9.01443  -2.25558 -5.42807  0.500 121.19174 ? 130 GLY A C   1 
ATOM   990  O O   A GLY A 1 130 ? 9.20378  -3.14047 -6.61287  0.500 119.66061 ? 130 GLY A O   1 
ATOM   991  O O   B GLY A 1 130 ? 9.70355  -2.10064 -4.41639  0.500 118.20644 ? 130 GLY A O   1 
ATOM   992  N N   A GLY A 1 131 ? 7.63792  -1.98996 -7.78760  0.500 105.33191 ? 131 GLY A N   1 
ATOM   993  N N   B GLY A 1 131 ? 9.52903  -2.67470 -6.58496  0.500 111.03513 ? 131 GLY A N   1 
ATOM   994  C CA  A GLY A 1 131 ? 8.17982  -2.33871 -9.06482  0.500 94.65912  ? 131 GLY A CA  1 
ATOM   995  C CA  B GLY A 1 131 ? 10.88133 -3.17939 -6.68198  0.500 94.54614  ? 131 GLY A CA  1 
ATOM   996  C C   A GLY A 1 131 ? 9.49894  -1.64666 -9.34361  0.500 91.38046  ? 131 GLY A C   1 
ATOM   997  C C   B GLY A 1 131 ? 11.89210 -2.17203 -7.19759  0.500 87.48462  ? 131 GLY A C   1 
ATOM   998  O O   A GLY A 1 131 ? 10.07146 -0.94761 -8.49857  0.500 92.93287  ? 131 GLY A O   1 
ATOM   999  O O   B GLY A 1 131 ? 12.00345 -1.05327 -6.69052  0.500 86.49772  ? 131 GLY A O   1 
ATOM   1000 N N   A PRO A 1 132 ? 9.98930  -1.82430 -10.56229 0.500 67.01719  ? 132 PRO A N   1 
ATOM   1001 N N   B PRO A 1 132 ? 12.68037 -2.56606 -8.19750  0.500 66.81693  ? 132 PRO A N   1 
ATOM   1002 C CA  A PRO A 1 132 ? 11.35472 -1.39957 -10.86938 0.500 67.59472  ? 132 PRO A CA  1 
ATOM   1003 C CA  B PRO A 1 132 ? 13.65048 -1.62763 -8.77453  0.500 60.43542  ? 132 PRO A CA  1 
ATOM   1004 C C   A PRO A 1 132 ? 11.48863 0.11794  -10.82557 0.500 67.22758  ? 132 PRO A C   1 
ATOM   1005 C C   B PRO A 1 132 ? 12.96667 -0.64029 -9.70992  0.500 60.67276  ? 132 PRO A C   1 
ATOM   1006 O O   A PRO A 1 132 ? 10.58744 0.85172  -11.22708 0.500 69.26902  ? 132 PRO A O   1 
ATOM   1007 O O   B PRO A 1 132 ? 12.09481 -1.01328 -10.49800 0.500 65.46196  ? 132 PRO A O   1 
ATOM   1008 C CB  A PRO A 1 132 ? 11.58012 -1.95260 -12.27604 0.500 61.39959  ? 132 PRO A CB  1 
ATOM   1009 C CB  B PRO A 1 132 ? 14.62062 -2.54258 -9.53218  0.500 57.66862  ? 132 PRO A CB  1 
ATOM   1010 C CG  A PRO A 1 132 ? 10.22168 -1.91948 -12.89904 0.500 65.46174  ? 132 PRO A CG  1 
ATOM   1011 C CG  B PRO A 1 132 ? 13.80239 -3.74486 -9.86913  0.500 57.94866  ? 132 PRO A CG  1 
ATOM   1012 C CD  A PRO A 1 132 ? 9.23667  -2.17201 -11.77654 0.500 68.12961  ? 132 PRO A CD  1 
ATOM   1013 C CD  B PRO A 1 132 ? 12.85802 -3.93487 -8.71261  0.500 62.78009  ? 132 PRO A CD  1 
ATOM   1014 N N   A PHE A 1 133 ? 12.63481 0.58130  -10.33324 0.500 63.99723  ? 133 PHE A N   1 
ATOM   1015 N N   B PHE A 1 133 ? 13.36545 0.62835  -9.61791  0.500 61.12694  ? 133 PHE A N   1 
ATOM   1016 C CA  A PHE A 1 133 ? 12.89928 2.00930  -10.19982 0.500 62.44146  ? 133 PHE A CA  1 
ATOM   1017 C CA  B PHE A 1 133 ? 12.81853 1.66340  -10.48453 0.500 62.60801  ? 133 PHE A CA  1 
ATOM   1018 C C   A PHE A 1 133 ? 13.93283 2.41158  -11.24237 0.500 58.33977  ? 133 PHE A C   1 
ATOM   1019 C C   B PHE A 1 133 ? 13.91888 2.30666  -11.31647 0.500 58.32395  ? 133 PHE A C   1 
ATOM   1020 O O   A PHE A 1 133 ? 15.10799 2.04801  -11.13136 0.500 54.61723  ? 133 PHE A O   1 
ATOM   1021 O O   B PHE A 1 133 ? 15.11381 2.06935  -11.10931 0.500 55.10929  ? 133 PHE A O   1 
ATOM   1022 C CB  A PHE A 1 133 ? 13.38130 2.35396  -8.79335  0.500 61.90422  ? 133 PHE A CB  1 
ATOM   1023 C CB  B PHE A 1 133 ? 12.04294 2.73002  -9.69059  0.500 62.34154  ? 133 PHE A CB  1 
ATOM   1024 C CG  A PHE A 1 133 ? 13.42961 3.82745  -8.52323  0.500 59.87557  ? 133 PHE A CG  1 
ATOM   1025 C CG  B PHE A 1 133 ? 12.89260 3.79379  -9.02462  0.500 61.71231  ? 133 PHE A CG  1 
ATOM   1026 C CD1 A PHE A 1 133 ? 12.27851 4.59007  -8.60797  0.500 63.81087  ? 133 PHE A CD1 1 
ATOM   1027 C CD1 B PHE A 1 133 ? 14.17607 3.54406  -8.55439  0.500 59.17593  ? 133 PHE A CD1 1 
ATOM   1028 C CD2 A PHE A 1 133 ? 14.61960 4.45240  -8.19068  0.500 59.42861  ? 133 PHE A CD2 1 
ATOM   1029 C CD2 B PHE A 1 133 ? 12.36174 5.05911  -8.83993  0.500 64.49999  ? 133 PHE A CD2 1 
ATOM   1030 C CE1 A PHE A 1 133 ? 12.30760 5.94790  -8.36915  0.500 65.13350  ? 133 PHE A CE1 1 
ATOM   1031 C CE1 B PHE A 1 133 ? 14.91445 4.55355  -7.93937  0.500 59.04435  ? 133 PHE A CE1 1 
ATOM   1032 C CE2 A PHE A 1 133 ? 14.65708 5.81364  -7.94862  0.500 58.53008  ? 133 PHE A CE2 1 
ATOM   1033 C CE2 B PHE A 1 133 ? 13.08652 6.06240  -8.22051  0.500 62.98910  ? 133 PHE A CE2 1 
ATOM   1034 C CZ  A PHE A 1 133 ? 13.50038 6.56250  -8.03748  0.500 61.29787  ? 133 PHE A CZ  1 
ATOM   1035 C CZ  B PHE A 1 133 ? 14.36434 5.81121  -7.76909  0.500 59.03275  ? 133 PHE A CZ  1 
ATOM   1036 N N   . VAL A 1 134 ? 13.48993 3.13682  -12.26390 1.000 55.82760  ? 134 VAL A N   1 
ATOM   1037 C CA  . VAL A 1 134 ? 14.37332 3.74769  -13.24604 1.000 51.78053  ? 134 VAL A CA  1 
ATOM   1038 C C   . VAL A 1 134 ? 14.08802 5.24175  -13.27809 1.000 58.49820  ? 134 VAL A C   1 
ATOM   1039 O O   . VAL A 1 134 ? 12.92737 5.65444  -13.38509 1.000 61.25398  ? 134 VAL A O   1 
ATOM   1040 C CB  . VAL A 1 134 ? 14.19211 3.13427  -14.64713 1.000 62.06767  ? 134 VAL A CB  1 
ATOM   1041 C CG1 . VAL A 1 134 ? 15.21837 3.70606  -15.59607 1.000 51.94751  ? 134 VAL A CG1 1 
ATOM   1042 C CG2 . VAL A 1 134 ? 14.30435 1.61549  -14.59260 1.000 59.40132  ? 134 VAL A CG2 1 
ATOM   1043 N N   . VAL A 1 135 ? 15.14219 6.04833  -13.18250 1.000 48.59135  ? 135 VAL A N   1 
ATOM   1044 C CA  . VAL A 1 135 ? 15.03134 7.49819  -13.29406 1.000 55.11583  ? 135 VAL A CA  1 
ATOM   1045 C C   . VAL A 1 135 ? 16.21912 8.02165  -14.08643 1.000 53.44079  ? 135 VAL A C   1 
ATOM   1046 O O   . VAL A 1 135 ? 17.34703 7.54262  -13.92800 1.000 51.84808  ? 135 VAL A O   1 
ATOM   1047 C CB  . VAL A 1 135 ? 14.95640 8.19093  -11.91565 1.000 56.18922  ? 135 VAL A CB  1 
ATOM   1048 C CG1 . VAL A 1 135 ? 13.58172 8.00532  -11.29226 1.000 65.71820  ? 135 VAL A CG1 1 
ATOM   1049 C CG2 . VAL A 1 135 ? 16.05055 7.67089  -10.98728 1.000 46.23939  ? 135 VAL A CG2 1 
ATOM   1050 N N   . ASP A 1 136 ? 15.96051 9.00072  -14.94910 1.000 54.00858  ? 136 ASP A N   1 
ATOM   1051 C CA  . ASP A 1 136 ? 17.03276 9.73606  -15.60156 1.000 50.49679  ? 136 ASP A CA  1 
ATOM   1052 C C   . ASP A 1 136 ? 17.48947 10.86624 -14.68960 1.000 49.89780  ? 136 ASP A C   1 
ATOM   1053 O O   . ASP A 1 136 ? 16.66823 11.63866 -14.18365 1.000 55.26059  ? 136 ASP A O   1 
ATOM   1054 C CB  . ASP A 1 136 ? 16.56943 10.28956 -16.94832 1.000 51.53915  ? 136 ASP A CB  1 
ATOM   1055 C CG  . ASP A 1 136 ? 16.53218 9.23179  -18.03377 1.000 54.00758  ? 136 ASP A CG  1 
ATOM   1056 O OD1 . ASP A 1 136 ? 17.37210 8.30724  -17.99839 1.000 53.21500  ? 136 ASP A OD1 1 
ATOM   1057 O OD2 . ASP A 1 136 ? 15.66397 9.32662  -18.92701 1.000 59.10289  ? 136 ASP A OD2 1 
ATOM   1058 N N   . VAL A 1 137 ? 18.79662 10.95360 -14.46930 1.000 46.16541  ? 137 VAL A N   1 
ATOM   1059 C CA  . VAL A 1 137 ? 19.37880 11.96364 -13.59524 1.000 52.56821  ? 137 VAL A CA  1 
ATOM   1060 C C   . VAL A 1 137 ? 19.94504 13.07514 -14.46419 1.000 48.28986  ? 137 VAL A C   1 
ATOM   1061 O O   . VAL A 1 137 ? 20.87072 12.85113 -15.25356 1.000 47.33098  ? 137 VAL A O   1 
ATOM   1062 C CB  . VAL A 1 137 ? 20.46052 11.36686 -12.68371 1.000 48.42981  ? 137 VAL A CB  1 
ATOM   1063 C CG1 . VAL A 1 137 ? 21.03580 12.44271 -11.77605 1.000 45.25757  ? 137 VAL A CG1 1 
ATOM   1064 C CG2 . VAL A 1 137 ? 19.88244 10.22564 -11.86592 1.000 41.08985  ? 137 VAL A CG2 1 
ATOM   1065 N N   . VAL A 1 138 ? 19.39289 14.27404 -14.31327 1.000 48.87771  ? 138 VAL A N   1 
ATOM   1066 C CA  . VAL A 1 138 ? 19.77839 15.43700 -15.10087 1.000 48.86464  ? 138 VAL A CA  1 
ATOM   1067 C C   . VAL A 1 138 ? 20.41734 16.45686 -14.17013 1.000 50.46020  ? 138 VAL A C   1 
ATOM   1068 O O   . VAL A 1 138 ? 19.81528 16.85179 -13.16373 1.000 46.13390  ? 138 VAL A O   1 
ATOM   1069 C CB  . VAL A 1 138 ? 18.56935 16.04004 -15.83525 1.000 50.70531  ? 138 VAL A CB  1 
ATOM   1070 C CG1 . VAL A 1 138 ? 18.99616 17.23004 -16.65231 1.000 40.29698  ? 138 VAL A CG1 1 
ATOM   1071 C CG2 . VAL A 1 138 ? 17.91428 14.99262 -16.72003 1.000 49.00926  ? 138 VAL A CG2 1 
ATOM   1072 N N   . ILE A 1 139 ? 21.63262 16.88005 -14.50433 1.000 47.61576  ? 139 ILE A N   1 
ATOM   1073 C CA  . ILE A 1 139 ? 22.38325 17.84568 -13.71152 1.000 42.85012  ? 139 ILE A CA  1 
ATOM   1074 C C   . ILE A 1 139 ? 22.52816 19.11185 -14.54230 1.000 44.16798  ? 139 ILE A C   1 
ATOM   1075 O O   . ILE A 1 139 ? 23.26240 19.12852 -15.53876 1.000 42.04349  ? 139 ILE A O   1 
ATOM   1076 C CB  . ILE A 1 139 ? 23.75463 17.30023 -13.29342 1.000 45.86024  ? 139 ILE A CB  1 
ATOM   1077 C CG1 . ILE A 1 139 ? 23.59488 16.03833 -12.44401 1.000 43.04927  ? 139 ILE A CG1 1 
ATOM   1078 C CG2 . ILE A 1 139 ? 24.53470 18.36150 -12.53496 1.000 42.17700  ? 139 ILE A CG2 1 
ATOM   1079 C CD1 . ILE A 1 139 ? 24.90800 15.37326 -12.09286 1.000 34.37371  ? 139 ILE A CD1 1 
ATOM   1080 N N   . ASN A 1 140 ? 21.83464 20.17306 -14.12860 1.000 40.72728  ? 140 ASN A N   1 
ATOM   1081 C CA  . ASN A 1 140 ? 21.88930 21.46992 -14.80435 1.000 50.78179  ? 140 ASN A CA  1 
ATOM   1082 C C   . ASN A 1 140 ? 21.52851 21.33120 -16.28250 1.000 48.98110  ? 140 ASN A C   1 
ATOM   1083 O O   . ASN A 1 140 ? 22.23520 21.81287 -17.17136 1.000 46.71950  ? 140 ASN A O   1 
ATOM   1084 C CB  . ASN A 1 140 ? 23.26195 22.12286 -14.63241 1.000 44.72212  ? 140 ASN A CB  1 
ATOM   1085 C CG  . ASN A 1 140 ? 23.61277 22.37346 -13.17674 1.000 54.49127  ? 140 ASN A CG  1 
ATOM   1086 O OD1 . ASN A 1 140 ? 22.80693 22.90633 -12.41235 1.000 50.82754  ? 140 ASN A OD1 1 
ATOM   1087 N ND2 . ASN A 1 140 ? 24.82211 21.98920 -12.78680 1.000 47.27701  ? 140 ASN A ND2 1 
ATOM   1088 N N   . ASP A 1 141 ? 20.41551 20.63898 -16.53406 1.000 47.12821  ? 141 ASP A N   1 
ATOM   1089 C CA  . ASP A 1 141 ? 19.82285 20.40776 -17.85080 1.000 57.81417  ? 141 ASP A CA  1 
ATOM   1090 C C   . ASP A 1 141 ? 20.64703 19.47877 -18.73396 1.000 54.96304  ? 141 ASP A C   1 
ATOM   1091 O O   . ASP A 1 141 ? 20.37339 19.38253 -19.93803 1.000 61.89329  ? 141 ASP A O   1 
ATOM   1092 C CB  . ASP A 1 141 ? 19.55742 21.72129 -18.59662 1.000 53.84796  ? 141 ASP A CB  1 
ATOM   1093 C CG  . ASP A 1 141 ? 18.60258 22.62854 -17.84748 1.000 63.50518  ? 141 ASP A CG  1 
ATOM   1094 O OD1 . ASP A 1 141 ? 17.79294 22.11193 -17.04815 1.000 62.21594  ? 141 ASP A OD1 1 
ATOM   1095 O OD2 . ASP A 1 141 ? 18.66103 23.85707 -18.05908 1.000 73.83029  ? 141 ASP A OD2 1 
ATOM   1096 N N   . ILE A 1 142 ? 21.63118 18.77663 -18.17700 1.000 54.61330  ? 142 ILE A N   1 
ATOM   1097 C CA  . ILE A 1 142 ? 22.44671 17.81816 -18.91705 1.000 55.42479  ? 142 ILE A CA  1 
ATOM   1098 C C   . ILE A 1 142 ? 22.16360 16.42748 -18.36793 1.000 50.02614  ? 142 ILE A C   1 
ATOM   1099 O O   . ILE A 1 142 ? 22.28421 16.19974 -17.15849 1.000 50.25313  ? 142 ILE A O   1 
ATOM   1100 C CB  . ILE A 1 142 ? 23.94699 18.14819 -18.81059 1.000 61.46537  ? 142 ILE A CB  1 
ATOM   1101 C CG1 . ILE A 1 142 ? 24.21030 19.60088 -19.20998 1.000 62.04776  ? 142 ILE A CG1 1 
ATOM   1102 C CG2 . ILE A 1 142 ? 24.76968 17.19027 -19.66136 1.000 66.33480  ? 142 ILE A CG2 1 
ATOM   1103 C CD1 . ILE A 1 142 ? 23.77219 19.93829 -20.61652 1.000 62.49041  ? 142 ILE A CD1 1 
ATOM   1104 N N   . HIS A 1 143 ? 21.78793 15.49967 -19.24825 1.000 56.69414  ? 143 HIS A N   1 
ATOM   1105 C CA  A HIS A 1 143 ? 21.54469 14.12972 -18.81498 0.700 54.65893  ? 143 HIS A CA  1 
ATOM   1106 C CA  B HIS A 1 143 ? 21.54462 14.12383 -18.83113 0.300 55.56168  ? 143 HIS A CA  1 
ATOM   1107 C C   . HIS A 1 143 ? 22.85410 13.49453 -18.36769 1.000 50.87775  ? 143 HIS A C   1 
ATOM   1108 O O   . HIS A 1 143 ? 23.81107 13.39961 -19.14367 1.000 49.72891  ? 143 HIS A O   1 
ATOM   1109 C CB  A HIS A 1 143 ? 20.90649 13.29967 -19.92376 0.700 52.45756  ? 143 HIS A CB  1 
ATOM   1110 C CB  B HIS A 1 143 ? 20.93069 13.32267 -19.97894 0.300 50.83071  ? 143 HIS A CB  1 
ATOM   1111 C CG  A HIS A 1 143 ? 20.71007 11.86378 -19.54678 0.700 55.36519  ? 143 HIS A CG  1 
ATOM   1112 C CG  B HIS A 1 143 ? 19.53118 13.73081 -20.32450 0.300 51.67492  ? 143 HIS A CG  1 
ATOM   1113 N ND1 A HIS A 1 143 ? 21.71286 10.92378 -19.64977 0.700 50.82453  ? 143 HIS A ND1 1 
ATOM   1114 N ND1 B HIS A 1 143 ? 18.43713 13.33211 -19.58717 0.300 51.64500  ? 143 HIS A ND1 1 
ATOM   1115 C CD2 A HIS A 1 143 ? 19.63530 11.21307 -19.04199 0.700 52.67699  ? 143 HIS A CD2 1 
ATOM   1116 C CD2 B HIS A 1 143 ? 19.04628 14.49455 -21.33213 0.300 53.69843  ? 143 HIS A CD2 1 
ATOM   1117 C CE1 A HIS A 1 143 ? 21.26051 9.75335  -19.23679 0.700 45.53811  ? 143 HIS A CE1 1 
ATOM   1118 C CE1 B HIS A 1 143 ? 17.33983 13.83743 -20.12147 0.300 50.84020  ? 143 HIS A CE1 1 
ATOM   1119 N NE2 A HIS A 1 143 ? 20.00235 9.90139  -18.86365 0.700 45.35835  ? 143 HIS A NE2 1 
ATOM   1120 N NE2 B HIS A 1 143 ? 17.68169 14.54672 -21.18189 0.300 54.32326  ? 143 HIS A NE2 1 
ATOM   1121 N N   . PHE A 1 144 ? 22.89624 13.06030 -17.11104 1.000 45.96899  ? 144 PHE A N   1 
ATOM   1122 C CA  . PHE A 1 144 ? 24.10461 12.50514 -16.51426 1.000 38.42290  ? 144 PHE A CA  1 
ATOM   1123 C C   . PHE A 1 144 ? 24.11850 10.98376 -16.48200 1.000 33.99389  ? 144 PHE A C   1 
ATOM   1124 O O   . PHE A 1 144 ? 25.15617 10.37587 -16.75922 1.000 35.40775  ? 144 PHE A O   1 
ATOM   1125 C CB  . PHE A 1 144 ? 24.27567 13.04819 -15.09358 1.000 43.48725  ? 144 PHE A CB  1 
ATOM   1126 C CG  . PHE A 1 144 ? 25.48547 12.51868 -14.37913 1.000 41.31089  ? 144 PHE A CG  1 
ATOM   1127 C CD1 . PHE A 1 144 ? 26.74675 13.01505 -14.66189 1.000 35.27360  ? 144 PHE A CD1 1 
ATOM   1128 C CD2 . PHE A 1 144 ? 25.35947 11.53003 -13.41781 1.000 40.97403  ? 144 PHE A CD2 1 
ATOM   1129 C CE1 . PHE A 1 144 ? 27.85998 12.53015 -14.00444 1.000 43.17693  ? 144 PHE A CE1 1 
ATOM   1130 C CE2 . PHE A 1 144 ? 26.46756 11.04013 -12.75656 1.000 34.32388  ? 144 PHE A CE2 1 
ATOM   1131 C CZ  . PHE A 1 144 ? 27.72166 11.53997 -13.04875 1.000 37.62055  ? 144 PHE A CZ  1 
ATOM   1132 N N   . GLU A 1 145 ? 22.99553 10.35142 -16.15338 1.000 32.94799  ? 145 GLU A N   1 
ATOM   1133 C CA  . GLU A 1 145 ? 22.94859 8.89975  -16.04125 1.000 38.17082  ? 145 GLU A CA  1 
ATOM   1134 C C   . GLU A 1 145 ? 21.49729 8.44942  -16.02245 1.000 38.10543  ? 145 GLU A C   1 
ATOM   1135 O O   . GLU A 1 145 ? 20.58795 9.23713  -15.74762 1.000 42.89769  ? 145 GLU A O   1 
ATOM   1136 C CB  . GLU A 1 145 ? 23.66397 8.41088  -14.77907 1.000 38.39797  ? 145 GLU A CB  1 
ATOM   1137 C CG  . GLU A 1 145 ? 22.96331 8.79581  -13.49009 0.700 34.28820  ? 145 GLU A CG  1 
ATOM   1138 C CD  . GLU A 1 145 ? 23.73493 8.36922  -12.26097 0.700 32.23271  ? 145 GLU A CD  1 
ATOM   1139 O OE1 . GLU A 1 145 ? 24.88304 7.90980  -12.41650 0.700 32.66421  ? 145 GLU A OE1 1 
ATOM   1140 O OE2 . GLU A 1 145 ? 23.19234 8.49299  -11.14434 0.700 28.08236  ? 145 GLU A OE2 1 
ATOM   1141 N N   . ARG A 1 146 ? 21.29668 7.16715  -16.32001 1.000 36.44479  ? 146 ARG A N   1 
ATOM   1142 C CA  . ARG A 1 146 ? 20.01147 6.49702  -16.15611 1.000 49.70825  ? 146 ARG A CA  1 
ATOM   1143 C C   . ARG A 1 146 ? 20.15589 5.51673  -14.99917 1.000 44.01673  ? 146 ARG A C   1 
ATOM   1144 O O   . ARG A 1 146 ? 20.79090 4.46614  -15.14164 1.000 45.14470  ? 146 ARG A O   1 
ATOM   1145 C CB  . ARG A 1 146 ? 19.58398 5.78898  -17.43967 1.000 46.36840  ? 146 ARG A CB  1 
ATOM   1146 C CG  . ARG A 1 146 ? 18.32512 4.94382  -17.28698 0.800 47.73886  ? 146 ARG A CG  1 
ATOM   1147 C CD  . ARG A 1 146 ? 17.64870 4.68745  -18.62587 0.800 49.48570  ? 146 ARG A CD  1 
ATOM   1148 N NE  . ARG A 1 146 ? 16.95382 5.86950  -19.12400 0.800 56.59215  ? 146 ARG A NE  1 
ATOM   1149 C CZ  . ARG A 1 146 ? 16.22645 5.89760  -20.23312 0.800 60.72672  ? 146 ARG A CZ  1 
ATOM   1150 N NH1 . ARG A 1 146 ? 16.08274 4.82402  -20.99339 0.800 58.68479  ? 146 ARG A NH1 1 
ATOM   1151 N NH2 . ARG A 1 146 ? 15.62624 7.03025  -20.58801 0.800 53.47614  ? 146 ARG A NH2 1 
ATOM   1152 N N   . PHE A 1 147 ? 19.57673 5.86654  -13.85545 1.000 51.50235  ? 147 PHE A N   1 
ATOM   1153 C CA  . PHE A 1 147 ? 19.71573 5.07409  -12.64289 1.000 42.13062  ? 147 PHE A CA  1 
ATOM   1154 C C   . PHE A 1 147 ? 18.63905 3.99959  -12.59041 1.000 44.63402  ? 147 PHE A C   1 
ATOM   1155 O O   . PHE A 1 147 ? 17.45071 4.29387  -12.75221 1.000 49.09924  ? 147 PHE A O   1 
ATOM   1156 C CB  . PHE A 1 147 ? 19.62372 5.96528  -11.40243 1.000 54.39475  ? 147 PHE A CB  1 
ATOM   1157 C CG  . PHE A 1 147 ? 19.77323 5.21866  -10.10425 1.000 45.77462  ? 147 PHE A CG  1 
ATOM   1158 C CD1 . PHE A 1 147 ? 18.66841 4.68595  -9.45735  1.000 48.09101  ? 147 PHE A CD1 1 
ATOM   1159 C CD2 . PHE A 1 147 ? 21.01969 5.05640  -9.52895  1.000 38.72545  ? 147 PHE A CD2 1 
ATOM   1160 C CE1 . PHE A 1 147 ? 18.80757 4.00061  -8.26549  1.000 46.89325  ? 147 PHE A CE1 1 
ATOM   1161 C CE2 . PHE A 1 147 ? 21.16562 4.37352  -8.33621  1.000 39.56753  ? 147 PHE A CE2 1 
ATOM   1162 C CZ  . PHE A 1 147 ? 20.05821 3.84538  -7.70442  1.000 38.54924  ? 147 PHE A CZ  1 
ATOM   1163 N N   . ARG A 1 148 ? 19.05776 2.75828  -12.35490 1.000 41.29314  ? 148 ARG A N   1 
ATOM   1164 C CA  . ARG A 1 148 ? 18.13972 1.67375  -12.03369 1.000 51.48014  ? 148 ARG A CA  1 
ATOM   1165 C C   . ARG A 1 148 ? 18.60203 1.02120  -10.74089 1.000 44.44134  ? 148 ARG A C   1 
ATOM   1166 O O   . ARG A 1 148 ? 19.73452 0.53488  -10.65761 1.000 45.68758  ? 148 ARG A O   1 
ATOM   1167 C CB  . ARG A 1 148 ? 18.05228 0.63886  -13.15824 1.000 51.26093  ? 148 ARG A CB  1 
ATOM   1168 C CG  . ARG A 1 148 ? 17.00669 -0.42706 -12.87132 1.000 60.83829  ? 148 ARG A CG  1 
ATOM   1169 C CD  . ARG A 1 148 ? 16.74836 -1.34873 -14.04688 1.000 65.17503  ? 148 ARG A CD  1 
ATOM   1170 N NE  . ARG A 1 148 ? 15.69349 -2.30330 -13.72674 0.800 62.05825  ? 148 ARG A NE  1 
ATOM   1171 C CZ  . ARG A 1 148 ? 15.24040 -3.23590 -14.55226 0.700 60.62851  ? 148 ARG A CZ  1 
ATOM   1172 N NH1 . ARG A 1 148 ? 15.73072 -3.37637 -15.77191 0.700 59.97913  ? 148 ARG A NH1 1 
ATOM   1173 N NH2 . ARG A 1 148 ? 14.26994 -4.04801 -14.14229 0.700 53.93842  ? 148 ARG A NH2 1 
ATOM   1174 N N   . GLY A 1 149 ? 17.72797 1.01489  -9.74006  1.000 47.48503  ? 149 GLY A N   1 
ATOM   1175 C CA  . GLY A 1 149 ? 18.07403 0.45098  -8.44481  1.000 49.34922  ? 149 GLY A CA  1 
ATOM   1176 C C   . GLY A 1 149 ? 16.93655 0.62108  -7.46274  1.000 50.87182  ? 149 GLY A C   1 
ATOM   1177 O O   . GLY A 1 149 ? 15.76231 0.62444  -7.84444  1.000 53.28529  ? 149 GLY A O   1 
ATOM   1178 N N   . ASP A 1 150 ? 17.30104 0.77085  -6.19053  1.000 49.19051  ? 150 ASP A N   1 
ATOM   1179 C CA  . ASP A 1 150 ? 16.30057 0.91823  -5.14046  1.000 51.81407  ? 150 ASP A CA  1 
ATOM   1180 C C   . ASP A 1 150 ? 15.88938 2.36972  -4.91928  1.000 47.49358  ? 150 ASP A C   1 
ATOM   1181 O O   . ASP A 1 150 ? 14.71532 2.64093  -4.64360  1.000 50.32671  ? 150 ASP A O   1 
ATOM   1182 C CB  . ASP A 1 150 ? 16.81372 0.31135  -3.83137  1.000 49.82252  ? 150 ASP A CB  1 
ATOM   1183 C CG  . ASP A 1 150 ? 16.77456 -1.20625 -3.83951  1.000 42.41061  ? 150 ASP A CG  1 
ATOM   1184 O OD1 . ASP A 1 150 ? 16.39814 -1.78378 -4.88126  1.000 46.12007  ? 150 ASP A OD1 1 
ATOM   1185 O OD2 . ASP A 1 150 ? 17.11165 -1.82163 -2.80723  1.000 42.86851  ? 150 ASP A OD2 1 
ATOM   1186 N N   . GLY A 1 151 ? 16.81716 3.31005  -5.03938  1.000 42.43299  ? 151 GLY A N   1 
ATOM   1187 C CA  . GLY A 1 151 ? 16.46289 4.70181  -4.85538  1.000 40.85259  ? 151 GLY A CA  1 
ATOM   1188 C C   . GLY A 1 151 ? 17.68492 5.58960  -4.77890  1.000 37.33327  ? 151 GLY A C   1 
ATOM   1189 O O   . GLY A 1 151 ? 18.82917 5.14015  -4.90326  1.000 37.94543  ? 151 GLY A O   1 
ATOM   1190 N N   . LEU A 1 152 ? 17.40905 6.87634  -4.57310  1.000 35.90817  ? 152 LEU A N   1 
ATOM   1191 C CA  . LEU A 1 152 ? 18.43029 7.90472  -4.46154  1.000 39.00676  ? 152 LEU A CA  1 
ATOM   1192 C C   . LEU A 1 152 ? 18.15597 8.74900  -3.22693  1.000 40.03248  ? 152 LEU A C   1 
ATOM   1193 O O   . LEU A 1 152 ? 17.00520 8.92171  -2.81565  1.000 38.89155  ? 152 LEU A O   1 
ATOM   1194 C CB  . LEU A 1 152 ? 18.46681 8.79983  -5.70827  1.000 38.60002  ? 152 LEU A CB  1 
ATOM   1195 C CG  . LEU A 1 152 ? 18.83071 8.10953  -7.02531  1.000 38.19604  ? 152 LEU A CG  1 
ATOM   1196 C CD1 . LEU A 1 152 ? 18.40309 8.94727  -8.22297  1.000 47.15996  ? 152 LEU A CD1 1 
ATOM   1197 C CD2 . LEU A 1 152 ? 20.32185 7.81695  -7.08214  1.000 35.84482  ? 152 LEU A CD2 1 
ATOM   1198 N N   . CYS A 1 153 ? 19.22523 9.28395  -2.64466  1.000 39.33456  ? 153 CYS A N   1 
ATOM   1199 C CA  . CYS A 1 153 ? 19.13986 10.06809 -1.41949  1.000 34.26735  ? 153 CYS A CA  1 
ATOM   1200 C C   . CYS A 1 153 ? 19.94025 11.34745 -1.60027  1.000 37.67774  ? 153 CYS A C   1 
ATOM   1201 O O   . CYS A 1 153 ? 21.13151 11.29385 -1.92186  1.000 42.43683  ? 153 CYS A O   1 
ATOM   1202 C CB  . CYS A 1 153 ? 19.66018 9.26857  -0.22218  1.000 35.89099  ? 153 CYS A CB  1 
ATOM   1203 S SG  . CYS A 1 153 ? 19.78937 10.21355 1.31076   1.000 39.24773  ? 153 CYS A SG  1 
ATOM   1204 N N   . MET A 1 154 ? 19.28750 12.49053 -1.40098  1.000 37.15261  ? 154 MET A N   1 
ATOM   1205 C CA  . MET A 1 154 ? 19.92872 13.79876 -1.47609  1.000 43.67455  ? 154 MET A CA  1 
ATOM   1206 C C   . MET A 1 154 ? 19.95079 14.40585 -0.08020  1.000 39.88849  ? 154 MET A C   1 
ATOM   1207 O O   . MET A 1 154 ? 18.89102 14.67757 0.49349   1.000 39.08409  ? 154 MET A O   1 
ATOM   1208 C CB  . MET A 1 154 ? 19.19614 14.71775 -2.45352  1.000 40.60544  ? 154 MET A CB  1 
ATOM   1209 C CG  . MET A 1 154 ? 19.89523 16.05418 -2.67759  1.000 38.17537  ? 154 MET A CG  1 
ATOM   1210 S SD  . MET A 1 154 ? 21.44269 15.89595 -3.58457  1.000 41.09086  ? 154 MET A SD  1 
ATOM   1211 C CE  . MET A 1 154 ? 20.84753 15.88652 -5.27454  1.000 39.61035  ? 154 MET A CE  1 
ATOM   1212 N N   . SER A 1 155 ? 21.15080 14.62942 0.45398   1.000 42.40232  ? 155 SER A N   1 
ATOM   1213 C CA  . SER A 1 155 ? 21.33659 14.97094 1.85660   1.000 42.28421  ? 155 SER A CA  1 
ATOM   1214 C C   . SER A 1 155 ? 21.86147 16.39083 2.02183   1.000 43.88419  ? 155 SER A C   1 
ATOM   1215 O O   . SER A 1 155 ? 22.66118 16.87087 1.21100   1.000 38.42728  ? 155 SER A O   1 
ATOM   1216 C CB  . SER A 1 155 ? 22.30170 13.98820 2.52246   1.000 40.24652  ? 155 SER A CB  1 
ATOM   1217 O OG  . SER A 1 155 ? 22.64353 14.40941 3.83365   1.000 39.14091  ? 155 SER A OG  1 
ATOM   1218 N N   . THR A 1 156 ? 21.40539 17.05154 3.08750   1.000 43.28404  ? 156 THR A N   1 
ATOM   1219 C CA  . THR A 1 156 ? 21.99202 18.30246 3.53647   1.000 37.94954  ? 156 THR A CA  1 
ATOM   1220 C C   . THR A 1 156 ? 23.33855 18.00320 4.19031   1.000 36.61101  ? 156 THR A C   1 
ATOM   1221 O O   . THR A 1 156 ? 23.69175 16.83995 4.39261   1.000 37.97523  ? 156 THR A O   1 
ATOM   1222 C CB  . THR A 1 156 ? 21.05582 19.00657 4.52031   1.000 40.93301  ? 156 THR A CB  1 
ATOM   1223 O OG1 . THR A 1 156 ? 21.09825 18.33677 5.78868   1.000 40.82880  ? 156 THR A OG1 1 
ATOM   1224 C CG2 . THR A 1 156 ? 19.62683 18.99541 4.00118   1.000 40.83615  ? 156 THR A CG2 1 
ATOM   1225 N N   . PRO A 1 157 ? 24.13199 19.03059 4.51178   1.000 38.87722  ? 157 PRO A N   1 
ATOM   1226 C CA  . PRO A 1 157 ? 25.36606 18.76246 5.27350   1.000 35.22223  ? 157 PRO A CA  1 
ATOM   1227 C C   . PRO A 1 157 ? 25.11070 18.09631 6.61565   1.000 42.67138  ? 157 PRO A C   1 
ATOM   1228 O O   . PRO A 1 157 ? 25.72529 17.06575 6.92091   1.000 33.73662  ? 157 PRO A O   1 
ATOM   1229 C CB  . PRO A 1 157 ? 25.98167 20.15716 5.42537   1.000 39.78084  ? 157 PRO A CB  1 
ATOM   1230 C CG  . PRO A 1 157 ? 25.51291 20.89136 4.22929   1.000 50.60172  ? 157 PRO A CG  1 
ATOM   1231 C CD  . PRO A 1 157 ? 24.11520 20.40145 3.96870   1.000 43.14400  ? 157 PRO A CD  1 
ATOM   1232 N N   . SER A 1 158 ? 24.21355 18.65412 7.43157   1.000 38.25252  ? 158 SER A N   1 
ATOM   1233 C CA  . SER A 1 158 ? 23.93194 18.05702 8.73173   1.000 44.56900  ? 158 SER A CA  1 
ATOM   1234 C C   . SER A 1 158 ? 23.22735 16.71305 8.60930   1.000 40.06600  ? 158 SER A C   1 
ATOM   1235 O O   . SER A 1 158 ? 23.19653 15.95273 9.58233   1.000 41.50502  ? 158 SER A O   1 
ATOM   1236 C CB  . SER A 1 158 ? 23.09144 19.01016 9.57907   1.000 42.00284  ? 158 SER A CB  1 
ATOM   1237 O OG  . SER A 1 158 ? 21.83413 19.24854 8.97276   1.000 43.19421  ? 158 SER A OG  1 
ATOM   1238 N N   . GLY A 1 159 ? 22.66141 16.40450 7.44356   1.000 39.27777  ? 159 GLY A N   1 
ATOM   1239 C CA  . GLY A 1 159 ? 22.07497 15.09766 7.22655   1.000 37.29643  ? 159 GLY A CA  1 
ATOM   1240 C C   . GLY A 1 159 ? 23.04883 14.01768 6.80951   1.000 41.04842  ? 159 GLY A C   1 
ATOM   1241 O O   . GLY A 1 159 ? 22.65933 12.84812 6.74504   1.000 41.22375  ? 159 GLY A O   1 
ATOM   1242 N N   . THR A 1 160 ? 24.30567 14.37531 6.52922   1.000 35.88157  ? 160 THR A N   1 
ATOM   1243 C CA  . THR A 1 160 ? 25.27264 13.38914 6.05974   1.000 36.52428  ? 160 THR A CA  1 
ATOM   1244 C C   . THR A 1 160 ? 25.62642 12.35971 7.12497   1.000 40.65721  ? 160 THR A C   1 
ATOM   1245 O O   . THR A 1 160 ? 26.05061 11.25340 6.77919   1.000 37.22642  ? 160 THR A O   1 
ATOM   1246 C CB  . THR A 1 160 ? 26.54164 14.08215 5.56613   1.000 37.34689  ? 160 THR A CB  1 
ATOM   1247 O OG1 . THR A 1 160 ? 27.01513 14.98762 6.56985   1.000 37.45631  ? 160 THR A OG1 1 
ATOM   1248 C CG2 . THR A 1 160 ? 26.25641 14.85006 4.28827   1.000 36.36850  ? 160 THR A CG2 1 
ATOM   1249 N N   . THR A 1 161 ? 25.47374 12.68952 8.40422   1.000 41.37834  ? 161 THR A N   1 
ATOM   1250 C CA  . THR A 1 161 ? 25.66789 11.69915 9.45515   1.000 39.38798  ? 161 THR A CA  1 
ATOM   1251 C C   . THR A 1 161 ? 24.46456 10.78321 9.62887   1.000 38.70258  ? 161 THR A C   1 
ATOM   1252 O O   . THR A 1 161 ? 24.51573 9.87403  10.46305  1.000 41.68773  ? 161 THR A O   1 
ATOM   1253 C CB  . THR A 1 161 ? 25.97695 12.38982 10.78504  1.000 42.45970  ? 161 THR A CB  1 
ATOM   1254 O OG1 . THR A 1 161 ? 25.02151 13.43416 11.01146  1.000 44.04917  ? 161 THR A OG1 1 
ATOM   1255 C CG2 . THR A 1 161 ? 27.37927 12.98078 10.77000  1.000 40.61949  ? 161 THR A CG2 1 
ATOM   1256 N N   . ALA A 1 162 ? 23.39229 10.99369 8.86612   1.000 41.04792  ? 162 ALA A N   1 
ATOM   1257 C CA  . ALA A 1 162 ? 22.18784 10.18447 9.00173   1.000 39.55943  ? 162 ALA A CA  1 
ATOM   1258 C C   . ALA A 1 162 ? 22.08459 9.14760  7.88924   1.000 38.41262  ? 162 ALA A C   1 
ATOM   1259 O O   . ALA A 1 162 ? 22.96778 8.29620  7.74313   1.000 41.41600  ? 162 ALA A O   1 
ATOM   1260 C CB  . ALA A 1 162 ? 20.94469 11.07657 9.01250   1.000 41.56917  ? 162 ALA A CB  1 
ATOM   1261 N N   . TYR A 1 163 ? 21.00220 9.21383  7.10696   1.000 40.16785  ? 163 TYR A N   1 
ATOM   1262 C CA  . TYR A 1 163 ? 20.77678 8.23904  6.04170   1.000 41.88055  ? 163 TYR A CA  1 
ATOM   1263 C C   . TYR A 1 163 ? 21.93175 8.23182  5.04622   1.000 37.79793  ? 163 TYR A C   1 
ATOM   1264 O O   . TYR A 1 163 ? 22.36892 7.16514  4.59736   1.000 36.57266  ? 163 TYR A O   1 
ATOM   1265 C CB  . TYR A 1 163 ? 19.45702 8.55065  5.33322   1.000 45.87277  ? 163 TYR A CB  1 
ATOM   1266 C CG  . TYR A 1 163 ? 18.80821 7.38292  4.61773   1.000 44.58647  ? 163 TYR A CG  1 
ATOM   1267 C CD1 . TYR A 1 163 ? 19.45045 6.15525  4.50846   1.000 42.26294  ? 163 TYR A CD1 1 
ATOM   1268 C CD2 . TYR A 1 163 ? 17.54830 7.51366  4.04912   1.000 49.99305  ? 163 TYR A CD2 1 
ATOM   1269 C CE1 . TYR A 1 163 ? 18.85551 5.09285  3.85333   1.000 44.90755  ? 163 TYR A CE1 1 
ATOM   1270 C CE2 . TYR A 1 163 ? 16.94523 6.45698  3.39282   1.000 55.65254  ? 163 TYR A CE2 1 
ATOM   1271 C CZ  . TYR A 1 163 ? 17.60281 5.24966  3.29722   1.000 48.64441  ? 163 TYR A CZ  1 
ATOM   1272 O OH  . TYR A 1 163 ? 17.00827 4.19440  2.64490   1.000 41.43923  ? 163 TYR A OH  1 
ATOM   1273 N N   . ASN A 1 164 ? 22.43823 9.41673  4.69487   1.000 38.82921  ? 164 ASN A N   1 
ATOM   1274 C CA  . ASN A 1 164 ? 23.56441 9.52125  3.77111   1.000 36.13973  ? 164 ASN A CA  1 
ATOM   1275 C C   . ASN A 1 164 ? 24.73910 8.66255  4.22473   1.000 39.90371  ? 164 ASN A C   1 
ATOM   1276 O O   . ASN A 1 164 ? 25.41443 8.03024  3.40294   1.000 36.99841  ? 164 ASN A O   1 
ATOM   1277 C CB  . ASN A 1 164 ? 23.98518 10.98862 3.64490   1.000 36.51781  ? 164 ASN A CB  1 
ATOM   1278 C CG  . ASN A 1 164 ? 25.30753 11.16421 2.92114   1.000 32.98286  ? 164 ASN A CG  1 
ATOM   1279 O OD1 . ASN A 1 164 ? 25.34301 11.33502 1.70360   1.000 35.30077  ? 164 ASN A OD1 1 
ATOM   1280 N ND2 . ASN A 1 164 ? 26.40330 11.15049 3.67384   1.000 31.14879  ? 164 ASN A ND2 1 
ATOM   1281 N N   . LYS A 1 165 ? 24.98988 8.62048  5.53597   1.000 40.24722  ? 165 LYS A N   1 
ATOM   1282 C CA  . LYS A 1 165 ? 26.12920 7.86709  6.04976   1.000 35.49245  ? 165 LYS A CA  1 
ATOM   1283 C C   . LYS A 1 165 ? 25.96031 6.37032  5.81610   1.000 35.05324  ? 165 LYS A C   1 
ATOM   1284 O O   . LYS A 1 165 ? 26.90962 5.68510  5.41625   1.000 33.47252  ? 165 LYS A O   1 
ATOM   1285 C CB  . LYS A 1 165 ? 26.32023 8.16114  7.53571   1.000 40.32498  ? 165 LYS A CB  1 
ATOM   1286 C CG  . LYS A 1 165 ? 27.48569 7.42573  8.16405   1.000 35.08129  ? 165 LYS A CG  1 
ATOM   1287 C CD  . LYS A 1 165 ? 27.70975 7.86401  9.59749   1.000 36.99497  ? 165 LYS A CD  1 
ATOM   1288 C CE  . LYS A 1 165 ? 28.91661 7.16281  10.19392  1.000 40.85305  ? 165 LYS A CE  1 
ATOM   1289 N NZ  . LYS A 1 165 ? 28.77089 5.68168  10.13431  1.000 40.97938  ? 165 LYS A NZ  1 
ATOM   1290 N N   . SER A 1 166 ? 24.75815 5.84248  6.05859   1.000 33.51113  ? 166 SER A N   1 
ATOM   1291 C CA  . SER A 1 166 ? 24.52690 4.41250  5.88181   1.000 38.68200  ? 166 SER A CA  1 
ATOM   1292 C C   . SER A 1 166 ? 24.60788 3.98621  4.42262   1.000 38.66498  ? 166 SER A C   1 
ATOM   1293 O O   . SER A 1 166 ? 24.76342 2.79206  4.14545   1.000 36.93080  ? 166 SER A O   1 
ATOM   1294 C CB  . SER A 1 166 ? 23.16665 4.02220  6.45887   1.000 37.88025  ? 166 SER A CB  1 
ATOM   1295 O OG  . SER A 1 166 ? 23.12176 4.26603  7.85391   1.000 43.20083  ? 166 SER A OG  1 
ATOM   1296 N N   . LEU A 1 167 ? 24.50693 4.92989  3.48994   1.000 40.53087  ? 167 LEU A N   1 
ATOM   1297 C CA  . LEU A 1 167 ? 24.58876 4.64281  2.06624   1.000 41.77011  ? 167 LEU A CA  1 
ATOM   1298 C C   . LEU A 1 167 ? 25.98777 4.86782  1.50669   1.000 41.13763  ? 167 LEU A C   1 
ATOM   1299 O O   . LEU A 1 167 ? 26.16333 4.87583  0.28445   1.000 42.46672  ? 167 LEU A O   1 
ATOM   1300 C CB  . LEU A 1 167 ? 23.56775 5.49151  1.30787   1.000 32.76148  ? 167 LEU A CB  1 
ATOM   1301 C CG  . LEU A 1 167 ? 22.11797 5.25301  1.73663   1.000 36.49103  ? 167 LEU A CG  1 
ATOM   1302 C CD1 . LEU A 1 167 ? 21.19431 6.30608  1.15835   1.000 35.59853  ? 167 LEU A CD1 1 
ATOM   1303 C CD2 . LEU A 1 167 ? 21.67350 3.86471  1.31264   1.000 38.49184  ? 167 LEU A CD2 1 
ATOM   1304 N N   . GLY A 1 168 ? 26.98351 5.04724  2.37304   1.000 41.19565  ? 168 GLY A N   1 
ATOM   1305 C CA  . GLY A 1 168 ? 28.35353 5.24359  1.95331   1.000 33.70460  ? 168 GLY A CA  1 
ATOM   1306 C C   . GLY A 1 168 ? 28.75230 6.67715  1.68834   1.000 40.87976  ? 168 GLY A C   1 
ATOM   1307 O O   . GLY A 1 168 ? 29.89658 6.91681  1.28250   1.000 37.14022  ? 168 GLY A O   1 
ATOM   1308 N N   . GLY A 1 169 ? 27.85534 7.63522  1.90504   1.000 31.02578  ? 169 GLY A N   1 
ATOM   1309 C CA  . GLY A 1 169 ? 28.17507 9.01849  1.62882   1.000 31.24376  ? 169 GLY A CA  1 
ATOM   1310 C C   . GLY A 1 169 ? 29.21481 9.58117  2.57808   1.000 44.33625  ? 169 GLY A C   1 
ATOM   1311 O O   . GLY A 1 169 ? 29.49750 9.03563  3.64585   1.000 37.32156  ? 169 GLY A O   1 
ATOM   1312 N N   . ALA A 1 170 ? 29.79677 10.70323 2.16640   1.000 37.96142  ? 170 ALA A N   1 
ATOM   1313 C CA  . ALA A 1 170 ? 30.79978 11.37721 2.97366   1.000 41.59627  ? 170 ALA A CA  1 
ATOM   1314 C C   . ALA A 1 170 ? 30.13941 12.28110 4.00558   1.000 41.70313  ? 170 ALA A C   1 
ATOM   1315 O O   . ALA A 1 170 ? 29.02369 12.77185 3.81166   1.000 38.37598  ? 170 ALA A O   1 
ATOM   1316 C CB  . ALA A 1 170 ? 31.73789 12.19955 2.09181   1.000 38.36325  ? 170 ALA A CB  1 
ATOM   1317 N N   . LEU A 1 171 ? 30.84482 12.49791 5.11159   1.000 34.17934  ? 171 LEU A N   1 
ATOM   1318 C CA  . LEU A 1 171 ? 30.39369 13.41515 6.14557   1.000 38.08905  ? 171 LEU A CA  1 
ATOM   1319 C C   . LEU A 1 171 ? 30.91169 14.81084 5.82550   1.000 33.30881  ? 171 LEU A C   1 
ATOM   1320 O O   . LEU A 1 171 ? 32.11514 15.00192 5.62737   1.000 44.22876  ? 171 LEU A O   1 
ATOM   1321 C CB  . LEU A 1 171 ? 30.87368 12.95668 7.52205   1.000 36.19340  ? 171 LEU A CB  1 
ATOM   1322 C CG  . LEU A 1 171 ? 30.56089 11.50902 7.91988   1.000 37.58757  ? 171 LEU A CG  1 
ATOM   1323 C CD1 . LEU A 1 171 ? 30.87930 11.28078 9.38717   1.000 34.44326  ? 171 LEU A CD1 1 
ATOM   1324 C CD2 . LEU A 1 171 ? 29.11324 11.15515 7.62798   1.000 36.63241  ? 171 LEU A CD2 1 
ATOM   1325 N N   . MET A 1 172 ? 30.00048 15.77817 5.76014   1.000 34.80713  ? 172 MET A N   1 
ATOM   1326 C CA  . MET A 1 172 ? 30.31782 17.13476 5.33310   1.000 38.05087  ? 172 MET A CA  1 
ATOM   1327 C C   . MET A 1 172 ? 30.12372 18.10151 6.48995   1.000 39.74932  ? 172 MET A C   1 
ATOM   1328 O O   . MET A 1 172 ? 29.10442 18.04264 7.18486   1.000 41.43669  ? 172 MET A O   1 
ATOM   1329 C CB  . MET A 1 172 ? 29.43673 17.56219 4.15728   1.000 44.45913  ? 172 MET A CB  1 
ATOM   1330 C CG  . MET A 1 172 ? 29.57168 16.70885 2.91435   1.000 52.06687  ? 172 MET A CG  1 
ATOM   1331 S SD  . MET A 1 172 ? 28.65142 17.45211 1.56077   1.000 54.66865  ? 172 MET A SD  1 
ATOM   1332 C CE  . MET A 1 172 ? 29.31938 19.11335 1.61042   1.000 40.58274  ? 172 MET A CE  1 
ATOM   1333 N N   . HIS A 1 173 ? 31.09009 18.99460 6.68475   1.000 42.97245  ? 173 HIS A N   1 
ATOM   1334 C CA  . HIS A 1 173 ? 30.93944 20.01477 7.70815   1.000 46.93233  ? 173 HIS A CA  1 
ATOM   1335 C C   . HIS A 1 173 ? 29.81505 20.97120 7.31655   1.000 47.01257  ? 173 HIS A C   1 
ATOM   1336 O O   . HIS A 1 173 ? 29.71692 21.37441 6.15257   1.000 48.90990  ? 173 HIS A O   1 
ATOM   1337 C CB  . HIS A 1 173 ? 32.24046 20.78870 7.91509   1.000 42.62419  ? 173 HIS A CB  1 
ATOM   1338 C CG  . HIS A 1 173 ? 32.19864 21.72623 9.08132   1.000 54.01534  ? 173 HIS A CG  1 
ATOM   1339 N ND1 . HIS A 1 173 ? 31.74202 23.02254 8.97919   1.000 50.81021  ? 173 HIS A ND1 1 
ATOM   1340 C CD2 . HIS A 1 173 ? 32.54445 21.55017 10.37870  1.000 44.98764  ? 173 HIS A CD2 1 
ATOM   1341 C CE1 . HIS A 1 173 ? 31.81440 23.60663 10.16229  1.000 53.24082  ? 173 HIS A CE1 1 
ATOM   1342 N NE2 . HIS A 1 173 ? 32.29782 22.73475 11.02875  1.000 49.29630  ? 173 HIS A NE2 1 
ATOM   1343 N N   . PRO A 1 174 ? 28.95318 21.35375 8.26332   1.000 49.54125  ? 174 PRO A N   1 
ATOM   1344 C CA  . PRO A 1 174 ? 27.75088 22.12214 7.90329   1.000 46.57265  ? 174 PRO A CA  1 
ATOM   1345 C C   . PRO A 1 174 ? 28.02068 23.54634 7.44450   1.000 45.40043  ? 174 PRO A C   1 
ATOM   1346 O O   . PRO A 1 174 ? 27.08834 24.19639 6.95672   1.000 47.66532  ? 174 PRO A O   1 
ATOM   1347 C CB  . PRO A 1 174 ? 26.92607 22.10628 9.19742   1.000 53.64643  ? 174 PRO A CB  1 
ATOM   1348 C CG  . PRO A 1 174 ? 27.46542 20.95298 9.98709   1.000 49.47221  ? 174 PRO A CG  1 
ATOM   1349 C CD  . PRO A 1 174 ? 28.92491 20.91690 9.66753   1.000 39.99863  ? 174 PRO A CD  1 
ATOM   1350 N N   . SER A 1 175 ? 29.24262 24.06260 7.58048   1.000 43.84050  ? 175 SER A N   1 
ATOM   1351 C CA  . SER A 1 175 ? 29.52128 25.38360 7.02899   1.000 45.87992  ? 175 SER A CA  1 
ATOM   1352 C C   . SER A 1 175 ? 29.59251 25.37200 5.50830   1.000 51.77618  ? 175 SER A C   1 
ATOM   1353 O O   . SER A 1 175 ? 29.62969 26.44546 4.89656   1.000 52.59861  ? 175 SER A O   1 
ATOM   1354 C CB  . SER A 1 175 ? 30.82500 25.93975 7.60190   1.000 46.31559  ? 175 SER A CB  1 
ATOM   1355 O OG  . SER A 1 175 ? 31.92994 25.14229 7.22449   1.000 47.80342  ? 175 SER A OG  1 
ATOM   1356 N N   . ILE A 1 176 ? 29.61003 24.19410 4.89370   1.000 48.81939  ? 176 ILE A N   1 
ATOM   1357 C CA  . ILE A 1 176 ? 29.66317 24.05951 3.44376   1.000 50.69094  ? 176 ILE A CA  1 
ATOM   1358 C C   . ILE A 1 176 ? 28.23771 24.08326 2.90810   1.000 48.72478  ? 176 ILE A C   1 
ATOM   1359 O O   . ILE A 1 176 ? 27.41752 23.23106 3.26495   1.000 46.44711  ? 176 ILE A O   1 
ATOM   1360 C CB  . ILE A 1 176 ? 30.38311 22.76518 3.03935   1.000 48.04548  ? 176 ILE A CB  1 
ATOM   1361 C CG1 . ILE A 1 176 ? 31.72514 22.66166 3.76794   1.000 48.83721  ? 176 ILE A CG1 1 
ATOM   1362 C CG2 . ILE A 1 176 ? 30.57170 22.70284 1.53054   1.000 51.85442  ? 176 ILE A CG2 1 
ATOM   1363 C CD1 . ILE A 1 176 ? 32.40952 21.32779 3.59711   1.000 42.93423  ? 176 ILE A CD1 1 
ATOM   1364 N N   . GLU A 1 177 ? 27.93851 25.06138 2.05705   1.000 41.75945  ? 177 GLU A N   1 
ATOM   1365 C CA  . GLU A 1 177 ? 26.61864 25.17631 1.43682   1.000 46.66063  ? 177 GLU A CA  1 
ATOM   1366 C C   . GLU A 1 177 ? 26.57060 24.23320 0.24245   1.000 46.82395  ? 177 GLU A C   1 
ATOM   1367 O O   . GLU A 1 177 ? 26.92496 24.59381 -0.88178  1.000 44.39052  ? 177 GLU A O   1 
ATOM   1368 C CB  . GLU A 1 177 ? 26.33814 26.61620 1.02893   1.000 52.16776  ? 177 GLU A CB  1 
ATOM   1369 C CG  . GLU A 1 177 ? 26.05451 27.53530 2.20128   0.800 50.89321  ? 177 GLU A CG  1 
ATOM   1370 C CD  . GLU A 1 177 ? 25.86849 28.97635 1.78149   0.700 61.20165  ? 177 GLU A CD  1 
ATOM   1371 O OE1 . GLU A 1 177 ? 26.72414 29.49649 1.03467   0.700 59.52655  ? 177 GLU A OE1 1 
ATOM   1372 O OE2 . GLU A 1 177 ? 24.86151 29.58863 2.19437   0.700 66.26511  ? 177 GLU A OE2 1 
ATOM   1373 N N   . ALA A 1 178 ? 26.11666 23.00565 0.48818   1.000 43.12997  ? 178 ALA A N   1 
ATOM   1374 C CA  . ALA A 1 178 ? 26.14521 21.97113 -0.53397  1.000 37.72022  ? 178 ALA A CA  1 
ATOM   1375 C C   . ALA A 1 178 ? 25.07430 20.92743 -0.24841  1.000 38.91895  ? 178 ALA A C   1 
ATOM   1376 O O   . ALA A 1 178 ? 24.40116 20.95629 0.78491   1.000 42.36076  ? 178 ALA A O   1 
ATOM   1377 C CB  . ALA A 1 178 ? 27.52407 21.30943 -0.61401  1.000 35.06677  ? 178 ALA A CB  1 
ATOM   1378 N N   . MET A 1 179 ? 24.92568 20.00053 -1.19383  1.000 35.90250  ? 179 MET A N   1 
ATOM   1379 C CA  . MET A 1 179 ? 24.06477 18.83718 -1.04777  1.000 35.98818  ? 179 MET A CA  1 
ATOM   1380 C C   . MET A 1 179 ? 24.78999 17.62943 -1.62007  1.000 34.65481  ? 179 MET A C   1 
ATOM   1381 O O   . MET A 1 179 ? 25.62475 17.76183 -2.51816  1.000 40.60760  ? 179 MET A O   1 
ATOM   1382 C CB  . MET A 1 179 ? 22.71477 19.03304 -1.75146  1.000 40.96440  ? 179 MET A CB  1 
ATOM   1383 C CG  . MET A 1 179 ? 22.82148 19.29454 -3.24683  1.000 40.31985  ? 179 MET A CG  1 
ATOM   1384 S SD  . MET A 1 179 ? 21.22109 19.58411 -4.02393  1.000 46.57911  ? 179 MET A SD  1 
ATOM   1385 C CE  . MET A 1 179 ? 21.70815 19.79413 -5.73097  1.000 43.63050  ? 179 MET A CE  1 
ATOM   1386 N N   . GLN A 1 180 ? 24.47202 16.44858 -1.09346  1.000 34.33344  ? 180 GLN A N   1 
ATOM   1387 C CA  . GLN A 1 180 ? 25.16832 15.22980 -1.48186  1.000 33.87948  ? 180 GLN A CA  1 
