data_8QGA
# 
_entry.id   8QGA 
# 
_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   8QGA         pdb_00008qga 10.2210/pdb8qga/pdb 
WWPDB D_1292133130 ?            ?                   
# 
_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                        8QGA 
_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 
;1-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-naphthalen-1-yl-urea
;
751.751   1  ?        ? ? ? 
4 water       nat water 18.015    14 ?        ? ? ? 
# 
_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 
;1-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-naphthalen-1-yl-urea
;
UV0 
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 
UV0 non-polymer         . 
;1-[[(2~{R},3~{S},4~{R},5~{R})-5-[8-[3-[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl-methyl-amino]prop-1-ynyl]-6-azanyl-purin-9-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methyl]-3-naphthalen-1-yl-urea
;
? 'C35 H37 N13 O7' 751.751 
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 ?   ?   ?   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 ?   ?   ?   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        UV0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   UV0 
_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 UV0 1  302 1  UV0 DRG A . 
D 4 HOH 1  401 6  HOH HOH A . 
D 4 HOH 2  402 12 HOH HOH A . 
D 4 HOH 3  403 5  HOH HOH A . 
D 4 HOH 4  404 1  HOH HOH A . 
D 4 HOH 5  405 10 HOH HOH A . 
D 4 HOH 6  406 9  HOH HOH A . 
D 4 HOH 7  407 3  HOH HOH A . 
D 4 HOH 8  408 8  HOH HOH A . 
D 4 HOH 9  409 4  HOH HOH A . 
D 4 HOH 10 410 2  HOH HOH A . 
D 4 HOH 11 411 19 HOH HOH A . 
D 4 HOH 12 412 26 HOH HOH A . 
D 4 HOH 13 413 24 HOH HOH A . 
D 4 HOH 14 414 27 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 114 ? CG  ? A LYS 114 CG  
6  1 Y 1 A LYS 114 ? CD  ? A LYS 114 CD  
7  1 Y 1 A LYS 114 ? CE  ? A LYS 114 CE  
8  1 Y 1 A LYS 114 ? NZ  ? A LYS 114 NZ  
9  1 Y 1 A ARG 190 ? CG  ? A ARG 190 CG  
10 1 Y 1 A ARG 190 ? CD  ? A ARG 190 CD  
11 1 Y 1 A ARG 190 ? NE  ? A ARG 190 NE  
12 1 Y 1 A ARG 190 ? CZ  ? A ARG 190 CZ  
13 1 Y 1 A ARG 190 ? NH1 ? A ARG 190 NH1 
14 1 Y 1 A ARG 190 ? NH2 ? A ARG 190 NH2 
15 1 Y 1 A ARG 193 ? CD  ? A ARG 193 CD  
16 1 Y 1 A ARG 193 ? NE  ? A ARG 193 NE  
17 1 Y 1 A ARG 193 ? CZ  ? A ARG 193 CZ  
18 1 Y 1 A ARG 193 ? NH1 ? A ARG 193 NH1 
19 1 Y 1 A ARG 193 ? NH2 ? A ARG 193 NH2 
20 1 Y 1 A GLN 232 ? CG  ? A GLN 232 CG  
21 1 Y 1 A GLN 232 ? CD  ? A GLN 232 CD  
22 1 Y 1 A GLN 232 ? OE1 ? A GLN 232 OE1 
23 1 Y 1 A GLN 232 ? NE2 ? A GLN 232 NE2 
24 1 Y 1 A ARG 249 ? CG  ? A ARG 249 CG  
25 1 Y 1 A ARG 249 ? CD  ? A ARG 249 CD  
26 1 Y 1 A ARG 249 ? NE  ? A ARG 249 NE  
27 1 Y 1 A ARG 249 ? CZ  ? A ARG 249 CZ  
28 1 Y 1 A ARG 249 ? NH1 ? A ARG 249 NH1 
29 1 Y 1 A ARG 249 ? NH2 ? A ARG 249 NH2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .           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                     8QGA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.990 
_cell.length_a_esd                 ? 
_cell.length_b                     74.660 
_cell.length_b_esd                 ? 
_cell.length_c                     118.337 
_cell.length_c_esd                 ? 
_cell.volume                       556519.229 
_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                         8QGA 
_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                   8QGA 
_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             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.11 
_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         2014-11-07 
_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   0.97625 
_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                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97625 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          47.83 
_reflns.entry_id                                       8QGA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.23 
_reflns.d_resolution_low                               48.14 
_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                                     13674 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_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                                0.064 
_reflns.pdbx_Rpim_I_all                                0.031 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       56242 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.056 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.23 
_reflns_shell.d_res_low                                     2.31 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           4804 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1210 
_reflns_shell.percent_possible_obs                          89.5 
_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                               4.0 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.0 
_reflns_shell.pdbx_Rrim_I_all                               5.452 
_reflns_shell.pdbx_Rpim_I_all                               2.688 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.891 
_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                                  4.693 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               69.16 
_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                                 8QGA 
_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                            2.39 
_refine.ls_d_res_low                             37.34 
_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                     11218 
_refine.ls_number_reflns_R_free                  547 
_refine.ls_number_reflns_R_work                  10671 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.42 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2246 
_refine.ls_R_factor_R_free                       0.2597 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2228 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_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                 32.0922 
_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                            0.2948 
_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                       2.39 
_refine_hist.d_res_low                        37.34 
_refine_hist.number_atoms_solvent             14 
_refine_hist.number_atoms_total               2131 
_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        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         68 
_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' ? 0.0039  ? 2188 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.6107  ? 2971 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0486  ? 324  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0043  ? 373  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9371 ? 787  ? 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' 2.39 2.63  . . 147 2622 99.14 . . . . 0.2949 . . . . . . . . . . . 0.3421 
'X-RAY DIFFRACTION' 2.63 3.01  . . 145 2613 98.57 . . . . 0.2805 . . . . . . . . . . . 0.3648 
'X-RAY DIFFRACTION' 3.01 3.79  . . 118 2660 97.64 . . . . 0.2294 . . . . . . . . . . . 0.2686 
'X-RAY DIFFRACTION' 3.79 37.34 . . 137 2776 98.35 . . . . 0.1939 . . . . . . . . . . . 0.2172 
# 
_struct.entry_id                     8QGA 
_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        8QGA 
_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              8QGA 
_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 8QGA LEU A 265 ? UNP Q8Y8D7 ? ? 'expression tag' 265 1 
1 8QGA GLU A 266 ? UNP Q8Y8D7 ? ? 'expression tag' 266 2 
1 8QGA HIS A 267 ? UNP Q8Y8D7 ? ? 'expression tag' 267 3 
1 8QGA HIS A 268 ? UNP Q8Y8D7 ? ? 'expression tag' 268 4 
1 8QGA HIS A 269 ? UNP Q8Y8D7 ? ? 'expression tag' 269 5 
1 8QGA HIS A 270 ? UNP Q8Y8D7 ? ? 'expression tag' 270 6 
1 8QGA HIS A 271 ? UNP Q8Y8D7 ? ? 'expression tag' 271 7 
1 8QGA HIS A 272 ? UNP Q8Y8D7 ? ? 'expression tag' 272 8 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10340 ? 
1 MORE         -47   ? 
1 'SSA (A^2)'  39980 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      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 62.9900000000 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 62.9900000000 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  ? GLU A 26  ? ASP A 10  GLU A 26  1 ? 17 
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 PRO A 157 ? THR A 161 ? PRO A 157 THR A 161 5 ? 5  
HELX_P HELX_P7 AA7 ALA A 162 ? LEU A 167 ? ALA A 162 LEU A 167 1 ? 6  
HELX_P HELX_P8 AA8 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 ? 3 ? 
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      
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 TYR A 3   ? SER A 7   ? TYR A 3   SER A 7   
AA1 2 ILE A 38  ? GLY A 43  ? ILE A 38  GLY A 43  
AA1 3 ALA A 63  ? HIS A 68  ? ALA A 63  HIS A 68  
AA2 1 ALA A 116 ? ALA A 120 ? ALA A 116 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 ? PRO A 202 ? LEU A 199 PRO A 202 
AA3 2 ALA A 178 ? MET A 184 ? ALA A 178 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 N THR A 6   ? N THR A 6   O ILE A 40  ? O ILE A 40  
AA1 2 3 N SER A 41  ? N SER A 41  O ILE A 65  ? O ILE A 65  
AA2 1 2 O ALA A 116 ? O ALA A 116 N VAL A 107 ? N VAL A 107 
AA2 2 3 N VAL A 98  ? N VAL A 98  O PHE A 245 ? O PHE A 245 
AA2 3 4 O ILE A 234 ? O ILE A 234 N LEU A 209 ? N LEU A 209 
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 THR A 125 ? N THR A 125 O SER A 220 ? O SER A 220 
AA3 5 6 N VAL A 221 ? N VAL A 221 O LEU A 224 ? O LEU A 224 
# 
_pdbx_entry_details.entry_id                   8QGA 
_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 ASP A 77  ? ? -102.24 45.22   
2 1 ASN A 122 ? ? -99.17  -65.44  
3 1 SER A 129 ? ? -77.43  21.08   
4 1 ALA A 162 ? ? -101.92 -126.80 
5 1 ASN A 189 ? ? -145.18 -154.80 
6 1 VAL A 212 ? ? -102.47 -61.53  
7 1 ASN A 213 ? ? -122.08 -77.67  
8 1 ASP A 222 ? ? 57.30   -112.46 
9 1 ILE A 262 ? ? -93.07  -71.39  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     405 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 8.8010738786  21.8294294605 28.4047263497  0.580148920278 ? 0.131104877069   ? 0.00844069081015 ? 
0.811082339406 ? -0.117898245772 ? 0.469628544549 ? 6.60812909051  ? -1.04353535649  ? -0.290278847825 ? 4.51046447827 ? 
3.3692415275     ? 7.23518140564 ? -0.0907884568983 ? -1.36069386265  ? 0.0873101531869 ? 0.347866206613  ? 0.283525721127   ? 
-0.149914590439 ? -0.430593063644 ? -0.167998313033 ? 0.0333281426017  ? 
2 'X-RAY DIFFRACTION' ? refined 6.83949667149 32.9041248146 25.0351900525  0.879191571687 ? -0.0271288083004 ? 0.188905285497   ? 
1.49371924322  ? -0.432594603272 ? 0.815409504831 ? 0.773896336487 ? -0.447072033557 ? 1.28797470232   ? 3.11049354872 ? 
-2.90686723122   ? 3.84645519899 ? 0.586524091043   ? -0.758149327194 ? 1.06483436621   ? 0.611857280337  ? 1.20425406404    ? 
0.24420889527   ? -1.76721552376  ? -0.306505217424 ? -0.852716303507  ? 
3 'X-RAY DIFFRACTION' ? refined 12.2729563141 23.2948001326 15.7553414624  0.599575866561 ? 0.132444087152   ? 0.042780969823   ? 
0.781765026944 ? -0.112689328119 ? 0.516472214852 ? 2.70126680234  ? 1.39697394843   ? -2.21221419764  ? 2.00507948884 ? 
-0.605549501744  ? 5.78749060248 ? -0.0597874855349 ? -0.258834602535 ? 0.315953001017  ? 0.391169001471  ? 0.218000169416   ? 
0.235683347765  ? -0.532432895002 ? 0.151534822765  ? 0.0626173920035  ? 
4 'X-RAY DIFFRACTION' ? refined 20.4100771926 21.505252262  26.4188889215  0.564875335162 ? 0.0939907170789  ? 0.0763934627305  ? 
1.10018885085  ? -0.177683607513 ? 0.65945849764  ? 6.55859553352  ? -3.28100952225  ? -3.85810606122  ? 6.85622400551 ? 
4.98972935715    ? 9.46610244245 ? -0.209203406288  ? -1.77221764999  ? 1.38367603011   ? 0.636623133728  ? 1.40238261057    ? 
-1.16786728562  ? -0.520719780402 ? 2.29365055531   ? -1.08376926543   ? 
5 'X-RAY DIFFRACTION' ? refined 17.5165203462 14.9587525938 -2.27375464253 0.312759168321 ? 0.0805413076406  ? 0.0190025261957  ? 
0.56515456375  ? 0.0259849209797 ? 0.447002039069 ? 1.82462677553  ? -0.45064327613  ? -0.73487782577  ? 2.98671935368 ? 
1.31853704222    ? 4.62438673529 ? 0.181749358287   ? 0.22918592171   ? 0.266072535049  ? -0.232694540607 ? -0.109722580437  ? 
0.207837660242  ? -0.419266272217 ? -0.401846460679 ? 0.0307520827935  ? 
6 'X-RAY DIFFRACTION' ? refined 18.0667603122 12.3407113193 -5.84468851345 0.362761251338 ? 0.100328478599   ? 0.0171685814863  ? 
0.679896122796 ? 0.0461205275678 ? 0.434640250977 ? 3.02565298268  ? -0.2821145455   ? 0.556209430518  ? 3.76681084925 ? 
-0.0944367061083 ? 3.50323282562 ? 0.162517781869   ? 0.179182115415  ? 0.0843061996303 ? -0.167520375686 ? -0.0612570540991 ? 
0.562204475155  ? -0.134489632645 ? -0.696847102448 ? -0.0320226802376 ? 
7 'X-RAY DIFFRACTION' ? refined 26.9470194464 19.9072582743 15.6955812023  0.635109508674 ? -0.0929554493262 ? 0.0942404157153  ? 
0.522228159124 ? -0.132221445233 ? 0.459500823229 ? 6.02373195883  ? -3.82885206984  ? 2.02952050615   ? 5.01019442225 ? 
-0.798829097646  ? 5.51220035902 ? -0.269433763454  ? -0.725622041039 ? 0.800702523372  ? 0.481890870146  ? 0.161595409651   ? 
-0.591999318279 ? -0.73173661156  ? 0.146678324723  ? 0.0892786900601  ? 
# 
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 25  A 25  ? ? 
;chain 'A' and (resid    1  through   25 )
;
2 'X-RAY DIFFRACTION' 2 A 26  A 26  ? A 37  A 37  ? ? 
;chain 'A' and (resid   26  through   37 )
;
3 'X-RAY DIFFRACTION' 3 A 38  A 38  ? A 68  A 68  ? ? 
;chain 'A' and (resid   38  through   68 )
;
4 'X-RAY DIFFRACTION' 4 A 69  A 69  ? A 92  A 92  ? ? 
;chain 'A' and (resid   69  through   92 )
;
5 'X-RAY DIFFRACTION' 5 A 93  A 93  ? A 163 A 167 ? ? 
;chain 'A' and (resid   93  through  167 )
;
6 'X-RAY DIFFRACTION' 6 A 164 A 168 ? A 234 A 238 ? ? 
;chain 'A' and (resid  168  through  238 )
;
7 'X-RAY DIFFRACTION' 7 A 235 A 239 ? A 259 A 263 ? ? 
;chain 'A' and (resid  239  through  263 )
;
# 
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 GLY 110 ? A GLY 110 
2  1 Y 1 A ILE 111 ? A ILE 111 
3  1 Y 1 A GLY 112 ? A GLY 112 
4  1 Y 1 A LYS 113 ? A LYS 113 
5  1 Y 1 A ASP 264 ? A ASP 264 
6  1 Y 1 A LEU 265 ? A LEU 265 
7  1 Y 1 A GLU 266 ? A GLU 266 
8  1 Y 1 A HIS 267 ? A HIS 267 
9  1 Y 1 A HIS 268 ? A HIS 268 
10 1 Y 1 A HIS 269 ? A HIS 269 
11 1 Y 1 A HIS 270 ? A HIS 270 
12 1 Y 1 A HIS 271 ? A HIS 271 
13 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 
UV0 C4   C Y N 393 
UV0 C5   C Y N 394 
UV0 C6   C Y N 395 
UV0 C8   C Y N 396 
UV0 N1   N Y N 397 
UV0 N3   N Y N 398 
UV0 C2   C Y N 399 
UV0 CAA  C N N 400 
UV0 CAC  C N N 401 
UV0 CAD  C N N 402 
UV0 CAE  C N N 403 
UV0 CAP  C N R 404 
UV0 CAR  C N R 405 
UV0 CAS  C N N 406 
UV0 CAU  C N N 407 
UV0 CAX  C Y N 408 
UV0 CAY  C Y N 409 
UV0 CAZ  C Y N 410 
UV0 CBA  C Y N 411 
UV0 CBB  C Y N 412 
UV0 CBC  C Y N 413 
UV0 CBD  C Y N 414 
UV0 CBE  C Y N 415 
UV0 CBF  C Y N 416 
UV0 CBG  C Y N 417 
UV0 CBH  C N S 418 
UV0 CBJ  C N R 419 
UV0 CBL  C N N 420 
UV0 CBM  C N R 421 
UV0 CBO  C N R 422 
UV0 CBP  C N R 423 
UV0 CBR  C N S 424 
UV0 CBU  C Y N 425 
UV0 CBW  C Y N 426 
UV0 CBX  C Y N 427 
UV0 CBZ  C Y N 428 
UV0 CCB  C Y N 429 
UV0 N6   N N N 430 
UV0 N7   N Y N 431 
UV0 N9   N Y N 432 
UV0 NAB  N N N 433 
UV0 NAT  N N N 434 
UV0 NAW  N N N 435 
UV0 NBT  N Y N 436 
UV0 NBV  N Y N 437 
UV0 NBY  N Y N 438 
UV0 NCA  N Y N 439 
UV0 NCC  N N N 440 
UV0 OAQ  O N N 441 
UV0 OAV  O N N 442 
UV0 OBI  O N N 443 
UV0 OBK  O N N 444 
UV0 OBN  O N N 445 
UV0 OBQ  O N N 446 
UV0 OBS  O N N 447 
UV0 H1   H N N 448 
UV0 H2   H N N 449 
UV0 H3   H N N 450 
UV0 H4   H N N 451 
UV0 H5   H N N 452 
UV0 H6   H N N 453 
UV0 H7   H N N 454 
UV0 H8   H N N 455 
UV0 H9   H N N 456 
UV0 H10  H N N 457 
UV0 H11  H N N 458 
UV0 H12  H N N 459 
UV0 H13  H N N 460 
UV0 H14  H N N 461 
UV0 H15  H N N 462 
UV0 H16  H N N 463 
UV0 H17  H N N 464 
UV0 H18  H N N 465 
UV0 H19  H N N 466 
UV0 H20  H N N 467 
UV0 H21  H N N 468 
UV0 H22  H N N 469 
UV0 H23  H N N 470 
UV0 H24  H N N 471 
UV0 H25  H N N 472 
UV0 H26  H N N 473 
UV0 H27  H N N 474 
UV0 H28  H N N 475 
UV0 H29  H N N 476 
UV0 H31  H N N 477 
UV0 H32  H N N 478 
UV0 H33  H N N 479 
UV0 H34  H N N 480 
UV0 H35  H N N 481 
UV0 H36  H N N 482 
UV0 H37  H N N 483 
UV0 H38  H N N 484 
VAL N    N N N 485 
VAL CA   C N S 486 
VAL C    C N N 487 
VAL O    O N N 488 
VAL CB   C N N 489 
VAL CG1  C N N 490 
VAL CG2  C N N 491 
VAL OXT  O N N 492 
VAL H    H N N 493 
VAL H2   H N N 494 
VAL HA   H N N 495 
VAL HB   H N N 496 
VAL HG11 H N N 497 
VAL HG12 H N N 498 
VAL HG13 H N N 499 
VAL HG21 H N N 500 
VAL HG22 H N N 501 
VAL HG23 H N N 502 
VAL HXT  H N N 503 
# 
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 
UV0 NCC CCB  sing N N 378 
UV0 NBV CBU  doub Y N 379 
UV0 NBV CBW  sing Y N 380 
UV0 CCB CBW  doub Y N 381 
UV0 CCB NCA  sing Y N 382 
UV0 OBQ CBP  sing N N 383 
UV0 CBU NBT  sing Y N 384 
UV0 CBW CBX  sing Y N 385 
UV0 CBP CBR  sing N N 386 
UV0 CBP CBO  sing N N 387 
UV0 NCA CBZ  doub Y N 388 
UV0 CBB CBC  doub Y N 389 
UV0 CBB CBA  sing Y N 390 
UV0 NBT CBX  sing Y N 391 
UV0 NBT CBO  sing N N 392 
UV0 CBX NBY  doub Y N 393 
UV0 CBC CBD  sing Y N 394 
UV0 CBZ NBY  sing Y N 395 
UV0 CBR OBS  sing N N 396 
UV0 CBR CBM  sing N N 397 
UV0 CBA CAZ  doub Y N 398 
UV0 CBO OBN  sing N N 399 
UV0 CBD CBE  doub Y N 400 
UV0 CBD CAY  sing Y N 401 
UV0 CBE CBF  sing Y N 402 
UV0 CAZ CAY  sing Y N 403 
UV0 CAY CAX  doub Y N 404 
UV0 OBN CBM  sing N N 405 
UV0 CBF CBG  doub Y N 406 
UV0 CBM CBL  sing N N 407 
UV0 CAX CBG  sing Y N 408 
UV0 CAX NAW  sing N N 409 
UV0 CBL NAB  sing N N 410 
UV0 N6  C6   sing N N 411 
UV0 NAW CAU  sing N N 412 
UV0 C6  N1   doub Y N 413 
UV0 C6  C5   sing Y N 414 
UV0 N1  C2   sing Y N 415 
UV0 N7  C5   sing Y N 416 
UV0 N7  C8   doub Y N 417 
UV0 C5  C4   doub Y N 418 
UV0 NAB CAA  sing N N 419 
UV0 NAB CAC  sing N N 420 
UV0 CAU NAT  sing N N 421 
UV0 CAU OAV  doub N N 422 
UV0 C2  N3   doub Y N 423 
UV0 C8  CAE  sing N N 424 
UV0 C8  N9   sing Y N 425 
UV0 CAE CAD  trip N N 426 
UV0 C4  N3   sing Y N 427 
UV0 C4  N9   sing Y N 428 
UV0 CAD CAC  sing N N 429 
UV0 NAT CAS  sing N N 430 
UV0 N9  CAP  sing N N 431 
UV0 OAQ CAP  sing N N 432 
UV0 OAQ CAR  sing N N 433 
UV0 CAP CBJ  sing N N 434 
UV0 CAS CAR  sing N N 435 
UV0 CAR CBH  sing N N 436 
UV0 CBJ CBH  sing N N 437 
UV0 CBJ OBK  sing N N 438 
UV0 CBH OBI  sing N N 439 
UV0 C2  H1   sing N N 440 
UV0 CAA H2   sing N N 441 
UV0 CAA H3   sing N N 442 
UV0 CAA H4   sing N N 443 
UV0 CAC H5   sing N N 444 
UV0 CAC H6   sing N N 445 
UV0 CAP H7   sing N N 446 
UV0 CAR H8   sing N N 447 
UV0 CAS H9   sing N N 448 
UV0 CAS H10  sing N N 449 
UV0 CAZ H11  sing N N 450 
UV0 CBA H12  sing N N 451 
UV0 CBB H13  sing N N 452 
UV0 CBC H14  sing N N 453 
UV0 CBE H15  sing N N 454 
UV0 CBF H16  sing N N 455 
UV0 CBG H17  sing N N 456 
UV0 CBH H18  sing N N 457 
UV0 CBJ H19  sing N N 458 
UV0 CBL H20  sing N N 459 
UV0 CBL H21  sing N N 460 
UV0 CBM H22  sing N N 461 
UV0 CBO H23  sing N N 462 
UV0 CBP H24  sing N N 463 
UV0 CBR H25  sing N N 464 
UV0 CBU H26  sing N N 465 
UV0 CBZ H27  sing N N 466 
UV0 N6  H28  sing N N 467 
UV0 N6  H29  sing N N 468 
UV0 NAT H31  sing N N 469 
UV0 NAW H32  sing N N 470 
UV0 NCC H33  sing N N 471 
UV0 NCC H34  sing N N 472 
UV0 OBI H35  sing N N 473 
UV0 OBK H36  sing N N 474 
UV0 OBQ H37  sing N N 475 
UV0 OBS H38  sing N N 476 
VAL N   CA   sing N N 477 
VAL N   H    sing N N 478 
VAL N   H2   sing N N 479 
VAL CA  C    sing N N 480 
VAL CA  CB   sing N N 481 
VAL CA  HA   sing N N 482 
VAL C   O    doub N N 483 
VAL C   OXT  sing N N 484 
VAL CB  CG1  sing N N 485 
VAL CB  CG2  sing N N 486 
VAL CB  HB   sing N N 487 
VAL CG1 HG11 sing N N 488 
VAL CG1 HG12 sing N N 489 
VAL CG1 HG13 sing N N 490 
VAL CG2 HG21 sing N N 491 
VAL CG2 HG22 sing N N 492 
VAL CG2 HG23 sing N N 493 
VAL OXT HXT  sing N N 494 
# 
_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                    8QGA 
_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]   0.015876 
_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]   0.013394 
_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]   0.008450 
_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   ? 11.16427 36.65344 25.84018  1.000 111.97479 ? 1   MET A N   1 
ATOM   2    C CA  . MET A 1 1   ? 10.65010 36.66481 24.47571  1.000 111.56842 ? 1   MET A CA  1 
ATOM   3    C C   . MET A 1 1   ? 9.77449  35.43796 24.22387  1.000 105.53300 ? 1   MET A C   1 
ATOM   4    O O   . MET A 1 1   ? 9.81886  34.47396 24.98922  1.000 102.63006 ? 1   MET A O   1 
ATOM   5    C CB  . MET A 1 1   ? 11.80603 36.73159 23.47140  1.000 113.87635 ? 1   MET A CB  1 
ATOM   6    C CG  . MET A 1 1   ? 12.81182 35.59265 23.57244  0.770 111.16860 ? 1   MET A CG  1 
ATOM   7    S SD  . MET A 1 1   ? 14.40812 36.00289 22.83097  0.730 115.40174 ? 1   MET A SD  1 
ATOM   8    C CE  . MET A 1 1   ? 15.07958 37.11537 24.06545  0.910 121.33968 ? 1   MET A CE  1 
ATOM   9    N N   . LYS A 1 2   ? 8.97331  35.48595 23.15853  1.000 103.73150 ? 2   LYS A N   1 
ATOM   10   C CA  . LYS A 1 2   ? 8.04839  34.39769 22.86295  1.000 99.00772  ? 2   LYS A CA  1 
ATOM   11   C C   . LYS A 1 2   ? 8.80518  33.09596 22.62653  1.000 94.54965  ? 2   LYS A C   1 
ATOM   12   O O   . LYS A 1 2   ? 9.90757  33.09100 22.07264  1.000 96.02463  ? 2   LYS A O   1 
ATOM   13   C CB  . LYS A 1 2   ? 7.19460  34.74420 21.64115  1.000 99.83569  ? 2   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 2   ? 6.23994  35.90991 21.85746  1.000 104.23245 ? 2   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 2   ? 5.50973  36.27159 20.57387  0.870 105.55319 ? 2   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 2   ? 4.52124  37.40928 20.78416  1.000 108.61838 ? 2   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 2   ? 3.35494  36.99999 21.61526  0.970 105.58754 ? 2   LYS A NZ  1 
ATOM   18   N N   . TYR A 1 3   ? 8.20811  31.98594 23.05738  1.000 90.80654  ? 3   TYR A N   1 
ATOM   19   C CA  . TYR A 1 3   ? 8.85696  30.68565 22.95226  1.000 85.87476  ? 3   TYR A CA  1 
ATOM   20   C C   . TYR A 1 3   ? 7.80667  29.58934 23.03560  1.000 80.60627  ? 3   TYR A C   1 
ATOM   21   O O   . TYR A 1 3   ? 6.70788  29.79260 23.56059  1.000 81.54449  ? 3   TYR A O   1 
ATOM   22   C CB  . TYR A 1 3   ? 9.90169  30.48406 24.05520  1.000 87.06080  ? 3   TYR A CB  1 
ATOM   23   C CG  . TYR A 1 3   ? 9.30160  30.02018 25.36722  1.000 86.72248  ? 3   TYR A CG  1 
ATOM   24   C CD1 . TYR A 1 3   ? 8.68775  30.92053 26.22941  1.000 89.83334  ? 3   TYR A CD1 1 
ATOM   25   C CD2 . TYR A 1 3   ? 9.34408  28.68148 25.73967  1.000 84.15870  ? 3   TYR A CD2 1 
ATOM   26   C CE1 . TYR A 1 3   ? 8.13400  30.50237 27.42551  1.000 90.60997  ? 3   TYR A CE1 1 
ATOM   27   C CE2 . TYR A 1 3   ? 8.79175  28.25429 26.93048  1.000 85.19902  ? 3   TYR A CE2 1 
ATOM   28   C CZ  . TYR A 1 3   ? 8.18948  29.16853 27.77109  1.000 88.62890  ? 3   TYR A CZ  1 
ATOM   29   O OH  . TYR A 1 3   ? 7.64061  28.74589 28.96009  1.000 90.08987  ? 3   TYR A OH  1 
ATOM   30   N N   . MET A 1 4   ? 8.17441  28.41304 22.53043  1.000 75.77652  ? 4   MET A N   1 
ATOM   31   C CA  . MET A 1 4   ? 7.35928  27.21632 22.67164  1.000 72.63083  ? 4   MET A CA  1 
ATOM   32   C C   . MET A 1 4   ? 8.28391  26.02321 22.86597  1.000 69.43202  ? 4   MET A C   1 
ATOM   33   O O   . MET A 1 4   ? 9.48816  26.09828 22.61217  1.000 69.59945  ? 4   MET A O   1 
ATOM   34   C CB  . MET A 1 4   ? 6.42892  27.00481 21.46557  0.700 72.68071  ? 4   MET A CB  1 
ATOM   35   C CG  . MET A 1 4   ? 7.11059  26.50381 20.20327  0.700 72.43777  ? 4   MET A CG  1 
ATOM   36   S SD  . MET A 1 4   ? 7.19532  24.70482 20.11966  0.700 69.50626  ? 4   MET A SD  1 
ATOM   37   C CE  . MET A 1 4   ? 5.49931  24.26771 20.48933  0.700 69.33474  ? 4   MET A CE  1 
ATOM   38   N N   . ILE A 1 5   ? 7.70681  24.91544 23.32797  1.000 68.03082  ? 5   ILE A N   1 
ATOM   39   C CA  . ILE A 1 5   ? 8.46295  23.71274 23.66323  1.000 65.86923  ? 5   ILE A CA  1 
ATOM   40   C C   . ILE A 1 5   ? 7.69859  22.49046 23.17116  1.000 63.80613  ? 5   ILE A C   1 
ATOM   41   O O   . ILE A 1 5   ? 6.53793  22.28831 23.54283  1.000 63.27408  ? 5   ILE A O   1 
ATOM   42   C CB  . ILE A 1 5   ? 8.72355  23.60173 25.18039  1.000 65.99716  ? 5   ILE A CB  1 
ATOM   43   C CG1 . ILE A 1 5   ? 9.50501  24.81333 25.69400  1.000 67.72212  ? 5   ILE A CG1 1 
ATOM   44   C CG2 . ILE A 1 5   ? 9.48885  22.32468 25.49501  1.000 64.49872  ? 5   ILE A CG2 1 
ATOM   45   C CD1 . ILE A 1 5   ? 9.73726  24.80244 27.19151  1.000 69.37741  ? 5   ILE A CD1 1 
ATOM   46   N N   . THR A 1 6   ? 8.35467  21.66993 22.35332  1.000 62.86363  ? 6   THR A N   1 
ATOM   47   C CA  . THR A 1 6   ? 7.82222  20.40273 21.87285  1.000 61.49753  ? 6   THR A CA  1 
ATOM   48   C C   . THR A 1 6   ? 8.37499  19.26216 22.72157  1.000 61.84118  ? 6   THR A C   1 
ATOM   49   O O   . THR A 1 6   ? 9.51825  19.30882 23.18204  1.000 62.69234  ? 6   THR A O   1 
ATOM   50   C CB  . THR A 1 6   ? 8.19066  20.18145 20.39947  0.700 60.63307  ? 6   THR A CB  1 
ATOM   51   O OG1 . THR A 1 6   ? 7.82053  21.33334 19.63127  0.700 61.34247  ? 6   THR A OG1 1 
ATOM   52   C CG2 . THR A 1 6   ? 7.48228  18.95515 19.83257  0.700 60.07638  ? 6   THR A CG2 1 
ATOM   53   N N   . SER A 1 7   ? 7.55692  18.23256 22.93007  1.000 61.78104  ? 7   SER A N   1 
ATOM   54   C CA  . SER A 1 7   ? 7.94048  17.09580 23.75548  1.000 63.83194  ? 7   SER A CA  1 
ATOM   55   C C   . SER A 1 7   ? 7.79373  15.78935 22.98467  1.000 64.41830  ? 7   SER A C   1 
ATOM   56   O O   . SER A 1 7   ? 6.91490  15.64491 22.12817  1.000 64.47123  ? 7   SER A O   1 
ATOM   57   C CB  . SER A 1 7   ? 7.10207  17.03531 25.04117  1.000 66.20939  ? 7   SER A CB  1 
ATOM   58   O OG  . SER A 1 7   ? 7.40983  15.87901 25.79822  1.000 68.51703  ? 7   SER A OG  1 
ATOM   59   N N   . LYS A 1 8   ? 8.67645  14.83701 23.30078  1.000 66.01694  ? 8   LYS A N   1 
ATOM   60   C CA  . LYS A 1 8   ? 8.61351  13.51294 22.68864  1.000 66.40178  ? 8   LYS A CA  1 
ATOM   61   C C   . LYS A 1 8   ? 7.31698  12.79368 23.03996  1.000 68.00490  ? 8   LYS A C   1 
ATOM   62   O O   . LYS A 1 8   ? 6.80338  12.01838 22.22732  1.000 68.49656  ? 8   LYS A O   1 
ATOM   63   C CB  . LYS A 1 8   ? 9.82482  12.68342 23.12598  1.000 67.63094  ? 8   LYS A CB  1 
ATOM   64   C CG  . LYS A 1 8   ? 9.88519  11.26215 22.57466  1.000 68.71830  ? 8   LYS A CG  1 
ATOM   65   C CD  . LYS A 1 8   ? 10.92331 10.43991 23.33233  1.000 71.32932  ? 8   LYS A CD  1 
ATOM   66   C CE  . LYS A 1 8   ? 11.23232 9.12796  22.63122  0.790 73.97267  ? 8   LYS A CE  1 
ATOM   67   N NZ  . LYS A 1 8   ? 11.98538 9.34839  21.36570  0.720 73.18851  ? 8   LYS A NZ  1 
ATOM   68   N N   . GLY A 1 9   ? 6.77439  13.03226 24.23431  1.000 68.98615  ? 9   GLY A N   1 
ATOM   69   C CA  . GLY A 1 9   ? 5.50269  12.46532 24.63929  1.000 71.71217  ? 9   GLY A CA  1 
ATOM   70   C C   . GLY A 1 9   ? 5.58298  11.45285 25.76059  1.000 76.07933  ? 9   GLY A C   1 
ATOM   71   O O   . GLY A 1 9   ? 4.53290  11.00469 26.24178  1.000 79.47293  ? 9   GLY A O   1 
ATOM   72   N N   . ASP A 1 10  ? 6.78311  11.07260 26.19084  1.000 76.87382  ? 10  ASP A N   1 
ATOM   73   C CA  . ASP A 1 10  ? 6.94162  10.12619 27.28118  1.000 80.61908  ? 10  ASP A CA  1 
ATOM   74   C C   . ASP A 1 10  ? 7.01568  10.87342 28.61425  1.000 81.49533  ? 10  ASP A C   1 
ATOM   75   O O   . ASP A 1 10  ? 7.01041  12.10566 28.66566  1.000 79.05906  ? 10  ASP A O   1 
ATOM   76   C CB  . ASP A 1 10  ? 8.17758  9.25617  27.05292  1.000 81.48141  ? 10  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 10  ? 9.44049  10.07586 26.85220  1.000 78.83514  ? 10  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 10  ? 9.32692  11.29968 26.62807  0.880 76.02864  ? 10  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 10  ? 10.54678 9.50022  26.92148  0.870 80.13042  ? 10  ASP A OD2 1 
ATOM   80   N N   . GLU A 1 11  ? 7.09258  10.11763 29.71325  1.000 85.40235  ? 11  GLU A N   1 
ATOM   81   C CA  . GLU A 1 11  ? 7.05638  10.73990 31.03414  1.000 87.15275  ? 11  GLU A CA  1 
ATOM   82   C C   . GLU A 1 11  ? 8.24998  11.66178 31.25486  1.000 84.61162  ? 11  GLU A C   1 
ATOM   83   O O   . GLU A 1 11  ? 8.09510  12.76541 31.78904  1.000 84.06331  ? 11  GLU A O   1 
ATOM   84   C CB  . GLU A 1 11  ? 7.00006  9.66987  32.12585  1.000 93.27272  ? 11  GLU A CB  1 
ATOM   85   C CG  . GLU A 1 11  ? 5.61388  9.09935  32.37413  1.000 96.94358  ? 11  GLU A CG  1 
ATOM   86   C CD  . GLU A 1 11  ? 5.56045  8.24050  33.62085  0.670 103.88987 ? 11  GLU A CD  1 
ATOM   87   O OE1 . GLU A 1 11  ? 6.63905  7.83423  34.10311  1.000 106.17128 ? 11  GLU A OE1 1 
ATOM   88   O OE2 . GLU A 1 11  ? 4.44523  7.97976  34.12315  0.960 107.60539 ? 11  GLU A OE2 1 
ATOM   89   N N   . LYS A 1 12  ? 9.44514  11.23157 30.84921  1.000 83.27305  ? 12  LYS A N   1 
ATOM   90   C CA  . LYS A 1 12  ? 10.64151 12.02849 31.10279  1.000 82.25522  ? 12  LYS A CA  1 
ATOM   91   C C   . LYS A 1 12  ? 10.58274 13.37473 30.38636  1.000 78.09907  ? 12  LYS A C   1 
ATOM   92   O O   . LYS A 1 12  ? 10.88451 14.41396 30.98505  1.000 78.33548  ? 12  LYS A O   1 
ATOM   93   C CB  . LYS A 1 12  ? 11.88386 11.24283 30.68160  1.000 83.13617  ? 12  LYS A CB  1 
ATOM   94   C CG  . LYS A 1 12  ? 13.20184 11.95413 30.93799  0.890 83.31459  ? 12  LYS A CG  1 
ATOM   95   C CD  . LYS A 1 12  ? 14.38287 11.07957 30.54205  1.000 84.77923  ? 12  LYS A CD  1 
ATOM   96   C CE  . LYS A 1 12  ? 15.70648 11.81291 30.70714  0.840 85.02225  ? 12  LYS A CE  1 
ATOM   97   N NZ  . LYS A 1 12  ? 15.93577 12.24038 32.11459  0.900 88.24461  ? 12  LYS A NZ  1 
ATOM   98   N N   . SER A 1 13  ? 10.18263 13.38008 29.11045  1.000 74.92482  ? 13  SER A N   1 
ATOM   99   C CA  . SER A 1 13  ? 10.20110 14.61729 28.33343  1.000 71.80206  ? 13  SER A CA  1 
ATOM   100  C C   . SER A 1 13  ? 9.08203  15.55864 28.75674  1.000 70.85664  ? 13  SER A C   1 
ATOM   101  O O   . SER A 1 13  ? 9.28176  16.77752 28.82159  1.000 69.41723  ? 13  SER A O   1 
ATOM   102  C CB  . SER A 1 13  ? 10.09455 14.30600 26.83979  1.000 69.62575  ? 13  SER A CB  1 
ATOM   103  O OG  . SER A 1 13  ? 11.09033 13.38213 26.44133  1.000 70.48587  ? 13  SER A OG  1 
ATOM   104  N N   . ASP A 1 14  ? 7.89300  15.01621 29.03306  1.000 72.50103  ? 14  ASP A N   1 
ATOM   105  C CA  . ASP A 1 14  ? 6.78266  15.86077 29.46395  1.000 72.23934  ? 14  ASP A CA  1 
ATOM   106  C C   . ASP A 1 14  ? 7.08485  16.53273 30.80052  1.000 72.98473  ? 14  ASP A C   1 
ATOM   107  O O   . ASP A 1 14  ? 6.76332  17.71102 30.99799  1.000 72.82095  ? 14  ASP A O   1 
ATOM   108  C CB  . ASP A 1 14  ? 5.49315  15.03924 29.55540  1.000 74.75550  ? 14  ASP A CB  1 
ATOM   109  C CG  . ASP A 1 14  ? 4.95875  14.62121 28.19276  1.000 73.86632  ? 14  ASP A CG  1 
ATOM   110  O OD1 . ASP A 1 14  ? 5.53697  15.02973 27.15914  1.000 71.44970  ? 14  ASP A OD1 1 
ATOM   111  O OD2 . ASP A 1 14  ? 3.95098  13.87980 28.16043  0.840 76.11720  ? 14  ASP A OD2 1 
ATOM   112  N N   . LEU A 1 15  ? 7.71355  15.80588 31.72952  1.000 74.04457  ? 15  LEU A N   1 
ATOM   113  C CA  . LEU A 1 15  ? 7.96585  16.37967 33.05046  1.000 76.68686  ? 15  LEU A CA  1 
ATOM   114  C C   . LEU A 1 15  ? 9.07541  17.42047 33.00480  1.000 75.73142  ? 15  LEU A C   1 
ATOM   115  O O   . LEU A 1 15  ? 9.07782  18.36179 33.80644  1.000 77.99590  ? 15  LEU A O   1 
ATOM   116  C CB  . LEU A 1 15  ? 8.31006  15.28309 34.06092  1.000 80.50120  ? 15  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 15  ? 8.23840  15.70051 35.53902  0.700 85.41095  ? 15  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 15  ? 7.44128  14.69428 36.35549  0.700 89.86891  ? 15  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 15  ? 9.62640  15.89595 36.14194  0.700 87.54065  ? 15  LEU A CD2 1 
ATOM   120  N N   . LEU A 1 16  ? 10.02152 17.27249 32.07753  1.000 73.03628  ? 16  LEU A N   1 
ATOM   121  C CA  . LEU A 1 16  ? 11.05848 18.28470 31.92798  1.000 71.05861  ? 16  LEU A CA  1 
ATOM   122  C C   . LEU A 1 16  ? 10.51508 19.53792 31.25414  1.000 67.68277  ? 16  LEU A C   1 
ATOM   123  O O   . LEU A 1 16  ? 10.95380 20.65108 31.56669  1.000 67.74351  ? 16  LEU A O   1 
ATOM   124  C CB  . LEU A 1 16  ? 12.23293 17.71578 31.13390  1.000 69.72948  ? 16  LEU A CB  1 
ATOM   125  C CG  . LEU A 1 16  ? 13.45323 18.62487 30.97877  1.000 69.16241  ? 16  LEU A CG  1 
ATOM   126  C CD1 . LEU A 1 16  ? 14.08137 18.91370 32.33702  1.000 72.33776  ? 16  LEU A CD1 1 
ATOM   127  C CD2 . LEU A 1 16  ? 14.47107 18.00581 30.02807  1.000 67.90638  ? 16  LEU A CD2 1 
ATOM   128  N N   . ARG A 1 17  ? 9.55811  19.37679 30.33644  1.000 65.22872  ? 17  ARG A N   1 
ATOM   129  C CA  . ARG A 1 17  ? 8.93807  20.53032 29.69088  1.000 63.82334  ? 17  ARG A CA  1 
ATOM   130  C C   . ARG A 1 17  ? 8.14510  21.37009 30.68963  1.000 65.72577  ? 17  ARG A C   1 
ATOM   131  O O   . ARG A 1 17  ? 8.16426  22.60565 30.62549  1.000 65.73008  ? 17  ARG A O   1 
ATOM   132  C CB  . ARG A 1 17  ? 8.04287  20.06239 28.54182  1.000 61.68475  ? 17  ARG A CB  1 
ATOM   133  C CG  . ARG A 1 17  ? 7.18708  21.15396 27.92324  1.000 61.42280  ? 17  ARG A CG  1 
ATOM   134  C CD  . ARG A 1 17  ? 6.34369  20.60347 26.77782  1.000 60.47660  ? 17  ARG A CD  1 
ATOM   135  N NE  . ARG A 1 17  ? 5.42771  21.59403 26.22438  1.000 60.79028  ? 17  ARG A NE  1 
ATOM   136  C CZ  . ARG A 1 17  ? 4.22214  21.85189 26.71375  1.000 62.64586  ? 17  ARG A CZ  1 
ATOM   137  N NH1 . ARG A 1 17  ? 3.76723  21.23158 27.79083  1.000 64.34527  ? 17  ARG A NH1 1 
ATOM   138  N NH2 . ARG A 1 17  ? 3.45539  22.75747 26.10999  1.000 63.23321  ? 17  ARG A NH2 1 
ATOM   139  N N   . LEU A 1 18  ? 7.44547  20.72555 31.62490  1.000 67.97794  ? 18  LEU A N   1 
ATOM   140  C CA  . LEU A 1 18  ? 6.69145  21.49761 32.60843  1.000 70.07346  ? 18  LEU A CA  1 
ATOM   141  C C   . LEU A 1 18  ? 7.61622  22.24711 33.56292  1.000 71.34937  ? 18  LEU A C   1 
ATOM   142  O O   . LEU A 1 18  ? 7.27617  23.34810 34.01283  1.000 72.42171  ? 18  LEU A O   1 
ATOM   143  C CB  . LEU A 1 18  ? 5.73285  20.58764 33.38174  1.000 72.14740  ? 18  LEU A CB  1 
ATOM   144  C CG  . LEU A 1 18  ? 4.57446  19.97116 32.58406  1.000 70.43805  ? 18  LEU A CG  1 
ATOM   145  C CD1 . LEU A 1 18  ? 3.77201  19.00332 33.44447  1.000 73.39215  ? 18  LEU A CD1 1 
ATOM   146  C CD2 . LEU A 1 18  ? 3.66199  21.04483 31.99469  1.000 69.45723  ? 18  LEU A CD2 1 
ATOM   147  N N   . ASN A 1 19  ? 8.79168  21.68570 33.86439  1.000 71.52368  ? 19  ASN A N   1 
ATOM   148  C CA  . ASN A 1 19  ? 9.71568  22.36079 34.77256  1.000 74.03150  ? 19  ASN A CA  1 
ATOM   149  C C   . ASN A 1 19  ? 10.38507 23.55722 34.10775  1.000 73.01780  ? 19  ASN A C   1 
ATOM   150  O O   . ASN A 1 19  ? 10.61136 24.57996 34.76742  1.000 75.44947  ? 19  ASN A O   1 
ATOM   151  C CB  . ASN A 1 19  ? 10.76740 21.37899 35.29285  1.000 75.53416  ? 19  ASN A CB  1 
ATOM   152  C CG  . ASN A 1 19  ? 10.22672 20.46595 36.37964  1.000 78.86630  ? 19  ASN A CG  1 
ATOM   153  O OD1 . ASN A 1 19  ? 9.15873  20.71382 36.93992  1.000 80.73805  ? 19  ASN A OD1 1 
ATOM   154  N ND2 . ASN A 1 19  ? 10.96909 19.40978 36.69016  1.000 80.18500  ? 19  ASN A ND2 1 
ATOM   155  N N   . MET A 1 20  ? 10.70194 23.45184 32.80993  1.000 69.77854  ? 20  MET A N   1 
ATOM   156  C CA  . MET A 1 20  ? 11.26136 24.58890 32.08182  1.000 69.12053  ? 20  MET A CA  1 
ATOM   157  C C   . MET A 1 20  ? 10.25283 25.72777 31.98284  1.000 70.11778  ? 20  MET A C   1 
ATOM   158  O O   . MET A 1 20  ? 10.59805 26.89044 32.22894  1.000 71.55211  ? 20  MET A O   1 
ATOM   159  C CB  . MET A 1 20  ? 11.72714 24.15646 30.68286  1.000 66.07323  ? 20  MET A CB  1 
ATOM   160  C CG  . MET A 1 20  ? 12.98505 23.28419 30.67854  1.000 66.13956  ? 20  MET A CG  1 
ATOM   161  S SD  . MET A 1 20  ? 13.77863 23.02518 29.06598  0.800 63.77082  ? 20  MET A SD  1 
ATOM   162  C CE  . MET A 1 20  ? 14.20093 24.69969 28.58649  0.500 64.94830  ? 20  MET A CE  1 
ATOM   163  N N   . ILE A 1 21  ? 9.00126  25.40848 31.63444  1.000 69.84185  ? 21  ILE A N   1 
ATOM   164  C CA  . ILE A 1 21  ? 7.94257  26.41697 31.58043  1.000 70.82474  ? 21  ILE A CA  1 
ATOM   165  C C   . ILE A 1 21  ? 7.83521  27.15391 32.90954  1.000 73.84918  ? 21  ILE A C   1 
ATOM   166  O O   . ILE A 1 21  ? 7.79434  28.38981 32.95369  1.000 74.09776  ? 21  ILE A O   1 
ATOM   167  C CB  . ILE A 1 21  ? 6.60524  25.76315 31.19075  1.000 69.06423  ? 21  ILE A CB  1 
ATOM   168  C CG1 . ILE A 1 21  ? 6.65184  25.28703 29.73747  1.000 65.66815  ? 21  ILE A CG1 1 
ATOM   169  C CG2 . ILE A 1 21  ? 5.45100  26.72537 31.43090  1.000 70.54531  ? 21  ILE A CG2 1 
ATOM   170  C CD1 . ILE A 1 21  ? 5.44490  24.47918 29.31819  1.000 64.65140  ? 21  ILE A CD1 1 
ATOM   171  N N   . ALA A 1 22  ? 7.78262  26.40423 34.01425  1.000 76.06254  ? 22  ALA A N   1 
ATOM   172  C CA  . ALA A 1 22  ? 7.77565  27.03538 35.33120  1.000 79.89918  ? 22  ALA A CA  1 
ATOM   173  C C   . ALA A 1 22  ? 9.03321  27.86418 35.55032  1.000 81.69441  ? 22  ALA A C   1 
ATOM   174  O O   . ALA A 1 22  ? 8.97161  28.93808 36.16061  1.000 72.55066  ? 22  ALA A O   1 
ATOM   175  C CB  . ALA A 1 22  ? 7.63201  25.97758 36.42623  1.000 69.41181  ? 22  ALA A CB  1 
ATOM   176  N N   . GLY A 1 23  ? 10.17758 27.39080 35.04916  1.000 80.57343  ? 23  GLY A N   1 
ATOM   177  C CA  . GLY A 1 23  ? 11.38149 28.20051 35.08715  1.000 81.99809  ? 23  GLY A CA  1 
ATOM   178  C C   . GLY A 1 23  ? 11.26749 29.46530 34.26044  1.000 79.89953  ? 23  GLY A C   1 
ATOM   179  O O   . GLY A 1 23  ? 11.75815 30.52326 34.66974  1.000 81.80133  ? 23  GLY A O   1 
ATOM   180  N N   . PHE A 1 24  ? 10.61662 29.37819 33.09385  1.000 76.35480  ? 24  PHE A N   1 
ATOM   181  C CA  . PHE A 1 24  ? 10.41155 30.55610 32.25530  1.000 76.93993  ? 24  PHE A CA  1 
ATOM   182  C C   . PHE A 1 24  ? 9.41814  31.52899 32.87248  1.000 79.44486  ? 24  PHE A C   1 
ATOM   183  O O   . PHE A 1 24  ? 9.50830  32.73703 32.63007  1.000 81.50084  ? 24  PHE A O   1 
ATOM   184  C CB  . PHE A 1 24  ? 9.93422  30.14415 30.86245  1.000 73.58821  ? 24  PHE A CB  1 
ATOM   185  C CG  . PHE A 1 24  ? 11.03718 29.68438 29.94896  1.000 72.28944  ? 24  PHE A CG  1 
ATOM   186  C CD1 . PHE A 1 24  ? 12.04670 30.55381 29.56312  1.000 74.87792  ? 24  PHE A CD1 1 
ATOM   187  C CD2 . PHE A 1 24  ? 11.04641 28.39198 29.44677  1.000 69.58992  ? 24  PHE A CD2 1 
ATOM   188  C CE1 . PHE A 1 24  ? 13.05685 30.13635 28.70451  1.000 74.07610  ? 24  PHE A CE1 1 
ATOM   189  C CE2 . PHE A 1 24  ? 12.05223 27.96794 28.58245  1.000 68.71269  ? 24  PHE A CE2 1 
ATOM   190  C CZ  . PHE A 1 24  ? 13.05883 28.84214 28.21342  1.000 70.75766  ? 24  PHE A CZ  1 
ATOM   191  N N   . GLY A 1 25  ? 8.45610  31.02716 33.64850  1.000 80.86205  ? 25  GLY A N   1 
ATOM   192  C CA  . GLY A 1 25  ? 7.54929  31.91606 34.35324  1.000 84.59607  ? 25  GLY A CA  1 
ATOM   193  C C   . GLY A 1 25  ? 8.25422  32.82331 35.34313  1.000 89.39053  ? 25  GLY A C   1 
ATOM   194  O O   . GLY A 1 25  ? 7.76899  33.91841 35.64336  1.000 92.60622  ? 25  GLY A O   1 
ATOM   195  N N   . GLU A 1 26  ? 9.40504  32.39211 35.86299  1.000 110.86239 ? 26  GLU A N   1 
ATOM   196  C CA  . GLU A 1 26  ? 10.16890 33.22375 36.78755  1.000 117.90603 ? 26  GLU A CA  1 
ATOM   197  C C   . GLU A 1 26  ? 10.87657 34.36411 36.07534  1.000 122.57432 ? 26  GLU A C   1 
ATOM   198  O O   . GLU A 1 26  ? 11.53876 35.18368 36.72438  1.000 127.15609 ? 26  GLU A O   1 
ATOM   199  C CB  . GLU A 1 26  ? 11.17562 32.36536 37.55454  1.000 117.10701 ? 26  GLU A CB  1 
ATOM   200  C CG  . GLU A 1 26  ? 10.56523 31.10964 38.17783  1.000 116.65750 ? 26  GLU A CG  1 
ATOM   201  C CD  . GLU A 1 26  ? 9.31709  31.40511 38.98840  0.520 101.09481 ? 26  GLU A CD  1 
ATOM   202  O OE1 . GLU A 1 26  ? 9.28179  32.45348 39.66339  1.000 109.48105 ? 26  GLU A OE1 1 
ATOM   203  O OE2 . GLU A 1 26  ? 8.36550  30.59710 38.94353  1.000 99.03633  ? 26  GLU A OE2 1 
ATOM   204  N N   . TYR A 1 27  ? 10.74835 34.41218 34.75495  1.000 123.03327 ? 27  TYR A N   1 
ATOM   205  C CA  . TYR A 1 27  ? 11.12829 35.51694 33.88999  1.000 126.88526 ? 27  TYR A CA  1 
ATOM   206  C C   . TYR A 1 27  ? 9.86919  35.98494 33.15556  1.000 132.51335 ? 27  TYR A C   1 
ATOM   207  O O   . TYR A 1 27  ? 8.79025  35.40076 33.29983  1.000 131.05614 ? 27  TYR A O   1 
ATOM   208  C CB  . TYR A 1 27  ? 12.23226 35.08654 32.91272  1.000 118.69057 ? 27  TYR A CB  1 
ATOM   209  C CG  . TYR A 1 27  ? 13.42570 34.40002 33.56883  1.000 112.96514 ? 27  TYR A CG  1 
ATOM   210  C CD1 . TYR A 1 27  ? 13.42104 33.03003 33.81916  1.000 107.20063 ? 27  TYR A CD1 1 
ATOM   211  C CD2 . TYR A 1 27  ? 14.55849 35.12017 33.92550  1.000 114.12013 ? 27  TYR A CD2 1 
ATOM   212  C CE1 . TYR A 1 27  ? 14.50652 32.39995 34.41785  1.000 105.35939 ? 27  TYR A CE1 1 
ATOM   213  C CE2 . TYR A 1 27  ? 15.64788 34.50088 34.52245  1.000 112.42164 ? 27  TYR A CE2 1 
ATOM   214  C CZ  . TYR A 1 27  ? 15.61831 33.14153 34.76676  1.000 108.10125 ? 27  TYR A CZ  1 
ATOM   215  O OH  . TYR A 1 27  ? 16.70291 32.53166 35.36281  1.000 107.09215 ? 27  TYR A OH  1 
ATOM   216  N N   . ASP A 1 28  ? 9.99403  37.05498 32.37202  1.000 140.81120 ? 28  ASP A N   1 
ATOM   217  C CA  . ASP A 1 28  ? 8.88379  37.51480 31.53424  1.000 144.35140 ? 28  ASP A CA  1 
ATOM   218  C C   . ASP A 1 28  ? 8.98776  36.88780 30.14352  1.000 141.01178 ? 28  ASP A C   1 
ATOM   219  O O   . ASP A 1 28  ? 9.11731  37.56301 29.12308  1.000 141.73829 ? 28  ASP A O   1 
ATOM   220  C CB  . ASP A 1 28  ? 8.85748  39.03833 31.46190  0.800 151.87757 ? 28  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 28  ? 7.57229  39.57543 30.83860  0.700 153.64017 ? 28  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 28  ? 6.65577  38.77319 30.54160  0.700 150.96527 ? 28  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 28  ? 7.47089  40.80631 30.64669  0.700 157.54253 ? 28  ASP A OD2 1 
ATOM   224  N N   . MET A 1 29  ? 8.94157  35.55747 30.13051  1.000 137.60456 ? 29  MET A N   1 
ATOM   225  C CA  . MET A 1 29  ? 8.98675  34.77378 28.90223  1.000 131.48361 ? 29  MET A CA  1 
ATOM   226  C C   . MET A 1 29  ? 7.57275  34.29110 28.59904  1.000 127.44312 ? 29  MET A C   1 
ATOM   227  O O   . MET A 1 29  ? 7.03796  33.43233 29.30775  1.000 126.44646 ? 29  MET A O   1 
ATOM   228  C CB  . MET A 1 29  ? 9.95360  33.60074 29.04488  1.000 128.60547 ? 29  MET A CB  1 
ATOM   229  C CG  . MET A 1 29  ? 10.78985 33.31143 27.80726  1.000 126.92736 ? 29  MET A CG  1 
ATOM   230  S SD  . MET A 1 29  ? 12.28868 34.31046 27.70963  1.000 130.62757 ? 29  MET A SD  1 
ATOM   231  C CE  . MET A 1 29  ? 13.19233 33.42014 26.44567  0.780 127.13446 ? 29  MET A CE  1 
ATOM   232  N N   . GLU A 1 30  ? 6.96894  34.84602 27.55185  1.000 122.36647 ? 30  GLU A N   1 
ATOM   233  C CA  . GLU A 1 30  ? 5.60409  34.50587 27.17236  1.000 117.93523 ? 30  GLU A CA  1 
ATOM   234  C C   . GLU A 1 30  ? 5.58952  33.24109 26.32174  1.000 110.34804 ? 30  GLU A C   1 
ATOM   235  O O   . GLU A 1 30  ? 6.30156  33.15420 25.31520  1.000 109.89449 ? 30  GLU A O   1 
ATOM   236  C CB  . GLU A 1 30  ? 4.95538  35.65909 26.40546  0.800 119.29114 ? 30  GLU A CB  1 
ATOM   237  C CG  . GLU A 1 30  ? 3.57175  35.33470 25.86492  0.700 117.25221 ? 30  GLU A CG  1 
ATOM   238  C CD  . GLU A 1 30  ? 3.19374  36.19421 24.67347  0.600 115.51463 ? 30  GLU A CD  1 
ATOM   239  O OE1 . GLU A 1 30  ? 3.95059  37.13573 24.35455  0.600 115.83438 ? 30  GLU A OE1 1 
ATOM   240  O OE2 . GLU A 1 30  ? 2.14455  35.92394 24.05012  0.600 113.60202 ? 30  GLU A OE2 1 
ATOM   241  N N   . TYR A 1 31  ? 4.77629  32.26649 26.72995  1.000 104.43351 ? 31  TYR A N   1 
ATOM   242  C CA  . TYR A 1 31  ? 4.57113  31.06175 25.93896  1.000 98.30681  ? 31  TYR A CA  1 
ATOM   243  C C   . TYR A 1 31  ? 3.63879  31.36891 24.77570  1.000 96.90228  ? 31  TYR A C   1 
ATOM   244  O O   . TYR A 1 31  ? 2.53687  31.89051 24.97264  1.000 99.23599  ? 31  TYR A O   1 
ATOM   245  C CB  . TYR A 1 31  ? 3.98717  29.93901 26.79593  1.000 96.66440  ? 31  TYR A CB  1 
ATOM   246  C CG  . TYR A 1 31  ? 4.01292  28.58367 26.11845  1.000 91.95095  ? 31  TYR A CG  1 
ATOM   247  C CD1 . TYR A 1 31  ? 2.98586  28.18052 25.26694  1.000 90.51357  ? 31  TYR A CD1 1 
ATOM   248  C CD2 . TYR A 1 31  ? 5.07101  27.70843 26.32580  1.000 89.08230  ? 31  TYR A CD2 1 
ATOM   249  C CE1 . TYR A 1 31  ? 3.01586  26.94250 24.64715  1.000 87.34690  ? 31  TYR A CE1 1 
ATOM   250  C CE2 . TYR A 1 31  ? 5.11009  26.47098 25.70677  1.000 85.87059  ? 31  TYR A CE2 1 
ATOM   251  C CZ  . TYR A 1 31  ? 4.08309  26.09357 24.87199  1.000 85.43793  ? 31  TYR A CZ  1 
ATOM   252  O OH  . TYR A 1 31  ? 4.13019  24.85943 24.26607  1.000 83.28299  ? 31  TYR A OH  1 
ATOM   253  N N   . ASP A 1 32  ? 4.07976  31.03463 23.56259  1.000 93.37611  ? 32  ASP A N   1 
ATOM   254  C CA  . ASP A 1 32  ? 3.29186  31.31099 22.36448  1.000 94.53349  ? 32  ASP A CA  1 
ATOM   255  C C   . ASP A 1 32  ? 3.71456  30.28245 21.31690  1.000 93.41786  ? 32  ASP A C   1 
ATOM   256  O O   . ASP A 1 32  ? 4.80079  30.39733 20.74417  1.000 94.22362  ? 32  ASP A O   1 
ATOM   257  C CB  . ASP A 1 32  ? 3.51879  32.73505 21.88046  0.800 95.71412  ? 32  ASP A CB  1 
ATOM   258  C CG  . ASP A 1 32  ? 2.51756  33.16934 20.82201  0.700 96.43223  ? 32  ASP A CG  1 
ATOM   259  O OD1 . ASP A 1 32  ? 1.92482  32.30134 20.14776  0.600 94.37120  ? 32  ASP A OD1 1 
ATOM   260  O OD2 . ASP A 1 32  ? 2.32899  34.39309 20.65971  0.600 99.57201  ? 32  ASP A OD2 1 
ATOM   261  N N   . ASP A 1 33  ? 2.86283  29.28670 21.08533  1.000 92.23866  ? 33  ASP A N   1 
ATOM   262  C CA  . ASP A 1 33  ? 3.13454  28.27314 20.07583  1.000 90.27189  ? 33  ASP A CA  1 
ATOM   263  C C   . ASP A 1 33  ? 2.63091  28.66844 18.69144  1.000 92.07468  ? 33  ASP A C   1 
ATOM   264  O O   . ASP A 1 33  ? 2.63168  27.83168 17.78218  1.000 89.90256  ? 33  ASP A O   1 
ATOM   265  C CB  . ASP A 1 33  ? 2.52765  26.92952 20.49030  1.000 89.18692  ? 33  ASP A CB  1 
ATOM   266  C CG  . ASP A 1 33  ? 1.01261  26.94661 20.49738  1.000 90.68329  ? 33  ASP A CG  1 
ATOM   267  O OD1 . ASP A 1 33  ? 0.41701  28.04178 20.40812  0.830 93.89647  ? 33  ASP A OD1 1 
ATOM   268  O OD2 . ASP A 1 33  ? 0.41261  25.85547 20.59038  0.830 90.08192  ? 33  ASP A OD2 1 
ATOM   269  N N   . VAL A 1 34  ? 2.19276  29.90943 18.51259  1.000 97.13100  ? 34  VAL A N   1 
ATOM   270  C CA  . VAL A 1 34  ? 1.76430  30.40541 17.20900  1.000 101.27699 ? 34  VAL A CA  1 
ATOM   271  C C   . VAL A 1 34  ? 2.86044  31.21967 16.53969  1.000 103.38013 ? 34  VAL A C   1 
ATOM   272  O O   . VAL A 1 34  ? 3.21853  30.96676 15.38938  1.000 105.47431 ? 34  VAL A O   1 
ATOM   273  C CB  . VAL A 1 34  ? 0.46032  31.22304 17.34115  1.000 106.09165 ? 34  VAL A CB  1 
ATOM   274  C CG1 . VAL A 1 34  ? 0.08195  31.82456 15.99771  1.000 107.84697 ? 34  VAL A CG1 1 
ATOM   275  C CG2 . VAL A 1 34  ? -0.66112 30.34498 17.86383  1.000 107.26346 ? 34  VAL A CG2 1 
ATOM   276  N N   . GLU A 1 35  ? 3.41313  32.19983 17.25002  1.000 105.00884 ? 35  GLU A N   1 
ATOM   277  C CA  . GLU A 1 35  ? 4.52740  33.00544 16.75214  1.000 105.87244 ? 35  GLU A CA  1 
ATOM   278  C C   . GLU A 1 35  ? 5.66966  33.00101 17.76317  1.000 104.59101 ? 35  GLU A C   1 
ATOM   279  O O   . GLU A 1 35  ? 6.01240  34.04328 18.33333  1.000 107.87166 ? 35  GLU A O   1 
ATOM   280  C CB  . GLU A 1 35  ? 4.07326  34.43503 16.45227  1.000 111.34438 ? 35  GLU A CB  1 
ATOM   281  C CG  . GLU A 1 35  ? 3.19106  34.56986 15.21760  1.000 113.92220 ? 35  GLU A CG  1 
ATOM   282  C CD  . GLU A 1 35  ? 2.71038  35.99193 14.99551  0.720 117.64091 ? 35  GLU A CD  1 
ATOM   283  O OE1 . GLU A 1 35  ? 2.47514  36.70304 15.99676  1.000 120.65066 ? 35  GLU A OE1 1 
ATOM   284  O OE2 . GLU A 1 35  ? 2.57198  36.39689 13.82018  1.000 117.97310 ? 35  GLU A OE2 1 
ATOM   285  N N   . PRO A 1 36  ? 6.29154  31.84773 18.00179  1.000 100.38314 ? 36  PRO A N   1 
ATOM   286  C CA  . PRO A 1 36  ? 7.45773  31.82677 18.88500  1.000 99.38328  ? 36  PRO A CA  1 
ATOM   287  C C   . PRO A 1 36  ? 8.71612  32.27814 18.16232  1.000 96.50342  ? 36  PRO A C   1 
ATOM   288  O O   . PRO A 1 36  ? 8.85923  32.13168 16.94649  1.000 95.50100  ? 36  PRO A O   1 
ATOM   289  C CB  . PRO A 1 36  ? 7.55616  30.35468 19.30093  1.000 96.59841  ? 36  PRO A CB  1 
ATOM   290  C CG  . PRO A 1 36  ? 7.01200  29.61612 18.14543  1.000 94.64389  ? 36  PRO A CG  1 
ATOM   291  C CD  . PRO A 1 36  ? 5.95232  30.49412 17.52296  1.000 97.48653  ? 36  PRO A CD  1 
ATOM   292  N N   . GLU A 1 37  ? 9.62757  32.85930 18.93628  1.000 94.97550  ? 37  GLU A N   1 
ATOM   293  C CA  . GLU A 1 37  ? 10.95821 33.20103 18.46001  1.000 91.86812  ? 37  GLU A CA  1 
ATOM   294  C C   . GLU A 1 37  ? 11.99595 32.15694 18.84618  1.000 87.44387  ? 37  GLU A C   1 
ATOM   295  O O   . GLU A 1 37  ? 13.08617 32.13720 18.26252  1.000 87.24936  ? 37  GLU A O   1 
ATOM   296  C CB  . GLU A 1 37  ? 11.37085 34.57374 19.00761  1.000 95.33540  ? 37  GLU A CB  1 
ATOM   297  C CG  . GLU A 1 37  ? 10.47027 35.70996 18.55272  0.740 97.43963  ? 37  GLU A CG  1 
ATOM   298  C CD  . GLU A 1 37  ? 10.74261 37.00910 19.28539  0.660 101.63893 ? 37  GLU A CD  1 
ATOM   299  O OE1 . GLU A 1 37  ? 11.38618 36.97148 20.35514  1.000 102.79280 ? 37  GLU A OE1 1 
ATOM   300  O OE2 . GLU A 1 37  ? 10.31067 38.07005 18.78763  0.730 104.05115 ? 37  GLU A OE2 1 
ATOM   301  N N   . ILE A 1 38  ? 11.66872 31.29216 19.80657  1.000 73.66260  ? 38  ILE A N   1 
ATOM   302  C CA  . ILE A 1 38  ? 12.56215 30.27290 20.34326  1.000 70.78743  ? 38  ILE A CA  1 
ATOM   303  C C   . ILE A 1 38  ? 11.78312 28.96486 20.41594  1.000 68.04461  ? 38  ILE A C   1 
ATOM   304  O O   . ILE A 1 38  ? 10.73066 28.90505 21.05696  1.000 69.43279  ? 38  ILE A O   1 
ATOM   305  C CB  . ILE A 1 38  ? 13.08830 30.66681 21.73398  1.000 73.02460  ? 38  ILE A CB  1 
ATOM   306  C CG1 . ILE A 1 38  ? 13.82391 32.00894 21.66896  1.000 75.57705  ? 38  ILE A CG1 1 
ATOM   307  C CG2 . ILE A 1 38  ? 13.99390 29.58869 22.29955  1.000 72.35328  ? 38  ILE A CG2 1 
ATOM   308  C CD1 . ILE A 1 38  ? 15.04522 31.98719 20.77664  0.380 74.81546  ? 38  ILE A CD1 1 
ATOM   309  N N   . VAL A 1 39  ? 12.27790 27.92484 19.75103  1.000 65.02599  ? 39  VAL A N   1 
ATOM   310  C CA  . VAL A 1 39  ? 11.61990 26.61927 19.74125  1.000 62.03185  ? 39  VAL A CA  1 
ATOM   311  C C   . VAL A 1 39  ? 12.55780 25.60034 20.37652  1.000 60.49497  ? 39  VAL A C   1 
ATOM   312  O O   . VAL A 1 39  ? 13.67114 25.37333 19.88439  1.000 58.96315  ? 39  VAL A O   1 
ATOM   313  C CB  . VAL A 1 39  ? 11.20767 26.18453 18.32677  1.000 59.60109  ? 39  VAL A CB  1 
ATOM   314  C CG1 . VAL A 1 39  ? 10.77107 24.72730 18.33143  1.000 57.84678  ? 39  VAL A CG1 1 
ATOM   315  C CG2 . VAL A 1 39  ? 10.07095 27.06630 17.82340  1.000 60.32806  ? 39  VAL A CG2 1 
ATOM   316  N N   . ILE A 1 40  ? 12.10475 24.99661 21.47237  1.000 60.73700  ? 40  ILE A N   1 
ATOM   317  C CA  . ILE A 1 40  ? 12.87167 24.02812 22.24709  1.000 60.21713  ? 40  ILE A CA  1 
ATOM   318  C C   . ILE A 1 40  ? 12.27366 22.64665 22.01189  1.000 58.77864  ? 40  ILE A C   1 
ATOM   319  O O   . ILE A 1 40  ? 11.07576 22.43500 22.23503  1.000 59.18993  ? 40  ILE A O   1 
ATOM   320  C CB  . ILE A 1 40  ? 12.86414 24.39082 23.74574  1.000 61.89166  ? 40  ILE A CB  1 
ATOM   321  C CG1 . ILE A 1 40  ? 13.44476 25.79068 23.95041  1.000 63.81290  ? 40  ILE A CG1 1 
ATOM   322  C CG2 . ILE A 1 40  ? 13.61433 23.34816 24.57064  1.000 61.62238  ? 40  ILE A CG2 1 
ATOM   323  C CD1 . ILE A 1 40  ? 13.44731 26.25291 25.36536  1.000 66.15662  ? 40  ILE A CD1 1 
ATOM   324  N N   . SER A 1 41  ? 13.10641 21.71209 21.57247  1.000 57.88386  ? 41  SER A N   1 
ATOM   325  C CA  . SER A 1 41  ? 12.71469 20.33177 21.33273  1.000 57.45922  ? 41  SER A CA  1 
ATOM   326  C C   . SER A 1 41  ? 13.29728 19.45441 22.43073  1.000 58.60177  ? 41  SER A C   1 
ATOM   327  O O   . SER A 1 41  ? 14.45243 19.63703 22.82894  1.000 60.00061  ? 41  SER A O   1 
ATOM   328  C CB  . SER A 1 41  ? 13.20905 19.86297 19.95782  1.000 56.57828  ? 41  SER A CB  1 
ATOM   329  O OG  . SER A 1 41  ? 13.00827 18.47211 19.77888  1.000 56.46558  ? 41  SER A OG  1 
ATOM   330  N N   . ILE A 1 42  ? 12.49954 18.50578 22.92096  1.000 58.63401  ? 42  ILE A N   1 
ATOM   331  C CA  . ILE A 1 42  ? 12.87831 17.65211 24.04965  1.000 60.26934  ? 42  ILE A CA  1 
ATOM   332  C C   . ILE A 1 42  ? 12.54778 16.20957 23.68215  1.000 59.92488  ? 42  ILE A C   1 
ATOM   333  O O   . ILE A 1 42  ? 11.37188 15.85753 23.51928  1.000 58.75704  ? 42  ILE A O   1 
ATOM   334  C CB  . ILE A 1 42  ? 12.17472 18.05853 25.35391  1.000 61.68940  ? 42  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 42  ? 12.58556 19.47360 25.77231  1.000 62.43466  ? 42  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 42  ? 12.49017 17.07167 26.46446  1.000 63.57483  ? 42  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 42  ? 12.04083 19.88675 27.13530  1.000 63.92002  ? 42  ILE A CD1 1 
ATOM   338  N N   . GLY A 1 43  ? 13.57608 15.37321 23.56704  1.000 61.71933  ? 43  GLY A N   1 
ATOM   339  C CA  . GLY A 1 43  ? 13.39148 14.00087 23.13978  1.000 61.71404  ? 43  GLY A CA  1 
ATOM   340  C C   . GLY A 1 43  ? 14.56959 13.49429 22.33710  1.000 61.76049  ? 43  GLY A C   1 
ATOM   341  O O   . GLY A 1 43  ? 15.63047 13.20427 22.89727  1.000 63.44664  ? 43  GLY A O   1 
ATOM   342  N N   . GLY A 1 44  ? 14.39768 13.38182 21.02497  1.000 59.67343  ? 44  GLY A N   1 
ATOM   343  C CA  . GLY A 1 44  ? 15.47631 12.95827 20.15659  1.000 60.81018  ? 44  GLY A CA  1 
ATOM   344  C C   . GLY A 1 44  ? 15.48485 13.73889 18.85980  1.000 61.10514  ? 44  GLY A C   1 
ATOM   345  O O   . GLY A 1 44  ? 14.72600 14.70136 18.71009  1.000 60.80336  ? 44  GLY A O   1 
ATOM   346  N N   . ASP A 1 45  ? 16.33702 13.33910 17.91092  1.000 62.41262  ? 45  ASP A N   1 
ATOM   347  C CA  . ASP A 1 45  ? 16.38199 14.04055 16.63273  1.000 60.20998  ? 45  ASP A CA  1 
ATOM   348  C C   . ASP A 1 45  ? 15.03417 13.99282 15.92232  1.000 57.78901  ? 45  ASP A C   1 
ATOM   349  O O   . ASP A 1 45  ? 14.62787 14.98317 15.30083  1.000 56.17465  ? 45  ASP A O   1 
ATOM   350  C CB  . ASP A 1 45  ? 17.49296 13.46140 15.75123  1.000 60.97939  ? 45  ASP A CB  1 
ATOM   351  C CG  . ASP A 1 45  ? 18.88606 13.79919 16.27428  1.000 62.04404  ? 45  ASP A CG  1 
ATOM   352  O OD1 . ASP A 1 45  ? 19.01354 14.78919 17.02987  1.000 61.94335  ? 45  ASP A OD1 1 
ATOM   353  O OD2 . ASP A 1 45  ? 19.85152 13.08107 15.93577  1.000 62.86256  ? 45  ASP A OD2 1 
ATOM   354  N N   . GLY A 1 46  ? 14.31722 12.86860 16.02478  1.000 57.19389  ? 46  GLY A N   1 
ATOM   355  C CA  . GLY A 1 46  ? 12.98004 12.79776 15.45235  1.000 57.38332  ? 46  GLY A CA  1 
ATOM   356  C C   . GLY A 1 46  ? 12.04373 13.85325 16.01078  1.000 58.57510  ? 46  GLY A C   1 
ATOM   357  O O   . GLY A 1 46  ? 11.27070 14.46899 15.26924  1.000 58.32006  ? 46  GLY A O   1 
ATOM   358  N N   . THR A 1 47  ? 12.10012 14.07651 17.32843  1.000 60.25364  ? 47  THR A N   1 
ATOM   359  C CA  . THR A 1 47  ? 11.30037 15.13281 17.94195  1.000 58.67004  ? 47  THR A CA  1 
ATOM   360  C C   . THR A 1 47  ? 11.72366 16.50406 17.43159  1.000 57.31600  ? 47  THR A C   1 
ATOM   361  O O   . THR A 1 47  ? 10.88437 17.38970 17.23155  1.000 56.62764  ? 47  THR A O   1 
ATOM   362  C CB  . THR A 1 47  ? 11.42763 15.06706 19.46510  1.000 58.80775  ? 47  THR A CB  1 
ATOM   363  O OG1 . THR A 1 47  ? 11.11742 13.74141 19.91168  1.000 59.38382  ? 47  THR A OG1 1 
ATOM   364  C CG2 . THR A 1 47  ? 10.48885 16.05910 20.12966  1.000 58.10323  ? 47  THR A CG2 1 
ATOM   365  N N   . PHE A 1 48  ? 13.02571 16.70055 17.22056  1.000 57.32130  ? 48  PHE A N   1 
ATOM   366  C CA  . PHE A 1 48  ? 13.50168 17.96780 16.67618  1.000 58.41377  ? 48  PHE A CA  1 
ATOM   367  C C   . PHE A 1 48  ? 13.00214 18.17588 15.24946  1.000 59.11385  ? 48  PHE A C   1 
ATOM   368  O O   . PHE A 1 48  ? 12.53107 19.26741 14.90413  1.000 59.46246  ? 48  PHE A O   1 
ATOM   369  C CB  . PHE A 1 48  ? 15.03123 18.01500 16.73359  1.000 58.88074  ? 48  PHE A CB  1 
ATOM   370  C CG  . PHE A 1 48  ? 15.61390 19.33830 16.32893  1.000 58.78107  ? 48  PHE A CG  1 
ATOM   371  C CD1 . PHE A 1 48  ? 15.87375 19.61741 14.99611  1.000 58.06900  ? 48  PHE A CD1 1 
ATOM   372  C CD2 . PHE A 1 48  ? 15.89765 20.30269 17.27705  1.000 59.37932  ? 48  PHE A CD2 1 
ATOM   373  C CE1 . PHE A 1 48  ? 16.40158 20.83301 14.62091  1.000 58.05334  ? 48  PHE A CE1 1 
ATOM   374  C CE2 . PHE A 1 48  ? 16.42454 21.51854 16.90835  1.000 59.58561  ? 48  PHE A CE2 1 
ATOM   375  C CZ  . PHE A 1 48  ? 16.67614 21.78411 15.57808  1.000 59.01387  ? 48  PHE A CZ  1 
ATOM   376  N N   . LEU A 1 49  ? 13.09097 17.13451 14.41331  1.000 59.86313  ? 49  LEU A N   1 
ATOM   377  C CA  . LEU A 1 49  ? 12.59769 17.21911 13.03898  1.000 60.04235  ? 49  LEU A CA  1 
ATOM   378  C C   . LEU A 1 49  ? 11.14217 17.67069 12.99390  1.000 60.01804  ? 49  LEU A C   1 
ATOM   379  O O   . LEU A 1 49  ? 10.78795 18.56474 12.21538  1.000 59.60698  ? 49  LEU A O   1 
ATOM   380  C CB  . LEU A 1 49  ? 12.75879 15.86810 12.34069  1.000 60.12915  ? 49  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 49  ? 14.17573 15.46336 11.93231  1.000 60.68405  ? 49  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 49  ? 14.19057 14.04950 11.36622  1.000 61.42534  ? 49  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 49  ? 14.73670 16.44944 10.91765  1.000 60.55401  ? 49  LEU A CD2 1 
ATOM   384  N N   . SER A 1 50  ? 10.28494 17.06443 13.82489  1.000 61.31666  ? 50  SER A N   1 
ATOM   385  C CA  . SER A 1 50  ? 8.89258  17.49966 13.90682  1.000 62.26237  ? 50  SER A CA  1 
ATOM   386  C C   . SER A 1 50  ? 8.79548  18.98692 14.21888  1.000 62.06210  ? 50  SER A C   1 
ATOM   387  O O   . SER A 1 50  ? 8.01202  19.70981 13.59252  1.000 62.98705  ? 50  SER A O   1 
ATOM   388  C CB  . SER A 1 50  ? 8.14205  16.69635 14.97241  1.000 63.06267  ? 50  SER A CB  1 
ATOM   389  O OG  . SER A 1 50  ? 8.08250  15.31765 14.64720  1.000 62.74662  ? 50  SER A OG  1 
ATOM   390  N N   . ALA A 1 51  ? 9.58571  19.46166 15.18587  1.000 62.34321  ? 51  ALA A N   1 
ATOM   391  C CA  . ALA A 1 51  ? 9.53121  20.87118 15.56115  1.000 63.40749  ? 51  ALA A CA  1 
ATOM   392  C C   . ALA A 1 51  ? 9.96355  21.76601 14.40703  1.000 62.28677  ? 51  ALA A C   1 
ATOM   393  O O   . ALA A 1 51  ? 9.37405  22.83084 14.18234  1.000 63.11801  ? 51  ALA A O   1 
ATOM   394  C CB  . ALA A 1 51  ? 10.40172 21.12216 16.79339  1.000 64.33202  ? 51  ALA A CB  1 
ATOM   395  N N   . PHE A 1 52  ? 10.98799 21.34538 13.66232  1.000 61.10068  ? 52  PHE A N   1 
ATOM   396  C CA  . PHE A 1 52  ? 11.43632 22.11428 12.50647  1.000 59.89495  ? 52  PHE A CA  1 
ATOM   397  C C   . PHE A 1 52  ? 10.33238 22.22434 11.46240  1.000 59.42639  ? 52  PHE A C   1 
ATOM   398  O O   . PHE A 1 52  ? 10.04294 23.31626 10.95832  1.000 59.32830  ? 52  PHE A O   1 
ATOM   399  C CB  . PHE A 1 52  ? 12.68868 21.46948 11.90973  1.000 58.64530  ? 52  PHE A CB  1 
ATOM   400  C CG  . PHE A 1 52  ? 12.98780 21.90937 10.50642  1.000 57.97265  ? 52  PHE A CG  1 
ATOM   401  C CD1 . PHE A 1 52  ? 13.60527 23.12336 10.26326  1.000 58.46253  ? 52  PHE A CD1 1 
ATOM   402  C CD2 . PHE A 1 52  ? 12.65644 21.10545 9.43061   1.000 57.28383  ? 52  PHE A CD2 1 
ATOM   403  C CE1 . PHE A 1 52  ? 13.88709 23.52633 8.97233   1.000 58.46332  ? 52  PHE A CE1 1 
ATOM   404  C CE2 . PHE A 1 52  ? 12.93065 21.50536 8.14155   1.000 57.53846  ? 52  PHE A CE2 1 
ATOM   405  C CZ  . PHE A 1 52  ? 13.54639 22.71890 7.91301   1.000 58.11347  ? 52  PHE A CZ  1 
ATOM   406  N N   . HIS A 1 53  ? 9.69602  21.09827 11.13112  1.000 59.59587  ? 53  HIS A N   1 
ATOM   407  C CA  . HIS A 1 53  ? 8.63482  21.11728 10.13286  1.000 61.25731  ? 53  HIS A CA  1 
ATOM   408  C C   . HIS A 1 53  ? 7.37912  21.80842 10.63890  1.000 64.18004  ? 53  HIS A C   1 
ATOM   409  O O   . HIS A 1 53  ? 6.61294  22.34018 9.82903   1.000 65.42035  ? 53  HIS A O   1 
ATOM   410  C CB  . HIS A 1 53  ? 8.32279  19.69189 9.67606   1.000 60.23333  ? 53  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 53  ? 9.34996  19.13211 8.74052   1.000 59.21692  ? 53  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 53  ? 9.24497  19.24266 7.37025   1.000 59.23879  ? 53  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 53  ? 10.51376 18.48123 8.97647   1.000 58.32047  ? 53  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 53  ? 10.29141 18.67263 6.80209   1.000 58.58929  ? 53  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 53  ? 11.07993 18.20746 7.75427   1.000 58.30296  ? 53  HIS A NE2 1 
ATOM   416  N N   . GLN A 1 54  ? 7.15802  21.82528 11.95533  1.000 65.94226  ? 54  GLN A N   1 
ATOM   417  C CA  . GLN A 1 54  ? 5.98725  22.50918 12.49319  1.000 68.46138  ? 54  GLN A CA  1 
ATOM   418  C C   . GLN A 1 54  ? 6.06243  24.01285 12.26186  1.000 70.96090  ? 54  GLN A C   1 
ATOM   419  O O   . GLN A 1 54  ? 5.02537  24.67609 12.16137  1.000 73.02213  ? 54  GLN A O   1 
ATOM   420  C CB  . GLN A 1 54  ? 5.83480  22.21061 13.98663  0.800 68.10611  ? 54  GLN A CB  1 
ATOM   421  C CG  . GLN A 1 54  ? 4.54627  22.74481 14.59553  0.700 69.72675  ? 54  GLN A CG  1 
ATOM   422  C CD  . GLN A 1 54  ? 4.53865  22.68295 16.11116  0.600 70.23691  ? 54  GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 54  ? 5.41361  22.07304 16.72507  0.600 69.31430  ? 54  GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 54  ? 3.54753  23.32031 16.72255  0.600 72.20515  ? 54  GLN A NE2 1 
ATOM   425  N N   . TYR A 1 55  ? 7.26967  24.56652 12.16219  1.000 71.39115  ? 55  TYR A N   1 
ATOM   426  C CA  . TYR A 1 55  ? 7.45456  26.00057 11.97866  1.000 73.57956  ? 55  TYR A CA  1 
ATOM   427  C C   . TYR A 1 55  ? 8.34026  26.28707 10.77393  1.000 73.19403  ? 55  TYR A C   1 
ATOM   428  O O   . TYR A 1 55  ? 9.10214  27.25698 10.77362  1.000 73.98149  ? 55  TYR A O   1 
ATOM   429  C CB  . TYR A 1 55  ? 8.04249  26.64149 13.23716  1.000 74.74264  ? 55  TYR A CB  1 
ATOM   430  C CG  . TYR A 1 55  ? 7.17826  26.49498 14.47348  1.000 76.18825  ? 55  TYR A CG  1 
ATOM   431  C CD1 . TYR A 1 55  ? 6.09986  27.34122 14.69705  1.000 78.63792  ? 55  TYR A CD1 1 
ATOM   432  C CD2 . TYR A 1 55  ? 7.44785  25.51648 15.42045  1.000 75.29888  ? 55  TYR A CD2 1 
ATOM   433  C CE1 . TYR A 1 55  ? 5.30904  27.21005 15.82799  1.000 79.85146  ? 55  TYR A CE1 1 
ATOM   434  C CE2 . TYR A 1 55  ? 6.66503  25.37773 16.54985  1.000 76.36018  ? 55  TYR A CE2 1 
ATOM   435  C CZ  . TYR A 1 55  ? 5.59769  26.22598 16.74956  1.000 78.60312  ? 55  TYR A CZ  1 
ATOM   436  O OH  . TYR A 1 55  ? 4.82020  26.08887 17.87584  1.000 79.85110  ? 55  TYR A OH  1 
ATOM   437  N N   . GLU A 1 56  ? 8.25187  25.45675 9.73647   1.000 72.36555  ? 56  GLU A N   1 
ATOM   438  C CA  . GLU A 1 56  ? 9.15467  25.61019 8.60128   1.000 71.78870  ? 56  GLU A CA  1 
ATOM   439  C C   . GLU A 1 56  ? 8.83111  26.82305 7.74400   1.000 73.32256  ? 56  GLU A C   1 
ATOM   440  O O   . GLU A 1 56  ? 9.57713  27.10554 6.80013   1.000 73.59822  ? 56  GLU A O   1 
ATOM   441  C CB  . GLU A 1 56  ? 9.14130  24.34699 7.74162   0.900 70.57932  ? 56  GLU A CB  1 
ATOM   442  C CG  . GLU A 1 56  ? 7.81373  24.04915 7.09220   0.800 71.63619  ? 56  GLU A CG  1 
ATOM   443  C CD  . GLU A 1 56  ? 7.85875  22.78220 6.26983   0.700 70.77576  ? 56  GLU A CD  1 
ATOM   444  O OE1 . GLU A 1 56  ? 8.44768  21.78959 6.74343   0.600 69.45260  ? 56  GLU A OE1 1 
ATOM   445  O OE2 . GLU A 1 56  ? 7.31778  22.78026 5.14560   0.600 71.74734  ? 56  GLU A OE2 1 
ATOM   446  N N   . GLU A 1 57  ? 7.75765  27.54727 8.04589   1.000 74.80066  ? 57  GLU A N   1 
ATOM   447  C CA  . GLU A 1 57  ? 7.41087  28.76181 7.32395   1.000 77.26077  ? 57  GLU A CA  1 
ATOM   448  C C   . GLU A 1 57  ? 7.79299  30.02824 8.07823   1.000 78.63063  ? 57  GLU A C   1 
ATOM   449  O O   . GLU A 1 57  ? 7.51398  31.12862 7.59442   1.000 80.15665  ? 57  GLU A O   1 
ATOM   450  C CB  . GLU A 1 57  ? 5.91282  28.77092 7.00153   1.000 79.85462  ? 57  GLU A CB  1 
ATOM   451  C CG  . GLU A 1 57  ? 5.51412  27.73873 5.95176   1.000 79.76124  ? 57  GLU A CG  1 
ATOM   452  C CD  . GLU A 1 57  ? 4.04470  27.80408 5.59865   0.350 82.61715  ? 57  GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 57  ? 3.29347  28.50805 6.30785   0.860 84.82883  ? 57  GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 57  ? 3.64354  27.15369 4.60988   0.630 82.90874  ? 57  GLU A OE2 1 
ATOM   455  N N   . ARG A 1 58  ? 8.41952  29.90173 9.24600   1.000 78.51002  ? 58  ARG A N   1 
ATOM   456  C CA  . ARG A 1 58  ? 8.95373  31.03433 9.99416   1.000 80.44145  ? 58  ARG A CA  1 
ATOM   457  C C   . ARG A 1 58  ? 10.38516 30.75365 10.43068  1.000 79.29626  ? 58  ARG A C   1 
ATOM   458  O O   . ARG A 1 58  ? 10.81355 31.15085 11.51707  1.000 80.50355  ? 58  ARG A O   1 
ATOM   459  C CB  . ARG A 1 58  ? 8.07358  31.36829 11.19860  1.000 82.54272  ? 58  ARG A CB  1 
ATOM   460  C CG  . ARG A 1 58  ? 6.72948  31.98875 10.83826  0.720 85.40237  ? 58  ARG A CG  1 
ATOM   461  C CD  . ARG A 1 58  ? 5.90950  32.34659 12.07562  1.000 87.52771  ? 58  ARG A CD  1 
ATOM   462  N NE  . ARG A 1 58  ? 6.57150  33.33380 12.92170  1.000 89.41836  ? 58  ARG A NE  1 
ATOM   463  C CZ  . ARG A 1 58  ? 7.15366  33.05977 14.08198  0.940 89.06334  ? 58  ARG A CZ  1 
ATOM   464  N NH1 . ARG A 1 58  ? 7.16336  31.83303 14.57877  0.980 86.82068  ? 58  ARG A NH1 1 
ATOM   465  N NH2 . ARG A 1 58  ? 7.73633  34.04238 14.76415  1.000 91.19744  ? 58  ARG A NH2 1 
ATOM   466  N N   . LEU A 1 59  ? 11.15120 30.06734 9.57820   1.000 77.08960  ? 59  LEU A N   1 
ATOM   467  C CA  . LEU A 1 59  ? 12.51889 29.70082 9.93105   1.000 76.78129  ? 59  LEU A CA  1 
ATOM   468  C C   . LEU A 1 59  ? 13.40349 30.92263 10.13317  1.000 79.79590  ? 59  LEU A C   1 
ATOM   469  O O   . LEU A 1 59  ? 14.34030 30.87995 10.94013  1.000 81.47994  ? 59  LEU A O   1 
ATOM   470  C CB  . LEU A 1 59  ? 13.11414 28.79591 8.85329   1.000 73.92240  ? 59  LEU A CB  1 
ATOM   471  C CG  . LEU A 1 59  ? 12.43192 27.43860 8.67212   1.000 72.01847  ? 59  LEU A CG  1 
ATOM   472  C CD1 . LEU A 1 59  ? 13.04836 26.67805 7.51278   1.000 70.69508  ? 59  LEU A CD1 1 
ATOM   473  C CD2 . LEU A 1 59  ? 12.51592 26.62713 9.95607   1.000 71.05532  ? 59  LEU A CD2 1 
ATOM   474  N N   . ASP A 1 60  ? 13.12858 32.01455 9.42259   1.000 81.76623  ? 60  ASP A N   1 
ATOM   475  C CA  . ASP A 1 60  ? 13.98957 33.18330 9.51897   1.000 84.21525  ? 60  ASP A CA  1 
ATOM   476  C C   . ASP A 1 60  ? 13.81949 33.94412 10.82862  1.000 86.10295  ? 60  ASP A C   1 
ATOM   477  O O   . ASP A 1 60  ? 14.65944 34.79539 11.14052  1.000 89.76642  ? 60  ASP A O   1 
ATOM   478  C CB  . ASP A 1 60  ? 13.73725 34.12020 8.33538   1.000 86.88812  ? 60  ASP A CB  1 
ATOM   479  C CG  . ASP A 1 60  ? 14.99636 34.83571 7.88715   1.000 87.47745  ? 60  ASP A CG  1 
ATOM   480  O OD1 . ASP A 1 60  ? 15.91096 34.15578 7.37456   1.000 85.29033  ? 60  ASP A OD1 1 
ATOM   481  O OD2 . ASP A 1 60  ? 15.07487 36.07266 8.05005   1.000 90.04766  ? 60  ASP A OD2 1 
ATOM   482  N N   . GLU A 1 61  ? 12.76826 33.65915 11.60203  1.000 84.69430  ? 61  GLU A N   1 
ATOM   483  C CA  . GLU A 1 61  ? 12.49805 34.37101 12.84693  1.000 85.75263  ? 61  GLU A CA  1 
ATOM   484  C C   . GLU A 1 61  ? 12.56995 33.45654 14.06816  1.000 83.23290  ? 61  GLU A C   1 
ATOM   485  O O   . GLU A 1 61  ? 11.98913 33.77850 15.10969  1.000 85.48166  ? 61  GLU A O   1 
ATOM   486  C CB  . GLU A 1 61  ? 11.12687 35.05078 12.78445  1.000 88.34730  ? 61  GLU A CB  1 
ATOM   487  C CG  . GLU A 1 61  ? 10.77187 35.64596 11.42939  0.800 90.51066  ? 61  GLU A CG  1 
ATOM   488  C CD  . GLU A 1 61  ? 9.47458  35.08938 10.86837  0.700 90.32876  ? 61  GLU A CD  1 
ATOM   489  O OE1 . GLU A 1 61  ? 8.59490  34.70877 11.66902  0.700 90.42141  ? 61  GLU A OE1 1 
ATOM   490  O OE2 . GLU A 1 61  ? 9.33777  35.02721 9.62736   0.700 90.00782  ? 61  GLU A OE2 1 
ATOM   491  N N   . ILE A 1 62  ? 13.27276 32.32847 13.97222  1.000 79.13161  ? 62  ILE A N   1 
ATOM   492  C CA  . ILE A 1 62  ? 13.29447 31.32402 15.03189  1.000 75.56622  ? 62  ILE A CA  1 
ATOM   493  C C   . ILE A 1 62  ? 14.71771 30.81000 15.21227  1.000 73.12471  ? 62  ILE A C   1 
ATOM   494  O O   . ILE A 1 62  ? 15.45774 30.63841 14.23722  1.000 72.10913  ? 62  ILE A O   1 
ATOM   495  C CB  . ILE A 1 62  ? 12.32599 30.15968 14.71885  1.000 72.95425  ? 62  ILE A CB  1 
ATOM   496  C CG1 . ILE A 1 62  ? 10.87118 30.61070 14.87442  1.000 74.23532  ? 62  ILE A CG1 1 
ATOM   497  C CG2 . ILE A 1 62  ? 12.60148 28.94623 15.59783  1.000 71.10267  ? 62  ILE A CG2 1 
ATOM   498  C CD1 . ILE A 1 62  ? 9.86054  29.50670 14.64300  1.000 72.60851  ? 62  ILE A CD1 1 
ATOM   499  N N   . ALA A 1 63  ? 15.10379 30.57876 16.46654  1.000 71.97925  ? 63  ALA A N   1 
ATOM   500  C CA  . ALA A 1 63  ? 16.30480 29.82560 16.80162  1.000 70.61150  ? 63  ALA A CA  1 
ATOM   501  C C   . ALA A 1 63  ? 15.88979 28.54976 17.52230  1.000 67.95497  ? 63  ALA A C   1 
ATOM   502  O O   . ALA A 1 63  ? 15.18142 28.60657 18.53388  1.000 69.34055  ? 63  ALA A O   1 
ATOM   503  C CB  . ALA A 1 63  ? 17.26419 30.64899 17.66822  1.000 73.41299  ? 63  ALA A CB  1 
ATOM   504  N N   . PHE A 1 64  ? 16.32225 27.40728 16.99747  1.000 64.61539  ? 64  PHE A N   1 
ATOM   505  C CA  . PHE A 1 64  ? 15.99355 26.10452 17.55769  1.000 62.39562  ? 64  PHE A CA  1 
ATOM   506  C C   . PHE A 1 64  ? 17.03842 25.66360 18.58358  1.000 63.47933  ? 64  PHE A C   1 
ATOM   507  O O   . PHE A 1 64  ? 18.20851 26.05643 18.52192  1.000 64.07887  ? 64  PHE A O   1 
ATOM   508  C CB  . PHE A 1 64  ? 15.89001 25.05598 16.44808  1.000 59.38560  ? 64  PHE A CB  1 
ATOM   509  C CG  . PHE A 1 64  ? 14.70525 25.23864 15.53498  1.000 57.87241  ? 64  PHE A CG  1 
ATOM   510  C CD1 . PHE A 1 64  ? 13.49355 24.63314 15.82636  1.000 56.80207  ? 64  PHE A CD1 1 
ATOM   511  C CD2 . PHE A 1 64  ? 14.81032 25.99934 14.37317  1.000 57.46022  ? 64  PHE A CD2 1 
ATOM   512  C CE1 . PHE A 1 64  ? 12.40665 24.78915 14.98649  1.000 56.18873  ? 64  PHE A CE1 1 
ATOM   513  C CE2 . PHE A 1 64  ? 13.72500 26.16432 13.52934  1.000 56.64327  ? 64  PHE A CE2 1 
ATOM   514  C CZ  . PHE A 1 64  ? 12.52151 25.55714 13.83525  1.000 56.20242  ? 64  PHE A CZ  1 
ATOM   515  N N   . ILE A 1 65  ? 16.59336 24.84722 19.54273  1.000 64.38917  ? 65  ILE A N   1 
ATOM   516  C CA  . ILE A 1 65  ? 17.44954 24.25307 20.56893  1.000 66.13535  ? 65  ILE A CA  1 
ATOM   517  C C   . ILE A 1 65  ? 16.98022 22.82664 20.81483  1.000 64.62376  ? 65  ILE A C   1 
ATOM   518  O O   . ILE A 1 65  ? 15.77745 22.57266 20.94092  1.000 63.51273  ? 65  ILE A O   1 
ATOM   519  C CB  . ILE A 1 65  ? 17.41971 25.04755 21.89271  1.000 68.62846  ? 65  ILE A CB  1 
ATOM   520  C CG1 . ILE A 1 65  ? 17.72149 26.52527 21.66088  1.000 70.04267  ? 65  ILE A CG1 1 
ATOM   521  C CG2 . ILE A 1 65  ? 18.39903 24.45334 22.89797  1.000 69.98197  ? 65  ILE A CG2 1 
ATOM   522  C CD1 . ILE A 1 65  ? 16.92885 27.43456 22.56952  0.920 71.73001  ? 65  ILE A CD1 1 
ATOM   523  N N   . GLY A 1 66  ? 17.91582 21.89700 20.90606  1.000 65.89145  ? 66  GLY A N   1 
ATOM   524  C CA  . GLY A 1 66  ? 17.59397 20.49601 21.11185  1.000 64.40257  ? 66  GLY A CA  1 
ATOM   525  C C   . GLY A 1 66  ? 18.07435 19.99011 22.46721  1.000 66.41535  ? 66  GLY A C   1 
ATOM   526  O O   . GLY A 1 66  ? 19.17844 20.32391 22.90062  1.000 67.85862  ? 66  GLY A O   1 
ATOM   527  N N   . ILE A 1 67  ? 17.23462 19.18447 23.10879  1.000 66.07925  ? 67  ILE A N   1 
ATOM   528  C CA  . ILE A 1 67  ? 17.58018 18.50676 24.35608  1.000 69.69605  ? 67  ILE A CA  1 
ATOM   529  C C   . ILE A 1 67  ? 17.26118 17.03060 24.18028  1.000 72.30436  ? 67  ILE A C   1 
ATOM   530  O O   . ILE A 1 67  ? 16.10439 16.67038 23.93167  1.000 71.82868  ? 67  ILE A O   1 
ATOM   531  C CB  . ILE A 1 67  ? 16.81914 19.08048 25.56363  1.000 70.37512  ? 67  ILE A CB  1 
ATOM   532  C CG1 . ILE A 1 67  ? 17.13545 20.56436 25.73613  1.000 70.80048  ? 67  ILE A CG1 1 
ATOM   533  C CG2 . ILE A 1 67  ? 17.16231 18.30593 26.83707  1.000 73.43772  ? 67  ILE A CG2 1 
ATOM   534  C CD1 . ILE A 1 67  ? 16.40139 21.21568 26.88750  1.000 72.00809  ? 67  ILE A CD1 1 
ATOM   535  N N   . HIS A 1 68  ? 18.27654 16.17866 24.30522  1.000 77.21247  ? 68  HIS A N   1 
ATOM   536  C CA  . HIS A 1 68  ? 18.09665 14.74576 24.10961  1.000 80.86759  ? 68  HIS A CA  1 
ATOM   537  C C   . HIS A 1 68  ? 17.80645 14.08183 25.45059  1.000 86.85780  ? 68  HIS A C   1 
ATOM   538  O O   . HIS A 1 68  ? 18.61025 14.17341 26.38524  1.000 87.83203  ? 68  HIS A O   1 
ATOM   539  C CB  . HIS A 1 68  ? 19.32183 14.11972 23.43839  1.000 79.91458  ? 68  HIS A CB  1 
ATOM   540  C CG  . HIS A 1 68  ? 20.55814 14.12531 24.28453  1.000 80.94120  ? 68  HIS A CG  1 
ATOM   541  N ND1 . HIS A 1 68  ? 21.41908 15.20028 24.33824  1.000 81.24542  ? 68  HIS A ND1 1 
ATOM   542  C CD2 . HIS A 1 68  ? 21.08570 13.18044 25.09963  1.000 83.00782  ? 68  HIS A CD2 1 
ATOM   543  C CE1 . HIS A 1 68  ? 22.41976 14.92054 25.15427  1.000 84.12709  ? 68  HIS A CE1 1 
ATOM   544  N NE2 . HIS A 1 68  ? 22.24098 13.70130 25.63009  1.000 85.43227  ? 68  HIS A NE2 1 
ATOM   545  N N   . THR A 1 69  ? 16.64711 13.43285 25.54894  1.000 76.95494  ? 69  THR A N   1 
ATOM   546  C CA  . THR A 1 69  ? 16.32563 12.64507 26.73141  1.000 80.65469  ? 69  THR A CA  1 
ATOM   547  C C   . THR A 1 69  ? 16.78769 11.20224 26.60155  1.000 81.54190  ? 69  THR A C   1 
ATOM   548  O O   . THR A 1 69  ? 17.12059 10.57239 27.61334  1.000 87.66165  ? 69  THR A O   1 
ATOM   549  C CB  . THR A 1 69  ? 14.81984 12.68276 27.01261  1.000 81.02188  ? 69  THR A CB  1 
ATOM   550  O OG1 . THR A 1 69  ? 14.09778 12.34331 25.82216  1.000 78.20878  ? 69  THR A OG1 1 
ATOM   551  C CG2 . THR A 1 69  ? 14.40137 14.06714 27.48420  1.000 81.23149  ? 69  THR A CG2 1 
ATOM   552  N N   . GLY A 1 70  ? 16.81490 10.66686 25.38439  0.500 73.87752  ? 70  GLY A N   1 
ATOM   553  C CA  . GLY A 1 70  ? 17.42609 9.37593  25.15141  0.500 73.18585  ? 70  GLY A CA  1 
ATOM   554  C C   . GLY A 1 70  ? 18.92340 9.52342  24.98849  0.500 75.47273  ? 70  GLY A C   1 
ATOM   555  O O   . GLY A 1 70  ? 19.59250 10.10889 25.84460  0.500 80.68918  ? 70  GLY A O   1 
ATOM   556  N N   . HIS A 1 71  ? 19.46320 9.01257  23.89093  0.500 71.76218  ? 71  HIS A N   1 
ATOM   557  C CA  . HIS A 1 71  ? 20.87363 9.20159  23.60046  0.500 68.19492  ? 71  HIS A CA  1 
ATOM   558  C C   . HIS A 1 71  ? 21.09310 10.53341 22.88692  0.500 62.72887  ? 71  HIS A C   1 
ATOM   559  O O   . HIS A 1 71  ? 20.15152 11.20378 22.46026  0.500 57.46521  ? 71  HIS A O   1 
ATOM   560  C CB  . HIS A 1 71  ? 21.40913 8.03417  22.77390  0.500 64.64274  ? 71  HIS A CB  1 
ATOM   561  C CG  . HIS A 1 71  ? 21.53391 6.76342  23.55294  0.500 65.70712  ? 71  HIS A CG  1 
ATOM   562  N ND1 . HIS A 1 71  ? 20.50242 5.85712  23.67237  0.500 64.55684  ? 71  HIS A ND1 1 
ATOM   563  C CD2 . HIS A 1 71  ? 22.56213 6.26139  24.27646  0.500 70.71240  ? 71  HIS A CD2 1 
ATOM   564  C CE1 . HIS A 1 71  ? 20.89514 4.84390  24.42393  0.500 69.70118  ? 71  HIS A CE1 1 
ATOM   565  N NE2 . HIS A 1 71  ? 22.14058 5.06540  24.80417  0.500 73.74570  ? 71  HIS A NE2 1 
ATOM   566  N N   . LEU A 1 72  ? 22.36125 10.92264 22.77928  0.700 65.01608  ? 72  LEU A N   1 
ATOM   567  C CA  . LEU A 1 72  ? 22.70618 12.18793 22.14442  0.700 65.13206  ? 72  LEU A CA  1 
ATOM   568  C C   . LEU A 1 72  ? 22.30636 12.18239 20.67370  0.700 62.87061  ? 72  LEU A C   1 
ATOM   569  O O   . LEU A 1 72  ? 22.57761 11.22682 19.94392  0.700 63.79546  ? 72  LEU A O   1 
ATOM   570  C CB  . LEU A 1 72  ? 24.20824 12.45420 22.27811  0.700 68.41135  ? 72  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 72  ? 24.82205 13.52508 21.36164  0.700 67.47903  ? 72  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 72  ? 24.47793 14.93264 21.83065  0.700 67.43355  ? 72  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 72  ? 26.32762 13.34558 21.24360  0.700 72.50265  ? 72  LEU A CD2 1 
ATOM   574  N N   . GLY A 1 73  ? 21.64691 13.25270 20.24670  1.000 61.50641  ? 73  GLY A N   1 
ATOM   575  C CA  . GLY A 1 73  ? 21.36692 13.48202 18.84986  1.000 60.34780  ? 73  GLY A CA  1 
ATOM   576  C C   . GLY A 1 73  ? 22.27125 14.56825 18.28680  1.000 63.84196  ? 73  GLY A C   1 
ATOM   577  O O   . GLY A 1 73  ? 23.00839 15.23702 19.00880  1.000 69.69331  ? 73  GLY A O   1 
ATOM   578  N N   . PHE A 1 74  ? 22.20323 14.73167 16.96534  1.000 59.07962  ? 74  PHE A N   1 
ATOM   579  C CA  . PHE A 1 74  ? 22.99946 15.77202 16.33084  1.000 60.68675  ? 74  PHE A CA  1 
ATOM   580  C C   . PHE A 1 74  ? 22.34719 17.13339 16.44049  1.000 62.48725  ? 74  PHE A C   1 
ATOM   581  O O   . PHE A 1 74  ? 23.04599 18.15247 16.45242  1.000 67.33566  ? 74  PHE A O   1 
ATOM   582  C CB  . PHE A 1 74  ? 23.25705 15.42833 14.86567  1.000 56.82777  ? 74  PHE A CB  1 
ATOM   583  C CG  . PHE A 1 74  ? 24.45067 14.57004 14.68057  1.000 57.33740  ? 74  PHE A CG  1 
ATOM   584  C CD1 . PHE A 1 74  ? 24.41257 13.23877 15.03637  1.000 55.29439  ? 74  PHE A CD1 1 
ATOM   585  C CD2 . PHE A 1 74  ? 25.63284 15.10176 14.22668  1.000 60.52499  ? 74  PHE A CD2 1 
ATOM   586  C CE1 . PHE A 1 74  ? 25.50772 12.43534 14.88320  1.000 56.56889  ? 74  PHE A CE1 1 
ATOM   587  C CE2 . PHE A 1 74  ? 26.74761 14.30578 14.07998  1.000 62.30782  ? 74  PHE A CE2 1 
ATOM   588  C CZ  . PHE A 1 74  ? 26.68523 12.96832 14.40933  1.000 60.26529  ? 74  PHE A CZ  1 
ATOM   589  N N   . TYR A 1 75  ? 21.02465 17.16990 16.50779  1.000 60.46110  ? 75  TYR A N   1 
ATOM   590  C CA  . TYR A 1 75  ? 20.30846 18.41089 16.74224  1.000 61.06522  ? 75  TYR A CA  1 
ATOM   591  C C   . TYR A 1 75  ? 19.92548 18.60065 18.20586  1.000 61.00616  ? 75  TYR A C   1 
ATOM   592  O O   . TYR A 1 75  ? 19.87731 19.74046 18.68110  1.000 62.06695  ? 75  TYR A O   1 
ATOM   593  C CB  . TYR A 1 75  ? 19.05608 18.46160 15.86073  1.000 57.40693  ? 75  TYR A CB  1 
ATOM   594  C CG  . TYR A 1 75  ? 19.32635 18.19471 14.38737  1.000 56.26324  ? 75  TYR A CG  1 
ATOM   595  C CD1 . TYR A 1 75  ? 20.12470 19.05029 13.63944  1.000 59.32194  ? 75  TYR A CD1 1 
ATOM   596  C CD2 . TYR A 1 75  ? 18.77205 17.09041 13.74490  1.000 53.28415  ? 75  TYR A CD2 1 
ATOM   597  C CE1 . TYR A 1 75  ? 20.37112 18.81066 12.29168  1.000 60.38336  ? 75  TYR A CE1 1 
ATOM   598  C CE2 . TYR A 1 75  ? 19.01170 16.84119 12.39682  1.000 53.87649  ? 75  TYR A CE2 1 
ATOM   599  C CZ  . TYR A 1 75  ? 19.81261 17.70547 11.67613  1.000 57.67368  ? 75  TYR A CZ  1 
ATOM   600  O OH  . TYR A 1 75  ? 20.06304 17.47454 10.33960  1.000 59.16778  ? 75  TYR A OH  1 
ATOM   601  N N   . ALA A 1 76  ? 19.68624 17.51482 18.94318  1.000 60.67800  ? 76  ALA A N   1 
ATOM   602  C CA  . ALA A 1 76  ? 19.40960 17.59425 20.37859  1.000 63.50586  ? 76  ALA A CA  1 
ATOM   603  C C   . ALA A 1 76  ? 20.72306 17.39079 21.12756  1.000 69.17036  ? 76  ALA A C   1 
ATOM   604  O O   . ALA A 1 76  ? 20.99718 16.32635 21.68015  1.000 70.19483  ? 76  ALA A O   1 
ATOM   605  C CB  . ALA A 1 76  ? 18.35774 16.56711 20.78804  1.000 60.10496  ? 76  ALA A CB  1 
ATOM   606  N N   . ASP A 1 77  ? 21.54636 18.43480 21.13473  1.000 73.47061  ? 77  ASP A N   1 
ATOM   607  C CA  . ASP A 1 77  ? 22.87181 18.39218 21.75780  1.000 77.76729  ? 77  ASP A CA  1 
ATOM   608  C C   . ASP A 1 77  ? 22.88976 19.08636 23.12075  1.000 80.48505  ? 77  ASP A C   1 
ATOM   609  O O   . ASP A 1 77  ? 23.79137 19.85751 23.44254  1.000 86.16308  ? 77  ASP A O   1 
ATOM   610  C CB  . ASP A 1 77  ? 23.90399 18.99684 20.81730  1.000 82.06365  ? 77  ASP A CB  1 
ATOM   611  C CG  . ASP A 1 77  ? 23.43375 20.29122 20.17360  1.000 83.35870  ? 77  ASP A CG  1 
ATOM   612  O OD1 . ASP A 1 77  ? 22.41380 20.85977 20.61061  1.000 82.01410  ? 77  ASP A OD1 1 
ATOM   613  O OD2 . ASP A 1 77  ? 24.10032 20.73404 19.21354  1.000 86.31367  ? 77  ASP A OD2 1 
ATOM   614  N N   . TRP A 1 78  ? 21.88548 18.81175 23.94984  1.000 76.70420  ? 78  TRP A N   1 
ATOM   615  C CA  . TRP A 1 78  ? 21.82328 19.32146 25.31641  1.000 79.65322  ? 78  TRP A CA  1 
ATOM   616  C C   . TRP A 1 78  ? 21.27738 18.22895 26.22092  1.000 77.85355  ? 78  TRP A C   1 
ATOM   617  O O   . TRP A 1 78  ? 20.22160 17.65552 25.93585  1.000 74.09527  ? 78  TRP A O   1 
ATOM   618  C CB  . TRP A 1 78  ? 20.94097 20.57178 25.42125  0.800 78.73096  ? 78  TRP A CB  1 
ATOM   619  C CG  . TRP A 1 78  ? 21.65694 21.83975 25.09993  0.700 82.65510  ? 78  TRP A CG  1 
ATOM   620  C CD1 . TRP A 1 78  ? 21.79431 22.42117 23.87243  0.600 82.04434  ? 78  TRP A CD1 1 
ATOM   621  C CD2 . TRP A 1 78  ? 22.34278 22.68715 26.02568  0.600 88.56533  ? 78  TRP A CD2 1 
ATOM   622  N NE1 . TRP A 1 78  ? 22.52617 23.58028 23.97905  0.600 87.44382  ? 78  TRP A NE1 1 
ATOM   623  C CE2 . TRP A 1 78  ? 22.87495 23.76522 25.29188  0.600 91.41317  ? 78  TRP A CE2 1 
ATOM   624  C CE3 . TRP A 1 78  ? 22.55974 22.63767 27.40529  0.600 92.27155  ? 78  TRP A CE3 1 
ATOM   625  C CZ2 . TRP A 1 78  ? 23.61066 24.78627 25.89390  0.600 97.90538  ? 78  TRP A CZ2 1 
ATOM   626  C CZ3 . TRP A 1 78  ? 23.28916 23.64992 28.00080  0.600 98.64093  ? 78  TRP A CZ3 1 
ATOM   627  C CH2 . TRP A 1 78  ? 23.80590 24.70988 27.24638  0.600 101.41909 ? 78  TRP A CH2 1 
ATOM   628  N N   . ARG A 1 79  ? 21.99378 17.92737 27.29534  1.000 81.31754  ? 79  ARG A N   1 
ATOM   629  C CA  . ARG A 1 79  ? 21.46949 16.93033 28.20884  1.000 79.36262  ? 79  ARG A CA  1 
ATOM   630  C C   . ARG A 1 79  ? 20.36795 17.52919 29.06812  1.000 76.75813  ? 79  ARG A C   1 
ATOM   631  O O   . ARG A 1 79  ? 20.30841 18.74660 29.26010  1.000 77.20667  ? 79  ARG A O   1 
ATOM   632  C CB  . ARG A 1 79  ? 22.57371 16.38286 29.09657  1.000 85.41686  ? 79  ARG A CB  1 
ATOM   633  C CG  . ARG A 1 79  ? 23.59006 15.53883 28.37421  0.800 86.57603  ? 79  ARG A CG  1 
ATOM   634  C CD  . ARG A 1 79  ? 24.47452 14.84575 29.37684  0.700 93.82208  ? 79  ARG A CD  1 
ATOM   635  N NE  . ARG A 1 79  ? 24.64938 15.63934 30.58792  0.700 99.88095  ? 79  ARG A NE  1 
ATOM   636  C CZ  . ARG A 1 79  ? 25.46353 16.68158 30.69099  0.700 104.64074 ? 79  ARG A CZ  1 
ATOM   637  N NH1 . ARG A 1 79  ? 26.13451 17.13942 29.64620  0.700 104.33948 ? 79  ARG A NH1 1 
ATOM   638  N NH2 . ARG A 1 79  ? 25.60792 17.27907 31.87119  0.700 110.15288 ? 79  ARG A NH2 1 
ATOM   639  N N   . PRO A 1 80  ? 19.47317 16.68852 29.59255  1.000 74.50041  ? 80  PRO A N   1 
ATOM   640  C CA  . PRO A 1 80  ? 18.43098 17.21004 30.49086  1.000 74.52402  ? 80  PRO A CA  1 
ATOM   641  C C   . PRO A 1 80  ? 18.98214 17.90418 31.72243  1.000 81.35566  ? 80  PRO A C   1 
ATOM   642  O O   . PRO A 1 80  ? 18.35558 18.84817 32.21759  1.000 82.32337  ? 80  PRO A O   1 
ATOM   643  C CB  . PRO A 1 80  ? 17.63335 15.95197 30.86292  1.000 73.43172  ? 80  PRO A CB  1 
ATOM   644  C CG  . PRO A 1 80  ? 17.90523 14.98052 29.75391  1.000 69.90990  ? 80  PRO A CG  1 
ATOM   645  C CD  . PRO A 1 80  ? 19.31851 15.24552 29.33629  1.000 72.17488  ? 80  PRO A CD  1 
ATOM   646  N N   . ALA A 1 81  ? 20.13167 17.46509 32.24203  1.000 86.40100  ? 81  ALA A N   1 
ATOM   647  C CA  . ALA A 1 81  ? 20.64872 18.04442 33.48080  1.000 93.40853  ? 81  ALA A CA  1 
ATOM   648  C C   . ALA A 1 81  ? 21.09013 19.48848 33.30465  1.000 91.69791  ? 81  ALA A C   1 
ATOM   649  O O   . ALA A 1 81  ? 21.33246 20.17716 34.30100  1.000 96.87077  ? 81  ALA A O   1 
ATOM   650  C CB  . ALA A 1 81  ? 21.81155 17.20436 34.01784  1.000 86.72809  ? 81  ALA A CB  1 
ATOM   651  N N   . GLU A 1 82  ? 21.18381 19.96230 32.06523  1.000 93.32780  ? 82  GLU A N   1 
ATOM   652  C CA  . GLU A 1 82  ? 21.57354 21.32922 31.76153  1.000 95.06311  ? 82  GLU A CA  1 
ATOM   653  C C   . GLU A 1 82  ? 20.37706 22.20172 31.41468  1.000 89.53742  ? 82  GLU A C   1 
ATOM   654  O O   . GLU A 1 82  ? 20.54619 23.27420 30.82351  1.000 89.35260  ? 82  GLU A O   1 
ATOM   655  C CB  . GLU A 1 82  ? 22.59351 21.33234 30.62531  1.000 92.93288  ? 82  GLU A CB  1 
ATOM   656  C CG  . GLU A 1 82  ? 23.87931 20.63482 31.01442  0.390 96.44214  ? 82  GLU A CG  1 
ATOM   657  C CD  . GLU A 1 82  ? 24.84132 20.48644 29.86518  0.870 95.79799  ? 82  GLU A CD  1 
ATOM   658  O OE1 . GLU A 1 82  ? 24.38152 20.37385 28.70711  1.000 89.86240  ? 82  GLU A OE1 1 
ATOM   659  O OE2 . GLU A 1 82  ? 26.06138 20.48090 30.12712  0.830 102.36780 ? 82  GLU A OE2 1 
ATOM   660  N N   . ALA A 1 83  ? 19.17143 21.76565 31.78828  1.000 86.20336  ? 83  ALA A N   1 
ATOM   661  C CA  . ALA A 1 83  ? 17.96536 22.49402 31.41279  1.000 82.45692  ? 83  ALA A CA  1 
ATOM   662  C C   . ALA A 1 83  ? 17.83757 23.79939 32.18611  1.000 86.96448  ? 83  ALA A C   1 
ATOM   663  O O   . ALA A 1 83  ? 17.48233 24.83255 31.60661  1.000 87.11152  ? 83  ALA A O   1 
ATOM   664  C CB  . ALA A 1 83  ? 16.73280 21.61740 31.63155  1.000 78.53654  ? 83  ALA A CB  1 
ATOM   665  N N   . ASP A 1 84  ? 18.11418 23.77495 33.49286  1.000 89.60679  ? 84  ASP A N   1 
ATOM   666  C CA  . ASP A 1 84  ? 18.03767 24.99969 34.28109  1.000 91.85969  ? 84  ASP A CA  1 
ATOM   667  C C   . ASP A 1 84  ? 19.02068 26.03953 33.75799  1.000 94.28495  ? 84  ASP A C   1 
ATOM   668  O O   . ASP A 1 84  ? 18.66049 27.20568 33.56097  1.000 95.39475  ? 84  ASP A O   1 
ATOM   669  C CB  . ASP A 1 84  ? 18.29126 24.69296 35.76023  0.800 97.14187  ? 84  ASP A CB  1 
ATOM   670  C CG  . ASP A 1 84  ? 17.12740 23.96437 36.41372  0.700 96.32044  ? 84  ASP A CG  1 
ATOM   671  O OD1 . ASP A 1 84  ? 15.97066 24.18954 35.99801  0.700 92.54502  ? 84  ASP A OD1 1 
ATOM   672  O OD2 . ASP A 1 84  ? 17.36820 23.16397 37.34146  0.700 100.63453 ? 84  ASP A OD2 1 
ATOM   673  N N   . LYS A 1 85  ? 20.26866 25.62718 33.50884  1.000 96.32375  ? 85  LYS A N   1 
ATOM   674  C CA  . LYS A 1 85  ? 21.26087 26.54701 32.96073  1.000 101.15718 ? 85  LYS A CA  1 
ATOM   675  C C   . LYS A 1 85  ? 20.86982 27.02337 31.56793  1.000 97.33054  ? 85  LYS A C   1 
ATOM   676  O O   . LYS A 1 85  ? 21.23730 28.13242 31.16355  1.000 101.34475 ? 85  LYS A O   1 
ATOM   677  C CB  . LYS A 1 85  ? 22.63644 25.87845 32.92750  1.000 97.10707  ? 85  LYS A CB  1 
ATOM   678  N N   . LEU A 1 86  ? 20.12269 26.20423 30.82718  1.000 90.04494  ? 86  LEU A N   1 
ATOM   679  C CA  . LEU A 1 86  ? 19.63599 26.61593 29.51751  1.000 85.87054  ? 86  LEU A CA  1 
ATOM   680  C C   . LEU A 1 86  ? 18.56343 27.69225 29.62917  1.000 84.22883  ? 86  LEU A C   1 
ATOM   681  O O   . LEU A 1 86  ? 18.53597 28.62934 28.82250  1.000 85.50210  ? 86  LEU A O   1 
ATOM   682  C CB  . LEU A 1 86  ? 19.08932 25.40139 28.77216  1.000 79.45810  ? 86  LEU A CB  1 
ATOM   683  C CG  . LEU A 1 86  ? 18.92027 25.56870 27.26987  1.000 67.24991  ? 86  LEU A CG  1 
ATOM   684  C CD1 . LEU A 1 86  ? 20.24174 25.98860 26.65457  1.000 71.47458  ? 86  LEU A CD1 1 
ATOM   685  C CD2 . LEU A 1 86  ? 18.42722 24.27236 26.66711  1.000 65.76390  ? 86  LEU A CD2 1 
ATOM   686  N N   . VAL A 1 87  ? 17.68077 27.57373 30.62322  1.000 82.86227  ? 87  VAL A N   1 
ATOM   687  C CA  . VAL A 1 87  ? 16.57989 28.51947 30.78862  1.000 82.97508  ? 87  VAL A CA  1 
ATOM   688  C C   . VAL A 1 87  ? 17.10701 29.92479 31.05295  1.000 89.71939  ? 87  VAL A C   1 
ATOM   689  O O   . VAL A 1 87  ? 16.58954 30.91000 30.51273  1.000 89.84757  ? 87  VAL A O   1 
ATOM   690  C CB  . VAL A 1 87  ? 15.64984 28.03860 31.91948  1.000 81.41677  ? 87  VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 87  ? 14.64142 29.11371 32.30149  1.000 82.49562  ? 87  VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 87  ? 14.93875 26.75638 31.50763  1.000 74.84751  ? 87  VAL A CG2 1 
ATOM   693  N N   . LYS A 1 88  ? 18.14854 30.03770 31.87890  1.000 96.60661  ? 88  LYS A N   1 
ATOM   694  C CA  . LYS A 1 88  ? 18.66943 31.34678 32.26397  1.000 105.91462 ? 88  LYS A CA  1 
ATOM   695  C C   . LYS A 1 88  ? 19.17177 32.12131 31.05152  1.000 109.41463 ? 88  LYS A C   1 
ATOM   696  O O   . LYS A 1 88  ? 18.70661 33.23293 30.77186  1.000 113.18503 ? 88  LYS A O   1 
ATOM   697  C CB  . LYS A 1 88  ? 19.78776 31.17779 33.29758  0.710 112.04129 ? 88  LYS A CB  1 
ATOM   698  C CG  . LYS A 1 88  ? 19.38024 30.41141 34.55526  0.960 111.44941 ? 88  LYS A CG  1 
ATOM   699  C CD  . LYS A 1 88  ? 20.57104 30.13991 35.47783  1.000 117.75855 ? 88  LYS A CD  1 
ATOM   700  C CE  . LYS A 1 88  ? 20.11238 29.57616 36.82124  0.960 117.69850 ? 88  LYS A CE  1 
ATOM   701  N NZ  . LYS A 1 88  ? 21.24607 29.09535 37.66120  1.000 123.53818 ? 88  LYS A NZ  1 
ATOM   702  N N   . LEU A 1 89  ? 20.11228 31.53556 30.30803  1.000 109.29570 ? 89  LEU A N   1 
ATOM   703  C CA  . LEU A 1 89  ? 20.70961 32.22909 29.17357  1.000 112.25204 ? 89  LEU A CA  1 
ATOM   704  C C   . LEU A 1 89  ? 19.69149 32.50308 28.07513  1.000 107.38636 ? 89  LEU A C   1 
ATOM   705  O O   . LEU A 1 89  ? 19.81367 33.50379 27.36044  1.000 110.39868 ? 89  LEU A O   1 
ATOM   706  C CB  . LEU A 1 89  ? 21.87737 31.40905 28.63149  1.000 111.92114 ? 89  LEU A CB  1 
ATOM   707  C CG  . LEU A 1 89  ? 22.85944 30.89712 29.68865  1.000 116.17093 ? 89  LEU A CG  1 
ATOM   708  C CD1 . LEU A 1 89  ? 23.66351 29.73087 29.14055  1.000 114.13902 ? 89  LEU A CD1 1 
ATOM   709  C CD2 . LEU A 1 89  ? 23.77514 32.01597 30.15454  1.000 126.16051 ? 89  LEU A CD2 1 
ATOM   710  N N   . LEU A 1 90  ? 18.69078 31.63231 27.92328  1.000 101.46356 ? 90  LEU A N   1 
ATOM   711  C CA  . LEU A 1 90  ? 17.63400 31.87898 26.94951  1.000 98.36467  ? 90  LEU A CA  1 
ATOM   712  C C   . LEU A 1 90  ? 16.85775 33.14195 27.29523  1.000 102.26998 ? 90  LEU A C   1 
ATOM   713  O O   . LEU A 1 90  ? 16.55740 33.95855 26.41794  1.000 104.46283 ? 90  LEU A O   1 
ATOM   714  C CB  . LEU A 1 90  ? 16.69165 30.67731 26.88199  1.000 91.95440  ? 90  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 90  ? 16.67941 29.82304 25.61419  1.000 87.30281  ? 90  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 90  ? 17.23779 30.58310 24.40978  1.000 90.39682  ? 90  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 90  ? 17.43145 28.52851 25.84877  1.000 84.64214  ? 90  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 91  ? 16.51476 33.31353 28.57434  0.840 104.48669 ? 91  ALA A N   1 
ATOM   719  C CA  . ALA A 1 91  ? 15.68122 34.44320 28.96859  1.000 108.74017 ? 91  ALA A CA  1 
ATOM   720  C C   . ALA A 1 91  ? 16.40563 35.76552 28.75861  1.000 115.88727 ? 91  ALA A C   1 
ATOM   721  O O   . ALA A 1 91  ? 15.79867 36.74917 28.32215  1.000 119.08887 ? 91  ALA A O   1 
ATOM   722  C CB  . ALA A 1 91  ? 15.24629 34.28938 30.42458  1.000 109.73339 ? 91  ALA A CB  1 
ATOM   723  N N   . LYS A 1 92  ? 17.70568 35.80867 29.05957  1.000 119.66183 ? 92  LYS A N   1 
ATOM   724  C CA  . LYS A 1 92  ? 18.47638 37.03050 28.84531  1.000 126.71583 ? 92  LYS A CA  1 
ATOM   725  C C   . LYS A 1 92  ? 18.72700 37.27578 27.36361  1.000 126.78482 ? 92  LYS A C   1 
ATOM   726  O O   . LYS A 1 92  ? 18.45868 38.36803 26.85041  1.000 129.75472 ? 92  LYS A O   1 
ATOM   727  C CB  . LYS A 1 92  ? 19.80949 36.96505 29.59499  1.000 131.34853 ? 92  LYS A CB  1 
ATOM   728  C CG  . LYS A 1 92  ? 20.90809 37.79471 28.92663  0.880 138.58992 ? 92  LYS A CG  1 
ATOM   729  C CD  . LYS A 1 92  ? 21.88854 38.40284 29.91920  0.810 147.86207 ? 92  LYS A CD  1 
ATOM   730  C CE  . LYS A 1 92  ? 23.11826 37.53041 30.13496  1.000 149.42324 ? 92  LYS A CE  1 
ATOM   731  N NZ  . LYS A 1 92  ? 22.95711 36.60538 31.28899  1.000 146.22826 ? 92  LYS A NZ  1 
ATOM   732  N N   . GLY A 1 93  ? 19.24711 36.27328 26.66210  1.000 92.46911  ? 93  GLY A N   1 
ATOM   733  C CA  . GLY A 1 93  ? 19.72659 36.47481 25.31215  1.000 93.54462  ? 93  GLY A CA  1 
ATOM   734  C C   . GLY A 1 93  ? 21.22857 36.30977 25.21611  1.000 96.83640  ? 93  GLY A C   1 
ATOM   735  O O   . GLY A 1 93  ? 21.78242 35.32499 25.71484  1.000 95.05409  ? 93  GLY A O   1 
ATOM   736  N N   . GLU A 1 94  ? 21.89147 37.26992 24.57062  0.500 102.03383 ? 94  GLU A N   1 
ATOM   737  C CA  . GLU A 1 94  ? 23.34957 37.28599 24.44171  0.500 107.14426 ? 94  GLU A CA  1 
ATOM   738  C C   . GLU A 1 94  ? 23.87826 35.95610 23.91433  0.500 108.32006 ? 94  GLU A C   1 
ATOM   739  O O   . GLU A 1 94  ? 24.92427 35.45805 24.33779  0.500 111.13674 ? 94  GLU A O   1 
ATOM   740  C CB  . GLU A 1 94  ? 24.00510 37.65412 25.76772  0.500 107.65519 ? 94  GLU A CB  1 
ATOM   741  C CG  . GLU A 1 94  ? 23.35407 38.85438 26.41194  0.500 108.60179 ? 94  GLU A CG  1 
ATOM   742  C CD  . GLU A 1 94  ? 24.35725 39.78940 27.03540  0.500 110.03145 ? 94  GLU A CD  1 
ATOM   743  O OE1 . GLU A 1 94  ? 25.57047 39.51042 26.93536  0.500 109.26850 ? 94  GLU A OE1 1 
ATOM   744  O OE2 . GLU A 1 94  ? 23.93233 40.80579 27.62181  0.500 112.27732 ? 94  GLU A OE2 1 
ATOM   745  N N   . TYR A 1 95  ? 23.13563 35.37352 22.98258  1.000 107.58382 ? 95  TYR A N   1 
ATOM   746  C CA  . TYR A 1 95  ? 23.52388 34.14322 22.31657  1.000 108.19604 ? 95  TYR A CA  1 
ATOM   747  C C   . TYR A 1 95  ? 23.62455 34.40153 20.82148  1.000 107.98089 ? 95  TYR A C   1 
ATOM   748  O O   . TYR A 1 95  ? 22.81365 35.13736 20.24966  1.000 108.32411 ? 95  TYR A O   1 
ATOM   749  C CB  . TYR A 1 95  ? 22.52275 33.00829 22.59622  1.000 108.22903 ? 95  TYR A CB  1 
ATOM   750  C CG  . TYR A 1 95  ? 21.08790 33.34515 22.24788  1.000 109.64742 ? 95  TYR A CG  1 
ATOM   751  C CD1 . TYR A 1 95  ? 20.58309 33.10762 20.97425  1.000 108.53444 ? 95  TYR A CD1 1 
ATOM   752  C CD2 . TYR A 1 95  ? 20.23497 33.89097 23.19599  1.000 112.57267 ? 95  TYR A CD2 1 
ATOM   753  C CE1 . TYR A 1 95  ? 19.27329 33.41568 20.65451  1.000 109.70324 ? 95  TYR A CE1 1 
ATOM   754  C CE2 . TYR A 1 95  ? 18.92392 34.20159 22.88603  1.000 113.75445 ? 95  TYR A CE2 1 
ATOM   755  C CZ  . TYR A 1 95  ? 18.44937 33.96159 21.61502  1.000 112.48253 ? 95  TYR A CZ  1 
ATOM   756  O OH  . TYR A 1 95  ? 17.14612 34.27050 21.30510  1.000 113.54877 ? 95  TYR A OH  1 
ATOM   757  N N   . GLN A 1 96  ? 24.63185 33.80834 20.19937  1.000 107.62368 ? 96  GLN A N   1 
ATOM   758  C CA  . GLN A 1 96  ? 24.79644 33.88651 18.75927  1.000 108.11820 ? 96  GLN A CA  1 
ATOM   759  C C   . GLN A 1 96  ? 23.95861 32.81186 18.08052  1.000 105.58585 ? 96  GLN A C   1 
ATOM   760  O O   . GLN A 1 96  ? 23.63019 31.77763 18.66808  1.000 104.79218 ? 96  GLN A O   1 
ATOM   761  C CB  . GLN A 1 96  ? 26.26391 33.72144 18.36921  1.000 108.76058 ? 96  GLN A CB  1 
ATOM   762  C CG  . GLN A 1 96  ? 27.20669 34.66838 19.07947  1.000 112.53854 ? 96  GLN A CG  1 
ATOM   763  C CD  . GLN A 1 96  ? 28.31912 33.93547 19.80353  0.540 112.31411 ? 96  GLN A CD  1 
ATOM   764  O OE1 . GLN A 1 96  ? 28.08037 33.24540 20.79580  0.790 111.29292 ? 96  GLN A OE1 1 
ATOM   765  N NE2 . GLN A 1 96  ? 29.54290 34.07459 19.30485  0.990 113.28636 ? 96  GLN A NE2 1 
ATOM   766  N N   . LYS A 1 97  ? 23.62092 33.06746 16.82242  1.000 105.08479 ? 97  LYS A N   1 
ATOM   767  C CA  . LYS A 1 97  ? 22.86992 32.12788 16.00814  1.000 101.93303 ? 97  LYS A CA  1 
ATOM   768  C C   . LYS A 1 97  ? 23.79484 31.49110 14.98207  1.000 99.60193  ? 97  LYS A C   1 
ATOM   769  O O   . LYS A 1 97  ? 24.62063 32.17317 14.36717  1.000 101.32485 ? 97  LYS A O   1 
ATOM   770  C CB  . LYS A 1 97  ? 21.69827 32.82061 15.30689  1.000 103.13489 ? 97  LYS A CB  1 
ATOM   771  C CG  . LYS A 1 97  ? 20.89686 33.73776 16.22492  1.000 106.18403 ? 97  LYS A CG  1 
ATOM   772  C CD  . LYS A 1 97  ? 19.43564 33.84913 15.80708  1.000 107.38993 ? 97  LYS A CD  1 
ATOM   773  C CE  . LYS A 1 97  ? 19.26806 34.58572 14.48897  1.000 109.86458 ? 97  LYS A CE  1 
ATOM   774  N NZ  . LYS A 1 97  ? 17.82892 34.70814 14.11659  1.000 111.04614 ? 97  LYS A NZ  1 
ATOM   775  N N   . VAL A 1 98  ? 23.66814 30.17787 14.81902  1.000 92.86920  ? 98  VAL A N   1 
ATOM   776  C CA  . VAL A 1 98  ? 24.36512 29.43941 13.77464  1.000 86.35592  ? 98  VAL A CA  1 
ATOM   777  C C   . VAL A 1 98  ? 23.31841 28.90200 12.80835  1.000 80.89935  ? 98  VAL A C   1 
ATOM   778  O O   . VAL A 1 98  ? 22.20786 28.54914 13.22031  1.000 81.25424  ? 98  VAL A O   1 
ATOM   779  C CB  . VAL A 1 98  ? 25.24078 28.30594 14.35493  1.000 84.02429  ? 98  VAL A CB  1 
ATOM   780  C CG1 . VAL A 1 98  ? 26.02042 28.81046 15.56327  1.000 85.86951  ? 98  VAL A CG1 1 
ATOM   781  C CG2 . VAL A 1 98  ? 24.40805 27.08767 14.73109  1.000 81.47865  ? 98  VAL A CG2 1 
ATOM   782  N N   . SER A 1 99  ? 23.65573 28.88125 11.52080  1.000 75.79910  ? 99  SER A N   1 
ATOM   783  C CA  . SER A 1 99  ? 22.70357 28.52627 10.47842  1.000 73.23687  ? 99  SER A CA  1 
ATOM   784  C C   . SER A 1 99  ? 23.23537 27.36183 9.66371   1.000 69.10167  ? 99  SER A C   1 
ATOM   785  O O   . SER A 1 99  ? 24.38343 27.38559 9.21201   1.000 69.96049  ? 99  SER A O   1 
ATOM   786  C CB  . SER A 1 99  ? 22.41032 29.71576 9.56617   1.000 75.87704  ? 99  SER A CB  1 
ATOM   787  O OG  . SER A 1 99  ? 21.83943 30.78187 10.30082  1.000 79.34893  ? 99  SER A OG  1 
ATOM   788  N N   . TYR A 1 100 ? 22.39709 26.35335 9.47840   1.000 65.81072  ? 100 TYR A N   1 
ATOM   789  C CA  . TYR A 1 100 ? 22.70287 25.21127 8.63048   1.000 60.83860  ? 100 TYR A CA  1 
ATOM   790  C C   . TYR A 1 100 ? 21.90652 25.28358 7.33017   1.000 59.13697  ? 100 TYR A C   1 
ATOM   791  O O   . TYR A 1 100 ? 20.72706 25.65195 7.34831   1.000 58.46993  ? 100 TYR A O   1 
ATOM   792  C CB  . TYR A 1 100 ? 22.38587 23.90050 9.35224   1.000 56.90330  ? 100 TYR A CB  1 
ATOM   793  C CG  . TYR A 1 100 ? 23.38066 23.52565 10.43917  0.700 55.12797  ? 100 TYR A CG  1 
ATOM   794  C CD1 . TYR A 1 100 ? 24.47009 24.33867 10.72889  0.700 56.05979  ? 100 TYR A CD1 1 
ATOM   795  C CD2 . TYR A 1 100 ? 23.23813 22.34071 11.16288  0.700 53.20655  ? 100 TYR A CD2 1 
ATOM   796  C CE1 . TYR A 1 100 ? 25.38268 23.98861 11.71490  0.700 56.62149  ? 100 TYR A CE1 1 
ATOM   797  C CE2 . TYR A 1 100 ? 24.14606 21.98179 12.14460  0.700 53.54211  ? 100 TYR A CE2 1 
ATOM   798  C CZ  . TYR A 1 100 ? 25.21685 22.80693 12.41711  0.700 55.61613  ? 100 TYR A CZ  1 
ATOM   799  O OH  . TYR A 1 100 ? 26.12150 22.45063 13.39645  0.700 56.84143  ? 100 TYR A OH  1 
ATOM   800  N N   . PRO A 1 101 ? 22.52378 24.97165 6.19050   1.000 58.55693  ? 101 PRO A N   1 
ATOM   801  C CA  . PRO A 1 101 ? 21.79128 24.99975 4.92049   1.000 58.66145  ? 101 PRO A CA  1 
ATOM   802  C C   . PRO A 1 101 ? 20.68523 23.95906 4.90336   1.000 57.20076  ? 101 PRO A C   1 
ATOM   803  O O   . PRO A 1 101 ? 20.68105 23.00084 5.67900   1.000 55.53178  ? 101 PRO A O   1 
ATOM   804  C CB  . PRO A 1 101 ? 22.86589 24.67927 3.87048   1.000 58.28297  ? 101 PRO A CB  1 
ATOM   805  C CG  . PRO A 1 101 ? 24.17442 24.93273 4.55578   1.000 58.93801  ? 101 PRO A CG  1 
ATOM   806  C CD  . PRO A 1 101 ? 23.93763 24.61353 6.00067   1.000 58.40563  ? 101 PRO A CD  1 
ATOM   807  N N   . LEU A 1 102 ? 19.73445 24.16569 3.99679   1.000 58.32856  ? 102 LEU A N   1 
ATOM   808  C CA  . LEU A 1 102 ? 18.58277 23.29113 3.84393   1.000 57.00912  ? 102 LEU A CA  1 
ATOM   809  C C   . LEU A 1 102 ? 18.45748 22.86003 2.38790   1.000 55.96743  ? 102 LEU A C   1 
ATOM   810  O O   . LEU A 1 102 ? 19.07989 23.42975 1.48895   1.000 56.55009  ? 102 LEU A O   1 
ATOM   811  C CB  . LEU A 1 102 ? 17.29741 23.98610 4.31309   1.000 58.87949  ? 102 LEU A CB  1 
ATOM   812  C CG  . LEU A 1 102 ? 17.25253 24.43096 5.78011   1.000 59.51697  ? 102 LEU A CG  1 
ATOM   813  C CD1 . LEU A 1 102 ? 16.10498 25.39632 6.01557   1.000 61.08252  ? 102 LEU A CD1 1 
ATOM   814  C CD2 . LEU A 1 102 ? 17.14547 23.23148 6.71319   1.000 57.91637  ? 102 LEU A CD2 1 
ATOM   815  N N   . LEU A 1 103 ? 17.63123 21.84288 2.16430   1.000 54.23294  ? 103 LEU A N   1 
ATOM   816  C CA  . LEU A 1 103 ? 17.43313 21.25002 0.84982   1.000 53.99688  ? 103 LEU A CA  1 
ATOM   817  C C   . LEU A 1 103 ? 16.01461 21.52628 0.37139   1.000 55.74811  ? 103 LEU A C   1 
ATOM   818  O O   . LEU A 1 103 ? 15.05383 21.32846 1.12160   1.000 56.61710  ? 103 LEU A O   1 
ATOM   819  C CB  . LEU A 1 103 ? 17.69400 19.74327 0.89680   1.000 52.03345  ? 103 LEU A CB  1 
ATOM   820  C CG  . LEU A 1 103 ? 17.36884 18.91847 -0.34960  1.000 52.23819  ? 103 LEU A CG  1 
ATOM   821  C CD1 . LEU A 1 103 ? 18.17054 19.39161 -1.54994  1.000 52.77820  ? 103 LEU A CD1 1 
ATOM   822  C CD2 . LEU A 1 103 ? 17.63246 17.45448 -0.06761  1.000 50.78978  ? 103 LEU A CD2 1 
ATOM   823  N N   . LYS A 1 104 ? 15.88593 21.97620 -0.87476  1.000 56.53200  ? 104 LYS A N   1 
ATOM   824  C CA  . LYS A 1 104 ? 14.59084 22.23035 -1.49364  1.000 57.06776  ? 104 LYS A CA  1 
ATOM   825  C C   . LYS A 1 104 ? 14.29813 21.12849 -2.50088  1.000 55.89302  ? 104 LYS A C   1 
ATOM   826  O O   . LYS A 1 104 ? 15.17690 20.74227 -3.27797  1.000 54.87430  ? 104 LYS A O   1 
ATOM   827  C CB  . LYS A 1 104 ? 14.56046 23.59733 -2.17737  0.800 58.47861  ? 104 LYS A CB  1 
ATOM   828  C CG  . LYS A 1 104 ? 13.22869 23.93929 -2.82967  0.700 59.89237  ? 104 LYS A CG  1 
ATOM   829  C CD  . LYS A 1 104 ? 13.26427 25.32375 -3.45817  0.700 62.01724  ? 104 LYS A CD  1 
ATOM   830  C CE  . LYS A 1 104 ? 11.88936 25.75535 -3.93671  0.600 64.55780  ? 104 LYS A CE  1 
ATOM   831  N NZ  . LYS A 1 104 ? 11.93301 27.08998 -4.59873  0.600 67.60519  ? 104 LYS A NZ  1 
ATOM   832  N N   . THR A 1 105 ? 13.06892 20.62161 -2.47728  1.000 56.51709  ? 105 THR A N   1 
ATOM   833  C CA  . THR A 1 105 ? 12.64049 19.53344 -3.34752  1.000 55.78480  ? 105 THR A CA  1 
ATOM   834  C C   . THR A 1 105 ? 11.35826 19.94987 -4.04717  1.000 57.75694  ? 105 THR A C   1 
ATOM   835  O O   . THR A 1 105 ? 10.33768 20.16898 -3.38702  1.000 58.35894  ? 105 THR A O   1 
ATOM   836  C CB  . THR A 1 105 ? 12.41549 18.24397 -2.55340  1.000 54.32847  ? 105 THR A CB  1 
ATOM   837  O OG1 . THR A 1 105 ? 13.65953 17.80175 -2.00906  1.000 52.45135  ? 105 THR A OG1 1 
ATOM   838  C CG2 . THR A 1 105 ? 11.84291 17.15046 -3.44569  1.000 54.66293  ? 105 THR A CG2 1 
ATOM   839  N N   . THR A 1 106 ? 11.40905 20.05722 -5.37423  1.000 58.47261  ? 106 THR A N   1 
ATOM   840  C CA  . THR A 1 106 ? 10.25191 20.42988 -6.17898  1.000 61.64201  ? 106 THR A CA  1 
ATOM   841  C C   . THR A 1 106 ? 9.75631  19.21062 -6.94570  1.000 61.82724  ? 106 THR A C   1 
ATOM   842  O O   . THR A 1 106 ? 10.55198 18.49591 -7.56535  1.000 60.33346  ? 106 THR A O   1 
ATOM   843  C CB  . THR A 1 106 ? 10.59077 21.56847 -7.14606  1.000 64.11807  ? 106 THR A CB  1 
ATOM   844  O OG1 . THR A 1 106 ? 11.17000 22.65605 -6.41148  1.000 64.52558  ? 106 THR A OG1 1 
ATOM   845  C CG2 . THR A 1 106 ? 9.33577  22.05637 -7.85468  1.000 67.35277  ? 106 THR A CG2 1 
ATOM   846  N N   . VAL A 1 107 ? 8.44646  18.97580 -6.89359  1.000 63.90054  ? 107 VAL A N   1 
ATOM   847  C CA  . VAL A 1 107 ? 7.80987  17.81636 -7.51145  1.000 65.25051  ? 107 VAL A CA  1 
ATOM   848  C C   . VAL A 1 107 ? 6.74348  18.33181 -8.46943  1.000 70.07426  ? 107 VAL A C   1 
ATOM   849  O O   . VAL A 1 107 ? 5.69835  18.83050 -8.03220  1.000 72.24482  ? 107 VAL A O   1 
ATOM   850  C CB  . VAL A 1 107 ? 7.19388  16.87385 -6.46801  1.000 64.30392  ? 107 VAL A CB  1 
ATOM   851  C CG1 . VAL A 1 107 ? 6.57419  15.65811 -7.14650  1.000 65.01115  ? 107 VAL A CG1 1 
ATOM   852  C CG2 . VAL A 1 107 ? 8.23870  16.45892 -5.42645  1.000 61.13345  ? 107 VAL A CG2 1 
ATOM   853  N N   . LYS A 1 108 ? 6.99619  18.21223 -9.77018  1.000 72.02417  ? 108 LYS A N   1 
ATOM   854  C CA  . LYS A 1 108 ? 6.04124  18.63165 -10.78454 1.000 77.12269  ? 108 LYS A CA  1 
ATOM   855  C C   . LYS A 1 108 ? 5.23830  17.43878 -11.28920 1.000 79.97333  ? 108 LYS A C   1 
ATOM   856  O O   . LYS A 1 108 ? 5.71266  16.29983 -11.29002 1.000 77.60543  ? 108 LYS A O   1 
ATOM   857  C CB  . LYS A 1 108 ? 6.74710  19.31116 -11.95856 0.800 77.67715  ? 108 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 108 ? 7.55973  20.53518 -11.57797 0.700 76.89179  ? 108 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 108 ? 8.01589  21.28666 -12.81817 0.700 78.58772  ? 108 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 108 ? 8.76903  22.55192 -12.45198 0.700 78.22878  ? 108 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 108 ? 8.95763  23.43772 -13.63331 0.700 80.82219  ? 108 LYS A NZ  1 