ATOM   1388 C C   . GLN A 1 180 ? 24.16955 14.16484 -1.90913  1.000 43.14332  ? 180 GLN A C   1 
ATOM   1389 O O   . GLN A 1 180 ? 23.22241 13.86278 -1.17572  1.000 34.25067  ? 180 GLN A O   1 
ATOM   1390 C CB  . GLN A 1 180 ? 26.04626 14.70247 -0.34492  1.000 34.50717  ? 180 GLN A CB  1 
ATOM   1391 C CG  . GLN A 1 180 ? 26.92063 13.52947 -0.75051  1.000 31.94685  ? 180 GLN A CG  1 
ATOM   1392 C CD  . GLN A 1 180 ? 27.81085 13.04213 0.37260   1.000 38.58641  ? 180 GLN A CD  1 
ATOM   1393 O OE1 . GLN A 1 180 ? 28.52774 12.05231 0.22403   1.000 35.70100  ? 180 GLN A OE1 1 
ATOM   1394 N NE2 . GLN A 1 180 ? 27.77056 13.73437 1.50457   1.000 41.24240  ? 180 GLN A NE2 1 
ATOM   1395 N N   . LEU A 1 181 ? 24.39468 13.59256 -3.09004  1.000 34.34447  ? 181 LEU A N   1 
ATOM   1396 C CA  . LEU A 1 181 ? 23.53709 12.55548 -3.64888  1.000 35.70397  ? 181 LEU A CA  1 
ATOM   1397 C C   . LEU A 1 181 ? 24.20654 11.19569 -3.50469  1.000 34.06703  ? 181 LEU A C   1 
ATOM   1398 O O   . LEU A 1 181 ? 25.38917 11.04577 -3.82834  1.000 35.97216  ? 181 LEU A O   1 
ATOM   1399 C CB  . LEU A 1 181 ? 23.23649 12.83021 -5.12173  1.000 35.96462  ? 181 LEU A CB  1 
ATOM   1400 C CG  . LEU A 1 181 ? 22.35471 11.79228 -5.82230  1.000 35.15334  ? 181 LEU A CG  1 
ATOM   1401 C CD1 . LEU A 1 181 ? 20.90174 11.91524 -5.38376  1.000 28.71063  ? 181 LEU A CD1 1 
ATOM   1402 C CD2 . LEU A 1 181 ? 22.47817 11.91711 -7.33107  1.000 37.61658  ? 181 LEU A CD2 1 
ATOM   1403 N N   . THR A 1 182 ? 23.45034 10.21003 -3.01988  1.000 28.43835  ? 182 THR A N   1 
ATOM   1404 C CA  . THR A 1 182 ? 23.94613 8.85065  -2.86779  1.000 31.83605  ? 182 THR A CA  1 
ATOM   1405 C C   . THR A 1 182 ? 22.97332 7.86924  -3.50303  1.000 33.84015  ? 182 THR A C   1 
ATOM   1406 O O   . THR A 1 182 ? 21.77194 8.13085  -3.59412  1.000 33.50559  ? 182 THR A O   1 
ATOM   1407 C CB  . THR A 1 182 ? 24.15687 8.47799  -1.38864  1.000 37.05135  ? 182 THR A CB  1 
ATOM   1408 O OG1 . THR A 1 182 ? 22.95259 8.72592  -0.65049  1.000 32.98392  ? 182 THR A OG1 1 
ATOM   1409 C CG2 . THR A 1 182 ? 25.29765 9.28330  -0.78947  1.000 35.04094  ? 182 THR A CG2 1 
ATOM   1410 N N   . GLU A 1 183 ? 23.50827 6.73397  -3.93990  1.000 39.14184  ? 183 GLU A N   1 
ATOM   1411 C CA  . GLU A 1 183 ? 22.71634 5.69893  -4.58466  1.000 38.10369  ? 183 GLU A CA  1 
ATOM   1412 C C   . GLU A 1 183 ? 22.29204 4.63635  -3.57852  1.000 44.49324  ? 183 GLU A C   1 
ATOM   1413 O O   . GLU A 1 183 ? 22.95284 4.41506  -2.56024  1.000 40.55098  ? 183 GLU A O   1 
ATOM   1414 C CB  . GLU A 1 183 ? 23.50491 5.03444  -5.71404  1.000 40.97965  ? 183 GLU A CB  1 
ATOM   1415 C CG  . GLU A 1 183 ? 24.13531 5.99030  -6.70851  1.000 40.69319  ? 183 GLU A CG  1 
ATOM   1416 C CD  . GLU A 1 183 ? 24.94459 5.26421  -7.76291  1.000 45.15802  ? 183 GLU A CD  1 
ATOM   1417 O OE1 . GLU A 1 183 ? 25.20510 4.05555  -7.58046  1.000 44.16802  ? 183 GLU A OE1 1 
ATOM   1418 O OE2 . GLU A 1 183 ? 25.31977 5.89506  -8.77661  1.000 45.21942  ? 183 GLU A OE2 1 
ATOM   1419 N N   . MET A 1 184 ? 21.17593 3.97416  -3.88057  1.000 44.98797  ? 184 MET A N   1 
ATOM   1420 C CA  . MET A 1 184 ? 20.69661 2.82463  -3.11862  1.000 40.17871  ? 184 MET A CA  1 
ATOM   1421 C C   . MET A 1 184 ? 20.67790 1.61560  -4.04397  1.000 38.46343  ? 184 MET A C   1 
ATOM   1422 O O   . MET A 1 184 ? 19.78392 1.49629  -4.88952  1.000 50.29380  ? 184 MET A O   1 
ATOM   1423 C CB  . MET A 1 184 ? 19.30335 3.07226  -2.54012  1.000 40.16993  ? 184 MET A CB  1 
ATOM   1424 C CG  . MET A 1 184 ? 19.16205 4.31048  -1.67993  1.000 37.97629  ? 184 MET A CG  1 
ATOM   1425 S SD  . MET A 1 184 ? 17.46605 4.49421  -1.09797  1.000 49.20256  ? 184 MET A SD  1 
ATOM   1426 C CE  . MET A 1 184 ? 17.56673 6.04865  -0.21782  1.000 47.38378  ? 184 MET A CE  1 
ATOM   1427 N N   . ALA A 1 185 ? 21.66182 0.73045  -3.88264  1.000 34.59183  ? 185 ALA A N   1 
ATOM   1428 C CA  . ALA A 1 185 ? 21.72583 -0.55336 -4.58152  1.000 42.89769  ? 185 ALA A CA  1 
ATOM   1429 C C   . ALA A 1 185 ? 21.51805 -0.37731 -6.08881  1.000 53.69890  ? 185 ALA A C   1 
ATOM   1430 O O   . ALA A 1 185 ? 20.47334 -0.70491 -6.65289  1.000 44.98320  ? 185 ALA A O   1 
ATOM   1431 C CB  . ALA A 1 185 ? 20.70703 -1.53404 -3.99303  1.000 38.78270  ? 185 ALA A CB  1 
ATOM   1432 N N   . SER A 1 186 ? 22.55778 0.14803  -6.72916  1.000 49.32521  ? 186 SER A N   1 
ATOM   1433 C CA  . SER A 1 186 ? 22.50746 0.39852  -8.16101  1.000 45.22345  ? 186 SER A CA  1 
ATOM   1434 C C   . SER A 1 186 ? 22.80038 -0.87088 -8.94550  1.000 43.94882  ? 186 SER A C   1 
ATOM   1435 O O   . SER A 1 186 ? 23.71592 -1.62946 -8.61324  1.000 43.68007  ? 186 SER A O   1 
ATOM   1436 C CB  . SER A 1 186 ? 23.50719 1.48677  -8.55025  1.000 43.52174  ? 186 SER A CB  1 
ATOM   1437 O OG  . SER A 1 186 ? 23.62280 1.58557  -9.95986  1.000 66.45691  ? 186 SER A OG  1 
ATOM   1438 N N   . ILE A 1 187 ? 22.00822 -1.10204 -9.98560  1.000 51.47293  ? 187 ILE A N   1 
ATOM   1439 C CA  . ILE A 1 187 ? 22.31923 -2.14184 -10.95754 1.000 54.13273  ? 187 ILE A CA  1 
ATOM   1440 C C   . ILE A 1 187 ? 23.39256 -1.61256 -11.89448 1.000 48.83607  ? 187 ILE A C   1 
ATOM   1441 O O   . ILE A 1 187 ? 23.23969 -0.53861 -12.48847 1.000 56.27012  ? 187 ILE A O   1 
ATOM   1442 C CB  . ILE A 1 187 ? 21.06500 -2.56076 -11.74112 1.000 58.05223  ? 187 ILE A CB  1 
ATOM   1443 C CG1 . ILE A 1 187 ? 19.90011 -2.85078 -10.79510 1.000 58.86413  ? 187 ILE A CG1 1 
ATOM   1444 C CG2 . ILE A 1 187 ? 21.36361 -3.78062 -12.60107 1.000 58.36867  ? 187 ILE A CG2 1 
ATOM   1445 C CD1 . ILE A 1 187 ? 18.69844 -3.47003 -11.48361 1.000 57.63410  ? 187 ILE A CD1 1 
ATOM   1446 N N   . ASN A 1 188 ? 24.48721 -2.35375 -12.02130 1.000 55.03721  ? 188 ASN A N   1 
ATOM   1447 C CA  . ASN A 1 188 ? 25.56429 -1.99359 -12.93571 1.000 66.30276  ? 188 ASN A CA  1 
ATOM   1448 C C   . ASN A 1 188 ? 25.98334 -3.24444 -13.69344 1.000 66.70448  ? 188 ASN A C   1 
ATOM   1449 O O   . ASN A 1 188 ? 26.61513 -4.13850 -13.12293 1.000 71.13912  ? 188 ASN A O   1 
ATOM   1450 C CB  . ASN A 1 188 ? 26.74165 -1.37361 -12.18410 1.000 58.43607  ? 188 ASN A CB  1 
ATOM   1451 C CG  . ASN A 1 188 ? 26.59679 0.13013  -12.01034 1.000 56.50611  ? 188 ASN A CG  1 
ATOM   1452 O OD1 . ASN A 1 188 ? 26.99368 0.90264  -12.88411 1.000 56.98795  ? 188 ASN A OD1 1 
ATOM   1453 N ND2 . ASN A 1 188 ? 26.01870 0.55124  -10.89176 1.000 47.38012  ? 188 ASN A ND2 1 
ATOM   1454 N N   . ASN A 1 189 ? 25.61310 -3.31104 -14.97543 1.000 67.77865  ? 189 ASN A N   1 
ATOM   1455 C CA  . ASN A 1 189 ? 26.05703 -4.37525 -15.86924 1.000 68.94650  ? 189 ASN A CA  1 
ATOM   1456 C C   . ASN A 1 189 ? 26.25730 -3.84789 -17.28283 1.000 84.49954  ? 189 ASN A C   1 
ATOM   1457 O O   . ASN A 1 189 ? 26.56129 -2.66642 -17.46565 1.000 87.48282  ? 189 ASN A O   1 
ATOM   1458 C CB  . ASN A 1 189 ? 25.05689 -5.52591 -15.87593 1.000 67.67207  ? 189 ASN A CB  1 
ATOM   1459 C CG  . ASN A 1 189 ? 23.63895 -5.07261 -16.15207 1.000 73.10625  ? 189 ASN A CG  1 
ATOM   1460 O OD1 . ASN A 1 189 ? 23.41063 -3.98078 -16.67405 1.000 75.92895  ? 189 ASN A OD1 1 
ATOM   1461 N ND2 . ASN A 1 189 ? 22.67747 -5.90610 -15.79684 1.000 70.49122  ? 189 ASN A ND2 1 
ATOM   1462 N N   . ARG A 1 190 ? 26.07329 -4.71102 -18.28404 1.000 77.37154  ? 190 ARG A N   1 
ATOM   1463 C CA  . ARG A 1 190 ? 26.30019 -4.28779 -19.65621 1.000 78.14450  ? 190 ARG A CA  1 
ATOM   1464 C C   . ARG A 1 190 ? 25.28909 -3.24002 -20.09908 1.000 81.12855  ? 190 ARG A C   1 
ATOM   1465 O O   . ARG A 1 190 ? 25.64214 -2.33859 -20.87181 1.000 95.79574  ? 190 ARG A O   1 
ATOM   1466 C CB  . ARG A 1 190 ? 26.24922 -5.49923 -20.58985 1.000 85.79344  ? 190 ARG A CB  1 
ATOM   1467 N N   . VAL A 1 191 ? 24.05418 -3.31196 -19.60651 1.000 88.37696  ? 191 VAL A N   1 
ATOM   1468 C CA  . VAL A 1 191 ? 22.99934 -2.39528 -20.03949 1.000 84.01003  ? 191 VAL A CA  1 
ATOM   1469 C C   . VAL A 1 191 ? 22.99533 -1.11102 -19.21941 1.000 79.62171  ? 191 VAL A C   1 
ATOM   1470 O O   . VAL A 1 191 ? 22.90574 -0.01610 -19.77121 1.000 74.85347  ? 191 VAL A O   1 
ATOM   1471 C CB  . VAL A 1 191 ? 21.63260 -3.10767 -19.96522 1.000 86.71970  ? 191 VAL A CB  1 
ATOM   1472 C CG1 . VAL A 1 191 ? 20.48538 -2.10972 -20.13489 1.000 90.76276  ? 191 VAL A CG1 1 
ATOM   1473 C CG2 . VAL A 1 191 ? 21.53153 -4.18961 -21.02987 1.000 82.21617  ? 191 VAL A CG2 1 
ATOM   1474 N N   . TYR A 1 192 ? 23.09125 -1.21240 -17.89412 1.000 78.66538  ? 192 TYR A N   1 
ATOM   1475 C CA  . TYR A 1 192 ? 22.95716 -0.05602 -17.02196 1.000 79.23961  ? 192 TYR A CA  1 
ATOM   1476 C C   . TYR A 1 192 ? 24.30088 0.34035  -16.42432 1.000 75.45971  ? 192 TYR A C   1 
ATOM   1477 O O   . TYR A 1 192 ? 25.18207 -0.49979 -16.21451 1.000 68.68185  ? 192 TYR A O   1 
ATOM   1478 C CB  . TYR A 1 192 ? 21.94325 -0.33234 -15.91262 1.000 80.83497  ? 192 TYR A CB  1 
ATOM   1479 C CG  . TYR A 1 192 ? 20.52223 -0.34448 -16.41657 1.000 87.14230  ? 192 TYR A CG  1 
ATOM   1480 C CD1 . TYR A 1 192 ? 19.84804 0.84425  -16.66133 1.000 81.08915  ? 192 TYR A CD1 1 
ATOM   1481 C CD2 . TYR A 1 192 ? 19.86151 -1.53854 -16.66900 1.000 83.86135  ? 192 TYR A CD2 1 
ATOM   1482 C CE1 . TYR A 1 192 ? 18.55384 0.84708  -17.13191 1.000 73.94085  ? 192 TYR A CE1 1 
ATOM   1483 C CE2 . TYR A 1 192 ? 18.56107 -1.54720 -17.14159 1.000 84.75274  ? 192 TYR A CE2 1 
ATOM   1484 C CZ  . TYR A 1 192 ? 17.91398 -0.34893 -17.37022 1.000 80.60167  ? 192 TYR A CZ  1 
ATOM   1485 O OH  . TYR A 1 192 ? 16.62116 -0.33862 -17.83973 1.000 79.43230  ? 192 TYR A OH  1 
ATOM   1486 N N   . ARG A 1 193 ? 24.43981 1.63591  -16.14405 1.000 62.52428  ? 193 ARG A N   1 
ATOM   1487 C CA  . ARG A 1 193 ? 25.72491 2.19416  -15.73722 1.000 55.10780  ? 193 ARG A CA  1 
ATOM   1488 C C   . ARG A 1 193 ? 25.47846 3.47716  -14.96272 1.000 61.05294  ? 193 ARG A C   1 
ATOM   1489 O O   . ARG A 1 193 ? 24.92547 4.43401  -15.51340 1.000 54.37670  ? 193 ARG A O   1 
ATOM   1490 C CB  . ARG A 1 193 ? 26.59494 2.46026  -16.96218 1.000 63.31796  ? 193 ARG A CB  1 
ATOM   1491 C CG  . ARG A 1 193 ? 28.07892 2.55607  -16.69674 0.800 68.42657  ? 193 ARG A CG  1 
ATOM   1492 C CD  . ARG A 1 193 ? 28.82903 1.98000  -17.88086 0.800 65.57605  ? 193 ARG A CD  1 
ATOM   1493 N NE  . ARG A 1 193 ? 30.27116 2.15131  -17.77570 0.700 61.38889  ? 193 ARG A NE  1 
ATOM   1494 C CZ  . ARG A 1 193 ? 31.13503 1.73013  -18.68839 0.700 73.58023  ? 193 ARG A CZ  1 
ATOM   1495 N NH1 . ARG A 1 193 ? 30.73280 1.10151  -19.78174 0.700 65.97537  ? 193 ARG A NH1 1 
ATOM   1496 N NH2 . ARG A 1 193 ? 32.43370 1.94604  -18.50086 0.700 83.68758  ? 193 ARG A NH2 1 
ATOM   1497 N N   . THR A 1 194 ? 25.87856 3.49932  -13.69517 1.000 48.69377  ? 194 THR A N   1 
ATOM   1498 C CA  . THR A 1 194 ? 25.79076 4.68641  -12.85787 1.000 41.41544  ? 194 THR A CA  1 
ATOM   1499 C C   . THR A 1 194 ? 27.17973 5.05376  -12.35095 1.000 43.62415  ? 194 THR A C   1 
ATOM   1500 O O   . THR A 1 194 ? 28.13004 4.27291  -12.44828 1.000 38.99864  ? 194 THR A O   1 
ATOM   1501 C CB  . THR A 1 194 ? 24.83670 4.47162  -11.67509 1.000 46.21077  ? 194 THR A CB  1 
ATOM   1502 O OG1 . THR A 1 194 ? 25.39454 3.50127  -10.77776 1.000 39.52583  ? 194 THR A OG1 1 
ATOM   1503 C CG2 . THR A 1 194 ? 23.47955 3.98785  -12.16106 1.000 44.44027  ? 194 THR A CG2 1 
ATOM   1504 N N   . ILE A 1 195 ? 27.28859 6.26454  -11.79902 1.000 42.67275  ? 195 ILE A N   1 
ATOM   1505 C CA  . ILE A 1 195 ? 28.57971 6.73565  -11.31176 1.000 42.68793  ? 195 ILE A CA  1 
ATOM   1506 C C   . ILE A 1 195 ? 29.01470 5.94377  -10.08612 1.000 47.47632  ? 195 ILE A C   1 
ATOM   1507 O O   . ILE A 1 195 ? 30.21501 5.74384  -9.86068  1.000 38.66952  ? 195 ILE A O   1 
ATOM   1508 C CB  . ILE A 1 195 ? 28.51769 8.24809  -11.02209 1.000 43.48522  ? 195 ILE A CB  1 
ATOM   1509 C CG1 . ILE A 1 195 ? 29.89938 8.78431  -10.63978 1.000 41.57697  ? 195 ILE A CG1 1 
ATOM   1510 C CG2 . ILE A 1 195 ? 27.50231 8.55235  -9.92811  1.000 37.92233  ? 195 ILE A CG2 1 
ATOM   1511 C CD1 . ILE A 1 195 ? 30.92044 8.69059  -11.75116 1.000 41.20332  ? 195 ILE A CD1 1 
ATOM   1512 N N   . GLY A 1 196 ? 28.06531 5.46821  -9.29178  1.000 40.74539  ? 196 GLY A N   1 
ATOM   1513 C CA  . GLY A 1 196 ? 28.38894 4.74553  -8.06412  1.000 41.83125  ? 196 GLY A CA  1 
ATOM   1514 C C   . GLY A 1 196 ? 28.83858 5.61756  -6.91674  1.000 42.08486  ? 196 GLY A C   1 
ATOM   1515 O O   . GLY A 1 196 ? 28.31612 5.49663  -5.80526  1.000 45.94012  ? 196 GLY A O   1 
ATOM   1516 N N   . SER A 1 197 ? 29.79748 6.50724  -7.16053  1.000 43.57704  ? 197 SER A N   1 
ATOM   1517 C CA  . SER A 1 197 ? 30.31006 7.36272  -6.10524  1.000 40.81794  ? 197 SER A CA  1 
ATOM   1518 C C   . SER A 1 197 ? 29.25077 8.37659  -5.67630  1.000 42.36764  ? 197 SER A C   1 
ATOM   1519 O O   . SER A 1 197 ? 28.37677 8.74730  -6.46468  1.000 40.17375  ? 197 SER A O   1 
ATOM   1520 C CB  . SER A 1 197 ? 31.56146 8.10241  -6.57274  1.000 33.17818  ? 197 SER A CB  1 
ATOM   1521 O OG  . SER A 1 197 ? 32.55363 7.20400  -7.03527  1.000 40.46458  ? 197 SER A OG  1 
ATOM   1522 N N   . PRO A 1 198 ? 29.29621 8.82847  -4.42471  1.000 39.69807  ? 198 PRO A N   1 
ATOM   1523 C CA  . PRO A 1 198 ? 28.44272 9.95072  -4.02680  1.000 38.45564  ? 198 PRO A CA  1 
ATOM   1524 C C   . PRO A 1 198 ? 28.85046 11.21587 -4.76342  1.000 37.94600  ? 198 PRO A C   1 
ATOM   1525 O O   . PRO A 1 198 ? 29.99935 11.37487 -5.18071  1.000 34.17336  ? 198 PRO A O   1 
ATOM   1526 C CB  . PRO A 1 198 ? 28.69090 10.07542 -2.51851  1.000 40.89032  ? 198 PRO A CB  1 
ATOM   1527 C CG  . PRO A 1 198 ? 29.24995 8.75137  -2.10324  1.000 41.00518  ? 198 PRO A CG  1 
ATOM   1528 C CD  . PRO A 1 198 ? 30.03106 8.25867  -3.28354  1.000 33.87323  ? 198 PRO A CD  1 
ATOM   1529 N N   . LEU A 1 199 ? 27.88958 12.11747 -4.93238  1.000 32.88795  ? 199 LEU A N   1 
ATOM   1530 C CA  . LEU A 1 199 ? 28.11742 13.37841 -5.62061  1.000 37.17979  ? 199 LEU A CA  1 
ATOM   1531 C C   . LEU A 1 199 ? 27.77272 14.53433 -4.69523  1.000 39.73408  ? 199 LEU A C   1 
ATOM   1532 O O   . LEU A 1 199 ? 26.74311 14.50874 -4.01642  1.000 39.26417  ? 199 LEU A O   1 
ATOM   1533 C CB  . LEU A 1 199 ? 27.28327 13.47026 -6.90051  1.000 37.57432  ? 199 LEU A CB  1 
ATOM   1534 C CG  . LEU A 1 199 ? 27.50355 12.35945 -7.92663  1.000 36.77309  ? 199 LEU A CG  1 
ATOM   1535 C CD1 . LEU A 1 199 ? 26.66354 12.60484 -9.16984  1.000 40.18988  ? 199 LEU A CD1 1 
ATOM   1536 C CD2 . LEU A 1 199 ? 28.97599 12.24939 -8.28208  1.000 29.54175  ? 199 LEU A CD2 1 
ATOM   1537 N N   . VAL A 1 200 ? 28.63296 15.54860 -4.67684  1.000 42.15528  ? 200 VAL A N   1 
ATOM   1538 C CA  . VAL A 1 200 ? 28.45120 16.72917 -3.84070  1.000 34.61234  ? 200 VAL A CA  1 
ATOM   1539 C C   . VAL A 1 200 ? 28.29084 17.93593 -4.75407  1.000 41.49926  ? 200 VAL A C   1 
ATOM   1540 O O   . VAL A 1 200 ? 29.18992 18.24649 -5.54552  1.000 40.81975  ? 200 VAL A O   1 
ATOM   1541 C CB  . VAL A 1 200 ? 29.62470 16.92749 -2.87017  1.000 43.67615  ? 200 VAL A CB  1 
ATOM   1542 C CG1 . VAL A 1 200 ? 29.46983 18.23889 -2.11881  1.000 40.57226  ? 200 VAL A CG1 1 
ATOM   1543 C CG2 . VAL A 1 200 ? 29.71376 15.75744 -1.89837  1.000 38.72433  ? 200 VAL A CG2 1 
ATOM   1544 N N   . PHE A 1 201 ? 27.14818 18.62358 -4.63666  1.000 43.54775  ? 201 PHE A N   1 
ATOM   1545 C CA  . PHE A 1 201 ? 26.81083 19.74207 -5.50443  1.000 43.45556  ? 201 PHE A CA  1 
ATOM   1546 C C   . PHE A 1 201 ? 26.85426 21.06032 -4.74273  1.000 45.41910  ? 201 PHE A C   1 
ATOM   1547 O O   . PHE A 1 201 ? 26.45733 21.11061 -3.57468  1.000 46.71025  ? 201 PHE A O   1 
ATOM   1548 C CB  . PHE A 1 201 ? 25.41423 19.56213 -6.10741  1.000 38.57703  ? 201 PHE A CB  1 
ATOM   1549 C CG  . PHE A 1 201 ? 25.24616 18.28485 -6.87178  1.000 45.19499  ? 201 PHE A CG  1 
ATOM   1550 C CD1 . PHE A 1 201 ? 24.82446 17.12916 -6.23446  1.000 36.60166  ? 201 PHE A CD1 1 
ATOM   1551 C CD2 . PHE A 1 201 ? 25.51472 18.23791 -8.23000  1.000 39.11953  ? 201 PHE A CD2 1 
ATOM   1552 C CE1 . PHE A 1 201 ? 24.67253 15.95007 -6.93825  1.000 45.58624  ? 201 PHE A CE1 1 
ATOM   1553 C CE2 . PHE A 1 201 ? 25.36455 17.06337 -8.93972  1.000 43.95320  ? 201 PHE A CE2 1 
ATOM   1554 C CZ  . PHE A 1 201 ? 24.94286 15.91568 -8.29300  1.000 40.83707  ? 201 PHE A CZ  1 
ATOM   1555 N N   . PRO A 1 202 ? 27.32112 22.14244 -5.37358  1.000 47.83376  ? 202 PRO A N   1 
ATOM   1556 C CA  . PRO A 1 202 ? 27.31423 23.44795 -4.70130  1.000 41.26446  ? 202 PRO A CA  1 
ATOM   1557 C C   . PRO A 1 202 ? 25.97500 24.15354 -4.83439  1.000 40.89402  ? 202 PRO A C   1 
ATOM   1558 O O   . PRO A 1 202 ? 25.00061 23.55965 -5.30653  1.000 44.22787  ? 202 PRO A O   1 
ATOM   1559 C CB  . PRO A 1 202 ? 28.42609 24.21168 -5.42719  1.000 41.67223  ? 202 PRO A CB  1 
ATOM   1560 C CG  . PRO A 1 202 ? 28.37190 23.66574 -6.82162  1.000 48.58421  ? 202 PRO A CG  1 
ATOM   1561 C CD  . PRO A 1 202 ? 27.96865 22.20780 -6.69613  1.000 42.87259  ? 202 PRO A CD  1 
ATOM   1562 N N   . LYS A 1 203 ? 25.91556 25.41877 -4.42466  1.000 43.32430  ? 203 LYS A N   1 
ATOM   1563 C CA  . LYS A 1 203 ? 24.69531 26.19395 -4.58532  1.000 53.40870  ? 203 LYS A CA  1 
ATOM   1564 C C   . LYS A 1 203 ? 24.37548 26.39158 -6.06392  1.000 49.55668  ? 203 LYS A C   1 
ATOM   1565 O O   . LYS A 1 203 ? 25.24199 26.28489 -6.93735  1.000 52.53637  ? 203 LYS A O   1 
ATOM   1566 C CB  . LYS A 1 203 ? 24.81730 27.55592 -3.90043  1.000 54.08497  ? 203 LYS A CB  1 
ATOM   1567 C CG  . LYS A 1 203 ? 24.47390 27.55574 -2.42026  1.000 52.38560  ? 203 LYS A CG  1 
ATOM   1568 C CD  . LYS A 1 203 ? 24.25184 28.97325 -1.90985  1.000 59.94549  ? 203 LYS A CD  1 
ATOM   1569 C CE  . LYS A 1 203 ? 25.44020 29.86504 -2.22727  1.000 66.46857  ? 203 LYS A CE  1 
ATOM   1570 N NZ  . LYS A 1 203 ? 26.69499 29.33835 -1.62435  1.000 55.83465  ? 203 LYS A NZ  1 
ATOM   1571 N N   . HIS A 1 204 ? 23.09530 26.65963 -6.33307  1.000 50.53417  ? 204 HIS A N   1 
ATOM   1572 C CA  . HIS A 1 204 ? 22.58944 27.01574 -7.65684  1.000 60.62077  ? 204 HIS A CA  1 
ATOM   1573 C C   . HIS A 1 204 ? 22.64386 25.85261 -8.64206  1.000 56.97966  ? 204 HIS A C   1 
ATOM   1574 O O   . HIS A 1 204 ? 22.11956 25.95765 -9.75537  1.000 57.10826  ? 204 HIS A O   1 
ATOM   1575 C CB  . HIS A 1 204 ? 23.34960 28.22489 -8.21214  1.000 53.16244  ? 204 HIS A CB  1 
ATOM   1576 C CG  . HIS A 1 204 ? 23.41786 29.37841 -7.25971  1.000 61.52803  ? 204 HIS A CG  1 
ATOM   1577 N ND1 . HIS A 1 204 ? 22.30854 30.11336 -6.90022  1.000 62.54489  ? 204 HIS A ND1 1 
ATOM   1578 C CD2 . HIS A 1 204 ? 24.46169 29.92124 -6.58926  1.000 61.64288  ? 204 HIS A CD2 1 
ATOM   1579 C CE1 . HIS A 1 204 ? 22.66618 31.05991 -6.05081  1.000 66.28803  ? 204 HIS A CE1 1 
ATOM   1580 N NE2 . HIS A 1 204 ? 23.96755 30.96528 -5.84552  1.000 59.71275  ? 204 HIS A NE2 1 
ATOM   1581 N N   . HIS A 1 205 ? 23.26770 24.74368 -8.25303  1.000 50.92207  ? 205 HIS A N   1 
ATOM   1582 C CA  . HIS A 1 205 ? 23.22119 23.53429 -9.06270  1.000 50.44750  ? 205 HIS A CA  1 
ATOM   1583 C C   . HIS A 1 205 ? 21.88086 22.84175 -8.85893  1.000 54.39418  ? 205 HIS A C   1 
ATOM   1584 O O   . HIS A 1 205 ? 21.42060 22.68431 -7.72359  1.000 46.27301  ? 205 HIS A O   1 
ATOM   1585 C CB  . HIS A 1 205 ? 24.36942 22.59110 -8.70548  1.000 44.16152  ? 205 HIS A CB  1 
ATOM   1586 C CG  . HIS A 1 205 ? 25.64922 22.89954 -9.41819  1.000 44.32949  ? 205 HIS A CG  1 
ATOM   1587 N ND1 . HIS A 1 205 ? 26.59382 21.93593 -9.69807  1.000 38.45182  ? 205 HIS A ND1 1 
ATOM   1588 C CD2 . HIS A 1 205 ? 26.14121 24.06204 -9.90862  1.000 46.54850  ? 205 HIS A CD2 1 
ATOM   1589 C CE1 . HIS A 1 205 ? 27.61255 22.49172 -10.32853 1.000 51.91224  ? 205 HIS A CE1 1 
ATOM   1590 N NE2 . HIS A 1 205 ? 27.36256 23.78096 -10.47010 1.000 48.88320  ? 205 HIS A NE2 1 
ATOM   1591 N N   . VAL A 1 206 ? 21.25392 22.43457 -9.95896  1.000 49.12515  ? 206 VAL A N   1 
ATOM   1592 C CA  . VAL A 1 206 ? 19.93151 21.82180 -9.93663  1.000 43.40538  ? 206 VAL A CA  1 
ATOM   1593 C C   . VAL A 1 206 ? 20.06263 20.38209 -10.41173 1.000 54.98702  ? 206 VAL A C   1 
ATOM   1594 O O   . VAL A 1 206 ? 20.45432 20.13527 -11.56027 1.000 47.11604  ? 206 VAL A O   1 
ATOM   1595 C CB  . VAL A 1 206 ? 18.93094 22.59534 -10.80866 1.000 48.06470  ? 206 VAL A CB  1 
ATOM   1596 C CG1 . VAL A 1 206 ? 17.61611 21.83735 -10.89405 1.000 46.35841  ? 206 VAL A CG1 1 
ATOM   1597 C CG2 . VAL A 1 206 ? 18.71053 23.99451 -10.25317 1.000 44.93216  ? 206 VAL A CG2 1 
ATOM   1598 N N   . VAL A 1 207 ? 19.73518 19.43752 -9.53165  1.000 40.18311  ? 207 VAL A N   1 
ATOM   1599 C CA  . VAL A 1 207 ? 19.68810 18.02138 -9.86911  1.000 41.24982  ? 207 VAL A CA  1 
ATOM   1600 C C   . VAL A 1 207 ? 18.23183 17.62952 -10.05969 1.000 46.77530  ? 207 VAL A C   1 
ATOM   1601 O O   . VAL A 1 207 ? 17.39728 17.85764 -9.17511  1.000 49.77075  ? 207 VAL A O   1 
ATOM   1602 C CB  . VAL A 1 207 ? 20.35559 17.16490 -8.78177  1.000 40.28975  ? 207 VAL A CB  1 
ATOM   1603 C CG1 . VAL A 1 207 ? 20.19337 15.68426 -9.09850  1.000 41.94176  ? 207 VAL A CG1 1 
ATOM   1604 C CG2 . VAL A 1 207 ? 21.82252 17.52543 -8.65792  1.000 36.05704  ? 207 VAL A CG2 1 
ATOM   1605 N N   . SER A 1 208 ? 17.92452 17.04326 -11.21170 1.000 51.82392  ? 208 SER A N   1 
ATOM   1606 C CA  . SER A 1 208 ? 16.55721 16.72714 -11.59462 1.000 48.96704  ? 208 SER A CA  1 
ATOM   1607 C C   . SER A 1 208 ? 16.42232 15.23067 -11.83051 1.000 54.21474  ? 208 SER A C   1 
ATOM   1608 O O   . SER A 1 208 ? 17.24922 14.63032 -12.52512 1.000 55.50114  ? 208 SER A O   1 
ATOM   1609 C CB  . SER A 1 208 ? 16.15427 17.50285 -12.85137 1.000 47.68551  ? 208 SER A CB  1 
ATOM   1610 O OG  . SER A 1 208 ? 14.89595 17.07248 -13.33411 1.000 49.65557  ? 208 SER A OG  1 
ATOM   1611 N N   . LEU A 1 209 ? 15.38561 14.63466 -11.24808 1.000 54.79883  ? 209 LEU A N   1 
ATOM   1612 C CA  . LEU A 1 209 ? 15.06223 13.22911 -11.44695 1.000 53.47810  ? 209 LEU A CA  1 
ATOM   1613 C C   . LEU A 1 209 ? 13.81263 13.13089 -12.30937 1.000 58.72785  ? 209 LEU A C   1 
ATOM   1614 O O   . LEU A 1 209 ? 12.79710 13.76736 -12.01016 1.000 68.68670  ? 209 LEU A O   1 
ATOM   1615 C CB  . LEU A 1 209 ? 14.84992 12.51940 -10.10791 1.000 52.83661  ? 209 LEU A CB  1 
ATOM   1616 C CG  . LEU A 1 209 ? 15.99904 12.62515 -9.10278  1.000 54.27673  ? 209 LEU A CG  1 
ATOM   1617 C CD1 . LEU A 1 209 ? 15.74945 11.71650 -7.91025  1.000 53.45426  ? 209 LEU A CD1 1 
ATOM   1618 C CD2 . LEU A 1 209 ? 17.33576 12.30419 -9.75994  1.000 54.16403  ? 209 LEU A CD2 1 
ATOM   1619 N N   . GLN A 1 210 ? 13.89119 12.34074 -13.37865 1.000 58.19004  ? 210 GLN A N   1 
ATOM   1620 C CA  . GLN A 1 210 ? 12.81161 12.25741 -14.34791 1.000 64.69201  ? 210 GLN A CA  1 
ATOM   1621 C C   . GLN A 1 210 ? 12.45274 10.80346 -14.62406 1.000 68.15151  ? 210 GLN A C   1 
ATOM   1622 O O   . GLN A 1 210 ? 13.34308 9.95728  -14.76832 1.000 68.08053  ? 210 GLN A O   1 
ATOM   1623 C CB  . GLN A 1 210 ? 13.20583 12.96500 -15.65305 1.000 61.87430  ? 210 GLN A CB  1 
ATOM   1624 C CG  . GLN A 1 210 ? 13.53988 14.43943 -15.45930 1.000 60.33321  ? 210 GLN A CG  1 
ATOM   1625 C CD  . GLN A 1 210 ? 14.06232 15.10025 -16.71807 1.000 67.70720  ? 210 GLN A CD  1 
ATOM   1626 O OE1 . GLN A 1 210 ? 14.11361 14.48393 -17.78181 1.000 71.38639  ? 210 GLN A OE1 1 
ATOM   1627 N NE2 . GLN A 1 210 ? 14.45642 16.36394 -16.60175 1.000 67.31815  ? 210 GLN A NE2 1 
ATOM   1628 N N   . PRO A 1 211 ? 11.16420 10.48500 -14.70656 1.000 81.31738  ? 211 PRO A N   1 
ATOM   1629 C CA  . PRO A 1 211 ? 10.75069 9.08853  -14.86358 1.000 81.82251  ? 211 PRO A CA  1 
ATOM   1630 C C   . PRO A 1 211 ? 10.96097 8.58507  -16.28436 1.000 86.27875  ? 211 PRO A C   1 
ATOM   1631 O O   . PRO A 1 211 ? 11.08625 9.35163  -17.24148 1.000 79.51519  ? 211 PRO A O   1 
ATOM   1632 C CB  . PRO A 1 211 ? 9.26052  9.12516  -14.51009 1.000 87.87583  ? 211 PRO A CB  1 
ATOM   1633 C CG  . PRO A 1 211 ? 8.83168  10.49182 -14.92284 1.000 93.36756  ? 211 PRO A CG  1 
ATOM   1634 C CD  . PRO A 1 211 ? 10.01023 11.40113 -14.66176 1.000 82.75637  ? 211 PRO A CD  1 
ATOM   1635 N N   . VAL A 1 212 ? 10.99133 7.25718  -16.40352 1.000 85.28268  ? 212 VAL A N   1 
ATOM   1636 C CA  . VAL A 1 212 ? 11.22774 6.57426  -17.66936 1.000 80.81462  ? 212 VAL A CA  1 
ATOM   1637 C C   . VAL A 1 212 ? 10.00783 5.77070  -18.10473 1.000 98.75102  ? 212 VAL A C   1 
ATOM   1638 O O   . VAL A 1 212 ? 9.54037  5.89494  -19.24150 1.000 103.23966 ? 212 VAL A O   1 
ATOM   1639 C CB  . VAL A 1 212 ? 12.47847 5.67147  -17.59378 1.000 71.73453  ? 212 VAL A CB  1 
ATOM   1640 C CG1 . VAL A 1 212 ? 12.64573 4.88471  -18.88230 1.000 73.51292  ? 212 VAL A CG1 1 
ATOM   1641 C CG2 . VAL A 1 212 ? 13.71475 6.51094  -17.30943 1.000 68.17518  ? 212 VAL A CG2 1 
ATOM   1642 N N   . ASN A 1 213 ? 9.48145  4.93376  -17.21262 1.000 102.07374 ? 213 ASN A N   1 
ATOM   1643 C CA  . ASN A 1 213 ? 8.24680  4.20657  -17.47821 1.000 101.57707 ? 213 ASN A CA  1 
ATOM   1644 C C   . ASN A 1 213 ? 7.23568  4.47640  -16.37411 1.000 97.90619  ? 213 ASN A C   1 
ATOM   1645 O O   . ASN A 1 213 ? 6.26353  5.21013  -16.57614 1.000 106.39542 ? 213 ASN A O   1 
ATOM   1646 C CB  . ASN A 1 213 ? 8.51589  2.70535  -17.60273 1.000 103.14914 ? 213 ASN A CB  1 
ATOM   1647 C CG  . ASN A 1 213 ? 8.76028  2.27407  -19.03505 1.000 111.05317 ? 213 ASN A CG  1 
ATOM   1648 O OD1 . ASN A 1 213 ? 7.96770  2.57298  -19.92843 1.000 117.02339 ? 213 ASN A OD1 1 
ATOM   1649 N ND2 . ASN A 1 213 ? 9.86534  1.57357  -19.26286 1.000 112.50615 ? 213 ASN A ND2 1 
ATOM   1650 N N   . ASP A 1 214 ? 7.46090  3.88802  -15.20337 1.000 98.92832  ? 214 ASP A N   1 
ATOM   1651 C CA  . ASP A 1 214 ? 6.58722  4.11873  -14.06341 1.000 103.88079 ? 214 ASP A CA  1 
ATOM   1652 C C   . ASP A 1 214 ? 6.74793  5.55066  -13.56774 1.000 101.82107 ? 214 ASP A C   1 
ATOM   1653 O O   . ASP A 1 214 ? 7.87049  6.04943  -13.43031 1.000 100.41293 ? 214 ASP A O   1 
ATOM   1654 C CB  . ASP A 1 214 ? 6.90710  3.12032  -12.94940 1.000 97.24664  ? 214 ASP A CB  1 
ATOM   1655 C CG  . ASP A 1 214 ? 5.74359  2.90511  -12.00148 1.000 107.32268 ? 214 ASP A CG  1 
ATOM   1656 O OD1 . ASP A 1 214 ? 5.40892  3.83525  -11.23715 1.000 104.88802 ? 214 ASP A OD1 1 
ATOM   1657 O OD2 . ASP A 1 214 ? 5.15745  1.80241  -12.03001 1.000 107.84800 ? 214 ASP A OD2 1 
ATOM   1658 N N   . LYS A 1 215 ? 5.62245  6.21957  -13.31687 1.000 104.24585 ? 215 LYS A N   1 
ATOM   1659 C CA  . LYS A 1 215 ? 5.62196  7.58549  -12.80837 1.000 106.06872 ? 215 LYS A CA  1 
ATOM   1660 C C   . LYS A 1 215 ? 5.14205  7.66559  -11.36311 1.000 102.84627 ? 215 LYS A C   1 
ATOM   1661 O O   . LYS A 1 215 ? 4.76393  8.74558  -10.89833 1.000 93.51955  ? 215 LYS A O   1 
ATOM   1662 C CB  . LYS A 1 215 ? 4.76706  8.49104  -13.69738 1.000 101.83871 ? 215 LYS A CB  1 
ATOM   1663 C CG  . LYS A 1 215 ? 5.42191  8.90486  -15.00922 1.000 97.81755  ? 215 LYS A CG  1 
ATOM   1664 C CD  . LYS A 1 215 ? 4.88356  8.10486  -16.18574 1.000 107.43270 ? 215 LYS A CD  1 
ATOM   1665 C CE  . LYS A 1 215 ? 5.36695  8.67505  -17.51211 1.000 99.73393  ? 215 LYS A CE  1 
ATOM   1666 N NZ  . LYS A 1 215 ? 6.85202  8.65496  -17.62182 1.000 99.71256  ? 215 LYS A NZ  1 
ATOM   1667 N N   . ASP A 1 216 ? 5.14159  6.54483  -10.64565 1.000 112.21966 ? 216 ASP A N   1 
ATOM   1668 C CA  . ASP A 1 216 ? 4.70333  6.49441  -9.25726  1.000 105.48950 ? 216 ASP A CA  1 
ATOM   1669 C C   . ASP A 1 216 ? 5.85319  6.02045  -8.38084  1.000 105.17364 ? 216 ASP A C   1 
ATOM   1670 O O   . ASP A 1 216 ? 6.44368  4.96666  -8.64082  1.000 107.19555 ? 216 ASP A O   1 
ATOM   1671 C CB  . ASP A 1 216 ? 3.49462  5.56795  -9.08690  1.000 108.17376 ? 216 ASP A CB  1 
ATOM   1672 C CG  . ASP A 1 216 ? 2.23645  6.12036  -9.73123  1.000 116.65751 ? 216 ASP A CG  1 
ATOM   1673 O OD1 . ASP A 1 216 ? 2.34445  7.01899  -10.59141 1.000 117.56370 ? 216 ASP A OD1 1 
ATOM   1674 O OD2 . ASP A 1 216 ? 1.13393  5.65931  -9.36919  1.000 126.32470 ? 216 ASP A OD2 1 
ATOM   1675 N N   . PHE A 1 217 ? 6.16723  6.79882  -7.34717  1.000 97.11583  ? 217 PHE A N   1 
ATOM   1676 C CA  . PHE A 1 217 ? 7.22415  6.44732  -6.41021  1.000 89.06163  ? 217 PHE A CA  1 
ATOM   1677 C C   . PHE A 1 217 ? 6.89198  7.01950  -5.03953  1.000 78.90233  ? 217 PHE A C   1 
ATOM   1678 O O   . PHE A 1 217 ? 5.98184  7.83739  -4.88572  1.000 83.69955  ? 217 PHE A O   1 
ATOM   1679 C CB  . PHE A 1 217 ? 8.60451  6.95635  -6.85839  1.000 82.29297  ? 217 PHE A CB  1 
ATOM   1680 C CG  . PHE A 1 217 ? 8.59890  7.75638  -8.13023  1.000 91.40937  ? 217 PHE A CG  1 
ATOM   1681 C CD1 . PHE A 1 217 ? 8.00804  9.00821  -8.18680  1.000 89.37027  ? 217 PHE A CD1 1 
ATOM   1682 C CD2 . PHE A 1 217 ? 9.23958  7.27289  -9.25862  1.000 95.41039  ? 217 PHE A CD2 1 
ATOM   1683 C CE1 . PHE A 1 217 ? 8.02354  9.73898  -9.35494  1.000 90.66160  ? 217 PHE A CE1 1 
ATOM   1684 C CE2 . PHE A 1 217 ? 9.26258  8.00262  -10.42734 1.000 94.16333  ? 217 PHE A CE2 1 
ATOM   1685 C CZ  . PHE A 1 217 ? 8.65327  9.23775  -10.47675 1.000 96.47904  ? 217 PHE A CZ  1 
ATOM   1686 N N   . GLN A 1 218 ? 7.65161  6.57848  -4.03864  1.000 72.53078  ? 218 GLN A N   1 
ATOM   1687 C CA  . GLN A 1 218 ? 7.59044  7.15625  -2.70258  1.000 70.19450  ? 218 GLN A CA  1 
ATOM   1688 C C   . GLN A 1 218 ? 8.66847  8.22240  -2.56387  1.000 63.20549  ? 218 GLN A C   1 
ATOM   1689 O O   . GLN A 1 218 ? 9.84243  7.96870  -2.85158  1.000 55.22648  ? 218 GLN A O   1 
ATOM   1690 C CB  . GLN A 1 218 ? 7.77341  6.08670  -1.62353  1.000 68.16167  ? 218 GLN A CB  1 
ATOM   1691 C CG  . GLN A 1 218 ? 6.49416  5.38182  -1.20387  0.700 75.43502  ? 218 GLN A CG  1 
ATOM   1692 C CD  . GLN A 1 218 ? 6.25000  4.10430  -1.97790  0.600 83.00429  ? 218 GLN A CD  1 
ATOM   1693 O OE1 . GLN A 1 218 ? 7.18262  3.35910  -2.27640  0.600 83.02132  ? 218 GLN A OE1 1 
ATOM   1694 N NE2 . GLN A 1 218 ? 4.99071  3.84426  -2.30941  0.600 83.66476  ? 218 GLN A NE2 1 
ATOM   1695 N N   . ILE A 1 219 ? 8.26835  9.41031  -2.12191  1.000 64.53224  ? 219 ILE A N   1 
ATOM   1696 C CA  . ILE A 1 219 ? 9.18006  10.53101 -1.92504  1.000 62.63397  ? 219 ILE A CA  1 
ATOM   1697 C C   . ILE A 1 219 ? 9.16172  10.89747 -0.45014  1.000 66.26632  ? 219 ILE A C   1 
ATOM   1698 O O   . ILE A 1 219 ? 8.12255  11.31123 0.08013   1.000 59.52855  ? 219 ILE A O   1 
ATOM   1699 C CB  . ILE A 1 219 ? 8.79972  11.73982 -2.79278  1.000 64.37586  ? 219 ILE A CB  1 
ATOM   1700 C CG1 . ILE A 1 219 ? 8.84602  11.36558 -4.27572  1.000 58.02551  ? 219 ILE A CG1 1 
ATOM   1701 C CG2 . ILE A 1 219 ? 9.72504  12.91336 -2.50287  1.000 49.17885  ? 219 ILE A CG2 1 
ATOM   1702 C CD1 . ILE A 1 219 ? 8.35919  12.46121 -5.19251  1.000 61.27240  ? 219 ILE A CD1 1 
ATOM   1703 N N   . SER A 1 220 ? 10.30476 10.74665 0.20814   1.000 57.38556  ? 220 SER A N   1 
ATOM   1704 C CA  . SER A 1 220 ? 10.43980 11.08227 1.61565   1.000 54.28248  ? 220 SER A CA  1 
ATOM   1705 C C   . SER A 1 220 ? 11.13144 12.42970 1.76101   1.000 56.02278  ? 220 SER A C   1 
ATOM   1706 O O   . SER A 1 220 ? 12.07931 12.73320 1.03251   1.000 59.14991  ? 220 SER A O   1 
ATOM   1707 C CB  . SER A 1 220 ? 11.23337 10.01114 2.36311   1.000 57.08963  ? 220 SER A CB  1 
ATOM   1708 O OG  . SER A 1 220 ? 12.61586 10.10808 2.07281   1.000 58.52653  ? 220 SER A OG  1 
ATOM   1709 N N   . VAL A 1 221 ? 10.63919 13.23922 2.69381   1.000 59.99650  ? 221 VAL A N   1 
ATOM   1710 C CA  . VAL A 1 221 ? 11.29653 14.46995 3.11391   1.000 58.19743  ? 221 VAL A CA  1 
ATOM   1711 C C   . VAL A 1 221 ? 11.46643 14.37238 4.62034   1.000 63.15017  ? 221 VAL A C   1 
ATOM   1712 O O   . VAL A 1 221 ? 10.49228 14.49906 5.37374   1.000 60.39958  ? 221 VAL A O   1 
ATOM   1713 C CB  . VAL A 1 221 ? 10.50829 15.72724 2.72291   1.000 64.58536  ? 221 VAL A CB  1 
ATOM   1714 C CG1 . VAL A 1 221 ? 11.18071 16.96172 3.30208   1.000 60.58626  ? 221 VAL A CG1 1 
ATOM   1715 C CG2 . VAL A 1 221 ? 10.40389 15.83877 1.21017   1.000 57.13105  ? 221 VAL A CG2 1 
ATOM   1716 N N   . ASP A 1 222 ? 12.70507 14.14025 5.06075   1.000 55.71140  ? 222 ASP A N   1 
ATOM   1717 C CA  . ASP A 1 222 ? 13.02344 13.82498 6.45637   1.000 64.01224  ? 222 ASP A CA  1 
ATOM   1718 C C   . ASP A 1 222 ? 12.23367 12.57482 6.83654   1.000 64.91113  ? 222 ASP A C   1 
ATOM   1719 O O   . ASP A 1 222 ? 12.45814 11.51962 6.21861   1.000 72.61509  ? 222 ASP A O   1 
ATOM   1720 C CB  . ASP A 1 222 ? 12.79645 15.06213 7.32652   1.000 52.87688  ? 222 ASP A CB  1 
ATOM   1721 C CG  . ASP A 1 222 ? 13.79003 16.17278 7.02745   1.000 52.97133  ? 222 ASP A CG  1 
ATOM   1722 O OD1 . ASP A 1 222 ? 14.90080 15.85848 6.55410   1.000 47.44085  ? 222 ASP A OD1 1 
ATOM   1723 O OD2 . ASP A 1 222 ? 13.47316 17.35650 7.25382   1.000 48.78331  ? 222 ASP A OD2 1 
ATOM   1724 N N   . HIS A 1 223 ? 11.32041 12.63625 7.80970   1.000 73.12783  ? 223 HIS A N   1 
ATOM   1725 C CA  . HIS A 1 223 ? 10.61634 11.48037 8.35339   1.000 79.02787  ? 223 HIS A CA  1 
ATOM   1726 C C   . HIS A 1 223 ? 9.21589  11.30101 7.76536   1.000 82.66631  ? 223 HIS A C   1 
ATOM   1727 O O   . HIS A 1 223 ? 8.38814  10.59266 8.35081   1.000 91.97808  ? 223 HIS A O   1 
ATOM   1728 C CB  . HIS A 1 223 ? 10.53767 11.59804 9.87989   1.000 90.72678  ? 223 HIS A CB  1 
ATOM   1729 C CG  . HIS A 1 223 ? 9.92980  12.88036 10.36645  1.000 96.80121  ? 223 HIS A CG  1 
ATOM   1730 N ND1 . HIS A 1 223 ? 10.46477 14.11862 10.07967  1.000 87.54409  ? 223 HIS A ND1 1 
ATOM   1731 C CD2 . HIS A 1 223 ? 8.84187  13.11268 11.13902  1.000 88.37890  ? 223 HIS A CD2 1 
ATOM   1732 C CE1 . HIS A 1 223 ? 9.72498  15.05787 10.64158  1.000 88.12963  ? 223 HIS A CE1 1 
ATOM   1733 N NE2 . HIS A 1 223 ? 8.73369  14.47410 11.29063  1.000 84.30837  ? 223 HIS A NE2 1 
ATOM   1734 N N   . LEU A 1 224 ? 8.94137  11.91379 6.61498   1.000 76.19492  ? 224 LEU A N   1 
ATOM   1735 C CA  . LEU A 1 224 ? 7.59640  11.97034 6.04112   1.000 81.57892  ? 224 LEU A CA  1 
ATOM   1736 C C   . LEU A 1 224 ? 7.62723  11.40559 4.62173   1.000 88.60785  ? 224 LEU A C   1 
ATOM   1737 O O   . LEU A 1 224 ? 7.98702  12.11191 3.67513   1.000 76.19694  ? 224 LEU A O   1 
ATOM   1738 C CB  . LEU A 1 224 ? 7.07526  13.40480 6.05641   1.000 73.11015  ? 224 LEU A CB  1 
ATOM   1739 C CG  . LEU A 1 224 ? 7.34214  14.14812 7.36922   1.000 82.44104  ? 224 LEU A CG  1 
ATOM   1740 C CD1 . LEU A 1 224 ? 7.28233  15.64232 7.13903   1.000 80.26591  ? 224 LEU A CD1 1 
ATOM   1741 C CD2 . LEU A 1 224 ? 6.35941  13.73651 8.45977   1.000 76.10167  ? 224 LEU A CD2 1 
ATOM   1742 N N   . SER A 1 225 ? 7.24588  10.13598 4.47587   1.000 100.69446 ? 225 SER A N   1 
ATOM   1743 C CA  . SER A 1 225 ? 7.21557  9.47648  3.17519   1.000 101.31587 ? 225 SER A CA  1 
ATOM   1744 C C   . SER A 1 225 ? 5.85684  9.70651  2.52328   1.000 94.85525  ? 225 SER A C   1 
ATOM   1745 O O   . SER A 1 225 ? 4.81801  9.36127  3.09833   1.000 86.40142  ? 225 SER A O   1 
ATOM   1746 C CB  . SER A 1 225 ? 7.49732  7.98232  3.31728   1.000 105.87011 ? 225 SER A CB  1 
ATOM   1747 O OG  . SER A 1 225 ? 7.76342  7.39223  2.05667   1.000 101.80346 ? 225 SER A OG  1 
ATOM   1748 N N   . ILE A 1 226 ? 5.86840  10.28165 1.32370   1.000 93.59997  ? 226 ILE A N   1 
ATOM   1749 C CA  . ILE A 1 226 ? 4.65638  10.68197 0.61880   1.000 90.99073  ? 226 ILE A CA  1 
ATOM   1750 C C   . ILE A 1 226 ? 4.63756  9.98485  -0.73375  1.000 87.82303  ? 226 ILE A C   1 
ATOM   1751 O O   . ILE A 1 226 ? 5.56416  10.15427 -1.53645  1.000 77.41802  ? 226 ILE A O   1 
ATOM   1752 C CB  . ILE A 1 226 ? 4.58369  12.20624 0.43803   1.000 89.24979  ? 226 ILE A CB  1 
ATOM   1753 C CG1 . ILE A 1 226 ? 5.24236  12.91973 1.61972   1.000 80.80768  ? 226 ILE A CG1 1 
ATOM   1754 C CG2 . ILE A 1 226 ? 3.13875  12.65608 0.28008   1.000 86.96942  ? 226 ILE A CG2 1 
ATOM   1755 C CD1 . ILE A 1 226 ? 6.04868  14.13461 1.21965   1.000 68.63388  ? 226 ILE A CD1 1 
ATOM   1756 N N   . LEU A 1 227 ? 3.58463  9.21196  -0.99159  1.000 93.18524  ? 227 LEU A N   1 
ATOM   1757 C CA  . LEU A 1 227 ? 3.37867  8.63905  -2.31593  1.000 97.80092  ? 227 LEU A CA  1 
ATOM   1758 C C   . LEU A 1 227 ? 2.82122  9.71481  -3.23814  1.000 100.89406 ? 227 LEU A C   1 
ATOM   1759 O O   . LEU A 1 227 ? 1.73392  10.24880 -2.99288  1.000 97.50650  ? 227 LEU A O   1 
ATOM   1760 C CB  . LEU A 1 227 ? 2.43031  7.44437  -2.26168  1.000 99.79324  ? 227 LEU A CB  1 
ATOM   1761 C CG  . LEU A 1 227 ? 2.10025  6.88000  -3.64834  1.000 99.19761  ? 227 LEU A CG  1 
ATOM   1762 C CD1 . LEU A 1 227 ? 3.28946  6.12271  -4.22737  1.000 94.28765  ? 227 LEU A CD1 1 
ATOM   1763 C CD2 . LEU A 1 227 ? 0.85734  6.00303  -3.61896  1.000 89.35238  ? 227 LEU A CD2 1 
ATOM   1764 N N   . HIS A 1 228 ? 3.56018  10.03156 -4.29492  1.000 106.47218 ? 228 HIS A N   1 
ATOM   1765 C CA  . HIS A 1 228 ? 3.17327  11.06446 -5.24408  1.000 111.01300 ? 228 HIS A CA  1 
ATOM   1766 C C   . HIS A 1 228 ? 2.87957  10.42566 -6.59453  1.000 110.48034 ? 228 HIS A C   1 
ATOM   1767 O O   . HIS A 1 228 ? 3.65538  9.59102  -7.07360  1.000 102.86309 ? 228 HIS A O   1 
ATOM   1768 C CB  . HIS A 1 228 ? 4.27176  12.12108 -5.37113  1.000 97.22564  ? 228 HIS A CB  1 
ATOM   1769 N N   . ARG A 1 229 ? 1.76026  10.81435 -7.19974  1.000 105.71912 ? 229 ARG A N   1 
ATOM   1770 C CA  . ARG A 1 229 ? 1.31125  10.24721 -8.46141  1.000 98.59848  ? 229 ARG A CA  1 
ATOM   1771 C C   . ARG A 1 229 ? 1.43112  11.26275 -9.58820  1.000 101.29018 ? 229 ARG A C   1 
ATOM   1772 O O   . ARG A 1 229 ? 1.39428  12.47616 -9.36332  1.000 101.13233 ? 229 ARG A O   1 
ATOM   1773 C CB  . ARG A 1 229 ? -0.13703 9.76307  -8.37049  1.000 108.55622 ? 229 ARG A CB  1 
ATOM   1774 C CG  . ARG A 1 229 ? -0.27046 8.31649  -7.95652  1.000 111.92222 ? 229 ARG A CG  1 
ATOM   1775 C CD  . ARG A 1 229 ? -1.68656 7.81104  -8.15574  1.000 114.40194 ? 229 ARG A CD  1 
ATOM   1776 N NE  . ARG A 1 229 ? -2.17060 7.11611  -6.97021  1.000 120.98849 ? 229 ARG A NE  1 
ATOM   1777 C CZ  . ARG A 1 229 ? -1.78810 5.89965  -6.60687  1.000 122.97787 ? 229 ARG A CZ  1 
ATOM   1778 N NH1 . ARG A 1 229 ? -0.91594 5.20592  -7.32064  1.000 119.32678 ? 229 ARG A NH1 1 
ATOM   1779 N NH2 . ARG A 1 229 ? -2.28845 5.36776  -5.49591  1.000 126.05327 ? 229 ARG A NH2 1 
ATOM   1780 N N   . ASP A 1 230 ? 1.56042  10.73972 -10.80867 1.000 102.63381 ? 230 ASP A N   1 
ATOM   1781 C CA  . ASP A 1 230 ? 1.69097  11.55419 -12.01631 1.000 99.50826  ? 230 ASP A CA  1 
ATOM   1782 C C   . ASP A 1 230 ? 2.83951  12.55035 -11.88224 1.000 101.37269 ? 230 ASP A C   1 
ATOM   1783 O O   . ASP A 1 230 ? 2.72849  13.71911 -12.25837 1.000 105.67676 ? 230 ASP A O   1 
ATOM   1784 C CB  . ASP A 1 230 ? 0.37882  12.27007 -12.34388 1.000 104.22568 ? 230 ASP A CB  1 
ATOM   1785 C CG  . ASP A 1 230 ? 0.31966  12.74868 -13.78097 1.000 109.42175 ? 230 ASP A CG  1 
ATOM   1786 O OD1 . ASP A 1 230 ? 1.09239  12.22824 -14.61284 1.000 107.96459 ? 230 ASP A OD1 1 