ATOM   862  N N   . TYR A 1 109 ? 4.01696  17.71825 -11.73322 1.000 86.06498  ? 109 TYR A N   1 
ATOM   863  C CA  . TYR A 1 109 ? 3.10785  16.67959 -12.20702 1.000 89.24431  ? 109 TYR A CA  1 
ATOM   864  C C   . TYR A 1 109 ? 2.70450  16.92625 -13.65706 1.000 92.14032  ? 109 TYR A C   1 
ATOM   865  O O   . TYR A 1 109 ? 2.49589  18.06890 -14.06466 1.000 93.94170  ? 109 TYR A O   1 
ATOM   866  C CB  . TYR A 1 109 ? 1.86244  16.61142 -11.31691 1.000 92.50909  ? 109 TYR A CB  1 
ATOM   867  C CG  . TYR A 1 109 ? 2.17504  16.44457 -9.84408  1.000 90.96767  ? 109 TYR A CG  1 
ATOM   868  C CD1 . TYR A 1 109 ? 2.41072  17.54942 -9.03453  1.000 91.07467  ? 109 TYR A CD1 1 
ATOM   869  C CD2 . TYR A 1 109 ? 2.23578  15.18419 -9.26364  1.000 89.75932  ? 109 TYR A CD2 1 
ATOM   870  C CE1 . TYR A 1 109 ? 2.69888  17.40453 -7.69071  1.000 89.40021  ? 109 TYR A CE1 1 
ATOM   871  C CE2 . TYR A 1 109 ? 2.52051  15.03034 -7.92064  1.000 88.22798  ? 109 TYR A CE2 1 
ATOM   872  C CZ  . TYR A 1 109 ? 2.75265  16.14355 -7.14008  1.000 88.13310  ? 109 TYR A CZ  1 
ATOM   873  O OH  . TYR A 1 109 ? 3.04022  15.99492 -5.80363  1.000 86.62023  ? 109 TYR A OH  1 
ATOM   874  N N   . LYS A 1 114 ? -0.24079 20.53701 -10.54804 1.000 101.35143 ? 114 LYS A N   1 
ATOM   875  C CA  . LYS A 1 114 ? 0.63309  21.69060 -10.36282 1.000 100.24339 ? 114 LYS A CA  1 
ATOM   876  C C   . LYS A 1 114 ? 2.05412  21.25242 -9.98836  1.000 95.57616  ? 114 LYS A C   1 
ATOM   877  O O   . LYS A 1 114 ? 2.61231  20.33860 -10.60264 1.000 94.04199  ? 114 LYS A O   1 
ATOM   878  C CB  . LYS A 1 114 ? 0.05954  22.62363 -9.29292  1.000 101.69964 ? 114 LYS A CB  1 
ATOM   879  N N   . GLU A 1 115 ? 2.63947  21.91658 -8.99026  1.000 93.25399  ? 115 GLU A N   1 
ATOM   880  C CA  . GLU A 1 115 ? 3.95352  21.55666 -8.47347  1.000 88.82759  ? 115 GLU A CA  1 
ATOM   881  C C   . GLU A 1 115 ? 3.96241  21.75945 -6.96230  1.000 86.57095  ? 115 GLU A C   1 
ATOM   882  O O   . GLU A 1 115 ? 3.29334  22.65348 -6.43881  1.000 89.01138  ? 115 GLU A O   1 
ATOM   883  C CB  . GLU A 1 115 ? 5.07821  22.37481 -9.14543  1.000 88.98897  ? 115 GLU A CB  1 
ATOM   884  C CG  . GLU A 1 115 ? 5.52315  23.63023 -8.38562  1.000 89.65849  ? 115 GLU A CG  1 
ATOM   885  C CD  . GLU A 1 115 ? 6.78126  24.26836 -8.97056  1.000 89.28915  ? 115 GLU A CD  1 
ATOM   886  O OE1 . GLU A 1 115 ? 7.13976  23.93805 -10.12322 0.860 89.59241  ? 115 GLU A OE1 1 
ATOM   887  O OE2 . GLU A 1 115 ? 7.41131  25.09774 -8.27405  1.000 88.71228  ? 115 GLU A OE2 1 
ATOM   888  N N   . ALA A 1 116 ? 4.71584  20.91212 -6.26108  1.000 82.02832  ? 116 ALA A N   1 
ATOM   889  C CA  . ALA A 1 116 ? 4.79960  20.95264 -4.80414  1.000 79.76392  ? 116 ALA A CA  1 
ATOM   890  C C   . ALA A 1 116 ? 6.25736  21.02601 -4.37583  1.000 75.54316  ? 116 ALA A C   1 
ATOM   891  O O   . ALA A 1 116 ? 7.09084  20.26502 -4.87501  1.000 73.58517  ? 116 ALA A O   1 
ATOM   892  C CB  . ALA A 1 116 ? 4.13246  19.72646 -4.17278  1.000 79.41553  ? 116 ALA A CB  1 
ATOM   893  N N   . THR A 1 117 ? 6.56075  21.92977 -3.44609  1.000 74.43494  ? 117 THR A N   1 
ATOM   894  C CA  . THR A 1 117 ? 7.91337  22.11128 -2.93760  1.000 71.17856  ? 117 THR A CA  1 
ATOM   895  C C   . THR A 1 117 ? 7.98287  21.72663 -1.46398  1.000 68.82757  ? 117 THR A C   1 
ATOM   896  O O   . THR A 1 117 ? 7.02815  21.91935 -0.70507  1.000 70.52955  ? 117 THR A O   1 
ATOM   897  C CB  . THR A 1 117 ? 8.39844  23.56171 -3.11201  1.000 72.49838  ? 117 THR A CB  1 
ATOM   898  O OG1 . THR A 1 117 ? 7.72503  24.40916 -2.17579  1.000 74.28121  ? 117 THR A OG1 1 
ATOM   899  C CG2 . THR A 1 117 ? 8.11292  24.05690 -4.52020  1.000 74.78380  ? 117 THR A CG2 1 
ATOM   900  N N   . TYR A 1 118 ? 9.12726  21.17709 -1.06759  1.000 65.01872  ? 118 TYR A N   1 
ATOM   901  C CA  . TYR A 1 118 ? 9.35792  20.74635 0.30203   1.000 62.87593  ? 118 TYR A CA  1 
ATOM   902  C C   . TYR A 1 118 ? 10.72375 21.21692 0.77679   1.000 60.70549  ? 118 TYR A C   1 
ATOM   903  O O   . TYR A 1 118 ? 11.65951 21.39073 -0.00774  1.000 59.63791  ? 118 TYR A O   1 
ATOM   904  C CB  . TYR A 1 118 ? 9.27682  19.21953 0.44700   1.000 61.30132  ? 118 TYR A CB  1 
ATOM   905  C CG  . TYR A 1 118 ? 7.98555  18.63192 -0.05429  1.000 62.96273  ? 118 TYR A CG  1 
ATOM   906  C CD1 . TYR A 1 118 ? 7.86955  18.18320 -1.36282  1.000 63.35263  ? 118 TYR A CD1 1 
ATOM   907  C CD2 . TYR A 1 118 ? 6.88253  18.52500 0.77790   1.000 64.36999  ? 118 TYR A CD2 1 
ATOM   908  C CE1 . TYR A 1 118 ? 6.68977  17.64572 -1.82802  1.000 65.23741  ? 118 TYR A CE1 1 
ATOM   909  C CE2 . TYR A 1 118 ? 5.69605  17.99033 0.32154   1.000 66.29689  ? 118 TYR A CE2 1 
ATOM   910  C CZ  . TYR A 1 118 ? 5.60521  17.55152 -0.98140  1.000 66.79122  ? 118 TYR A CZ  1 
ATOM   911  O OH  . TYR A 1 118 ? 4.42590  17.01541 -1.44294  1.000 69.20854  ? 118 TYR A OH  1 
ATOM   912  N N   . LEU A 1 119 ? 10.82794 21.40089 2.08817   1.000 60.18741  ? 119 LEU A N   1 
ATOM   913  C CA  . LEU A 1 119 ? 12.07352 21.77173 2.74021   1.000 58.30592  ? 119 LEU A CA  1 
ATOM   914  C C   . LEU A 1 119 ? 12.48241 20.64188 3.66984   1.000 56.08985  ? 119 LEU A C   1 
ATOM   915  O O   . LEU A 1 119 ? 11.67483 20.18677 4.48690   1.000 56.70175  ? 119 LEU A O   1 
ATOM   916  C CB  . LEU A 1 119 ? 11.91507 23.07653 3.52107   1.000 60.19933  ? 119 LEU A CB  1 
ATOM   917  C CG  . LEU A 1 119 ? 13.13752 23.98894 3.52889   1.000 60.05719  ? 119 LEU A CG  1 
ATOM   918  C CD1 . LEU A 1 119 ? 13.60889 24.24875 2.10882   1.000 60.07187  ? 119 LEU A CD1 1 
ATOM   919  C CD2 . LEU A 1 119 ? 12.79926 25.29317 4.22314   1.000 61.98865  ? 119 LEU A CD2 1 
ATOM   920  N N   . ALA A 1 120 ? 13.72460 20.18740 3.54464   1.000 53.73071  ? 120 ALA A N   1 
ATOM   921  C CA  . ALA A 1 120 ? 14.23323 19.09230 4.35467   1.000 53.04681  ? 120 ALA A CA  1 
ATOM   922  C C   . ALA A 1 120 ? 15.41224 19.56438 5.19084   1.000 53.35481  ? 120 ALA A C   1 
ATOM   923  O O   . ALA A 1 120 ? 16.22377 20.37877 4.73460   1.000 54.58470  ? 120 ALA A O   1 
ATOM   924  C CB  . ALA A 1 120 ? 14.66466 17.90268 3.49108   1.000 51.99255  ? 120 ALA A CB  1 
ATOM   925  N N   . LEU A 1 121 ? 15.49405 19.04596 6.41734   1.000 52.18262  ? 121 LEU A N   1 
ATOM   926  C CA  . LEU A 1 121 ? 16.65172 19.23200 7.28259   1.000 51.51896  ? 121 LEU A CA  1 
ATOM   927  C C   . LEU A 1 121 ? 17.63782 18.07434 7.20529   1.000 50.00410  ? 121 LEU A C   1 
ATOM   928  O O   . LEU A 1 121 ? 18.84882 18.29573 7.32221   1.000 49.44987  ? 121 LEU A O   1 
ATOM   929  C CB  . LEU A 1 121 ? 16.20555 19.41652 8.73971   1.000 52.01503  ? 121 LEU A CB  1 
ATOM   930  C CG  . LEU A 1 121 ? 17.30521 19.61538 9.78939   1.000 51.83151  ? 121 LEU A CG  1 
ATOM   931  C CD1 . LEU A 1 121 ? 18.18742 20.80185 9.43136   1.000 51.90378  ? 121 LEU A CD1 1 
ATOM   932  C CD2 . LEU A 1 121 ? 16.70621 19.78764 11.18754  1.000 52.98632  ? 121 LEU A CD2 1 
ATOM   933  N N   . ASN A 1 122 ? 17.15557 16.84864 6.99419   1.000 49.48311  ? 122 ASN A N   1 
ATOM   934  C CA  . ASN A 1 122 ? 18.04961 15.70704 6.85078   1.000 48.10167  ? 122 ASN A CA  1 
ATOM   935  C C   . ASN A 1 122 ? 18.26499 15.35483 5.38515   1.000 47.86786  ? 122 ASN A C   1 
ATOM   936  O O   . ASN A 1 122 ? 19.38102 15.49753 4.87469   1.000 47.93906  ? 122 ASN A O   1 
ATOM   937  C CB  . ASN A 1 122 ? 17.50765 14.50059 7.61399   1.000 48.01263  ? 122 ASN A CB  1 
ATOM   938  C CG  . ASN A 1 122 ? 17.99925 14.44729 9.04902   1.000 47.77791  ? 122 ASN A CG  1 
ATOM   939  O OD1 . ASN A 1 122 ? 18.80628 15.27309 9.47938   1.000 47.52453  ? 122 ASN A OD1 1 
ATOM   940  N ND2 . ASN A 1 122 ? 17.50912 13.47149 9.79726   1.000 48.06216  ? 122 ASN A ND2 1 
ATOM   941  N N   . GLU A 1 123 ? 17.21121 14.91581 4.69595   1.000 47.29604  ? 123 GLU A N   1 
ATOM   942  C CA  . GLU A 1 123 ? 17.36035 14.44271 3.32556   1.000 46.73718  ? 123 GLU A CA  1 
ATOM   943  C C   . GLU A 1 123 ? 15.98994 14.26422 2.68367   1.000 48.42302  ? 123 GLU A C   1 
ATOM   944  O O   . GLU A 1 123 ? 14.96212 14.20299 3.36497   1.000 49.29680  ? 123 GLU A O   1 
ATOM   945  C CB  . GLU A 1 123 ? 18.14264 13.12568 3.26808   1.000 45.51953  ? 123 GLU A CB  1 
ATOM   946  C CG  . GLU A 1 123 ? 17.34745 11.90826 3.69137   1.000 45.65265  ? 123 GLU A CG  1 
ATOM   947  C CD  . GLU A 1 123 ? 17.02530 11.90323 5.17025   1.000 45.55347  ? 123 GLU A CD  1 
ATOM   948  O OE1 . GLU A 1 123 ? 17.96723 11.91131 5.99122   1.000 45.16831  ? 123 GLU A OE1 1 
ATOM   949  O OE2 . GLU A 1 123 ? 15.82752 11.90597 5.51409   1.000 45.86067  ? 123 GLU A OE2 1 
ATOM   950  N N   . SER A 1 124 ? 15.99890 14.18495 1.35350   1.000 49.15067  ? 124 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 14.82974 13.86692 0.54220   1.000 50.39567  ? 124 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 15.13295 12.61231 -0.26911  1.000 49.17702  ? 124 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 16.16790 12.54036 -0.93567  1.000 48.34111  ? 124 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 14.47382 15.03525 -0.38024  1.000 52.10795  ? 124 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 13.31498 14.75570 -1.14377  1.000 53.69041  ? 124 SER A OG  1 
ATOM   956  N N   . THR A 1 125 ? 14.23483 11.63013 -0.21259  1.000 50.05289  ? 125 THR A N   1 
ATOM   957  C CA  . THR A 1 125 ? 14.46178 10.29813 -0.76132  1.000 49.57690  ? 125 THR A CA  1 
ATOM   958  C C   . THR A 1 125 ? 13.37300 9.95172  -1.77077  1.000 51.24512  ? 125 THR A C   1 
ATOM   959  O O   . THR A 1 125 ? 12.20626 10.30320 -1.57735  1.000 52.94783  ? 125 THR A O   1 
ATOM   960  C CB  . THR A 1 125 ? 14.48904 9.25796  0.37985   1.000 49.79018  ? 125 THR A CB  1 
ATOM   961  O OG1 . THR A 1 125 ? 15.82283 9.13863  0.89404   1.000 49.50928  ? 125 THR A OG1 1 
ATOM   962  C CG2 . THR A 1 125 ? 13.99482 7.89030  -0.06943  1.000 49.78980  ? 125 THR A CG2 1 
ATOM   963  N N   . VAL A 1 126 ? 13.75774 9.25870  -2.84549  1.000 50.78607  ? 126 VAL A N   1 
ATOM   964  C CA  . VAL A 1 126 ? 12.82834 8.75244  -3.84968  1.000 53.32574  ? 126 VAL A CA  1 
ATOM   965  C C   . VAL A 1 126 ? 13.00688 7.24683  -3.98182  1.000 54.04907  ? 126 VAL A C   1 
ATOM   966  O O   . VAL A 1 126 ? 14.13478 6.75266  -4.05463  1.000 53.41607  ? 126 VAL A O   1 
ATOM   967  C CB  . VAL A 1 126 ? 13.03418 9.42153  -5.22490  1.000 54.82475  ? 126 VAL A CB  1 
ATOM   968  C CG1 . VAL A 1 126 ? 11.75619 9.33716  -6.04939  1.000 57.49530  ? 126 VAL A CG1 1 
ATOM   969  C CG2 . VAL A 1 126 ? 13.49820 10.84965 -5.06859  1.000 55.07128  ? 126 VAL A CG2 1 
ATOM   970  N N   . LYS A 1 127 ? 11.89194 6.52366  -4.04379  1.000 56.94087  ? 127 LYS A N   1 
ATOM   971  C CA  . LYS A 1 127 ? 11.88798 5.09441  -4.32474  1.000 58.28147  ? 127 LYS A CA  1 
ATOM   972  C C   . LYS A 1 127 ? 10.74695 4.80478  -5.28960  1.000 62.10470  ? 127 LYS A C   1 
ATOM   973  O O   . LYS A 1 127 ? 9.92309  5.67460  -5.58261  1.000 62.34226  ? 127 LYS A O   1 
ATOM   974  C CB  . LYS A 1 127 ? 11.74567 4.26092  -3.04128  0.900 57.18422  ? 127 LYS A CB  1 
ATOM   975  C CG  . LYS A 1 127 ? 12.82428 4.53764  -2.00335  0.800 54.32747  ? 127 LYS A CG  1 
ATOM   976  C CD  . LYS A 1 127 ? 12.56802 3.82295  -0.68440  0.800 54.28684  ? 127 LYS A CD  1 
ATOM   977  C CE  . LYS A 1 127 ? 13.66279 4.16355  0.32616   0.700 53.07710  ? 127 LYS A CE  1 
ATOM   978  N NZ  . LYS A 1 127 ? 13.43532 3.58503  1.68705   0.700 53.92789  ? 127 LYS A NZ  1 
ATOM   979  N N   . SER A 1 128 ? 10.69562 3.57332  -5.79075  1.000 65.78242  ? 128 SER A N   1 
ATOM   980  C CA  . SER A 1 128 ? 9.60331  3.19304  -6.67599  1.000 71.03641  ? 128 SER A CA  1 
ATOM   981  C C   . SER A 1 128 ? 8.37937  2.78283  -5.87053  1.000 78.77081  ? 128 SER A C   1 
ATOM   982  O O   . SER A 1 128 ? 8.48248  2.32502  -4.72893  1.000 78.74813  ? 128 SER A O   1 
ATOM   983  C CB  A SER A 1 128 ? 10.01508 2.04387  -7.59749  0.610 71.31824  ? 128 SER A CB  1 
ATOM   984  C CB  B SER A 1 128 ? 10.02097 2.04786  -7.60074  0.390 71.30983  ? 128 SER A CB  1 
ATOM   985  O OG  A SER A 1 128 ? 9.97215  0.80183  -6.91506  0.610 71.63983  ? 128 SER A OG  1 
ATOM   986  O OG  B SER A 1 128 ? 8.95333  1.65590  -8.44769  0.390 73.66857  ? 128 SER A OG  1 
ATOM   987  N N   . SER A 1 129 ? 7.20982  2.94848  -6.48581  1.000 86.01836  ? 129 SER A N   1 
ATOM   988  C CA  . SER A 1 129 ? 5.93437  2.54439  -5.91041  1.000 96.33847  ? 129 SER A CA  1 
ATOM   989  C C   . SER A 1 129 ? 5.69145  1.04789  -6.00661  1.000 102.72841 ? 129 SER A C   1 
ATOM   990  O O   . SER A 1 129 ? 4.53840  0.61242  -5.93518  1.000 107.95335 ? 129 SER A O   1 
ATOM   991  C CB  . SER A 1 129 ? 4.79566  3.28727  -6.60533  1.000 100.29722 ? 129 SER A CB  1 
ATOM   992  O OG  . SER A 1 129 ? 4.78368  2.96807  -7.98651  1.000 103.42259 ? 129 SER A OG  1 
ATOM   993  N N   . GLY A 1 130 ? 6.74098  0.25228  -6.16965  0.970 104.94418 ? 130 GLY A N   1 
ATOM   994  C CA  . GLY A 1 130 ? 6.57840  -1.15965 -6.43902  0.970 106.89105 ? 130 GLY A CA  1 
ATOM   995  C C   . GLY A 1 130 ? 7.21534  -1.53657 -7.75759  0.970 106.58879 ? 130 GLY A C   1 
ATOM   996  O O   . GLY A 1 130 ? 6.84307  -1.00921 -8.81077  0.970 107.70696 ? 130 GLY A O   1 
ATOM   997  N N   . GLY A 1 131 ? 8.18563  -2.44150 -7.71101  1.000 100.80844 ? 131 GLY A N   1 
ATOM   998  C CA  . GLY A 1 131 ? 8.92211  -2.81514 -8.89059  1.000 94.48592  ? 131 GLY A CA  1 
ATOM   999  C C   . GLY A 1 131 ? 10.17529 -1.98230 -9.05505  1.000 87.61434  ? 131 GLY A C   1 
ATOM   1000 O O   . GLY A 1 131 ? 10.69764 -1.40456 -8.09641  1.000 86.09703  ? 131 GLY A O   1 
ATOM   1001 N N   . PRO A 1 132 ? 10.67757 -1.89784 -10.28420 0.980 85.17553  ? 132 PRO A N   1 
ATOM   1002 C CA  . PRO A 1 132 ? 11.95939 -1.22297 -10.51674 0.980 80.88701  ? 132 PRO A CA  1 
ATOM   1003 C C   . PRO A 1 132 ? 11.84876 0.29407  -10.47440 0.980 74.84853  ? 132 PRO A C   1 
ATOM   1004 O O   . PRO A 1 132 ? 10.89652 0.88994  -10.98501 0.980 75.78337  ? 132 PRO A O   1 
ATOM   1005 C CB  . PRO A 1 132 ? 12.35530 -1.70891 -11.91607 0.980 82.58165  ? 132 PRO A CB  1 
ATOM   1006 C CG  . PRO A 1 132 ? 11.05654 -1.98144 -12.58030 0.980 85.94654  ? 132 PRO A CG  1 
ATOM   1007 C CD  . PRO A 1 132 ? 10.14496 -2.51338 -11.51099 0.980 87.78222  ? 132 PRO A CD  1 
ATOM   1008 N N   . PHE A 1 133 ? 12.85070 0.91519  -9.85629  1.000 68.68248  ? 133 PHE A N   1 
ATOM   1009 C CA  . PHE A 1 133 ? 13.00393 2.36612  -9.83932  1.000 62.76550  ? 133 PHE A CA  1 
ATOM   1010 C C   . PHE A 1 133 ? 14.00176 2.74310  -10.92613 1.000 58.62881  ? 133 PHE A C   1 
ATOM   1011 O O   . PHE A 1 133 ? 15.17871 2.37515  -10.85092 1.000 56.51482  ? 133 PHE A O   1 
ATOM   1012 C CB  . PHE A 1 133 ? 13.47222 2.84628  -8.46831  1.000 59.63226  ? 133 PHE A CB  1 
ATOM   1013 C CG  . PHE A 1 133 ? 13.79619 4.31682  -8.40363  1.000 57.01156  ? 133 PHE A CG  1 
ATOM   1014 C CD1 . PHE A 1 133 ? 12.78909 5.26143  -8.28050  1.000 57.14184  ? 133 PHE A CD1 1 
ATOM   1015 C CD2 . PHE A 1 133 ? 15.11316 4.75049  -8.42755  1.000 55.01261  ? 133 PHE A CD2 1 
ATOM   1016 C CE1 . PHE A 1 133 ? 13.08936 6.61292  -8.19995  1.000 56.51619  ? 133 PHE A CE1 1 
ATOM   1017 C CE2 . PHE A 1 133 ? 15.41945 6.09839  -8.34941  1.000 54.40166  ? 133 PHE A CE2 1 
ATOM   1018 C CZ  . PHE A 1 133 ? 14.40609 7.03024  -8.23214  1.000 55.29363  ? 133 PHE A CZ  1 
ATOM   1019 N N   . VAL A 1 134 ? 13.52612 3.45944  -11.94249 1.000 57.51612  ? 134 VAL A N   1 
ATOM   1020 C CA  . VAL A 1 134 ? 14.34713 3.88452  -13.07041 1.000 56.14198  ? 134 VAL A CA  1 
ATOM   1021 C C   . VAL A 1 134 ? 14.10949 5.36826  -13.28425 1.000 55.94526  ? 134 VAL A C   1 
ATOM   1022 O O   . VAL A 1 134 ? 12.99238 5.77533  -13.62064 1.000 58.67397  ? 134 VAL A O   1 
ATOM   1023 C CB  . VAL A 1 134 ? 14.01848 3.11635  -14.36256 1.000 57.81622  ? 134 VAL A CB  1 
ATOM   1024 C CG1 . VAL A 1 134 ? 15.02056 3.48035  -15.45398 1.000 57.70482  ? 134 VAL A CG1 1 
ATOM   1025 C CG2 . VAL A 1 134 ? 13.98869 1.61743  -14.11770 1.000 58.21563  ? 134 VAL A CG2 1 
ATOM   1026 N N   . VAL A 1 135 ? 15.15036 6.17590  -13.11543 1.000 52.88157  ? 135 VAL A N   1 
ATOM   1027 C CA  . VAL A 1 135 ? 15.05497 7.59310  -13.43698 1.000 52.65486  ? 135 VAL A CA  1 
ATOM   1028 C C   . VAL A 1 135 ? 16.27814 7.99890  -14.24272 1.000 52.50789  ? 135 VAL A C   1 
ATOM   1029 O O   . VAL A 1 135 ? 17.35838 7.41845  -14.10137 1.000 51.61169  ? 135 VAL A O   1 
ATOM   1030 C CB  . VAL A 1 135 ? 14.91396 8.47938  -12.17680 1.000 50.99166  ? 135 VAL A CB  1 
ATOM   1031 C CG1 . VAL A 1 135 ? 13.61418 8.16607  -11.45186 1.000 51.59074  ? 135 VAL A CG1 1 
ATOM   1032 C CG2 . VAL A 1 135 ? 16.10803 8.29989  -11.25433 1.000 48.65449  ? 135 VAL A CG2 1 
ATOM   1033 N N   . ASP A 1 136 ? 16.08771 8.98535  -15.11649 1.000 54.03435  ? 136 ASP A N   1 
ATOM   1034 C CA  . ASP A 1 136 ? 17.18893 9.68290  -15.76578 1.000 54.33475  ? 136 ASP A CA  1 
ATOM   1035 C C   . ASP A 1 136 ? 17.62196 10.82462 -14.85798 1.000 53.27296  ? 136 ASP A C   1 
ATOM   1036 O O   . ASP A 1 136 ? 16.79651 11.65692 -14.46815 1.000 53.59197  ? 136 ASP A O   1 
ATOM   1037 C CB  . ASP A 1 136 ? 16.77291 10.22810 -17.13117 1.000 56.72021  ? 136 ASP A CB  1 
ATOM   1038 C CG  . ASP A 1 136 ? 16.78335 9.17410  -18.21358 1.000 57.49291  ? 136 ASP A CG  1 
ATOM   1039 O OD1 . ASP A 1 136 ? 17.78643 8.44161  -18.33310 0.690 56.64343  ? 136 ASP A OD1 1 
ATOM   1040 O OD2 . ASP A 1 136 ? 15.78453 9.08799  -18.95367 1.000 59.50991  ? 136 ASP A OD2 1 
ATOM   1041 N N   . VAL A 1 137 ? 18.90484 10.86860 -14.52140 1.000 52.07270  ? 137 VAL A N   1 
ATOM   1042 C CA  . VAL A 1 137 ? 19.43732 11.92620 -13.66939 1.000 51.35423  ? 137 VAL A CA  1 
ATOM   1043 C C   . VAL A 1 137 ? 20.01623 13.01700 -14.56173 1.000 52.83773  ? 137 VAL A C   1 
ATOM   1044 O O   . VAL A 1 137 ? 20.83753 12.73976 -15.44309 1.000 54.01730  ? 137 VAL A O   1 
ATOM   1045 C CB  . VAL A 1 137 ? 20.48795 11.38039 -12.69083 1.000 49.61991  ? 137 VAL A CB  1 
ATOM   1046 C CG1 . VAL A 1 137 ? 21.07968 12.50674 -11.87117 1.000 49.26038  ? 137 VAL A CG1 1 
ATOM   1047 C CG2 . VAL A 1 137 ? 19.85353 10.33526 -11.77646 1.000 47.95082  ? 137 VAL A CG2 1 
ATOM   1048 N N   . VAL A 1 138 ? 19.56711 14.25315 -14.34550 1.000 53.51622  ? 138 VAL A N   1 
ATOM   1049 C CA  . VAL A 1 138 ? 19.95087 15.41086 -15.14588 1.000 55.45892  ? 138 VAL A CA  1 
ATOM   1050 C C   . VAL A 1 138 ? 20.54865 16.45178 -14.20794 1.000 55.36924  ? 138 VAL A C   1 
ATOM   1051 O O   . VAL A 1 138 ? 19.94523 16.78385 -13.18186 1.000 54.59874  ? 138 VAL A O   1 
ATOM   1052 C CB  . VAL A 1 138 ? 18.74644 15.99102 -15.91244 1.000 57.45024  ? 138 VAL A CB  1 
ATOM   1053 C CG1 . VAL A 1 138 ? 19.16399 17.18363 -16.73753 1.000 59.46129  ? 138 VAL A CG1 1 
ATOM   1054 C CG2 . VAL A 1 138 ? 18.10448 14.93214 -16.79248 1.000 58.07362  ? 138 VAL A CG2 1 
ATOM   1055 N N   . ILE A 1 139 ? 21.72467 16.96752 -14.55990 1.000 56.02754  ? 139 ILE A N   1 
ATOM   1056 C CA  . ILE A 1 139 ? 22.45501 17.92629 -13.73650 1.000 55.39732  ? 139 ILE A CA  1 
ATOM   1057 C C   . ILE A 1 139 ? 22.63913 19.19960 -14.54871 1.000 58.06625  ? 139 ILE A C   1 
ATOM   1058 O O   . ILE A 1 139 ? 23.38231 19.20672 -15.53481 1.000 60.19172  ? 139 ILE A O   1 
ATOM   1059 C CB  . ILE A 1 139 ? 23.81278 17.37675 -13.28102 1.000 54.20491  ? 139 ILE A CB  1 
ATOM   1060 C CG1 . ILE A 1 139 ? 23.64064 16.04490 -12.54676 1.000 51.68911  ? 139 ILE A CG1 1 
ATOM   1061 C CG2 . ILE A 1 139 ? 24.50902 18.38539 -12.38294 1.000 54.60401  ? 139 ILE A CG2 1 
ATOM   1062 C CD1 . ILE A 1 139 ? 24.95033 15.35169 -12.23042 1.000 50.39081  ? 139 ILE A CD1 1 
ATOM   1063 N N   . ASN A 1 140 ? 21.99024 20.28160 -14.12559 1.000 58.49492  ? 140 ASN A N   1 
ATOM   1064 C CA  . ASN A 1 140 ? 22.06658 21.56372 -14.82664 1.000 62.29776  ? 140 ASN A CA  1 
ATOM   1065 C C   . ASN A 1 140 ? 21.73091 21.38677 -16.30911 1.000 65.73343  ? 140 ASN A C   1 
ATOM   1066 O O   . ASN A 1 140 ? 22.44960 21.84670 -17.19829 1.000 67.85353  ? 140 ASN A O   1 
ATOM   1067 C CB  . ASN A 1 140 ? 23.44180 22.21527 -14.63944 1.000 62.88548  ? 140 ASN A CB  1 
ATOM   1068 C CG  . ASN A 1 140 ? 23.77350 22.48056 -13.17502 1.000 62.55380  ? 140 ASN A CG  1 
ATOM   1069 O OD1 . ASN A 1 140 ? 22.88693 22.75596 -12.35735 1.000 62.06296  ? 140 ASN A OD1 1 
ATOM   1070 N ND2 . ASN A 1 140 ? 25.05662 22.39583 -12.83610 1.000 62.57598  ? 140 ASN A ND2 1 
ATOM   1071 N N   . ASP A 1 141 ? 20.62527 20.68347 -16.56039 1.000 67.06699  ? 141 ASP A N   1 
ATOM   1072 C CA  . ASP A 1 141 ? 20.10148 20.38599 -17.89593 1.000 70.99533  ? 141 ASP A CA  1 
ATOM   1073 C C   . ASP A 1 141 ? 21.04667 19.51576 -18.72310 1.000 72.52552  ? 141 ASP A C   1 
ATOM   1074 O O   . ASP A 1 141 ? 21.00177 19.54788 -19.95442 1.000 74.61666  ? 141 ASP A O   1 
ATOM   1075 C CB  . ASP A 1 141 ? 19.75196 21.66829 -18.66063 1.000 73.54538  ? 141 ASP A CB  1 
ATOM   1076 C CG  . ASP A 1 141 ? 18.70233 22.49770 -17.94864 0.560 73.27797  ? 141 ASP A CG  1 
ATOM   1077 O OD1 . ASP A 1 141 ? 17.84250 21.90733 -17.25885 0.770 71.13325  ? 141 ASP A OD1 1 
ATOM   1078 O OD2 . ASP A 1 141 ? 18.74027 23.73926 -18.07513 0.270 75.44671  ? 141 ASP A OD2 1 
ATOM   1079 N N   . ILE A 1 142 ? 21.89045 18.72203 -18.06719 1.000 72.31770  ? 142 ILE A N   1 
ATOM   1080 C CA  A ILE A 1 142 ? 22.83715 17.83494 -18.73413 0.360 72.47911  ? 142 ILE A CA  1 
ATOM   1081 C CA  B ILE A 1 142 ? 22.83924 17.83495 -18.73249 0.640 72.49031  ? 142 ILE A CA  1 
ATOM   1082 C C   . ILE A 1 142 ? 22.51135 16.40733 -18.31739 1.000 70.08349  ? 142 ILE A C   1 
ATOM   1083 O O   . ILE A 1 142 ? 22.57062 16.07658 -17.12693 1.000 68.05305  ? 142 ILE A O   1 
ATOM   1084 C CB  A ILE A 1 142 ? 24.29163 18.19010 -18.38551 0.360 73.54558  ? 142 ILE A CB  1 
ATOM   1085 C CB  B ILE A 1 142 ? 24.29242 18.18888 -18.37628 0.640 73.38353  ? 142 ILE A CB  1 
ATOM   1086 C CG1 A ILE A 1 142 ? 24.62146 19.61153 -18.85129 0.360 75.73023  ? 142 ILE A CG1 1 
ATOM   1087 C CG1 B ILE A 1 142 ? 24.64780 19.58413 -18.89944 0.640 75.84146  ? 142 ILE A CG1 1 
ATOM   1088 C CG2 A ILE A 1 142 ? 25.25421 17.17273 -18.98000 0.360 72.50107  ? 142 ILE A CG2 1 
ATOM   1089 C CG2 B ILE A 1 142 ? 25.25432 17.13537 -18.91127 0.640 72.35732  ? 142 ILE A CG2 1 
ATOM   1090 C CD1 A ILE A 1 142 ? 24.35296 19.85239 -20.31708 0.360 78.53610  ? 142 ILE A CD1 1 
ATOM   1091 C CD1 B ILE A 1 142 ? 25.99103 20.08983 -18.41684 0.640 77.59040  ? 142 ILE A CD1 1 
ATOM   1092 N N   . HIS A 1 143 ? 22.16635 15.56197 -19.29204 1.000 67.90900  ? 143 HIS A N   1 
ATOM   1093 C CA  . HIS A 1 143 ? 21.84792 14.17884 -18.95437 1.000 64.13829  ? 143 HIS A CA  1 
ATOM   1094 C C   . HIS A 1 143 ? 23.09803 13.46170 -18.46550 1.000 59.52327  ? 143 HIS A C   1 
ATOM   1095 O O   . HIS A 1 143 ? 24.05063 13.26454 -19.22713 1.000 61.33090  ? 143 HIS A O   1 
ATOM   1096 C CB  A HIS A 1 143 ? 21.25262 13.41289 -20.13026 0.600 64.74425  ? 143 HIS A CB  1 
ATOM   1097 C CB  B HIS A 1 143 ? 21.24280 13.46773 -20.16373 0.400 64.86371  ? 143 HIS A CB  1 
ATOM   1098 C CG  A HIS A 1 143 ? 20.99582 11.97193 -19.80634 0.600 64.85127  ? 143 HIS A CG  1 
ATOM   1099 C CG  B HIS A 1 143 ? 19.82107 13.85118 -20.43825 0.400 68.14287  ? 143 HIS A CG  1 
ATOM   1100 N ND1 A HIS A 1 143 ? 21.98254 11.01000 -19.85806 0.600 63.44287  ? 143 HIS A ND1 1 
ATOM   1101 N ND1 B HIS A 1 143 ? 18.76756 12.98104 -20.25744 0.400 66.71391  ? 143 HIS A ND1 1 
ATOM   1102 C CD2 A HIS A 1 143 ? 19.88129 11.34203 -19.36305 0.600 63.89497  ? 143 HIS A CD2 1 
ATOM   1103 C CD2 B HIS A 1 143 ? 19.27766 15.01597 -20.86435 0.400 69.65379  ? 143 HIS A CD2 1 
ATOM   1104 C CE1 A HIS A 1 143 ? 21.47952 9.84471  -19.49090 0.600 62.72794  ? 143 HIS A CE1 1 
ATOM   1105 C CE1 B HIS A 1 143 ? 17.63763 13.59060 -20.56816 0.400 69.28192  ? 143 HIS A CE1 1 
ATOM   1106 N NE2 A HIS A 1 143 ? 20.20647 10.01887 -19.18396 0.600 62.40795  ? 143 HIS A NE2 1 
ATOM   1107 N NE2 B HIS A 1 143 ? 17.91930 14.82643 -20.93909 0.400 70.44356  ? 143 HIS A NE2 1 
ATOM   1108 N N   . PHE A 1 144 ? 23.07688 13.04216 -17.20252 1.000 54.35732  ? 144 PHE A N   1 
ATOM   1109 C CA  . PHE A 1 144 ? 24.24494 12.47264 -16.54557 1.000 50.69563  ? 144 PHE A CA  1 
ATOM   1110 C C   . PHE A 1 144 ? 24.26723 10.95079 -16.54216 1.000 47.30067  ? 144 PHE A C   1 
ATOM   1111 O O   . PHE A 1 144 ? 25.33083 10.35796 -16.72850 1.000 47.09108  ? 144 PHE A O   1 
ATOM   1112 C CB  . PHE A 1 144 ? 24.33106 12.97842 -15.10181 1.000 49.77984  ? 144 PHE A CB  1 
ATOM   1113 C CG  . PHE A 1 144 ? 25.51707 12.46012 -14.35631 1.000 48.91500  ? 144 PHE A CG  1 
ATOM   1114 C CD1 . PHE A 1 144 ? 26.78780 12.92172 -14.65590 1.000 50.14746  ? 144 PHE A CD1 1 
ATOM   1115 C CD2 . PHE A 1 144 ? 25.36785 11.51262 -13.35932 1.000 47.11676  ? 144 PHE A CD2 1 
ATOM   1116 C CE1 . PHE A 1 144 ? 27.89313 12.45111 -13.96878 1.000 49.46877  ? 144 PHE A CE1 1 
ATOM   1117 C CE2 . PHE A 1 144 ? 26.47077 11.03980 -12.66764 1.000 46.49700  ? 144 PHE A CE2 1 
ATOM   1118 C CZ  . PHE A 1 144 ? 27.73574 11.51019 -12.97909 1.000 47.60313  ? 144 PHE A CZ  1 
ATOM   1119 N N   . GLU A 1 145 ? 23.13218 10.29937 -16.31558 1.000 45.46248  ? 145 GLU A N   1 
ATOM   1120 C CA  . GLU A 1 145 ? 23.11059 8.84869  -16.17930 1.000 44.83408  ? 145 GLU A CA  1 
ATOM   1121 C C   . GLU A 1 145 ? 21.65869 8.40685  -16.13154 1.000 44.44493  ? 145 GLU A C   1 
ATOM   1122 O O   . GLU A 1 145 ? 20.76976 9.19276  -15.79271 1.000 44.66838  ? 145 GLU A O   1 
ATOM   1123 C CB  . GLU A 1 145 ? 23.85393 8.37782  -14.91047 1.000 44.19555  ? 145 GLU A CB  1 
ATOM   1124 C CG  . GLU A 1 145 ? 23.10906 8.70329  -13.61174 1.000 43.32407  ? 145 GLU A CG  1 
ATOM   1125 C CD  . GLU A 1 145 ? 23.83386 8.26271  -12.32935 1.000 42.43248  ? 145 GLU A CD  1 
ATOM   1126 O OE1 . GLU A 1 145 ? 24.99360 7.78274  -12.39178 0.730 42.17884  ? 145 GLU A OE1 1 
ATOM   1127 O OE2 . GLU A 1 145 ? 23.22135 8.40878  -11.24714 0.620 36.55298  ? 145 GLU A OE2 1 
ATOM   1128 N N   . ARG A 1 146 ? 21.42695 7.13953  -16.46994 1.000 44.96309  ? 146 ARG A N   1 
ATOM   1129 C CA  . ARG A 1 146 ? 20.12921 6.49786  -16.27437 1.000 46.11910  ? 146 ARG A CA  1 
ATOM   1130 C C   . ARG A 1 146 ? 20.26696 5.53607  -15.09727 1.000 45.99516  ? 146 ARG A C   1 
ATOM   1131 O O   . ARG A 1 146 ? 20.97517 4.52735  -15.19360 1.000 45.56735  ? 146 ARG A O   1 
ATOM   1132 C CB  . ARG A 1 146 ? 19.65950 5.77705  -17.53500 1.000 47.50071  ? 146 ARG A CB  1 
ATOM   1133 C CG  . ARG A 1 146 ? 18.36577 4.99110  -17.33978 1.000 48.15929  ? 146 ARG A CG  1 
ATOM   1134 C CD  . ARG A 1 146 ? 17.64333 4.72251  -18.66051 1.000 50.30543  ? 146 ARG A CD  1 
ATOM   1135 N NE  . ARG A 1 146 ? 16.96097 5.90838  -19.16358 1.000 51.51003  ? 146 ARG A NE  1 
ATOM   1136 C CZ  . ARG A 1 146 ? 16.25256 5.95076  -20.28514 1.000 54.21622  ? 146 ARG A CZ  1 
ATOM   1137 N NH1 . ARG A 1 146 ? 16.11660 4.88471  -21.05828 1.000 55.62472  ? 146 ARG A NH1 1 
ATOM   1138 N NH2 . ARG A 1 146 ? 15.66464 7.09139  -20.63916 1.000 55.15293  ? 146 ARG A NH2 1 
ATOM   1139 N N   . PHE A 1 147 ? 19.59553 5.85582  -13.98821 1.000 46.36845  ? 147 PHE A N   1 
ATOM   1140 C CA  . PHE A 1 147 ? 19.72798 5.10521  -12.74407 1.000 46.25993  ? 147 PHE A CA  1 
ATOM   1141 C C   . PHE A 1 147 ? 18.66984 4.01455  -12.65376 1.000 47.67489  ? 147 PHE A C   1 
ATOM   1142 O O   . PHE A 1 147 ? 17.47168 4.29558  -12.74786 1.000 48.86667  ? 147 PHE A O   1 
ATOM   1143 C CB  . PHE A 1 147 ? 19.59933 6.03055  -11.53158 1.000 45.36581  ? 147 PHE A CB  1 
ATOM   1144 C CG  . PHE A 1 147 ? 19.77489 5.32375  -10.21151 1.000 44.40431  ? 147 PHE A CG  1 
ATOM   1145 C CD1 . PHE A 1 147 ? 18.70404 4.70577  -9.58046  1.000 44.76077  ? 147 PHE A CD1 1 
ATOM   1146 C CD2 . PHE A 1 147 ? 21.01139 5.27309  -9.60696  1.000 43.29063  ? 147 PHE A CD2 1 
ATOM   1147 C CE1 . PHE A 1 147 ? 18.87782 4.05342  -8.38060  1.000 43.98835  ? 147 PHE A CE1 1 
ATOM   1148 C CE2 . PHE A 1 147 ? 21.18478 4.62654  -8.40525  1.000 42.56917  ? 147 PHE A CE2 1 
ATOM   1149 C CZ  . PHE A 1 147 ? 20.12994 4.01669  -7.79473  1.000 42.87414  ? 147 PHE A CZ  1 
ATOM   1150 N N   . ARG A 1 148 ? 19.11311 2.78079  -12.42953 1.000 48.47274  ? 148 ARG A N   1 
ATOM   1151 C CA  . ARG A 1 148 ? 18.21830 1.67054  -12.13464 1.000 51.09323  ? 148 ARG A CA  1 
ATOM   1152 C C   . ARG A 1 148 ? 18.64605 1.03341  -10.82262 1.000 50.03521  ? 148 ARG A C   1 
ATOM   1153 O O   . ARG A 1 148 ? 19.75704 0.50123  -10.72138 1.000 49.44582  ? 148 ARG A O   1 
ATOM   1154 C CB  . ARG A 1 148 ? 18.22738 0.63663  -13.25704 1.000 54.45227  ? 148 ARG A CB  1 
ATOM   1155 C CG  . ARG A 1 148 ? 17.18368 -0.45142 -13.08447 0.900 57.05149  ? 148 ARG A CG  1 
ATOM   1156 C CD  . ARG A 1 148 ? 17.19284 -1.40540 -14.26279 0.800 59.58964  ? 148 ARG A CD  1 
ATOM   1157 N NE  . ARG A 1 148 ? 16.32551 -2.55208 -14.03358 0.800 61.55748  ? 148 ARG A NE  1 
ATOM   1158 C CZ  . ARG A 1 148 ? 15.07278 -2.63890 -14.45688 0.800 63.53336  ? 148 ARG A CZ  1 
ATOM   1159 N NH1 . ARG A 1 148 ? 14.51167 -1.66788 -15.15763 0.800 64.02975  ? 148 ARG A NH1 1 
ATOM   1160 N NH2 . ARG A 1 148 ? 14.36605 -3.72854 -14.17113 0.800 65.18773  ? 148 ARG A NH2 1 
ATOM   1161 N N   . GLY A 1 149 ? 17.76470 1.08189  -9.82617  1.000 50.71934  ? 149 GLY A N   1 
ATOM   1162 C CA  . GLY A 1 149 ? 18.06284 0.52421  -8.52131  1.000 49.98913  ? 149 GLY A CA  1 
ATOM   1163 C C   . GLY A 1 149 ? 16.90559 0.63720  -7.55373  1.000 49.32213  ? 149 GLY A C   1 
ATOM   1164 O O   . GLY A 1 149 ? 15.74299 0.61769  -7.97041  1.000 50.90123  ? 149 GLY A O   1 
ATOM   1165 N N   . ASP A 1 150 ? 17.21070 0.75344  -6.25891  1.000 47.07682  ? 150 ASP A N   1 
ATOM   1166 C CA  . ASP A 1 150 ? 16.17481 0.87681  -5.24021  1.000 46.22103  ? 150 ASP A CA  1 
ATOM   1167 C C   . ASP A 1 150 ? 15.75058 2.31426  -4.98956  1.000 45.91819  ? 150 ASP A C   1 
ATOM   1168 O O   . ASP A 1 150 ? 14.58844 2.54902  -4.64568  1.000 47.96336  ? 150 ASP A O   1 
ATOM   1169 C CB  . ASP A 1 150 ? 16.64561 0.25697  -3.92158  1.000 44.88936  ? 150 ASP A CB  1 
ATOM   1170 C CG  . ASP A 1 150 ? 16.67187 -1.24719 -3.96963  1.000 46.64148  ? 150 ASP A CG  1 
ATOM   1171 O OD1 . ASP A 1 150 ? 16.34035 -1.81208 -5.03358  1.000 48.23915  ? 150 ASP A OD1 1 
ATOM   1172 O OD2 . ASP A 1 150 ? 17.02469 -1.86557 -2.94785  1.000 46.94509  ? 150 ASP A OD2 1 
ATOM   1173 N N   . GLY A 1 151 ? 16.65433 3.27714  -5.13534  1.000 44.57232  ? 151 GLY A N   1 
ATOM   1174 C CA  . GLY A 1 151 ? 16.28146 4.66043  -4.93349  1.000 43.68519  ? 151 GLY A CA  1 
ATOM   1175 C C   . GLY A 1 151 ? 17.49345 5.56687  -4.85461  1.000 41.40616  ? 151 GLY A C   1 
ATOM   1176 O O   . GLY A 1 151 ? 18.62621 5.15824  -5.12278  1.000 40.83474  ? 151 GLY A O   1 
ATOM   1177 N N   . LEU A 1 152 ? 17.21877 6.81625  -4.48023  1.000 40.75288  ? 152 LEU A N   1 
ATOM   1178 C CA  . LEU A 1 152 ? 18.22103 7.86923  -4.38016  1.000 39.84131  ? 152 LEU A CA  1 
ATOM   1179 C C   . LEU A 1 152 ? 17.95872 8.71161  -3.13327  1.000 39.91169  ? 152 LEU A C   1 
ATOM   1180 O O   . LEU A 1 152 ? 16.82130 8.85432  -2.68324  1.000 40.31231  ? 152 LEU A O   1 
ATOM   1181 C CB  . LEU A 1 152 ? 18.21909 8.75821  -5.63969  1.000 40.10927  ? 152 LEU A CB  1 
ATOM   1182 C CG  . LEU A 1 152 ? 18.79929 8.14310  -6.92470  1.000 40.29974  ? 152 LEU A CG  1 
ATOM   1183 C CD1 . LEU A 1 152 ? 18.52774 9.00608  -8.15331  1.000 41.42879  ? 152 LEU A CD1 1 
ATOM   1184 C CD2 . LEU A 1 152 ? 20.29342 7.90364  -6.79378  1.000 38.75120  ? 152 LEU A CD2 1 
ATOM   1185 N N   . CYS A 1 153 ? 19.02841 9.26767  -2.56744  1.000 40.29710  ? 153 CYS A N   1 
ATOM   1186 C CA  . CYS A 1 153 ? 18.93891 10.07293 -1.34992  1.000 40.41489  ? 153 CYS A CA  1 
ATOM   1187 C C   . CYS A 1 153 ? 19.69976 11.36970 -1.56083  1.000 40.80379  ? 153 CYS A C   1 
ATOM   1188 O O   . CYS A 1 153 ? 20.91312 11.34219 -1.77112  1.000 40.66008  ? 153 CYS A O   1 
ATOM   1189 C CB  . CYS A 1 153 ? 19.50928 9.32636  -0.13164  1.000 39.96368  ? 153 CYS A CB  1 
ATOM   1190 S SG  . CYS A 1 153 ? 19.64546 10.31863 1.42873   1.000 39.61927  ? 153 CYS A SG  1 
ATOM   1191 N N   . MET A 1 154 ? 19.00304 12.49999 -1.49378  1.000 42.35961  ? 154 MET A N   1 
ATOM   1192 C CA  . MET A 1 154 ? 19.65142 13.80576 -1.51654  1.000 44.12473  ? 154 MET A CA  1 
ATOM   1193 C C   . MET A 1 154 ? 19.67635 14.34283 -0.09430  1.000 44.65624  ? 154 MET A C   1 
ATOM   1194 O O   . MET A 1 154 ? 18.61924 14.54875 0.51337   1.000 44.67642  ? 154 MET A O   1 
ATOM   1195 C CB  . MET A 1 154 ? 18.94323 14.78858 -2.44730  1.000 45.48368  ? 154 MET A CB  1 
ATOM   1196 C CG  . MET A 1 154 ? 19.77093 16.05362 -2.71513  1.000 46.94689  ? 154 MET A CG  1 
ATOM   1197 S SD  . MET A 1 154 ? 21.25117 15.77230 -3.73230  1.000 47.37687  ? 154 MET A SD  1 
ATOM   1198 C CE  . MET A 1 154 ? 20.53665 15.82369 -5.37353  1.000 48.26951  ? 154 MET A CE  1 
ATOM   1199 N N   . SER A 1 155 ? 20.87994 14.56049 0.43007   1.000 45.35586  ? 155 SER A N   1 
ATOM   1200 C CA  . SER A 1 155 ? 21.09791 14.85795 1.84025   1.000 44.30624  ? 155 SER A CA  1 
ATOM   1201 C C   . SER A 1 155 ? 21.65482 16.26412 2.01041   1.000 44.72273  ? 155 SER A C   1 
ATOM   1202 O O   . SER A 1 155 ? 22.50812 16.70013 1.23409   1.000 45.55943  ? 155 SER A O   1 
ATOM   1203 C CB  . SER A 1 155 ? 22.06797 13.85221 2.46193   1.000 43.54263  ? 155 SER A CB  1 
ATOM   1204 O OG  . SER A 1 155 ? 22.53759 14.30290 3.72312   1.000 44.16540  ? 155 SER A OG  1 
ATOM   1205 N N   . THR A 1 156 ? 21.16263 16.96999 3.02546   1.000 43.18295  ? 156 THR A N   1 
ATOM   1206 C CA  . THR A 1 156 ? 21.74143 18.23059 3.45254   1.000 43.81044  ? 156 THR A CA  1 
ATOM   1207 C C   . THR A 1 156 ? 23.12085 17.97473 4.04960   1.000 43.26212  ? 156 THR A C   1 
ATOM   1208 O O   . THR A 1 156 ? 23.50526 16.82431 4.27130   1.000 42.99180  ? 156 THR A O   1 
ATOM   1209 C CB  . THR A 1 156 ? 20.83919 18.89780 4.48918   1.000 45.64255  ? 156 THR A CB  1 
ATOM   1210 O OG1 . THR A 1 156 ? 20.93247 18.17868 5.72808   1.000 45.79331  ? 156 THR A OG1 1 
ATOM   1211 C CG2 . THR A 1 156 ? 19.39719 18.91563 4.01345   1.000 46.40584  ? 156 THR A CG2 1 
ATOM   1212 N N   . PRO A 1 157 ? 23.90019 19.03369 4.32581   1.000 44.00935  ? 157 PRO A N   1 
ATOM   1213 C CA  . PRO A 1 157 ? 25.15204 18.83221 5.07065   1.000 44.58454  ? 157 PRO A CA  1 
ATOM   1214 C C   . PRO A 1 157 ? 24.92432 18.15695 6.41516   1.000 43.68880  ? 157 PRO A C   1 
ATOM   1215 O O   . PRO A 1 157 ? 25.54689 17.13063 6.70707   1.000 42.86547  ? 157 PRO A O   1 
ATOM   1216 C CB  . PRO A 1 157 ? 25.69531 20.25453 5.24769   1.000 46.43701  ? 157 PRO A CB  1 
ATOM   1217 C CG  . PRO A 1 157 ? 25.08091 21.03320 4.16260   1.000 46.93497  ? 157 PRO A CG  1 
ATOM   1218 C CD  . PRO A 1 157 ? 23.74191 20.43210 3.88517   1.000 45.40928  ? 157 PRO A CD  1 
ATOM   1219 N N   . SER A 1 158 ? 24.02588 18.70869 7.23639   1.000 44.16419  ? 158 SER A N   1 
ATOM   1220 C CA  . SER A 1 158 ? 23.80188 18.13209 8.55915   1.000 43.80508  ? 158 SER A CA  1 
ATOM   1221 C C   . SER A 1 158 ? 23.05071 16.81154 8.49070   1.000 42.08749  ? 158 SER A C   1 
ATOM   1222 O O   . SER A 1 158 ? 23.05722 16.05752 9.46722   1.000 41.43265  ? 158 SER A O   1 
ATOM   1223 C CB  . SER A 1 158 ? 23.05072 19.11608 9.46083   1.000 44.30005  ? 158 SER A CB  1 
ATOM   1224 O OG  . SER A 1 158 ? 21.73011 19.34282 8.99550   1.000 43.57559  ? 158 SER A OG  1 
ATOM   1225 N N   . GLY A 1 159 ? 22.40842 16.51265 7.36726   1.000 41.69762  ? 159 GLY A N   1 
ATOM   1226 C CA  . GLY A 1 159 ? 21.82436 15.20016 7.17671   1.000 40.18628  ? 159 GLY A CA  1 
ATOM   1227 C C   . GLY A 1 159 ? 22.81466 14.11101 6.83016   1.000 39.99144  ? 159 GLY A C   1 
ATOM   1228 O O   . GLY A 1 159 ? 22.45785 12.93196 6.90365   1.000 40.34579  ? 159 GLY A O   1 
ATOM   1229 N N   . THR A 1 160 ? 24.05581 14.46440 6.47323   1.000 39.03757  ? 160 THR A N   1 
ATOM   1230 C CA  . THR A 1 160 ? 24.99721 13.44139 6.03030   1.000 40.29027  ? 160 THR A CA  1 
ATOM   1231 C C   . THR A 1 160 ? 25.34844 12.44643 7.12711   1.000 41.85276  ? 160 THR A C   1 
ATOM   1232 O O   . THR A 1 160 ? 25.79450 11.33750 6.80975   1.000 41.88580  ? 160 THR A O   1 
ATOM   1233 C CB  . THR A 1 160 ? 26.28815 14.06319 5.47026   1.000 41.60620  ? 160 THR A CB  1 
ATOM   1234 O OG1 . THR A 1 160 ? 26.93705 14.87182 6.46120   1.000 42.41809  ? 160 THR A OG1 1 
ATOM   1235 C CG2 . THR A 1 160 ? 25.99502 14.89193 4.21189   1.000 41.99017  ? 160 THR A CG2 1 
ATOM   1236 N N   . THR A 1 161 ? 25.17162 12.80477 8.40170   1.000 43.46528  ? 161 THR A N   1 
ATOM   1237 C CA  . THR A 1 161 ? 25.39794 11.83083 9.46114   1.000 43.77949  ? 161 THR A CA  1 
ATOM   1238 C C   . THR A 1 161 ? 24.21389 10.88551 9.64887   1.000 42.93514  ? 161 THR A C   1 
ATOM   1239 O O   . THR A 1 161 ? 24.28483 9.98845  10.49563  1.000 43.28136  ? 161 THR A O   1 
ATOM   1240 C CB  . THR A 1 161 ? 25.73791 12.54429 10.77825  1.000 44.92118  ? 161 THR A CB  1 
ATOM   1241 O OG1 . THR A 1 161 ? 24.77547 13.56925 11.04289  1.000 44.53367  ? 161 THR A OG1 1 
ATOM   1242 C CG2 . THR A 1 161 ? 27.11647 13.18328 10.69769  1.000 45.82715  ? 161 THR A CG2 1 
ATOM   1243 N N   . ALA A 1 162 ? 23.14956 11.04025 8.85808   1.000 42.39179  ? 162 ALA A N   1 
ATOM   1244 C CA  . ALA A 1 162 ? 21.94897 10.21819 8.97692   1.000 42.77655  ? 162 ALA A CA  1 
ATOM   1245 C C   . ALA A 1 162 ? 21.87679 9.12829  7.91123   1.000 41.83022  ? 162 ALA A C   1 
ATOM   1246 O O   . ALA A 1 162 ? 22.81308 8.33715  7.75581   1.000 41.36852  ? 162 ALA A O   1 
ATOM   1247 C CB  . ALA A 1 162 ? 20.69963 11.09935 8.89354   1.000 43.29004  ? 162 ALA A CB  1 
ATOM   1248 N N   . TYR A 1 163 ? 20.75364 9.07939  7.18419   1.000 42.06967  ? 163 TYR A N   1 
ATOM   1249 C CA  . TYR A 1 163 ? 20.57771 8.09775  6.11266   1.000 42.09718  ? 163 TYR A CA  1 
ATOM   1250 C C   . TYR A 1 163 ? 21.74434 8.12695  5.13235   1.000 41.21332  ? 163 TYR A C   1 
ATOM   1251 O O   . TYR A 1 163 ? 22.26540 7.07546  4.73905   1.000 40.90850  ? 163 TYR A O   1 
ATOM   1252 C CB  . TYR A 1 163 ? 19.26255 8.37045  5.37851   1.000 42.42833  ? 163 TYR A CB  1 
ATOM   1253 C CG  . TYR A 1 163 ? 18.67287 7.19961  4.61939   1.000 42.81636  ? 163 TYR A CG  1 
ATOM   1254 C CD1 . TYR A 1 163 ? 19.29970 5.95925  4.59346   1.000 42.84336  ? 163 TYR A CD1 1 
ATOM   1255 C CD2 . TYR A 1 163 ? 17.47416 7.34471  3.92968   1.000 43.69963  ? 163 TYR A CD2 1 
ATOM   1256 C CE1 . TYR A 1 163 ? 18.74485 4.89356  3.89594   1.000 43.82630  ? 163 TYR A CE1 1 
ATOM   1257 C CE2 . TYR A 1 163 ? 16.90951 6.29150  3.22720   1.000 44.44961  ? 163 TYR A CE2 1 
ATOM   1258 C CZ  . TYR A 1 163 ? 17.54898 5.07034  3.20787   1.000 44.42041  ? 163 TYR A CZ  1 
ATOM   1259 O OH  . TYR A 1 163 ? 16.97319 4.03310  2.51040   1.000 44.72830  ? 163 TYR A OH  1 
ATOM   1260 N N   . ASN A 1 164 ? 22.16117 9.32678  4.72646   1.000 40.83459  ? 164 ASN A N   1 
ATOM   1261 C CA  . ASN A 1 164 ? 23.28521 9.47314  3.81080   1.000 40.82463  ? 164 ASN A CA  1 
ATOM   1262 C C   . ASN A 1 164 ? 24.48604 8.64373  4.24539   1.000 41.89712  ? 164 ASN A C   1 
ATOM   1263 O O   . ASN A 1 164 ? 25.13819 8.00370  3.41211   1.000 42.59509  ? 164 ASN A O   1 
ATOM   1264 C CB  . ASN A 1 164 ? 23.66166 10.95045 3.70445   1.000 40.99414  ? 164 ASN A CB  1 
ATOM   1265 C CG  . ASN A 1 164 ? 24.95616 11.17118 2.95577   1.000 41.80588  ? 164 ASN A CG  1 
ATOM   1266 O OD1 . ASN A 1 164 ? 24.95815 11.33219 1.73585   1.000 42.18650  ? 164 ASN A OD1 1 
ATOM   1267 N ND2 . ASN A 1 164 ? 26.06937 11.18917 3.68428   1.000 42.03211  ? 164 ASN A ND2 1 
ATOM   1268 N N   . LYS A 1 165 ? 24.79031 8.64044  5.54891   1.000 42.03306  ? 165 LYS A N   1 
ATOM   1269 C CA  . LYS A 1 165 ? 25.93938 7.89575  6.05412   1.000 42.40126  ? 165 LYS A CA  1 
ATOM   1270 C C   . LYS A 1 165 ? 25.76880 6.39673  5.84617   1.000 42.03800  ? 165 LYS A C   1 
ATOM   1271 O O   . LYS A 1 165 ? 26.71068 5.71352  5.42667   1.000 42.10073  ? 165 LYS A O   1 
ATOM   1272 C CB  . LYS A 1 165 ? 26.15427 8.20987  7.53830   1.000 43.85735  ? 165 LYS A CB  1 
ATOM   1273 C CG  . LYS A 1 165 ? 27.28861 7.42199  8.20812   1.000 45.28785  ? 165 LYS A CG  1 
ATOM   1274 C CD  . LYS A 1 165 ? 27.54211 7.93593  9.61767   1.000 47.21439  ? 165 LYS A CD  1 
ATOM   1275 C CE  . LYS A 1 165 ? 28.85070 7.40094  10.18717  1.000 49.14811  ? 165 LYS A CE  1 
ATOM   1276 N NZ  . LYS A 1 165 ? 28.89141 5.91267  10.22857  1.000 49.97866  ? 165 LYS A NZ  1 
ATOM   1277 N N   . SER A 1 166 ? 24.58243 5.86162  6.16268   1.000 42.40483  ? 166 SER A N   1 
ATOM   1278 C CA  . SER A 1 166 ? 24.30239 4.44246  5.94688   1.000 43.31792  ? 166 SER A CA  1 
ATOM   1279 C C   . SER A 1 166 ? 24.39339 4.04683  4.48023   1.000 42.26705  ? 166 SER A C   1 
ATOM   1280 O O   . SER A 1 166 ? 24.56740 2.86259  4.17478   1.000 42.36488  ? 166 SER A O   1 
ATOM   1281 C CB  . SER A 1 166 ? 22.90764 4.08598  6.46388   1.000 44.71430  ? 166 SER A CB  1 
ATOM   1282 O OG  . SER A 1 166 ? 22.81743 4.24421  7.86866   1.000 46.69833  ? 166 SER A OG  1 
ATOM   1283 N N   . LEU A 1 167 ? 24.25196 5.00150  3.57001   1.000 41.15294  ? 167 LEU A N   1 
ATOM   1284 C CA  . LEU A 1 167 ? 24.34228 4.72441  2.14664   1.000 41.33426  ? 167 LEU A CA  1 
ATOM   1285 C C   . LEU A 1 167 ? 25.74632 4.93575  1.60328   1.000 42.14501  ? 167 LEU A C   1 
ATOM   1286 O O   . LEU A 1 167 ? 25.91148 5.09526  0.39433   1.000 41.94164  ? 167 LEU A O   1 
ATOM   1287 C CB  . LEU A 1 167 ? 23.33929 5.58822  1.37822   1.000 39.92029  ? 167 LEU A CB  1 
ATOM   1288 C CG  . LEU A 1 167 ? 21.86444 5.34519  1.70610   1.000 39.45753  ? 167 LEU A CG  1 
ATOM   1289 C CD1 . LEU A 1 167 ? 21.02258 6.41247  1.06708   1.000 38.95824  ? 167 LEU A CD1 1 
ATOM   1290 C CD2 . LEU A 1 167 ? 21.41218 3.96100  1.24396   1.000 39.99873  ? 167 LEU A CD2 1 
ATOM   1291 N N   . GLY A 1 168 ? 26.75724 4.95096  2.46728   1.000 44.80578  ? 168 GLY A N   1 
ATOM   1292 C CA  . GLY A 1 168 ? 28.12576 5.13434  2.02998   1.000 43.96950  ? 168 GLY A CA  1 
ATOM   1293 C C   . GLY A 1 168 ? 28.50817 6.56242  1.71120   1.000 42.82681  ? 168 GLY A C   1 
ATOM   1294 O O   . GLY A 1 168 ? 29.62749 6.79679  1.25014   1.000 42.92713  ? 168 GLY A O   1 
ATOM   1295 N N   . GLY A 1 169 ? 27.63064 7.52766  1.95336   1.000 41.59073  ? 169 GLY A N   1 
ATOM   1296 C CA  . GLY A 1 169 ? 27.94796 8.90443  1.63728   1.000 41.59204  ? 169 GLY A CA  1 
ATOM   1297 C C   . GLY A 1 169 ? 29.02477 9.49131  2.53518   1.000 42.59256  ? 169 GLY A C   1 
ATOM   1298 O O   . GLY A 1 169 ? 29.35528 8.97705  3.61325   1.000 43.09769  ? 169 GLY A O   1 
ATOM   1299 N N   . ALA A 1 170 ? 29.58036 10.60841 2.07448   1.000 42.34444  ? 170 ALA A N   1 
ATOM   1300 C CA  . ALA A 1 170 ? 30.54837 11.33204 2.87851   1.000 41.05000  ? 170 ALA A CA  1 
ATOM   1301 C C   . ALA A 1 170 ? 29.84382 12.15156 3.95168   1.000 41.26344  ? 170 ALA A C   1 
ATOM   1302 O O   . ALA A 1 170 ? 28.69224 12.56013 3.78891   1.000 41.21495  ? 170 ALA A O   1 
ATOM   1303 C CB  . ALA A 1 170 ? 31.39897 12.24944 2.00060   1.000 40.04884  ? 170 ALA A CB  1 
ATOM   1304 N N   . LEU A 1 171 ? 30.54684 12.38024 5.06134   1.000 41.35952  ? 171 LEU A N   1 
ATOM   1305 C CA  . LEU A 1 171 ? 30.09175 13.30373 6.09379   1.000 42.72957  ? 171 LEU A CA  1 
ATOM   1306 C C   . LEU A 1 171 ? 30.74773 14.65471 5.85381   1.000 44.53058  ? 171 LEU A C   1 
ATOM   1307 O O   . LEU A 1 171 ? 31.96629 14.73052 5.67460   1.000 45.50684  ? 171 LEU A O   1 
ATOM   1308 C CB  . LEU A 1 171 ? 30.44751 12.79373 7.49221   1.000 43.13099  ? 171 LEU A CB  1 
ATOM   1309 C CG  . LEU A 1 171 ? 30.24460 11.30776 7.78429   1.000 43.45454  ? 171 LEU A CG  1 
ATOM   1310 C CD1 . LEU A 1 171 ? 30.54622 10.99976 9.23471   1.000 45.28644  ? 171 LEU A CD1 1 
ATOM   1311 C CD2 . LEU A 1 171 ? 28.83529 10.87763 7.42301   1.000 43.27610  ? 171 LEU A CD2 1 
ATOM   1312 N N   . MET A 1 172 ? 29.95345 15.71846 5.83722   1.000 46.24637  ? 172 MET A N   1 
ATOM   1313 C CA  . MET A 1 172 ? 30.50424 17.02923 5.52884   1.000 47.02154  ? 172 MET A CA  1 
ATOM   1314 C C   . MET A 1 172 ? 30.04004 18.06714 6.53946   1.000 48.24498  ? 172 MET A C   1 
ATOM   1315 O O   . MET A 1 172 ? 28.89991 18.04288 7.01545   1.000 48.39280  ? 172 MET A O   1 
ATOM   1316 C CB  . MET A 1 172 ? 30.15916 17.48391 4.08844   1.000 45.88735  ? 172 MET A CB  1 
ATOM   1317 C CG  . MET A 1 172 ? 28.71007 17.79730 3.79566   0.850 45.69265  ? 172 MET A CG  1 
ATOM   1318 S SD  . MET A 1 172 ? 28.50136 18.10585 2.01672   0.780 46.00227  ? 172 MET A SD  1 
ATOM   1319 C CE  . MET A 1 172 ? 28.53903 16.43844 1.40213   0.750 44.18218  ? 172 MET A CE  1 
ATOM   1320 N N   . HIS A 1 173 ? 30.95599 18.97809 6.85325   1.000 49.45526  ? 173 HIS A N   1 
ATOM   1321 C CA  . HIS A 1 173 ? 30.69964 20.00689 7.84558   1.000 52.55411  ? 173 HIS A CA  1 
ATOM   1322 C C   . HIS A 1 173 ? 29.53209 20.88815 7.40694   1.000 54.05155  ? 173 HIS A C   1 
ATOM   1323 O O   . HIS A 1 173 ? 29.43283 21.24764 6.23174   1.000 54.26188  ? 173 HIS A O   1 
ATOM   1324 C CB  . HIS A 1 173 ? 31.95062 20.85844 8.05822   1.000 53.48942  ? 173 HIS A CB  1 
ATOM   1325 C CG  . HIS A 1 173 ? 31.84618 21.79103 9.22168   1.000 55.88500  ? 173 HIS A CG  1 
ATOM   1326 N ND1 . HIS A 1 173 ? 31.30168 23.05202 9.11533   1.000 57.20581  ? 173 HIS A ND1 1 
ATOM   1327 C CD2 . HIS A 1 173 ? 32.18829 21.63579 10.52146  1.000 57.38448  ? 173 HIS A CD2 1 
ATOM   1328 C CE1 . HIS A 1 173 ? 31.32555 23.63970 10.29731  1.000 59.62145  ? 173 HIS A CE1 1 
ATOM   1329 N NE2 . HIS A 1 173 ? 31.86037 22.80251 11.16789  1.000 59.83717  ? 173 HIS A NE2 1 
ATOM   1330 N N   . PRO A 1 174 ? 28.63153 21.25693 8.32300   1.000 56.67798  ? 174 PRO A N   1 
ATOM   1331 C CA  . PRO A 1 174 ? 27.41990 21.98939 7.92075   1.000 56.86488  ? 174 PRO A CA  1 
ATOM   1332 C C   . PRO A 1 174 ? 27.67087 23.40827 7.43815   1.000 59.04930  ? 174 PRO A C   1 
ATOM   1333 O O   . PRO A 1 174 ? 26.73370 24.03491 6.93051   1.000 60.34190  ? 174 PRO A O   1 
ATOM   1334 C CB  . PRO A 1 174 ? 26.56625 21.99245 9.19774   1.000 58.41187  ? 174 PRO A CB  1 
ATOM   1335 C CG  . PRO A 1 174 ? 27.15712 20.94402 10.08369  1.000 58.20873  ? 174 PRO A CG  1 
ATOM   1336 C CD  . PRO A 1 174 ? 28.60879 20.88594 9.74659   1.000 57.70595  ? 174 PRO A CD  1 
ATOM   1337 N N   . SER A 1 175 ? 28.88009 23.94826 7.58098   1.000 60.32570  ? 175 SER A N   1 
ATOM   1338 C CA  . SER A 1 175 ? 29.14260 25.26675 7.01654   1.000 64.24687  ? 175 SER A CA  1 
ATOM   1339 C C   . SER A 1 175 ? 29.23416 25.24497 5.49514   1.000 64.31085  ? 175 SER A C   1 
ATOM   1340 O O   . SER A 1 175 ? 29.21921 26.31375 4.87317   1.000 66.45902  ? 175 SER A O   1 
ATOM   1341 C CB  . SER A 1 175 ? 30.43103 25.84242 7.60071   1.000 67.06425  ? 175 SER A CB  1 
ATOM   1342 O OG  . SER A 1 175 ? 31.53157 24.99906 7.31377   1.000 66.96073  ? 175 SER A OG  1 
ATOM   1343 N N   . ILE A 1 176 ? 29.32886 24.06484 4.88835   1.000 62.55243  ? 176 ILE A N   1 
ATOM   1344 C CA  . ILE A 1 176 ? 29.43631 23.93399 3.43842   1.000 61.06791  ? 176 ILE A CA  1 
ATOM   1345 C C   . ILE A 1 176 ? 28.02789 23.96276 2.85437   1.000 60.33232  ? 176 ILE A C   1 
ATOM   1346 O O   . ILE A 1 176 ? 27.22273 23.06641 3.11267   1.000 58.82412  ? 176 ILE A O   1 
ATOM   1347 C CB  . ILE A 1 176 ? 30.16809 22.64527 3.04935   1.000 58.21651  ? 176 ILE A CB  1 
ATOM   1348 C CG1 . ILE A 1 176 ? 31.57324 22.62585 3.65494   1.000 58.44714  ? 176 ILE A CG1 1 
ATOM   1349 C CG2 . ILE A 1 176 ? 30.21310 22.49998 1.53928   1.000 56.89152  ? 176 ILE A CG2 1 
ATOM   1350 C CD1 . ILE A 1 176 ? 32.24627 21.27441 3.58937   1.000 56.72905  ? 176 ILE A CD1 1 
ATOM   1351 N N   . GLU A 1 177 ? 27.72500 24.99126 2.06819   1.000 61.62110  ? 177 GLU A N   1 
ATOM   1352 C CA  . GLU A 1 177 ? 26.41209 25.10184 1.43500   1.000 60.88943  ? 177 GLU A CA  1 
ATOM   1353 C C   . GLU A 1 177 ? 26.39078 24.16223 0.23658   1.000 58.25527  ? 177 GLU A C   1 
ATOM   1354 O O   . GLU A 1 177 ? 26.78544 24.51806 -0.87750  1.000 58.70469  ? 177 GLU A O   1 
ATOM   1355 C CB  . GLU A 1 177 ? 26.11822 26.54459 1.04473   1.000 63.60033  ? 177 GLU A CB  1 
ATOM   1356 C CG  . GLU A 1 177 ? 25.95799 27.47907 2.23600   1.000 66.47912  ? 177 GLU A CG  1 
ATOM   1357 C CD  . GLU A 1 177 ? 25.45448 28.85411 1.84585   1.000 70.03031  ? 177 GLU A CD  1 
ATOM   1358 O OE1 . GLU A 1 177 ? 25.85014 29.35474 0.77478   0.710 70.96239  ? 177 GLU A OE1 1 
ATOM   1359 O OE2 . GLU A 1 177 ? 24.65598 29.43575 2.60942   0.790 72.42858  ? 177 GLU A OE2 1 
ATOM   1360 N N   . ALA A 1 178 ? 25.92529 22.93777 0.47116   1.000 55.33043  ? 178 ALA A N   1 
ATOM   1361 C CA  . ALA A 1 178 ? 25.93528 21.90893 -0.56160  1.000 52.96216  ? 178 ALA A CA  1 
ATOM   1362 C C   . ALA A 1 178 ? 24.84973 20.88088 -0.25715  1.000 51.16958  ? 178 ALA A C   1 
ATOM   1363 O O   . ALA A 1 178 ? 24.18099 20.93460 0.78027   1.000 51.60150  ? 178 ALA A O   1 
ATOM   1364 C CB  . ALA A 1 178 ? 27.31101 21.24702 -0.66164  1.000 52.05222  ? 178 ALA A CB  1 
ATOM   1365 N N   . MET A 1 179 ? 24.68936 19.93527 -1.18167  1.000 48.84414  ? 179 MET A N   1 
ATOM   1366 C CA  . MET A 1 179 ? 23.79168 18.79937 -1.03941  1.000 47.46432  ? 179 MET A CA  1 
ATOM   1367 C C   . MET A 1 179 ? 24.49616 17.57654 -1.60427  1.000 45.46577  ? 179 MET A C   1 
ATOM   1368 O O   . MET A 1 179 ? 25.31773 17.69354 -2.51864  1.000 45.96849  ? 179 MET A O   1 
ATOM   1369 C CB  . MET A 1 179 ? 22.46852 19.03325 -1.77563  1.000 48.74811  ? 179 MET A CB  1 
ATOM   1370 C CG  . MET A 1 179 ? 22.62612 19.23776 -3.28949  1.000 48.80963  ? 179 MET A CG  1 
ATOM   1371 S SD  . MET A 1 179 ? 21.05688 19.58909 -4.09205  1.000 50.33931  ? 179 MET A SD  1 
ATOM   1372 C CE  . MET A 1 179 ? 21.56894 19.73270 -5.80619  1.000 50.30197  ? 179 MET A CE  1 
ATOM   1373 N N   . GLN A 1 180 ? 24.18388 16.40111 -1.06426  1.000 43.33325  ? 180 GLN A N   1 
ATOM   1374 C CA  . GLN A 1 180 ? 24.88090 15.18357 -1.46003  1.000 42.07600  ? 180 GLN A CA  1 
ATOM   1375 C C   . GLN A 1 180 ? 23.89548 14.10907 -1.88837  1.000 41.67802  ? 180 GLN A C   1 
ATOM   1376 O O   . GLN A 1 180 ? 22.96040 13.78421 -1.15159  1.000 42.16093  ? 180 GLN A O   1 
ATOM   1377 C CB  . GLN A 1 180 ? 25.77198 14.64145 -0.34100  1.000 41.97390  ? 180 GLN A CB  1 
ATOM   1378 C CG  . GLN A 1 180 ? 26.59602 13.43090 -0.78040  1.000 41.63126  ? 180 GLN A CG  1 
ATOM   1379 C CD  . GLN A 1 180 ? 27.54895 12.93155 0.29025   1.000 42.01412  ? 180 GLN A CD  1 
ATOM   1380 O OE1 . GLN A 1 180 ? 28.29941 11.97905 0.07513   1.000 41.50249  ? 180 GLN A OE1 1 
ATOM   1381 N NE2 . GLN A 1 180 ? 27.51210 13.56354 1.45768   1.000 42.62922  ? 180 GLN A NE2 1 
ATOM   1382 N N   . LEU A 1 181 ? 24.13683 13.54172 -3.06374  1.000 41.50405  ? 181 LEU A N   1 
ATOM   1383 C CA  . LEU A 1 181 ? 23.30833 12.49193 -3.63511  1.000 41.11267  ? 181 LEU A CA  1 
ATOM   1384 C C   . LEU A 1 181 ? 24.01939 11.15793 -3.48131  1.000 40.08218  ? 181 LEU A C   1 
ATOM   1385 O O   . LEU A 1 181 ? 25.19575 11.03651 -3.84242  1.000 39.10191  ? 181 LEU A O   1 
ATOM   1386 C CB  . LEU A 1 181 ? 23.03535 12.77030 -5.11585  1.000 40.77268  ? 181 LEU A CB  1 
ATOM   1387 C CG  . LEU A 1 181 ? 22.17811 11.76679 -5.88885  1.000 39.89197  ? 181 LEU A CG  1 
ATOM   1388 C CD1 . LEU A 1 181 ? 20.68418 11.99092 -5.59949  1.000 40.19317  ? 181 LEU A CD1 1 
ATOM   1389 C CD2 . LEU A 1 181 ? 22.47398 11.83767 -7.38229  1.000 39.78527  ? 181 LEU A CD2 1 
ATOM   1390 N N   . THR A 1 182 ? 23.30764 10.16550 -2.94360  1.000 40.58359  ? 182 THR A N   1 
ATOM   1391 C CA  . THR A 1 182 ? 23.82071 8.80781  -2.82100  1.000 40.70522  ? 182 THR A CA  1 
ATOM   1392 C C   . THR A 1 182 ? 22.84273 7.82570  -3.45156  1.000 42.30315  ? 182 THR A C   1 
ATOM   1393 O O   . THR A 1 182 ? 21.64802 8.10572  -3.56965  1.000 43.34382  ? 182 THR A O   1 
ATOM   1394 C CB  . THR A 1 182 ? 24.05876 8.40615  -1.36168  1.000 40.53052  ? 182 THR A CB  1 
ATOM   1395 O OG1 . THR A 1 182 ? 22.87511 8.66154  -0.60313  1.000 41.48335  ? 182 THR A OG1 1 
ATOM   1396 C CG2 . THR A 1 182 ? 25.22526 9.18682  -0.76330  1.000 39.43681  ? 182 THR A CG2 1 
ATOM   1397 N N   . GLU A 1 183 ? 23.36004 6.66234  -3.83480  1.000 42.28083  ? 183 GLU A N   1 
ATOM   1398 C CA  . GLU A 1 183 ? 22.59397 5.61619  -4.49357  1.000 43.41860  ? 183 GLU A CA  1 
ATOM   1399 C C   . GLU A 1 183 ? 22.15033 4.56070  -3.48951  1.000 44.15165  ? 183 GLU A C   1 
ATOM   1400 O O   . GLU A 1 183 ? 22.80906 4.32180  -2.47710  1.000 44.34815  ? 183 GLU A O   1 
ATOM   1401 C CB  . GLU A 1 183 ? 23.43021 4.94330  -5.58585  1.000 43.76279  ? 183 GLU A CB  1 
ATOM   1402 C CG  . GLU A 1 183 ? 24.06937 5.89441  -6.58492  1.000 43.48082  ? 183 GLU A CG  1 
ATOM   1403 C CD  . GLU A 1 183 ? 24.81412 5.16174  -7.68945  1.000 43.54173  ? 183 GLU A CD  1 
ATOM   1404 O OE1 . GLU A 1 183 ? 25.19171 3.99017  -7.47319  1.000 43.58436  ? 183 GLU A OE1 1 
ATOM   1405 O OE2 . GLU A 1 183 ? 25.02010 5.75466  -8.76991  1.000 43.58542  ? 183 GLU A OE2 1 
ATOM   1406 N N   . MET A 1 184 ? 21.02976 3.90691  -3.79485  1.000 45.29191  ? 184 MET A N   1 
ATOM   1407 C CA  . MET A 1 184 ? 20.62729 2.68256  -3.10351  1.000 46.41279  ? 184 MET A CA  1 
ATOM   1408 C C   . MET A 1 184 ? 20.64240 1.54800  -4.12273  1.000 46.90413  ? 184 MET A C   1 
ATOM   1409 O O   . MET A 1 184 ? 19.79882 1.51633  -5.02416  1.000 48.28779  ? 184 MET A O   1 
ATOM   1410 C CB  . MET A 1 184 ? 19.23780 2.79757  -2.46123  1.000 47.54362  ? 184 MET A CB  1 
ATOM   1411 C CG  . MET A 1 184 ? 18.92348 4.10189  -1.73689  1.000 47.29329  ? 184 MET A CG  1 
ATOM   1412 S SD  . MET A 1 184 ? 17.21477 4.16502  -1.08210  1.000 50.09106  ? 184 MET A SD  1 
ATOM   1413 C CE  . MET A 1 184 ? 17.17836 5.82859  -0.43074  1.000 49.16546  ? 184 MET A CE  1 
ATOM   1414 N N   . ALA A 1 185 ? 21.59881 0.63087  -3.97883  1.000 46.26906  ? 185 ALA A N   1 
ATOM   1415 C CA  . ALA A 1 185 ? 21.64299 -0.64465 -4.70218  1.000 47.56074  ? 185 ALA A CA  1 
ATOM   1416 C C   . ALA A 1 185 ? 21.39267 -0.47434 -6.20293  1.000 48.38757  ? 185 ALA A C   1 
ATOM   1417 O O   . ALA A 1 185 ? 20.48065 -1.06568 -6.78155  1.000 50.47838  ? 185 ALA A O   1 
ATOM   1418 C CB  . ALA A 1 185 ? 20.65153 -1.64101 -4.09751  1.000 48.85162  ? 185 ALA A CB  1 
ATOM   1419 N N   . SER A 1 186 ? 22.22266 0.34944  -6.83316  1.000 46.94390  ? 186 SER A N   1 
ATOM   1420 C CA  . SER A 1 186 ? 22.16420 0.47675  -8.28210  1.000 48.39026  ? 186 SER A CA  1 
ATOM   1421 C C   . SER A 1 186 ? 22.67790 -0.79153 -8.95225  1.000 49.65280  ? 186 SER A C   1 
ATOM   1422 O O   . SER A 1 186 ? 23.70837 -1.34934 -8.56717  1.000 49.28626  ? 186 SER A O   1 
ATOM   1423 C CB  . SER A 1 186 ? 22.98471 1.67749  -8.75033  1.000 47.80517  ? 186 SER A CB  1 
ATOM   1424 O OG  . SER A 1 186 ? 24.32124 1.58311  -8.28278  1.000 47.55964  ? 186 SER A OG  1 
ATOM   1425 N N   . ILE A 1 187 ? 21.94844 -1.25838 -9.94586  1.000 52.00291  ? 187 ILE A N   1 
ATOM   1426 C CA  . ILE A 1 187 ? 22.46191 -2.33058 -10.78525 1.000 54.94003  ? 187 ILE A CA  1 
ATOM   1427 C C   . ILE A 1 187 ? 23.51172 -1.74219 -11.71738 1.000 55.13374  ? 187 ILE A C   1 
ATOM   1428 O O   . ILE A 1 187 ? 23.39129 -0.59740 -12.16848 1.000 53.39604  ? 187 ILE A O   1 
ATOM   1429 C CB  . ILE A 1 187 ? 21.31941 -3.01685 -11.55398 1.000 57.25632  ? 187 ILE A CB  1 
ATOM   1430 C CG1 . ILE A 1 187 ? 21.83921 -4.22828 -12.32700 1.000 58.85767  ? 187 ILE A CG1 1 
ATOM   1431 C CG2 . ILE A 1 187 ? 20.62593 -2.03938 -12.48279 1.000 58.18858  ? 187 ILE A CG2 1 
ATOM   1432 C CD1 . ILE A 1 187 ? 20.74386 -4.99156 -13.04441 0.750 61.56168  ? 187 ILE A CD1 1 
ATOM   1433 N N   . ASN A 1 188 ? 24.58273 -2.49237 -11.95669 1.000 58.32315  ? 188 ASN A N   1 
ATOM   1434 C CA  . ASN A 1 188 ? 25.62998 -2.05406 -12.87152 1.000 60.03049  ? 188 ASN A CA  1 
ATOM   1435 C C   . ASN A 1 188 ? 26.12335 -3.25235 -13.66290 1.000 64.41474  ? 188 ASN A C   1 
ATOM   1436 O O   . ASN A 1 188 ? 26.63912 -4.21417 -13.08498 1.000 64.64841  ? 188 ASN A O   1 
ATOM   1437 C CB  . ASN A 1 188 ? 26.78103 -1.37608 -12.12320 1.000 57.93595  ? 188 ASN A CB  1 
ATOM   1438 C CG  . ASN A 1 188 ? 26.51632 0.10060  -11.86880 1.000 55.63780  ? 188 ASN A CG  1 
ATOM   1439 O OD1 . ASN A 1 188 ? 26.99556 0.96678  -12.60489 1.000 55.09961  ? 188 ASN A OD1 1 
ATOM   1440 N ND2 . ASN A 1 188 ? 25.73431 0.39260  -10.83716 1.000 54.36887  ? 188 ASN A ND2 1 
ATOM   1441 N N   . ASN A 1 189 ? 25.94924 -3.19236 -14.98074 1.000 68.04989  ? 189 ASN A N   1 
ATOM   1442 C CA  . ASN A 1 189 ? 26.42805 -4.23295 -15.88157 1.000 75.08413  ? 189 ASN A CA  1 
ATOM   1443 C C   . ASN A 1 189 ? 26.88385 -3.61766 -17.19717 0.250 80.05884  ? 189 ASN A C   1 
ATOM   1444 O O   . ASN A 1 189 ? 27.26670 -2.44334 -17.24066 0.570 80.01051  ? 189 ASN A O   1 
ATOM   1445 C CB  . ASN A 1 189 ? 25.33809 -5.28093 -16.12668 1.000 76.85140  ? 189 ASN A CB  1 
ATOM   1446 C CG  . ASN A 1 189 ? 23.95603 -4.66710 -16.25460 1.000 76.94393  ? 189 ASN A CG  1 
ATOM   1447 O OD1 . ASN A 1 189 ? 23.80546 -3.52669 -16.69831 1.000 76.13235  ? 189 ASN A OD1 1 
ATOM   1448 N ND2 . ASN A 1 189 ? 22.93888 -5.41844 -15.85284 1.000 78.28825  ? 189 ASN A ND2 1 
ATOM   1449 N N   . ARG A 1 190 ? 26.85412 -4.40822 -18.27207 1.000 86.31150  ? 190 ARG A N   1 
ATOM   1450 C CA  . ARG A 1 190 ? 27.16368 -3.87125 -19.59244 1.000 88.29276  ? 190 ARG A CA  1 
ATOM   1451 C C   . ARG A 1 190 ? 26.05999 -2.95129 -20.09797 1.000 88.28085  ? 190 ARG A C   1 
ATOM   1452 O O   . ARG A 1 190 ? 26.34409 -1.99908 -20.83192 1.000 88.54587  ? 190 ARG A O   1 
ATOM   1453 C CB  . ARG A 1 190 ? 27.40428 -5.01536 -20.58077 1.000 91.83763  ? 190 ARG A CB  1 
ATOM   1454 N N   . VAL A 1 191 ? 24.81060 -3.21740 -19.71513 1.000 85.46211  ? 191 VAL A N   1 
ATOM   1455 C CA  . VAL A 1 191 ? 23.68310 -2.40029 -20.15314 1.000 84.92238  ? 191 VAL A CA  1 
ATOM   1456 C C   . VAL A 1 191 ? 23.58471 -1.12851 -19.32324 1.000 80.18552  ? 191 VAL A C   1 
ATOM   1457 O O   . VAL A 1 191 ? 23.63558 -0.01110 -19.84946 1.000 80.04301  ? 191 VAL A O   1 
ATOM   1458 C CB  . VAL A 1 191 ? 22.37639 -3.20883 -20.07093 1.000 87.73783  ? 191 VAL A CB  1 
ATOM   1459 C CG1 . VAL A 1 191 ? 21.18099 -2.29916 -20.34762 1.000 88.57780  ? 191 VAL A CG1 1 
ATOM   1460 C CG2 . VAL A 1 191 ? 22.40666 -4.38381 -21.03817 1.000 92.08522  ? 191 VAL A CG2 1 
ATOM   1461 N N   . TYR A 1 192 ? 23.42712 -1.28725 -18.01116 1.000 76.78120  ? 192 TYR A N   1 
ATOM   1462 C CA  . TYR A 1 192 ? 23.21081 -0.17124 -17.10686 1.000 70.36554  ? 192 TYR A CA  1 
ATOM   1463 C C   . TYR A 1 192 ? 24.52563 0.26050  -16.48132 1.000 64.30611  ? 192 TYR A C   1 
ATOM   1464 O O   . TYR A 1 192 ? 25.36437 -0.57298 -16.12614 1.000 63.85871  ? 192 TYR A O   1 
ATOM   1465 C CB  . TYR A 1 192 ? 22.20726 -0.55433 -16.02112 1.000 70.42210  ? 192 TYR A CB  1 
ATOM   1466 C CG  . TYR A 1 192 ? 20.77190 -0.54543 -16.49234 1.000 72.61643  ? 192 TYR A CG  1 
ATOM   1467 C CD1 . TYR A 1 192 ? 20.02627 0.62961  -16.47708 1.000 72.41939  ? 192 TYR A CD1 1 
ATOM   1468 C CD2 . TYR A 1 192 ? 20.15818 -1.70674 -16.95292 1.000 75.40937  ? 192 TYR A CD2 1 
ATOM   1469 C CE1 . TYR A 1 192 ? 18.70642 0.64989  -16.90811 1.000 74.84376  ? 192 TYR A CE1 1 
ATOM   1470 C CE2 . TYR A 1 192 ? 18.83789 -1.69473 -17.38688 1.000 77.96279  ? 192 TYR A CE2 1 
ATOM   1471 C CZ  . TYR A 1 192 ? 18.12012 -0.51286 -17.36071 1.000 77.83838  ? 192 TYR A CZ  1 
ATOM   1472 O OH  . TYR A 1 192 ? 16.80983 -0.49255 -17.78115 1.000 80.72873  ? 192 TYR A OH  1 
ATOM   1473 N N   . ARG A 1 193 ? 24.69700 1.57242  -16.34815 1.000 59.71961  ? 193 ARG A N   1 
ATOM   1474 C CA  . ARG A 1 193 ? 25.93029 2.14191  -15.82641 1.000 57.06321  ? 193 ARG A CA  1 
ATOM   1475 C C   . ARG A 1 193 ? 25.58650 3.36364  -14.99450 1.000 54.55005  ? 193 ARG A C   1 
ATOM   1476 O O   . ARG A 1 193 ? 25.01401 4.32445  -15.51527 1.000 55.83570  ? 193 ARG A O   1 
ATOM   1477 C CB  . ARG A 1 193 ? 26.88647 2.52071  -16.96226 1.000 58.84050  ? 193 ARG A CB  1 
ATOM   1478 C CG  . ARG A 1 193 ? 28.32995 2.08004  -16.73739 0.660 59.67633  ? 193 ARG A CG  1 
ATOM   1479 N N   . THR A 1 194 ? 25.93292 3.33425  -13.71097 1.000 50.92004  ? 194 THR A N   1 
ATOM   1480 C CA  . THR A 1 194 ? 25.83924 4.52091  -12.87916 1.000 48.04999  ? 194 THR A CA  1 
ATOM   1481 C C   . THR A 1 194 ? 27.22018 4.87142  -12.34303 1.000 46.56757  ? 194 THR A C   1 
ATOM   1482 O O   . THR A 1 194 ? 28.15111 4.06618  -12.38662 1.000 47.03846  ? 194 THR A O   1 
ATOM   1483 C CB  . THR A 1 194 ? 24.84346 4.34582  -11.72178 1.000 46.75229  ? 194 THR A CB  1 
ATOM   1484 O OG1 . THR A 1 194 ? 25.39799 3.48858  -10.71484 1.000 45.74241  ? 194 THR A OG1 1 
ATOM   1485 C CG2 . THR A 1 194 ? 23.53326 3.75972  -12.22535 1.000 48.10503  ? 194 THR A CG2 1 
ATOM   1486 N N   . ILE A 1 195 ? 27.33716 6.09708  -11.83065 1.000 45.58031  ? 195 ILE A N   1 
ATOM   1487 C CA  . ILE A 1 195 ? 28.61720 6.59074  -11.33999 1.000 44.67717  ? 195 ILE A CA  1 
ATOM   1488 C C   . ILE A 1 195 ? 29.03435 5.85776  -10.06651 1.000 43.74936  ? 195 ILE A C   1 
ATOM   1489 O O   . ILE A 1 195 ? 30.23290 5.72564  -9.77980  1.000 43.02032  ? 195 ILE A O   1 
ATOM   1490 C CB  . ILE A 1 195 ? 28.52326 8.11604  -11.13001 1.000 43.44233  ? 195 ILE A CB  1 
ATOM   1491 C CG1 . ILE A 1 195 ? 29.89456 8.71318  -10.82831 1.000 42.95614  ? 195 ILE A CG1 1 
ATOM   1492 C CG2 . ILE A 1 195 ? 27.52421 8.45958  -10.00661 1.000 42.03334  ? 195 ILE A CG2 1 
ATOM   1493 C CD1 . ILE A 1 195 ? 30.94410 8.35799  -11.83344 1.000 44.05179  ? 195 ILE A CD1 1 
ATOM   1494 N N   . GLY A 1 196 ? 28.06997 5.37320  -9.28865  1.000 43.92299  ? 196 GLY A N   1 
ATOM   1495 C CA  . GLY A 1 196 ? 28.35810 4.68361  -8.02800  1.000 42.72873  ? 196 GLY A CA  1 
ATOM   1496 C C   . GLY A 1 196 ? 28.73371 5.61056  -6.90188  1.000 41.08461  ? 196 GLY A C   1 
ATOM   1497 O O   . GLY A 1 196 ? 28.08528 5.61073  -5.84934  1.000 41.21854  ? 196 GLY A O   1 
ATOM   1498 N N   . SER A 1 197 ? 29.75915 6.42749  -7.10984  1.000 39.91068  ? 197 SER A N   1 
ATOM   1499 C CA  . SER A 1 197 ? 30.22896 7.33988  -6.08522  1.000 39.70487  ? 197 SER A CA  1 
ATOM   1500 C C   . SER A 1 197 ? 29.11264 8.27676  -5.62500  1.000 39.26153  ? 197 SER A C   1 
ATOM   1501 O O   . SER A 1 197 ? 28.18692 8.58052  -6.38342  1.000 39.59508  ? 197 SER A O   1 
ATOM   1502 C CB  . SER A 1 197 ? 31.40015 8.16319  -6.60889  1.000 40.47745  ? 197 SER A CB  1 
ATOM   1503 O OG  . SER A 1 197 ? 32.40931 7.32277  -7.12378  1.000 42.92845  ? 197 SER A OG  1 
ATOM   1504 N N   . PRO A 1 198 ? 29.16377 8.72890  -4.37637  1.000 38.57856  ? 198 PRO A N   1 
ATOM   1505 C CA  . PRO A 1 198 ? 28.28541 9.82203  -3.96058  1.000 38.62520  ? 198 PRO A CA  1 
ATOM   1506 C C   . PRO A 1 198 ? 28.69984 11.10316 -4.66366  1.000 39.00724  ? 198 PRO A C   1 
ATOM   1507 O O   . PRO A 1 198 ? 29.87081 11.30693 -4.99301  1.000 39.11116  ? 198 PRO A O   1 
ATOM   1508 C CB  . PRO A 1 198 ? 28.51179 9.91505  -2.44235  1.000 38.13430  ? 198 PRO A CB  1 
ATOM   1509 C CG  . PRO A 1 198 ? 29.18387 8.61754  -2.05380  1.000 37.76842  ? 198 PRO A CG  1 
ATOM   1510 C CD  . PRO A 1 198 ? 29.98730 8.22354  -3.26326  1.000 38.08563  ? 198 PRO A CD  1 
ATOM   1511 N N   . LEU A 1 199 ? 27.72409 11.97632 -4.88082  1.000 39.47495  ? 199 LEU A N   1 
ATOM   1512 C CA  . LEU A 1 199 ? 27.93459 13.24581 -5.56061  1.000 40.04194  ? 199 LEU A CA  1 
ATOM   1513 C C   . LEU A 1 199 ? 27.59774 14.38730 -4.61213  1.000 41.37914  ? 199 LEU A C   1 
ATOM   1514 O O   . LEU A 1 199 ? 26.58742 14.32905 -3.90105  1.000 41.15947  ? 199 LEU A O   1 
ATOM   1515 C CB  . LEU A 1 199 ? 27.07796 13.33254 -6.82446  1.000 39.52503  ? 199 LEU A CB  1 
ATOM   1516 C CG  . LEU A 1 199 ? 27.34514 12.29042 -7.91948  1.000 38.52673  ? 199 LEU A CG  1 
ATOM   1517 C CD1 . LEU A 1 199 ? 26.47036 12.55087 -9.11918  1.000 38.94161  ? 199 LEU A CD1 1 
ATOM   1518 C CD2 . LEU A 1 199 ? 28.80618 12.27244 -8.31826  1.000 38.17573  ? 199 LEU A CD2 1 
ATOM   1519 N N   . VAL A 1 200 ? 28.44482 15.41588 -4.59994  1.000 42.80925  ? 200 VAL A N   1 
ATOM   1520 C CA  . VAL A 1 200 ? 28.27586 16.58726 -3.74098  1.000 44.16628  ? 200 VAL A CA  1 
ATOM   1521 C C   . VAL A 1 200 ? 28.08913 17.78996 -4.65663  1.000 46.33531  ? 200 VAL A C   1 
ATOM   1522 O O   . VAL A 1 200 ? 29.00970 18.16440 -5.39581  1.000 47.07131  ? 200 VAL A O   1 
ATOM   1523 C CB  . VAL A 1 200 ? 29.46950 16.78874 -2.79207  1.000 43.96431  ? 200 VAL A CB  1 
ATOM   1524 C CG1 . VAL A 1 200 ? 29.32651 18.08261 -1.99479  1.000 44.55360  ? 200 VAL A CG1 1 
ATOM   1525 C CG2 . VAL A 1 200 ? 29.61542 15.59772 -1.85575  1.000 42.93433  ? 200 VAL A CG2 1 
ATOM   1526 N N   . PHE A 1 201 ? 26.89880 18.39118 -4.61864  1.000 47.56626  ? 201 PHE A N   1 
ATOM   1527 C CA  . PHE A 1 201 ? 26.59499 19.49898 -5.51706  1.000 49.25812  ? 201 PHE A CA  1 
ATOM   1528 C C   . PHE A 1 201 ? 26.62856 20.81730 -4.76242  1.000 51.14659  ? 201 PHE A C   1 
ATOM   1529 O O   . PHE A 1 201 ? 26.22015 20.87302 -3.60127  1.000 50.87595  ? 201 PHE A O   1 
ATOM   1530 C CB  . PHE A 1 201 ? 25.21674 19.32190 -6.15592  1.000 49.29827  ? 201 PHE A CB  1 
ATOM   1531 C CG  . PHE A 1 201 ? 25.07042 18.04320 -6.91797  1.000 48.85526  ? 201 PHE A CG  1 
ATOM   1532 C CD1 . PHE A 1 201 ? 25.41413 17.98013 -8.26135  1.000 49.78939  ? 201 PHE A CD1 1 
ATOM   1533 C CD2 . PHE A 1 201 ? 24.59827 16.90044 -6.29392  1.000 47.97987  ? 201 PHE A CD2 1 
ATOM   1534 C CE1 . PHE A 1 201 ? 25.28766 16.79773 -8.97823  1.000 49.57396  ? 201 PHE A CE1 1 
ATOM   1535 C CE2 . PHE A 1 201 ? 24.46684 15.71804 -6.99510  1.000 48.04388  ? 201 PHE A CE2 1 
ATOM   1536 C CZ  . PHE A 1 201 ? 24.81557 15.66574 -8.34974  1.000 48.61246  ? 201 PHE A CZ  1 
ATOM   1537 N N   . PRO A 1 202 ? 27.10491 21.88891 -5.37978  1.000 53.36620  ? 202 PRO A N   1 
ATOM   1538 C CA  . PRO A 1 202 ? 27.16080 23.18301 -4.69878  1.000 55.66338  ? 202 PRO A CA  1 
ATOM   1539 C C   . PRO A 1 202 ? 25.82743 23.91027 -4.81855  1.000 57.74838  ? 202 PRO A C   1 
ATOM   1540 O O   . PRO A 1 202 ? 24.89147 23.45244 -5.47127  1.000 57.88441  ? 202 PRO A O   1 
ATOM   1541 C CB  . PRO A 1 202 ? 28.26978 23.91838 -5.44974  1.000 56.79317  ? 202 PRO A CB  1 
ATOM   1542 C CG  . PRO A 1 202 ? 28.15218 23.39349 -6.84698  1.000 56.35117  ? 202 PRO A CG  1 
ATOM   1543 C CD  . PRO A 1 202 ? 27.71460 21.94727 -6.72054  1.000 54.11992  ? 202 PRO A CD  1 
ATOM   1544 N N   . LYS A 1 203 ? 25.76123 25.06535 -4.16546  1.000 60.05791  ? 203 LYS A N   1 
ATOM   1545 C CA  . LYS A 1 203 ? 24.59986 25.93150 -4.28088  1.000 62.51493  ? 203 LYS A CA  1 
ATOM   1546 C C   . LYS A 1 203 ? 24.39864 26.33762 -5.73772  1.000 64.12244  ? 203 LYS A C   1 
ATOM   1547 O O   . LYS A 1 203 ? 25.34370 26.37832 -6.52940  1.000 64.29747  ? 203 LYS A O   1 
ATOM   1548 C CB  . LYS A 1 203 ? 24.78645 27.16609 -3.39830  0.800 64.05658  ? 203 LYS A CB  1 
ATOM   1549 C CG  . LYS A 1 203 ? 23.51003 27.78187 -2.86754  0.700 65.24715  ? 203 LYS A CG  1 
ATOM   1550 C CD  . LYS A 1 203 ? 23.83027 29.00652 -2.02742  0.600 67.08518  ? 203 LYS A CD  1 
ATOM   1551 C CE  . LYS A 1 203 ? 22.57705 29.60967 -1.42259  0.600 68.68260  ? 203 LYS A CE  1 
ATOM   1552 N NZ  . LYS A 1 203 ? 21.94042 28.69246 -0.43905  0.600 67.11917  ? 203 LYS A NZ  1 
ATOM   1553 N N   . HIS A 1 204 ? 23.14566 26.61647 -6.09304  1.000 66.01373  ? 204 HIS A N   1 
ATOM   1554 C CA  . HIS A 1 204 ? 22.71335 27.02457 -7.43117  1.000 68.46926  ? 204 HIS A CA  1 
ATOM   1555 C C   . HIS A 1 204 ? 22.86837 25.93424 -8.48929  1.000 65.91648  ? 204 HIS A C   1 
ATOM   1556 O O   . HIS A 1 204 ? 22.71434 26.22385 -9.67926  1.000 67.23635  ? 204 HIS A O   1 
ATOM   1557 C CB  . HIS A 1 204 ? 23.43773 28.28900 -7.91969  1.000 72.35811  ? 204 HIS A CB  1 
ATOM   1558 C CG  . HIS A 1 204 ? 23.34897 29.45047 -6.97553  1.000 75.38986  ? 204 HIS A CG  1 
ATOM   1559 N ND1 . HIS A 1 204 ? 22.15451 30.05238 -6.64056  1.000 77.47869  ? 204 HIS A ND1 1 
ATOM   1560 C CD2 . HIS A 1 204 ? 24.31118 30.12974 -6.30649  1.000 76.44277  ? 204 HIS A CD2 1 
ATOM   1561 C CE1 . HIS A 1 204 ? 22.38335 31.04345 -5.79664  1.000 79.16367  ? 204 HIS A CE1 1 
ATOM   1562 N NE2 . HIS A 1 204 ? 23.68419 31.11254 -5.57883  1.000 78.54062  ? 204 HIS A NE2 1 
ATOM   1563 N N   . HIS A 1 205 ? 23.17897 24.69681 -8.10855  1.000 61.67271  ? 205 HIS A N   1 
ATOM   1564 C CA  . HIS A 1 205 ? 23.13046 23.56780 -9.03231  1.000 59.23122  ? 205 HIS A CA  1 
ATOM   1565 C C   . HIS A 1 205 ? 21.79769 22.84896 -8.86078  1.000 59.34690  ? 205 HIS A C   1 
ATOM   1566 O O   . HIS A 1 205 ? 21.34923 22.62690 -7.73208  1.000 59.68865  ? 205 HIS A O   1 
ATOM   1567 C CB  . HIS A 1 205 ? 24.28837 22.59228 -8.80069  1.000 55.75566  ? 205 HIS A CB  1 
ATOM   1568 C CG  . HIS A 1 205 ? 25.57207 22.99897 -9.45685  1.000 56.62341  ? 205 HIS A CG  1 
ATOM   1569 N ND1 . HIS A 1 205 ? 26.56602 22.09551 -9.76837  1.000 55.77474  ? 205 HIS A ND1 1 
ATOM   1570 C CD2 . HIS A 1 205 ? 26.02542 24.21002 -9.86104  1.000 58.76622  ? 205 HIS A CD2 1 
ATOM   1571 C CE1 . HIS A 1 205 ? 27.57562 22.73183 -10.33639 1.000 57.02914  ? 205 HIS A CE1 1 
ATOM   1572 N NE2 . HIS A 1 205 ? 27.27367 24.01615 -10.40290 1.000 58.76363  ? 205 HIS A NE2 1 
ATOM   1573 N N   . VAL A 1 206 ? 21.16414 22.49328 -9.97452  1.000 60.04952  ? 206 VAL A N   1 
ATOM   1574 C CA  . VAL A 1 206 ? 19.85502 21.84948 -9.96200  1.000 59.34920  ? 206 VAL A CA  1 
ATOM   1575 C C   . VAL A 1 206 ? 20.01491 20.41745 -10.45440 1.000 56.97137  ? 206 VAL A C   1 
ATOM   1576 O O   . VAL A 1 206 ? 20.38060 20.18622 -11.61323 1.000 56.89934  ? 206 VAL A O   1 
ATOM   1577 C CB  . VAL A 1 206 ? 18.83546 22.61796 -10.81678 1.000 61.60205  ? 206 VAL A CB  1 
ATOM   1578 C CG1 . VAL A 1 206 ? 17.50553 21.88352 -10.83800 1.000 61.84659  ? 206 VAL A CG1 1 
ATOM   1579 C CG2 . VAL A 1 206 ? 18.65167 24.02963 -10.27927 1.000 63.02271  ? 206 VAL A CG2 1 
ATOM   1580 N N   . VAL A 1 207 ? 19.75377 19.45992 -9.57157  1.000 55.29803  ? 207 VAL A N   1 
ATOM   1581 C CA  . VAL A 1 207 ? 19.69341 18.04804 -9.92530  1.000 53.87209  ? 207 VAL A CA  1 
ATOM   1582 C C   . VAL A 1 207 ? 18.23233 17.68823 -10.15339 1.000 55.27243  ? 207 VAL A C   1 
ATOM   1583 O O   . VAL A 1 207 ? 17.39658 17.85162 -9.25436  1.000 55.92774  ? 207 VAL A O   1 
ATOM   1584 C CB  . VAL A 1 207 ? 20.31173 17.16816 -8.83103  1.000 51.58177  ? 207 VAL A CB  1 
ATOM   1585 C CG1 . VAL A 1 207 ? 20.05441 15.70328 -9.13189  1.000 51.06800  ? 207 VAL A CG1 1 
ATOM   1586 C CG2 . VAL A 1 207 ? 21.79923 17.43713 -8.71503  1.000 50.61820  ? 207 VAL A CG2 1 
ATOM   1587 N N   . SER A 1 208 ? 17.92288 17.19578 -11.34950 1.000 55.70776  ? 208 SER A N   1 
ATOM   1588 C CA  . SER A 1 208 ? 16.55631 16.88469 -11.74403 1.000 57.71368  ? 208 SER A CA  1 
ATOM   1589 C C   . SER A 1 208 ? 16.42726 15.39916 -12.04672 1.000 57.16186  ? 208 SER A C   1 
ATOM   1590 O O   . SER A 1 208 ? 17.25950 14.83103 -12.76063 1.000 56.80550  ? 208 SER A O   1 
ATOM   1591 C CB  . SER A 1 208 ? 16.13966 17.70110 -12.96476 1.000 60.71455  ? 208 SER A CB  1 
ATOM   1592 O OG  . SER A 1 208 ? 14.81945 17.37034 -13.34622 1.000 63.60223  ? 208 SER A OG  1 
ATOM   1593 N N   . LEU A 1 209 ? 15.38607 14.77490 -11.50645 1.000 57.50271  ? 209 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 209 ? 15.09400 13.37284 -11.76728 1.000 57.22291  ? 209 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 209 ? 13.88387 13.28746 -12.68762 1.000 60.85665  ? 209 LEU A C   1 
ATOM   1596 O O   . LEU A 1 209 ? 12.84941 13.91115 -12.42230 1.000 62.46438  ? 209 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 209 ? 14.83677 12.61020 -10.46548 1.000 55.68916  ? 209 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 209 ? 15.89614 12.66267 -9.35343  1.000 52.38083  ? 209 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 209 ? 15.50113 11.73948 -8.21765  1.000 51.74081  ? 209 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 209 ? 17.29098 12.31409 -9.86517  1.000 50.29526  ? 209 LEU A CD2 1 
ATOM   1601 N N   . GLN A 1 210 ? 14.01974 12.52551 -13.77197 1.000 62.32951  ? 210 GLN A N   1 
ATOM   1602 C CA  . GLN A 1 210 ? 12.98640 12.43401 -14.78919 1.000 66.72389  ? 210 GLN A CA  1 
ATOM   1603 C C   . GLN A 1 210 ? 12.61737 10.97997 -15.00956 1.000 68.88269  ? 210 GLN A C   1 
ATOM   1604 O O   . GLN A 1 210 ? 13.50181 10.13539 -15.25515 1.000 68.76810  ? 210 GLN A O   1 
ATOM   1605 C CB  . GLN A 1 210 ? 13.46465 13.10085 -16.09155 0.900 67.08927  ? 210 GLN A CB  1 
ATOM   1606 C CG  . GLN A 1 210 ? 13.84778 14.56751 -15.88776 0.800 65.66257  ? 210 GLN A CG  1 
ATOM   1607 C CD  . GLN A 1 210 ? 14.38067 15.24380 -17.13576 0.700 65.86558  ? 210 GLN A CD  1 
ATOM   1608 O OE1 . GLN A 1 210 ? 14.28479 14.71038 -18.24196 0.700 67.23085  ? 210 GLN A OE1 1 
ATOM   1609 N NE2 . GLN A 1 210 ? 14.94579 16.43432 -16.96152 0.700 64.77626  ? 210 GLN A NE2 1 
ATOM   1610 N N   . PRO A 1 211 ? 11.33562 10.62717 -14.92373 1.000 72.49311  ? 211 PRO A N   1 
ATOM   1611 C CA  . PRO A 1 211 ? 10.93204 9.22524  -15.05251 1.000 73.82622  ? 211 PRO A CA  1 
ATOM   1612 C C   . PRO A 1 211 ? 11.14160 8.70064  -16.46461 1.000 76.04510  ? 211 PRO A C   1 
ATOM   1613 O O   . PRO A 1 211 ? 11.16696 9.44603  -17.44635 1.000 77.40464  ? 211 PRO A O   1 
ATOM   1614 C CB  . PRO A 1 211 ? 9.43982  9.24256  -14.69572 1.000 75.82317  ? 211 PRO A CB  1 
ATOM   1615 C CG  . PRO A 1 211 ? 9.18761  10.59066 -14.07863 1.000 75.31487  ? 211 PRO A CG  1 
ATOM   1616 C CD  . PRO A 1 211 ? 10.18633 11.51530 -14.68374 1.000 74.07582  ? 211 PRO A CD  1 
ATOM   1617 N N   . VAL A 1 212 ? 11.27957 7.38015  -16.54928 1.000 77.01232  ? 212 VAL A N   1 
ATOM   1618 C CA  . VAL A 1 212 ? 11.45969 6.68767  -17.81801 1.000 81.37378  ? 212 VAL A CA  1 
ATOM   1619 C C   . VAL A 1 212 ? 10.14005 6.04242  -18.22157 1.000 86.10368  ? 212 VAL A C   1 
ATOM   1620 O O   . VAL A 1 212 ? 9.56891  6.37501  -19.26572 1.000 91.21533  ? 212 VAL A O   1 
ATOM   1621 C CB  . VAL A 1 212 ? 12.59511 5.65262  -17.71773 1.000 81.31261  ? 212 VAL A CB  1 
ATOM   1622 C CG1 . VAL A 1 212 ? 12.64480 4.78350  -18.95936 1.000 84.99881  ? 212 VAL A CG1 1 
ATOM   1623 C CG2 . VAL A 1 212 ? 13.92513 6.35743  -17.50684 1.000 79.74902  ? 212 VAL A CG2 1 
ATOM   1624 N N   . ASN A 1 213 ? 9.64764  5.12017  -17.39483 1.000 85.16622  ? 213 ASN A N   1 
ATOM   1625 C CA  . ASN A 1 213 ? 8.36608  4.45419  -17.64591 1.000 89.73187  ? 213 ASN A CA  1 
ATOM   1626 C C   . ASN A 1 213 ? 7.41649  4.66255  -16.49958 1.000 89.39983  ? 213 ASN A C   1 
ATOM   1627 O O   . ASN A 1 213 ? 6.50567  5.49694  -16.60349 1.000 91.93175  ? 213 ASN A O   1 
ATOM   1628 C CB  . ASN A 1 213 ? 8.60867  2.97097  -17.94275 1.000 92.28624  ? 213 ASN A CB  1 
ATOM   1629 C CG  . ASN A 1 213 ? 9.33304  2.73876  -19.25468 1.000 94.70929  ? 213 ASN A CG  1 
ATOM   1630 O OD1 . ASN A 1 213 ? 9.10286  3.44061  -20.24080 1.000 98.60943  ? 213 ASN A OD1 1 
ATOM   1631 N ND2 . ASN A 1 213 ? 10.22284 1.75404  -19.26953 0.540 93.58514  ? 213 ASN A ND2 1 
ATOM   1632 N N   . ASP A 1 214 ? 7.56420  3.94225  -15.37522 1.000 85.74126  ? 214 ASP A N   1 
ATOM   1633 C CA  . ASP A 1 214 ? 6.69696  4.12705  -14.22027 1.000 84.15568  ? 214 ASP A CA  1 
ATOM   1634 C C   . ASP A 1 214 ? 6.79237  5.56355  -13.72645 1.000 81.07595  ? 214 ASP A C   1 
ATOM   1635 O O   . ASP A 1 214 ? 7.88893  6.09852  -13.54442 1.000 78.37751  ? 214 ASP A O   1 
ATOM   1636 C CB  . ASP A 1 214 ? 7.08896  3.14790  -13.11038 0.800 81.77936  ? 214 ASP A CB  1 
ATOM   1637 C CG  . ASP A 1 214 ? 6.15035  3.19495  -11.90901 0.600 83.99318  ? 214 ASP A CG  1 
ATOM   1638 O OD1 . ASP A 1 214 ? 5.07157  3.81880  -12.00083 0.600 87.00416  ? 214 ASP A OD1 1 
ATOM   1639 O OD2 . ASP A 1 214 ? 6.49041  2.59713  -10.86014 0.600 83.56507  ? 214 ASP A OD2 1 
ATOM   1640 N N   . LYS A 1 215 ? 5.64028  6.19111  -13.51715 1.000 82.24654  ? 215 LYS A N   1 
ATOM   1641 C CA  . LYS A 1 215 ? 5.59331  7.57679  -13.08042 1.000 78.87372  ? 215 LYS A CA  1 
ATOM   1642 C C   . LYS A 1 215 ? 5.23666  7.72375  -11.60634 1.000 77.08909  ? 215 LYS A C   1 
ATOM   1643 O O   . LYS A 1 215 ? 5.13295  8.85465  -11.11764 1.000 76.41778  ? 215 LYS A O   1 
ATOM   1644 C CB  . LYS A 1 215 ? 4.60286  8.36028  -13.94957 1.000 81.23375  ? 215 LYS A CB  1 
ATOM   1645 C CG  . LYS A 1 215 ? 4.94047  8.31010  -15.43401 1.000 81.13909  ? 215 LYS A CG  1 
ATOM   1646 C CD  . LYS A 1 215 ? 3.89770  9.00601  -16.29514 1.000 84.50222  ? 215 LYS A CD  1 
ATOM   1647 C CE  . LYS A 1 215 ? 4.26111  8.90837  -17.77121 0.540 86.23743  ? 215 LYS A CE  1 
ATOM   1648 N NZ  . LYS A 1 215 ? 3.22618  9.52343  -18.64832 0.730 90.97824  ? 215 LYS A NZ  1 
ATOM   1649 N N   . ASP A 1 216 ? 5.04824  6.62018  -10.88678 1.000 76.10442  ? 216 ASP A N   1 
ATOM   1650 C CA  . ASP A 1 216 ? 4.69030  6.65744  -9.47508  1.000 76.73187  ? 216 ASP A CA  1 
ATOM   1651 C C   . ASP A 1 216 ? 5.91671  6.37073  -8.61807  1.000 73.92149  ? 216 ASP A C   1 
ATOM   1652 O O   . ASP A 1 216 ? 6.64175  5.39880  -8.86099  1.000 74.17240  ? 216 ASP A O   1 
ATOM   1653 C CB  . ASP A 1 216 ? 3.58096  5.65351  -9.17016  0.800 79.82178  ? 216 ASP A CB  1 
ATOM   1654 C CG  . ASP A 1 216 ? 2.36377  5.86564  -10.02912 0.700 84.03247  ? 216 ASP A CG  1 
ATOM   1655 O OD1 . ASP A 1 216 ? 2.12575  7.01762  -10.44358 0.700 84.69175  ? 216 ASP A OD1 1 
ATOM   1656 O OD2 . ASP A 1 216 ? 1.65040  4.87949  -10.29610 0.700 87.29416  ? 216 ASP A OD2 1 
ATOM   1657 N N   . PHE A 1 217 ? 6.14440  7.22290  -7.62106  1.000 72.51323  ? 217 PHE A N   1 
ATOM   1658 C CA  . PHE A 1 217 ? 7.29905  7.11554  -6.74493  1.000 68.94027  ? 217 PHE A CA  1 
ATOM   1659 C C   . PHE A 1 217 ? 6.88467  7.43486  -5.31928  1.000 68.29395  ? 217 PHE A C   1 
ATOM   1660 O O   . PHE A 1 217 ? 5.96713  8.22587  -5.08297  1.000 70.43998  ? 217 PHE A O   1 
ATOM   1661 C CB  . PHE A 1 217 ? 8.42209  8.05999  -7.17118  1.000 67.33201  ? 217 PHE A CB  1 
ATOM   1662 C CG  . PHE A 1 217 ? 8.81332  7.91089  -8.60027  1.000 68.28342  ? 217 PHE A CG  1 
ATOM   1663 C CD1 . PHE A 1 217 ? 9.78587  6.99999  -8.97013  1.000 67.22750  ? 217 PHE A CD1 1 
ATOM   1664 C CD2 . PHE A 1 217 ? 8.20064  8.67158  -9.58071  1.000 70.46428  ? 217 PHE A CD2 1 
ATOM   1665 C CE1 . PHE A 1 217 ? 10.15036 6.85542  -10.29371 1.000 68.20960  ? 217 PHE A CE1 1 
ATOM   1666 C CE2 . PHE A 1 217 ? 8.55851  8.53193  -10.90479 1.000 71.42773  ? 217 PHE A CE2 1 
ATOM   1667 C CZ  . PHE A 1 217 ? 9.53630  7.62213  -11.26224 1.000 70.39408  ? 217 PHE A CZ  1 
ATOM   1668 N N   . GLN A 1 218 ? 7.56846  6.80032  -4.37441  1.000 65.83933  ? 218 GLN A N   1 
ATOM   1669 C CA  . GLN A 1 218 ? 7.40848  7.07677  -2.95372  1.000 66.05152  ? 218 GLN A CA  1 
ATOM   1670 C C   . GLN A 1 218 ? 8.51526  8.04845  -2.55844  1.000 63.77203  ? 218 GLN A C   1 
ATOM   1671 O O   . GLN A 1 218 ? 9.69360  7.67795  -2.54119  1.000 61.78034  ? 218 GLN A O   1 
ATOM   1672 C CB  . GLN A 1 218 ? 7.48506  5.78374  -2.14551  0.800 66.26535  ? 218 GLN A CB  1 
ATOM   1673 C CG  . GLN A 1 218 ? 6.97715  5.89528  -0.73005  0.700 67.82955  ? 218 GLN A CG  1 
ATOM   1674 C CD  . GLN A 1 218 ? 5.46632  5.91387  -0.65939  0.600 71.26259  ? 218 GLN A CD  1 
ATOM   1675 O OE1 . GLN A 1 218 ? 4.78780  5.21971  -1.41730  0.600 72.90204  ? 218 GLN A OE1 1 
ATOM   1676 N NE2 . GLN A 1 218 ? 4.92818  6.71078  0.25505   0.600 72.42451  ? 218 GLN A NE2 1 
ATOM   1677 N N   . ILE A 1 219 ? 8.14281  9.29684  -2.27456  1.000 64.71980  ? 219 ILE A N   1 
ATOM   1678 C CA  . ILE A 1 219 ? 9.10016  10.34788 -1.93603  1.000 63.09105  ? 219 ILE A CA  1 
ATOM   1679 C C   . ILE A 1 219 ? 8.97527  10.65764 -0.45170  1.000 63.76710  ? 219 ILE A C   1 
ATOM   1680 O O   . ILE A 1 219 ? 7.86043  10.78470 0.07187   1.000 66.90259  ? 219 ILE A O   1 
ATOM   1681 C CB  . ILE A 1 219 ? 8.87636  11.61756 -2.77689  1.000 62.85573  ? 219 ILE A CB  1 
ATOM   1682 C CG1 . ILE A 1 219 ? 8.91219  11.29767 -4.27550  1.000 62.10345  ? 219 ILE A CG1 1 
ATOM   1683 C CG2 . ILE A 1 219 ? 9.92721  12.66512 -2.44183  1.000 60.32126  ? 219 ILE A CG2 1 
ATOM   1684 C CD1 . ILE A 1 219 ? 8.37251  12.41993 -5.14311  1.000 62.92425  ? 219 ILE A CD1 1 
ATOM   1685 N N   . SER A 1 220 ? 10.11584 10.78720 0.22947   1.000 61.56186  ? 220 SER A N   1 
ATOM   1686 C CA  . SER A 1 220 ? 10.12596 11.05786 1.65974   1.000 62.82700  ? 220 SER A CA  1 
ATOM   1687 C C   . SER A 1 220 ? 10.99899 12.26376 1.96434   1.000 61.67482  ? 220 SER A C   1 
ATOM   1688 O O   . SER A 1 220 ? 12.09589 12.40687 1.41454   1.000 59.98519  ? 220 SER A O   1 
ATOM   1689 C CB  . SER A 1 220 ? 10.63685 9.85967  2.45578   1.000 62.85616  ? 220 SER A CB  1 
ATOM   1690 O OG  . SER A 1 220 ? 12.04823 9.78837  2.36471   1.000 60.85753  ? 220 SER A OG  1 
ATOM   1691 N N   . VAL A 1 221 ? 10.51705 13.11360 2.86434   1.000 62.89600  ? 221 VAL A N   1 
ATOM   1692 C CA  . VAL A 1 221 ? 11.26475 14.26684 3.34695   1.000 63.67122  ? 221 VAL A CA  1 
ATOM   1693 C C   . VAL A 1 221 ? 11.34501 14.17314 4.86631   1.000 66.81620  ? 221 VAL A C   1 
ATOM   1694 O O   . VAL A 1 221 ? 10.34760 14.41080 5.55542   1.000 70.99186  ? 221 VAL A O   1 
ATOM   1695 C CB  . VAL A 1 221 ? 10.61485 15.58447 2.90615   1.000 66.04560  ? 221 VAL A CB  1 
ATOM   1696 C CG1 . VAL A 1 221 ? 11.27745 16.76724 3.58816   1.000 66.26706  ? 221 VAL A CG1 1 
ATOM   1697 C CG2 . VAL A 1 221 ? 10.69637 15.73152 1.38392   1.000 65.77028  ? 221 VAL A CG2 1 
ATOM   1698 N N   . ASP A 1 222 ? 12.52234 13.81927 5.38743   1.000 65.98665  ? 222 ASP A N   1 
ATOM   1699 C CA  . ASP A 1 222 ? 12.75749 13.66422 6.82809   1.000 68.30344  ? 222 ASP A CA  1 
ATOM   1700 C C   . ASP A 1 222 ? 11.76987 12.63586 7.35974   1.000 71.58262  ? 222 ASP A C   1 
ATOM   1701 O O   . ASP A 1 222 ? 11.88297 11.44481 7.00755   1.000 71.30055  ? 222 ASP A O   1 
ATOM   1702 C CB  . ASP A 1 222 ? 12.68744 15.03082 7.52446   1.000 68.65723  ? 222 ASP A CB  1 
ATOM   1703 C CG  . ASP A 1 222 ? 13.69975 16.02878 6.99397   1.000 65.62552  ? 222 ASP A CG  1 
ATOM   1704 O OD1 . ASP A 1 222 ? 14.72214 15.60724 6.41857   1.000 62.53359  ? 222 ASP A OD1 1 
ATOM   1705 O OD2 . ASP A 1 222 ? 13.46985 17.24671 7.17360   1.000 66.61853  ? 222 ASP A OD2 1 
ATOM   1706 N N   . HIS A 1 223 ? 10.80560 13.01860 8.19512   1.000 75.74713  ? 223 HIS A N   1 
ATOM   1707 C CA  . HIS A 1 223 ? 9.80914  12.07909 8.69669   1.000 80.42994  ? 223 HIS A CA  1 
ATOM   1708 C C   . HIS A 1 223 ? 8.88710  11.59984 7.58050   1.000 80.55869  ? 223 HIS A C   1 
ATOM   1709 O O   . HIS A 1 223 ? 8.83729  10.40556 7.26533   1.000 80.59180  ? 223 HIS A O   1 
ATOM   1710 C CB  . HIS A 1 223 ? 8.98403  12.73096 9.81129   0.800 86.05414  ? 223 HIS A CB  1 
ATOM   1711 C CG  . HIS A 1 223 ? 9.52337  12.50594 11.18906  0.700 88.25592  ? 223 HIS A CG  1 
ATOM   1712 N ND1 . HIS A 1 223 ? 9.80927  11.25128 11.68310  0.700 88.55906  ? 223 HIS A ND1 1 
ATOM   1713 C CD2 . HIS A 1 223 ? 9.79967  13.37575 12.18990  0.700 89.83241  ? 223 HIS A CD2 1 
ATOM   1714 C CE1 . HIS A 1 223 ? 10.25207 11.35906 12.92373  0.700 89.71944  ? 223 HIS A CE1 1 
ATOM   1715 N NE2 . HIS A 1 223 ? 10.25524 12.63771 13.25554  0.700 90.45551  ? 223 HIS A NE2 1 
ATOM   1716 N N   . LEU A 1 224 ? 8.15647  12.52510 6.96354   1.000 80.92543  ? 224 LEU A N   1 
ATOM   1717 C CA  . LEU A 1 224 ? 7.01301  12.15345 6.14251   1.000 82.64226  ? 224 LEU A CA  1 
ATOM   1718 C C   . LEU A 1 224 ? 7.44231  11.49940 4.83408   1.000 80.02182  ? 224 LEU A C   1 
ATOM   1719 O O   . LEU A 1 224 ? 8.42821  11.89457 4.20651   1.000 77.56491  ? 224 LEU A O   1 
ATOM   1720 C CB  . LEU A 1 224 ? 6.13438  13.37576 5.85970   0.900 85.03867  ? 224 LEU A CB  1 
ATOM   1721 C CG  . LEU A 1 224 ? 6.73049  14.57650 5.12301   0.800 84.76679  ? 224 LEU A CG  1 
ATOM   1722 C CD1 . LEU A 1 224 ? 5.62653  15.32769 4.39786   0.800 88.02976  ? 224 LEU A CD1 1 
ATOM   1723 C CD2 . LEU A 1 224 ? 7.45132  15.50617 6.08753   0.800 85.13272  ? 224 LEU A CD2 1 
ATOM   1724 N N   . SER A 1 225 ? 6.68139  10.48373 4.43413   1.000 81.19473  ? 225 SER A N   1 
ATOM   1725 C CA  . SER A 1 225 ? 6.87340  9.76052  3.18325   1.000 76.72666  ? 225 SER A CA  1 
ATOM   1726 C C   . SER A 1 225 ? 5.50641  9.60021  2.53677   1.000 78.15471  ? 225 SER A C   1 
ATOM   1727 O O   . SER A 1 225 ? 4.65319  8.87377  3.05575   1.000 80.14452  ? 225 SER A O   1 
ATOM   1728 C CB  . SER A 1 225 ? 7.52291  8.40133  3.42582   1.000 74.34768  ? 225 SER A CB  1 
ATOM   1729 O OG  . SER A 1 225 ? 7.48789  7.61637  2.24905   1.000 73.23883  ? 225 SER A OG  1 
ATOM   1730 N N   . ILE A 1 226 ? 5.29465  10.27959 1.41602   1.000 76.75317  ? 226 ILE A N   1 
ATOM   1731 C CA  . ILE A 1 226 ? 4.01387  10.27749 0.72440   1.000 81.07479  ? 226 ILE A CA  1 
ATOM   1732 C C   . ILE A 1 226 ? 4.21968  9.74073  -0.68394  1.000 81.34409  ? 226 ILE A C   1 
ATOM   1733 O O   . ILE A 1 226 ? 5.25672  9.99142  -1.30335  1.000 78.87905  ? 226 ILE A O   1 
ATOM   1734 C CB  . ILE A 1 226 ? 3.39719  11.68935 0.69243   0.700 83.06112  ? 226 ILE A CB  1 
ATOM   1735 C CG1 . ILE A 1 226 ? 4.43651  12.70411 0.21602   0.600 79.69610  ? 226 ILE A CG1 1 
ATOM   1736 C CG2 . ILE A 1 226 ? 2.87741  12.07120 2.06941   0.600 86.57029  ? 226 ILE A CG2 1 
ATOM   1737 C CD1 . ILE A 1 226 ? 3.93517  14.13266 0.22122   0.600 81.62521  ? 226 ILE A CD1 1 
ATOM   1738 N N   . LEU A 1 227 ? 3.23341  8.99752  -1.18292  1.000 85.58911  ? 227 LEU A N   1 
ATOM   1739 C CA  . LEU A 1 227 ? 3.27598  8.46782  -2.54117  1.000 85.48127  ? 227 LEU A CA  1 
ATOM   1740 C C   . LEU A 1 227 ? 2.77797  9.53029  -3.51145  1.000 86.82360  ? 227 LEU A C   1 
ATOM   1741 O O   . LEU A 1 227 ? 1.66962  10.05214 -3.35071  1.000 89.13621  ? 227 LEU A O   1 
ATOM   1742 C CB  . LEU A 1 227 ? 2.42588  7.20265  -2.64842  1.000 87.69795  ? 227 LEU A CB  1 
ATOM   1743 C CG  . LEU A 1 227 ? 2.13008  6.69089  -4.06101  1.000 87.45671  ? 227 LEU A CG  1 
ATOM   1744 C CD1 . LEU A 1 227 ? 3.38540  6.14928  -4.72577  1.000 83.63910  ? 227 LEU A CD1 1 
ATOM   1745 C CD2 . LEU A 1 227 ? 1.03300  5.63550  -4.04559  1.000 90.87753  ? 227 LEU A CD2 1 
ATOM   1746 N N   . HIS A 1 228 ? 3.59070  9.85098  -4.51227  1.000 85.96621  ? 228 HIS A N   1 
ATOM   1747 C CA  . HIS A 1 228 ? 3.22059  10.81240 -5.54023  1.000 88.58488  ? 228 HIS A CA  1 
ATOM   1748 C C   . HIS A 1 228 ? 2.83066  10.08558 -6.82070  1.000 90.19679  ? 228 HIS A C   1 
ATOM   1749 O O   . HIS A 1 228 ? 3.47067  9.10614  -7.21469  1.000 88.15261  ? 228 HIS A O   1 
ATOM   1750 C CB  . HIS A 1 228 ? 4.36658  11.78787 -5.81115  1.000 87.15580  ? 228 HIS A CB  1 
ATOM   1751 C CG  . HIS A 1 228 ? 4.63198  12.73173 -4.68017  1.000 87.83082  ? 228 HIS A CG  1 
ATOM   1752 N ND1 . HIS A 1 228 ? 4.32299  14.07355 -4.74392  1.000 89.41692  ? 228 HIS A ND1 1 
ATOM   1753 C CD2 . HIS A 1 228 ? 5.16343  12.52606 -3.45148  1.000 86.71676  ? 228 HIS A CD2 1 
ATOM   1754 C CE1 . HIS A 1 228 ? 4.65944  14.65502 -3.60598  1.000 88.76670  ? 228 HIS A CE1 1 
ATOM   1755 N NE2 . HIS A 1 228 ? 5.17296  13.73844 -2.80552  1.000 87.02828  ? 228 HIS A NE2 1 
ATOM   1756 N N   . ARG A 1 229 ? 1.77289  10.56867 -7.46253  1.000 94.19570  ? 229 ARG A N   1 
ATOM   1757 C CA  . ARG A 1 229 ? 1.21958  9.94346  -8.65215  1.000 97.30741  ? 229 ARG A CA  1 
ATOM   1758 C C   . ARG A 1 229 ? 1.43594  10.84618 -9.85876  1.000 97.38215  ? 229 ARG A C   1 
ATOM   1759 O O   . ARG A 1 229 ? 1.31786  12.07157 -9.75600  1.000 98.21448  ? 229 ARG A O   1 
ATOM   1760 C CB  . ARG A 1 229 ? -0.27287 9.65994  -8.47230  1.000 102.84921 ? 229 ARG A CB  1 
ATOM   1761 C CG  . ARG A 1 229 ? -0.78575 8.51271  -9.31917  1.000 106.12648 ? 229 ARG A CG  1 
ATOM   1762 C CD  . ARG A 1 229 ? -0.59980 7.18333  -8.60926  1.000 106.26617 ? 229 ARG A CD  1 
ATOM   1763 N NE  . ARG A 1 229 ? -1.53269 7.03791  -7.49901  0.780 109.40666 ? 229 ARG A NE  1 
ATOM   1764 C CZ  . ARG A 1 229 ? -1.67217 5.93559  -6.77611  0.880 110.44550 ? 229 ARG A CZ  1 
ATOM   1765 N NH1 . ARG A 1 229 ? -0.93949 4.85855  -7.00972  1.000 108.71218 ? 229 ARG A NH1 1 
ATOM   1766 N NH2 . ARG A 1 229 ? -2.57186 5.91212  -5.79671  0.890 113.48394 ? 229 ARG A NH2 1 
ATOM   1767 N N   . ASP A 1 230 ? 1.75241  10.23041 -10.99728 1.000 96.57961  ? 230 ASP A N   1 
ATOM   1768 C CA  . ASP A 1 230 ? 1.93617  10.92710 -12.27112 1.000 96.43542  ? 230 ASP A CA  1 
ATOM   1769 C C   . ASP A 1 230 ? 2.95697  12.05883 -12.13803 1.000 92.99231  ? 230 ASP A C   1 
ATOM   1770 O O   . ASP A 1 230 ? 2.65959  13.23868 -12.33871 1.000 95.03966  ? 230 ASP A O   1 
ATOM   1771 C CB  . ASP A 1 230 ? 0.59787  11.44537 -12.80598 1.000 100.86282 ? 230 ASP A CB  1 
ATOM   1772 C CG  . ASP A 1 230 ? 0.71918  12.05507 -14.19088 1.000 101.63420 ? 230 ASP A CG  1 
ATOM   1773 O OD1 . ASP A 1 230 ? 1.19183  11.35423 -15.11164 1.000 101.06326 ? 230 ASP A OD1 1 
ATOM   1774 O OD2 . ASP A 1 230 ? 0.34313  13.23564 -14.35498 1.000 103.03818 ? 230 ASP A OD2 1 
ATOM   1775 N N   . VAL A 1 231 ? 4.18187  11.66956 -11.79506 1.000 87.90041  ? 231 VAL A N   1 
ATOM   1776 C CA  . VAL A 1 231 ? 5.26905  12.61273 -11.55878 1.000 84.20548  ? 231 VAL A CA  1 
ATOM   1777 C C   . VAL A 1 231 ? 5.97090  12.90461 -12.87659 1.000 82.88018  ? 231 VAL A C   1 
ATOM   1778 O O   . VAL A 1 231 ? 6.31009  11.98334 -13.62902 1.000 82.77321  ? 231 VAL A O   1 
ATOM   1779 C CB  . VAL A 1 231 ? 6.25946  12.05764 -10.52275 1.000 80.87367  ? 231 VAL A CB  1 
ATOM   1780 C CG1 . VAL A 1 231 ? 7.36206  13.06823 -10.24313 1.000 78.12602  ? 231 VAL A CG1 1 
ATOM   1781 C CG2 . VAL A 1 231 ? 5.52816  11.68165 -9.24511  1.000 82.05407  ? 231 VAL A CG2 1 
ATOM   1782 N N   . GLN A 1 232 ? 6.19203  14.18807 -13.15656 1.000 82.14246  ? 232 GLN A N   1 
ATOM   1783 C CA  . GLN A 1 232 ? 6.92105  14.60345 -14.34768 1.000 79.87987  ? 232 GLN A CA  1 
ATOM   1784 C C   . GLN A 1 232 ? 8.36299  14.98716 -14.06066 1.000 75.27992  ? 232 GLN A C   1 
ATOM   1785 O O   . GLN A 1 232 ? 9.22572  14.80129 -14.92633 1.000 74.38951  ? 232 GLN A O   1 
ATOM   1786 C CB  . GLN A 1 232 ? 6.21493  15.78511 -15.02144 1.000 82.79206  ? 232 GLN A CB  1 
ATOM   1787 N N   . GLU A 1 233 ? 8.65296  15.49759 -12.86504 1.000 72.25503  ? 233 GLU A N   1 
ATOM   1788 C CA  . GLU A 1 233 ? 10.00090 15.94803 -12.55575 1.000 68.43695  ? 233 GLU A CA  1 
ATOM   1789 C C   . GLU A 1 233 ? 10.16855 16.09829 -11.04985 1.000 66.08728  ? 233 GLU A C   1 
ATOM   1790 O O   . GLU A 1 233 ? 9.23498  16.50306 -10.35233 1.000 67.90118  ? 233 GLU A O   1 
ATOM   1791 C CB  . GLU A 1 233 ? 10.30612 17.27768 -13.25248 1.000 70.17108  ? 233 GLU A CB  1 
ATOM   1792 C CG  . GLU A 1 233 ? 11.76228 17.65909 -13.20955 1.000 68.54815  ? 233 GLU A CG  1 
ATOM   1793 C CD  . GLU A 1 233 ? 12.01828 19.04916 -13.73406 1.000 70.07377  ? 233 GLU A CD  1 
ATOM   1794 O OE1 . GLU A 1 233 ? 11.03548 19.78409 -13.96241 1.000 72.96592  ? 233 GLU A OE1 1 
ATOM   1795 O OE2 . GLU A 1 233 ? 13.20346 19.40300 -13.91540 1.000 68.59267  ? 233 GLU A OE2 1 
ATOM   1796 N N   . ILE A 1 234 ? 11.36546 15.76819 -10.56486 1.000 62.17632  ? 234 ILE A N   1 
ATOM   1797 C CA  . ILE A 1 234 ? 11.78090 15.99829 -9.18391  1.000 60.05692  ? 234 ILE A CA  1 
ATOM   1798 C C   . ILE A 1 234 ? 13.04154 16.84966 -9.23257  1.000 58.53992  ? 234 ILE A C   1 
ATOM   1799 O O   . ILE A 1 234 ? 14.05498 16.43023 -9.80769  1.000 57.36211  ? 234 ILE A O   1 
ATOM   1800 C CB  . ILE A 1 234 ? 12.05023 14.68574 -8.42887  1.000 58.06502  ? 234 ILE A CB  1 
ATOM   1801 C CG1 . ILE A 1 234 ? 10.78839 13.83311 -8.31919  1.000 59.41745  ? 234 ILE A CG1 1 
ATOM   1802 C CG2 . ILE A 1 234 ? 12.60855 14.97048 -7.04022  1.000 57.06101  ? 234 ILE A CG2 1 
ATOM   1803 C CD1 . ILE A 1 234 ? 11.04688 12.47740 -7.70072  1.000 57.77084  ? 234 ILE A CD1 1 
ATOM   1804 N N   . ARG A 1 235 ? 12.98761 18.03632 -8.63568  1.000 58.69101  ? 235 ARG A N   1 
ATOM   1805 C CA  . ARG A 1 235 ? 14.10949 18.96615 -8.65711  1.000 56.99079  ? 235 ARG A CA  1 
ATOM   1806 C C   . ARG A 1 235 ? 14.70507 19.10134 -7.26150  1.000 54.93059  ? 235 ARG A C   1 
ATOM   1807 O O   . ARG A 1 235 ? 13.97511 19.28387 -6.28221  1.000 56.08192  ? 235 ARG A O   1 
ATOM   1808 C CB  . ARG A 1 235 ? 13.68143 20.33819 -9.18388  0.800 59.17585  ? 235 ARG A CB  1 
ATOM   1809 C CG  . ARG A 1 235 ? 12.93489 20.28643 -10.50048 0.700 61.30500  ? 235 ARG A CG  1 
ATOM   1810 C CD  . ARG A 1 235 ? 13.42417 21.36709 -11.44851 0.600 62.43630  ? 235 ARG A CD  1 
ATOM   1811 N NE  . ARG A 1 235 ? 13.51933 22.67039 -10.80394 0.500 63.28827  ? 235 ARG A NE  1 
ATOM   1812 C CZ  . ARG A 1 235 ? 14.04403 23.74720 -11.37171 0.500 64.43202  ? 235 ARG A CZ  1 
ATOM   1813 N NH1 . ARG A 1 235 ? 14.53021 23.71192 -12.60357 0.500 64.73735  ? 235 ARG A NH1 1 
ATOM   1814 N NH2 . ARG A 1 235 ? 14.08501 24.88649 -10.68580 0.500 65.53005  ? 235 ARG A NH2 1 
ATOM   1815 N N   . TYR A 1 236 ? 16.02905 19.01553 -7.18277  1.000 52.21272  ? 236 TYR A N   1 
ATOM   1816 C CA  . TYR A 1 236 ? 16.78198 19.21734 -5.95483  1.000 51.17096  ? 236 TYR A CA  1 
ATOM   1817 C C   . TYR A 1 236 ? 17.72222 20.39851 -6.12556  1.000 51.56277  ? 236 TYR A C   1 
ATOM   1818 O O   . TYR A 1 236 ? 18.38738 20.53040 -7.15897  1.000 50.65524  ? 236 TYR A O   1 
ATOM   1819 C CB  . TYR A 1 236 ? 17.60421 17.98273 -5.58707  1.000 48.53028  ? 236 TYR A CB  1 
ATOM   1820 C CG  . TYR A 1 236 ? 16.78580 16.78923 -5.19677  0.700 48.75958  ? 236 TYR A CG  1 
ATOM   1821 C CD1 . TYR A 1 236 ? 16.01033 16.81248 -4.05335  0.700 50.06732  ? 236 TYR A CD1 1 
ATOM   1822 C CD2 . TYR A 1 236 ? 16.80411 15.62997 -5.95390  0.700 48.43343  ? 236 TYR A CD2 1 
ATOM   1823 C CE1 . TYR A 1 236 ? 15.26892 15.72699 -3.68107  0.700 50.63566  ? 236 TYR A CE1 1 
ATOM   1824 C CE2 . TYR A 1 236 ? 16.05793 14.53166 -5.58535  0.700 49.03025  ? 236 TYR A CE2 1 
ATOM   1825 C CZ  . TYR A 1 236 ? 15.29588 14.58978 -4.44800  0.700 50.45235  ? 236 TYR A CZ  1 
ATOM   1826 O OH  . TYR A 1 236 ? 14.54739 13.51256 -4.06050  0.700 52.24555  ? 236 TYR A OH  1 
ATOM   1827 N N   . GLU A 1 237 ? 17.78997 21.24125 -5.09981  1.000 52.99789  ? 237 GLU A N   1 
ATOM   1828 C CA  . GLU A 1 237 ? 18.73669 22.34565 -5.09454  1.000 53.02274  ? 237 GLU A CA  1 
ATOM   1829 C C   . GLU A 1 237 ? 18.91475 22.81979 -3.66486  1.000 53.04240  ? 237 GLU A C   1 
ATOM   1830 O O   . GLU A 1 237 ? 18.04071 22.61728 -2.81789  1.000 53.68756  ? 237 GLU A O   1 
ATOM   1831 C CB  . GLU A 1 237 ? 18.26762 23.49726 -5.98522  1.000 54.74489  ? 237 GLU A CB  1 
ATOM   1832 C CG  . GLU A 1 237 ? 16.82935 23.87341 -5.76151  1.000 56.88856  ? 237 GLU A CG  1 
ATOM   1833 C CD  . GLU A 1 237 ? 16.31381 24.83948 -6.80468  0.400 59.66621  ? 237 GLU A CD  1 
ATOM   1834 O OE1 . GLU A 1 237 ? 17.10133 25.68246 -7.27771  1.000 60.47704  ? 237 GLU A OE1 1 
ATOM   1835 O OE2 . GLU A 1 237 ? 15.12151 24.75234 -7.15916  0.810 61.54944  ? 237 GLU A OE2 1 
ATOM   1836 N N   . VAL A 1 238 ? 20.05966 23.44423 -3.40234  1.000 52.53240  ? 238 VAL A N   1 
ATOM   1837 C CA  . VAL A 1 238 ? 20.28674 24.00709 -2.08095  1.000 53.32578  ? 238 VAL A CA  1 
ATOM   1838 C C   . VAL A 1 238 ? 19.28262 25.12642 -1.85876  1.000 56.64884  ? 238 VAL A C   1 
ATOM   1839 O O   . VAL A 1 238 ? 19.15808 26.04567 -2.67861  1.000 58.71086  ? 238 VAL A O   1 
ATOM   1840 C CB  . VAL A 1 238 ? 21.72898 24.49387 -1.93173  1.000 52.63468  ? 238 VAL A CB  1 
ATOM   1841 C CG1 . VAL A 1 238 ? 21.91311 25.17611 -0.56908  1.000 53.94438  ? 238 VAL A CG1 1 
ATOM   1842 C CG2 . VAL A 1 238 ? 22.69237 23.32422 -2.07250  1.000 50.11063  ? 238 VAL A CG2 1 
ATOM   1843 N N   . SER A 1 239 ? 18.54259 25.03909 -0.75865  1.000 58.06596  ? 239 SER A N   1 
ATOM   1844 C CA  . SER A 1 239 ? 17.53487 26.04126 -0.45409  1.000 59.72799  ? 239 SER A CA  1 
ATOM   1845 C C   . SER A 1 239 ? 18.17994 27.39831 -0.19634  1.000 61.90416  ? 239 SER A C   1 
ATOM   1846 O O   . SER A 1 239 ? 19.34515 27.49701 0.19799   1.000 62.31784  ? 239 SER A O   1 
ATOM   1847 C CB  . SER A 1 239 ? 16.71051 25.61755 0.76375   1.000 57.70814  ? 239 SER A CB  1 
ATOM   1848 O OG  . SER A 1 239 ? 15.86011 26.67114 1.19896   1.000 59.33836  ? 239 SER A OG  1 
ATOM   1849 N N   . ALA A 1 240 ? 17.41154 28.45629 -0.45022  1.000 64.29048  ? 240 ALA A N   1 
ATOM   1850 C CA  . ALA A 1 240 ? 17.82707 29.78362 -0.02710  1.000 66.08929  ? 240 ALA A CA  1 
ATOM   1851 C C   . ALA A 1 240 ? 17.56192 30.01353 1.45548   1.000 64.82739  ? 240 ALA A C   1 
ATOM   1852 O O   . ALA A 1 240 ? 18.19241 30.89280 2.05619   1.000 67.15045  ? 240 ALA A O   1 
ATOM   1853 C CB  . ALA A 1 240 ? 17.11998 30.85159 -0.86786  1.000 69.25018  ? 240 ALA A CB  1 
ATOM   1854 N N   . LYS A 1 241 ? 16.65708 29.23782 2.05340   1.000 61.40759  ? 241 LYS A N   1 
ATOM   1855 C CA  . LYS A 1 241 ? 16.35539 29.35374 3.47191   1.000 61.62589  ? 241 LYS A CA  1 
ATOM   1856 C C   . LYS A 1 241 ? 17.33708 28.52745 4.29416   1.000 60.37599  ? 241 LYS A C   1 
ATOM   1857 O O   . LYS A 1 241 ? 17.89698 27.53783 3.81640   1.000 58.74159  ? 241 LYS A O   1 
ATOM   1858 C CB  . LYS A 1 241 ? 14.92693 28.88689 3.75313   0.800 60.95576  ? 241 LYS A CB  1 
ATOM   1859 C CG  . LYS A 1 241 ? 13.87029 29.50915 2.85387   0.700 63.88335  ? 241 LYS A CG  1 
ATOM   1860 C CD  . LYS A 1 241 ? 12.58350 28.70113 2.88416   0.600 62.90905  ? 241 LYS A CD  1 
ATOM   1861 C CE  . LYS A 1 241 ? 11.57786 29.22207 1.87463   0.500 64.59552  ? 241 LYS A CE  1 
ATOM   1862 N NZ  . LYS A 1 241 ? 10.36426 28.36502 1.81105   0.500 63.39559  ? 241 LYS A NZ  1 
ATOM   1863 N N   . LYS A 1 242 ? 17.53231 28.93736 5.55041   1.000 62.01401  ? 242 LYS A N   1 
ATOM   1864 C CA  . LYS A 1 242 ? 18.46596 28.28124 6.45705   1.000 59.33675  ? 242 LYS A CA  1 
ATOM   1865 C C   . LYS A 1 242 ? 17.82938 28.13885 7.83231   1.000 58.34138  ? 242 LYS A C   1 
ATOM   1866 O O   . LYS A 1 242 ? 17.07041 29.01386 8.26403   1.000 60.39888  ? 242 LYS A O   1 
ATOM   1867 C CB  . LYS A 1 242 ? 19.78025 29.07125 6.57186   0.700 61.22299  ? 242 LYS A CB  1 
ATOM   1868 C CG  . LYS A 1 242 ? 20.43955 29.40115 5.23621   0.600 62.21388  ? 242 LYS A CG  1 
ATOM   1869 C CD  . LYS A 1 242 ? 21.70751 30.22426 5.41778   0.500 65.36542  ? 242 LYS A CD  1 
ATOM   1870 C CE  . LYS A 1 242 ? 22.86290 29.36388 5.89773   0.500 64.64836  ? 242 LYS A CE  1 
ATOM   1871 N NZ  . LYS A 1 242 ? 23.23322 28.33761 4.88299   0.500 63.48292  ? 242 LYS A NZ  1 
ATOM   1872 N N   . ILE A 1 243 ? 18.13626 27.03621 8.52131   1.000 54.94938  ? 243 ILE A N   1 
ATOM   1873 C CA  . ILE A 1 243 ? 17.66157 26.83292 9.88751   1.000 54.99170  ? 243 ILE A CA  1 
ATOM   1874 C C   . ILE A 1 243 ? 18.66937 27.43970 10.85163  1.000 57.07044  ? 243 ILE A C   1 
ATOM   1875 O O   . ILE A 1 243 ? 19.88207 27.25205 10.70432  1.000 57.50178  ? 243 ILE A O   1 
ATOM   1876 C CB  . ILE A 1 243 ? 17.42641 25.34345 10.19906  1.000 52.34018  ? 243 ILE A CB  1 
ATOM   1877 C CG1 . ILE A 1 243 ? 16.88361 25.19882 11.62915  1.000 53.43034  ? 243 ILE A CG1 1 
ATOM   1878 C CG2 . ILE A 1 243 ? 18.69775 24.52567 10.01497  1.000 50.47499  ? 243 ILE A CG2 1 
ATOM   1879 C CD1 . ILE A 1 243 ? 16.60846 23.77650 12.06322  1.000 51.97473  ? 243 ILE A CD1 1 
ATOM   1880 N N   . HIS A 1 244 ? 18.16944 28.18019 11.83202  1.000 58.87526  ? 244 HIS A N   1 
ATOM   1881 C CA  . HIS A 1 244 ? 19.00341 28.87378 12.80228  1.000 61.53298  ? 244 HIS A CA  1 
ATOM   1882 C C   . HIS A 1 244 ? 18.95004 28.14547 14.13906  1.000 62.40503  ? 244 HIS A C   1 
ATOM   1883 O O   . HIS A 1 244 ? 17.86339 27.87711 14.66254  1.000 62.04407  ? 244 HIS A O   1 
ATOM   1884 C CB  . HIS A 1 244 ? 18.55551 30.33073 12.96270  1.000 64.61930  ? 244 HIS A CB  1 
ATOM   1885 C CG  . HIS A 1 244 ? 18.50115 31.08903 11.67086  0.700 65.11694  ? 244 HIS A CG  1 
ATOM   1886 N ND1 . HIS A 1 244 ? 19.62192 31.62214 11.06997  0.700 66.37170  ? 244 HIS A ND1 1 
ATOM   1887 C CD2 . HIS A 1 244 ? 17.45732 31.41184 10.87060  0.700 65.33516  ? 244 HIS A CD2 1 
ATOM   1888 C CE1 . HIS A 1 244 ? 19.27126 32.23706 9.95387   0.700 67.46224  ? 244 HIS A CE1 1 
ATOM   1889 N NE2 . HIS A 1 244 ? 17.96361 32.12272 9.80890   0.700 66.77007  ? 244 HIS A NE2 1 
ATOM   1890 N N   . PHE A 1 245 ? 20.11991 27.82296 14.68319  1.000 64.37553  ? 245 PHE A N   1 
ATOM   1891 C CA  . PHE A 1 245 ? 20.23505 27.26983 16.02408  1.000 66.25705  ? 245 PHE A CA  1 
ATOM   1892 C C   . PHE A 1 245 ? 20.70055 28.35138 16.98716  1.000 72.67135  ? 245 PHE A C   1 
ATOM   1893 O O   . PHE A 1 245 ? 21.42060 29.27886 16.60740  1.000 74.23158  ? 245 PHE A O   1 
ATOM   1894 C CB  . PHE A 1 245 ? 21.22122 26.09746 16.08250  1.000 62.64562  ? 245 PHE A CB  1 
ATOM   1895 C CG  . PHE A 1 245 ? 20.81194 24.91267 15.26631  1.000 58.36866  ? 245 PHE A CG  1 
ATOM   1896 C CD1 . PHE A 1 245 ? 21.10069 24.85702 13.91320  1.000 56.52796  ? 245 PHE A CD1 1 
ATOM   1897 C CD2 . PHE A 1 245 ? 20.15580 23.84506 15.85215  1.000 57.09183  ? 245 PHE A CD2 1 
ATOM   1898 C CE1 . PHE A 1 245 ? 20.72978 23.76488 13.15613  1.000 54.01908  ? 245 PHE A CE1 1 
ATOM   1899 C CE2 . PHE A 1 245 ? 19.78404 22.74805 15.09821  1.000 54.72997  ? 245 PHE A CE2 1 
ATOM   1900 C CZ  . PHE A 1 245 ? 20.07017 22.70882 13.75235  1.000 53.17838  ? 245 PHE A CZ  1 
ATOM   1901 N N   . ALA A 1 246 ? 20.27909 28.22512 18.24016  1.000 77.37397  ? 246 ALA A N   1 
ATOM   1902 C CA  . ALA A 1 246 ? 20.79704 29.04546 19.32659  1.000 84.15088  ? 246 ALA A CA  1 
ATOM   1903 C C   . ALA A 1 246 ? 21.89389 28.24531 20.01592  1.000 87.03447  ? 246 ALA A C   1 
ATOM   1904 O O   . ALA A 1 246 ? 21.62483 27.19656 20.60933  1.000 85.58443  ? 246 ALA A O   1 
ATOM   1905 C CB  . ALA A 1 246 ? 19.69045 29.43068 20.30594  1.000 86.94713  ? 246 ALA A CB  1 
ATOM   1906 N N   . ARG A 1 247 ? 23.12837 28.72461 19.92342  1.000 92.23729  ? 247 ARG A N   1 
ATOM   1907 C CA  . ARG A 1 247 ? 24.26680 28.05079 20.52733  1.000 96.17503  ? 247 ARG A CA  1 
ATOM   1908 C C   . ARG A 1 247 ? 24.76535 28.84737 21.72402  1.000 104.32179 ? 247 ARG A C   1 
ATOM   1909 O O   . ARG A 1 247 ? 24.87968 30.07678 21.66366  1.000 108.91562 ? 247 ARG A O   1 
ATOM   1910 C CB  . ARG A 1 247 ? 25.39579 27.85471 19.51229  0.700 94.46372  ? 247 ARG A CB  1 
ATOM   1911 C CG  . ARG A 1 247 ? 25.08015 26.83441 18.42569  0.700 89.49661  ? 247 ARG A CG  1 
ATOM   1912 C CD  . ARG A 1 247 ? 25.29498 25.40086 18.89959  0.700 86.70036  ? 247 ARG A CD  1 
ATOM   1913 N NE  . ARG A 1 247 ? 25.01561 24.42543 17.84912  0.700 82.07179  ? 247 ARG A NE  1 
ATOM   1914 C CZ  . ARG A 1 247 ? 23.98800 23.58691 17.85851  0.700 79.16423  ? 247 ARG A CZ  1 
ATOM   1915 N NH1 . ARG A 1 247 ? 23.12604 23.56221 18.86320  0.700 80.63182  ? 247 ARG A NH1 1 
ATOM   1916 N NH2 . ARG A 1 247 ? 23.82726 22.74569 16.84063  0.700 75.42353  ? 247 ARG A NH2 1 
ATOM   1917 N N   . PHE A 1 248 ? 25.05094 28.13526 22.81405  1.000 107.64592 ? 248 PHE A N   1 
ATOM   1918 C CA  . PHE A 1 248 ? 25.56286 28.74525 24.03653  1.000 114.70623 ? 248 PHE A CA  1 
ATOM   1919 C C   . PHE A 1 248 ? 26.97183 28.26658 24.35381  1.000 114.77282 ? 248 PHE A C   1 
ATOM   1920 O O   . PHE A 1 248 ? 27.88416 29.08920 24.48581  1.000 119.44862 ? 248 PHE A O   1 
ATOM   1921 C CB  . PHE A 1 248 ? 24.61310 28.45501 25.20487  1.000 118.48780 ? 248 PHE A CB  1 
ATOM   1922 C CG  . PHE A 1 248 ? 23.23749 29.01424 25.01109  0.700 120.89532 ? 248 PHE A CG  1 
ATOM   1923 C CD1 . PHE A 1 248 ? 22.25326 28.26541 24.38894  0.700 117.93447 ? 248 PHE A CD1 1 
ATOM   1924 C CD2 . PHE A 1 248 ? 22.93082 30.29422 25.43868  0.700 126.95823 ? 248 PHE A CD2 1 
ATOM   1925 C CE1 . PHE A 1 248 ? 20.98674 28.78111 24.20394  0.700 119.54067 ? 248 PHE A CE1 1 
ATOM   1926 C CE2 . PHE A 1 248 ? 21.66591 30.81447 25.25592  0.700 128.51132 ? 248 PHE A CE2 1 
ATOM   1927 C CZ  . PHE A 1 248 ? 20.69364 30.05768 24.63947  0.700 124.64829 ? 248 PHE A CZ  1 
ATOM   1928 N N   . ARG A 1 249 ? 27.17731 26.96263 24.48626  1.000 110.74199 ? 249 ARG A N   1 
ATOM   1929 C CA  . ARG A 1 249 ? 28.51386 26.41108 24.62194  1.000 111.35687 ? 249 ARG A CA  1 
ATOM   1930 C C   . ARG A 1 249 ? 29.06169 26.00936 23.25317  1.000 102.05819 ? 249 ARG A C   1 
ATOM   1931 O O   . ARG A 1 249 ? 28.33347 25.90148 22.26289  1.000 98.96440  ? 249 ARG A O   1 