ATOM   1787 O OD2 . ASP A 1 230 ? -0.49243 13.65050 -14.07637 1.000 115.07576 ? 230 ASP A OD2 1 
ATOM   1788 N N   . VAL A 1 231 ? 3.95426  12.08254 -11.33200 1.000 96.50425  ? 231 VAL A N   1 
ATOM   1789 C CA  . VAL A 1 231 ? 5.11936  12.93480 -11.13077 1.000 85.90257  ? 231 VAL A CA  1 
ATOM   1790 C C   . VAL A 1 231 ? 5.91631  13.00493 -12.42423 1.000 86.58303  ? 231 VAL A C   1 
ATOM   1791 O O   . VAL A 1 231 ? 6.27609  11.97429 -13.00580 1.000 94.30543  ? 231 VAL A O   1 
ATOM   1792 C CB  . VAL A 1 231 ? 5.98419  12.41129 -9.97553  1.000 89.28672  ? 231 VAL A CB  1 
ATOM   1793 C CG1 . VAL A 1 231 ? 7.27937  13.20501 -9.87823  1.000 82.16949  ? 231 VAL A CG1 1 
ATOM   1794 C CG2 . VAL A 1 231 ? 5.21722  12.48522 -8.67921  1.000 92.67680  ? 231 VAL A CG2 1 
ATOM   1795 N N   . GLN A 1 232 ? 6.19355  14.22569 -12.87822 1.000 82.23858  ? 232 GLN A N   1 
ATOM   1796 C CA  . GLN A 1 232 ? 7.00934  14.43713 -14.06324 1.000 80.02573  ? 232 GLN A CA  1 
ATOM   1797 C C   . GLN A 1 232 ? 8.45217  14.79474 -13.74179 1.000 75.41231  ? 232 GLN A C   1 
ATOM   1798 O O   . GLN A 1 232 ? 9.32041  14.61956 -14.60410 1.000 75.93266  ? 232 GLN A O   1 
ATOM   1799 C CB  . GLN A 1 232 ? 6.40515  15.54488 -14.93563 1.000 76.26365  ? 232 GLN A CB  1 
ATOM   1800 N N   . GLU A 1 233 ? 8.73121  15.27819 -12.53317 1.000 67.81922  ? 233 GLU A N   1 
ATOM   1801 C CA  . GLU A 1 233 ? 10.07099 15.74921 -12.21548 1.000 62.78798  ? 233 GLU A CA  1 
ATOM   1802 C C   . GLU A 1 233 ? 10.20739 15.92810 -10.71028 1.000 69.48411  ? 233 GLU A C   1 
ATOM   1803 O O   . GLU A 1 233 ? 9.23535  16.24719 -10.01835 1.000 62.07282  ? 233 GLU A O   1 
ATOM   1804 C CB  . GLU A 1 233 ? 10.37294 17.07064 -12.93132 1.000 65.33759  ? 233 GLU A CB  1 
ATOM   1805 C CG  . GLU A 1 233 ? 11.83585 17.44967 -12.93718 1.000 67.97051  ? 233 GLU A CG  1 
ATOM   1806 C CD  . GLU A 1 233 ? 12.06802 18.84777 -13.46620 1.000 62.77449  ? 233 GLU A CD  1 
ATOM   1807 O OE1 . GLU A 1 233 ? 11.09584 19.62879 -13.52287 1.000 65.88837  ? 233 GLU A OE1 1 
ATOM   1808 O OE2 . GLU A 1 233 ? 13.22214 19.16666 -13.81945 1.000 64.15016  ? 233 GLU A OE2 1 
ATOM   1809 N N   . ILE A 1 234 ? 11.42665 15.71360 -10.21848 1.000 65.78090  ? 234 ILE A N   1 
ATOM   1810 C CA  . ILE A 1 234 ? 11.80809 16.00733 -8.84157  1.000 58.77677  ? 234 ILE A CA  1 
ATOM   1811 C C   . ILE A 1 234 ? 13.10326 16.80419 -8.89498  1.000 57.85459  ? 234 ILE A C   1 
ATOM   1812 O O   . ILE A 1 234 ? 14.12326 16.30028 -9.38052  1.000 56.27354  ? 234 ILE A O   1 
ATOM   1813 C CB  . ILE A 1 234 ? 11.99358 14.73276 -8.00223  1.000 60.65389  ? 234 ILE A CB  1 
ATOM   1814 C CG1 . ILE A 1 234 ? 10.73815 13.86132 -8.06360  1.000 59.36231  ? 234 ILE A CG1 1 
ATOM   1815 C CG2 . ILE A 1 234 ? 12.32899 15.09355 -6.56120  1.000 50.52896  ? 234 ILE A CG2 1 
ATOM   1816 C CD1 . ILE A 1 234 ? 10.98298 12.41306 -7.71248  1.000 55.68313  ? 234 ILE A CD1 1 
ATOM   1817 N N   . ARG A 1 235 ? 13.06760 18.04004 -8.40537  1.000 53.10180  ? 235 ARG A N   1 
ATOM   1818 C CA  . ARG A 1 235 ? 14.19240 18.95851 -8.52477  1.000 58.99579  ? 235 ARG A CA  1 
ATOM   1819 C C   . ARG A 1 235 ? 14.83158 19.19502 -7.16363  1.000 49.00930  ? 235 ARG A C   1 
ATOM   1820 O O   . ARG A 1 235 ? 14.14296 19.53731 -6.19753  1.000 51.89104  ? 235 ARG A O   1 
ATOM   1821 C CB  . ARG A 1 235 ? 13.75002 20.28447 -9.14473  1.000 51.58691  ? 235 ARG A CB  1 
ATOM   1822 C CG  . ARG A 1 235 ? 13.19220 20.13362 -10.55113 1.000 61.43879  ? 235 ARG A CG  1 
ATOM   1823 C CD  . ARG A 1 235 ? 13.36237 21.40087 -11.37208 0.800 56.80496  ? 235 ARG A CD  1 
ATOM   1824 N NE  . ARG A 1 235 ? 12.55559 22.50608 -10.86851 0.700 58.22813  ? 235 ARG A NE  1 
ATOM   1825 C CZ  . ARG A 1 235 ? 11.29443 22.72870 -11.21135 0.700 59.68488  ? 235 ARG A CZ  1 
ATOM   1826 N NH1 . ARG A 1 235 ? 10.65284 21.92400 -12.04170 0.700 61.44384  ? 235 ARG A NH1 1 
ATOM   1827 N NH2 . ARG A 1 235 ? 10.66160 23.78524 -10.70847 0.700 65.47882  ? 235 ARG A NH2 1 
ATOM   1828 N N   . TYR A 1 236 ? 16.14801 19.01402 -7.09841  1.000 44.11062  ? 236 TYR A N   1 
ATOM   1829 C CA  . TYR A 1 236 ? 16.92533 19.17954 -5.87800  1.000 48.89539  ? 236 TYR A CA  1 
ATOM   1830 C C   . TYR A 1 236 ? 17.91419 20.32167 -6.05357  1.000 48.75105  ? 236 TYR A C   1 
ATOM   1831 O O   . TYR A 1 236 ? 18.60150 20.40118 -7.07747  1.000 49.73575  ? 236 TYR A O   1 
ATOM   1832 C CB  . TYR A 1 236 ? 17.68415 17.89570 -5.52620  1.000 42.49172  ? 236 TYR A CB  1 
ATOM   1833 C CG  . TYR A 1 236 ? 16.81964 16.76784 -5.01429  1.000 44.21059  ? 236 TYR A CG  1 
ATOM   1834 C CD1 . TYR A 1 236 ? 15.92342 16.96753 -3.97296  1.000 48.04142  ? 236 TYR A CD1 1 
ATOM   1835 C CD2 . TYR A 1 236 ? 16.90346 15.50019 -5.57308  1.000 41.84566  ? 236 TYR A CD2 1 
ATOM   1836 C CE1 . TYR A 1 236 ? 15.13783 15.93497 -3.50254  1.000 47.18639  ? 236 TYR A CE1 1 
ATOM   1837 C CE2 . TYR A 1 236 ? 16.11880 14.46190 -5.11010  1.000 49.84213  ? 236 TYR A CE2 1 
ATOM   1838 C CZ  . TYR A 1 236 ? 15.23747 14.68640 -4.07385  1.000 53.78863  ? 236 TYR A CZ  1 
ATOM   1839 O OH  . TYR A 1 236 ? 14.45159 13.66000 -3.60399  1.000 54.38266  ? 236 TYR A OH  1 
ATOM   1840 N N   . GLU A 1 237 ? 17.98578 21.19603 -5.05383  1.000 46.86031  ? 237 GLU A N   1 
ATOM   1841 C CA  . GLU A 1 237 ? 18.98097 22.25759 -5.02617  1.000 49.36222  ? 237 GLU A CA  1 
ATOM   1842 C C   . GLU A 1 237 ? 19.09079 22.76645 -3.59851  1.000 44.77605  ? 237 GLU A C   1 
ATOM   1843 O O   . GLU A 1 237 ? 18.15143 22.65276 -2.80471  1.000 46.08305  ? 237 GLU A O   1 
ATOM   1844 C CB  . GLU A 1 237 ? 18.62955 23.39978 -5.98841  1.000 48.05063  ? 237 GLU A CB  1 
ATOM   1845 C CG  . GLU A 1 237 ? 17.36535 24.16005 -5.62194  1.000 54.37313  ? 237 GLU A CG  1 
ATOM   1846 C CD  . GLU A 1 237 ? 16.90320 25.08536 -6.73339  1.000 65.91283  ? 237 GLU A CD  1 
ATOM   1847 O OE1 . GLU A 1 237 ? 17.56781 26.11768 -6.97635  1.000 58.78676  ? 237 GLU A OE1 1 
ATOM   1848 O OE2 . GLU A 1 237 ? 15.87536 24.77392 -7.37069  1.000 56.18213  ? 237 GLU A OE2 1 
ATOM   1849 N N   . VAL A 1 238 ? 20.26220 23.32332 -3.28155  1.000 45.79270  ? 238 VAL A N   1 
ATOM   1850 C CA  . VAL A 1 238 ? 20.46829 23.90924 -1.96478  1.000 49.58771  ? 238 VAL A CA  1 
ATOM   1851 C C   . VAL A 1 238 ? 19.51962 25.08215 -1.78741  1.000 53.38350  ? 238 VAL A C   1 
ATOM   1852 O O   . VAL A 1 238 ? 19.42125 25.96265 -2.65226  1.000 53.61997  ? 238 VAL A O   1 
ATOM   1853 C CB  . VAL A 1 238 ? 21.93167 24.33862 -1.78780  1.000 48.09508  ? 238 VAL A CB  1 
ATOM   1854 C CG1 . VAL A 1 238 ? 22.12384 25.00684 -0.44120  1.000 44.17776  ? 238 VAL A CG1 1 
ATOM   1855 C CG2 . VAL A 1 238 ? 22.85448 23.13984 -1.92762  1.000 37.94673  ? 238 VAL A CG2 1 
ATOM   1856 N N   . SER A 1 239 ? 18.81146 25.09981 -0.66290  1.000 51.44506  ? 239 SER A N   1 
ATOM   1857 C CA  . SER A 1 239 ? 17.78764 26.10827 -0.43892  1.000 47.37930  ? 239 SER A CA  1 
ATOM   1858 C C   . SER A 1 239 ? 18.40815 27.45902 -0.10568  1.000 53.15665  ? 239 SER A C   1 
ATOM   1859 O O   . SER A 1 239 ? 19.51615 27.54738 0.42664   1.000 52.95720  ? 239 SER A O   1 
ATOM   1860 C CB  . SER A 1 239 ? 16.85256 25.67247 0.69048   1.000 50.62016  ? 239 SER A CB  1 
ATOM   1861 O OG  . SER A 1 239 ? 15.95476 26.71168 1.03394   1.000 51.65085  ? 239 SER A OG  1 
ATOM   1862 N N   . ALA A 1 240 ? 17.67639 28.52483 -0.43775  1.000 54.33745  ? 240 ALA A N   1 
ATOM   1863 C CA  . ALA A 1 240 ? 18.07535 29.85880 -0.00787  1.000 59.09828  ? 240 ALA A CA  1 
ATOM   1864 C C   . ALA A 1 240 ? 17.77153 30.09201 1.46428   1.000 63.31629  ? 240 ALA A C   1 
ATOM   1865 O O   . ALA A 1 240 ? 18.29421 31.04450 2.04943   1.000 59.34058  ? 240 ALA A O   1 
ATOM   1866 C CB  . ALA A 1 240 ? 17.38282 30.92081 -0.86491  1.000 47.34477  ? 240 ALA A CB  1 
ATOM   1867 N N   . LYS A 1 241 ? 16.94732 29.24305 2.06978   1.000 58.51852  ? 241 LYS A N   1 
ATOM   1868 C CA  . LYS A 1 241 ? 16.59791 29.35283 3.47661   1.000 58.54133  ? 241 LYS A CA  1 
ATOM   1869 C C   . LYS A 1 241 ? 17.56405 28.54210 4.33072   1.000 56.05048  ? 241 LYS A C   1 
ATOM   1870 O O   . LYS A 1 241 ? 18.15119 27.55628 3.87652   1.000 49.50577  ? 241 LYS A O   1 
ATOM   1871 C CB  . LYS A 1 241 ? 15.16647 28.86925 3.71550   1.000 59.48204  ? 241 LYS A CB  1 
ATOM   1872 C CG  . LYS A 1 241 ? 14.11067 29.59308 2.89390   1.000 58.43613  ? 241 LYS A CG  1 
ATOM   1873 C CD  . LYS A 1 241 ? 12.74278 28.96283 3.09901   1.000 70.90498  ? 241 LYS A CD  1 
ATOM   1874 C CE  . LYS A 1 241 ? 11.65189 29.73469 2.37784   1.000 76.83030  ? 241 LYS A CE  1 
ATOM   1875 N NZ  . LYS A 1 241 ? 10.31661 29.10857 2.58658   1.000 72.00870  ? 241 LYS A NZ  1 
ATOM   1876 N N   . LYS A 1 242 ? 17.72142 28.96914 5.58153   1.000 60.42927  ? 242 LYS A N   1 
ATOM   1877 C CA  . LYS A 1 242 ? 18.61291 28.31580 6.52714   1.000 57.16362  ? 242 LYS A CA  1 
ATOM   1878 C C   . LYS A 1 242 ? 17.92067 28.16082 7.87362   1.000 59.62705  ? 242 LYS A C   1 
ATOM   1879 O O   . LYS A 1 242 ? 17.05157 28.95762 8.23929   1.000 65.10358  ? 242 LYS A O   1 
ATOM   1880 C CB  . LYS A 1 242 ? 19.91849 29.10281 6.71121   1.000 62.16001  ? 242 LYS A CB  1 
ATOM   1881 C CG  . LYS A 1 242 ? 20.79459 29.17218 5.47320   1.000 65.47343  ? 242 LYS A CG  1 
ATOM   1882 C CD  . LYS A 1 242 ? 22.20443 29.59694 5.83992   1.000 66.40421  ? 242 LYS A CD  1 
ATOM   1883 C CE  . LYS A 1 242 ? 23.23332 28.71098 5.16190   1.000 66.57853  ? 242 LYS A CE  1 
ATOM   1884 N NZ  . LYS A 1 242 ? 24.52022 28.69556 5.90877   1.000 64.73984  ? 242 LYS A NZ  1 
ATOM   1885 N N   . ILE A 1 243 ? 18.31487 27.12041 8.60750   1.000 56.36412  ? 243 ILE A N   1 
ATOM   1886 C CA  . ILE A 1 243 ? 17.85210 26.90590 9.97248   1.000 58.33887  ? 243 ILE A CA  1 
ATOM   1887 C C   . ILE A 1 243 ? 18.84479 27.55331 10.92531  1.000 57.34296  ? 243 ILE A C   1 
ATOM   1888 O O   . ILE A 1 243 ? 20.06294 27.44685 10.74324  1.000 48.35417  ? 243 ILE A O   1 
ATOM   1889 C CB  . ILE A 1 243 ? 17.67965 25.40377 10.26997  1.000 53.65153  ? 243 ILE A CB  1 
ATOM   1890 C CG1 . ILE A 1 243 ? 17.21764 25.19782 11.71788  1.000 52.95856  ? 243 ILE A CG1 1 
ATOM   1891 C CG2 . ILE A 1 243 ? 18.96764 24.63590 9.99257   1.000 43.52939  ? 243 ILE A CG2 1 
ATOM   1892 C CD1 . ILE A 1 243 ? 17.12413 23.74896 12.13616  1.000 49.32814  ? 243 ILE A CD1 1 
ATOM   1893 N N   . HIS A 1 244 ? 18.32802 28.24085 11.93819  1.000 53.94527  ? 244 HIS A N   1 
ATOM   1894 C CA  . HIS A 1 244 ? 19.15203 28.98061 12.88260  1.000 57.48062  ? 244 HIS A CA  1 
ATOM   1895 C C   . HIS A 1 244 ? 19.11478 28.29662 14.24141  1.000 50.80986  ? 244 HIS A C   1 
ATOM   1896 O O   . HIS A 1 244 ? 18.03454 28.02691 14.77705  1.000 51.85159  ? 244 HIS A O   1 
ATOM   1897 C CB  . HIS A 1 244 ? 18.67667 30.43006 12.99996  1.000 63.58937  ? 244 HIS A CB  1 
ATOM   1898 C CG  . HIS A 1 244 ? 18.53217 31.12529 11.68190  1.000 67.44270  ? 244 HIS A CG  1 
ATOM   1899 N ND1 . HIS A 1 244 ? 19.59514 31.33321 10.82963  1.000 67.17300  ? 244 HIS A ND1 1 
ATOM   1900 C CD2 . HIS A 1 244 ? 17.44864 31.65716 11.06823  1.000 73.05899  ? 244 HIS A CD2 1 
ATOM   1901 C CE1 . HIS A 1 244 ? 19.17298 31.96378 9.74840   1.000 67.88157  ? 244 HIS A CE1 1 
ATOM   1902 N NE2 . HIS A 1 244 ? 17.87428 32.17244 9.86820   1.000 73.19934  ? 244 HIS A NE2 1 
ATOM   1903 N N   . PHE A 1 245 ? 20.29282 28.01277 14.78729  1.000 53.57711  ? 245 PHE A N   1 
ATOM   1904 C CA  . PHE A 1 245 ? 20.42885 27.42127 16.10978  1.000 61.10369  ? 245 PHE A CA  1 
ATOM   1905 C C   . PHE A 1 245 ? 20.85379 28.48595 17.10852  1.000 59.10894  ? 245 PHE A C   1 
ATOM   1906 O O   . PHE A 1 245 ? 21.64923 29.37164 16.78399  1.000 60.31798  ? 245 PHE A O   1 
ATOM   1907 C CB  . PHE A 1 245 ? 21.46270 26.29471 16.11079  1.000 55.71385  ? 245 PHE A CB  1 
ATOM   1908 C CG  . PHE A 1 245 ? 21.08854 25.11869 15.25843  1.000 55.38021  ? 245 PHE A CG  1 
ATOM   1909 C CD1 . PHE A 1 245 ? 21.34742 25.11905 13.89804  1.000 54.24849  ? 245 PHE A CD1 1 
ATOM   1910 C CD2 . PHE A 1 245 ? 20.50417 23.99964 15.82410  1.000 50.79189  ? 245 PHE A CD2 1 
ATOM   1911 C CE1 . PHE A 1 245 ? 21.01300 24.03208 13.11604  1.000 53.62266  ? 245 PHE A CE1 1 
ATOM   1912 C CE2 . PHE A 1 245 ? 20.16872 22.91025 15.04957  1.000 62.27716  ? 245 PHE A CE2 1 
ATOM   1913 C CZ  . PHE A 1 245 ? 20.42316 22.92552 13.69198  1.000 56.65997  ? 245 PHE A CZ  1 
ATOM   1914 N N   . ALA A 1 246 ? 20.32855 28.39289 18.32597  1.000 69.11490  ? 246 ALA A N   1 
ATOM   1915 C CA  . ALA A 1 246 ? 20.82232 29.22381 19.41493  1.000 66.20821  ? 246 ALA A CA  1 
ATOM   1916 C C   . ALA A 1 246 ? 22.14199 28.64606 19.90560  1.000 68.14451  ? 246 ALA A C   1 
ATOM   1917 O O   . ALA A 1 246 ? 22.18705 27.51599 20.40309  1.000 68.86798  ? 246 ALA A O   1 
ATOM   1918 C CB  . ALA A 1 246 ? 19.80979 29.30332 20.55308  1.000 70.04997  ? 246 ALA A CB  1 
ATOM   1919 N N   . ARG A 1 247 ? 23.21310 29.41218 19.75314  1.000 78.85607  ? 247 ARG A N   1 
ATOM   1920 C CA  . ARG A 1 247 ? 24.54959 28.97307 20.12245  1.000 82.69563  ? 247 ARG A CA  1 
ATOM   1921 C C   . ARG A 1 247 ? 24.89851 29.56607 21.48364  1.000 89.88641  ? 247 ARG A C   1 
ATOM   1922 O O   . ARG A 1 247 ? 24.89883 30.79000 21.65263  1.000 92.62058  ? 247 ARG A O   1 
ATOM   1923 C CB  . ARG A 1 247 ? 25.56299 29.38906 19.05543  1.000 87.24603  ? 247 ARG A CB  1 
ATOM   1924 C CG  . ARG A 1 247 ? 26.95972 29.64661 19.58800  1.000 90.63493  ? 247 ARG A CG  1 
ATOM   1925 C CD  . ARG A 1 247 ? 27.99000 29.63616 18.47822  1.000 92.26475  ? 247 ARG A CD  1 
ATOM   1926 N NE  . ARG A 1 247 ? 29.32263 29.99195 18.94980  1.000 97.02842  ? 247 ARG A NE  1 
ATOM   1927 C CZ  . ARG A 1 247 ? 30.09787 29.20053 19.67951  1.000 94.64865  ? 247 ARG A CZ  1 
ATOM   1928 N NH1 . ARG A 1 247 ? 29.68015 28.01550 20.09788  1.000 95.44968  ? 247 ARG A NH1 1 
ATOM   1929 N NH2 . ARG A 1 247 ? 31.32197 29.60989 20.00041  1.000 91.11040  ? 247 ARG A NH2 1 
ATOM   1930 N N   . PHE A 1 248 ? 25.17017 28.70001 22.45386  1.000 79.76521  ? 248 PHE A N   1 
ATOM   1931 C CA  . PHE A 1 248 ? 25.57165 29.12054 23.78929  1.000 91.32907  ? 248 PHE A CA  1 
ATOM   1932 C C   . PHE A 1 248 ? 26.96871 28.66722 24.18566  1.000 88.35135  ? 248 PHE A C   1 
ATOM   1933 O O   . PHE A 1 248 ? 27.65544 29.38724 24.91656  1.000 92.14594  ? 248 PHE A O   1 
ATOM   1934 C CB  . PHE A 1 248 ? 24.58863 28.59441 24.84158  1.000 94.00531  ? 248 PHE A CB  1 
ATOM   1935 C CG  . PHE A 1 248 ? 23.26988 29.28559 24.82640  1.000 94.71087  ? 248 PHE A CG  1 
ATOM   1936 C CD1 . PHE A 1 248 ? 23.15261 30.57936 25.30942  0.700 91.52331  ? 248 PHE A CD1 1 
ATOM   1937 C CD2 . PHE A 1 248 ? 22.14414 28.64661 24.33013  0.700 93.42735  ? 248 PHE A CD2 1 
ATOM   1938 C CE1 . PHE A 1 248 ? 21.93957 31.22309 25.30316  0.700 90.51339  ? 248 PHE A CE1 1 
ATOM   1939 C CE2 . PHE A 1 248 ? 20.93242 29.28022 24.31664  0.700 86.61612  ? 248 PHE A CE2 1 
ATOM   1940 C CZ  . PHE A 1 248 ? 20.82992 30.57583 24.80277  0.700 91.20728  ? 248 PHE A CZ  1 
ATOM   1941 N N   . ARG A 1 249 ? 27.39777 27.48631 23.74498  1.000 76.51526  ? 249 ARG A N   1 
ATOM   1942 C CA  . ARG A 1 249 ? 28.70135 26.93147 24.07263  1.000 77.57632  ? 249 ARG A CA  1 
ATOM   1943 C C   . ARG A 1 249 ? 29.34370 26.42608 22.78744  1.000 77.76265  ? 249 ARG A C   1 
ATOM   1944 O O   . ARG A 1 249 ? 28.72089 26.41789 21.72177  1.000 67.48607  ? 249 ARG A O   1 
ATOM   1945 C CB  . ARG A 1 249 ? 28.55888 25.81404 25.11458  1.000 72.61650  ? 249 ARG A CB  1 
ATOM   1946 C CG  . ARG A 1 249 ? 29.83137 25.44329 25.87034  0.700 80.73077  ? 249 ARG A CG  1 
ATOM   1947 C CD  . ARG A 1 249 ? 29.54646 24.30697 26.83422  0.600 82.01112  ? 249 ARG A CD  1 
ATOM   1948 N NE  . ARG A 1 249 ? 28.29306 23.64035 26.49953  0.500 78.00969  ? 249 ARG A NE  1 
ATOM   1949 C CZ  . ARG A 1 249 ? 27.87163 22.50879 27.04758  0.500 84.53881  ? 249 ARG A CZ  1 
ATOM   1950 N NH1 . ARG A 1 249 ? 28.59732 21.86302 27.94528  0.500 75.63183  ? 249 ARG A NH1 1 
ATOM   1951 N NH2 . ARG A 1 249 ? 26.69223 22.01219 26.68508  0.500 90.58604  ? 249 ARG A NH2 1 
ATOM   1952 N N   . SER A 1 250 ? 30.60902 26.01711 22.88746  1.000 77.67327  ? 250 SER A N   1 
ATOM   1953 C CA  . SER A 1 250 ? 31.34259 25.45686 21.75601  1.000 66.72969  ? 250 SER A CA  1 
ATOM   1954 C C   . SER A 1 250 ? 31.20581 23.93917 21.78157  1.000 64.25654  ? 250 SER A C   1 
ATOM   1955 O O   . SER A 1 250 ? 31.72423 23.27662 22.68574  1.000 64.16298  ? 250 SER A O   1 
ATOM   1956 C CB  . SER A 1 250 ? 32.81395 25.86635 21.79113  1.000 70.62178  ? 250 SER A CB  1 
ATOM   1957 O OG  . SER A 1 250 ? 33.51190 25.39086 20.64828  1.000 66.57645  ? 250 SER A OG  1 
ATOM   1958 N N   . PHE A 1 251 ? 30.49020 23.39472 20.79951  1.000 55.66328  ? 251 PHE A N   1 
ATOM   1959 C CA  . PHE A 1 251 ? 30.38807 21.95265 20.58546  1.000 53.66521  ? 251 PHE A CA  1 
ATOM   1960 C C   . PHE A 1 251 ? 30.60811 21.73807 19.09512  1.000 52.21645  ? 251 PHE A C   1 
ATOM   1961 O O   . PHE A 1 251 ? 29.64643 21.68448 18.31384  1.000 47.44176  ? 251 PHE A O   1 
ATOM   1962 C CB  . PHE A 1 251 ? 29.03847 21.40345 21.04656  1.000 52.08664  ? 251 PHE A CB  1 
ATOM   1963 C CG  . PHE A 1 251 ? 29.01481 19.91063 21.23293  1.000 62.64306  ? 251 PHE A CG  1 
ATOM   1964 C CD1 . PHE A 1 251 ? 30.12867 19.13760 20.94255  1.000 59.99562  ? 251 PHE A CD1 1 
ATOM   1965 C CD2 . PHE A 1 251 ? 27.87270 19.28070 21.69791  1.000 65.74618  ? 251 PHE A CD2 1 
ATOM   1966 C CE1 . PHE A 1 251 ? 30.10174 17.76500 21.11458  1.000 58.38319  ? 251 PHE A CE1 1 
ATOM   1967 C CE2 . PHE A 1 251 ? 27.83928 17.90964 21.87166  1.000 63.47188  ? 251 PHE A CE2 1 
ATOM   1968 C CZ  . PHE A 1 251 ? 28.95665 17.15150 21.57920  1.000 62.84686  ? 251 PHE A CZ  1 
ATOM   1969 N N   . PRO A 1 252 ? 31.86403 21.62559 18.66160  1.000 47.61432  ? 252 PRO A N   1 
ATOM   1970 C CA  . PRO A 1 252 ? 32.14388 21.56621 17.22248  1.000 51.92944  ? 252 PRO A CA  1 
ATOM   1971 C C   . PRO A 1 252 ? 31.51801 20.34172 16.56977  1.000 48.28561  ? 252 PRO A C   1 
ATOM   1972 O O   . PRO A 1 252 ? 31.24103 19.32887 17.21757  1.000 47.34750  ? 252 PRO A O   1 
ATOM   1973 C CB  . PRO A 1 252 ? 33.67257 21.50931 17.16020  1.000 50.82589  ? 252 PRO A CB  1 
ATOM   1974 C CG  . PRO A 1 252 ? 34.13181 22.09248 18.46198  1.000 45.75865  ? 252 PRO A CG  1 
ATOM   1975 C CD  . PRO A 1 252 ? 33.09745 21.67915 19.46677  1.000 56.29677  ? 252 PRO A CD  1 
ATOM   1976 N N   . PHE A 1 253 ? 31.28487 20.45460 15.26055  1.000 51.53009  ? 253 PHE A N   1 
ATOM   1977 C CA  . PHE A 1 253 ? 30.64006 19.37652 14.51797  1.000 44.27647  ? 253 PHE A CA  1 
ATOM   1978 C C   . PHE A 1 253 ? 31.46829 18.10030 14.55626  1.000 42.83978  ? 253 PHE A C   1 
ATOM   1979 O O   . PHE A 1 253 ? 30.91966 17.00383 14.70486  1.000 44.96181  ? 253 PHE A O   1 
ATOM   1980 C CB  . PHE A 1 253 ? 30.39750 19.81918 13.07268  1.000 45.88520  ? 253 PHE A CB  1 
ATOM   1981 C CG  . PHE A 1 253 ? 29.80750 18.75137 12.19565  1.000 41.71891  ? 253 PHE A CG  1 
ATOM   1982 C CD1 . PHE A 1 253 ? 28.45867 18.44175 12.26799  1.000 41.43359  ? 253 PHE A CD1 1 
ATOM   1983 C CD2 . PHE A 1 253 ? 30.59982 18.06840 11.28660  1.000 42.56929  ? 253 PHE A CD2 1 
ATOM   1984 C CE1 . PHE A 1 253 ? 27.91307 17.46362 11.45764  1.000 45.41141  ? 253 PHE A CE1 1 
ATOM   1985 C CE2 . PHE A 1 253 ? 30.05950 17.08932 10.47325  1.000 48.56979  ? 253 PHE A CE2 1 
ATOM   1986 C CZ  . PHE A 1 253 ? 28.71456 16.78618 10.55791  1.000 46.34801  ? 253 PHE A CZ  1 
ATOM   1987 N N   . TRP A 1 254 ? 32.79196 18.22112 14.43827  1.000 42.29099  ? 254 TRP A N   1 
ATOM   1988 C CA  . TRP A 1 254 ? 33.63702 17.03174 14.41032  1.000 47.44539  ? 254 TRP A CA  1 
ATOM   1989 C C   . TRP A 1 254 ? 33.73834 16.37505 15.78115  1.000 45.27326  ? 254 TRP A C   1 
ATOM   1990 O O   . TRP A 1 254 ? 33.89102 15.15197 15.86766  1.000 42.46993  ? 254 TRP A O   1 
ATOM   1991 C CB  . TRP A 1 254 ? 35.02597 17.38176 13.87443  1.000 40.82553  ? 254 TRP A CB  1 
ATOM   1992 C CG  . TRP A 1 254 ? 35.00356 17.89993 12.46704  1.000 49.30926  ? 254 TRP A CG  1 
ATOM   1993 C CD1 . TRP A 1 254 ? 35.47255 19.10377 12.03092  1.000 47.93860  ? 254 TRP A CD1 1 
ATOM   1994 C CD2 . TRP A 1 254 ? 34.47074 17.23581 11.31183  1.000 41.72215  ? 254 TRP A CD2 1 
ATOM   1995 N NE1 . TRP A 1 254 ? 35.27496 19.22910 10.67497  1.000 49.31374  ? 254 TRP A NE1 1 
ATOM   1996 C CE2 . TRP A 1 254 ? 34.66036 18.09572 10.21083  1.000 50.11658  ? 254 TRP A CE2 1 
ATOM   1997 C CE3 . TRP A 1 254 ? 33.85650 15.99590 11.10029  1.000 46.64514  ? 254 TRP A CE3 1 
ATOM   1998 C CZ2 . TRP A 1 254 ? 34.25821 17.75630 8.92067   1.000 41.42794  ? 254 TRP A CZ2 1 
ATOM   1999 C CZ3 . TRP A 1 254 ? 33.45690 15.66266 9.81760   1.000 38.97988  ? 254 TRP A CZ3 1 
ATOM   2000 C CH2 . TRP A 1 254 ? 33.65942 16.53914 8.74566   1.000 44.76351  ? 254 TRP A CH2 1 
ATOM   2001 N N   . ARG A 1 255 ? 33.66468 17.15835 16.85876  1.000 46.68840  ? 255 ARG A N   1 
ATOM   2002 C CA  . ARG A 1 255 ? 33.55383 16.55697 18.18345  1.000 48.15452  ? 255 ARG A CA  1 
ATOM   2003 C C   . ARG A 1 255 ? 32.21258 15.85496 18.34412  1.000 43.05792  ? 255 ARG A C   1 
ATOM   2004 O O   . ARG A 1 255 ? 32.13473 14.77888 18.94706  1.000 45.00853  ? 255 ARG A O   1 
ATOM   2005 C CB  . ARG A 1 255 ? 33.74209 17.61957 19.26505  1.000 50.65389  ? 255 ARG A CB  1 
ATOM   2006 C CG  . ARG A 1 255 ? 33.78547 17.06918 20.68362  1.000 58.16447  ? 255 ARG A CG  1 
ATOM   2007 C CD  . ARG A 1 255 ? 34.20203 18.15155 21.66397  0.800 57.13579  ? 255 ARG A CD  1 
ATOM   2008 N NE  . ARG A 1 255 ? 33.25051 18.31072 22.75644  0.700 61.20749  ? 255 ARG A NE  1 
ATOM   2009 C CZ  . ARG A 1 255 ? 33.15687 19.39835 23.50876  0.600 63.39310  ? 255 ARG A CZ  1 
ATOM   2010 N NH1 . ARG A 1 255 ? 33.93434 20.44897 23.30425  0.600 62.25857  ? 255 ARG A NH1 1 
ATOM   2011 N NH2 . ARG A 1 255 ? 32.25558 19.43638 24.48510  0.600 60.97776  ? 255 ARG A NH2 1 
ATOM   2012 N N   . ARG A 1 256 ? 31.14751 16.45000 17.80267  1.000 41.41193  ? 256 ARG A N   1 
ATOM   2013 C CA  . ARG A 1 256 ? 29.84509 15.79374 17.80072  1.000 44.44720  ? 256 ARG A CA  1 
ATOM   2014 C C   . ARG A 1 256 ? 29.89581 14.48873 17.01623  1.000 52.22568  ? 256 ARG A C   1 
ATOM   2015 O O   . ARG A 1 256 ? 29.29410 13.48723 17.42004  1.000 46.26066  ? 256 ARG A O   1 
ATOM   2016 C CB  . ARG A 1 256 ? 28.79075 16.74172 17.22177  1.000 48.57048  ? 256 ARG A CB  1 
ATOM   2017 C CG  . ARG A 1 256 ? 27.45071 16.70598 17.93644  1.000 62.31581  ? 256 ARG A CG  1 
ATOM   2018 C CD  . ARG A 1 256 ? 26.76347 18.07298 17.93487  1.000 59.89762  ? 256 ARG A CD  1 
ATOM   2019 N NE  . ARG A 1 256 ? 26.36588 18.51581 16.60281  1.000 54.00203  ? 256 ARG A NE  1 
ATOM   2020 C CZ  . ARG A 1 256 ? 26.88333 19.56240 15.97231  1.000 55.43478  ? 256 ARG A CZ  1 
ATOM   2021 N NH1 . ARG A 1 256 ? 27.82857 20.30604 16.52403  1.000 57.03301  ? 256 ARG A NH1 1 
ATOM   2022 N NH2 . ARG A 1 256 ? 26.43492 19.87690 14.76069  1.000 54.92062  ? 256 ARG A NH2 1 
ATOM   2023 N N   . VAL A 1 257 ? 30.62210 14.47749 15.89656  1.000 48.33579  ? 257 VAL A N   1 
ATOM   2024 C CA  . VAL A 1 257 ? 30.79058 13.24712 15.13036  1.000 44.05925  ? 257 VAL A CA  1 
ATOM   2025 C C   . VAL A 1 257 ? 31.60715 12.23400 15.92141  1.000 42.85548  ? 257 VAL A C   1 
ATOM   2026 O O   . VAL A 1 257 ? 31.27159 11.04364 15.96428  1.000 40.80291  ? 257 VAL A O   1 
ATOM   2027 C CB  . VAL A 1 257 ? 31.43569 13.55569 13.76735  1.000 43.52854  ? 257 VAL A CB  1 
ATOM   2028 C CG1 . VAL A 1 257 ? 31.83201 12.26756 13.05922  1.000 33.63943  ? 257 VAL A CG1 1 
ATOM   2029 C CG2 . VAL A 1 257 ? 30.48181 14.36701 12.90452  1.000 38.28003  ? 257 VAL A CG2 1 
ATOM   2030 N N   . HIS A 1 258 ? 32.68383 12.68969 16.56635  1.000 41.65398  ? 258 HIS A N   1 
ATOM   2031 C CA  . HIS A 1 258 ? 33.51708 11.79152 17.35968  1.000 48.52751  ? 258 HIS A CA  1 
ATOM   2032 C C   . HIS A 1 258 ? 32.71257 11.13429 18.47575  1.000 47.82117  ? 258 HIS A C   1 
ATOM   2033 O O   . HIS A 1 258 ? 32.77397 9.91379  18.66871  1.000 51.75050  ? 258 HIS A O   1 
ATOM   2034 C CB  . HIS A 1 258 ? 34.70657 12.55976 17.93597  1.000 48.81020  ? 258 HIS A CB  1 
ATOM   2035 C CG  . HIS A 1 258 ? 35.41879 11.83370 19.03514  1.000 44.57685  ? 258 HIS A CG  1 
ATOM   2036 N ND1 . HIS A 1 258 ? 35.03644 11.92254 20.35638  1.000 58.04019  ? 258 HIS A ND1 1 
ATOM   2037 C CD2 . HIS A 1 258 ? 36.49237 11.01016 19.01073  1.000 45.60153  ? 258 HIS A CD2 1 
ATOM   2038 C CE1 . HIS A 1 258 ? 35.84099 11.18259 21.09770  1.000 44.81721  ? 258 HIS A CE1 1 
ATOM   2039 N NE2 . HIS A 1 258 ? 36.73390 10.61849 20.30517  1.000 57.56077  ? 258 HIS A NE2 1 
ATOM   2040 N N   . ASP A 1 259 ? 31.94539 11.93304 19.22187  1.000 41.65888  ? 259 ASP A N   1 
ATOM   2041 C CA  . ASP A 1 259 ? 31.19558 11.39702 20.35308  1.000 52.77364  ? 259 ASP A CA  1 
ATOM   2042 C C   . ASP A 1 259 ? 30.10316 10.43456 19.90718  1.000 49.58910  ? 259 ASP A C   1 
ATOM   2043 O O   . ASP A 1 259 ? 29.81315 9.45998  20.61062  1.000 50.67506  ? 259 ASP A O   1 
ATOM   2044 C CB  . ASP A 1 259 ? 30.59137 12.53856 21.16810  1.000 54.85804  ? 259 ASP A CB  1 
ATOM   2045 C CG  . ASP A 1 259 ? 31.64607 13.46472 21.74176  1.000 50.61049  ? 259 ASP A CG  1 
ATOM   2046 O OD1 . ASP A 1 259 ? 32.78940 13.00453 21.94779  1.000 50.35857  ? 259 ASP A OD1 1 
ATOM   2047 O OD2 . ASP A 1 259 ? 31.32897 14.64535 21.99081  1.000 59.56260  ? 259 ASP A OD2 1 
ATOM   2048 N N   . SER A 1 260 ? 29.49479 10.68144 18.74695  1.000 49.48376  ? 260 SER A N   1 
ATOM   2049 C CA  . SER A 1 260 ? 28.36992 9.86228  18.31305  1.000 46.90714  ? 260 SER A CA  1 
ATOM   2050 C C   . SER A 1 260 ? 28.80936 8.54233  17.68976  1.000 48.08014  ? 260 SER A C   1 
ATOM   2051 O O   . SER A 1 260 ? 28.10909 7.53417  17.83744  1.000 52.28199  ? 260 SER A O   1 
ATOM   2052 C CB  . SER A 1 260 ? 27.50634 10.63702 17.31661  1.000 49.32369  ? 260 SER A CB  1 
ATOM   2053 O OG  . SER A 1 260 ? 26.98085 11.82002 17.89499  1.000 63.14251  ? 260 SER A OG  1 
ATOM   2054 N N   . PHE A 1 261 ? 29.94855 8.51690  16.99823  1.000 48.14705  ? 261 PHE A N   1 
ATOM   2055 C CA  . PHE A 1 261 ? 30.33855 7.34538  16.22409  1.000 46.03245  ? 261 PHE A CA  1 
ATOM   2056 C C   . PHE A 1 261 ? 31.62664 6.67779  16.68111  1.000 53.24032  ? 261 PHE A C   1 
ATOM   2057 O O   . PHE A 1 261 ? 31.73228 5.45471  16.57196  1.000 49.55546  ? 261 PHE A O   1 
ATOM   2058 C CB  . PHE A 1 261 ? 30.47408 7.70789  14.73795  1.000 47.23451  ? 261 PHE A CB  1 
ATOM   2059 C CG  . PHE A 1 261 ? 29.17099 8.04635  14.08063  1.000 41.54781  ? 261 PHE A CG  1 
ATOM   2060 C CD1 . PHE A 1 261 ? 28.21056 7.06978  13.87811  1.000 48.85569  ? 261 PHE A CD1 1 
ATOM   2061 C CD2 . PHE A 1 261 ? 28.90549 9.33898  13.66335  1.000 42.35050  ? 261 PHE A CD2 1 
ATOM   2062 C CE1 . PHE A 1 261 ? 27.00631 7.37783  13.27343  1.000 45.18502  ? 261 PHE A CE1 1 
ATOM   2063 C CE2 . PHE A 1 261 ? 27.70636 9.65277  13.05641  1.000 43.31656  ? 261 PHE A CE2 1 
ATOM   2064 C CZ  . PHE A 1 261 ? 26.75471 8.67021  12.86285  1.000 41.92728  ? 261 PHE A CZ  1 
ATOM   2065 N N   . ILE A 1 262 ? 32.60729 7.42900  17.17704  1.000 47.39055  ? 262 ILE A N   1 
ATOM   2066 C CA  . ILE A 1 262 ? 33.85262 6.82205  17.63419  1.000 52.37767  ? 262 ILE A CA  1 
ATOM   2067 C C   . ILE A 1 262 ? 33.63582 6.23926  19.02571  1.000 64.18696  ? 262 ILE A C   1 
ATOM   2068 O O   . ILE A 1 262 ? 33.58690 5.01407  19.18572  1.000 72.07040  ? 262 ILE A O   1 
ATOM   2069 C CB  . ILE A 1 262 ? 35.01020 7.83467  17.61041  1.000 50.92281  ? 262 ILE A CB  1 
ATOM   2070 C CG1 . ILE A 1 262 ? 35.12677 8.46075  16.21978  1.000 49.69008  ? 262 ILE A CG1 1 
ATOM   2071 C CG2 . ILE A 1 262 ? 36.31655 7.15446  17.98056  1.000 49.94767  ? 262 ILE A CG2 1 
ATOM   2072 C CD1 . ILE A 1 262 ? 35.38840 7.44948  15.11965  1.000 42.57587  ? 262 ILE A CD1 1 
ATOM   2073 N N   . GLU A 1 263 ? 33.51515 7.11242  20.03387  1.000 52.14190  ? 263 GLU A N   1 
ATOM   2074 C CA  . GLU A 1 263 ? 33.06282 6.74820  21.37667  1.000 71.31250  ? 263 GLU A CA  1 
ATOM   2075 C C   . GLU A 1 263 ? 33.02469 7.97533  22.27978  1.000 71.35700  ? 263 GLU A C   1 
ATOM   2076 O O   . GLU A 1 263 ? 33.79566 8.92048  22.08540  1.000 71.49794  ? 263 GLU A O   1 
ATOM   2077 C CB  . GLU A 1 263 ? 33.95430 5.67186  22.00836  1.000 71.79471  ? 263 GLU A CB  1 
ATOM   2078 C CG  . GLU A 1 263 ? 33.33751 4.98529  23.23345  0.800 81.23474  ? 263 GLU A CG  1 
ATOM   2079 C CD  . GLU A 1 263 ? 31.99368 4.32950  22.93974  0.700 82.08293  ? 263 GLU A CD  1 
ATOM   2080 O OE1 . GLU A 1 263 ? 31.72527 3.99092  21.76633  0.700 76.92530  ? 263 GLU A OE1 1 
ATOM   2081 O OE2 . GLU A 1 263 ? 31.20109 4.15117  23.89021  0.700 70.50853  ? 263 GLU A OE2 1 
ATOM   2082 N N   . ASP A 1 264 ? 32.13614 7.96946  23.26915  1.000 78.94714  ? 264 ASP A N   1 
ATOM   2083 C CA  . ASP A 1 264 ? 32.03929 9.07504  24.21481  1.000 73.48796  ? 264 ASP A CA  1 
ATOM   2084 C C   . ASP A 1 264 ? 32.41211 8.61273  25.61963  1.000 91.42293  ? 264 ASP A C   1 
ATOM   2085 O O   . ASP A 1 264 ? 31.74805 8.95891  26.59799  1.000 89.60174  ? 264 ASP A O   1 
ATOM   2086 C CB  . ASP A 1 264 ? 30.62863 9.66913  24.20587  1.000 69.56128  ? 264 ASP A CB  1 
ATOM   2087 C CG  . ASP A 1 264 ? 30.59852 11.10775 24.68061  1.000 82.08081  ? 264 ASP A CG  1 
ATOM   2088 O OD1 . ASP A 1 264 ? 31.68194 11.67444 24.93566  1.000 87.34029  ? 264 ASP A OD1 1 
ATOM   2089 O OD2 . ASP A 1 264 ? 29.49166 11.67429 24.79607  1.000 81.94511  ? 264 ASP A OD2 1 
HETATM 2090 C C1  . CIT B 2 .   ? 32.09259 23.99337 14.19595  1.000 52.23787  ? 301 CIT A C1  1 
HETATM 2091 O O1  . CIT B 2 .   ? 31.77495 22.80080 13.99886  1.000 47.68462  ? 301 CIT A O1  1 
HETATM 2092 O O2  . CIT B 2 .   ? 33.30853 24.27537 14.25177  1.000 56.11708  ? 301 CIT A O2  1 
HETATM 2093 C C2  . CIT B 2 .   ? 31.06137 25.09042 14.35966  1.000 52.03414  ? 301 CIT A C2  1 
HETATM 2094 C C3  . CIT B 2 .   ? 29.87005 24.69878 15.23389  1.000 61.30992  ? 301 CIT A C3  1 
HETATM 2095 O O7  . CIT B 2 .   ? 30.35985 24.22202 16.51331  1.000 61.26312  ? 301 CIT A O7  1 
HETATM 2096 C C4  . CIT B 2 .   ? 28.96261 25.90113 15.46673  1.000 60.44501  ? 301 CIT A C4  1 
HETATM 2097 C C5  . CIT B 2 .   ? 29.52550 26.75017 16.58188  1.000 72.41092  ? 301 CIT A C5  1 
HETATM 2098 O O3  . CIT B 2 .   ? 29.83496 27.94354 16.38075  1.000 65.14380  ? 301 CIT A O3  1 
HETATM 2099 O O4  . CIT B 2 .   ? 29.68507 26.26657 17.72489  1.000 75.17680  ? 301 CIT A O4  1 
HETATM 2100 C C6  . CIT B 2 .   ? 29.05980 23.59521 14.57104  1.000 62.02815  ? 301 CIT A C6  1 
HETATM 2101 O O5  . CIT B 2 .   ? 28.26699 23.87198 13.64550  1.000 55.70286  ? 301 CIT A O5  1 
HETATM 2102 O O6  . CIT B 2 .   ? 29.18762 22.40185 14.92563  1.000 60.51069  ? 301 CIT A O6  1 
HETATM 2103 N N1  . UXO C 3 .   ? 19.81756 4.09062  7.64465   1.000 45.19343  ? 302 UXO A N1  1 
HETATM 2104 C C7  . UXO C 3 .   ? 14.18058 9.73810  10.53638  1.000 45.89479  ? 302 UXO A C7  1 
HETATM 2105 C C8  . UXO C 3 .   ? 12.99690 8.89816  12.50104  1.000 56.89224  ? 302 UXO A C8  1 
HETATM 2106 N N2  . UXO C 3 .   ? 19.37384 6.23706  8.64407   1.000 46.99612  ? 302 UXO A N2  1 
HETATM 2107 C C9  . UXO C 3 .   ? 12.96018 7.38146  12.47658  1.000 67.28689  ? 302 UXO A C9  1 
HETATM 2108 O O1  . UXO C 3 .   ? 19.00192 8.33763  12.88502  1.000 47.58624  ? 302 UXO A O1  1 
HETATM 2109 C C1  . UXO C 3 .   ? 20.14305 5.19406  8.32384   1.000 42.27023  ? 302 UXO A C1  1 
HETATM 2110 O O5  . UXO C 3 .   ? 15.61599 11.49834 8.24251   1.000 38.37416  ? 302 UXO A O5  1 
HETATM 2111 C C5  . UXO C 3 .   ? 17.09857 8.27504  8.91709   1.000 52.08660  ? 302 UXO A C5  1 
HETATM 2112 C C6  . UXO C 3 .   ? 15.53704 9.69181  9.85903   1.000 52.73659  ? 302 UXO A C6  1 
HETATM 2113 N N3  . UXO C 3 .   ? 16.30736 5.17966  7.14582   1.000 51.60540  ? 302 UXO A N3  1 
HETATM 2114 C C4  . UXO C 3 .   ? 16.02379 6.35259  7.66004   1.000 51.61873  ? 302 UXO A C4  1 
HETATM 2115 O O4  . UXO C 3 .   ? 19.39741 9.46015  16.25486  1.000 52.21452  ? 302 UXO A O4  1 
HETATM 2116 C C3  . UXO C 3 .   ? 17.64350 4.99555  7.46679   1.000 50.47559  ? 302 UXO A C3  1 
HETATM 2117 O O3  . UXO C 3 .   ? 19.38401 6.83719  15.81345  1.000 58.23347  ? 302 UXO A O3  1 
HETATM 2118 C C2  . UXO C 3 .   ? 18.13074 6.07866  8.18030   1.000 49.53024  ? 302 UXO A C2  1 
HETATM 2119 N N4  . UXO C 3 .   ? 17.07832 6.95490  8.29421   1.000 53.83796  ? 302 UXO A N4  1 
HETATM 2120 N N   . UXO C 3 .   ? 18.23359 2.84678  6.51598   1.000 44.24260  ? 302 UXO A N   1 
HETATM 2121 C C   . UXO C 3 .   ? 18.55170 3.95407  7.19340   1.000 50.72421  ? 302 UXO A C   1 
HETATM 2122 O O   . UXO C 3 .   ? 16.05216 8.34737  9.86980   1.000 49.08038  ? 302 UXO A O   1 
HETATM 2123 C C10 . UXO C 3 .   ? 12.44534 6.81825  11.16135  1.000 76.42352  ? 302 UXO A C10 1 
HETATM 2124 C C11 . UXO C 3 .   ? 11.31633 5.90311  11.33264  1.000 80.56741  ? 302 UXO A C11 1 
HETATM 2125 C C12 . UXO C 3 .   ? 10.39726 5.19004  11.50855  1.000 81.32006  ? 302 UXO A C12 1 
HETATM 2126 C C13 . UXO C 3 .   ? 14.63966 10.62341 12.78881  1.000 49.45967  ? 302 UXO A C13 1 
HETATM 2127 C C14 . UXO C 3 .   ? 16.09290 10.84210 12.85641  1.000 51.35544  ? 302 UXO A C14 1 
HETATM 2128 C C15 . UXO C 3 .   ? 17.28007 10.95395 12.91765  1.000 47.55471  ? 302 UXO A C15 1 
HETATM 2129 C C16 . UXO C 3 .   ? 18.63647 11.35832 12.84488  1.000 39.16630  ? 302 UXO A C16 1 
HETATM 2130 C C17 . UXO C 3 .   ? 20.43334 12.40223 12.36558  1.000 45.47218  ? 302 UXO A C17 1 
HETATM 2131 C C18 . UXO C 3 .   ? 20.83109 11.20790 12.94495  1.000 42.47683  ? 302 UXO A C18 1 
HETATM 2132 C C19 . UXO C 3 .   ? 22.96230 11.67815 12.65310  1.000 40.97613  ? 302 UXO A C19 1 
HETATM 2133 C C20 . UXO C 3 .   ? 21.45002 13.26201 11.91176  1.000 40.52982  ? 302 UXO A C20 1 
HETATM 2134 C C21 . UXO C 3 .   ? 19.57572 9.20499  13.83684  1.000 48.68925  ? 302 UXO A C21 1 
HETATM 2135 C C22 . UXO C 3 .   ? 18.47629 7.18639  13.58196  1.000 57.79219  ? 302 UXO A C22 1 
HETATM 2136 C C23 . UXO C 3 .   ? 17.16107 6.77928  12.95916  1.000 52.97174  ? 302 UXO A C23 1 
HETATM 2137 C C24 . UXO C 3 .   ? 18.40973 7.56135  15.06996  1.000 49.92676  ? 302 UXO A C24 1 
HETATM 2138 C C25 . UXO C 3 .   ? 18.69906 9.06945  15.07761  1.000 49.52966  ? 302 UXO A C25 1 
HETATM 2139 C C26 . UXO C 3 .   ? 15.59130 10.08320 8.39121   1.000 44.55799  ? 302 UXO A C26 1 
HETATM 2140 C C27 . UXO C 3 .   ? 16.90369 9.43769  7.92408   1.000 46.34265  ? 302 UXO A C27 1 
HETATM 2141 N N10 . UXO C 3 .   ? 19.66704 10.53564 13.25636  1.000 41.97646  ? 302 UXO A N10 1 
HETATM 2142 N N5  . UXO C 3 .   ? 14.23954 9.47731  11.97970  1.000 55.27890  ? 302 UXO A N5  1 
HETATM 2143 N N6  . UXO C 3 .   ? 19.04701 12.49657 12.31552  1.000 43.47740  ? 302 UXO A N6  1 
HETATM 2144 N N7  . UXO C 3 .   ? 22.08656 10.78743 13.12150  1.000 39.81017  ? 302 UXO A N7  1 
HETATM 2145 N N8  . UXO C 3 .   ? 22.72911 12.86036 12.07648  1.000 40.36629  ? 302 UXO A N8  1 
HETATM 2146 N N9  . UXO C 3 .   ? 21.22242 14.43966 11.32189  1.000 44.11332  ? 302 UXO A N9  1 
HETATM 2147 O O2  . UXO C 3 .   ? 16.17931 7.79509  13.11528  1.000 54.02796  ? 302 UXO A O2  1 
HETATM 2148 O O6  . UXO C 3 .   ? 17.98955 10.35419 7.99955   1.000 48.29398  ? 302 UXO A O6  1 
HETATM 2149 O O   . HOH D 4 .   ? 13.86348 10.87891 4.53371   1.000 44.37739  ? 401 HOH A O   1 
HETATM 2150 O O   . HOH D 4 .   ? 1.17536  17.03943 -4.16926  1.000 71.75546  ? 402 HOH A O   1 
HETATM 2151 O O   . HOH D 4 .   ? 24.37752 8.18263  -8.99007  1.000 30.82171  ? 403 HOH A O   1 
HETATM 2152 O O   . HOH D 4 .   ? 5.23427  18.49728 29.38606  1.000 57.88881  ? 404 HOH A O   1 
HETATM 2153 O O   . HOH D 4 .   ? 17.69878 11.89458 23.40208  1.000 71.47587  ? 405 HOH A O   1 
HETATM 2154 O O   . HOH D 4 .   ? 15.29425 17.29855 20.40675  1.000 47.64166  ? 406 HOH A O   1 
HETATM 2155 O O   . HOH D 4 .   ? 15.81898 28.73189 12.00082  1.000 45.44824  ? 407 HOH A O   1 
HETATM 2156 O O   . HOH D 4 .   ? 29.46413 6.69708  4.74352   1.000 31.81004  ? 408 HOH A O   1 
HETATM 2157 O O   . HOH D 4 .   ? 20.28907 26.60163 2.78272   1.000 54.54941  ? 409 HOH A O   1 
HETATM 2158 O O   . HOH D 4 .   ? 25.36245 3.68566  -1.95396  1.000 43.44132  ? 410 HOH A O   1 
HETATM 2159 O O   . HOH D 4 .   ? 27.51520 5.70215  -1.77806  1.000 47.04385  ? 411 HOH A O   1 
HETATM 2160 O O   . HOH D 4 .   ? 33.60618 20.96568 13.72450  1.000 44.94575  ? 412 HOH A O   1 
HETATM 2161 O O   . HOH D 4 .   ? 14.58239 4.18851  5.46047   1.000 50.24824  ? 413 HOH A O   1 
HETATM 2162 O O   . HOH D 4 .   ? 23.57159 5.68896  -17.36435 1.000 47.90886  ? 414 HOH A O   1 
HETATM 2163 O O   . HOH D 4 .   ? 23.04689 11.36198 0.39436   1.000 32.86709  ? 415 HOH A O   1 
HETATM 2164 O O   . HOH D 4 .   ? 24.65704 16.32951 11.75890  1.000 46.25712  ? 416 HOH A O   1 
HETATM 2165 O O   . HOH D 4 .   ? 11.45793 7.75937  -0.32353  1.000 46.36873  ? 417 HOH A O   1 
HETATM 2166 O O   . HOH D 4 .   ? 13.84935 22.68022 -6.15726  1.000 53.32552  ? 418 HOH A O   1 
HETATM 2167 O O   . HOH D 4 .   ? 28.61037 2.39567  -10.58950 1.000 56.89041  ? 419 HOH A O   1 
HETATM 2168 O O   . HOH D 4 .   ? 22.32439 23.38017 -5.13204  1.000 44.69089  ? 420 HOH A O   1 
HETATM 2169 O O   . HOH D 4 .   ? 20.89157 26.97780 -4.66561  1.000 48.02132  ? 421 HOH A O   1 
HETATM 2170 O O   . HOH D 4 .   ? 22.64961 21.15172 6.86793   1.000 42.18383  ? 422 HOH A O   1 
HETATM 2171 O O   . HOH D 4 .   ? 15.11619 28.24812 -1.26245  1.000 62.04144  ? 423 HOH A O   1 
HETATM 2172 O O   . HOH D 4 .   ? 25.69322 9.22819  -6.47455  1.000 30.49369  ? 424 HOH A O   1 
HETATM 2173 O O   . HOH D 4 .   ? 20.78079 11.59108 4.81346   1.000 39.58483  ? 425 HOH A O   1 
HETATM 2174 O O   . HOH D 4 .   ? 21.00135 22.38186 19.59416  1.000 53.30492  ? 426 HOH A O   1 
HETATM 2175 O O   . HOH D 4 .   ? 24.402   5.294    10.112    1.000 46.96238  ? 427 HOH A O   1 
HETATM 2176 O O   . HOH D 4 .   ? 26.31585 6.81665  -3.69958  1.000 42.44941  ? 428 HOH A O   1 
HETATM 2177 O O   . HOH D 4 .   ? 13.47746 26.90653 -0.31442  1.000 56.22891  ? 429 HOH A O   1 
HETATM 2178 O O   . HOH D 4 .   ? 20.68965 7.86297  10.65441  1.000 46.38826  ? 430 HOH A O   1 
HETATM 2179 O O   . HOH D 4 .   ? 23.48513 7.26734  11.08125  1.000 39.51840  ? 431 HOH A O   1 
HETATM 2180 O O   . HOH D 4 .   ? 29.08013 26.02366 11.88366  1.000 56.00294  ? 432 HOH A O   1 
HETATM 2181 O O   . HOH D 4 .   ? 24.82896 1.53621  -5.51388  1.000 42.82778  ? 433 HOH A O   1 
HETATM 2182 O O   . HOH D 4 .   ? 13.13670 11.44985 18.76604  1.000 52.05551  ? 434 HOH A O   1 
HETATM 2183 O O   . HOH D 4 .   ? 31.99074 5.14163  -12.13485 1.000 49.12338  ? 435 HOH A O   1 
HETATM 2184 O O   . HOH D 4 .   ? 26.63858 3.22269  -4.80839  1.000 53.91734  ? 436 HOH A O   1 
HETATM 2185 O O   . HOH D 4 .   ? 27.051   21.392   -14.713   1.000 50.55984  ? 437 HOH A O   1 