ATOM   1932 C CB  . ARG A 1 249 ? 28.50894 25.21169 25.57165  1.000 114.29740 ? 249 ARG A CB  1 
ATOM   1933 N N   . SER A 1 250 ? 30.37176 25.79432 23.21017  1.000 96.38509  ? 250 SER A N   1 
ATOM   1934 C CA  . SER A 1 250 ? 31.04449 25.28385 22.02599  1.000 86.47816  ? 250 SER A CA  1 
ATOM   1935 C C   . SER A 1 250 ? 30.86112 23.77385 21.95606  1.000 77.83049  ? 250 SER A C   1 
ATOM   1936 O O   . SER A 1 250 ? 31.35193 23.04390 22.82534  1.000 77.79476  ? 250 SER A O   1 
ATOM   1937 C CB  . SER A 1 250 ? 32.52901 25.63664 22.06479  1.000 86.70999  ? 250 SER A CB  1 
ATOM   1938 O OG  . SER A 1 250 ? 33.28350 24.74727 21.25322  0.920 82.81679  ? 250 SER A OG  1 
ATOM   1939 N N   . PHE A 1 251 ? 30.15886 23.30823 20.92659  1.000 71.91328  ? 251 PHE A N   1 
ATOM   1940 C CA  . PHE A 1 251 ? 30.01811 21.88195 20.63853  1.000 67.38240  ? 251 PHE A CA  1 
ATOM   1941 C C   . PHE A 1 251 ? 30.28014 21.70235 19.14869  1.000 64.40491  ? 251 PHE A C   1 
ATOM   1942 O O   . PHE A 1 251 ? 29.34217 21.67636 18.34007  1.000 62.20694  ? 251 PHE A O   1 
ATOM   1943 C CB  . PHE A 1 251 ? 28.63646 21.36305 21.04319  1.000 65.75360  ? 251 PHE A CB  1 
ATOM   1944 C CG  . PHE A 1 251 ? 28.57095 19.86610 21.23806  1.000 63.97767  ? 251 PHE A CG  1 
ATOM   1945 C CD1 . PHE A 1 251 ? 29.69665 19.07331 21.07688  1.000 63.34236  ? 251 PHE A CD1 1 
ATOM   1946 C CD2 . PHE A 1 251 ? 27.37495 19.25223 21.57653  1.000 63.26410  ? 251 PHE A CD2 1 
ATOM   1947 C CE1 . PHE A 1 251 ? 29.63142 17.69845 21.25555  1.000 61.43500  ? 251 PHE A CE1 1 
ATOM   1948 C CE2 . PHE A 1 251 ? 27.30397 17.87757 21.75429  1.000 61.59567  ? 251 PHE A CE2 1 
ATOM   1949 C CZ  . PHE A 1 251 ? 28.43535 17.10202 21.59484  1.000 60.66818  ? 251 PHE A CZ  1 
ATOM   1950 N N   . PRO A 1 252 ? 31.55002 21.59695 18.74803  1.000 64.73189  ? 252 PRO A N   1 
ATOM   1951 C CA  . PRO A 1 252 ? 31.86821 21.49852 17.31713  1.000 62.52115  ? 252 PRO A CA  1 
ATOM   1952 C C   . PRO A 1 252 ? 31.23289 20.27912 16.67199  1.000 57.68730  ? 252 PRO A C   1 
ATOM   1953 O O   . PRO A 1 252 ? 31.04715 19.23669 17.30347  1.000 56.00287  ? 252 PRO A O   1 
ATOM   1954 C CB  . PRO A 1 252 ? 33.39881 21.40113 17.29735  1.000 64.97280  ? 252 PRO A CB  1 
ATOM   1955 C CG  . PRO A 1 252 ? 33.83202 22.07255 18.57071  1.000 69.08454  ? 252 PRO A CG  1 
ATOM   1956 C CD  . PRO A 1 252 ? 32.76422 21.72157 19.57786  1.000 68.08363  ? 252 PRO A CD  1 
ATOM   1957 N N   . PHE A 1 253 ? 30.90131 20.43187 15.38782  1.000 56.13158  ? 253 PHE A N   1 
ATOM   1958 C CA  . PHE A 1 253 ? 30.29242 19.34389 14.62898  1.000 52.09400  ? 253 PHE A CA  1 
ATOM   1959 C C   . PHE A 1 253 ? 31.12650 18.07316 14.70574  1.000 49.94907  ? 253 PHE A C   1 
ATOM   1960 O O   . PHE A 1 253 ? 30.58705 16.97886 14.90232  1.000 47.37899  ? 253 PHE A O   1 
ATOM   1961 C CB  . PHE A 1 253 ? 30.11313 19.76798 13.17238  1.000 52.41736  ? 253 PHE A CB  1 
ATOM   1962 C CG  . PHE A 1 253 ? 29.46915 18.72104 12.30601  1.000 50.67225  ? 253 PHE A CG  1 
ATOM   1963 C CD1 . PHE A 1 253 ? 28.10031 18.51989 12.34768  1.000 49.45054  ? 253 PHE A CD1 1 
ATOM   1964 C CD2 . PHE A 1 253 ? 30.22656 17.95758 11.43243  1.000 51.09873  ? 253 PHE A CD2 1 
ATOM   1965 C CE1 . PHE A 1 253 ? 27.49287 17.57188 11.54955  1.000 48.13636  ? 253 PHE A CE1 1 
ATOM   1966 C CE2 . PHE A 1 253 ? 29.62637 17.00444 10.62638  1.000 50.08455  ? 253 PHE A CE2 1 
ATOM   1967 C CZ  . PHE A 1 253 ? 28.25043 16.81050 10.69009  1.000 48.61520  ? 253 PHE A CZ  1 
ATOM   1968 N N   . TRP A 1 254 ? 32.44671 18.19513 14.55551  1.000 51.41773  ? 254 TRP A N   1 
ATOM   1969 C CA  . TRP A 1 254 ? 33.28344 17.00077 14.53591  1.000 51.38037  ? 254 TRP A CA  1 
ATOM   1970 C C   . TRP A 1 254 ? 33.37479 16.35370 15.91601  1.000 52.08711  ? 254 TRP A C   1 
ATOM   1971 O O   . TRP A 1 254 ? 33.52864 15.13034 16.02005  1.000 51.14064  ? 254 TRP A O   1 
ATOM   1972 C CB  . TRP A 1 254 ? 34.67384 17.33824 13.99688  1.000 53.78934  ? 254 TRP A CB  1 
ATOM   1973 C CG  . TRP A 1 254 ? 34.70131 17.82957 12.55363  1.000 54.11673  ? 254 TRP A CG  1 
ATOM   1974 C CD1 . TRP A 1 254 ? 35.19782 19.02156 12.10645  1.000 57.05947  ? 254 TRP A CD1 1 
ATOM   1975 C CD2 . TRP A 1 254 ? 34.22663 17.13531 11.38523  1.000 51.91033  ? 254 TRP A CD2 1 
ATOM   1976 N NE1 . TRP A 1 254 ? 35.06863 19.11199 10.74063  1.000 56.83377  ? 254 TRP A NE1 1 
ATOM   1977 C CE2 . TRP A 1 254 ? 34.47318 17.96937 10.27443  1.000 53.65704  ? 254 TRP A CE2 1 
ATOM   1978 C CE3 . TRP A 1 254 ? 33.62487 15.89069 11.17100  1.000 49.37268  ? 254 TRP A CE3 1 
ATOM   1979 C CZ2 . TRP A 1 254 ? 34.13618 17.60024 8.97278   1.000 52.56385  ? 254 TRP A CZ2 1 
ATOM   1980 C CZ3 . TRP A 1 254 ? 33.28794 15.52709 9.87425   1.000 48.51985  ? 254 TRP A CZ3 1 
ATOM   1981 C CH2 . TRP A 1 254 ? 33.54642 16.37818 8.79504   1.000 50.08192  ? 254 TRP A CH2 1 
ATOM   1982 N N   . ARG A 1 255 ? 33.27730 17.14024 16.98600  1.000 54.05055  ? 255 ARG A N   1 
ATOM   1983 C CA  . ARG A 1 255 ? 33.13261 16.52290 18.29797  1.000 54.76813  ? 255 ARG A CA  1 
ATOM   1984 C C   . ARG A 1 255 ? 31.81367 15.76841 18.39477  1.000 52.24839  ? 255 ARG A C   1 
ATOM   1985 O O   . ARG A 1 255 ? 31.76218 14.65215 18.92670  1.000 51.45795  ? 255 ARG A O   1 
ATOM   1986 C CB  . ARG A 1 255 ? 33.22639 17.57644 19.39974  0.900 57.75299  ? 255 ARG A CB  1 
ATOM   1987 C CG  . ARG A 1 255 ? 32.97938 17.01506 20.78199  0.800 58.75002  ? 255 ARG A CG  1 
ATOM   1988 C CD  . ARG A 1 255 ? 33.47111 17.95064 21.86613  0.700 62.87751  ? 255 ARG A CD  1 
ATOM   1989 N NE  . ARG A 1 255 ? 34.91509 18.13964 21.81117  0.600 65.64513  ? 255 ARG A NE  1 
ATOM   1990 C CZ  . ARG A 1 255 ? 35.80416 17.22038 22.16275  0.500 66.67614  ? 255 ARG A CZ  1 
ATOM   1991 N NH1 . ARG A 1 255 ? 35.43369 16.00171 22.52250  0.500 65.18973  ? 255 ARG A NH1 1 
ATOM   1992 N NH2 . ARG A 1 255 ? 37.09729 17.53263 22.15889  0.500 69.59102  ? 255 ARG A NH2 1 
ATOM   1993 N N   . ARG A 1 256 ? 30.73847 16.36477 17.87860  1.000 51.42710  ? 256 ARG A N   1 
ATOM   1994 C CA  . ARG A 1 256 ? 29.44667 15.68897 17.84948  1.000 50.43495  ? 256 ARG A CA  1 
ATOM   1995 C C   . ARG A 1 256 ? 29.51680 14.38835 17.05536  1.000 48.02049  ? 256 ARG A C   1 
ATOM   1996 O O   . ARG A 1 256 ? 28.88532 13.39119 17.42679  1.000 47.82860  ? 256 ARG A O   1 
ATOM   1997 C CB  . ARG A 1 256 ? 28.39854 16.62612 17.25592  0.900 51.11584  ? 256 ARG A CB  1 
ATOM   1998 C CG  . ARG A 1 256 ? 26.96741 16.19128 17.45412  0.800 51.50240  ? 256 ARG A CG  1 
ATOM   1999 C CD  . ARG A 1 256 ? 26.16384 17.36703 17.95318  0.800 54.19462  ? 256 ARG A CD  1 
ATOM   2000 N NE  . ARG A 1 256 ? 26.70193 18.62498 17.44941  0.700 55.81531  ? 256 ARG A NE  1 
ATOM   2001 C CZ  . ARG A 1 256 ? 26.28478 19.22253 16.34380  0.700 55.71650  ? 256 ARG A CZ  1 
ATOM   2002 N NH1 . ARG A 1 256 ? 25.31991 18.70561 15.60335  0.700 54.50666  ? 256 ARG A NH1 1 
ATOM   2003 N NH2 . ARG A 1 256 ? 26.85004 20.36671 15.97095  0.700 57.42929  ? 256 ARG A NH2 1 
ATOM   2004 N N   . VAL A 1 257 ? 30.27511 14.38133 15.95371  1.000 46.31946  ? 257 VAL A N   1 
ATOM   2005 C CA  . VAL A 1 257 ? 30.48970 13.14522 15.20456  1.000 44.57715  ? 257 VAL A CA  1 
ATOM   2006 C C   . VAL A 1 257 ? 31.25621 12.13229 16.04833  1.000 45.97824  ? 257 VAL A C   1 
ATOM   2007 O O   . VAL A 1 257 ? 30.88140 10.95395 16.11705  1.000 46.16528  ? 257 VAL A O   1 
ATOM   2008 C CB  . VAL A 1 257 ? 31.22694 13.43010 13.88163  1.000 44.15912  ? 257 VAL A CB  1 
ATOM   2009 C CG1 . VAL A 1 257 ? 31.58682 12.12328 13.18857  1.000 43.10101  ? 257 VAL A CG1 1 
ATOM   2010 C CG2 . VAL A 1 257 ? 30.39439 14.31499 12.97011  1.000 43.25909  ? 257 VAL A CG2 1 
ATOM   2011 N N   . HIS A 1 258 ? 32.35804 12.56770 16.67678  1.000 47.15508  ? 258 HIS A N   1 
ATOM   2012 C CA  . HIS A 1 258 ? 33.16608 11.67115 17.50337  1.000 48.68359  ? 258 HIS A CA  1 
ATOM   2013 C C   . HIS A 1 258 ? 32.31932 10.98831 18.56976  1.000 49.03736  ? 258 HIS A C   1 
ATOM   2014 O O   . HIS A 1 258 ? 32.35969 9.76087  18.72839  1.000 48.97591  ? 258 HIS A O   1 
ATOM   2015 C CB  . HIS A 1 258 ? 34.31235 12.44636 18.16192  1.000 50.50006  ? 258 HIS A CB  1 
ATOM   2016 C CG  . HIS A 1 258 ? 35.04153 11.66886 19.21576  0.700 51.83330  ? 258 HIS A CG  1 
ATOM   2017 N ND1 . HIS A 1 258 ? 34.70685 11.72854 20.55344  0.700 53.24151  ? 258 HIS A ND1 1 
ATOM   2018 C CD2 . HIS A 1 258 ? 36.09157 10.81841 19.12896  0.700 52.68882  ? 258 HIS A CD2 1 
ATOM   2019 C CE1 . HIS A 1 258 ? 35.51910 10.94775 21.24397  0.700 54.97198  ? 258 HIS A CE1 1 
ATOM   2020 N NE2 . HIS A 1 258 ? 36.36683 10.38251 20.40345  0.700 54.94170  ? 258 HIS A NE2 1 
ATOM   2021 N N   . ASP A 1 259 ? 31.54528 11.77503 19.31514  1.000 50.44132  ? 259 ASP A N   1 
ATOM   2022 C CA  . ASP A 1 259 ? 30.76924 11.21273 20.41424  1.000 52.29713  ? 259 ASP A CA  1 
ATOM   2023 C C   . ASP A 1 259 ? 29.74200 10.20806 19.91586  1.000 50.57524  ? 259 ASP A C   1 
ATOM   2024 O O   . ASP A 1 259 ? 29.53295 9.16979  20.55667  1.000 50.37345  ? 259 ASP A O   1 
ATOM   2025 C CB  . ASP A 1 259 ? 30.09261 12.33547 21.19878  1.000 53.33885  ? 259 ASP A CB  1 
ATOM   2026 C CG  . ASP A 1 259 ? 31.09491 13.26272 21.85781  1.000 55.79081  ? 259 ASP A CG  1 
ATOM   2027 O OD1 . ASP A 1 259 ? 32.30543 12.94925 21.81323  1.000 56.67884  ? 259 ASP A OD1 1 
ATOM   2028 O OD2 . ASP A 1 259 ? 30.67942 14.30033 22.41679  1.000 57.58604  ? 259 ASP A OD2 1 
ATOM   2029 N N   . SER A 1 260 ? 29.13760 10.47569 18.75008  1.000 50.14833  ? 260 SER A N   1 
ATOM   2030 C CA  . SER A 1 260 ? 28.04503 9.65383  18.23876  1.000 49.90595  ? 260 SER A CA  1 
ATOM   2031 C C   . SER A 1 260 ? 28.51988 8.33643  17.63716  1.000 49.78349  ? 260 SER A C   1 
ATOM   2032 O O   . SER A 1 260 ? 27.81425 7.32670  17.75401  1.000 50.41201  ? 260 SER A O   1 
ATOM   2033 C CB  . SER A 1 260 ? 27.24290 10.43636 17.19312  1.000 48.43735  ? 260 SER A CB  1 
ATOM   2034 O OG  . SER A 1 260 ? 26.60976 11.57110 17.76845  1.000 48.35014  ? 260 SER A OG  1 
ATOM   2035 N N   . PHE A 1 261 ? 29.69336 8.31032  17.00143  1.000 49.49540  ? 261 PHE A N   1 
ATOM   2036 C CA  . PHE A 1 261 ? 30.11035 7.12299  16.26324  1.000 51.22649  ? 261 PHE A CA  1 
ATOM   2037 C C   . PHE A 1 261 ? 31.39811 6.47369  16.75533  1.000 55.69772  ? 261 PHE A C   1 
ATOM   2038 O O   . PHE A 1 261 ? 31.55094 5.26119  16.58914  1.000 58.02625  ? 261 PHE A O   1 
ATOM   2039 C CB  . PHE A 1 261 ? 30.25900 7.44900  14.76624  1.000 49.23818  ? 261 PHE A CB  1 
ATOM   2040 C CG  . PHE A 1 261 ? 28.98191 7.92679  14.12632  1.000 46.97869  ? 261 PHE A CG  1 
ATOM   2041 C CD1 . PHE A 1 261 ? 27.96144 7.03428  13.83853  1.000 46.70764  ? 261 PHE A CD1 1 
ATOM   2042 C CD2 . PHE A 1 261 ? 28.79765 9.26938  13.83534  1.000 45.41793  ? 261 PHE A CD2 1 
ATOM   2043 C CE1 . PHE A 1 261 ? 26.78429 7.47131  13.26695  1.000 45.72891  ? 261 PHE A CE1 1 
ATOM   2044 C CE2 . PHE A 1 261 ? 27.62590 9.71718  13.26232  1.000 44.00520  ? 261 PHE A CE2 1 
ATOM   2045 C CZ  . PHE A 1 261 ? 26.61564 8.81873  12.97547  1.000 44.25134  ? 261 PHE A CZ  1 
ATOM   2046 N N   . ILE A 1 262 ? 32.32509 7.22388  17.34834  1.000 57.64740  ? 262 ILE A N   1 
ATOM   2047 C CA  . ILE A 1 262 ? 33.59994 6.64002  17.75745  1.000 61.68779  ? 262 ILE A CA  1 
ATOM   2048 C C   . ILE A 1 262 ? 33.52524 6.17683  19.20786  1.000 65.93888  ? 262 ILE A C   1 
ATOM   2049 O O   . ILE A 1 262 ? 33.51170 4.97241  19.48633  1.000 68.29376  ? 262 ILE A O   1 
ATOM   2050 C CB  . ILE A 1 262 ? 34.76334 7.62746  17.56416  1.000 61.26364  ? 262 ILE A CB  1 
ATOM   2051 C CG1 . ILE A 1 262 ? 34.82892 8.10203  16.11256  1.000 59.38394  ? 262 ILE A CG1 1 
ATOM   2052 C CG2 . ILE A 1 262 ? 36.07685 6.98527  17.98795  1.000 63.73619  ? 262 ILE A CG2 1 
ATOM   2053 C CD1 . ILE A 1 262 ? 35.09242 6.99738  15.09786  1.000 58.72423  ? 262 ILE A CD1 1 
ATOM   2054 N N   . GLU A 1 263 ? 33.49069 7.12414  20.13943  1.000 68.50768  ? 263 GLU A N   1 
ATOM   2055 C CA  . GLU A 1 263 ? 33.46951 6.79281  21.56520  1.000 72.16852  ? 263 GLU A CA  1 
ATOM   2056 C C   . GLU A 1 263 ? 32.31042 7.49053  22.26884  1.000 71.94092  ? 263 GLU A C   1 
ATOM   2057 O O   . GLU A 1 263 ? 32.50698 8.45508  23.00768  1.000 72.56722  ? 263 GLU A O   1 
ATOM   2058 C CB  . GLU A 1 263 ? 34.79936 7.17451  22.22858  0.800 75.39180  ? 263 GLU A CB  1 
ATOM   2059 C CG  . GLU A 1 263 ? 34.99121 6.63794  23.64707  0.700 79.34378  ? 263 GLU A CG  1 
ATOM   2060 C CD  . GLU A 1 263 ? 35.34241 5.16272  23.67656  0.600 81.84366  ? 263 GLU A CD  1 
ATOM   2061 O OE1 . GLU A 1 263 ? 35.55721 4.57589  22.59734  0.600 80.99810  ? 263 GLU A OE1 1 
ATOM   2062 O OE2 . GLU A 1 263 ? 35.40551 4.58732  24.78143  0.600 85.34165  ? 263 GLU A OE2 1 
HETATM 2063 C C1  . CIT B 2 .   ? 31.59199 23.89527 14.36191  0.930 79.32253  ? 301 CIT A C1  1 
HETATM 2064 O O1  . CIT B 2 .   ? 32.82874 24.01137 14.22428  0.930 79.34039  ? 301 CIT A O1  1 
HETATM 2065 O O2  . CIT B 2 .   ? 31.11951 22.73879 14.31218  0.930 79.34352  ? 301 CIT A O2  1 
HETATM 2066 C C2  . CIT B 2 .   ? 30.75818 25.14785 14.58349  0.930 79.37021  ? 301 CIT A C2  1 
HETATM 2067 C C3  . CIT B 2 .   ? 29.41437 25.00267 15.31496  0.930 79.61689  ? 301 CIT A C3  1 
HETATM 2068 O O7  . CIT B 2 .   ? 29.66452 24.69823 16.71261  0.930 79.89076  ? 301 CIT A O7  1 
HETATM 2069 C C4  . CIT B 2 .   ? 28.64055 26.31882 15.25224  0.930 79.49304  ? 301 CIT A C4  1 
HETATM 2070 C C5  . CIT B 2 .   ? 29.23512 27.34333 16.19752  0.930 79.43750  ? 301 CIT A C5  1 
HETATM 2071 O O3  . CIT B 2 .   ? 29.63828 28.44646 15.76252  0.930 79.39282  ? 301 CIT A O3  1 
HETATM 2072 O O4  . CIT B 2 .   ? 29.32828 27.10893 17.42506  0.930 79.33050  ? 301 CIT A O4  1 
HETATM 2073 C C6  . CIT B 2 .   ? 28.54528 23.88581 14.74570  0.930 79.69911  ? 301 CIT A C6  1 
HETATM 2074 O O5  . CIT B 2 .   ? 27.82164 24.08967 13.74405  0.930 79.70052  ? 301 CIT A O5  1 
HETATM 2075 O O6  . CIT B 2 .   ? 28.55183 22.74768 15.26955  0.930 79.69726  ? 301 CIT A O6  1 
HETATM 2076 C C4  . UV0 C 3 .   ? 20.71300 11.55400 12.89400  0.800 62.62599  ? 302 UV0 A C4  1 
HETATM 2077 C C5  . UV0 C 3 .   ? 20.37400 12.67900 12.16900  0.800 62.62108  ? 302 UV0 A C5  1 
HETATM 2078 C C6  . UV0 C 3 .   ? 21.38800 13.50500 11.70700  0.800 62.39079  ? 302 UV0 A C6  1 
HETATM 2079 C C8  . UV0 C 3 .   ? 18.56500 11.64600 12.71700  0.800 62.48393  ? 302 UV0 A C8  1 
HETATM 2080 N N1  . UV0 C 3 .   ? 22.66000 13.18300 11.97900  0.800 62.34035  ? 302 UV0 A N1  1 
HETATM 2081 N N3  . UV0 C 3 .   ? 22.00400 11.28900 13.13300  0.800 62.43558  ? 302 UV0 A N3  1 
HETATM 2082 C C2  . UV0 C 3 .   ? 22.94900 12.09600 12.67800  0.800 62.36605  ? 302 UV0 A C2  1 
HETATM 2083 C CAA . UV0 C 3 .   ? 13.00600 8.90700  12.73500  0.800 59.90395  ? 302 UV0 A CAA 1 
HETATM 2084 C CAC . UV0 C 3 .   ? 14.57100 10.69200 13.09300  0.800 60.64187  ? 302 UV0 A CAC 1 
HETATM 2085 C CAD . UV0 C 3 .   ? 15.99300 11.03200 12.95900  0.800 61.28245  ? 302 UV0 A CAD 1 
HETATM 2086 C CAE . UV0 C 3 .   ? 17.17900 11.31500 12.84700  0.800 61.79954  ? 302 UV0 A CAE 1 
HETATM 2087 C CAP . UV0 C 3 .   ? 19.46400 9.68700  13.99700  0.800 64.39907  ? 302 UV0 A CAP 1 
HETATM 2088 C CAR . UV0 C 3 .   ? 18.03600 8.05800  14.65400  0.800 65.70947  ? 302 UV0 A CAR 1 
HETATM 2089 C CAS . UV0 C 3 .   ? 16.58800 7.57100  14.56900  0.800 66.22531  ? 302 UV0 A CAS 1 
HETATM 2090 C CAU . UV0 C 3 .   ? 16.09700 6.19900  12.59900  0.800 67.49677  ? 302 UV0 A CAU 1 
HETATM 2091 C CAX . UV0 C 3 .   ? 15.60200 5.03900  10.63900  0.800 68.01684  ? 302 UV0 A CAX 1 
HETATM 2092 C CAY . UV0 C 3 .   ? 14.49100 4.84800  9.82600   0.800 68.18441  ? 302 UV0 A CAY 1 
HETATM 2093 C CAZ . UV0 C 3 .   ? 13.53100 5.84700  9.71400   0.800 68.21667  ? 302 UV0 A CAZ 1 
HETATM 2094 C CBA . UV0 C 3 .   ? 12.42100 5.65500  8.90100   0.800 68.24885  ? 302 UV0 A CBA 1 
HETATM 2095 C CBB . UV0 C 3 .   ? 12.27000 4.46500  8.19900   0.800 68.18850  ? 302 UV0 A CBB 1 
HETATM 2096 C CBC . UV0 C 3 .   ? 13.23000 3.46600  8.31100   0.800 68.20326  ? 302 UV0 A CBC 1 
HETATM 2097 C CBD . UV0 C 3 .   ? 14.34100 3.65700  9.12500   0.800 68.29646  ? 302 UV0 A CBD 1 
HETATM 2098 C CBE . UV0 C 3 .   ? 15.30000 2.65800  9.23700   0.800 68.27599  ? 302 UV0 A CBE 1 
HETATM 2099 C CBF . UV0 C 3 .   ? 16.41100 2.85000  10.05000  0.800 68.07773  ? 302 UV0 A CBF 1 
HETATM 2100 C CBG . UV0 C 3 .   ? 16.56200 4.04000  10.75100  0.800 68.00132  ? 302 UV0 A CBG 1 
HETATM 2101 C CBH . UV0 C 3 .   ? 18.21200 8.91900  15.90600  0.800 65.57672  ? 302 UV0 A CBH 1 
HETATM 2102 C CBJ . UV0 C 3 .   ? 19.17400 10.02200 15.46200  0.800 65.01415  ? 302 UV0 A CBJ 1 
HETATM 2103 C CBL . UV0 C 3 .   ? 14.16000 9.88400  10.87000  0.800 59.72142  ? 302 UV0 A CBL 1 
HETATM 2104 C CBM . UV0 C 3 .   ? 15.52600 9.75000  10.19400  0.800 59.40615  ? 302 UV0 A CBM 1 
HETATM 2105 C CBO . UV0 C 3 .   ? 16.82200 8.39000  8.93000   0.800 58.62545  ? 302 UV0 A CBO 1 
HETATM 2106 C CBP . UV0 C 3 .   ? 16.34600 9.46100  7.94700   0.800 58.89339  ? 302 UV0 A CBP 1 
HETATM 2107 C CBR . UV0 C 3 .   ? 15.47100 10.38000 8.80100   0.800 59.10953  ? 302 UV0 A CBR 1 
HETATM 2108 C CBU . UV0 C 3 .   ? 15.90800 6.54900  7.49500   0.800 57.80545  ? 302 UV0 A CBU 1 
HETATM 2109 C CBW . UV0 C 3 .   ? 17.52800 5.13300  7.50700   0.800 57.74774  ? 302 UV0 A CBW 1 
HETATM 2110 C CBX . UV0 C 3 .   ? 17.89100 6.22400  8.27200   0.800 57.78644  ? 302 UV0 A CBX 1 
HETATM 2111 C CBZ . UV0 C 3 .   ? 19.93000 5.22800  8.71300   0.800 57.29834  ? 302 UV0 A CBZ 1 
HETATM 2112 C CCB . UV0 C 3 .   ? 18.42600 4.08500  7.37100   0.800 57.27808  ? 302 UV0 A CCB 1 
HETATM 2113 N N6  . UV0 C 3 .   ? 21.10200 14.59700 11.00400  0.800 62.40202  ? 302 UV0 A N6  1 
HETATM 2114 N N7  . UV0 C 3 .   ? 19.04900 12.71000 12.07500  0.800 62.60495  ? 302 UV0 A N7  1 
HETATM 2115 N N9  . UV0 C 3 .   ? 19.58000 10.93900 13.21700  0.800 62.89027  ? 302 UV0 A N9  1 
HETATM 2116 N NAB . UV0 C 3 .   ? 14.27300 9.50100  12.28500  0.800 60.09298  ? 302 UV0 A NAB 1 
HETATM 2117 N NAT . UV0 C 3 .   ? 16.20900 7.40100  13.15900  0.800 66.78739  ? 302 UV0 A NAT 1 
HETATM 2118 N NAW . UV0 C 3 .   ? 15.74700 6.18100  11.31200  0.800 67.89036  ? 302 UV0 A NAW 1 
HETATM 2119 N NBT . UV0 C 3 .   ? 16.87400 7.07900  8.24600   0.800 57.98705  ? 302 UV0 A NBT 1 
HETATM 2120 N NBV . UV0 C 3 .   ? 16.30500 5.35900  7.04100   0.800 57.82903  ? 302 UV0 A NBV 1 
HETATM 2121 N NBY . UV0 C 3 .   ? 19.09400 6.24400  8.86100   0.800 57.50709  ? 302 UV0 A NBY 1 
HETATM 2122 N NCA . UV0 C 3 .   ? 19.61500 4.16700  7.98700   0.800 57.12551  ? 302 UV0 A NCA 1 
HETATM 2123 N NCC . UV0 C 3 .   ? 18.11400 3.01700  6.64300   0.800 57.21347  ? 302 UV0 A NCC 1 
HETATM 2124 O OAQ . UV0 C 3 .   ? 18.30100 8.96200  13.57100  0.800 65.22375  ? 302 UV0 A OAQ 1 
HETATM 2125 O OAV . UV0 C 3 .   ? 16.30700 5.17100  13.24300  0.800 67.67904  ? 302 UV0 A OAV 1 
HETATM 2126 O OBI . UV0 C 3 .   ? 18.82200 8.14100  16.93900  0.800 66.03300  ? 302 UV0 A OBI 1 
HETATM 2127 O OBK . UV0 C 3 .   ? 20.38300 9.93500  16.22000  0.800 65.18744  ? 302 UV0 A OBK 1 
HETATM 2128 O OBN . UV0 C 3 .   ? 15.79900 8.36400  9.93800   0.800 59.07391  ? 302 UV0 A OBN 1 
HETATM 2129 O OBQ . UV0 C 3 .   ? 17.47200 10.19400 7.45800   0.800 59.05900  ? 302 UV0 A OBQ 1 
HETATM 2130 O OBS . UV0 C 3 .   ? 16.05000 11.68700 8.84500   0.800 58.97650  ? 302 UV0 A OBS 1 
HETATM 2131 O O   . HOH D 4 .   ? 24.37764 7.95176  -9.07956  1.000 27.92090  ? 401 HOH A O   1 
HETATM 2132 O O   . HOH D 4 .   ? 13.49112 22.22376 -5.87773  1.000 46.41404  ? 402 HOH A O   1 
HETATM 2133 O O   . HOH D 4 .   ? 22.84239 11.38108 0.38354   1.000 39.60332  ? 403 HOH A O   1 
HETATM 2134 O O   . HOH D 4 .   ? 29.38125 6.78033  4.84641   1.000 40.64002  ? 404 HOH A O   1 
HETATM 2135 O O   . HOH D 4 .   ? 31.49500 5.60239  0.00000   0.50  66.98803  ? 405 HOH A O   1 
HETATM 2136 O O   . HOH D 4 .   ? 10.82951 26.58933 -0.00260  1.000 51.14362  ? 406 HOH A O   1 
HETATM 2137 O O   . HOH D 4 .   ? 20.80359 26.92740 -4.89777  1.000 51.94339  ? 407 HOH A O   1 
HETATM 2138 O O   . HOH D 4 .   ? 22.48002 20.87009 6.85021   1.000 50.10227  ? 408 HOH A O   1 
HETATM 2139 O O   . HOH D 4 .   ? 24.64580 1.29740  -5.54336  1.000 52.87433  ? 409 HOH A O   1 
HETATM 2140 O O   . HOH D 4 .   ? 23.67412 7.26139  10.78549  1.000 46.86769  ? 410 HOH A O   1 
HETATM 2141 O O   . HOH D 4 .   ? 26.15465 6.84524  -3.55724  1.000 55.28866  ? 411 HOH A O   1 
HETATM 2142 O O   . HOH D 4 .   ? 21.44057 14.82533 31.94730  1.000 62.57953  ? 412 HOH A O   1 
HETATM 2143 O O   . HOH D 4 .   ? 13.01884 11.50200 18.64841  1.000 36.35705  ? 413 HOH A O   1 
HETATM 2144 O O   . HOH D 4 .   ? -0.65294 12.62372 -6.77005  1.000 61.51076  ? 414 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   ? 1.74720 1.10388 1.40345 0.06208  0.10298  -0.41606 1   MET A N   
2    C CA  . MET A 1   ? 1.78705 1.05665 1.39539 0.07719  0.11002  -0.36589 1   MET A CA  
3    C C   . MET A 1   ? 1.67783 1.03829 1.29365 0.11359  0.09133  -0.32912 1   MET A C   
4    O O   . MET A 1   ? 1.58602 1.06828 1.24517 0.11381  0.07955  -0.33561 1   MET A O   
5    C CB  . MET A 1   ? 1.83958 1.04697 1.44023 0.02032  0.13895  -0.34979 1   MET A CB  
6    C CG  . MET A 1   ? 1.74821 1.07085 1.40484 -0.01850 0.14240  -0.35208 1   MET A CG  
7    S SD  . MET A 1   ? 1.81697 1.08364 1.48414 -0.09625 0.18158  -0.36295 1   MET A SD  
8    C CE  . MET A 1   ? 1.88536 1.13926 1.58573 -0.12724 0.18655  -0.43326 1   MET A CE  
9    N N   . LYS A 2   ? 1.69043 0.98900 1.26190 0.14455  0.08834  -0.29139 2   LYS A N   
10   C CA  . LYS A 2   ? 1.59972 0.98074 1.18138 0.17846  0.07054  -0.26254 2   LYS A CA  
11   C C   . LYS A 2   ? 1.50210 0.96732 1.12304 0.14260  0.07558  -0.24564 2   LYS A C   
12   O O   . LYS A 2   ? 1.53162 0.96413 1.15275 0.09884  0.09463  -0.24148 2   LYS A O   
13   C CB  . LYS A 2   ? 1.65715 0.95421 1.18194 0.21600  0.06516  -0.22938 2   LYS A CB  
14   C CG  . LYS A 2   ? 1.75065 0.97212 1.23759 0.26733  0.05296  -0.24433 2   LYS A CG  
15   C CD  . LYS A 2   ? 1.81858 0.95067 1.24129 0.30774  0.04481  -0.20904 2   LYS A CD  
16   C CE  . LYS A 2   ? 1.88982 0.95578 1.28141 0.36506  0.02776  -0.22281 2   LYS A CE  
17   N NZ  . LYS A 2   ? 1.79257 0.98531 1.23396 0.40830  0.00359  -0.24537 2   LYS A NZ  
18   N N   . TYR A 3   ? 1.40699 0.98047 1.06278 0.16083  0.05995  -0.23754 3   TYR A N   
19   C CA  . TYR A 3   ? 1.30531 0.95700 1.00054 0.13335  0.06134  -0.22312 3   TYR A CA  
20   C C   . TYR A 3   ? 1.20425 0.93786 0.92056 0.16159  0.04565  -0.20390 3   TYR A C   
21   O O   . TYR A 3   ? 1.20825 0.96801 0.92206 0.19655  0.03482  -0.21083 3   TYR A O   
22   C CB  . TYR A 3   ? 1.28708 0.99926 1.02158 0.10323  0.06348  -0.25074 3   TYR A CB  
23   C CG  . TYR A 3   ? 1.24436 1.04911 1.00159 0.12605  0.04806  -0.26200 3   TYR A CG  
24   C CD1 . TYR A 3   ? 1.29067 1.08907 1.03352 0.15018  0.04320  -0.28973 3   TYR A CD1 
25   C CD2 . TYR A 3   ? 1.17133 1.06584 0.96047 0.12389  0.04007  -0.24449 3   TYR A CD2 
26   C CE1 . TYR A 3   ? 1.26555 1.15391 1.02331 0.16963  0.03300  -0.29989 3   TYR A CE1 
27   C CE2 . TYR A 3   ? 1.15464 1.12791 0.95463 0.14206  0.03037  -0.24909 3   TYR A CE2 
28   C CZ  . TYR A 3   ? 1.20316 1.17786 0.98647 0.16391  0.02797  -0.27689 3   TYR A CZ  
29   O OH  . TYR A 3   ? 1.19174 1.25066 0.98060 0.18052  0.02200  -0.28155 3   TYR A OH  
30   N N   . MET A 4   ? 1.12035 0.89698 0.86183 0.14400  0.04616  -0.18345 4   MET A N   
31   C CA  . MET A 4   ? 1.04446 0.89989 0.81529 0.15906  0.03483  -0.16702 4   MET A CA  
32   C C   . MET A 4   ? 0.97305 0.88242 0.78263 0.13063  0.03631  -0.15899 4   MET A C   
33   O O   . MET A 4   ? 0.98041 0.86921 0.79484 0.10292  0.04497  -0.16587 4   MET A O   
34   C CB  . MET A 4   ? 1.05741 0.89247 0.81166 0.18121  0.02878  -0.14815 4   MET A CB  
35   C CG  . MET A 4   ? 1.06632 0.87183 0.81415 0.16035  0.03544  -0.13183 4   MET A CG  
36   S SD  . MET A 4   ? 0.98296 0.87196 0.78600 0.14523  0.03027  -0.11872 4   MET A SD  
37   C CE  . MET A 4   ? 0.95417 0.90394 0.77629 0.17755  0.01603  -0.11623 4   MET A CE  
38   N N   . ILE A 5   ? 0.92264 0.90106 0.76117 0.13793  0.02858  -0.14551 5   ILE A N   
39   C CA  . ILE A 5   ? 0.86814 0.89387 0.74072 0.11918  0.02655  -0.13518 5   ILE A CA  
40   C C   . ILE A 5   ? 0.82435 0.87992 0.72008 0.12368  0.02247  -0.11251 5   ILE A C   
41   O O   . ILE A 5   ? 0.80499 0.89370 0.70544 0.13899  0.02026  -0.10675 5   ILE A O   
42   C CB  . ILE A 5   ? 0.84950 0.92830 0.72979 0.12019  0.02211  -0.14300 5   ILE A CB  
43   C CG1 . ILE A 5   ? 0.88462 0.93996 0.74856 0.11332  0.02470  -0.17429 5   ILE A CG1 
44   C CG2 . ILE A 5   ? 0.80759 0.92677 0.71629 0.10839  0.01634  -0.12792 5   ILE A CG2 
45   C CD1 . ILE A 5   ? 0.88568 0.99933 0.75102 0.11835  0.01757  -0.18796 5   ILE A CD1 
46   N N   . THR A 6   ? 0.80859 0.85684 0.72311 0.10863  0.02276  -0.10419 6   THR A N   
47   C CA  . THR A 6   ? 0.77373 0.84607 0.71682 0.10783  0.01880  -0.08782 6   THR A CA  
48   C C   . THR A 6   ? 0.75647 0.86446 0.72875 0.09870  0.01507  -0.07515 6   THR A C   
49   O O   . THR A 6   ? 0.76546 0.87635 0.74021 0.09185  0.01293  -0.08172 6   THR A O   
50   C CB  . THR A 6   ? 0.77363 0.81362 0.71653 0.10056  0.02053  -0.09007 6   THR A CB  
51   O OG1 . THR A 6   ? 0.81132 0.80650 0.71291 0.11154  0.02378  -0.09712 6   THR A OG1 
52   C CG2 . THR A 6   ? 0.74824 0.81220 0.72219 0.10101  0.01502  -0.08092 6   THR A CG2 
53   N N   . SER A 7   ? 0.73957 0.87398 0.73385 0.09906  0.01404  -0.05758 7   SER A N   
54   C CA  . SER A 7   ? 0.75256 0.90726 0.76551 0.09337  0.01108  -0.03794 7   SER A CA  
55   C C   . SER A 7   ? 0.75177 0.89654 0.79930 0.08419  0.00955  -0.02704 7   SER A C   
56   O O   . SER A 7   ? 0.74853 0.89207 0.80901 0.08167  0.01206  -0.03237 7   SER A O   
57   C CB  . SER A 7   ? 0.77446 0.96555 0.77565 0.09793  0.01644  -0.02276 7   SER A CB  
58   O OG  . SER A 7   ? 0.79836 0.99779 0.80718 0.09335  0.01483  0.00386  7   SER A OG  
59   N N   . LYS A 8   ? 0.76881 0.90742 0.83211 0.08205  0.00311  -0.01516 8   LYS A N   
60   C CA  . LYS A 8   ? 0.76788 0.88912 0.86596 0.07463  0.00087  -0.00633 8   LYS A CA  
61   C C   . LYS A 8   ? 0.78095 0.91094 0.89199 0.06420  0.01004  0.01365  8   LYS A C   
62   O O   . LYS A 8   ? 0.78003 0.89937 0.92316 0.05323  0.01168  0.00937  8   LYS A O   
63   C CB  . LYS A 8   ? 0.78371 0.89339 0.89257 0.08179  -0.01037 0.00313  8   LYS A CB  
64   C CG  . LYS A 8   ? 0.79494 0.87577 0.94027 0.07800  -0.01447 0.01073  8   LYS A CG  
65   C CD  . LYS A 8   ? 0.83159 0.89908 0.97952 0.09392  -0.02835 0.02732  8   LYS A CD  
66   C CE  . LYS A 8   ? 0.86448 0.89476 1.05139 0.09564  -0.03527 0.02584  8   LYS A CE  
67   N NZ  . LYS A 8   ? 0.84348 0.88153 1.05582 0.09716  -0.03883 -0.01385 8   LYS A NZ  
68   N N   . GLY A 9   ? 0.79287 0.94688 0.88141 0.06496  0.01787  0.03189  9   GLY A N   
69   C CA  . GLY A 9   ? 0.81720 0.98945 0.91808 0.04990  0.03284  0.04882  9   GLY A CA  
70   C C   . GLY A 9   ? 0.87996 1.04006 0.97065 0.04252  0.03981  0.08779  9   GLY A C   
71   O O   . GLY A 9   ? 0.91535 1.09213 1.01213 0.02438  0.05841  0.10510  9   GLY A O   
72   N N   . ASP A 10  ? 0.90459 1.03753 0.97873 0.05646  0.02615  0.10225  10  ASP A N   
73   C CA  . ASP A 10  ? 0.96664 1.07858 1.01795 0.05684  0.02924  0.14460  10  ASP A CA  
74   C C   . ASP A 10  ? 0.98242 1.13363 0.98041 0.07049  0.03117  0.15655  10  ASP A C   
75   O O   . ASP A 10  ? 0.94269 1.13293 0.92826 0.07915  0.02901  0.12794  10  ASP A O   
76   C CB  . ASP A 10  ? 0.99017 1.05459 1.05116 0.07276  0.00885  0.15237  10  ASP A CB  
77   C CG  . ASP A 10  ? 0.95170 1.03591 1.00776 0.09639  -0.01223 0.12211  10  ASP A CG  
78   O OD1 . ASP A 10  ? 0.90640 1.02621 0.95613 0.09527  -0.00938 0.09335  10  ASP A OD1 
79   O OD2 . ASP A 10  ? 0.97350 1.03725 1.03385 0.11601  -0.03112 0.12544  10  ASP A OD2 
80   N N   . GLU A 11  ? 1.04886 1.18547 1.01057 0.07366  0.03516  0.19924  11  GLU A N   
81   C CA  . GLU A 11  ? 1.07541 1.25564 0.98036 0.08630  0.03873  0.21128  11  GLU A CA  
82   C C   . GLU A 11  ? 1.04048 1.24648 0.92789 0.11524  0.01250  0.18183  11  GLU A C   
83   O O   . GLU A 11  ? 1.02515 1.28007 0.88881 0.12174  0.01461  0.15950  11  GLU A O   
84   C CB  . GLU A 11  ? 1.17775 1.32963 1.03656 0.08656  0.04714  0.26812  11  GLU A CB  
85   C CG  . GLU A 11  ? 1.22407 1.37470 1.08464 0.05073  0.08417  0.29659  11  GLU A CG  
86   C CD  . GLU A 11  ? 1.34246 1.46613 1.13875 0.05020  0.09757  0.35719  11  GLU A CD  
87   O OE1 . GLU A 11  ? 1.39617 1.48509 1.15277 0.08159  0.07241  0.38073  11  GLU A OE1 
88   O OE2 . GLU A 11  ? 1.38840 1.52821 1.17190 0.01946  0.13356  0.38104  11  GLU A OE2 
89   N N   . LYS A 12  ? 1.02776 1.20493 0.93131 0.13201  -0.01173 0.17653  12  LYS A N   
90   C CA  . LYS A 12  ? 1.00704 1.21689 0.90139 0.15567  -0.03567 0.14522  12  LYS A CA  
91   C C   . LYS A 12  ? 0.93806 1.17388 0.85546 0.14542  -0.03127 0.09574  12  LYS A C   
92   O O   . LYS A 12  ? 0.93519 1.21089 0.83031 0.15394  -0.03645 0.07068  12  LYS A O   
93   C CB  . LYS A 12  ? 1.01940 1.20088 0.93852 0.17468  -0.06064 0.14385  12  LYS A CB  
94   C CG  . LYS A 12  ? 1.00657 1.23216 0.92684 0.19710  -0.08582 0.10696  12  LYS A CG  
95   C CD  . LYS A 12  ? 1.02111 1.22830 0.97181 0.21957  -0.11062 0.10353  12  LYS A CD  
96   C CE  . LYS A 12  ? 0.99993 1.26515 0.96537 0.23737  -0.13396 0.05762  12  LYS A CE  
97   N NZ  . LYS A 12  ? 1.04163 1.35601 0.95525 0.25908  -0.14879 0.06187  12  LYS A NZ  
98   N N   . SER A 13  ? 0.89296 1.10285 0.85099 0.12797  -0.02194 0.08097  13  SER A N   
99   C CA  . SER A 13  ? 0.84578 1.06511 0.81726 0.12108  -0.01850 0.03973  13  SER A CA  
100  C C   . SER A 13  ? 0.83286 1.07792 0.78145 0.11713  -0.00311 0.03264  13  SER A C   
101  O O   . SER A 13  ? 0.81395 1.07282 0.75076 0.12120  -0.00440 0.00160  13  SER A O   
102  C CB  . SER A 13  ? 0.81618 1.00160 0.82769 0.10821  -0.01465 0.02849  13  SER A CB  
103  O OG  . SER A 13  ? 0.82551 0.99057 0.86206 0.11407  -0.02799 0.03105  13  SER A OG  
104  N N   . ASP A 14  ? 0.85245 1.10420 0.79806 0.10834  0.01279  0.05790  14  ASP A N   
105  C CA  . ASP A 14  ? 0.84250 1.13026 0.77201 0.10786  0.02777  0.04717  14  ASP A CA  
106  C C   . ASP A 14  ? 0.85360 1.18047 0.73901 0.12282  0.02466  0.04153  14  ASP A C   
107  O O   . ASP A 14  ? 0.84796 1.19764 0.72127 0.13045  0.02747  0.01107  14  ASP A O   
108  C CB  . ASP A 14  ? 0.86615 1.16586 0.80836 0.09127  0.04827  0.07282  14  ASP A CB  
109  C CG  . ASP A 14  ? 0.84719 1.12284 0.83655 0.07713  0.05091  0.06461  14  ASP A CG  
110  O OD1 . ASP A 14  ? 0.82056 1.06947 0.82473 0.08256  0.03801  0.04138  14  ASP A OD1 
111  O OD2 . ASP A 14  ? 0.86470 1.15172 0.87569 0.05874  0.06730  0.07974  14  ASP A OD2 
112  N N   . LEU A 15  ? 0.87395 1.20730 0.73211 0.13047  0.01689  0.06880  15  LEU A N   
113  C CA  . LEU A 15  ? 0.90800 1.28720 0.71855 0.14684  0.01234  0.06247  15  LEU A CA  
114  C C   . LEU A 15  ? 0.89233 1.27999 0.70513 0.15865  -0.00792 0.01797  15  LEU A C   
115  O O   . LEU A 15  ? 0.91714 1.34367 0.70268 0.16873  -0.00956 -0.00884 15  LEU A O   
116  C CB  . LEU A 15  ? 0.96852 1.35073 0.73942 0.15606  0.00765  0.10792  15  LEU A CB  
117  C CG  . LEU A 15  ? 1.03252 1.47107 0.74163 0.17230  0.00856  0.11012  15  LEU A CG  
118  C CD1 . LEU A 15  ? 1.10215 1.54330 0.76915 0.16498  0.03054  0.16561  15  LEU A CD1 
119  C CD2 . LEU A 15  ? 1.06090 1.51878 0.74646 0.19849  -0.02347 0.09448  15  LEU A CD2 
120  N N   . LEU A 16  ? 0.85761 1.21230 0.70514 0.15519  -0.02140 0.00581  16  LEU A N   
121  C CA  . LEU A 16  ? 0.82644 1.18922 0.68425 0.15761  -0.03485 -0.03976 16  LEU A CA  
122  C C   . LEU A 16  ? 0.78691 1.13053 0.65420 0.14695  -0.02170 -0.07314 16  LEU A C   
123  O O   . LEU A 16  ? 0.78649 1.14140 0.64606 0.14821  -0.02565 -0.11182 16  LEU A O   
124  C CB  . LEU A 16  ? 0.80465 1.14581 0.69894 0.15517  -0.04915 -0.04411 16  LEU A CB  
125  C CG  . LEU A 16  ? 0.78577 1.14308 0.69900 0.15155  -0.06046 -0.09248 16  LEU A CG  
126  C CD1 . LEU A 16  ? 0.81551 1.23106 0.70193 0.16973  -0.07903 -0.10931 16  LEU A CD1 
127  C CD2 . LEU A 16  ? 0.76063 1.10238 0.71712 0.14650  -0.06867 -0.09821 16  LEU A CD2 
128  N N   . ARG A 17  ? 0.76095 1.07352 0.64393 0.13804  -0.00745 -0.06024 17  ARG A N   
129  C CA  . ARG A 17  ? 0.75062 1.03973 0.63465 0.13592  0.00219  -0.08684 17  ARG A CA  
130  C C   . ARG A 17  ? 0.77273 1.09660 0.62795 0.14917  0.00835  -0.10290 17  ARG A C   
131  O O   . ARG A 17  ? 0.78105 1.08857 0.62782 0.15373  0.00882  -0.13782 17  ARG A O   
132  C CB  . ARG A 17  ? 0.72584 0.98651 0.63139 0.12949  0.01141  -0.07003 17  ARG A CB  
133  C CG  . ARG A 17  ? 0.73169 0.97090 0.63120 0.13655  0.01829  -0.09138 17  ARG A CG  
134  C CD  . ARG A 17  ? 0.71788 0.94062 0.63933 0.13348  0.02253  -0.07763 17  ARG A CD  
135  N NE  . ARG A 17  ? 0.73015 0.93767 0.64193 0.14879  0.02476  -0.09607 17  ARG A NE  
136  C CZ  . ARG A 17  ? 0.74092 0.98791 0.65143 0.16362  0.02997  -0.10169 17  ARG A CZ  
137  N NH1 . ARG A 17  ? 0.74195 1.04628 0.65660 0.15980  0.03830  -0.08892 17  ARG A NH1 
138  N NH2 . ARG A 17  ? 0.75685 0.98630 0.65943 0.18439  0.02736  -0.12051 17  ARG A NH2 
139  N N   . LEU A 18  ? 0.79180 1.16104 0.63001 0.15493  0.01505  -0.07880 18  LEU A N   
140  C CA  . LEU A 18  ? 0.81279 1.22613 0.62356 0.16855  0.02302  -0.09789 18  LEU A CA  
141  C C   . LEU A 18  ? 0.82961 1.26664 0.61470 0.17802  0.01010  -0.12962 18  LEU A C   
142  O O   . LEU A 18  ? 0.84317 1.29460 0.61393 0.18923  0.01260  -0.16644 18  LEU A O   
143  C CB  . LEU A 18  ? 0.82791 1.28925 0.62412 0.16739  0.03883  -0.06319 18  LEU A CB  
144  C CG  . LEU A 18  ? 0.79775 1.25301 0.62557 0.15552  0.05497  -0.04278 18  LEU A CG  
145  C CD1 . LEU A 18  ? 0.82429 1.32602 0.63825 0.14553  0.07540  -0.00715 18  LEU A CD1 
146  C CD2 . LEU A 18  ? 0.77986 1.23569 0.62350 0.16740  0.05929  -0.07795 18  LEU A CD2 
147  N N   . ASN A 19  ? 0.83058 1.27413 0.61287 0.17591  -0.00572 -0.12113 19  ASN A N   
148  C CA  . ASN A 19  ? 0.85728 1.33510 0.62049 0.18489  -0.02138 -0.15739 19  ASN A CA  
149  C C   . ASN A 19  ? 0.84917 1.28803 0.63714 0.17423  -0.02550 -0.20631 19  ASN A C   
150  O O   . ASN A 19  ? 0.87773 1.33603 0.65298 0.17930  -0.02991 -0.25066 19  ASN A O   
151  C CB  . ASN A 19  ? 0.87039 1.37450 0.62506 0.19122  -0.04084 -0.13599 19  ASN A CB  
152  C CG  . ASN A 19  ? 0.91430 1.46002 0.62224 0.20562  -0.03750 -0.09316 19  ASN A CG  
153  O OD1 . ASN A 19  ? 0.93804 1.51048 0.61916 0.20892  -0.01952 -0.08928 19  ASN A OD1 
154  N ND2 . ASN A 19  ? 0.93335 1.48421 0.62910 0.21544  -0.05388 -0.06080 19  ASN A ND2 
155  N N   . MET A 20  ? 0.81616 1.19802 0.63709 0.15769  -0.02212 -0.19997 20  MET A N   
156  C CA  . MET A 20  ? 0.81851 1.15117 0.65658 0.14245  -0.01922 -0.23960 20  MET A CA  
157  C C   . MET A 20  ? 0.84780 1.14701 0.66935 0.15070  -0.00722 -0.26039 20  MET A C   
158  O O   . MET A 20  ? 0.87380 1.15429 0.69057 0.14737  -0.00747 -0.30412 20  MET A O   
159  C CB  . MET A 20  ? 0.78693 1.06858 0.65498 0.12384  -0.01452 -0.22314 20  MET A CB  
160  C CG  . MET A 20  ? 0.76962 1.08023 0.66315 0.11648  -0.02801 -0.21888 20  MET A CG  
161  S SD  . MET A 20  ? 0.74339 1.00448 0.67513 0.09185  -0.01992 -0.21727 20  MET A SD  
162  C CE  . MET A 20  ? 0.77577 0.98569 0.70627 0.06694  -0.00459 -0.26388 20  MET A CE  
163  N N   . ILE A 21  ? 0.84843 1.14094 0.66431 0.16257  0.00245  -0.23306 21  ILE A N   
164  C CA  . ILE A 21  ? 0.87288 1.14327 0.67487 0.17955  0.01044  -0.25342 21  ILE A CA  
165  C C   . ILE A 21  ? 0.90307 1.21991 0.68295 0.19460  0.00757  -0.29059 21  ILE A C   
166  O O   . ILE A 21  ? 0.92104 1.20114 0.69320 0.20142  0.00816  -0.33133 21  ILE A O   
167  C CB  . ILE A 21  ? 0.84367 1.12975 0.65070 0.19160  0.01891  -0.22161 21  ILE A CB  
168  C CG1 . ILE A 21  ? 0.81184 1.04444 0.63881 0.17970  0.02006  -0.19663 21  ILE A CG1 
169  C CG2 . ILE A 21  ? 0.86509 1.15544 0.65987 0.21775  0.02408  -0.24760 21  ILE A CG2 
170  C CD1 . ILE A 21  ? 0.78590 1.04329 0.62727 0.18657  0.02608  -0.16899 21  ILE A CD1 
171  N N   . ALA A 22  ? 0.91017 1.30457 0.67529 0.20096  0.00485  -0.27712 22  ALA A N   
172  C CA  . ALA A 22  ? 0.94921 1.39879 0.68781 0.21586  0.00102  -0.31450 22  ALA A CA  
173  C C   . ALA A 22  ? 0.97575 1.40853 0.71973 0.20477  -0.01226 -0.36154 22  ALA A C   
174  O O   . ALA A 22  ? 0.86203 1.29985 0.59472 0.21427  -0.01387 -0.41149 22  ALA A O   
175  C CB  . ALA A 22  ? 0.79793 1.32981 0.50959 0.22303  0.00078  -0.28389 22  ALA A CB  
176  N N   . GLY A 23  ? 0.95981 1.37568 0.72593 0.18376  -0.02113 -0.35145 23  GLY A N   
177  C CA  . GLY A 23  ? 0.97723 1.37771 0.76061 0.16594  -0.03014 -0.40030 23  GLY A CA  
178  C C   . GLY A 23  ? 0.97743 1.28731 0.77108 0.15348  -0.01784 -0.43117 23  GLY A C   
179  O O   . GLY A 23  ? 1.00477 1.30204 0.80127 0.14532  -0.02014 -0.48527 23  GLY A O   
180  N N   . PHE A 24  ? 0.95408 1.19658 0.75047 0.15262  -0.00526 -0.39796 24  PHE A N   
181  C CA  . PHE A 24  ? 0.99545 1.13933 0.78859 0.14688  0.00607  -0.41792 24  PHE A CA  
182  C C   . PHE A 24  ? 1.03776 1.17292 0.80787 0.17625  0.00716  -0.44921 24  PHE A C   
183  O O   . PHE A 24  ? 1.09163 1.14928 0.85574 0.17304  0.01218  -0.48418 24  PHE A O   
184  C CB  . PHE A 24  ? 0.97298 1.05594 0.76710 0.14523  0.01539  -0.37270 24  PHE A CB  
185  C CG  . PHE A 24  ? 0.95802 1.01444 0.77420 0.11194  0.01968  -0.35758 24  PHE A CG  
186  C CD1 . PHE A 24  ? 1.00696 1.00641 0.83165 0.08085  0.02864  -0.38869 24  PHE A CD1 
187  C CD2 . PHE A 24  ? 0.90875 0.99605 0.73930 0.10995  0.01730  -0.31499 24  PHE A CD2 
188  C CE1 . PHE A 24  ? 0.99396 0.97890 0.84169 0.04864  0.03644  -0.37814 24  PHE A CE1 
189  C CE2 . PHE A 24  ? 0.89643 0.96492 0.74942 0.08235  0.02183  -0.30597 24  PHE A CE2 
190  C CZ  . PHE A 24  ? 0.93474 0.95723 0.79649 0.05191  0.03211  -0.33783 24  PHE A CZ  
191  N N   . GLY A 25  ? 1.03508 1.24524 0.79207 0.20454  0.00456  -0.43781 25  GLY A N   
192  C CA  . GLY A 25  ? 1.08428 1.30165 0.82833 0.23111  0.00530  -0.46674 25  GLY A CA  
193  C C   . GLY A 25  ? 1.14076 1.36617 0.88950 0.21984  -0.00185 -0.51121 25  GLY A C   
194  O O   . GLY A 25  ? 1.19442 1.38432 0.93987 0.23257  -0.00062 -0.53942 25  GLY A O   
195  N N   . GLU A 26  ? 1.34563 1.83995 1.02668 -0.00296 0.13232  -0.62581 26  GLU A N   
196  C CA  . GLU A 26  ? 1.48934 1.88242 1.10813 -0.01327 0.14169  -0.65584 26  GLU A CA  
197  C C   . GLU A 26  ? 1.58329 1.89252 1.18145 -0.03605 0.16017  -0.67793 26  GLU A C   
198  O O   . GLU A 26  ? 1.69004 1.91001 1.23131 -0.04525 0.16598  -0.70276 26  GLU A O   
199  C CB  . GLU A 26  ? 1.45877 1.88077 1.10998 -0.04325 0.09437  -0.66171 26  GLU A CB  
200  C CG  . GLU A 26  ? 1.41125 1.92535 1.09586 -0.02590 0.06927  -0.63821 26  GLU A CG  
201  C CD  . GLU A 26  ? 1.23870 1.74268 0.85976 0.02358  0.10341  -0.62950 26  GLU A CD  
202  O OE1 . GLU A 26  ? 1.40658 1.80920 0.94400 0.04011  0.13882  -0.64792 26  GLU A OE1 
203  O OE2 . GLU A 26  ? 1.17127 1.76810 0.82356 0.04975  0.09640  -0.59948 26  GLU A OE2 
204  N N   . TYR A 27  ? 1.56479 1.90306 1.20686 -0.04544 0.16674  -0.66842 27  TYR A N   
205  C CA  . TYR A 27  ? 1.64195 1.91068 1.26844 -0.06053 0.19204  -0.68338 27  TYR A CA  
206  C C   . TYR A 27  ? 1.71939 1.98363 1.33189 -0.02247 0.23915  -0.66277 27  TYR A C   
207  O O   . TYR A 27  ? 1.67752 2.00298 1.29903 0.01392  0.24901  -0.63400 27  TYR A O   
208  C CB  . TYR A 27  ? 1.49939 1.81153 1.19878 -0.10759 0.15860  -0.68573 27  TYR A CB  
209  C CG  . TYR A 27  ? 1.40743 1.74652 1.13821 -0.13653 0.11602  -0.69080 27  TYR A CG  
210  C CD1 . TYR A 27  ? 1.28740 1.71395 1.07178 -0.13506 0.08145  -0.66921 27  TYR A CD1 
211  C CD2 . TYR A 27  ? 1.45082 1.72741 1.15782 -0.16265 0.11204  -0.71326 27  TYR A CD2 
212  C CE1 . TYR A 27  ? 1.24876 1.69346 1.06095 -0.15471 0.05054  -0.66744 27  TYR A CE1 
213  C CE2 . TYR A 27  ? 1.41155 1.71343 1.14654 -0.18409 0.07829  -0.71249 27  TYR A CE2 
214  C CZ  . TYR A 27  ? 1.31229 1.69572 1.09934 -0.17824 0.05041  -0.68855 27  TYR A CZ  
215  O OH  . TYR A 27  ? 1.28586 1.68626 1.09689 -0.19408 0.02317  -0.68385 27  TYR A OH  
216  N N   . ASP A 28  ? 1.85340 2.04936 1.44742 -0.02876 0.27011  -0.67233 28  ASP A N   
217  C CA  . ASP A 28  ? 1.90009 2.09239 1.49222 0.00528  0.31754  -0.64680 28  ASP A CA  
218  C C   . ASP A 28  ? 1.80818 2.07430 1.47532 -0.02093 0.29920  -0.63284 28  ASP A C   
219  O O   . ASP A 28  ? 1.82720 2.05643 1.50177 -0.03442 0.32076  -0.63520 28  ASP A O   
220  C CB  . ASP A 28  ? 2.05678 2.12932 1.58455 0.01754  0.36364  -0.66128 28  ASP A CB  
221  C CG  . ASP A 28  ? 2.08529 2.14650 1.60583 0.06456  0.42138  -0.62623 28  ASP A CG  
222  O OD1 . ASP A 28  ? 2.00625 2.15817 1.57157 0.09008  0.42719  -0.58745 28  ASP A OD1 
223  O OD2 . ASP A 28  ? 2.18199 2.14772 1.65619 0.07667  0.45970  -0.63303 28  ASP A OD2 
224  N N   . MET A 29  ? 1.71335 2.08240 1.43259 -0.02771 0.25657  -0.61791 29  MET A N   
225  C CA  . MET A 29  ? 1.58968 2.03411 1.37199 -0.04744 0.23154  -0.60235 29  MET A CA  
226  C C   . MET A 29  ? 1.50879 2.02664 1.30683 -0.00374 0.24901  -0.55616 29  MET A C   
227  O O   . MET A 29  ? 1.47062 2.05432 1.27945 0.01814  0.22560  -0.52993 29  MET A O   
228  C CB  . MET A 29  ? 1.51613 2.02341 1.34688 -0.08246 0.16857  -0.60961 29  MET A CB  
229  C CG  . MET A 29  ? 1.47190 1.99857 1.35220 -0.11929 0.14573  -0.61125 29  MET A CG  
230  S SD  . MET A 29  ? 1.54644 1.99516 1.42166 -0.15926 0.15322  -0.64270 29  MET A SD  
231  C CE  . MET A 29  ? 1.45789 1.96853 1.40411 -0.18838 0.11963  -0.62857 29  MET A CE  
232  N N   . GLU A 30  ? 1.44844 1.93683 1.26410 0.00860  0.27615  -0.51291 30  GLU A N   
233  C CA  . GLU A 30  ? 1.36655 1.89795 1.21650 0.04921  0.28045  -0.42880 30  GLU A CA  
234  C C   . GLU A 30  ? 1.22266 1.83735 1.13271 0.02941  0.22351  -0.39429 30  GLU A C   
235  O O   . GLU A 30  ? 1.21344 1.81993 1.14211 -0.00585 0.20645  -0.41278 30  GLU A O   
236  C CB  . GLU A 30  ? 1.40989 1.87089 1.25174 0.07060  0.33273  -0.39546 30  GLU A CB  
237  C CG  . GLU A 30  ? 1.35421 1.86166 1.23918 0.10820  0.33520  -0.30313 30  GLU A CG  
238  C CD  . GLU A 30  ? 1.34696 1.79956 1.24250 0.11146  0.36809  -0.27167 30  GLU A CD  
239  O OE1 . GLU A 30  ? 1.38804 1.76099 1.25215 0.08879  0.39476  -0.32192 30  GLU A OE1 
240  O OE2 . GLU A 30  ? 1.29692 1.78645 1.23299 0.13470  0.36514  -0.19480 30  GLU A OE2 
241  N N   . TYR A 31  ? 1.11328 1.80499 1.04972 0.05289  0.19384  -0.34279 31  TYR A N   
242  C CA  . TYR A 31  ? 0.99523 1.75832 0.98166 0.03910  0.13767  -0.29957 31  TYR A CA  
243  C C   . TYR A 31  ? 0.97237 1.72236 0.98712 0.05426  0.15216  -0.22935 31  TYR A C   
244  O O   . TYR A 31  ? 1.00362 1.74655 1.02035 0.09416  0.18800  -0.17506 31  TYR A O   
245  C CB  . TYR A 31  ? 0.94064 1.78780 0.94436 0.05688  0.09837  -0.26455 31  TYR A CB  
246  C CG  . TYR A 31  ? 0.84528 1.75945 0.88899 0.03535  0.02985  -0.23442 31  TYR A CG  
247  C CD1 . TYR A 31  ? 0.80565 1.74784 0.88561 0.04800  0.01118  -0.15229 31  TYR A CD1 
248  C CD2 . TYR A 31  ? 0.79935 1.74441 0.84096 0.00239  -0.01794 -0.28712 31  TYR A CD2 
249  C CE1 . TYR A 31  ? 0.74054 1.73187 0.84637 0.02764  -0.05512 -0.12548 31  TYR A CE1 
250  C CE2 . TYR A 31  ? 0.73248 1.72904 0.80117 -0.01460 -0.08109 -0.26136 31  TYR A CE2 
251  C CZ  . TYR A 31  ? 0.71121 1.72674 0.80830 -0.00226 -0.10034 -0.18159 31  TYR A CZ  
252  O OH  . TYR A 31  ? 0.69471 1.67487 0.79479 -0.01659 -0.14405 -0.14672 31  TYR A OH  
253  N N   . ASP A 32  ? 0.92178 1.66886 0.95723 0.02385  0.12437  -0.22866 32  ASP A N   
254  C CA  . ASP A 32  ? 0.93455 1.66339 0.99390 0.03261  0.13375  -0.16536 32  ASP A CA  
255  C C   . ASP A 32  ? 0.90345 1.66132 0.98469 0.00096  0.07536  -0.15747 32  ASP A C   
256  O O   . ASP A 32  ? 0.92762 1.65517 0.99728 -0.03093 0.07163  -0.21115 32  ASP A O   
257  C CB  . ASP A 32  ? 0.98648 1.62749 1.02273 0.03201  0.19340  -0.18971 32  ASP A CB  
258  C CG  . ASP A 32  ? 0.99507 1.61482 1.05409 0.04937  0.21199  -0.11801 32  ASP A CG  
259  O OD1 . ASP A 32  ? 0.94225 1.60839 1.03503 0.04821  0.16962  -0.05830 32  ASP A OD1 
260  O OD2 . ASP A 32  ? 1.06355 1.61580 1.10393 0.06323  0.26747  -0.12097 32  ASP A OD2 
261  N N   . ASP A 33  ? 0.86013 1.67465 0.96987 0.01056  0.02974  -0.08931 33  ASP A N   
262  C CA  . ASP A 33  ? 0.82538 1.65826 0.94628 -0.01511 -0.02896 -0.07451 33  ASP A CA  
263  C C   . ASP A 33  ? 0.85895 1.64995 0.98951 -0.01688 -0.02072 -0.02595 33  ASP A C   
264  O O   . ASP A 33  ? 0.82718 1.62665 0.96205 -0.03311 -0.07046 0.00050  33  ASP A O   
265  C CB  . ASP A 33  ? 0.78027 1.68807 0.92036 -0.00917 -0.09140 -0.02618 33  ASP A CB  
266  C CG  . ASP A 33  ? 0.77985 1.71596 0.94974 0.02112  -0.08880 0.06887  33  ASP A CG  
267  O OD1 . ASP A 33  ? 0.83051 1.73229 1.00484 0.04391  -0.03213 0.09289  33  ASP A OD1 
268  O OD2 . ASP A 33  ? 0.74652 1.74014 0.93604 0.02208  -0.14481 0.12231  33  ASP A OD2 
269  N N   . VAL A 34  ? 0.93974 1.68154 1.06925 0.00017  0.03925  -0.01300 34  VAL A N   
270  C CA  . VAL A 34  ? 1.00478 1.70125 1.14203 -0.00235 0.05209  0.02898  34  VAL A CA  
271  C C   . VAL A 34  ? 1.06168 1.69129 1.17500 -0.02735 0.08427  -0.03575 34  VAL A C   
272  O O   . VAL A 34  ? 1.09654 1.70430 1.20670 -0.04895 0.06275  -0.03321 34  VAL A O   
273  C CB  . VAL A 34  ? 1.06234 1.75034 1.21832 0.03479  0.09561  0.09661  34  VAL A CB  
274  C CG1 . VAL A 34  ? 1.09960 1.73568 1.26241 0.03041  0.11164  0.13557  34  VAL A CG1 
275  C CG2 . VAL A 34  ? 1.04178 1.80473 1.22902 0.05729  0.05922  0.17232  34  VAL A CG2 
276  N N   . GLU A 35  ? 1.10081 1.69508 1.19396 -0.02519 0.13474  -0.09307 35  GLU A N   
277  C CA  . GLU A 35  ? 1.13875 1.67335 1.21057 -0.05225 0.16467  -0.15690 35  GLU A CA  
278  C C   . GLU A 35  ? 1.12667 1.66912 1.17819 -0.06941 0.16655  -0.23740 35  GLU A C   
279  O O   . GLU A 35  ? 1.19155 1.68691 1.22017 -0.06846 0.21255  -0.27860 35  GLU A O   
280  C CB  . GLU A 35  ? 1.23445 1.69873 1.29740 -0.03734 0.22751  -0.14376 35  GLU A CB  
281  C CG  . GLU A 35  ? 1.26703 1.71230 1.34919 -0.02942 0.22772  -0.07308 35  GLU A CG  
282  C CD  . GLU A 35  ? 1.34004 1.71644 1.41334 -0.01170 0.29082  -0.05927 35  GLU A CD  
283  O OE1 . GLU A 35  ? 1.38986 1.74770 1.44661 0.01251  0.33093  -0.07366 35  GLU A OE1 
284  O OE2 . GLU A 35  ? 1.35573 1.69252 1.43419 -0.02089 0.30000  -0.03431 35  GLU A OE2 
285  N N   . PRO A 36  ? 1.05348 1.65077 1.10985 -0.08615 0.11533  -0.26104 36  PRO A N   
286  C CA  . PRO A 36  ? 1.04316 1.64955 1.08340 -0.10637 0.11422  -0.33732 36  PRO A CA  
287  C C   . PRO A 36  ? 1.02118 1.59170 1.05381 -0.14154 0.12612  -0.39128 36  PRO A C   
288  O O   . PRO A 36  ? 1.00985 1.56838 1.05037 -0.15311 0.11659  -0.37387 36  PRO A O   
289  C CB  . PRO A 36  ? 0.97886 1.66063 1.03081 -0.10870 0.05200  -0.33290 36  PRO A CB  
290  C CG  . PRO A 36  ? 0.94471 1.63944 1.01189 -0.10725 0.01557  -0.27543 36  PRO A CG  
291  C CD  . PRO A 36  ? 0.99313 1.64411 1.06680 -0.08727 0.05341  -0.21836 36  PRO A CD  
292  N N   . GLU A 37  ? 1.01381 1.56561 1.02922 -0.15874 0.14746  -0.45531 37  GLU A N   
293  C CA  . GLU A 37  ? 0.98174 1.51402 0.99482 -0.19580 0.15402  -0.50997 37  GLU A CA  
294  C C   . GLU A 37  ? 0.90209 1.49522 0.92516 -0.21656 0.10913  -0.54998 37  GLU A C   
295  O O   . GLU A 37  ? 0.89492 1.47916 0.94100 -0.23504 0.10453  -0.55341 37  GLU A O   
296  C CB  . GLU A 37  ? 1.05605 1.52251 1.04375 -0.20663 0.20356  -0.55229 37  GLU A CB  
297  C CG  . GLU A 37  ? 1.11019 1.50667 1.08540 -0.18650 0.25159  -0.51588 37  GLU A CG  
298  C CD  . GLU A 37  ? 1.19968 1.52385 1.13829 -0.19121 0.29672  -0.55568 37  GLU A CD  
299  O OE1 . GLU A 37  ? 1.21838 1.54911 1.13817 -0.20338 0.28905  -0.60416 37  GLU A OE1 
300  O OE2 . GLU A 37  ? 1.25750 1.51356 1.18241 -0.18307 0.33815  -0.53802 37  GLU A OE2 
301  N N   . ILE A 38  ? 1.06091 0.94867 0.78926 0.11670  0.13658  -0.19157 38  ILE A N   
302  C CA  . ILE A 38  ? 1.00700 0.94858 0.73403 0.09921  0.11692  -0.19854 38  ILE A CA  
303  C C   . ILE A 38  ? 0.94449 0.93270 0.70820 0.12286  0.10985  -0.18159 38  ILE A C   
304  O O   . ILE A 38  ? 0.96477 0.94271 0.73065 0.14240  0.12521  -0.17883 38  ILE A O   
305  C CB  . ILE A 38  ? 1.05684 0.98197 0.73579 0.07795  0.12576  -0.22244 38  ILE A CB  
306  C CG1 . ILE A 38  ? 1.12119 0.99345 0.75694 0.04853  0.13649  -0.24201 38  ILE A CG1 
307  C CG2 . ILE A 38  ? 1.02691 1.01545 0.70673 0.06438  0.10411  -0.22436 38  ILE A CG2 
308  C CD1 . ILE A 38  ? 1.10023 1.00069 0.74172 0.02284  0.11598  -0.24266 38  ILE A CD1 
309  N N   . VAL A 39  ? 0.88121 0.91771 0.67177 0.12022  0.08944  -0.17090 39  VAL A N   
310  C CA  . VAL A 39  ? 0.82077 0.89554 0.64062 0.13766  0.08442  -0.15587 39  VAL A CA  
311  C C   . VAL A 39  ? 0.79145 0.90409 0.60300 0.12844  0.07100  -0.15909 39  VAL A C   
312  O O   . VAL A 39  ? 0.76333 0.89928 0.57772 0.11475  0.05629  -0.16023 39  VAL A O   
313  C CB  . VAL A 39  ? 0.77132 0.86454 0.62871 0.14528  0.07663  -0.13793 39  VAL A CB  
314  C CG1 . VAL A 39  ? 0.72929 0.86021 0.60841 0.15430  0.07181  -0.12632 39  VAL A CG1 
315  C CG2 . VAL A 39  ? 0.78550 0.85175 0.65494 0.16136  0.09002  -0.12854 39  VAL A CG2 
316  N N   . ILE A 40  ? 0.79538 0.91563 0.59672 0.13744  0.07710  -0.15902 40  ILE A N   
317  C CA  . ILE A 40  ? 0.78150 0.93534 0.57113 0.13378  0.06659  -0.15822 40  ILE A CA  
318  C C   . ILE A 40  ? 0.74846 0.92286 0.56201 0.15056  0.06595  -0.14093 40  ILE A C   
319  O O   . ILE A 40  ? 0.75494 0.91858 0.57543 0.16276  0.07881  -0.13582 40  ILE A O   
320  C CB  . ILE A 40  ? 0.81915 0.96236 0.57010 0.12771  0.07503  -0.17115 40  ILE A CB  
321  C CG1 . ILE A 40  ? 0.86298 0.97821 0.58341 0.10540  0.07928  -0.19131 40  ILE A CG1 
322  C CG2 . ILE A 40  ? 0.80663 0.98961 0.54512 0.12688  0.06294  -0.16542 40  ILE A CG2 
323  C CD1 . ILE A 40  ? 0.91229 1.01264 0.58872 0.09364  0.08984  -0.20743 40  ILE A CD1 
324  N N   . SER A 41  ? 0.72392 0.92698 0.54842 0.15032  0.05335  -0.13243 41  SER A N   
325  C CA  . SER A 41  ? 0.70963 0.92435 0.54921 0.16297  0.05524  -0.11740 41  SER A CA  
326  C C   . SER A 41  ? 0.72526 0.95738 0.54396 0.16943  0.05223  -0.11203 41  SER A C   
327  O O   . SER A 41  ? 0.73963 0.99438 0.54574 0.16351  0.04077  -0.11538 41  SER A O   
328  C CB  . SER A 41  ? 0.68619 0.91285 0.55067 0.16034  0.04777  -0.11064 41  SER A CB  
329  O OG  . SER A 41  ? 0.68089 0.91255 0.55200 0.16977  0.05229  -0.09820 41  SER A OG  
330  N N   . ILE A 42  ? 0.72969 0.95438 0.54376 0.18063  0.06254  -0.10239 42  ILE A N   
331  C CA  . ILE A 42  ? 0.75504 0.99013 0.54479 0.18932  0.06218  -0.09389 42  ILE A CA  
332  C C   . ILE A 42  ? 0.75092 0.97824 0.54771 0.20120  0.07030  -0.07773 42  ILE A C   
333  O O   . ILE A 42  ? 0.74079 0.94915 0.54256 0.20087  0.08383  -0.07582 42  ILE A O   
334  C CB  . ILE A 42  ? 0.78617 1.00931 0.54844 0.18767  0.07151  -0.10071 42  ILE A CB  
335  C CG1 . ILE A 42  ? 0.80099 1.02363 0.54760 0.17283  0.06715  -0.11907 42  ILE A CG1 
336  C CG2 . ILE A 42  ? 0.81565 1.04903 0.55087 0.19687  0.07123  -0.08831 42  ILE A CG2 
337  C CD1 . ILE A 42  ? 0.83543 1.04499 0.54825 0.16891  0.07811  -0.12826 42  ILE A CD1 
338  N N   . GLY A 43  ? 0.76907 1.01115 0.56483 0.21121  0.06405  -0.06602 43  GLY A N   
339  C CA  . GLY A 43  ? 0.77422 0.99889 0.57174 0.22228  0.07543  -0.05155 43  GLY A CA  
340  C C   . GLY A 43  ? 0.76520 1.00460 0.57681 0.23086  0.06954  -0.04414 43  GLY A C   
341  O O   . GLY A 43  ? 0.78089 1.04547 0.58432 0.24472  0.06145  -0.03412 43  GLY A O   
342  N N   . GLY A 44  ? 0.73535 0.96364 0.56833 0.22292  0.07396  -0.04814 44  GLY A N   
343  C CA  . GLY A 44  ? 0.74082 0.98136 0.58833 0.22954  0.07140  -0.04366 44  GLY A CA  
344  C C   . GLY A 44  ? 0.73457 0.98064 0.60650 0.21108  0.06569  -0.05649 44  GLY A C   
345  O O   . GLY A 44  ? 0.73003 0.97266 0.60756 0.19592  0.06185  -0.06698 44  GLY A O   
346  N N   . ASP A 45  ? 0.74395 0.99780 0.62964 0.21366  0.06657  -0.05459 45  ASP A N   
347  C CA  . ASP A 45  ? 0.70777 0.96644 0.61350 0.19451  0.06151  -0.06575 45  ASP A CA  
348  C C   . ASP A 45  ? 0.68560 0.91660 0.59352 0.17843  0.07074  -0.06953 45  ASP A C   
349  O O   . ASP A 45  ? 0.65928 0.89570 0.57940 0.16241  0.06298  -0.07745 45  ASP A O   
350  C CB  . ASP A 45  ? 0.70971 0.97981 0.62743 0.20039  0.06489  -0.06295 45  ASP A CB  
351  C CG  . ASP A 45  ? 0.70577 1.02166 0.62997 0.21190  0.05161  -0.06018 45  ASP A CG  
352  O OD1 . ASP A 45  ? 0.69840 1.03692 0.61825 0.20459  0.03686  -0.06596 45  ASP A OD1 
353  O OD2 . ASP A 45  ? 0.70818 1.03932 0.64099 0.22735  0.05720  -0.05245 45  ASP A OD2 
354  N N   . GLY A 46  ? 0.69179 0.89484 0.58647 0.18167  0.08768  -0.06282 46  GLY A N   
355  C CA  . GLY A 46  ? 0.69879 0.88639 0.59513 0.16311  0.09578  -0.06586 46  GLY A CA  
356  C C   . GLY A 46  ? 0.70823 0.90726 0.61010 0.15858  0.08786  -0.06943 46  GLY A C   
357  O O   . GLY A 46  ? 0.69752 0.90425 0.61412 0.14407  0.08485  -0.07266 46  GLY A O   
358  N N   . THR A 47  ? 0.73306 0.93414 0.62217 0.17202  0.08556  -0.06784 47  THR A N   
359  C CA  . THR A 47  ? 0.71001 0.91760 0.60158 0.17006  0.08153  -0.07288 47  THR A CA  
360  C C   . THR A 47  ? 0.68374 0.90428 0.58972 0.16370  0.06787  -0.08113 47  THR A C   
361  O O   . THR A 47  ? 0.67163 0.89224 0.58772 0.15899  0.06772  -0.08391 47  THR A O   
362  C CB  . THR A 47  ? 0.71999 0.92535 0.58909 0.18308  0.08294  -0.07120 47  THR A CB  
363  O OG1 . THR A 47  ? 0.73901 0.92673 0.59057 0.18943  0.09686  -0.06143 47  THR A OG1 
364  C CG2 . THR A 47  ? 0.71129 0.91684 0.57954 0.18124  0.08472  -0.07780 47  THR A CG2 
365  N N   . PHE A 48  ? 0.67989 0.91169 0.58636 0.16414  0.05777  -0.08405 48  PHE A N   
366  C CA  . PHE A 48  ? 0.68810 0.92769 0.60367 0.15385  0.04658  -0.09256 48  PHE A CA  
367  C C   . PHE A 48  ? 0.69165 0.92851 0.62589 0.14155  0.04660  -0.09124 48  PHE A C   
368  O O   . PHE A 48  ? 0.69535 0.92780 0.63615 0.13582  0.04331  -0.09370 48  PHE A O   
369  C CB  . PHE A 48  ? 0.68797 0.94837 0.60087 0.15377  0.03653  -0.09573 48  PHE A CB  
370  C CG  . PHE A 48  ? 0.68388 0.95019 0.59934 0.13898  0.02639  -0.10627 48  PHE A CG  
371  C CD1 . PHE A 48  ? 0.66944 0.93695 0.59996 0.12675  0.02317  -0.10768 48  PHE A CD1 
372  C CD2 . PHE A 48  ? 0.69707 0.96399 0.59508 0.13424  0.02188  -0.11554 48  PHE A CD2 
373  C CE1 . PHE A 48  ? 0.66996 0.93728 0.59853 0.11144  0.01571  -0.11672 48  PHE A CE1 
374  C CE2 . PHE A 48  ? 0.70188 0.96603 0.59608 0.11708  0.01582  -0.12641 48  PHE A CE2 
375  C CZ  . PHE A 48  ? 0.68971 0.95310 0.59945 0.10634  0.01275  -0.12629 48  PHE A CZ  
376  N N   . LEU A 49  ? 0.69909 0.93643 0.63901 0.13738  0.05178  -0.08658 49  LEU A N   
377  C CA  . LEU A 49  ? 0.69630 0.93507 0.64997 0.12171  0.05175  -0.08500 49  LEU A CA  
378  C C   . LEU A 49  ? 0.69290 0.93297 0.65454 0.11894  0.05432  -0.08013 49  LEU A C   
379  O O   . LEU A 49  ? 0.68150 0.92810 0.65519 0.11162  0.04793  -0.07792 49  LEU A O   
380  C CB  . LEU A 49  ? 0.70049 0.93311 0.65102 0.11563  0.06230  -0.08260 49  LEU A CB  
381  C CG  . LEU A 49  ? 0.70662 0.94259 0.65651 0.11816  0.06187  -0.08574 49  LEU A CG  
382  C CD1 . LEU A 49  ? 0.72491 0.94291 0.66606 0.11506  0.07903  -0.08366 49  LEU A CD1 
383  C CD2 . LEU A 49  ? 0.69643 0.94600 0.65834 0.10386  0.05036  -0.09110 49  LEU A CD2 
384  N N   . SER A 50  ? 0.71265 0.94909 0.66801 0.12580  0.06436  -0.07673 50  SER A N   
385  C CA  . SER A 50  ? 0.71752 0.96421 0.68396 0.12586  0.06806  -0.07137 50  SER A CA  
386  C C   . SER A 50  ? 0.71364 0.95846 0.68598 0.13584  0.06210  -0.07296 50  SER A C   
387  O O   . SER A 50  ? 0.71606 0.97223 0.70492 0.13519  0.06033  -0.06599 50  SER A O   
388  C CB  . SER A 50  ? 0.73272 0.97522 0.68816 0.13209  0.08096  -0.06953 50  SER A CB  
389  O OG  . SER A 50  ? 0.73448 0.96991 0.67970 0.12084  0.09077  -0.06761 50  SER A OG  
390  N N   . ALA A 51  ? 0.72740 0.95739 0.68397 0.14474  0.06020  -0.08134 51  ALA A N   
391  C CA  . ALA A 51  ? 0.74616 0.96324 0.69980 0.15124  0.05914  -0.08592 51  ALA A CA  
392  C C   . ALA A 51  ? 0.73028 0.94400 0.69233 0.14245  0.05027  -0.08495 51  ALA A C   
393  O O   . ALA A 51  ? 0.74229 0.94588 0.71003 0.14823  0.05273  -0.08090 51  ALA A O   
394  C CB  . ALA A 51  ? 0.77040 0.97457 0.69935 0.15486  0.05875  -0.09738 51  ALA A CB  
395  N N   . PHE A 52  ? 0.71303 0.93358 0.67493 0.12987  0.04179  -0.08750 52  PHE A N   
396  C CA  . PHE A 52  ? 0.69676 0.91474 0.66424 0.11827  0.03383  -0.08648 52  PHE A CA  
397  C C   . PHE A 52  ? 0.68072 0.91043 0.66679 0.11636  0.03379  -0.07238 52  PHE A C   
398  O O   . PHE A 52  ? 0.68144 0.90169 0.67108 0.11824  0.03174  -0.06610 52  PHE A O   
399  C CB  . PHE A 52  ? 0.67786 0.90676 0.64364 0.10537  0.02734  -0.09188 52  PHE A CB  
400  C CG  . PHE A 52  ? 0.66604 0.89762 0.63903 0.08983  0.02079  -0.08900 52  PHE A CG  
401  C CD1 . PHE A 52  ? 0.67985 0.89691 0.64455 0.08217  0.01573  -0.09378 52  PHE A CD1 
402  C CD2 . PHE A 52  ? 0.64903 0.89507 0.63243 0.07958  0.02114  -0.08227 52  PHE A CD2 
403  C CE1 . PHE A 52  ? 0.67844 0.89628 0.64663 0.06679  0.01024  -0.09007 52  PHE A CE1 
404  C CE2 . PHE A 52  ? 0.64989 0.89962 0.63668 0.06330  0.01513  -0.07941 52  PHE A CE2 
405  C CZ  . PHE A 52  ? 0.66403 0.90007 0.64395 0.05803  0.00922  -0.08238 52  PHE A CZ  
406  N N   . HIS A 53  ? 0.67262 0.92341 0.66835 0.11166  0.03683  -0.06622 53  HIS A N   
407  C CA  . HIS A 53  ? 0.68009 0.95421 0.69320 0.10531  0.03520  -0.05223 53  HIS A CA  
408  C C   . HIS A 53  ? 0.71012 0.99250 0.73593 0.12334  0.04068  -0.04171 53  HIS A C   
409  O O   . HIS A 53  ? 0.71357 1.01637 0.75573 0.12436  0.03694  -0.02665 53  HIS A O   
410  C CB  . HIS A 53  ? 0.66044 0.95352 0.67463 0.08920  0.03933  -0.05147 53  HIS A CB  
411  C CG  . HIS A 53  ? 0.65191 0.94022 0.65784 0.07076  0.03607  -0.05793 53  HIS A CG  
412  N ND1 . HIS A 53  ? 0.64520 0.94923 0.65637 0.05151  0.02975  -0.05199 53  HIS A ND1 
413  C CD2 . HIS A 53  ? 0.65026 0.92230 0.64335 0.06998  0.03929  -0.06892 53  HIS A CD2 
414  C CE1 . HIS A 53  ? 0.64386 0.93773 0.64453 0.03826  0.03102  -0.06138 53  HIS A CE1 
415  N NE2 . HIS A 53  ? 0.64930 0.92499 0.64096 0.05106  0.03709  -0.07101 53  HIS A NE2 
416  N N   . GLN A 54  ? 0.73912 1.00863 0.75776 0.13869  0.05012  -0.04807 54  GLN A N   
417  C CA  . GLN A 54  ? 0.76470 1.04083 0.79569 0.15837  0.05900  -0.03930 54  GLN A CA  
418  C C   . GLN A 54  ? 0.80454 1.05651 0.83514 0.17168  0.05890  -0.03447 54  GLN A C   
419  O O   . GLN A 54  ? 0.82097 1.08467 0.86888 0.18941  0.06496  -0.01992 54  GLN A O   
420  C CB  . GLN A 54  ? 0.76903 1.03179 0.78689 0.16953  0.07096  -0.04955 54  GLN A CB  
421  C CG  . GLN A 54  ? 0.78120 1.05494 0.81316 0.18993  0.08403  -0.04164 54  GLN A CG  
422  C CD  . GLN A 54  ? 0.80134 1.05355 0.81379 0.19992  0.09696  -0.05425 54  GLN A CD  
423  O OE1 . GLN A 54  ? 0.80271 1.03883 0.79209 0.19097  0.09452  -0.06630 54  GLN A OE1 
424  N NE2 . GLN A 54  ? 0.82265 1.07678 0.84404 0.21968  0.11158  -0.05026 54  GLN A NE2 
425  N N   . TYR A 55  ? 0.82781 1.04643 0.83830 0.16364  0.05368  -0.04545 55  TYR A N   
426  C CA  . TYR A 55  ? 0.87046 1.05366 0.87157 0.17220  0.05667  -0.04323 55  TYR A CA  
427  C C   . TYR A 55  ? 0.86919 1.04662 0.86523 0.15354  0.04418  -0.04153 55  TYR A C   
428  O O   . TYR A 55  ? 0.89901 1.03768 0.87427 0.14925  0.04559  -0.04901 55  TYR A O   
429  C CB  . TYR A 55  ? 0.90918 1.04904 0.88166 0.17667  0.06712  -0.06183 55  TYR A CB  
430  C CG  . TYR A 55  ? 0.92734 1.06739 0.90008 0.19471  0.08196  -0.06470 55  TYR A CG  
431  C CD1 . TYR A 55  ? 0.95938 1.08754 0.94097 0.21922  0.09735  -0.05443 55  TYR A CD1 
432  C CD2 . TYR A 55  ? 0.91533 1.06707 0.87861 0.18884  0.08216  -0.07638 55  TYR A CD2 
433  C CE1 . TYR A 55  ? 0.97405 1.10398 0.95596 0.23512  0.11314  -0.05818 55  TYR A CE1 
434  C CE2 . TYR A 55  ? 0.92979 1.08124 0.89031 0.20293  0.09642  -0.07924 55  TYR A CE2 
435  C CZ  . TYR A 55  ? 0.95832 1.09973 0.92852 0.22488  0.11217  -0.07140 55  TYR A CZ  
436  O OH  . TYR A 55  ? 0.97460 1.11727 0.94211 0.23831  0.12846  -0.07539 55  TYR A OH  
437  N N   . GLU A 56  ? 0.84142 1.05533 0.85280 0.13913  0.03362  -0.03301 56  GLU A N   
438  C CA  . GLU A 56  ? 0.83753 1.04796 0.84216 0.11861  0.02289  -0.03344 56  GLU A CA  
439  C C   . GLU A 56  ? 0.86178 1.05733 0.86681 0.12431  0.02114  -0.01649 56  GLU A C   
440  O O   . GLU A 56  ? 0.87096 1.05878 0.86666 0.10653  0.01331  -0.01620 56  GLU A O   
441  C CB  . GLU A 56  ? 0.80565 1.05463 0.82142 0.09944  0.01544  -0.03104 56  GLU A CB  
442  C CG  . GLU A 56  ? 0.79853 1.08757 0.83575 0.10116  0.01351  -0.01129 56  GLU A CG  
443  C CD  . GLU A 56  ? 0.77659 1.09639 0.81618 0.07555  0.00927  -0.01320 56  GLU A CD  
444  O OE1 . GLU A 56  ? 0.76558 1.07763 0.79567 0.06807  0.01442  -0.02875 56  GLU A OE1 
445  O OE2 . GLU A 56  ? 0.77592 1.12600 0.82415 0.06264  0.00200  0.00137  56  GLU A OE2 
446  N N   . GLU A 57  ? 0.87892 1.06948 0.89368 0.15001  0.02972  -0.00125 57  GLU A N   
447  C CA  . GLU A 57  ? 0.91739 1.08752 0.93065 0.16240  0.03108  0.01868  57  GLU A CA  
448  C C   . GLU A 57  ? 0.96645 1.06863 0.95252 0.17564  0.04647  0.00985  57  GLU A C   
449  O O   . GLU A 57  ? 0.99854 1.06945 0.97760 0.18968  0.05246  0.02661  57  GLU A O   
450  C CB  . GLU A 57  ? 0.92503 1.13965 0.96943 0.18545  0.03183  0.04668  57  GLU A CB  
451  C CG  . GLU A 57  ? 0.89497 1.17558 0.96002 0.16516  0.01607  0.05839  57  GLU A CG  
452  C CD  . GLU A 57  ? 0.90183 1.23852 0.99873 0.18470  0.01494  0.08772  57  GLU A CD  
453  O OE1 . GLU A 57  ? 0.92948 1.25659 1.03704 0.21838  0.02836  0.09786  57  GLU A OE1 
454  O OE2 . GLU A 57  ? 0.88208 1.27526 0.99282 0.16548  0.00161  0.10050  57  GLU A OE2 
455  N N   . ARG A 58  ? 0.97961 1.05657 0.94685 0.17043  0.05415  -0.01538 58  ARG A N   
456  C CA  . ARG A 58  ? 1.03769 1.04818 0.97054 0.17257  0.06949  -0.02992 58  ARG A CA  
457  C C   . ARG A 58  ? 1.03478 1.03537 0.94274 0.14211  0.06363  -0.05752 58  ARG A C   
458  O O   . ARG A 58  ? 1.06986 1.03728 0.95162 0.13855  0.07456  -0.07708 58  ARG A O   
459  C CB  . ARG A 58  ? 1.07114 1.06206 1.00304 0.20022  0.08941  -0.03195 58  ARG A CB  
460  C CG  . ARG A 58  ? 1.09956 1.09211 1.05323 0.23558  0.10032  -0.00353 58  ARG A CG  
461  C CD  . ARG A 58  ? 1.13429 1.10524 1.08612 0.26371  0.12400  -0.00785 58  ARG A CD  
462  N NE  . ARG A 58  ? 1.19977 1.09191 1.10581 0.25882  0.14379  -0.03013 58  ARG A NE  
463  C CZ  . ARG A 58  ? 1.20836 1.08598 1.08966 0.24245  0.14892  -0.05835 58  ARG A CZ  
464  N NH1 . ARG A 58  ? 1.15646 1.08798 1.05434 0.23362  0.13672  -0.06618 58  ARG A NH1 
465  N NH2 . ARG A 58  ? 1.27463 1.08049 1.10997 0.23326  0.16769  -0.07866 58  ARG A NH2 
466  N N   . LEU A 59  ? 0.99346 1.02660 0.90899 0.11908  0.04694  -0.05913 59  LEU A N   
467  C CA  . LEU A 59  ? 0.99335 1.03148 0.89251 0.09317  0.04051  -0.08208 59  LEU A CA  
468  C C   . LEU A 59  ? 1.06130 1.04731 0.92328 0.07592  0.04829  -0.09656 59  LEU A C   
469  O O   . LEU A 59  ? 1.08920 1.07467 0.93200 0.05876  0.04831  -0.11794 59  LEU A O   
470  C CB  . LEU A 59  ? 0.93755 1.01801 0.85315 0.07484  0.02503  -0.07922 59  LEU A CB  
471  C CG  . LEU A 59  ? 0.88781 1.01627 0.83230 0.08314  0.01932  -0.07016 59  LEU A CG  
472  C CD1 . LEU A 59  ? 0.85799 1.01644 0.81166 0.06276  0.00866  -0.06904 59  LEU A CD1 
473  C CD2 . LEU A 59  ? 0.87139 1.01261 0.81578 0.09080  0.02296  -0.08259 59  LEU A CD2 
474  N N   . ASP A 60  ? 1.10503 1.04776 0.95396 0.07872  0.05554  -0.08454 60  ASP A N   
475  C CA  . ASP A 60  ? 1.16883 1.05451 0.97646 0.05716  0.06545  -0.09895 60  ASP A CA  
476  C C   . ASP A 60  ? 1.22049 1.05421 0.99682 0.06342  0.08596  -0.11451 60  ASP A C   
477  O O   . ASP A 60  ? 1.29550 1.08400 1.03122 0.03782  0.09547  -0.13333 60  ASP A O   
478  C CB  . ASP A 60  ? 1.21883 1.06569 1.01684 0.05899  0.06936  -0.07911 60  ASP A CB  
479  C CG  . ASP A 60  ? 1.24877 1.06323 1.01174 0.02185  0.07005  -0.09353 60  ASP A CG  
480  O OD1 . ASP A 60  ? 1.20201 1.06306 0.97558 -0.00331 0.05422  -0.10169 60  ASP A OD1 
481  O OD2 . ASP A 60  ? 1.31903 1.05996 1.04241 0.01720  0.08862  -0.09717 60  ASP A OD2 
482  N N   . GLU A 61  ? 1.19582 1.03501 0.98717 0.09329  0.09450  -0.10873 61  GLU A N   
483  C CA  . GLU A 61  ? 1.23677 1.02433 0.99712 0.10079  0.11721  -0.12361 61  GLU A CA  
484  C C   . GLU A 61  ? 1.18991 1.01696 0.95560 0.09974  0.11331  -0.13936 61  GLU A C   
485  O O   . GLU A 61  ? 1.23318 1.03122 0.98351 0.11382  0.13169  -0.14696 61  GLU A O   
486  C CB  . GLU A 61  ? 1.27984 1.02922 1.04773 0.14050  0.13726  -0.10238 61  GLU A CB  
487  C CG  . GLU A 61  ? 1.30995 1.04209 1.08695 0.15228  0.13597  -0.07514 61  GLU A CG  
488  C CD  . GLU A 61  ? 1.27391 1.05798 1.10020 0.18791  0.12900  -0.04371 61  GLU A CD  
489  O OE1 . GLU A 61  ? 1.26191 1.06656 1.10713 0.21219  0.13720  -0.04201 61  GLU A OE1 
490  O OE2 . GLU A 61  ? 1.25564 1.06380 1.10045 0.18884  0.11530  -0.02102 61  GLU A OE2 
491  N N   . ILE A 62  ? 1.11059 1.00051 0.89554 0.08452  0.09170  -0.14364 62  ILE A N   
492  C CA  . ILE A 62  ? 1.04915 0.98030 0.84172 0.08758  0.08653  -0.15255 62  ILE A CA  
493  C C   . ILE A 62  ? 1.00868 0.97739 0.79234 0.05770  0.07051  -0.16818 62  ILE A C   
494  O O   . ILE A 62  ? 0.98504 0.97550 0.77927 0.04226  0.05764  -0.16518 62  ILE A O   
495  C CB  . ILE A 62  ? 0.98549 0.96486 0.82158 0.11248  0.07864  -0.13275 62  ILE A CB  
496  C CG1 . ILE A 62  ? 1.00591 0.96210 0.85260 0.14372  0.09576  -0.11858 62  ILE A CG1 
497  C CG2 . ILE A 62  ? 0.94513 0.96890 0.78754 0.11101  0.07043  -0.14003 62  ILE A CG2 
498  C CD1 . ILE A 62  ? 0.95473 0.96251 0.84155 0.16309  0.08953  -0.10078 62  ILE A CD1 
499  N N   . ALA A 63  ? 0.99693 0.97693 0.76103 0.04989  0.07182  -0.18393 63  ALA A N   
500  C CA  . ALA A 63  ? 0.96148 0.99564 0.72580 0.03051  0.05499  -0.19301 63  ALA A CA  
501  C C   . ALA A 63  ? 0.90748 0.98320 0.69130 0.05123  0.04953  -0.18524 63  ALA A C   
502  O O   . ALA A 63  ? 0.93538 0.99365 0.70560 0.06288  0.06099  -0.18866 63  ALA A O   
503  C CB  . ALA A 63  ? 1.01647 1.03657 0.73632 -0.00162 0.05904  -0.21689 63  ALA A CB  
504  N N   . PHE A 64  ? 0.83889 0.96464 0.65155 0.05558  0.03474  -0.17497 64  PHE A N   
505  C CA  . PHE A 64  ? 0.79412 0.95379 0.62285 0.07472  0.03107  -0.16556 64  PHE A CA  
506  C C   . PHE A 64  ? 0.80043 0.99827 0.61323 0.06530  0.02227  -0.17347 64  PHE A C   
507  O O   . PHE A 64  ? 0.80443 1.02351 0.60676 0.04306  0.01372  -0.18324 64  PHE A O   
508  C CB  . PHE A 64  ? 0.73570 0.92171 0.59898 0.08481  0.02387  -0.15003 64  PHE A CB  
509  C CG  . PHE A 64  ? 0.71812 0.88128 0.59949 0.09566  0.03043  -0.13820 64  PHE A CG  
510  C CD1 . PHE A 64  ? 0.70055 0.86355 0.59412 0.11494  0.03793  -0.12801 64  PHE A CD1 
511  C CD2 . PHE A 64  ? 0.71670 0.86394 0.60258 0.08527  0.02863  -0.13580 64  PHE A CD2 
512  C CE1 . PHE A 64  ? 0.68898 0.84416 0.60178 0.12371  0.04231  -0.11531 64  PHE A CE1 
513  C CE2 . PHE A 64  ? 0.70471 0.83978 0.60770 0.09602  0.03268  -0.12145 64  PHE A CE2 
514  C CZ  . PHE A 64  ? 0.69140 0.83456 0.60948 0.11530  0.03886  -0.11095 64  PHE A CZ  
515  N N   . ILE A 65  ? 0.80860 1.01888 0.61901 0.08164  0.02443  -0.16791 65  ILE A N   
516  C CA  . ILE A 65  ? 0.82138 1.07332 0.61815 0.07883  0.01533  -0.16914 65  ILE A CA  
517  C C   . ILE A 65  ? 0.79095 1.06045 0.60401 0.10466  0.01565  -0.15173 65  ILE A C   
518  O O   . ILE A 65  ? 0.78462 1.02712 0.60146 0.11912  0.02707  -0.14625 65  ILE A O   
519  C CB  . ILE A 65  ? 0.87169 1.10805 0.62783 0.06473  0.02159  -0.18485 65  ILE A CB  
520  C CG1 . ILE A 65  ? 0.90931 1.11066 0.64133 0.03724  0.02768  -0.20402 65  ILE A CG1 
521  C CG2 . ILE A 65  ? 0.87559 1.16619 0.61721 0.05921  0.00872  -0.18358 65  ILE A CG2 
522  C CD1 . ILE A 65  ? 0.96020 1.10880 0.65642 0.03267  0.04676  -0.21824 65  ILE A CD1 
523  N N   . GLY A 66  ? 0.78924 1.10361 0.61072 0.11078  0.00500  -0.14235 66  GLY A N   
524  C CA  . GLY A 66  ? 0.76384 1.08758 0.59558 0.13526  0.00792  -0.12480 66  GLY A CA  
525  C C   . GLY A 66  ? 0.78671 1.14030 0.59648 0.14221  0.00278  -0.11892 66  GLY A C   
526  O O   . GLY A 66  ? 0.79461 1.18920 0.59451 0.13042  -0.00951 -0.12293 66  GLY A O   
527  N N   . ILE A 67  ? 0.79103 1.12729 0.59239 0.15944  0.01209  -0.10857 67  ILE A N   
528  C CA  . ILE A 67  ? 0.83590 1.19706 0.61517 0.17014  0.00843  -0.09771 67  ILE A CA  
529  C C   . ILE A 67  ? 0.86871 1.22064 0.65789 0.19620  0.01670  -0.07665 67  ILE A C   
530  O O   . ILE A 67  ? 0.87474 1.18744 0.66699 0.20102  0.03095  -0.07530 67  ILE A O   
531  C CB  . ILE A 67  ? 0.86256 1.20268 0.60869 0.16137  0.01553  -0.10788 67  ILE A CB  
532  C CG1 . ILE A 67  ? 0.87441 1.21209 0.60360 0.13330  0.01218  -0.13094 67  ILE A CG1 
533  C CG2 . ILE A 67  ? 0.90086 1.26817 0.62127 0.17194  0.01107  -0.09397 67  ILE A CG2 
534  C CD1 . ILE A 67  ? 0.91080 1.22123 0.60394 0.12307  0.02339  -0.14426 67  ILE A CD1 
535  N N   . HIS A 68  ? 0.91751 1.30561 0.71061 0.21267  0.00950  -0.05976 68  HIS A N   
536  C CA  . HIS A 68  ? 0.96801 1.33897 0.76562 0.23867  0.02103  -0.03910 68  HIS A CA  
537  C C   . HIS A 68  ? 1.05544 1.42288 0.82188 0.25257  0.02488  -0.02454 68  HIS A C   
538  O O   . HIS A 68  ? 1.05854 1.46932 0.80935 0.25595  0.01190  -0.01690 68  HIS A O   
539  C CB  . HIS A 68  ? 0.93722 1.34242 0.75675 0.25487  0.01608  -0.02609 68  HIS A CB  
540  C CG  . HIS A 68  ? 0.93084 1.40019 0.74437 0.26370  -0.00022 -0.01442 68  HIS A CG  
541  N ND1 . HIS A 68  ? 0.91594 1.43631 0.73470 0.24198  -0.01796 -0.02761 68  HIS A ND1 
542  C CD2 . HIS A 68  ? 0.95249 1.44705 0.75438 0.29109  -0.00146 0.01081  68  HIS A CD2 
543  C CE1 . HIS A 68  ? 0.93382 1.51609 0.74654 0.25353  -0.03103 -0.01171 68  HIS A CE1 
544  N NE2 . HIS A 68  ? 0.95791 1.52672 0.76141 0.28584  -0.02191 0.01335  68  HIS A NE2 
545  N N   . THR A 69  ? 0.97360 1.20079 0.74955 0.33370  0.10610  0.18534  69  THR A N   
546  C CA  . THR A 69  ? 1.04916 1.23739 0.77796 0.36889  0.11554  0.18726  69  THR A CA  
547  C C   . THR A 69  ? 1.07509 1.23739 0.78574 0.39302  0.12371  0.19305  69  THR A C   
548  O O   . THR A 69  ? 1.17375 1.32786 0.82914 0.43950  0.12424  0.18974  69  THR A O   
549  C CB  . THR A 69  ? 1.07658 1.19115 0.81074 0.34472  0.14427  0.20375  69  THR A CB  
550  O OG1 . THR A 69  ? 1.03547 1.11340 0.82271 0.30306  0.15909  0.21376  69  THR A OG1 
551  C CG2 . THR A 69  ? 1.07411 1.20867 0.80365 0.33379  0.14042  0.19524  69  THR A CG2 
552  N N   . GLY A 70  ? 0.97080 1.11687 0.71933 0.36591  0.13153  0.20120  70  GLY A N   
553  C CA  . GLY A 70  ? 0.97517 1.10427 0.70129 0.38998  0.13755  0.20372  70  GLY A CA  
554  C C   . GLY A 70  ? 0.97706 1.19140 0.69916 0.41747  0.10616  0.18187  70  GLY A C   
555  O O   . GLY A 70  ? 1.02810 1.30824 0.72948 0.44857  0.08058  0.15777  70  GLY A O   
556  N N   . HIS A 71  ? 0.91838 1.14284 0.66542 0.40641  0.10461  0.18266  71  HIS A N   
557  C CA  . HIS A 71  ? 0.83726 1.15492 0.59891 0.42509  0.07229  0.15470  71  HIS A CA  
558  C C   . HIS A 71  ? 0.71802 1.11118 0.55422 0.38773  0.05478  0.13849  71  HIS A C   
559  O O   . HIS A 71  ? 0.65388 1.01257 0.51697 0.35240  0.07038  0.15926  71  HIS A O   
560  C CB  . HIS A 71  ? 0.80077 1.09788 0.55747 0.43397  0.07913  0.16048  71  HIS A CB  
561  C CG  . HIS A 71  ? 0.85616 1.09905 0.54136 0.48294  0.09251  0.16828  71  HIS A CG  
562  N ND1 . HIS A 71  ? 0.88568 1.02508 0.54210 0.47894  0.13013  0.19628  71  HIS A ND1 
563  C CD2 . HIS A 71  ? 0.92318 1.20319 0.56038 0.53996  0.07433  0.14883  71  HIS A CD2 
564  C CE1 . HIS A 71  ? 0.98520 1.09054 0.57258 0.53216  0.13872  0.19986  71  HIS A CE1 
565  N NE2 . HIS A 71  ? 1.01464 1.20247 0.58489 0.57313  0.10450  0.17294  71  HIS A NE2 
566  N N   . LEU A 72  ? 0.69545 1.19741 0.57746 0.39384  0.02699  0.09276  72  LEU A N   
567  C CA  . LEU A 72  ? 0.63922 1.21950 0.61600 0.34411  0.02820  0.05709  72  LEU A CA  
568  C C   . LEU A 72  ? 0.61939 1.14221 0.62720 0.29283  0.05682  0.08271  72  LEU A C   
569  O O   . LEU A 72  ? 0.63560 1.14905 0.63928 0.31023  0.06087  0.09852  72  LEU A O   
570  C CB  . LEU A 72  ? 0.62074 1.32847 0.65011 0.34734  0.00231  -0.01026 72  LEU A CB  
571  C CG  . LEU A 72  ? 0.55359 1.32714 0.68317 0.27685  0.02100  -0.05512 72  LEU A CG  
572  C CD1 . LEU A 72  ? 0.54653 1.31416 0.70148 0.22540  0.03081  -0.08318 72  LEU A CD1 
573  C CD2 . LEU A 72  ? 0.56628 1.44527 0.74322 0.27936  0.00073  -0.11493 72  LEU A CD2 
574  N N   . GLY A 73  ? 0.60816 1.08931 0.63949 0.23555  0.07629  0.08614  73  GLY A N   
575  C CA  . GLY A 73  ? 0.60040 1.03753 0.65502 0.19060  0.10067  0.10347  73  GLY A CA  
576  C C   . GLY A 73  ? 0.60737 1.09658 0.72176 0.14006  0.11450  0.06129  73  GLY A C   
577  O O   . GLY A 73  ? 0.64591 1.20659 0.79553 0.13087  0.10613  0.01277  73  GLY A O   
578  N N   . PHE A 74  ? 0.55676 1.00771 0.68029 0.10627  0.13970  0.07730  74  PHE A N   
579  C CA  . PHE A 74  ? 0.55300 1.02970 0.72311 0.05306  0.16760  0.04379  74  PHE A CA  
580  C C   . PHE A 74  ? 0.60126 1.00946 0.76351 0.01402  0.18954  0.04718  74  PHE A C   
581  O O   . PHE A 74  ? 0.64141 1.07209 0.84495 -0.03052 0.21392  0.00662  74  PHE A O   
582  C CB  . PHE A 74  ? 0.51131 0.96795 0.67993 0.03721  0.19152  0.06094  74  PHE A CB  
583  C CG  . PHE A 74  ? 0.47356 1.02501 0.67999 0.05548  0.18329  0.03014  74  PHE A CG  
584  C CD1 . PHE A 74  ? 0.44861 1.01979 0.63254 0.11344  0.15310  0.04366  74  PHE A CD1 
585  C CD2 . PHE A 74  ? 0.47076 1.09193 0.73698 0.01640  0.20923  -0.01627 74  PHE A CD2 
586  C CE1 . PHE A 74  ? 0.43096 1.07663 0.64176 0.13795  0.14123  0.01491  74  PHE A CE1 
587  C CE2 . PHE A 74  ? 0.45559 1.15525 0.75657 0.03692  0.19472  -0.04901 74  PHE A CE2 
588  C CZ  . PHE A 74  ? 0.43634 1.14702 0.70645 0.10014  0.15754  -0.03288 74  PHE A CZ  
589  N N   . TYR A 75  ? 0.61965 0.94438 0.73322 0.02929  0.18495  0.09072  75  TYR A N   
590  C CA  . TYR A 75  ? 0.65440 0.91151 0.75430 0.00559  0.20137  0.09513  75  TYR A CA  
591  C C   . TYR A 75  ? 0.64826 0.92412 0.74558 0.02503  0.17920  0.07880  75  TYR A C   
592  O O   . TYR A 75  ? 0.66493 0.92056 0.77277 -0.00082 0.19256  0.05496  75  TYR A O   
593  C CB  . TYR A 75  ? 0.65556 0.81902 0.70662 0.01466  0.20955  0.14665  75  TYR A CB  
594  C CG  . TYR A 75  ? 0.65295 0.79513 0.68967 0.00529  0.22811  0.16576  75  TYR A CG  
595  C CD1 . TYR A 75  ? 0.69598 0.81849 0.73949 -0.03472 0.26706  0.15253  75  TYR A CD1 
596  C CD2 . TYR A 75  ? 0.62594 0.75904 0.63957 0.03370  0.20433  0.18745  75  TYR A CD2 
597  C CE1 . TYR A 75  ? 0.72749 0.82353 0.74327 -0.04023 0.27176  0.16162  75  TYR A CE1 
598  C CE2 . TYR A 75  ? 0.64660 0.75850 0.64196 0.02736  0.20751  0.19012  75  TYR A CE2 
599  C CZ  . TYR A 75  ? 0.70197 0.79632 0.69305 -0.00692 0.24027  0.17997  75  TYR A CZ  
600  O OH  . TYR A 75  ? 0.73668 0.81090 0.70052 -0.01039 0.24597  0.18454  75  TYR A OH  
601  N N   . ALA A 76  ? 0.64009 0.94758 0.71782 0.07073  0.15027  0.08987  76  ALA A N   
602  C CA  . ALA A 76  ? 0.67413 1.00248 0.73632 0.09635  0.13116  0.07513  76  ALA A CA  
603  C C   . ALA A 76  ? 0.70006 1.13670 0.79140 0.11062  0.10975  0.02271  76  ALA A C   
604  O O   . ALA A 76  ? 0.70746 1.18575 0.77387 0.16083  0.08570  0.02715  76  ALA A O   
605  C CB  . ALA A 76  ? 0.66082 0.94901 0.67388 0.13930  0.12130  0.11860  76  ALA A CB  
606  N N   . ASP A 77  ? 0.72183 1.20368 0.86605 0.06772  0.12085  -0.03085 77  ASP A N   
607  C CA  . ASP A 77  ? 0.71788 1.32681 0.91011 0.07445  0.09979  -0.09807 77  ASP A CA  
608  C C   . ASP A 77  ? 0.73760 1.38957 0.93090 0.08188  0.08139  -0.14561 77  ASP A C   
609  O O   . ASP A 77  ? 0.76151 1.49510 1.01719 0.04936  0.08203  -0.21859 77  ASP A O   
610  C CB  . ASP A 77  ? 0.73433 1.38386 0.99986 0.01547  0.12958  -0.13986 77  ASP A CB  
611  C CG  . ASP A 77  ? 0.78200 1.33115 1.05410 -0.04860 0.17726  -0.13214 77  ASP A CG  
612  O OD1 . ASP A 77  ? 0.80510 1.27369 1.03737 -0.04640 0.18052  -0.10866 77  ASP A OD1 
613  O OD2 . ASP A 77  ? 0.80684 1.35325 1.11944 -0.09819 0.21537  -0.14888 77  ASP A OD2 
614  N N   . TRP A 78  ? 0.72910 1.33009 0.85522 0.12316  0.06752  -0.10987 78  TRP A N   
615  C CA  . TRP A 78  ? 0.75899 1.39900 0.86847 0.14247  0.04742  -0.15019 78  TRP A CA  
616  C C   . TRP A 78  ? 0.76831 1.39755 0.79223 0.21891  0.02253  -0.10978 78  TRP A C   
617  O O   . TRP A 78  ? 0.76860 1.30286 0.74383 0.23232  0.03869  -0.04312 78  TRP A O   
618  C CB  . TRP A 78  ? 0.77551 1.33054 0.88536 0.09900  0.07524  -0.14994 78  TRP A CB  
619  C CG  . TRP A 78  ? 0.79371 1.36929 0.97752 0.03072  0.09981  -0.21299 78  TRP A CG  
620  C CD1 . TRP A 78  ? 0.79376 1.30945 1.01411 -0.02667 0.14125  -0.20344 78  TRP A CD1 
621  C CD2 . TRP A 78  ? 0.82715 1.48367 1.05426 0.01101  0.09040  -0.29897 78  TRP A CD2 
622  N NE1 . TRP A 78  ? 0.83189 1.37462 1.11595 -0.08554 0.16583  -0.27550 78  TRP A NE1 
623  C CE2 . TRP A 78  ? 0.84696 1.48227 1.14405 -0.06660 0.13361  -0.33995 78  TRP A CE2 
624  C CE3 . TRP A 78  ? 0.85096 1.59482 1.06012 0.05273  0.05151  -0.34815 78  TRP A CE3 
625  C CZ2 . TRP A 78  ? 0.88565 1.58605 1.24825 -0.11174 0.14172  -0.43427 78  TRP A CZ2 
626  C CZ3 . TRP A 78  ? 0.88495 1.70593 1.15702 0.01410  0.05088  -0.44383 78  TRP A CZ3 
627  C CH2 . TRP A 78  ? 0.89965 1.69964 1.25418 -0.07142 0.09692  -0.48905 78  TRP A CH2 
628  N N   . ARG A 79  ? 0.78683 1.51270 0.79016 0.27038  -0.01385 -0.15220 79  ARG A N   
629  C CA  . ARG A 79  ? 0.80543 1.50183 0.70815 0.34754  -0.02898 -0.10894 79  ARG A CA  
630  C C   . ARG A 79  ? 0.81062 1.44134 0.66450 0.34680  -0.01583 -0.09581 79  ARG A C   
631  O O   . ARG A 79  ? 0.79778 1.44057 0.69514 0.30130  -0.00996 -0.14076 79  ARG A O   
632  C CB  . ARG A 79  ? 0.85062 1.66752 0.72731 0.41875  -0.07460 -0.15440 79  ARG A CB  
633  C CG  . ARG A 79  ? 0.83302 1.71420 0.74227 0.44063  -0.08959 -0.16039 79  ARG A CG  
634  C CD  . ARG A 79  ? 0.92401 1.86930 0.77150 0.51581  -0.12217 -0.19289 79  ARG A CD  
635  N NE  . ARG A 79  ? 0.97755 1.99762 0.81985 0.53364  -0.14565 -0.25379 79  ARG A NE  
636  C CZ  . ARG A 79  ? 0.96347 2.11299 0.89942 0.49396  -0.16712 -0.34683 79  ARG A CZ  
637  N NH1 . ARG A 79  ? 0.90109 2.11274 0.95060 0.42673  -0.15998 -0.38713 79  ARG A NH1 
638  N NH2 . ARG A 79  ? 1.01708 2.22568 0.94255 0.51632  -0.18579 -0.40202 79  ARG A NH2 
639  N N   . PRO A 80  ? 0.83740 1.39231 0.60097 0.39509  -0.00499 -0.03602 80  PRO A N   
640  C CA  . PRO A 80  ? 0.87189 1.37272 0.58696 0.39882  0.01053  -0.02646 80  PRO A CA  
641  C C   . PRO A 80  ? 0.93603 1.52279 0.63232 0.42452  -0.01973 -0.09311 80  PRO A C   
642  O O   . PRO A 80  ? 0.95556 1.51846 0.65390 0.40000  -0.00773 -0.11261 80  PRO A O   
643  C CB  . PRO A 80  ? 0.91793 1.33552 0.53662 0.45206  0.03141  0.04435  80  PRO A CB  
644  C CG  . PRO A 80  ? 0.87388 1.26799 0.51439 0.44862  0.03826  0.08014  80  PRO A CG  
645  C CD  . PRO A 80  ? 0.84449 1.34850 0.54933 0.44198  0.00289  0.02476  80  PRO A CD  
646  N N   . ALA A 81  ? 0.97102 1.66306 0.64876 0.47788  -0.06080 -0.13355 81  ALA A N   
647  C CA  . ALA A 81  ? 1.03618 1.82421 0.68871 0.51251  -0.09591 -0.20396 81  ALA A CA  
648  C C   . ALA A 81  ? 0.95624 1.80971 0.71816 0.43700  -0.09936 -0.28843 81  ALA A C   
649  O O   . ALA A 81  ? 1.00156 1.92431 0.75477 0.44946  -0.12184 -0.35495 81  ALA A O   
650  C CB  . ALA A 81  ? 0.92251 1.79442 0.57835 0.58030  -0.13191 -0.22360 81  ALA A CB  
651  N N   . GLU A 82  ? 0.95443 1.77931 0.81229 0.35973  -0.07323 -0.28783 82  GLU A N   
652  C CA  . GLU A 82  ? 0.93255 1.78897 0.89045 0.28041  -0.06077 -0.36012 82  GLU A CA  
653  C C   . GLU A 82  ? 0.90542 1.62999 0.86660 0.22760  -0.01571 -0.32514 82  GLU A C   
654  O O   . GLU A 82  ? 0.88517 1.58819 0.92162 0.15628  0.01048  -0.36141 82  GLU A O   
655  C CB  . GLU A 82  ? 0.85489 1.76633 0.90981 0.23297  -0.05557 -0.38736 82  GLU A CB  
656  C CG  . GLU A 82  ? 0.84252 1.90950 0.91235 0.28532  -0.10377 -0.44159 82  GLU A CG  
657  C CD  . GLU A 82  ? 0.78445 1.90745 0.94799 0.24367  -0.09461 -0.46293 82  GLU A CD  
658  O OE1 . GLU A 82  ? 0.73981 1.75917 0.91538 0.20260  -0.05552 -0.40046 82  GLU A OE1 
659  O OE2 . GLU A 82  ? 0.79498 2.07390 1.02062 0.25469  -0.12711 -0.54666 82  GLU A OE2 
660  N N   . ALA A 83  ? 0.92057 1.55505 0.79972 0.26384  -0.00273 -0.25739 83  ALA A N   
661  C CA  . ALA A 83  ? 0.91051 1.42854 0.79394 0.22463  0.03678  -0.22203 83  ALA A CA  
662  C C   . ALA A 83  ? 0.96099 1.48349 0.85977 0.19991  0.04180  -0.28611 83  ALA A C   
663  O O   . ALA A 83  ? 0.97053 1.42372 0.91559 0.14494  0.07300  -0.29414 83  ALA A O   
664  C CB  . ALA A 83  ? 0.91356 1.35226 0.71821 0.26806  0.05177  -0.14253 83  ALA A CB  
665  N N   . ASP A 84  ? 0.98502 1.58212 0.83751 0.24445  0.01270  -0.33245 84  ASP A N   
666  C CA  . ASP A 84  ? 1.00482 1.61342 0.87202 0.22185  0.01576  -0.40323 84  ASP A CA  
667  C C   . ASP A 84  ? 0.98597 1.63713 0.95930 0.14892  0.02273  -0.48405 84  ASP A C   
668  O O   . ASP A 84  ? 1.01126 1.59088 1.02242 0.09548  0.05659  -0.50901 84  ASP A O   
669  C CB  . ASP A 84  ? 1.06713 1.76489 0.85893 0.29000  -0.02247 -0.44448 84  ASP A CB  
670  C CG  . ASP A 84  ? 1.11792 1.74408 0.79774 0.35088  -0.00983 -0.36961 84  ASP A CG  
671  O OD1 . ASP A 84  ? 1.10682 1.62357 0.78590 0.32753  0.03004  -0.31575 84  ASP A OD1 
672  O OD2 . ASP A 84  ? 1.18427 1.86242 0.77697 0.42342  -0.03734 -0.36478 84  ASP A OD2 
673  N N   . LYS A 85  ? 0.95788 1.72099 0.98099 0.14574  -0.00379 -0.52672 85  LYS A N   
674  C CA  . LYS A 85  ? 0.96664 1.77600 1.10086 0.06853  0.01199  -0.60775 85  LYS A CA  
675  C C   . LYS A 85  ? 0.94839 1.62666 1.12306 0.00313  0.06740  -0.55597 85  LYS A C   
676  O O   . LYS A 85  ? 0.98627 1.63354 1.23083 -0.06967 0.10463  -0.60895 85  LYS A O   
677  C CB  . LYS A 85  ? 0.84610 1.81406 1.02947 0.08460  -0.02734 -0.66131 85  LYS A CB  
678  N N   . LEU A 86  ? 0.89937 1.49581 1.02612 0.02953  0.07627  -0.45513 86  LEU A N   
679  C CA  . LEU A 86  ? 0.88165 1.35297 1.02807 -0.01766 0.12347  -0.40103 86  LEU A CA  
680  C C   . LEU A 86  ? 0.90984 1.25706 1.03341 -0.03571 0.15788  -0.38844 86  LEU A C   
681  O O   . LEU A 86  ? 0.94595 1.20173 1.10101 -0.08926 0.20222  -0.39054 86  LEU A O   
682  C CB  . LEU A 86  ? 0.82789 1.26124 0.92991 0.02109  0.11736  -0.30701 86  LEU A CB  
683  C CG  . LEU A 86  ? 0.69626 1.03842 0.82051 -0.01901 0.15478  -0.25833 86  LEU A CG  
684  C CD1 . LEU A 86  ? 0.70647 1.10139 0.90785 -0.07640 0.17196  -0.31565 86  LEU A CD1 
685  C CD2 . LEU A 86  ? 0.69614 1.02243 0.78015 0.02255  0.14189  -0.17985 86  LEU A CD2 
686  N N   . VAL A 87  ? 0.91593 1.25336 0.97910 0.01212  0.14181  -0.37464 87  VAL A N   
687  C CA  . VAL A 87  ? 0.96216 1.18907 1.00144 0.00601  0.17165  -0.36189 87  VAL A CA  
688  C C   . VAL A 87  ? 1.03698 1.24623 1.12572 -0.05016 0.19725  -0.44694 87  VAL A C   
689  O O   . VAL A 87  ? 1.07791 1.16447 1.17143 -0.08129 0.24043  -0.43562 87  VAL A O   
690  C CB  . VAL A 87  ? 0.96142 1.20212 0.92992 0.06831  0.15103  -0.34048 87  VAL A CB  
691  C CG1 . VAL A 87  ? 1.01059 1.16112 0.96275 0.06427  0.17871  -0.34826 87  VAL A CG1 
692  C CG2 . VAL A 87  ? 0.89855 1.12232 0.82300 0.11164  0.14382  -0.25244 87  VAL A CG2 
693  N N   . LYS A 88  ? 1.07175 1.40205 1.19681 -0.06153 0.17222  -0.53684 88  LYS A N   
694  C CA  . LYS A 88  ? 1.17273 1.49880 1.35274 -0.11928 0.19716  -0.63363 88  LYS A CA  
695  C C   . LYS A 88  ? 1.22472 1.46508 1.46745 -0.19659 0.25334  -0.64123 88  LYS A C   
696  O O   . LYS A 88  ? 1.31760 1.42372 1.55920 -0.23229 0.30374  -0.64390 88  LYS A O   
697  C CB  . LYS A 88  ? 1.17947 1.68106 1.39654 -0.11414 0.15246  -0.73695 88  LYS A CB  
698  C CG  . LYS A 88  ? 1.17214 1.75457 1.30786 -0.02961 0.09930  -0.73023 88  LYS A CG  
699  C CD  . LYS A 88  ? 1.18065 1.94986 1.34378 -0.01003 0.04676  -0.83023 88  LYS A CD  
700  C CE  . LYS A 88  ? 1.19434 2.02202 1.25565 0.07790  0.00174  -0.82700 88  LYS A CE  
701  N NZ  . LYS A 88  ? 1.20381 2.20589 1.28419 0.11819  -0.05858 -0.88317 88  LYS A NZ  
702  N N   . LEU A 89  ? 1.18484 1.49280 1.47510 -0.21932 0.24982  -0.64176 89  LEU A N   
703  C CA  . LEU A 89  ? 1.22816 1.46143 1.57548 -0.29568 0.30987  -0.65323 89  LEU A CA  
704  C C   . LEU A 89  ? 1.24802 1.29659 1.53558 -0.29084 0.35391  -0.55200 89  LEU A C   
705  O O   . LEU A 89  ? 1.32227 1.24790 1.62447 -0.34704 0.41809  -0.55867 89  LEU A O   
706  C CB  . LEU A 89  ? 1.16274 1.52039 1.56936 -0.31140 0.29375  -0.67130 89  LEU A CB  
707  C CG  . LEU A 89  ? 1.13113 1.69561 1.58723 -0.29184 0.23503  -0.76362 89  LEU A CG  
708  C CD1 . LEU A 89  ? 1.05874 1.73652 1.54151 -0.27093 0.20536  -0.74634 89  LEU A CD1 
709  C CD2 . LEU A 89  ? 1.20598 1.82948 1.75806 -0.36736 0.26146  -0.89523 89  LEU A CD2 
710  N N   . LEU A 90  ? 1.20362 1.22967 1.42186 -0.22284 0.32299  -0.46125 90  LEU A N   
711  C CA  . LEU A 90  ? 1.23508 1.10577 1.39656 -0.20652 0.35485  -0.37300 90  LEU A CA  
712  C C   . LEU A 90  ? 1.33604 1.07970 1.47005 -0.21166 0.39047  -0.38572 90  LEU A C   
713  O O   . LEU A 90  ? 1.42090 1.01694 1.53128 -0.23118 0.44243  -0.35448 90  LEU A O   
714  C CB  . LEU A 90  ? 1.16361 1.05898 1.27126 -0.13541 0.31217  -0.29182 90  LEU A CB  
715  C CG  . LEU A 90  ? 1.11376 0.99458 1.20876 -0.12516 0.31166  -0.22084 90  LEU A CG  
716  C CD1 . LEU A 90  ? 1.17916 0.96640 1.28911 -0.17890 0.36649  -0.21763 90  LEU A CD1 
717  C CD2 . LEU A 90  ? 1.02558 1.04730 1.14314 -0.10819 0.26835  -0.22881 90  LEU A CD2 
718  N N   . ALA A 91  ? 1.34979 1.14294 1.47729 -0.18808 0.36459  -0.42998 91  ALA A N   
719  C CA  . ALA A 91  ? 1.45271 1.12848 1.55044 -0.18342 0.39510  -0.44116 91  ALA A CA  
720  C C   . ALA A 91  ? 1.55935 1.14636 1.69748 -0.25799 0.45651  -0.50842 91  ALA A C   
721  O O   . ALA A 91  ? 1.66656 1.08952 1.76876 -0.26192 0.50622  -0.48515 91  ALA A O   
722  C CB  . ALA A 91  ? 1.44285 1.20237 1.52415 -0.14341 0.35543  -0.48050 91  ALA A CB  
723  N N   . LYS A 92  ? 1.54702 1.23905 1.76054 -0.31648 0.45707  -0.59534 92  LYS A N   
724  C CA  . LYS A 92  ? 1.64513 1.25832 1.91117 -0.40064 0.52484  -0.66987 92  LYS A CA  
725  C C   . LYS A 92  ? 1.69246 1.17629 1.94850 -0.43796 0.58706  -0.61334 92  LYS A C   
726  O O   . LYS A 92  ? 1.79192 1.12338 2.01479 -0.45322 0.64684  -0.58413 92  LYS A O   
727  C CB  . LYS A 92  ? 1.61296 1.40081 1.97688 -0.45385 0.50551  -0.79119 92  LYS A CB  
728  C CG  . LYS A 92  ? 1.68670 1.45560 2.12348 -0.53519 0.57009  -0.82437 92  LYS A CG  
729  C CD  . LYS A 92  ? 1.72719 1.63556 2.25534 -0.57596 0.56489  -0.93558 92  LYS A CD  
730  C CE  . LYS A 92  ? 1.64475 1.77346 2.25919 -0.58727 0.52058  -1.00048 92  LYS A CE  
731  N NZ  . LYS A 92  ? 1.55580 1.84403 2.15618 -0.52311 0.42859  -1.03445 92  LYS A NZ  
732  N N   . GLY A 93  ? 1.46872 0.97416 1.07053 0.01519  0.21169  -0.38113 93  GLY A N   
733  C CA  . GLY A 93  ? 1.47353 0.97287 1.10787 0.00404  0.20913  -0.36547 93  GLY A CA  
734  C C   . GLY A 93  ? 1.50511 1.02324 1.15100 -0.03503 0.18884  -0.37734 93  GLY A C   
735  O O   . GLY A 93  ? 1.46158 1.03489 1.11515 -0.04472 0.16893  -0.37969 93  GLY A O   
736  N N   . GLU A 94  ? 1.58609 1.05823 1.23250 -0.05704 0.19454  -0.38510 94  GLU A N   
737  C CA  . GLU A 94  ? 1.64035 1.12940 1.30124 -0.09788 0.17874  -0.40067 94  GLU A CA  
738  C C   . GLU A 94  ? 1.61445 1.18300 1.31821 -0.10217 0.15813  -0.38211 94  GLU A C   
739  O O   . GLU A 94  ? 1.63188 1.24475 1.34606 -0.12491 0.13724  -0.39702 94  GLU A O   
740  C CB  . GLU A 94  ? 1.66028 1.14101 1.28912 -0.11930 0.16915  -0.43776 94  GLU A CB  
741  C CG  . GLU A 94  ? 1.71423 1.11650 1.29564 -0.11024 0.19001  -0.45669 94  GLU A CG  
742  C CD  . GLU A 94  ? 1.75335 1.11766 1.30969 -0.14821 0.18701  -0.49514 94  GLU A CD  
743  O OE1 . GLU A 94  ? 1.72185 1.12716 1.30269 -0.18227 0.16830  -0.50735 94  GLU A OE1 
744  O OE2 . GLU A 94  ? 1.81934 1.11424 1.33245 -0.14406 0.20357  -0.51470 94  GLU A OE2 
745  N N   . TYR A 95  ? 1.59081 1.17801 1.31888 -0.07833 0.16333  -0.35037 95  TYR A N   
746  C CA  . TYR A 95  ? 1.56332 1.21712 1.33052 -0.07957 0.14709  -0.33030 95  TYR A CA  
747  C C   . TYR A 95  ? 1.55652 1.19661 1.34965 -0.08321 0.15604  -0.30999 95  TYR A C   
748  O O   . TYR A 95  ? 1.58113 1.17154 1.36315 -0.06603 0.17474  -0.29860 95  TYR A O   
749  C CB  . TYR A 95  ? 1.54878 1.24361 1.31982 -0.04888 0.14382  -0.31090 95  TYR A CB  
750  C CG  . TYR A 95  ? 1.57800 1.24449 1.34361 -0.01709 0.16438  -0.29443 95  TYR A CG  
751  C CD1 . TYR A 95  ? 1.55150 1.22690 1.34541 -0.00290 0.16948  -0.26789 95  TYR A CD1 
752  C CD2 . TYR A 95  ? 1.63675 1.27127 1.36923 0.00028  0.17801  -0.30678 95  TYR A CD2 
753  C CE1 . TYR A 95  ? 1.57319 1.22998 1.36505 0.02843  0.18560  -0.25475 95  TYR A CE1 
754  C CE2 . TYR A 95  ? 1.65808 1.27406 1.39001 0.03180  0.19631  -0.29377 95  TYR A CE2 
755  C CZ  . TYR A 95  ? 1.62716 1.25646 1.39020 0.04616  0.19898  -0.26802 95  TYR A CZ  
756  O OH  . TYR A 95  ? 1.64378 1.26153 1.40902 0.07970  0.21462  -0.25685 95  TYR A OH  
757  N N   . GLN A 96  ? 1.52694 1.21031 1.35196 -0.10385 0.14268  -0.30605 96  GLN A N   
758  C CA  . GLN A 96  ? 1.52718 1.20476 1.37605 -0.10797 0.15028  -0.28561 96  GLN A CA  
759  C C   . GLN A 96  ? 1.47509 1.19176 1.34493 -0.07875 0.14644  -0.25528 96  GLN A C   
760  O O   . GLN A 96  ? 1.44814 1.21038 1.32311 -0.06484 0.13408  -0.25134 96  GLN A O   
761  C CB  . GLN A 96  ? 1.51526 1.22590 1.39125 -0.14377 0.13979  -0.29661 96  GLN A CB  
762  C CG  . GLN A 96  ? 1.57639 1.26138 1.43818 -0.17832 0.14076  -0.33076 96  GLN A CG  
763  C CD  . GLN A 96  ? 1.54385 1.29758 1.42599 -0.19759 0.11547  -0.35188 96  GLN A CD  
764  O OE1 . GLN A 96  ? 1.52408 1.30922 1.39533 -0.18148 0.09940  -0.35705 96  GLN A OE1 
765  N NE2 . GLN A 96  ? 1.53842 1.31670 1.44924 -0.23120 0.11220  -0.36429 96  GLN A NE2 
766  N N   . LYS A 97  ? 1.47280 1.16832 1.35162 -0.07052 0.15755  -0.23416 97  LYS A N   
767  C CA  . LYS A 97  ? 1.41397 1.14501 1.31402 -0.04577 0.15388  -0.20670 97  LYS A CA  
768  C C   . LYS A 97  ? 1.36240 1.12966 1.29236 -0.06292 0.14547  -0.19639 97  LYS A C   
769  O O   . LYS A 97  ? 1.39254 1.13406 1.32329 -0.08627 0.15304  -0.20086 97  LYS A O   
770  C CB  . LYS A 97  ? 1.44889 1.13433 1.33544 -0.01778 0.17030  -0.18983 97  LYS A CB  
771  C CG  . LYS A 97  ? 1.51417 1.15183 1.36851 -0.00169 0.18287  -0.20304 97  LYS A CG  
772  C CD  . LYS A 97  ? 1.53345 1.16136 1.38552 0.03829  0.19204  -0.18535 97  LYS A CD  
773  C CE  . LYS A 97  ? 1.58233 1.16461 1.42741 0.04839  0.20202  -0.16802 97  LYS A CE  
774  N NZ  . LYS A 97  ? 1.59870 1.17761 1.44295 0.09117  0.20790  -0.15296 97  LYS A NZ  
775  N N   . VAL A 98  ? 1.25023 1.07534 1.20304 -0.05246 0.13148  -0.18365 98  VAL A N   
776  C CA  . VAL A 98  ? 1.14615 1.00793 1.12705 -0.06188 0.12405  -0.17140 98  VAL A CA  
777  C C   . VAL A 98  ? 1.07159 0.94152 1.06069 -0.03551 0.12657  -0.14499 98  VAL A C   
778  O O   . VAL A 98  ? 1.07535 0.95247 1.05947 -0.01209 0.12637  -0.13865 98  VAL A O   
779  C CB  . VAL A 98  ? 1.09051 1.01226 1.08977 -0.07233 0.10377  -0.18080 98  VAL A CB  
780  C CG1 . VAL A 98  ? 1.11929 1.03721 1.10615 -0.09192 0.09794  -0.20941 98  VAL A CG1 
781  C CG2 . VAL A 98  ? 1.04642 1.00218 1.04722 -0.04848 0.09397  -0.16844 98  VAL A CG2 
782  N N   . SER A 99  ? 1.00335 0.87243 1.00424 -0.04017 0.12995  -0.13099 99  SER A N   
783  C CA  . SER A 99  ? 0.96831 0.84057 0.97379 -0.01611 0.13196  -0.10736 99  SER A CA  
784  C C   . SER A 99  ? 0.89143 0.81197 0.92214 -0.02113 0.12096  -0.09676 99  SER A C   
785  O O   . SER A 99  ? 0.89663 0.82440 0.93715 -0.04335 0.12109  -0.10133 99  SER A O   
786  C CB  . SER A 99  ? 1.02847 0.84134 1.01317 -0.01033 0.14824  -0.09760 99  SER A CB  
787  O OG  . SER A 99  ? 1.09757 0.86113 1.05620 -0.00144 0.15901  -0.10714 99  SER A OG  
788  N N   . TYR A 100 ? 0.83513 0.78876 0.87661 -0.00136 0.11276  -0.08412 100 TYR A N   
789  C CA  . TYR A 100 ? 0.75213 0.74592 0.81354 -0.00187 0.10312  -0.07284 100 TYR A CA  
790  C C   . TYR A 100 ? 0.73440 0.71815 0.79439 0.01552  0.10750  -0.05321 100 TYR A C   
791  O O   . TYR A 100 ? 0.73359 0.70279 0.78522 0.03682  0.11146  -0.04707 100 TYR A O   
792  C CB  . TYR A 100 ? 0.68474 0.72117 0.75615 0.00517  0.09017  -0.07386 100 TYR A CB  
793  C CG  . TYR A 100 ? 0.65583 0.71086 0.72792 -0.00998 0.08071  -0.09075 100 TYR A CG  
794  C CD1 . TYR A 100 ? 0.67260 0.71455 0.74287 -0.03036 0.08285  -0.10652 100 TYR A CD1 
795  C CD2 . TYR A 100 ? 0.62120 0.70649 0.69392 -0.00395 0.06928  -0.09141 100 TYR A CD2 
796  C CE1 . TYR A 100 ? 0.67126 0.73664 0.74346 -0.04213 0.07102  -0.12375 100 TYR A CE1 
797  C CE2 . TYR A 100 ? 0.62146 0.72282 0.69007 -0.01339 0.05821  -0.10600 100 TYR A CE2 
798  C CZ  . TYR A 100 ? 0.64940 0.74435 0.71941 -0.03138 0.05764  -0.12273 100 TYR A CZ  
799  O OH  . TYR A 100 ? 0.65854 0.77550 0.72567 -0.03882 0.04364  -0.13909 100 TYR A OH  
800  N N   . PRO A 101 ? 0.72179 0.71423 0.78888 0.00833  0.10678  -0.04419 101 PRO A N   
801  C CA  . PRO A 101 ? 0.72799 0.71155 0.78933 0.02591  0.10885  -0.02577 101 PRO A CA  
802  C C   . PRO A 101 ? 0.69269 0.71367 0.76701 0.04554  0.09780  -0.01870 101 PRO A C   
803  O O   . PRO A 101 ? 0.65592 0.71046 0.74357 0.04195  0.08935  -0.02542 101 PRO A O   
804  C CB  . PRO A 101 ? 0.71846 0.71085 0.78518 0.01008  0.11001  -0.02099 101 PRO A CB  
805  C CG  . PRO A 101 ? 0.72352 0.71826 0.79760 -0.01709 0.11321  -0.03823 101 PRO A CG  
806  C CD  . PRO A 101 ? 0.70882 0.72135 0.78897 -0.01530 0.10432  -0.05173 101 PRO A CD  
807  N N   . LEU A 102 ? 0.71149 0.72500 0.77973 0.06628  0.09814  -0.00539 102 LEU A N   
808  C CA  . LEU A 102 ? 0.67754 0.72820 0.76034 0.08389  0.08861  -0.00007 102 LEU A CA  
809  C C   . LEU A 102 ? 0.66092 0.72222 0.74337 0.09138  0.08265  0.01347  102 LEU A C   
810  O O   . LEU A 102 ? 0.68352 0.71606 0.74907 0.08789  0.08818  0.02095  102 LEU A O   
811  C CB  . LEU A 102 ? 0.70554 0.74673 0.78489 0.10680  0.09259  -0.00107 102 LEU A CB  
812  C CG  . LEU A 102 ? 0.71860 0.74813 0.79464 0.10243  0.09964  -0.01528 102 LEU A CG  
813  C CD1 . LEU A 102 ? 0.74776 0.75750 0.81560 0.12802  0.10681  -0.01567 102 LEU A CD1 
814  C CD2 . LEU A 102 ? 0.67888 0.74994 0.77173 0.09299  0.09365  -0.02314 102 LEU A CD2 
815  N N   . LEU A 103 ? 0.61996 0.72160 0.71904 0.10036  0.07233  0.01575  103 LEU A N   
816  C CA  . LEU A 103 ? 0.61123 0.72958 0.71083 0.10696  0.06405  0.02582  103 LEU A CA  
817  C C   . LEU A 103 ? 0.62891 0.75870 0.73056 0.13351  0.05851  0.03118  103 LEU A C   
818  O O   . LEU A 103 ? 0.62567 0.78074 0.74479 0.14144  0.05695  0.02428  103 LEU A O   
819  C CB  . LEU A 103 ? 0.56773 0.72468 0.68463 0.09368  0.05529  0.02181  103 LEU A CB  
820  C CG  . LEU A 103 ? 0.56214 0.74152 0.68115 0.09912  0.04541  0.02872  103 LEU A CG  
821  C CD1 . LEU A 103 ? 0.58439 0.73835 0.68259 0.09862  0.04861  0.03812  103 LEU A CD1 
822  C CD2 . LEU A 103 ? 0.52949 0.73806 0.66224 0.08510  0.03905  0.02263  103 LEU A CD2 
823  N N   . LYS A 104 ? 0.65046 0.76375 0.73375 0.14785  0.05569  0.04284  104 LYS A N   
824  C CA  . LYS A 104 ? 0.65218 0.78018 0.73595 0.17685  0.04675  0.04801  104 LYS A CA  
825  C C   . LYS A 104 ? 0.62107 0.78844 0.71416 0.17711  0.03251  0.05056  104 LYS A C   
826  O O   . LYS A 104 ? 0.61621 0.77327 0.69549 0.16478  0.03219  0.05598  104 LYS A O   
827  C CB  . LYS A 104 ? 0.69951 0.77468 0.74774 0.19794  0.05220  0.05993  104 LYS A CB  
828  C CG  . LYS A 104 ? 0.71316 0.80343 0.75905 0.23409  0.04045  0.06535  104 LYS A CG  
829  C CD  . LYS A 104 ? 0.77617 0.80240 0.77780 0.25743  0.04680  0.07888  104 LYS A CD  
830  C CE  . LYS A 104 ? 0.80367 0.84597 0.80327 0.29964  0.03358  0.08277  104 LYS A CE  
831  N NZ  . LYS A 104 ? 0.88343 0.85416 0.83110 0.32600  0.03942  0.09817  104 LYS A NZ  
832  N N   . THR A 105 ? 0.60534 0.81937 0.72268 0.18995  0.02168  0.04486  105 THR A N   
833  C CA  . THR A 105 ? 0.57825 0.83396 0.70735 0.18855  0.00720  0.04352  105 THR A CA  
834  C C   . THR A 105 ? 0.59377 0.87428 0.72645 0.21973  -0.00582 0.04520  105 THR A C   
835  O O   . THR A 105 ? 0.58358 0.89312 0.74068 0.23265  -0.00653 0.03707  105 THR A O   
836  C CB  . THR A 105 ? 0.53554 0.83269 0.69601 0.16673  0.00634  0.03068  105 THR A CB  
837  O OG1 . THR A 105 ? 0.52165 0.79627 0.67499 0.14224  0.01512  0.02979  105 THR A OG1 
838  C CG2 . THR A 105 ? 0.52185 0.86062 0.69448 0.16434  -0.00820 0.02683  105 THR A CG2 
839  N N   . THR A 106 ? 0.61415 0.88552 0.72203 0.23309  -0.01621 0.05493  106 THR A N   
840  C CA  . THR A 106 ? 0.64652 0.94258 0.75302 0.26620  -0.03258 0.05691  106 THR A CA  
841  C C   . THR A 106 ? 0.62481 0.97517 0.74917 0.25940  -0.05009 0.04885  106 THR A C   
842  O O   . THR A 106 ? 0.61447 0.95440 0.72353 0.24077  -0.05086 0.05150  106 THR A O   
843  C CB  . THR A 106 ? 0.71374 0.95281 0.76965 0.29087  -0.03241 0.07474  106 THR A CB  
844  O OG1 . THR A 106 ? 0.74432 0.92597 0.78138 0.29086  -0.01357 0.08067  106 THR A OG1 
845  C CG2 . THR A 106 ? 0.74782 1.01132 0.79996 0.33185  -0.05117 0.07678  106 THR A CG2 
846  N N   . VAL A 107 ? 0.62014 1.02986 0.77793 0.27383  -0.06340 0.03722  107 VAL A N   
847  C CA  . VAL A 107 ? 0.60996 1.07830 0.79096 0.26487  -0.08027 0.02506  107 VAL A CA  
848  C C   . VAL A 107 ? 0.66130 1.16166 0.83954 0.30249  -0.10219 0.02513  107 VAL A C   
849  O O   . VAL A 107 ? 0.66719 1.20444 0.87334 0.32480  -0.10661 0.01763  107 VAL A O   
850  C CB  . VAL A 107 ? 0.56407 1.08436 0.79483 0.24030  -0.07506 0.00648  107 VAL A CB  
851  C CG1 . VAL A 107 ? 0.54733 1.12309 0.79971 0.22652  -0.09102 -0.00759 107 VAL A CG1 
852  C CG2 . VAL A 107 ? 0.53703 1.02108 0.76468 0.20877  -0.05452 0.00768  107 VAL A CG2 
853  N N   . LYS A 108 ? 0.70150 1.18976 0.84533 0.31154  -0.11629 0.03283  108 LYS A N   
854  C CA  . LYS A 108 ? 0.75928 1.27731 0.89372 0.34911  -0.14068 0.03316  108 LYS A CA  
855  C C   . LYS A 108 ? 0.76285 1.34754 0.92823 0.33206  -0.15842 0.01284  108 LYS A C   
856  O O   . LYS A 108 ? 0.72395 1.32408 0.90063 0.30110  -0.15683 0.00515  108 LYS A O   
857  C CB  . LYS A 108 ? 0.80958 1.26448 0.87731 0.36937  -0.14428 0.05430  108 LYS A CB  
858  C CG  . LYS A 108 ? 0.83938 1.21369 0.86846 0.37876  -0.12299 0.07368  108 LYS A CG  
859  C CD  . LYS A 108 ? 0.90373 1.21813 0.86412 0.40321  -0.12697 0.09455  108 LYS A CD  
860  C CE  . LYS A 108 ? 0.94055 1.17095 0.86085 0.41043  -0.10398 0.11274  108 LYS A CE  
861  N NZ  . LYS A 108 ? 1.01738 1.18675 0.86675 0.44098  -0.10770 0.13403  108 LYS A NZ  
862  N N   . TYR A 109 ? 0.82564 1.44299 1.00145 0.34994  -0.17366 0.00339  109 TYR A N   
863  C CA  . TYR A 109 ? 0.83545 1.51400 1.04143 0.33256  -0.18920 -0.01801 109 TYR A CA  
864  C C   . TYR A 109 ? 0.88424 1.56220 1.05447 0.35731  -0.21211 -0.01538 109 TYR A C   
865  O O   . TYR A 109 ? 0.92729 1.57615 1.06591 0.39346  -0.21734 -0.00253 109 TYR A O   
866  C CB  . TYR A 109 ? 0.83989 1.57340 1.10164 0.32664  -0.18601 -0.03675 109 TYR A CB  
867  C CG  . TYR A 109 ? 0.81066 1.54214 1.10356 0.30421  -0.16210 -0.03931 109 TYR A CG  
868  C CD1 . TYR A 109 ? 0.82582 1.52291 1.11169 0.32410  -0.14787 -0.02762 109 TYR A CD1 
869  C CD2 . TYR A 109 ? 0.77519 1.53489 1.10036 0.26329  -0.15307 -0.05367 109 TYR A CD2 
870  C CE1 . TYR A 109 ? 0.79703 1.49163 1.10814 0.30431  -0.12612 -0.03075 109 TYR A CE1 
871  C CE2 . TYR A 109 ? 0.74985 1.50440 1.09800 0.24355  -0.13076 -0.05542 109 TYR A CE2 
872  C CZ  . TYR A 109 ? 0.76113 1.48495 1.10258 0.26437  -0.11776 -0.04421 109 TYR A CZ  
873  O OH  . TYR A 109 ? 0.73734 1.45548 1.09835 0.24531  -0.09568 -0.04675 109 TYR A OH  
874  N N   . LYS A 114 ? 0.96309 1.67233 1.21547 0.43964  -0.18692 -0.02237 114 LYS A N   
875  C CA  . LYS A 114 ? 0.99067 1.62197 1.19615 0.46283  -0.17490 0.00007  114 LYS A CA  
876  C C   . LYS A 114 ? 0.95083 1.53982 1.14081 0.43582  -0.15844 0.01097  114 LYS A C   
877  O O   . LYS A 114 ? 0.93227 1.52669 1.11420 0.41437  -0.16437 0.01096  114 LYS A O   
878  C CB  . LYS A 114 ? 1.00346 1.63243 1.22823 0.48123  -0.16220 -0.00275 114 LYS A CB  
879  N N   . GLU A 115 ? 0.93709 1.48414 1.12200 0.43813  -0.13792 0.01945  115 GLU A N   
880  C CA  . GLU A 115 ? 0.89569 1.40779 1.07156 0.41396  -0.12090 0.02810  115 GLU A CA  
881  C C   . GLU A 115 ? 0.85585 1.37011 1.06334 0.40359  -0.09967 0.02110  115 GLU A C   
882  O O   . GLU A 115 ? 0.88668 1.39585 1.09949 0.42573  -0.09505 0.01861  115 GLU A O   
883  C CB  . GLU A 115 ? 0.94660 1.37716 1.05742 0.43266  -0.11673 0.05334  115 GLU A CB  
884  C CG  . GLU A 115 ? 0.98500 1.35026 1.07136 0.45139  -0.09740 0.06578  115 GLU A CG  
885  C CD  . GLU A 115 ? 1.03321 1.30560 1.05377 0.44823  -0.08524 0.08813  115 GLU A CD  
886  O OE1 . GLU A 115 ? 1.05123 1.31295 1.03993 0.44759  -0.09565 0.09713  115 GLU A OE1 
887  O OE2 . GLU A 115 ? 1.05367 1.26326 1.05374 0.44336  -0.06385 0.09517  115 GLU A OE2 
888  N N   . ALA A 116 ? 0.78955 1.31114 1.01602 0.37032  -0.08663 0.01726  116 ALA A N   
889  C CA  . ALA A 116 ? 0.75310 1.27301 1.00456 0.35308  -0.06504 0.00947  116 ALA A CA  
890  C C   . ALA A 116 ? 0.73540 1.18218 0.95272 0.32537  -0.04646 0.02082  116 ALA A C   
891  O O   . ALA A 116 ? 0.72010 1.15287 0.92292 0.30012  -0.04797 0.02511  116 ALA A O   
892  C CB  . ALA A 116 ? 0.70794 1.29746 1.01203 0.32215  -0.06315 -0.01097 116 ALA A CB  
893  N N   . THR A 117 ? 0.73968 1.14292 0.94559 0.33033  -0.02923 0.02377  117 THR A N   
894  C CA  . THR A 117 ? 0.72931 1.06837 0.90678 0.30480  -0.01201 0.03146  117 THR A CA  
895  C C   . THR A 117 ? 0.68674 1.03814 0.89025 0.28031  0.00381  0.01898  117 THR A C   
896  O O   . THR A 117 ? 0.68787 1.07296 0.91898 0.29225  0.00792  0.00799  117 THR A O   
897  C CB  . THR A 117 ? 0.78598 1.05051 0.91812 0.32715  -0.00387 0.04542  117 THR A CB  
898  O OG1 . THR A 117 ? 0.80647 1.06747 0.94840 0.34773  0.00502  0.03871  117 THR A OG1 
899  C CG2 . THR A 117 ? 0.83014 1.08023 0.93107 0.35886  -0.01929 0.05872  117 THR A CG2 
900  N N   . TYR A 118 ? 0.65082 0.97569 0.84391 0.24735  0.01273  0.02037  118 TYR A N   
901  C CA  . TYR A 118 ? 0.61713 0.94637 0.82550 0.22338  0.02645  0.01024  118 TYR A CA  
902  C C   . TYR A 118 ? 0.61962 0.88868 0.79823 0.20719  0.03812  0.01560  118 TYR A C   
903  O O   . TYR A 118 ? 0.62597 0.86066 0.77934 0.20216  0.03613  0.02571  118 TYR A O   
904  C CB  . TYR A 118 ? 0.57465 0.94732 0.80721 0.19575  0.02305  0.00220  118 TYR A CB  
905  C CG  . TYR A 118 ? 0.56334 1.00024 0.82871 0.20443  0.01170  -0.00618 118 TYR A CG  
906  C CD1 . TYR A 118 ? 0.56288 1.01810 0.82613 0.20886  -0.00516 -0.00254 118 TYR A CD1 
907  C CD2 . TYR A 118 ? 0.55491 1.03695 0.85391 0.20707  0.01833  -0.01944 118 TYR A CD2 
908  C CE1 . TYR A 118 ? 0.55491 1.07358 0.85023 0.21515  -0.01729 -0.01303 118 TYR A CE1 
909  C CE2 . TYR A 118 ? 0.54541 1.09365 0.87992 0.21242  0.00833  -0.02998 118 TYR A CE2 
910  C CZ  . TYR A 118 ? 0.54571 1.11300 0.87905 0.21611  -0.01055 -0.02730 118 TYR A CZ  
911  O OH  . TYR A 118 ? 0.54042 1.17814 0.91104 0.21980  -0.02225 -0.04052 118 TYR A OH  
912  N N   . LEU A 119 ? 0.61485 0.87465 0.79734 0.19778  0.05086  0.00716  119 LEU A N   
913  C CA  . LEU A 119 ? 0.61442 0.82674 0.77420 0.17973  0.06090  0.00753  119 LEU A CA  
914  C C   . LEU A 119 ? 0.57595 0.80795 0.74725 0.15257  0.06361  -0.00064 119 LEU A C   
915  O O   . LEU A 119 ? 0.56730 0.83006 0.75705 0.15108  0.06789  -0.00943 119 LEU A O   
916  C CB  . LEU A 119 ? 0.65535 0.83096 0.80099 0.19408  0.07279  0.00375  119 LEU A CB  
917  C CG  . LEU A 119 ? 0.68508 0.79839 0.79843 0.18479  0.08056  0.00779  119 LEU A CG  
918  C CD1 . LEU A 119 ? 0.69948 0.78944 0.79354 0.18978  0.07491  0.02194  119 LEU A CD1 