HETATM 2186 O O   . HOH D 4 .   ? 27.72492 27.34923 9.64359   1.000 52.32711  ? 438 HOH A O   1 
HETATM 2187 O O   . HOH D 4 .   ? 30.01771 27.16607 1.19218   1.000 54.64789  ? 439 HOH A O   1 
HETATM 2188 O O   . HOH D 4 .   ? 29.17697 26.29709 -11.68090 1.000 60.22452  ? 440 HOH A O   1 
HETATM 2189 O O   . HOH D 4 .   ? 16.58540 34.35607 14.17749  1.000 61.72277  ? 441 HOH A O   1 
HETATM 2190 O O   . HOH D 4 .   ? 13.67230 8.30873  5.65428   1.000 53.71223  ? 442 HOH A O   1 
HETATM 2191 O O   . HOH D 4 .   ? 33.70036 10.60824 29.11617  1.000 77.13416  ? 443 HOH A O   1 
HETATM 2192 O O   . HOH D 4 .   ? 26.67801 15.69478 25.66414  1.000 69.69176  ? 444 HOH A O   1 
HETATM 2193 O O   . HOH D 4 .   ? 0.63594  14.42650 -2.48965  1.000 66.42524  ? 445 HOH A O   1 
HETATM 2194 O O   . HOH D 4 .   ? 12.03445 7.63859  7.76041   1.000 65.43614  ? 446 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   . MET A 1   ? 1.66184 1.17853 1.31241 0.26427  0.10498  -0.26878 1   MET A N   
2    C CA  . MET A 1   ? 1.50496 1.01709 1.15024 0.29484  0.10867  -0.24292 1   MET A CA  
3    C C   . MET A 1   ? 1.29187 0.89940 0.96965 0.30769  0.09576  -0.22765 1   MET A C   
4    O O   . MET A 1   ? 1.22549 0.89087 0.92061 0.29965  0.08798  -0.23577 1   MET A O   
5    C CB  . MET A 1   ? 1.59216 1.06034 1.23940 0.27392  0.11461  -0.22875 1   MET A CB  
6    C CG  . MET A 1   ? 1.58096 1.06570 1.25752 0.22370  0.10826  -0.23769 1   MET A CG  
7    S SD  . MET A 1   ? 1.69021 1.11783 1.36519 0.19957  0.11991  -0.22344 1   MET A SD  
8    C CE  . MET A 1   ? 1.59692 1.04793 1.30246 0.14309  0.11394  -0.24794 1   MET A CE  
9    N N   . LYS A 2   ? 1.35253 0.97490 1.03583 0.32722  0.09542  -0.20671 2   LYS A N   
10   C CA  . LYS A 2   ? 1.19702 0.90913 0.91200 0.33615  0.08620  -0.19583 2   LYS A CA  
11   C C   . LYS A 2   ? 1.03278 0.78510 0.78390 0.29638  0.07734  -0.18755 2   LYS A C   
12   O O   . LYS A 2   ? 1.05244 0.76941 0.80646 0.27309  0.07716  -0.18146 2   LYS A O   
13   C CB  . LYS A 2   ? 1.21029 0.93090 0.91729 0.37374  0.08799  -0.18110 2   LYS A CB  
14   C CG  . LYS A 2   ? 1.25843 0.92504 0.91966 0.42054  0.09838  -0.18607 2   LYS A CG  
15   C CD  . LYS A 2   ? 1.38214 1.11908 1.04817 0.46547  0.09472  -0.18279 2   LYS A CD  
16   C CE  . LYS A 2   ? 1.45336 1.15515 1.08426 0.49790  0.09992  -0.18187 2   LYS A CE  
17   N NZ  . LYS A 2   ? 1.52463 1.13809 1.11499 0.51075  0.10844  -0.16563 2   LYS A NZ  
18   N N   . TYR A 3   ? 1.00291 0.82666 0.77870 0.28931  0.07237  -0.18745 3   TYR A N   
19   C CA  . TYR A 3   ? 0.94214 0.79908 0.74505 0.25613  0.06634  -0.17922 3   TYR A CA  
20   C C   . TYR A 3   ? 0.91254 0.84272 0.73811 0.25802  0.06727  -0.17384 3   TYR A C   
21   O O   . TYR A 3   ? 0.94908 0.91271 0.77203 0.27965  0.07199  -0.18118 3   TYR A O   
22   C CB  . TYR A 3   ? 0.92483 0.77006 0.72328 0.23246  0.06313  -0.19091 3   TYR A CB  
23   C CG  . TYR A 3   ? 1.02088 0.90675 0.81589 0.23816  0.06464  -0.19972 3   TYR A CG  
24   C CD1 . TYR A 3   ? 1.09766 0.97061 0.87038 0.25945  0.06889  -0.21590 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 0.91279 0.84463 0.72207 0.22343  0.06434  -0.19126 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 1.09593 1.00726 0.86346 0.26548  0.07167  -0.22349 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 0.99653 0.96036 0.79715 0.22908  0.06943  -0.19715 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 1.03100 0.98770 0.81209 0.24985  0.07251  -0.21335 3   TYR A CZ  
29   O OH  . TYR A 3   ? 0.90568 0.89540 0.67619 0.25621  0.07882  -0.21891 3   TYR A OH  
30   N N   . MET A 4   ? 0.87384 0.82802 0.72114 0.23366  0.06476  -0.16257 4   MET A N   
31   C CA  . MET A 4   ? 0.80268 0.81726 0.66997 0.22498  0.06995  -0.15919 4   MET A CA  
32   C C   . MET A 4   ? 0.70739 0.71924 0.58136 0.19505  0.06915  -0.15018 4   MET A C   
33   O O   . MET A 4   ? 0.75574 0.73149 0.62571 0.18357  0.06205  -0.14630 4   MET A O   
34   C CB  . MET A 4   ? 0.77472 0.82946 0.66129 0.23562  0.07076  -0.15557 4   MET A CB  
35   C CG  . MET A 4   ? 0.73381 0.77648 0.63249 0.22146  0.06515  -0.14332 4   MET A CG  
36   S SD  . MET A 4   ? 0.84639 0.92271 0.76814 0.18565  0.07031  -0.13633 4   MET A SD  
37   C CE  . MET A 4   ? 0.79833 0.94783 0.73629 0.18816  0.08326  -0.14881 4   MET A CE  
38   N N   . ILE A 5   ? 0.70559 0.75536 0.58764 0.18317  0.07864  -0.14744 5   ILE A N   
39   C CA  . ILE A 5   ? 0.79485 0.83761 0.67458 0.16051  0.08155  -0.13722 5   ILE A CA  
40   C C   . ILE A 5   ? 0.76502 0.84280 0.66193 0.14482  0.09445  -0.13190 5   ILE A C   
41   O O   . ILE A 5   ? 0.76743 0.88355 0.67034 0.14614  0.10704  -0.13909 5   ILE A O   
42   C CB  . ILE A 5   ? 0.77557 0.81079 0.63059 0.16182  0.08513  -0.14020 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.73796 0.74343 0.57797 0.17349  0.07279  -0.15178 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.69286 0.71739 0.53785 0.14611  0.08883  -0.12731 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.76402 0.77181 0.57893 0.18032  0.07467  -0.15986 5   ILE A CD1 
46   N N   . THR A 6   ? 0.68066 0.74676 0.58587 0.12824  0.09294  -0.12171 6   THR A N   
47   C CA  . THR A 6   ? 0.74144 0.83030 0.65899 0.10761  0.10754  -0.11846 6   THR A CA  
48   C C   . THR A 6   ? 0.72984 0.79113 0.62355 0.09380  0.11949  -0.10735 6   THR A C   
49   O O   . THR A 6   ? 0.78326 0.81164 0.65754 0.10005  0.11009  -0.10005 6   THR A O   
50   C CB  . THR A 6   ? 0.73964 0.83107 0.67727 0.09991  0.10027  -0.11529 6   THR A CB  
51   O OG1 . THR A 6   ? 0.69489 0.74460 0.62321 0.10210  0.08670  -0.10559 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.73664 0.86412 0.69359 0.11701  0.09284  -0.12575 6   THR A CG2 
53   N N   . SER A 7   ? 0.75446 0.83020 0.64768 0.07567  0.14195  -0.10723 7   SER A N   
54   C CA  . SER A 7   ? 0.71451 0.75608 0.57556 0.06576  0.15953  -0.09456 7   SER A CA  
55   C C   . SER A 7   ? 0.82647 0.85875 0.69300 0.03914  0.17723  -0.09055 7   SER A C   
56   O O   . SER A 7   ? 0.80943 0.87943 0.70700 0.02308  0.18321  -0.10324 7   SER A O   
57   C CB  . SER A 7   ? 0.83723 0.88955 0.67830 0.06818  0.17871  -0.09737 7   SER A CB  
58   O OG  . SER A 7   ? 0.80847 0.82033 0.61005 0.06170  0.19929  -0.08229 7   SER A OG  
59   N N   . LYS A 8   ? 0.91128 0.89405 0.74514 0.03647  0.18575  -0.07451 8   LYS A N   
60   C CA  . LYS A 8   ? 0.95275 0.91243 0.78286 0.01127  0.20650  -0.07039 8   LYS A CA  
61   C C   . LYS A 8   ? 0.94772 0.91907 0.77569 -0.01471 0.24096  -0.07831 8   LYS A C   
62   O O   . LYS A 8   ? 1.00099 0.97458 0.84262 -0.04413 0.25936  -0.08625 8   LYS A O   
63   C CB  . LYS A 8   ? 0.96662 0.86510 0.75352 0.02128  0.20983  -0.05014 8   LYS A CB  
64   C CG  . LYS A 8   ? 1.11234 0.97533 0.89127 -0.00093 0.22898  -0.04546 8   LYS A CG  
65   C CD  . LYS A 8   ? 1.17584 0.97058 0.89556 0.01172  0.24576  -0.02384 8   LYS A CD  
66   C CE  . LYS A 8   ? 1.36006 1.11004 1.06779 -0.00675 0.26364  -0.01929 8   LYS A CE  
67   N NZ  . LYS A 8   ? 1.46820 1.23248 1.20038 -0.04832 0.29009  -0.03660 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.91369 0.89433 0.72496 -0.00646 0.25164  -0.07853 9   GLY A N   
69   C CA  . GLY A 9   ? 1.01870 1.01690 0.82935 -0.03157 0.28625  -0.08758 9   GLY A CA  
70   C C   . GLY A 9   ? 0.93333 0.87173 0.68559 -0.03297 0.31814  -0.06927 9   GLY A C   
71   O O   . GLY A 9   ? 1.21147 1.16344 0.95637 -0.04856 0.34764  -0.07498 9   GLY A O   
72   N N   . ASP A 10  ? 1.00546 0.87976 0.71346 -0.01491 0.31449  -0.04741 10  ASP A N   
73   C CA  . ASP A 10  ? 1.13604 0.94806 0.77820 -0.00741 0.34462  -0.02688 10  ASP A CA  
74   C C   . ASP A 10  ? 1.15262 0.98153 0.77223 0.02403  0.33454  -0.02323 10  ASP A C   
75   O O   . ASP A 10  ? 1.10728 0.98717 0.76004 0.04063  0.30259  -0.03608 10  ASP A O   
76   C CB  . ASP A 10  ? 1.14138 0.88395 0.73933 0.00946  0.34280  -0.00512 10  ASP A CB  
77   C CG  . ASP A 10  ? 1.10202 0.86316 0.71244 0.04323  0.29735  -0.00320 10  ASP A CG  
78   O OD1 . ASP A 10  ? 1.08956 0.90865 0.74342 0.04917  0.26904  -0.01886 10  ASP A OD1 
79   O OD2 . ASP A 10  ? 1.19454 0.91173 0.76985 0.06394  0.29175  0.01301  10  ASP A OD2 
80   N N   . GLU A 11  ? 1.18006 0.96032 0.73743 0.03322  0.36431  -0.00547 11  GLU A N   
81   C CA  . GLU A 11  ? 1.20050 0.99755 0.73126 0.06193  0.35934  -0.00319 11  GLU A CA  
82   C C   . GLU A 11  ? 1.17517 0.98634 0.70331 0.10205  0.31497  -0.00248 11  GLU A C   
83   O O   . GLU A 11  ? 1.13744 0.99201 0.67931 0.11891  0.29475  -0.01514 11  GLU A O   
84   C CB  . GLU A 11  ? 1.33022 1.06413 0.78489 0.06839  0.40116  0.01928  11  GLU A CB  
85   C CG  . GLU A 11  ? 1.25331 0.98038 0.70871 0.02575  0.45071  0.01443  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.52356 1.18222 0.89605 0.03514  0.49488  0.03864  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.56059 1.19727 0.87969 0.08112  0.48157  0.05575  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.58113 1.20927 0.94153 -0.00351 0.54280  0.03943  11  GLU A OE2 
89   N N   . LYS A 12  ? 1.13328 0.91021 0.64431 0.11665  0.30057  0.00968  12  LYS A N   
90   C CA  . LYS A 12  ? 1.04991 0.84605 0.55900 0.15146  0.26114  0.00715  12  LYS A CA  
91   C C   . LYS A 12  ? 1.08544 0.93892 0.66092 0.14366  0.22750  -0.01650 12  LYS A C   
92   O O   . LYS A 12  ? 0.96734 0.85259 0.54839 0.16271  0.20477  -0.02877 12  LYS A O   
93   C CB  . LYS A 12  ? 1.27471 1.03069 0.75644 0.16775  0.25404  0.02292  12  LYS A CB  
94   C CG  . LYS A 12  ? 1.32575 1.11393 0.81359 0.19888  0.21352  0.01527  12  LYS A CG  
95   C CD  . LYS A 12  ? 1.34416 1.09855 0.78961 0.22657  0.20960  0.03226  12  LYS A CD  
96   C CE  . LYS A 12  ? 1.39223 1.19124 0.83675 0.26006  0.17305  0.02077  12  LYS A CE  
97   N NZ  . LYS A 12  ? 1.32729 1.11250 0.74384 0.28815  0.16278  0.03194  12  LYS A NZ  
98   N N   . SER A 13  ? 1.05574 0.91975 0.67806 0.11666  0.22548  -0.02376 13  SER A N   
99   C CA  . SER A 13  ? 0.91828 0.82683 0.59512 0.11346  0.19607  -0.04267 13  SER A CA  
100  C C   . SER A 13  ? 0.93592 0.88576 0.63521 0.10941  0.19963  -0.05881 13  SER A C   
101  O O   . SER A 13  ? 0.90902 0.88568 0.62836 0.12250  0.17615  -0.07274 13  SER A O   
102  C CB  . SER A 13  ? 0.97800 0.88674 0.69201 0.09106  0.19299  -0.04450 13  SER A CB  
103  O OG  . SER A 13  ? 0.92046 0.78916 0.61072 0.09570  0.19301  -0.02944 13  SER A OG  
104  N N   . ASP A 14  ? 0.99104 0.94554 0.68602 0.09098  0.23089  -0.05849 14  ASP A N   
105  C CA  . ASP A 14  ? 0.98858 0.99046 0.70594 0.08885  0.23597  -0.07508 14  ASP A CA  
106  C C   . ASP A 14  ? 0.88707 0.89423 0.57662 0.11763  0.22625  -0.07795 14  ASP A C   
107  O O   . ASP A 14  ? 0.83113 0.87394 0.54349 0.12854  0.21120  -0.09469 14  ASP A O   
108  C CB  . ASP A 14  ? 0.98280 0.99179 0.69828 0.06068  0.27553  -0.07558 14  ASP A CB  
109  C CG  . ASP A 14  ? 1.07210 1.12021 0.83997 0.03222  0.27907  -0.09083 14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.88270 0.93978 0.68026 0.03592  0.25260  -0.09520 14  ASP A OD1 
111  O OD2 . ASP A 14  ? 1.14715 1.22108 0.92618 0.00599  0.30923  -0.10007 14  ASP A OD2 
112  N N   . LEU A 15  ? 0.98721 0.95815 0.62367 0.13317  0.23483  -0.06251 15  LEU A N   
113  C CA  . LEU A 15  ? 1.02843 1.00871 0.63464 0.16100  0.22687  -0.06723 15  LEU A CA  
114  C C   . LEU A 15  ? 0.92026 0.90592 0.53180 0.18260  0.18920  -0.07700 15  LEU A C   
115  O O   . LEU A 15  ? 0.90288 0.90904 0.50877 0.20049  0.17590  -0.09176 15  LEU A O   
116  C CB  . LEU A 15  ? 0.99344 0.93693 0.53462 0.17278  0.25365  -0.04720 15  LEU A CB  
117  C CG  . LEU A 15  ? 1.26720 1.21624 0.79541 0.15700  0.29291  -0.04507 15  LEU A CG  
118  C CD1 . LEU A 15  ? 1.14154 1.07493 0.68791 0.11840  0.32328  -0.03923 15  LEU A CD1 
119  C CD2 . LEU A 15  ? 1.10448 1.02263 0.56085 0.18087  0.31349  -0.02851 15  LEU A CD2 
120  N N   . LEU A 16  ? 0.87803 0.84693 0.50054 0.17948  0.17330  -0.07145 16  LEU A N   
121  C CA  . LEU A 16  ? 0.86145 0.84248 0.50028 0.19138  0.13992  -0.08561 16  LEU A CA  
122  C C   . LEU A 16  ? 0.90019 0.90445 0.58453 0.18251  0.12708  -0.10501 16  LEU A C   
123  O O   . LEU A 16  ? 0.91969 0.93384 0.60917 0.19334  0.10753  -0.12261 16  LEU A O   
124  C CB  . LEU A 16  ? 0.86899 0.83152 0.51231 0.18830  0.12872  -0.07570 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.91487 0.89262 0.57467 0.19654  0.09760  -0.09137 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.84677 0.84021 0.47152 0.22230  0.08693  -0.10130 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.80695 0.77206 0.47536 0.19180  0.08956  -0.08141 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.86311 0.87564 0.57775 0.16404  0.13911  -0.10338 17  ARG A N   
129  C CA  . ARG A 17  ? 0.86661 0.90106 0.61742 0.16288  0.12912  -0.11947 17  ARG A CA  
130  C C   . ARG A 17  ? 0.83705 0.89201 0.57759 0.17840  0.13280  -0.13362 17  ARG A C   
131  O O   . ARG A 17  ? 0.87131 0.92884 0.62133 0.19006  0.11736  -0.14953 17  ARG A O   
132  C CB  . ARG A 17  ? 0.73829 0.78845 0.52090 0.14361  0.14127  -0.11616 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.71870 0.79940 0.53234 0.14944  0.13506  -0.13138 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.81541 0.92239 0.66055 0.13161  0.14497  -0.13063 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.77081 0.91545 0.64181 0.14403  0.13928  -0.14512 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.76469 0.95312 0.64227 0.15021  0.15204  -0.15672 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.71710 0.91477 0.57772 0.14159  0.17326  -0.15543 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.68421 0.90857 0.58301 0.16797  0.14460  -0.16957 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.84843 0.91362 0.56623 0.17879  0.15562  -0.12820 18  LEU A N   
140  C CA  . LEU A 18  ? 0.94217 1.03018 0.64866 0.19474  0.16082  -0.14172 18  LEU A CA  
141  C C   . LEU A 18  ? 0.85242 0.92820 0.53022 0.21619  0.14303  -0.15193 18  LEU A C   
142  O O   . LEU A 18  ? 0.86266 0.95115 0.53894 0.23114  0.13727  -0.16982 18  LEU A O   
143  C CB  . LEU A 18  ? 0.97768 1.07841 0.66371 0.18769  0.19296  -0.13273 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.97629 1.10897 0.69651 0.16503  0.21390  -0.13426 18  LEU A CG  
145  C CD1 . LEU A 18  ? 1.04210 1.18860 0.74027 0.15571  0.24939  -0.12968 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.97140 1.14286 0.73006 0.17498  0.19965  -0.15392 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.86844 0.92310 0.52270 0.21932  0.13423  -0.14329 19  ASN A N   
148  C CA  . ASN A 19  ? 0.90437 0.95888 0.53463 0.23823  0.11551  -0.15808 19  ASN A CA  
149  C C   . ASN A 19  ? 0.92828 0.97743 0.58754 0.23443  0.09146  -0.17807 19  ASN A C   
150  O O   . ASN A 19  ? 0.97994 1.03269 0.63082 0.24544  0.08002  -0.20056 19  ASN A O   
151  C CB  . ASN A 19  ? 0.90664 0.95029 0.50117 0.24746  0.11332  -0.14426 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.95674 1.00154 0.50045 0.26526  0.13328  -0.13336 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.97418 1.03410 0.50903 0.27244  0.14341  -0.14244 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.98614 1.01272 0.49182 0.27554  0.14025  -0.11318 19  ASN A ND2 
155  N N   . MET A 20  ? 0.83485 0.87162 0.52534 0.21789  0.08582  -0.17102 20  MET A N   
156  C CA  . MET A 20  ? 0.88009 0.90366 0.59431 0.21231  0.06828  -0.18759 20  MET A CA  
157  C C   . MET A 20  ? 0.91317 0.93423 0.63877 0.21909  0.07182  -0.20075 20  MET A C   
158  O O   . MET A 20  ? 1.00971 1.01360 0.73435 0.22313  0.06185  -0.22109 20  MET A O   
159  C CB  . MET A 20  ? 0.77993 0.79064 0.52039 0.19514  0.06364  -0.17455 20  MET A CB  
160  C CG  . MET A 20  ? 0.84117 0.85246 0.57041 0.19264  0.05585  -0.16638 20  MET A CG  
161  S SD  . MET A 20  ? 0.84525 0.84237 0.60574 0.17369  0.04945  -0.15463 20  MET A SD  
162  C CE  . MET A 20  ? 0.86665 0.84897 0.64919 0.16564  0.03577  -0.17823 20  MET A CE  
163  N N   . ILE A 21  ? 0.88213 0.92072 0.61685 0.22102  0.08744  -0.19128 21  ILE A N   
164  C CA  . ILE A 21  ? 0.85602 0.90129 0.59759 0.23523  0.09129  -0.20396 21  ILE A CA  
165  C C   . ILE A 21  ? 0.89883 0.94567 0.61231 0.25317  0.09077  -0.22268 21  ILE A C   
166  O O   . ILE A 21  ? 0.93195 0.96024 0.64178 0.26566  0.08512  -0.24080 21  ILE A O   
167  C CB  . ILE A 21  ? 0.83997 0.92109 0.59891 0.23347  0.10865  -0.19390 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.79952 0.88042 0.58789 0.21721  0.10705  -0.18100 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.83243 0.93279 0.59392 0.25551  0.11306  -0.20868 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.75513 0.87989 0.56481 0.21040  0.12391  -0.17628 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.87563 0.93984 0.56404 0.25634  0.09810  -0.21853 22  ALA A N   
172  C CA  . ALA A 22  ? 0.93183 1.00169 0.59019 0.27470  0.09722  -0.23692 22  ALA A CA  
173  C C   . ALA A 22  ? 0.94953 0.99437 0.60006 0.27494  0.07729  -0.25937 22  ALA A C   
174  O O   . ALA A 22  ? 0.95854 0.99198 0.59857 0.28692  0.07397  -0.28270 22  ALA A O   
175  C CB  . ALA A 22  ? 0.93045 1.01993 0.55738 0.27945  0.10942  -0.22486 22  ALA A CB  
176  N N   . GLY A 23  ? 0.91427 0.95147 0.56981 0.26074  0.06526  -0.25501 23  GLY A N   
177  C CA  . GLY A 23  ? 0.92940 0.95025 0.58462 0.25424  0.04803  -0.27999 23  GLY A CA  
178  C C   . GLY A 23  ? 1.10100 1.08336 0.77560 0.24656  0.04653  -0.29217 23  GLY A C   
179  O O   . GLY A 23  ? 1.12247 1.08265 0.78868 0.24471  0.04044  -0.32005 23  GLY A O   
180  N N   . PHE A 24  ? 0.94391 0.91537 0.64091 0.24266  0.05360  -0.27248 24  PHE A N   
181  C CA  . PHE A 24  ? 1.01918 0.94965 0.72563 0.24321  0.05504  -0.27985 24  PHE A CA  
182  C C   . PHE A 24  ? 1.07172 0.99181 0.75922 0.26744  0.06289  -0.29507 24  PHE A C   
183  O O   . PHE A 24  ? 1.14517 1.01828 0.82424 0.27223  0.06421  -0.31012 24  PHE A O   
184  C CB  . PHE A 24  ? 1.02649 0.95732 0.75792 0.23894  0.05960  -0.25518 24  PHE A CB  
185  C CG  . PHE A 24  ? 1.04104 0.95861 0.79045 0.21581  0.05177  -0.24606 24  PHE A CG  
186  C CD1 . PHE A 24  ? 1.08109 0.96339 0.82928 0.20149  0.04513  -0.26318 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.96714 0.90769 0.73445 0.20657  0.05310  -0.22252 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 1.14030 1.01641 0.90665 0.18003  0.03932  -0.25590 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.98365 0.91367 0.76631 0.18783  0.04618  -0.21460 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.99494 0.89568 0.77806 0.17535  0.03894  -0.23079 24  PHE A CZ  
191  N N   . GLY A 25  ? 1.07390 1.03339 0.75116 0.28362  0.07060  -0.29142 25  GLY A N   
192  C CA  . GLY A 25  ? 0.99618 0.95288 0.65501 0.30949  0.07829  -0.30679 25  GLY A CA  
193  C C   . GLY A 25  ? 1.17497 1.10290 0.80651 0.31311  0.07267  -0.33772 25  GLY A C   
194  O O   . GLY A 25  ? 1.16111 1.07000 0.77369 0.33488  0.07873  -0.35433 25  GLY A O   
195  N N   . GLU A 26  ? 1.19289 1.12079 0.82153 0.29330  0.06127  -0.34831 26  GLU A N   
196  C CA  . GLU A 26  ? 1.22350 1.13096 0.83029 0.29065  0.05464  -0.38351 26  GLU A CA  
197  C C   . GLU A 26  ? 1.29018 1.13542 0.90191 0.27255  0.05375  -0.40105 26  GLU A C   
198  O O   . GLU A 26  ? 1.37890 1.20367 0.97675 0.26126  0.04961  -0.43459 26  GLU A O   
199  C CB  . GLU A 26  ? 1.10981 1.05979 0.71011 0.28080  0.04225  -0.39073 26  GLU A CB  
200  C CG  . GLU A 26  ? 1.09034 1.09069 0.67542 0.29930  0.04740  -0.37166 26  GLU A CG  
201  C CD  . GLU A 26  ? 1.12592 1.13317 0.68574 0.32502  0.05763  -0.38321 26  GLU A CD  
202  O OE1 . GLU A 26  ? 1.18687 1.16804 0.73834 0.32432  0.05450  -0.40821 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 1.13483 1.17244 0.69045 0.33822  0.07029  -0.36138 26  GLU A OE2 
204  N N   . TYR A 27  ? 1.22983 1.04444 0.85904 0.26851  0.05929  -0.38048 27  TYR A N   
205  C CA  . TYR A 27  ? 1.35757 1.10241 0.98498 0.25403  0.06434  -0.39195 27  TYR A CA  
206  C C   . TYR A 27  ? 1.36919 1.07515 0.98853 0.28059  0.07706  -0.37518 27  TYR A C   
207  O O   . TYR A 27  ? 1.34550 1.09093 0.96890 0.30599  0.07960  -0.35695 27  TYR A O   
208  C CB  . TYR A 27  ? 1.34934 1.09534 1.00393 0.22152  0.05760  -0.38247 27  TYR A CB  
209  C CG  . TYR A 27  ? 1.33889 1.13254 1.00247 0.19998  0.04335  -0.39874 27  TYR A CG  
210  C CD1 . TYR A 27  ? 1.12389 0.98171 0.79701 0.20576  0.03425  -0.37893 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 1.40383 1.17869 1.06411 0.17475  0.04043  -0.43528 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 1.13597 1.03876 0.81116 0.19430  0.02069  -0.39248 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 1.33167 1.16289 1.00117 0.15925  0.02528  -0.45313 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 1.29011 1.18565 0.96517 0.17273  0.01446  -0.43029 27  TYR A CZ  
215  O OH  . TYR A 27  ? 1.20699 1.15989 0.88513 0.16527  -0.00113 -0.44688 27  TYR A OH  
216  N N   . ASP A 28  ? 1.51919 1.14830 1.12504 0.27547  0.08667  -0.38233 28  ASP A N   
217  C CA  . ASP A 28  ? 1.54431 1.13271 1.13763 0.30515  0.09824  -0.36354 28  ASP A CA  
218  C C   . ASP A 28  ? 1.55871 1.16839 1.18182 0.29562  0.09424  -0.33217 28  ASP A C   
219  O O   . ASP A 28  ? 1.63490 1.19036 1.25528 0.28413  0.10052  -0.32499 28  ASP A O   
220  C CB  . ASP A 28  ? 1.74953 1.23916 1.30953 0.30547  0.11403  -0.37942 28  ASP A CB  
221  C CG  . ASP A 28  ? 1.86261 1.32145 1.41190 0.33871  0.12470  -0.35339 28  ASP A CG  
222  O OD1 . ASP A 28  ? 1.77329 1.29221 1.33447 0.36856  0.11939  -0.33407 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 2.01924 1.39828 1.54842 0.33464  0.13848  -0.35276 28  ASP A OD2 
224  N N   . MET A 29  ? 1.44850 1.13669 1.09814 0.29929  0.08566  -0.31413 29  MET A N   
225  C CA  . MET A 29  ? 1.45771 1.17633 1.13636 0.29181  0.08172  -0.28626 29  MET A CA  
226  C C   . MET A 29  ? 1.48412 1.26211 1.17291 0.31995  0.08348  -0.27190 29  MET A C   
227  O O   . MET A 29  ? 1.52571 1.35988 1.22218 0.31987  0.08192  -0.27371 29  MET A O   
228  C CB  . MET A 29  ? 1.39836 1.15466 1.10253 0.25709  0.07102  -0.28192 29  MET A CB  
229  C CG  . MET A 29  ? 1.47745 1.19144 1.17996 0.22630  0.06863  -0.29827 29  MET A CG  
230  S SD  . MET A 29  ? 1.67614 1.33931 1.38763 0.21250  0.07450  -0.28115 29  MET A SD  
231  C CE  . MET A 29  ? 1.70268 1.28783 1.39231 0.18755  0.08437  -0.31290 29  MET A CE  
232  N N   . GLU A 30  ? 1.33570 1.10389 1.02288 0.34443  0.08806  -0.25902 30  GLU A N   
233  C CA  . GLU A 30  ? 1.26117 1.09479 0.96153 0.37156  0.08995  -0.25036 30  GLU A CA  
234  C C   . GLU A 30  ? 1.13766 1.02229 0.87405 0.35334  0.08513  -0.23064 30  GLU A C   
235  O O   . GLU A 30  ? 1.14797 1.00229 0.89021 0.34007  0.08185  -0.21905 30  GLU A O   
236  C CB  . GLU A 30  ? 1.25104 1.05500 0.92537 0.41723  0.09673  -0.25131 30  GLU A CB  
237  C CG  . GLU A 30  ? 1.35149 1.09116 1.01178 0.42225  0.09871  -0.23856 30  GLU A CG  
238  C CD  . GLU A 30  ? 1.45297 1.15882 1.08508 0.46087  0.10447  -0.23201 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.47921 1.24842 1.12022 0.48836  0.10185  -0.22932 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 1.48466 1.10266 1.08634 0.46015  0.11211  -0.22850 30  GLU A OE2 
241  N N   . TYR A 31  ? 1.04494 1.00488 0.80386 0.35083  0.08702  -0.22820 31  TYR A N   
242  C CA  . TYR A 31  ? 1.03730 1.04691 0.82937 0.33187  0.08558  -0.21327 31  TYR A CA  
243  C C   . TYR A 31  ? 1.00016 1.03624 0.80088 0.35996  0.08551  -0.20892 31  TYR A C   
244  O O   . TYR A 31  ? 0.94003 1.01469 0.73744 0.39199  0.08996  -0.21817 31  TYR A O   
245  C CB  . TYR A 31  ? 0.82150 0.89473 0.63011 0.31590  0.09288  -0.21413 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.92444 1.03298 0.76202 0.28694  0.09455  -0.20053 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.96298 1.12378 0.82622 0.29190  0.09722  -0.19863 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.98568 1.07683 0.82279 0.25656  0.09377  -0.19166 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.79405 0.98308 0.68227 0.26277  0.10047  -0.18962 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.91459 1.02850 0.77261 0.23169  0.09765  -0.17953 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.80586 0.96593 0.68969 0.23258  0.10174  -0.17924 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.76509 0.94414 0.66844 0.20519  0.10723  -0.17048 31  TYR A OH  
253  N N   . ASP A 32  ? 0.88734 0.90752 0.69780 0.35088  0.08007  -0.19591 32  ASP A N   
254  C CA  . ASP A 32  ? 0.93235 0.98219 0.74939 0.37869  0.07802  -0.19121 32  ASP A CA  
255  C C   . ASP A 32  ? 0.95322 1.01993 0.79635 0.35094  0.07301  -0.17833 32  ASP A C   
256  O O   . ASP A 32  ? 0.91144 0.91990 0.74623 0.33364  0.06955  -0.16824 32  ASP A O   
257  C CB  . ASP A 32  ? 1.12349 1.10224 0.90109 0.41618  0.07851  -0.18920 32  ASP A CB  
258  C CG  . ASP A 32  ? 1.18640 1.20151 0.96195 0.45797  0.07613  -0.18500 32  ASP A CG  
259  O OD1 . ASP A 32  ? 1.06334 1.14871 0.87221 0.44818  0.07121  -0.18217 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 1.33415 1.30649 1.07356 0.49695  0.07837  -0.18318 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.92491 1.07272 0.79997 0.34509  0.07400  -0.18112 33  ASP A N   
262  C CA  . ASP A 33  ? 0.93216 1.10112 0.83180 0.32029  0.07021  -0.17219 33  ASP A CA  
263  C C   . ASP A 33  ? 0.89325 1.08287 0.79257 0.35128  0.06339  -0.16961 33  ASP A C   
264  O O   . ASP A 33  ? 0.87829 1.10014 0.79980 0.33520  0.05981  -0.16610 33  ASP A O   
265  C CB  . ASP A 33  ? 0.80387 1.04280 0.73675 0.28859  0.07841  -0.17903 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.85357 1.17966 0.80468 0.30798  0.08443  -0.19658 33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.89744 1.23494 0.83493 0.35182  0.07981  -0.20279 33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.77982 1.16324 0.75753 0.27928  0.09580  -0.20498 33  ASP A OD2 
269  N N   . VAL A 34  ? 0.94215 1.11251 0.81272 0.39809  0.06215  -0.17154 34  VAL A N   
270  C CA  . VAL A 34  ? 1.02274 1.20325 0.88080 0.43752  0.05601  -0.16651 34  VAL A CA  
271  C C   . VAL A 34  ? 1.06602 1.14280 0.88543 0.44536  0.05627  -0.14852 34  VAL A C   
272  O O   . VAL A 34  ? 0.99302 1.06353 0.81261 0.44459  0.05186  -0.13718 34  VAL A O   
273  C CB  . VAL A 34  ? 1.00881 1.23601 0.85353 0.49168  0.05620  -0.17868 34  VAL A CB  
274  C CG1 . VAL A 34  ? 0.98600 1.21520 0.80988 0.52659  0.04591  -0.16623 34  VAL A CG1 
275  C CG2 . VAL A 34  ? 0.88029 1.21895 0.76865 0.47640  0.05772  -0.19782 34  VAL A CG2 
276  N N   . GLU A 35  ? 1.09061 1.08495 0.87601 0.45059  0.06334  -0.14747 35  GLU A N   
277  C CA  . GLU A 35  ? 1.13452 1.02342 0.88251 0.45027  0.06898  -0.13386 35  GLU A CA  
278  C C   . GLU A 35  ? 1.13431 0.96723 0.88305 0.40672  0.07337  -0.13816 35  GLU A C   
279  O O   . GLU A 35  ? 1.22525 0.98592 0.94023 0.41468  0.08209  -0.14348 35  GLU A O   
280  C CB  . GLU A 35  ? 1.28727 1.11910 0.98270 0.50425  0.07655  -0.13033 35  GLU A CB  
281  C CG  . GLU A 35  ? 1.33530 1.21382 1.02358 0.54001  0.06843  -0.11848 35  GLU A CG  
282  C CD  . GLU A 35  ? 1.45103 1.25714 1.08135 0.57561  0.07477  -0.10428 35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.37795 1.14973 0.98685 0.58466  0.08091  -0.11080 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.60428 1.38549 1.20687 0.59489  0.07497  -0.08648 35  GLU A OE2 
285  N N   . PRO A 36  ? 0.98306 0.84756 0.76744 0.36162  0.06799  -0.13763 36  PRO A N   
286  C CA  . PRO A 36  ? 1.05723 0.87849 0.84166 0.32467  0.06995  -0.14292 36  PRO A CA  
287  C C   . PRO A 36  ? 1.04505 0.79150 0.81325 0.30794  0.07430  -0.13429 36  PRO A C   
288  O O   . PRO A 36  ? 1.14025 0.88015 0.90807 0.31208  0.07395  -0.12010 36  PRO A O   
289  C CB  . PRO A 36  ? 0.96195 0.84800 0.78531 0.29099  0.06362  -0.14296 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.94674 0.87777 0.78932 0.29588  0.05954  -0.13300 36  PRO A CG  
291  C CD  . PRO A 36  ? 1.01859 0.95830 0.84196 0.34332  0.06073  -0.13367 36  PRO A CD  
292  N N   . GLU A 37  ? 1.04217 0.73491 0.79667 0.28800  0.07956  -0.14529 37  GLU A N   
293  C CA  . GLU A 37  ? 1.09316 0.72516 0.84027 0.26035  0.08554  -0.14277 37  GLU A CA  
294  C C   . GLU A 37  ? 1.06326 0.72921 0.84324 0.21818  0.07686  -0.14708 37  GLU A C   
295  O O   . GLU A 37  ? 1.01679 0.65459 0.80101 0.19294  0.07969  -0.14426 37  GLU A O   
296  C CB  . GLU A 37  ? 1.11192 0.65984 0.82137 0.26243  0.09983  -0.15676 37  GLU A CB  
297  C CG  . GLU A 37  ? 1.20868 0.71496 0.87644 0.31105  0.11008  -0.15348 37  GLU A CG  
298  C CD  . GLU A 37  ? 1.37640 0.77659 0.99849 0.31082  0.13006  -0.16405 37  GLU A CD  
299  O OE1 . GLU A 37  ? 1.29081 0.63019 0.90176 0.28657  0.14240  -0.15963 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 1.23725 0.61307 0.83354 0.33334  0.13555  -0.17804 37  GLU A OE2 
301  N N   . ILE A 38  ? 1.02017 0.74557 0.82028 0.21251  0.06801  -0.15335 38  ILE A N   
302  C CA  . ILE A 38  ? 0.96756 0.72744 0.79170 0.18167  0.05992  -0.15543 38  ILE A CA  
303  C C   . ILE A 38  ? 0.84272 0.66800 0.68744 0.18534  0.05469  -0.14619 38  ILE A C   
304  O O   . ILE A 38  ? 0.84731 0.70150 0.68930 0.20232  0.05646  -0.15091 38  ILE A O   
305  C CB  . ILE A 38  ? 0.95477 0.70747 0.77126 0.16908  0.05845  -0.17655 38  ILE A CB  
306  C CG1 . ILE A 38  ? 1.06452 0.75665 0.86777 0.15170  0.06535  -0.18995 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 0.86225 0.66524 0.69726 0.15143  0.04908  -0.17651 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 1.21455 0.89612 1.00614 0.14273  0.06536  -0.21711 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.83130 0.67814 0.69547 0.16824  0.05065  -0.13441 39  VAL A N   
310  C CA  . VAL A 39  ? 0.86950 0.76863 0.75124 0.16509  0.04966  -0.12677 39  VAL A CA  
311  C C   . VAL A 39  ? 0.76441 0.67426 0.65174 0.14340  0.04634  -0.12552 39  VAL A C   
312  O O   . VAL A 39  ? 0.67085 0.56688 0.56388 0.12881  0.04227  -0.12107 39  VAL A O   
313  C CB  . VAL A 39  ? 0.71497 0.62954 0.61001 0.16830  0.04937  -0.11468 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.75989 0.72048 0.67358 0.15456  0.05088  -0.11007 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.73396 0.65291 0.62034 0.19851  0.05179  -0.11641 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.70735 0.64240 0.58996 0.14418  0.04923  -0.12901 40  ILE A N   
317  C CA  . ILE A 40  ? 0.70731 0.65106 0.58518 0.13226  0.04762  -0.12635 40  ILE A CA  
318  C C   . ILE A 40  ? 0.68535 0.65309 0.56957 0.12563  0.05618  -0.11390 40  ILE A C   
319  O O   . ILE A 40  ? 0.76608 0.75673 0.65221 0.12999  0.06578  -0.11526 40  ILE A O   
320  C CB  . ILE A 40  ? 0.82183 0.76892 0.68039 0.13985  0.04727  -0.13890 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.80785 0.72763 0.66002 0.14132  0.04072  -0.15597 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.66105 0.61985 0.50758 0.13525  0.04620  -0.13379 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.84615 0.76991 0.67891 0.15129  0.04047  -0.17279 40  ILE A CD1 
324  N N   . SER A 41  ? 0.69244 0.65499 0.57951 0.11406  0.05459  -0.10374 41  SER A N   
325  C CA  . SER A 41  ? 0.68791 0.66080 0.57606 0.10459  0.06557  -0.09283 41  SER A CA  
326  C C   . SER A 41  ? 0.62658 0.59120 0.48949 0.10549  0.07030  -0.08660 41  SER A C   
327  O O   . SER A 41  ? 0.69211 0.64734 0.54680 0.10893  0.06018  -0.08581 41  SER A O   
328  C CB  . SER A 41  ? 0.60428 0.57196 0.50850 0.09472  0.06244  -0.08504 41  SER A CB  
329  O OG  . SER A 41  ? 0.63033 0.59999 0.53160 0.08327  0.07462  -0.07674 41  SER A OG  
330  N N   . ILE A 42  ? 0.64473 0.61487 0.49334 0.10390  0.08695  -0.08289 42  ILE A N   
331  C CA  . ILE A 42  ? 0.76145 0.71699 0.57557 0.10982  0.09609  -0.07390 42  ILE A CA  
332  C C   . ILE A 42  ? 0.73182 0.67067 0.53773 0.09581  0.11574  -0.06091 42  ILE A C   
333  O O   . ILE A 42  ? 0.82034 0.76941 0.63468 0.08156  0.13353  -0.06324 42  ILE A O   
334  C CB  . ILE A 42  ? 0.75283 0.71826 0.54679 0.12023  0.10432  -0.07959 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.68543 0.66283 0.48741 0.13213  0.08628  -0.09602 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.78282 0.72963 0.53298 0.13190  0.11403  -0.06804 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.70884 0.69597 0.48750 0.14561  0.09169  -0.10354 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.73586 0.65050 0.52512 0.09935  0.11384  -0.04955 43  GLY A N   
339  C CA  . GLY A 43  ? 0.87831 0.76504 0.65346 0.08703  0.13391  -0.03755 43  GLY A CA  
340  C C   . GLY A 43  ? 0.84763 0.71676 0.62069 0.09156  0.12386  -0.02965 43  GLY A C   
341  O O   . GLY A 43  ? 0.96849 0.83172 0.71969 0.11233  0.11299  -0.02460 43  GLY A O   
342  N N   . GLY A 44  ? 0.92223 0.78915 0.71818 0.07385  0.12685  -0.03052 44  GLY A N   
343  C CA  . GLY A 44  ? 0.76892 0.62203 0.56526 0.07794  0.11775  -0.02416 44  GLY A CA  
344  C C   . GLY A 44  ? 0.77808 0.65724 0.61602 0.06948  0.10023  -0.03302 44  GLY A C   
345  O O   . GLY A 44  ? 0.69235 0.59786 0.55474 0.06645  0.09203  -0.04332 44  GLY A O   
346  N N   . ASP A 45  ? 0.75481 0.62378 0.59657 0.06865  0.09571  -0.02821 45  ASP A N   
347  C CA  . ASP A 45  ? 0.74324 0.63254 0.61910 0.06101  0.08264  -0.03446 45  ASP A CA  
348  C C   . ASP A 45  ? 0.70310 0.60682 0.59914 0.04363  0.09148  -0.04227 45  ASP A C   
349  O O   . ASP A 45  ? 0.62390 0.55192 0.54509 0.04311  0.08078  -0.04918 45  ASP A O   
350  C CB  . ASP A 45  ? 0.70367 0.58120 0.57699 0.06484  0.07756  -0.02783 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.70903 0.59393 0.57522 0.08217  0.06345  -0.02623 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.69167 0.59561 0.56746 0.08554  0.05301  -0.03426 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.73156 0.60594 0.58247 0.09270  0.06326  -0.01928 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.72111 0.61109 0.60442 0.02994  0.11235  -0.04260 46  GLY A N   
355  C CA  . GLY A 46  ? 0.61114 0.52862 0.51752 0.01108  0.12125  -0.05591 46  GLY A CA  
356  C C   . GLY A 46  ? 0.70975 0.66303 0.63135 0.01496  0.11798  -0.06547 46  GLY A C   
357  O O   . GLY A 46  ? 0.59735 0.58977 0.54579 0.01308  0.11171  -0.07724 46  GLY A O   
358  N N   . THR A 47  ? 0.64920 0.59136 0.55088 0.02425  0.12194  -0.06097 47  THR A N   
359  C CA  . THR A 47  ? 0.61623 0.58957 0.52914 0.03190  0.11795  -0.07010 47  THR A CA  
360  C C   . THR A 47  ? 0.57374 0.55974 0.50257 0.04876  0.09500  -0.07260 47  THR A C   
361  O O   . THR A 47  ? 0.59081 0.60654 0.53609 0.05559  0.09036  -0.08232 47  THR A O   
362  C CB  . THR A 47  ? 0.73428 0.69004 0.61789 0.04013  0.12674  -0.06461 47  THR A CB  
363  O OG1 . THR A 47  ? 0.79174 0.72542 0.65334 0.02437  0.15342  -0.06009 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.60750 0.59524 0.50128 0.04891  0.12374  -0.07547 47  THR A CG2 
365  N N   . PHE A 48  ? 0.55951 0.52231 0.48155 0.05625  0.08252  -0.06455 48  PHE A N   
366  C CA  . PHE A 48  ? 0.58789 0.55332 0.52206 0.06690  0.06608  -0.06701 48  PHE A CA  
367  C C   . PHE A 48  ? 0.64458 0.62569 0.59820 0.06496  0.06265  -0.06905 48  PHE A C   
368  O O   . PHE A 48  ? 0.53724 0.52718 0.49810 0.07687  0.05570  -0.07315 48  PHE A O   
369  C CB  . PHE A 48  ? 0.57813 0.52247 0.50361 0.07043  0.05650  -0.06125 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.67986 0.61956 0.61430 0.07589  0.04496  -0.06571 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.60188 0.53794 0.54842 0.07383  0.04114  -0.06240 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.67682 0.61171 0.60410 0.08214  0.04042  -0.07402 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.64381 0.56512 0.59248 0.07699  0.03602  -0.06519 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.75902 0.68002 0.69099 0.08285  0.03468  -0.07991 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.68545 0.59643 0.62681 0.07980  0.03399  -0.07444 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.62882 0.61061 0.58652 0.05272  0.06806  -0.06637 49  LEU A N   
377  C CA  . LEU A 49  ? 0.61791 0.62128 0.59250 0.05209  0.06425  -0.07050 49  LEU A CA  
378  C C   . LEU A 49  ? 0.55570 0.60163 0.54415 0.05600  0.06706  -0.08366 49  LEU A C   
379  O O   . LEU A 49  ? 0.54435 0.61192 0.54162 0.07037  0.05853  -0.08726 49  LEU A O   
380  C CB  . LEU A 49  ? 0.58876 0.58588 0.56356 0.03613  0.07148  -0.06912 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.66228 0.62879 0.62763 0.03803  0.06577  -0.05745 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.68680 0.64267 0.64750 0.02407  0.07576  -0.05756 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.72617 0.69626 0.70017 0.04951  0.05268  -0.05428 49  LEU A CD2 
384  N N   . SER A 50  ? 0.62069 0.68112 0.60885 0.04566  0.08010  -0.09105 50  SER A N   
385  C CA  . SER A 50  ? 0.71571 0.82691 0.71984 0.04991  0.08341  -0.10642 50  SER A CA  
386  C C   . SER A 50  ? 0.67743 0.79107 0.67717 0.07785  0.07201  -0.10586 50  SER A C   
387  O O   . SER A 50  ? 0.63236 0.78400 0.64258 0.09543  0.06623  -0.11469 50  SER A O   
388  C CB  . SER A 50  ? 0.68088 0.80259 0.68319 0.03041  0.10357  -0.11383 50  SER A CB  
389  O OG  . SER A 50  ? 0.82880 0.93555 0.82848 0.00350  0.11885  -0.11446 50  SER A OG  
390  N N   . ALA A 51  ? 0.60607 0.67937 0.58766 0.08418  0.06912  -0.09701 51  ALA A N   
391  C CA  . ALA A 51  ? 0.68020 0.74497 0.65324 0.10781  0.06144  -0.09851 51  ALA A CA  
392  C C   . ALA A 51  ? 0.60526 0.65335 0.57551 0.12434  0.05093  -0.09304 51  ALA A C   
393  O O   . ALA A 51  ? 0.61997 0.67273 0.58408 0.14875  0.04762  -0.09646 51  ALA A O   
394  C CB  . ALA A 51  ? 0.61242 0.64054 0.56730 0.10654  0.06120  -0.09454 51  ALA A CB  
395  N N   . PHE A 52  ? 0.62540 0.65101 0.59592 0.11375  0.04753  -0.08374 52  PHE A N   
396  C CA  . PHE A 52  ? 0.70321 0.70992 0.66770 0.12770  0.04118  -0.07679 52  PHE A CA  
397  C C   . PHE A 52  ? 0.63197 0.68045 0.60301 0.14619  0.03873  -0.08212 52  PHE A C   
398  O O   . PHE A 52  ? 0.63474 0.67364 0.59122 0.17365  0.03577  -0.07963 52  PHE A O   
399  C CB  . PHE A 52  ? 0.62831 0.61321 0.59459 0.11130  0.03957  -0.06734 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.71996 0.69297 0.68074 0.12294  0.03615  -0.05969 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.71507 0.64461 0.65866 0.13280  0.03711  -0.05310 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.64441 0.64717 0.61428 0.12298  0.03419  -0.06012 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.72572 0.63744 0.65781 0.14434  0.03787  -0.04363 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.69214 0.68426 0.65216 0.13696  0.03160  -0.05192 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.69346 0.63783 0.63281 0.14858  0.03429  -0.04192 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.60690 0.70193 0.59711 0.13251  0.04105  -0.09093 53  HIS A N   