919  C CD2 . LEU A 119 ? 0.72791 0.80219 0.82519 0.20162  0.09218  0.00291  119 LEU A CD2 
920  N N   . ALA A 120 ? 0.55614 0.77023 0.71515 0.13227  0.06192  0.00217  120 ALA A N   
921  C CA  . ALA A 120 ? 0.54187 0.76846 0.70521 0.11011  0.06243  -0.00396 120 ALA A CA  
922  C C   . ALA A 120 ? 0.56296 0.75560 0.70867 0.09756  0.06836  -0.00820 120 ALA A C   
923  O O   . ALA A 120 ? 0.59331 0.75542 0.72524 0.09683  0.06997  -0.00470 120 ALA A O   
924  C CB  . ALA A 120 ? 0.52153 0.76531 0.68865 0.09872  0.05257  0.00055  120 ALA A CB  
925  N N   . LEU A 121 ? 0.54662 0.74479 0.69129 0.08680  0.07195  -0.01648 121 LEU A N   
926  C CA  . LEU A 121 ? 0.55104 0.72630 0.68014 0.07351  0.07360  -0.02291 121 LEU A CA  
927  C C   . LEU A 121 ? 0.52913 0.71416 0.65664 0.05894  0.06490  -0.02216 121 LEU A C   
928  O O   . LEU A 121 ? 0.52907 0.70078 0.64903 0.04972  0.06225  -0.02561 121 LEU A O   
929  C CB  . LEU A 121 ? 0.56117 0.73253 0.68264 0.07347  0.08187  -0.03288 121 LEU A CB  
930  C CG  . LEU A 121 ? 0.57194 0.72261 0.67481 0.06114  0.08159  -0.04222 121 LEU A CG  
931  C CD1 . LEU A 121 ? 0.58495 0.70635 0.68081 0.05820  0.08275  -0.04471 121 LEU A CD1 
932  C CD2 . LEU A 121 ? 0.59220 0.73821 0.68283 0.06331  0.09058  -0.05176 121 LEU A CD2 
933  N N   . ASN A 122 ? 0.51235 0.72060 0.64719 0.05678  0.06069  -0.01891 122 ASN A N   
934  C CA  . ASN A 122 ? 0.49488 0.70777 0.62500 0.04676  0.05250  -0.01771 122 ASN A CA  
935  C C   . ASN A 122 ? 0.48616 0.70801 0.62459 0.04814  0.04610  -0.01027 122 ASN A C   
936  O O   . ASN A 122 ? 0.49036 0.70505 0.62605 0.04440  0.04271  -0.00942 122 ASN A O   
937  C CB  . ASN A 122 ? 0.49270 0.71455 0.61701 0.04149  0.05355  -0.01924 122 ASN A CB  
938  C CG  . ASN A 122 ? 0.50147 0.70833 0.60554 0.03726  0.05555  -0.02589 122 ASN A CG  
939  O OD1 . ASN A 122 ? 0.50467 0.69887 0.60217 0.03717  0.05415  -0.03138 122 ASN A OD1 
940  N ND2 . ASN A 122 ? 0.50938 0.71596 0.60080 0.03273  0.05922  -0.02604 122 ASN A ND2 
941  N N   . GLU A 123 ? 0.46939 0.70929 0.61834 0.05288  0.04484  -0.00634 123 GLU A N   
942  C CA  . GLU A 123 ? 0.45818 0.70685 0.61077 0.05407  0.03768  -0.00049 123 GLU A CA  
943  C C   . GLU A 123 ? 0.46712 0.73945 0.63329 0.06123  0.03560  0.00096  123 GLU A C   
944  O O   . GLU A 123 ? 0.46986 0.75709 0.64610 0.06206  0.04033  -0.00361 123 GLU A O   
945  C CB  . GLU A 123 ? 0.44483 0.69429 0.59042 0.04441  0.03206  -0.00140 123 GLU A CB  
946  C CG  . GLU A 123 ? 0.44324 0.70265 0.58871 0.03786  0.03215  -0.00390 123 GLU A CG  
947  C CD  . GLU A 123 ? 0.44655 0.69913 0.58514 0.03395  0.03962  -0.00842 123 GLU A CD  
948  O OE1 . GLU A 123 ? 0.45205 0.68819 0.57595 0.03227  0.03891  -0.01058 123 GLU A OE1 
949  O OE2 . GLU A 123 ? 0.44283 0.70898 0.59069 0.03297  0.04626  -0.01078 123 GLU A OE2 
950  N N   . SER A 124 ? 0.47416 0.75264 0.64070 0.06634  0.02857  0.00617  124 SER A N   
951  C CA  . SER A 124 ? 0.47648 0.78272 0.65560 0.07282  0.02222  0.00596  124 SER A CA  
952  C C   . SER A 124 ? 0.46008 0.77340 0.63502 0.06314  0.01467  0.00546  124 SER A C   
953  O O   . SER A 124 ? 0.45948 0.75663 0.62064 0.06229  0.01237  0.00980  124 SER A O   
954  C CB  . SER A 124 ? 0.49996 0.80345 0.67646 0.09218  0.01898  0.01254  124 SER A CB  
955  O OG  . SER A 124 ? 0.50453 0.84102 0.69444 0.10123  0.00984  0.01066  124 SER A OG  
956  N N   . THR A 125 ? 0.45943 0.79635 0.64600 0.05474  0.01237  -0.00109 125 THR A N   
957  C CA  . THR A 125 ? 0.45544 0.79308 0.63518 0.04249  0.00719  -0.00407 125 THR A CA  
958  C C   . THR A 125 ? 0.46152 0.83120 0.65436 0.04372  -0.00199 -0.00896 125 THR A C   
959  O O   . THR A 125 ? 0.46589 0.86576 0.68013 0.04769  -0.00207 -0.01392 125 THR A O   
960  C CB  . THR A 125 ? 0.46308 0.79059 0.63813 0.02603  0.01468  -0.00917 125 THR A CB  
961  O OG1 . THR A 125 ? 0.47599 0.77327 0.63186 0.02546  0.01679  -0.00550 125 THR A OG1 
962  C CG2 . THR A 125 ? 0.46094 0.79583 0.63501 0.01149  0.01177  -0.01567 125 THR A CG2 
963  N N   . VAL A 126 ? 0.46096 0.82703 0.64165 0.04097  -0.01011 -0.00921 126 VAL A N   
964  C CA  . VAL A 126 ? 0.48033 0.87611 0.66970 0.03947  -0.02100 -0.01640 126 VAL A CA  
965  C C   . VAL A 126 ? 0.49595 0.88213 0.67553 0.01970  -0.02120 -0.02423 126 VAL A C   
966  O O   . VAL A 126 ? 0.50588 0.86016 0.66352 0.01728  -0.01880 -0.02055 126 VAL A O   
967  C CB  . VAL A 126 ? 0.50317 0.90020 0.67972 0.05741  -0.03188 -0.00993 126 VAL A CB  
968  C CG1 . VAL A 126 ? 0.51798 0.95696 0.70962 0.06280  -0.04561 -0.01812 126 VAL A CG1 
969  C CG2 . VAL A 126 ? 0.51461 0.89362 0.68422 0.07510  -0.02704 0.00178  126 VAL A CG2 
970  N N   . LYS A 127 ? 0.51775 0.93195 0.71380 0.00580  -0.02375 -0.03623 127 LYS A N   
971  C CA  . LYS A 127 ? 0.54227 0.94522 0.72694 -0.01455 -0.02419 -0.04563 127 LYS A CA  
972  C C   . LYS A 127 ? 0.57072 1.01614 0.77283 -0.02003 -0.03649 -0.05870 127 LYS A C   
973  O O   . LYS A 127 ? 0.55246 1.03869 0.77758 -0.00677 -0.04443 -0.06025 127 LYS A O   
974  C CB  . LYS A 127 ? 0.53536 0.91924 0.71814 -0.03530 -0.00934 -0.04941 127 LYS A CB  
975  C CG  . LYS A 127 ? 0.51785 0.86379 0.68256 -0.02834 0.00026  -0.03809 127 LYS A CG  
976  C CD  . LYS A 127 ? 0.52625 0.85241 0.68399 -0.04591 0.01483  -0.04045 127 LYS A CD  
977  C CE  . LYS A 127 ? 0.52890 0.82099 0.66679 -0.03561 0.02073  -0.03011 127 LYS A CE  
978  N NZ  . LYS A 127 ? 0.55207 0.82091 0.67603 -0.04916 0.03491  -0.03041 127 LYS A NZ  
979  N N   . SER A 128 ? 0.62455 1.06028 0.81460 -0.03853 -0.03900 -0.06933 128 SER A N   
980  C CA  . SER A 128 ? 0.67107 1.14967 0.87833 -0.04777 -0.05164 -0.08540 128 SER A CA  
981  C C   . SER A 128 ? 0.74688 1.25928 0.98678 -0.07124 -0.04312 -0.09932 128 SER A C   
982  O O   . SER A 128 ? 0.75641 1.24296 0.99270 -0.08745 -0.02542 -0.09771 128 SER A O   
983  C CB  A SER A 128 ? 0.69231 1.14568 0.87178 -0.06000 -0.05750 -0.09387 128 SER A CB  
984  C CB  B SER A 128 ? 0.69229 1.14553 0.87163 -0.05985 -0.05753 -0.09379 128 SER A CB  
985  O OG  A SER A 128 ? 0.70937 1.13290 0.87971 -0.08807 -0.04429 -0.10215 128 SER A OG  
986  O OG  B SER A 128 ? 0.70225 1.19886 0.89797 -0.07108 -0.07110 -0.11205 128 SER A OG  
987  N N   . SER A 129 ? 0.80824 1.38070 1.07937 -0.07267 -0.05576 -0.11373 129 SER A N   
988  C CA  . SER A 129 ? 0.91086 1.52927 1.22029 -0.09719 -0.04848 -0.13135 129 SER A CA  
989  C C   . SER A 129 ? 1.00014 1.60246 1.30062 -0.13521 -0.04208 -0.14801 129 SER A C   
990  O O   . SER A 129 ? 1.03917 1.68919 1.37337 -0.15959 -0.04012 -0.16799 129 SER A O   
991  C CB  . SER A 129 ? 0.92197 1.61778 1.27108 -0.08195 -0.06701 -0.14285 129 SER A CB  
992  O OG  . SER A 129 ? 0.96182 1.66949 1.29828 -0.07803 -0.08862 -0.15118 129 SER A OG  
993  N N   . GLY A 130 ? 1.06481 1.60145 1.32113 -0.14105 -0.03802 -0.14156 130 GLY A N   
994  C CA  . GLY A 130 ? 1.10321 1.61517 1.34300 -0.17398 -0.03362 -0.15743 130 GLY A CA  
995  C C   . GLY A 130 ? 1.11656 1.60769 1.32564 -0.16467 -0.05044 -0.16000 130 GLY A C   
996  O O   . GLY A 130 ? 1.11139 1.64766 1.33332 -0.14965 -0.07106 -0.16606 130 GLY A O   
997  N N   . GLY A 131 ? 1.08103 1.50270 1.24653 -0.17101 -0.04184 -0.15537 131 GLY A N   
998  C CA  . GLY A 131 ? 1.02068 1.41642 1.15293 -0.16022 -0.05444 -0.15708 131 GLY A CA  
999  C C   . GLY A 131 ? 0.94823 1.32063 1.06009 -0.12466 -0.05731 -0.13529 131 GLY A C   
1000 O O   . GLY A 131 ? 0.93322 1.29066 1.04741 -0.11261 -0.04674 -0.11898 131 GLY A O   
1001 N N   . PRO A 132 ? 0.92515 1.29509 1.01604 -0.10870 -0.07096 -0.13591 132 PRO A N   
1002 C CA  . PRO A 132 ? 0.88667 1.23107 0.95560 -0.07916 -0.07039 -0.11708 132 PRO A CA  
1003 C C   . PRO A 132 ? 0.79041 1.17185 0.88164 -0.05522 -0.07599 -0.10305 132 PRO A C   
1004 O O   . PRO A 132 ? 0.77874 1.20915 0.89153 -0.05043 -0.08937 -0.10868 132 PRO A O   
1005 C CB  . PRO A 132 ? 0.92253 1.25473 0.96046 -0.07395 -0.08136 -0.12542 132 PRO A CB  
1006 C CG  . PRO A 132 ? 0.94468 1.32135 0.99954 -0.09048 -0.09600 -0.14561 132 PRO A CG  
1007 C CD  . PRO A 132 ? 0.95531 1.34212 1.03789 -0.11957 -0.08587 -0.15557 132 PRO A CD  
1008 N N   . PHE A 133 ? 0.72296 1.07928 0.80739 -0.03928 -0.06599 -0.08550 133 PHE A N   
1009 C CA  . PHE A 133 ? 0.63756 1.01348 0.73377 -0.01607 -0.06836 -0.07076 133 PHE A CA  
1010 C C   . PHE A 133 ? 0.60055 0.95918 0.66789 0.00295  -0.07229 -0.06250 133 PHE A C   
1011 O O   . PHE A 133 ? 0.59271 0.91529 0.63931 0.00558  -0.06314 -0.05758 133 PHE A O   
1012 C CB  . PHE A 133 ? 0.59975 0.95966 0.70635 -0.01378 -0.05412 -0.05904 133 PHE A CB  
1013 C CG  . PHE A 133 ? 0.56130 0.93015 0.67474 0.00825  -0.05393 -0.04438 133 PHE A CG  
1014 C CD1 . PHE A 133 ? 0.54240 0.94804 0.68069 0.01642  -0.05931 -0.04353 133 PHE A CD1 
1015 C CD2 . PHE A 133 ? 0.55168 0.89146 0.64709 0.02035  -0.04719 -0.03261 133 PHE A CD2 
1016 C CE1 . PHE A 133 ? 0.53457 0.93902 0.67377 0.03679  -0.05767 -0.03003 133 PHE A CE1 
1017 C CE2 . PHE A 133 ? 0.54183 0.88406 0.64113 0.03661  -0.04474 -0.02022 133 PHE A CE2 
1018 C CZ  . PHE A 133 ? 0.53747 0.90755 0.65589 0.04501  -0.04973 -0.01831 133 PHE A CZ  
1019 N N   . VAL A 134 ? 0.57850 0.96363 0.64322 0.01708  -0.08554 -0.06150 134 VAL A N   
1020 C CA  . VAL A 134 ? 0.57704 0.94613 0.60997 0.03453  -0.08808 -0.05330 134 VAL A CA  
1021 C C   . VAL A 134 ? 0.56818 0.95287 0.60461 0.05626  -0.09216 -0.03931 134 VAL A C   
1022 O O   . VAL A 134 ? 0.58689 1.00690 0.63556 0.06340  -0.10665 -0.04352 134 VAL A O   
1023 C CB  . VAL A 134 ? 0.60396 0.97914 0.61366 0.03122  -0.10160 -0.06711 134 VAL A CB  
1024 C CG1 . VAL A 134 ? 0.62316 0.97488 0.59448 0.04819  -0.09948 -0.05788 134 VAL A CG1 
1025 C CG2 . VAL A 134 ? 0.61558 0.97404 0.62231 0.00740  -0.09834 -0.08380 134 VAL A CG2 
1026 N N   . VAL A 135 ? 0.54200 0.90039 0.56687 0.06726  -0.07963 -0.02370 135 VAL A N   
1027 C CA  . VAL A 135 ? 0.54108 0.90078 0.55879 0.08788  -0.08097 -0.00922 135 VAL A CA  
1028 C C   . VAL A 135 ? 0.56196 0.88888 0.54422 0.09651  -0.07089 0.00203  135 VAL A C   
1029 O O   . VAL A 135 ? 0.55957 0.86599 0.53544 0.08729  -0.05868 0.00054  135 VAL A O   
1030 C CB  . VAL A 135 ? 0.51051 0.87179 0.55515 0.09022  -0.07227 -0.00135 135 VAL A CB  
1031 C CG1 . VAL A 135 ? 0.49416 0.89234 0.57371 0.08280  -0.08039 -0.01275 135 VAL A CG1 
1032 C CG2 . VAL A 135 ? 0.48877 0.82276 0.53712 0.07938  -0.05481 0.00226  135 VAL A CG2 
1033 N N   . ASP A 136 ? 0.59105 0.91340 0.54862 0.11525  -0.07565 0.01290  136 ASP A N   
1034 C CA  . ASP A 136 ? 0.61754 0.90575 0.54118 0.12297  -0.06151 0.02672  136 ASP A CA  
1035 C C   . ASP A 136 ? 0.60559 0.87655 0.54199 0.12497  -0.04681 0.03932  136 ASP A C   
1036 O O   . ASP A 136 ? 0.60366 0.88199 0.55061 0.13626  -0.05290 0.04461  136 ASP A O   
1037 C CB  . ASP A 136 ? 0.66336 0.94612 0.54563 0.14244  -0.07214 0.03398  136 ASP A CB  
1038 C CG  . ASP A 136 ? 0.67969 0.96805 0.53673 0.13938  -0.08151 0.02237  136 ASP A CG  
1039 O OD1 . ASP A 136 ? 0.67653 0.94966 0.52601 0.12727  -0.06864 0.01746  136 ASP A OD1 
1040 O OD2 . ASP A 136 ? 0.70246 1.01181 0.54684 0.15044  -0.10247 0.01695  136 ASP A OD2 
1041 N N   . VAL A 137 ? 0.59744 0.84740 0.53369 0.11455  -0.02785 0.04240  137 VAL A N   
1042 C CA  . VAL A 137 ? 0.59036 0.82303 0.53784 0.11269  -0.01308 0.05166  137 VAL A CA  
1043 C C   . VAL A 137 ? 0.63276 0.83246 0.54237 0.12103  -0.00045 0.06646  137 VAL A C   
1044 O O   . VAL A 137 ? 0.66003 0.84781 0.54457 0.11775  0.00881  0.06743  137 VAL A O   
1045 C CB  . VAL A 137 ? 0.55961 0.79349 0.53223 0.09579  -0.00093 0.04437  137 VAL A CB  
1046 C CG1 . VAL A 137 ? 0.55716 0.77468 0.53983 0.09204  0.01352  0.05156  137 VAL A CG1 
1047 C CG2 . VAL A 137 ? 0.52103 0.77811 0.52277 0.08822  -0.01184 0.03201  137 VAL A CG2 
1048 N N   . VAL A 138 ? 0.64972 0.83159 0.55206 0.13219  0.00130  0.07787  138 VAL A N   
1049 C CA  . VAL A 138 ? 0.70224 0.84300 0.56195 0.14129  0.01399  0.09408  138 VAL A CA  
1050 C C   . VAL A 138 ? 0.70574 0.82117 0.57688 0.13216  0.03232  0.09954  138 VAL A C   
1051 O O   . VAL A 138 ? 0.68427 0.80820 0.58203 0.13497  0.02674  0.09688  138 VAL A O   
1052 C CB  . VAL A 138 ? 0.73974 0.87407 0.56903 0.16832  -0.00296 0.10350  138 VAL A CB  
1053 C CG1 . VAL A 138 ? 0.80068 0.88191 0.57666 0.17886  0.01176  0.12238  138 VAL A CG1 
1054 C CG2 . VAL A 138 ? 0.74013 0.90524 0.56116 0.17535  -0.02369 0.09451  138 VAL A CG2 
1055 N N   . ILE A 139 ? 0.73082 0.81614 0.58183 0.11991  0.05515  0.10565  139 ILE A N   
1056 C CA  . ILE A 139 ? 0.72751 0.78856 0.58878 0.10580  0.07465  0.10794  139 ILE A CA  
1057 C C   . ILE A 139 ? 0.79689 0.80218 0.60718 0.11172  0.09117  0.12548  139 ILE A C   
1058 O O   . ILE A 139 ? 0.84040 0.82744 0.61917 0.10528  0.10609  0.13101  139 ILE A O   
1059 C CB  . ILE A 139 ? 0.69667 0.77632 0.58655 0.08073  0.08949  0.09589  139 ILE A CB  
1060 C CG1 . ILE A 139 ? 0.63580 0.76182 0.56633 0.07795  0.07313  0.08035  139 ILE A CG1 
1061 C CG2 . ILE A 139 ? 0.70392 0.76353 0.60725 0.06447  0.10723  0.09519  139 ILE A CG2 
1062 C CD1 . ILE A 139 ? 0.60409 0.75149 0.55904 0.06019  0.08390  0.06817  139 ILE A CD1 
1063 N N   . ASN A 140 ? 0.81631 0.79075 0.61548 0.12399  0.09056  0.13423  140 ASN A N   
1064 C CA  . ASN A 140 ? 0.90435 0.81447 0.64821 0.13234  0.10638  0.15257  140 ASN A CA  
1065 C C   . ASN A 140 ? 0.97000 0.86561 0.66195 0.15150  0.10001  0.16471  140 ASN A C   
1066 O O   . ASN A 140 ? 1.02611 0.87973 0.67228 0.14483  0.12077  0.17595  140 ASN A O   
1067 C CB  . ASN A 140 ? 0.92396 0.80179 0.66361 0.10206  0.13839  0.15254  140 ASN A CB  
1068 C CG  . ASN A 140 ? 0.90006 0.79025 0.68644 0.08394  0.14307  0.13949  140 ASN A CG  
1069 O OD1 . ASN A 140 ? 0.88763 0.78094 0.68954 0.09805  0.12926  0.13771  140 ASN A OD1 
1070 N ND2 . ASN A 140 ? 0.88929 0.78970 0.69861 0.05318  0.16240  0.12895  140 ASN A ND2 
1071 N N   . ASP A 141 ? 0.97200 0.90487 0.67137 0.17404  0.07128  0.16096  141 ASP A N   
1072 C CA  . ASP A 141 ? 1.03771 0.96784 0.69195 0.19566  0.05748  0.16879  141 ASP A CA  
1073 C C   . ASP A 141 ? 1.05762 0.99809 0.69992 0.17829  0.06809  0.16395  141 ASP A C   
1074 O O   . ASP A 141 ? 1.10940 1.02760 0.69810 0.19096  0.06769  0.17384  141 ASP A O   
1075 C CB  . ASP A 141 ? 1.11434 0.97902 0.70102 0.22024  0.06288  0.19117  141 ASP A CB  
1076 C CG  . ASP A 141 ? 1.11141 0.96661 0.70621 0.24460  0.04980  0.19538  141 ASP A CG  
1077 O OD1 . ASP A 141 ? 1.04901 0.96012 0.69361 0.25210  0.02720  0.18158  141 ASP A OD1 
1078 O OD2 . ASP A 141 ? 1.17561 0.96541 0.72561 0.25598  0.06376  0.21206  141 ASP A OD2 
1079 N N   . ILE A 142 ? 1.02814 1.00220 0.71741 0.15188  0.07693  0.14841  142 ILE A N   
1080 C CA  A ILE A 142 ? 1.02674 1.01547 0.71167 0.13657  0.08782  0.14097  142 ILE A CA  
1081 C CA  B ILE A 142 ? 1.02685 1.01559 0.71185 0.13652  0.08786  0.14095  142 ILE A CA  
1082 C C   . ILE A 142 ? 0.96239 1.00808 0.69238 0.13393  0.06698  0.12185  142 ILE A C   
1083 O O   . ILE A 142 ? 0.91086 0.98336 0.69148 0.12285  0.06373  0.11077  142 ILE A O   
1084 C CB  A ILE A 142 ? 1.04037 1.01584 0.73819 0.10820  0.11998  0.13877  142 ILE A CB  
1085 C CB  B ILE A 142 ? 1.03812 1.01378 0.73633 0.10811  0.11995  0.13869  142 ILE A CB  
1086 C CG1 A ILE A 142 ? 1.10615 1.01739 0.75386 0.10663  0.14420  0.15762  142 ILE A CG1 
1087 C CG1 B ILE A 142 ? 1.10788 1.01931 0.75443 0.10645  0.14461  0.15759  142 ILE A CG1 
1088 C CG2 A ILE A 142 ? 1.01744 1.01790 0.71937 0.09498  0.13030  0.12793  142 ILE A CG2 
1089 C CG2 B ILE A 142 ? 1.01363 1.01654 0.71908 0.09450  0.12964  0.12703  142 ILE A CG2 
1090 C CD1 A ILE A 142 ? 1.17819 1.05156 0.75426 0.12441  0.14614  0.17360  142 ILE A CD1 
1091 C CD1 B ILE A 142 ? 1.12740 1.02789 0.79279 0.07475  0.17678  0.15329  142 ILE A CD1 
1092 N N   . HIS A 143 ? 0.93760 0.99760 0.64503 0.14364  0.05344  0.11774  143 HIS A N   
1093 C CA  . HIS A 143 ? 0.86212 0.96830 0.60654 0.13926  0.03536  0.09909  143 HIS A CA  
1094 C C   . HIS A 143 ? 0.78844 0.90940 0.56376 0.11760  0.05235  0.08715  143 HIS A C   
1095 O O   . HIS A 143 ? 0.82196 0.93325 0.57509 0.11122  0.06958  0.08681  143 HIS A O   
1096 C CB  A HIS A 143 ? 0.87744 0.99359 0.58896 0.15213  0.01768  0.09468  143 HIS A CB  
1097 C CB  B HIS A 143 ? 0.88024 0.99471 0.58957 0.15284  0.01789  0.09554  143 HIS A CB  
1098 C CG  A HIS A 143 ? 0.85432 1.00990 0.59983 0.14394  0.00244  0.07448  143 HIS A CG  
1099 C CG  B HIS A 143 ? 0.92458 1.04500 0.61954 0.17589  -0.00786 0.10043  143 HIS A CG  
1100 N ND1 A HIS A 143 ? 0.83109 0.99377 0.58568 0.12982  0.01419  0.06291  143 HIS A ND1 
1101 N ND1 B HIS A 143 ? 0.88371 1.04600 0.60511 0.17988  -0.03444 0.08566  143 HIS A ND1 
1102 C CD2 A HIS A 143 ? 0.82229 1.00998 0.59544 0.14688  -0.02163 0.06330  143 HIS A CD2 
1103 C CD2 B HIS A 143 ? 0.96591 1.05700 0.62362 0.19702  -0.01105 0.11752  143 HIS A CD2 
1104 C CE1 A HIS A 143 ? 0.80429 0.99436 0.58473 0.12539  -0.00230 0.04675  143 HIS A CE1 
1105 C CE1 B HIS A 143 ? 0.91995 1.08645 0.62601 0.20281  -0.05400 0.09197  143 HIS A CE1 
1106 N NE2 A HIS A 143 ? 0.79072 0.99693 0.58357 0.13324  -0.02325 0.04641  143 HIS A NE2 
1107 N NE2 B HIS A 143 ? 0.96303 1.08492 0.62858 0.21595  -0.04117 0.11201  143 HIS A NE2 
1108 N N   . PHE A 144 ? 0.69808 0.84400 0.52326 0.10822  0.04708  0.07676  144 PHE A N   
1109 C CA  . PHE A 144 ? 0.63592 0.79705 0.49323 0.09148  0.06071  0.06577  144 PHE A CA  
1110 C C   . PHE A 144 ? 0.57948 0.76640 0.45133 0.09019  0.04942  0.04984  144 PHE A C   
1111 O O   . PHE A 144 ? 0.57337 0.76680 0.44907 0.08370  0.06186  0.04191  144 PHE A O   
1112 C CB  . PHE A 144 ? 0.60906 0.77619 0.50615 0.08285  0.06288  0.06437  144 PHE A CB  
1113 C CG  . PHE A 144 ? 0.58078 0.76671 0.51106 0.06855  0.07377  0.05262  144 PHE A CG  
1114 C CD1 . PHE A 144 ? 0.59912 0.77959 0.52667 0.05730  0.09704  0.05288  144 PHE A CD1 
1115 C CD2 . PHE A 144 ? 0.53916 0.74883 0.50224 0.06679  0.06115  0.04086  144 PHE A CD2 
1116 C CE1 . PHE A 144 ? 0.57063 0.77637 0.53259 0.04664  0.10495  0.04003  144 PHE A CE1 
1117 C CE2 . PHE A 144 ? 0.51641 0.74340 0.50687 0.05817  0.06873  0.03026  144 PHE A CE2 
1118 C CZ  . PHE A 144 ? 0.52928 0.75796 0.52146 0.04921  0.08937  0.02907  144 PHE A CZ  
1119 N N   . GLU A 145 ? 0.54848 0.74988 0.42901 0.09581  0.02735  0.04390  145 GLU A N   
1120 C CA  . GLU A 145 ? 0.53081 0.74892 0.42376 0.09192  0.01796  0.02834  145 GLU A CA  
1121 C C   . GLU A 145 ? 0.52028 0.75172 0.41671 0.09599  -0.00499 0.02345  145 GLU A C   
1122 O O   . GLU A 145 ? 0.51909 0.75489 0.42322 0.10147  -0.01314 0.03050  145 GLU A O   
1123 C CB  . GLU A 145 ? 0.50683 0.73508 0.43732 0.08218  0.02414  0.02049  145 GLU A CB  
1124 C CG  . GLU A 145 ? 0.48316 0.71928 0.44368 0.07901  0.01554  0.02185  145 GLU A CG  
1125 C CD  . GLU A 145 ? 0.45923 0.70269 0.45032 0.07139  0.02012  0.01479  145 GLU A CD  
1126 O OE1 . GLU A 145 ? 0.45443 0.70016 0.44802 0.06997  0.02972  0.00877  145 GLU A OE1 
1127 O OE2 . GLU A 145 ? 0.37627 0.62460 0.38798 0.06848  0.01371  0.01486  145 GLU A OE2 
1128 N N   . ARG A 146 ? 0.52607 0.76469 0.41763 0.09290  -0.01457 0.00983  146 ARG A N   
1129 C CA  . ARG A 146 ? 0.53119 0.78721 0.43391 0.09014  -0.03448 0.00026  146 ARG A CA  
1130 C C   . ARG A 146 ? 0.51893 0.77773 0.45095 0.07743  -0.03311 -0.00990 146 ARG A C   
1131 O O   . ARG A 146 ? 0.51970 0.76740 0.44426 0.07342  -0.02800 -0.01897 146 ARG A O   
1132 C CB  . ARG A 146 ? 0.55847 0.81650 0.42984 0.09329  -0.04683 -0.00929 146 ARG A CB  
1133 C CG  . ARG A 146 ? 0.55433 0.83445 0.44105 0.08539  -0.06648 -0.02347 146 ARG A CG  
1134 C CD  . ARG A 146 ? 0.58870 0.87829 0.44439 0.09149  -0.08346 -0.03144 146 ARG A CD  
1135 N NE  . ARG A 146 ? 0.60366 0.90529 0.44820 0.10868  -0.09377 -0.01965 146 ARG A NE  
1136 C CZ  . ARG A 146 ? 0.64358 0.95697 0.45942 0.11956  -0.11161 -0.02373 146 ARG A CZ  
1137 N NH1 . ARG A 146 ? 0.66729 0.98313 0.46306 0.11246  -0.12096 -0.04073 146 ARG A NH1 
1138 N NH2 . ARG A 146 ? 0.65689 0.97768 0.46099 0.13944  -0.12105 -0.01103 146 ARG A NH2 
1139 N N   . PHE A 147 ? 0.50989 0.78045 0.47145 0.07292  -0.03690 -0.00809 147 PHE A N   
1140 C CA  . PHE A 147 ? 0.50163 0.76976 0.48628 0.06186  -0.03375 -0.01460 147 PHE A CA  
1141 C C   . PHE A 147 ? 0.51550 0.79152 0.50441 0.05048  -0.04540 -0.02804 147 PHE A C   
1142 O O   . PHE A 147 ? 0.51947 0.81819 0.51905 0.04894  -0.05652 -0.03031 147 PHE A O   
1143 C CB  . PHE A 147 ? 0.47959 0.75355 0.49055 0.06149  -0.02909 -0.00624 147 PHE A CB  
1144 C CG  . PHE A 147 ? 0.46346 0.73173 0.49197 0.05180  -0.02544 -0.01143 147 PHE A CG  
1145 C CD1 . PHE A 147 ? 0.46117 0.73737 0.50217 0.04134  -0.03184 -0.01860 147 PHE A CD1 
1146 C CD2 . PHE A 147 ? 0.45265 0.70848 0.48371 0.05321  -0.01533 -0.00969 147 PHE A CD2 
1147 C CE1 . PHE A 147 ? 0.45291 0.71672 0.50174 0.03295  -0.02684 -0.02168 147 PHE A CE1 
1148 C CE2 . PHE A 147 ? 0.44313 0.69062 0.48368 0.04776  -0.01366 -0.01350 147 PHE A CE2 
1149 C CZ  . PHE A 147 ? 0.44519 0.69263 0.49119 0.03791  -0.01872 -0.01836 147 PHE A CZ  
1150 N N   . ARG A 148 ? 0.53440 0.79164 0.51570 0.04246  -0.04213 -0.03770 148 ARG A N   
1151 C CA  . ARG A 148 ? 0.56720 0.82271 0.55140 0.02674  -0.04868 -0.05090 148 ARG A CA  
1152 C C   . ARG A 148 ? 0.55869 0.79206 0.55036 0.01976  -0.03956 -0.05111 148 ARG A C   
1153 O O   . ARG A 148 ? 0.56431 0.77283 0.54158 0.02621  -0.03234 -0.05119 148 ARG A O   
1154 C CB  . ARG A 148 ? 0.62351 0.86612 0.57931 0.02332  -0.05405 -0.06412 148 ARG A CB  
1155 C CG  . ARG A 148 ? 0.65633 0.89730 0.61406 0.00286  -0.06074 -0.07995 148 ARG A CG  
1156 C CD  . ARG A 148 ? 0.70369 0.93004 0.63040 -0.00096 -0.06667 -0.09482 148 ARG A CD  
1157 N NE  . ARG A 148 ? 0.73202 0.94875 0.65813 -0.02460 -0.07005 -0.11185 148 ARG A NE  
1158 C CZ  . ARG A 148 ? 0.74288 0.99079 0.68031 -0.03926 -0.08298 -0.12471 148 ARG A CZ  
1159 N NH1 . ARG A 148 ? 0.73169 1.02194 0.67921 -0.02854 -0.09626 -0.12186 148 ARG A NH1 
1160 N NH2 . ARG A 148 ? 0.76777 1.00372 0.70534 -0.06516 -0.08252 -0.14147 148 ARG A NH2 
1161 N N   . GLY A 149 ? 0.55719 0.80025 0.56967 0.00829  -0.03981 -0.05154 149 GLY A N   
1162 C CA  . GLY A 149 ? 0.55536 0.77459 0.56942 0.00200  -0.03117 -0.05039 149 GLY A CA  
1163 C C   . GLY A 149 ? 0.53487 0.76871 0.57044 -0.01270 -0.02995 -0.05177 149 GLY A C   
1164 O O   . GLY A 149 ? 0.54204 0.80187 0.59011 -0.02369 -0.03654 -0.05984 149 GLY A O   
1165 N N   . ASP A 150 ? 0.50936 0.72973 0.54962 -0.01270 -0.02158 -0.04517 150 ASP A N   
1166 C CA  . ASP A 150 ? 0.48846 0.72083 0.54690 -0.02647 -0.01696 -0.04617 150 ASP A CA  
1167 C C   . ASP A 150 ? 0.46347 0.73165 0.54957 -0.01761 -0.01834 -0.03914 150 ASP A C   
1168 O O   . ASP A 150 ? 0.47338 0.76808 0.58092 -0.02722 -0.01775 -0.04346 150 ASP A O   
1169 C CB  . ASP A 150 ? 0.48921 0.68452 0.53186 -0.03033 -0.00673 -0.04258 150 ASP A CB  
1170 C CG  . ASP A 150 ? 0.53502 0.68898 0.54816 -0.04278 -0.00315 -0.05034 150 ASP A CG  
1171 O OD1 . ASP A 150 ? 0.55670 0.71238 0.56379 -0.05023 -0.00849 -0.06020 150 ASP A OD1 
1172 O OD2 . ASP A 150 ? 0.55849 0.67463 0.55058 -0.04443 0.00487  -0.04680 150 ASP A OD2 
1173 N N   . GLY A 151 ? 0.44613 0.71511 0.53231 -0.00008 -0.01886 -0.02949 151 GLY A N   
1174 C CA  . GLY A 151 ? 0.41978 0.71361 0.52645 0.00912  -0.01917 -0.02281 151 GLY A CA  
1175 C C   . GLY A 151 ? 0.39620 0.67894 0.49811 0.02318  -0.01560 -0.01314 151 GLY A C   
1176 O O   . GLY A 151 ? 0.40011 0.66459 0.48683 0.02709  -0.01406 -0.01240 151 GLY A O   
1177 N N   . LEU A 152 ? 0.37900 0.67420 0.49523 0.03033  -0.01352 -0.00719 152 LEU A N   
1178 C CA  . LEU A 152 ? 0.37134 0.65701 0.48544 0.04008  -0.00863 0.00069  152 LEU A CA  
1179 C C   . LEU A 152 ? 0.36751 0.65421 0.49475 0.04050  -0.00275 0.00289  152 LEU A C   
1180 O O   . LEU A 152 ? 0.36323 0.66493 0.50352 0.03850  -0.00290 0.00044  152 LEU A O   
1181 C CB  . LEU A 152 ? 0.37499 0.66610 0.48288 0.05111  -0.01167 0.00678  152 LEU A CB  
1182 C CG  . LEU A 152 ? 0.38558 0.67118 0.47445 0.05281  -0.01488 0.00566  152 LEU A CG  
1183 C CD1 . LEU A 152 ? 0.40268 0.69203 0.47939 0.06430  -0.01846 0.01244  152 LEU A CD1 
1184 C CD2 . LEU A 152 ? 0.37380 0.64345 0.45512 0.05196  -0.00705 0.00587  152 LEU A CD2 
1185 N N   . CYS A 153 ? 0.37776 0.65091 0.50244 0.04264  0.00284  0.00572  153 CYS A N   
1186 C CA  . CYS A 153 ? 0.37764 0.64758 0.51036 0.04261  0.00847  0.00616  153 CYS A CA  
1187 C C   . CYS A 153 ? 0.38562 0.64704 0.51769 0.04807  0.01323  0.01080  153 CYS A C   
1188 O O   . CYS A 153 ? 0.38760 0.64239 0.51491 0.04620  0.01529  0.01031  153 CYS A O   
1189 C CB  . CYS A 153 ? 0.37763 0.63627 0.50454 0.03642  0.01028  0.00186  153 CYS A CB  
1190 S SG  . CYS A 153 ? 0.37436 0.62618 0.50482 0.03639  0.01657  0.00049  153 CYS A SG  
1191 N N   . MET A 154 ? 0.40393 0.66491 0.54063 0.05458  0.01607  0.01434  154 MET A N   
1192 C CA  . MET A 154 ? 0.43352 0.67731 0.56571 0.05737  0.02327  0.01824  154 MET A CA  
1193 C C   . MET A 154 ? 0.44075 0.67751 0.57847 0.05405  0.02840  0.01335  154 MET A C   
1194 O O   . MET A 154 ? 0.43704 0.67949 0.58097 0.05861  0.02899  0.01195  154 MET A O   
1195 C CB  . MET A 154 ? 0.45515 0.69273 0.58030 0.07003  0.02354  0.02630  154 MET A CB  
1196 C CG  . MET A 154 ? 0.48745 0.69671 0.59961 0.07023  0.03364  0.03171  154 MET A CG  
1197 S SD  . MET A 154 ? 0.49886 0.70136 0.59988 0.06043  0.03897  0.03359  154 MET A SD  
1198 C CE  . MET A 154 ? 0.51832 0.71736 0.59833 0.07476  0.03396  0.04435  154 MET A CE  
1199 N N   . SER A 155 ? 0.45313 0.68084 0.58934 0.04617  0.03208  0.00915  155 SER A N   
1200 C CA  . SER A 155 ? 0.44098 0.66344 0.57902 0.04154  0.03453  0.00197  155 SER A CA  
1201 C C   . SER A 155 ? 0.45346 0.65689 0.58891 0.03840  0.04279  0.00040  155 SER A C   
1202 O O   . SER A 155 ? 0.46704 0.66358 0.60043 0.03349  0.04711  0.00219  155 SER A O   
1203 C CB  . SER A 155 ? 0.42891 0.65919 0.56632 0.03539  0.02913  -0.00468 155 SER A CB  
1204 O OG  . SER A 155 ? 0.43916 0.66395 0.57498 0.03124  0.03016  -0.01252 155 SER A OG  
1205 N N   . THR A 156 ? 0.43808 0.63085 0.57183 0.03991  0.04675  -0.00374 156 THR A N   
1206 C CA  . THR A 156 ? 0.45519 0.62548 0.58392 0.03399  0.05479  -0.00874 156 THR A CA  
1207 C C   . THR A 156 ? 0.44389 0.62277 0.57711 0.02016  0.05202  -0.01949 156 THR A C   
1208 O O   . THR A 156 ? 0.43208 0.63178 0.56963 0.01966  0.04326  -0.02208 156 THR A O   
1209 C CB  . THR A 156 ? 0.48403 0.64196 0.60822 0.04035  0.05911  -0.01273 156 THR A CB  
1210 O OG1 . THR A 156 ? 0.48168 0.65211 0.60615 0.03593  0.05450  -0.02127 156 THR A OG1 
1211 C CG2 . THR A 156 ? 0.49123 0.65432 0.61767 0.05667  0.05929  -0.00468 156 THR A CG2 
1212 N N   . PRO A 157 ? 0.45910 0.62218 0.59088 0.00907  0.05906  -0.02708 157 PRO A N   
1213 C CA  . PRO A 157 ? 0.45824 0.63760 0.59817 -0.00363 0.05412  -0.04115 157 PRO A CA  
1214 C C   . PRO A 157 ? 0.44487 0.63492 0.58019 0.00119  0.04420  -0.04832 157 PRO A C   
1215 O O   . PRO A 157 ? 0.42566 0.63833 0.56470 0.00243  0.03358  -0.05230 157 PRO A O   
1216 C CB  . PRO A 157 ? 0.49068 0.64600 0.62772 -0.01788 0.06520  -0.04953 157 PRO A CB  
1217 C CG  . PRO A 157 ? 0.51063 0.63597 0.63671 -0.01319 0.07703  -0.03631 157 PRO A CG  
1218 C CD  . PRO A 157 ? 0.49165 0.62058 0.61312 0.00711  0.07175  -0.02382 157 PRO A CD  
1219 N N   . SER A 158 ? 0.46087 0.63247 0.58470 0.00574  0.04828  -0.04970 158 SER A N   
1220 C CA  . SER A 158 ? 0.45797 0.63511 0.57131 0.00936  0.04148  -0.05628 158 SER A CA  
1221 C C   . SER A 158 ? 0.43340 0.62235 0.54337 0.01920  0.03668  -0.04681 158 SER A C   
1222 O O   . SER A 158 ? 0.42831 0.62058 0.52536 0.02156  0.03072  -0.05029 158 SER A O   
1223 C CB  . SER A 158 ? 0.47633 0.63001 0.57686 0.01116  0.04979  -0.06172 158 SER A CB  
1224 O OG  . SER A 158 ? 0.47017 0.61460 0.57091 0.02255  0.05815  -0.05128 158 SER A OG  
1225 N N   . GLY A 159 ? 0.42451 0.61728 0.54253 0.02424  0.03935  -0.03547 159 GLY A N   
1226 C CA  . GLY A 159 ? 0.40221 0.60631 0.51837 0.02927  0.03493  -0.02864 159 GLY A CA  
1227 C C   . GLY A 159 ? 0.39564 0.61183 0.51202 0.02832  0.02532  -0.02880 159 GLY A C   
1228 O O   . GLY A 159 ? 0.40225 0.62028 0.51042 0.03153  0.02158  -0.02494 159 GLY A O   
1229 N N   . THR A 160 ? 0.37804 0.60196 0.50326 0.02372  0.02241  -0.03421 160 THR A N   
1230 C CA  . THR A 160 ? 0.38759 0.62715 0.51610 0.02614  0.01395  -0.03519 160 THR A CA  
1231 C C   . THR A 160 ? 0.41223 0.65290 0.52509 0.03250  0.00355  -0.03978 160 THR A C   
1232 O O   . THR A 160 ? 0.41207 0.65855 0.52084 0.03948  -0.00347 -0.03809 160 THR A O   
1233 C CB  . THR A 160 ? 0.39375 0.64803 0.53907 0.01881  0.01493  -0.04240 160 THR A CB  
1234 O OG1 . THR A 160 ? 0.40236 0.65918 0.55016 0.01141  0.01347  -0.05506 160 THR A OG1 
1235 C CG2 . THR A 160 ? 0.39906 0.64493 0.55145 0.01379  0.02647  -0.03488 160 THR A CG2 
1236 N N   . THR A 161 ? 0.44008 0.67171 0.53969 0.03195  0.00250  -0.04545 161 THR A N   
1237 C CA  . THR A 161 ? 0.45391 0.67986 0.52965 0.04023  -0.00709 -0.04756 161 THR A CA  
1238 C C   . THR A 161 ? 0.45683 0.66258 0.51193 0.04320  -0.00181 -0.03715 161 THR A C   
1239 O O   . THR A 161 ? 0.47518 0.66666 0.50266 0.04989  -0.00710 -0.03620 161 THR A O   
1240 C CB  . THR A 161 ? 0.47302 0.69646 0.53732 0.03855  -0.01093 -0.05879 161 THR A CB  
1241 O OG1 . THR A 161 ? 0.47263 0.68232 0.53713 0.03145  0.00161  -0.05853 161 THR A OG1 
1242 C CG2 . THR A 161 ? 0.46950 0.71788 0.55385 0.03413  -0.01909 -0.07253 161 THR A CG2 
1243 N N   . ALA A 162 ? 0.44656 0.65089 0.51324 0.03826  0.00841  -0.02984 162 ALA A N   
1244 C CA  . ALA A 162 ? 0.45996 0.65163 0.51372 0.03657  0.01536  -0.02270 162 ALA A CA  
1245 C C   . ALA A 162 ? 0.44714 0.63931 0.50291 0.03711  0.01298  -0.01680 162 ALA A C   
1246 O O   . ALA A 162 ? 0.44556 0.63438 0.49188 0.04374  0.00408  -0.01739 162 ALA A O   
1247 C CB  . ALA A 162 ? 0.46041 0.65645 0.52797 0.03172  0.02732  -0.02146 162 ALA A CB  
1248 N N   . TYR A 163 ? 0.44434 0.64198 0.51214 0.03134  0.02029  -0.01257 163 TYR A N   
1249 C CA  . TYR A 163 ? 0.44403 0.64219 0.51328 0.02979  0.01811  -0.00900 163 TYR A CA  
1250 C C   . TYR A 163 ? 0.42677 0.63414 0.50501 0.03613  0.01008  -0.00984 163 TYR A C   
1251 O O   . TYR A 163 ? 0.42934 0.62867 0.49633 0.04006  0.00498  -0.00951 163 TYR A O   
1252 C CB  . TYR A 163 ? 0.43704 0.65021 0.52483 0.02352  0.02453  -0.00722 163 TYR A CB  
1253 C CG  . TYR A 163 ? 0.44361 0.65505 0.52816 0.01693  0.02430  -0.00620 163 TYR A CG  
1254 C CD1 . TYR A 163 ? 0.45877 0.64824 0.52084 0.01727  0.02032  -0.00575 163 TYR A CD1 
1255 C CD2 . TYR A 163 ? 0.44173 0.67357 0.54508 0.01119  0.02744  -0.00709 163 TYR A CD2 
1256 C CE1 . TYR A 163 ? 0.47540 0.65807 0.53173 0.00916  0.02113  -0.00648 163 TYR A CE1 
1257 C CE2 . TYR A 163 ? 0.45157 0.68419 0.55313 0.00229  0.02661  -0.00900 163 TYR A CE2 
1258 C CZ  . TYR A 163 ? 0.46841 0.67390 0.54546 -0.00015 0.02426  -0.00883 163 TYR A CZ  
1259 O OH  . TYR A 163 ? 0.47507 0.67658 0.54782 -0.01101 0.02440  -0.01233 163 TYR A OH  
1260 N N   . ASN A 164 ? 0.41103 0.63280 0.50769 0.03690  0.01074  -0.01135 164 ASN A N   
1261 C CA  . ASN A 164 ? 0.40393 0.63672 0.51050 0.04013  0.00688  -0.01297 164 ASN A CA  
1262 C C   . ASN A 164 ? 0.42094 0.65326 0.51770 0.04739  -0.00145 -0.01798 164 ASN A C   
1263 O O   . ASN A 164 ? 0.42746 0.66531 0.52565 0.05243  -0.00469 -0.01866 164 ASN A O   
1264 C CB  . ASN A 164 ? 0.39837 0.63907 0.52015 0.03677  0.01146  -0.01515 164 ASN A CB  
1265 C CG  . ASN A 164 ? 0.40071 0.65441 0.53331 0.03644  0.01063  -0.01881 164 ASN A CG  
1266 O OD1 . ASN A 164 ? 0.40273 0.65977 0.54039 0.03572  0.01466  -0.01446 164 ASN A OD1 
1267 N ND2 . ASN A 164 ? 0.39916 0.66272 0.53515 0.03699  0.00561  -0.02781 164 ASN A ND2 
1268 N N   . LYS A 165 ? 0.42866 0.65485 0.51355 0.05026  -0.00557 -0.02213 165 LYS A N   
1269 C CA  . LYS A 165 ? 0.43643 0.66433 0.51030 0.06167  -0.01634 -0.02751 165 LYS A CA  
1270 C C   . LYS A 165 ? 0.44684 0.65326 0.49716 0.06986  -0.01934 -0.02263 165 LYS A C   
1271 O O   . LYS A 165 ? 0.44623 0.65810 0.49530 0.08150  -0.02632 -0.02578 165 LYS A O   
1272 C CB  . LYS A 165 ? 0.46132 0.68413 0.52093 0.06429  -0.02145 -0.03264 165 LYS A CB  
1273 C CG  . LYS A 165 ? 0.48408 0.70899 0.52766 0.08051  -0.03588 -0.03843 165 LYS A CG  
1274 C CD  . LYS A 165 ? 0.51320 0.73755 0.54317 0.08260  -0.04249 -0.04529 165 LYS A CD  
1275 C CE  . LYS A 165 ? 0.53579 0.77445 0.55716 0.10100  -0.06043 -0.05412 165 LYS A CE  
1276 N NZ  . LYS A 165 ? 0.56649 0.77773 0.55475 0.11910  -0.06639 -0.04637 165 LYS A NZ  
1277 N N   . SER A 166 ? 0.46640 0.64745 0.49734 0.06356  -0.01298 -0.01612 166 SER A N   
1278 C CA  . SER A 166 ? 0.49600 0.64881 0.50107 0.06687  -0.01299 -0.01192 166 SER A CA  
1279 C C   . SER A 166 ? 0.47581 0.63660 0.49354 0.06645  -0.01253 -0.01211 166 SER A C   
1280 O O   . SER A 166 ? 0.49159 0.62980 0.48828 0.07288  -0.01471 -0.01147 166 SER A O   
1281 C CB  . SER A 166 ? 0.52727 0.65640 0.51527 0.05362  -0.00246 -0.00675 166 SER A CB  
1282 O OG  . SER A 166 ? 0.56446 0.67877 0.53110 0.05506  -0.00125 -0.00604 166 SER A OG  
1283 N N   . LEU A 167 ? 0.44322 0.63061 0.48980 0.05969  -0.00911 -0.01282 167 LEU A N   
1284 C CA  . LEU A 167 ? 0.44003 0.63534 0.49515 0.05966  -0.00842 -0.01306 167 LEU A CA  
1285 C C   . LEU A 167 ? 0.43918 0.65494 0.50721 0.07007  -0.01224 -0.01822 167 LEU A C   
1286 O O   . LEU A 167 ? 0.42904 0.65696 0.50759 0.06887  -0.00916 -0.01855 167 LEU A O   
1287 C CB  . LEU A 167 ? 0.41133 0.62101 0.48445 0.04853  -0.00251 -0.00993 167 LEU A CB  
1288 C CG  . LEU A 167 ? 0.41019 0.61063 0.47838 0.03762  0.00193  -0.00744 167 LEU A CG  
1289 C CD1 . LEU A 167 ? 0.38984 0.61133 0.47906 0.03279  0.00508  -0.00538 167 LEU A CD1 
1290 C CD2 . LEU A 167 ? 0.42968 0.61049 0.47960 0.03322  0.00158  -0.00866 167 LEU A CD2 
1291 N N   . GLY A 168 ? 0.54159 0.66442 0.49641 0.01957  0.00510  0.04641  168 GLY A N   
1292 C CA  . GLY A 168 ? 0.53041 0.64847 0.49176 0.02911  -0.00206 0.04110  168 GLY A CA  
1293 C C   . GLY A 168 ? 0.50942 0.64023 0.47757 0.03566  0.00454  0.03602  168 GLY A C   
1294 O O   . GLY A 168 ? 0.50682 0.63882 0.48540 0.04175  0.00097  0.03246  168 GLY A O   
1295 N N   . GLY A 169 ? 0.49200 0.63197 0.45628 0.03473  0.01454  0.03593  169 GLY A N   
1296 C CA  . GLY A 169 ? 0.48853 0.63378 0.45799 0.04068  0.02001  0.03186  169 GLY A CA  
1297 C C   . GLY A 169 ? 0.50701 0.64144 0.46987 0.03989  0.01452  0.02951  169 GLY A C   
1298 O O   . GLY A 169 ? 0.52163 0.64548 0.47041 0.03573  0.00689  0.03118  169 GLY A O   
1299 N N   . ALA A 170 ? 0.50019 0.63617 0.47254 0.04303  0.01719  0.02625  170 ALA A N   
1300 C CA  . ALA A 170 ? 0.48802 0.61433 0.45737 0.04004  0.01063  0.02252  170 ALA A CA  
1301 C C   . ALA A 170 ? 0.50194 0.61682 0.44906 0.03911  0.01469  0.01830  170 ALA A C   
1302 O O   . ALA A 170 ? 0.50165 0.62004 0.44429 0.04333  0.02606  0.01811  170 ALA A O   
1303 C CB  . ALA A 170 ? 0.46726 0.59771 0.45670 0.04074  0.01279  0.02156  170 ALA A CB  
1304 N N   . LEU A 171 ? 0.51212 0.61427 0.44509 0.03477  0.00463  0.01395  171 LEU A N   
1305 C CA  . LEU A 171 ? 0.54295 0.63004 0.45054 0.03490  0.00770  0.00636  171 LEU A CA  
1306 C C   . LEU A 171 ? 0.56606 0.64228 0.48362 0.03378  0.00539  -0.00081 171 LEU A C   
1307 O O   . LEU A 171 ? 0.57222 0.64962 0.50721 0.02779  -0.00617 -0.00101 171 LEU A O   
1308 C CB  . LEU A 171 ? 0.56166 0.63698 0.44014 0.03026  -0.00386 0.00487  171 LEU A CB  
1309 C CG  . LEU A 171 ? 0.56706 0.64703 0.43698 0.02818  -0.00730 0.01518  171 LEU A CG  
1310 C CD1 . LEU A 171 ? 0.60777 0.67183 0.44108 0.02439  -0.01857 0.01514  171 LEU A CD1 
1311 C CD2 . LEU A 171 ? 0.56111 0.65220 0.43098 0.02998  0.00992  0.02078  171 LEU A CD2 
1312 N N   . MET A 172 ? 0.59393 0.65978 0.50344 0.03946  0.01629  -0.00624 172 MET A N   
1313 C CA  . MET A 172 ? 0.60611 0.65548 0.52502 0.03759  0.01442  -0.01161 172 MET A CA  
1314 C C   . MET A 172 ? 0.63978 0.66279 0.53052 0.04126  0.01629  -0.02492 172 MET A C   
1315 O O   . MET A 172 ? 0.64809 0.67148 0.51914 0.05073  0.02784  -0.02825 172 MET A O   
1316 C CB  . MET A 172 ? 0.58156 0.63827 0.52368 0.04301  0.02518  -0.00352 172 MET A CB  
1317 C CG  . MET A 172 ? 0.58043 0.63946 0.51622 0.05603  0.03903  -0.00263 172 MET A CG  
1318 S SD  . MET A 172 ? 0.57286 0.64227 0.53275 0.06168  0.04598  0.00980  172 MET A SD  
1319 C CE  . MET A 172 ? 0.53610 0.63615 0.50647 0.05885  0.04405  0.01750  172 MET A CE  
1320 N N   . HIS A 173 ? 0.66254 0.66338 0.55316 0.03334  0.00504  -0.03328 173 HIS A N   
1321 C CA  . HIS A 173 ? 0.72240 0.69131 0.58311 0.03601  0.00352  -0.04946 173 HIS A CA  
1322 C C   . HIS A 173 ? 0.74596 0.70336 0.60439 0.05095  0.02080  -0.05172 173 HIS A C   
1323 O O   . HIS A 173 ? 0.73860 0.70010 0.62300 0.05359  0.02681  -0.04179 173 HIS A O   
1324 C CB  . HIS A 173 ? 0.73934 0.68553 0.60748 0.02196  -0.01396 -0.05754 173 HIS A CB  
1325 C CG  . HIS A 173 ? 0.79426 0.70324 0.62587 0.02277  -0.02053 -0.07766 173 HIS A CG  
1326 N ND1 . HIS A 173 ? 0.82453 0.70100 0.64803 0.03051  -0.01250 -0.08728 173 HIS A ND1 
1327 C CD2 . HIS A 173 ? 0.82902 0.72542 0.62591 0.01838  -0.03484 -0.09085 173 HIS A CD2 
1328 C CE1 . HIS A 173 ? 0.87838 0.72290 0.66407 0.03085  -0.02085 -0.10761 173 HIS A CE1 
1329 N NE2 . HIS A 173 ? 0.88321 0.73992 0.65041 0.02303  -0.03466 -0.11011 173 HIS A NE2 
1330 N N   . PRO A 174 ? 0.79438 0.73787 0.62126 0.06246  0.02934  -0.06434 174 PRO A N   
1331 C CA  . PRO A 174 ? 0.79758 0.73626 0.62677 0.08074  0.04649  -0.06616 174 PRO A CA  
1332 C C   . PRO A 174 ? 0.83473 0.73708 0.67180 0.08348  0.04371  -0.07131 174 PRO A C   
1333 O O   . PRO A 174 ? 0.85046 0.74794 0.69432 0.10031  0.05573  -0.07003 174 PRO A O   
1334 C CB  . PRO A 174 ? 0.83131 0.76518 0.62289 0.09184  0.05673  -0.08059 174 PRO A CB  
1335 C CG  . PRO A 174 ? 0.83250 0.77661 0.60255 0.07881  0.04694  -0.07988 174 PRO A CG  
1336 C CD  . PRO A 174 ? 0.82297 0.75964 0.60995 0.06122  0.02531  -0.07592 174 PRO A CD  
1337 N N   . SER A 175 ? 0.85921 0.73550 0.69740 0.06746  0.02755  -0.07636 175 SER A N   
1338 C CA  . SER A 175 ? 0.91769 0.75692 0.76647 0.06681  0.02509  -0.07779 175 SER A CA  
1339 C C   . SER A 175 ? 0.90137 0.75668 0.78547 0.06519  0.03026  -0.05575 175 SER A C   
1340 O O   . SER A 175 ? 0.93601 0.76123 0.82790 0.06775  0.03169  -0.05206 175 SER A O   
1341 C CB  . SER A 175 ? 0.96523 0.77376 0.80915 0.04637  0.00537  -0.08899 175 SER A CB  
1342 O OG  . SER A 175 ? 0.94581 0.78441 0.81398 0.02740  -0.00574 -0.07770 175 SER A OG  
1343 N N   . ILE A 176 ? 0.85886 0.75710 0.76076 0.06141  0.03279  -0.04122 176 ILE A N   
1344 C CA  . ILE A 176 ? 0.82525 0.74072 0.75433 0.06033  0.03795  -0.02143 176 ILE A CA  
1345 C C   . ILE A 176 ? 0.81259 0.73881 0.74095 0.08192  0.05082  -0.01545 176 ILE A C   
1346 O O   . ILE A 176 ? 0.78495 0.74063 0.70947 0.09032  0.05653  -0.01646 176 ILE A O   
1347 C CB  . ILE A 176 ? 0.77050 0.72464 0.71683 0.04867  0.03431  -0.01157 176 ILE A CB  
1348 C CG1 . ILE A 176 ? 0.77299 0.72175 0.72598 0.02899  0.01968  -0.01742 176 ILE A CG1 
1349 C CG2 . ILE A 176 ? 0.74095 0.71222 0.70845 0.04967  0.04151  0.00685  176 ILE A CG2 
1350 C CD1 . ILE A 176 ? 0.73429 0.71985 0.70131 0.02175  0.01442  -0.01165 176 ILE A CD1 
1351 N N   . GLU A 177 ? 0.83505 0.73762 0.76865 0.09037  0.05437  -0.00815 177 GLU A N   
1352 C CA  . GLU A 177 ? 0.82097 0.73488 0.75767 0.11241  0.06340  -0.00130 177 GLU A CA  
1353 C C   . GLU A 177 ? 0.76956 0.72142 0.72245 0.10971  0.06483  0.01639  177 GLU A C   
1354 O O   . GLU A 177 ? 0.77496 0.71998 0.73556 0.10639  0.06439  0.03151  177 GLU A O   
1355 C CB  . GLU A 177 ? 0.87070 0.74124 0.80458 0.12430  0.06417  0.00107  177 GLU A CB  
1356 C CG  . GLU A 177 ? 0.92738 0.75671 0.84181 0.13138  0.06328  -0.02013 177 GLU A CG  
1357 C CD  . GLU A 177 ? 0.98834 0.77245 0.90004 0.14857  0.06444  -0.01840 177 GLU A CD  
1358 O OE1 . GLU A 177 ? 1.00255 0.76970 0.92399 0.14318  0.06155  0.00011  177 GLU A OE1 
1359 O OE2 . GLU A 177 ? 1.02975 0.79405 0.92815 0.16858  0.06900  -0.03511 177 GLU A OE2 
1360 N N   . ALA A 178 ? 0.71900 0.70905 0.67425 0.11057  0.06678  0.01442  178 ALA A N   
1361 C CA  . ALA A 178 ? 0.67375 0.69750 0.64107 0.10702  0.06634  0.02715  178 ALA A CA  
1362 C C   . ALA A 178 ? 0.63859 0.69699 0.60863 0.11431  0.06953  0.02377  178 ALA A C   
1363 O O   . ALA A 178 ? 0.64599 0.70552 0.60911 0.12080  0.07422  0.01300  178 ALA A O   
1364 C CB  . ALA A 178 ? 0.65848 0.68842 0.63084 0.08760  0.06130  0.02964  178 ALA A CB  
1365 N N   . MET A 179 ? 0.59668 0.68302 0.57615 0.11225  0.06755  0.03288  179 MET A N   
1366 C CA  . MET A 179 ? 0.56592 0.68566 0.55185 0.11367  0.06843  0.03149  179 MET A CA  
1367 C C   . MET A 179 ? 0.53471 0.66943 0.52336 0.10095  0.06288  0.03585  179 MET A C   
1368 O O   . MET A 179 ? 0.54324 0.67135 0.53201 0.09727  0.06047  0.04251  179 MET A O   
1369 C CB  . MET A 179 ? 0.57198 0.71047 0.56976 0.12959  0.06945  0.03690  179 MET A CB  
1370 C CG  . MET A 179 ? 0.57255 0.71035 0.57165 0.13318  0.06348  0.04943  179 MET A CG  
1371 S SD  . MET A 179 ? 0.57996 0.73990 0.59280 0.15376  0.05985  0.05589  179 MET A SD  
1372 C CE  . MET A 179 ? 0.58611 0.73805 0.58709 0.15428  0.05164  0.07120  179 MET A CE  
1373 N N   . GLN A 180 ? 0.50095 0.65443 0.49109 0.09459  0.06192  0.03240  180 GLN A N   
1374 C CA  . GLN A 180 ? 0.48174 0.64374 0.47321 0.08402  0.05592  0.03436  180 GLN A CA  
1375 C C   . GLN A 180 ? 0.46583 0.65244 0.46530 0.08357  0.05328  0.03605  180 GLN A C   
1376 O O   . GLN A 180 ? 0.46628 0.66588 0.46976 0.08291  0.05668  0.03398  180 GLN A O   
1377 C CB  . GLN A 180 ? 0.48621 0.63865 0.46995 0.07334  0.05314  0.02923  180 GLN A CB  
1378 C CG  . GLN A 180 ? 0.47878 0.63688 0.46613 0.06576  0.04631  0.03099  180 GLN A CG  
1379 C CD  . GLN A 180 ? 0.48888 0.63726 0.47020 0.05749  0.04053  0.02752  180 GLN A CD  
1380 O OE1 . GLN A 180 ? 0.48013 0.63093 0.46585 0.05365  0.03427  0.02829  180 GLN A OE1 
1381 N NE2 . GLN A 180 ? 0.50462 0.64097 0.47413 0.05630  0.04157  0.02297  180 GLN A NE2 
1382 N N   . LEU A 181 ? 0.46099 0.65382 0.46216 0.08279  0.04762  0.03931  181 LEU A N   
1383 C CA  . LEU A 181 ? 0.44737 0.65965 0.45508 0.08053  0.04153  0.03930  181 LEU A CA  
1384 C C   . LEU A 181 ? 0.43720 0.64459 0.44115 0.06986  0.03638  0.03598  181 LEU A C   
1385 O O   . LEU A 181 ? 0.43062 0.62648 0.42860 0.06933  0.03548  0.03519  181 LEU A O   
1386 C CB  . LEU A 181 ? 0.44150 0.66025 0.44742 0.08876  0.03655  0.04339  181 LEU A CB  
1387 C CG  . LEU A 181 ? 0.42242 0.66000 0.43330 0.08640  0.02633  0.04160  181 LEU A CG  
1388 C CD1 . LEU A 181 ? 0.41167 0.67363 0.44185 0.08992  0.02489  0.04290  181 LEU A CD1 
1389 C CD2 . LEU A 181 ? 0.42672 0.66182 0.42312 0.09277  0.02038  0.04379  181 LEU A CD2 
1390 N N   . THR A 182 ? 0.43879 0.65504 0.44816 0.06162  0.03357  0.03476  182 THR A N   
1391 C CA  . THR A 182 ? 0.44460 0.65179 0.45023 0.05221  0.02682  0.03246  182 THR A CA  
1392 C C   . THR A 182 ? 0.45816 0.67739 0.47177 0.04620  0.01881  0.03112  182 THR A C   
1393 O O   . THR A 182 ? 0.46009 0.70024 0.48653 0.04629  0.01934  0.03301  182 THR A O   
1394 C CB  . THR A 182 ? 0.44751 0.64471 0.44775 0.04403  0.02931  0.03402  182 THR A CB  
1395 O OG1 . THR A 182 ? 0.45285 0.66476 0.45857 0.04107  0.03667  0.03682  182 THR A OG1 
1396 C CG2 . THR A 182 ? 0.44148 0.62406 0.43288 0.04787  0.03204  0.03308  182 THR A CG2 
1397 N N   . GLU A 183 ? 0.46421 0.67005 0.47222 0.04117  0.01040  0.02703  183 GLU A N   
1398 C CA  . GLU A 183 ? 0.47572 0.68541 0.48857 0.03357  -0.00032 0.02322  183 GLU A CA  
1399 C C   . GLU A 183 ? 0.48525 0.68836 0.50395 0.01792  -0.00240 0.02663  183 GLU A C   
1400 O O   . GLU A 183 ? 0.49567 0.68268 0.50668 0.01504  0.00136  0.03050  183 GLU A O   
1401 C CB  . GLU A 183 ? 0.49007 0.68329 0.48943 0.03874  -0.00822 0.01461  183 GLU A CB  
1402 C CG  . GLU A 183 ? 0.48879 0.68570 0.47758 0.05300  -0.00346 0.01332  183 GLU A CG  
1403 C CD  . GLU A 183 ? 0.49922 0.68295 0.47222 0.05897  -0.00845 0.00364  183 GLU A CD  
1404 O OE1 . GLU A 183 ? 0.50626 0.67226 0.47748 0.05476  -0.01438 -0.00273 183 GLU A OE1 
1405 O OE2 . GLU A 183 ? 0.50219 0.69145 0.46241 0.06879  -0.00587 0.00260  183 GLU A OE2 
1406 N N   . MET A 184 ? 0.49117 0.70644 0.52327 0.00672  -0.00970 0.02609  184 MET A N   
1407 C CA  . MET A 184 ? 0.50744 0.71142 0.54462 -0.01150 -0.01378 0.02989  184 MET A CA  
1408 C C   . MET A 184 ? 0.52072 0.70684 0.55458 -0.01706 -0.03052 0.02026  184 MET A C   
1409 O O   . MET A 184 ? 0.52888 0.73240 0.57344 -0.02007 -0.03973 0.01483  184 MET A O   
1410 C CB  . MET A 184 ? 0.50388 0.73816 0.56440 -0.02438 -0.00702 0.03804  184 MET A CB  
1411 C CG  . MET A 184 ? 0.49083 0.74942 0.55668 -0.01478 0.00962  0.04343  184 MET A CG  
1412 S SD  . MET A 184 ? 0.50057 0.80281 0.59986 -0.02767 0.02025  0.05158  184 MET A SD  
1413 C CE  . MET A 184 ? 0.48394 0.80368 0.58045 -0.00742 0.03891  0.05232  184 MET A CE  
1414 N N   . ALA A 185 ? 0.52962 0.68027 0.54812 -0.01712 -0.03583 0.01721  185 ALA A N   
1415 C CA  . ALA A 185 ? 0.55698 0.68050 0.56962 -0.02342 -0.05159 0.00716  185 ALA A CA  
1416 C C   . ALA A 185 ? 0.56576 0.69896 0.57379 -0.01563 -0.06125 -0.00678 185 ALA A C   
1417 O O   . ALA A 185 ? 0.58873 0.72473 0.60449 -0.02793 -0.07469 -0.01281 185 ALA A O   
1418 C CB  . ALA A 185 ? 0.57082 0.68771 0.59760 -0.04805 -0.05766 0.01422  185 ALA A CB  
1419 N N   . SER A 186 ? 0.55045 0.68867 0.54453 0.00398  -0.05482 -0.01135 186 SER A N   
1420 C CA  . SER A 186 ? 0.57214 0.71438 0.55209 0.01351  -0.06286 -0.02380 186 SER A CA  
1421 C C   . SER A 186 ? 0.60601 0.71288 0.56770 0.01470  -0.07484 -0.03962 186 SER A C   
1422 O O   . SER A 186 ? 0.61249 0.69312 0.56705 0.02103  -0.07119 -0.04183 186 SER A O   
1423 C CB  . SER A 186 ? 0.56474 0.71912 0.53252 0.03279  -0.05008 -0.02190 186 SER A CB  
1424 O OG  . SER A 186 ? 0.56937 0.70643 0.53125 0.04153  -0.04042 -0.02144 186 SER A OG  
1425 N N   . ILE A 187 ? 0.63873 0.74407 0.59308 0.00952  -0.09067 -0.05163 187 ILE A N   
1426 C CA  . ILE A 187 ? 0.69591 0.76562 0.62594 0.01469  -0.10193 -0.07087 187 ILE A CA  
1427 C C   . ILE A 187 ? 0.70678 0.77826 0.60979 0.03893  -0.09118 -0.07870 187 ILE A C   
1428 O O   . ILE A 187 ? 0.67659 0.77681 0.57540 0.04695  -0.08366 -0.07213 187 ILE A O   
1429 C CB  . ILE A 187 ? 0.72707 0.79299 0.65542 -0.00029 -0.12480 -0.08315 187 ILE A CB  
1430 C CG1 . ILE A 187 ? 0.77182 0.79246 0.67204 0.00449  -0.13758 -0.10586 187 ILE A CG1 
1431 C CG2 . ILE A 187 ? 0.72870 0.83042 0.65178 0.00507  -0.12938 -0.08344 187 ILE A CG2 
1432 C CD1 . ILE A 187 ? 0.81018 0.82121 0.70767 -0.01297 -0.16362 -0.12037 187 ILE A CD1 
1433 N N   . ASN A 188 ? 0.76288 0.80400 0.64914 0.05136  -0.08863 -0.09111 188 ASN A N   
1434 C CA  . ASN A 188 ? 0.79148 0.83604 0.65336 0.07404  -0.07563 -0.09930 188 ASN A CA  
1435 C C   . ASN A 188 ? 0.86795 0.87583 0.70369 0.08409  -0.08356 -0.12313 188 ASN A C   
1436 O O   . ASN A 188 ? 0.87850 0.85603 0.72182 0.08518  -0.08646 -0.12805 188 ASN A O   
1437 C CB  . ASN A 188 ? 0.75568 0.81273 0.63289 0.08468  -0.05517 -0.08636 188 ASN A CB  
1438 C CG  . ASN A 188 ? 0.71087 0.80351 0.59961 0.08260  -0.04393 -0.06825 188 ASN A CG  
1439 O OD1 . ASN A 188 ? 0.70311 0.81193 0.57849 0.09451  -0.03177 -0.06633 188 ASN A OD1 
1440 N ND2 . ASN A 188 ? 0.68355 0.78661 0.59561 0.06763  -0.04716 -0.05477 188 ASN A ND2 
1441 N N   . ASN A 189 ? 0.92505 0.93331 0.72723 0.09254  -0.08786 -0.13808 189 ASN A N   
1442 C CA  . ASN A 189 ? 1.03673 1.00998 0.80614 0.10547  -0.09373 -0.16435 189 ASN A CA  
1443 C C   . ASN A 189 ? 1.10800 1.09579 0.83808 0.12468  -0.08173 -0.17322 189 ASN A C   
1444 O O   . ASN A 189 ? 1.09507 1.11606 0.82890 0.13130  -0.06311 -0.15665 189 ASN A O   
1445 C CB  . ASN A 189 ? 1.07169 1.01496 0.83336 0.08777  -0.12230 -0.17969 189 ASN A CB  
1446 C CG  . ASN A 189 ? 1.05997 1.03238 0.83117 0.06827  -0.13706 -0.16975 189 ASN A CG  
1447 O OD1 . ASN A 189 ? 1.04038 1.04790 0.80440 0.07453  -0.12897 -0.15939 189 ASN A OD1 
1448 N ND2 . ASN A 189 ? 1.07530 1.03382 0.86548 0.04445  -0.15882 -0.17169 189 ASN A ND2 
1449 N N   . ARG A 190 ? 1.20992 1.17020 0.89933 0.13327  -0.09207 -0.19928 190 ARG A N   
1450 C CA  . ARG A 190 ? 1.24647 1.21875 0.88951 0.15048  -0.08171 -0.20798 190 ARG A CA  
1451 C C   . ARG A 190 ? 1.24135 1.24048 0.87244 0.13935  -0.09383 -0.19628 190 ARG A C   
1452 O O   . ARG A 190 ? 1.24579 1.26764 0.85091 0.15098  -0.07926 -0.18801 190 ARG A O   
1453 C CB  . ARG A 190 ? 1.32004 1.25199 0.91739 0.16377  -0.09050 -0.24185 190 ARG A CB  
1454 N N   . VAL A 191 ? 1.19929 1.19714 0.85074 0.11720  -0.12005 -0.19416 191 VAL A N   
1455 C CA  . VAL A 191 ? 1.18445 1.21065 0.83157 0.10774  -0.13503 -0.18346 191 VAL A CA  
1456 C C   . VAL A 191 ? 1.09906 1.16333 0.78430 0.10403  -0.11983 -0.15267 191 VAL A C   
1457 O O   . VAL A 191 ? 1.09484 1.18268 0.76374 0.11354  -0.11008 -0.13928 191 VAL A O   
1458 C CB  . VAL A 191 ? 1.21912 1.23437 0.88014 0.08481  -0.16911 -0.19402 191 VAL A CB  
1459 C CG1 . VAL A 191 ? 1.21405 1.26730 0.88420 0.07561  -0.18486 -0.17975 191 VAL A CG1 
1460 C CG2 . VAL A 191 ? 1.30307 1.27656 0.91919 0.08832  -0.18770 -0.22714 191 VAL A CG2 
1461 N N   . TYR A 192 ? 1.03888 1.10616 0.77230 0.09016  -0.11806 -0.14110 192 TYR A N   
1462 C CA  . TYR A 192 ? 0.93477 1.03416 0.70464 0.08519  -0.10621 -0.11507 192 TYR A CA  
1463 C C   . TYR A 192 ? 0.85435 0.95454 0.63445 0.09652  -0.07863 -0.10506 192 TYR A C   
1464 O O   . TYR A 192 ? 0.85541 0.93263 0.63829 0.10060  -0.07269 -0.11459 192 TYR A O   
1465 C CB  . TYR A 192 ? 0.91893 1.02423 0.73256 0.06284  -0.11951 -0.10800 192 TYR A CB  
1466 C CG  . TYR A 192 ? 0.93890 1.06193 0.75826 0.04986  -0.14460 -0.11008 192 TYR A CG  
1467 C CD1 . TYR A 192 ? 0.91844 1.07933 0.75384 0.05072  -0.14472 -0.09298 192 TYR A CD1 
1468 C CD2 . TYR A 192 ? 0.98406 1.08591 0.79524 0.03702  -0.16973 -0.12960 192 TYR A CD2 
1469 C CE1 . TYR A 192 ? 0.93811 1.12098 0.78463 0.04047  -0.16928 -0.09446 192 TYR A CE1 
1470 C CE2 . TYR A 192 ? 1.00580 1.12880 0.82762 0.02360  -0.19522 -0.13169 192 TYR A CE2 
1471 C CZ  . TYR A 192 ? 0.98334 1.14965 0.82451 0.02608  -0.19484 -0.11366 192 TYR A CZ  
1472 O OH  . TYR A 192 ? 1.00570 1.19838 0.86325 0.01437  -0.22146 -0.11527 192 TYR A OH  
1473 N N   . ARG A 193 ? 0.78521 0.91125 0.57262 0.10166  -0.06349 -0.08582 193 ARG A N   
1474 C CA  . ARG A 193 ? 0.74607 0.87710 0.54498 0.11047  -0.03874 -0.07547 193 ARG A CA  
1475 C C   . ARG A 193 ? 0.69708 0.85120 0.52438 0.10436  -0.03178 -0.05334 193 ARG A C   
1476 O O   . ARG A 193 ? 0.71131 0.88115 0.52904 0.10683  -0.03317 -0.04329 193 ARG A O   
1477 C CB  . ARG A 193 ? 0.78003 0.91240 0.54325 0.12798  -0.02206 -0.07902 193 ARG A CB  
1478 C CG  . ARG A 193 ? 0.79100 0.91581 0.56062 0.13871  -0.00308 -0.08532 193 ARG A CG  
1479 N N   . THR A 194 ? 0.64061 0.79428 0.49984 0.09775  -0.02528 -0.04617 194 THR A N   
1480 C CA  . THR A 194 ? 0.59090 0.76195 0.47284 0.09446  -0.01573 -0.02797 194 THR A CA  
1481 C C   . THR A 194 ? 0.56903 0.73893 0.46139 0.09990  0.00238  -0.02287 194 THR A C   
1482 O O   . THR A 194 ? 0.57949 0.73788 0.46988 0.10536  0.00621  -0.03261 194 THR A O   
1483 C CB  . THR A 194 ? 0.56336 0.73937 0.47364 0.08003  -0.02510 -0.02271 194 THR A CB  
1484 O OG1 . THR A 194 ? 0.55107 0.71141 0.47552 0.07410  -0.02408 -0.02563 194 THR A OG1 
1485 C CG2 . THR A 194 ? 0.57999 0.75982 0.48796 0.07189  -0.04477 -0.02970 194 THR A CG2 
1486 N N   . ILE A 195 ? 0.54806 0.73012 0.45367 0.09879  0.01231  -0.00808 195 ILE A N   
1487 C CA  . ILE A 195 ? 0.53150 0.71574 0.45029 0.10145  0.02758  -0.00236 195 ILE A CA  
1488 C C   . ILE A 195 ? 0.51506 0.69118 0.45604 0.09560  0.02367  -0.00543 195 ILE A C   
1489 O O   . ILE A 195 ? 0.50205 0.67840 0.45413 0.09969  0.03127  -0.00653 195 ILE A O   
1490 C CB  . ILE A 195 ? 0.51066 0.70420 0.43576 0.09996  0.03617  0.01322  195 ILE A CB  
1491 C CG1 . ILE A 195 ? 0.49880 0.69586 0.43747 0.10059  0.05124  0.01901  195 ILE A CG1 
1492 C CG2 . ILE A 195 ? 0.48671 0.68159 0.42878 0.09171  0.02839  0.01835  195 ILE A CG2 
1493 C CD1 . ILE A 195 ? 0.51476 0.71649 0.44251 0.10912  0.06295  0.01421  195 ILE A CD1 
1494 N N   . GLY A 196 ? 0.51665 0.68716 0.46507 0.08601  0.01179  -0.00567 196 GLY A N   
1495 C CA  . GLY A 196 ? 0.50008 0.65975 0.46366 0.07955  0.00726  -0.00558 196 GLY A CA  
1496 C C   . GLY A 196 ? 0.47233 0.63827 0.45042 0.07580  0.01372  0.00470  196 GLY A C   
1497 O O   . GLY A 196 ? 0.47276 0.63658 0.45678 0.06694  0.00975  0.00952  196 GLY A O   
1498 N N   . SER A 197 ? 0.45321 0.62700 0.43622 0.08152  0.02411  0.00792  197 SER A N   
1499 C CA  . SER A 197 ? 0.44520 0.62214 0.44126 0.07710  0.02811  0.01544  197 SER A CA  
1500 C C   . SER A 197 ? 0.43971 0.61895 0.43310 0.07180  0.02870  0.02189  197 SER A C   
1501 O O   . SER A 197 ? 0.44485 0.62956 0.43003 0.07408  0.02894  0.02319  197 SER A O   
1502 C CB  . SER A 197 ? 0.44897 0.63593 0.45306 0.08153  0.03948  0.01848  197 SER A CB  
1503 O OG  . SER A 197 ? 0.47705 0.66751 0.48653 0.08919  0.04175  0.01168  197 SER A OG  
1504 N N   . PRO A 198 ? 0.43037 0.60572 0.42973 0.06621  0.02810  0.02516  198 PRO A N   
1505 C CA  . PRO A 198 ? 0.43097 0.60821 0.42841 0.06476  0.03192  0.02970  198 PRO A CA  
1506 C C   . PRO A 198 ? 0.43524 0.61360 0.43326 0.06926  0.03998  0.03438  198 PRO A C   
1507 O O   . PRO A 198 ? 0.43455 0.61309 0.43841 0.06937  0.04399  0.03528  198 PRO A O   
1508 C CB  . PRO A 198 ? 0.42723 0.59626 0.42544 0.05863  0.02959  0.02963  198 PRO A CB  
1509 C CG  . PRO A 198 ? 0.42420 0.58723 0.42360 0.05595  0.02143  0.02707  198 PRO A CG  
1510 C CD  . PRO A 198 ? 0.42468 0.59236 0.43004 0.06245  0.02254  0.02405  198 PRO A CD  
1511 N N   . LEU A 199 ? 0.44210 0.62169 0.43608 0.07297  0.04261  0.03843  199 LEU A N   
1512 C CA  . LEU A 199 ? 0.45176 0.62655 0.44310 0.07750  0.04934  0.04548  199 LEU A CA  
1513 C C   . LEU A 199 ? 0.47183 0.63502 0.46537 0.07744  0.05158  0.04664  199 LEU A C   
1514 O O   . LEU A 199 ? 0.46797 0.63429 0.46161 0.07934  0.04981  0.04350  199 LEU A O   
1515 C CB  . LEU A 199 ? 0.44619 0.62831 0.42728 0.08570  0.04826  0.04988  199 LEU A CB  
1516 C CG  . LEU A 199 ? 0.43413 0.62407 0.40564 0.08748  0.04580  0.04649  199 LEU A CG  
1517 C CD1 . LEU A 199 ? 0.44259 0.63791 0.39910 0.09566  0.04215  0.05106  199 LEU A CD1 
1518 C CD2 . LEU A 199 ? 0.43021 0.61813 0.40217 0.08605  0.05447  0.04737  199 LEU A CD2 
1519 N N   . VAL A 200 ? 0.49370 0.64335 0.48950 0.07486  0.05621  0.05053  200 VAL A N   
1520 C CA  . VAL A 200 ? 0.51723 0.64843 0.51245 0.07481  0.05750  0.04944  200 VAL A CA  
1521 C C   . VAL A 200 ? 0.55051 0.66857 0.54144 0.08103  0.06240  0.05957  200 VAL A C   
1522 O O   . VAL A 200 ? 0.56091 0.67408 0.55350 0.07603  0.06694  0.06744  200 VAL A O   
1523 C CB  . VAL A 200 ? 0.51604 0.63664 0.51776 0.06371  0.05502  0.04441  200 VAL A CB  
1524 C CG1 . VAL A 200 ? 0.53348 0.62900 0.53035 0.06348  0.05521  0.04105  200 VAL A CG1 
1525 C CG2 . VAL A 200 ? 0.49971 0.63007 0.50152 0.05936  0.04822  0.03665  200 VAL A CG2 
1526 N N   . PHE A 201 ? 0.56928 0.68241 0.55561 0.09244  0.06207  0.06060  201 PHE A N   
1527 C CA  . PHE A 201 ? 0.59789 0.69567 0.57802 0.10127  0.06443  0.07210  201 PHE A CA  
1528 C C   . PHE A 201 ? 0.63249 0.69875 0.61209 0.10304  0.06616  0.07021  201 PHE A C   
1529 O O   . PHE A 201 ? 0.62986 0.69252 0.61067 0.10511  0.06533  0.05830  201 PHE A O   
1530 C CB  . PHE A 201 ? 0.59382 0.70779 0.57150 0.11611  0.06021  0.07554  201 PHE A CB  
1531 C CG  . PHE A 201 ? 0.57998 0.72070 0.55560 0.11409  0.05586  0.07511  201 PHE A CG  
1532 C CD1 . PHE A 201 ? 0.59583 0.73791 0.55803 0.11560  0.05587  0.08484  201 PHE A CD1 
1533 C CD2 . PHE A 201 ? 0.55919 0.72063 0.54320 0.11018  0.05201  0.06489  201 PHE A CD2 
1534 C CE1 . PHE A 201 ? 0.58833 0.75087 0.54438 0.11461  0.05092  0.08140  201 PHE A CE1 
1535 C CE2 . PHE A 201 ? 0.55467 0.73470 0.53607 0.10748  0.04637  0.06296  201 PHE A CE2 
1536 C CZ  . PHE A 201 ? 0.56677 0.74675 0.53352 0.11038  0.04522  0.06973  201 PHE A CZ  
1537 N N   . PRO A 202 ? 0.67065 0.71108 0.64595 0.10198  0.06898  0.08151  202 PRO A N   
1538 C CA  . PRO A 202 ? 0.71283 0.71565 0.68647 0.10307  0.06914  0.07873  202 PRO A CA  
1539 C C   . PRO A 202 ? 0.74475 0.73619 0.71324 0.12487  0.06777  0.08069  202 PRO A C   
1540 O O   . PRO A 202 ? 0.73831 0.75393 0.70710 0.13771  0.06556  0.08570  202 PRO A O   
1541 C CB  . PRO A 202 ? 0.73452 0.71535 0.70801 0.09026  0.07305  0.09307  202 PRO A CB  
1542 C CG  . PRO A 202 ? 0.72414 0.72649 0.69046 0.09454  0.07635  0.10801  202 PRO A CG  
1543 C CD  . PRO A 202 ? 0.68169 0.72343 0.65120 0.09792  0.07313  0.09758  202 PRO A CD  
1544 N N   . LYS A 203 ? 0.78769 0.74139 0.75284 0.12948  0.06781  0.07556  203 LYS A N   
1545 C CA  . LYS A 203 ? 0.82532 0.76230 0.78766 0.15295  0.06678  0.07757  203 LYS A CA  
1546 C C   . LYS A 203 ? 0.84975 0.78051 0.80611 0.16094  0.06452  0.10005  203 LYS A C   
1547 O O   . LYS A 203 ? 0.85667 0.77953 0.80681 0.14620  0.06657  0.11407  203 LYS A O   
1548 C CB  . LYS A 203 ? 0.86327 0.75098 0.81961 0.15519  0.06699  0.06753  203 LYS A CB  
1549 C CG  . LYS A 203 ? 0.88155 0.75963 0.83791 0.18211  0.06802  0.05756  203 LYS A CG  
1550 C CD  . LYS A 203 ? 0.92713 0.74893 0.87287 0.18348  0.06767  0.04530  203 LYS A CD  
1551 C CE  . LYS A 203 ? 0.95056 0.76302 0.89605 0.21343  0.07103  0.03215  203 LYS A CE  
1552 N NZ  . LYS A 203 ? 0.91499 0.77083 0.86440 0.21829  0.07807  0.01450  203 LYS A NZ  
1553 N N   . HIS A 204 ? 0.87086 0.80820 0.82916 0.18507  0.06044  0.10399  204 HIS A N   
1554 C CA  . HIS A 204 ? 0.90674 0.83877 0.85601 0.19788  0.05475  0.12542  204 HIS A CA  
1555 C C   . HIS A 204 ? 0.86384 0.83364 0.80705 0.18994  0.05231  0.13512  204 HIS A C   
1556 O O   . HIS A 204 ? 0.88770 0.85132 0.81566 0.19715  0.04756  0.15409  204 HIS A O   
1557 C CB  . HIS A 204 ? 0.97952 0.85605 0.91371 0.19347  0.05601  0.14210  204 HIS A CB  
1558 C CG  . HIS A 204 ? 1.03307 0.86208 0.96931 0.20100  0.05660  0.13207  204 HIS A CG  
1559 N ND1 . HIS A 204 ? 1.06069 0.88041 1.00274 0.22975  0.05256  0.12585  204 HIS A ND1 
1560 C CD2 . HIS A 204 ? 1.06125 0.84848 0.99475 0.18400  0.05999  0.12583  204 HIS A CD2 
1561 C CE1 . HIS A 204 ? 1.09935 0.87015 1.03835 0.23147  0.05446  0.11489  204 HIS A CE1 
1562 N NE2 . HIS A 204 ? 1.10070 0.84978 1.03371 0.20269  0.05774  0.11456  204 HIS A NE2 
1563 N N   . HIS A 205 ? 0.79574 0.80077 0.74677 0.17607  0.05479  0.12275  205 HIS A N   
1564 C CA  . HIS A 205 ? 0.75481 0.79545 0.70026 0.17205  0.05099  0.12713  205 HIS A CA  
1565 C C   . HIS A 205 ? 0.73846 0.81734 0.69911 0.18505  0.04266  0.11804  205 HIS A C   
1566 O O   . HIS A 205 ? 0.73297 0.82374 0.71118 0.18626  0.04548  0.10323  205 HIS A O   
1567 C CB  . HIS A 205 ? 0.70603 0.76006 0.65237 0.15003  0.05762  0.11962  205 HIS A CB  
1568 C CG  . HIS A 205 ? 0.72806 0.76141 0.66196 0.13646  0.06560  0.13251  205 HIS A CG  
1569 N ND1 . HIS A 205 ? 0.71151 0.76328 0.64440 0.12167  0.07147  0.13073  205 HIS A ND1 
1570 C CD2 . HIS A 205 ? 0.77071 0.76736 0.69478 0.13511  0.06986  0.14810  205 HIS A CD2 
1571 C CE1 . HIS A 205 ? 0.73624 0.76900 0.66161 0.11154  0.08062  0.14462  205 HIS A CE1 
1572 N NE2 . HIS A 205 ? 0.77191 0.76971 0.69113 0.11778  0.07965  0.15622  205 HIS A NE2 
1573 N N   . VAL A 206 ? 0.74308 0.84203 0.69650 0.19384  0.03235  0.12713  206 VAL A N   
1574 C CA  . VAL A 206 ? 0.71473 0.85325 0.68702 0.20475  0.02178  0.12036  206 VAL A CA  
1575 C C   . VAL A 206 ? 0.67608 0.84461 0.64396 0.19098  0.01682  0.11466  206 VAL A C   
1576 O O   . VAL A 206 ? 0.68406 0.85007 0.62779 0.18905  0.01170  0.12362  206 VAL A O   
1577 C CB  . VAL A 206 ? 0.74362 0.88240 0.71458 0.22808  0.00860  0.13382  206 VAL A CB  
1578 C CG1 . VAL A 206 ? 0.72175 0.90909 0.71905 0.23691  -0.00393 0.12648  206 VAL A CG1 
1579 C CG2 . VAL A 206 ? 0.77155 0.87537 0.74765 0.24413  0.01326  0.13796  206 VAL A CG2 
1580 N N   . VAL A 207 ? 0.63978 0.83345 0.62784 0.18157  0.01887  0.09980  207 VAL A N   
1581 C CA  . VAL A 207 ? 0.61278 0.83311 0.60100 0.16963  0.01199  0.09252  207 VAL A CA  
1582 C C   . VAL A 207 ? 0.61111 0.86776 0.62123 0.17857  -0.00208 0.09052  207 VAL A C   
1583 O O   . VAL A 207 ? 0.60388 0.87859 0.64253 0.18393  0.00108  0.08535  207 VAL A O   
1584 C CB  . VAL A 207 ? 0.58015 0.80282 0.57690 0.15239  0.02133  0.07989  207 VAL A CB  
1585 C CG1 . VAL A 207 ? 0.56447 0.81137 0.56451 0.14151  0.01254  0.07208  207 VAL A CG1 
1586 C CG2 . VAL A 207 ? 0.58338 0.77672 0.56316 0.14300  0.03198  0.08170  207 VAL A CG2 
1587 N N   . SER A 208 ? 0.61667 0.88605 0.61392 0.18001  -0.01750 0.09395  208 SER A N   
1588 C CA  . SER A 208 ? 0.62258 0.92859 0.64169 0.18770  -0.03544 0.09291  208 SER A CA  
1589 C C   . SER A 208 ? 0.60821 0.93523 0.62845 0.17075  -0.04588 0.08179  208 SER A C   
1590 O O   . SER A 208 ? 0.61985 0.93012 0.60838 0.16270  -0.04751 0.07972  208 SER A O   
1591 C CB  . SER A 208 ? 0.66824 0.96939 0.66925 0.20637  -0.05069 0.10706  208 SER A CB  
1592 O OG  . SER A 208 ? 0.68314 1.02417 0.70928 0.21359  -0.07130 0.10537  208 SER A OG  
1593 N N   . LEU A 209 ? 0.58816 0.95114 0.64555 0.16529  -0.05206 0.07443  209 LEU A N   
1594 C CA  . LEU A 209 ? 0.57637 0.95814 0.63971 0.14774  -0.06465 0.06399  209 LEU A CA  
1595 C C   . LEU A 209 ? 0.60634 1.02138 0.68455 0.15472  -0.09017 0.06541  209 LEU A C   
1596 O O   . LEU A 209 ? 0.60498 1.04994 0.71845 0.16709  -0.09407 0.07032  209 LEU A O   
1597 C CB  . LEU A 209 ? 0.54107 0.93864 0.63623 0.13136  -0.05338 0.05604  209 LEU A CB  
1598 C CG  . LEU A 209 ? 0.51205 0.88152 0.59666 0.12444  -0.03076 0.05421  209 LEU A CG  
1599 C CD1 . LEU A 209 ? 0.48958 0.87613 0.60021 0.10721  -0.02360 0.04814  209 LEU A CD1 
1600 C CD2 . LEU A 209 ? 0.51050 0.84420 0.55629 0.11882  -0.02826 0.05215  209 LEU A CD2 
1601 N N   . GLN A 210 ? 0.63553 1.04593 0.68678 0.14806  -0.10827 0.06013  210 GLN A N   
1602 C CA  . GLN A 210 ? 0.68009 1.11813 0.73698 0.15425  -0.13708 0.06065  210 GLN A CA  
1603 C C   . GLN A 210 ? 0.69957 1.15249 0.76517 0.13235  -0.15386 0.04548  210 GLN A C   
1604 O O   . GLN A 210 ? 0.71893 1.14259 0.75135 0.12012  -0.15086 0.03574  210 GLN A O   
1605 C CB  . GLN A 210 ? 0.71071 1.12314 0.71524 0.17048  -0.14677 0.06993  210 GLN A CB  
1606 C CG  . GLN A 210 ? 0.70265 1.09390 0.69833 0.19022  -0.13073 0.08670  210 GLN A CG  
1607 C CD  . GLN A 210 ? 0.73303 1.09530 0.67426 0.20401  -0.13709 0.09960  210 GLN A CD  
1608 O OE1 . GLN A 210 ? 0.76073 1.12416 0.66958 0.20289  -0.15659 0.09635  210 GLN A OE1 
1609 N NE2 . GLN A 210 ? 0.73302 1.06685 0.66133 0.21641  -0.12056 0.11454  210 GLN A NE2 
1610 N N   . PRO A 211 ? 0.71495 1.21256 0.82690 0.12640  -0.17178 0.04249  211 PRO A N   
1611 C CA  . PRO A 211 ? 0.72323 1.23320 0.84863 0.10168  -0.18852 0.02805  211 PRO A CA  
1612 C C   . PRO A 211 ? 0.77336 1.26479 0.85122 0.10102  -0.21472 0.01890  211 PRO A C   
1613 O O   . PRO A 211 ? 0.80345 1.28915 0.84843 0.12027  -0.22690 0.02588  211 PRO A O   
1614 C CB  . PRO A 211 ? 0.70660 1.27577 0.89857 0.09813  -0.20153 0.03031  211 PRO A CB  
1615 C CG  . PRO A 211 ? 0.68729 1.27193 0.90240 0.12163  -0.18374 0.04430  211 PRO A CG  
1616 C CD  . PRO A 211 ? 0.70529 1.24547 0.86379 0.14231  -0.17726 0.05223  211 PRO A CD  
1617 N N   . VAL A 212 ? 0.79173 1.27096 0.86343 0.07856  -0.22362 0.00294  212 VAL A N   
1618 C CA  . VAL A 212 ? 0.86942 1.32810 0.89432 0.07550  -0.24874 -0.01093 212 VAL A CA  
1619 C C   . VAL A 212 ? 0.90461 1.40157 0.96536 0.06095  -0.28388 -0.01984 212 VAL A C   
1620 O O   . VAL A 212 ? 0.96919 1.48166 1.01491 0.07180  -0.31207 -0.01978 212 VAL A O   
1621 C CB  . VAL A 212 ? 0.89596 1.30823 0.88532 0.06285  -0.23612 -0.02521 212 VAL A CB  
1622 C CG1 . VAL A 212 ? 0.96456 1.35620 0.90881 0.05816  -0.26312 -0.04410 212 VAL A CG1 
1623 C CG2 . VAL A 212 ? 0.89876 1.27848 0.85286 0.07850  -0.20512 -0.01631 212 VAL A CG2 
1624 N N   . ASN A 213 ? 0.87158 1.38424 0.98011 0.03531  -0.28335 -0.02647 213 ASN A N   
1625 C CA  . ASN A 213 ? 0.90068 1.45406 1.05466 0.01607  -0.31539 -0.03435 213 ASN A CA  
1626 C C   . ASN A 213 ? 0.85272 1.45865 1.08541 0.00665  -0.30345 -0.02281 213 ASN A C   
1627 O O   . ASN A 213 ? 0.85569 1.51068 1.12662 0.02066  -0.31297 -0.01268 213 ASN A O   
1628 C CB  . ASN A 213 ? 0.95104 1.47058 1.08484 -0.01026 -0.33079 -0.05550 213 ASN A CB  
1629 C CG  . ASN A 213 ? 1.02221 1.49764 1.07867 0.00083  -0.34764 -0.07042 213 ASN A CG  
1630 O OD1 . ASN A 213 ? 1.07738 1.56353 1.10580 0.02002  -0.36607 -0.06762 213 ASN A OD1 
1631 N ND2 . ASN A 213 ? 1.03725 1.46186 1.05670 -0.00966 -0.34065 -0.08596 213 ASN A ND2 
1632 N N   . ASP A 214 ? 0.79962 1.39894 1.05922 -0.01558 -0.28194 -0.02304 214 ASP A N   
1633 C CA  . ASP A 214 ? 0.73914 1.38871 1.06968 -0.02488 -0.26537 -0.01135 214 ASP A CA  
1634 C C   . ASP A 214 ? 0.69261 1.35843 1.02947 0.00544  -0.24087 0.00413  214 ASP A C   
1635 O O   . ASP A 214 ? 0.68791 1.31132 0.97876 0.02156  -0.21936 0.00775  214 ASP A O   
1636 C CB  . ASP A 214 ? 0.71383 1.33974 1.05367 -0.05147 -0.24303 -0.01212 214 ASP A CB  
1637 C CG  . ASP A 214 ? 0.70075 1.37945 1.11116 -0.06507 -0.22428 -0.00002 214 ASP A CG  
1638 O OD1 . ASP A 214 ? 0.70147 1.44125 1.16304 -0.05711 -0.23226 0.00600  214 ASP A OD1 
1639 O OD2 . ASP A 214 ? 0.70019 1.36023 1.11466 -0.08301 -0.20090 0.00405  214 ASP A OD2 
1640 N N   . LYS A 215 ? 0.66709 1.39460 1.06330 0.01343  -0.24482 0.01256  215 LYS A N   
1641 C CA  . LYS A 215 ? 0.61583 1.35911 1.02191 0.04426  -0.22431 0.02560  215 LYS A CA  
1642 C C   . LYS A 215 ? 0.56752 1.33960 1.02192 0.03881  -0.19056 0.03302  215 LYS A C   
1643 O O   . LYS A 215 ? 0.55074 1.33610 1.01668 0.06431  -0.17163 0.04166  215 LYS A O   
1644 C CB  . LYS A 215 ? 0.62122 1.41072 1.05458 0.06596  -0.25226 0.03018  215 LYS A CB  
1645 C CG  . LYS A 215 ? 0.64854 1.40868 1.02570 0.07394  -0.28589 0.02427  215 LYS A CG  
1646 C CD  . LYS A 215 ? 0.66641 1.47365 1.07063 0.09445  -0.31830 0.02990  215 LYS A CD  
1647 C CE  . LYS A 215 ? 0.72117 1.49565 1.05981 0.10143  -0.35183 0.02421  215 LYS A CE  
1648 N NZ  . LYS A 215 ? 0.76018 1.57568 1.12091 0.12033  -0.38732 0.03042  215 LYS A NZ  
1649 N N   . ASP A 216 ? 0.54434 1.32335 1.02392 0.00671  -0.18219 0.03001  216 ASP A N   
1650 C CA  . ASP A 216 ? 0.52948 1.33601 1.04997 -0.00111 -0.14888 0.03787  216 ASP A CA  
1651 C C   . ASP A 216 ? 0.53000 1.27723 1.00145 -0.00784 -0.12127 0.03840  216 ASP A C   
1652 O O   . ASP A 216 ? 0.56035 1.26214 0.99572 -0.02680 -0.12958 0.03176  216 ASP A O   
1653 C CB  . ASP A 216 ? 0.52971 1.38806 1.11509 -0.03405 -0.15615 0.03803  216 ASP A CB  
1654 C CG  . ASP A 216 ? 0.54381 1.46564 1.18340 -0.02952 -0.18737 0.03669  216 ASP A CG  
1655 O OD1 . ASP A 216 ? 0.54424 1.48591 1.18775 0.00427  -0.19254 0.04019  216 ASP A OD1 
1656 O OD2 . ASP A 216 ? 0.56261 1.51294 1.24123 -0.05998 -0.20852 0.03241  216 ASP A OD2 
1657 N N   . PHE A 217 ? 0.51263 1.25985 0.98269 0.00910  -0.08996 0.04528  217 PHE A N   
1658 C CA  . PHE A 217 ? 0.50000 1.19480 0.92461 0.00612  -0.06497 0.04632  217 PHE A CA  
1659 C C   . PHE A 217 ? 0.47362 1.19540 0.92584 0.00607  -0.03165 0.05358  217 PHE A C   
1660 O O   . PHE A 217 ? 0.47001 1.24180 0.96459 0.02236  -0.02313 0.05691  217 PHE A O   
1661 C CB  . PHE A 217 ? 0.51386 1.16088 0.88357 0.03277  -0.06321 0.04476  217 PHE A CB  
1662 C CG  . PHE A 217 ? 0.54427 1.16778 0.88241 0.03718  -0.09213 0.03875  217 PHE A CG  
1663 C CD1 . PHE A 217 ? 0.56106 1.13678 0.85650 0.02275  -0.09954 0.03166  217 PHE A CD1 
1664 C CD2 . PHE A 217 ? 0.55971 1.20866 0.90894 0.05728  -0.11202 0.04016  217 PHE A CD2 
1665 C CE1 . PHE A 217 ? 0.59191 1.14613 0.85362 0.02806  -0.12374 0.02468  217 PHE A CE1 
1666 C CE2 . PHE A 217 ? 0.59162 1.21778 0.90453 0.06152  -0.13818 0.03513  217 PHE A CE2 
1667 C CZ  . PHE A 217 ? 0.60921 1.18834 0.87711 0.04669  -0.14281 0.02667  217 PHE A CZ  
1668 N N   . GLN A 218 ? 0.46247 1.15046 0.88866 -0.01098 -0.01307 0.05582  218 GLN A N   
1669 C CA  . GLN A 218 ? 0.45808 1.15909 0.89249 -0.01081 0.02049  0.06229  218 GLN A CA  
1670 C C   . GLN A 218 ? 0.46151 1.11650 0.84504 0.01340  0.03465  0.05980  218 GLN A C   
1671 O O   . GLN A 218 ? 0.47019 1.07095 0.80623 0.00783  0.03189  0.05773  218 GLN A O   
1672 C CB  . GLN A 218 ? 0.46543 1.15442 0.89793 -0.04488 0.03006  0.06826  218 GLN A CB  
1673 C CG  . GLN A 218 ? 0.47003 1.18721 0.91997 -0.04999 0.06408  0.07709  218 GLN A CG  
1674 C CD  . GLN A 218 ? 0.46357 1.25861 0.98547 -0.05639 0.07013  0.08181  218 GLN A CD  
1675 O OE1 . GLN A 218 ? 0.46182 1.28495 1.02318 -0.07528 0.04786  0.08181  218 GLN A OE1 
1676 N NE2 . GLN A 218 ? 0.45977 1.29156 1.00047 -0.04038 0.10010  0.08475  218 GLN A NE2 
1677 N N   . ILE A 219 ? 0.46235 1.13868 0.85804 0.04070  0.04832  0.05929  219 ILE A N   
1678 C CA  . ILE A 219 ? 0.47062 1.10407 0.82248 0.06381  0.05983  0.05593  219 ILE A CA  
1679 C C   . ILE A 219 ? 0.47804 1.11778 0.82703 0.06618  0.09188  0.05682  219 ILE A C   
1680 O O   . ILE A 219 ? 0.48609 1.17805 0.87785 0.06849  0.10743  0.05904  219 ILE A O   
1681 C CB  . ILE A 219 ? 0.46317 1.10314 0.82192 0.09528  0.04933  0.05379  219 ILE A CB  
1682 C CG1 . ILE A 219 ? 0.45515 1.09190 0.81260 0.09316  0.01716  0.05371  219 ILE A CG1 
1683 C CG2 . ILE A 219 ? 0.46309 1.05261 0.77624 0.11489  0.06000  0.05063  219 ILE A CG2 
1684 C CD1 . ILE A 219 ? 0.45428 1.10904 0.82751 0.12237  0.00389  0.05521  219 ILE A CD1 
1685 N N   . SER A 220 ? 0.48386 1.07268 0.78253 0.06615  0.10183  0.05463  220 SER A N   
1686 C CA  . SER A 220 ? 0.50556 1.09238 0.78920 0.06811  0.13031  0.05414  220 SER A CA  
1687 C C   . SER A 220 ? 0.51833 1.06284 0.76219 0.09163  0.13614  0.04615  220 SER A C   
1688 O O   . SER A 220 ? 0.52251 1.02242 0.73424 0.09308  0.12095  0.04406  220 SER A O   
1689 C CB  . SER A 220 ? 0.52164 1.08665 0.77996 0.03971  0.13643  0.06033  220 SER A CB  
1690 O OG  . SER A 220 ? 0.53203 1.03864 0.74163 0.03862  0.12532  0.05746  220 SER A OG  
1691 N N   . VAL A 221 ? 0.52823 1.08679 0.77474 0.10921  0.15904  0.04109  221 VAL A N   
1692 C CA  . VAL A 221 ? 0.56494 1.08126 0.77302 0.12986  0.16631  0.03154  221 VAL A CA  
1693 C C   . VAL A 221 ? 0.61645 1.12613 0.79613 0.12496  0.19176  0.02809  221 VAL A C   
1694 O O   . VAL A 221 ? 0.64926 1.19793 0.85018 0.13385  0.21467  0.02603  221 VAL A O   
1695 C CB  . VAL A 221 ? 0.58216 1.11297 0.81430 0.16216  0.16748  0.02554  221 VAL A CB  
1696 C CG1 . VAL A 221 ? 0.61327 1.09842 0.80616 0.18190  0.17770  0.01408  221 VAL A CG1 
1697 C CG2 . VAL A 221 ? 0.57434 1.10244 0.82219 0.16748  0.13996  0.03055  221 VAL A CG2 
1698 N N   . ASP A 222 ? 0.63765 1.10028 0.76926 0.11165  0.18787  0.02763  222 ASP A N   
1699 C CA  . ASP A 222 ? 0.68434 1.13304 0.77784 0.10547  0.20776  0.02526  222 ASP A CA  
1700 C C   . ASP A 222 ? 0.70281 1.19716 0.81984 0.08715  0.22479  0.03639  222 ASP A C   
1701 O O   . ASP A 222 ? 0.69551 1.19228 0.82131 0.06237  0.21296  0.04821  222 ASP A O   
1702 C CB  . ASP A 222 ? 0.70007 1.13509 0.77349 0.13242  0.22363  0.01003  222 ASP A CB  
1703 C CG  . ASP A 222 ? 0.68543 1.07114 0.73690 0.14628  0.20578  0.00081  222 ASP A CG  
1704 O OD1 . ASP A 222 ? 0.66053 1.01689 0.69857 0.13256  0.18489  0.00570  222 ASP A OD1 
1705 O OD2 . ASP A 222 ? 0.70234 1.07817 0.75069 0.17112  0.21380  -0.01142 222 ASP A OD2 
1706 N N   . HIS A 223 ? 0.73992 1.27005 0.86807 0.09752  0.25304  0.03332  223 HIS A N   
1707 C CA  . HIS A 223 ? 0.77373 1.35290 0.92934 0.07841  0.27254  0.04582  223 HIS A CA  
1708 C C   . HIS A 223 ? 0.73602 1.36544 0.95940 0.07052  0.26063  0.05379  223 HIS A C   
1709 O O   . HIS A 223 ? 0.72953 1.36548 0.96710 0.04215  0.24978  0.06648  223 HIS A O   
1710 C CB  . HIS A 223 ? 0.83534 1.44557 0.98876 0.09522  0.30875  0.03901  223 HIS A CB  
1711 C CG  . HIS A 223 ? 0.89510 1.47385 0.98437 0.08697  0.32687  0.03931  223 HIS A CG  
1712 N ND1 . HIS A 223 ? 0.91002 1.47827 0.97655 0.05573  0.32725  0.05621  223 HIS A ND1 
1713 C CD2 . HIS A 223 ? 0.93970 1.49354 0.97999 0.10642  0.34426  0.02472  223 HIS A CD2 
1714 C CE1 . HIS A 223 ? 0.95484 1.49441 0.95968 0.05661  0.34346  0.05353  223 HIS A CE1 
1715 N NE2 . HIS A 223 ? 0.97300 1.50387 0.96002 0.08676  0.35388  0.03335  223 HIS A NE2 
1716 N N   . LEU A 224 ? 0.71571 1.37844 0.98065 0.09591  0.26021  0.04602  224 LEU A N   
1717 C CA  . LEU A 224 ? 0.69335 1.41830 1.02838 0.09075  0.25378  0.05294  224 LEU A CA  
1718 C C   . LEU A 224 ? 0.66248 1.37058 1.00740 0.07533  0.21759  0.05799  224 LEU A C   
1719 O O   . LEU A 224 ? 0.65869 1.31749 0.97093 0.08439  0.19695  0.05252  224 LEU A O   
1720 C CB  . LEU A 224 ? 0.69759 1.46051 1.07298 0.12599  0.26091  0.04316  224 LEU A CB  
1721 C CG  . LEU A 224 ? 0.71332 1.43661 1.07082 0.15641  0.24237  0.03238  224 LEU A CG  
1722 C CD1 . LEU A 224 ? 0.72125 1.48739 1.13609 0.18114  0.23596  0.02920  224 LEU A CD1 
1723 C CD2 . LEU A 224 ? 0.75330 1.42710 1.05426 0.17528  0.25915  0.01950  224 LEU A CD2 
1724 N N   . SER A 225 ? 0.64815 1.39832 1.03856 0.05097  0.21092  0.06810  225 SER A N   
1725 C CA  . SER A 225 ? 0.58973 1.33136 0.99417 0.03511  0.17714  0.07123  225 SER A CA  
1726 C C   . SER A 225 ? 0.55906 1.37265 1.03781 0.03219  0.17058  0.07457  225 SER A C   
1727 O O   . SER A 225 ? 0.55624 1.41583 1.07305 0.01027  0.18559  0.08330  225 SER A O   
1728 C CB  . SER A 225 ? 0.58093 1.28716 0.95678 0.00064  0.17064  0.07982  225 SER A CB  
1729 O OG  . SER A 225 ? 0.56049 1.26587 0.95637 -0.01563 0.14022  0.08111  225 SER A OG  
1730 N N   . ILE A 226 ? 0.53059 1.35505 1.03064 0.05345  0.14780  0.06882  226 ILE A N   
1731 C CA  . ILE A 226 ? 0.53802 1.43252 1.10994 0.05569  0.13658  0.07083  226 ILE A CA  
1732 C C   . ILE A 226 ? 0.54549 1.42593 1.11928 0.04471  0.09632  0.07019  226 ILE A C   
1733 O O   . ILE A 226 ? 0.55023 1.37304 1.07378 0.05361  0.07933  0.06569  226 ILE A O   
1734 C CB  . ILE A 226 ? 0.54418 1.46944 1.14232 0.09667  0.14530  0.06453  226 ILE A CB  
1735 C CG1 . ILE A 226 ? 0.54056 1.40276 1.08476 0.12426  0.13318  0.05743  226 ILE A CG1 
1736 C CG2 . ILE A 226 ? 0.58606 1.51885 1.18436 0.10289  0.18329  0.06110  226 ILE A CG2 
1737 C CD1 . ILE A 226 ? 0.55492 1.43060 1.11587 0.16529  0.14067  0.05107  226 ILE A CD1 
1738 N N   . LEU A 227 ? 0.56218 1.49622 1.19360 0.02457  0.08151  0.07420  227 LEU A N   
1739 C CA  . LEU A 227 ? 0.56224 1.48827 1.19738 0.01409  0.04148  0.07146  227 LEU A CA  
1740 C C   . LEU A 227 ? 0.56211 1.51563 1.22117 0.04745  0.02134  0.06769  227 LEU A C   
1741 O O   . LEU A 227 ? 0.55074 1.56737 1.26867 0.06174  0.02853  0.06926  227 LEU A O   
1742 C CB  . LEU A 227 ? 0.55894 1.52782 1.24536 -0.02416 0.03114  0.07636  227 LEU A CB  
1743 C CG  . LEU A 227 ? 0.54726 1.52430 1.25140 -0.03465 -0.01245 0.07125  227 LEU A CG  
1744 C CD1 . LEU A 227 ? 0.54885 1.44650 1.18256 -0.04248 -0.03295 0.06476  227 LEU A CD1 
1745 C CD2 . LEU A 227 ? 0.54910 1.58332 1.32052 -0.07103 -0.02055 0.07585  227 LEU A CD2 
1746 N N   . HIS A 228 ? 0.58352 1.48726 1.19554 0.06051  -0.00321 0.06333  228 HIS A N   
1747 C CA  . HIS A 228 ? 0.60739 1.52696 1.23147 0.09125  -0.02611 0.06226  228 HIS A CA  
1748 C C   . HIS A 228 ? 0.61733 1.55298 1.25676 0.07584  -0.06644 0.06033  228 HIS A C   
1749 O O   . HIS A 228 ? 0.61604 1.51269 1.22066 0.05056  -0.08030 0.05654  228 HIS A O   
1750 C CB  . HIS A 228 ? 0.63330 1.48639 1.19183 0.11756  -0.02484 0.06065  228 HIS A CB  
1751 C CG  . HIS A 228 ? 0.65063 1.48966 1.19688 0.13832  0.00915  0.06024  228 HIS A CG  
1752 N ND1 . HIS A 228 ? 0.66525 1.51123 1.22096 0.17564  0.01314  0.06046  228 HIS A ND1 
1753 C CD2 . HIS A 228 ? 0.65203 1.46798 1.17483 0.12753  0.03924  0.05882  228 HIS A CD2 
1754 C CE1 . HIS A 228 ? 0.66942 1.49576 1.20755 0.18649  0.04457  0.05714  228 HIS A CE1 
1755 N NE2 . HIS A 228 ? 0.66022 1.46947 1.17699 0.15760  0.06051  0.05620  228 HIS A NE2 
1756 N N   . ARG A 229 ? 0.63167 1.62440 1.32293 0.09248  -0.08636 0.06196  229 ARG A N   
1757 C CA  . ARG A 229 ? 0.65557 1.67346 1.36820 0.07904  -0.12766 0.05926  229 ARG A CA  
1758 C C   . ARG A 229 ? 0.67562 1.66998 1.35448 0.11060  -0.15571 0.05969  229 ARG A C   
1759 O O   . ARG A 229 ? 0.68907 1.67675 1.36589 0.14458  -0.14552 0.06381  229 ARG A O   
1760 C CB  . ARG A 229 ? 0.68059 1.75722 1.46999 0.06714  -0.13048 0.05863  229 ARG A CB  
1761 C CG  . ARG A 229 ? 0.70824 1.80306 1.52103 0.03513  -0.16675 0.05337  229 ARG A CG  
1762 C CD  . ARG A 229 ? 0.70746 1.80175 1.52842 -0.00848 -0.15356 0.05321  229 ARG A CD  
1763 N NE  . ARG A 229 ? 0.71287 1.85035 1.59373 -0.02050 -0.12280 0.05779  229 ARG A NE  
1764 C CZ  . ARG A 229 ? 0.71732 1.86155 1.61755 -0.05906 -0.10801 0.06073  229 ARG A CZ  
1765 N NH1 . ARG A 229 ? 0.71827 1.82698 1.58532 -0.09015 -0.12204 0.05922  229 ARG A NH1 
1766 N NH2 . ARG A 229 ? 0.72485 1.90970 1.67733 -0.06653 -0.07817 0.06546  229 ARG A NH2 
1767 N N   . ASP A 230 ? 0.68475 1.65490 1.32994 0.09805  -0.18994 0.05474  230 ASP A N   
1768 C CA  . ASP A 230 ? 0.70239 1.65171 1.31000 0.12387  -0.22028 0.05649  230 ASP A CA  
1769 C C   . ASP A 230 ? 0.69774 1.58858 1.24697 0.15337  -0.19946 0.06253  230 ASP A C   
1770 O O   . ASP A 230 ? 0.71828 1.61799 1.27480 0.18730  -0.20151 0.07050  230 ASP A O   
1771 C CB  . ASP A 230 ? 0.72752 1.71811 1.38669 0.13860  -0.24225 0.05885  230 ASP A CB  
1772 C CG  . ASP A 230 ? 0.76118 1.72396 1.37650 0.16112  -0.27662 0.06215  230 ASP A CG  
1773 O OD1 . ASP A 230 ? 0.77688 1.71538 1.34769 0.14663  -0.30305 0.05622  230 ASP A OD1 
1774 O OD2 . ASP A 230 ? 0.77690 1.73892 1.39916 0.19330  -0.27673 0.07063  230 ASP A OD2 
1775 N N   . VAL A 231 ? 0.67256 1.50205 1.16520 0.13940  -0.18039 0.05882  231 VAL A N   
1776 C CA  . VAL A 231 ? 0.66274 1.43486 1.10182 0.16015  -0.15875 0.06358  231 VAL A CA  
1777 C C   . VAL A 231 ? 0.68138 1.40900 1.05869 0.17145  -0.18171 0.06607  231 VAL A C   
1778 O O   . VAL A 231 ? 0.69574 1.40621 1.04306 0.15254  -0.20063 0.05892  231 VAL A O   
1779 C CB  . VAL A 231 ? 0.64274 1.37527 1.05482 0.13982  -0.12816 0.05897  231 VAL A CB  
1780 C CG1 . VAL A 231 ? 0.64265 1.32012 1.00566 0.15956  -0.10756 0.06322  231 VAL A CG1 
1781 C CG2 . VAL A 231 ? 0.62446 1.40119 1.09203 0.12635  -0.10532 0.05801  231 VAL A CG2 
1782 N N   . GLN A 232 ? 0.68625 1.39266 1.04214 0.20245  -0.17921 0.07628  232 GLN A N   
1783 C CA  . GLN A 232 ? 0.69389 1.35475 0.98643 0.21436  -0.19567 0.08238  232 GLN A CA  
1784 C C   . GLN A 232 ? 0.67605 1.27215 0.91209 0.21461  -0.16970 0.08481  232 GLN A C   
1785 O O   . GLN A 232 ? 0.69668 1.25342 0.87636 0.21068  -0.17707 0.08561  232 GLN A O   
1786 C CB  . GLN A 232 ? 0.72238 1.39856 1.02478 0.24820  -0.21459 0.09558  232 GLN A CB  
1787 N N   . GLU A 233 ? 0.63654 1.22239 0.88643 0.21853  -0.13947 0.08516  233 GLU A N   
1788 C CA  . GLU A 233 ? 0.62355 1.15111 0.82563 0.21861  -0.11706 0.08751  233 GLU A CA  
1789 C C   . GLU A 233 ? 0.58679 1.11311 0.81111 0.21440  -0.08673 0.08231  233 GLU A C   
1790 O O   . GLU A 233 ? 0.58265 1.14466 0.85263 0.22594  -0.07967 0.08182  233 GLU A O   
1791 C CB  . GLU A 233 ? 0.66720 1.16145 0.83753 0.24527  -0.12133 0.10189  233 GLU A CB  
1792 C CG  . GLU A 233 ? 0.68351 1.11853 0.80247 0.24104  -0.10279 0.10556  233 GLU A CG  
1793 C CD  . GLU A 233 ? 0.72330 1.12311 0.81607 0.26524  -0.10371 0.12179  233 GLU A CD  
1794 O OE1 . GLU A 233 ? 0.74535 1.16477 0.86225 0.28870  -0.11696 0.12959  233 GLU A OE1 
1795 O OE2 . GLU A 233 ? 0.73436 1.08721 0.78463 0.26062  -0.09133 0.12750  233 GLU A OE2 
1796 N N   . ILE A 234 ? 0.56162 1.04816 0.75264 0.19895  -0.06920 0.07806  234 ILE A N   
1797 C CA  . ILE A 234 ? 0.53735 1.01054 0.73400 0.19543  -0.04178 0.07356  234 ILE A CA  
1798 C C   . ILE A 234 ? 0.55143 0.96878 0.70405 0.20228  -0.03102 0.07822  234 ILE A C   
1799 O O   . ILE A 234 ? 0.55821 0.94667 0.67461 0.19062  -0.03383 0.07880  234 ILE A O   
1800 C CB  . ILE A 234 ? 0.50821 0.98807 0.70993 0.16722  -0.03283 0.06436  234 ILE A CB  
1801 C CG1 . ILE A 234 ? 0.49104 1.02610 0.74045 0.15620  -0.04193 0.06105  234 ILE A CG1 
1802 C CG2 . ILE A 234 ? 0.50377 0.96387 0.70042 0.16451  -0.00639 0.06068  234 ILE A CG2 
1803 C CD1 . ILE A 234 ? 0.46955 1.00494 0.72054 0.12662  -0.03584 0.05455  234 ILE A CD1 
1804 N N   . ARG A 235 ? 0.55683 0.95918 0.71398 0.22086  -0.01841 0.08086  235 ARG A N   
1805 C CA  . ARG A 235 ? 0.56534 0.91416 0.68590 0.22636  -0.00935 0.08597  235 ARG A CA  
1806 C C   . ARG A 235 ? 0.54641 0.87592 0.66479 0.21864  0.01283  0.07659  235 ARG A C   
1807 O O   . ARG A 235 ? 0.54531 0.89551 0.69004 0.22585  0.02373  0.06965  235 ARG A O   
1808 C CB  . ARG A 235 ? 0.59820 0.93214 0.71808 0.25437  -0.01593 0.09707  235 ARG A CB  
1809 C CG  . ARG A 235 ? 0.61672 0.97315 0.73945 0.26562  -0.04070 0.10729  235 ARG A CG  
1810 C CD  . ARG A 235 ? 0.65743 0.97046 0.74440 0.28099  -0.04794 0.12374  235 ARG A CD  
1811 N NE  . ARG A 235 ? 0.67885 0.95808 0.76774 0.29892  -0.03543 0.12681  235 ARG A NE  
1812 C CZ  . ARG A 235 ? 0.71932 0.95063 0.77817 0.31036  -0.03713 0.14162  235 ARG A CZ  
1813 N NH1 . ARG A 235 ? 0.74112 0.95502 0.76359 0.30646  -0.04871 0.15642  235 ARG A NH1 
1814 N NH2 . ARG A 235 ? 0.74304 0.94072 0.80608 0.32564  -0.02635 0.14157  235 ARG A NH2 
1815 N N   . TYR A 236 ? 0.53504 0.82702 0.62179 0.20460  0.01929  0.07620  236 TYR A N   
1816 C CA  . TYR A 236 ? 0.53297 0.80040 0.61089 0.19671  0.03613  0.06792  236 TYR A CA  
1817 C C   . TYR A 236 ? 0.56243 0.78115 0.61557 0.20282  0.03966  0.07358  236 TYR A C   
1818 O O   . TYR A 236 ? 0.56378 0.76411 0.59678 0.19985  0.03288  0.08385  236 TYR A O   
1819 C CB  . TYR A 236 ? 0.50278 0.77078 0.57037 0.17207  0.03901  0.06194  236 TYR A CB  
1820 C CG  . TYR A 236 ? 0.48482 0.79262 0.57521 0.16154  0.03778  0.05647  236 TYR A CG  
1821 C CD1 . TYR A 236 ? 0.48752 0.81619 0.59862 0.16410  0.04974  0.05040  236 TYR A CD1 
1822 C CD2 . TYR A 236 ? 0.47596 0.79853 0.56576 0.14809  0.02571  0.05711  236 TYR A CD2 
1823 C CE1 . TYR A 236 ? 0.47514 0.84024 0.60854 0.15156  0.05045  0.04787  236 TYR A CE1 
1824 C CE2 . TYR A 236 ? 0.46532 0.82024 0.57737 0.13549  0.02379  0.05288  236 TYR A CE2 
1825 C CZ  . TYR A 236 ? 0.46833 0.84523 0.60340 0.13619  0.03662  0.04964  236 TYR A CZ  
1826 O OH  . TYR A 236 ? 0.47223 0.88178 0.63108 0.12108  0.03669  0.04789  236 TYR A OH  
1827 N N   . GLU A 237 ? 0.58787 0.78475 0.64106 0.21013  0.05096  0.06654  237 GLU A N   
1828 C CA  . GLU A 237 ? 0.61217 0.75866 0.64379 0.21166  0.05417  0.07003  237 GLU A CA  
1829 C C   . GLU A 237 ? 0.61971 0.74671 0.64895 0.21202  0.06634  0.05541  237 GLU A C   
1830 O O   . GLU A 237 ? 0.61458 0.76634 0.65896 0.21990  0.07364  0.04512  237 GLU A O   
1831 C CB  . GLU A 237 ? 0.64095 0.76819 0.67091 0.23344  0.04675  0.08291  237 GLU A CB  
1832 C CG  . GLU A 237 ? 0.65081 0.80355 0.70715 0.25857  0.04537  0.07968  237 GLU A CG  
1833 C CD  . GLU A 237 ? 0.69121 0.82918 0.74665 0.28158  0.03343  0.09513  237 GLU A CD  
1834 O OE1 . GLU A 237 ? 0.72577 0.81554 0.75654 0.28110  0.03197  0.10597  237 GLU A OE1 
1835 O OE2 . GLU A 237 ? 0.69433 0.86947 0.77479 0.29961  0.02471  0.09769  237 GLU A OE2 
1836 N N   . VAL A 238 ? 0.63424 0.71789 0.64386 0.20251  0.06864  0.05431  238 VAL A N   
1837 C CA  . VAL A 238 ? 0.65548 0.71377 0.65689 0.20309  0.07713  0.03886  238 VAL A CA  
1838 C C   . VAL A 238 ? 0.69972 0.74460 0.70807 0.23068  0.08061  0.03468  238 VAL A C   
1839 O O   . VAL A 238 ? 0.73443 0.75430 0.74202 0.24424  0.07457  0.04584  238 VAL A O   
1840 C CB  . VAL A 238 ? 0.66733 0.68238 0.65017 0.18572  0.07539  0.03868  238 VAL A CB  
1841 C CG1 . VAL A 238 ? 0.69838 0.68247 0.66880 0.18740  0.08084  0.02045  238 VAL A CG1 
1842 C CG2 . VAL A 238 ? 0.62964 0.66375 0.61058 0.16185  0.07279  0.04123  238 VAL A CG2 
1843 N N   . SER A 239 ? 1.00870 0.60980 0.58774 0.17980  0.18279  0.02479  239 SER A N   
1844 C CA  . SER A 239 ? 1.04177 0.61298 0.61464 0.19296  0.17422  0.01497  239 SER A CA  
1845 C C   . SER A 239 ? 1.08800 0.60216 0.66192 0.17762  0.19035  0.03727  239 SER A C   
1846 O O   . SER A 239 ? 1.08658 0.59510 0.68611 0.14373  0.20414  0.05218  239 SER A O   
1847 C CB  . SER A 239 ? 0.99355 0.59790 0.60119 0.17912  0.15725  -0.01872 239 SER A CB  
1848 O OG  . SER A 239 ? 1.02489 0.60260 0.62710 0.19356  0.15177  -0.02888 239 SER A OG  
1849 N N   . ALA A 240 ? 1.14136 0.61118 0.69020 0.20361  0.18564  0.03953  240 ALA A N   
1850 C CA  . ALA A 240 ? 1.18391 0.58877 0.73841 0.18862  0.19225  0.05323  240 ALA A CA  
1851 C C   . ALA A 240 ? 1.15854 0.56211 0.74250 0.16818  0.17758  0.01859  240 ALA A C   
1852 O O   . ALA A 240 ? 1.19907 0.55349 0.79886 0.14490  0.17778  0.02234  240 ALA A O   
1853 C CB  . ALA A 240 ? 1.25706 0.60610 0.76803 0.22882  0.19110  0.06966  240 ALA A CB  
1854 N N   . LYS A 241 ? 1.09431 0.55179 0.68711 0.17737  0.16406  -0.01384 241 LYS A N   
1855 C CA  . LYS A 241 ? 1.08645 0.55484 0.70021 0.16555  0.15368  -0.04477 241 LYS A CA  
1856 C C   . LYS A 241 ? 1.04781 0.55133 0.69488 0.12522  0.15774  -0.04923 241 LYS A C   
1857 O O   . LYS A 241 ? 1.01176 0.55109 0.66906 0.11207  0.16531  -0.03618 241 LYS A O   
1858 C CB  . LYS A 241 ? 1.06039 0.58094 0.67471 0.19408  0.14201  -0.06999 241 LYS A CB  
1859 C CG  . LYS A 241 ? 1.11398 0.61524 0.69805 0.23894  0.13476  -0.06771 241 LYS A CG  
1860 C CD  . LYS A 241 ? 1.07163 0.64614 0.67249 0.26069  0.12300  -0.08686 241 LYS A CD  
1861 C CE  . LYS A 241 ? 1.10620 0.66904 0.67910 0.30740  0.11213  -0.08517 241 LYS A CE  
1862 N NZ  . LYS A 241 ? 1.05495 0.69661 0.65718 0.32444  0.09695  -0.10260 241 LYS A NZ  
1863 N N   . LYS A 242 ? 1.06824 0.56037 0.72764 0.11076  0.15014  -0.07026 242 LYS A N   
1864 C CA  . LYS A 242 ? 1.01535 0.53671 0.70247 0.07632  0.15047  -0.07704 242 LYS A CA  
1865 C C   . LYS A 242 ? 0.99270 0.54374 0.68026 0.08394  0.14042  -0.10905 242 LYS A C   
1866 O O   . LYS A 242 ? 1.03417 0.55867 0.70204 0.10970  0.13166  -0.12772 242 LYS A O   
1867 C CB  . LYS A 242 ? 1.05098 0.52049 0.75473 0.04624  0.15023  -0.06500 242 LYS A CB  
1868 C CG  . LYS A 242 ? 1.07306 0.51308 0.77770 0.04054  0.16578  -0.02525 242 LYS A CG  
1869 C CD  . LYS A 242 ? 1.11755 0.51188 0.85416 0.00554  0.16540  -0.00931 242 LYS A CD  
1870 C CE  . LYS A 242 ? 1.07883 0.52323 0.85428 -0.02892 0.16866  -0.00770 242 LYS A CE  
1871 N NZ  . LYS A 242 ? 1.04727 0.54268 0.82211 -0.02565 0.19040  0.02003  242 LYS A NZ  
1872 N N   . ILE A 243 ? 0.92498 0.53149 0.63135 0.06585  0.14257  -0.11380 243 ILE A N   
1873 C CA  . ILE A 243 ? 0.91487 0.55567 0.61889 0.07354  0.13735  -0.13792 243 ILE A CA  
1874 C C   . ILE A 243 ? 0.95307 0.55941 0.65594 0.05678  0.12577  -0.15384 243 ILE A C   
1875 O O   . ILE A 243 ? 0.95512 0.55116 0.67852 0.02586  0.12508  -0.14265 243 ILE A O   
1876 C CB  . ILE A 243 ? 0.85012 0.56461 0.57396 0.06430  0.14462  -0.13147 243 ILE A CB  
1877 C CG1 . ILE A 243 ? 0.85291 0.60676 0.57043 0.07687  0.14434  -0.14949 243 ILE A CG1 
1878 C CG2 . ILE A 243 ? 0.81786 0.53968 0.56028 0.03183  0.14707  -0.11710 243 ILE A CG2 
1879 C CD1 . ILE A 243 ? 0.80384 0.62711 0.54386 0.06658  0.15280  -0.13749 243 ILE A CD1 
1880 N N   . HIS A 244 ? 0.98892 0.57960 0.66847 0.08023  0.11439  -0.18181 244 HIS A N   
1881 C CA  . HIS A 244 ? 1.03813 0.58868 0.71116 0.07150  0.09471  -0.20577 244 HIS A CA  
1882 C C   . HIS A 244 ? 1.03379 0.64132 0.69599 0.07887  0.09337  -0.22346 244 HIS A C   
1883 O O   . HIS A 244 ? 1.02065 0.67352 0.66322 0.11031  0.10246  -0.23071 244 HIS A O   
1884 C CB  . HIS A 244 ? 1.11069 0.58897 0.75557 0.09936  0.07676  -0.22958 244 HIS A CB  
1885 C CG  . HIS A 244 ? 1.13523 0.55397 0.78495 0.09738  0.07952  -0.20776 244 HIS A CG  
1886 N ND1 . HIS A 244 ? 1.16140 0.52317 0.83725 0.06311  0.07403  -0.18915 244 HIS A ND1 
1887 C CD2 . HIS A 244 ? 1.14674 0.55693 0.77877 0.12750  0.08776  -0.19872 244 HIS A CD2 
1888 C CE1 . HIS A 244 ? 1.19213 0.50997 0.86115 0.07319  0.08129  -0.16660 244 HIS A CE1 
1889 N NE2 . HIS A 244 ? 1.18431 0.52860 0.82404 0.11357  0.08780  -0.17417 244 HIS A NE2 
1890 N N   . PHE A 245 ? 1.05311 0.66319 0.72968 0.05166  0.08321  -0.22734 245 PHE A N   
1891 C CA  . PHE A 245 ? 1.06843 0.72213 0.72691 0.06152  0.07787  -0.24521 245 PHE A CA  
1892 C C   . PHE A 245 ? 1.17536 0.77678 0.80904 0.07414  0.04618  -0.28507 245 PHE A C   
1893 O O   . PHE A 245 ? 1.21188 0.74523 0.86335 0.05493  0.02562  -0.29286 245 PHE A O   
1894 C CB  . PHE A 245 ? 0.99951 0.69482 0.68591 0.02894  0.08316  -0.22640 245 PHE A CB  
1895 C CG  . PHE A 245 ? 0.92240 0.66558 0.62976 0.01916  0.10779  -0.19281 245 PHE A CG  
1896 C CD1 . PHE A 245 ? 0.89672 0.62096 0.63012 -0.00007 0.11552  -0.17005 245 PHE A CD1 
1897 C CD2 . PHE A 245 ? 0.88757 0.69310 0.58856 0.03045  0.12164  -0.18311 245 PHE A CD2 
1898 C CE1 . PHE A 245 ? 0.84732 0.60962 0.59553 -0.00464 0.13133  -0.14561 245 PHE A CE1 
1899 C CE2 . PHE A 245 ? 0.83760 0.67865 0.56324 0.01925  0.13736  -0.15510 245 PHE A CE2 
1900 C CZ  . PHE A 245 ? 0.81871 0.63605 0.56577 0.00322  0.13950  -0.14009 245 PHE A CZ  
1901 N N   . ALA A 246 ? 1.23788 0.87121 0.83078 0.10794  0.04119  -0.30938 246 ALA A N   
1902 C CA  . ALA A 246 ? 1.34794 0.93987 0.90954 0.12520  0.00571  -0.35331 246 ALA A CA  
1903 C C   . ALA A 246 ? 1.36922 0.99561 0.94209 0.10283  -0.00423 -0.35393 246 ALA A C   
1904 O O   . ALA A 246 ? 1.33320 1.02939 0.88923 0.11513  0.01496  -0.34053 246 ALA A O   
1905 C CB  . ALA A 246 ? 1.39386 1.00852 0.90121 0.18215  0.00660  -0.37686 246 ALA A CB  
1906 N N   . ARG A 247 ? 1.43967 1.01927 1.04566 0.06941  -0.03410 -0.36623 247 ARG A N   
1907 C CA  . ARG A 247 ? 1.47333 1.08461 1.09627 0.04813  -0.04858 -0.36921 247 ARG A CA  
1908 C C   . ARG A 247 ? 1.59929 1.17322 1.19124 0.06903  -0.09602 -0.42210 247 ARG A C   
1909 O O   . ARG A 247 ? 1.67980 1.18075 1.27774 0.06857  -0.12624 -0.44861 247 ARG A O   
1910 C CB  . ARG A 247 ? 1.43016 1.03385 1.12519 -0.00689 -0.04687 -0.34054 247 ARG A CB  
1911 C CG  . ARG A 247 ? 1.34444 0.99297 1.06306 -0.02297 -0.00468 -0.29226 247 ARG A CG  
1912 C CD  . ARG A 247 ? 1.28684 1.00749 0.99989 -0.02244 0.00996  -0.27609 247 ARG A CD  
1913 N NE  . ARG A 247 ? 1.20952 0.96349 0.94535 -0.03657 0.04299  -0.23522 247 ARG A NE  
1914 C CZ  . ARG A 247 ? 1.16642 0.96026 0.88120 -0.01810 0.06731  -0.21801 247 ARG A CZ  
1915 N NH1 . ARG A 247 ? 1.19206 1.00773 0.86385 0.01557  0.06969  -0.23140 247 ARG A NH1 
1916 N NH2 . ARG A 247 ? 1.10398 0.91842 0.84335 -0.03249 0.08879  -0.18615 247 ARG A NH2 
1917 N N   . PHE A 248 ? 1.63566 1.25966 1.19474 0.08854  -0.10331 -0.43463 248 PHE A N   
1918 C CA  . PHE A 248 ? 1.73632 1.34770 1.27429 0.10710  -0.14331 -0.46987 248 PHE A CA  
1919 C C   . PHE A 248 ? 1.72077 1.34783 1.29224 0.07749  -0.17145 -0.47858 248 PHE A C   
1920 O O   . PHE A 248 ? 1.78109 1.36559 1.39182 0.05443  -0.21202 -0.50052 248 PHE A O   
1921 C CB  . PHE A 248 ? 1.78893 1.45293 1.26014 0.16276  -0.12733 -0.46948 248 PHE A CB  
1922 C CG  . PHE A 248 ? 1.82954 1.48769 1.27624 0.19444  -0.10435 -0.46291 248 PHE A CG  
1923 C CD1 . PHE A 248 ? 1.77787 1.48042 1.22268 0.19915  -0.05828 -0.42821 248 PHE A CD1 
1924 C CD2 . PHE A 248 ? 1.92801 1.53822 1.35761 0.22014  -0.13133 -0.49148 248 PHE A CD2 
1925 C CE1 . PHE A 248 ? 1.80218 1.50723 1.23259 0.22812  -0.03935 -0.42172 248 PHE A CE1 
1926 C CE2 . PHE A 248 ? 1.95507 1.56404 1.36373 0.25210  -0.11219 -0.48595 248 PHE A CE2 
1927 C CZ  . PHE A 248 ? 1.88862 1.54781 1.29964 0.25571  -0.06604 -0.45085 248 PHE A CZ  
1928 N N   . ARG A 249 ? 1.65179 1.34234 1.21356 0.07743  -0.15158 -0.45979 249 ARG A N   
1929 C CA  . ARG A 249 ? 1.63581 1.35292 1.24233 0.04585  -0.17168 -0.45675 249 ARG A CA  
1930 C C   . ARG A 249 ? 1.48739 1.21419 1.17616 -0.00916 -0.14615 -0.41130 249 ARG A C   
1931 O O   . ARG A 249 ? 1.44583 1.16861 1.14576 -0.01813 -0.10879 -0.37846 249 ARG A O   
1932 C CB  . ARG A 249 ? 1.66678 1.45283 1.22317 0.07630  -0.15992 -0.44728 249 ARG A CB  
1933 N N   . SER A 250 ? 1.39095 1.13475 1.13650 -0.04214 -0.16818 -0.41088 250 SER A N   
1934 C CA  . SER A 250 ? 1.23282 1.00083 1.05213 -0.08695 -0.14355 -0.36763 250 SER A CA  
1935 C C   . SER A 250 ? 1.10874 0.94104 0.90743 -0.07644 -0.10738 -0.33227 250 SER A C   
1936 O O   . SER A 250 ? 1.10188 0.97413 0.87983 -0.06133 -0.12059 -0.34012 250 SER A O   
1937 C CB  . SER A 250 ? 1.20968 0.98123 1.10367 -0.12347 -0.18114 -0.38010 250 SER A CB  
1938 O OG  . SER A 250 ? 1.12424 0.94845 1.07398 -0.15187 -0.15541 -0.33883 250 SER A OG  
1939 N N   . PHE A 251 ? 1.03023 0.86835 0.83380 -0.08285 -0.06542 -0.29439 251 PHE A N   
1940 C CA  . PHE A 251 ? 0.95863 0.84640 0.75520 -0.07939 -0.03410 -0.25876 251 PHE A CA  
1941 C C   . PHE A 251 ? 0.90333 0.79072 0.75304 -0.10925 -0.00954 -0.22474 251 PHE A C   
1942 O O   . PHE A 251 ? 0.88354 0.75666 0.72338 -0.10579 0.01703  -0.20579 251 PHE A O   
1943 C CB  . PHE A 251 ? 0.95444 0.85362 0.69028 -0.04619 -0.00959 -0.24958 251 PHE A CB  
1944 C CG  . PHE A 251 ? 0.92087 0.86740 0.64259 -0.03828 0.01013  -0.22016 251 PHE A CG  
1945 C CD1 . PHE A 251 ? 0.89370 0.86634 0.64667 -0.05420 0.00378  -0.20804 251 PHE A CD1 
1946 C CD2 . PHE A 251 ? 0.91904 0.88415 0.60056 -0.01469 0.03465  -0.20251 251 PHE A CD2 
1947 C CE1 . PHE A 251 ? 0.86365 0.86921 0.60139 -0.04497 0.01873  -0.18125 251 PHE A CE1 
1948 C CE2 . PHE A 251 ? 0.88867 0.88894 0.56274 -0.01084 0.05067  -0.17190 251 PHE A CE2 
1949 C CZ  . PHE A 251 ? 0.86370 0.87873 0.56267 -0.02517 0.04129  -0.16245 251 PHE A CZ  
1950 N N   . PRO A 252 ? 0.88194 0.78921 0.78837 -0.13553 -0.01826 -0.21648 252 PRO A N   
1951 C CA  . PRO A 252 ? 0.83698 0.74855 0.78998 -0.15811 0.00696  -0.18296 252 PRO A CA  
1952 C C   . PRO A 252 ? 0.77695 0.71038 0.70452 -0.14366 0.03837  -0.15469 252 PRO A C   
1953 O O   . PRO A 252 ? 0.75731 0.71688 0.65366 -0.12615 0.03915  -0.15337 252 PRO A O   
1954 C CB  . PRO A 252 ? 0.83480 0.78342 0.85045 -0.18135 -0.00870 -0.17993 252 PRO A CB  
1955 C CG  . PRO A 252 ? 0.89029 0.82859 0.90602 -0.18116 -0.05163 -0.22004 252 PRO A CG  
1956 C CD  . PRO A 252 ? 0.90822 0.83641 0.84224 -0.14397 -0.05403 -0.23942 252 PRO A CD  
1957 N N   . PHE A 253 ? 0.75759 0.67634 0.69881 -0.15029 0.06208  -0.13147 253 PHE A N   
1958 C CA  . PHE A 253 ? 0.70874 0.64104 0.62956 -0.13653 0.08584  -0.10870 253 PHE A CA  
1959 C C   . PHE A 253 ? 0.66425 0.63941 0.59417 -0.13294 0.08537  -0.09808 253 PHE A C   
1960 O O   . PHE A 253 ? 0.63846 0.62275 0.53897 -0.11714 0.09009  -0.09172 253 PHE A O   
1961 C CB  . PHE A 253 ? 0.71381 0.62770 0.65012 -0.14169 0.10648  -0.08733 253 PHE A CB  
1962 C CG  . PHE A 253 ? 0.69640 0.61838 0.61053 -0.12464 0.12408  -0.06990 253 PHE A CG  
1963 C CD1 . PHE A 253 ? 0.69784 0.60279 0.57827 -0.10975 0.12794  -0.07363 253 PHE A CD1 
1964 C CD2 . PHE A 253 ? 0.68802 0.63599 0.61751 -0.12144 0.13439  -0.05131 253 PHE A CD2 
1965 C CE1 . PHE A 253 ? 0.68425 0.59328 0.55143 -0.09641 0.13696  -0.06106 253 PHE A CE1 
1966 C CE2 . PHE A 253 ? 0.68329 0.63062 0.58908 -0.10244 0.14345  -0.04135 253 PHE A CE2 
1967 C CZ  . PHE A 253 ? 0.68163 0.60694 0.55859 -0.09216 0.14232  -0.04719 253 PHE A CZ  
1968 N N   . TRP A 254 ? 0.65881 0.66119 0.63363 -0.14733 0.07881  -0.09450 254 TRP A N   
1969 C CA  . TRP A 254 ? 0.64114 0.68616 0.62492 -0.13880 0.07861  -0.08438 254 TRP A CA  
1970 C C   . TRP A 254 ? 0.65419 0.71368 0.61120 -0.12671 0.05780  -0.10061 254 TRP A C   
1971 O O   . TRP A 254 ? 0.64153 0.71969 0.58189 -0.11090 0.05908  -0.09098 254 TRP A O   
1972 C CB  . TRP A 254 ? 0.63866 0.72067 0.68443 -0.15525 0.07941  -0.07364 254 TRP A CB  
1973 C CG  . TRP A 254 ? 0.63674 0.71361 0.70584 -0.16177 0.10599  -0.04817 254 TRP A CG  
1974 C CD1 . TRP A 254 ? 0.65854 0.73202 0.77744 -0.18660 0.11054  -0.03783 254 TRP A CD1 
1975 C CD2 . TRP A 254 ? 0.61918 0.69250 0.66067 -0.14068 0.12992  -0.02862 254 TRP A CD2 
1976 N NE1 . TRP A 254 ? 0.65583 0.72780 0.77580 -0.18021 0.14037  -0.00876 254 TRP A NE1 
1977 C CE2 . TRP A 254 ? 0.63233 0.70457 0.70182 -0.14971 0.15096  -0.00590 254 TRP A CE2 
1978 C CE3 . TRP A 254 ? 0.60372 0.67175 0.60046 -0.11449 0.13274  -0.02823 254 TRP A CE3 
1979 C CZ2 . TRP A 254 ? 0.62751 0.69718 0.67249 -0.12753 0.17485  0.01444  254 TRP A CZ2 
1980 C CZ3 . TRP A 254 ? 0.60146 0.66238 0.57969 -0.09561 0.15139  -0.01247 254 TRP A CZ3 
1981 C CH2 . TRP A 254 ? 0.61376 0.67747 0.61166 -0.09933 0.17234  0.00734  254 TRP A CH2 
1982 N N   . ARG A 255 ? 0.68613 0.73389 0.63365 -0.12985 0.03711  -0.12520 255 ARG A N   
1983 C CA  . ARG A 255 ? 0.70550 0.76436 0.61109 -0.11002 0.02133  -0.13778 255 ARG A CA  
1984 C C   . ARG A 255 ? 0.69543 0.73860 0.55117 -0.09199 0.03997  -0.12360 255 ARG A C   
1985 O O   . ARG A 255 ? 0.68899 0.74729 0.51888 -0.07631 0.04010  -0.11233 255 ARG A O   
1986 C CB  . ARG A 255 ? 0.75030 0.79738 0.64667 -0.10974 -0.00672 -0.17110 255 ARG A CB  
1987 C CG  . ARG A 255 ? 0.77749 0.83691 0.61783 -0.08142 -0.02060 -0.18306 255 ARG A CG  
1988 C CD  . ARG A 255 ? 0.83297 0.88887 0.66722 -0.07626 -0.05812 -0.22213 255 ARG A CD  
1989 N NE  . ARG A 255 ? 0.83886 0.92187 0.73349 -0.09546 -0.08459 -0.23303 255 ARG A NE  
1990 C CZ  . ARG A 255 ? 0.83500 0.96126 0.73713 -0.08648 -0.09521 -0.22743 255 ARG A CZ  
1991 N NH1 . ARG A 255 ? 0.82837 0.96783 0.68072 -0.06055 -0.08065 -0.20774 255 ARG A NH1 
1992 N NH2 . ARG A 255 ? 0.84044 0.99795 0.80575 -0.10414 -0.12212 -0.24018 255 ARG A NH2 
1993 N N   . ARG A 256 ? 0.69793 0.71159 0.54448 -0.09457 0.05502  -0.12169 256 ARG A N   
1994 C CA  . ARG A 256 ? 0.69860 0.70439 0.51331 -0.08169 0.07268  -0.10585 256 ARG A CA  
1995 C C   . ARG A 256 ? 0.66266 0.67532 0.48657 -0.08094 0.08296  -0.08121 256 ARG A C   
1996 O O   . ARG A 256 ? 0.66611 0.68160 0.46955 -0.07109 0.08782  -0.06582 256 ARG A O   
1997 C CB  . ARG A 256 ? 0.71728 0.69481 0.53008 -0.08423 0.08453  -0.10951 256 ARG A CB  
1998 C CG  . ARG A 256 ? 0.73071 0.70871 0.51743 -0.07079 0.09942  -0.09785 256 ARG A CG  
1999 C CD  . ARG A 256 ? 0.77650 0.74044 0.54221 -0.05998 0.09914  -0.11690 256 ARG A CD  
2000 N NE  . ARG A 256 ? 0.80102 0.73447 0.58524 -0.07157 0.08881  -0.13542 256 ARG A NE  
2001 C CZ  . ARG A 256 ? 0.80330 0.71085 0.60282 -0.07831 0.09839  -0.13028 256 ARG A CZ  
2002 N NH1 . ARG A 256 ? 0.78745 0.69793 0.58563 -0.07303 0.11506  -0.11271 256 ARG A NH1 
2003 N NH2 . ARG A 256 ? 0.82885 0.70573 0.64747 -0.09057 0.08896  -0.14202 256 ARG A NH2 
2004 N N   . VAL A 257 ? 0.63019 0.64467 0.48507 -0.08950 0.08592  -0.07603 257 VAL A N   
2005 C CA  . VAL A 257 ? 0.60568 0.62438 0.46367 -0.08160 0.09039  -0.05887 257 VAL A CA  
2006 C C   . VAL A 257 ? 0.61916 0.65910 0.46870 -0.07109 0.07721  -0.05566 257 VAL A C   
2007 O O   . VAL A 257 ? 0.63025 0.66102 0.46281 -0.06049 0.07663  -0.04143 257 VAL A O   
2008 C CB  . VAL A 257 ? 0.58892 0.61317 0.47576 -0.08514 0.09859  -0.05404 257 VAL A CB  
2009 C CG1 . VAL A 257 ? 0.57513 0.60473 0.45779 -0.06828 0.09870  -0.04229 257 VAL A CG1 
2010 C CG2 . VAL A 257 ? 0.58600 0.58436 0.47330 -0.09043 0.11215  -0.05258 257 VAL A CG2 
2011 N N   . HIS A 258 ? 0.62019 0.68678 0.48470 -0.07383 0.06358  -0.06846 258 HIS A N   
2012 C CA  . HIS A 258 ? 0.63487 0.72497 0.48991 -0.05982 0.04822  -0.06706 258 HIS A CA  
2013 C C   . HIS A 258 ? 0.65845 0.73617 0.46858 -0.04663 0.04690  -0.05805 258 HIS A C   
2014 O O   . HIS A 258 ? 0.66428 0.73792 0.45866 -0.03337 0.04475  -0.04069 258 HIS A O   
2015 C CB  . HIS A 258 ? 0.63877 0.76114 0.51887 -0.06580 0.02863  -0.08730 258 HIS A CB  
2016 C CG  . HIS A 258 ? 0.65296 0.80067 0.51580 -0.04720 0.00864  -0.08998 258 HIS A CG  
2017 N ND1 . HIS A 258 ? 0.68537 0.83125 0.50631 -0.03422 -0.00447 -0.09946 258 HIS A ND1 
2018 C CD2 . HIS A 258 ? 0.64913 0.82614 0.52667 -0.03427 -0.00067 -0.08407 258 HIS A CD2 
2019 C CE1 . HIS A 258 ? 0.70293 0.87348 0.51227 -0.01520 -0.02173 -0.09819 258 HIS A CE1 
2020 N NE2 . HIS A 258 ? 0.68439 0.87357 0.52958 -0.01547 -0.02055 -0.08954 258 HIS A NE2 
2021 N N   . ASP A 259 ? 0.68550 0.75692 0.47412 -0.04781 0.04886  -0.06750 259 ASP A N   
2022 C CA  . ASP A 259 ? 0.72346 0.79452 0.46908 -0.03200 0.05227  -0.05438 259 ASP A CA  
2023 C C   . ASP A 259 ? 0.70889 0.75996 0.45278 -0.03396 0.06917  -0.02449 259 ASP A C   
2024 O O   . ASP A 259 ? 0.71341 0.76418 0.43636 -0.02307 0.07014  -0.00102 259 ASP A O   
2025 C CB  . ASP A 259 ? 0.74449 0.81651 0.46562 -0.02700 0.05331  -0.07223 259 ASP A CB  
2026 C CG  . ASP A 259 ? 0.77107 0.85638 0.49235 -0.02353 0.02759  -0.10561 259 ASP A CG  
2027 O OD1 . ASP A 259 ? 0.76903 0.87202 0.51249 -0.02559 0.01054  -0.11081 259 ASP A OD1 
2028 O OD2 . ASP A 259 ? 0.80260 0.88110 0.50430 -0.01728 0.02165  -0.12830 259 ASP A OD2 
2029 N N   . SER A 260 ? 0.70151 0.73405 0.46985 -0.04767 0.07978  -0.02406 260 SER A N   
2030 C CA  . SER A 260 ? 0.70293 0.71594 0.47733 -0.05195 0.09014  -0.00101 260 SER A CA  
2031 C C   . SER A 260 ? 0.70430 0.69920 0.48804 -0.04849 0.08034  0.01272  260 SER A C   
2032 O O   . SER A 260 ? 0.71797 0.69559 0.50187 -0.04952 0.08080  0.03640  260 SER A O   
2033 C CB  . SER A 260 ? 0.68232 0.68219 0.47589 -0.06278 0.09974  -0.00969 260 SER A CB  
2034 O OG  . SER A 260 ? 0.68171 0.69177 0.46361 -0.06194 0.10813  -0.02101 260 SER A OG  
2035 N N   . PHE A 261 ? 0.69586 0.69467 0.49006 -0.04329 0.07081  -0.00043 261 PHE A N   
2036 C CA  . PHE A 261 ? 0.72301 0.70148 0.52189 -0.03300 0.06047  0.00744  261 PHE A CA  
2037 C C   . PHE A 261 ? 0.77741 0.77115 0.56770 -0.01568 0.04670  0.00740  261 PHE A C   
2038 O O   . PHE A 261 ? 0.81751 0.78684 0.60039 -0.00248 0.03550  0.01914  261 PHE A O   
2039 C CB  . PHE A 261 ? 0.69467 0.66530 0.51086 -0.03215 0.06330  -0.00506 261 PHE A CB  
2040 C CG  . PHE A 261 ? 0.67012 0.62183 0.49303 -0.04387 0.07237  -0.00531 261 PHE A CG  
2041 C CD1 . PHE A 261 ? 0.67616 0.59672 0.50180 -0.04574 0.06538  0.00632  261 PHE A CD1 
2042 C CD2 . PHE A 261 ? 0.64381 0.60772 0.47415 -0.05319 0.08495  -0.01687 261 PHE A CD2 
2043 C CE1 . PHE A 261 ? 0.66337 0.57364 0.50048 -0.05525 0.07066  0.00474  261 PHE A CE1 
2044 C CE2 . PHE A 261 ? 0.62971 0.57811 0.46418 -0.05959 0.09186  -0.01754 261 PHE A CE2 
2045 C CZ  . PHE A 261 ? 0.63903 0.56476 0.47756 -0.05991 0.08468  -0.00756 261 PHE A CZ  
2046 N N   . ILE A 262 ? 0.78861 0.81980 0.58193 -0.01414 0.04348  -0.00677 262 ILE A N   
2047 C CA  . ILE A 262 ? 0.83289 0.88692 0.62405 0.00447  0.02797  -0.00886 262 ILE A CA  
2048 C C   . ILE A 262 ? 0.89720 0.95341 0.65477 0.01522  0.01945  0.00264  262 ILE A C   
2049 O O   . ILE A 262 ? 0.94119 0.97470 0.67897 0.03028  0.01221  0.02252  262 ILE A O   
2050 C CB  . ILE A 262 ? 0.80129 0.90156 0.62489 0.00021  0.02466  -0.02955 262 ILE A CB  
2051 C CG1 . ILE A 262 ? 0.76721 0.86846 0.62065 -0.00766 0.03858  -0.03314 262 ILE A CG1 
2052 C CG2 . ILE A 262 ? 0.82023 0.95340 0.64805 0.02159  0.00694  -0.03188 262 ILE A CG2 
2053 C CD1 . ILE A 262 ? 0.76484 0.85226 0.61416 0.01451  0.03790  -0.02536 262 ILE A CD1 
2054 N N   . GLU A 263 ? 0.92515 1.00540 0.67243 0.01092  0.01867  -0.00955 263 GLU A N   
2055 C CA  . GLU A 263 ? 0.98243 1.07127 0.68838 0.02838  0.01093  -0.00022 263 GLU A CA  
2056 C C   . GLU A 263 ? 0.98858 1.07514 0.66971 0.02296  0.02525  0.00261  263 GLU A C   
2057 O O   . GLU A 263 ? 0.99376 1.10275 0.66072 0.02798  0.01737  -0.02019 263 GLU A O   
2058 C CB  . GLU A 263 ? 1.00909 1.13876 0.71669 0.04225  -0.01264 -0.02364 263 GLU A CB  
2059 C CG  . GLU A 263 ? 1.07268 1.21235 0.72966 0.07028  -0.02564 -0.01408 263 GLU A CG  
2060 C CD  . GLU A 263 ? 1.11560 1.23761 0.75648 0.09070  -0.03104 0.01350  263 GLU A CD  
2061 O OE1 . GLU A 263 ? 1.10118 1.20524 0.77114 0.08558  -0.02901 0.01869  263 GLU A OE1 
2062 O OE2 . GLU A 263 ? 1.17487 1.29815 0.76957 0.11570  -0.03841 0.02996  263 GLU A OE2 
# 