407  C CA  . HIS A 53  ? 0.57738 0.72775 0.57797 0.14881  0.03707  -0.10135 53  HIS A CA  
408  C C   . HIS A 53  ? 0.69956 0.89238 0.70333 0.17021  0.03765  -0.11408 53  HIS A C   
409  O O   . HIS A 53  ? 0.71701 0.95405 0.72206 0.19753  0.03148  -0.12155 53  HIS A O   
410  C CB  . HIS A 53  ? 0.56658 0.75648 0.58889 0.12207  0.04132  -0.11255 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.61855 0.77716 0.63646 0.11012  0.03897  -0.10199 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.64117 0.80644 0.65334 0.12820  0.03043  -0.09791 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.62315 0.74452 0.63845 0.08560  0.04456  -0.09438 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.65049 0.78579 0.65986 0.11234  0.03115  -0.08920 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.72234 0.83151 0.73391 0.08748  0.03920  -0.08725 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.69576 0.88014 0.69893 0.16182  0.04467  -0.11725 54  GLN A N   
417  C CA  . GLN A 54  ? 0.66973 0.89106 0.67331 0.18523  0.04573  -0.12879 54  GLN A CA  
418  C C   . GLN A 54  ? 0.66590 0.85416 0.64212 0.22613  0.03859  -0.12043 54  GLN A C   
419  O O   . GLN A 54  ? 0.72029 0.94961 0.69356 0.25956  0.03554  -0.12919 54  GLN A O   
420  C CB  . GLN A 54  ? 0.77544 0.98479 0.77801 0.16877  0.05564  -0.13162 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.70449 0.98148 0.73030 0.15409  0.06689  -0.15004 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.89734 1.15287 0.91541 0.13646  0.07941  -0.14887 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.92675 1.14824 0.93942 0.10923  0.08718  -0.14065 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.75385 1.02831 0.76708 0.15591  0.08176  -0.15660 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.76736 0.88117 0.72138 0.22462  0.03772  -0.10454 55  TYR A N   
426  C CA  . TYR A 55  ? 0.79786 0.85879 0.71899 0.25674  0.03723  -0.09593 55  TYR A CA  
427  C C   . TYR A 55  ? 0.81958 0.83561 0.72400 0.26037  0.03583  -0.08042 55  TYR A C   
428  O O   . TYR A 55  ? 0.80828 0.75373 0.68685 0.26338  0.04099  -0.07037 55  TYR A O   
429  C CB  . TYR A 55  ? 0.78752 0.79568 0.69447 0.24812  0.04251  -0.09604 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.81617 0.86392 0.73410 0.24718  0.04550  -0.10994 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.78987 0.85118 0.69403 0.28202  0.04676  -0.11788 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.78530 0.85404 0.72286 0.21422  0.04896  -0.11423 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.80447 0.90531 0.71879 0.28121  0.05092  -0.13110 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.88214 0.98418 0.82586 0.21305  0.05486  -0.12556 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.89447 1.01544 0.82885 0.24515  0.05559  -0.13465 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.80946 0.96700 0.75023 0.24410  0.06277  -0.14649 55  TYR A OH  
437  N N   . GLU A 56  ? 0.69785 0.75518 0.61646 0.25817  0.03068  -0.08018 56  GLU A N   
438  C CA  . GLU A 56  ? 0.84906 0.86985 0.75190 0.26142  0.03017  -0.06533 56  GLU A CA  
439  C C   . GLU A 56  ? 0.82269 0.81310 0.68635 0.30738  0.03196  -0.05512 56  GLU A C   
440  O O   . GLU A 56  ? 0.95619 0.89782 0.79697 0.31165  0.03631  -0.03969 56  GLU A O   
441  C CB  . GLU A 56  ? 0.67675 0.75298 0.60434 0.24670  0.02417  -0.07051 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.72960 0.88916 0.66992 0.27002  0.01733  -0.08657 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.76723 0.98276 0.73564 0.24662  0.01335  -0.09799 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.63883 0.82688 0.61772 0.21091  0.01722  -0.09345 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.72110 1.00994 0.69996 0.26518  0.00656  -0.11341 56  GLU A OE2 
446  N N   . GLU A 57  ? 0.84757 0.86340 0.69933 0.34383  0.03054  -0.06258 57  GLU A N   
447  C CA  . GLU A 57  ? 0.94825 0.92998 0.75375 0.39600  0.03384  -0.05165 57  GLU A CA  
448  C C   . GLU A 57  ? 1.03358 0.92547 0.80202 0.40629  0.04689  -0.04431 57  GLU A C   
449  O O   . GLU A 57  ? 1.05574 0.89794 0.77587 0.45015  0.05452  -0.03297 57  GLU A O   
450  C CB  . GLU A 57  ? 0.96976 1.03941 0.78015 0.43836  0.02403  -0.06574 57  GLU A CB  
451  C CG  . GLU A 57  ? 0.90283 1.06010 0.74215 0.43456  0.01224  -0.07571 57  GLU A CG  
452  C CD  . GLU A 57  ? 0.94535 1.21342 0.80798 0.45988  0.00241  -0.09991 57  GLU A CD  
453  O OE1 . GLU A 57  ? 1.07684 1.37414 0.96082 0.44910  0.00483  -0.11441 57  GLU A OE1 
454  O OE2 . GLU A 57  ? 1.19755 1.52890 1.05748 0.49089  -0.00745 -0.10615 57  GLU A OE2 
455  N N   . ARG A 58  ? 0.95790 0.82606 0.74397 0.36862  0.05067  -0.05141 58  ARG A N   
456  C CA  . ARG A 58  ? 1.09952 0.88371 0.85512 0.36857  0.06339  -0.04974 58  ARG A CA  
457  C C   . ARG A 58  ? 1.01778 0.75560 0.78580 0.31865  0.06898  -0.04810 58  ARG A C   
458  O O   . ARG A 58  ? 1.15556 0.86147 0.92380 0.29886  0.07385  -0.05751 58  ARG A O   
459  C CB  . ARG A 58  ? 1.04528 0.85709 0.80764 0.37866  0.06147  -0.06594 58  ARG A CB  
460  C CG  . ARG A 58  ? 1.17798 1.02465 0.91933 0.43538  0.05893  -0.06895 58  ARG A CG  
461  C CD  . ARG A 58  ? 1.22616 1.11365 0.98124 0.44131  0.05707  -0.08692 58  ARG A CD  
462  N NE  . ARG A 58  ? 1.22450 1.04721 0.97108 0.41483  0.06561  -0.09159 58  ARG A NE  
463  C CZ  . ARG A 58  ? 1.34869 1.08269 1.05000 0.43316  0.07822  -0.08893 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 1.28410 0.97113 0.93790 0.48085  0.08606  -0.07752 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 1.14113 0.83022 0.84117 0.40404  0.08434  -0.09886 58  ARG A NH2 
466  N N   . LEU A 59  ? 1.00729 0.74713 0.78597 0.29946  0.06774  -0.03809 59  LEU A N   
467  C CA  . LEU A 59  ? 1.00886 0.72415 0.80576 0.25339  0.07082  -0.03879 59  LEU A CA  
468  C C   . LEU A 59  ? 1.04888 0.67574 0.81544 0.24381  0.08784  -0.03794 59  LEU A C   
469  O O   . LEU A 59  ? 1.12568 0.74038 0.90821 0.20866  0.08960  -0.04881 59  LEU A O   
470  C CB  . LEU A 59  ? 0.96706 0.70236 0.77753 0.24053  0.06737  -0.02815 59  LEU A CB  
471  C CG  . LEU A 59  ? 1.00678 0.82516 0.85342 0.23380  0.05287  -0.03393 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.74988 0.57698 0.60512 0.22064  0.05119  -0.02461 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.77816 0.62498 0.65430 0.20472  0.04808  -0.04688 59  LEU A CD2 
474  N N   . ASP A 60  ? 1.13495 0.69892 0.85510 0.27509  0.10198  -0.02654 60  ASP A N   
475  C CA  . ASP A 60  ? 1.29060 0.75913 0.97714 0.26185  0.12404  -0.02640 60  ASP A CA  
476  C C   . ASP A 60  ? 1.27147 0.70890 0.94599 0.26304  0.12907  -0.04348 60  ASP A C   
477  O O   . ASP A 60  ? 1.34319 0.70775 0.99810 0.24062  0.14714  -0.05116 60  ASP A O   
478  C CB  . ASP A 60  ? 1.26873 0.66656 0.89955 0.29700  0.14238  -0.00563 60  ASP A CB  
479  C CG  . ASP A 60  ? 1.46422 0.77968 1.07462 0.26459  0.16698  -0.00003 60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.44993 0.79157 1.08565 0.23725  0.16451  0.00528  60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.58918 0.81323 1.15782 0.26503  0.19067  -0.00249 60  ASP A OD2 
482  N N   . GLU A 61  ? 1.21297 0.70528 0.89919 0.28626  0.11511  -0.05193 61  GLU A N   
483  C CA  . GLU A 61  ? 1.20687 0.67531 0.88021 0.29201  0.11903  -0.06857 61  GLU A CA  
484  C C   . GLU A 61  ? 1.18097 0.71660 0.89920 0.26259  0.10370  -0.08645 61  GLU A C   
485  O O   . GLU A 61  ? 1.15777 0.69729 0.87078 0.27241  0.10263  -0.10055 61  GLU A O   
486  C CB  . GLU A 61  ? 1.22437 0.69550 0.86573 0.34973  0.11903  -0.06442 61  GLU A CB  
487  C CG  . GLU A 61  ? 1.49231 0.89452 1.07837 0.39041  0.13466  -0.04434 61  GLU A CG  
488  C CD  . GLU A 61  ? 1.52516 0.99783 1.11764 0.42666  0.12085  -0.03079 61  GLU A CD  
489  O OE1 . GLU A 61  ? 1.56017 1.10274 1.16268 0.46030  0.10771  -0.03785 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 1.54590 1.00930 1.13465 0.42059  0.12343  -0.01545 61  GLU A OE2 
491  N N   . ILE A 62  ? 1.23212 0.81709 0.98944 0.22969  0.09319  -0.08541 62  ILE A N   
492  C CA  . ILE A 62  ? 1.04846 0.69803 0.84186 0.20869  0.07961  -0.09751 62  ILE A CA  
493  C C   . ILE A 62  ? 0.99985 0.65056 0.81526 0.16667  0.07777  -0.10248 62  ILE A C   
494  O O   . ILE A 62  ? 0.91228 0.55195 0.73251 0.15355  0.08071  -0.09209 62  ILE A O   
495  C CB  . ILE A 62  ? 0.97473 0.70227 0.79313 0.22122  0.06735  -0.09087 62  ILE A CB  
496  C CG1 . ILE A 62  ? 0.90943 0.65600 0.71248 0.26255  0.06742  -0.09273 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.86027 0.64058 0.70982 0.19533  0.05842  -0.09898 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.93308 0.76258 0.76308 0.27169  0.05784  -0.09170 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.96460 0.63326 0.79189 0.14858  0.07272  -0.11925 63  ALA A N   
500  C CA  . ALA A 63  ? 0.91840 0.60970 0.76901 0.11535  0.06686  -0.12662 63  ALA A CA  
501  C C   . ALA A 63  ? 0.89297 0.64918 0.76433 0.11525  0.05394  -0.12590 63  ALA A C   
502  O O   . ALA A 63  ? 0.89099 0.66487 0.75709 0.12795  0.05171  -0.13308 63  ALA A O   
503  C CB  . ALA A 63  ? 0.86528 0.52458 0.70799 0.09497  0.07259  -0.14971 63  ALA A CB  
504  N N   . PHE A 64  ? 0.78796 0.57480 0.67894 0.10175  0.04797  -0.11688 64  PHE A N   
505  C CA  . PHE A 64  ? 0.75912 0.59470 0.66281 0.10211  0.04053  -0.11245 64  PHE A CA  
506  C C   . PHE A 64  ? 0.78889 0.64313 0.69657 0.08807  0.03434  -0.12319 64  PHE A C   
507  O O   . PHE A 64  ? 0.74807 0.59448 0.66096 0.07215  0.03291  -0.13171 64  PHE A O   
508  C CB  . PHE A 64  ? 0.71931 0.57343 0.63633 0.09968  0.03917  -0.09641 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.74398 0.60182 0.65883 0.11780  0.04222  -0.08801 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.73802 0.56285 0.64171 0.12761  0.04677  -0.08217 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.71328 0.61028 0.63553 0.12556  0.04192  -0.08712 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.78195 0.61823 0.68055 0.15071  0.04760  -0.07541 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.70968 0.62477 0.63352 0.14303  0.04302  -0.08414 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.67348 0.56099 0.58487 0.15855  0.04416  -0.07817 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.73033 0.61279 0.63403 0.09524  0.03179  -0.12362 65  ILE A N   
516  C CA  . ILE A 65  ? 0.70349 0.60906 0.60396 0.09074  0.02551  -0.13019 65  ILE A CA  
517  C C   . ILE A 65  ? 0.69771 0.62508 0.59484 0.09636  0.02785  -0.11511 65  ILE A C   
518  O O   . ILE A 65  ? 0.67498 0.60700 0.56962 0.10315  0.03515  -0.10899 65  ILE A O   
519  C CB  . ILE A 65  ? 0.73198 0.63921 0.61806 0.09639  0.02358  -0.14906 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.77203 0.64907 0.65833 0.08629  0.02487  -0.16748 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.76078 0.69920 0.63850 0.09860  0.01604  -0.15467 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.90096 0.74565 0.77426 0.09882  0.03298  -0.17071 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.64883 0.58927 0.54439 0.09362  0.02359  -0.11049 66  GLY A N   
524  C CA  . GLY A 66  ? 0.75039 0.69824 0.63397 0.09924  0.02969  -0.09594 66  GLY A CA  
525  C C   . GLY A 66  ? 0.79722 0.75785 0.65641 0.11151  0.02728  -0.09810 66  GLY A C   
526  O O   . GLY A 66  ? 0.80307 0.77908 0.66150 0.11425  0.01639  -0.10764 66  GLY A O   
527  N N   . ILE A 67  ? 0.80323 0.76102 0.64102 0.11978  0.03846  -0.09034 67  ILE A N   
528  C CA  . ILE A 67  ? 0.76054 0.72441 0.56496 0.13679  0.03979  -0.08782 67  ILE A CA  
529  C C   . ILE A 67  ? 0.74765 0.69099 0.53029 0.13956  0.05587  -0.06686 67  ILE A C   
530  O O   . ILE A 67  ? 0.79669 0.72715 0.58146 0.12874  0.07224  -0.05976 67  ILE A O   
531  C CB  . ILE A 67  ? 0.80582 0.77630 0.59453 0.14530  0.04354  -0.09711 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.85950 0.84046 0.66627 0.14122  0.03039  -0.11992 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.75974 0.73575 0.50731 0.16698  0.04572  -0.09256 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.69455 0.68099 0.48576 0.15083  0.03368  -0.13135 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.77827 0.71917 0.53881 0.15421  0.05265  -0.05888 68  HIS A N   
536  C CA  . HIS A 68  ? 0.84678 0.75567 0.57797 0.15946  0.07043  -0.03844 68  HIS A CA  
537  C C   . HIS A 68  ? 0.91253 0.80707 0.59269 0.18154  0.08336  -0.02915 68  HIS A C   
538  O O   . HIS A 68  ? 0.96949 0.88317 0.62628 0.20704  0.07108  -0.03322 68  HIS A O   
539  C CB  . HIS A 68  ? 0.89728 0.80553 0.62822 0.16769  0.06180  -0.03276 68  HIS A CB  
540  C CG  . HIS A 68  ? 0.81346 0.75154 0.52722 0.19445  0.04483  -0.03962 68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.88843 0.81424 0.55062 0.22636  0.05106  -0.02676 68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.78730 0.77011 0.52746 0.19445  0.02287  -0.06002 68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.92080 0.89209 0.58058 0.24805  0.03044  -0.04011 68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.93887 0.94707 0.64841 0.22578  0.01363  -0.06218 68  HIS A NE2 
545  N N   . THR A 69  ? 0.97360 0.83824 0.63609 0.17149  0.10911  -0.01843 69  THR A N   
546  C CA  . THR A 69  ? 1.16125 1.00031 0.76803 0.19077  0.12861  -0.00536 69  THR A CA  
547  C C   . THR A 69  ? 1.21258 1.00275 0.77183 0.20595  0.14611  0.01655  69  THR A C   
548  O O   . THR A 69  ? 1.22910 0.99392 0.73014 0.23353  0.15911  0.03031  69  THR A O   
549  C CB  . THR A 69  ? 1.08017 0.91002 0.68846 0.17020  0.15287  -0.00563 69  THR A CB  
550  O OG1 . THR A 69  ? 1.06764 0.88312 0.70364 0.13917  0.16759  -0.00452 69  THR A OG1 
551  C CG2 . THR A 69  ? 1.00034 0.87422 0.64078 0.16664  0.13694  -0.02579 69  THR A CG2 
552  N N   . GLY A 70  ? 1.24404 1.01680 0.82173 0.19142  0.14797  0.02051  70  GLY A N   
553  C CA  . GLY A 70  ? 1.26133 0.98656 0.79333 0.21041  0.16123  0.03935  70  GLY A CA  
554  C C   . GLY A 70  ? 1.16284 0.91788 0.70259 0.23510  0.13337  0.03576  70  GLY A C   
555  O O   . GLY A 70  ? 1.15121 0.95203 0.69194 0.25759  0.11057  0.02547  70  GLY A O   
556  N N   . HIS A 71  ? 1.25926 0.99366 0.80592 0.22996  0.13550  0.04129  71  HIS A N   
557  C CA  . HIS A 71  ? 1.23387 1.00270 0.79209 0.25154  0.11063  0.03642  71  HIS A CA  
558  C C   . HIS A 71  ? 1.12209 0.95181 0.74954 0.22773  0.08403  0.01385  71  HIS A C   
559  O O   . HIS A 71  ? 1.12248 0.95861 0.78607 0.19676  0.08591  0.00496  71  HIS A O   
560  C CB  . HIS A 71  ? 1.21919 0.94304 0.75887 0.25542  0.12359  0.04978  71  HIS A CB  
561  C CG  . HIS A 71  ? 1.28355 0.98860 0.86160 0.21289  0.13462  0.04561  71  HIS A CG  
562  N ND1 . HIS A 71  ? 1.22268 0.96977 0.85894 0.19255  0.11459  0.03141  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 1.27920 0.93184 0.84476 0.18704  0.16419  0.05173  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 1.17204 0.89708 0.82873 0.16043  0.12861  0.02954  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.33143 1.00309 0.94922 0.15442  0.15822  0.03952  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.95110 0.82510 0.59383 0.24400  0.06111  0.00431  72  LEU A N   
567  C CA  . LEU A 72  ? 0.97899 0.90403 0.68070 0.22177  0.03969  -0.01685 72  LEU A CA  
568  C C   . LEU A 72  ? 0.94766 0.85449 0.68479 0.19091  0.04549  -0.01491 72  LEU A C   
569  O O   . LEU A 72  ? 0.97750 0.85771 0.70321 0.19442  0.05412  -0.00340 72  LEU A O   
570  C CB  . LEU A 72  ? 0.89191 0.86961 0.60057 0.24349  0.01870  -0.02852 72  LEU A CB  
571  C CG  . LEU A 72  ? 0.92948 0.95483 0.69619 0.21771  0.00144  -0.05054 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.85854 0.90080 0.65020 0.19622  -0.00454 -0.06874 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.89381 0.97783 0.66610 0.23873  -0.01589 -0.06397 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.83124 0.75225 0.60762 0.16412  0.04064  -0.02679 73  GLY A N   
575  C CA  . GLY A 73  ? 0.80706 0.72016 0.61693 0.13899  0.04298  -0.02711 73  GLY A CA  
576  C C   . GLY A 73  ? 0.79089 0.73911 0.63836 0.12939  0.02619  -0.04085 73  GLY A C   
577  O O   . GLY A 73  ? 0.83068 0.81189 0.68459 0.13538  0.01349  -0.05446 73  GLY A O   
578  N N   . PHE A 74  ? 0.57298 0.51382 0.44414 0.11278  0.02812  -0.03862 74  PHE A N   
579  C CA  . PHE A 74  ? 0.72755 0.69251 0.63060 0.10087  0.01763  -0.04944 74  PHE A CA  
580  C C   . PHE A 74  ? 0.68632 0.64972 0.60785 0.08540  0.01648  -0.05919 74  PHE A C   
581  O O   . PHE A 74  ? 0.68326 0.66193 0.62290 0.07610  0.01013  -0.07184 74  PHE A O   
582  C CB  . PHE A 74  ? 0.60705 0.56385 0.52179 0.09395  0.02089  -0.04172 74  PHE A CB  
583  C CG  . PHE A 74  ? 0.54360 0.51416 0.44896 0.10961  0.01757  -0.03851 74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.57040 0.51629 0.44323 0.12717  0.02602  -0.02591 74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.57453 0.58175 0.50143 0.10724  0.00823  -0.04909 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.64129 0.59746 0.50031 0.14788  0.02336  -0.02231 74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.54066 0.56952 0.46010 0.12531  0.00453  -0.04778 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.66055 0.66349 0.54452 0.14871  0.01109  -0.03363 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.62748 0.57222 0.54340 0.08250  0.02441  -0.05487 75  TYR A N   
590  C CA  . TYR A 75  ? 0.64654 0.58855 0.57217 0.07587  0.02389  -0.06375 75  TYR A CA  
591  C C   . TYR A 75  ? 0.74144 0.68880 0.65099 0.08451  0.02327  -0.07105 75  TYR A C   
592  O O   . TYR A 75  ? 0.77490 0.72557 0.68989 0.08181  0.01886  -0.08431 75  TYR A O   
593  C CB  . TYR A 75  ? 0.66327 0.59350 0.59544 0.07076  0.03165  -0.05760 75  TYR A CB  
594  C CG  . TYR A 75  ? 0.71917 0.64608 0.66359 0.06470  0.03218  -0.05086 75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.67181 0.59678 0.62866 0.05964  0.02790  -0.05328 75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.67174 0.59563 0.61326 0.06244  0.03920  -0.04346 75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.60314 0.52552 0.56780 0.05609  0.02928  -0.04627 75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.63800 0.56148 0.58910 0.05819  0.03897  -0.03920 75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.69101 0.61492 0.65297 0.05686  0.03332  -0.03951 75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.59770 0.52158 0.56589 0.05457  0.03399  -0.03439 75  TYR A OH  
601  N N   . ALA A 76  ? 0.71207 0.65565 0.59780 0.09519  0.02975  -0.06272 76  ALA A N   
602  C CA  . ALA A 76  ? 0.83871 0.78782 0.70254 0.10706  0.03038  -0.06753 76  ALA A CA  
603  C C   . ALA A 76  ? 0.80925 0.77860 0.65825 0.12269  0.02026  -0.07188 76  ALA A C   
604  O O   . ALA A 76  ? 0.82270 0.78550 0.64253 0.13974  0.02518  -0.06032 76  ALA A O   
605  C CB  . ALA A 76  ? 0.79958 0.73012 0.64100 0.10986  0.04731  -0.05544 76  ALA A CB  
606  N N   . ASP A 77  ? 0.75374 0.74852 0.62103 0.11761  0.00720  -0.09037 77  ASP A N   
607  C CA  . ASP A 77  ? 0.83814 0.86943 0.70027 0.13041  -0.00515 -0.10140 77  ASP A CA  
608  C C   . ASP A 77  ? 0.75765 0.81445 0.60833 0.13933  -0.01330 -0.12056 77  ASP A C   
609  O O   . ASP A 77  ? 0.86554 0.96521 0.72333 0.14296  -0.02628 -0.14025 77  ASP A O   
610  C CB  . ASP A 77  ? 0.76258 0.81426 0.65776 0.11358  -0.01239 -0.11296 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.81873 0.85486 0.73900 0.08815  -0.00975 -0.12510 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.80298 0.81849 0.71571 0.08709  -0.00525 -0.12688 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.81581 0.85746 0.75995 0.07086  -0.01020 -0.13216 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.74042 0.77764 0.57462 0.14267  -0.00585 -0.11778 78  TRP A N   
615  C CA  . TRP A 78  ? 0.85712 0.91601 0.67499 0.15390  -0.01232 -0.13503 78  TRP A CA  
616  C C   . TRP A 78  ? 0.83664 0.88660 0.60989 0.18088  -0.00406 -0.11809 78  TRP A C   
617  O O   . TRP A 78  ? 0.88005 0.89400 0.64054 0.17952  0.01272  -0.09719 78  TRP A O   
618  C CB  . TRP A 78  ? 0.91970 0.96177 0.75120 0.13766  -0.00882 -0.14795 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.92241 0.96683 0.78610 0.11399  -0.01438 -0.16814 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.89848 0.91704 0.78537 0.09560  -0.00846 -0.16113 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.95439 1.02553 0.82715 0.10487  -0.02410 -0.19985 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.86799 0.88765 0.77441 0.07548  -0.01112 -0.18375 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 1.03916 1.09129 0.93956 0.07789  -0.02020 -0.20964 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.98426 1.09419 0.84262 0.11649  -0.03465 -0.22262 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 1.01303 1.07849 0.92813 0.05734  -0.02347 -0.24237 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.96456 1.09687 0.84117 0.09689  -0.04135 -0.25787 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 1.06794 1.17560 0.97324 0.06520  -0.03433 -0.26802 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.86806 0.95217 0.61581 0.20520  -0.01435 -0.12849 79  ARG A N   
629  C CA  . ARG A 79  ? 0.91857 0.98696 0.61482 0.23458  -0.00349 -0.10961 79  ARG A CA  
630  C C   . ARG A 79  ? 1.00679 1.06472 0.68914 0.23370  0.00464  -0.11422 79  ARG A C   
631  O O   . ARG A 79  ? 0.96372 1.04038 0.66937 0.22021  -0.00478 -0.13852 79  ARG A O   
632  C CB  . ARG A 79  ? 0.92562 1.03635 0.59134 0.26990  -0.01747 -0.11598 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.99275 1.12188 0.66973 0.27657  -0.02581 -0.11266 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.98494 1.15923 0.62398 0.32089  -0.03862 -0.11654 79  ARG A CD  
635  N NE  . ARG A 79  ? 1.00331 1.23638 0.64395 0.32867  -0.05623 -0.14790 79  ARG A NE  
636  C CZ  . ARG A 79  ? 1.02453 1.31693 0.71107 0.30764  -0.07495 -0.18414 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 1.04202 1.34193 0.77617 0.27789  -0.07770 -0.19174 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 0.97118 1.31552 0.65437 0.31490  -0.08929 -0.21493 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.94837 0.97308 0.59107 0.24695  0.02479  -0.09176 80  PRO A N   
640  C CA  . PRO A 80  ? 1.04004 1.05844 0.66942 0.24648  0.03488  -0.09575 80  PRO A CA  
641  C C   . PRO A 80  ? 1.14060 1.19914 0.75338 0.26593  0.01899  -0.11895 80  PRO A C   
642  O O   . PRO A 80  ? 1.05745 1.11964 0.67448 0.25977  0.02080  -0.13245 80  PRO A O   
643  C CB  . PRO A 80  ? 0.94943 0.92609 0.53248 0.25852  0.06231  -0.06648 80  PRO A CB  
644  C CG  . PRO A 80  ? 0.99017 0.93895 0.57936 0.25050  0.06949  -0.04869 80  PRO A CG  
645  C CD  . PRO A 80  ? 0.95460 0.93931 0.56459 0.25786  0.04355  -0.06225 80  PRO A CD  
646  N N   . ALA A 81  ? 1.07423 1.16774 0.66781 0.29108  0.00294  -0.12627 81  ALA A N   
647  C CA  . ALA A 81  ? 1.13948 1.28114 0.71749 0.31022  -0.01396 -0.15297 81  ALA A CA  
648  C C   . ALA A 81  ? 1.08636 1.25575 0.71393 0.28090  -0.02989 -0.18955 81  ALA A C   
649  O O   . ALA A 81  ? 1.18304 1.37912 0.80296 0.28617  -0.03833 -0.21495 81  ALA A O   
650  C CB  . ALA A 81  ? 1.17393 1.35770 0.72226 0.34650  -0.02908 -0.15506 81  ALA A CB  
651  N N   . GLU A 82  ? 1.09737 1.25597 0.77148 0.25028  -0.03196 -0.19291 82  GLU A N   
652  C CA  . GLU A 82  ? 1.06323 1.23362 0.77932 0.22036  -0.04158 -0.22489 82  GLU A CA  
653  C C   . GLU A 82  ? 1.03134 1.15743 0.75966 0.20154  -0.02806 -0.22293 82  GLU A C   
654  O O   . GLU A 82  ? 0.95921 1.07530 0.71787 0.17668  -0.03045 -0.24295 82  GLU A O   
655  C CB  . GLU A 82  ? 1.10844 1.28697 0.86349 0.19867  -0.04789 -0.22867 82  GLU A CB  
656  C CG  . GLU A 82  ? 1.12299 1.35209 0.90457 0.18337  -0.06464 -0.26926 82  GLU A CG  
657  C CD  . GLU A 82  ? 1.11663 1.39950 0.90327 0.19604  -0.07783 -0.27300 82  GLU A CD  
658  O OE1 . GLU A 82  ? 1.09228 1.36585 0.85436 0.22182  -0.07395 -0.24210 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 1.13308 1.46778 0.94749 0.17999  -0.09055 -0.30840 82  GLU A OE2 
660  N N   . ALA A 83  ? 1.03222 1.13174 0.73523 0.21393  -0.01213 -0.20007 83  ALA A N   
661  C CA  . ALA A 83  ? 1.09269 1.15946 0.80902 0.20013  0.00066  -0.19753 83  ALA A CA  
662  C C   . ALA A 83  ? 1.05207 1.12581 0.76736 0.19899  -0.00496 -0.22802 83  ALA A C   
663  O O   . ALA A 83  ? 1.06946 1.11815 0.80599 0.18320  -0.00146 -0.23781 83  ALA A O   
664  C CB  . ALA A 83  ? 1.09956 1.14732 0.79106 0.21141  0.02071  -0.17005 83  ALA A CB  
665  N N   . ASP A 84  ? 1.02081 1.12589 0.70716 0.21835  -0.01289 -0.24358 84  ASP A N   
666  C CA  . ASP A 84  ? 1.06599 1.17764 0.74861 0.21722  -0.01796 -0.27596 84  ASP A CA  
667  C C   . ASP A 84  ? 1.04073 1.15947 0.75347 0.19240  -0.03059 -0.30952 84  ASP A C   
668  O O   . ASP A 84  ? 1.03633 1.12994 0.75791 0.17847  -0.02735 -0.33146 84  ASP A O   
669  C CB  . ASP A 84  ? 1.07029 1.21782 0.71124 0.24608  -0.02329 -0.28492 84  ASP A CB  
670  C CG  . ASP A 84  ? 1.07142 1.20283 0.67855 0.26667  -0.00450 -0.25538 84  ASP A CG  
671  O OD1 . ASP A 84  ? 1.16555 1.26406 0.78687 0.25548  0.01173  -0.23771 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 1.15014 1.30423 0.71519 0.29440  -0.00479 -0.25099 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.93283 1.08392 0.65968 0.18641  -0.04270 -0.31503 85  LYS A N   
674  C CA  . LYS A 85  ? 0.91333 1.06856 0.67432 0.15534  -0.04936 -0.34478 85  LYS A CA  
675  C C   . LYS A 85  ? 1.13825 1.23585 0.92500 0.13150  -0.03583 -0.32969 85  LYS A C   
676  O O   . LYS A 85  ? 1.15949 1.23600 0.96601 0.10448  -0.03319 -0.35347 85  LYS A O   
677  C CB  . LYS A 85  ? 0.87597 1.08776 0.64905 0.15582  -0.06426 -0.35291 85  LYS A CB  
678  N N   . LEU A 86  ? 1.09561 1.16642 0.87953 0.14107  -0.02558 -0.29197 86  LEU A N   
679  C CA  . LEU A 86  ? 1.02732 1.05093 0.83244 0.12430  -0.01435 -0.27682 86  LEU A CA  
680  C C   . LEU A 86  ? 1.03081 1.01213 0.82875 0.12418  -0.00398 -0.28544 86  LEU A C   
681  O O   . LEU A 86  ? 1.02880 0.97040 0.83881 0.10698  0.00251  -0.29409 86  LEU A O   
682  C CB  . LEU A 86  ? 1.04739 1.06484 0.85227 0.13431  -0.00754 -0.23894 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.95448 0.95024 0.78505 0.11780  -0.00358 -0.22304 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.95790 0.96746 0.80881 0.09738  -0.01182 -0.24317 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.97315 0.97708 0.79951 0.12784  -0.00024 -0.19295 86  LEU A CD2 
686  N N   . VAL A 87  ? 1.07764 1.06419 0.85208 0.14555  -0.00030 -0.28234 87  VAL A N   
687  C CA  . VAL A 87  ? 1.06059 1.01096 0.82619 0.15193  0.01006  -0.28832 87  VAL A CA  
688  C C   . VAL A 87  ? 1.07373 1.00097 0.83580 0.13854  0.00863  -0.32513 87  VAL A C   
689  O O   . VAL A 87  ? 1.12867 1.00481 0.88898 0.13480  0.01908  -0.33027 87  VAL A O   
690  C CB  . VAL A 87  ? 1.14027 1.10968 0.88214 0.17695  0.01538  -0.27945 87  VAL A CB  
691  C CG1 . VAL A 87  ? 1.10055 1.08021 0.84698 0.18353  0.02380  -0.24490 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 1.17736 1.18555 0.89672 0.18738  0.00579  -0.29611 87  VAL A CG2 
693  N N   . LYS A 88  ? 1.14467 1.10822 0.90290 0.13208  -0.00311 -0.35277 88  LYS A N   
694  C CA  . LYS A 88  ? 1.28135 1.22650 1.03763 0.11342  -0.00304 -0.39402 88  LYS A CA  
695  C C   . LYS A 88  ? 1.13723 1.03823 0.91500 0.08232  0.00553  -0.39986 88  LYS A C   
696  O O   . LYS A 88  ? 1.17767 1.01689 0.94642 0.07254  0.01928  -0.41362 88  LYS A O   
697  C CB  . LYS A 88  ? 1.12006 1.12900 0.87336 0.11104  -0.01950 -0.42506 88  LYS A CB  
698  N N   . LEU A 89  ? 1.21214 1.14019 1.01430 0.06815  -0.00032 -0.38869 89  LEU A N   
699  C CA  . LEU A 89  ? 1.07935 0.96912 0.90141 0.03742  0.00975  -0.39278 89  LEU A CA  
700  C C   . LEU A 89  ? 1.25145 1.07622 1.06782 0.04611  0.02511  -0.36068 89  LEU A C   
701  O O   . LEU A 89  ? 1.30584 1.07065 1.12099 0.02753  0.04032  -0.36676 89  LEU A O   
702  C CB  . LEU A 89  ? 1.10787 1.05212 0.95723 0.02380  -0.00107 -0.38941 89  LEU A CB  
703  N N   . LEU A 90  ? 1.22327 1.05903 1.03360 0.07447  0.02304  -0.32803 90  LEU A N   
704  C CA  . LEU A 90  ? 1.24577 1.03202 1.04888 0.08846  0.03565  -0.30292 90  LEU A CA  
705  C C   . LEU A 90  ? 1.37730 1.10884 1.15374 0.09929  0.04755  -0.31868 90  LEU A C   
706  O O   . LEU A 90  ? 1.40203 1.07409 1.16728 0.10456  0.06128  -0.30905 90  LEU A O   
707  C CB  . LEU A 90  ? 1.17874 0.99939 0.98341 0.11321  0.03177  -0.27234 90  LEU A CB  
708  C CG  . LEU A 90  ? 1.15702 0.98419 0.97964 0.11247  0.03247  -0.24168 90  LEU A CG  
709  C CD1 . LEU A 90  ? 1.19007 0.98029 1.02364 0.09155  0.03804  -0.24172 90  LEU A CD1 
710  C CD2 . LEU A 90  ? 1.08541 0.96579 0.91770 0.11249  0.02265  -0.22955 90  LEU A CD2 
711  N N   . ALA A 91  ? 1.35305 1.10200 1.11454 0.10640  0.04305  -0.34260 91  ALA A N   
712  C CA  . ALA A 91  ? 1.48841 1.18590 1.22106 0.12069  0.05450  -0.35855 91  ALA A CA  
713  C C   . ALA A 91  ? 1.55613 1.18759 1.27902 0.09323  0.06774  -0.38708 91  ALA A C   
714  O O   . ALA A 91  ? 1.61051 1.16623 1.31039 0.10173  0.08527  -0.38315 91  ALA A O   
715  C CB  . ALA A 91  ? 1.52352 1.26187 1.24145 0.13717  0.04628  -0.37601 91  ALA A CB  
716  N N   . LYS A 92  ? 1.57872 1.23810 1.31669 0.06060  0.06127  -0.41721 92  LYS A N   
717  C CA  . LYS A 92  ? 1.61360 1.21448 1.34629 0.02517  0.07709  -0.44936 92  LYS A CA  
718  C C   . LYS A 92  ? 1.66768 1.20465 1.40157 0.01305  0.09493  -0.42669 92  LYS A C   
719  O O   . LYS A 92  ? 1.81942 1.26822 1.52849 0.00062  0.11832  -0.43850 92  LYS A O   
720  C CB  . LYS A 92  ? 1.52856 1.19380 1.28731 -0.00973 0.06475  -0.48562 92  LYS A CB  
721  C CG  . LYS A 92  ? 1.61579 1.23432 1.38173 -0.05756 0.08307  -0.51719 92  LYS A CG  
722  C CD  . LYS A 92  ? 1.64768 1.35212 1.45124 -0.09091 0.06857  -0.54647 92  LYS A CD  
723  C CE  . LYS A 92  ? 1.68593 1.34803 1.50328 -0.14282 0.09056  -0.57185 92  LYS A CE  
724  N NZ  . LYS A 92  ? 1.61043 1.37151 1.46962 -0.17308 0.07478  -0.59790 92  LYS A NZ  
725  N N   . GLY A 93  ? 1.57151 1.14626 1.32901 0.01812  0.08621  -0.39361 93  GLY A N   
726  C CA  . GLY A 93  ? 1.62886 1.15337 1.38870 0.00591  0.10143  -0.37293 93  GLY A CA  
727  C C   . GLY A 93  ? 1.59463 1.12905 1.37858 -0.04209 0.10652  -0.39767 93  GLY A C   
728  O O   . GLY A 93  ? 1.43335 1.04934 1.24640 -0.05692 0.08838  -0.41495 93  GLY A O   
729  N N   . GLU A 94  ? 1.71134 1.16486 1.48132 -0.06514 0.13254  -0.39999 94  GLU A N   
730  C CA  . GLU A 94  ? 1.76265 1.21739 1.55499 -0.11613 0.14432  -0.42496 94  GLU A CA  
731  C C   . GLU A 94  ? 1.70211 1.24164 1.53674 -0.12463 0.12683  -0.40996 94  GLU A C   
732  O O   . GLU A 94  ? 1.74437 1.31292 1.60617 -0.16556 0.13150  -0.43402 94  GLU A O   
733  C CB  . GLU A 94  ? 1.69930 1.17539 1.49874 -0.15024 0.14460  -0.48005 94  GLU A CB  
734  N N   . TYR A 95  ? 1.55187 1.13279 1.39252 -0.08786 0.10831  -0.37305 95  TYR A N   
735  C CA  . TYR A 95  ? 1.44873 1.09970 1.32289 -0.09102 0.09344  -0.35613 95  TYR A CA  
736  C C   . TYR A 95  ? 1.46666 1.06940 1.34115 -0.10393 0.11207  -0.33361 95  TYR A C   
737  O O   . TYR A 95  ? 1.52677 1.04113 1.36985 -0.09905 0.13445  -0.32158 95  TYR A O   
738  C CB  . TYR A 95  ? 1.34980 1.05051 1.22538 -0.05024 0.07191  -0.32596 95  TYR A CB  
739  C CG  . TYR A 95  ? 1.33739 0.98545 1.18594 -0.01613 0.07899  -0.29515 95  TYR A CG  
740  C CD1 . TYR A 95  ? 1.26341 0.88749 1.11112 -0.00601 0.08544  -0.26261 95  TYR A CD1 
741  C CD2 . TYR A 95  ? 1.42124 1.05123 1.24540 0.00800  0.07854  -0.30072 95  TYR A CD2 
742  C CE1 . TYR A 95  ? 1.23541 0.82454 1.06005 0.02779  0.09004  -0.23820 95  TYR A CE1 
743  C CE2 . TYR A 95  ? 1.43189 1.02612 1.23393 0.04165  0.08420  -0.27561 95  TYR A CE2 
744  C CZ  . TYR A 95  ? 1.31065 0.88754 1.11374 0.05174  0.08929  -0.24524 95  TYR A CZ  
745  O OH  . TYR A 95  ? 1.39793 0.95172 1.18055 0.08775  0.09314  -0.22378 95  TYR A OH  
746  N N   . GLN A 96  ? 1.34882 1.00969 1.25509 -0.11698 0.10336  -0.32742 96  GLN A N   
747  C CA  . GLN A 96  ? 1.27823 0.90626 1.18683 -0.12667 0.11857  -0.30414 96  GLN A CA  
748  C C   . GLN A 96  ? 1.20616 0.85140 1.11324 -0.08922 0.10540  -0.26231 96  GLN A C   
749  O O   . GLN A 96  ? 1.11905 0.81903 1.03378 -0.06481 0.08375  -0.25427 96  GLN A O   
750  C CB  . GLN A 96  ? 1.26220 0.94460 1.20744 -0.16543 0.11965  -0.32506 96  GLN A CB  
751  C CG  . GLN A 96  ? 1.35644 0.98707 1.29908 -0.21291 0.14926  -0.35611 96  GLN A CG  
752  C CD  . GLN A 96  ? 1.43680 1.11709 1.41593 -0.25016 0.15553  -0.36933 96  GLN A CD  
753  O OE1 . GLN A 96  ? 1.32508 1.09555 1.33537 -0.24067 0.13244  -0.36563 96  GLN A OE1 
754  N NE2 . GLN A 96  ? 1.52972 1.14847 1.50231 -0.29201 0.18930  -0.38468 96  GLN A NE2 
755  N N   . LYS A 97  ? 1.10197 0.69761 0.99636 -0.08583 0.12086  -0.23680 97  LYS A N   
756  C CA  . LYS A 97  ? 1.04537 0.65671 0.93920 -0.05492 0.11083  -0.20093 97  LYS A CA  
757  C C   . LYS A 97  ? 1.04024 0.67841 0.95651 -0.07207 0.11267  -0.19109 97  LYS A C   
758  O O   . LYS A 97  ? 1.07245 0.67706 0.98830 -0.10128 0.13305  -0.19965 97  LYS A O   
759  C CB  . LYS A 97  ? 1.08843 0.62654 0.94383 -0.02630 0.12471  -0.17781 97  LYS A CB  
760  C CG  . LYS A 97  ? 1.11756 0.61505 0.94464 -0.00885 0.12874  -0.18890 97  LYS A CG  
761  C CD  . LYS A 97  ? 1.13841 0.58147 0.92840 0.03049  0.13783  -0.16314 97  LYS A CD  
762  C CE  . LYS A 97  ? 1.20011 0.59134 0.95602 0.04935  0.14640  -0.17509 97  LYS A CE  
763  N NZ  . LYS A 97  ? 1.24711 0.55204 0.97560 0.02313  0.17407  -0.19380 97  LYS A NZ  
764  N N   . VAL A 98  ? 0.91543 0.61139 0.84945 -0.05503 0.09386  -0.17407 98  VAL A N   
765  C CA  . VAL A 98  ? 0.88580 0.60443 0.83642 -0.06290 0.09480  -0.16024 98  VAL A CA  
766  C C   . VAL A 98  ? 0.88632 0.58944 0.82219 -0.03253 0.09237  -0.12808 98  VAL A C   
767  O O   . VAL A 98  ? 0.89303 0.60171 0.81923 -0.00627 0.08222  -0.11928 98  VAL A O   
768  C CB  . VAL A 98  ? 0.91276 0.71345 0.89521 -0.06939 0.07634  -0.17074 98  VAL A CB  
769  C CG1 . VAL A 98  ? 0.97769 0.80900 0.97430 -0.09269 0.07394  -0.20666 98  VAL A CG1 
770  C CG2 . VAL A 98  ? 0.86544 0.70146 0.84645 -0.03856 0.05692  -0.15474 98  VAL A CG2 
771  N N   . SER A 99  ? 0.89448 0.58258 0.82918 -0.03711 0.10261  -0.11278 99  SER A N   
772  C CA  . SER A 99  ? 0.86922 0.54277 0.78780 -0.00933 0.10190  -0.08557 99  SER A CA  
773  C C   . SER A 99  ? 0.72856 0.44721 0.66762 -0.01121 0.09385  -0.07468 99  SER A C   
774  O O   . SER A 99  ? 0.74788 0.48001 0.70265 -0.03481 0.10036  -0.08158 99  SER A O   
775  C CB  . SER A 99  ? 0.93021 0.52733 0.81333 -0.00369 0.12519  -0.07369 99  SER A CB  
776  O OG  . SER A 99  ? 0.96292 0.51008 0.82105 0.00239  0.13423  -0.08313 99  SER A OG  
777  N N   . TYR A 100 ? 0.73179 0.47563 0.67099 0.01273  0.08090  -0.06008 100 TYR A N   
778  C CA  . TYR A 100 ? 0.72899 0.50804 0.68176 0.01499  0.07404  -0.04931 100 TYR A CA  
779  C C   . TYR A 100 ? 0.81350 0.57228 0.74737 0.03544  0.07860  -0.03009 100 TYR A C   
780  O O   . TYR A 100 ? 0.80795 0.54839 0.72327 0.05683  0.07848  -0.02501 100 TYR A O   
781  C CB  . TYR A 100 ? 0.63884 0.46569 0.60625 0.02286  0.05686  -0.05173 100 TYR A CB  
782  C CG  . TYR A 100 ? 0.70062 0.56061 0.68481 0.00911  0.04992  -0.06762 100 TYR A CG  
783  C CD1 . TYR A 100 ? 0.71959 0.57729 0.71217 -0.01260 0.05686  -0.08395 100 TYR A CD1 
784  C CD2 . TYR A 100 ? 0.58326 0.47781 0.57234 0.01863  0.03790  -0.06755 100 TYR A CD2 
785  C CE1 . TYR A 100 ? 0.62602 0.52707 0.63483 -0.02161 0.04814  -0.10191 100 TYR A CE1 
786  C CE2 . TYR A 100 ? 0.62914 0.55674 0.62729 0.01391  0.03064  -0.08091 100 TYR A CE2 
787  C CZ  . TYR A 100 ? 0.73206 0.66895 0.74181 -0.00477 0.03385  -0.09905 100 TYR A CZ  
788  O OH  . TYR A 100 ? 0.71627 0.69857 0.73595 -0.00608 0.02433  -0.11565 100 TYR A OH  
789  N N   . PRO A 101 ? 0.69009 0.45685 0.62714 0.03229  0.08208  -0.02049 101 PRO A N   
790  C CA  . PRO A 101 ? 0.78122 0.53488 0.69803 0.05442  0.08513  -0.00367 101 PRO A CA  
791  C C   . PRO A 101 ? 0.74280 0.53549 0.66592 0.07338  0.06916  -0.00243 101 PRO A C   
792  O O   . PRO A 101 ? 0.66963 0.49679 0.61262 0.06622  0.05832  -0.01063 101 PRO A O   
793  C CB  . PRO A 101 ? 0.70942 0.46966 0.63183 0.04245  0.09229  0.00281  101 PRO A CB  
794  C CG  . PRO A 101 ? 0.67614 0.44245 0.61849 0.01236  0.09822  -0.01138 101 PRO A CG  
795  C CD  . PRO A 101 ? 0.71068 0.50081 0.66800 0.01006  0.08451  -0.02609 101 PRO A CD  
796  N N   . LEU A 102 ? 0.75794 0.54481 0.66119 0.09835  0.06961  0.00700  102 LEU A N   
797  C CA  . LEU A 102 ? 0.73767 0.56757 0.64796 0.11425  0.05679  0.00425  102 LEU A CA  
798  C C   . LEU A 102 ? 0.66893 0.51278 0.57030 0.12726  0.05623  0.01291  102 LEU A C   
799  O O   . LEU A 102 ? 0.69180 0.50513 0.57430 0.13059  0.06703  0.02463  102 LEU A O   
800  C CB  . LEU A 102 ? 0.68296 0.51184 0.58038 0.13710  0.05448  0.00101  102 LEU A CB  
801  C CG  . LEU A 102 ? 0.78895 0.59926 0.68888 0.12873  0.05627  -0.00782 102 LEU A CG  
802  C CD1 . LEU A 102 ? 0.73330 0.53420 0.61267 0.15761  0.05709  -0.00849 102 LEU A CD1 
803  C CD2 . LEU A 102 ? 0.60283 0.45053 0.52988 0.11059  0.04718  -0.01915 102 LEU A CD2 
804  N N   . LEU A 103 ? 0.60179 0.54897 0.62333 0.09440  0.03281  0.00087  103 LEU A N   
805  C CA  . LEU A 103 ? 0.62319 0.58134 0.64729 0.09544  0.02849  0.00743  103 LEU A CA  
806  C C   . LEU A 103 ? 0.68977 0.66604 0.71213 0.11861  0.02403  0.00939  103 LEU A C   
807  O O   . LEU A 103 ? 0.70670 0.71666 0.74425 0.12518  0.02265  0.00476  103 LEU A O   
808  C CB  . LEU A 103 ? 0.61709 0.60603 0.66229 0.07967  0.02466  0.00667  103 LEU A CB  
809  C CG  . LEU A 103 ? 0.55154 0.55928 0.60237 0.08090  0.01881  0.01096  103 LEU A CG  
810  C CD1 . LEU A 103 ? 0.49303 0.47488 0.52901 0.07705  0.02005  0.01557  103 LEU A CD1 
811  C CD2 . LEU A 103 ? 0.50582 0.54190 0.57477 0.06726  0.01553  0.00848  103 LEU A CD2 
812  N N   . LYS A 104 ? 0.71009 0.66629 0.71260 0.13178  0.02211  0.01535  104 LYS A N   
813  C CA  . LYS A 104 ? 0.66148 0.63960 0.66084 0.15789  0.01517  0.01578  104 LYS A CA  
814  C C   . LYS A 104 ? 0.62951 0.64495 0.64602 0.15279  0.00764  0.01653  104 LYS A C   
815  O O   . LYS A 104 ? 0.57022 0.56857 0.57935 0.14129  0.00792  0.02170  104 LYS A O   
816  C CB  . LYS A 104 ? 0.66663 0.59549 0.62540 0.18159  0.01628  0.02177  104 LYS A CB  
817  C CG  . LYS A 104 ? 0.70195 0.65707 0.65461 0.21443  0.00639  0.02104  104 LYS A CG  
818  C CD  . LYS A 104 ? 0.67633 0.57703 0.58147 0.24567  0.00723  0.02599  104 LYS A CD  
819  C CE  . LYS A 104 ? 0.68873 0.52860 0.55499 0.24078  0.01256  0.03778  104 LYS A CE  
820  N NZ  . LYS A 104 ? 1.04958 0.82909 0.86039 0.27423  0.01338  0.04406  104 LYS A NZ  
821  N N   . THR A 105 ? 0.62960 0.69798 0.66915 0.16022  0.00160  0.00973  105 THR A N   
822  C CA  . THR A 105 ? 0.66093 0.76936 0.71777 0.15564  -0.00636 0.00701  105 THR A CA  
823  C C   . THR A 105 ? 0.69387 0.83125 0.74641 0.18660  -0.01556 0.00276  105 THR A C   
824  O O   . THR A 105 ? 0.71194 0.87505 0.77142 0.20368  -0.01602 -0.00415 105 THR A O   
825  C CB  . THR A 105 ? 0.60143 0.75192 0.69072 0.13209  -0.00474 -0.00037 105 THR A CB  
826  O OG1 . THR A 105 ? 0.56036 0.68198 0.64833 0.10924  0.00216  0.00323  105 THR A OG1 
827  C CG2 . THR A 105 ? 0.61235 0.79943 0.71738 0.12402  -0.01255 -0.00505 105 THR A CG2 
828  N N   . THR A 106 ? 0.71729 0.85296 0.75708 0.19625  -0.02336 0.00577  106 THR A N   
829  C CA  . THR A 106 ? 0.73879 0.90660 0.77281 0.22860  -0.03496 0.00028  106 THR A CA  
830  C C   . THR A 106 ? 0.67062 0.89391 0.73184 0.21726  -0.04429 -0.00889 106 THR A C   
831  O O   . THR A 106 ? 0.64291 0.84994 0.70143 0.19842  -0.04436 -0.00430 106 THR A O   
832  C CB  . THR A 106 ? 0.77360 0.88509 0.75859 0.25600  -0.03697 0.01158  106 THR A CB  
833  O OG1 . THR A 106 ? 0.74059 0.79462 0.69767 0.26295  -0.02706 0.01866  106 THR A OG1 
834  C CG2 . THR A 106 ? 0.62515 0.77081 0.59967 0.29587  -0.05125 0.00503  106 THR A CG2 
835  N N   . VAL A 107 ? 0.66220 0.95300 0.74991 0.22803  -0.05181 -0.02367 107 VAL A N   
836  C CA  . VAL A 107 ? 0.70373 1.05442 0.82059 0.21481  -0.06055 -0.03668 107 VAL A CA  
837  C C   . VAL A 107 ? 0.76285 1.15410 0.87270 0.25333  -0.07619 -0.04600 107 VAL A C   
838  O O   . VAL A 107 ? 0.68697 1.10914 0.79974 0.28137  -0.07952 -0.05383 107 VAL A O   
839  C CB  . VAL A 107 ? 0.64422 1.04848 0.80344 0.18585  -0.05396 -0.04982 107 VAL A CB  
840  C CG1 . VAL A 107 ? 0.70371 1.16555 0.89076 0.16794  -0.06184 -0.06506 107 VAL A CG1 
841  C CG2 . VAL A 107 ? 0.62902 0.98817 0.78749 0.15374  -0.03970 -0.03989 107 VAL A CG2 
842  N N   . LYS A 108 ? 0.82069 1.21358 0.91964 0.25748  -0.08655 -0.04627 108 LYS A N   
843  C CA  . LYS A 108 ? 0.77840 1.20523 0.86383 0.29710  -0.10336 -0.05467 108 LYS A CA  
844  C C   . LYS A 108 ? 0.91090 1.41544 1.03384 0.27913  -0.11158 -0.07739 108 LYS A C   
845  O O   . LYS A 108 ? 0.95603 1.48659 1.11138 0.24477  -0.11017 -0.08361 108 LYS A O   
846  C CB  . LYS A 108 ? 0.85042 1.21742 0.88753 0.31454  -0.10787 -0.03942 108 LYS A CB  
847  N N   . TYR A 109 ? 1.14874 1.68740 1.26390 0.30206  -0.11961 -0.09092 109 TYR A N   
848  C CA  . TYR A 109 ? 1.08461 1.69649 1.23024 0.28890  -0.12735 -0.11480 109 TYR A CA  
849  C C   . TYR A 109 ? 1.17644 1.78784 1.28751 0.32191  -0.14104 -0.11976 109 TYR A C   
850  O O   . TYR A 109 ? 1.27621 1.82739 1.33824 0.35238  -0.14311 -0.10350 109 TYR A O   
851  C CB  . TYR A 109 ? 1.04109 1.71357 1.21887 0.28208  -0.12221 -0.13260 109 TYR A CB  
852  C CG  . TYR A 109 ? 1.17322 1.84422 1.37921 0.25349  -0.10684 -0.12761 109 TYR A CG  
853  C CD1 . TYR A 109 ? 1.15201 1.84594 1.39466 0.20812  -0.09928 -0.13317 109 TYR A CD1 
854  C CD2 . TYR A 109 ? 1.23132 1.87507 1.42349 0.27187  -0.09925 -0.11819 109 TYR A CD2 
855  C CE1 . TYR A 109 ? 1.22684 1.91718 1.49052 0.18266  -0.08389 -0.12863 109 TYR A CE1 
856  C CE2 . TYR A 109 ? 1.08932 1.73240 1.30513 0.24745  -0.08468 -0.11444 109 TYR A CE2 
857  C CZ  . TYR A 109 ? 1.13687 1.80409 1.38804 0.20332  -0.07671 -0.11935 109 TYR A CZ  
858  O OH  . TYR A 109 ? 1.14601 1.80992 1.41561 0.17965  -0.06089 -0.11540 109 TYR A OH  
859  N N   . GLY A 110 ? 1.09853 1.77609 1.23319 0.31475  -0.14904 -0.14321 110 GLY A N   
860  C CA  . GLY A 110 ? 0.96595 1.65474 1.07175 0.34651  -0.16236 -0.15245 110 GLY A CA  
861  C C   . GLY A 110 ? 0.85963 1.62411 0.98432 0.35798  -0.16796 -0.17942 110 GLY A C   
862  O O   . GLY A 110 ? 0.70023 1.47109 0.79317 0.39697  -0.17785 -0.18659 110 GLY A O   
863  N N   . LYS A 114 ? 1.02582 1.57410 1.06411 0.40064  -0.13552 -0.10673 114 LYS A N   
864  C CA  . LYS A 114 ? 1.07831 1.60563 1.11286 0.40752  -0.12609 -0.10083 114 LYS A CA  
865  C C   . LYS A 114 ? 1.06735 1.55224 1.11590 0.37876  -0.11304 -0.08362 114 LYS A C   
866  O O   . LYS A 114 ? 1.13101 1.62827 1.20777 0.34760  -0.11132 -0.08250 114 LYS A O   
867  C CB  . LYS A 114 ? 1.02731 1.63556 1.10148 0.40195  -0.12602 -0.12380 114 LYS A CB  
868  C CG  . LYS A 114 ? 1.08795 1.67996 1.14549 0.42391  -0.12074 -0.12205 114 LYS A CG  
869  C CD  . LYS A 114 ? 1.19635 1.87426 1.29213 0.41871  -0.12074 -0.14619 114 LYS A CD  
870  C CE  . LYS A 114 ? 1.24782 1.98574 1.34173 0.43857  -0.13484 -0.16816 114 LYS A CE  
871  N NZ  . LYS A 114 ? 1.01557 1.83765 1.14288 0.43601  -0.13430 -0.19299 114 LYS A NZ  
872  N N   . GLU A 115 ? 0.84487 1.27931 0.87182 0.38985  -0.10409 -0.07163 115 GLU A N   
873  C CA  . GLU A 115 ? 0.87323 1.26052 0.90593 0.36800  -0.09161 -0.05565 115 GLU A CA  
874  C C   . GLU A 115 ? 0.82161 1.22732 0.87921 0.35913  -0.08137 -0.06059 115 GLU A C   
875  O O   . GLU A 115 ? 0.86702 1.27783 0.90994 0.38247  -0.08226 -0.06686 115 GLU A O   
876  C CB  . GLU A 115 ? 0.75102 1.04166 0.72584 0.38607  -0.08756 -0.03404 115 GLU A CB  
877  C CG  . GLU A 115 ? 0.95036 1.21247 0.90243 0.38502  -0.09260 -0.02450 115 GLU A CG  
878  C CD  . GLU A 115 ? 1.02468 1.18825 0.92009 0.39466  -0.08391 -0.00255 115 GLU A CD  
879  O OE1 . GLU A 115 ? 1.12422 1.24010 0.99977 0.39982  -0.07415 0.00437  115 GLU A OE1 
880  O OE2 . GLU A 115 ? 1.07927 1.21199 0.94852 0.39497  -0.08570 0.00697  115 GLU A OE2 
881  N N   . ALA A 116 ? 0.82325 1.23819 0.91565 0.32638  -0.07154 -0.05811 116 ALA A N   
882  C CA  . ALA A 116 ? 0.69163 1.11518 0.80430 0.31500  -0.05921 -0.06035 116 ALA A CA  
883  C C   . ALA A 116 ? 0.71573 1.06819 0.81459 0.29083  -0.04705 -0.04336 116 ALA A C   
884  O O   . ALA A 116 ? 0.67870 1.01456 0.78274 0.26039  -0.04514 -0.03727 116 ALA A O   
885  C CB  . ALA A 116 ? 0.67155 1.17762 0.83692 0.28469  -0.05510 -0.07763 116 ALA A CB  
886  N N   . THR A 117 ? 0.69508 1.00119 0.77247 0.30057  -0.03867 -0.03703 117 THR A N   
887  C CA  . THR A 117 ? 0.80680 1.04037 0.86523 0.27614  -0.02729 -0.02297 117 THR A CA  
888  C C   . THR A 117 ? 0.75250 0.99831 0.83315 0.25392  -0.01570 -0.02713 117 THR A C   
889  O O   . THR A 117 ? 0.63645 0.92525 0.73193 0.26797  -0.01442 -0.03791 117 THR A O   
890  C CB  . THR A 117 ? 0.83870 0.99371 0.84528 0.30243  -0.02615 -0.01173 117 THR A CB  
891  O OG1 . THR A 117 ? 0.96959 1.12547 0.96561 0.33121  -0.02515 -0.01804 117 THR A OG1 
892  C CG2 . THR A 117 ? 0.81797 0.95724 0.79428 0.32935  -0.03697 -0.00665 117 THR A CG2 
893  N N   . TYR A 118 ? 0.77780 0.98725 0.85886 0.22105  -0.00739 -0.01923 118 TYR A N   
894  C CA  . TYR A 118 ? 0.67142 0.88593 0.76771 0.19942  0.00314  -0.02179 118 TYR A CA  
895  C C   . TYR A 118 ? 0.67878 0.82554 0.75160 0.18684  0.00964  -0.01236 118 TYR A C   
896  O O   . TYR A 118 ? 0.61828 0.72196 0.67104 0.18424  0.00786  -0.00409 118 TYR A O   
897  C CB  . TYR A 118 ? 0.57919 0.83733 0.70772 0.16680  0.00615  -0.02623 118 TYR A CB  
898  C CG  . TYR A 118 ? 0.64535 0.97523 0.80123 0.17106  0.00040  -0.03832 118 TYR A CG  
899  C CD1 . TYR A 118 ? 0.61406 0.95760 0.77220 0.17381  -0.01021 -0.03925 118 TYR A CD1 
900  C CD2 . TYR A 118 ? 0.62180 1.00999 0.80201 0.17127  0.00599  -0.05063 118 TYR A CD2 
901  C CE1 . TYR A 118 ? 0.66735 1.08206 0.85259 0.17664  -0.01660 -0.05353 118 TYR A CE1 
902  C CE2 . TYR A 118 ? 0.74408 1.20633 0.95337 0.17222  0.00135  -0.06506 118 TYR A CE2 
903  C CZ  . TYR A 118 ? 0.70000 1.17598 0.91243 0.17478  -0.01070 -0.06717 118 TYR A CZ  
904  O OH  . TYR A 118 ? 0.78581 1.34079 1.02914 0.17480  -0.01648 -0.08460 118 TYR A OH  
905  N N   . LEU A 119 ? 0.61538 0.75706 0.69128 0.17833  0.01768  -0.01515 119 LEU A N   
906  C CA  . LEU A 119 ? 0.57277 0.66131 0.63126 0.16523  0.02335  -0.01057 119 LEU A CA  
907  C C   . LEU A 119 ? 0.53496 0.63844 0.61084 0.13753  0.02853  -0.01176 119 LEU A C   
908  O O   . LEU A 119 ? 0.62457 0.76642 0.71652 0.13425  0.03269  -0.01713 119 LEU A O   
909  C CB  . LEU A 119 ? 0.63040 0.69005 0.66756 0.18551  0.02690  -0.01412 119 LEU A CB  
910  C CG  . LEU A 119 ? 0.70072 0.69136 0.70395 0.18882  0.02860  -0.00932 119 LEU A CG  
911  C CD1 . LEU A 119 ? 0.77807 0.74775 0.76398 0.19860  0.02368  -0.00156 119 LEU A CD1 
912  C CD2 . LEU A 119 ? 0.77993 0.74305 0.75986 0.21177  0.03142  -0.01482 119 LEU A CD2 
913  N N   . ALA A 120 ? 0.48310 0.55624 0.55310 0.11874  0.02888  -0.00722 120 ALA A N   
914  C CA  . ALA A 120 ? 0.54291 0.62240 0.62170 0.09666  0.03197  -0.00762 120 ALA A CA  
915  C C   . ALA A 120 ? 0.53287 0.57660 0.59755 0.09106  0.03451  -0.00911 120 ALA A C   
916  O O   . ALA A 120 ? 0.53004 0.54174 0.58242 0.09170  0.03343  -0.00819 120 ALA A O   
917  C CB  . ALA A 120 ? 0.42431 0.50991 0.51092 0.08081  0.02775  -0.00374 120 ALA A CB  
918  N N   . LEU A 121 ? 0.49534 0.54582 0.56055 0.08465  0.03851  -0.01241 121 LEU A N   
919  C CA  . LEU A 121 ? 0.48050 0.50583 0.53418 0.07916  0.03907  -0.01642 121 LEU A CA  
920  C C   . LEU A 121 ? 0.54308 0.56542 0.59719 0.06404  0.03587  -0.01492 121 LEU A C   
921  O O   . LEU A 121 ? 0.53286 0.53753 0.58091 0.05978  0.03321  -0.01930 121 LEU A O   
922  C CB  . LEU A 121 ? 0.59449 0.62650 0.64238 0.08549  0.04426  -0.02165 121 LEU A CB  
923  C CG  . LEU A 121 ? 0.50506 0.51729 0.53997 0.08259  0.04376  -0.02841 121 LEU A CG  
924  C CD1 . LEU A 121 ? 0.40322 0.38586 0.43001 0.08507  0.04178  -0.03465 121 LEU A CD1 
925  C CD2 . LEU A 121 ? 0.60696 0.63018 0.63444 0.09005  0.04950  -0.03230 121 LEU A CD2 
926  N N   . ASN A 122 ? 0.47648 0.51591 0.53640 0.05607  0.03613  -0.01039 122 ASN A N   
927  C CA  . ASN A 122 ? 0.53055 0.56168 0.58539 0.04538  0.03236  -0.00867 122 ASN A CA  
928  C C   . ASN A 122 ? 0.51050 0.54269 0.57308 0.04091  0.02735  -0.00527 122 ASN A C   
929  O O   . ASN A 122 ? 0.55633 0.57603 0.61679 0.03977  0.02335  -0.00708 122 ASN A O   
930  C CB  . ASN A 122 ? 0.48601 0.52328 0.53370 0.03771  0.03704  -0.00572 122 ASN A CB  
931  C CG  . ASN A 122 ? 0.55059 0.57289 0.57875 0.04062  0.03855  -0.00831 122 ASN A CG  
932  O OD1 . ASN A 122 ? 0.50811 0.52271 0.53271 0.04863  0.03568  -0.01455 122 ASN A OD1 
933  N ND2 . ASN A 122 ? 0.53368 0.54949 0.54592 0.03368  0.04338  -0.00418 122 ASN A ND2 
934  N N   . GLU A 123 ? 0.56769 0.61832 0.63974 0.03778  0.02789  -0.00193 123 GLU A N   
935  C CA  . GLU A 123 ? 0.42834 0.48123 0.50555 0.03406  0.02244  0.00050  123 GLU A CA  
936  C C   . GLU A 123 ? 0.56526 0.64678 0.65579 0.03427  0.02268  0.00071  123 GLU A C   
937  O O   . GLU A 123 ? 0.45422 0.55698 0.55161 0.03463  0.02799  -0.00158 123 GLU A O   
938  C CB  . GLU A 123 ? 0.42115 0.46160 0.48961 0.02393  0.01919  0.00108  123 GLU A CB  
939  C CG  . GLU A 123 ? 0.48038 0.52594 0.54529 0.01241  0.02286  0.00226  123 GLU A CG  
940  C CD  . GLU A 123 ? 0.56219 0.60337 0.61681 0.01150  0.03041  0.00220  123 GLU A CD  
941  O OE1 . GLU A 123 ? 0.43221 0.45261 0.47071 0.01636  0.02892  0.00145  123 GLU A OE1 
942  O OE2 . GLU A 123 ? 0.41781 0.47984 0.48034 0.00684  0.03777  0.00174  123 GLU A OE2 
943  N N   . SER A 124 ? 0.51422 0.60042 0.60879 0.03450  0.01679  0.00190  124 SER A N   
944  C CA  . SER A 124 ? 0.51293 0.63070 0.62088 0.03292  0.01428  -0.00063 124 SER A CA  
945  C C   . SER A 124 ? 0.51057 0.62286 0.61631 0.02053  0.00926  -0.00067 124 SER A C   
946  O O   . SER A 124 ? 0.53391 0.62508 0.63029 0.02327  0.00509  0.00206  124 SER A O   
947  C CB  . SER A 124 ? 0.55614 0.68631 0.66703 0.05238  0.01001  -0.00065 124 SER A CB  
948  O OG  . SER A 124 ? 0.50219 0.67095 0.62778 0.05299  0.00553  -0.00594 124 SER A OG  
949  N N   . THR A 125 ? 0.49118 0.62209 0.60441 0.00566  0.01068  -0.00494 125 THR A N   
950  C CA  . THR A 125 ? 0.50149 0.62247 0.60906 -0.00743 0.00629  -0.00654 125 THR A CA  
951  C C   . THR A 125 ? 0.55383 0.71244 0.67825 -0.01259 0.00202  -0.01418 125 THR A C   
952  O O   . THR A 125 ? 0.54085 0.73733 0.68263 -0.01340 0.00536  -0.01994 125 THR A O   
953  C CB  . THR A 125 ? 0.40523 0.50089 0.49733 -0.02498 0.01253  -0.00591 125 THR A CB  
954  O OG1 . THR A 125 ? 0.53783 0.65750 0.63959 -0.04157 0.02057  -0.01081 125 THR A OG1 
955  C CG2 . THR A 125 ? 0.45926 0.52873 0.53670 -0.01737 0.01661  -0.00087 125 THR A CG2 
956  N N   . VAL A 126 ? 0.58702 0.73915 0.70673 -0.01511 -0.00584 -0.01608 126 VAL A N   
957  C CA  . VAL A 126 ? 0.55008 0.73648 0.68358 -0.02207 -0.01177 -0.02585 126 VAL A CA  
958  C C   . VAL A 126 ? 0.51917 0.68314 0.64119 -0.04514 -0.01124 -0.03005 126 VAL A C   
959  O O   . VAL A 126 ? 0.57262 0.69805 0.67444 -0.04279 -0.01435 -0.02542 126 VAL A O   
960  C CB  . VAL A 126 ? 0.49527 0.69214 0.62841 -0.00153 -0.02267 -0.02544 126 VAL A CB  
961  C CG1 . VAL A 126 ? 0.57837 0.81889 0.72725 -0.00567 -0.03056 -0.03810 126 VAL A CG1 
962  C CG2 . VAL A 126 ? 0.49235 0.69214 0.62485 0.02261  -0.02189 -0.01895 126 VAL A CG2 
963  N N   . LYS A 127 ? 0.53252 0.71988 0.66573 -0.06769 -0.00656 -0.03993 127 LYS A N   
964  C CA  . LYS A 127 ? 0.64998 0.80823 0.76696 -0.09304 -0.00403 -0.04471 127 LYS A CA  
965  C C   . LYS A 127 ? 0.81090 1.01240 0.94798 -0.11129 -0.00728 -0.06102 127 LYS A C   
966  O O   . LYS A 127 ? 0.76027 1.02021 0.92624 -0.10798 -0.00818 -0.06945 127 LYS A O   
967  C CB  . LYS A 127 ? 0.70152 0.82757 0.80118 -0.11191 0.01052  -0.04018 127 LYS A CB  
968  C CG  . LYS A 127 ? 0.67817 0.76602 0.75783 -0.09490 0.01328  -0.02696 127 LYS A CG  
969  C CD  . LYS A 127 ? 0.76886 0.81839 0.82265 -0.11301 0.02644  -0.02300 127 LYS A CD  
970  C CE  . LYS A 127 ? 0.79258 0.82056 0.83278 -0.09543 0.02976  -0.01269 127 LYS A CE  
971  N NZ  . LYS A 127 ? 0.72367 0.71019 0.73166 -0.11044 0.04231  -0.00804 127 LYS A NZ  
972  N N   . SER A 128 ? 0.94867 1.12209 1.06932 -0.13005 -0.00940 -0.06729 128 SER A N   
973  C CA  . SER A 128 ? 1.07573 1.28790 1.21403 -0.15138 -0.01292 -0.08573 128 SER A CA  
974  C C   . SER A 128 ? 1.14235 1.37812 1.29397 -0.18499 0.00249  -0.09520 128 SER A C   
975  O O   . SER A 128 ? 1.21336 1.40896 1.34470 -0.19883 0.01706  -0.08629 128 SER A O   
976  C CB  . SER A 128 ? 1.05911 1.22661 1.17122 -0.16240 -0.01912 -0.09047 128 SER A CB  
977  O OG  . SER A 128 ? 1.12734 1.22326 1.20198 -0.15950 -0.01388 -0.07694 128 SER A OG  
978  N N   . SER A 129 ? 1.20888 1.51293 1.39384 -0.19768 -0.00059 -0.11439 129 SER A N   
979  C CA  . SER A 129 ? 1.34716 1.68310 1.54855 -0.23687 0.01466  -0.12892 129 SER A CA  
980  C C   . SER A 129 ? 1.40084 1.66244 1.56373 -0.27267 0.02709  -0.12714 129 SER A C   
981  O O   . SER A 129 ? 1.38265 1.60243 1.52288 -0.28673 0.04425  -0.11620 129 SER A O   
982  C CB  . SER A 129 ? 1.21409 1.63437 1.45529 -0.24619 0.00546  -0.15465 129 SER A CB  
983  O OG  . SER A 129 ? 1.07794 1.55015 1.34122 -0.20459 -0.01137 -0.15509 129 SER A OG  
984  N N   A GLY A 130 ? 1.46472 1.70628 1.61576 -0.28620 0.01848  -0.13824 130 GLY A N   
985  N N   B GLY A 130 ? 1.48006 1.71732 1.62888 -0.28358 0.01782  -0.13669 130 GLY A N   
986  C CA  A GLY A 130 ? 1.48981 1.64852 1.59548 -0.31431 0.02746  -0.13637 130 GLY A CA  
987  C CA  B GLY A 130 ? 1.49145 1.64975 1.59690 -0.31430 0.02741  -0.13636 130 GLY A CA  
988  C C   A GLY A 130 ? 1.43155 1.56144 1.51990 -0.30154 0.00950  -0.14102 130 GLY A C   
989  C C   B GLY A 130 ? 1.49100 1.56424 1.54949 -0.28895 0.02067  -0.11808 130 GLY A C   
990  O O   A GLY A 130 ? 1.48496 1.53395 1.52765 -0.29651 0.00889  -0.13078 130 GLY A O   
991  O O   B GLY A 130 ? 1.47638 1.50497 1.50995 -0.27722 0.02892  -0.10012 130 GLY A O   
992  N N   A GLY A 131 ? 1.22675 1.42531 1.35007 -0.29189 -0.00610 -0.15682 131 GLY A N   
993  N N   B GLY A 131 ? 1.37279 1.42705 1.41899 -0.27879 0.00527  -0.12401 131 GLY A N   
994  C CA  A GLY A 131 ? 1.10176 1.28333 1.21152 -0.27789 -0.02365 -0.16280 131 GLY A CA  
995  C CA  B GLY A 131 ? 1.20569 1.18099 1.20564 -0.25884 -0.00031 -0.11140 131 GLY A CA  
996  C C   A GLY A 131 ? 1.07674 1.22690 1.16840 -0.23292 -0.03424 -0.14261 131 GLY A C   
997  C C   B GLY A 131 ? 1.10903 1.09825 1.11674 -0.21351 -0.01498 -0.09990 131 GLY A C   
998  O O   A GLY A 131 ? 1.10292 1.23798 1.19013 -0.21400 -0.02813 -0.12404 131 GLY A O   
999  O O   B GLY A 131 ? 1.07922 1.09981 1.10749 -0.19360 -0.01358 -0.08923 131 GLY A O   
1000 N N   A PRO A 132 ? 0.77383 0.91712 0.85539 -0.21649 -0.04990 -0.14776 132 PRO A N   
1001 N N   B PRO A 132 ? 0.86263 0.82516 0.85095 -0.19756 -0.02798 -0.10231 132 PRO A N   
1002 C CA  A PRO A 132 ? 0.80126 0.90706 0.85997 -0.17991 -0.05733 -0.13057 132 PRO A CA  
1003 C CA  B PRO A 132 ? 0.77465 0.75208 0.76954 -0.15828 -0.03965 -0.09263 132 PRO A CA  
1004 C C   A PRO A 132 ? 0.77401 0.92363 0.85671 -0.14754 -0.06064 -0.11819 132 PRO A C   
1005 C C   B PRO A 132 ? 0.73956 0.79148 0.77424 -0.14725 -0.04939 -0.09983 132 PRO A C   
1006 O O   A PRO A 132 ? 0.76776 0.98229 0.88186 -0.14161 -0.06625 -0.12640 132 PRO A O   
1007 O O   B PRO A 132 ? 0.78492 0.86887 0.83347 -0.16265 -0.05535 -0.11683 132 PRO A O   
1008 C CB  A PRO A 132 ? 0.72833 0.82967 0.77491 -0.17404 -0.07231 -0.14324 132 PRO A CB  
1009 C CB  B PRO A 132 ? 0.76947 0.69411 0.72756 -0.14845 -0.04842 -0.09549 132 PRO A CB  
1010 C CG  A PRO A 132 ? 0.74533 0.91625 0.82566 -0.19108 -0.07857 -0.16520 132 PRO A CG  
1011 C CG  B PRO A 132 ? 0.78361 0.68915 0.72902 -0.18206 -0.04694 -0.11248 132 PRO A CG  
1012 C CD  A PRO A 132 ? 0.76783 0.95503 0.86575 -0.22636 -0.06264 -0.17097 132 PRO A CD  
1013 C CD  B PRO A 132 ? 0.84245 0.74871 0.79420 -0.21436 -0.03032 -0.11261 132 PRO A CD  
1014 N N   A PHE A 133 ? 0.75137 0.86364 0.81659 -0.12580 -0.05739 -0.09956 133 PHE A N   
1015 N N   B PHE A 133 ? 0.73172 0.80917 0.78166 -0.11977 -0.05123 -0.08771 133 PHE A N   
1016 C CA  A PHE A 133 ? 0.71726 0.85706 0.79817 -0.09776 -0.05823 -0.08690 133 PHE A CA  
1017 C CA  B PHE A 133 ? 0.72103 0.85879 0.79900 -0.10255 -0.06054 -0.09162 133 PHE A CA  
1018 C C   A PHE A 133 ? 0.67399 0.80202 0.74064 -0.07002 -0.06799 -0.08080 133 PHE A C   
1019 C C   B PHE A 133 ? 0.67448 0.80151 0.74006 -0.07126 -0.06863 -0.08204 133 PHE A C   
1020 O O   A PHE A 133 ? 0.65020 0.73272 0.69229 -0.06274 -0.06654 -0.07325 133 PHE A O   
1021 O O   B PHE A 133 ? 0.65634 0.73892 0.69864 -0.06254 -0.06635 -0.07295 133 PHE A O   
1022 C CB  A PHE A 133 ? 0.72140 0.83445 0.79623 -0.09673 -0.04574 -0.07244 133 PHE A CB  
1023 C CB  B PHE A 133 ? 0.69352 0.87532 0.79986 -0.09913 -0.05403 -0.08771 133 PHE A CB  
1024 C CG  A PHE A 133 ? 0.68025 0.82227 0.77249 -0.07359 -0.04488 -0.06233 133 PHE A CG  
1025 C CG  B PHE A 133 ? 0.69247 0.85811 0.79421 -0.07590 -0.04921 -0.06959 133 PHE A CG  
1026 C CD1 A PHE A 133 ? 0.70185 0.90016 0.82251 -0.07082 -0.04629 -0.06853 133 PHE A CD1 
1027 C CD1 B PHE A 133 ? 0.68660 0.79907 0.76274 -0.06997 -0.04527 -0.05817 133 PHE A CD1 
1028 C CD2 A PHE A 133 ? 0.68851 0.80202 0.76749 -0.05426 -0.04283 -0.04846 133 PHE A CD2 
1029 C CD2 B PHE A 133 ? 0.70731 0.91328 0.83012 -0.05956 -0.04895 -0.06611 133 PHE A CD2 
1030 C CE1 A PHE A 133 ? 0.70929 0.92597 0.83952 -0.04747 -0.04564 -0.05948 133 PHE A CE1 
1031 C CE1 B PHE A 133 ? 0.68797 0.79216 0.76328 -0.05162 -0.04098 -0.04492 133 PHE A CE1 
1032 C CE2 A PHE A 133 ? 0.66657 0.79971 0.75759 -0.03568 -0.04107 -0.04018 133 PHE A CE2 
1033 C CE2 B PHE A 133 ? 0.69552 0.88466 0.81312 -0.04114 -0.04398 -0.05151 133 PHE A CE2 
1034 C CZ  A PHE A 133 ? 0.67833 0.85844 0.79227 -0.03139 -0.04244 -0.04484 133 PHE A CZ  
1035 C CZ  B PHE A 133 ? 0.66914 0.80914 0.76469 -0.03912 -0.03977 -0.04151 133 PHE A CZ  
1036 N N   . VAL A 134 ? 0.62367 0.79392 0.70360 -0.05374 -0.07766 -0.08499 134 VAL A N   
1037 C CA  . VAL A 134 ? 0.57948 0.74272 0.64522 -0.02689 -0.08411 -0.07736 134 VAL A CA  
1038 C C   . VAL A 134 ? 0.65046 0.84376 0.72844 -0.00482 -0.08384 -0.06834 134 VAL A C   
1039 O O   . VAL A 134 ? 0.66381 0.90209 0.76147 -0.00291 -0.08830 -0.07618 134 VAL A O   
1040 C CB  . VAL A 134 ? 0.70913 0.88308 0.76608 -0.02461 -0.09685 -0.09067 134 VAL A CB  
1041 C CG1 . VAL A 134 ? 0.59179 0.75295 0.62903 0.00160  -0.10029 -0.08131 134 VAL A CG1 
1042 C CG2 . VAL A 134 ? 0.69147 0.83186 0.73364 -0.04840 -0.09722 -0.10214 134 VAL A CG2 
1043 N N   . VAL A 135 ? 0.53763 0.70611 0.60251 0.01194  -0.07844 -0.05332 135 VAL A N   
1044 C CA  . VAL A 135 ? 0.61530 0.79724 0.68160 0.03364  -0.07694 -0.04338 135 VAL A CA  
1045 C C   . VAL A 135 ? 0.61076 0.76653 0.65322 0.04991  -0.07509 -0.03305 135 VAL A C   
1046 O O   . VAL A 135 ? 0.60372 0.73067 0.63560 0.04420  -0.07012 -0.02998 135 VAL A O   
1047 C CB  . VAL A 135 ? 0.62644 0.80424 0.70426 0.03102  -0.06653 -0.03539 135 VAL A CB  
1048 C CG1 . VAL A 135 ? 0.72624 0.94216 0.82860 0.01983  -0.06733 -0.04560 135 VAL A CG1 
1049 C CG2 . VAL A 135 ? 0.51572 0.65531 0.58586 0.01875  -0.05769 -0.02976 135 VAL A CG2 
1050 N N   . ASP A 136 ? 0.61797 0.78442 0.64969 0.07103  -0.07863 -0.02837 136 ASP A N   
1051 C CA  . ASP A 136 ? 0.59096 0.73028 0.59741 0.08455  -0.07247 -0.01642 136 ASP A CA  
1052 C C   . ASP A 136 ? 0.59059 0.70939 0.59591 0.08693  -0.06003 -0.00397 136 ASP A C   
1053 O O   . ASP A 136 ? 0.65258 0.78201 0.66506 0.09476  -0.06009 -0.00186 136 ASP A O   
1054 C CB  . ASP A 136 ? 0.60719 0.75773 0.59333 0.10683  -0.08049 -0.01560 136 ASP A CB  
1055 C CG  . ASP A 136 ? 0.63667 0.79927 0.61610 0.10562  -0.09132 -0.02720 136 ASP A CG  
1056 O OD1 . ASP A 136 ? 0.63234 0.77901 0.61058 0.09205  -0.08871 -0.03071 136 ASP A OD1 
1057 O OD2 . ASP A 136 ? 0.69462 0.88295 0.66808 0.12042  -0.10337 -0.03404 136 ASP A OD2 
1058 N N   . VAL A 137 ? 0.55501 0.64722 0.55185 0.08043  -0.04970 0.00216  137 VAL A N   
1059 C CA  . VAL A 137 ? 0.64317 0.71511 0.63908 0.07871  -0.03743 0.01124  137 VAL A CA  
1060 C C   . VAL A 137 ? 0.60579 0.65544 0.57356 0.09006  -0.02922 0.02167  137 VAL A C   
1061 O O   . VAL A 137 ? 0.60115 0.64242 0.55479 0.08810  -0.02493 0.02254  137 VAL A O   
1062 C CB  . VAL A 137 ? 0.59069 0.65256 0.59686 0.06304  -0.03118 0.00849  137 VAL A CB  
1063 C CG1 . VAL A 137 ? 0.55589 0.60109 0.56260 0.06017  -0.01949 0.01502  137 VAL A CG1 
1064 C CG2 . VAL A 137 ? 0.48787 0.56133 0.51202 0.05214  -0.03787 -0.00009 137 VAL A CG2 
1065 N N   . VAL A 138 ? 0.62113 0.65857 0.57743 0.10216  -0.02596 0.02941  138 VAL A N   
1066 C CA  . VAL A 138 ? 0.64353 0.64886 0.56424 0.11356  -0.01670 0.04100  138 VAL A CA  
1067 C C   . VAL A 138 ? 0.67509 0.65025 0.59191 0.10445  -0.00195 0.04731  138 VAL A C   
1068 O O   . VAL A 138 ? 0.61556 0.59230 0.54501 0.10660  -0.00334 0.04635  138 VAL A O   
1069 C CB  . VAL A 138 ? 0.67308 0.68080 0.57269 0.14037  -0.02627 0.04445  138 VAL A CB  
1070 C CG1 . VAL A 138 ? 0.57189 0.53465 0.42457 0.15316  -0.01526 0.05837  138 VAL A CG1 
1071 C CG2 . VAL A 138 ? 0.63711 0.68097 0.54404 0.14738  -0.04222 0.03455  138 VAL A CG2 
1072 N N   . ILE A 139 ? 0.65308 0.60327 0.55283 0.09309  0.01272  0.05211  139 ILE A N   
1073 C CA  . ILE A 139 ? 0.60376 0.52539 0.49896 0.07973  0.02815  0.05545  139 ILE A CA  
1074 C C   . ILE A 139 ? 0.65164 0.52621 0.50033 0.08695  0.04104  0.06818  139 ILE A C   
1075 O O   . ILE A 139 ? 0.63573 0.49911 0.46263 0.08173  0.05039  0.07212  139 ILE A O   
1076 C CB  . ILE A 139 ? 0.63051 0.56567 0.54630 0.05640  0.03643  0.04723  139 ILE A CB  
1077 C CG1 . ILE A 139 ? 0.57086 0.54190 0.52291 0.05266  0.02363  0.03612  139 ILE A CG1 
1078 C CG2 . ILE A 139 ? 0.59395 0.50327 0.50532 0.04051  0.05243  0.04792  139 ILE A CG2 
1079 C CD1 . ILE A 139 ? 0.44976 0.43746 0.41882 0.03708  0.02815  0.02648  139 ILE A CD1 
1080 N N   . ASN A 140 ? 0.62474 0.46847 0.45423 0.09965  0.04247  0.07462  140 ASN A N   
1081 C CA  . ASN A 140 ? 0.78946 0.57470 0.56532 0.10886  0.05530  0.08797  140 ASN A CA  
1082 C C   . ASN A 140 ? 0.77982 0.55963 0.52161 0.12916  0.05046  0.09563  140 ASN A C   
1083 O O   . ASN A 140 ? 0.77623 0.51977 0.47913 0.12355  0.06561  0.10471  140 ASN A O   
1084 C CB  . ASN A 140 ? 0.72807 0.47952 0.49164 0.07926  0.07860  0.08948  140 ASN A CB  
1085 C CG  . ASN A 140 ? 0.84081 0.59585 0.63375 0.06125  0.08251  0.08055  140 ASN A CG  
1086 O OD1 . ASN A 140 ? 0.79937 0.54107 0.59078 0.07460  0.07669  0.08115  140 ASN A OD1 
1087 N ND2 . ASN A 140 ? 0.73356 0.50992 0.55283 0.03286  0.09175  0.07077  140 ASN A ND2 
1088 N N   . ASP A 141 ? 0.73830 0.55726 0.49511 0.15161  0.02957  0.09057  141 ASP A N   
1089 C CA  . ASP A 141 ? 0.88066 0.70582 0.61019 0.17617  0.01902  0.09407  141 ASP A CA  
1090 C C   . ASP A 141 ? 0.83656 0.68130 0.57048 0.16245  0.02154  0.09097  141 ASP A C   
1091 O O   . ASP A 141 ? 0.93541 0.77759 0.63866 0.18085  0.01619  0.09495  141 ASP A O   
1092 C CB  . ASP A 141 ? 0.87316 0.63647 0.53634 0.20055  0.02658  0.10979  141 ASP A CB  
1093 C CG  . ASP A 141 ? 1.00544 0.74926 0.65820 0.22274  0.02099  0.11174  141 ASP A CG  
1094 O OD1 . ASP A 141 ? 0.95791 0.75102 0.65499 0.22772  0.00589  0.09986  141 ASP A OD1 
1095 O OD2 . ASP A 141 ? 1.17693 0.85392 0.77436 0.23523  0.03265  0.12485  141 ASP A OD2 
1096 N N   . ILE A 142 ? 0.81330 0.67915 0.58261 0.13385  0.02833  0.08285  142 ILE A N   
1097 C CA  . ILE A 142 ? 0.81357 0.70228 0.59004 0.12265  0.02991  0.07733  142 ILE A CA  
1098 C C   . ILE A 142 ? 0.71232 0.65156 0.53688 0.11711  0.01323  0.06208  142 ILE A C   
1099 O O   . ILE A 142 ? 0.70021 0.65146 0.55772 0.10354  0.01289  0.05585  142 ILE A O   
1100 C CB  . ILE A 142 ? 0.89701 0.76857 0.66982 0.09573  0.05282  0.07879  142 ILE A CB  
1101 C CG1 . ILE A 142 ? 0.94126 0.75314 0.66313 0.09527  0.07281  0.09400  142 ILE A CG1 
1102 C CG2 . ILE A 142 ? 0.94836 0.84658 0.72547 0.08879  0.05449  0.07222  142 ILE A CG2 
1103 C CD1 . ILE A 142 ? 0.97360 0.75844 0.64231 0.11855  0.07258  0.10586  142 ILE A CD1 
1104 N N   . HIS A 143 ? 0.78829 0.75297 0.61286 0.12737  -0.00012 0.05583  143 HIS A N   
1105 C CA  A HIS A 143 ? 0.73690 0.74024 0.59965 0.11992  -0.01438 0.04117  143 HIS A CA  
1106 C CA  B HIS A 143 ? 0.74839 0.75182 0.61089 0.12005  -0.01445 0.04115  143 HIS A CA  
1107 C C   . HIS A 143 ? 0.68112 0.68995 0.56205 0.09925  -0.00528 0.03508  143 HIS A C   
1108 O O   . HIS A 143 ? 0.67305 0.67818 0.53824 0.09594  0.00385  0.03566  143 HIS A O   
1109 C CB  A HIS A 143 ? 0.70418 0.72978 0.55919 0.13383  -0.03010 0.03394  143 HIS A CB  
1110 C CB  B HIS A 143 ? 0.68447 0.70915 0.53771 0.13429  -0.02974 0.03432  143 HIS A CB  
1111 C CG  A HIS A 143 ? 0.72018 0.77585 0.60760 0.12310  -0.04275 0.01843  143 HIS A CG  
1112 C CG  B HIS A 143 ? 0.69518 0.72954 0.53869 0.15663  -0.04349 0.03475  143 HIS A CG  
1113 N ND1 A HIS A 143 ? 0.65957 0.71845 0.55308 0.11160  -0.04006 0.01136  143 HIS A ND1 
1114 N ND1 B HIS A 143 ? 0.67437 0.73884 0.54906 0.15665  -0.05676 0.02490  143 HIS A ND1 
1115 C CD2 A HIS A 143 ? 0.66947 0.75011 0.58191 0.12140  -0.05686 0.00819  143 HIS A CD2 
1116 C CD2 B HIS A 143 ? 0.73830 0.75899 0.54300 0.18128  -0.04616 0.04265  143 HIS A CD2 
1117 C CE1 A HIS A 143 ? 0.57937 0.65570 0.49518 0.10444  -0.05234 -0.00129 143 HIS A CE1 
1118 C CE1 B HIS A 143 ? 0.66524 0.74111 0.52535 0.18076  -0.06787 0.02481  143 HIS A CE1 
1119 N NE2 A HIS A 143 ? 0.56829 0.65839 0.49673 0.10755  -0.06161 -0.00342 143 HIS A NE2 
1120 N NE2 B HIS A 143 ? 0.73362 0.78116 0.54926 0.19814  -0.06274 0.03592  143 HIS A NE2 
1121 N N   . PHE A 144 ? 0.60481 0.62454 0.51726 0.08721  -0.00777 0.02849  144 PHE A N   
1122 C CA  . PHE A 144 ? 0.50128 0.52798 0.43063 0.07195  -0.00116 0.02141  144 PHE A CA  
1123 C C   . PHE A 144 ? 0.43369 0.48002 0.37790 0.07117  -0.01400 0.00895  144 PHE A C   
1124 O O   . PHE A 144 ? 0.44954 0.50285 0.39295 0.06836  -0.01096 0.00236  144 PHE A O   
1125 C CB  . PHE A 144 ? 0.56136 0.58183 0.50913 0.06119  0.00497  0.02210  144 PHE A CB  
1126 C CG  . PHE A 144 ? 0.52414 0.55610 0.48939 0.04892  0.00965  0.01300  144 PHE A CG  
1127 C CD1 . PHE A 144 ? 0.44943 0.48187 0.40893 0.03983  0.02443  0.01188  144 PHE A CD1 
1128 C CD2 . PHE A 144 ? 0.50948 0.55256 0.49478 0.04693  -0.00027 0.00468  144 PHE A CD2 
1129 C CE1 . PHE A 144 ? 0.53698 0.58889 0.51465 0.03166  0.02698  0.00049  144 PHE A CE1 
1130 C CE2 . PHE A 144 ? 0.41790 0.47143 0.41482 0.04122  0.00199  -0.00438 144 PHE A CE2 
1131 C CZ  . PHE A 144 ? 0.45737 0.51941 0.45264 0.03492  0.01452  -0.00756 144 PHE A CZ  
1132 N N   . GLU A 145 ? 0.41380 0.46842 0.36966 0.07330  -0.02749 0.00448  145 GLU A N   
1133 C CA  . GLU A 145 ? 0.47432 0.53711 0.43889 0.06959  -0.03829 -0.00729 145 GLU A CA  
1134 C C   . GLU A 145 ? 0.46726 0.54070 0.43987 0.06977  -0.05088 -0.01184 145 GLU A C   
1135 O O   . GLU A 145 ? 0.52388 0.60362 0.50241 0.07302  -0.05131 -0.00684 145 GLU A O   
1136 C CB  . GLU A 145 ? 0.47406 0.53191 0.45298 0.06010  -0.03529 -0.01157 145 GLU A CB  
1137 C CG  . GLU A 145 ? 0.41747 0.47279 0.41254 0.05329  -0.03447 -0.00817 145 GLU A CG  
1138 C CD  . GLU A 145 ? 0.39075 0.43950 0.39445 0.04695  -0.03167 -0.01198 145 GLU A CD  
1139 O OE1 . GLU A 145 ? 0.39782 0.44699 0.39628 0.04958  -0.03018 -0.01754 145 GLU A OE1 
1140 O OE2 . GLU A 145 ? 0.33572 0.38117 0.35011 0.04138  -0.03131 -0.01027 145 GLU A OE2 
1141 N N   . ARG A 146 ? 0.44545 0.52177 0.41752 0.06608  -0.06084 -0.02308 146 ARG A N   
1142 C CA  . ARG A 146 ? 0.60570 0.69406 0.58893 0.05875  -0.07141 -0.03167 146 ARG A CA  
1143 C C   . ARG A 146 ? 0.53622 0.60881 0.52741 0.04358  -0.07057 -0.03686 146 ARG A C   
1144 O O   . ARG A 146 ? 0.56043 0.61553 0.53933 0.04159  -0.07342 -0.04385 146 ARG A O   
1145 C CB  . ARG A 146 ? 0.56380 0.66266 0.53533 0.06360  -0.08303 -0.04212 146 ARG A CB  
1146 C CG  . ARG A 146 ? 0.57169 0.68574 0.55644 0.05049  -0.09336 -0.05537 146 ARG A CG  
1147 C CD  . ARG A 146 ? 0.58919 0.72530 0.56574 0.05849  -0.10609 -0.06609 146 ARG A CD  
1148 N NE  . ARG A 146 ? 0.67012 0.83244 0.64768 0.07568  -0.10888 -0.06040 146 ARG A NE  
1149 C CZ  . ARG A 146 ? 0.71631 0.90446 0.68657 0.08801  -0.12119 -0.06902 146 ARG A CZ  
1150 N NH1 . ARG A 146 ? 0.69079 0.88421 0.65476 0.08248  -0.13170 -0.08472 146 ARG A NH1 
1151 N NH2 . ARG A 146 ? 0.61955 0.82676 0.58554 0.10826  -0.12381 -0.06262 146 ARG A NH2 
1152 N N   . PHE A 147 ? 0.62465 0.70030 0.63191 0.03508  -0.06638 -0.03329 147 PHE A N   
1153 C CA  . PHE A 147 ? 0.51179 0.56778 0.52120 0.02193  -0.06342 -0.03554 147 PHE A CA  
1154 C C   . PHE A 147 ? 0.54239 0.59932 0.55418 0.00545  -0.06930 -0.04635 147 PHE A C   
1155 O O   . PHE A 147 ? 0.58398 0.66996 0.61161 0.00020  -0.07222 -0.05026 147 PHE A O   
1156 C CB  . PHE A 147 ? 0.66192 0.72000 0.68483 0.01993  -0.05477 -0.02698 147 PHE A CB  
1157 C CG  . PHE A 147 ? 0.56095 0.59697 0.58130 0.00871  -0.05105 -0.02796 147 PHE A CG  
1158 C CD1 . PHE A 147 ? 0.58735 0.62540 0.61450 -0.00737 -0.05029 -0.03184 147 PHE A CD1 
1159 C CD2 . PHE A 147 ? 0.48239 0.49728 0.49171 0.01468  -0.04782 -0.02582 147 PHE A CD2 
1160 C CE1 . PHE A 147 ? 0.58445 0.59544 0.60183 -0.01739 -0.04518 -0.03109 147 PHE A CE1 
1161 C CE2 . PHE A 147 ? 0.50407 0.49495 0.50437 0.00857  -0.04536 -0.02615 147 PHE A CE2 
1162 C CZ  . PHE A 147 ? 0.49281 0.47754 0.49435 -0.00754 -0.04343 -0.02752 147 PHE A CZ  
1163 N N   . ARG A 148 ? 0.51656 0.54148 0.51092 -0.00261 -0.07068 -0.05238 148 ARG A N   
1164 C CA  . ARG A 148 ? 0.65055 0.66360 0.64187 -0.02433 -0.07216 -0.06205 148 ARG A CA  
1165 C C   . ARG A 148 ? 0.58068 0.55231 0.55559 -0.03194 -0.06494 -0.05807 148 ARG A C   
1166 O O   . ARG A 148 ? 0.61486 0.55435 0.56671 -0.01995 -0.06604 -0.05681 148 ARG A O   
1167 C CB  . ARG A 148 ? 0.65673 0.65933 0.63162 -0.02775 -0.08166 -0.07525 148 ARG A CB  
1168 C CG  . ARG A 148 ? 0.78296 0.77353 0.75509 -0.05580 -0.08159 -0.08728 148 ARG A CG  
1169 C CD  . ARG A 148 ? 0.84416 0.82939 0.80280 -0.06165 -0.09187 -0.10327 148 ARG A CD  
1170 N NE  . ARG A 148 ? 0.80842 0.78341 0.76610 -0.09411 -0.08963 -0.11640 148 ARG A NE  
1171 C CZ  . ARG A 148 ? 0.79645 0.76401 0.74315 -0.10849 -0.09711 -0.13391 148 ARG A CZ  
1172 N NH1 . ARG A 148 ? 0.79170 0.76106 0.72618 -0.09058 -0.10857 -0.14032 148 ARG A NH1 
1173 N NH2 . ARG A 148 ? 0.71484 0.67285 0.66172 -0.14334 -0.09198 -0.14627 148 ARG A NH2 
1174 N N   . GLY A 149 ? 0.61503 0.58929 0.59990 -0.04978 -0.05762 -0.05677 149 GLY A N   
1175 C CA  . GLY A 149 ? 0.65919 0.59193 0.62392 -0.05632 -0.04971 -0.05159 149 GLY A CA  
1176 C C   . GLY A 149 ? 0.66875 0.61545 0.64870 -0.07734 -0.03990 -0.05040 149 GLY A C   
1177 O O   . GLY A 149 ? 0.68138 0.66146 0.68177 -0.09422 -0.03991 -0.05890 149 GLY A O   
1178 N N   . ASP A 150 ? 0.65779 0.58320 0.62802 -0.07518 -0.03165 -0.04126 150 ASP A N   
1179 C CA  . ASP A 150 ? 0.68377 0.62019 0.66474 -0.09426 -0.02022 -0.03943 150 ASP A CA  
1180 C C   . ASP A 150 ? 0.59987 0.58855 0.61612 -0.08435 -0.01842 -0.03513 150 ASP A C   
1181 O O   . ASP A 150 ? 0.61676 0.64034 0.65509 -0.09895 -0.01265 -0.03927 150 ASP A O   
1182 C CB  . ASP A 150 ? 0.68760 0.57110 0.63433 -0.09621 -0.01172 -0.03181 150 ASP A CB  
1183 C CG  . ASP A 150 ? 0.62694 0.45157 0.53291 -0.11305 -0.00943 -0.03641 150 ASP A CG  
1184 O OD1 . ASP A 150 ? 0.67283 0.49961 0.57991 -0.12430 -0.01496 -0.04685 150 ASP A OD1 
1185 O OD2 . ASP A 150 ? 0.66238 0.43506 0.53137 -0.11438 -0.00217 -0.02995 150 ASP A OD2 
1186 N N   . GLY A 151 ? 0.53215 0.52711 0.55300 -0.06029 -0.02261 -0.02825 151 GLY A N   
1187 C CA  . GLY A 151 ? 0.49043 0.52427 0.53752 -0.04995 -0.02068 -0.02415 151 GLY A CA  
1188 C C   . GLY A 151 ? 0.44957 0.47556 0.49336 -0.02868 -0.02228 -0.01679 151 GLY A C   
1189 O O   . GLY A 151 ? 0.47234 0.47162 0.49780 -0.02083 -0.02549 -0.01609 151 GLY A O   
1190 N N   . LEU A 152 ? 0.41727 0.46840 0.47868 -0.01954 -0.01968 -0.01288 152 LEU A N   
1191 C CA  . LEU A 152 ? 0.45860 0.50449 0.51899 -0.00397 -0.01884 -0.00725 152 LEU A CA  
1192 C C   . LEU A 152 ? 0.46754 0.51830 0.53521 -0.00227 -0.01156 -0.00364 152 LEU A C   
1193 O O   . LEU A 152 ? 0.44244 0.51331 0.52195 -0.00781 -0.00801 -0.00495 152 LEU A O   
1194 C CB  . LEU A 152 ? 0.44579 0.50836 0.51247 0.00788  -0.02289 -0.00594 152 LEU A CB  
1195 C CG  . LEU A 152 ? 0.44457 0.50429 0.50241 0.00932  -0.03011 -0.00963 152 LEU A CG  
1196 C CD1 . LEU A 152 ? 0.55031 0.62971 0.61184 0.02047  -0.03384 -0.00825 152 LEU A CD1 
1197 C CD2 . LEU A 152 ? 0.42665 0.46474 0.47055 0.01433  -0.02992 -0.00929 152 LEU A CD2 
1198 N N   . CYS A 153 ? 0.46564 0.50185 0.52705 0.00551  -0.00940 -0.00102 153 CYS A N   
1199 C CA  . CYS A 153 ? 0.40025 0.43681 0.46494 0.00809  -0.00322 0.00098  153 CYS A CA  
1200 C C   . CYS A 153 ? 0.44298 0.47836 0.51024 0.01818  -0.00205 0.00232  153 CYS A C   
1201 O O   . CYS A 153 ? 0.50827 0.53455 0.56959 0.02041  -0.00379 0.00046  153 CYS A O   
1202 C CB  . CYS A 153 ? 0.43333 0.44818 0.48219 0.00458  -0.00116 0.00038  153 CYS A CB  
1203 S SG  . CYS A 153 ? 0.47616 0.49000 0.52508 0.01006  0.00512  0.00116  153 CYS A SG  
1204 N N   . MET A 154 ? 0.43094 0.47519 0.50551 0.02387  0.00162  0.00436  154 MET A N   
1205 C CA  . MET A 154 ? 0.51778 0.55213 0.58953 0.03088  0.00499  0.00562  154 MET A CA  
1206 C C   . MET A 154 ? 0.47165 0.50067 0.54327 0.03217  0.00985  0.00368  154 MET A C   
1207 O O   . MET A 154 ? 0.45653 0.49574 0.53274 0.03574  0.01212  0.00427  154 MET A O   
1208 C CB  . MET A 154 ? 0.47776 0.51637 0.54870 0.04063  0.00475  0.00959  154 MET A CB  
1209 C CG  . MET A 154 ? 0.45829 0.47454 0.51766 0.04557  0.01028  0.01206  154 MET A CG  
1210 S SD  . MET A 154 ? 0.50171 0.50597 0.55359 0.03701  0.01237  0.01126  154 MET A SD  
1211 C CE  . MET A 154 ? 0.48548 0.49203 0.52751 0.04579  0.00864  0.01756  154 MET A CE  
1212 N N   . SER A 155 ? 0.50882 0.52632 0.57596 0.02989  0.01124  -0.00044 155 SER A N   
1213 C CA  . SER A 155 ? 0.50947 0.52270 0.57444 0.03083  0.01397  -0.00461 155 SER A CA  
1214 C C   . SER A 155 ? 0.53447 0.53571 0.59722 0.03221  0.01865  -0.00802 155 SER A C   
1215 O O   . SER A 155 ? 0.46838 0.46224 0.52943 0.02798  0.02051  -0.00921 155 SER A O   
1216 C CB  . SER A 155 ? 0.48627 0.49770 0.54522 0.02858  0.01010  -0.00984 155 SER A CB  
1217 O OG  . SER A 155 ? 0.47479 0.48297 0.52942 0.03137  0.01157  -0.01543 155 SER A OG  
1218 N N   . THR A 156 ? 0.52891 0.52630 0.58939 0.03677  0.02177  -0.01021 156 THR A N   
1219 C CA  . THR A 156 ? 0.46865 0.44968 0.52358 0.03614  0.02613  -0.01635 156 THR A CA  
1220 C C   . THR A 156 ? 0.44957 0.43524 0.50623 0.02875  0.02384  -0.02703 156 THR A C   
1221 O O   . THR A 156 ? 0.46202 0.46051 0.52035 0.02897  0.01833  -0.02821 156 THR A O   
1222 C CB  . THR A 156 ? 0.50932 0.48618 0.55977 0.04568  0.02912  -0.01704 156 THR A CB  
1223 O OG1 . THR A 156 ? 0.50425 0.49205 0.55501 0.04595  0.02746  -0.02139 156 THR A OG1 
1224 C CG2 . THR A 156 ? 0.50387 0.49091 0.55681 0.05600  0.02925  -0.00917 156 THR A CG2 
1225 N N   . PRO A 157 ? 0.48255 0.45766 0.53694 0.02262  0.02764  -0.03643 157 PRO A N   
1226 C CA  . PRO A 157 ? 0.43002 0.41938 0.48888 0.01742  0.02382  -0.05049 157 PRO A CA  
1227 C C   . PRO A 157 ? 0.52306 0.52120 0.57705 0.02757  0.01813  -0.05328 157 PRO A C   
1228 O O   . PRO A 157 ? 0.40544 0.41794 0.45846 0.03138  0.01117  -0.05728 157 PRO A O   
1229 C CB  . PRO A 157 ? 0.49358 0.46777 0.55014 0.00650  0.03068  -0.06104 157 PRO A CB  
1230 C CG  . PRO A 157 ? 0.64151 0.59089 0.69024 0.00293  0.03858  -0.05053 157 PRO A CG  
1231 C CD  . PRO A 157 ? 0.54822 0.49716 0.59390 0.01824  0.03561  -0.03587 157 PRO A CD  
1232 N N   . SER A 158 ? 0.47290 0.46070 0.51983 0.03408  0.02125  -0.05124 158 SER A N   
1233 C CA  . SER A 158 ? 0.55390 0.54770 0.59182 0.04327  0.01805  -0.05297 158 SER A CA  
1234 C C   . SER A 158 ? 0.49682 0.49530 0.53020 0.04709  0.01666  -0.04131 158 SER A C   
1235 O O   . SER A 158 ? 0.51949 0.51815 0.53936 0.05319  0.01451  -0.04155 158 SER A O   
1236 C CB  . SER A 158 ? 0.52709 0.51066 0.55817 0.04952  0.02323  -0.05408 158 SER A CB  
1237 O OG  . SER A 158 ? 0.54267 0.52241 0.57610 0.05330  0.02846  -0.04279 158 SER A OG  
1238 N N   . GLY A 159 ? 0.48404 0.48338 0.52496 0.04307  0.01828  -0.03169 159 GLY A N   
1239 C CA  . GLY A 159 ? 0.45953 0.46149 0.49608 0.04235  0.01727  -0.02305 159 GLY A CA  
1240 C C   . GLY A 159 ? 0.50921 0.51009 0.54036 0.04167  0.01032  -0.02482 159 GLY A C   
1241 O O   . GLY A 159 ? 0.51705 0.51150 0.53777 0.04090  0.00944  -0.01866 159 GLY A O   
1242 N N   . THR A 160 ? 0.43984 0.44691 0.47658 0.04154  0.00602  -0.03439 160 THR A N   
1243 C CA  . THR A 160 ? 0.44777 0.45945 0.48054 0.04441  -0.00121 -0.03816 160 THR A CA  
1244 C C   . THR A 160 ? 0.51012 0.51428 0.52039 0.05626  -0.00744 -0.04085 160 THR A C   
1245 O O   . THR A 160 ? 0.47274 0.47098 0.47071 0.06236  -0.01331 -0.04026 160 THR A O   
1246 C CB  . THR A 160 ? 0.44789 0.47645 0.49467 0.04035  -0.00274 -0.05050 160 THR A CB  
1247 O OG1 . THR A 160 ? 0.44649 0.48116 0.49552 0.04022  -0.00225 -0.06205 160 THR A OG1 
1248 C CG2 . THR A 160 ? 0.43192 0.45864 0.49128 0.02947  0.00413  -0.04499 160 THR A CG2 
1249 N N   . THR A 161 ? 0.52388 0.52449 0.52382 0.06181  -0.00649 -0.04385 161 THR A N   
1250 C CA  . THR A 161 ? 0.51338 0.49967 0.48351 0.07517  -0.01132 -0.04386 161 THR A CA  
1251 C C   . THR A 161 ? 0.51994 0.48068 0.46990 0.07120  -0.00430 -0.02891 161 THR A C   
1252 O O   . THR A 161 ? 0.57627 0.51445 0.49322 0.08077  -0.00577 -0.02598 161 THR A O   
1253 C CB  . THR A 161 ? 0.55259 0.54492 0.51577 0.08338  -0.01291 -0.05353 161 THR A CB  
1254 O OG1 . THR A 161 ? 0.56836 0.56145 0.54386 0.07427  -0.00338 -0.04996 161 THR A OG1 
1255 C CG2 . THR A 161 ? 0.51531 0.53473 0.49331 0.08737  -0.02165 -0.07254 161 THR A CG2 
1256 N N   . ALA A 162 ? 0.54309 0.50674 0.50980 0.05722  0.00362  -0.02038 162 ALA A N   
1257 C CA  . ALA A 162 ? 0.53412 0.48175 0.48721 0.04839  0.01199  -0.00926 162 ALA A CA  
1258 C C   . ALA A 162 ? 0.52428 0.46083 0.47440 0.04119  0.00992  -0.00458 162 ALA A C   
1259 O O   . ALA A 162 ? 0.57452 0.49400 0.50510 0.05006  0.00215  -0.00682 162 ALA A O   
1260 C CB  . ALA A 162 ? 0.54652 0.51231 0.52061 0.03925  0.02169  -0.00605 162 ALA A CB  
1261 N N   . TYR A 163 ? 0.53671 0.48446 0.50502 0.02711  0.01592  0.00029  163 TYR A N   
1262 C CA  . TYR A 163 ? 0.56236 0.50075 0.52816 0.01827  0.01408  0.00316  163 TYR A CA  
1263 C C   . TYR A 163 ? 0.50724 0.44943 0.47949 0.02695  0.00356  -0.00211 163 TYR A C   
1264 O O   . TYR A 163 ? 0.50450 0.42658 0.45852 0.02920  -0.00153 -0.00235 163 TYR A O   
1265 C CB  . TYR A 163 ? 0.59684 0.55881 0.58731 0.00398  0.02030  0.00554  163 TYR A CB  
1266 C CG  . TYR A 163 ? 0.58631 0.53780 0.56996 -0.01107 0.02194  0.00751  163 TYR A CG  
1267 C CD1 . TYR A 163 ? 0.57904 0.49395 0.53280 -0.01051 0.01787  0.00826  163 TYR A CD1 
1268 C CD2 . TYR A 163 ? 0.63831 0.61708 0.64412 -0.02483 0.02693  0.00673  163 TYR A CD2 
1269 C CE1 . TYR A 163 ? 0.62066 0.52046 0.56516 -0.02626 0.01979  0.00863  163 TYR A CE1 
1270 C CE2 . TYR A 163 ? 0.71371 0.68587 0.71496 -0.04161 0.02834  0.00559  163 TYR A CE2 
1271 C CZ  . TYR A 163 ? 0.64961 0.57927 0.61939 -0.04380 0.02529  0.00677  163 TYR A CZ  
1272 O OH  . TYR A 163 ? 0.56504 0.48239 0.52707 -0.06236 0.02706  0.00432  163 TYR A OH  
1273 N N   . ASN A 164 ? 0.50467 0.47050 0.50016 0.03139  0.00136  -0.00692 164 ASN A N   
1274 C CA  . ASN A 164 ? 0.46503 0.43975 0.46836 0.03697  -0.00573 -0.01297 164 ASN A CA  
1275 C C   . ASN A 164 ? 0.52410 0.48668 0.50538 0.05040  -0.01373 -0.01934 164 ASN A C   
1276 O O   . ASN A 164 ? 0.48890 0.45071 0.46616 0.05548  -0.01982 -0.02288 164 ASN A O   
1277 C CB  . ASN A 164 ? 0.45584 0.45100 0.48067 0.03684  -0.00364 -0.01784 164 ASN A CB  
1278 C CG  . ASN A 164 ? 0.40435 0.41231 0.43654 0.03997  -0.00817 -0.02639 164 ASN A CG  
1279 O OD1 . ASN A 164 ? 0.42831 0.44282 0.47014 0.03529  -0.00719 -0.02464 164 ASN A OD1 
1280 N ND2 . ASN A 164 ? 0.38017 0.39554 0.40781 0.04822  -0.01283 -0.03697 164 ASN A ND2 
1281 N N   . LYS A 165 ? 0.53703 0.49083 0.50136 0.05922  -0.01451 -0.02168 165 LYS A N   
1282 C CA  . LYS A 165 ? 0.48797 0.43254 0.42804 0.07775  -0.02409 -0.02927 165 LYS A CA  
1283 C C   . LYS A 165 ? 0.50601 0.41350 0.41236 0.08248  -0.02682 -0.02336 165 LYS A C   
1284 O O   . LYS A 165 ? 0.49160 0.39538 0.38482 0.09750  -0.03618 -0.03006 165 LYS A O   
1285 C CB  . LYS A 165 ? 0.55533 0.49671 0.48013 0.08794  -0.02476 -0.03275 165 LYS A CB  
1286 C CG  . LYS A 165 ? 0.50069 0.43521 0.39703 0.11228  -0.03662 -0.04204 165 LYS A CG  
1287 C CD  . LYS A 165 ? 0.52844 0.46568 0.41152 0.12355  -0.03849 -0.04748 165 LYS A CD  
1288 C CE  . LYS A 165 ? 0.58751 0.52333 0.44139 0.15258  -0.05280 -0.05896 165 LYS A CE  
1289 N NZ  . LYS A 165 ? 0.62111 0.50781 0.42811 0.16534  -0.05535 -0.04918 165 LYS A NZ  
1290 N N   . SER A 166 ? 0.50102 0.38054 0.39172 0.06929  -0.01808 -0.01215 166 SER A N   
1291 C CA  . SER A 166 ? 0.59375 0.42886 0.44712 0.06932  -0.01844 -0.00673 166 SER A CA  
1292 C C   . SER A 166 ? 0.58840 0.42735 0.45335 0.06420  -0.02256 -0.00887 166 SER A C   
1293 O O   . SER A 166 ? 0.59000 0.39128 0.42192 0.06929  -0.02617 -0.00809 166 SER A O   
1294 C CB  . SER A 166 ? 0.59761 0.40658 0.43509 0.04977  -0.00502 0.00397  166 SER A CB  
1295 O OG  . SER A 166 ? 0.67453 0.47403 0.49287 0.05660  -0.00060 0.00650  166 SER A OG  
1296 N N   . LEU A 167 ? 0.53342 0.45758 0.54899 0.00592  0.06351  0.02883  167 LEU A N   
1297 C CA  . LEU A 167 ? 0.55062 0.46996 0.56650 0.01219  0.05541  0.02288  167 LEU A CA  
1298 C C   . LEU A 167 ? 0.54219 0.46966 0.55120 0.03218  0.05222  0.02159  167 LEU A C   
1299 O O   . LEU A 167 ? 0.55814 0.48861 0.56679 0.03991  0.04792  0.01677  167 LEU A O   
1300 C CB  . LEU A 167 ? 0.41987 0.36338 0.46153 0.00397  0.05521  0.01824  167 LEU A CB  
1301 C CG  . LEU A 167 ? 0.46130 0.40799 0.51720 -0.01559 0.05848  0.01882  167 LEU A CG  
1302 C CD1 . LEU A 167 ? 0.42951 0.40855 0.51452 -0.01842 0.05809  0.01439  167 LEU A CD1 
1303 C CD2 . LEU A 167 ? 0.50217 0.41681 0.54353 -0.02580 0.05078  0.01758  167 LEU A CD2 
1304 N N   . GLY A 168 ? 0.54240 0.47679 0.54606 0.04051  0.05423  0.02592  168 GLY A N   
1305 C CA  . GLY A 168 ? 0.44213 0.39355 0.44494 0.05797  0.05199  0.02570  168 GLY A CA  
1306 C C   . GLY A 168 ? 0.51330 0.50110 0.53884 0.05558  0.05517  0.02618  168 GLY A C   
1307 O O   . GLY A 168 ? 0.45750 0.46665 0.48701 0.06656  0.05469  0.02728  168 GLY A O   
1308 N N   . GLY A 169 ? 0.38106 0.37646 0.42132 0.04180  0.05850  0.02573  169 GLY A N   
1309 C CA  . GLY A 169 ? 0.37029 0.38973 0.42710 0.03867  0.06002  0.02655  169 GLY A CA  
1310 C C   . GLY A 169 ? 0.53032 0.56443 0.58982 0.03873  0.05931  0.02930  169 GLY A C   
1311 O O   . GLY A 169 ? 0.44761 0.47421 0.49623 0.04098  0.05780  0.03031  169 GLY A O   
1312 N N   . ALA A 170 ? 0.43865 0.49257 0.51114 0.03497  0.05919  0.03110  170 ALA A N   
1313 C CA  . ALA A 170 ? 0.47734 0.54757 0.55556 0.03092  0.05605  0.03295  170 ALA A CA  
1314 C C   . ALA A 170 ? 0.48329 0.54135 0.55988 0.02047  0.05553  0.02952  170 ALA A C   
1315 O O   . ALA A 170 ? 0.44482 0.49038 0.52291 0.01654  0.05885  0.02679  170 ALA A O   
1316 C CB  . ALA A 170 ? 0.42305 0.51882 0.51576 0.02722  0.05629  0.03749  170 ALA A CB  
1317 N N   . LEU A 171 ? 0.38773 0.45080 0.46013 0.01810  0.05046  0.02876  171 LEU A N   
1318 C CA  . LEU A 171 ? 0.44379 0.49407 0.50935 0.01013  0.04900  0.02368  171 LEU A CA  
1319 C C   . LEU A 171 ? 0.37768 0.43380 0.45410 -0.00103 0.04421  0.02340  171 LEU A C   
1320 O O   . LEU A 171 ? 0.50518 0.58310 0.59221 -0.00584 0.03853  0.02725  171 LEU A O   
1321 C CB  . LEU A 171 ? 0.42600 0.47401 0.47517 0.01299  0.04389  0.02226  171 LEU A CB  
1322 C CG  . LEU A 171 ? 0.45285 0.48954 0.48577 0.02292  0.04728  0.02543  171 LEU A CG  
1323 C CD1 . LEU A 171 ? 0.42321 0.45203 0.43344 0.02519  0.04222  0.02473  171 LEU A CD1 
1324 C CD2 . LEU A 171 ? 0.44714 0.46686 0.47786 0.02121  0.05775  0.02481  171 LEU A CD2 
1325 N N   . MET A 172 ? 0.40380 0.44077 0.47795 -0.00514 0.04633  0.01933  172 MET A N   
1326 C CA  . MET A 172 ? 0.44532 0.47579 0.52465 -0.01610 0.04156  0.02008  172 MET A CA  
1327 C C   . MET A 172 ? 0.47946 0.48695 0.54388 -0.02101 0.03575  0.01100  172 MET A C   
1328 O O   . MET A 172 ? 0.51016 0.50228 0.56197 -0.01249 0.04052  0.00371  172 MET A O   
1329 C CB  . MET A 172 ? 0.52849 0.54837 0.61238 -0.01332 0.04636  0.02280  172 MET A CB  
1330 C CG  . MET A 172 ? 0.61582 0.65371 0.70877 -0.00793 0.05105  0.03012  172 MET A CG  
1331 S SD  . MET A 172 ? 0.65344 0.67684 0.74688 -0.00566 0.05262  0.03366  172 MET A SD  
1332 C CE  . MET A 172 ? 0.48213 0.48804 0.57179 -0.02103 0.04628  0.03758  172 MET A CE  
1333 N N   . HIS A 173 ? 0.52055 0.52637 0.58584 -0.03525 0.02565  0.01107  173 HIS A N   
1334 C CA  . HIS A 173 ? 0.58683 0.56329 0.63309 -0.04038 0.01764  0.00052  173 HIS A CA  
1335 C C   . HIS A 173 ? 0.60199 0.54486 0.63941 -0.03507 0.02110  -0.00365 173 HIS A C   
1336 O O   . HIS A 173 ? 0.62383 0.56336 0.67117 -0.03819 0.02279  0.00428  173 HIS A O   
1337 C CB  . HIS A 173 ? 0.52972 0.50977 0.58003 -0.06082 0.00346  0.00151  173 HIS A CB  
1338 C CG  . HIS A 173 ? 0.69348 0.63989 0.71896 -0.06639 -0.00805 -0.01174 173 HIS A CG  
1339 N ND1 . HIS A 173 ? 0.67230 0.57548 0.68278 -0.07170 -0.01261 -0.01744 173 HIS A ND1 
1340 C CD2 . HIS A 173 ? 0.58526 0.53070 0.59337 -0.06557 -0.01694 -0.02126 173 HIS A CD2 
1341 C CE1 . HIS A 173 ? 0.72072 0.59675 0.70544 -0.07395 -0.02365 -0.03134 173 HIS A CE1 
1342 N NE2 . HIS A 173 ? 0.66262 0.56516 0.64525 -0.07080 -0.02645 -0.03384 173 HIS A NE2 
1343 N N   . PRO A 174 ? 0.64910 0.56732 0.66592 -0.02475 0.02233  -0.01591 174 PRO A N   
1344 C CA  . PRO A 174 ? 0.62233 0.51437 0.63285 -0.01274 0.02676  -0.02074 174 PRO A CA  
1345 C C   . PRO A 174 ? 0.62294 0.47779 0.62428 -0.02201 0.01610  -0.02086 174 PRO A C   
1346 O O   . PRO A 174 ? 0.66096 0.49276 0.65735 -0.00985 0.01809  -0.02280 174 PRO A O   
1347 C CB  . PRO A 174 ? 0.72245 0.60379 0.71207 0.00174  0.03200  -0.03465 174 PRO A CB  
1348 C CG  . PRO A 174 ? 0.66162 0.56858 0.64951 -0.00120 0.03427  -0.03281 174 PRO A CG  
1349 C CD  . PRO A 174 ? 0.53441 0.45297 0.53239 -0.01914 0.02218  -0.02517 174 PRO A CD  
1350 N N   . SER A 175 ? 0.60648 0.45399 0.60527 -0.04342 0.00396  -0.01837 175 SER A N   
1351 C CA  . SER A 175 ? 0.64857 0.45666 0.63799 -0.05679 -0.00606 -0.01536 175 SER A CA  
1352 C C   . SER A 175 ? 0.71380 0.53277 0.72069 -0.06180 -0.00101 0.00177  175 SER A C   
1353 O O   . SER A 175 ? 0.74025 0.52207 0.73620 -0.07050 -0.00728 0.00723  175 SER A O   
1354 C CB  . SER A 175 ? 0.65845 0.45848 0.64286 -0.08330 -0.02137 -0.01680 175 SER A CB  
1355 O OG  . SER A 175 ? 0.65094 0.50198 0.66339 -0.09841 -0.02027 -0.00468 175 SER A OG  
1356 N N   . ILE A 176 ? 0.65402 0.51802 0.68287 -0.05603 0.00953  0.01025  176 ILE A N   
1357 C CA  . ILE A 176 ? 0.66927 0.54624 0.71052 -0.05805 0.01512  0.02534  176 ILE A CA  
1358 C C   . ILE A 176 ? 0.65095 0.51340 0.68697 -0.03535 0.02019  0.02288  176 ILE A C   
1359 O O   . ILE A 176 ? 0.61371 0.49502 0.65604 -0.01866 0.02704  0.01558  176 ILE A O   
1360 C CB  . ILE A 176 ? 0.61090 0.54034 0.67427 -0.06007 0.02263  0.03324  176 ILE A CB  
1361 C CG1 . ILE A 176 ? 0.61054 0.56239 0.68265 -0.07789 0.01621  0.03328  176 ILE A CG1 
1362 C CG2 . ILE A 176 ? 0.65250 0.59432 0.72342 -0.06277 0.02850  0.04824  176 ILE A CG2 
1363 C CD1 . ILE A 176 ? 0.51246 0.51487 0.60397 -0.07342 0.02244  0.03809  176 ILE A CD1 
1364 N N   . GLU A 177 ? 0.57753 0.40704 0.60210 -0.03544 0.01606  0.02977  177 GLU A N   
1365 C CA  . GLU A 177 ? 0.64465 0.46271 0.66553 -0.01262 0.01791  0.02840  177 GLU A CA  
1366 C C   . GLU A 177 ? 0.62994 0.48335 0.66580 -0.00962 0.02469  0.03934  177 GLU A C   
1367 O O   . GLU A 177 ? 0.60362 0.44942 0.63360 -0.01658 0.02358  0.05310  177 GLU A O   
1368 C CB  . GLU A 177 ? 0.74077 0.50343 0.73794 -0.01110 0.00840  0.03168  177 GLU A CB  
1369 C CG  . GLU A 177 ? 0.74566 0.46569 0.72236 -0.00552 0.00087  0.01637  177 GLU A CG  
1370 C CD  . GLU A 177 ? 0.90737 0.56262 0.85540 -0.00413 -0.01048 0.01998  177 GLU A CD  
1371 O OE1 . GLU A 177 ? 0.89524 0.53101 0.83549 -0.02715 -0.01500 0.03591  177 GLU A OE1 
1372 O OE2 . GLU A 177 ? 0.98741 0.61079 0.91958 0.02070  -0.01439 0.00746  177 GLU A OE2 
1373 N N   . ALA A 178 ? 0.56597 0.45515 0.61762 0.00050  0.03165  0.03321  178 ALA A N   
1374 C CA  . ALA A 178 ? 0.48349 0.40355 0.54615 0.00295  0.03672  0.04062  178 ALA A CA  
1375 C C   . ALA A 178 ? 0.48711 0.42939 0.56224 0.01759  0.04091  0.03128  178 ALA A C   
1376 O O   . ALA A 178 ? 0.53061 0.47090 0.60801 0.02463  0.04254  0.02064  178 ALA A O   
1377 C CB  . ALA A 178 ? 0.43870 0.38518 0.50849 -0.01221 0.04093  0.04765  178 ALA A CB  
1378 N N   . MET A 179 ? 0.43980 0.40296 0.52137 0.02108  0.04288  0.03550  179 MET A N   
1379 C CA  . MET A 179 ? 0.42955 0.41431 0.52353 0.02893  0.04589  0.02848  179 MET A CA  
1380 C C   . MET A 179 ? 0.40631 0.40949 0.50093 0.02462  0.04886  0.03270  179 MET A C   
1381 O O   . MET A 179 ? 0.48406 0.48800 0.57085 0.02102  0.04873  0.04129  179 MET A O   
1382 C CB  . MET A 179 ? 0.49053 0.47592 0.59001 0.04220  0.04071  0.02590  179 MET A CB  
1383 C CG  . MET A 179 ? 0.48816 0.46684 0.57697 0.04515  0.03438  0.03502  179 MET A CG  
1384 S SD  . MET A 179 ? 0.56430 0.54587 0.65962 0.06299  0.02410  0.03137  179 MET A SD  
1385 C CE  . MET A 179 ? 0.53877 0.50813 0.61086 0.06407  0.01733  0.04425  179 MET A CE  
1386 N N   . GLN A 180 ? 0.39548 0.41190 0.49713 0.02558  0.05218  0.02694  180 GLN A N   
1387 C CA  . GLN A 180 ? 0.38736 0.41440 0.48550 0.02454  0.05413  0.02897  180 GLN A CA  
1388 C C   . GLN A 180 ? 0.50219 0.53316 0.60389 0.02856  0.05183  0.02395  180 GLN A C   
1389 O O   . GLN A 180 ? 0.38530 0.41920 0.49686 0.02708  0.05320  0.01851  180 GLN A O   
1390 C CB  . GLN A 180 ? 0.39412 0.42580 0.49119 0.02001  0.05819  0.02814  180 GLN A CB  
1391 C CG  . GLN A 180 ? 0.36067 0.40126 0.45191 0.02334  0.05940  0.03035  180 GLN A CG  
1392 C CD  . GLN A 180 ? 0.44367 0.48939 0.53304 0.02201  0.06101  0.03023  180 GLN A CD  
1393 O OE1 . GLN A 180 ? 0.40699 0.45867 0.49082 0.02831  0.06134  0.03124  180 GLN A OE1 
1394 N NE2 . GLN A 180 ? 0.47807 0.51983 0.56912 0.01614  0.06088  0.02825  180 GLN A NE2 
1395 N N   . LEU A 181 ? 0.39355 0.42519 0.48619 0.03257  0.04852  0.02564  181 LEU A N   
1396 C CA  . LEU A 181 ? 0.41112 0.44208 0.50339 0.03445  0.04305  0.01991  181 LEU A CA  
1397 C C   . LEU A 181 ? 0.39606 0.42128 0.47705 0.03478  0.04499  0.01793  181 LEU A C   
1398 O O   . LEU A 181 ? 0.42362 0.45032 0.49283 0.04021  0.04820  0.02148  181 LEU A O   
1399 C CB  . LEU A 181 ? 0.41813 0.44749 0.50087 0.04111  0.03519  0.02108  181 LEU A CB  
1400 C CG  . LEU A 181 ? 0.40944 0.43668 0.48955 0.04190  0.02569  0.01351  181 LEU A CG  
1401 C CD1 . LEU A 181 ? 0.31622 0.35453 0.42012 0.03698  0.02045  0.00836  181 LEU A CD1 
1402 C CD2 . LEU A 181 ? 0.44904 0.47157 0.50865 0.05074  0.01825  0.01485  181 LEU A CD2 
1403 N N   . THR A 182 ? 0.32572 0.34461 0.41019 0.02926  0.04317  0.01278  182 THR A N   
1404 C CA  . THR A 182 ? 0.37913 0.38239 0.44810 0.03033  0.04289  0.01075  182 THR A CA  
1405 C C   . THR A 182 ? 0.41035 0.40039 0.47503 0.02551  0.03372  0.00410  182 THR A C   
1406 O O   . THR A 182 ? 0.39699 0.39708 0.47898 0.01721  0.02934  0.00150  182 THR A O   
1407 C CB  . THR A 182 ? 0.44619 0.44492 0.51667 0.02468  0.04949  0.01313  182 THR A CB  
1408 O OG1 . THR A 182 ? 0.38670 0.39241 0.47413 0.01351  0.05207  0.01213  182 THR A OG1 
1409 C CG2 . THR A 182 ? 0.41677 0.42669 0.48793 0.02923  0.05509  0.01809  182 THR A CG2 
1410 N N   . GLU A 183 ? 0.49263 0.46042 0.53417 0.03137  0.02975  0.00060  183 GLU A N   
1411 C CA  . GLU A 183 ? 0.49000 0.43667 0.52110 0.02563  0.01843  -0.00719 183 GLU A CA  
1412 C C   . GLU A 183 ? 0.57873 0.50371 0.60809 0.01182  0.01883  -0.00683 183 GLU A C   
1413 O O   . GLU A 183 ? 0.53304 0.45096 0.55675 0.01380  0.02695  -0.00123 183 GLU A O   
1414 C CB  . GLU A 183 ? 0.54366 0.47026 0.54311 0.04177  0.01274  -0.01300 183 GLU A CB  
1415 C CG  . GLU A 183 ? 0.53494 0.48169 0.52953 0.05578  0.01556  -0.01068 183 GLU A CG  
1416 C CD  . GLU A 183 ? 0.60840 0.53841 0.56899 0.07400  0.01299  -0.01684 183 GLU A CD  
1417 O OE1 . GLU A 183 ? 0.61240 0.51290 0.55289 0.07903  0.00953  -0.02304 183 GLU A OE1 
1418 O OE2 . GLU A 183 ? 0.60784 0.55175 0.55854 0.08445  0.01481  -0.01528 183 GLU A OE2 
1419 N N   . MET A 184 ? 0.58732 0.50151 0.62052 -0.00354 0.00900  -0.01213 184 MET A N   
1420 C CA  . MET A 184 ? 0.53755 0.42438 0.56468 -0.02099 0.00784  -0.01091 184 MET A CA  
1421 C C   . MET A 184 ? 0.54003 0.38426 0.53715 -0.02115 -0.00741 -0.02027 184 MET A C   
1422 O O   . MET A 184 ? 0.68674 0.53366 0.69053 -0.03136 -0.02039 -0.02796 184 MET A O   
1423 C CB  . MET A 184 ? 0.51699 0.43072 0.57857 -0.04462 0.01019  -0.00826 184 MET A CB  
1424 C CG  . MET A 184 ? 0.46671 0.42067 0.55555 -0.04225 0.02430  -0.00186 184 MET A CG  
1425 S SD  . MET A 184 ? 0.58251 0.57431 0.71266 -0.06618 0.02826  -0.00040 184 MET A SD  
1426 C CE  . MET A 184 ? 0.54021 0.56978 0.69037 -0.05288 0.04405  0.00377  184 MET A CE  
1427 N N   . ALA A 185 ? 0.51581 0.32002 0.47850 -0.00822 -0.00738 -0.02058 185 ALA A N   
1428 C CA  . ALA A 185 ? 0.65102 0.40206 0.57684 -0.00603 -0.02177 -0.03030 185 ALA A CA  
1429 C C   . ALA A 185 ? 0.78958 0.54421 0.70653 0.00249  -0.03460 -0.04289 185 ALA A C   
1430 O O   . ALA A 185 ? 0.68039 0.42731 0.60146 -0.01567 -0.04904 -0.05033 185 ALA A O   
1431 C CB  . ALA A 185 ? 0.60964 0.32873 0.53520 -0.03657 -0.02835 -0.02832 185 ALA A CB  
1432 N N   . SER A 186 ? 0.73385 0.50244 0.63785 0.03003  -0.02919 -0.04463 186 SER A N   
1433 C CA  . SER A 186 ? 0.68534 0.45843 0.57451 0.04188  -0.03865 -0.05476 186 SER A CA  
1434 C C   . SER A 186 ? 0.70374 0.42141 0.54471 0.05398  -0.05202 -0.06897 186 SER A C   
1435 O O   . SER A 186 ? 0.71990 0.40591 0.53383 0.07085  -0.04796 -0.06991 186 SER A O   
1436 C CB  . SER A 186 ? 0.64992 0.46103 0.54268 0.06433  -0.02530 -0.04903 186 SER A CB  
1437 O OG  . SER A 186 ? 0.94944 0.75850 0.81712 0.07913  -0.03262 -0.05785 186 SER A OG  
1438 N N   . ILE A 187 ? 0.80765 0.51208 0.63601 0.04692  -0.06965 -0.08100 187 ILE A N   
1439 C CA  . ILE A 187 ? 0.87627 0.52815 0.65238 0.06273  -0.08373 -0.09759 187 ILE A CA  
1440 C C   . ILE A 187 ? 0.81052 0.48175 0.56327 0.09722  -0.07414 -0.10026 187 ILE A C   
1441 O O   . ILE A 187 ? 0.88518 0.59928 0.65355 0.09927  -0.07067 -0.09600 187 ILE A O   
1442 C CB  . ILE A 187 ? 0.93482 0.56641 0.70449 0.04100  -0.10855 -0.11064 187 ILE A CB  
1443 C CG1 . ILE A 187 ? 0.93284 0.56477 0.73896 0.00168  -0.11464 -0.10451 187 ILE A CG1 
1444 C CG2 . ILE A 187 ? 0.98147 0.54564 0.69063 0.05550  -0.12528 -0.12987 187 ILE A CG2 
1445 C CD1 . ILE A 187 ? 0.92653 0.53565 0.72765 -0.02383 -0.14156 -0.11804 187 ILE A CD1 
1446 N N   . ASN A 188 ? 0.91192 0.55255 0.62669 0.12518  -0.06911 -0.10632 188 ASN A N   
1447 C CA  . ASN A 188 ? 1.05604 0.71691 0.74626 0.15922  -0.05790 -0.10937 188 ASN A CA  
1448 C C   . ASN A 188 ? 1.10102 0.70246 0.73099 0.18433  -0.06868 -0.12890 188 ASN A C   
1449 O O   . ASN A 188 ? 1.17543 0.74111 0.78642 0.19885  -0.06693 -0.13169 188 ASN A O   
1450 C CB  . ASN A 188 ? 0.93360 0.63829 0.64841 0.17405  -0.03432 -0.09429 188 ASN A CB  
1451 C CG  . ASN A 188 ? 0.87366 0.64026 0.63306 0.16008  -0.02241 -0.07839 188 ASN A CG  
1452 O OD1 . ASN A 188 ? 0.87103 0.66898 0.62527 0.17208  -0.01454 -0.07571 188 ASN A OD1 
1453 N ND2 . ASN A 188 ? 0.73994 0.52090 0.53939 0.13511  -0.02088 -0.06764 188 ASN A ND2 
1454 N N   . ASN A 189 ? 1.13052 0.71796 0.72680 0.19108  -0.08125 -0.14302 189 ASN A N   
1455 C CA  . ASN A 189 ? 1.18517 0.71746 0.71703 0.21990  -0.09092 -0.16415 189 ASN A CA  
1456 C C   . ASN A 189 ? 1.38510 0.93899 0.88650 0.24052  -0.08904 -0.17165 189 ASN A C   
1457 O O   . ASN A 189 ? 1.39320 1.00918 0.92157 0.24234  -0.07197 -0.15671 189 ASN A O   
1458 C CB  . ASN A 189 ? 1.20244 0.66080 0.70799 0.19857  -0.11945 -0.18006 189 ASN A CB  
1459 C CG  . ASN A 189 ? 1.25801 0.72997 0.78973 0.16091  -0.13801 -0.18013 189 ASN A CG  
1460 O OD1 . ASN A 189 ? 1.26878 0.79450 0.82168 0.15911  -0.13317 -0.17315 189 ASN A OD1 
1461 N ND2 . ASN A 189 ? 1.24109 0.66517 0.77208 0.13038  -0.15975 -0.18717 189 ASN A ND2 
1462 N N   . ARG A 190 ? 1.33308 0.83210 0.77459 0.25516  -0.10719 -0.19449 190 ARG A N   
1463 C CA  . ARG A 190 ? 1.35034 0.86546 0.75333 0.27781  -0.10512 -0.20242 190 ARG A CA  
1464 C C   . ARG A 190 ? 1.36691 0.91917 0.79643 0.25116  -0.11455 -0.19390 190 ARG A C   
1465 O O   . ARG A 190 ? 1.54121 1.13546 0.96313 0.26517  -0.10175 -0.18627 190 ARG A O   
1466 C CB  . ARG A 190 ? 1.49446 0.93886 0.82644 0.29750  -0.12522 -0.22929 190 ARG A CB  
1467 N N   . VAL A 191 ? 1.45192 0.99244 0.91357 0.21360  -0.13569 -0.19353 191 VAL A N   
1468 C CA  . VAL A 191 ? 1.37679 0.95144 0.86376 0.19102  -0.14859 -0.18763 191 VAL A CA  
1469 C C   . VAL A 191 ? 1.27756 0.91794 0.82976 0.17661  -0.12885 -0.16165 191 VAL A C   
1470 O O   . VAL A 191 ? 1.20098 0.88192 0.76119 0.17965  -0.12367 -0.15114 191 VAL A O   
1471 C CB  . VAL A 191 ? 1.42180 0.95868 0.91448 0.15786  -0.18204 -0.20117 191 VAL A CB  
1472 C CG1 . VAL A 191 ? 1.44300 1.02714 0.97843 0.13312  -0.19453 -0.19227 191 VAL A CG1 
1473 C CG2 . VAL A 191 ? 1.41068 0.88134 0.83182 0.17123  -0.20652 -0.22883 191 VAL A CG2 
1474 N N   . TYR A 192 ? 1.24872 0.89628 0.84392 0.16141  -0.11834 -0.15091 192 TYR A N   
1475 C CA  . TYR A 192 ? 1.21763 0.92026 0.87285 0.14538  -0.10304 -0.12912 192 TYR A CA  
1476 C C   . TYR A 192 ? 1.15712 0.88685 0.82316 0.16372  -0.07391 -0.11532 192 TYR A C   
1477 O O   . TYR A 192 ? 1.08770 0.79227 0.72962 0.18246  -0.06658 -0.12143 192 TYR A O   
1478 C CB  . TYR A 192 ? 1.22448 0.92296 0.92392 0.11143  -0.11298 -0.12613 192 TYR A CB  
1479 C CG  . TYR A 192 ? 1.30168 0.99874 1.01059 0.08828  -0.13967 -0.13465 192 TYR A CG  
1480 C CD1 . TYR A 192 ? 1.19825 0.94346 0.93931 0.08109  -0.14199 -0.12520 192 TYR A CD1 
1481 C CD2 . TYR A 192 ? 1.28480 0.93175 0.96981 0.07409  -0.16422 -0.15241 192 TYR A CD2 
1482 C CE1 . TYR A 192 ? 1.10163 0.85284 0.85494 0.06245  -0.16791 -0.13318 192 TYR A CE1 
1483 C CE2 . TYR A 192 ? 1.28988 0.94230 0.98803 0.05092  -0.19063 -0.16059 192 TYR A CE2 
1484 C CZ  . TYR A 192 ? 1.20656 0.91512 0.94082 0.04634  -0.19228 -0.15092 192 TYR A CZ  
1485 O OH  . TYR A 192 ? 1.18183 0.90317 0.93307 0.02570  -0.21990 -0.15908 192 TYR A OH  
1486 N N   . ARG A 193 ? 0.96404 0.74479 0.66681 0.15830  -0.05897 -0.09699 193 ARG A N   
1487 C CA  . ARG A 193 ? 0.85502 0.66928 0.56954 0.17312  -0.03278 -0.08318 193 ARG A CA  
1488 C C   . ARG A 193 ? 0.89921 0.75578 0.66475 0.15395  -0.02345 -0.06443 193 ARG A C   
1489 O O   . ARG A 193 ? 0.80628 0.68154 0.57824 0.14767  -0.02737 -0.05802 193 ARG A O   
1490 C CB  . ARG A 193 ? 0.96795 0.79485 0.64299 0.20002  -0.02181 -0.08382 193 ARG A CB  
1491 C CG  . ARG A 193 ? 1.02221 0.87804 0.69964 0.22030  0.00359  -0.07544 193 ARG A CG  
1492 C CD  . ARG A 193 ? 1.00776 0.85334 0.63049 0.25272  0.00922  -0.08710 193 ARG A CD  
1493 N NE  . ARG A 193 ? 0.93955 0.82545 0.56750 0.27388  0.03529  -0.07836 193 ARG A NE  
1494 C CZ  . ARG A 193 ? 1.10607 0.99699 0.69265 0.30578  0.04701  -0.08615 193 ARG A CZ  
1495 N NH1 . ARG A 193 ? 1.04147 0.89315 0.57215 0.32162  0.03445  -0.10398 193 ARG A NH1 
1496 N NH2 . ARG A 193 ? 1.21304 1.15203 0.81468 0.32260  0.07167  -0.07649 193 ARG A NH2 
1497 N N   . THR A 194 ? 0.72822 0.59608 0.52584 0.14642  -0.01256 -0.05624 194 THR A N   
1498 C CA  . THR A 194 ? 0.60945 0.51319 0.45096 0.13082  -0.00274 -0.04015 194 THR A CA  
1499 C C   . THR A 194 ? 0.62485 0.55627 0.47640 0.14144  0.01795  -0.02940 194 THR A C   
1500 O O   . THR A 194 ? 0.57513 0.50036 0.40628 0.16064  0.02443  -0.03450 194 THR A O   
1501 C CB  . THR A 194 ? 0.66206 0.55770 0.53604 0.10795  -0.01033 -0.04022 194 THR A CB  
1502 O OG1 . THR A 194 ? 0.58499 0.46100 0.45582 0.11084  -0.00615 -0.04272 194 THR A OG1 
1503 C CG2 . THR A 194 ? 0.64850 0.52259 0.51743 0.09509  -0.03162 -0.05142 194 THR A CG2 
1504 N N   . ILE A 195 ? 0.59169 0.55429 0.47539 0.12930  0.02711  -0.01505 195 ILE A N   
1505 C CA  . ILE A 195 ? 0.57676 0.57048 0.47471 0.13454  0.04460  -0.00423 195 ILE A CA  
1506 C C   . ILE A 195 ? 0.63541 0.62273 0.54574 0.13569  0.04614  -0.00695 195 ILE A C   
1507 O O   . ILE A 195 ? 0.51701 0.52400 0.42825 0.14922  0.05684  -0.00406 195 ILE A O   
1508 C CB  . ILE A 195 ? 0.56909 0.58879 0.49436 0.11851  0.05078  0.01069  195 ILE A CB  
1509 C CG1 . ILE A 195 ? 0.52838 0.58281 0.46855 0.12024  0.06729  0.02204  195 ILE A CG1 
1510 C CG2 . ILE A 195 ? 0.49216 0.50320 0.44551 0.10007  0.04277  0.01066  195 ILE A CG2 
1511 C CD1 . ILE A 195 ? 0.52436 0.59939 0.44179 0.13734  0.07935  0.02491  195 ILE A CD1 
1512 N N   . GLY A 196 ? 0.55551 0.51765 0.47498 0.12221  0.03562  -0.01176 196 GLY A N   
1513 C CA  . GLY A 196 ? 0.57052 0.52149 0.49738 0.12174  0.03650  -0.01214 196 GLY A CA  
1514 C C   . GLY A 196 ? 0.55361 0.53359 0.51183 0.11165  0.04533  -0.00078 196 GLY A C   
1515 O O   . GLY A 196 ? 0.60148 0.57105 0.57298 0.09863  0.04262  0.00058  196 GLY A O   
1516 N N   . SER A 197 ? 0.55698 0.57300 0.52575 0.11599  0.05583  0.00755  197 SER A N   
1517 C CA  . SER A 197 ? 0.50424 0.54607 0.50058 0.10525  0.06189  0.01701  197 SER A CA  
1518 C C   . SER A 197 ? 0.51903 0.55753 0.53321 0.08465  0.05864  0.02058  197 SER A C   
1519 O O   . SER A 197 ? 0.49554 0.52578 0.50510 0.08053  0.05417  0.01916  197 SER A O   
1520 C CB  . SER A 197 ? 0.39122 0.47342 0.39598 0.11056  0.07302  0.02559  197 SER A CB  
1521 O OG  . SER A 197 ? 0.48469 0.57785 0.47493 0.13358  0.07782  0.02170  197 SER A OG  
1522 N N   . PRO A 198 ? 0.47707 0.52162 0.50966 0.07391  0.05991  0.02433  198 PRO A N   
1523 C CA  . PRO A 198 ? 0.45611 0.50062 0.50440 0.05855  0.05862  0.02722  198 PRO A CA  
1524 C C   . PRO A 198 ? 0.44270 0.50369 0.49538 0.05496  0.06244  0.03519  198 PRO A C   
1525 O O   . PRO A 198 ? 0.38840 0.47008 0.43995 0.05914  0.06878  0.04090  198 PRO A O   
1526 C CB  . PRO A 198 ? 0.48221 0.52934 0.54210 0.05160  0.06006  0.02854  198 PRO A CB  
1527 C CG  . PRO A 198 ? 0.49034 0.52945 0.53822 0.06224  0.05914  0.02560  198 PRO A CG  
1528 C CD  . PRO A 198 ? 0.40142 0.44870 0.43691 0.07773  0.06089  0.02472  198 PRO A CD  
1529 N N   . LEU A 199 ? 0.37993 0.43221 0.43745 0.04741  0.05873  0.03633  199 LEU A N   
1530 C CA  . LEU A 199 ? 0.43299 0.49015 0.48952 0.04294  0.06064  0.04534  199 LEU A CA  
1531 C C   . LEU A 199 ? 0.46325 0.51341 0.53306 0.03188  0.05903  0.04746  199 LEU A C   
1532 O O   . LEU A 199 ? 0.45834 0.49812 0.53539 0.03121  0.05489  0.04077  199 LEU A O   
1533 C CB  . LEU A 199 ? 0.44653 0.49291 0.48822 0.04913  0.05499  0.04495  199 LEU A CB  
1534 C CG  . LEU A 199 ? 0.44307 0.48984 0.46430 0.06166  0.05465  0.04033  199 LEU A CG  
1535 C CD1 . LEU A 199 ? 0.49593 0.53143 0.49967 0.06693  0.04657  0.04000  199 LEU A CD1 
1536 C CD2 . LEU A 199 ? 0.34665 0.41458 0.36123 0.06676  0.06612  0.04687  199 LEU A CD2 
1537 N N   . VAL A 200 ? 0.49126 0.54709 0.56336 0.02287  0.06254  0.05651  200 VAL A N   
1538 C CA  . VAL A 200 ? 0.39803 0.44021 0.47687 0.01241  0.05964  0.05771  200 VAL A CA  
1539 C C   . VAL A 200 ? 0.49426 0.52023 0.56230 0.00848  0.05768  0.06734  200 VAL A C   
1540 O O   . VAL A 200 ? 0.48470 0.52007 0.54619 0.00241  0.06279  0.07853  200 VAL A O   
1541 C CB  . VAL A 200 ? 0.50493 0.56083 0.59373 0.00147  0.06198  0.05957  200 VAL A CB  
1542 C CG1 . VAL A 200 ? 0.47257 0.50704 0.56195 -0.01002 0.05709  0.05967  200 VAL A CG1 
1543 C CG2 . VAL A 200 ? 0.43700 0.50306 0.53130 0.00770  0.06222  0.05105  200 VAL A CG2 
1544 N N   . PHE A 201 ? 0.52901 0.53127 0.59433 0.01278  0.05078  0.06381  201 PHE A N   
1545 C CA  . PHE A 201 ? 0.54060 0.51957 0.59095 0.01327  0.04626  0.07281  201 PHE A CA  
1546 C C   . PHE A 201 ? 0.57552 0.52659 0.62361 0.00456  0.04234  0.07434  201 PHE A C   
1547 O O   . PHE A 201 ? 0.59033 0.53676 0.64769 0.00623  0.04045  0.06347  201 PHE A O   
1548 C CB  . PHE A 201 ? 0.48243 0.45421 0.52911 0.02943  0.03832  0.06734  201 PHE A CB  
1549 C CG  . PHE A 201 ? 0.56028 0.55182 0.60511 0.03712  0.03872  0.06354  201 PHE A CG  
1550 C CD1 . PHE A 201 ? 0.44171 0.44799 0.50099 0.03987  0.03905  0.05172  201 PHE A CD1 
1551 C CD2 . PHE A 201 ? 0.49033 0.48148 0.51455 0.04116  0.03851  0.07191  201 PHE A CD2 
1552 C CE1 . PHE A 201 ? 0.55417 0.57024 0.60766 0.04583  0.03731  0.04715  201 PHE A CE1 
1553 C CE2 . PHE A 201 ? 0.54963 0.55356 0.56682 0.04951  0.03732  0.06608  201 PHE A CE2 
1554 C CZ  . PHE A 201 ? 0.50178 0.51608 0.53376 0.05152  0.03579  0.05307  201 PHE A CZ  
1555 N N   . PRO A 202 ? 0.61897 0.54742 0.65108 -0.00498 0.04099  0.08769  202 PRO A N   
1556 C CA  . PRO A 202 ? 0.55102 0.44172 0.57512 -0.01332 0.03468  0.08835  202 PRO A CA  
1557 C C   . PRO A 202 ? 0.56152 0.41858 0.57369 0.00528  0.02504  0.08379  202 PRO A C   
1558 O O   . PRO A 202 ? 0.59770 0.46850 0.61426 0.02331  0.02280  0.07869  202 PRO A O   
1559 C CB  . PRO A 202 ? 0.56405 0.44432 0.57498 -0.03418 0.03775  0.10698  202 PRO A CB  
1560 C CG  . PRO A 202 ? 0.64918 0.54663 0.65017 -0.02598 0.04303  0.11689  202 PRO A CG  
1561 C CD  . PRO A 202 ? 0.55909 0.49342 0.57646 -0.01030 0.04609  0.10348  202 PRO A CD  
1562 N N   . LYS A 203 ? 0.61210 0.42492 0.60910 0.00171  0.01797  0.08491  203 LYS A N   
1563 C CA  . LYS A 203 ? 0.75589 0.53416 0.73924 0.02339  0.00796  0.08103  203 LYS A CA  
1564 C C   . LYS A 203 ? 0.71662 0.48459 0.68172 0.03171  0.00372  0.09538  203 LYS A C   
1565 O O   . LYS A 203 ? 0.75578 0.52974 0.71062 0.01655  0.00917  0.11091  203 LYS A O   
1566 C CB  . LYS A 203 ? 0.78950 0.51258 0.75291 0.01856  0.00014  0.07955  203 LYS A CB  
1567 C CG  . LYS A 203 ? 0.76479 0.48763 0.73800 0.02534  -0.00004 0.05980  203 LYS A CG  
1568 C CD  . LYS A 203 ? 0.89109 0.54962 0.83694 0.03029  -0.01080 0.05526  203 LYS A CD  
1569 C CE  . LYS A 203 ? 0.99482 0.61191 0.91877 0.00045  -0.01551 0.07058  203 LYS A CE  
1570 N NZ  . LYS A 203 ? 0.84383 0.49279 0.78484 -0.02880 -0.00932 0.07086  203 LYS A NZ  
1571 N N   . HIS A 204 ? 0.73421 0.49052 0.69534 0.05773  -0.00597 0.08977  204 HIS A N   
1572 C CA  . HIS A 204 ? 0.87512 0.61418 0.81402 0.07106  -0.01466 0.10196  204 HIS A CA  
1573 C C   . HIS A 204 ? 0.81275 0.59444 0.75777 0.07125  -0.01053 0.10562  204 HIS A C   
1574 O O   . HIS A 204 ? 0.82288 0.59732 0.74965 0.08472  -0.01901 0.11329  204 HIS A O   
1575 C CB  . HIS A 204 ? 0.81109 0.49532 0.71352 0.05651  -0.01747 0.12183  204 HIS A CB  
1576 C CG  . HIS A 204 ? 0.93807 0.57101 0.82871 0.05320  -0.02325 0.11763  204 HIS A CG  
1577 N ND1 . HIS A 204 ? 0.96496 0.56448 0.84698 0.08094  -0.03546 0.10741  204 HIS A ND1 
1578 C CD2 . HIS A 204 ? 0.94941 0.55835 0.83439 0.02623  -0.01972 0.12091  204 HIS A CD2 
1579 C CE1 . HIS A 204 ? 1.03349 0.58468 0.90047 0.07243  -0.03892 0.10379  204 HIS A CE1 
1580 N NE2 . HIS A 204 ? 0.94830 0.50357 0.81694 0.03747  -0.03048 0.11188  204 HIS A NE2 
1581 N N   . HIS A 205 ? 0.71518 0.53778 0.68185 0.05832  0.00091  0.09961  205 HIS A N   
1582 C CA  . HIS A 205 ? 0.69532 0.55475 0.66671 0.06177  0.00361  0.09853  205 HIS A CA  
1583 C C   . HIS A 205 ? 0.73002 0.61343 0.72328 0.08038  -0.00464 0.08243  205 HIS A C   
1584 O O   . HIS A 205 ? 0.61534 0.51011 0.63271 0.08264  -0.00289 0.06950  205 HIS A O   
1585 C CB  . HIS A 205 ? 0.60099 0.49147 0.58547 0.04441  0.01765  0.09747  205 HIS A CB  
1586 C CG  . HIS A 205 ? 0.61067 0.49754 0.57611 0.02802  0.02685  0.11499  205 HIS A CG  
1587 N ND1 . HIS A 205 ? 0.52304 0.44441 0.49354 0.02058  0.03858  0.11659  205 HIS A ND1 
1588 C CD2 . HIS A 205 ? 0.65771 0.51184 0.59908 0.01739  0.02690  0.13241  205 HIS A CD2 
1589 C CE1 . HIS A 205 ? 0.70022 0.61789 0.65432 0.00617  0.04703  0.13411  205 HIS A CE1 
1590 N NE2 . HIS A 205 ? 0.68196 0.55767 0.61771 0.00165  0.04023  0.14491  205 HIS A NE2 
1591 N N   . VAL A 206 ? 0.66319 0.55593 0.64741 0.09258  -0.01373 0.08349  206 VAL A N   
1592 C CA  . VAL A 206 ? 0.57462 0.49344 0.58115 0.10787  -0.02436 0.06960  206 VAL A CA  
1593 C C   . VAL A 206 ? 0.70959 0.65840 0.72127 0.10204  -0.02249 0.06358  206 VAL A C   
1594 O O   . VAL A 206 ? 0.62029 0.56437 0.60553 0.10279  -0.02484 0.07095  206 VAL A O   
1595 C CB  . VAL A 206 ? 0.64364 0.54696 0.63564 0.12919  -0.04213 0.07363  206 VAL A CB  
1596 C CG1 . VAL A 206 ? 0.59998 0.54126 0.62016 0.14201  -0.05422 0.05930  206 VAL A CG1 
1597 C CG2 . VAL A 206 ? 0.61823 0.48567 0.60331 0.13884  -0.04537 0.07733  206 VAL A CG2 
1598 N N   . VAL A 207 ? 0.50319 0.47895 0.54463 0.09668  -0.01820 0.05036  207 VAL A N   
1599 C CA  . VAL A 207 ? 0.50782 0.50536 0.55413 0.09162  -0.01905 0.04243  207 VAL A CA  
1600 C C   . VAL A 207 ? 0.56344 0.58291 0.63091 0.10020  -0.03413 0.03170  207 VAL A C   
1601 O O   . VAL A 207 ? 0.58621 0.62169 0.68316 0.10305  -0.03431 0.02501  207 VAL A O   
1602 C CB  . VAL A 207 ? 0.48696 0.49532 0.54855 0.07773  -0.00500 0.03696  207 VAL A CB  
1603 C CG1 . VAL A 207 ? 0.50261 0.52481 0.56618 0.07370  -0.00802 0.02801  207 VAL A CG1 
1604 C CG2 . VAL A 207 ? 0.44330 0.43843 0.48828 0.06927  0.00778  0.04722  207 VAL A CG2 
1605 N N   . SER A 208 ? 0.63113 0.65418 0.68376 0.10431  -0.04688 0.02958  208 SER A N   
1606 C CA  . SER A 208 ? 0.58083 0.62710 0.65259 0.11138  -0.06540 0.02006  208 SER A CA  
1607 C C   . SER A 208 ? 0.64182 0.70077 0.71732 0.09939  -0.06999 0.00912  208 SER A C   
1608 O O   . SER A 208 ? 0.67441 0.71607 0.71831 0.09682  -0.06804 0.01026  208 SER A O   
1609 C CB  . SER A 208 ? 0.57720 0.61147 0.62317 0.12890  -0.08296 0.02670  208 SER A CB  
1610 O OG  . SER A 208 ? 0.58701 0.64835 0.65133 0.13508  -0.10396 0.01649  208 SER A OG  
1611 N N   . LEU A 209 ? 0.62700 0.71521 0.73990 0.09200  -0.07559 -0.00141 209 LEU A N   
1612 C CA  . LEU A 209 ? 0.60574 0.70228 0.72391 0.07766  -0.08344 -0.01222 209 LEU A CA  
1613 C C   . LEU A 209 ? 0.66054 0.77998 0.79086 0.08233  -0.10884 -0.01973 209 LEU A C   
1614 O O   . LEU A 209 ? 0.76491 0.91564 0.92923 0.08939  -0.11542 -0.02077 209 LEU A O   
1615 C CB  . LEU A 209 ? 0.58137 0.69373 0.73245 0.06002  -0.07048 -0.01687 209 LEU A CB  
1616 C CG  . LEU A 209 ? 0.60855 0.70268 0.75104 0.05602  -0.04762 -0.01030 209 LEU A CG  
1617 C CD1 . LEU A 209 ? 0.58636 0.69169 0.75297 0.03825  -0.03746 -0.01462 209 LEU A CD1 
1618 C CD2 . LEU A 209 ? 0.63137 0.69408 0.73254 0.05874  -0.04304 -0.00621 209 LEU A CD2 
1619 N N   . GLN A 210 ? 0.66796 0.77316 0.76984 0.08013  -0.12394 -0.02591 210 GLN A N   
1620 C CA  . GLN A 210 ? 0.74272 0.86645 0.84883 0.08513  -0.15192 -0.03350 210 GLN A CA  
1621 C C   . GLN A 210 ? 0.78652 0.90967 0.89325 0.06542  -0.16559 -0.04766 210 GLN A C   
1622 O O   . GLN A 210 ? 0.80805 0.89705 0.88165 0.05874  -0.15842 -0.05062 210 GLN A O   
1623 C CB  . GLN A 210 ? 0.73132 0.83065 0.78897 0.10624  -0.16279 -0.02664 210 GLN A CB  
1624 C CG  . GLN A 210 ? 0.71644 0.80757 0.76838 0.12378  -0.15180 -0.01129 210 GLN A CG  
1625 C CD  . GLN A 210 ? 0.83797 0.89881 0.83579 0.14118  -0.15895 -0.00093 210 GLN A CD  
1626 O OE1 . GLN A 210 ? 0.89969 0.94937 0.86330 0.14312  -0.17294 -0.00629 210 GLN A OE1 
1627 N NE2 . GLN A 210 ? 0.84259 0.88657 0.82863 0.15335  -0.14938 0.01422  210 GLN A NE2 
1628 N N   . PRO A 211 ? 0.92862 1.08866 1.07242 0.05596  -0.18610 -0.05691 211 PRO A N   
1629 C CA  . PRO A 211 ? 0.93460 1.09186 1.08242 0.03150  -0.20032 -0.07045 211 PRO A CA  
1630 C C   . PRO A 211 ? 1.01912 1.14411 1.11496 0.03788  -0.22350 -0.07956 211 PRO A C   
1631 O O   . PRO A 211 ? 0.94600 1.06418 1.01103 0.06071  -0.23367 -0.07564 211 PRO A O   
1632 C CB  . PRO A 211 ? 0.97049 1.18763 1.18076 0.01953  -0.21488 -0.07559 211 PRO A CB  
1633 C CG  . PRO A 211 ? 1.02867 1.27172 1.24715 0.04805  -0.22282 -0.06914 211 PRO A CG  
1634 C CD  . PRO A 211 ? 0.91719 1.12480 1.10237 0.06750  -0.19828 -0.05558 211 PRO A CD  
1635 N N   . VAL A 212 ? 1.01915 1.11995 1.10125 0.01737  -0.23214 -0.09191 212 VAL A N   
1636 C CA  . VAL A 212 ? 0.99351 1.05640 1.02068 0.02191  -0.25383 -0.10421 212 VAL A CA  
1637 C C   . VAL A 212 ? 1.20815 1.28827 1.25567 0.00012  -0.28749 -0.12035 212 VAL A C   
1638 O O   . VAL A 212 ? 1.27150 1.35412 1.29701 0.00996  -0.31585 -0.12851 212 VAL A O   
1639 C CB  . VAL A 212 ? 0.91297 0.92001 0.89260 0.02123  -0.23741 -0.10732 212 VAL A CB  
1640 C CG1 . VAL A 212 ? 0.96887 0.93505 0.88923 0.02715  -0.26050 -0.12316 212 VAL A CG1 
1641 C CG2 . VAL A 212 ? 0.87784 0.87449 0.83801 0.04259  -0.20710 -0.09157 212 VAL A CG2 
1642 N N   . ASN A 213 ? 1.23271 1.32463 1.32100 -0.03122 -0.28560 -0.12456 213 ASN A N   
1643 C CA  . ASN A 213 ? 1.20778 1.32464 1.32705 -0.05870 -0.31647 -0.13810 213 ASN A CA  
1644 C C   . ASN A 213 ? 1.11217 1.29606 1.31176 -0.07886 -0.30819 -0.13091 213 ASN A C   
1645 O O   . ASN A 213 ? 1.18546 1.42942 1.42766 -0.07233 -0.32272 -0.13028 213 ASN A O   
1646 C CB  . ASN A 213 ? 1.25832 1.31779 1.34309 -0.08350 -0.32619 -0.15194 213 ASN A CB  
1647 C CG  . ASN A 213 ? 1.39572 1.40952 1.41428 -0.07069 -0.35428 -0.16819 213 ASN A CG  
1648 O OD1 . ASN A 213 ? 1.46128 1.50180 1.48327 -0.06669 -0.38455 -0.17619 213 ASN A OD1 
1649 N ND2 . ASN A 213 ? 1.45770 1.40335 1.41367 -0.06169 -0.34475 -0.17367 213 ASN A ND2 
1650 N N   . ASP A 214 ? 1.12161 1.29673 1.34048 -0.10127 -0.28447 -0.12521 214 ASP A N   
1651 C CA  . ASP A 214 ? 1.13936 1.37752 1.43012 -0.11995 -0.27089 -0.11710 214 ASP A CA  
1652 C C   . ASP A 214 ? 1.09437 1.36855 1.40581 -0.08889 -0.24888 -0.10395 214 ASP A C   
1653 O O   . ASP A 214 ? 1.10200 1.33827 1.37497 -0.06615 -0.22850 -0.09603 214 ASP A O   
1654 C CB  . ASP A 214 ? 1.06374 1.27348 1.35770 -0.14993 -0.24966 -0.11254 214 ASP A CB  
1655 C CG  . ASP A 214 ? 1.14633 1.41960 1.51185 -0.18243 -0.24430 -0.10806 214 ASP A CG  
1656 O OD1 . ASP A 214 ? 1.08240 1.41138 1.49148 -0.17051 -0.22440 -0.09804 214 ASP A OD1 
1657 O OD2 . ASP A 214 ? 1.15129 1.41823 1.52822 -0.22038 -0.25992 -0.11474 214 ASP A OD2 
1658 N N   . LYS A 215 ? 1.08028 1.42806 1.45252 -0.08745 -0.25407 -0.10225 215 LYS A N   
1659 C CA  . LYS A 215 ? 1.08498 1.46645 1.47870 -0.05732 -0.23562 -0.09166 215 LYS A CA  
1660 C C   . LYS A 215 ? 1.01014 1.43835 1.45920 -0.07150 -0.20888 -0.08437 215 LYS A C   
1661 O O   . LYS A 215 ? 0.86717 1.33869 1.34746 -0.04904 -0.19788 -0.07897 215 LYS A O   
1662 C CB  . LYS A 215 ? 1.00974 1.43693 1.42274 -0.03278 -0.26192 -0.09528 215 LYS A CB  
1663 C CG  . LYS A 215 ? 0.99610 1.37516 1.34536 -0.00572 -0.28008 -0.09685 215 LYS A CG  
1664 C CD  . LYS A 215 ? 1.12349 1.49984 1.45862 -0.01883 -0.31817 -0.11127 215 LYS A CD  
1665 C CE  . LYS A 215 ? 1.05911 1.39793 1.33239 0.01240  -0.33685 -0.11180 215 LYS A CE  
1666 N NZ  . LYS A 215 ? 1.10513 1.37194 1.31155 0.02349  -0.31447 -0.10520 215 LYS A NZ  
1667 N N   . ASP A 216 ? 1.12955 1.54683 1.58745 -0.10720 -0.19821 -0.08401 216 ASP A N   
1668 C CA  . ASP A 216 ? 1.01497 1.47374 1.51941 -0.12399 -0.17113 -0.07594 216 ASP A CA  
1669 C C   . ASP A 216 ? 1.04453 1.44248 1.50911 -0.13125 -0.14378 -0.06779 216 ASP A C   
1670 O O   . ASP A 216 ? 1.10263 1.44236 1.52796 -0.14948 -0.14993 -0.07063 216 ASP A O   
1671 C CB  . ASP A 216 ? 1.01399 1.52414 1.57198 -0.16502 -0.18264 -0.07999 216 ASP A CB  
1672 C CG  . ASP A 216 ? 1.07674 1.66670 1.68901 -0.15722 -0.20733 -0.08714 216 ASP A CG  
1673 O OD1 . ASP A 216 ? 1.09448 1.68310 1.68930 -0.12133 -0.22343 -0.09088 216 ASP A OD1 
1674 O OD2 . ASP A 216 ? 1.15686 1.81295 1.82995 -0.18716 -0.21067 -0.08808 216 ASP A OD2 
1675 N N   . PHE A 217 ? 0.93580 1.34581 1.40835 -0.11510 -0.11528 -0.05863 217 PHE A N   
1676 C CA  . PHE A 217 ? 0.86186 1.22185 1.30023 -0.11978 -0.08978 -0.05041 217 PHE A CA  
1677 C C   . PHE A 217 ? 0.70788 1.11016 1.17989 -0.11734 -0.06099 -0.04222 217 PHE A C   
1678 O O   . PHE A 217 ? 0.73255 1.19840 1.24926 -0.10479 -0.05947 -0.04353 217 PHE A O   
1679 C CB  . PHE A 217 ? 0.81510 1.11544 1.19621 -0.09121 -0.08743 -0.04907 217 PHE A CB  
1680 C CG  . PHE A 217 ? 0.93467 1.23608 1.30239 -0.06475 -0.10866 -0.05447 217 PHE A CG  
1681 C CD1 . PHE A 217 ? 0.88472 1.23058 1.28037 -0.04044 -0.10994 -0.05343 217 PHE A CD1 
1682 C CD2 . PHE A 217 ? 1.01694 1.27012 1.33810 -0.06144 -0.12649 -0.06010 217 PHE A CD2 
1683 C CE1 . PHE A 217 ? 0.90897 1.24946 1.28630 -0.01571 -0.13003 -0.05624 217 PHE A CE1 
1684 C CE2 . PHE A 217 ? 1.00790 1.25939 1.31049 -0.03719 -0.14479 -0.06328 217 PHE A CE2 
1685 C CZ  . PHE A 217 ? 1.01391 1.30777 1.34408 -0.01512 -0.14703 -0.06040 217 PHE A CZ  
1686 N N   . GLN A 218 ? 0.64767 1.01330 1.09487 -0.12688 -0.03855 -0.03428 218 GLN A N   
1687 C CA  . GLN A 218 ? 0.60391 0.99594 1.06723 -0.12036 -0.00977 -0.02680 218 GLN A CA  
1688 C C   . GLN A 218 ? 0.53822 0.89700 0.96631 -0.08627 -0.00075 -0.02539 218 GLN A C   
1689 O O   . GLN A 218 ? 0.47232 0.77205 0.85398 -0.08152 -0.00325 -0.02406 218 GLN A O   
1690 C CB  . GLN A 218 ? 0.58843 0.95943 1.04197 -0.15069 0.00881  -0.01778 218 GLN A CB  
1691 C CG  . GLN A 218 ? 0.64615 1.07146 1.14858 -0.18549 0.01261  -0.01467 218 GLN A CG  
1692 C CD  . GLN A 218 ? 0.75247 1.15141 1.24990 -0.21917 -0.01011 -0.01773 218 GLN A CD  
1693 O OE1 . GLN A 218 ? 0.79394 1.11952 1.24098 -0.22387 -0.01783 -0.01790 218 GLN A OE1 
1694 N NE2 . GLN A 218 ? 0.72327 1.18253 1.27308 -0.24211 -0.02200 -0.02109 218 GLN A NE2 
1695 N N   . ILE A 219 ? 0.53474 0.93194 0.98525 -0.06269 0.00938  -0.02604 219 ILE A N   
1696 C CA  . ILE A 219 ? 0.53092 0.89785 0.95104 -0.03277 0.01708  -0.02494 219 ILE A CA  
1697 C C   . ILE A 219 ? 0.57019 0.95162 0.99601 -0.02981 0.04409  -0.02118 219 ILE A C   
1698 O O   . ILE A 219 ? 0.45299 0.89082 0.91800 -0.02483 0.05357  -0.02333 219 ILE A O   
1699 C CB  . ILE A 219 ? 0.54364 0.92869 0.97366 -0.00272 0.00179  -0.03014 219 ILE A CB  
1700 C CG1 . ILE A 219 ? 0.47300 0.84132 0.89038 -0.00478 -0.02548 -0.03362 219 ILE A CG1 
1701 C CG2 . ILE A 219 ? 0.37405 0.72292 0.77161 0.02382  0.01034  -0.02793 219 ILE A CG2 
1702 C CD1 . ILE A 219 ? 0.50530 0.89191 0.93086 0.02371  -0.04327 -0.03723 219 ILE A CD1 
1703 N N   . SER A 220 ? 0.48684 0.82033 0.87321 -0.03124 0.05612  -0.01617 220 SER A N   
1704 C CA  . SER A 220 ? 0.44771 0.78591 0.82887 -0.02750 0.08007  -0.01312 220 SER A CA  
1705 C C   . SER A 220 ? 0.48497 0.80029 0.84336 0.00231  0.08182  -0.01635 220 SER A C   
1706 O O   . SER A 220 ? 0.54765 0.82202 0.87776 0.01089  0.06968  -0.01596 220 SER A O   
1707 C CB  . SER A 220 ? 0.50623 0.80604 0.85687 -0.04905 0.09063  -0.00518 220 SER A CB  
1708 O OG  . SER A 220 ? 0.55670 0.80164 0.86540 -0.03990 0.08398  -0.00401 220 SER A OG  
1709 N N   . VAL A 221 ? 0.52265 0.86441 0.89254 0.01750  0.09718  -0.01967 221 VAL A N   
1710 C CA  . VAL A 221 ? 0.51826 0.83143 0.86155 0.04246  0.10091  -0.02340 221 VAL A CA  
1711 C C   . VAL A 221 ? 0.58601 0.89846 0.91495 0.03875  0.12359  -0.02233 221 VAL A C   
1712 O O   . VAL A 221 ? 0.52835 0.88559 0.88097 0.04303  0.13927  -0.02522 221 VAL A O   
1713 C CB  . VAL A 221 ? 0.58431 0.92214 0.94750 0.07208  0.09438  -0.03133 221 VAL A CB  
1714 C CG1 . VAL A 221 ? 0.55718 0.85694 0.88789 0.09501  0.09874  -0.03568 221 VAL A CG1 
1715 C CG2 . VAL A 221 ? 0.48902 0.82259 0.85912 0.07682  0.07024  -0.03106 221 VAL A CG2 
1716 N N   . ASP A 222 ? 0.52072 0.78556 0.81050 0.03177  0.12542  -0.01811 222 ASP A N   
1717 C CA  . ASP A 222 ? 0.63577 0.89261 0.90379 0.02488  0.14398  -0.01533 222 ASP A CA  
1718 C C   . ASP A 222 ? 0.62962 0.91867 0.91804 0.00022  0.15590  -0.00791 222 ASP A C   
1719 O O   . ASP A 222 ? 0.73182 1.00687 1.02035 -0.02034 0.14647  -0.00138 222 ASP A O   
1720 C CB  . ASP A 222 ? 0.49567 0.75812 0.75529 0.04947  0.15469  -0.02452 222 ASP A CB  
1721 C CG  . ASP A 222 ? 0.52180 0.73802 0.75285 0.06654  0.14135  -0.02976 222 ASP A CG  
1722 O OD1 . ASP A 222 ? 0.47042 0.65061 0.68150 0.05607  0.12994  -0.02426 222 ASP A OD1 
1723 O OD2 . ASP A 222 ? 0.47007 0.68531 0.69817 0.09018  0.14217  -0.03920 222 ASP A OD2 
1724 N N   . HIS A 223 ? 0.71483 1.04494 1.01876 0.00072  0.17647  -0.00841 223 HIS A N   
1725 C CA  . HIS A 223 ? 0.77457 1.13405 1.09408 -0.02648 0.19161  0.00130  223 HIS A CA  
1726 C C   . HIS A 223 ? 0.78017 1.20466 1.15612 -0.03444 0.19145  0.00001  223 HIS A C   
1727 O O   . HIS A 223 ? 0.87745 1.34211 1.27518 -0.05556 0.20843  0.00731  223 HIS A O   
1728 C CB  . HIS A 223 ? 0.92747 1.29450 1.22524 -0.02338 0.21742  0.00364  223 HIS A CB  
1729 C CG  . HIS A 223 ? 0.98971 1.39045 1.29785 0.00728  0.22884  -0.00858 223 HIS A CG  
1730 N ND1 . HIS A 223 ? 0.88724 1.26004 1.17900 0.03667  0.21638  -0.02058 223 HIS A ND1 
1731 C CD2 . HIS A 223 ? 0.85638 1.31450 1.18711 0.01407  0.25214  -0.01080 223 HIS A CD2 
1732 C CE1 . HIS A 223 ? 0.88048 1.28631 1.18173 0.06217  0.22970  -0.03089 223 HIS A CE1 
1733 N NE2 . HIS A 223 ? 0.80532 1.26670 1.13131 0.05071  0.25233  -0.02570 223 HIS A NE2 
1734 N N   . LEU A 224 ? 0.68613 1.12297 1.08596 -0.01924 0.17199  -0.00813 224 LEU A N   
1735 C CA  . LEU A 224 ? 0.71285 1.21781 1.16897 -0.01987 0.16852  -0.01179 224 LEU A CA  
1736 C C   . LEU A 224 ? 0.80172 1.29502 1.26996 -0.03363 0.14127  -0.01158 224 LEU A C   
1737 O O   . LEU A 224 ? 0.65435 1.12626 1.11453 -0.01291 0.12174  -0.01787 224 LEU A O   
1738 C CB  . LEU A 224 ? 0.58997 1.12571 1.06218 0.01928  0.16990  -0.02364 224 LEU A CB  
1739 C CG  . LEU A 224 ? 0.72109 1.24686 1.16443 0.03983  0.19236  -0.02754 224 LEU A CG  
1740 C CD1 . LEU A 224 ? 0.69684 1.21699 1.13591 0.08153  0.18473  -0.04055 224 LEU A CD1 
1741 C CD2 . LEU A 224 ? 0.61152 1.19965 1.08035 0.02978  0.22135  -0.02390 224 LEU A CD2 
1742 N N   . SER A 225 ? 0.94606 1.45001 1.42986 -0.06909 0.13969  -0.00421 225 SER A N   
1743 C CA  . SER A 225 ? 0.95563 1.44652 1.44739 -0.08455 0.11330  -0.00554 225 SER A CA  
1744 C C   . SER A 225 ? 0.82933 1.39415 1.38058 -0.08387 0.10299  -0.01159 225 SER A C   
1745 O O   . SER A 225 ? 0.68738 1.31458 1.28091 -0.10122 0.11737  -0.00828 225 SER A O   
1746 C CB  . SER A 225 ? 1.03053 1.48725 1.50480 -0.12309 0.11341  0.00402  225 SER A CB  
1747 O OG  . SER A 225 ? 0.99263 1.41738 1.45805 -0.13267 0.08647  0.00040  225 SER A OG  
1748 N N   . ILE A 226 ? 0.81379 1.37424 1.36834 -0.06411 0.07808  -0.01962 226 ILE A N   
1749 C CA  . ILE A 226 ? 0.74011 1.36920 1.34793 -0.05525 0.06370  -0.02664 226 ILE A CA  
1750 C C   . ILE A 226 ? 0.70596 1.31780 1.31311 -0.07186 0.03270  -0.02956 226 ILE A C   
1751 O O   . ILE A 226 ? 0.60846 1.16037 1.17270 -0.05954 0.01676  -0.03152 226 ILE A O   
1752 C CB  . ILE A 226 ? 0.71420 1.35411 1.32277 -0.00879 0.06056  -0.03425 226 ILE A CB  
1753 C CG1 . ILE A 226 ? 0.62734 1.23917 1.20382 0.01044  0.08571  -0.03298 226 ILE A CG1 
1754 C CG2 . ILE A 226 ? 0.63399 1.36411 1.30634 0.00407  0.05688  -0.04036 226 ILE A CG2 
1755 C CD1 . ILE A 226 ? 0.50299 1.06371 1.04108 0.04598  0.07588  -0.03749 226 ILE A CD1 
1756 N N   . LEU A 227 ? 0.74040 1.40596 1.39426 -0.10033 0.02411  -0.03013 227 LEU A N   
1757 C CA  . LEU A 227 ? 0.80053 1.45781 1.45765 -0.11410 -0.00886 -0.03589 227 LEU A CA  
1758 C C   . LEU A 227 ? 0.81940 1.51488 1.49923 -0.07914 -0.03015 -0.04477 227 LEU A C   
1759 O O   . LEU A 227 ? 0.73164 1.50672 1.46645 -0.06798 -0.02670 -0.04761 227 LEU A O   
1760 C CB  . LEU A 227 ? 0.79726 1.49751 1.49692 -0.16014 -0.01334 -0.03384 227 LEU A CB  
1761 C CG  . LEU A 227 ? 0.78959 1.48512 1.49435 -0.17466 -0.05107 -0.04252 227 LEU A CG  
1762 C CD1 . LEU A 227 ? 0.78293 1.37997 1.41960 -0.18363 -0.06342 -0.04324 227 LEU A CD1 
1763 C CD2 . LEU A 227 ? 0.62465 1.38327 1.38705 -0.21629 -0.05849 -0.04149 227 LEU A CD2 
1764 N N   . HIS A 228 ? 0.92290 1.56308 1.55948 -0.06045 -0.05162 -0.04851 228 HIS A N   
1765 C CA  . HIS A 228 ? 0.97063 1.63179 1.61556 -0.02545 -0.07368 -0.05484 228 HIS A CA  
1766 C C   . HIS A 228 ? 0.96553 1.62324 1.60898 -0.03920 -0.10880 -0.06129 228 HIS A C   
1767 O O   . HIS A 228 ? 0.90406 1.50019 1.50408 -0.05805 -0.11706 -0.06137 228 HIS A O   
1768 C CB  . HIS A 228 ? 0.83482 1.43342 1.42589 0.00978  -0.06905 -0.05225 228 HIS A CB  
1769 N N   . ARG A 229 ? 0.86777 1.59191 1.55717 -0.02778 -0.13028 -0.06766 229 ARG A N   
1770 C CA  . ARG A 229 ? 0.77397 1.50517 1.46715 -0.04059 -0.16691 -0.07547 229 ARG A CA  
1771 C C   . ARG A 229 ? 0.82277 1.53724 1.48856 0.00045  -0.19155 -0.07866 229 ARG A C   
1772 O O   . ARG A 229 ? 0.81647 1.54181 1.48429 0.03853  -0.18355 -0.07581 229 ARG A O   
1773 C CB  . ARG A 229 ? 0.84475 1.66771 1.61219 -0.06471 -0.17728 -0.07914 229 ARG A CB  
1774 C CG  . ARG A 229 ? 0.88453 1.70389 1.66411 -0.11914 -0.17208 -0.07736 229 ARG A CG  
1775 C CD  . ARG A 229 ? 0.87901 1.75848 1.70927 -0.14380 -0.18685 -0.07270 229 ARG A CD  
1776 N NE  . ARG A 229 ? 0.94330 1.84594 1.80777 -0.17748 -0.15920 -0.06148 229 ARG A NE  
1777 C CZ  . ARG A 229 ? 0.98693 1.84928 1.83639 -0.22096 -0.15283 -0.05946 229 ARG A CZ  
1778 N NH1 . ARG A 229 ? 0.97816 1.77615 1.77957 -0.23742 -0.17212 -0.06908 229 ARG A NH1 
1779 N NH2 . ARG A 229 ? 1.00936 1.89107 1.88903 -0.24645 -0.12571 -0.04899 229 ARG A NH2 
1780 N N   . ASP A 230 ? 0.85981 1.54386 1.49595 -0.00766 -0.22234 -0.08464 230 ASP A N   
1781 C CA  . ASP A 230 ? 0.83908 1.50124 1.44055 0.02744  -0.24861 -0.08656 230 ASP A CA  
1782 C C   . ASP A 230 ? 0.90282 1.50020 1.44868 0.05922  -0.22960 -0.07705 230 ASP A C   
1783 O O   . ASP A 230 ? 0.95984 1.55869 1.49671 0.09680  -0.23729 -0.07396 230 ASP A O   
1784 C CB  . ASP A 230 ? 0.85235 1.59753 1.51022 0.05039  -0.27031 -0.09129 230 ASP A CB  
1785 C CG  . ASP A 230 ? 0.93797 1.66120 1.55836 0.07653  -0.30574 -0.09368 230 ASP A CG  
1786 O OD1 . ASP A 230 ? 0.95968 1.61973 1.52275 0.06771  -0.31920 -0.09611 230 ASP A OD1 
1787 O OD2 . ASP A 230 ? 0.99481 1.74886 1.62869 0.10464  -0.31374 -0.08827 230 ASP A OD2 
1788 N N   . VAL A 231 ? 0.87310 1.41234 1.38128 0.04336  -0.20557 -0.07193 231 VAL A N   
1789 C CA  . VAL A 231 ? 0.77507 1.25509 1.23375 0.06677  -0.18666 -0.06271 231 VAL A CA  
1790 C C   . VAL A 231 ? 0.82435 1.24536 1.22005 0.07801  -0.20466 -0.06133 231 VAL A C   
1791 O O   . VAL A 231 ? 0.94045 1.33302 1.30970 0.05725  -0.21478 -0.06633 231 VAL A O   
1792 C CB  . VAL A 231 ? 0.83197 1.28114 1.27938 0.04625  -0.15462 -0.05780 231 VAL A CB  
1793 C CG1 . VAL A 231 ? 0.77972 1.16737 1.17498 0.06612  -0.13881 -0.04900 231 VAL A CG1 
1794 C CG2 . VAL A 231 ? 0.83738 1.34362 1.34030 0.03920  -0.13418 -0.05761 231 VAL A CG2 
1795 N N   . GLN A 232 ? 0.78556 1.18534 1.15379 0.11146  -0.20823 -0.05432 232 GLN A N   
1796 C CA  . GLN A 232 ? 0.79749 1.14119 1.10193 0.12388  -0.22077 -0.04975 232 GLN A CA  
1797 C C   . GLN A 232 ? 0.77497 1.05809 1.03227 0.12654  -0.19507 -0.03891 232 GLN A C   
1798 O O   . GLN A 232 ? 0.81443 1.05186 1.01880 0.12764  -0.19877 -0.03534 232 GLN A O   
1799 C CB  . GLN A 232 ? 0.74888 1.10277 1.04602 0.15789  -0.24441 -0.04649 232 GLN A CB  
1800 N N   . GLU A 233 ? 0.67246 0.95689 0.94748 0.12744  -0.16948 -0.03413 233 GLU A N   
1801 C CA  . GLU A 233 ? 0.63984 0.87168 0.87414 0.13024  -0.14783 -0.02379 233 GLU A CA  
1802 C C   . GLU A 233 ? 0.71199 0.95428 0.97381 0.12376  -0.12187 -0.02308 233 GLU A C   
1803 O O   . GLU A 233 ? 0.58901 0.87491 0.89457 0.13024  -0.12005 -0.02756 233 GLU A O   
1804 C CB  . GLU A 233 ? 0.69491 0.89475 0.89287 0.15805  -0.15506 -0.01307 233 GLU A CB  
1805 C CG  . GLU A 233 ? 0.76229 0.90728 0.91300 0.15589  -0.13708 -0.00130 233 GLU A CG  
1806 C CD  . GLU A 233 ? 0.71863 0.83001 0.83651 0.17968  -0.14204 0.01144  233 GLU A CD  
1807 O OE1 . GLU A 233 ? 0.74651 0.87505 0.88189 0.20145  -0.15593 0.01045  233 GLU A OE1 
1808 O OE2 . GLU A 233 ? 0.76484 0.83299 0.83958 0.17668  -0.13199 0.02301  233 GLU A OE2 
1809 N N   . ILE A 234 ? 0.68655 0.89121 0.92161 0.11231  -0.10201 -0.01778 234 ILE A N   
1810 C CA  . ILE A 234 ? 0.59443 0.79703 0.84179 0.10830  -0.07805 -0.01579 234 ILE A CA  
1811 C C   . ILE A 234 ? 0.61342 0.76617 0.81862 0.11534  -0.06788 -0.00547 234 ILE A C   
1812 O O   . ILE A 234 ? 0.61343 0.73774 0.78697 0.10561  -0.06497 -0.00126 234 ILE A O   
1813 C CB  . ILE A 234 ? 0.61019 0.82216 0.87221 0.08153  -0.06447 -0.02005 234 ILE A CB  
1814 C CG1 . ILE A 234 ? 0.56452 0.82383 0.86714 0.06813  -0.07581 -0.02876 234 ILE A CG1 
1815 C CG2 . ILE A 234 ? 0.47918 0.69018 0.75052 0.07974  -0.04112 -0.01799 234 ILE A CG2 
1816 C CD1 . ILE A 234 ? 0.52000 0.77288 0.82282 0.03900  -0.07004 -0.03164 234 ILE A CD1 
1817 N N   . ARG A 235 ? 0.55679 0.69938 0.76145 0.13206  -0.06272 -0.00177 235 ARG A N   
1818 C CA  . ARG A 235 ? 0.66032 0.75488 0.82637 0.13705  -0.05627 0.00897  235 ARG A CA  
1819 C C   . ARG A 235 ? 0.53632 0.61988 0.70594 0.12898  -0.03611 0.00853  235 ARG A C   
1820 O O   . ARG A 235 ? 0.55811 0.66088 0.75262 0.13648  -0.03021 0.00176  235 ARG A O   
1821 C CB  . ARG A 235 ? 0.57739 0.65382 0.72886 0.16238  -0.06992 0.01460  235 ARG A CB  
1822 C CG  . ARG A 235 ? 0.70357 0.78677 0.84405 0.17247  -0.09220 0.01635  235 ARG A CG  
1823 C CD  . ARG A 235 ? 0.67124 0.71329 0.77379 0.19278  -0.10315 0.02870  235 ARG A CD  
1824 N NE  . ARG A 235 ? 0.68458 0.72658 0.80124 0.21738  -0.10829 0.02653  235 ARG A NE  
1825 C CZ  . ARG A 235 ? 0.68491 0.75863 0.82421 0.24025  -0.12675 0.02050  235 ARG A CZ  
1826 N NH1 . ARG A 235 ? 0.69096 0.80030 0.84332 0.23862  -0.14352 0.01572  235 ARG A NH1 
1827 N NH2 . ARG A 235 ? 0.75645 0.82633 0.90511 0.26650  -0.12971 0.01822  235 ARG A NH2 
1828 N N   . TYR A 236 ? 0.49207 0.54761 0.63632 0.11497  -0.02593 0.01528  236 TYR A N   
1829 C CA  . TYR A 236 ? 0.55711 0.60042 0.70028 0.10544  -0.00953 0.01521  236 TYR A CA  
1830 C C   . TYR A 236 ? 0.57949 0.58094 0.69189 0.10707  -0.00813 0.02552  236 TYR A C   
1831 O O   . TYR A 236 ? 0.60616 0.58977 0.69380 0.10382  -0.01198 0.03551  236 TYR A O   
1832 C CB  . TYR A 236 ? 0.47325 0.52420 0.61704 0.08578  0.00044  0.01406  236 TYR A CB  
1833 C CG  . TYR A 236 ? 0.47436 0.55876 0.64668 0.07816  0.00231  0.00504  236 TYR A CG  
1834 C CD1 . TYR A 236 ? 0.50617 0.61406 0.70513 0.08173  0.00865  -0.00153 236 TYR A CD1 
1835 C CD2 . TYR A 236 ? 0.44293 0.53369 0.61333 0.06680  -0.00173 0.00327  236 TYR A CD2 
1836 C CE1 . TYR A 236 ? 0.47557 0.61605 0.70125 0.07079  0.01216  -0.00735 236 TYR A CE1 
1837 C CE2 . TYR A 236 ? 0.52777 0.64364 0.72237 0.05555  -0.00082 -0.00353 236 TYR A CE2 
1838 C CZ  . TYR A 236 ? 0.55918 0.70172 0.78282 0.05591  0.00676  -0.00768 236 TYR A CZ  
1839 O OH  . TYR A 236 ? 0.54929 0.71911 0.79790 0.04104  0.00947  -0.01213 236 TYR A OH  
1840 N N   . GLU A 237 ? 0.56106 0.54620 0.67323 0.11097  -0.00238 0.02307  237 GLU A N   
1841 C CA  . GLU A 237 ? 0.61641 0.55857 0.70056 0.10672  -0.00112 0.03206  237 GLU A CA  
1842 C C   . GLU A 237 ? 0.56065 0.49211 0.64853 0.10605  0.00683  0.02398  237 GLU A C   
1843 O O   . GLU A 237 ? 0.56335 0.51624 0.67135 0.11728  0.00990  0.01248  237 GLU A O   
1844 C CB  . GLU A 237 ? 0.61774 0.52810 0.67986 0.12257  -0.01436 0.04046  237 GLU A CB  
1845 C CG  . GLU A 237 ? 0.69450 0.60416 0.76728 0.14830  -0.02223 0.03155  237 GLU A CG  
1846 C CD  . GLU A 237 ? 0.85763 0.73876 0.90800 0.16768  -0.03851 0.04046  237 GLU A CD  
1847 O OE1 . GLU A 237 ? 0.79602 0.62487 0.81274 0.16562  -0.04142 0.05151  237 GLU A OE1 
1848 O OE2 . GLU A 237 ? 0.71967 0.62985 0.78514 0.18394  -0.04955 0.03707  237 GLU A OE2 
1849 N N   . VAL A 238 ? 0.59056 0.49094 0.65841 0.09193  0.01025  0.03001  238 VAL A N   
1850 C CA  . VAL A 238 ? 0.64589 0.52840 0.70982 0.09060  0.01482  0.02164  238 VAL A CA  
1851 C C   . VAL A 238 ? 0.70582 0.56128 0.76123 0.11427  0.00725  0.01534  238 VAL A C   
1852 O O   . VAL A 238 ? 0.72632 0.54851 0.76248 0.12290  -0.00332 0.02367  238 VAL A O   
1853 C CB  . VAL A 238 ? 0.64254 0.49738 0.68747 0.06847  0.01621  0.02979  238 VAL A CB  
1854 C CG1 . VAL A 238 ? 0.60370 0.43496 0.63990 0.06715  0.01733  0.01939  238 VAL A CG1 
1855 C CG2 . VAL A 238 ? 0.49962 0.38691 0.55527 0.05045  0.02395  0.03475  238 VAL A CG2 
1856 N N   . SER A 239 ? 0.67309 0.54155 0.74004 0.12680  0.01305  0.00092  239 SER A N   
1857 C CA  . SER A 239 ? 0.62921 0.47981 0.69118 0.15543  0.00731  -0.00788 239 SER A CA  
1858 C C   . SER A 239 ? 0.73682 0.52078 0.76211 0.15615  0.00037  -0.00791 239 SER A C   
1859 O O   . SER A 239 ? 0.74659 0.50852 0.75702 0.13352  0.00295  -0.00624 239 SER A O   
1860 C CB  . SER A 239 ? 0.64909 0.53974 0.73451 0.16901  0.01876  -0.02348 239 SER A CB  
1861 O OG  . SER A 239 ? 0.67012 0.54364 0.74873 0.19998  0.01494  -0.03397 239 SER A OG  
1862 N N   . ALA A 240 ? 0.76810 0.51833 0.77815 0.18268  -0.01034 -0.00997 240 ALA A N   
1863 C CA  . ALA A 240 ? 0.86495 0.54384 0.83667 0.18710  -0.01835 -0.01300 240 ALA A CA  
1864 C C   . ALA A 240 ? 0.92056 0.59650 0.88867 0.19969  -0.01087 -0.03326 240 ALA A C   
1865 O O   . ALA A 240 ? 0.90156 0.51753 0.83559 0.19721  -0.01686 -0.03883 240 ALA A O   
1866 C CB  . ALA A 240 ? 0.73725 0.37346 0.68817 0.21478  -0.03367 -0.00815 240 ALA A CB  
1867 N N   . LYS A 241 ? 0.82853 0.56636 0.82855 0.21167  0.00201  -0.04413 241 LYS A N   
1868 C CA  . LYS A 241 ? 0.82837 0.57166 0.82427 0.22478  0.01250  -0.06278 241 LYS A CA  
1869 C C   . LYS A 241 ? 0.79159 0.55020 0.78787 0.19407  0.02272  -0.06326 241 LYS A C   
1870 O O   . LYS A 241 ? 0.69234 0.48176 0.70690 0.16872  0.02591  -0.05119 241 LYS A O   
1871 C CB  . LYS A 241 ? 0.80729 0.61446 0.83830 0.25292  0.02325  -0.07260 241 LYS A CB  
1872 C CG  . LYS A 241 ? 0.79325 0.59710 0.82995 0.28787  0.01196  -0.07319 241 LYS A CG  
1873 C CD  . LYS A 241 ? 0.90967 0.79291 0.99149 0.31041  0.02319  -0.08161 241 LYS A CD  
1874 C CE  . LYS A 241 ? 0.98141 0.86675 1.07103 0.35024  0.01041  -0.08421 241 LYS A CE  
1875 N NZ  . LYS A 241 ? 0.87393 0.84739 1.01469 0.36942  0.02139  -0.09217 241 LYS A NZ  
1876 N N   . LYS A 242 ? 0.86278 0.59773 0.83552 0.19912  0.02678  -0.07816 242 LYS A N   
1877 C CA  . LYS A 242 ? 0.82007 0.56479 0.78710 0.17415  0.03402  -0.08029 242 LYS A CA  
1878 C C   . LYS A 242 ? 0.84581 0.61170 0.80805 0.19306  0.04848  -0.09789 242 LYS A C   
1879 O O   . LYS A 242 ? 0.92441 0.67506 0.87417 0.22490  0.04978  -0.11186 242 LYS A O   
1880 C CB  . LYS A 242 ? 0.91589 0.59805 0.84786 0.15188  0.02002  -0.07896 242 LYS A CB  
1881 C CG  . LYS A 242 ? 0.96149 0.62856 0.89765 0.12708  0.00933  -0.05926 242 LYS A CG  
1882 C CD  . LYS A 242 ? 0.99387 0.62208 0.90711 0.09647  -0.00059 -0.05680 242 LYS A CD  
1883 C CE  . LYS A 242 ? 0.97651 0.64045 0.91272 0.06574  0.00128  -0.03897 242 LYS A CE  
1884 N NZ  . LYS A 242 ? 0.95924 0.61494 0.88564 0.03790  -0.00404 -0.04032 242 LYS A NZ  
1885 N N   . ILE A 243 ? 0.79031 0.59112 0.76015 0.17497  0.05986  -0.09671 243 ILE A N   
1886 C CA  . ILE A 243 ? 0.81342 0.63173 0.77146 0.18769  0.07488  -0.11104 243 ILE A CA  
1887 C C   . ILE A 243 ? 0.83383 0.59815 0.74678 0.17882  0.06574  -0.12141 243 ILE A C   
1888 O O   . ILE A 243 ? 0.72920 0.47318 0.63485 0.15044  0.05387  -0.11294 243 ILE A O   
1889 C CB  . ILE A 243 ? 0.72384 0.60489 0.70979 0.17302  0.09161  -0.10258 243 ILE A CB  
1890 C CG1 . ILE A 243 ? 0.71538 0.61303 0.68377 0.18502  0.10903  -0.11525 243 ILE A CG1 
1891 C CG2 . ILE A 243 ? 0.59610 0.47437 0.58345 0.13962  0.08422  -0.08880 243 ILE A CG2 
1892 C CD1 . ILE A 243 ? 0.64610 0.59490 0.63325 0.16793  0.12524  -0.10533 243 ILE A CD1 
1893 N N   . HIS A 244 ? 0.80810 0.55091 0.69066 0.20376  0.07058  -0.14067 244 HIS A N   
1894 C CA  . HIS A 244 ? 0.88840 0.57342 0.72219 0.19874  0.05925  -0.15444 244 HIS A CA  
1895 C C   . HIS A 244 ? 0.80048 0.51235 0.61772 0.19995  0.07440  -0.16316 244 HIS A C   
1896 O O   . HIS A 244 ? 0.79943 0.54859 0.62211 0.22444  0.09473  -0.17052 244 HIS A O   
1897 C CB  . HIS A 244 ? 0.99799 0.62130 0.79681 0.22849  0.04960  -0.17219 244 HIS A CB  
1898 C CG  . HIS A 244 ? 1.05236 0.64706 0.86309 0.23261  0.03593  -0.16260 244 HIS A CG  
1899 N ND1 . HIS A 244 ? 1.05944 0.62196 0.87087 0.20091  0.01838  -0.14729 244 HIS A ND1 
1900 C CD2 . HIS A 244 ? 1.11989 0.71496 0.94105 0.26557  0.03728  -0.16520 244 HIS A CD2 
1901 C CE1 . HIS A 244 ? 1.07403 0.61368 0.89148 0.21318  0.01000  -0.13996 244 HIS A CE1 
1902 N NE2 . HIS A 244 ? 1.13344 0.69112 0.95668 0.25331  0.01977  -0.15091 244 HIS A NE2 
1903 N N   . PHE A 245 ? 0.84742 0.54338 0.64489 0.17356  0.06463  -0.16134 245 PHE A N   
1904 C CA  . PHE A 245 ? 0.94597 0.65747 0.71822 0.17318  0.07491  -0.16871 245 PHE A CA  
1905 C C   . PHE A 245 ? 0.96090 0.60956 0.67541 0.18150  0.06124  -0.19090 245 PHE A C   
1906 O O   . PHE A 245 ? 1.00004 0.59387 0.69790 0.16833  0.03778  -0.19447 245 PHE A O   
1907 C CB  . PHE A 245 ? 0.86385 0.60234 0.65068 0.14096  0.07123  -0.15217 245 PHE A CB  
1908 C CG  . PHE A 245 ? 0.82427 0.61961 0.66032 0.13230  0.08427  -0.13217 245 PHE A CG  
1909 C CD1 . PHE A 245 ? 0.79757 0.59630 0.66733 0.12000  0.07509  -0.11868 245 PHE A CD1 
1910 C CD2 . PHE A 245 ? 0.74778 0.58967 0.59242 0.13491  0.10514  -0.12658 245 PHE A CD2 
1911 C CE1 . PHE A 245 ? 0.76040 0.60659 0.67043 0.11251  0.08505  -0.10253 245 PHE A CE1 
1912 C CE2 . PHE A 245 ? 0.86411 0.75140 0.75074 0.12465  0.11477  -0.10928 245 PHE A CE2 
1913 C CZ  . PHE A 245 ? 0.78173 0.67052 0.70058 0.11427  0.10389  -0.09845 245 PHE A CZ  
1914 N N   . ALA A 246 ? 1.09625 0.75175 0.77805 0.20193  0.07587  -0.20563 246 ALA A N   
1915 C CA  . ALA A 246 ? 1.09934 0.69660 0.71967 0.20801  0.06222  -0.22788 246 ALA A CA  
1916 C C   . ALA A 246 ? 1.12864 0.72407 0.73647 0.17501  0.04700  -0.22128 246 ALA A C   
1917 O O   . ALA A 246 ? 1.12028 0.76171 0.73467 0.16831  0.06060  -0.21108 246 ALA A O   
1918 C CB  . ALA A 246 ? 1.15613 0.76377 0.74167 0.24349  0.08463  -0.24617 246 ALA A CB  
1919 N N   . ARG A 247 ? 1.28748 0.83053 0.87817 0.15397  0.01814  -0.22615 247 ARG A N   
1920 C CA  . ARG A 247 ? 1.33756 0.88216 0.92234 0.12196  -0.00051 -0.22026 247 ARG A CA  
1921 C C   . ARG A 247 ? 1.46606 0.96401 0.98521 0.12852  -0.01411 -0.24475 247 ARG A C   
1922 O O   . ARG A 247 ? 1.53462 0.96753 1.01701 0.13617  -0.02988 -0.26454 247 ARG A O   
1923 C CB  . ARG A 247 ? 1.39163 0.91814 1.00518 0.09013  -0.02355 -0.20826 247 ARG A CB  
1924 C CG  . ARG A 247 ? 1.44994 0.95151 1.04226 0.06056  -0.05197 -0.21330 247 ARG A CG  
1925 C CD  . ARG A 247 ? 1.45209 0.96544 1.08812 0.02562  -0.06709 -0.19408 247 ARG A CD  
1926 N NE  . ARG A 247 ? 1.52388 1.01762 1.14514 -0.00464 -0.09584 -0.19938 247 ARG A NE  
1927 C CZ  . ARG A 247 ? 1.48262 1.01128 1.10232 -0.01561 -0.10309 -0.19749 247 ARG A CZ  
1928 N NH1 . ARG A 247 ? 1.47514 1.05162 1.09988 0.00118  -0.08333 -0.19046 247 ARG A NH1 
1929 N NH2 . ARG A 247 ? 1.44488 0.95954 1.05735 -0.04476 -0.13197 -0.20219 247 ARG A NH2 
1930 N N   . PHE A 248 ? 1.33470 0.86128 0.83473 0.12674  -0.00885 -0.24373 248 PHE A N   
1931 C CA  . PHE A 248 ? 1.51621 1.00329 0.95059 0.13197  -0.02301 -0.26598 248 PHE A CA  
1932 C C   . PHE A 248 ? 1.47758 0.97161 0.90776 0.10092  -0.04836 -0.26016 248 PHE A C   
1933 O O   . PHE A 248 ? 1.55664 1.00337 0.94111 0.09329  -0.07461 -0.27931 248 PHE A O   
1934 C CB  . PHE A 248 ? 1.55414 1.06414 0.95349 0.16322  0.00551  -0.27333 248 PHE A CB  
1935 C CG  . PHE A 248 ? 1.57191 1.06797 0.95870 0.19970  0.02659  -0.28812 248 PHE A CG  
1936 C CD1 . PHE A 248 ? 1.56439 1.00247 0.91061 0.21404  0.01283  -0.31146 248 PHE A CD1 
1937 C CD2 . PHE A 248 ? 1.52277 1.07529 0.95175 0.21592  0.05901  -0.27407 248 PHE A CD2 
1938 C CE1 . PHE A 248 ? 1.54747 0.99052 0.90111 0.24442  0.03137  -0.31776 248 PHE A CE1 
1939 C CE2 . PHE A 248 ? 1.43753 0.98921 0.86429 0.24963  0.07746  -0.28601 248 PHE A CE2 
1940 C CZ  . PHE A 248 ? 1.52260 1.02479 0.91807 0.26226  0.06308  -0.30518 248 PHE A CZ  
1941 N N   . ARG A 249 ? 1.29350 0.84502 0.76871 0.08440  -0.04244 -0.23536 249 ARG A N   
1942 C CA  . ARG A 249 ? 1.30035 0.86914 0.77806 0.05920  -0.06514 -0.22778 249 ARG A CA  
1943 C C   . ARG A 249 ? 1.26692 0.87501 0.81269 0.03460  -0.06886 -0.20371 249 ARG A C   
1944 O O   . ARG A 249 ? 1.11933 0.74034 0.70449 0.03793  -0.05268 -0.19275 249 ARG A O   
1945 C CB  . ARG A 249 ? 1.23683 0.83613 0.68613 0.07190  -0.05196 -0.22276 249 ARG A CB  
1946 C CG  . ARG A 249 ? 1.34515 0.94890 0.77334 0.05520  -0.07982 -0.22304 249 ARG A CG  
1947 C CD  . ARG A 249 ? 1.36356 0.99275 0.75974 0.07096  -0.06368 -0.21498 249 ARG A CD  
1948 N NE  . ARG A 249 ? 1.29757 0.95422 0.71222 0.08834  -0.02506 -0.20177 249 ARG A NE  
1949 C CZ  . ARG A 249 ? 1.37587 1.06017 0.77605 0.09832  -0.00400 -0.18766 249 ARG A CZ  
1950 N NH1 . ARG A 249 ? 1.27412 0.96091 0.63863 0.09595  -0.01726 -0.18356 249 ARG A NH1 
1951 N NH2 . ARG A 249 ? 1.43690 1.14653 0.85842 0.11006  0.03017  -0.17665 249 ARG A NH2 
1952 N N   . SER A 250 ? 1.25456 0.88352 0.81315 0.01129  -0.09106 -0.19617 250 SER A N   
1953 C CA  . SER A 250 ? 1.08094 0.75314 0.70134 -0.01013 -0.09436 -0.17393 250 SER A CA  
1954 C C   . SER A 250 ? 1.02635 0.75029 0.66482 -0.00056 -0.07619 -0.15499 250 SER A C   
1955 O O   . SER A 250 ? 1.02868 0.76582 0.64340 0.00151  -0.08467 -0.15445 250 SER A O   
1956 C CB  . SER A 250 ? 1.12659 0.79976 0.75695 -0.04020 -0.12818 -0.17587 250 SER A CB  
1957 O OG  . SER A 250 ? 1.04003 0.75856 0.73101 -0.05903 -0.12873 -0.15480 250 SER A OG  
1958 N N   . PHE A 251 ? 0.89646 0.64528 0.57322 0.00564  -0.05274 -0.13973 251 PHE A N   
1959 C CA  . PHE A 251 ? 0.84904 0.64177 0.54823 0.01078  -0.03694 -0.12019 251 PHE A CA  
1960 C C   . PHE A 251 ? 0.80283 0.62182 0.55934 -0.00117 -0.03352 -0.10433 251 PHE A C   
1961 O O   . PHE A 251 ? 0.73426 0.55703 0.51129 0.00674  -0.01413 -0.09903 251 PHE A O   
1962 C CB  . PHE A 251 ? 0.83527 0.62977 0.51402 0.03292  -0.00807 -0.11935 251 PHE A CB  
1963 C CG  . PHE A 251 ? 0.95686 0.78327 0.64002 0.03649  0.00411  -0.10142 251 PHE A CG  
1964 C CD1 . PHE A 251 ? 0.90841 0.75851 0.61264 0.02540  -0.01066 -0.08838 251 PHE A CD1 
1965 C CD2 . PHE A 251 ? 1.00001 0.83225 0.66580 0.05116  0.03053  -0.09723 251 PHE A CD2 
1966 C CE1 . PHE A 251 ? 0.88177 0.75190 0.58463 0.03084  -0.00098 -0.07214 251 PHE A CE1 
1967 C CE2 . PHE A 251 ? 0.96426 0.81744 0.62995 0.05181  0.04095  -0.07946 251 PHE A CE2 
1968 C CZ  . PHE A 251 ? 0.94615 0.81383 0.62792 0.04259  0.02428  -0.06722 251 PHE A CZ  
1969 N N   . PRO A 252 ? 0.72841 0.56895 0.51176 -0.01961 -0.05220 -0.09680 252 PRO A N   
1970 C CA  . PRO A 252 ? 0.75858 0.62243 0.59207 -0.03122 -0.04896 -0.08295 252 PRO A CA  
1971 C C   . PRO A 252 ? 0.69532 0.58780 0.55151 -0.01912 -0.02705 -0.06754 252 PRO A C   
1972 O O   . PRO A 252 ? 0.68569 0.58792 0.52538 -0.00702 -0.01848 -0.06337 252 PRO A O   
1973 C CB  . PRO A 252 ? 0.72871 0.61980 0.58263 -0.05061 -0.07194 -0.07829 252 PRO A CB  
1974 C CG  . PRO A 252 ? 0.68599 0.55297 0.49966 -0.05463 -0.09305 -0.09481 252 PRO A CG  
1975 C CD  . PRO A 252 ? 0.84147 0.68737 0.61018 -0.03092 -0.07844 -0.10207 252 PRO A CD  
1976 N N   . PHE A 253 ? 0.72163 0.62355 0.61273 -0.02354 -0.01886 -0.05879 253 PHE A N   
1977 C CA  . PHE A 253 ? 0.61515 0.53968 0.52748 -0.01383 -0.00025 -0.04606 253 PHE A CA  
1978 C C   . PHE A 253 ? 0.58317 0.53905 0.50549 -0.01302 -0.00359 -0.03460 253 PHE A C   
1979 O O   . PHE A 253 ? 0.60986 0.57208 0.52640 -0.00195 0.00902  -0.02784 253 PHE A O   
1980 C CB  . PHE A 253 ? 0.62388 0.55149 0.56806 -0.01938 0.00482  -0.03967 253 PHE A CB  
1981 C CG  . PHE A 253 ? 0.55651 0.50611 0.52251 -0.01137 0.02032  -0.02804 253 PHE A CG  
1982 C CD1 . PHE A 253 ? 0.55652 0.50058 0.51720 0.00116  0.03664  -0.02971 253 PHE A CD1 
1983 C CD2 . PHE A 253 ? 0.54941 0.52663 0.54139 -0.01650 0.01819  -0.01627 253 PHE A CD2 
1984 C CE1 . PHE A 253 ? 0.59429 0.55644 0.57469 0.00526  0.04808  -0.02001 253 PHE A CE1 
1985 C CE2 . PHE A 253 ? 0.61587 0.60686 0.62270 -0.00896 0.03031  -0.00771 253 PHE A CE2 
1986 C CZ  . PHE A 253 ? 0.59284 0.57447 0.59370 0.00032  0.04403  -0.00966 253 PHE A CZ  
1987 N N   . TRP A 254 ? 0.56469 0.54033 0.50185 -0.02451 -0.02100 -0.03214 254 TRP A N   
1988 C CA  . TRP A 254 ? 0.61536 0.62336 0.56398 -0.01930 -0.02534 -0.02180 254 TRP A CA  
1989 C C   . TRP A 254 ? 0.60239 0.60308 0.51471 -0.00850 -0.03122 -0.02442 254 TRP A C   
1990 O O   . TRP A 254 ? 0.56395 0.57651 0.47321 0.00328  -0.02805 -0.01484 254 TRP A O   
1991 C CB  . TRP A 254 ? 0.51013 0.55093 0.49013 -0.03358 -0.04135 -0.01828 254 TRP A CB  
1992 C CG  . TRP A 254 ? 0.60369 0.65353 0.61630 -0.04412 -0.03376 -0.01214 254 TRP A CG  
1993 C CD1 . TRP A 254 ? 0.58235 0.62977 0.60933 -0.06475 -0.04223 -0.01403 254 TRP A CD1 
1994 C CD2 . TRP A 254 ? 0.49882 0.55743 0.52900 -0.03537 -0.01689 -0.00261 254 TRP A CD2 
1995 N NE1 . TRP A 254 ? 0.58917 0.64431 0.64022 -0.06835 -0.03043 -0.00472 254 TRP A NE1 
1996 C CE2 . TRP A 254 ? 0.59597 0.65908 0.64916 -0.04961 -0.01542 0.00135  254 TRP A CE2 
1997 C CE3 . TRP A 254 ? 0.56223 0.62198 0.58809 -0.01825 -0.00407 0.00304  254 TRP A CE3 
1998 C CZ2 . TRP A 254 ? 0.47767 0.54863 0.54776 -0.04481 -0.00181 0.00995  254 TRP A CZ2 
1999 C CZ3 . TRP A 254 ? 0.45666 0.52313 0.50126 -0.01504 0.00801  0.01004  254 TRP A CZ3 
2000 C CH2 . TRP A 254 ? 0.52066 0.59384 0.58631 -0.02703 0.00898  0.01306  254 TRP A CH2 
2001 N N   . ARG A 255 ? 0.63898 0.61599 0.51897 -0.01126 -0.04054 -0.03726 255 ARG A N   
2002 C CA  . ARG A 255 ? 0.67609 0.64067 0.51289 0.00083  -0.04294 -0.03941 255 ARG A CA  
2003 C C   . ARG A 255 ? 0.62338 0.57143 0.44119 0.01347  -0.01779 -0.03431 255 ARG A C   
2004 O O   . ARG A 255 ? 0.65623 0.60288 0.45101 0.02370  -0.01349 -0.02577 255 ARG A O   
2005 C CB  . ARG A 255 ? 0.72744 0.66774 0.52943 -0.00438 -0.05870 -0.05638 255 ARG A CB  
2006 C CG  . ARG A 255 ? 0.84345 0.77149 0.59504 0.00800  -0.06440 -0.05898 255 ARG A CG  
2007 C CD  . ARG A 255 ? 0.84904 0.75492 0.56694 0.00148  -0.08569 -0.07767 255 ARG A CD  
2008 N NE  . ARG A 255 ? 0.93080 0.80204 0.59277 0.01483  -0.07426 -0.08761 255 ARG A NE  
2009 C CZ  . ARG A 255 ? 0.98130 0.82052 0.60683 0.01320  -0.08489 -0.10751 255 ARG A CZ  
2010 N NH1 . ARG A 255 ? 0.96487 0.79723 0.60345 -0.00440 -0.10883 -0.11940 255 ARG A NH1 
2011 N NH2 . ARG A 255 ? 0.97719 0.78937 0.55031 0.02902  -0.07072 -0.11574 255 ARG A NH2 
2012 N N   . ARG A 256 ? 0.60321 0.53935 0.43091 0.01235  -0.00156 -0.03857 256 ARG A N   
2013 C CA  . ARG A 256 ? 0.64575 0.57652 0.46651 0.02124  0.02284  -0.03291 256 ARG A CA  
2014 C C   . ARG A 256 ? 0.73085 0.67889 0.57459 0.02252  0.02969  -0.01663 256 ARG A C   
2015 O O   . ARG A 256 ? 0.66291 0.60554 0.48924 0.02806  0.04255  -0.00798 256 ARG A O   
2016 C CB  . ARG A 256 ? 0.69605 0.61828 0.53113 0.02124  0.03542  -0.04102 256 ARG A CB  
2017 C CG  . ARG A 256 ? 0.88132 0.79419 0.69221 0.03192  0.05646  -0.04523 256 ARG A CG  
2018 C CD  . ARG A 256 ? 0.85765 0.75370 0.66448 0.03741  0.05954  -0.06123 256 ARG A CD  
2019 N NE  . ARG A 256 ? 0.76745 0.67026 0.61413 0.03471  0.06226  -0.05932 256 ARG A NE  
2020 C CZ  . ARG A 256 ? 0.78636 0.67500 0.64491 0.02822  0.04773  -0.06527 256 ARG A CZ  
2021 N NH1 . ARG A 256 ? 0.82030 0.68845 0.65824 0.02109  0.02851  -0.07452 256 ARG A NH1 
2022 N NH2 . ARG A 256 ? 0.76767 0.66130 0.65777 0.02751  0.05163  -0.06134 256 ARG A NH2 
2023 N N   . VAL A 257 ? 0.66332 0.62992 0.54330 0.01704  0.02140  -0.01218 257 VAL A N   
2024 C CA  . VAL A 257 ? 0.59904 0.57852 0.49649 0.02100  0.02553  0.00088  257 VAL A CA  
2025 C C   . VAL A 257 ? 0.59155 0.57124 0.46552 0.02969  0.01526  0.00792  257 VAL A C   
2026 O O   . VAL A 257 ? 0.57286 0.54275 0.43471 0.03656  0.02319  0.01820  257 VAL A O   
2027 C CB  . VAL A 257 ? 0.57164 0.57291 0.50934 0.01534  0.01990  0.00288  257 VAL A CB  
2028 C CG1 . VAL A 257 ? 0.43830 0.45179 0.38806 0.02329  0.02109  0.01393  257 VAL A CG1 
2029 C CG2 . VAL A 257 ? 0.50083 0.49663 0.45701 0.00962  0.03084  -0.00110 257 VAL A CG2 
2030 N N   . HIS A 258 ? 0.57609 0.56474 0.44183 0.02926  -0.00416 0.00267  258 HIS A N   
2031 C CA  . HIS A 258 ? 0.67025 0.66102 0.51255 0.04044  -0.01742 0.00895  258 HIS A CA  
2032 C C   . HIS A 258 ? 0.68770 0.64763 0.48166 0.04768  -0.00718 0.01348  258 HIS A C   
2033 O O   . HIS A 258 ? 0.74707 0.69617 0.52304 0.05781  -0.00566 0.02573  258 HIS A O   
2034 C CB  . HIS A 258 ? 0.66780 0.67646 0.51030 0.03637  -0.04191 0.00033  258 HIS A CB  
2035 C CG  . HIS A 258 ? 0.62590 0.63305 0.43477 0.04939  -0.05799 0.00420  258 HIS A CG  
2036 N ND1 . HIS A 258 ? 0.82258 0.80220 0.58049 0.05309  -0.05979 0.00010  258 HIS A ND1 
2037 C CD2 . HIS A 258 ? 0.62873 0.65866 0.44526 0.06205  -0.07355 0.01184  258 HIS A CD2 
2038 C CE1 . HIS A 258 ? 0.66208 0.64500 0.39577 0.06632  -0.07691 0.00599  258 HIS A CE1 
2039 N NE2 . HIS A 258 ? 0.80108 0.81490 0.57107 0.07287  -0.08613 0.01297  258 HIS A NE2 
2040 N N   . ASP A 259 ? 0.62327 0.56665 0.39293 0.04318  0.00064  0.00410  259 ASP A N   
2041 C CA  . ASP A 259 ? 0.78863 0.70691 0.50961 0.04920  0.01266  0.00874  259 ASP A CA  
2042 C C   . ASP A 259 ? 0.75006 0.65897 0.47512 0.04782  0.03633  0.02158  259 ASP A C   
2043 O O   . ASP A 259 ? 0.78219 0.67170 0.47153 0.05209  0.04351  0.03360  259 ASP A O   
2044 C CB  . ASP A 259 ? 0.82759 0.73376 0.52300 0.04705  0.01783  -0.00625 259 ASP A CB  
2045 C CG  . ASP A 259 ? 0.77717 0.68503 0.46077 0.04587  -0.00826 -0.02011 259 ASP A CG  
2046 O OD1 . ASP A 259 ? 0.77096 0.68990 0.45254 0.04933  -0.02951 -0.01556 259 ASP A OD1 
2047 O OD2 . ASP A 259 ? 0.89649 0.79413 0.57248 0.04195  -0.00871 -0.03602 259 ASP A OD2 
2048 N N   . SER A 260 ? 0.73098 0.65182 0.49736 0.04058  0.04739  0.01995  260 SER A N   
2049 C CA  . SER A 260 ? 0.69813 0.61271 0.47142 0.03598  0.06825  0.03009  260 SER A CA  
2050 C C   . SER A 260 ? 0.71342 0.62062 0.49279 0.03871  0.06338  0.04365  260 SER A C   
2051 O O   . SER A 260 ? 0.77820 0.66677 0.54151 0.03514  0.07590  0.05554  260 SER A O   
2052 C CB  . SER A 260 ? 0.71020 0.64055 0.52332 0.02889  0.07948  0.02228  260 SER A CB  
2053 O OG  . SER A 260 ? 0.88782 0.81947 0.69184 0.02984  0.08522  0.00924  260 SER A OG  
2054 N N   . PHE A 261 ? 0.70253 0.62320 0.50363 0.04487  0.04587  0.04215  261 PHE A N   
2055 C CA  . PHE A 261 ? 0.67515 0.58927 0.48461 0.05121  0.04188  0.05198  261 PHE A CA  
2056 C C   . PHE A 261 ? 0.77403 0.68502 0.56384 0.06736  0.02264  0.05738  261 PHE A C   
2057 O O   . PHE A 261 ? 0.74063 0.62849 0.51376 0.07622  0.02140  0.06816  261 PHE A O   
2058 C CB  . PHE A 261 ? 0.66735 0.60420 0.52315 0.04840  0.04128  0.04660  261 PHE A CB  
2059 C CG  . PHE A 261 ? 0.58848 0.52593 0.46422 0.03601  0.05815  0.04382  261 PHE A CG  
2060 C CD1 . PHE A 261 ? 0.68977 0.60773 0.55879 0.03040  0.07027  0.05190  261 PHE A CD1 
2061 C CD2 . PHE A 261 ? 0.58387 0.54046 0.48480 0.02966  0.06029  0.03340  261 PHE A CD2 
2062 C CE1 . PHE A 261 ? 0.63317 0.55883 0.52483 0.01900  0.08377  0.04893  261 PHE A CE1 
2063 C CE2 . PHE A 261 ? 0.58872 0.54854 0.50858 0.02176  0.07383  0.03079  261 PHE A CE2 
2064 C CZ  . PHE A 261 ? 0.57572 0.52411 0.49322 0.01661  0.08534  0.03822  261 PHE A CZ  
2065 N N   . ILE A 262 ? 0.69234 0.62488 0.48341 0.07185  0.00606  0.04996  262 ILE A N   
2066 C CA  . ILE A 262 ? 0.75883 0.69623 0.53505 0.08912  -0.01449 0.05457  262 ILE A CA  
2067 C C   . ILE A 262 ? 0.93869 0.84231 0.65782 0.09545  -0.01596 0.06274  262 ILE A C   
2068 O O   . ILE A 262 ? 1.05793 0.93120 0.74921 0.10600  -0.01525 0.07594  262 ILE A O   
2069 C CB  . ILE A 262 ? 0.71736 0.69652 0.52096 0.08855  -0.03361 0.04387  262 ILE A CB  
2070 C CG1 . ILE A 262 ? 0.67411 0.68369 0.53020 0.07930  -0.02861 0.03827  262 ILE A CG1 
2071 C CG2 . ILE A 262 ? 0.70234 0.69676 0.49868 0.10859  -0.05589 0.04861  262 ILE A CG2 
2072 C CD1 . ILE A 262 ? 0.57618 0.59064 0.45087 0.09179  -0.02524 0.04551  262 ILE A CD1 
2073 N N   . GLU A 263 ? 0.79321 0.69770 0.49025 0.08952  -0.01848 0.05505  263 GLU A N   
2074 C CA  . GLU A 263 ? 1.06656 0.93838 0.70462 0.09257  -0.01434 0.06191  263 GLU A CA  
2075 C C   . GLU A 263 ? 1.07052 0.94965 0.69108 0.08675  -0.01878 0.04764  263 GLU A C   
2076 O O   . GLU A 263 ? 1.05424 0.96111 0.70124 0.08397  -0.03565 0.03427  263 GLU A O   
2077 C CB  . GLU A 263 ? 1.09050 0.94527 0.69210 0.11243  -0.03283 0.07420  263 GLU A CB  
2078 C CG  . GLU A 263 ? 1.24708 1.05777 0.78170 0.11508  -0.02405 0.08759  263 GLU A CG  
2079 C CD  . GLU A 263 ? 1.26995 1.05140 0.79742 0.10132  0.00507  0.09947  263 GLU A CD  
2080 O OE1 . GLU A 263 ? 1.18989 0.97588 0.75704 0.09583  0.01256  0.10056  263 GLU A OE1 
2081 O OE2 . GLU A 263 ? 1.14724 0.90298 0.62878 0.09510  0.02046  0.10778  263 GLU A OE2 
2082 N N   . ASP A 264 ? 1.19065 1.04403 0.76496 0.08426  -0.00356 0.05025  264 ASP A N   
2083 C CA  . ASP A 264 ? 1.13060 0.98384 0.67778 0.08223  -0.00698 0.03531  264 ASP A CA  
2084 C C   . ASP A 264 ? 1.38785 1.21758 0.86822 0.09438  -0.01810 0.04156  264 ASP A C   
2085 O O   . ASP A 264 ? 1.38585 1.19815 0.82046 0.09413  -0.00622 0.03800  264 ASP A O   
2086 C CB  . ASP A 264 ? 1.08224 0.93061 0.63016 0.07206  0.02207  0.02950  264 ASP A CB  
2087 C CG  . ASP A 264 ? 1.24205 1.09468 0.78196 0.07033  0.01664  0.00780  264 ASP A CG  
2088 O OD1 . ASP A 264 ? 1.30704 1.16648 0.84502 0.07239  -0.01074 -0.00285 264 ASP A OD1 
2089 O OD2 . ASP A 264 ? 1.24282 1.09210 0.77862 0.06721  0.03890  0.00083  264 ASP A OD2 
# 
